"gene_id","gene_start","gene_stop","gene_length","gene_nuc_seq","pI","net_charge","mol_wt","gene_prot_seq","defline","comment","definition","cellular_location","blast_summary","interpro_summary","cogs_summary","blocks_summary","ProDom","gene_id_lmd","gene_start_lmd","gene_stop_lmd","gene_length_lmd","gene_nuc_seq_lmd","pI_lmd","net_charge_lmd","mol_wt_lmd","gene_prot_seq_lmd","defline_lmd","comment_lmd","definition_lmd","blast_summary_lmd","cogs_summary_lmd","blocks_summary_lmd","ProDom_lmd","revisit","revisit_lmd","paralog","paralog_lmd","pdb_hit_lmd","pdb_hit","bgene_id","bgene_id_lmd","pfam_summary","pfam_summary_lmd","gi","gi_lmd","case1","case2","case1_lmd","case2_lmd","mol_id","mol_id_lmd","island_id","genbank_locus_tag" "AA00001","1","1359","1359","GTGGAAAACCGGCCGAATTCTCTGTGGCAAAATTGTCTGCTGCAACTACAAGATAAAATTCCTGCGGACGATTTCAAAATCTGGCTTTATCCGTTGCAAGCCGATATAAATGCAAACGGTGTCCTACTTTACGCCTCAAACGCGTTTGTGCAAAAATGGGTGGTCGATAACTATCTTCCCTTGATCACCGACATCGCCCGTCAAACCAGTACCAATCCGAACCTCAACGTATCCGTCATCGAAGGTATTAAGCCTGCCGCACCGAAAGCCGAGAAACCGGCAAAGAAACAAAGTGCGGTCGGTTTTTCCGAAGAAAAAAGCTCCGCTAAAACACCTTATCATTCCAATTTAAATACCAAATTGGTGTTTGAAAATTTCGTTGAGGGGAAATCCAACCAACTGGCACGTGCTGTGGCGCAAAAGGTTGCGGACAATCCCGGCGAACAAACTGCCAACCCGCTTTTCTTATACGGCGGCACTGGTTTGGGTAAAACCCACTTATTGCACGCTATCGGCAACGGTATTATCGCCAATAATCCGAACGCGCGCGTGGTGTATATTCACTCCGAACGCTTTGTGCAGCAAGTCGTGGCTTATATTCGCGATAACAAAATGGAAGAATTCAAAAAATTCTACCGTTCGTTGGATGCCTTATTAGTGGATGATATTCAATTTTTCAGTGACAAAGAAAAAACCCAGGAAGAATTTTTCCATATTTTCAATACATTATTTGAACGTGGGCGCCAAATCATTCTCACCTCCGACCGTTATCCGCGCGAAATCGAAAAAATTGAGGAACGACTGAAATCCCGTTTCGGCTGGGGCTTAACCACCGCTATTGAGCCGCCCGATTTAGAAACCCGCGTGGCGATTTTAATGAAAAAAGCGGAAGAAAATAATGTTGATTTACCGCACGATGTGGCGTTTTTTATCGGGCAAAAACTACGTACCAACGTGCGTGAATTGGAAGGCGCGTTAAATCGTGTGAAAGCCATGCAAGAGTTCAAAGGCGAACCGATCACCATTGATTTTGTGCGGGAAACCTTAAAAGATATGCTGGCGCTACAGGACAAACTGGTCACCGTGGACAATATTCAAAAAGTCGTCGCCGAATACTATCGCATTAAGGTTTCCGATCTGAAATCCAAAAACCGTTCCCGTTCGGTGGCACGTCCGCGTCAGGTCGCCATGGCATTGGCAAAAGAATTAACCAACCGTAGCCTGCCGGAAATCGGTAAGTCCTTCGGCGATCGTGATCACACCACGGTTTTACACTCCTGCCGCACCATTGCAGGATTCCGCGACACCGATCCGAATATTCAAGAAGATTGGGCTAACTTAATCCGAATTTTATCCGTA","9.30","5.87","51515","VENRPNSLWQNCLLQLQDKIPADDFKIWLYPLQADINANGVLLYASNAFVQKWVVDNYLPLITDIARQTSTNPNLNVSVIEGIKPAAPKAEKPAKKQSAVGFSEEKSSAKTPYHSNLNTKLVFENFVEGKSNQLARAVAQKVADNPGEQTANPLFLYGGTGLGKTHLLHAIGNGIIANNPNARVVYIHSERFVQQVVAYIRDNKMEEFKKFYRSLDALLVDDIQFFSDKEKTQEEFFHIFNTLFERGRQIILTSDRYPREIEKIEERLKSRFGWGLTTAIEPPDLETRVAILMKKAEENNVDLPHDVAFFIGQKLRTNVRELEGALNRVKAMQEFKGEPITIDFVRETLKDMLALQDKLVTVDNIQKVVAEYYRIKVSDLKSKNRSRSVARPRQVAMALAKELTNRSLPEIGKSFGDRDHTTVLHSCRTIAGFRDTDPNIQEDWANLIRILSV","","","chromosomal replication initiator protein","Cytoplasm","AA00001 has significant similarity to the Haemophilus ducreyi gene HD0851, a chromosomal replication initiator protein, dnaA (1e-159).AA00001 has significant similarity to the Haemophilus influenzae Rd gene 16272931 (0.0).","
InterPro
IPR001957
Family
Bacterial chromosomal replication initiator protein, DnaA
PR00051\"[151-171]T\"[183-197]T\"[215-229]T\"[249-276]T\"[411-430]TDNAA
TIGR00362\"[2-451]TDnaA: chromosomal replication initiator pro
PS01008\"[411-430]TDNAA
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[150-278]TAAA
InterPro
IPR013159
Domain
Chromosomal replication initiator, DnaA C-terminal
PF08299\"[361-430]TBac_DnaA_C
SM00760\"[361-430]Tno description
InterPro
IPR013317
Domain
Chromosomal replication initiator, DnaA
PF00308\"[117-336]TBac_DnaA
noIPR
unintegrated
unintegrated
G3DSA:1.10.1750.10\"[348-451]Tno description
G3DSA:3.40.50.300\"[114-282]Tno description


","BeTs to 18 clades of COG0593COG name: ATPase involved in DNA replication initiationFunctional Class: LThe phylogenetic pattern of COG0593 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit (1.9e-112) to 4/4 blocks of the IPB001957 family, which is described as \"Bacterial chromosomal replication initiator protein, DnaA\". Interpro entry for IP:IPR001957. IPB001957A 151-168 6e-13 IPB001957B 208-254 2e-35 IPB001957C 265-296 6.6e-25 IPB001957D 379-430 9.7e-36","Residues 224 to 261 match (1e-08) PD:PD594301 which is described as REPLICATION INITIATOR CHROMOSOMAL DNA DNA-BINDING ATP-BINDING COMPLETE PROTEOME DNAA DNAA2 ","Fri Feb 27 08:06:48 2004","Fri Feb 27 08:06:48 2004","Fri Feb 27 08:06:48 2004","Fri Feb 27 08:06:48 2004","Fri Feb 27 08:06:48 2004","Fri Feb 27 08:06:48 2004","Fri Feb 27 08:06:48 2004","Fri Feb 27 08:06:48 2004","Fri Feb 27 08:06:48 2004","Fri Feb 27 08:06:48 2004","Fri Feb 27 08:06:48 2004","Fri Feb 27 08:06:48 2004","Fri Feb 27 08:06:48 2004","Fri Feb 27 08:06:48 2004","Fri Feb 27 08:06:48 2004","Fri Feb 27 08:06:48 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00001 is paralogous to AA00110, an ATPase involved in DNA replication (2e-16).AA00001 is paralogously related to AA00110 (2e-16).","Fri Feb 27 08:06:48 2004","Fri Feb 27 08:06:48 2004","pdb1L8Q1L8Q-A CRYSTAL STRUCTURE OF DNA REPLICATION INITIATION 188.0 1e-48","","","Residues 117 to 430 (E-value = 1.5e-203) place AA00001 in the Bac_DnaA family which is described as Bacterial dnaA protein (PF00308)","Fri Feb 27 08:06:48 2004","","","","Skovgaard,O. and Hansen,F.G.Comparison of dnaA nucleotide sequences of Escherichia coli,Salmonella typhimurium, and Serratia marcescensJ. Bacteriol. 169 (9), 3976-3981 (1987)PubMed: 3040670Hansen,F.G., Hansen,E.B. and Atlung,T.The nucleotide sequence of the dnaA gene promoter and of theadjacent rpmH gene, coding for the ribosomal protein L34, ofEscherichia coliEMBO J. 1 (9), 1043-1048 (1982)PubMed: 6329723Ohmori,H., Kimura,M., Nagata,T. and Sakakibara,Y.Structural analysis of the dnaA and dnaN genes of Escherichia coliGene 28 (2), 159-170 (1984)PubMed: 6234204Hansen,E.B., Hansen,F.G. and von Meyenburg,K.The nucleotide sequence of the dnaA gene and the first part of thednaN gene of Escherichia coli K-12Nucleic Acids Res. 10 (22), 7373-7385 (1982)PubMed: 6296774","","Fri Feb 27 08:38:48 2004","1","Fri Feb 27 08:06:48 2004","","" "AA00002","1373","2470","1098","ATGCAATTTATTATTTCCAGAGAAAATTTACTAAAACCCTTACAACAAGTGTGCGGCGTGCTGAATAGCCGCCCGAATATTCCGGTGTTAAATAATGTATTGCTGCAAATTGAAAATAATCAATTAAATATTACCGGTACGGATTTAGAAGTGGAACTGTCCACCCAAACCCCATTACTTCATGCGGAACAAGACGGCAAATTCACTATTCCGGCGAAAAAATTCCTGGATATTTGTCGCAGCCTGCCGGATAATGCAGAAATTGCTGTGACATTTGAAGAAGATCGCGCTATTGTGCGTTCCGATCGCAGTAAATTCAATTTATCCACTTTGCCGGCGGAAGATTATCCGAATTTAACGGACTGGCAATCGGAAGTGGATTTTACGCTTGAGCAAGCCACCTTGCGCCGCTTAATTGAAGCCACCCAATTTTCCATGGCGAACCAAGATGCCCGTTATTTCTTAAACGGTATGAAGTTTGAGACGGAAGGCAATTTATTGCGTACCGTAGCGACCGACGGTCACCGTTTGGCGGTATGCACCATTCCGCTGGAGCAGGATTTACAGACCCATTCGGTAATTTTACCGCGTAAGGGCGTGCTGGAACTTGCCCGTTTGCTGGAACCGAGTGATCAACCGGCGCGTTTACAAATCGGCACCAATAACTTACGCATTCAGCTAAACAATATCACCTTCACATCCAAACTCATTGACGGCCGCTTCCCGGATTATCGCCGCGTATTACCACGCAATGCCACCCGCATTGTGGAAGCCGGTTGGGAGACCTTAAAACAGGCTTTCGTACGTGCCGCGATTTTATCTAACGAACGTTTCCGCAGTGTGCGATTACAACTCAGTGAAAATCAACTCAAAATCACCGCCACCAACCCCGAACAGGAAGTGGCGGAAGAAATTATCGACGTGTCTTACAGCGGCGAGGAAATGGAAGTAGGCTTTAACGTGAGCTACATTTTGGATGTGCTCAACGCACTTAAGTGTAATCAGGTGCGTATGCGCTTAACGGACGCCTCCTCCAGCTGCTTAATTGAAGACTGTGAAGATGCCAGCGCGGAATATGTGATTATGCCGATGCGTTTA","","","41644","MQFIISRENLLKPLQQVCGVLNSRPNIPVLNNVLLQIENNQLNITGTDLEVELSTQTPLLHAEQDGKFTIPAKKFLDICRSLPDNAEIAVTFEEDRAIVRSDRSKFNLSTLPAEDYPNLTDWQSEVDFTLEQATLRRLIEATQFSMANQDARYFLNGMKFETEGNLLRTVATDGHRLAVCTIPLEQDLQTHSVILPRKGVLELARLLEPSDQPARLQIGTNNLRIQLNNITFTSKLIDGRFPDYRRVLPRNATRIVEAGWETLKQAFVRAAILSNERFRSVRLQLSENQLKITATNPEQEVAEEIIDVSYSGEEMEVGFNVSYILDVLNALKCNQVRMRLTDASSSCLIEDCEDASAEYVIMPMRL","2470","","DNA polymerase III, beta subunit","Cytoplasm","","
InterPro
IPR001001
Family
DNA polymerase III, beta chain
G3DSA:3.10.150.10\"[1-120]T\"[121-248]T\"[248-366]Tno description
PF00712\"[1-120]TDNA_pol3_beta
PF02767\"[129-243]TDNA_pol3_beta_2
PF02768\"[245-365]TDNA_pol3_beta_3
SM00480\"[17-362]TPOL3Bc
TIGR00663\"[1-366]Tdnan: DNA polymerase III, beta subunit


","BeTs to 18 clades of COG0592COG name: DNA polymerase sliding clamp subunit (PCNA homolog)Functional Class: LThe phylogenetic pattern of COG0592 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 1","Significant hit ( 1.8e-96) to 8/8 blocks of the IPB001001 family, which is described as \"DNA polymerase III, beta chain\". Interpro entry for IP:IPR001001. IPB001001A 5-53 2.3e-25 IPB001001B 66-80 1e-08 IPB001001C 99-117 1.4e-09 IPB001001D 135-158 6.6e-13 IPB001001E 169-179 1.6e-05 IPB001001F 193-203 0.00076 IPB001001G 234-249 1.2e-09 IPB001001H 312-331 1.3e-10","Residues 44 to 349 match (4e-22) PD:PD256123 which is described as CHAIN BETA DNA POLYMERASE III DNA-POLYMERASE REGULATION DNA-BINDING III PLASMID ","","","","","","","","","","","","Mon Nov 25 13:58:20 2002","","Wed May 19 13:11:24 2004","Wed May 19 13:11:24 2004","Wed May 19 13:11:24 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00002 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed May 19 13:11:24 2004","","","","","Residues 245 to 365 (E-value = 2.8e-61) place AA00002 in the DNA_pol3_beta_3 family which is described as DNA polymerase III beta subunit, C-terminal domain (PF02768)","Wed May 19 13:11:24 2004","","","","Tatusov,R.L., Mushegian,A.R., Bork,P., Brown,N.P., Hayes,W.S.,Borodovsky,M., Rudd,K.E. and Koonin,E.V.Metabolism and evolution of Haemophilus influenzae deduced from awhole-genome comparison with Escherichia coliCurr. Biol. 6 (3), 279-291 (1996)PubMed: 8805245Ohmori,H., Kimura,M., Nagata,T. and Sakakibara,Y. Structural analysis of the dnaA and dnaN genes of Escherichia coli Gene 28 (2), 159-170 (1984) PubMed: 6234204 Armengod,M.E., Garcia-Sogo,M. and Lambies,E. Transcriptional organization of the dnaN and recF genes of Escherichia coli K-12 J. Biol. Chem. 263 (24), 12109-12114 (1988) PubMed: 2841344 Armengod,M.E. and Lambies,E. Overlapping arrangement of the recF and dnaN operons of Escherichia coli;positive and negative control sequences Gene 43 (3), 183-196 (1986) PubMed: 3527871 Kong,X.P., Onrust,R., O\"Donnell,M. and Kuriyan,J. Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp Cell 69 (3), 425-437 (1992) PubMed: 1349852 O\"Donnell,M. Accessory protein function in the DNA polymerase III holoenzyme from E. coli Bioessays 14 (2), 105-111 (1992) PubMed: 1575709 ","","Wed May 19 13:11:24 2004","1","","","" "AA00003","2477","3550","1074","ATGGCGATTTCACGTTTAACCGTCGAAAATTTTCGTAATTTACAAGCCGTGGATCTGGAATTGGATCACGGCTTTAACTTTTTAGTCGGCAACAACGGCAGCGGCAAAACCAGTTTACTGGAAGCGATTTTTTATCTGGGGCACGGGCGCTCCTTTAAAAGTGCGGTCAGTAATCGAATCATTTCTTACGATCAACCGCACTTTACCCTGTTCGGGCAAATTCAGGAACAACAGCATCAATGGTCGGTGGGGTTGCAAAAACTGCGTCAGGGCAATACCCTCGTTAAAATTAACGGCGAAGACGGCAATAAAATTTCCGATTTGGCACACCTGCTTCCCATGCAAATCATTACGCCGGAAGGCTTAAATCTGCTCAACGGCGGGCCAAGCTATCGCCGCGCCTTTCTGGATTGGGGCTTATTTCATCATCATGTGGCTTTCTATAATTTATGGGCAAGTTTAAACCGTTTACTTAAGCAACGAAACGCCGCTTTACAACAAACCTCCGCTTATTCGCAAATGAAGATCTGGGATATGGAATTGGTCAAACTTGCCGAACAAGTCAGCCAACTGCGCGCCGACTATGCCCTGGCGCTACAACCGGAAATAGAACAAACCTGCCGTTTATTCTTACCCGAATTAGACATTAGCGTGAGTTTCCATCAAGGCTGGGAAAAAGAACAACATTATGCGGAATTACTGGAACGCAATTTTGAACGGGATCGCGCCTTAGGCTACACGGTTTCCGGCCCGCAAAAAGCGGATTTTCGTTTTAAAGCGAACGGGTTACCGGTGGAAGATGTGTTATCGCGCGGGCAGCTGAAATTATTAATGAGCGCCCTCCGCCTCGCCCAAGGGGAACACTTAATGCGGCAAAAGCAACGCCATTGTATTTTCTTAATTGACGACTTCGCTTCCGAATTGGATCAAACCAAACGGCGTCTTTTGGCAGAACGTCTGCAAAACAGCGGCTCGCAAGTATTTGTCACCGCCATCACATCAAACCAACTCAAAGAAATGCAACCGAAAAAGCACCGCACTTTTAAGATAGATACGGGAAAAATAGCATTGTTA","","","40999","MAISRLTVENFRNLQAVDLELDHGFNFLVGNNGSGKTSLLEAIFYLGHGRSFKSAVSNRIISYDQPHFTLFGQIQEQQHQWSVGLQKLRQGNTLVKINGEDGNKISDLAHLLPMQIITPEGLNLLNGGPSYRRAFLDWGLFHHHVAFYNLWASLNRLLKQRNAALQQTSAYSQMKIWDMELVKLAEQVSQLRADYALALQPEIEQTCRLFLPELDISVSFHQGWEKEQHYAELLERNFERDRALGYTVSGPQKADFRFKANGLPVEDVLSRGQLKLLMSALRLAQGEHLMRQKQRHCIFLIDDFASELDQTKRRLLAERLQNSGSQVFVTAITSNQLKEMQPKKHRTFKIDTGKIALL","3550","","DNA replication and repair protein","Cytoplasm","","
InterPro
IPR001238
Family
RecF protein
TIGR00611\"[1-355]Trecf: DNA replication and repair protein Re
PS00617\"[117-137]TRECF_1
PS00618\"[298-316]TRECF_2
InterPro
IPR003395
Domain
SMC protein, N-terminal
PF02463\"[2-356]TSMC_N
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[1-60]Tno description


","BeTs to 12 clades of COG1195COG name: Recombinational DNA repair ATPase (RecF pathway)Functional Class: LThe phylogenetic pattern of COG1195 is ---------drlbcefghs--jxit-Number of proteins in this genome belonging to this COG is 1","Significant hit ( 2.8e-71) to 5/5 blocks of the IPB001238 family, which is described as \"RecF protein\". Interpro entry for IP:IPR001238. IPB001238A 8-53 2.7e-29 IPB001238B 116-137 5.1e-11 IPB001238C 154-166 0.00058 IPB001238D 234-256 3.2e-12 IPB001238E 297-313 4.2e-09","Residues 6 to 81 match (5e-32) PD:PD000596 which is described as DNA COMPLETE PROTEOME REPAIR ATP-BINDING REPLICATION CHROMOSOME COILED COIL RECF ","","","","","","","","","","","","Fri Jan 24 13:27:04 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00003 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 325 (E-value = 2.4e-131) place AA00003 in the SMC_N family which is described as RecF/RecN/SMC N terminal domain (PF02463)","","","","","Loynds,B.M., Langford,P.R. and Kroll,J.S. 1992. recF in Actinobacillus pleuropneumoniae. Nucleic Acids Res. 20(3): 615. PubMed: 1741300. Blanar,M.A., Sandler,S.J., Armengod,M.E., Ream,L.W. and Clark,A.J. 1984. Molecular analysis of the recF gene of Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 81 (15), 4622-4626 (1984) PubMed: 6379647 Griffin,T.J. IV. and Kolodner,R.D. Purification and preliminary characterization of the Escherichia coli K-12 recF protein J. Bacteriol. 172 (11), 6291-6299 (1990) PubMed: 2228960 ","","Mon Nov 25 17:12:25 2002","1","","","" "AA00004","4355","3603","753","ATGGGTAAAGAAGAAGTCGGCCATAATTTTTTAGCGCGTTTAGGTAAAACCCGTTTACGTCCGGGCGGTCGTAAAGCGACGGATTGGTTGATTGCCAGTGGTGATTTTAGCCAAGATAAAAAGGTGCTGGAAGTGGCATGTAATATGTGTACCACGGCAATTGGGCTGGCGAAGCAATACGGTTGCCACATTGAAGGCGTGGATTTGGATGAAAACGCGTTGGAAAAAGCTAAAGCCCATATTGTGGCGAATAACTTGCAGGATAAAATTCATGTACAACGTGCCAACGCCATGAAATTGCCTTTTGAAGATGACACGTTTGATATTGTGATTAACGAGGCGATGCTCACCATGTTACCGGTGGAAGCCAAAATGAAAGCGGTTGCCGAATATTTTCGTGTGTTAAAACCGGGTGGTTTTTTGCTTACCCATGATGTTATGTTGGTAGGGGATGATCACCAGACGATTTTAAACAATATGCGCGATGCCATTAATGTCACGGTCACACCGCTTACCAAAGACGGCTGGAAAAAGATCTTTACCGACAGTGGATTCCGTAATGTTGAAACCTTCTCCGGCGAGATGACGTTGCTGTCACCGAAGGGTATGATTTATGACGAAGGCGTGTTTGGTGCGTTGAAAATCATTAGAAATGCCATGAAAGCGGAAAATCGCGAGCAGTTTAAGAAAATGTTTAAGACCTTTAATGATCCTGAACATAAATTGCATTTTATTGTGGTTTGCAGTCAGAAA","","","28191","MGKEEVGHNFLARLGKTRLRPGGRKATDWLIASGDFSQDKKVLEVACNMCTTAIGLAKQYGCHIEGVDLDENALEKAKAHIVANNLQDKIHVQRANAMKLPFEDDTFDIVINEAMLTMLPVEAKMKAVAEYFRVLKPGGFLLTHDVMLVGDDHQTILNNMRDAINVTVTPLTKDGWKKIFTDSGFRNVETFSGEMTLLSPKGMIYDEGVFGALKIIRNAMKAENREQFKKMFKTFNDPEHKLHFIVVCSQK","3603","","conserved hypothetical protein (possible methyltransferase)","Cytoplasm","","
InterPro
IPR013216
Domain
Methyltransferase type 11
PF08241\"[43-143]TMethyltransf_11
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[24-237]Tno description
PTHR10108\"[38-190]TMETHYLTRANSFERASE
PTHR10108:SF17\"[38-190]TUBIE/COQ5 METHYLTRANSFERASE


","No hits to the COGs database.","","Residues 9 to 206 match (6e-09) PD:PD074450 which is described as PLASMID MCCD ","","","","","","","","","","","","Tue Nov 26 08:40:15 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00004 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00007","4543","5115","573","ATGAAAATCAAAACTATTTTAGCCATAGTAATCGGCACAATCTGTTCTGCAGGCATTGCTAATGCTCATGAACATAAGCATGACAACATGATGATGCCTCTTAAAGGACCATCTATTGAAGTTAAAATACAGCAATTAGATCCGGTCAACGGCAACAAAGATGTGGGTACGGTCACTATCACCGAATCCAGCTACGGCTTGGTATTCACCCCAAATTTAAAAGGCTTGGCGGAAGGTTTGCACGGTTTCCACATTCACCAAAACCCAAGCTGTGAACCAAAAGAAAAAGACGGCAAACTTACCGCAGGTCTTGGCGCAGGCGGTCACTGGGATCCGAAAGACACCAAACAACACGGCTACCCATGGCAAGATGACGCCCATTTAGGTGATTTACCGGCATTAACCGTATTACACGACGGCACAGCCGCTAACCCGGTTTTAGCCCCACGCATTAAACACTTAGACGACGTGCGCGGTCACTCCCTCATGATCCACGCTGGTGGCGATAACCACTCCGATCACCCGGCCCCACTTGGCGGCGGCGGTCCGCGTATGGCGTGTGGTGTAATTAAA","","","20211","MKIKTILAIVIGTICSAGIANAHEHKHDNMMMPLKGPSIEVKIQQLDPVNGNKDVGTVTITESSYGLVFTPNLKGLAEGLHGFHIHQNPSCEPKEKDGKLTAGLGAGGHWDPKDTKQHGYPWQDDAHLGDLPALTVLHDGTAANPVLAPRIKHLDDVRGHSLMIHAGGDNHSDHPAPLGGGGPRMACGVIK","5115","","superoxide dismutase [Cu-Zn] precursor","Periplasm","","
InterPro
IPR001424
Domain
Superoxide dismutase, copper/zinc binding
PD000469\"[127-191]TSODC_NEIMB_Q59623;
G3DSA:2.60.40.200\"[40-191]Tno description
PF00080\"[41-191]TSod_Cu
PS00087\"[82-92]TSOD_CU_ZN_1
PS00332\"[179-190]TSOD_CU_ZN_2
noIPR
unintegrated
unintegrated
PTHR10003\"[72-190]TCU/ZN SUPEROXIDE DISMUTASE
PTHR10003:SF11\"[72-190]TSUPEROXIDE DISMUTASE [CU-ZN]
signalp\"[1-22]?signal-peptide
tmhmm\"[5-23]?transmembrane_regions


","BeTs to 8 clades of COG2032COG name: Cu/Zn superoxide dismutaseFunctional Class: PThe phylogenetic pattern of COG2032 is ------yq-dr-b-e-gh-n-j----Number of proteins in this genome belonging to this COG is 1","Significant hit ( 5.2e-26) to 2/2 blocks of the IPB001424 family, which is described as \"Copper/Zinc superoxide dismutase\". Interpro entry for IP:IPR001424. IPB001424A 66-107 2.2e-11 IPB001424B 151-186 3.4e-13 IPB001424A 90-131 0.67","Residues 41 to 191 match (6e-72) PD:PD000469 which is described as COPPER DISMUTASE ZINC OXIDOREDUCTASE SUPEROXIDE CU-ZN PRECURSOR SIGNAL CHLOROPLAST PROTEOME ","","","","","","","","","","","Tue Nov 26 09:16:45 2002","Tue Nov 26 08:48:46 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00007 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 41 to 191 (E-value = 8.7e-61) place AA00007 in the Sod_Cu family which is described as Copper/zinc superoxide dismutase (SODC) (PF00080)","","","","Kroll,J.S., Langford,P.R., Wilks,K.E. and Keil,A.D.Bacterial [Cu,Zn]-superoxide dismutase: phylogenetically distinctfrom the eukaryotic enzyme, and not so rare after all!Microbiology 141 (Pt 9), 2271-2279 (1995)PubMed: 7496539Langford,P.R., Loynds,B.M. and Kroll,J.S. Cloning and molecular characterization of Cu,Zn superoxide dismutase from Actinobacillus pleuropneumoniae Infect. Immun. 64 (12), 5035-5041 (1996) PubMed: 8945543","Forest,K.T., Langford,P.R., Kroll,J.S. and Getzoff,E.D. Cu,Zn Superoxide Dismutase Structure From A Microbial Pathogen Establishes Class With Conserved Dimer Interface J.Mol.Biol. 296, 145 (2000) Kroll,J.S., Langford,P.R. and Loynds,B.M. Copper-zinc superoxide dismutase of Haemophilus influenzae and H. parainfluenzae J. Bacteriol. 173 (23), 7449-7457 (1991) PubMed: 1938942 ","Tue Nov 26 08:55:19 2002","Tue Nov 26 08:55:19 2002","1","","","" "AA00008","5172","5555","384","TTGAGGTGCAGATTATGTCTTACTCTTATCAATTTCGTTAAAAAACTATCAAACAGGTCACCGAGCAGGATTTTGGTATCCGTGAGGTGGCTAAATTTCATCAGATTTCTCGTTCTCAAGTCATTTATTGGAAAAGCCTTTCGTGAAAGAGGGCTTAATGGCGTAAAATCCCCTTATATAAACCCTCAACGCCCTAAAATAGTGAAGCCAAAGATGAAAAAGAAAGCGATTGAAATCCCGGAACAAACAGACTTTTCCCCAAAAGCGTTTAAAAAGCTGCAACGAGAGCTGGCATTAGCACGTGCACAGATTGCTTACCTAAAGGAGTTGGAGGCACTCGACCGTCAAAAACAGCGACAGAAAAAAGAAAAATCATTGAAAGAT","","","15047","LRCRLCLTLINFVKKLSNRSPSRILVSVRWLNFIRFLVLKSFIGKAFRERGLNGVKSPYINPQRPKIVKPKMKKKAIEIPEQTDFSPKAFKKLQRELALARAQIAYLKELEALDRQKQRQKKEKSLKD","5555","","hypothetical protein (possible transposase fragment)","Periplasm, Cytoplasm","There are no significant matches to the NR database. A weak similarity (.009) is found to gi28867363, a predicted transposasesequence.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sat Feb 21 10:34:25 2004","Mon Feb 23 08:20:55 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA0348, a hypothetical protein, and to AA0834, a transposase fragment.AA00008 is paralogously related to AA02115 (4e-69), AA01289 (4e-69), AA01075 (4e-69), AA02340 (2e-66), AA00535 (1e-22), AA01267 (4e-18), AA00631 (1e-13), AA00227 (2e-11), AA01404 (6e-11) and AA01549 (0.001).","Sat Feb 21 10:34:25 2004","","","","","","","","","","","","","1","","","" "AA00009","5732","5854","123","ATGGGTTTCCATTTGAATCATAAAACGGTGTTAAAACTGATGAATGCGTTAGGTATTCATTCTATTTTACGCAAGAAAAGACATGGAAAACGAGGAAAACATCGCATATTGCCCCGAATGTGC","","","4810","MGFHLNHKTVLKLMNALGIHSILRKKRHGKRGKHRILPRMC","5854","","hypothetical protein (possible transposase fragment)","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sat Feb 21 10:43:18 2004","Sat Feb 21 10:40:57 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This seqeuence is paralogous to AA0945 and AA0835, transposase orfB fragments.AA00009 is paralogously related to AA02341 (1e-20), AA02116 (1e-20), AA01288 (1e-20), AA01076 (1e-20), AA01444 (3e-12) and AA01268 (3e-12).","Sat Feb 21 10:43:18 2004","","","","","","","","","","","","","1","","","" "AA00010","5851","6357","507","GTGCTAAATCGTGATTTTACAGCGACGGCGCTCAATCAAAAATGGGTAACCGATGTCACTGAGTTTCGAGTTGGGGAAGAAAAGCTCTATTTTTCACCGTTGATGGATTTAGCGAACCGGGAAATTATTGCCTATAATTTTGCGAAACGCCCTAAGTTCTCATTGGTAAAAAGAATGCCGGAAGAAGGACTTGGCAAACTAAAACCGAGCGAATGCCCGATTATTCACAGCGACCAAGGGGTATTGTACGGCTCAGCAGAATGGGTAAAGATGTTGGAAGGCAAGGCGATACAAAGTATGAGTCGCCGAGGGAATTGCTATGATAATGCGGTGATTGAAAGCTTTTTTGCGATATTAAAATCTGAGTGTTTTTACTCACGCACTTATACTTCGATTGCCGAATTACAGGCGGAAATTGAAGAATATTTGGTGTATTACAACCAAGAACGAATTAAACTTGATTTAAAAGGATTAAGCCCGGTGCAATACCGAGCTCAATATTTAAGT","","","19548","VLNRDFTATALNQKWVTDVTEFRVGEEKLYFSPLMDLANREIIAYNFAKRPKFSLVKRMPEEGLGKLKPSECPIIHSDQGVLYGSAEWVKMLEGKAIQSMSRRGNCYDNAVIESFFAILKSECFYSRTYTSIAELQAEIEEYLVYYNQERIKLDLKGLSPVQYRAQYLS","6357","","transposase orfB fragment","Cytoplasm","This sequence is similar to gi28872132, an ISPsy9, transposase OrfB sequence from Pseudomonas syringae. Numerous similarities are found to other transposase orfB fragments.","
InterPro
IPR001584
Domain
Integrase, catalytic core
PF00665\"[7-165]Trve
PS50994\"[7-168]TINTEGRASE


","BeTs to 10 clades of COG2801COG name: Putative transposaseFunctional Class: LThe phylogenetic pattern of COG2801 is ---p-----drlbcefgh-n-j---wNumber of proteins in this genome belonging to this COG is 5","","Residues 55 to 114 match (3e-09) PD:PD001459 which is described as TRANSPOSASE COMPLETE PROTEOME PLASMID ORFB IS629 INSERTION ELEMENT SEQUENCE FOR ","","","","","","","","","","","","Sat Feb 21 10:47:26 2004","Sat Feb 21 10:52:43 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogously related to AA1522, AA0945, AA0845, AA0835, AA0709, AA0006, AA1371, AA1578, all transposase related.AA00010 is paralogously related to AA02342 (1e-95), AA01444 (1e-95), AA01287 (1e-95), AA01268 (1e-95), AA01077 (1e-95), AA02117 (2e-89), AA00145 (2e-23) and AA02420 (4e-17).","Sat Feb 21 10:52:43 2004","","","","","Residues 7 to 165 (E-value = 5.6e-31) place AA00010 in the rve family which is described as Integrase core domain (PF00665)","","","","","","","","1","","","" "AA00012","6839","6573","267","TTGAATAGGCTACTCAAAATGAACATCAATCTAAATCACGGAGAAATCAACAAACGAATTGGCAAAGCCATTGCCAAACAGCGCCAACAAAGCGGCTACACGCAGGAACAGGTGGCGGAAATGCTGGAAATCGGCAACGAAGCCGTCTCGCGCATGGAGCGCGGTCTGATTATGCCCAACGTGGTGCGCTTAATCGAACTGGCGGAAAAAGACCGCCAACTGATGCTGGATTTTCTCGACAGCTTCGCTCGGCGGCTGAAACAGGAG","","","10347","LNRLLKMNINLNHGEINKRIGKAIAKQRQQSGYTQEQVAEMLEIGNEAVSRMERGLIMPNVVRLIELAEKDRQLMLDFLDSFARRLKQE","6573","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR001387
Domain
Helix-turn-helix type 3
PF01381\"[24-69]THTH_3
SM00530\"[23-81]THTH_XRE
PS50943\"[24-78]THTH_CROC1
noIPR
unintegrated
unintegrated
G3DSA:1.10.260.40\"[9-69]Tno description


","BeTs to 12 clades of COG1396COG name: Predicted transcriptional regulatorsFunctional Class: KThe phylogenetic pattern of COG1396 is --m----qvdrlb-efghsn-jx-t-Number of proteins in this genome belonging to this COG is 3","","","","","","","","","","","","","","Tue Nov 26 10:07:03 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00012 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 24 to 79 (E-value = 2.4e-09) place AA00012 in the HTH_3 family which is described as Helix-turn-helix (PF01381)","","","","","","","","1","","","" "AA00013","6951","6835","117","TTGAACGGGAAATCCCCATTCTTATTCTATACCAAACTTTATAGGTTGACTAAACATATTAAAAAGTCCTTAATTCGGTCAAAAAAATTCGCCATTATTTCAACCTTTAAAGTTGAA","","","4628","LNGKSPFLFYTKLYRLTKHIKKSLIRSKKFAIISTFKVE","6835","","hypothetical protein","Cytoplasm","No sequence similarity found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sat Feb 21 10:48:48 2004","Sat Feb 21 10:48:48 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA00013 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sat Feb 21 10:49:47 2004","","","","","","","","","","","","","1","","","" "AA00015","6972","8393","1422","ATGAGCAAAACCCCTGAAATTCTGCAAAACCCGCTGACCAACAAAGGCACGGCGTTTACCGCCGAAGAACGAAAAAAATACGGCTTGACCGGACGCCTGCCCGCAGCGGTGGAGACTCTCGACCAGCAAGCCGCGCGCGCCTACCGCCAATTCTCTTCTTACGCCGAAGATATTGAAAAATATATTTTTCTCGACCAACTGCACAACCGCAACGAAGTGCTGTATTACAAACTGCTGACCGACCATTTGGCGGAAATGCTGCCGATTGTGTACGACCCGACCGTGGGCGAAGCGATTAAAAAATGGAGTCGCGACTACCGCCGTTCGCGTGCGGTTTATTTGGATATCAACCATCCCGAAGCCATCCGTGAATCCTTTGAAACCTTGAGATTGGGTGCGGACGATGTGGATCTGATTGTGGTGTCGGACGCGGAAGAAATCCTCGGCATCGGCGACTGGGGCGTGAACGGTACAGATATTTCCGTCGGCAAGCTGGCGGTTTACACTGCTGCCGCAGGGATTGACCCCGCCCGCGCCATTGCCGTGAACCTTGATGTCGGCACAGATAACGAAGCCCTGCTCAGCGATCCCGCATATCTCGGTAACCGCCATGCCCGCGTGCGCGGCGAACGCTACGACGCGATGATTGCCGAATACCTGAAAACAGCGGCGGAACTGTTCCCGAATGCGCTGCTGCACTTTGAAGATTTCGGTCCGTCCAATGCTCGCCGCATTTTGGTGGAAAACCGCGACCACTACCGTATTTTCAACGACGATATGCAGGGGACGGGCGCGATTGTGATGGCGGCAGTATTCTCCGGATTGAAAGTAACCAAACAAAACTTTGCCGAACAGCGTCTGGTTGTTTATGGCGCGGGTACGGCGGGTACGGGCATGGCAGACCAAATCAGCGCGGCAATGCAGCGCGACGGACTGTCCCGCGAGGAAGCCAAAAAACGCGTATGGCTGATAGACATCAACGGCTTGGTTACCGACGATATGCCGAACCTGCCGGATTATCAGCAGGAATATGCCCGCCCCGCTGCCGAAGCTGCCGCGTGGGCGAAAACCGACGGCAAAATCGGCTTATTGGAAGTGGTCAAACAGGTCAAACCGACCATTTTAATCGGCACATCCACCGATCACGGCGCGTTTACTGAAGATGTGGTGAAAGCCCTGTGTGCGGGCGTTGAACGACCTATTTTGCTGCCGCTGTCTAATCCGACGGAGAGAATCGAGGTCATGCCGACCGACGCGGTTCAATGGTCTGACGGTAAAGCGTTAATTTCTGTCGGTATTCCTGTTCCGCCTGTTCCTTATAAAGGCGTGAACTACCAAATCGGACAAGCCAACAACGCCATGCTTTATCCGGGCTTAGGTTTGGGCGTGATCGTCTCCGGCGCGAAACAGGTTACCGACTGT","","","51961","MSKTPEILQNPLTNKGTAFTAEERKKYGLTGRLPAAVETLDQQAARAYRQFSSYAEDIEKYIFLDQLHNRNEVLYYKLLTDHLAEMLPIVYDPTVGEAIKKWSRDYRRSRAVYLDINHPEAIRESFETLRLGADDVDLIVVSDAEEILGIGDWGVNGTDISVGKLAVYTAAAGIDPARAIAVNLDVGTDNEALLSDPAYLGNRHARVRGERYDAMIAEYLKTAAELFPNALLHFEDFGPSNARRILVENRDHYRIFNDDMQGTGAIVMAAVFSGLKVTKQNFAEQRLVVYGAGTAGTGMADQISAAMQRDGLSREEAKKRVWLIDINGLVTDDMPNLPDYQQEYARPAAEAAAWAKTDGKIGLLEVVKQVKPTILIGTSTDHGAFTEDVVKALCAGVERPILLPLSNPTERIEVMPTDAVQWSDGKALISVGIPVPPVPYKGVNYQIGQANNAMLYPGLGLGVIVSGAKQVTDC","8393","","malate dehydrogenase","Cytoplasm","","
InterPro
IPR001891
Family
Malic oxidoreductase
PR00072\"[74-98]T\"[136-165]T\"[172-194]T\"[231-249]T\"[256-272]T\"[287-303]T\"[397-413]TMALOXRDTASE
PIRSF000106\"[1-473]TMalic enzyme
PS00331\"[256-272]TMALIC_ENZYMES
InterPro
IPR012301
Domain
Malic enzyme, N-terminal
PF00390\"[68-258]Tmalic
InterPro
IPR012302
Domain
Malic enzyme, NAD-binding
PF03949\"[260-473]TMalic_M
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[260-473]Tno description
PTHR23406\"[33-473]TMALIC ENZYME-RELATED
PTHR23406:SF2\"[33-473]TMALIC ENZYME


","BeTs to 19 clades of COG0281COG name: Malic enzymeFunctional Class: CThe phylogenetic pattern of COG0281 is ao-pkzy-vdrlbcefghsnujx---Number of proteins in this genome belonging to this COG is 1","Significant hit (5.8e-165) to 10/11 blocks of the IPB001891 family, which is described as \"Malic enzymes\". Interpro entry for IP:IPR001891. IPB001891A 7-35 4.2e-13 IPB001891B 67-111 4.4e-25 IPB001891C 139-174 7.8e-21 IPB001891D 176-228 6.5e-21 IPB001891E 234-284 6.5e-20 IPB001891F 291-300 0.00091 IPB001891G 319-330 0.0033 IPB001891H 363-393 1.8e-16 IPB001891I 398-438 5.2e-16 IPB001891J 441-474 9.7e-14","Residues 260 to 458 match (4e-55) PD:PD001213 which is described as OXIDOREDUCTASE ENZYME MALIC COMPLETE PROTEOME MALATE NADP-DEPENDENT NADP NAD NADP-ME ","","","","","","","","","","","","Tue Nov 26 10:36:46 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00015 is paralogously related to AA00066 (2e-08).","","","","","","Residues 260 to 473 (E-value = 1.5e-68) place AA00015 in the Malic_M family which is described as Malic enzyme, NAD binding domain (PF03949)","","","",""," Eaton P, Shattock MJ. Related Articles, Links Purification of proteins susceptible to oxidation at cysteine residues: identification of malate dehydrogenase as a target for S-glutathiolation. Ann N Y Acad Sci. 2002 Nov;973:529-32. PMID: 12485922Mahajan,S.K., Chu,C.C., Willis,D.K., Templin,A. and Clark,A.J. Physical analysis of spontaneous and mutagen-induced mutants of Escherichia coli K-12 expressing DNA exonuclease VIII activityGenetics 125 (2), 261-273 (1990)PubMed: 2199308Lapidus,A., Galleron,N., Sorokin,A. and Ehrlich,S.D. Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB regionMicrobiology 143 (Pt 11), 3431-3441 (1997)PubMed: 9387221","","Mon Feb 17 15:11:28 2003","1","","","" "AA00017","8499","10331","1833","ATGTCATTCGTAAATAAACTTACCATAAATGAAGTCACCTACGAACCTTATGACGGTTTCTGTCCTGATTTTTCAGCATATTTCAACAAACTCAAATATCCTGATAACCACAAAGAATTAAATCCAAAACCTACACCACCAATTCAAGGTAGCAGTTGGTATTTCCCTTCTTATGAATATATCGTTGTTTGGTACGACAGTAACTTTATCTTTCATCAAAAGAACTCTCAGGTATACGTCAAGATTAAATTAGTAAATCTAAGAAACCCTACCTATAAAAAAGGAGAACTTACCTATTTAAGTGTTCTATACATTACTGTGCCTATTAATATTCTTCATTACTTCTTTATCGGTAGCGTTTGGAAAGAAGGTAAGCCGATAAAACAAGTAAAACTTAAAGAGTACCTTGTTACAGCTAATCAAGCATTTGAGGGGAAAAGAGATAACGTAAGTTATCAGCCTTTCTATGATAAAGAAAAACACAAATACAACAAACCATTCTCGCCGAATTTATACACAATTGAATCGGATCGTAACAACTACAAATACGATCAGAATCAACTTGTTAAAATTAAGCAAAATGGCAGAGATTTTATTATTCATCCATTACATCTTTTCTGCTCTCATTATGGGTTATCGTCAGATATAAAAAGAATTTTAACAGCCTACAATTGGGATGAGGTTAAAAGTCGCCTTCATTTAGATGAGAATGAGCCATCTTTATATCCTGAAAAGCACGTTGTTCTACCAAAACATTTTGTGAAGAAAGACGCAATTTTCCTTTACCATCTAAAATATGATAATGCAGTCGCACTATCTCGAACTAAGTCTCTTAATAATGAAATCAAGTTTTCAAGCGAAAACCAGAAGCCTGTAAAGGTTCCATTTTGGCACGACCAAGAGGTACAGCTCAAAATTCGCGGTATTGAATTAGATGATATTGTTTTATGTGCGGAAATTGTAGGAATAAACCAACCTATTGGCGATGATATTACTCTTGTATTGCATCATACTAAAAAAGTAGATGAAGAAAATTCCCAATCAAGTGGAAATAAAAAAGCCATTATCAAAACGTATAAAAGAGACGTAAATACAGAATATCTTGGTACTAAAATTATAGATGGAGAACCTGATAACAGGACATCACAAAGTATCAAAAAGAGATTTGAAGAGTTAGGGCGAAAAAGAATTATTAACACGATTAATATCCAAAACCAGAATAGTAATTCTCATCAAACTAAAGGAATACAGCCTAAAGAAATCTGTGAACTAGGGTTTGGCGATCACTATGGTAAGGAAGGCAAGGTCGGATTGGTTGTTTGTTTCCTTGATAGCGAGAGTGAAAATAAAGATATAAAGCTCTTTCGCCTTTGGGATATGGCACAAGATTTTGCTTTACTAAATGGCGGACAGGCACACTGGTTTACCCCTAAACTAGGTTTCCGAAATGATGATAATTTAGTATTTCTCTCATTAGAGAATGATACTGCATTTGCCTATCCTGAAATCGCATTGGTGATTCGTATCATACTGGGCGATGAAACATTTTACATTGTAGATTTTTCCCAAAAATCGCACGACATTTCAATGAGCGGCATTGCTTATAAACAAAGTAATGGGGAAGATTTCATAACACTAAATGATATTCAGGGCAGTAAGTTGGCGGAAATAATCAGTGAAGTAGTTACTTCAGAACAACTACCGACTGAATATATTTTGCAGCAGAATGAGAAAGAAATGAAGATTGCCACTTTCAGGCATCCATCGGCGGAAAGTAGTAACTGGGTATTTAACGCAATTAGTAAGCTCACACACAAAACATTATCTAAATTT","","","70936","MSFVNKLTINEVTYEPYDGFCPDFSAYFNKLKYPDNHKELNPKPTPPIQGSSWYFPSYEYIVVWYDSNFIFHQKNSQVYVKIKLVNLRNPTYKKGELTYLSVLYITVPINILHYFFIGSVWKEGKPIKQVKLKEYLVTANQAFEGKRDNVSYQPFYDKEKHKYNKPFSPNLYTIESDRNNYKYDQNQLVKIKQNGRDFIIHPLHLFCSHYGLSSDIKRILTAYNWDEVKSRLHLDENEPSLYPEKHVVLPKHFVKKDAIFLYHLKYDNAVALSRTKSLNNEIKFSSENQKPVKVPFWHDQEVQLKIRGIELDDIVLCAEIVGINQPIGDDITLVLHHTKKVDEENSQSSGNKKAIIKTYKRDVNTEYLGTKIIDGEPDNRTSQSIKKRFEELGRKRIINTINIQNQNSNSHQTKGIQPKEICELGFGDHYGKEGKVGLVVCFLDSESENKDIKLFRLWDMAQDFALLNGGQAHWFTPKLGFRNDDNLVFLSLENDTAFAYPEIALVIRIILGDETFYIVDFSQKSHDISMSGIAYKQSNGEDFITLNDIQGSKLAEIISEVVTSEQLPTEYILQQNEKEMKIATFRHPSAESSNWVFNAISKLTHKTLSKF","10331","","hypothetical protein","Outer membrane, Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Dec 9 09:12:43 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00017 is paralogously related to AA00427 (5e-71).","","","","","","","","","","","","","","1","","6","" "AA00018","10690","11817","1128","ATGAAATGGAAGCTCAATAATATAACAATGATTATGAATAATCAAACTGATAAGGATTATAGATTACAACAGCTATTTGAAAATAAACATGAATTTGGCGTACCTTGCCATGAATTTATTTTACCCTTTGACGAGACCTTTAGAAAGAGTGCATATCAGATATTTAAATGTTTTATTGAAAACCCTCTAGATAACAATGCTATTTCCCTTTTGTTGAAAGGAAAGGAAGGTTATCGCCGCACAGAAGTATTGGATATTTTAGGATTTAAAAAATGGATTATTGTGTCAGACTACGTTTTTGATAAAAATAAGCCACAAGATGTAATTACATTTTCAATAATGCCATACGTTAAAGACTTTAATGAACTTAAAAACAAAATTAACACCTTACAAAAGAAAGATATTAAGCATTCTGACTCAATAAACCCTGAATTCATAAAGTTTTTTCAGGAATTTCCAATTTTCAATATATCCATCTCAATAAACAAGAAATTTAAATTATTTACTGACGAGAAGTTTTTCTCAAACCAACAAATTTCAGCATACATAAAACAAATAAATCATTGGATTGAGAATGAGAAAAGTATTGAAAAATATATAAAACAAAAAAAGACATTAATTAAGCTATTAGAAATATTTAATAAGAAAGATCCTAGCTTTAAAGAAATAAGAAGAATATTCTTTATTGGTGCGATTACTACGTATTTAATGTACCTAATAACTAGTCTTATACCAAAATTAGAAGTTATAGGTTGGTTTTCGGATAGAGATACTATTATATATTACAAAGAGAAAGAATTGGGCGGATGTTTGATATTTCAATATATTCAAGATTTGTACCATGCTTTTTGTGGATCAAAAAATCTAAGACAATCAAGCATAGCTTTTGGATTACCAGAGGAACAGGGGGAAATGTGGTTTGATGAATTAGTGAGACTACCTGATTTCATTGCAGGAACGCTAGCTGATTATAATAAAGAAGAAAATGAATTTTCTCATGATAAATTCATTCCTTTATTTGAAAAAGTATTTACAAATGAAAATAAAAATTTAATATTTAATGTTTTTATTGGAAAAAACAATAACAACTTTGAAATGAGAGTAAATAGAGCAACTTTCGACAAAATA","","","46017","MKWKLNNITMIMNNQTDKDYRLQQLFENKHEFGVPCHEFILPFDETFRKSAYQIFKCFIENPLDNNAISLLLKGKEGYRRTEVLDILGFKKWIIVSDYVFDKNKPQDVITFSIMPYVKDFNELKNKINTLQKKDIKHSDSINPEFIKFFQEFPIFNISISINKKFKLFTDEKFFSNQQISAYIKQINHWIENEKSIEKYIKQKKTLIKLLEIFNKKDPSFKEIRRIFFIGAITTYLMYLITSLIPKLEVIGWFSDRDTIIYYKEKELGGCLIFQYIQDLYHAFCGSKNLRQSSIAFGLPEEQGEMWFDELVRLPDFIAGTLADYNKEENEFSHDKFIPLFEKVFTNENKNLIFNVFIGKNNNNFEMRVNRATFDKI","11817","","hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
tmhmm\"[226-244]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Dec 9 09:13:21 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00018 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","6","" "AA00019","11839","12882","1044","ATGCTAAATAAACTGAATAAAATAAAGCAACGAGAAACATCAGGTAGCGATACATTTAAAAACTATGACTATCAGTATCACTGGGCTATCTACACTCTTTTAGAGAACTCAAGAGAAAATGATGATATAGCTGTTCTAGTTGAATTTCACGAAGATGTCATTCTTGTAGAAAATGTATCTTCAGAAAATAATCAATTTCATTTCTTTCAAATTAAAGCAAATGATAAAAGTTTAACATTAAGTGACATACTCAGAAAAGAAAATGGGAATAAGTCTATTTTAGATAAATTAACATTAGGAAAAGAATACTTAGAAATATTAGATAATATAAAATCTATCAAATTAGTATCTGCAAACGGATTTTCCTCTAAATTTTGTGCTAATGAATCCAACTTTTATGAACTATGTGACAAAGATAAGAAAAAAATAGAAGACAATCTAATGCTTGAAATAGATAAAAACTCTTTTTTAAGTAAACTTTATTTTTCTAAATCAAAGCTACCGAAAATAGGATTTATTCAAACTGTAAAAGGAATATTATCAGAAATTATTCAGGAAATTCACCCCGATAAAAGAACAAATGTGAATGCTATTTATCTTGTTCTAAAAGATGACTTACACGATAAAGGAAAAAAGAGACTAACTGATAAAGAAGATCCACTGCAAGAAAAAGGAATGACCTTTTCTACTGTAAAAGAAGTAATCAACCGCTATACAGATATAGAAGATGACAATCTGACATCGGTATTAGATATGCTTAATAATACCTCTTACGCTATAATCGAAAAACAAAAGATAAAGAAAGAGTTATTAAAATATAGTACACATCATTTAAACTCAGGAAGTATTCAAGCTCAAATAAAATTAGATATATTAAACTCTAACATACTTGATGATTTGATGTGTAGTAACAATAAACAACTTACTGAAATAATTAATAATTTCTGTTCAACTTTAGAATTAAAGTATGGTACTATAAGTACTGTTCAAATGATCAAGTCAGGGGTGTTATATGAGTTATCGAGATACATTAGAGAAACAGCG","","","40202","MLNKLNKIKQRETSGSDTFKNYDYQYHWAIYTLLENSRENDDIAVLVEFHEDVILVENVSSENNQFHFFQIKANDKSLTLSDILRKENGNKSILDKLTLGKEYLEILDNIKSIKLVSANGFSSKFCANESNFYELCDKDKKKIEDNLMLEIDKNSFLSKLYFSKSKLPKIGFIQTVKGILSEIIQEIHPDKRTNVNAIYLVLKDDLHDKGKKRLTDKEDPLQEKGMTFSTVKEVINRYTDIEDDNLTSVLDMLNNTSYAIIEKQKIKKELLKYSTHHLNSGSIQAQIKLDILNSNILDDLMCSNNKQLTEIINNFCSTLELKYGTISTVQMIKSGVLYELSRYIRETA","12882","","conserved hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","Residues 10 to 254 match (2e-14) PD:PD571555 which is described as PHAGE PROTEOME COMPLETE ","","","","","","","","","","","","Tue Nov 26 10:43:50 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00019 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","6","" "AA00020","12939","14546","1608","ATGAAAAGACTAATAATTAAGCAATTAGCTATTCTTTCTAAAGATAAAGATGCGGGAAACCTATTTACTTTTAGTGATGGAGTGAACTTTATTCTATCTGATAAAAACTCAGCAGGAAAAACTACACTATTGAACTTAATGTATAGTGCATTAGGCTGTGTAGTAAAATTTAAAAATGAATGGATCAATTCATTTATTAGATTAGATATAGCTATTGAAGGGAACTCTTACTCTCTGTATAAAACACCAAATGAAATATATTACATACACGATGAAAAAGATTTAGTAAAATATGAAAATGAATCAGATTATCATAAAAGACTATCTGAAATTTTAGGATATAAAATATACCTAAAAGTTCATTCAGGTACTCCTAAACTTGCTAGACCTGCCCATTTTTTCTTAACCAGCTATATCTCTCAAGCTAAAGGGTGGAATTCCTTTTTCCCAAATTCATTTGAAAAACTAGGGGAATTTAGAGCGTTTCAGCCTGATCTAGTAGAACAATTCTGTAAAGTAAAAAGTGATAAAGAATTAGAAAACGAAGAAGAATTCAATAGAGTTAAAGATAATTTAAAACAAAAAACTAATGAAAAACAAGTTCTGAATTTAACTAAAGAAAATCTTGAGAAAGAAACTAATTTCGACATTAATAAACTTAAAGAAAATGTTGAAAATTATGAGAAAAGCTTAAATCTATTACAAGATGAACTATCAAATTTAGTTGTTGAACGACAATTTTTACTTAATGAAATAAATTTTGTTACTCCAACAGTTAAAGAGGTTGATGAAGATTACCAAGAAGCTCGTATGCATGGAGCTAAAATAGAATGCCCTTATTGCGGTACAATTCACTCTAATACAATTACAGAAAAATCAGAGTTATTTTTCATAAAAACAAAATTAGAAGATGAATTAATCAATAATCAATCTCGCATAAAGGAAATTGACATAAAAATATCAGAAACAGAAATAAATATAAAAGAATTATCAGAGCTTAAATCAGGCATAGATCATCTTATTAGCGATAACACAAAACACTTAAGAAAAGCTATAACAGCAAATGAAATATTTGGAATAATAAGTGATTTAGAAAATGAAATAACACAATTAGAAAAACGCAAAAAATCTATAAATAAAATAAAGAATAGGAATAGAAAGGAATATGAAGAACACAGAGAAGCTGTTAATGACTTCTTCGTCACTAAGTTAAAATATTATGCTGATAGATTATCTATTGTGTTTAATAATTATGACGAAATCCAAAAGGTTACTGATTACAATAAAGTTTTAAATGCGGTTAAAGGTGGGGCTGCCGATAGTAATCGGACTGTTTTAGCATACTATTTAGCTATTTATGCTACTGCAATAAATTTTAATACTGATATTCTTCCACCTTTAGTACTCGATACTCCTAATCAGAATGAGCAGGATAAAGAGAATTATAAATCTATAATAGATACATTAATAAAAGAAAACAACAAACAGATAATAATCTGTTTAATTAGGAGTGAATATTCAGAAAAATTAAAACCTGTAAATAAAATTGAGGTTAATAGATTAATGAAAATGGGAGAGTATCATAAGTTTTTTGATGAATTAGAGATA","","","62572","MKRLIIKQLAILSKDKDAGNLFTFSDGVNFILSDKNSAGKTTLLNLMYSALGCVVKFKNEWINSFIRLDIAIEGNSYSLYKTPNEIYYIHDEKDLVKYENESDYHKRLSEILGYKIYLKVHSGTPKLARPAHFFLTSYISQAKGWNSFFPNSFEKLGEFRAFQPDLVEQFCKVKSDKELENEEEFNRVKDNLKQKTNEKQVLNLTKENLEKETNFDINKLKENVENYEKSLNLLQDELSNLVVERQFLLNEINFVTPTVKEVDEDYQEARMHGAKIECPYCGTIHSNTITEKSELFFIKTKLEDELINNQSRIKEIDIKISETEINIKELSELKSGIDHLISDNTKHLRKAITANEIFGIISDLENEITQLEKRKKSINKIKNRNRKEYEEHREAVNDFFVTKLKYYADRLSIVFNNYDEIQKVTDYNKVLNAVKGGAADSNRTVLAYYLAIYATAINFNTDILPPLVLDTPNQNEQDKENYKSIIDTLIKENNKQIIICLIRSEYSEKLKPVNKIEVNRLMKMGEYHKFFDELEI","14546","","conserved hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","Residues 1 to 529 match (2e-30) PD:PD576742 which is described as PHAGE PROTEOME COMPLETE ","","","","","","","","","","","","Tue Nov 26 10:47:12 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00020 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","6","" "AA00021","14770","17676","2907","ATGTTCCATCATTTATGTATAGCAATGCACTTCTCTACTATTATGACGGACAATGTAGATTCAGTTATTATCCTGTCTAACTTCTTGGGTAAAATTTTCGGTAAATTCAAACAAGTTGAGCTTCAGCAAGACACTGTGTTATTGACGGGTAAAGACGGAAAAACGAAATCCTATTCTACTTTCCATATTGAAACATTTCCTCAATTTACATCTTCAATTTTAGGTATTCAGTTAAGTTTCTTGTGTGAACAAGAGCTGGTGTCCGTTCGTTTTCTTTCAAAAGCGAATGTAGAACAGTTTTATCAAGGTTTAGAAGAGAAGATTGCACAGAACATACTCAACAAACTCAAACCTGCAATAACAACATTTAATAGACTTGCTAAAAATCAATATCTAAGAGATTCAGATATTCCTTTATTGGAAAGTCAACTTGACCTACTTATTTCCAAGTACATAGAGAACAAAGAAATTCTTCATCGTTATTTTGATAACCAAACGATTCAGGCACTGGACTACATTTGCAATGTTATGCCTGTCGGAAAAATCAAACAAGAGGTTGTTAGACAGGATTATGAGCGAAAACGATTAGTTGAAAGAAATCATTTCTTTGATGTGATTGAATCCAATCCGTTAACTCAACAGCAAAGATTGGCGGTTATTCGCAACAATGACATCAATATGGTTTTAGCTGCTGCTGGAACAGGTAAAACCTCCGTAATGGTCGCAAAAGCATTGGATTTAATTGATTCGGGTGTAGCAACTAGCGAAGAAATTCTTATCCTTGCTTACAATAAAGACGCGGCAACCGAATTAACAGAACGTTTAGAAGCGCGAGCCGAAGCCGCTAATCTTGACTTGAGCGAATCACCAAGTATTTCAACTTTCCACGCTTTAGGACGAAACATTATCAAAAGCTGTGGGAAATCTGTTCGTCTTTCTAAATTTGCCGAAGATTCCGCAAAATTAGATGAATGGTTTACTAAATGGCTTGAGAATTATATTCAAGAGGACCCAGACAATCTACTTTCATTCATTTCATTATCTTATCAGCCGATTGACCCATTTCAGTTTAAAACAAAACAGGAATATGATGCTTATGTACGAGATAATGAGTATCGCACTTTACAAGGTGAACGAGTAAGAGGTTATCAAGAATTACTAATTGCCAACTGGTTCTTTATGAATAATATTCCATATGAATACGAGCCGAGATATGTTTCTAAGCGACGTATTGAGATTGGATTTGATTATAAGCCTGATTTTGGTCTAGGTGACGGGGTTTATCTGGAACATTTTGGTATTGATAGACAAGGAAAAACACGTCCAGATATTGATGCCGTAAAATACAATAATGATATAGTCAGAAAACGCCAGTTACATCAAGAGCATAACACGACATTACTTGAAACCTATCATTATAACTGGACTGAAAACAATCTTTATAAAAGATTAGAACAGCTAATGCACCAACAGTTTATTGCTATTCGTCCGAAAACCGATAAAGAAATAAGGGAAGCACTCGAAAATTCAGGTATTTTTAAAGAAAGTAAAAACAAATACCTCAAATGCTTACAGGCAATTCGCACAGAAAGATTGGACTACACACAAGTATTAAAACGCTTGCAAAAAGCGAATGTAGCTCACGCTAGACAGTACACCGATTTCTTAATGCGTATTCACGACGCTTACGTCAAAAAACTTAATGAAGCACAAGAAATCGACTTCGATGATATGATTTTGCAAGCGACTATGCTAATTAAAAACGGTAGCTTTACACCTAAATGGAAGCATATTCTTGTTGATGAATTCCAAGACATCTCTATGGCGCGTTTAGAGCTATTAAAAGAAATTTACAGTAAAGGACCGCGCCCTATTTGGACAGTGGTAGGCGATGACTGGCAATCTATTTATCGTTTTTCGGGTGGTAAGTTAGAAGTGACCACACAATTTGGAAGAATGATTGGTTCCCACACGTTAAGTAAGTTAGAGAAAACCTACCGCTATAACAATAGTATTGCAAATACCGCAGGACGCTTCATTATGCAAAATCCTGAGCAATACAAAAAAGATATCGAAACGCATACTCAAGTCACCAGCTCGTGTGTTCATCTGTATGATTCCTACGTTTTAAAAGAAGGTAAACGAGAAAGCAATATCAGCCTTAAAGCATTAGAAATCTACAAGCAAATTCGTAAGGAACACCCTGAGGCTTCTATTGCGATTCTAGCTCGATACAGATATTTAATTAAAGAAGCGAGAGATGTTATTAAAGATACCAATGTAAAATTCTGGACGTTTCATGGTTCAAAAGGTTTAGAAGCAGATTATTGTATCTTACTTGGCTTCTTTCAAGGTAAAACAGGTTTTCCGAATAACAATAAAGAAGATACCGTCGTTGAAGCCTTGTTGCCTACGCTTGATAGCTATCCACATTCAGAAGAACGTCGATTGTTCTATGTTGCCTTAACGCGTGCGAAAAAAGAAAGCTATTTAATTGCTGATGCTACTGCATCATCAGAGTTCATCAATGAATTGCTTTCACCGCAATACAGTATCGACATTGTTTCAGAAGGTTTTAAAAATAAATATCGACAAATCTTCAAATGCCCTGTATGCAGCACGGGATATTTTGTGTTGAGAGCTGGTAAATTTGGTAATTTCTATTCTTGTACATCAGGTTCTGTCTGTCGTTCTTCACCTAGAGTATGTGAAAAATGTGGTTCACCTTCCATTGATACGGAGAATACAAGCACCTGTCAAAATCCAAATTGTCGGAATGCTTTCCCTATTTGTGATAAATGTGGTCGCCCTATGCGATTAAGAGAAGGAAAATTCGGCAAATTTTGGGGCTGTTCAGGGTATGGAATTAAAGATGACCCGTGTTCAAATACTCGAAAATATTTCATG","","","112221","MFHHLCIAMHFSTIMTDNVDSVIILSNFLGKIFGKFKQVELQQDTVLLTGKDGKTKSYSTFHIETFPQFTSSILGIQLSFLCEQELVSVRFLSKANVEQFYQGLEEKIAQNILNKLKPAITTFNRLAKNQYLRDSDIPLLESQLDLLISKYIENKEILHRYFDNQTIQALDYICNVMPVGKIKQEVVRQDYERKRLVERNHFFDVIESNPLTQQQRLAVIRNNDINMVLAAAGTGKTSVMVAKALDLIDSGVATSEEILILAYNKDAATELTERLEARAEAANLDLSESPSISTFHALGRNIIKSCGKSVRLSKFAEDSAKLDEWFTKWLENYIQEDPDNLLSFISLSYQPIDPFQFKTKQEYDAYVRDNEYRTLQGERVRGYQELLIANWFFMNNIPYEYEPRYVSKRRIEIGFDYKPDFGLGDGVYLEHFGIDRQGKTRPDIDAVKYNNDIVRKRQLHQEHNTTLLETYHYNWTENNLYKRLEQLMHQQFIAIRPKTDKEIREALENSGIFKESKNKYLKCLQAIRTERLDYTQVLKRLQKANVAHARQYTDFLMRIHDAYVKKLNEAQEIDFDDMILQATMLIKNGSFTPKWKHILVDEFQDISMARLELLKEIYSKGPRPIWTVVGDDWQSIYRFSGGKLEVTTQFGRMIGSHTLSKLEKTYRYNNSIANTAGRFIMQNPEQYKKDIETHTQVTSSCVHLYDSYVLKEGKRESNISLKALEIYKQIRKEHPEASIAILARYRYLIKEARDVIKDTNVKFWTFHGSKGLEADYCILLGFFQGKTGFPNNNKEDTVVEALLPTLDSYPHSEERRLFYVALTRAKKESYLIADATASSEFINELLSPQYSIDIVSEGFKNKYRQIFKCPVCSTGYFVLRAGKFGNFYSCTSGSVCRSSPRVCEKCGSPSIDTENTSTCQNPNCRNAFPICDKCGRPMRLREGKFGKFWGCSGYGIKDDPCSNTRKYFM","17676","","DNA helicase IV","Cytoplasm","","
InterPro
IPR000212
Family
UvrD/REP helicase
PTHR11070\"[222-345]T\"[527-780]TUVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER
PF00580\"[211-345]T\"[513-639]TUvrD-helicase
InterPro
IPR013498
Domain
DNA topoisomerase, type IA, zn finger
PF01396\"[866-901]T\"[930-959]Tzf-C4_Topoisom
InterPro
IPR014016
Domain
Helicase superfamily 1, UvrD-related
PS51198\"[209-669]TUVRD_HELICASE_ATP_BIND
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[208-660]T\"[663-854]Tno description
signalp\"[1-16]?signal-peptide


","BeTs to 21 clades of COG0210COG name: Superfamily I DNA and RNA helicasesFunctional Class: LThe phylogenetic pattern of COG0210 is -omp--yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 3","Significant hit ( 4.8e-36) to 7/7 blocks of the IPB000212 family, which is described as \"UvrD/REP helicase\". Interpro entry for IP:IPR000212. IPB000212A 230-240 0.0017 IPB000212B 258-275 0.25 IPB000212C 600-611 0.27 IPB000212D 629-642 5.3e-06 IPB000212E 662-680 1.3 IPB000212F 761-779 0.00017 IPB000212G 813-825 3.4e-08","Residues 765 to 842 match (1e-13) PD:PD002094 which is described as HELICASE DNA PROTEOME COMPLETE ATP-DEPENDENT HYDROLASE II 3.6.1.- ATP-BINDING DNA-BINDING ","","","","","Wed Feb 19 09:46:49 2003","","","","Wed Feb 19 09:46:49 2003","","","Wed Jan 22 16:17:20 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00021 is paralogously related to AA00527 (3e-14), AA02666 (2e-10), AA02266 (2e-04) and AA02128 (0.001).","","","","","","Residues 211 to 851 (E-value = 6.7e-12) place AA00021 in the UvrD-helicase family which is described as UvrD/REP helicase (PF00580)","","","","","Wood,E.R. and Matson,S.W.The molecular cloning of the gene encoding the Escherichia coli75-kDa helicase and the determination of its nucleotide sequenceand gentic map positionJ. Biol. Chem. 264 (14), 8297-8303 (1989)PubMed: 2542273","","Tue Nov 26 11:34:57 2002","1","","6","" "AA00022","17715","18944","1230","ATGTCAAATAACACATCACCAAATTACATTACTCATTCCTTAGAGTTATTGATAAAAATTGCCGAATACGGCGATGCTAATGCACAAAAAATGCTTGGGTGGCATTACTTAAACGGTTTGGCTATTGAAAAGAATGTAAAACAAGCTTTTATTTGGAACAGTAAAGCTGCAAGACAAAACGATATTGAAGCCTGTTTTATTGTCGGCTGGCATTATGAAAACGGTGTTGGCGTAGAAATCAGTTATAAAGATGCGCTTGAATGGTACGGCAAAGCAGCAAGAAAAGGTCATACCGAAGCTGCACTAAGACTTGCAGAATTGTATTTTTATGGCACTCAAAAAGTTGATGACTATCAATTCAATATCAAAGCTAATTTAGAAGAAGCTATTCATTACTCGGAACCACTCGCTAAAAATGGGAATACCGTTGCACAGCGTATATTCGCACTTTGTCTGATAAAGGAAAAAGACTTTGCAGCGATCCGTTATCTTGGACAAGCAAGCAAACAGGGCGATTTAATTGCCACAGAACGCCTTATTAAAATCTTAGAGAGAATGAATAGTGCACATGATTTAGATCAGGAAATTTATACTTATCTCGCCGAACTAATTGAAATTTTTGACAGAAATGTAGAATTTACTGATTGTGTATCTATGTTTAAAGATATAAAAGGCTTTGTTATCTATTTTTACCAAAAAGCCATTGAACAAGGTAGCACAACAGCTGAAGCTTGTTTAATGAAATTTTATGATAGATATAAAGATGACTCAGCCATTTCTTTGATAGCTAATAATAATCAAGAAGCTCAAGATTGGAAGAATTTTGCTTCTAAGAATTACTTATCTGAAAATCTACAAGAAGTTAAAAATCTCGCTTTAGAAGGTGATATTGACAGTCAATTAGCGCTTGCTAAGTTTTATCGCAATTCTGATAAGACTAAAAAATGGCTTGAAATGGCAGCATTACAAGGTGATGAAAACAGTCAATATCTTCTCGCACATTTCTATGAGGAAAATAAAAACTATCAAGAAGCACTTAATTGGTATAGAAAATGCAACCATGAACACAATTTACCTGAAGCTCAAGAACGTATGAGTTACTTTTTCGAGCATGGATGCGGTGTTGAGCAGAATGAATATTTAGCCTATTTTTGGGCGAAAATTGCGGCGGATAACGGAAGTGAAATTGCTTTTGATAGACTTCCTAAATTAATGTCTTATTCTGAAATA","","","47695","MSNNTSPNYITHSLELLIKIAEYGDANAQKMLGWHYLNGLAIEKNVKQAFIWNSKAARQNDIEACFIVGWHYENGVGVEISYKDALEWYGKAARKGHTEAALRLAELYFYGTQKVDDYQFNIKANLEEAIHYSEPLAKNGNTVAQRIFALCLIKEKDFAAIRYLGQASKQGDLIATERLIKILERMNSAHDLDQEIYTYLAELIEIFDRNVEFTDCVSMFKDIKGFVIYFYQKAIEQGSTTAEACLMKFYDRYKDDSAISLIANNNQEAQDWKNFASKNYLSENLQEVKNLALEGDIDSQLALAKFYRNSDKTKKWLEMAALQGDENSQYLLAHFYEENKNYQEALNWYRKCNHEHNLPEAQERMSYFFEHGCGVEQNEYLAYFWAKIAADNGSEIAFDRLPKLMSYSEI","18944","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR006597
Repeat
Sel1-like
PF08238\"[26-61]T\"[62-97]T\"[98-141]T\"[297-325]T\"[326-357]T\"[359-394]TSel1
SM00671\"[26-61]T\"[62-97]T\"[98-141]T\"[297-325]T\"[326-356]T\"[359-394]TSEL1
InterPro
IPR011990
Domain
Tetratricopeptide-like helical
G3DSA:1.25.40.10\"[8-175]T\"[228-404]Tno description
noIPR
unintegrated
unintegrated
PTHR11102\"[11-243]T\"[264-289]T\"[309-407]TSEL-1-LIKE PROTEIN
PTHR11102:SF11\"[11-243]T\"[264-289]T\"[309-407]TSEL-1-LIKE PROTEIN, SEL-1L


","BeTs to 8 clades of COG0790COG name: TPR repeat proteinsFunctional Class: RThe phylogenetic pattern of COG0790 is ------y--d----efgh-nuj----Number of proteins in this genome belonging to this COG is 1","","Residues 4 to 107 match (1e-08) PD:PD041265 which is described as HOMOLOG SEL-1L SIGNAL SUPPRESSOR PRECURSOR SEL-1 TRANSMEMBRANE LIN-12-LIKE GLYCOPROTEIN POBS ","","","","","","","","","","","","Tue Nov 26 11:35:56 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00022 is paralogously related to AA02493 (3e-11).","","","","","","","","","","","","","","1","","6","" "AA00024","19151","19360","210","ATGGATAAAAATCAATATTTAGTTTGCTTTGGCAAAAAAGTAAAAGAATTAAGAAAACAAAAGGGGTTAAGTCAGGAGGCATTAGCTCTACTTTGTGATCTTGATCGTTCTTATATTGGTGGTGTTGAGCGTGGAGAGAGAAATATTAGTTTAATTAATATTTATAAAATCACACTAGCTCTAAATATAAATATAAAAGATTTTTTCTTA","","","8046","MDKNQYLVCFGKKVKELRKQKGLSQEALALLCDLDRSYIGGVERGERNISLINIYKITLALNINIKDFFL","19360","","transcriptional regulatory protein","Cytoplasm","","
InterPro
IPR001387
Domain
Helix-turn-helix type 3
PF01381\"[14-68]THTH_3
SM00530\"[13-68]THTH_XRE
PS50943\"[14-68]THTH_CROC1
noIPR
unintegrated
unintegrated
G3DSA:1.10.260.40\"[10-69]Tno description


","No hits to the COGs database.","","Residues 13 to 65 match (7e-07) PD:PD000418 which is described as COMPLETE PROTEOME TRANSCRIPTIONAL REGULATOR REPRESSOR DNA-BINDING PLASMID TRANSCRIPTION REGULATION FAMILY ","","","","","","","","","","","","Tue Dec 10 16:19:57 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00024 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 14 to 68 (E-value = 6.8e-15) place AA00024 in the HTH_3 family which is described as Helix-turn-helix (PF01381)","","","","","","","","1","","6","" "AA00025","19375","20046","672","ATGAACTATCAACATTATAAACCTGAAAATCTAGAAGACATTAAAAAGAAAGCAATAACTTTTTCTGAGTTTAGAAATAGATGTAAAGAATATTTAATTAGAAATAATGTTAAATTTGACAAGTTTACAATAGTTGGTCATGATAGTGAAATAGGGTATATTTCTGAGAGAACCCTTAAATCATATTTAGAGTCTAATTATTCTGATGTTAAAATATGTTCATGGGAAAATAAATGTGATATAAAAAGAATTCTTCGCATATTAGATAATAATTTAACAGATCAAGAAAGTGTAAGAATAGTTAGTGAATATTTTTATGATAAATATGATCTAGTGCTATCTTATAATAATAAAAGTATCTATATTGATGTGAAAACAGCAAAAACAAAGAAAGAGCCAACATCTAACTGGAAATTTTTATACCCAGAGATTCAAACAACTAAAATTGGCAAAGATTACATAGCATTGATTTACTGTATTTATGATGATAATAATAACATTAAAGACACAGTAATAATTGGAGCTATAAAACATTCAGATATTAAAAATTATAATTTAGTTGAAAAGGGTTCGATAAATAGAAATGGTGCTCCAAGCCAAACTAAGAATTATGAAACAGATTTAAATGATTATTGTTCAATAGATGACTTAATAAACATTTTAAAACAATCC","","","26406","MNYQHYKPENLEDIKKKAITFSEFRNRCKEYLIRNNVKFDKFTIVGHDSEIGYISERTLKSYLESNYSDVKICSWENKCDIKRILRILDNNLTDQESVRIVSEYFYDKYDLVLSYNNKSIYIDVKTAKTKKEPTSNWKFLYPEIQTTKIGKDYIALIYCIYDDNNNIKDTVIIGAIKHSDIKNYNLVEKGSINRNGAPSQTKNYETDLNDYCSIDDLINILKQS","20046","","hypothetical protein","Periplasm, Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Dec 9 12:20:14 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00025 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","6","" "AA00026","20602","20132","471","ATGCAGCATATGACACACACCCCGCTTAACGTGGATTTAAAGAAAATGGACTATGAGACATTTAAAACCTTTATGCAAGAACTGGCTCAGATGTATTCAAATGTAAAAGATGATGCTTATTTTTTATTCTACCGAAATTTACGCGAACTCGCGAAAGAAGTTAGTGCTTTACCCCGTAATCCACTCGTATTTTACGGCGCTTATGAAATTGCCAATAATCAGGTAGTTGTAGCGATATTTGAAATGCAATTTACTGATGAAATTTATGAAACCGAAGATGGAAGACCTTATCAGATGCTTTCTATTATTAGTTTTGCAGAAGATAAAGTATATCTACGTTGTCCTACGAAAATTAGAAAACATCTAACCCAACCTGAATATGTTGCTCTCTGTGAACAAGCTTATCCCACCATTATGGAAAAAATGTTACTTGATGAGCAACGAGAAAAGTTTTTTAAAAAAAGTGAAACA","","","18743","MQHMTHTPLNVDLKKMDYETFKTFMQELAQMYSNVKDDAYFLFYRNLRELAKEVSALPRNPLVFYGAYEIANNQVVVAIFEMQFTDEIYETEDGRPYQMLSIISFAEDKVYLRCPTKIRKHLTQPEYVALCEQAYPTIMEKMLLDEQREKFFKKSET","20132","","conserved hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Jan 23 11:47:27 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00026 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","6","" "AA00028","23353","20735","2619","ATGGAATTAAACAGTTATCAAGTACAAGTGATTAACGATTTAAATGACTATTTAAGTGAATTAAATCAGTATGGTAGCCACAGATTAAAACAAGTCTTTTCAAATTATTGGGCGAAAAAAGGTGTGCCTAATCAACAGTATGTAGAGAAAATTACCAATACGCCCCACATTTGCGTCAAAGTGCCAACTGCTGGCGGAAAGACCTTTATTGCGGTTAATGCTTTACAATCAATTTATAGTGCGATCGAATTTCACGGAGAAATTAAACCACGATTTACCGTTTGGCTTGTGCCATCAACGGCTATTTTAGAACAGACCATTCGGAGTTTACGAAATCCTGAACACACTTACCGCCAAAAATTAAATGTGCTATTTAATGGGCGTGTGAATGTGTATGAAAAAGATGATATTCTTCTAGGACGTGGATTTGATGCAGATACTGTAAAAAGTGGTATTTCTATTGTAGTAATGACCTTTGATGCGTTTAGAACGAGAAACAAAGAAGGTCGGTTAATTTATCGTGAGAATGGCTATTTAGCTTCTTTTGATACCAAAGCGACCGCATTGCCTGATAGTGATGAAACTTCGCTAATCAATGTAATTCGCAGTCTTGAACCAGTTGTGATTGTGGACGAAAGCCATAATGCTACATCAGATTTATCGCTAGAAATGCTAACCAATCTAAATGCAAAATTTATCTTAGATTTAACTGCTACACCAAGAAAAGAAAGCAATATAATTTCTTATGTTAGTTCATTAGCATTAAAAAAAGAAAATATGGTAAAACTACCTGTTAATGCATCTAATCAAGCAAGCAAAGAAGATGTATTGATTTCAGCGGTAACGTTTCAACGTCATTTAGAACAAGTTGCTCAAAAAGCCTTTGAAAATGGCGAGCCTTATGTTCGCCCGATTGTATTATTCCAAGCCGAAGCGAAAACCAAAGGAGATAATACGACTTTTGAAAAGGTTAAAAGGACGTTAATCGAAGAATTAAACATTCCAATTGAGCAGATCAAAATCAAAACTGCTGATATAGATGAGCTAAAAAATGTTGATTTATTTTCGCCTGATTGCCCAGTTCGTTTTGTGATTACGGTAAATGCCTTAAAAGAAGGTTGGGACTGTTCTTTTGCTTATATTCTAGCAAACCTTGCAAATAAACATTCTGAAATTGATGTCACTCAAATTGTAGGGCGTATTTTGCGCCAACCTAATGCGAAACAGTTTAGCAATCCATTGCTTAATATGAGCTATGTTTTCACAGCATCCGCCCAATTTAGAAATGTGTTGGGTAATATCGTCGAAGGTTTAACTTTAGCTGGATTTAGCCCGAAAGATTATCGAGCAATCGGCAATAATAGTGAAAGCAATCAAGAATTTACTTCAGAGCTTGATAATTTGCCATTAACATTAATGTCCCCTCAACAAAATGAGCCAACTGAGAATGGATCTTTTGACTTTGATACAGATAAATTAAAAGAGAATATTCAGCAATCAACAACAGGAAATTCTGAATTTAATCCTATCTCAAATGAATTTATCCAAGATGTTGTAACACAAAGCGAGAGTTTTAATTTAGAAGTTCAAAATAGCACAGTTACTGTTCCGAATGAATTAAAAGAGAAAATGAATATGGCAAAAATCAATGCGGAATTTAAGGAATCTGTTGAAAATATCCGTATCCCACAATTTTTTGAAACAATGAGTAGCGGACTGTTTGATGATATTGTTTTATTTGAAAAAGAAAACTTATTAACGAAATTTGAACTCAATCAATGTGGTACACAAATTTCTTTTTCAGATTTAGATCCTGAATTATATAGCATTGATATTGAAAATGAACAAAATATTAAATTCACCCCATTGAATAAAGAAAAATCTGAACAGTTATTGAAATTATTTAGAGATTATTCATTAGAGCGTAAAAAGGAAAGTATTGTTAGCTCTTTACTCAATTTTGCAGGTAGAAATGCCTTTTATCCTATCGCTGATTCTGAAATTAAAGTTTATTTCAGAAGAATTATTGAGCAAATGAGTATTGCAGATATGGAAAATTGTTTAATTAAACCTAGCATATACTTTGACAAAATTAAAAATAAAATTAAACAATTACAAGAAAAGTTTTCTCAACAGGAATTTTATAAATGGATCGATCAAGAATGTTTTCAAATTAAAGCTGAATATCAACTTCCAATAGAAATTACGCCTCAAAACTTTGCTGACTCATTAAGTCGTAGCTTATATGAGAGAGAAGCAAGCATGAATAATTATGAATTTAATGTAATATCTCGTGTTATTAGCTTAGATAATGTTGTTTGGTGGCATCGTATTGATGACAAGAGAAAAGAATATAGCTTTAAAATAAATGGATTCATTAATCATTATCCCGACTTTCTAATTTTAACAAAGAAAAACACTTTGATATTAGTTGAAGTGAAAGGAGAGCAACTAGCCAACCCTGAATCTAAAAATAAATTAGAGTTAGGTAAAAAATGGGAGTCTCTTGCAAACCAACTTAGTTTACCACATAAATTTAAATACTTTATGGTGTTTATCACTAAACCTATGGAAGGAGCTAAATCACTAGATGAGTTAATTAAAACAATTTCTTATCTT","","","100172","MELNSYQVQVINDLNDYLSELNQYGSHRLKQVFSNYWAKKGVPNQQYVEKITNTPHICVKVPTAGGKTFIAVNALQSIYSAIEFHGEIKPRFTVWLVPSTAILEQTIRSLRNPEHTYRQKLNVLFNGRVNVYEKDDILLGRGFDADTVKSGISIVVMTFDAFRTRNKEGRLIYRENGYLASFDTKATALPDSDETSLINVIRSLEPVVIVDESHNATSDLSLEMLTNLNAKFILDLTATPRKESNIISYVSSLALKKENMVKLPVNASNQASKEDVLISAVTFQRHLEQVAQKAFENGEPYVRPIVLFQAEAKTKGDNTTFEKVKRTLIEELNIPIEQIKIKTADIDELKNVDLFSPDCPVRFVITVNALKEGWDCSFAYILANLANKHSEIDVTQIVGRILRQPNAKQFSNPLLNMSYVFTASAQFRNVLGNIVEGLTLAGFSPKDYRAIGNNSESNQEFTSELDNLPLTLMSPQQNEPTENGSFDFDTDKLKENIQQSTTGNSEFNPISNEFIQDVVTQSESFNLEVQNSTVTVPNELKEKMNMAKINAEFKESVENIRIPQFFETMSSGLFDDIVLFEKENLLTKFELNQCGTQISFSDLDPELYSIDIENEQNIKFTPLNKEKSEQLLKLFRDYSLERKKESIVSSLLNFAGRNAFYPIADSEIKVYFRRIIEQMSIADMENCLIKPSIYFDKIKNKIKQLQEKFSQQEFYKWIDQECFQIKAEYQLPIEITPQNFADSLSRSLYEREASMNNYEFNVISRVISLDNVVWWHRIDDKRKEYSFKINGFINHYPDFLILTKKNTLILVEVKGEQLANPESKNKLELGKKWESLANQLSLPHKFKYFMVFITKPMEGAKSLDELIKTISYL","20735","","conserved hypothetical protein (possible type III restriction-modification system restriction subunit)","Outer membrane, Cytoplasm","","
InterPro
IPR006935
Family
Type III restriction enzyme, res subunit
PF04851\"[1-242]TResIII


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Dec 9 12:28:30 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00028 is paralogously related to AA02541 (4e-10).","","","","","","","","","","","","","","1","","6","" "AA00029","25003","23366","1638","ATGCCTGAGCTTAATTGGATTGGAAAACAAAAGATTAAGAATCATCATAATGAAATACCATTTCATCTTTTAGAAAAAAAATATACTTATAAGTTAGAAAATGTTCATCATAAGAACAATGAAGATAATATCTTAATTCATGGTGATAATCTTCTAGCTTTGAAAAGTTTGTTACCTAAATATGAAGGTAAAATTAATTGTATTTATATTGATCCACCGTATAACACAGGTAAAACACCAGAAGAGGGTGGTTGGACTTACAATGATAATGTAAGCGATCCTCGCATTGAAAAATGGCTTGGTGATGTAGTAGGAAAAGAGGGGGAAGATTTAACTCGCCATGACAAATGGTTGTGTATGATGTATCCTCGTTTAAAAATTATGGAAAAACTACTTCATGAAGATGGAGTTATTTTTATTAGTATAGATGATACTGAATTAGCTCATTTACGATTGGTATGTGATGAAATTTTTGGTTATCAGAATTTTATAGAATGTTTTTGTTGGGAGAAAACCACGACCCCTGCATCTTTATCTAAGACATCTCGCTCTAACATTGATTATATTTTAACTTATCAGAAAAAGAATACACAAAAGATTTTTGATAGCCATAAAGAAGATAAAAAAAGTACAGATTCTCCAGTAGAGAATAAAGATAATCCTATTAGTACAATTATATTAAACTCCGGAGTAATTAAATGCAATTTTCCTGATGGAGTATATAATAAAGAAAAATATGGAGATGGTAAGTTACTGAATGATTTAGTTGTGAAAAATGGTACAAATCAAGAAACCTTGAAATATAGTTCAAATTTGAAATGGAGTCAGGATTATTTAGATAATGAAATAAAGCAAGGCACTGAGTTATTATTTAAATCGACTAAAATGTCATTAAGGTATAAAAAGATAGAAGGTAGAAAAAAAATAATGGCTCCAAATAAACTTATAGACAACAAGTTTGGAGTTGGAACAAATGATAATGCTAAATCAGATTTAGACGAATTAGGAATAACTTTCTCTTATTCTAAGCCATATAGTTTGGTATCATTTCTAATTAATATTATTTCTAATAAAGATGCCGTTATTTTAGATGGCTTTATGGGGAGCGGAACAACAGCTCATGCTGTTTTAAATCTTAACGCAAAAGATGGTGGAAACCGTCAATTTATAGGCATTGAAATGATGGACTATGCGGAAAATATTACAGCGGAACGAATCCGCAGAGTAATTAATGGTTATGGTTCAAAAGCAGAAACGCAAAAAGGTACTGGGGGAGGATTTAGTTTTTATACCATTGGCGAAACCTTGTTTGATTCAGACGGTAACTTAAATAATCAGGCAGATTTAATTAGTATTCGTGAATATATTGCTCATAGCGAAAAGCTAGAAACCGTTTTTGATAACCATACAAGTGGTTATTTTTTAGGTTTAAATTATCAAACAGCATATATTTTTTATTACGAATTAGATCAGGTTACAACATTAAGCCTAGATTTTTTACGCAGCTTAAATGCTAATTTTATGGCAGAAAAGCCGAAAGATTTTATTATTTATGCTGATAAATGCTCATTAACCGATGAACAATTAGCACAATTTAAAATCCGCTTCAAACGGATCCCACGAGATATTAGCAAACTA","","","62552","MPELNWIGKQKIKNHHNEIPFHLLEKKYTYKLENVHHKNNEDNILIHGDNLLALKSLLPKYEGKINCIYIDPPYNTGKTPEEGGWTYNDNVSDPRIEKWLGDVVGKEGEDLTRHDKWLCMMYPRLKIMEKLLHEDGVIFISIDDTELAHLRLVCDEIFGYQNFIECFCWEKTTTPASLSKTSRSNIDYILTYQKKNTQKIFDSHKEDKKSTDSPVENKDNPISTIILNSGVIKCNFPDGVYNKEKYGDGKLLNDLVVKNGTNQETLKYSSNLKWSQDYLDNEIKQGTELLFKSTKMSLRYKKIEGRKKIMAPNKLIDNKFGVGTNDNAKSDLDELGITFSYSKPYSLVSFLINIISNKDAVILDGFMGSGTTAHAVLNLNAKDGGNRQFIGIEMMDYAENITAERIRRVINGYGSKAETQKGTGGGFSFYTIGETLFDSDGNLNNQADLISIREYIAHSEKLETVFDNHTSGYFLGLNYQTAYIFYYELDQVTTLSLDFLRSLNANFMAEKPKDFIIYADKCSLTDEQLAQFKIRFKRIPRDISKL","23366","","type III restriction-modification system: methylase","Cytoplasm","","
InterPro
IPR001091
Family
Site-specific DNA-methyltransferase (cytosine-N4-specific)
PR00508\"[64-78]T\"[124-144]T\"[358-376]T\"[387-407]TS21N4MTFRASE
InterPro
IPR002052
Domain
N-6 Adenine-specific DNA methylase
PS00092\"[68-74]?N6_MTASE
InterPro
IPR002295
Family
N6 adenine-specific DNA methyltransferase, D21 class
PR00506\"[65-77]T\"[124-143]T\"[339-361]T\"[362-376]TD21N6MTFRASE
InterPro
IPR002941
Domain
DNA methylase N-4/N-6
PF01555\"[65-404]TN6_N4_Mtase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[42-409]Tno description


","No hits to the COGs database.","Significant hit ( 1.4e-21) to 4/4 blocks of the PR00506 family, which is described as \"D21 class N6 adenine-specific DNA methyltransferase signature\". Prints database entry for PR:PR00506. PR00506A 65-77 1.6e-05 PR00506B 124-143 0.0016 PR00506C 339-361 0.25 PR00506D 362-376 6.9e-06Significant hit ( 2.7e-09) to 2/2 blocks of the IPB001091 family, which is described as \"N-4 DNA methylase (N4-MTase)\". Interpro entry for IP:IPR001091. IPB001091A 62-74 0.0013 IPB001091B 362-372 0.00074","Residues 64 to 140 match (3e-08) PD:PD577242 which is described as METHYLTRANSFERASE PROTEOME COMPLETE TRANSFERASE TYPE DNA III PLI0029 MODIFICATION RESTRICTION-MODIFICATION ","","","","","Wed Feb 19 16:21:25 2003","","","","Wed Feb 19 16:21:25 2003","","","Tue Nov 26 13:07:32 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00029 is paralogously related to AA01923 (6e-66) and AA02031 (3e-12).","","","","","","Residues 128 to 406 (E-value = 2.4e-19) place AA00029 in the N6_N4_Mtase family which is described as DNA methylase (PF01555)","","","","","Humbelin,M., Suri,B., Rao,D.N., Hornby,D.P., Eberle,H., Pripfl,T., Kenel,S. and Bickle,T.A.Type III DNA restriction and modification systems EcoP1 and EcoP15. Nucleotide sequence of the EcoP1 operon, the EcoP15 mod gene and some EcoP1 mod mutantsJ. Mol. Biol. 200 (1), 23-29 (1988)PubMed: 2837577 ","","Wed Feb 19 16:21:25 2003","1","","6","" "AA00030","25228","25019","210","ATGAACAGCACAAAAAACTTAACCTTAAAAGCGCAATTTAAACAGTGGCTTGAGGAAGAACAGAAAACCGATGAGATGATCGCATTTGCCACTATACCGCACATTTTAAGACGGTTTGATAAGCGATTGGCGATTATTAAAGGAAATCGGTTTGAGAAACGTTATCTAAGCGAGTGGCGCAGAGCATTTCGTGTAGATAATACATTATAT","","","8589","MNSTKNLTLKAQFKQWLEEEQKTDEMIAFATIPHILRRFDKRLAIIKGNRFEKRYLSEWRRAFRVDNTLY","25019","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Tue Nov 26 13:14:26 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00030 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","6","" "AA00031","25777","25421","357","TTGCAACCAGCTATCGACTTAATCAACTCTCAAGCGGTTACAGACTATCCTACACAGGAACAGTTAAACCATTACTTGAGTGAGAAAATAGGTCAAATGGCGGCAATTACAGGTTTCATTAATCACCTGAAATCAGTATATTACCGAGAGTTAGACATTGACCGTAATCTTATTCAACAGATGAAAGCTAAACGACTCAAAAAGCATTATTCTCAACGTTTAGTTGAACTCTACAAGCAAACAGAATTAACCACTACGGAACAAATGGAACTGGTTTCGGTTGTTTTATATAGCTTGCATGGTATCGAAATCAAAAAGCCAAAACTTGATGCCATTGTATTGCTAGATGGTGTGACT","","","13726","LQPAIDLINSQAVTDYPTQEQLNHYLSEKIGQMAAITGFINHLKSVYYRELDIDRNLIQQMKAKRLKKHYSQRLVELYKQTELTTTEQMELVSVVLYSLHGIEIKKPKLDAIVLLDGVT","25421","","conserved hypothetical protein","Cytoplasm","No significant similarities were found to the NR database, however see the Paralogs field.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sat Feb 21 10:56:18 2004","Sat Feb 21 10:56:18 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is similar to AA0293, a conserved hypothetical protein.AA00031 is paralogously related to AA00442 (1e-43).","Sat Feb 21 10:56:18 2004","","","","","","","","","","","","","1","","6","" "AA00033","26553","25783","771","ATGGGTACAACCGACACAGGGCTTTCGAAAAATTATCGGATAAAATCAGGTGTTATCCGAACATCACTTTACCCCAATGAAAGTATTAGTTCGTGTCTTATTCGTGCAGCATTAGATTGTGGCACGGAGCCTATCATTTTTACTGGATTTTATTGGGGTAAATGGCGTTTATGGACGCTTGATTTAGACAGAGGATTCGAGCCGATAGCACCGCAAATTTATGCGGATATAACGGAATTATCCTTGAATAGACAGATTGATTTAGCTCACCATTCGCTTTATTCAGTCTTAAAACCGATTAATGGTGAACAGACGTTGTTAAAAGGTCAAGCCAAATGGGTACTTCCGCGAAGTTCTCGAAATCGCTCATATCGTAGCGGTCAACCGTATTGTGCTTGTTGTTTAGAAGAAACCCCTTATTTGCGTAATGAATGGCGTTTAGCGTGGCATTTTGGCTGTTTGAAACATCATACATTGCTTGAAACAAAATGCCCTCATTGTGGCGAACCTTATCAACCGCATTTGCTTTCAGCGGATAAACGACAGCTTAACCATTGCCATCACTGCGGTAAGCGTTTATCCGTAGCAGGTGAAAAACTTACCGAAGTGGAAATAGAAGCCTTGATGTTACTTGATGAAGTATTTAAAACCGATTCAGGACATTGTTTTCAGCAACAAGTAAATGCTCAAACCTATTTTGCGATATTACGCTATGTTATCAATCTTATTCGTCGTGCTGCTATGGTAAAACATCACTTAAATCGGTACGGT","","","29588","MGTTDTGLSKNYRIKSGVIRTSLYPNESISSCLIRAALDCGTEPIIFTGFYWGKWRLWTLDLDRGFEPIAPQIYADITELSLNRQIDLAHHSLYSVLKPINGEQTLLKGQAKWVLPRSSRNRSYRSGQPYCACCLEETPYLRNEWRLAWHFGCLKHHTLLETKCPHCGEPYQPHLLSADKRQLNHCHHCGKRLSVAGEKLTEVEIEALMLLDEVFKTDSGHCFQQQVNAQTYFAILRYVINLIRRAAMVKHHLNRYG","25783","","conserved hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Jan 23 11:48:48 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00033 is paralogously related to AA00443 (1e-110).","","","","","","","","","","","","","","1","","6","" "AA00034","27404","26514","891","ATGGAAAAGCAATATGAGCATATTCACGAAAAATTTCGTCATTTAGTAACGGCAAGTAATCAAGAGCGAATTGAATTTTTAGATGAACCACGTTGGGTAGGTTATGCCGTTGCGAATAAGATTATTGATAATTTGGTTTCTTTGATGCATAAACCCAAACGCCCTCGTATGTTAAATTTATTAGTCGTTGGGGATTCGAATAATGGAAAAACCACGTTAATACGCCATTTTTATAATTTACATGGAACACCTTTTGTCGATTCAAAGTCTGATGGTAATCGCCCTATTATCTTAGCGGAAGCACCACCTAGTGCGAATGAAAAGGAGCTTTATATCTCGTTGCTGGAACGTTTCTATGTACCTTACCGACCAACGGATAGCGTAGCTAAATTACGTTATCAGACAATTCACTTATTCCGTGAATATAAGGTAAAAATGCTGATTATTGACGAGTTTCATTCCTTATTAGTTGGAACACCACGCCAGCAACGGCAGGTAATGAATGCGATTAAGATGTTGTGTAACGAGCTACAAATCCCGATTGTGGGTGTAGGTACGCGTGATGCCATTCGGGTACTACATACCGACCCTCAACACGCGAGCCGTTTTGATGTTGCCGAGTTACCAACGTGGAAATTGGATAAGGAATTTCAAAAACTATTATTCCAGTTTCAAGGTATTTTGCCTTTGAAGAAATGTTCTAACCTTCAATCGCCTGAATTAGCAACCCGAATTCATACGATTTCAGGTGGTAATTTAGGGAATGTACATCGCTTATTAACCGCTTGTGCTGTTGAAGCTATCAACACAGGTACAGAGCAAATCACTTTAGATATTATTGAGCATAACGCATGGGTACAACCGACACAGGGCTTTCGAAAAATTATCGGA","","","34102","MEKQYEHIHEKFRHLVTASNQERIEFLDEPRWVGYAVANKIIDNLVSLMHKPKRPRMLNLLVVGDSNNGKTTLIRHFYNLHGTPFVDSKSDGNRPIILAEAPPSANEKELYISLLERFYVPYRPTDSVAKLRYQTIHLFREYKVKMLIIDEFHSLLVGTPRQQRQVMNAIKMLCNELQIPIVGVGTRDAIRVLHTDPQHASRFDVAELPTWKLDKEFQKLLFQFQGILPLKKCSNLQSPELATRIHTISGGNLGNVHRLLTACAVEAINTGTEQITLDIIEHNAWVQPTQGFRKIIG","26514","","NTP-binding protein","Cytoplasm","","
InterPro
IPR008868
Family
Bacterial TniB
PF05621\"[22-275]TTniB


","BeTs to 3 clades of COG0305COG name: Replicative DNA helicaseFunctional Class: LThe phylogenetic pattern of COG0305 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is 2","","Residues 7 to 124 match (8e-10) PD:PD016330 which is described as PLASMID TNIB ATP-BINDING NTP-BINDING COMPLETE PROTEOME DELTA2 TNIBDELTA1 TNIBDELTA2 ","","","","","Tue Feb 18 10:04:25 2003","","","","","","","Tue Nov 26 13:35:30 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00034 is paralogously related to AA00444 (1e-164).","","","","","","Residues 1 to 296 (E-value = 5.9e-33) place AA00034 in the TniB family which is described as Bacterial TniB protein (PF05621)","","","","","Mindlin,S., Kholodii,G., Gorlenko,Z., Minakhina,S., Minakhin,L., Kalyaeva,E., Kopteva,A., Petrova,M., Yurieva,O. and Nikiforov,V. Mercury resistance transposons of gram-negative environmental bacteria and their classification Res. Microbiol. 152 (9), 811-822 (2001) PubMed: 11763242","","Tue Feb 18 10:04:25 2003","1","","6","" "AA00036","29314","27407","1908","ATGACTAATTCAGCTAACTTCATTCACCCACGCCATCACCCAAAATTAACGCGTGGACGCATTATTTTAAAGAAAGGCAATGTCTATATAAACCGCGAGGACGGCGAGCAATATGAGTTAGTGGAATATCTTGATGAAAATGCACAAGTCTTGATCCGAAACCTTCATACACGTCAATGCAAAATTACCAGTATTTATCAGCTTGAAAATGTGAAAATCAACGAGCGTGAAGATTTATTGGTGGATTTAAGCGAAATCAGTGATGAATATTGGGAAAAAGCACTTGAACGCTATGAAATGATTAAGCCGTTATTGGAAAGAGAGCAACCGATTAAGGAACGTGCAGCGGAGTTAGGCGTAAGCGAACGCAGTTTATATCGTTGGTTAAACGCATATAACGCACTCGGCTCTGTTGCAGGATTAGTCGAGCGTAAACGCGGTTGGTCGAAAGGCAATTCACGACTAACCAAAGAACAAGATGAACTGGTAACAACCGTGATTAACGAATTTTACTTGCACAAACAACGTCCGACAGCCGAGCAAACTATTCGTGAAGTGCAGCGTGTGGCAAGTCAAAAAGGTATTAAAAGCCCTTGTCACCGTACAATCACTTTACGCATTTCAAGTATTTCAGAAGAAGAAAAATTGCGTAAACGCGGACAAAAGGAAAAAGCGAAAAACAAATTCACACCAAAGCCAAATAGTTTCCCGAATGCGGATCACCCTTTAAGTGTTATTCAAATCGACCATACACCTGTCGATCTAATTATTGTTGATAACCAATATCGTAAGCCGATTGGCAGACCTTATTTAACATTGGCAATGGACGTGTATAGCCGAATGATTACAGGGTACTACCTGTCACTTGATGCACCATCAGTAACATCAGTTGCAATGTGTATCGCTCGTAGTATTTTGCCGAAAGAACGTTTGCTACTCGACCATAATGTAAAAGGTGAATGGTCGGTATTTGGTTATCCCAATAAGATCCACGTTGATAATGGTGCAGATTTCCGTTCATTGGATTTATCAAAGTCTTGTCAAATGCACGGTATTACACTCGAGTTCCGTCCTGTTGGTCGCCCTGAATTTGGTGGACACATTGAGCGTGTAATAGGCACTTTTATGAAAGAAGTTCACGGTTTAAGTGGAACAACGTTCTCTAATATAGAGAAAGATACCTATCAATCAGAAGCCGAAGCGGTGATGACTTTAGATGAATTTGAAACGTGGTTAATCAATTACATCGTCAATGTGTATCACAAACGCACTCATTCTGCGTTAGGTACGTCGCCGGTTCAAAAATGGCGATTAGGCATTTTTGGCGATAGTAACAATGCTGGTAGAGGTTATCATCAAATGCCTGCTGATGAACAAACGTTACTACTTGATTTCTTGCCAAGTGAGAAACGAACTATTCAGCATAATGGTGTAACCATTGATGGCTTACGTTACTATGATGCTGCGTTGAATATGTATATCAACGATTCAGATGAAAAAGGCAAAAGTAAGGAATTTTTATTCCGTCGTGACCCACGAAATATCGGCAAGATTTGGTTCTACGATCCGAAATTAAAGCGTTATTTCCCTATTCCATTTGCAGACCAGTCTTTACCTGATATGAGTATTTGGGAATATAAACAGGTTCGCCAGTTCTTGAAAGATAAAGATGAAAAGCTGATTCACTCACAGCAAATTCACGATGCTTTAACTGAAATGCGTGATTTGGTTGAACAATCGGCACAACGCACGAAAAAAGCACGACGACAAGCTCAGCGACAGAAAGTCCATGCAAAAAGTAAAGTGGTTATTCCAACCGCATTACCCGAAAGCAAACCAAAAGAGCAAATTAAACAACCTACTTCTAACTTGCTTTTAGATGATGATTTCACGTTTGGAGAGATTGAA","","","73749","MTNSANFIHPRHHPKLTRGRIILKKGNVYINREDGEQYELVEYLDENAQVLIRNLHTRQCKITSIYQLENVKINEREDLLVDLSEISDEYWEKALERYEMIKPLLEREQPIKERAAELGVSERSLYRWLNAYNALGSVAGLVERKRGWSKGNSRLTKEQDELVTTVINEFYLHKQRPTAEQTIREVQRVASQKGIKSPCHRTITLRISSISEEEKLRKRGQKEKAKNKFTPKPNSFPNADHPLSVIQIDHTPVDLIIVDNQYRKPIGRPYLTLAMDVYSRMITGYYLSLDAPSVTSVAMCIARSILPKERLLLDHNVKGEWSVFGYPNKIHVDNGADFRSLDLSKSCQMHGITLEFRPVGRPEFGGHIERVIGTFMKEVHGLSGTTFSNIEKDTYQSEAEAVMTLDEFETWLINYIVNVYHKRTHSALGTSPVQKWRLGIFGDSNNAGRGYHQMPADEQTLLLDFLPSEKRTIQHNGVTIDGLRYYDAALNMYINDSDEKGKSKEFLFRRDPRNIGKIWFYDPKLKRYFPIPFADQSLPDMSIWEYKQVRQFLKDKDEKLIHSQQIHDALTEMRDLVEQSAQRTKKARRQAQRQKVHAKSKVVIPTALPESKPKEQIKQPTSNLLLDDDFTFGEIE","27407","","transposase","Cytoplasm","","
InterPro
IPR001584
Domain
Integrase, catalytic core
PF00665\"[238-437]Trve
PS50994\"[238-440]TINTEGRASE
InterPro
IPR015378
Domain
Transposase-like, Mu, C-terminal
PF09299\"[461-532]TMu-transpos_C
noIPR
unintegrated
unintegrated
G3DSA:3.30.420.10\"[241-379]Tno description


","No hits to the COGs database.","","Residues 111 to 187 match (2e-08) PD:PD483826 which is described as PROTEOME COMPLETE TRANSPOSASE PLASMID ","","","","","Wed Feb 19 16:37:51 2003","","","","Wed Feb 19 16:37:51 2003","","","Tue Nov 26 13:43:43 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00036 is paralogously related to AA00446 (0.0).","","","","","","Residues 238 to 437 (E-value = 1e-19) place AA00036 in the rve family which is described as Integrase core domain (PF00665)","","","","","Kahn,K. and Schaefer,M.R.Characterization of transposon Tn5469 from the cyanobacteriumFremyella diplosiphonJ. Bacteriol. 177 (24), 7026-7032 (1995)PubMed: 8522506 Schaefer,M.R. and Kahn,K.Cyanobacterial transposons Tn5469 and Tn5541 represent a novelnoncomposite transposon familyJ. Bacteriol. 180 (22), 6059-6063 (1998)PubMed: 9811670 ","","Tue Dec 3 11:46:03 2002","1","","6","" "AA00037","29966","29310","657","ATGAAAACAGAACAAACTTTTAAACAAGTTCGTAAGATCAAACCCACACGCTTTAGCGTATCAGGCTATCTTCCTTTCAGAGAGGGAATAAGCATACCTTACGAATCTACTCTTGAACGAGATTTTTTGCTTTATTTCACTTACCTTCCATCGGTAGCGGAAATCATTGCACAACCTGCACGCATACTGTTTGTAAAAAACGGTATGACTTATCCTTACACGCCCGATTACCTGATTCGTTTTAACGACGGACGACGTTCACTTTTGGTTGAAGTAAAGCCGAAATCACAATGGCAAGCACATTGGAAAGAGTGGAAAGAAAAATGGAAAGCGGCAATGGCGTTTGCCAAAGAGAGTGATTGTGTCTTTCATATCTATGATGAAGATAAAATCTACCATAGCGCTTTTCTCAACATTCATTTTCTACAACGCTACAAGCGATTGCAATGCGATCCTGAAGATATTCAAGCTGTACTTTCTCAAGTGGAATTAATGGGTATAACTAACATTGATTACCTACTGGCGCGTTTCTTTGGCGGCTCACTCTATCGAGGACAAGGAATGCGTATCATCTATCATTTATTGGCAAGCAAGCAATTAACCTGCAACTGGTTTGAGCCAATGACCGAATTTACCGAAGTATGGGGGTTTTATGAC","","","26066","MKTEQTFKQVRKIKPTRFSVSGYLPFREGISIPYESTLERDFLLYFTYLPSVAEIIAQPARILFVKNGMTYPYTPDYLIRFNDGRRSLLVEVKPKSQWQAHWKEWKEKWKAAMAFAKESDCVFHIYDEDKIYHSAFLNIHFLQRYKRLQCDPEDIQAVLSQVELMGITNIDYLLARFFGGSLYRGQGMRIIYHLLASKQLTCNWFEPMTEFTEVWGFYD","29310","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR014832
Domain
TnsA endonuclease C terminal
PF08721\"[130-204]TTnsA_C
InterPro
IPR014833
Domain
TnsA endonuclease N terminal
PF08722\"[50-128]TTnsA_N


","No hits to the COGs database.","","","","","","","","","","","","","Wed Jan 22 15:03:51 2003","Wed Jan 22 15:03:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00037 is paralogously related to AA00447 (1e-100).","","","","","","","","","","","","","","1","","6","" "AA00038","30452","30081","372","ATGAGTCGAACCGTCAGCCATGAGACCCTCATTATCGGCGCCGGGGCGGCAGGCTTATTCTGTGCGGCACTGTTGGCAAAGTGCGGTGGAAACGTCCGGATTTTAGATAACGGGAAAAAAGTCGGGCGGAAAATTTTAATGTCCGGCGGTGGGTTTTGTAATTTCACCAATATGGAGATGTCTTCGGACCGCTATCTCAGCCAAAATCCGCATTTTGTGAAATCGGCATTGAAACGCTTTACCCAGTGGGATTTCATCGGCTTGGTAGCGGACTACAGCATTGCTTACCATGAAAAAGAACTGGGGCAGTTGTTTTGCGATAACGGTGTAAAACGTACAAATAAGTGGCATAATAGGCAAAACTTAGAACGG","","","13856","MSRTVSHETLIIGAGAAGLFCAALLAKCGGNVRILDNGKKVGRKILMSGGGFCNFTNMEMSSDRYLSQNPHFVKSALKRFTQWDFIGLVADYSIAYHEKELGQLFCDNGVKRTNKWHNRQNLER","30081","","conserved hypothetical protein","Periplasm, Cytoplasm, Extracellular","","
InterPro
IPR003953
Domain
Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal
PF00890\"[8-53]TFAD_binding_2
noIPR
unintegrated
unintegrated
G3DSA:3.50.50.60\"[6-42]Tno description
signalp\"[1-30]?signal-peptide
tmhmm\"[10-30]?transmembrane_regions


","BeTs to 6 clades of COG2081COG name: Predicted flavoproteinsFunctional Class: RThe phylogenetic pattern of COG2081 is -----------lbcefgh---j----Number of proteins in this genome belonging to this COG is","Significant hit ( 6.1e-06) to 1/5 blocks of the IPB000171 family, which is described as \"Bacterial-type phytoene dehydrogenase\". Interpro entry for IP:IPR000171. IPB000171A 10-40 5.9e-06","Residues 32 to 105 match (8e-32) PD:PD004630 which is described as COMPLETE PROTEOME OXIDOREDUCTASE FLAVOPROTEIN FAD OXIDASE DEHYDROGENASE REDUCTASE SUBUNIT TRANSHYDROGENASE ","","","","","","","","","","","","Tue Nov 26 16:05:18 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00038 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00039","31498","30452","1047","ATGAAACGATTTCTAGCGTTATTTTTTTTATTGATCAGCGTCGGTGCTTTTGCCGAAATGGTGGATACCTTTGAATTCCACAATCCGGCAGATCGTGCGCGCGCGGTGGAATTAGCAAAATCTTTGCGCTGCCCGCAATGTCAGAATCAAAATCTGGTGGAGTCCAATTCTCCTATCGCCTATGATCTGCGCCTTGAAGTGTATAACATGGTCAAGGAAGGCAAAACCAATCAGCAAATTATTGATGCCATGACGGTACGCTTCGGCAATTTTGTGAATTACAAACCGCCCTTTCAGTGGAACACTGCATTGCTTTGGCTGTTGCCGGCGGGGTTGCTGTTAATGGCGTTTGGGTTGATTTGGAATTCTGCCCGCAGTTCATCAAGCCTGAAATCTGAAAAACAACTGGCAAATCCACCGCACTTTCATGCCATTCAAGAGAAAAGTGCGGTCAAATTTGAACGTAAATCTACGCTCATTGTTTTCACGTTATTGCTGATCGTACCCCTAGTTTATTACTTCTCTCTGGATCGCTTCGCCCGTGCCAAACAAGGGGAACGGGCACAAATCGCGCAGTTGAATCATCAAATTGAAACGCCGGAAGAAAACAAAACGGAAGCGATTATCGGCAAACTGCAGGATAAATTACGGCAAAATCCGAATCATGGAGAAAACTGGATAAAGCTGGGCGATGCTTATATGCAAAACAATGATTTTGACAGCGCATTAATTTGTTACACCAACGCGGAAAAAATCGAAGGGCGCAAACCGACCATTTTAGGGTTAATGGCGATGTCGTTATATCTTCAGGAAAATCAGCAAGTTACGCCACAGGTGCAACAGCTGGTAGAGGAGGTTTTGACGCAGGATCGCAAAGAGGTATCGGTTCTGTCCCTTTTGGCGGCGGAAGCCTTAAAAACGCGGGATTATTCCACCGCACTTGATTATTGGCAGCAAATTCTAGATTCGGGCAATGCCACGGTGGATCGTCGTGCGATCATTCAGAAAATGAAAATGGTGGATTTTATGCAGAAGGGGAATATGCAA","","","39916","MKRFLALFFLLISVGAFAEMVDTFEFHNPADRARAVELAKSLRCPQCQNQNLVESNSPIAYDLRLEVYNMVKEGKTNQQIIDAMTVRFGNFVNYKPPFQWNTALLWLLPAGLLLMAFGLIWNSARSSSSLKSEKQLANPPHFHAIQEKSAVKFERKSTLIVFTLLLIVPLVYYFSLDRFARAKQGERAQIAQLNHQIETPEENKTEAIIGKLQDKLRQNPNHGENWIKLGDAYMQNNDFDSALICYTNAEKIEGRKPTILGLMAMSLYLQENQQVTPQVQQLVEEVLTQDRKEVSVLSLLAAEALKTRDYSTALDYWQQILDSGNATVDRRAIIQKMKMVDFMQKGNMQ","30452","","cytochrome c-type biogenesis protein","Inner membrane, Periplasm, Cytoplasm","","
InterPro
IPR005616
Family
Cytochrome C biogenesis protein
PD005662\"[8-102]TQ9CPK8_PASMU_Q9CPK8;
PF03918\"[3-141]TCcmH
InterPro
IPR011990
Domain
Tetratricopeptide-like helical
G3DSA:1.25.40.10\"[215-322]Tno description
InterPro
IPR013026
Domain
Tetratricopeptide region
SM00028\"[223-256]T\"[294-327]TTPR
PS50005\"[223-256]T\"[294-327]TTPR
InterPro
IPR013105
Repeat
Tetratricopeptide TPR_2
PF07719\"[223-256]TTPR_2
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide
tmhmm\"[5-23]?\"[103-121]?\"[158-176]?transmembrane_regions


","No hits to the COGs database.","","Residues 3 to 102 match (6e-39) PD:PD005662 which is described as CYTOCHROME C-TYPE BIOGENESIS PROTEOME COMPLETE HEME CYCL PERIPLASMIC CCMH PRECURSOR ","","","","","Mon Feb 17 06:27:34 2003","","","","","","","Tue Nov 26 15:47:17 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00039 is paralogously related to AA00052 (1e-23) and AA00050 (5e-07).","","","","","","Residues 3 to 141 (E-value = 3.3e-59) place AA00039 in the CcmH family which is described as Cytochrome C biogenesis protein (PF03918)","","","","","Hussain,H., Grove,J., Griffiths,L., Busby,S. and Cole,J. A seven-gene operon essential for formate-dependent nitrite reduction to ammonia by enteric bacteria Mol. Microbiol. 12 (1), 153-163 (1994) PubMed: 8057835Grovc J, Busby S, Cole J.The role of the genes nrf EFG and ccmFH in cytochrome c biosynthesis in Escherichia coli.Mol Gen Genet. 1996 Sep 13;252(3):332-41.PMID: 8842153 ","","Mon Feb 17 06:27:34 2003","1","","","" "AA00040","32025","31498","528","ATGAATAGAAAAGTGATTTTTTTCCTGCCGTTAATTTTATTGCTCGGTGTGTGCGTGCTATTGTTGGCGGGGTTGCATCAGGATCCGAAAAAAATTGCCTCCGCTTTAATTGATAAGTCTGTGCCGGAATTTTATCAGGCGAATTTGCTGGATAACCGCCAAACGCTCAGCCCCAAGGATTTTCCGAAACGTCCCTTTCTGATAAATATTTGGGGCAGTTGGTGCGGTTATTGCCAACAGGAACATCCGTTGTTGATGGAATTGGCACAGGAAATGCCTATTGTCGGCGTGGATTATCGCGATAAACCGCAAAACGGCATTGAAATGCTGCAACGGATGGGTAATCCTTATGCGTTAGTGATTGATGACAGTCGTGGCGAGCTGGCGTTGAAGCTGGGCGTAGATGGCGCGCCGGAAACCTATTTAGTGGACGCCGACGGTATTATTCGTTACCGTCATTCGGGTTTATTGGATCGTGAAACCTGGCAAAATACGTTTGTACCTCAACTTAATCGGTTAATGCAGCCA","","","20159","MNRKVIFFLPLILLLGVCVLLLAGLHQDPKKIASALIDKSVPEFYQANLLDNRQTLSPKDFPKRPFLINIWGSWCGYCQQEHPLLMELAQEMPIVGVDYRDKPQNGIEMLQRMGNPYALVIDDSRGELALKLGVDGAPETYLVDADGIIRYRHSGLLDRETWQNTFVPQLNRLMQP","31498","","thiol:disulfide interchange protein","Periplasm, Inner membrane, Cytoplasm","","
InterPro
IPR004799
Family
Periplasmic protein thiol:disulfide oxidoreductase DsbE
TIGR00385\"[5-172]TdsbE: periplasmic protein thiol:disulfide o
InterPro
IPR006662
Domain
Thioredoxin-related
PR00421\"[66-74]T\"[74-83]TTHIOREDOXIN
PS00194\"[67-85]TTHIOREDOXIN
InterPro
IPR011594
Domain
Thioredoxin-like
PD003679\"[83-162]TNRFX_HAEIN_P44943;
InterPro
IPR012335
Domain
Thioredoxin fold
G3DSA:3.40.30.10\"[28-175]Tno description
InterPro
IPR013740
Domain
Redoxin
PF08534\"[36-170]TRedoxin
InterPro
IPR015467
Domain
Thioredoxin family
PTHR10438\"[64-92]TTHIOREDOXIN-RELATED
noIPR
unintegrated
unintegrated
PTHR10438:SF13\"[64-92]TTHIOREDOXIN M(MITOCHONDRIAL)-TYPE
signalp\"[1-27]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","BeTs to 19 clades of COG0526COG name: Thiol-disulfide isomerase and thioredoxinsFunctional Class: O,CThe phylogenetic pattern of COG0526 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 96 to 175 match (7e-09) PD:PD580053 which is described as E DISULFIDE FORMATION BOUND ","","","","","","","","","","","","Tue Nov 26 15:54:20 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00040 is paralogously related to AA00054 (4e-33) and AA02442 (9e-08).","","","","","","","","","","","Fabianek,R.A., Hennecke,H. and Thony-Meyer,L. The active-site cysteines of the periplasmic thioredoxin-like protein CcmG of Escherichia coli are important but not essential for cytochrome c maturation in vivo J. Bacteriol. 180 (7), 1947-1950 (1998) PubMed: 9537397 Li,Q., Hu,H. and Xu,G. Biochemical characterization of the thioredoxin domain of Escherichia coli DsbE protein reveals a weak reductant Biochem. Biophys. Res. Commun. 283 (4), 849-853 (2001) PubMed: 11350062 Li,Q., Hu,H.Y., Wang,W.Q. and Xu,G.J. Structural and redox properties of the leaderless DsbE (CcmG) protein: both active-site cysteines of the reduced form are involved in its function in the Escherichia coli periplasm Biol. Chem. 382 (12), 1679-1686 (2001) PubMed: 11843181 ","","Tue Nov 26 15:54:20 2002","1","","","" "AA00041","33877","32021","1857","TTGCTCCTCGCGGTAGTGCCGCAGCTTGGGCTTTGGTTGCGTAAGCCGGCGCTTACCCAATTGGCGTGGGGCTTAAGTTACTGCTTCGGGTTATTCACGCTGGCGCCTATTTCCATATTAGCATACTCCTTTGCGGCGGATGATTTTACGTTGGAATATGTCGCCGCCCATTCCAATTCCCAACTGCCGACCTTTTTCAAAATCGCCGCGACCTGGGGCGGGCATGAAGGTTCCATGTTGTTTTGGTTGTTTTCGCTTTCTGTTTGGGTGGTGTTGTTTGCGTTATTTAACCGAAAAAACGACCGCACTTTTGTGGCGCAAAGTCTGGTGATTTTGGGGCTGATTTGCTTTAGTTTCGCCGTGTTTATCGTCTTTTTCTCTAATCCGTTCGGACGAATTTTCCCGGCGCCGTTGGAAGGGCGGGATTTGAATCCGATGTTGCAGGATGTCGGTTTGATTTTTCACCCGCCGTTGCTTTACCTCGGTTACGTGGGCTTTGCAGTGAATTTTGCCATCAGTATTACCGCCTTGCTTCATCAGCATTTGGAACGCCAGATTGCTCAAATCATGCGGGCTTGGGTGTCGGTGTCATGGTTGTTTTTAACTTTGGGCATTGTGCTTGGCGCCTGGTGGGCGTATTACGAACTGGGCTGGGGAGGTTGGTGGTTCTGGGATCCGGTGGAAAATGCGTCGCTCATGCCGTGGTTGCTCGGCTTGGCATTGTTGCACAGTTTAATCGTCAGCGAAAAACGCGGAATTTTTAATTACTGGACGACCTTATTTTCCTTGTTGGCATTTGCCTTCAGCGTATTAGGCACGTTTATCGTGCGCTCCGGCGCGCTTACCTCCGTACACGCTTTCGCTGTGGACAGCCAACGCGGCTCGGCATTATTACTGATTTTCTTCCTGCTCACCGTGGGTTCTCTCGGTTTATTCGCGTTCAAAGCCAATTTGCAGCAACGCCGCGTCAAATTAACGCTGCTTTCCAAAGAAAGTGCGGTGCTTTTTTTGAATGTTTTATTGAGTATCGCCACCGTTAGCACCTTTCTCGGCACCTTTTATCCCATGCTGTTCCAAGCCATGAATTGGGGTTCCATTTCCGTCGGTGCGCCTTATTTCAACAGTATTTTCTTGCCGCTGCTTACGCTGATTTTAATCGCCATGGTGTTTTCCCTCGGCTTGCACTGGGCGAAGGCGGACAAAGGCATTTTGTTTAAACGCGCGGCGTTGTTACTGCCGTCTTTGTTGATCGCTTATTTTATGATTCGTCAGGTGATGCAAAACGACAGCGCTTTGCAGTTTAACCTGACGGCATATTTTCTGTTCACCTTGGCGATCTGGCTCTTATCGGCGACCTTATGGCAAAATTGGTGCAAGTTAAGTGTTTCCCGTTACGCCATGATTTTCGCCCACAGCGGCGTTGCCATTGCGACCATGGGCGCGGTGATGAGCAGTTACTTCGGTAGTGAAATCGGCGTGCGTTTGTCGCCGCAAGAGAGCCAAACCTTGGGGCAATTTGATTTTCGATATACGCGTTTCTCCAGTGAAATCGGACCGAATTTTACCGCTGAAGTGGCGGATTTTCATGTCACGGCGAACGGTAAACCTTATGCTGATTTGCAGCCGGAGCGCCGTTATTATGATGTGCGTACTATGACCATGAGCGAAGTGGGGCTTGCCGGCGGGTTTTGGGGCGATTTGTATATTGTGATGGGCGATCCGCTCGGCAAAGGCGAGTTTACCTTCCGCCTGCATTACAAACCGCTGATTCGCTGGTTATGGCTAGGCGGTGTGTTAATGGCGTTCGGGGCGTTGTGTTCCCTATTGACGATGAAGCGAAAAGGAAAGCGTGATGAA","","","71314","LLLAVVPQLGLWLRKPALTQLAWGLSYCFGLFTLAPISILAYSFAADDFTLEYVAAHSNSQLPTFFKIAATWGGHEGSMLFWLFSLSVWVVLFALFNRKNDRTFVAQSLVILGLICFSFAVFIVFFSNPFGRIFPAPLEGRDLNPMLQDVGLIFHPPLLYLGYVGFAVNFAISITALLHQHLERQIAQIMRAWVSVSWLFLTLGIVLGAWWAYYELGWGGWWFWDPVENASLMPWLLGLALLHSLIVSEKRGIFNYWTTLFSLLAFAFSVLGTFIVRSGALTSVHAFAVDSQRGSALLLIFFLLTVGSLGLFAFKANLQQRRVKLTLLSKESAVLFLNVLLSIATVSTFLGTFYPMLFQAMNWGSISVGAPYFNSIFLPLLTLILIAMVFSLGLHWAKADKGILFKRAALLLPSLLIAYFMIRQVMQNDSALQFNLTAYFLFTLAIWLLSATLWQNWCKLSVSRYAMIFAHSGVAIATMGAVMSSYFGSEIGVRLSPQESQTLGQFDFRYTRFSSEIGPNFTAEVADFHVTANGKPYADLQPERRYYDVRTMTMSEVGLAGGFWGDLYIVMGDPLGKGEFTFRLHYKPLIRWLWLGGVLMAFGALCSLLTMKRKGKRDE","32021","","cytochrome c-type biogenesis protein","Inner membrane, Cytoplasm","","
InterPro
IPR002541
Family
Cytochrome c assembly protein
PF01578\"[72-281]TCytochrom_C_asm
InterPro
IPR003567
Family
Cytochrome c-type biogenesis protein
PR01410\"[63-89]T\"[115-132]T\"[142-164]T\"[193-219]T\"[227-247]T\"[257-277]T\"[277-293]T\"[293-312]TCCBIOGENESIS
InterPro
IPR003568
Family
Cytochrome c-type biogenesis protein CcmF
TIGR00353\"[36-614]TnrfE: cytochrome c-type biogenesis protein
InterPro
IPR003570
Family
Cytochrome c-type biogenesis protein NrfE
PR01413\"[301-316]T\"[322-340]T\"[356-368]T\"[490-509]T\"[603-616]TNRFEBIOGNSIS
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[302-446]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-45]?signal-peptide
tmhmm\"[21-41]?\"[78-96]?\"[106-126]?\"[159-179]?\"[194-214]?\"[220-238]?\"[253-275]?\"[294-314]?\"[334-354]?\"[373-393]?\"[403-423]?\"[437-457]?\"[467-487]?\"[590-610]?transmembrane_regions


","No hits to the COGs database.","Significant hit (3.5e-114) to 8/8 blocks of the PR01410 family, which is described as \"Cytochrome c-type biogenesis protein signature\". Prints database entry for PR:PR01410. PR01410A 63-89 1.4e-17 PR01410B 115-132 6.6e-07 PR01410C 142-164 1.4e-19 PR01410D 193-219 5.1e-20 PR01410E 227-247 7.7e-16 PR01410F 257-277 6e-11 PR01410G 277-293 9.2e-09 PR01410H 293-312 8.7e-05","Residues 277 to 614 match (6e-07) PD:PD320716 which is described as C-TYPE PROTEOME COMPLETE CCMF BIOGENESIS CYTOCHROME ","","","","","Wed Feb 19 16:23:52 2003","","","","Wed Feb 19 16:23:52 2003","","","Tue Nov 26 15:58:52 2002","","Thu Mar 18 09:17:36 2004","Thu Mar 18 09:17:36 2004","Thu Mar 18 09:17:36 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00041 is paralogously related to AA00055 (1e-141) and AA00058 (1e-04).","Thu Mar 18 09:17:36 2004","","","","","Residues 72 to 281 (E-value = 1.1e-76) place AA00041 in the Cytochrom_C_asm family which is described as Cytochrome C assembly protein (PF01578)","Thu Mar 18 09:17:36 2004","","","","Thony-Meyer,L., Fischer,F., Kunzler,P., Ritz,D. and Hennecke,H. Escherichia coli genes required for cytochrome c maturation J. Bacteriol. 177 (15), 4321-4326 (1995) PubMed: 7635817Ren Q, Ahuja U, Thony-Meyer L.A bacterial cytochrome c heme lyase. CcmF forms a complex with the heme chaperone CcmE and CcmH but not with apocytochrome c.J Biol Chem. 2002 Mar 8;277(10):7657-63.PMID: 11744735 Thony-Meyer L.Haem-polypeptide interactions during cytochrome c maturation.Biochim Biophys Acta. 2000 Aug 15;1459(2-3):316-24. Review.PMID: 11004446","","Mon Feb 17 06:33:57 2003","1","","","" "AA00042","33950","34315","366","TTGTGGTTTTTAATTGGTTCAATTTTATTGGGTATAACAAGTTCGGTTTTCGCCGAAGGCGAGTTACTTTTCTTTGCTTCGCCAAAGAAAAGTAACCAAAAGAAAGGCGACCCTGTTTTGCCTTATTTCCCTTGTTCCATTGAATTTGCTTCACGGAAATTTTGTAAACTCGCTTCGCTCAAACAGTACAAAATTTCCTACAAATTCAATTCCACAAGGGCGGCAAAGAAGGGAATCCAATTTCTTTTTCCGAATAAAGTGCGGTCATTTTTTCAAGCGTTTTTATCATTAAAAAACTATTTTAAAAACCACCGCACTTTTAATAATGCACCATGGGGGCCCCATCTGACCCGCCTGAGCGACTTG","","","14020","LWFLIGSILLGITSSVFAEGELLFFASPKKSNQKKGDPVLPYFPCSIEFASRKFCKLASLKQYKISYKFNSTRAAKKGIQFLFPNKVRSFFQAFLSLKNYFKNHRTFNNAPWGPHLTRLSDL","34315","","hypothetical protein","Periplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide
tmhmm\"[4-26]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Tue Dec 3 11:58:13 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00042 is paralogously related to AA00239 (7e-12) and AA00240 (3e-07).","","","","","","","","","","","","","","1","","","" "AA00043","35480","34518","963","ATGACACTAGATTATCCTGTTCCGTTTCATACACCGAACCTCGTGTGGGATTCCAGTATCGCCATCTATTTGTTCTTACTGGGTATTTCTTCCGGTTCCTTATTGCTTGCCGTGCTTTATAAACGCAATCGCAAACCGGAAAAAACAAGCGAAAACTGGATTATTCGCAGTGCTGCGATCTTAGCGCCTGGCACGGTGATTATCGGTTTATTGCTGTTGATTTTCCACTTGGCGCGCCCTTGGACGTTCTGGTATTTGATGTTTAACTACCAGTTCAATTCCGTGATGTCCATGGGGGTACTGTTATTCCAAATCTATATGGCGGCGGTTCTCCTCTGGATTGCGATTCTCTTTAAAAATGAACTTGCCGCCTTGCTCGATAGATTTTTACCGAAATTAAAATTTATCGTGAAATGGATTTTCGCCTGTGAACGCATTACCAACCCGTTGGAACTGTTCCTGTTGTTCCTTGCGGTGTTGCTAGGCGCTTATACCGGTTTCTTATTGTCGGCGTTAATCAGCTACCCGATGCTAAACAATCCCGTATTGCCGGCATTATTCCTCGCTTCGGGCACGTCTTCCGGTATCGCGGCGGTATTCTTAACCATCCTGATTGTGGGCAAATTAAAAGGGCATTCCGACGAAGTGAATTTCATGCATAAATTTGAAGTGCCGATCATGCTCGCCGAACTCTTTTGCATCGGCTGCTTCTTCGCCGGATTATATTTCGGCGGCGGACAAAAAATGGTCGCCATGCACAACGCCCTAAGCGGTTTCTGGGGTGCGATTTTCTGGATCGGCGTCATGCTTATCGGCATCCTCATCCCGCTCGCCGGTAATCTATTGGTTAGCGATAAATTAAGATACAATCGTCATTTCATCATTCTGGTATCTATATTTGATTTAATCGGCGTGTTGTGTCTGCGATATTTTATTTTGTACGGCGGACAATTGACCGTTGCG","","","35993","MTLDYPVPFHTPNLVWDSSIAIYLFLLGISSGSLLLAVLYKRNRKPEKTSENWIIRSAAILAPGTVIIGLLLLIFHLARPWTFWYLMFNYQFNSVMSMGVLLFQIYMAAVLLWIAILFKNELAALLDRFLPKLKFIVKWIFACERITNPLELFLLFLAVLLGAYTGFLLSALISYPMLNNPVLPALFLASGTSSGIAAVFLTILIVGKLKGHSDEVNFMHKFEVPIMLAELFCIGCFFAGLYFGGGQKMVAMHNALSGFWGAIFWIGVMLIGILIPLAGNLLVSDKLRYNRHFIILVSIFDLIGVLCLRYFILYGGQLTVA","34518","","formate dependent nitrite reductase, transmembrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR005614
Family
Polysulphide reductase, NrfD
PF03916\"[6-321]TNrfD
noIPR
unintegrated
unintegrated
signalp\"[1-32]?signal-peptide
tmhmm\"[19-39]?\"[59-79]?\"[98-118]?\"[153-173]?\"[187-207]?\"[222-244]?\"[263-283]?\"[293-313]?transmembrane_regions


","BeTs to 3 clades of COG3301COG name: Formate-dependent nitrite reductase, membrane componentFunctional Class: PThe phylogenetic pattern of COG3301 is a-------------e--h--------Number of proteins in this genome belonging to this COG is","","Residues 263 to 320 match (9e-11) PD:PD565667 which is described as PROTEOME COMPLETE TRANSMEMBRANE NRFD REDUCTASE INNER NITRATE MEMBRANE C CHAIN ","","","","","Mon Feb 17 08:30:31 2003","","","","","","","Tue Nov 26 16:12:24 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00043 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 6 to 321 (E-value = 4.8e-137) place AA00043 in the NrfD family which is described as Polysulphide reductase, NrfD (PF03916)","","","","","Hussain H, Grove J, Griffiths L, Busby S, Cole J. A seven-gene operon essential for formate-dependent nitritereduction to ammonia by enteric bacteria. Mol Microbiol. 1994 Apr;12(1):153-63. PMID: 8057835","","Tue Nov 26 16:12:24 2002","1","","","" "AA00044","36154","35480","675","ATGACAGCCTGTTCACGCCGAAACTTTGTTTCCGGCATGGGGGCGTTAATCCTTATGACGGGGACATCAGTCACCTCTTTGGCAAAAGAGGAAAAGGCGGATAAACCGAAACGCTACGCCATGGTGCACGATGAAAACGCGTGCATCGGCTGTACCGCTTGTATGGATGCCTGTCGTGAAACCAACCAAGTGCCGCAAGGCGTTTCCCGCTTGGAGATTTTGCGCAGCGAGCCTTACGGCGAATTTCCGAATCAGGAATATGAGTTTTTCCGCCAATCTTGCCAACATTGCACCAACGCGCCTTGCGTAGCGGTTTGCCCGACCGGCGCGTCATTTATCGATAAAGATACCGGCATTGTGGATGTACACAAAGAGTTGTGCGTCGGTTGCCAATACTGTATCGCCGTTTGTCCGTATCGCGTGCGCTTTATTCATCCGGTGCACAGAACGGCGGATAAATGTAATTTCTGTCGCGATACCAACCTGGCACAAGGCAAACAACCAGCTTGTGTTGAAGCCTGCCCGACCAAAGCCTTAACCTTTGGTGATATGAACGATCCGACCAGCGCAGTGGCTCGCAAGGTAAAAGAAAAACCTGTTTACCGCACGAAAGTGGAATTGGGAACCCAACCGAATCTTTACCATATTCCATTCCAACATGGAGAACCGAAAAGA","","","24990","MTACSRRNFVSGMGALILMTGTSVTSLAKEEKADKPKRYAMVHDENACIGCTACMDACRETNQVPQGVSRLEILRSEPYGEFPNQEYEFFRQSCQHCTNAPCVAVCPTGASFIDKDTGIVDVHKELCVGCQYCIAVCPYRVRFIHPVHRTADKCNFCRDTNLAQGKQPACVEACPTKALTFGDMNDPTSAVARKVKEKPVYRTKVELGTQPNLYHIPFQHGEPKR","35480","","formate dependent nitrite reductase, Fe-S protein/ anaerobic DMSO reductase B","Periplasm","","
InterPro
IPR001450
Domain
4Fe-4S ferredoxin, iron-sulfur binding
PR00353\"[41-52]T\"[169-180]T4FE4SFRDOXIN
PF00037\"[41-64]T\"[120-143]T\"[147-180]TFer4
PS00198\"[127-138]T4FE4S_FERREDOXIN
InterPro
IPR006311
Domain
Twin-arginine translocation pathway signal
TIGR01409\"[4-28]TTAT_signal_seq: Tat (twin-arginine transloc
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.20\"[66-156]Tno description
PTHR11938\"[42-186]TFAD NADPH DEHYDROGENASE/OXIDOREDUCTASE
PTHR11938:SF10\"[42-186]TMOLYBDOPTERIN OXIDOREDUCTASE
signalp\"[1-28]?signal-peptide


","BeTs to 10 clades of COG0437COG name: Fe-S-cluster-containing hydrogenase components 1Functional Class: CThe phylogenetic pattern of COG0437 is ao--kz-q------efgh--uj----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.8e-10) to 2/2 blocks of the PR00353 family, which is described as \"4Fe-4S ferredoxin signature\". Prints database entry for PR:PR00353. PR00353A 41-52 0.002 PR00353B 169-180 3.4e-05 PR00353A 120-131 0.29Significant hit ( 9.2e-06) to 2/3 blocks of the PR00354 family, which is described as \"7Fe ferredoxin signature\". Prints database entry for PR:PR00354. PR00354A 94-104 14 PR00354C 122-139 0.00035","Residues 152 to 216 match (9e-07) PD:PD057141 which is described as PROTEOME COMPLETE SUBUNIT IRON-SULFUR OXIDOREDUCTASE REDUCTASE BINDING MOLYBDOPTERIN B DEHYDROGENASE ","","","","","Mon Feb 17 08:32:29 2003","","","","","","","Tue Nov 26 16:17:17 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00044 is paralogously related to AA02677 (1e-24), AA01138 (2e-22), AA02683 (2e-13), AA01807 (6e-05) and AA00550 (2e-04).","","","","","","Residues 120 to 143 (E-value = 1.9e-05) place AA00044 in the Fer4 family which is described as 4Fe-4S binding domain (PF00037)","","","","","Hussain H, Grove J, Griffiths L, Busby S, Cole J. A seven-gene operon essential for formate-dependent nitritereduction to ammonia by enteric bacteria. Mol Microbiol. 1994 Apr;12(1):153-63. PMID: 8057835","","Tue Nov 26 16:17:17 2002","1","","","" "AA00046","36816","36154","663","ATGAATGTAACTTCCTTAATCCGCAAACCTGTAAAAGCGCTCGCACTGTTCGCTATGCTTGCGGCGCTGCCGATGGTTGCACAGGCGAAAACGCCATCGGCTGATAATCAGCTGACTTATGAACCGCAGTTGGACAATCAACGGGATCCGAATCAATATTGCGCCAAATGCCATAAATTTGACAAAGTGGATAAAAGCCAAACCTTGGATCAATCCGGCGGCGAATTGCATTTCGGTAAATTCCACGGCGCCCATTTAAGCCAAAAAAATCCGAATAACGGTAAACCGATTAATTGTGTGAACTGCCACGGTAATATTTCCGAAGATCACCGTCGTGGTGCGAAAGACGTGATGCGTTTTGAAGGTGATATTTTCGGTGAGAAAAAACCGATGTATAGCGCACAAGAACAAAACCAAGTGTGTTTTTCTTGTCATCAACAGGACAAACTGCGTGAAAAATTCTGGGCGCATGATGTGCACGCCATGAAATTACCTTGCGCAAGCTGCCACACATTGCACCCGAAAGCGGATGCGATGAAAGACATTGAACCGAAAAATCACGTAAAACTTTGTGTGGATTGCCATGGAAAACAACAGGCAGAGCAACAAAAACGCAAAGCACAACAAGAACAAACTCCATCAACCGAACAAAAGGGTAAACAA","","","24970","MNVTSLIRKPVKALALFAMLAALPMVAQAKTPSADNQLTYEPQLDNQRDPNQYCAKCHKFDKVDKSQTLDQSGGELHFGKFHGAHLSQKNPNNGKPINCVNCHGNISEDHRRGAKDVMRFEGDIFGEKKPMYSAQEQNQVCFSCHQQDKLREKFWAHDVHAMKLPCASCHTLHPKADAMKDIEPKNHVKLCVDCHGKQQAEQQKRKAQQEQTPSTEQKGKQ","36154","","formate dependent nitrite reductase, cytochrome-c type protein","Periplasm","","
InterPro
IPR011031
Domain
Multihaem cytochrome
PS51008\"[49-200]TMULTIHEME_CYTC
InterPro
IPR013237
Domain
Phage P4 alpha, zinc-binding
SM00778\"[94-150]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-29]?signal-peptide


","No hits to the COGs database.","","Residues 43 to 196 match (8e-70) PD:PD036148 which is described as CYTOCHROME COMPLETE PROTEOME C-TYPE NRFB SIGNAL NITRITE PRECURSOR FORMATE-DEPENDENT PENTA-HAEME ","","","","","Mon Feb 17 08:33:08 2003","","","","","","","Wed Nov 27 14:28:38 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00046 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Hussain,H., Grove,J., Griffiths,L., Busby,S. and Cole,J. A seven-gene operon essential for formate-dependent nitrite reduction to ammonia by enteric bacteria Mol. Microbiol. 12 (1), 153-163 (1994) PubMed: 8057835 ","","Tue Nov 26 16:20:40 2002","1","","","" "AA00047","38413","36893","1521","GTGAACGCATTGAGCAAAAGCCTGGTAGTGGCAGCTTCTTTCGCAGCTTTAGGTGTGTTTAATTTGGCAATGGCGGAGTTGGTGTATAAACCGCTTGAGCAACCTGTGGAAGCACCAAATCCGAATCTAAAAATTGAAGCGGTAAACGAACAGTTTGCGGCAAAATACCCGAAACAATTTGCGTCTTGGAAAGCCACCGAAAAAGGCGACAAGATTATTTATGCAGATGAGGAAAATCCACGTTTAATCATATTATGGGGCGGTTATGCCTTTGCGAAAGAATATAACGCACCGCGCGGACACATTTATGCCATTAAAGATTTACGCAATATTTTGCGTACCGGTGCGCCGAAAACCGCTAACGACGGTCCACAACCGATGGCGTGTTGGACCTGTAAAGGTCCGGATGTGCCGCGTTTAATCGCCGAATGGGGAGAAGAAGGCTATTTCAATGGTAAATGGGCAAAAGGCGGGGCGGAAGTGGTGAATGCCATCGGTTGTGCCGACTGTCACGACACGACCTCTAAAGAGTTTGCTGAAGGTAAACCGGCATTGCGAATTGCCCGTCCACACGTTATTCGTGCTTTGGATCATTTAAACAATGCGTTGCAAGCCCGAGCGAAAGCGGAAGGCAAAACACAGCCTGATTTACGTTTCGGCACTGCCGCCCGCACCGAAAAACGGGCGGAAATTTGTGCGAACTGTCACGTTGAATATTATTTCGCAGGTGACTTGAAACAAGTGACTTTCCCATGGAATAACGGTCAAACCGTCGATGACATGGAAAAATACTACGATGACATCGGGTTCACCGACTTCACTCATATCTTATCCAAAGCGCCGATCTTAAAAGCACAACACCCTGACTTTGAAATTTGGTCTTTAGGTATGCACGGTAAAAACGGCGTGACCTGTATCGATTGCCACATGCCGAAAGTGCAAGGGGCGGATGGTAAAGTTTATACCGACCACCAAATTCAAAATCCATTTGATGCCTTTGATAGCACTTGTGCCAACTGTCACGATCAAAGTAAAGAGAAGTTAAAAGACATTGTGGCTTCCCGCAAAAAAGAAGTGAAAGACATTATGGGGCGCTTAGAAAATCAAGTAGTTCGTTTGCACTTTGAAGCGAAAGCCGCATGGGATGCCGGCGCAACCAAAGAAGAAATGGAACCGGCGTTAATGGACATTCGTCACGCGCAATGGCGCTGGGATTACGCCGCAGCCAGCCACGGCGGACATATGCACGCACCTGATGTGATGTTACGCGTGTTAGGTTCCGGTCTTGACCGCGCTGCTGATGCCCGTGCCAAATTGGCTGCCATCTTAACCAAACATGGCGTGAAAACACCGATTGAAGTGCCGGATATTTCCACCGCGGAAAAAGCCTGGAAAGCCGTGGGCATTGACATCGAAAAAGAACGCAAAGCCAAAGAAGAATTCTTAAAAACTGTTGTACCTCAATGGGAAAAAGAAGCGAAAGCCACAGGCAAATTAGCTGAAGATTCCGCAACAAAACAA","","","56545","VNALSKSLVVAASFAALGVFNLAMAELVYKPLEQPVEAPNPNLKIEAVNEQFAAKYPKQFASWKATEKGDKIIYADEENPRLIILWGGYAFAKEYNAPRGHIYAIKDLRNILRTGAPKTANDGPQPMACWTCKGPDVPRLIAEWGEEGYFNGKWAKGGAEVVNAIGCADCHDTTSKEFAEGKPALRIARPHVIRALDHLNNALQARAKAEGKTQPDLRFGTAARTEKRAEICANCHVEYYFAGDLKQVTFPWNNGQTVDDMEKYYDDIGFTDFTHILSKAPILKAQHPDFEIWSLGMHGKNGVTCIDCHMPKVQGADGKVYTDHQIQNPFDAFDSTCANCHDQSKEKLKDIVASRKKEVKDIMGRLENQVVRLHFEAKAAWDAGATKEEMEPALMDIRHAQWRWDYAAASHGGHMHAPDVMLRVLGSGLDRAADARAKLAAILTKHGVKTPIEVPDISTAEKAWKAVGIDIEKERKAKEEFLKTVVPQWEKEAKATGKLAEDSATKQ","36893","","formate dependent nitrite reductase, cytochrome c552","Periplasm","","
InterPro
IPR003321
Family
Cytochrome c552
PF02335\"[33-499]TCytochrom_C552
InterPro
IPR011031
Domain
Multihaem cytochrome
PS51008\"[162-346]TMULTIHEME_CYTC
noIPR
unintegrated
unintegrated
PD043029\"[77-428]TNRFA_HAEIN_P45017;
G3DSA:1.20.1270.40\"[323-470]Tno description
G3DSA:3.90.910.10\"[22-321]Tno description
signalp\"[1-25]?signal-peptide


","BeTs to 3 clades of COG3303COG name: Formate-dependent nitrite reductase, periplasmic cytochrome c552 subunitFunctional Class: PThe phylogenetic pattern of COG3303 is --------------e--h--u-----Number of proteins in this genome belonging to this COG is","","Residues 33 to 499 match (4e-228) PD:PD043029 which is described as CYTOCHROME C552 COMPLETE PERIPLASMIC PROTEOME SIGNAL ELECTRON HEME PRECURSOR NITRITE ","","","","","Mon Feb 17 08:33:47 2003","","","","","","","Tue Nov 26 16:32:12 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00047 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Hussain,H., Grove,J., Griffiths,L., Busby,S. and Cole,J. A seven-gene operon essential for formate-dependent nitrite reduction to ammonia by enteric bacteria Mol. Microbiol. 12 (1), 153-163 (1994) PubMed: 8057835 ","","Tue Nov 26 16:32:12 2002","1","","","" "AA00048","39280","38993","288","ATGCAAAAATTGTTACTCGTCACAGTGATTAGTGGTGTTTTAGTTGCTTGTTCTTCTAAGGCTCCACAAATCAATCAAGCTCCTTTAGATAAGCAGACAGTTGAAGCTTATCAAGCGAAAGTGTATAGCGGTAATACGGTGTCGAAGAAATATCAAGTAAGAGACGTTAAACCGGAAGACAATGTGTTAAATGCTAGTGATTCGGAACCGAAAACCGTGATTTATCGCGAGCGTCAGCCAAGACTGGTTGTGACACCGAGCATTGGCTATTATCGCGGTTGGCACTGG","","","10833","MQKLLLVTVISGVLVACSSKAPQINQAPLDKQTVEAYQAKVYSGNTVSKKYQVRDVKPEDNVLNASDSEPKTVIYRERQPRLVVTPSIGYYRGWHW","38993","","conserved hypothetical protein","Outer membrane, Periplasm, Extracellular","","
noIPR
unintegrated
unintegrated
PD068627\"[1-96]TYA99_HAEIN_P44112;
PS51257\"[1-17]TPROKAR_LIPOPROTEIN
signalp\"[1-19]?signal-peptide


","No hits to the COGs database.","","Residues 1 to 96 match (3e-09) PD:PD068627 which is described as PROTEOME COMPLETE TRANSMEMBRANE HI1099 PM0016 ","","","","","","","","","","","","Tue Nov 26 16:35:18 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00048 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00049","39924","39301","624","ATGATGCTTTTCAAAAAATTAACGCTCGGTCTGAGTTTTACTTTCCTTTCATCATTGGCTTTTGCAGAATCTTGGACTATGCATATTTCCGAAGATGGCGTGATAACCGATAAAACCGCTCAACAGCTTAATCCGGCTAGGTATGCCGGAGCTGTGTACAAACAACAATTTTCTTTTTCTGACAGCGGCGGGCAAGGTAAAACCACTTACATTAATCAAAATAACGGCAAGAAATTCGATCCTAAAAATGCTGCTGATGTGAGTGAATTGGGTAAAAGCATCGCCTTTGAAGTGTTTGAGATTAAAGAAAATAAAGACTCTCACTCAGTATTTGAATCCGGCGCCGGCATTTGTTACGGCTTCAAATATACCGATGGCGTCGCGTTCACCGATTCTACAACCTATTATGTAGATAAATCCAAGCAGCAATATTACGCCAGTATCATCGGCGCCACCGTATCTTCTGACGTGGAACCGAAAAACGTGCAATATGCGCCGGTGTTTAATATTCAGGATCCCGAGTTAGATAAAGAAGTAAAGTCGGAAGAACAACGAAACGGTAAAACCTTGATTAATAAAAATTTGCAAAAGAGCAGAGAAATTCTTTCTAACGTAGTTTGTAAG","","","23148","MMLFKKLTLGLSFTFLSSLAFAESWTMHISEDGVITDKTAQQLNPARYAGAVYKQQFSFSDSGGQGKTTYINQNNGKKFDPKNAADVSELGKSIAFEVFEIKENKDSHSVFESGAGICYGFKYTDGVAFTDSTTYYVDKSKQQYYASIIGATVSSDVEPKNVQYAPVFNIQDPELDKEVKSEEQRNGKTLINKNLQKSREILSNVVCK","39301","","conserved hypothetical protein","Periplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide
tmhmm\"[9-29]?transmembrane_regions


","No hits to the COGs database.","","Residues 69 to 208 match (5e-31) PD:PD415486 which is described as PROTEOME COMPLETE PM1509 PM0015 ","","","","","","","","","","","","Tue Nov 26 16:37:14 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00049 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00050","40979","40059","921","ATGAATTTGTGGACAAGCATTTTTGTGTTAACGCTGATTGCCGCGTTAATTTGTTTTTTCCCGTTGCTGTCTGCGCGTTTTGTGCAAACCCAATCAACCCGTCGTGATGATCTCAACAAGGCGTTTTATTTTGAACGTTTAAAAGAGCTGGAATGGGATGAAAAACAAGGCTTGTTGGAAAACGCCGAACAACTCAAAACCGAATTGCAAAAATCCTTATTGGAAGATATTCCGCAACAGCCTGAAAGTGCGGTGCGCAGTGAAAAGAGTTACGGCAAGCTGTGGTTTGTCTCCGGCTTTCTGGTACTCGGCATTTTGTCCGTGTCGGCGTATTTTGTAGTGGGCTCCTGGCAGGCGGAAATTATGTTGGAAAAAAGCGCGGAAAAACTACCGCACTTTTATGAGCGTTTAAAACGTGAAAGCACAAATCCGTTAAACGATGCTGAAATGCAGCAATTTGCCACCGCGTTACGGGTGGATTTGCAAAAAGATCCGAATAATGCGAAGAACTGGTGGTTGTTAGGGCAAATCGGTATGAACTTGGAACAGCCGAGAATGGCATTAGACAGCTTTGCCCGCGCGAATAAATTAGAACCGAAAAATAATCTGTATAAATTGGCGTATGCCCGTATTTTGATGTTCTCCGGGGATGAAACGGATAAATTGAAAGGGGATAGTTTATTGCGCGACGTCATTCGTGAAGATCATACCAACGTTGAAGCTTTGAGTTTGTTGGCGTTCCGTTATTTTGAAACGGAAGACTACAAAATGGCAGCGGTCAGCTGGGCGATGATGTTGAAACTATTACCGAAAGATGACCGGCGTGTTCCGATTATTGAACGAAGTATTCGTTCCGCACGTGATGCGCTGGAAGCACAGAAACAGGAAAAACACCAACAACTGACGCCACAACAGGAAAAA","","","35702","MNLWTSIFVLTLIAALICFFPLLSARFVQTQSTRRDDLNKAFYFERLKELEWDEKQGLLENAEQLKTELQKSLLEDIPQQPESAVRSEKSYGKLWFVSGFLVLGILSVSAYFVVGSWQAEIMLEKSAEKLPHFYERLKRESTNPLNDAEMQQFATALRVDLQKDPNNAKNWWLLGQIGMNLEQPRMALDSFARANKLEPKNNLYKLAYARILMFSGDETDKLKGDSLLRDVIREDHTNVEALSLLAFRYFETEDYKMAAVSWAMMLKLLPKDDRRVPIIERSIRSARDALEAQKQEKHQQLTPQQEK","40059","","cytochrome c-type biogenesis protein precursor (reductase)","Cytoplasm, Periplasm","","
InterPro
IPR011990
Domain
Tetratricopeptide-like helical
G3DSA:1.25.40.10\"[160-272]Tno description
InterPro
IPR013026
Domain
Tetratricopeptide region
SM00028\"[168-201]T\"[239-272]TTPR
PS50005\"[168-201]T\"[239-272]TTPR
PS50293\"[168-272]TTPR_REGION
noIPR
unintegrated
unintegrated
PTHR12558\"[145-295]TCELL DIVISION CYCLE 16,23,27
signalp\"[1-25]?signal-peptide
tmhmm\"[4-24]?\"[94-114]?transmembrane_regions


","No hits to the COGs database.","","Residues 185 to 288 match (2e-38) PD:PD033291 which is described as BIOGENESIS C-TYPE CYTOCHROME COMPLETE PROTEOME LYASE HEME CCMH PRECURSOR SUBUNIT ","","","","","","","","","","","","Tue Dec 10 16:29:07 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00050 is paralogously related to AA00039 (4e-07).","","","","","","","","","","","Reid E, Cole J, Eaves DJ.The Escherichia coli CcmG protein fulfils a specific role in cytochrome c assembly.Biochem J. 2001 Apr 1;355(Pt 1):51-8.PMID: 11256948Fabianek RA, Hofer T, Thony-Meyer L.Characterization of the Escherichia coli CcmH protein reveals new insights into the redox pathway required for cytochrome cmaturation.Arch Microbiol. 1999 Jan;171(2):92-100.PMID: 9914305 ","","Tue Dec 10 16:29:07 2002","1","","","" "AA00052","41530","40982","549","ATGAAAAAAAAACTTTTATTTATATTTATAAGCTCACTTGTTCGTTTATTCACCCCTTCGGGGCCGTTGGCAAAGCCAACGTTCAAAAAACGTTGTTTTTTGTTAACCGCACTTTTCTTCAGCATCAATGTGTTTGCCGCCATCGACGTGCTGAATTTCAGCTCGCCGCAGCAGGAAGCCGACTATCACGCCTTAACGCGGGAACTGCGCTGTCCGCAATGTCAGAATAACAATATCGCCGATTCTAACGCCGCTATTGCTGTGGATATGCGCACTAAAGTGTTTGAATTGTTACAGGAAGGCAAATCCAAACAGGATGTGGTGCAATACATGGTGGATCGCTATGGCAATTTTGTTACTTATGACCCGCCATTGACCGTTGCCACCCTTGTTTTATGGGTTACGCCTTTTGCTTTGATCTTATGCGGGCTGGTATGGCTTTTCGGGCGGAAAAGAACGATGCCGAGTGGGGCGGATAATGCCGCGCCACAGGCCTTAAGTGAAGCACAACAGCAGCGCCTTAATGCTTTGTTAAATAAGGAAAATGAC","","","22351","MKKKLLFIFISSLVRLFTPSGPLAKPTFKKRCFLLTALFFSINVFAAIDVLNFSSPQQEADYHALTRELRCPQCQNNNIADSNAAIAVDMRTKVFELLQEGKSKQDVVQYMVDRYGNFVTYDPPLTVATLVLWVTPFALILCGLVWLFGRKRTMPSGADNAAPQALSEAQQQRLNALLNKEND","40982","","cytochrome c-type biogenesis protein precursor","Periplasm, Inner membrane","","
InterPro
IPR005616
Family
Cytochrome C biogenesis protein
PD005662\"[37-136]TCCMH_HAEIN_P46458;
PF03918\"[28-179]TCcmH
noIPR
unintegrated
unintegrated
signalp\"[1-16]?signal-peptide
tmhmm\"[33-53]?\"[126-148]?transmembrane_regions


","BeTs to 5 clades of COG3088COG name: Uncharacterized protein involved in biosynthesis of c-type cytochromesFunctional Class: OThe phylogenetic pattern of COG3088 is ---------d----ef-hs--j----Number of proteins in this genome belonging to this COG is","","Residues 35 to 136 match (1e-34) PD:PD005662 which is described as CYTOCHROME C-TYPE BIOGENESIS PROTEOME COMPLETE HEME CYCL PERIPLASMIC CCMH PRECURSOR ","","","","","","","","","","","","Wed Nov 27 08:29:55 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00052 is paralogously related to AA00039 (4e-24) and AA01953 (5e-04).","","","","","","Residues 28 to 179 (E-value = 1.4e-72) place AA00052 in the CcmH family which is described as Cytochrome C biogenesis protein (PF03918)","","","","","Allen JW, Tomlinson EJ, Hong L, Ferguson SJ. The Escherichia coli Cytochrome c Maturation (Ccm) System DoesNot Detectably Attach Heme to Single Cysteine Variants of anApocytochrome c. J Biol Chem. 2002 Sep 13;277(37):33559-63. PMID: 12048216 Kranz RG, Beckett CS, Goldman BS. Genomic analyses of bacterial respiratory and cytochrome cassembly systems: Bordetella as a model for the system IIcytochrome c biogenesis pathway. Res Microbiol. 2002 Jan-Feb;153(1):1-6. Review. PMID: 11881892","","Wed Nov 27 08:29:55 2002","1","","","" "AA00054","42081","41533","549","TTGATAATGAAAAAGAAATTATATTTACCTTTAATTATTTTCTTCGTTTTGGTTACCGCCTTTCTGGTGCAATTACAACGCAATGCACTGGGTGATGATCCGAAAGCATTGGAATCGGCGTTGGTGGGTAAGCCGGTTCCGCCGAAGACGTTGCAGGATTTATTATCGGATAAAACCTATGATGAAACGCTGTTTAAACAGGGCAAACCGCTTTTACTCAATGTATGGGCGACATGGTGCCCGACTTGTTATGCGGAGCACCAATATTTGAATCAACTGGCGAAGCAGGGCGTGCCGATTATCGGCTTGGATTATAAAGATAACAGTGCCAAAGCGACGAAATGGCTGAAGAATTTGGGCAATCCTTATCAGGCTGTGTTAAAAGATGAAAAAGGTTCATTTGCCTTGGATTTAGGCGTATATGGCGCGCCGGAAACTTTTCTGGTGGACGGCAACGGCGTGATTCATTATCGCCATGCGGGTGATGTAAACGCGAAAGTGTGGCAGGAAACCTTGCAACCCATTTACCAAAAATTAGGCAGTGCGCAG","","","20429","LIMKKKLYLPLIIFFVLVTAFLVQLQRNALGDDPKALESALVGKPVPPKTLQDLLSDKTYDETLFKQGKPLLLNVWATWCPTCYAEHQYLNQLAKQGVPIIGLDYKDNSAKATKWLKNLGNPYQAVLKDEKGSFALDLGVYGAPETFLVDGNGVIHYRHAGDVNAKVWQETLQPIYQKLGSAQ","41533","From Genbank:[gi:1169432]This protein is involved in disulfide bond formation. It catalyzes a late, reductive step in the assembly of periplasmic c-type cytochromes, probably the reduction of disulfide bonds of the apocytochrome c to allow covalent linkage with the heme.It is a possible subunit of a heme lyase.","cytochrome c biogenesis protein","Periplasm, Inner membrane","","
InterPro
IPR004799
Family
Periplasmic protein thiol:disulfide oxidoreductase DsbE
TIGR00385\"[7-178]TdsbE: periplasmic protein thiol:disulfide o
InterPro
IPR006662
Domain
Thioredoxin-related
PS00194\"[72-90]TTHIOREDOXIN
InterPro
IPR011594
Domain
Thioredoxin-like
PD003679\"[98-174]TDSBE_HAEIN_P45038;
InterPro
IPR012335
Domain
Thioredoxin fold
G3DSA:3.40.30.10\"[33-181]Tno description
InterPro
IPR013740
Domain
Redoxin
PF08534\"[41-182]TRedoxin
noIPR
unintegrated
unintegrated
signalp\"[1-31]?signal-peptide
tmhmm\"[7-25]?transmembrane_regions


","BeTs to 20 clades of COG0526COG name: Thiol-disulfide isomerase and thioredoxinsFunctional Class: O,CThe phylogenetic pattern of COG0526 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","","","","","","","","","","","","Fri Jan 10 11:25:58 2003","Fri Jan 10 11:25:58 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00054 is paralogously related to AA00040 (4e-33), AA02442 (4e-07), AA02010 (4e-06) and AA02915 (5e-04).","","","","","","","","","","","Fabianek,R.A., Hennecke,H. and Thony-Meyer,L. The active-site cysteines of the periplasmic thioredoxin-like protein CcmG of Escherichia coli are important but not essentialfor cytochrome c maturation in vivo J. Bacteriol. 180 (7), 1947-1950 (1998) PubMed: 9537397 Li,Q., Hu,H. and Xu,G. Biochemical characterization of the thioredoxin domain of Escherichia coli DsbE protein reveals a weak reductant Biochem. Biophys. Res. Commun. 283 (4), 849-853 (2001) PubMed: 11350062 Li,Q., Hu,H.Y., Wang,W.Q. and Xu,G.J. Structural and redox properties of the leaderless DsbE (CcmG) protein: both active-site cysteines of the reduced form are involved in its function in the Escherichia coli periplasm Biol. Chem. 382 (12), 1679-1686 (2001) PubMed: 11843181 ","","Fri Jan 10 11:31:08 2003","1","","","" "AA00055","44062","42107","1956","GTGGTTGCAGAATTAGGAAATTATGCCTTAGCCCTAAGTCTGGCGATCGCCGTTTTATTGGCGATTTTCCCTCTATGGGGGGCGGAAAAAGGCAACGCCCAACTGATGTCCTTGGCGCGCCCGATGACTTACGGCTTGTTTTTCGTGTTAACCTTTTCATTTGGTGCTTTGTTTTATTTGTTCGCCGTGAATGATTTCAGCGTGCAATATGTGGTGAACAACTCCAATACCACCTTGCCCATTTACTATCGCTTATCTGCAGTTTGGGGTTCCCACGAAGGTTCATTGCTATTGTGGATTTGGTTGCTGTCGTTGTGGGGCGCGGCAGTCGCCTTGTTTAGTAAACACTTACCGCAGGAAGCCACCGCCCGCGTACTCGGCATTATGGGCATTATCAGCATCGGTTTTCTGCTTTTCGTGTTATTTACCTCCAACCCGTTTAACCGCACTTTCCCTGATTTTCCGGTGGACGGCAAAGAACTGAATCCGTTATTGCAAGATGTTGGCTTAATTTTCCACCCGCCGTTGTTATATATGGGGTATGTTGGTTTTTCCGTTGCGTTTGCTTTTTCCATCGCCTCTTTAATGACCGGTAAACTGGATACCGCATGGGCGCGTTGGTCACGTCCTTGGACCATGGCGGCCTGGATCTTTTTAACTCTGGGTATCGTGCTTGGTTCCTGGTGGGCGTATTACGAACTGGGCTGGGGTGGCTGGTGGTTCTGGGATCCGGTAGAAAACGCCTCTTTCATGCCTTGGCTGGCGGGCACGGCATTGTTGCACTCTTTAGCTGTGACGGAAAAACGGGGTTCTTTCAAAGCCTGGACGGTGTTGCTGGCGATTTTAGCCTTCTCGCTGTGTTTGCTCGGTACTTTCTTAGTGCGTTCCGGTATTTTGGTCTCGGTACACGCCTTTGCCTCCGACCCAACCCGCGGTTTATATGTGTTGGCGTATTTAATCGTGGTGATCGGCGGTTCACTGACCTTATACGCTTATAAAGGCAGCCAAATTCGCTCCCGTGATAATGCGGAACGCTATTCCCGCGAAAGTTTGCTACTGTTAAATAATATTTTATTAATGACCGCACTTTGTGTGGTGTTGCTGGGTACGCTGCTGCCGCTTGTTCACAAACAATTAGGCTTGGGTTCCATTTCCATCGGCGCGCCGTTTTTTGATCAAATGTTCCTGATTATCATGACCCCGTTCGCCTTGTTATTGGGTATCGGACCGCTGGTAAAGTGGCGCCGTGATCAGTTCTCTGCCATTCGCACGCCGGTGATTGTCAGCCTAGTGATTATGCTTCTTGCCGGTTTTGCCTTGCCGTATGCGCTCCAAAACAAATTAACCATCAGCGCCGTACTCGGCACCATGATGTCGGTGATTATCGTGCTGTTAAGCCTGTATGAAATGCAGCAACGGGCGACGCACCGTGAATCTTTTTGGCGCGGTATAACTAAATTATCCCGCTCCCATTGGGGCATGATTTTGGCACATTTGGGGGTCGCCATGACCGTTTGGGGCATTGCCTTCAGTCAAAATTACAGCGTAGAACGGGATGTGCGGATGCACGTCGGTGATACGGTACAAATTGCCGGTTATGATTTCACTTTCAAAGGCATCAGCGATGCCAACGGACCGAACTACATCGGCGGCAAAGCGCAAATTGATATTCATCGTGACGGCAAAAAAGAAACCACGCTTTATGCGGAAAAACGCTTATACACCGTGAGCAAAATGCCGATGACCGAAGCCGCGATCGATTGGGGTTTCAGCCGTGACTTGTATGTGGCGTTAGGTGAAAAATTAGACGACAATTCCTGGGCGTTGCGCTTGTATTACAAACCCTTTATCCGCTGGATATGGCTTGGTGGGTTGTTTATGGTGCTCGGCGGGATATTATGCCTGTTCGACCGCCGTTATCGGTTTAGTAAAATTTTAGGTAAAGAAACCGTGCAG","","","72986","VVAELGNYALALSLAIAVLLAIFPLWGAEKGNAQLMSLARPMTYGLFFVLTFSFGALFYLFAVNDFSVQYVVNNSNTTLPIYYRLSAVWGSHEGSLLLWIWLLSLWGAAVALFSKHLPQEATARVLGIMGIISIGFLLFVLFTSNPFNRTFPDFPVDGKELNPLLQDVGLIFHPPLLYMGYVGFSVAFAFSIASLMTGKLDTAWARWSRPWTMAAWIFLTLGIVLGSWWAYYELGWGGWWFWDPVENASFMPWLAGTALLHSLAVTEKRGSFKAWTVLLAILAFSLCLLGTFLVRSGILVSVHAFASDPTRGLYVLAYLIVVIGGSLTLYAYKGSQIRSRDNAERYSRESLLLLNNILLMTALCVVLLGTLLPLVHKQLGLGSISIGAPFFDQMFLIIMTPFALLLGIGPLVKWRRDQFSAIRTPVIVSLVIMLLAGFALPYALQNKLTISAVLGTMMSVIIVLLSLYEMQQRATHRESFWRGITKLSRSHWGMILAHLGVAMTVWGIAFSQNYSVERDVRMHVGDTVQIAGYDFTFKGISDANGPNYIGGKAQIDIHRDGKKETTLYAEKRLYTVSKMPMTEAAIDWGFSRDLYVALGEKLDDNSWALRLYYKPFIRWIWLGGLFMVLGGILCLFDRRYRFSKILGKETVQ","42107","From Genbank:[gi:1168839] This protein is required for the biogenesis of c-type cytochromes. It is a possible subunit of a heme lyase.","cytochrome c-type biogenesis protein","Inner membrane, Cytoplasm","","
InterPro
IPR002541
Family
Cytochrome c assembly protein
PF01578\"[89-299]TCytochrom_C_asm
InterPro
IPR003567
Family
Cytochrome c-type biogenesis protein
PR01410\"[80-106]T\"[132-149]T\"[160-182]T\"[211-237]T\"[245-265]T\"[275-295]T\"[295-311]T\"[311-330]TCCBIOGENESIS
InterPro
IPR003568
Family
Cytochrome c-type biogenesis protein CcmF
PR01411\"[4-28]T\"[113-136]T\"[190-205]T\"[314-329]T\"[352-369]T\"[395-414]T\"[631-644]TCCMFBIOGNSIS
TIGR00353\"[53-641]TnrfE: cytochrome c-type biogenesis protein
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[13-201]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-28]?signal-peptide
tmhmm\"[10-28]?\"[43-63]?\"[95-113]?\"[125-145]?\"[177-197]?\"[212-232]?\"[238-260]?\"[275-295]?\"[314-332]?\"[353-375]?\"[394-412]?\"[422-442]?\"[448-468]?\"[490-510]?\"[616-636]?transmembrane_regions


","BeTs to 9 clades of COG1138COG name: Cytochrome c biogenesis factorFunctional Class: OThe phylogenetic pattern of COG1138 is a----z---d----efghs--jx---Number of proteins in this genome belonging to this COG is","Significant hit (5.1e-137) to 8/8 blocks of the PR01410 family, which is described as \"Cytochrome c-type biogenesis protein signature\". Prints database entry for PR:PR01410. PR01410A 80-106 1.3e-19 PR01410B 132-149 5.2e-11 PR01410C 160-182 1.3e-18 PR01410D 211-237 3.8e-25 PR01410E 245-265 6.9e-18 PR01410F 275-295 3.7e-16 PR01410G 295-311 8.9e-13 PR01410H 311-330 1.6e-06Significant hit ( 4.9e-77) to 7/7 blocks of the PR01411 family, which is described as \"Cytochrome c-type biogenesis protein CcmF signature\". Prints database entry for PR:PR01411. PR01411A 4-28 2.2e-14 PR01411B 113-136 5e-13 PR01411C 190-205 6.9e-08 PR01411D 314-329 3.3e-06 PR01411E 352-369 1.4e-09 PR01411F 395-414 3.8e-10 PR01411G 631-644 8.8e-07","Residues 182 to 215 match (7e-09) PD:PD511984 which is described as C-TYPE BIOGENESIS CYTOCHROME COMPLETE PROTEOME CCMF MEMBRANE INNER TRANSMEMBRANE PERIPLASMIC ","","","","","","","","","","","Fri Jan 10 13:02:28 2003","Wed Nov 27 11:07:29 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00055 is paralogously related to AA00041 (1e-141).","","","","","","Residues 89 to 299 (E-value = 3.1e-83) place AA00055 in the Cytochrom_C_asm family which is described as Cytochrome C assembly protein (PF01578)","","","","","Hussain,H., Grove,J., Griffiths,L., Busby,S. and Cole,J. A seven-gene operon essential for formate-dependent nitrite reduction to ammonia by enteric bacteria Mol. Microbiol. 12 (1), 153-163 (1994) PubMed: 8057835 Thony-Meyer,L., Fischer,F., Kunzler,P., Ritz,D. and Hennecke,H. Escherichia coli genes required for cytochrome c maturation J. Bacteriol. 177 (15), 4321-4326 (1995) PubMed: 7635817","","Wed Nov 27 11:07:29 2002","1","","","" "AA00056","44580","44065","516","ATGAACCCAAGACGTAAATCCCGTTTGTCTGTTGTTTTATTTGTCTTGTTAGGTGTCGCGGTGGCTTCGGCATTGGTGTTGTACGCGTTACGCCAAAATATCGATTTATTCTATACCCCGTCGGAAGTGGTGTACGGCAAAAATGACAATGCCGATCAAAAACCGGAAGTAGGGCAGCGCATTCGCGTCGGCGGCATGGTGGTTGCCGGCACGGTGCAACGGGATTCGAAAAGCCTGAAAGTGCAGTTTGATTTAAACGACATTGGACCGTCCATCAGCGTGGAATATGAAGGTATCTTGCCGGATTTATTCCGTGAAGGGCAGGGCATTGTGGCACAGGGCGTGCTAAAAGAACCTACCTTGTTGGAAGCCACCGAAGTATTGGCAAAACACGATGAAAATTATGTGCCGCCGGATCTGGAACAGCAAATGCAGAAAATCCATAAACCGATGGGCATCTCTGATCTGAAAGGCGAAAGCGAACGCGATCGTCAGGAAAAAATGAAAGAAGGTCAG","","","19146","MNPRRKSRLSVVLFVLLGVAVASALVLYALRQNIDLFYTPSEVVYGKNDNADQKPEVGQRIRVGGMVVAGTVQRDSKSLKVQFDLNDIGPSISVEYEGILPDLFREGQGIVAQGVLKEPTLLEATEVLAKHDENYVPPDLEQQMQKIHKPMGISDLKGESERDRQEKMKEGQ","44065","From PF03100CcmE is the product of one of a cluster of Ccm genes that are necessary for cytochrome c biosynthesis in eubacteria.Expressions of these proteins is induced when the organisms are grown under anaerobic conditions with nitrate or nitrite as the final electron acceptor.","cytochrome c-type biogenesis protein","Periplasm, Inner membrane, Cytoplasm","","
InterPro
IPR004329
Family
CcmE/CycJ protein
PD006742\"[38-133]TQ9CPM8_PASMU_Q9CPM8;
PF03100\"[2-139]TCcmE
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[26-131]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-24]?signal-peptide
tmhmm\"[10-30]?transmembrane_regions


","BeTs to 7 clades of COG2332COG name: Cytochrome c-type biogenesis protein CcmEFunctional Class: OThe phylogenetic pattern of COG2332 is ---------d----efghs--jx---Number of proteins in this genome belonging to this COG is","","Residues 1 to 139 match (7e-54) PD:PD006742 which is described as CYTOCHROME C-TYPE BIOGENESIS PROTEOME COMPLETE CCME CYCJ TRANSMEMBRANE MEMBRANE INNER ","","","","","","","","","","","Mon Jan 13 09:35:42 2003","Wed Nov 27 11:12:25 2002","","Wed Mar 10 09:28:23 2004","","Wed Mar 10 09:28:23 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00056 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Mar 10 09:28:23 2004","","","","","Residues 2 to 139 (E-value = 8.9e-84) place AA00056 in the CcmE family which is described as CcmE (PF03100)","Wed Mar 10 09:28:23 2004","","","","Thöny-Meyer L, Fischer F, Künzler P, Ritz D, Hennecke H.Escherichia coli genes required for cytochrome c maturation.J Bacteriol. 1995 Aug;177(15):4321-6.PMID: 7635817","","Wed Mar 10 09:28:23 2004","1","","","" "AA00057","44801","44580","222","GTGTTTACCGGGGGAAATATGTTTTTTCAATCTTGGAGTGAGTTTATCAACATGGGAGGCTACGGTTTTTATGTGTGGCTTTCTTATGGTTTAAGTTTATTGGTGATTGGGGTGTTAATTGTGCAAAGCCTTGCTGGCAAAAGTGCGGTGTTAAAATCCATCAAACATGAACAACAACGTGAAACCCGTTTACAACAACTGAAACAAAAAGGAGAAGCGCTA","","","8311","VFTGGNMFFQSWSEFINMGGYGFYVWLSYGLSLLVIGVLIVQSLAGKSAVLKSIKHEQQRETRLQQLKQKGEAL","44580","From PF04995The CcmD protein is part of a C-type cytochrome biogenesis operon.The exact function of this protein is uncertain.It has been proposed that CcmC, CcmD and CcmE interact directly with each other,establishing a cytoplasm to periplasm haem delivery pathway for cytochrome c maturation. This protein is found fused to CcmE. These proteins contain a predicted transmembrane helix.","cytochrome c-type biogenesis protein","Inner membrane, Cytoplasm, Extracellular","","
InterPro
IPR007078
Family
Heme exporter protein D (CcmD)
PF04995\"[19-64]TCcmD
noIPR
unintegrated
unintegrated
signalp\"[1-45]?signal-peptide
tmhmm\"[25-45]?transmembrane_regions


","BeTs to 4 clades of COG3114COG name: Heme exporter protein DFunctional Class: NThe phylogenetic pattern of COG3114 is --------------efgh--------Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","Mon Jan 13 10:11:24 2003","Mon Jan 13 10:04:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00057 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 19 to 64 (E-value = 9e-18) place AA00057 in the CcmD family which is described as Heme exporter protein D (CcmD) (PF04995)","","","","","Thony-Meyer,L., Fischer,F., Kunzler,P., Ritz,D. andHennecke,H. Escherichia coli genes required for cytochrome c maturation Journal of bacteriology. 177 (15), 4321-4326 (1995) PubMed: 7635817 ","","Tue Dec 3 12:30:00 2002","1","","","" "AA00058","45538","44804","735","ATGTGGAAGTGGTTGCATCCTTATGCAAAGTCGGAAACACAATATCGATTATGCGGCAAGTTTAGCCCTTTCTTTGCGATTTTAACCGCACTTTTATTAGCGGTCGGTGTCGTTTGGGGGCTGGCATTCGCACCGGCGGATTATCAACAGGGCAATAGTTTCCGCATTATGTATGTGCACGTACCGACGGCGATTTGGTCTATGGGCGTTTACGGCTCCATGGCGATTGCTGCGTTGGTGGCGTTAGTGTGGCAAATTAAACAGGCGCAGCTGGCGATGATTGCCATGGCGCCGATTGGGGCGTTATTTACGTTCTTAGCGTTGGTTACCGGTGCTATTTGGGGCAAACCCATGTGGGGTACCTGGTGGGTGTGGGATGCCCGTTTAACCGCCGAATTAATTTTGTTTTTCTTATATTTAGGCGTACTCGCCTTATATTCCGCCTTTCAGGATCGCAATGTGGGCGCAAAAGCCGCCTGCGTATTATGCCTTGTGGGCGTGGTGAATCTGCCGATTATCCATTTCTCGGTGGAATGGTGGAATACGTTGCATCAAGGGGCGAGCATTACCAAACTGGAGCGCCCGTCCATTGCCACGCCGATGTTGATTCCGTTGATTTTATGTATCTTCGGTTTTATGACTTTATCAATTTGGTTAACCTTAGTGCGTTACCGCAATGAATTATTAAAAGAAGATGCCAAACGCCCGTGGGTTAAAGCGTTGGCTGAAAAACTT","","","27570","MWKWLHPYAKSETQYRLCGKFSPFFAILTALLLAVGVVWGLAFAPADYQQGNSFRIMYVHVPTAIWSMGVYGSMAIAALVALVWQIKQAQLAMIAMAPIGALFTFLALVTGAIWGKPMWGTWWVWDARLTAELILFFLYLGVLALYSAFQDRNVGAKAACVLCLVGVVNLPIIHFSVEWWNTLHQGASITKLERPSIATPMLIPLILCIFGFMTLSIWLTLVRYRNELLKEDAKRPWVKALAEKL","44804","From Genbank:[gi:1168830] This protein is required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.","cytochrome c-type biogenesis protein","Inner membrane, Cytoplasm","","
InterPro
IPR002541
Family
Cytochrome c assembly protein
PF01578\"[5-184]TCytochrom_C_asm
InterPro
IPR003557
Family
Cytochrome c-type biogenesis protein CcmC
PR01386\"[45-62]T\"[62-82]T\"[100-120]T\"[121-141]T\"[156-182]T\"[204-228]TCCMCBIOGNSIS
TIGR01191\"[45-228]TccmC: heme exporter protein CcmC
noIPR
unintegrated
unintegrated
signalp\"[1-40]?signal-peptide
tmhmm\"[21-43]?\"[62-82]?\"[97-117]?\"[123-143]?\"[153-173]?\"[202-222]?transmembrane_regions


","BeTs to 16 clades of COG0755COG name: ABC-type transport system involved in cytochrome c biogenesis, permease componentFunctional Class: OThe phylogenetic pattern of COG0755 is a----z-q-dr-bcefghsnujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 2.5e-99) to 6/6 blocks of the PR01386 family, which is described as \"Cytochrome c-type biogenesis protein CcmC signature\". Prints database entry for PR:PR01386. PR01386A 45-62 1e-14 PR01386B 62-82 2.8e-10 PR01386C 100-120 1.9e-17 PR01386D 121-141 1.5e-18 PR01386E 156-182 5e-20 PR01386F 204-228 1.6e-11","Residues 1 to 55 match (8e-09) PD:PD555327 which is described as PROTEOME COMPLETE CCMC ","","","","","Mon Feb 17 11:23:38 2003","","","","","","Mon Jan 13 11:04:41 2003","Mon Jan 13 10:47:43 2003","","Thu Mar 18 09:19:08 2004","Wed May 12 16:13:18 2004","Thu Mar 18 09:19:08 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00058 is paralogously related to AA00041 (4e-05).","Thu Mar 18 09:19:08 2004","","","","","Residues 5 to 184 (E-value = 8.8e-63) place AA00058 in the Cytochrom_C_asm family which is described as Cytochrome C assembly protein (PF01578)","Thu Mar 18 09:19:08 2004","","","","Thony-Meyer,L., Fischer,F., Kunzler,P., Ritz,D. andHennecke,H. Escherichia coli genes required for cytochrome c maturation Journal of bacteriology. 177 (15), 4321-4326 (1995) PubMed: 7635817 ","","Wed Nov 27 11:27:03 2002","1","","","" "AA00059","46214","45552","663","ATGATTTTTTGGCAGATTATTAAACGCGAATTACAAATCGCCATGCGTAAACAGGCGGAAATTTTGAATCCGTTGTGGTTTTTCCTCATCGTGATTACGTTGTTTCCGCTGGTTATCGGACCTGATCCGAAACTGCTTTCCCGTATCGCGCCCGGTGTGGCTTGGGTGGCGGCGTTGTTGTCTGCATTGCTGTCTTTTGAGCGCTTATTTCGGGATGATTTTATTGACGGTTCTCTGGAACAACTCATGCTCACGCCGCAACCGTTGATGTTGACGGCATTGGCGAAAGTGCTTGCTCATTGGTTGCTCACGGGCTTGCCGTTGATTTTGTTATCGCCTGTCGCCGCATTATTGCTGTCATTGGAAAGAGCAATTTGGTGGGCATTAGTGCTGACTTTGTTATTAGGTACGCTGGTGTTGAGCTGCCTTGGGGCCATAGGCGTGGCGCTTACGGTGGGGTTGCGCAAAGGCGGCGTATTATTGAGTTTATTGGTGGTGCCGTTGTTTATTCCGGTGCTGATTTTTTCTGCGTCGGTACTGGATGCCGCCGCATTGAATTTACCTTACGGCGGGCAATTAGCCATTCTCGGTGCGATTTTAGCCGCCGTTGTTACCTTATCGCCTTTTGCGATTGCGACGGCGTTGCGGATTAGTTTGGATCAA","","","23809","MIFWQIIKRELQIAMRKQAEILNPLWFFLIVITLFPLVIGPDPKLLSRIAPGVAWVAALLSALLSFERLFRDDFIDGSLEQLMLTPQPLMLTALAKVLAHWLLTGLPLILLSPVAALLLSLERAIWWALVLTLLLGTLVLSCLGAIGVALTVGLRKGGVLLSLLVVPLFIPVLIFSASVLDAAALNLPYGGQLAILGAILAAVVTLSPFAIATALRISLDQ","45552","","heme exporter protein B (cytochrome c-type biogenesis protein)","Inner membrane, Cytoplasm","","
InterPro
IPR003544
Family
Cytochrome c-type biogenesis protein CcmB
PR01414\"[27-48]T\"[53-70]T\"[76-99]T\"[101-119]T\"[156-175]T\"[193-216]TCCMBBIOGNSIS
PF03379\"[3-217]TCcmB
TIGR01190\"[6-216]TccmB: heme exporter protein CcmB
noIPR
unintegrated
unintegrated
signalp\"[1-40]?signal-peptide
tmhmm\"[21-41]?\"[47-65]?\"[97-119]?\"[125-154]?\"[159-179]?\"[193-215]?transmembrane_regions


","BeTs to 5 clades of COG2386COG name: ABC-type transport system involved in cytochrome c biogenesis, permease componentFunctional Class: OThe phylogenetic pattern of COG2386 is a--------d----efghs--j----Number of proteins in this genome belonging to this COG is","Significant hit (7.5e-100) to 7/7 blocks of the PR01414 family, which is described as \"Cytochrome c-type biogenesis protein CcmB signature\". Prints database entry for PR:PR01414. PR01414A 27-48 2.9e-15 PR01414B 53-70 4.2e-10 PR01414C 76-99 4.7e-14 PR01414D 101-119 1.8e-11 PR01414E 132-155 2.2e-14 PR01414F 156-175 5.1e-14 PR01414G 193-216 4.1e-12","Residues 23 to 158 match (2e-19) PD:PD444727 which is described as MITOCHONDRION C CYTOCHROME HEME ORF206 BIOGENESIS B TRANSPORTER PROTEOME SUBUNIT ","","","","","","","","","","","","Wed Nov 27 11:33:16 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00059 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 217 (E-value = 2.1e-123) place AA00059 in the CcmB family which is described as CcmB protein (PF03379)","","","","","Thony-Meyer,L., Fischer,F., Kunzler,P., Ritz,D. andHennecke,H. Escherichia coli genes required for cytochrome c maturation Journal of bacteriology. 177 (15), 4321-4326 (1995) PubMed: 7635817 ","","Wed Nov 27 11:33:16 2002","1","","","" "AA00061","46854","46222","633","ATGCACAATCAACTCAATCTTGAACAACTCGCCTGCCAACGTGGCGACAAAGTGTTATTTCACCACCTGAATTTACACATTCGGGCGGGCGATTTTGTGCAGATTGAAGGGAATAACGGTATCGGTAAAACCAGTTTACTACGCATTATTGCGGGGCTTGCTACGCCGCTGGAAGGAAAAGTGCGGTGGAATTCTGAAGAGATTTTTAAACAGTGTGAAGCTTTTCATGATGATTTGCTGTATTTGGGGCATCAAAATGGGATTAAACCCGAATTGACAGCGTGGGAAAATCTGCATTTTTATCAGCAAATCGGACGCTGCCGGCAGGGCGATGACATTCTGTGGGAAGTGTTGCAAACCGTAGGCTTGCTTGGGCGTGAAGATATTCCGGCGGCGCAACTATCTGCCGGGCAGCAAAAACGCATAGCCTTGGCGCGTTTATGGTTGTCGGAAGCGTCGTTGTGGATTTTAGACGAACCCTTCAATGCTATCGATAAAAAAGGCGTGGCAGTATTGACCGCACTTTTTGAGCGACATGCGCAACATAACGGCATCGTGATTTTAACCAGCCATCAGGAAGTGCCGAGTGCGCGGTTGAAAAAAATCCATTTAGAACAGTTTAAATGTGTAGAA","","","23930","MHNQLNLEQLACQRGDKVLFHHLNLHIRAGDFVQIEGNNGIGKTSLLRIIAGLATPLEGKVRWNSEEIFKQCEAFHDDLLYLGHQNGIKPELTAWENLHFYQQIGRCRQGDDILWEVLQTVGLLGREDIPAAQLSAGQQKRIALARLWLSEASLWILDEPFNAIDKKGVAVLTALFERHAQHNGIVILTSHQEVPSARLKKIHLEQFKCVE","46222","From Genbank:[gi:1168828]This protein is required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.","cytochrome c-type biogenesis ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[133-175]TCCMA_HAEIN_P45032;
PF00005\"[30-192]TABC_tran
PS50893\"[5-207]TABC_TRANSPORTER_2
PS00211\"[134-148]?ABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[29-208]TAAA
InterPro
IPR005895
Family
Heme exporter protein CcmA
PTHR19222:SF5\"[5-198]THEME EXPORTER PROTEIN A
TIGR01189\"[5-204]TccmA: heme ABC exporter, ATP-binding protei
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[5-191]Tno description
PTHR19222\"[5-198]TATP BINDING CASSETE (ABC) TRANSPORTER


","No hits to the COGs database.","Significant hit ( 1.6e-21) to 2/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 19-65 1.4e-10 IPB001140B 131-169 1.9e-09","Residues 73 to 132 match (5e-11) PD:PD019161 which is described as HEME EXPORTER COMPLETE PROTEOME A C-TYPE BIOGENESIS CYTOCHROME CCMA MEMBRANE ","","","","","","","","","","","Mon Jan 13 11:34:25 2003","Mon Jan 13 11:33:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00061 is paralogously related to AA02324 (3e-17), AA02440 (2e-16), AA00700 (3e-15), AA02718 (6e-15), AA01051 (1e-14), AA01867 (2e-14), AA01656 (7e-13), AA02080 (9e-13), AA01645 (3e-12), AA00799 (5e-12), AA02320 (7e-11), AA01510 (7e-11), AA02573 (9e-11), AA01422 (1e-10), AA01779 (2e-10), AA00858 (2e-10), AA01524 (3e-10), AA01820 (4e-10), AA01684 (4e-10), AA01616 (4e-10), AA02484 (6e-10), AA02152 (6e-10), AA01456 (6e-10), AA02353 (9e-10), AA00591 (9e-10), AA02140 (3e-09), AA01824 (4e-09), AA02899 (5e-09), AA01757 (6e-09), AA00933 (8e-09), AA02609 (1e-08), AA01509 (1e-08), AA01393 (7e-08), AA00207 (7e-08), AA02805 (1e-07), AA02606 (2e-07), AA01568 (2e-07), AA02786 (3e-07), AA02550 (4e-07), AA01555 (1e-06), AA00415 (2e-06), AA02331 (2e-06), AA00751 (4e-06), AA02642 (6e-06), A02145 (8e-06), AA01961 (2e-05), AA02898 (5e-05), AA02225 (2e-04) and AA01947 (0.001).","","","","","","Residues 30 to 207 (E-value = 9.6e-30) place AA00061 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Thony-Meyer,L., Fischer,F., Kunzler,P., Ritz,D. andHennecke,H. Escherichia coli genes required for cytochrome c maturation Journal of bacteriology. 177 (15), 4321-4326 (1995) PubMed: 7635817 ","","Wed Nov 27 11:37:34 2002","1","","","" "AA00062","48090","47029","1062","GTGACTAATGATCAGGTGCAGCATACGTTAACGTCCTTTGCTTATGGCTTGGCACTCGGACAGTTGTTCTGGGGACCGTTTGGCGACAGTTTTGGGCGTAAGCCGATTATTTTGTTGGGGGTGACCGTGGCGGCGTTGGCGGCATTGATCCTGACGCAAATCCATGCAATCGGTAATTTCACCGCACTTCGTTTCATTCAAGGCTTTTTTGGCGCAGCACCGGTAGTGTTGGTGGGTGCGCTGTTACGGGATTTGTTCGATAAAAACGAGCTGTCCAAAATGATGTCAACCATCACGCTGGTGTTTATGATAGCACCATTGGTGGCGCCGATTCTGGGCGGTTATATCGTGTATTTCTTCCATTGGCACGCGATTTTTTATGTGATCGCCATGATGGGCTTGTTAAGTATCCTGTTGGTCTTTTTCGTAGTGCCGGAAACCCATCATAAAGAAAAACACATTCCCTTGCGGTTGAACATCATAGCCCGCAATTTCATAGCGTTATGGAAACAAAAACCGGTGCTGGGGTATATGTTCGCCGCTTCTTTTGCTTTCGGGGGCTTATTTTCTTTCATCACGGCGGGGTCTATTGTGTATATCGGCATTTACGGCATTAAGCCGGAGAATTTCGGTTATTTCTTTATGCTGAATATCTCGGTGATGACCTTTGGTTCCTTCCTGAATGGGCGATTGGTGCATAAGGTCGGCGCGGAAACTATGTTGCGCGTTGGTTTGATGGTTCAGTTTTTGGCGGCAATTTGGTTGGTTCTGGTGCTGTTGCTGAATTTGGGCTTTTGGGCAATTGCAATTGGCATTGCGATTTTTGTGGGACAAAACTCGCTGATTTCTTCCAACGCCATGGCGTCCATTTTAGAAAAATTCCCGAATGCCGCCGGCTCGGCAAATTCTATGGTCGGTAGTGTACGTTTCGGCACCGGCGCCTGCGTGGGATCACTGGTTGCCCTTATGAATATGAGCAGCACAACGCCAATGTTGCTGACCATGGCGGCGTGTTCGTTGATGGCGGTGGTTTGCTATTATTTTTTAACCGCGCGCAATTTA","","","43268","VTNDQVQHTLTSFAYGLALGQLFWGPFGDSFGRKPIILLGVTVAALAALILTQIHAIGNFTALRFIQGFFGAAPVVLVGALLRDLFDKNELSKMMSTITLVFMIAPLVAPILGGYIVYFFHWHAIFYVIAMMGLLSILLVFFVVPETHHKEKHIPLRLNIIARNFIALWKQKPVLGYMFAASFAFGGLFSFITAGSIVYIGIYGIKPENFGYFFMLNISVMTFGSFLNGRLVHKVGAETMLRVGLMVQFLAAIWLVLVLLLNLGFWAIAIGIAIFVGQNSLISSNAMASILEKFPNAAGSANSMVGSVRFGTGACVGSLVALMNMSSTTPMLLTMAACSLMAVVCYYFLTARNL","47029","","bicyclomycin resistance protein (Sulfonamide resistance protein)","Inner membrane, Cytoplasm","","
InterPro
IPR004812
Family
Drug resistance transporter Bcr/CflA subfamily
TIGR00710\"[1-350]Tefflux_Bcr_CflA: drug resistance transporte
InterPro
IPR006162
PTM
Phosphopantetheine attachment site
PS00012\"[322-337]?PHOSPHOPANTETHEINE
InterPro
IPR007114
Family
Major facilitator superfamily
PS50850\"[1-354]TMFS
InterPro
IPR011701
Family
Major facilitator superfamily MFS_1
PF07690\"[1-326]TMFS_1
noIPR
unintegrated
unintegrated
PTHR10074\"[1-352]TMAJOR FACILITATOR SUPERFAMILY MEMBER
PTHR10074:SF28\"[1-352]TBICYCLOMYCIN RESISTANCE PROTEIN
signalp\"[1-47]?signal-peptide
tmhmm\"[10-28]?\"[37-59]?\"[65-85]?\"[100-120]?\"[124-144]?\"[179-199]?\"[209-229]?\"[239-257]?\"[263-283]?\"[304-324]?\"[330-350]?transmembrane_regions


","BeTs to 21 clades of COG0477COG name: Permeases of the major facilitator superfamilyFunctional Class: G,E,P,RThe phylogenetic pattern of COG0477 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 192 to 266 match (6e-08) PD:PD413016 which is described as COMPLETE PROTEOME TRANSMEMBRANE TRANSPORTER RESISTANCE MEMBRANE MULTIDRUG PROBABLE EFFLUX PERMEASE ","","","","","Sun Feb 16 15:57:53 2003","","","","","","","Wed Nov 27 12:04:37 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00062 is paralogously related to AA01463 (2e-09), AA01731 (9e-09) and AA00266 (5e-04).","","","","","","","","","","","Bentley,J., Hyatt,L.S., Ainley,K., Parish,J.H., Herbert,R.B. andWhite,G.R.Cloning and sequence analysis of an Escherichia coli gene conferring bicyclomycin resistanceGene 127 (1), 117-120 (1993)PubMed: 8486276 ","","Wed Nov 27 12:04:37 2002","1","","","" "AA00064","49006","48227","780","GTGGTTTTTCCAAATGTTTTTCATCAGGCAGGAAAGTCAATTTGGGTTTATAATGCGGGTAAGGAAAAGAAAAGGATCATTATGCGATTAGATAAATTTTTAGCAGAGCATACGGGGCTGACCCGTTCGCAGGCGACTAAGGCGTTGCGTCAAGGTGCGGTTACGATTAACGGTAAAATTGAGAAGAGCGGGGCGACCAAAGTGTCGCCGCAAGATGCGATTTATTTTGACGGTGAACTACTGACGTGGCTGGATGTCGGGCAATATTTGATGTTTAACAAACCGCAAGGCTATGTATGTTCACACGACGAAGATGAACATCCCTCCATTTATCAGTTTTTCGATTACCCTTTATCCGCCCGTTTGCATAGCGCGGGGCGTTTGGATATAGATACCACGGGCTTGGTGTTGTTAACCGATGACGGGCAATGGTCTCATCGCGTTACTTCGCCAAAACATCATCAGCCGAAAACCTATTTGGTGACGCTGGCGGATCCGGTGGAAGCCAATTATGCACAAGCCTGTGCTGAGGGCATTTTGCTACGCGGCGAGAAAGATCCCACCAAACCGGCGGTACTTGAAATTTTAGATAATTACAACGTGAATTTAACCATTAGCGAAGGGCGTTATCATCAGGTGAAACGGATGTTTGCCGCATTGGGGAATAAAGTGCTCGGGTTGCATCGTTGGAAAATCGGTAATCTGACCTTGGATGACAATTTAGCAGAAGGCGATTTTCGTGCGTTAAACGCGGAAGAAATCGCATATTTTTCCGGAGAA","","","29749","VVFPNVFHQAGKSIWVYNAGKEKKRIIMRLDKFLAEHTGLTRSQATKALRQGAVTINGKIEKSGATKVSPQDAIYFDGELLTWLDVGQYLMFNKPQGYVCSHDEDEHPSIYQFFDYPLSARLHSAGRLDIDTTGLVLLTDDGQWSHRVTSPKHHQPKTYLVTLADPVEANYAQACAEGILLRGEKDPTKPAVLEILDNYNVNLTISEGRYHQVKRMFAALGNKVLGLHRWKIGNLTLDDNLAEGDFRALNAEEIAYFSGE","48227","","ribosomal small subunit pseudouridine synthase","Cytoplasm","","
InterPro
IPR000748
Domain
Pseudouridine synthase, Rsu
TIGR00093\"[93-251]TTIGR00093: conserved hypothetical protein
PS01149\"[126-140]TPSI_RSU
InterPro
IPR002942
Domain
RNA-binding S4
PF01479\"[28-74]TS4
SM00363\"[28-88]TS4
PS50889\"[28-95]TS4
InterPro
IPR006145
Domain
Pseudouridine synthase
PF00849\"[88-219]TPseudoU_synth_2
noIPR
unintegrated
unintegrated
PTHR21600\"[32-256]TRIBOSOMAL LARGE SUBUNIT PSEUDOURIDINE SYNTHASE B
PTHR21600:SF2\"[32-256]TRIBOSOMAL LARGE SUBUNIT PSEUDOURIDINE SYNTHASE B


","BeTs to 17 clades of COG1187COG name: 16S rRNA uridine-516 pseudouridylate synthase and related pseudouridylate synthasesFunctional Class: JThe phylogenetic pattern of COG1187 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 3.9e-60) to 4/4 blocks of the IPB000748 family, which is described as \"Pseudouridine synthase, Rsu family\". Interpro entry for IP:IPR000748. IPB000748A 29-54 1.3e-08 IPB000748B 93-108 1.2e-05 IPB000748C 125-157 6e-19 IPB000748D 203-237 9.8e-23Significant hit ( 1e-07) to 2/4 blocks of the IPB000613 family, which is described as \"Pseudouridine synthase\". Interpro entry for IP:IPR000613. IPB000613B 125-164 0.0027 IPB000613C 207-231 0.014","Residues 28 to 88 match (8e-18) PD:PD595448 which is described as SYNTHASE 16S COMPLETE PROTEOME PSEUDOURIDINE HYDROLYASE A SUBUNIT RSUA URACIL ","","","","","","","","","","","","Wed Nov 27 14:26:59 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00064 is paralogously related to AA01998 (3e-18).","","","","","","Residues 88 to 219 (E-value = 2e-22) place AA00064 in the PseudoU_synth_2 family which is described as RNA pseudouridylate synthase (PF00849)","","","","","Ofengand J, Bakin A, Wrzesinski J, Nurse K, Lane BG. The pseudouridine residues of ribosomal RNA. Biochem Cell Biol. 1995 Nov-Dec;73(11-12):915-24. Review. PMID: 8722007 Wrzesinski J, Bakin A, Nurse K, Lane BG, Ofengand J. Purification, cloning, and properties of the 16S RNApseudouridine 516 synthase from Escherichia coli. Biochemistry. 1995 Jul 11;34(27):8904-13. PMID: 7612632","","Wed Nov 27 12:15:18 2002","1","","","" "AA00065","48994","49146","153","TTGGAAAAACCACCGCACTTTCCCTCATTCACAACCATCCACCAAGAAAATCATCAGGAATGTGTGAAATATCACAGAATTCTTTTGGAATTTAATTATAATATTTGGTGTTTTTTCACCCTATTATTCAAAAAAGAGGATTTATTTTATGGA","","","7427","LEKPPHFPSFTTIHQENHQECVKYHRILLEFNYNIWCFFTLLFKKEDLFYG","49146","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","Mon Dec 9 13:05:43 2002","Mon Dec 9 13:05:43 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00065 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00066","49142","51403","2262","ATGGATGAACAACTTAAAAAAGCCGCACTCGATTTTCATGAATTTCCGATTCCGGGGAAAATTGAAGTTACTCCGACAAAATCTCTTGCAACCCAACGCGATTTAGCGTTGGCGTATTCACCAGGCGTGGCGGCGCCTTGTTTGGCAATTCAGGCGGATCCTGCTGATTCCTATAAATATACCTCGCGCGGCAATCTGGTTGCTGTGATTTCCAACGGAACCGCGGTGCTCGGGTTGGGCAATATCGGCGCGTTAGCCGGTAAGCCGGTGATGGAAGGGAAAGGCGTGTTATTTAAAAAATTCGCCGGGGTGAACGTGTTCGATATTGAAATCAACGAACATGACCCGGATAAATTGGTGGATATTATCGCTTCCCTTGAACCGACTTTCGGCGGGATTAACCTGGAAGACATTAAAGCGCCGGAATGTTTCTATATTGAACGCAAGCTGCGCGAAAGAATGAATATTCCGGTCTTCCATGATGACCAACACGGCACGGCGATCATTTCTGCCGCCGCGGTATTGAACGGTTTACGCATCGTCGGTAAAAAAATTGAAGATGTGAAATTAGTGGCATCCGGCGCGGGTGCAGCATCTATCGCCTGTTTGAACCTGTTGGTTTCCCTAGGCATGAAACGGGAAAATATCACGGTGTGCGACTCCAAGGGGGTCATTTATAAAAACCGTGACGACCGCATGGACGAAACCAAAAAACTTTACGCCATTGATGACAACGGCAAACGCACATTAGCCGACGCCATTCCGAATGCGGATATTTTCTTAGGCTGCTCTGCCGCAGGTGCGTTGACGCAAGATATGGTAAAAACCATGGCGGCGCATCCGTTAATTTTGGCATTGGCGAACCCTGAACCGGAAATTTTACCGCCGCTCGCCAAAGCCGTGCGCCCGGATGCCATTGTGTGTACCGGTCGTTCGGACTATCCGAACCAAGTAAACAACGTCCTGTGCTTCCCGTTCATTTTCCGTGGTGCGTTAGATGTGAGCGCCACCACCATTAACGAAGAAATGAAATTGGCGGCGGTGCGCGCCATTGCCGATTTGGCGTTGGCGGAACAAAGCGAAGTGGTCACCTCCGCTTACGGCGACAGTGAATTGTCCTTCGGCCCGGAATACATCATTCCGAAACCGTTCGATCCGCGCTTGATCGTGCGTATCGCGCCTGCAGTGGCAAAAGCCGCCATGGATTCCGGCGTGGCGACCCGTCCGATTGAAGATTTCGATGCTTATATCGAAAAACTGGCGCAATTCGTTTACAAAACCAACCTGTTCATGAAGCCGGTATTCGCGCAAGCCAAACAGGACAAAAAACGTGTCTTGCTCACCGACGGCGAAGAAACCCGCGTATTACACGCCGTACAGGAAATCGCCACCTTGGGCATTGCCTACCCGATTTTATTGGGTCGTCCGAGCGTCATTGAACAACGCATTAAAAAACTGGGCTTGCACATTCAGGCAGGACGTGATTTCGATCTGATCAACATCGAAAACGATGAACGCTACAACCAATGCTGCACCACCTACTACAATATGCTTAAACGCGCCGGCATCACACCGGGTATTGCCAAACGCGAAATGTTCAATAACCCGACTGCCATCGGTTCCGTGTTGTTACATTTAGGTCATGCCGACGCCATGTTGTGCGGCTTGGTTGGACATTACGCGTCCCACTTAAAAACCATCAAAAACGTCATCGGTTTACGTCCGGGCGTACGCACACCGGCAACGGTGAACGGTTTGGTATTACCAACCGGCAACCTATTCCTGACCGACACCTTCGTGAACAACGATCCGAGCGCAGAAGAACTTGCCGAAATTACCATGATGGCGGCCAAAGAAGTGAGTTTATTCGGTATCGAACCGCAAATTGCCTTGATCTCGCACTCCAATTACGGCAGCAACAACAGCCCAAGTGCGGTCAAAATGCGCGACGTTTTAGCCTTAGTGCGGGAAAAAGCGCCGGAACTCAACATTGACGGCGAAATGCACTGTGACGTGGCGTTGTCTCAACGTTTACGTGACGAAGTGATGCCTGACAGCCCGTTAAAAGGCGCGGCAAATCTGCTCGTCATGCCAAACATGGAAGCGGCACGTATCAGCCTGAACCTGTTACAAGGCACGGCAACACCGACTACCGTAGGGCCGATTCTCATGGGTTTGAACAAACCGGCGCACATTTTGACCTCCGTATCTTCCGTTCGCCGTATTATCAACATGGTGGCAATTGCTGCAGCCAAAGCCCAA","","","81343","MDEQLKKAALDFHEFPIPGKIEVTPTKSLATQRDLALAYSPGVAAPCLAIQADPADSYKYTSRGNLVAVISNGTAVLGLGNIGALAGKPVMEGKGVLFKKFAGVNVFDIEINEHDPDKLVDIIASLEPTFGGINLEDIKAPECFYIERKLRERMNIPVFHDDQHGTAIISAAAVLNGLRIVGKKIEDVKLVASGAGAASIACLNLLVSLGMKRENITVCDSKGVIYKNRDDRMDETKKLYAIDDNGKRTLADAIPNADIFLGCSAAGALTQDMVKTMAAHPLILALANPEPEILPPLAKAVRPDAIVCTGRSDYPNQVNNVLCFPFIFRGALDVSATTINEEMKLAAVRAIADLALAEQSEVVTSAYGDSELSFGPEYIIPKPFDPRLIVRIAPAVAKAAMDSGVATRPIEDFDAYIEKLAQFVYKTNLFMKPVFAQAKQDKKRVLLTDGEETRVLHAVQEIATLGIAYPILLGRPSVIEQRIKKLGLHIQAGRDFDLINIENDERYNQCCTTYYNMLKRAGITPGIAKREMFNNPTAIGSVLLHLGHADAMLCGLVGHYASHLKTIKNVIGLRPGVRTPATVNGLVLPTGNLFLTDTFVNNDPSAEELAEITMMAAKEVSLFGIEPQIALISHSNYGSNNSPSAVKMRDVLALVREKAPELNIDGEMHCDVALSQRLRDEVMPDSPLKGAANLLVMPNMEAARISLNLLQGTATPTTVGPILMGLNKPAHILTSVSSVRRIINMVAIAAAKAQ","51403","","NADP-dependent malic enzyme (NADP-ME)","Cytoplasm, Inner membrane","","
InterPro
IPR001891
Family
Malic oxidoreductase
PS00331\"[159-175]TMALIC_ENZYMES
InterPro
IPR002505
Domain
Phosphate acetyl/butaryl transferase
PF01515\"[429-750]TPTA_PTB
InterPro
IPR012188
Family
Malic enzyme, phosphate acetyl/butaryl transferase
PIRSF036684\"[1-754]TMalic enzyme with phosphate acetyl/butaryl transferase domain
InterPro
IPR012301
Domain
Malic enzyme, N-terminal
PF00390\"[18-161]Tmalic
InterPro
IPR012302
Domain
Malic enzyme, NAD-binding
PF03949\"[163-401]TMalic_M
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.10380\"[2-160]Tno description
G3DSA:3.40.50.720\"[163-424]Tno description
PTHR23406\"[1-442]TMALIC ENZYME-RELATED
PTHR23406:SF2\"[1-442]TMALIC ENZYME


","No hits to the COGs database.","Significant hit ( 1.1e-66) to 5/5 blocks of the IPB002505 family, which is described as \"Phosphate acetyl/butaryl transferase\". Interpro entry for IP:IPR002505. IPB002505A 66-100 5e-13 IPB002505B 595-617 3.1e-09 IPB002505C 627-636 0.18 IPB002505D 660-703 5.1e-22 IPB002505E 720-752 3.4e-15Significant hit ( 6.3e-11) to 4/11 blocks of the IPB001891 family, which is described as \"Malic enzymes\". Interpro entry for IP:IPR001891. IPB001891E 137-187 0.0057 IPB001891F 194-203 1.6e+02 IPB001891G 214-225 16 IPB001891J 309-343 0.00054","Residues 326 to 387 match (3e-07) PD:PD261955 which is described as PROTEOME COMPLETE OXIDOREDUCTASE MALATE ","","","","","","","","","","","","Wed Nov 27 12:21:21 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00066 is paralogously related to AA01972 (1e-36) and AA00015 (3e-08).","","","","","","Residues 429 to 750 (E-value = 1.3e-114) place AA00066 in the PTA_PTB family which is described as Phosphate acetyl/butaryl transferase (PF01515)","","","","","Iwakura,M., Hattori,J., Arita,Y., Tokushige,M. and Katsuki,H.Studies on regulatory functions of malic enzymes. VI.Purification and molecular properties of NADP-linked malicenzyme from Escherichia coli W. J. Biochem. 85(5): 1355-1365, 1979. PubMed: 36376.","","Wed Nov 27 12:21:21 2002","1","","","" "AA00068","51550","52191","642","ATGGCTTATACTTTACCTGAATTAGGCTATGCCTATGATGCATTAGAACCCCACTTCGATGCACAAACCATGGAAATCCACCACAGCAAACATCACCAAGCATATGTTAACAACGCGAATGCGGCACTAGAAAATCCCCCTGAATTACAAGCACTTTCCGAAGGCTGTCCGGGCAAGTTATTGGCACACTTAAGCGAAATCACTCCGGAAAAACGCCCGGCATTACGCAACAACGTAGGCGGTCACTTAAACCACAGCTTGTTCTGGAAAAGCCTGAAAAAAGGCACAACCTTAAAAGGCCCATTGAAAGATGCCATCGAACGTGATTTCGGTTCCGTTGAAAACTTCAAAGCGGAATTTGAAAAAGCGGCGGCAACCCGTTTCGGTTCCGGCTGGGCATGGTTAGTTTTAGAAAACGGCAAACTCGCCGTGGTTTCTACCGCCAACCAAGACAATCCGATTATGGGCAAAGAATACGCCGGCTGCTCCGGTGTGCCGATTTTCGGTTTAGACGTTTGGGAGCACGCCTACTACTTGAAATTCCAAAATCGCCGCCCGGATTACATCAAAGAATTCTGGAACGTACTGAACTGGGATTTCGCCAATGAACGTTTTGAAAAAATCTTAGCCGGTACACCACAC","","","26339","MAYTLPELGYAYDALEPHFDAQTMEIHHSKHHQAYVNNANAALENPPELQALSEGCPGKLLAHLSEITPEKRPALRNNVGGHLNHSLFWKSLKKGTTLKGPLKDAIERDFGSVENFKAEFEKAAATRFGSGWAWLVLENGKLAVVSTANQDNPIMGKEYAGCSGVPIFGLDVWEHAYYLKFQNRRPDYIKEFWNVLNWDFANERFEKILAGTPH","52191","","manganese superoxide dismutase","Periplasm, Cytoplasm","","
InterPro
IPR001189
Family
Manganese and iron superoxide dismutase
PD000475\"[104-207]TSODM_HAEIN_P43725;
PR01703\"[6-17]T\"[27-40]T\"[76-89]T\"[127-135]T\"[169-181]TMNSODISMTASE
PTHR11404\"[1-209]TSUPEROXIDE DISMUTASE 2
PF00081\"[2-93]TSod_Fe_N
PF02777\"[95-205]TSod_Fe_C
PS00088\"[171-178]TSOD_MN
noIPR
unintegrated
unintegrated
PTHR11404:SF9\"[1-209]TSUPEROXIDE DISMUTASE [MN]


","BeTs to 21 clades of COG0605COG name: Superoxide dismutaseFunctional Class: PThe phylogenetic pattern of COG0605 is -omp-zyq-drlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.6e-95) to 4/4 blocks of the IPB001189 family, which is described as \"Manganese and iron superoxide dismutase (SODM)\". Interpro entry for IP:IPR001189. IPB001189A 5-40 3.3e-29 IPB001189B 78-94 4.3e-08 IPB001189C 98-135 1.1e-26 IPB001189D 166-198 6.6e-28","Residues 1 to 89 match (2e-27) PD:PD583305 which is described as DISMUTASE SUPEROXIDE OXIDOREDUCTASE MANGANESE PROTEOME COMPLETE IRON MN PRECURSOR FE ","","","","","","","","","","","","Wed Nov 27 12:26:00 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00068 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 95 to 205 (E-value = 1.4e-67) place AA00068 in the Sod_Fe_C family which is described as Iron/manganese superoxide dismutases, C-terminal domain (PF02777)","","","","","San Mateo,L.R., Toffer,K.L. and Kawula,T.H. The sodA gene of Haemophilus ducreyi encodes a hydrogen peroxide-inhibitable superoxide dismutase Gene 207 (2), 251-257 (1998) PubMed: 9511768 Nakayama,K. Nucleotide sequence of Streptococcus mutans superoxide dismutasegene and isolation of insertion mutants J. Bacteriol. 174 (15), 4928-4934 (1992) PubMed: 1321118 Martin,M.E., Byers,B.R., Olson,M.O., Salin,M.L., Arceneaux,J.E.and Tolbert,C. A Streptococcus mutans superoxide dismutase that is active with either manganese or iron as a cofactor J. Biol. Chem. 261 (20), 9361-9367 (1986) PubMed: 3722201 Poyart,C., Quesne,G., Coulon,S., Berche,P. and Trieu-Cuot,P. Identification of streptococci to species level by sequencingthe gene encoding the manganese-dependent superoxide dismutase J. Clin. Microbiol. 36 (1), 41-47 (1998) PubMed: 9431917 Gerlach,D., Reichardt,W. and Vettermann,S. Extracellular superoxide dismutase from Streptococcus pyogenestype 12 strain is manganese-dependent FEMS Microbiol. Lett. 160 (2), 217-224 (1998) PubMed: 9532741 Gibson,C.M. and Caparon,M.G. Insertional inactivation of Streptococcus pyogenes sod suggests that prtF is regulated in response to a superoxide signal J. Bacteriol. 178 (15), 4688-4695 (1996) PubMed: 8755901 Poyart,C., Berche,P. and Trieu-Cuot,P. Characterization of superoxide dismutase genes fromgram-positive bacteria by polymerase chain reaction using degenerate primers FEMS Microbiol. Lett. 131 (1), 41-45 (1995) PubMed: 7557308 Inaoka,T., Matsumura,Y. and Tsuchido,T. Molecular cloning and nucleotide sequence of the superoxide dismutase gene and characterization of its product from Bacillussubtilis J. Bacteriol. 180 (14), 3697-3703 (1998) PubMed: 9658017 Sanders,J.W., Leenhouts,K.J., Haandrikman,A.J., Venema,G. and Kok,J. Stress response in Lactococcus lactis: cloning, expression analysis, and mutation of the lactococcal superoxide dismutasegene J. Bacteriol. 177 (18), 5254-5260 (1995) PubMed: 7665513 Bowler,C., Van Kaer,L., Van Camp,W., Van Montagu,M., Inze,D. andDhaese,P. Characterization of the Bacillus stearothermophilus manganese superoxide dismutase gene and its ability to complementcopper/zinc superoxide dismutase deficiency in Saccharomyces cerevisiae J. Bacteriol. 172 (3), 1539-1546 (1990) PubMed: 2407726 C","","Wed Nov 27 12:26:00 2002","1","","","" "AA00069","52605","53393","789","ATGAAAACGAAATATTTATTGGCGGCGCTGACCGTCGCCTGCACATTATCCGCATGCAGCCAAGCTGCCGGGGGGTTGGCGGATGGTCTACTGAAACCGTTCGATCCGAAAGCAAAAGACTGGAAGCAGTTAACCATCTCCGAATCTGTTCCCGATAACGGCACTTTGGAACTAACCGACCGCGGCGGCAAAACCCGGATCTTGCGTAAAGGCGGCGTTCTGGATACAGGCTATTTGAGATCCGATAAGATCTCTGACTACGATTACGTCAAAAAAATCAACGTGAACGGTCAAATAATCGAGTTGGAACGAGGCGATTTTCTGATATATAAACAGAGTAATTCCATCATCGCTGCTACGTTAGCGAAACAGAAAACCAACGCAGATGGTACACGCTCCTCTGCCTTTGATTTCCATGTCAACGAAATTCAAGGGCGAGACATCGCCTTTAATAATCTGCCGGCTTCGGGACAGGTAAACTATCGCGGCATCGCATTTACCGGCGATGACCGTGGAGGTCGTTTATCCTACACTATCGACTTCGCTAAAAAACAAGGCAGCGGTAGCATCAGTGGTCTACATGGCGATTATAACGTAGATTTGGCGCAAACAAACGTCCGCGCAATGGGAAACGGTTCCGGGTTGAGTGGTAAAGCTATGAAAGATGGCGTGGAAAGAGGAAATTACACGCTAAAAATCTTCGGTAGCAAGGCAGAAGAAATCGCCGGCAAAGCTGAGATCAAAACCGGTAAGGGAACTCAAGAAATCGGTCTGGCAGGTAAAAAAGAA","","","28111","MKTKYLLAALTVACTLSACSQAAGGLADGLLKPFDPKAKDWKQLTISESVPDNGTLELTDRGGKTRILRKGGVLDTGYLRSDKISDYDYVKKINVNGQIIELERGDFLIYKQSNSIIAATLAKQKTNADGTRSSAFDFHVNEIQGRDIAFNNLPASGQVNYRGIAFTGDDRGGRLSYTIDFAKKQGSGSISGLHGDYNVDLAQTNVRAMGNGSGLSGKAMKDGVERGNYTLKIFGSKAEEIAGKAEIKTGKGTQEIGLAGKKE","53393","many weak hits to a variety of proteins.","conserved hypothetical protein","Extracellular, Outer membrane","","
InterPro
IPR014902
Family
Lipoprotein GNA1870 C terminal like
PF08794\"[112-262]TLipoprot_C
noIPR
unintegrated
unintegrated
PS51257\"[1-19]TPROKAR_LIPOPROTEIN
signalp\"[1-22]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","","Residues 2 to 262 match (2e-45) PD:PD360144 which is described as LIPOPROTEIN PROTEOME COMPLETE NMB1870 ","","","","","","","","","","","Wed Nov 27 12:30:29 2002","Wed Nov 27 12:30:29 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00069 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00071","54427","53603","825","ATGCGTTGGCAAGGGCGTAGAGAAAGCTCAAACGTGGAAGACAGACGTTCGTCAGGTGGTGGTTTTGGCGGTGGCAGACCCACCGGTATTCTCGGGTTAATTATTATCTTAGTGGGCGCTTATTATGGCGTGGATTTATCGGGATTAGTCGGCGGGGTTGATGTGGGCGCAACCCAAACCACGCCTTTGCAATCGCAGCAGGAACAAGAGCTGGCGGGGCTTTCCAAAGTGGTGCTGGGCGATACTGAGGATGTTTGGAATGCGTATTTTGCCAAACATAATAAACAATATATCGAACCGACGATGGTGTTGTATAACGGTGCGACACCGACCGCCTGCGGCACCGGTCAATCGGCAATGGGGCCGTTTTATTGCCCCAATGATCAACGGGTGTATTTAGATTTGTCTTTTTATAACGACATGAAAAATAAGCTCGGTGCGGCGGGCGAAGCGGCGTTTGCGTATGTGATTGCCCATGAAGTGGGGCATCATGTGCAAAATCTGTTCGGCACCTTATCGCAGGTTCATCGCCTGCAACGACAAACCTCCCGCACGGAAGCCAATCAGCTTTCCGTAAAATTGGAATTACAGGCGGATTGTTATGCGGGCGTGTGGGCAAGTCTGGCAATACGAAAAGGTTTGTTTGAAAGCGGCGATATTGAAAAAGCATTCAATGCGGCGGAATCCGTGGGCGACGATCGTTTGCAAAAGCGTAGCCAAGGTTATGTGGTACCGGACAGCTTTACCCACGGCACATCGGCGCAACGCTTGCAATGGTTTAAACGCGGTGTAAATACGGCGGATCCGGCACAGTGTAATACGTTT","","","29923","MRWQGRRESSNVEDRRSSGGGFGGGRPTGILGLIIILVGAYYGVDLSGLVGGVDVGATQTTPLQSQQEQELAGLSKVVLGDTEDVWNAYFAKHNKQYIEPTMVLYNGATPTACGTGQSAMGPFYCPNDQRVYLDLSFYNDMKNKLGAAGEAAFAYVIAHEVGHHVQNLFGTLSQVHRLQRQTSRTEANQLSVKLELQADCYAGVWASLAIRKGLFESGDIEKAFNAAESVGDDRLQKRSQGYVVPDSFTHGTSAQRLQWFKRGVNTADPAQCNTF","53603","","conserved hypothetical protein (possible zinc protease)","Outer membrane, Extracellular","","
InterPro
IPR006025
Binding_site
Peptidase M, neutral zinc metallopeptidases, zinc-binding site
PS00142\"[156-165]?ZINC_PROTEASE
InterPro
IPR007343
Family
Protein of unknown function, zinc metallopeptidase putative
PF04228\"[1-275]TZn_peptidase
noIPR
unintegrated
unintegrated
signalp\"[1-43]?signal-peptide
tmhmm\"[21-43]?transmembrane_regions


","BeTs to 4 clades of COG2321COG name: Predicted metalloproteaseFunctional Class: RThe phylogenetic pattern of COG2321 is ---------drl--ef-h---j----Number of proteins in this genome belonging to this COG is","","Residues 1 to 275 match (2e-102) PD:PD023842 which is described as COMPLETE PROTEOME TRANSMEMBRANE MEMBRANE INNER RSC2503 PROTEASE MLL2493 SPY0775 RV2575 ","","","","","","","","","","","","Wed Nov 27 13:03:03 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00071 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 275 (E-value = 3.4e-164) place AA00071 in the Zn_peptidase family which is described as Putative neutral zinc metallopeptidase (PF04228)","","","","","","","","1","","","" "AA00072","54567","55007","441","ATGGGTTTATTTGATTTTATCGGTGACATCGGTAAAAAAATCTTCAGCAAAGAAGAAGAGGCCTCCACTGCCGTCACCAAACACATTAACGAAGACAATCCCGGCGTTGCCGATGTGGAAGTGAAAGTAGAAAACGGTGTGGCGAAAATCGCCGGTGTTGCCAGTTCCGCCACTGCGCTGGAAAAAGCCGTGTTAATGACGGGCAATATTGTCGGTATCAGCGAAGTCAATATCGATGAAGTCACCGTGCAAAACGGTGAAAAGATTGCCGGCGAAGATGAATTTTACGTGATTCAAAAAGGCGACACCCTTTGGAAAATCGCTGAAAAACATTACCGCAATGGCAGCAAATACACTGCTATCGTAGCAGCCAATAAAGAAGTGATTAAAGACGCGGATAAAATCTTCCCCGGGCAAAAAATTCGTTTGCCGAAAAGCTTG","","","17243","MGLFDFIGDIGKKIFSKEEEASTAVTKHINEDNPGVADVEVKVENGVAKIAGVASSATALEKAVLMTGNIVGISEVNIDEVTVQNGEKIAGEDEFYVIQKGDTLWKIAEKHYRNGSKYTAIVAANKEVIKDADKIFPGQKIRLPKSL","55007","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR002482
Domain
Peptidoglycan-binding LysM
PF01476\"[96-144]TLysM
SM00257\"[95-144]TLysM
InterPro
IPR007055
Domain
Transport-associated
PF04972\"[22-85]TBON
PS50914\"[16-85]TBON


","No hits to the COGs database.","Significant hit ( 3.1e-05) to 1/1 blocks of the IPB002482 family, which is described as \"LysM motif\". Interpro entry for IP:IPR002482. IPB002482 98-108 3.4e-05","Residues 96 to 144 match (9e-18) PD:PD407905 which is described as PROTEOME COMPLETE PRECURSOR HYDROLASE CELL REPEAT SIGNAL LIPOPROTEIN WALL ENZYME ","","","","","","","","","","","","Wed Nov 27 13:06:47 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00072 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 96 to 144 (E-value = 8e-13) place AA00072 in the LysM family which is described as LysM domain (PF01476)","","","","","","","","1","","","" "AA00075","55696","55103","594","ATGAGCCTTTTCGCCCTTTTTTATATGCTATTGAGCTATTTGCTCGGTTCCATTTCCGGTGCGATTTTATTATGCCGAGTCACCGGCTTGCCGGACCCCAGAACCTCCGGTTCCCATAACCCCGGCGCGACCAACGTGTTACGTATCGGCGGGCGTTGGATTGCCTTGGCGGTGCTTATTTTCGACATCTTAAAAGGCATGTTACCGGTGTGGTTGGGTTATTATTTGGGGTTAACACAATTTGAATTGGGCATGGTGGCGTTAGCGGCGTGTTTGGGGCATATTTTCCCGATTTTCTTTAAATTTAAAGGCGGCAAAGGCGTTGCCACCGCCTTCGGTGCCATCGCACCTATCGCTTGGGGCGTCTTATTTTCGACACTCGGCACCTGGATTGTCGTGTTCCTTATCAGCGGCTATTCCTCTCTCAGTGCTGTCGTCACCGCATTACTGGTGCCGCTTTATGTGTGGTGGTTCAAACCCGAATTCACCTTTCCCGTCGCCTTGGTTTGCTGCCTGCTCATCTATCGACACCACGAAAATATCCAACGTCTCTGGCGCGGACAGGAAGACAAAATATGGCGCAAGTTTAAAAAG","","","22032","MSLFALFYMLLSYLLGSISGAILLCRVTGLPDPRTSGSHNPGATNVLRIGGRWIALAVLIFDILKGMLPVWLGYYLGLTQFELGMVALAACLGHIFPIFFKFKGGKGVATAFGAIAPIAWGVLFSTLGTWIVVFLISGYSSLSAVVTALLVPLYVWWFKPEFTFPVALVCCLLIYRHHENIQRLWRGQEDKIWRKFKK","55103","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR003811
Family
Protein of unknown function DUF205
PF02660\"[9-187]TDUF205
TIGR00023\"[1-195]TTIGR00023: conserved hypothetical protein T
noIPR
unintegrated
unintegrated
signalp\"[1-20]?signal-peptide
tmhmm\"[4-24]?\"[49-69]?\"[75-95]?\"[104-124]?\"[130-152]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 3.9e-61) to 4/4 blocks of the IPB003811 family, which is described as \"DUF205\". Interpro entry for IP:IPR003811. IPB003811A 8-21 0.00057 IPB003811B 32-68 2e-21 IPB003811C 92-113 5.1e-18 IPB003811D 172-192 1.7e-13","Residues 11 to 189 match (4e-72) PD:PD007519 which is described as PROTEOME COMPLETE TRANSMEMBRANE MEMBRANE INTEGRAL MG247 DR2270 LIN1323 PROBABLE VC0523 ","","","","","","","","","","","","Wed Nov 27 13:08:40 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00075 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 9 to 187 (E-value = 1.6e-101) place AA00075 in the DUF205 family which is described as Domain of unknown function DUF (PF02660)","","","","","","","","1","","","" "AA00076","55793","56143","351","ATGCAAGATCTTATTTTTATCGAAGGTTTAACGGTATTTGCGCAAATCGGCATTTATGACTGGGAACAACAAATTAAACAAAAACTCATTTTTGATGTCGAAATGGCGTGGGGCACGCGTCAGGCGGCAGCTGCCGATGACGTTCAATTTGCACTAAATTATGCGGAAGTCAGCCAATTCATTATTGATTATGTGCAATCCAAACCGTTTTTATTAATTGAGCGGGTTGCCAATGAAGTGGCGGAACAATTACAACAACAATTTAAAATTTCGTGGCTTCGTCTCAAATTAAGTAAACCGAAAGCCGTCGCGCAAGCGGAAAACGTCGGTATTATTATTGAACGAAGCCGC","","","13488","MQDLIFIEGLTVFAQIGIYDWEQQIKQKLIFDVEMAWGTRQAAAADDVQFALNYAEVSQFIIDYVQSKPFLLIERVANEVAEQLQQQFKISWLRLKLSKPKAVAQAENVGIIIERSR","56143","","dihydroneopterin aldolase","Cytoplasm","","
InterPro
IPR006156
Family
Dihydroneopterin aldolase family
TIGR00525\"[3-115]TfolB: dihydroneopterin aldolase
InterPro
IPR006157
Domain
Dihydroneopterin aldolase
PF02152\"[5-117]TFolB
TIGR00526\"[2-117]TfolB_dom: FolB domain
noIPR
unintegrated
unintegrated
G3DSA:3.30.1130.10\"[2-117]Tno description
PTHR20941\"[1-116]TFOLATE SYNTHESIS PROTEINS
PTHR20941:SF3\"[1-116]TDIHYDRONEOPTERIN ALDOLASE


","No hits to the COGs database.","Significant hit ( 9.8e-39) to 3/3 blocks of the IPB003098 family, which is described as \"Dihydroneopterin aldolase\". Interpro entry for IP:IPR003098. IPB003098A 3-47 6.9e-21 IPB003098B 72-81 0.0053 IPB003098C 90-117 6.5e-12","Residues 1 to 115 match (5e-42) PD:PD004848 which is described as DIHYDRONEOPTERIN PROTEOME COMPLETE ALDOLASE LYASE DHNA FOLATE BIOSYNTHESIS PROBABLE DIHYDROPTEROATE ","","","","","","","","","","","","Wed Nov 27 13:36:43 2002","","Tue Mar 9 09:57:57 2004","Tue Mar 9 09:57:57 2004","Tue Mar 9 09:57:57 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00076 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Tue Mar 9 09:57:57 2004","","","","","Residues 5 to 117 (E-value = 1.9e-45) place AA00076 in the FolB family which is described as Dihydroneopterin aldolase (PF02152)","Tue Mar 9 09:57:57 2004","","","","Haussmann C, Rohdich F, Schmidt E, Bacher A, Richter G.Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase.J Biol Chem. 1998 Jul;273(28):17418-24.PMID: 9651328","","Tue Mar 9 09:57:57 2004","1","","","" "AA00077","56251","57594","1344","ATGCATTCGGAAGAAAATGCTTATCATGCCATTCAAGATCGCGGCAAACTGGTGGTGGGGACGATTAATAATCCGGTTTCTTATTTCATCAATGCCGAAGGTGAATCCGGCTTAGAGTATGAATTAAGCAAAGCCTTTGCCGATTATTTGGGCGTGGAACTTGAAATGCAGCCGATGAATAATACGGATGATCTTTTTTCTGCGTTAAACGATCGTCAAATTGATATTGCCGCCGCCAATTTATTTTATCACCCGACCAAAGCCGAGCGTTTTCAGCTTGGTCCGTCCTATTACTCCGCTTCCTGGCAAATCGCTTATCGTAAAGGGAAAAATCGCCCGCGTTCGTTAGCACAGATTAACGGCAGCCTTGTAGTTCCTGACAGTTCCGAATTGCAGCAAATTTTAAAAGAAGCGCAGCTGAAAAAACCGAAATTAAGCTGGACGGTAGACAGTAAATTAACGCAAGAAGAATTATTGTTACAGGTGGCGGAAGGGAAAATTGATTATACCATCGCCAATTCTTTAGATATTTCTGCCACCCAGCAAATTAAACCGCAAATTGCCGTGGCTTTCGATTTAACCGATGAAATGAGCGTGCATTGGTATTTACCGAATAATTCTTCAAGTGAATTACAATCGGCATTGCTGGGCTTCATGAACAGCTCCATTGATTCGGGCTTAATCGCCAACATTGAAGAGAAGTATTTTAATCATTTCCGTCAGTTTGACTATGTGGACATTAAATCCTATTTGAATTCCATTGAAACGATTCTCCCGAAATTCGAACCGCTCTTTACTAAACACAAAGGCAATTTGGATTGGCGTTTATTGGCAGCAATTGCGTATCAGGAATCCCACTGGAACCCGGATGCCACATCGCCCACCGGCGTGCGTGGCATGATGATGTTGACCAAAGACACCGCAGAACGCATGAAAATCAGTGACAGAACCGATCCGGAGCAAAGCATTAAAGCCGGTTCGGAATACTTACATTGGTTGATCGGACAGATTCCCGACAGCATTAACAGTGAAGATCGTATTTGGTTCGCCCTTGCCGCTTACAATATGGGATTAGGGCATTTATTGGATGCCCGCCGTTTAACCAAAAATTTAGGCGGCAATCCGGATAATTGGCTGGATGTGAAAAATAACTTGCCTTTGTTGGCAGAAAAGCGATATTACCGTAATCTGAAATACGGTTATGCTCGTGGTTACGAAGCCTTTCAGTATGTAGAAAATATTCGGCGCTATATGAACAGTATCATGAATTATTATCGTATTCAGGAAAAACAAAACGATAAAACCACGGAAACTGCCACAGGGCAAACAAAACCACAAAGTAAA","","","54484","MHSEENAYHAIQDRGKLVVGTINNPVSYFINAEGESGLEYELSKAFADYLGVELEMQPMNNTDDLFSALNDRQIDIAAANLFYHPTKAERFQLGPSYYSASWQIAYRKGKNRPRSLAQINGSLVVPDSSELQQILKEAQLKKPKLSWTVDSKLTQEELLLQVAEGKIDYTIANSLDISATQQIKPQIAVAFDLTDEMSVHWYLPNNSSSELQSALLGFMNSSIDSGLIANIEEKYFNHFRQFDYVDIKSYLNSIETILPKFEPLFTKHKGNLDWRLLAAIAYQESHWNPDATSPTGVRGMMMLTKDTAERMKISDRTDPEQSIKAGSEYLHWLIGQIPDSINSEDRIWFALAAYNMGLGHLLDARRLTKNLGGNPDNWLDVKNNLPLLAEKRYYRNLKYGYARGYEAFQYVENIRRYMNSIMNYYRIQEKQNDKTTETATGQTKPQSK","57594","","conserved hypothetical protein (possible periplasmic binding transport protein)","Outer membrane, Periplasm, Extracellular","","
InterPro
IPR000189
Active_site
Prokaryotic transglycosylase, active site
PS00922\"[280-308]TTRANSGLYCOSYLASE
InterPro
IPR001638
Family
Bacterial extracellular solute-binding protein, family 3
PF00497\"[17-238]TSBP_bac_3
SM00062\"[16-239]TPBPb
InterPro
IPR008258
Domain
Lytic transglycosylase, catalytic
PF01464\"[261-377]TSLT
noIPR
unintegrated
unintegrated
G3DSA:1.10.530.10\"[260-418]Tno description
G3DSA:3.40.190.10\"[12-148]Tno description
PTHR21666\"[271-362]TPEPTIDASE-RELATED
PTHR21666:SF10\"[271-362]TLYTIC TRANSGLYCOSYLASE


","BeTs to 6 clades of COG0834COG name: ABC-type amino acid transport system, periplasmic componentFunctional Class: EThe phylogenetic pattern of COG0834 is a----z--vdrlbcefgh-nujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 5.2e-13) to 2/2 blocks of the IPB000189 family, which is described as \"SLT domain\". Interpro entry for IP:IPR000189. IPB000189A 284-308 2.4e-10 IPB000189B 316-330 0.61","Residues 272 to 307 match (3e-08) PD:PD488114 which is described as PA3764 PROTEOME COMPLETE ","","","","","","","","","","","","Wed Nov 27 13:43:33 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00077 is paralogously related to AA00777 (2e-08) and AA01042 (2e-07).","","","","","","Residues 261 to 377 (E-value = 9.5e-39) place AA00077 in the SLT family which is described as Transglycosylase SLT domain (PF01464)","","","","","","","","1","","","" "AA00078","57608","57751","144","ATGCTTAGAAGACGTTTTCTAAAACCGGCTAAAAAGAAATTCTTTCATCAACAACAAGCCCGTTCTTTGCGCCTGAAACATTTAAAACAACGCAAAGCCAAGCTATTCGCCCGCCACGCCTTACAATTTGTTGTGCAGGATATA","","","5925","MLRRRFLKPAKKKFFHQQQARSLRLKHLKQRKAKLFARHALQFVVQDI","57751","","hypothetical protein","Periplasm, Cytoplasm","No similarities were found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sat Feb 21 10:58:13 2004","Sat Feb 21 10:58:13 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found.AA00078 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sat Feb 21 10:59:04 2004","","","","","","","","","","","","","1","","","" "AA00079","58336","57800","537","ATGCTAAAATTTTTCAAAACACTTTCCGTGCAACGGACCGGTTGGTTGTTGTTGGTTATTTCAGCATTGACGTTAGAAGGCACGGCACTTTATTTCCAATATGGCATGGAATTACAACCCTGCGTCATGTGTATTTATGAACGGGTTGCCTTATTCGGTATTGCTTTTGCCGGAATTGTCGGATTAATTGCACCGCGCTTTTTGGTTTTCCGTTTATTGGCATTGCTTATCGCGTTTTTCAGTACCGTGAAAGGATTATTAATTTCCCTTAAGCACGTAGATTATCAACTGCACCCGGCACCCTGGAATCAATGTTCCTATTTGCCGGAATTTCCACAAACCCTGCCGTTGGATAAATGGTTTCCGGCATTATTCCAACCCACCGGTTCTTGCAGCGATGTGGTTTGGTCGTGGTTAGGGCTTTCCATGGCGCAGTGGATTGTGGTGATTTTTGCCATATATTTGATTGTTTTGGTGTTAGTGTTAATTAGCCAATTTAAACGTCTTGATAATAGAGGAAGAAGACGTTTATTTAAT","","","22832","MLKFFKTLSVQRTGWLLLVISALTLEGTALYFQYGMELQPCVMCIYERVALFGIAFAGIVGLIAPRFLVFRLLALLIAFFSTVKGLLISLKHVDYQLHPAPWNQCSYLPEFPQTLPLDKWFPALFQPTGSCSDVVWSWLGLSMAQWIVVIFAIYLIVLVLVLISQFKRLDNRGRRRLFN","57800","","disulfide bond formation protein B (disulfide oxidoreductase)","Inner membrane, Cytoplasm","","
InterPro
IPR003752
Family
Disulphide bond formation protein DsbB
PF02600\"[4-165]TDsbB
InterPro
IPR012139
Family
Disulphide bond formation protein B, proteobacteria
PIRSF000258\"[2-179]TDisulphide bond formation protein B (disulphide oxidoreductase B)
noIPR
unintegrated
unintegrated
signalp\"[1-29]?signal-peptide
tmhmm\"[15-35]?\"[45-63]?\"[68-88]?\"[146-166]?transmembrane_regions


","BeTs to 11 clades of COG1495COG name: Disulfide bond formation protein DsbBFunctional Class: OThe phylogenetic pattern of COG1495 is ---------d--b-efghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-17) to 1/1 blocks of the IPB003752 family, which is described as \"Disulfide bond formation protein DsbB\". Interpro entry for IP:IPR003752. IPB003752 29-61 1.2e-17","Residues 11 to 131 match (6e-13) PD:PD124082 which is described as ISOMERASE DISULFIDE PROTEOME COMPLETE OXIDOREDUCTASE ","","","","","","","","","","","","Wed Nov 27 13:47:00 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00079 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 165 (E-value = 9.5e-53) place AA00079 in the DsbB family which is described as Disulfide bond formation protein DsbB (PF02600)","","","","","Missiakas,D., Georgopoulos,C. and Raina,S. Identification and characterization of the Escherichia coligene dsbB, whose product is involved in the formation ofdisulfide bonds in vivo Proc. Natl. Acad. Sci. U.S.A. 90 (15), 7084-7088 (1993) PubMed: 7688471 ","","Wed Nov 27 13:47:00 2002","1","","","" "AA00080","59904","58363","1542","ATGGATAGTAATTATACACAGGCATTTTTTAAAAACTTTCTTGGTTCTAGCCCGGGCTGGTATAAAATAGCGATCGTCGCATTTCTTGTCATTAATCCCGTCTTATTTGCTATTTCACCTTTTTGGGCGGGGTGGTTATTAGTCATTGAATTCATTTTCACCCTAGCTATGGCGCTAAAATGTTATCCGTTACAGCCCGGCGGGTTACTTGCCATTGAAGCGGTATTTATAGGAATGACAAATCCTGCCCACATTAAAGCAGAAGTGCTGGCAAATTTTGAAGTGATTTTGCTCTTGATGTTTATGGTGGCAGGAATTTACTTCATGAAACAATTGTTGCTTTTCGTGTTTACTAAGCTTCTTCTTAATATTCATTCCAAATTGGTGCTTTCTTTATCTTTCTGTTTTAGTGCCGCGTTTTTATCTGCCTTCTTAGATGCGCTAACCGTAGTGGCTGTCATTATCAGCGTGGCTATGGGGTTTTATGGGGTATATCACAAAGTGGCATCGGGGGGTACATTCTACGATCCTACCGATATTACTAATGATGAGAAAATCGGTAAAGATCGTGAAACTTTAGAGGAGTTTCGGGCATTTCTGCGTAATTTGATGATGCATTCCTGTGTAGGTACTGCGCTCGGTGGTGTAATGACCATGGTGGGCGAACCACAGAATTTAATCATTGCGGAACAGTCGGGTTGGAATTTTGTTGAATTCTTTTTTCGTATGGTGCCGGTGACGATTCCGGTCTTTTTATTCGGATTACTAACCTGCGTAGTAATAGAAAAGTTTCATCTCTTTGGTTATGGCGCGAAATTACCAAATCAAGTATGGATGGTTTTATCTGAATTTGATAAAGCCAGTATGAAAAAAATGACCAAGCAGGAGCGTTTGAAGCTTATCGCGCAGGCAATTGTCGGGATTTGGTTGATTATCGGTTTAGCATTCCACTTGGCGTCTGTCGGTTTAATCGGTTTAAGTGTCATTATTTTTTGTACCGCACTTTGTGGTGTTACCAGCGAACATGCATTGGGTAAAGCATTCCAGGAATCTTTGCCGTTTACTGCACTACTGGTTGTGTTCTTTACCGTAGTTGCCGTGATTATTGACCAAAAACTGTTTGCGCCGATTATTCATTACGTTTTATCTTCAGAGGAAACTGTTCAGTTAACTTTATTCTACGCCTTTAATGGTTTGTTATCCGCTATTTCCGATAACGTGTTCGTTGCAACGGTTTATATCAATGAAGCAAAAAATGCGTTAACTGCTAATGTGATTCCGCCACATCAATTTGAATTGTTGGCGGTAGCGATTAATACCGGTACCAACCTGCCTTCTGTAGCGACACCAAACGGACAGGCTGCGTTCTTATTCTTATTGACTTCCTCTTTGGCGCCCCTAATCAACCTCTCTTATGGTAGAATGGTTTACATGGCGTTGCCTTATACCATTGTATTATCGTTAGTGGGTTTGTTCGCCGTGGAATATATTTTACCGCCGATGACTATTTGGCTGGCAAACTTAGGCTTGATCATGCCGATT","","","56595","MDSNYTQAFFKNFLGSSPGWYKIAIVAFLVINPVLFAISPFWAGWLLVIEFIFTLAMALKCYPLQPGGLLAIEAVFIGMTNPAHIKAEVLANFEVILLLMFMVAGIYFMKQLLLFVFTKLLLNIHSKLVLSLSFCFSAAFLSAFLDALTVVAVIISVAMGFYGVYHKVASGGTFYDPTDITNDEKIGKDRETLEEFRAFLRNLMMHSCVGTALGGVMTMVGEPQNLIIAEQSGWNFVEFFFRMVPVTIPVFLFGLLTCVVIEKFHLFGYGAKLPNQVWMVLSEFDKASMKKMTKQERLKLIAQAIVGIWLIIGLAFHLASVGLIGLSVIIFCTALCGVTSEHALGKAFQESLPFTALLVVFFTVVAVIIDQKLFAPIIHYVLSSEETVQLTLFYAFNGLLSAISDNVFVATVYINEAKNALTANVIPPHQFELLAVAINTGTNLPSVATPNGQAAFLFLLTSSLAPLINLSYGRMVYMALPYTIVLSLVGLFAVEYILPPMTIWLANLGLIMPI","58363","","Na+/H+ antiporter protein","Inner membrane, Cytoplasm","","
InterPro
IPR004671
Family
Na+/H+ antiporter NhaB
PF06450\"[1-513]TNhaB
TIGR00774\"[1-514]TNhaB: Na+/H+ antiporter NhaB
noIPR
unintegrated
unintegrated
signalp\"[1-58]?signal-peptide
tmhmm\"[20-40]?\"[46-64]?\"[89-109]?\"[128-162]?\"[203-221]?\"[240-260]?\"[298-316]?\"[322-340]?\"[352-370]?\"[453-473]?\"[478-498]?transmembrane_regions


","BeTs to 4 clades of COG3067COG name: Na+/H+ antiporterFunctional Class: PThe phylogenetic pattern of COG3067 is --------------efgh--------Number of proteins in this genome belonging to this COG is","","Residues 149 to 202 match (1e-16) PD:PD515970 which is described as ANTIPORTER PROTEOME COMPLETE NA/H SODIUM/PROTON NHAB REGULATOR TRANSMEMBRANE SODIUM MEMBRANE ","","","","","","","","","","","","Wed Nov 27 13:50:08 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00080 is paralogously related to AA00136 (2e-05) and AA00615 (1e-04).","","","","","","","","","","","Nakamura T, Fujisaki Y, Enomoto H, Nakayama Y, Takabe T,Yamaguchi N, Uozumi N. Residue aspartate-147 from the third transmembrane regionof Na(+)/H(+) antiporter NhaB of Vibrio alginolyticusplays a role in its activity. J Bacteriol. 2001 Oct;183(19):5762-7. PMID: 11544242 Pinner,E., Padan,E. and Schuldiner,S. Cloning, sequencing, and expression of the nhaB gene,encoding a Na+/H+ antiporter in Escherichia coli J. Biol. Chem. 267 (16), 11064-11068 (1992) PubMed: 1317851 ","","Wed Feb 5 15:50:05 2003","1","","","" "AA00081","60099","60827","729","ATGAATAACAATTCCCCCCTTCTGAAAGCACAAAGCCCGGCGGCATTAGCAGAAGAATACATTGTAAAAAGCATTTGGAATAATCATTTCCCACCCGGTTCGGATTTACCGGCAGAACGTGAATTGGCCGACAAAATCGGTGTTACCCGCACCACCCTGCGTGAAGTTTTGCAACGATTGGCACGTGATGGCTGGTTAAATATCCAACATGGCAAACCCACCAAAGTTAATGATATTTGGGAAACCTCAGGTTTAAACATTCTGGAAACCATGATCCAACTTGACGGTTCACGCCTGCCTTCGCTGACTGCCAATATGCGTTCCGCGCGCACCGACATCTCCATGATCTACATTCCGAAAGCCTTTAAACGTGCACCCGAGCGTTCTCTGCATATCCTTCACCCGATGGACAACTTGGAAGATACCGCGGAAGACTATACAAAATTCGACTATGACGTATTTCGCAATCTGGCTTTTGCTTCCGATAATCCCGTTTACGGATTGATTTTGAACAGCTTTAAAAGTTTATATACCAGAATCGGTTTATTCTATTTTCAAAGCGCCGAAGCACGAGAATTAGCAAGACGGTTTTACTTCAACCTAAGGGATATTTGCCAGCGCCAAAGCATCGAAGAAGTCGCTCCTTGCATTTTACAATACGGCAAAGAAAGCAGCGCACAATGGACGAAAATGCAGGAGTTTTTACCGAAAGATTTCAGCGAGTATACA","","","28021","MNNNSPLLKAQSPAALAEEYIVKSIWNNHFPPGSDLPAERELADKIGVTRTTLREVLQRLARDGWLNIQHGKPTKVNDIWETSGLNILETMIQLDGSRLPSLTANMRSARTDISMIYIPKAFKRAPERSLHILHPMDNLEDTAEDYTKFDYDVFRNLAFASDNPVYGLILNSFKSLYTRIGLFYFQSAEARELARRFYFNLRDICQRQSIEEVAPCILQYGKESSAQWTKMQEFLPKDFSEYT","60827","","fatty acid metabolism regulator protein","Cytoplasm","","
InterPro
IPR000524
Domain
Bacterial regulatory protein GntR, HTH
PR00035\"[36-50]T\"[50-66]THTHGNTR
PF00392\"[13-76]TGntR
SM00345\"[17-76]THTH_GNTR
PS50949\"[11-79]THTH_GNTR
InterPro
IPR008920
Domain
Fatty acid responsive transcription factor FadR, C-terminal
PF07840\"[77-241]TFadR_C
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[6-79]Tno description
InterPro
IPR014178
Family
Fatty acid metabolism transcriptional regulator FadR
TIGR02812\"[7-241]TfadR_gamma: fatty acid metabolism transcrip


","BeTs to 7 clades of COG2186COG name: Transcriptional regulatorsFunctional Class: KThe phylogenetic pattern of COG2186 is ---------dr-b-efgh-n-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.3e-15) to 1/1 blocks of the IPB000524 family, which is described as \"Bacterial regulatory proteins, GntR family\". Interpro entry for IP:IPR000524. IPB000524 36-76 1.2e-15","Residues 10 to 83 match (8e-36) PD:PD266930 which is described as COMPLETE PROTEOME DNA-BINDING FATTY TRANSCRIPTION REGULATION METABOLISM REGULATOR ACID ACTIVATOR ","","","","","","","","","","","","Wed Nov 27 13:53:12 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00081 is paralogously related to AA02389 (1e-04).","","","","","","Residues 13 to 76 (E-value = 1.1e-20) place AA00081 in the GntR family which is described as Bacterial regulatory proteins, gntR family (PF00392)","","","","","Burley SK, Kamada K. Transcription factor complexes. Curr Opin Struct Biol. 2002 Apr;12(2):225-30. Review. PMID: 11959501 Rigali S, Derouaux A, Giannotta F, Dusart J. Subdivision of the helix-turn-helix GntR family ofbacterial regulators in the FadR, HutC, MocR, and YtrAsubfamilies. J Biol Chem. 2002 Apr 12;277(15):12507-15. PMID: 11756427 Campbell JW, Cronan JE Jr. Escherichia coli FadR positively regulates transcriptionof the fabB fatty acid biosynthetic gene. J Bacteriol. 2001 Oct;183(20):5982-90. PMID: 11566998 van Aalten DM, DiRusso CC, Knudsen J. The structural basis of acyl coenzyme A-dependentregulation of the transcription factor FadR. EMBO J. 2001 Apr 17;20(8):2041-50. PMID: 11296236 Xu Y, Heath RJ, Li Z, Rock CO, White SW. The FadR.DNA complex. Transcriptional control of fattyacid metabolism in Escherichia coli. J Biol Chem. 2001 May 18;276(20):17373-9. PMID: 11279025 ","","Wed Nov 27 13:53:12 2002","1","","","" "AA00083","60911","60804","108","TTGAACTTGAAAAGTGCGGTGGTTTTTATCAGTGTTTTTCAGCATGATAAAGAAAAAACACCGAAAAAAACTACCGCACTTTTATGTATACTCGCTGAAATCTTTCGG","","","4085","LNLKSAVVFISVFQHDKEKTPKKTTALLCILAEIFR","60804","","hypothetical protein","Cytoplasm","No similarities were found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-2]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Sat Feb 21 11:00:18 2004","Sat Feb 21 11:00:18 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences found to this sequence.AA00083 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sat Feb 21 11:01:01 2004","","","","","","","","","","","","","1","","","" "AA00084","62165","60954","1212","ATGGAACGCTTTCCGAAATCCGATAAATTAGAGCACGTTTGTTATTATATTCGCGGGCCTGTGCATAAAGAGGCACTGCGTCTCGAAGAAGAAGGGCATAAAATTTTAAAATTGAATATCGGCAACCCCGCGCCGTTCGGTTTCGAAGCGCCTGATGAGATTTTGGTGGATGTGTTGCGTAATTTGCCGTCGGCGCAAGGGTATTGCGATTCCAAGGGGCTTTATTCGGCGCGTAAAGCCATTGTGCAATATTATCAATCGAAAGATATTCGTAACGTAACGGTAAACGATGTGTATATCGGCAACGGTGTGTCTGAGTTGATTACTATGGCAATGCAGGCGTTGCTGAATGACGGTGATGAAGTGTTGATCCCGATGCCGGATTATCCGTTATGGACGGCGGCGGCGACCTTGGCGGGCGGCAAAGCGGTGCATTATTTGTGTGATGAACAGGCGGATTGGTCCCCCGATGTGGAAGACATTAAAAGCAAAATTACTTCGCGTACCAAAGCCATTGTGATTATCAACCCGAACAACCCGACGGGAGCAGTGTACAGCAAAGACTTGTTATTGGACATTGTGGACGTGGCGCGTCAGCATAACCTGATTATCTTTGCCGATGAAATTTACGACAAAATTTTATACGACGGCGCAGTGCATCATCATATCGCCGCCTTGGCGCCGGATTTATTAACGGTGACGTTGAACGGGTTGTCAAAAGCCTATCGGGTTGCCGGTTTCCGTCAAGGTTGGATGATTTTGAACGGACCGAAAAAACACGCCAGAGGTTACATTGAAGGTTTGGATATGCTGGCGTCTATGCGTTTGTGCGCCAATGTGCCGATGCAGCACGCCATTCAAACCGCCTTGGGCGGCTACCAAAGCATTAACGAATTTATCCTGCCGGGCGGGCGTTTGTTGGAACAACGGAATAAAGCCTACGAATTAATTAATCAGATTCCGGGCATCAGCTGTACCAAACCGATGGGCGCGTTGTATATGTTCCCGAAAATCGACATCAAAAAATTCAATATGTATGACGATGAAAAAATGGTGTTCGATTTATTGGCGCAGGAAAAAGTGTTGTTGGTACACGGGCGCGGCTTTAACTGGCATTCACCGGATCACTTCCGTATTGTTACATTGCCGTATGTGCATCAAATTGAAGAGGCATTGGACAAATTCGCCGGATTCTTGTCTCATTATCATCAA","","","45450","MERFPKSDKLEHVCYYIRGPVHKEALRLEEEGHKILKLNIGNPAPFGFEAPDEILVDVLRNLPSAQGYCDSKGLYSARKAIVQYYQSKDIRNVTVNDVYIGNGVSELITMAMQALLNDGDEVLIPMPDYPLWTAAATLAGGKAVHYLCDEQADWSPDVEDIKSKITSRTKAIVIINPNNPTGAVYSKDLLLDIVDVARQHNLIIFADEIYDKILYDGAVHHHIAALAPDLLTVTLNGLSKAYRVAGFRQGWMILNGPKKHARGYIEGLDMLASMRLCANVPMQHAIQTALGGYQSINEFILPGGRLLEQRNKAYELINQIPGISCTKPMGALYMFPKIDIKKFNMYDDEKMVFDLLAQEKVLLVHGRGFNWHSPDHFRIVTLPYVHQIEEALDKFAGFLSHYHQ","60954","Probably belongs to class-I of pyridoxal-phosphate-dependent aminotransferease. superfamily: aspartate transaminase","aminotransferase","Cytoplasm","","
InterPro
IPR001176
Family
1-aminocyclopropane-1-carboxylate synthase
PR00753\"[119-140]T\"[166-190]T\"[231-255]TACCSYNTHASE
InterPro
IPR004839
Domain
Aminotransferase, class I and II
PF00155\"[33-395]TAminotran_1_2
InterPro
IPR015421
Domain
Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10\"[63-293]Tno description
noIPR
unintegrated
unintegrated
PTHR11751\"[53-404]TSUBGROUP I AMINOTRANSFERASE RELATED
PTHR11751:SF30\"[53-404]TAMINOTRANSFERASE RELATED


","BeTs to 25 clades of COG0436COG name: PLP-dependent aminotransferasesFunctional Class: EThe phylogenetic pattern of COG0436 is aompkzyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 1e-14) to 3/3 blocks of the IPB001511 family, which is described as \"Aminotransferases class-I\". Interpro entry for IP:IPR001511. IPB001511A 68-78 3.2 IPB001511B 172-186 1.2e-07 IPB001511C 237-250 0.0033","Residues 9 to 74 match (3e-07) PD:PD518318 which is described as PROTEOME COMPLETE AMINOTRANSFERASE ","","","","","Thu Feb 13 17:21:30 2003","","","","","","Wed Dec 11 09:22:08 2002","Wed Dec 11 09:22:08 2002","","Fri May 20 13:44:08 2005","Fri May 20 13:44:08 2005","Fri May 20 13:44:08 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA00084 is paralogously related to AA02757 (1e-11), AA01458 (2e-06), AA02776 (1e-04), AA02579 (6e-04) and AA02917 (0.001).","Fri May 20 13:44:08 2005","","","","","Residues 85 to 399 (E-value = 1.1e-40) place AA00084 in the Aminotran_1_2 family which is described as Aminotransferase class I and II (PF00155)","Fri May 20 13:44:08 2005","","","","Tatusov,R.L., Mushegian,A.R., Bork,P., Brown,N.P., Hayes,W.S.,Borodovsky,M., Rudd,K.E. and Koonin,E.V.Metabolism and evolution of Haemophilus influenzae deduced from awhole-genome comparison with Escherichia coliCurr. Biol. 6 (3), 279-291 (1996)PubMed: 8805245","","Wed Nov 27 14:22:55 2002","1","","","" "AA00085","62282","63583","1302","ATGGATAGTTTGCAATCAATAAAAGCGCAATTAATCAGCCAAATTCATCAATTAGAATCAGAACAACATGCTATTTCGGTTTGCTCGGCGCAGGTCGAAGGCAGCGTTAATTTACTTGCCTGGCTAAAAGCGCAGCCACACTATCCGCAGTGCTATTTCAAATTACAACAAGGCGAATCGGCTTTTGCCGCCATCGGCGAAGTGCGCGCCTTTGATCAATTGATTGCCGCCCAACATTTTATTGAACACGCTGATTTGTCTTTATTCGGCGGCATGACCTTTAACGGCGACACCTATTTTTTCCTGCCGCAACTGCTGTTGGAACAAACGCAATATCGGCTTACGGTGAAAGTGTTTATCGATCACGCCGATTTCAAAGAAAGCAAGCAGCAGGCACTGACGTTCTTAAAAACGCTGGAAAAAACCACCGCACTTTTGGATGTGCAAAGTAAAGCGACCTTATCCCACCGACAAGCCGACCAAGCCCGCTGGCAACATTGGGTAGAACAGGCGTTAGCGCAAATCAGAAGCGGCTATGTGGACAAACTGGTGCTGGCGAATGAAACCACATTTCATCTTAACGCGCCATTAAATGCACAGGATTTTCTCGCCAAAAGCGAAGCCCATAATCACGGTTGTTATCATTTTCTATTGGCGAAAAGCCCTTCTTCCGTTTTTCTTGGCTCTACGCCGGAACGCCTATACGCACGCCATCAGCGCCGGCTCACTACCGAAGCCTTGGCAGGCACGGCATTGGTGAGCGACGACCCCGCAGAAAACCGCCAACAGGCGCAATGGCTCTTGCGGGATAGGAAAAATATTCATGAAAATCAGCTGGTTGCCGAAGGCATTTGCGCCAATCTAAGCGCCTTTGCCAAACAGATTCAGCTCGGTGAAATCGGTTTGAAGCCGCTGCGTCGGGTTCAACATTTACGCCGCGAAATCACCGCACTTTTAACGGAAAACTGCACTGATCTGGATTGTTTAAAAGCCATTCATCCCACTGCTGCCGTTGCCGGTTTGCCACAACAAAGCGCCAAAACCTTATTGGCACAAATTGAAAATTACGATCGGAGCTGGTATGCAGGCACGTTGGGATTTTTTAATCGGGGGCGAGCCGAATTTTGCGTAACCATTCGTTCCGCCTTTATTGAAGCGGACAAAATTCGCGTTTTTGCCGGTGCCGGTATTGTTGAAGGGTCTGTTCCCTTGCTAGAATGGCAGGAAATCGAACGTAAAGCCGCCGGTTTAATCTCATTGTTACAAATAACGGAATCTAAAAACGGAGAGAAAAAATGTCAG","","","48635","MDSLQSIKAQLISQIHQLESEQHAISVCSAQVEGSVNLLAWLKAQPHYPQCYFKLQQGESAFAAIGEVRAFDQLIAAQHFIEHADLSLFGGMTFNGDTYFFLPQLLLEQTQYRLTVKVFIDHADFKESKQQALTFLKTLEKTTALLDVQSKATLSHRQADQARWQHWVEQALAQIRSGYVDKLVLANETTFHLNAPLNAQDFLAKSEAHNHGCYHFLLAKSPSSVFLGSTPERLYARHQRRLTTEALAGTALVSDDPAENRQQAQWLLRDRKNIHENQLVAEGICANLSAFAKQIQLGEIGLKPLRRVQHLRREITALLTENCTDLDCLKAIHPTAAVAGLPQQSAKTLLAQIENYDRSWYAGTLGFFNRGRAEFCVTIRSAFIEADKIRVFAGAGIVEGSVPLLEWQEIERKAAGLISLLQITESKNGEKKCQ","63583","","menaquinone-specific isochorismate; isochorismate mutase","Cytoplasm","","
InterPro
IPR004561
Family
Isochorismate synthase
PIRSF001502\"[8-425]TIsochorismate synthase
PTHR11236:SF3\"[100-426]TISOCHORISMATE SYNTHASE
TIGR00543\"[86-421]Tisochor_syn: isochorismate synthases
InterPro
IPR005801
Domain
Anthranilate synthase component I and chorismate binding protein
PD000779\"[174-414]TMENF_PASMU_Q9CPI5;
PF00425\"[160-421]TChorismate_bind
noIPR
unintegrated
unintegrated
G3DSA:3.60.120.10\"[10-424]Tno description
PTHR11236\"[100-426]TAMINOBENZOATE/ANTHRANILATE SYNTHASE


","BeTs to 8 clades of COG1169COG name: Isochorismate synthaseFunctional Class: H,QThe phylogenetic pattern of COG1169 is -o--------rlbcefgh--------Number of proteins in this genome belonging to this COG is","","Residues 350 to 422 match (4e-22) PD:PD000779 which is described as SYNTHASE PROTEOME COMPLETE ANTHRANILATE COMPONENT I LYASE BIOSYNTHESIS TRYPTOPHAN ISOCHORISMATE ","","","","","","","","","","","","Thu Jan 23 09:23:32 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00085 is paralogously related to AA02173 (4e-12) and AA01609 (2e-06).","","","","","","Residues 160 to 420 (E-value = 1.1e-85) place AA00085 in the Chorismate_bind family which is described as chorismate binding enzyme (PF00425)","","","","","Daruwala,R., Kwon,O., Meganathan,R. and Hudspeth,M.E. A new isochorismate synthase specifically involved inmenaquinone (vitamin K2) biosynthesis encoded by the menF gene FEMS Microbiol. Lett. 140 (2-3), 159-163 (1996) PubMed: 8764478 ","","Wed Nov 27 17:11:48 2002","1","","","" "AA00086","63577","65280","1704","ATGTCAGTAAGCGTATTTAATCGTTGTTGGTCGAAAGTGATCTTGGAAACCCTTGTGCGCCAAGGCGTGTCCCACTTTTGTATCGCGCCCGGTTCGCGTTCGACCCCGCTGACATTGGAAGCCGTCCGTTTACAAAACGCCAACCGCGCCCTTTGCCACACGCACTTCGACGAACGCGGCTTGGGATTTTTTGCTCTTGGTGTGGCGAAAGCCACCAAAAAACCCGTCGCCGTTATTGTCACCTCCGGCACGGCTGGTGCGAATTTATACCCGGCGATCATCGAAGCGCGCCAAAGCCATGTAAACCTCATCGTGCTCACCGCCGATCGCCCGCAGGAATTATGGGAATGCGGCGCCAATCAAGCGATTTTACAAGAAAATATGTTTGCCGATTACCCACTGGCAAGCCTGAATTTACCACGCCCAAGCCAGGATTATGCGGCAAGCTGGTTCATTTCCAAAATCGAACAGGCTTGTCATCAACAGGCGGAAGAAGGCGGCGTCATTCACATTAACGTACCGTTCTCCGAACCGTTATATGACGCCAATGCGGAAGAAATTGACGTTCATCCGTGGCTGGCACAGGTTCAGTGCTGGTTAAGCCAAAATAAAAGTTGGACGACTTATCCCGCCTTGCACCAAGAAGTGATCATTCACGAGAATTGGGATCATTGGCGCACCAAACGCGGTGTTGTCGTGGCGGGCAGAATGCCGGCGGAACAAGCCATGGGTATCGCCGCCTGGGCAAATACCATGGGCTGGGTGTTGTTGACCGACATTCAATCGGGCGTGGAAGCATCACTGCCTTATGCCGACATTTGGCTTGCCAATCAAACGGTAAAACAAAAAATGTTGCAAGCGGATATTGTCATTCAACTTGGCAGCCGTTTTATCAGTAAACGCATTAATCAATTTTTAGCGGAATTTAAAAACGAATATTGGATTGTGGATGAAAACCCGCAAGCCGTGGATCCGTATCATCACTCCCATACCCGTTTTGTTGCCAAAATTCACCATTGGTTACGTGCCCACCCGCCGTTAAGACAAAAACCTTGGCTGTTGGAAGCGTTGGCACTGTCCAAATTCTGCGCCACATTCATTGAGCAACAAGTGGGCGGCAATTTGAACGAAGCCTCTTTAGCTCACCACATTGAACGCCTGCTGCCGAACAACGGCGCACTTTTCCTAGGCAACAGTTTATTTGTGCGCTTGGTGGACGCACTGACCAAATTGCCGGAAGGCTATCCGATTTACACCAATCGCGGCGCCAGTGGCATCGACGGTTTACTTGCCACCGTCGCCGGCATCGGTATCGGTTCCAATCAGCCGGTGGTCGCGTTAGTGGGCGACACGTCCGCGCTGTATGATTTAAACTCGCTGGCGTTATTCAAAAAAATCACCCAACCGACGATTCTTTTTATCATTAATAATAACGGCGGGGCGATTTTCGATATGTTGCCGGTGGATGCGGAAGTGAAAGACAAATTCTACCGTATGCCGCACCATACGGAATTTTCCCAAGTGGCGTCCATGTTCGATTTAAAATATGCGCGCCCTTACACCTGGGCGGATTTGAGTTCCGTACTGAAACAAGCCTATTCACGCCGTGAAGCCACCATCATCGAAATCAAAGTGGCGCCGAATGACGGCAGCACCGTTTATAAACGCCTAATCGAACAAATCAGCTATGCTGTCGTCGGCGAA","","","63383","MSVSVFNRCWSKVILETLVRQGVSHFCIAPGSRSTPLTLEAVRLQNANRALCHTHFDERGLGFFALGVAKATKKPVAVIVTSGTAGANLYPAIIEARQSHVNLIVLTADRPQELWECGANQAILQENMFADYPLASLNLPRPSQDYAASWFISKIEQACHQQAEEGGVIHINVPFSEPLYDANAEEIDVHPWLAQVQCWLSQNKSWTTYPALHQEVIIHENWDHWRTKRGVVVAGRMPAEQAMGIAAWANTMGWVLLTDIQSGVEASLPYADIWLANQTVKQKMLQADIVIQLGSRFISKRINQFLAEFKNEYWIVDENPQAVDPYHHSHTRFVAKIHHWLRAHPPLRQKPWLLEALALSKFCATFIEQQVGGNLNEASLAHHIERLLPNNGALFLGNSLFVRLVDALTKLPEGYPIYTNRGASGIDGLLATVAGIGIGSNQPVVALVGDTSALYDLNSLALFKKITQPTILFIINNNGGAIFDMLPVDAEVKDKFYRMPHHTEFSQVASMFDLKYARPYTWADLSSVLKQAYSRREATIIEIKVAPNDGSTVYKRLIEQISYAVVGE","65280","","2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase","Inner membrane, Cytoplasm","","
InterPro
IPR004433
Family
Menaquinone biosynthesis protein
PIRSF004983\"[4-568]T2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenD
TIGR00173\"[1-564]TmenD: 2-succinyl-6-hydroxy-2,4-cyclohexadie
InterPro
IPR012001
Domain
Thiamine pyrophosphate enzyme, N-terminal TPP binding region
PF02776\"[8-186]TTPP_enzyme_N
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.970\"[7-204]T\"[372-550]Tno description
PTHR18968\"[284-564]TTHIAMINE PYROPHOSPHATE ENZYMES
PTHR18968:SF3\"[284-564]TMENAQUINONE BIOSYNTHESIS PROTEIN


","BeTs to 7 clades of COG1165COG name: 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthaseFunctional Class: HThe phylogenetic pattern of COG1165 is -o--------rlbce-gh--------Number of proteins in this genome belonging to this COG is","Significant hit ( 2.9e-06) to 5/5 blocks of the IPB000399 family, which is described as \"Thiamine pyrophosphate dependent enzyme\". Interpro entry for IP:IPR000399. IPB000399A 18-41 29 IPB000399B 57-70 1.4e+02 IPB000399C 81-104 1e+02 IPB000399D 273-302 5.7 IPB000399E 423-462 0.42","Residues 172 to 329 match (4e-10) PD:PD570946 which is described as 2-KETOGLUTARATE MEND DECARBOXYLASE ","","","","","","","","","","","","Mon Dec 2 08:20:40 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00086 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Saffarini DA, Blumerman SL, Mansoorabadi KJ. Role of menaquinones in Fe(III) reduction by membranefractions of Shewanella putrefaciens. J Bacteriol. 2002 Feb;184(3):846-8. PMID: 11790756 ","","Mon Dec 2 08:20:40 2002","1","","","" "AA00087","65336","66082","747","ATGAAACCGTATCTCGTCTTTTTACACGGCTTACTCGGTACGCAAGCCGACTGGCAAAAACTCACGGAAAATCTACCGCACTTTCATTGCATTGCCCTGGATTTACCGTGGCACGGCAGCGCCAAAAACCACCCTGCGAAAAATTTTGACGAAGCCTGCGCTTATGTGGCGCAACAAATCCAATCGGCAGTGGGGAATCAACCTTATTTTTTAATCGGTTACTCGCTCGGCGGACGGATTGCGCTGTATTACGCACTTCATAGCAACTGTGAAAAATACAACCTGCTGGGCTTGATTATTGAAGGCGGTAATCTTGGGCTGACCGATGAACAAGCGAAAAAAGTGCGGTGGAAAAATGATGTATTTTGGGCGCAACGTTTTCGCTATGAAACGGCGGAATCCGTACTGAACGACTGGTATCAACAGGCGGTATTTGCCCATTTGACCGAACATCAACGCAACGCCCTCATCGAAAAACGCCGAGCCAATTGCGGGGAGAATATTGCACAAATGCTGTTGGCGACCTCCCTTGCCAAACAGCCGGATTTACGTTCTGCCGTCAAAAACAGCCCTTATCCCATTTATTATTTCTGTGGCGAGCGGGATCATAAATTCAAACACATGGCACTGGAAAATCAGCTTAACTTAACCGTTATCCCTAACGCGGGACATAACGCCCATCAGGAAAATCCAACGGCATTTGCCGCGCAATTAAATGCGTTGTTAGAGGATAAATTCGTTGCTTTT","","","28330","MKPYLVFLHGLLGTQADWQKLTENLPHFHCIALDLPWHGSAKNHPAKNFDEACAYVAQQIQSAVGNQPYFLIGYSLGGRIALYYALHSNCEKYNLLGLIIEGGNLGLTDEQAKKVRWKNDVFWAQRFRYETAESVLNDWYQQAVFAHLTEHQRNALIEKRRANCGENIAQMLLATSLAKQPDLRSAVKNSPYPIYYFCGERDHKFKHMALENQLNLTVIPNAGHNAHQENPTAFAAQLNALLEDKFVAF","66082","","possible hydrolase (alpha/beta fold family)","Cytoplasm, Extracellular","","
InterPro
IPR000073
Domain
Alpha/beta hydrolase fold-1
PF00561\"[28-240]TAbhydrolase_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1820\"[2-244]Tno description
PTHR10992\"[3-235]TALPHA/BETA HYDROLASE RELATED
PTHR10992:SF17\"[3-235]TVALACYCLOVIR HYDROLASE
signalp\"[1-16]?signal-peptide


","BeTs to 16 clades of COG0596COG name: Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily)Functional Class: RThe phylogenetic pattern of COG0596 is ao-p-zyq-drlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is","","Residues 110 to 231 match (2e-38) PD:PD013188 which is described as COMPLETE PROTEOME HYDROLASE PM0055 YPO2526 VC1974 YFBB HI0282 ENZYME ","","","","","Wed Feb 19 09:24:24 2003","","","","","","","Mon Dec 2 08:41:54 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00087 is paralogously related to AA02514 (2e-05).","","","","","","Residues 28 to 240 (E-value = 6.9e-23) place AA00087 in the Abhydrolase_1 family which is described as alpha/beta hydrolase fold (PF00561)","","","","","","","","1","","","" "AA00088","66181","66447","267","ATGTCTCTAAGTACTGAACAAAAAGCAAAAATCGTTGCTGAATATGGTCGCGATGGTAAAGATACCGGTTCTTCCGAAGTTCAAATCGCTTTATTAACCGCACAAATCAACCATTTGCAAGCACACTTTGCGGAACACAAAAAAGACCACCACGGTCGCCGCGGTTTATTACGTATGGTTTCCCGTCGTCGTAAACTTTTAGATTACTTAAAACGTACAAATCTTGAACTTTACAGCAGCTTAATCGCTCGTTTAGGTTTACGTCGC","","","10236","MSLSTEQKAKIVAEYGRDGKDTGSSEVQIALLTAQINHLQAHFAEHKKDHHGRRGLLRMVSRRRKLLDYLKRTNLELYSSLIARLGLRR","66447","","30S ribosomal protein S15","Cytoplasm","","
InterPro
IPR000589
Family
Ribosomal protein S15
PF00312\"[6-88]TRibosomal_S15
PS00362\"[39-69]TRIBOSOMAL_S15
InterPro
IPR005290
Family
Ribosomal protein S15, bacterial chloroplast and mitochondrial type
PD157043\"[11-88]TQ9CNX1_PASMU_Q9CNX1;
PTHR23321:SF10\"[4-88]T30S RIBOSOMAL PROTEIN S15
TIGR00952\"[4-89]TS15_bact: ribosomal protein S15
InterPro
IPR009068
Domain
S15/NS1, RNA-binding
G3DSA:1.10.287.10\"[2-89]Tno description
noIPR
unintegrated
unintegrated
PTHR23321\"[4-88]TRIBOSOMAL PROTEIN S15, BACTERIAL AND ORGANELLAR


","BeTs to 19 clades of COG0184COG name: Ribosomal protein S15P/S13EFunctional Class: JThe phylogenetic pattern of COG0184 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 4.8e-33) to 1/1 blocks of the IPB000589 family, which is described as \"Ribosomal protein S15\". Interpro entry for IP:IPR000589. IPB000589 26-71 4.1e-33","Residues 3 to 88 match (6e-24) PD:PD157043 which is described as RIBOSOMAL S15 30S COMPLETE PROTEOME RRNA-BINDING CHLOROPLAST MITOCHONDRIAL TRANSIT PEPTIDE ","","","","","","","","","","","","Mon Dec 2 08:47:10 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00088 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 6 to 88 (E-value = 1.1e-38) place AA00088 in the Ribosomal_S15 family which is described as Ribosomal protein S15 (PF00312)","","","","","Secondary Laboratory Evidence:Takata,R., Mukai,T., Aoyagi,M. and Hori,K. Nucleotide sequence of the gene for Escherichia coliribosomal protein S15 (rpsO) Mol. Gen. Genet. 197 (2), 225-229 (1984) PubMed: 6394953 Evans,S. and Dennis,P.P. Promoter activity and transcript mapping in the regulatoryregion for genes encoding ribosomal protein S15 and polynucleotide phosphorylase of Escherichia coli Gene 40 (1), 15-22 (1985) PubMed: 3005122 Morinaga,T., Funatsu,G., Funatsu,M. and Wittman,H.G. Primary structure of the 16S rRNA binding protein S15 from Escherichia coli ribosomes FEBS Lett. 64 (2), 307-309 (1976) PubMed: 776686 ","","Mon Dec 2 08:47:10 2002","1","","","" "AA00089","66658","67809","1152","ATGAGCCAATATTTATTTACATCCGAATCCGTTTCCGAAGGACATCCGGATAAAATCGCCGATCAGATTTCTGATGCGGTATTAGACGAAATCATCAAACAGGACCCGAAAGCCCGCGTTGCCTGCGAAACCTATGTCAAAACCGGCATGGCGTTGGTGGGCGGTGAAATCACCACTTCCGCGTGGGTGGATATTGAAAACTTGGCCCGTGAAGTAATTTGTGAGATTGGTTACACCAGCTCCGAAATGGGCTTTGACGGTCGTTCCTGCGCGGTATTAAACGCCATCGGTAAGCAATCTTCCGACATCAACCAAGGTGTAGATCGCGAAAACCCGTTGGATCAAGGCGCGGGCGACCAAGGAATCATGTTCGGGTATGCCACCAATGAAACCGATGTATTCATGCCTGCCGCCATCACCTATGCCCATCGTTTAATGGAACGCCAGGCACAAGTGCGCAAAAGCGGAAAATTAGATTGGTTGCGCCCTGATGCGAAAAGCCAATTGACCTTTAAATATGAAGACAACAACATCATCGGAATCGATGCCGTGGTGCTTTCCACCCAGCATTCCGAGGCCATCAGCCCAAAAGAGTTGCATGAAGGCGTCATGGAAGAAATTATCAAACCGATTTTACCGAGCCAATGGTTATCCAAAGACACCAAATATTTCATCAACCCGACCGGTCGTTTTGTCATCGGCGGACCGATGGGCGACTGCGGTTTAACCGGTCGTAAAATCATCGTCGATACTTACGGCGGTGCGGCGCGCCATGGCGGCGGCGCATTTTCCGGTAAGGATCCGTCTAAAGTTGACCGTTCCGCCGCTTATGCCGCCCGTTATGTAGCGAAAAATATCGTCGCGGCGGGCTTGGCGGATCGCTGTGAAATCCAACTGTCTTACGCTATCGGCGTTGCCGAACCGACCTCCATCATGATCGAAACCTTCGGCACCGGTAAAGTGGCTGATGAATCATTGGTGAAATTAATACGCGAATTCTTTGATTTGCGTCCATACGGTTTAATCAAAATGTTAGATTTAATCCAACCGATTTATCGCCAAACGGCGGCTTACGGTCACTTCGGGCGTGAGCAATTCCCGTGGGAGAAAATCGATCGTGCGGCAGATTTACGTGCTGCGGCAGGATTAAAA","","","41993","MSQYLFTSESVSEGHPDKIADQISDAVLDEIIKQDPKARVACETYVKTGMALVGGEITTSAWVDIENLAREVICEIGYTSSEMGFDGRSCAVLNAIGKQSSDINQGVDRENPLDQGAGDQGIMFGYATNETDVFMPAAITYAHRLMERQAQVRKSGKLDWLRPDAKSQLTFKYEDNNIIGIDAVVLSTQHSEAISPKELHEGVMEEIIKPILPSQWLSKDTKYFINPTGRFVIGGPMGDCGLTGRKIIVDTYGGAARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQLSYAIGVAEPTSIMIETFGTGKVADESLVKLIREFFDLRPYGLIKMLDLIQPIYRQTAAYGHFGREQFPWEKIDRAADLRAAAGLK","67809","","S-adenosylmethionine synthase; methionine adenosyltransferase","Cytoplasm","","
InterPro
IPR002133
Family
S-adenosylmethionine synthetase
PIRSF000497\"[2-382]TMethionine adenosyltransferase
PTHR11964\"[1-380]TS-ADENOSYLMETHIONINE SYNTHETASE
PF00438\"[2-101]TS-AdoMet_synt_N
PF02772\"[113-231]TS-AdoMet_synt_M
PF02773\"[233-370]TS-AdoMet_synt_C
TIGR01034\"[5-381]TmetK: S-adenosylmethionine synthetase
PS00376\"[116-126]TADOMET_SYNTHETASE_1
PS00377\"[259-267]TADOMET_SYNTHETASE_2
noIPR
unintegrated
unintegrated
G3DSA:3.30.300.10\"[2-113]T\"[128-233]T\"[244-384]Tno description


","BeTs to 17 clades of COG0192COG name: S-adenosylmethionine synthetaseFunctional Class: HThe phylogenetic pattern of COG0192 is ------yqvdrlbcefghsnuj--twNumber of proteins in this genome belonging to this COG is","Significant hit (7.3e-211) to 7/7 blocks of the IPB002133 family, which is described as \"S-adenosylmethionine synthetase\". Interpro entry for IP:IPR002133. IPB002133A 4-48 1e-37 IPB002133B 76-108 1e-21 IPB002133C 113-143 1e-22 IPB002133D 162-213 2e-22 IPB002133E 239-275 2.8e-36 IPB002133F 276-313 1e-32 IPB002133G 314-363 9.1e-31","Residues 248 to 273 match (8e-07) PD:PD585370 which is described as SYNTHETASE S-ADENOSYLMETHIONINE COMPLETE PROTEOME TRANSFERASE ADENOSYLTRANSFERASE METHIONINE ADOMET METABOLISM ONE-CARBON ","","","","","","","","","","","","Thu Jan 23 09:00:05 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00089 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 233 to 370 (E-value = 3.8e-92) place AA00089 in the S-AdoMet_synt_C family which is described as S-adenosylmethionine synthetase, C-terminal domain (PF02773)","","","","","Takusagawa,F., Kamitori,S., Misaki,S. and Markham,G.D. Crystal structure of S-adenosylmethionine synthetase The Journal of biological chemistry. 271 (1), 136-147 (1996)PubMed: 8550549 Satischandran,C., Taylor,J.C. and Markham,G.D. Isozymes of S-adenosylmethionine synthetase are encoded bytandemly duplicated genes in Escherichia coli Molecular microbiology. 9 (4), 835-846 (1993) PubMed: 8231813 Moore,R.C. and Boyle,S.M. Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli Journal of bacteriology. 172 (8), 4631-4640 (1990) PubMed: 2198270 Markham,G.D., DeParasis,J. and Gatmaitan,J. The sequence of metK, the structural gene forS-adenosylmethionine synthetase in Escherichia coli The Journal of biological chemistry. 259 (23), 14505-14507(1984) PubMed: 6094561 (","","Mon Dec 2 08:55:44 2002","1","","","" "AA00091","67881","68378","498","ATGCAAACAGAAGAAAATTTCCGCATCCTGAAAATGCAGATTCTGCGCCGTTTACAGAGTGGTTTACAGCTGGCAGAAGCGCATTTCAACCAACCCTTTTCAATGCCGCAAATTAATTATGAATTAAAAGGCAGCAAAGCGGGGCTGGCATACCTACAGGAAAACACCATCAAATTTAACCGCACTTTATTACTGGAAAACACCGAAAGATTTATTCATCAAGTGGTGCTACACGAATTGGCGCATTTGGTGGTATATCAACACTATGGCAGAGTACAACCGCACGGCAAAGAATGGCAGTTTGTGATGACCGAGATTTTTCATCTGCCGGCTGAGGTGCGCCATCAATTTGATTTAACCTCTGTGCAAGGCAAAACCTTCACTTACCGTTGCGCCTGTCAAACCCATCAATTAAGTATTCGTCGTCATAATAAAATTCAACGTGATGGTGCAGTATATTTTTGCCGTAAATGCAAAACCCGGTTAAATTGGGTTGTT","","","19767","MQTEENFRILKMQILRRLQSGLQLAEAHFNQPFSMPQINYELKGSKAGLAYLQENTIKFNRTLLLENTERFIHQVVLHELAHLVVYQHYGRVQPHGKEWQFVMTEIFHLPAEVRHQFDLTSVQGKTFTYRCACQTHQLSIRRHNKIQRDGAVYFCRKCKTRLNWVV","68378","","short-patch reverse transcription protein","Cytoplasm","","
InterPro
IPR005622
Family
Protein of unknown function DUF335, SprT
PF03926\"[16-165]TDUF335
InterPro
IPR006025
Binding_site
Peptidase M, neutral zinc metallopeptidases, zinc-binding site
PS00142\"[75-84]?ZINC_PROTEASE
InterPro
IPR006640
Family
Protein of unknown function SprT
SM00731\"[16-165]TSprT


","No hits to the COGs database.","","Residues 16 to 162 match (8e-50) PD:PD034213 which is described as COMPLETE PROTEOME SPRT ZINC CYTOPLASMIC PROTEIN YPO0932 STY3245 HOMOLOG PA1189 ","","","","","","","","","","","","Tue Feb 4 17:24:19 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00091 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 16 to 165 (E-value = 3e-75) place AA00091 in the DUF335 family which is described as Putative metallopeptidase (SprT family) (PF03926)","","","","","Thaler DS, Tombline G, Zahn K.Short-patch reverse transcription in Escherichia coli.Genetics. 1995 Jul;140(3):909-15.PMID: 7545627","","Tue Feb 4 17:24:19 2003","1","","","" "AA00092","68538","69776","1239","ATGTCAAATCAAAATGAAAAAAAATGGCGTAAATTCGATATTATTTGGATGCTTAATCTGTTTGGCACGGCGGTAGGAGCAGGTGTACTGTTTTTGCCGATTAATGCGGGTATGGGGGGATTTTGGCCGTTAATTGTGATGGCGATTTTAGTAGGACCAATGACTTATTTGGCACATCGCGGTTTATCCCGATTCGTGCTGTCGTCCGCCAAGCCGGGCAGTGATATTACCGAAGTGGTAGAGGAACATTTCGGTAAAACAGCAGGGAAATTAATCACCTTGCTGTATTTTTTTGCGATTTTTCCGATTTTGTTAATTTATGGCAATGGCATCACCAACACCGTGGACTCCTTTATCGTCCACCAGCTAGGCATGCCATCGCCGAATCGGGTGCTGCTCTCTTTTGTTCTCATCGCCACATTAATTTCCATTATGCTGATGAATGAAAAAGTGATGCTGAAAATCACCGAATTCTTGGTTTATCCGTTAGTCATCATTCTTGTCGCTTTATCGGTTTACCTGATTCCGAACTGGAACACCTCTATGCTACAGGAAATGCCGACGACTCAAGGCTTTATCATGACCTTGTGGCTCACCATTCCGGTATTGGTATTTTCTTTTAACCACTCTCCTGCCATTTCCGCCTTTTCGCAATCGCAACAACGGGAATACCAAGATCCCGTTTTGGCGGAAAAGCACGCGAGCAAAACATTGAAAGGCACGGCAACCATTTTGTTATTTTTCGTCATGTTCTTTGTGTTCAGCTGCGTATTGACTTTAACCCCGGCGGAGCTTACCGAAGCGAAAGCACAAAATATCAGTATTTTGTCTTATTTAGCCAACAAATTCGACAACCCGTATATTTCCTACCTCGGCCCGTTAGTGGCGTTTTTAGCCATTACCAGCTCCTTCTTCGGACATTATTTGGGCGCCCGTGAAGGGTTGGAAGGCTTGTACTTAAAAATGACCGACAACAAAACCATCAATCGAAAAACACTGAATTATGGCACCGCACTTTTCTTCCTCATCACCCTTTGGCTGGTGGCTATTCGCAATCCGAGCATCCTTGGTTTAATCGAATCGTTGGGCGGCCCGATTATCGCCATGATTTTGTTCATCATGCCAATGTATGCCATTCGTAACGTACCCGCCATGCGACGTTACAGAGGCAGACTCAGCAACGTATTTGTGGTTGTCATGGGGTCCATTGCGATTTCAGCGGTAGTCTATGGATTATTT","","","46025","MSNQNEKKWRKFDIIWMLNLFGTAVGAGVLFLPINAGMGGFWPLIVMAILVGPMTYLAHRGLSRFVLSSAKPGSDITEVVEEHFGKTAGKLITLLYFFAIFPILLIYGNGITNTVDSFIVHQLGMPSPNRVLLSFVLIATLISIMLMNEKVMLKITEFLVYPLVIILVALSVYLIPNWNTSMLQEMPTTQGFIMTLWLTIPVLVFSFNHSPAISAFSQSQQREYQDPVLAEKHASKTLKGTATILLFFVMFFVFSCVLTLTPAELTEAKAQNISILSYLANKFDNPYISYLGPLVAFLAITSSFFGHYLGAREGLEGLYLKMTDNKTINRKTLNYGTALFFLITLWLVAIRNPSILGLIESLGGPIIAMILFIMPMYAIRNVPAMRRYRGRLSNVFVVVMGSIAISAVVYGLF","69776","","serine transporter","Inner membrane, Cytoplasm","","
InterPro
IPR004694
Family
Serine transporter
TIGR00814\"[9-403]Tstp: serine transporter
InterPro
IPR013057
Family
Amino acid transporter, transmembrane
PF01490\"[17-411]TAa_trans
noIPR
unintegrated
unintegrated
signalp\"[1-26]?signal-peptide
tmhmm\"[15-33]?\"[39-59]?\"[91-111]?\"[130-148]?\"[158-178]?\"[192-212]?\"[242-262]?\"[290-310]?\"[331-351]?\"[357-377]?\"[392-412]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 8.7e-39) to 6/6 blocks of the IPB002091 family, which is described as \"Aromatic amino acids permease\". Interpro entry for IP:IPR002091. IPB002091A 16-59 2.4e-10 IPB002091B 78-115 3.5e-05 IPB002091C 201-216 0.025 IPB002091D 236-278 0.13 IPB002091E 295-319 7e-07 IPB002091F 333-383 0.00053","Residues 9 to 411 match (4e-165) PD:PD008790 which is described as PROTEOME COMPLETE TRANSPORTER SERINE TRANSMEMBRANE INNER MEMBRANE HAAAP AMINO ACID ","","","","","","","","","","","","Mon Dec 2 09:05:09 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00092 is paralogously related to AA02973 (4e-10), AA01245 (8e-10), AA01704 (1e-06) and AA00468 (1e-05).","","","","","","Residues 22 to 408 (E-value = 9.5e-06) place AA00092 in the Trp_Tyr_perm family which is described as Tryptophan/tyrosine permease family (PF03222)","","","","","Shao,Z., Lin,R.T. and Newman,E.B. Sequencing and characterization of the sdaC gene andidentification of the sdaCB operon in Escherichia coli K12 Eur. J. Biochem. 222 (3), 901-907 (1994) PubMed: 8026499 ","","Wed Dec 11 09:42:20 2002","1","","","" "AA00093","69872","71233","1362","ATGATTAGTGTTTTTGATATGTTTAAAATCGGCATCGGCCCGTCCAGCTCACACACGGTGGGTCCGATGAAGGCGGGGAAACAGTTTATTGACGATTTAATTGCGCAACATCTCTTGGAAAAAACAGAGAAAATCCAAGTGGATGTTTACGGTTCACTCTCCATGACCGGTCTTGGACACGGCACCGACATCGCCATCATCATGGGGCTGGCAGGCTATTTACCGCATAATGTGGAAATTGAACGTATCCCCGGGTTCATTGCGGAGGTAAAGAAAACCGCCAAACTGCCCCTTGCCAAAGGCAAACAGACTGCACAATTTGACCCGGCAACGGACATGATTTTTCACCAAACCTTCCTGCCGCTGCACGAAAACGGCATGACCATTACCGCATTTCATCAGGCGCAAGAATTATATAAACAAACCTATTATTCTATCGGCGGCGGGTTTATTGTAGACGAAGCCCATTTCAACCAAACCGAAAAAAATGAAATGAACGTGCCTTATCCCTACCACATTGCGGCGGATATTTTACGTAACTGTCAGGAAAGCGGGTTATCCATTTCCAGTTTAATGATGCAAAATGAACTGGCACTACATAGTGAAGAAGAATTAAAAACCCATTTGCATCAAGTGTGGCAGACCATGAAAGATTGTATCGAACACGGTTTACACACTGAAGGGGTTCTACCCGGTCCGTTAAAAGTAGCTCGTCGTGCGGCAACACTTTATCGCATGCTGAAAGCGAACAGCGAGCTTTCAATGGATCCAATGAGTGTCATCGACTGGGTAAATATGTTTGCTTTGGCGGTGAACGAAGAAAATGCTGCCGGCGGACGAGTCGTCACCGCCCCCACTAACGGTGCTTGCGGTATTGTGCCTGCGGTGCTGGCGTATTATGAGAAATTTGTCGGCACACTCACCGATGAAATCGTCGAACGCTACTTACTCGCCTGCGGCATGATCGGTTCGTTGTACAAAATGAACGCCTCCATTTCCGGTGCGGAAGTAGGCTGTCAGGGGGAAGTGGGCGTTGCCTGCTCGATGGCGGCGGCAGGACTTTCGGAAATTCTCGGCGGCAGCCCGGAACAGGTGTGCATTGCGGCGGAGATCGCCATGGAACACAACCTTGGCTTAACCTGCGACCCAGTGGGCGGGCAAGTGCAGGTGCCTTGCATCGAACGCAACGCTATCGCCTCCGTCAAAGCCATTAACGCCAGCCGCATGGCATTGCGTCGCACCACCAGCCCGCGCGTCAGTCTGGATAAGGTGATCGAAACCATGTACGAAACCGGTAAAGACATGAACGCCAAATACCGCGAAACCTCACAAGGCGGCTTAGCGATTAAAGTGGTTTGCTCG","","","49205","MISVFDMFKIGIGPSSSHTVGPMKAGKQFIDDLIAQHLLEKTEKIQVDVYGSLSMTGLGHGTDIAIIMGLAGYLPHNVEIERIPGFIAEVKKTAKLPLAKGKQTAQFDPATDMIFHQTFLPLHENGMTITAFHQAQELYKQTYYSIGGGFIVDEAHFNQTEKNEMNVPYPYHIAADILRNCQESGLSISSLMMQNELALHSEEELKTHLHQVWQTMKDCIEHGLHTEGVLPGPLKVARRAATLYRMLKANSELSMDPMSVIDWVNMFALAVNEENAAGGRVVTAPTNGACGIVPAVLAYYEKFVGTLTDEIVERYLLACGMIGSLYKMNASISGAEVGCQGEVGVACSMAAAGLSEILGGSPEQVCIAAEIAMEHNLGLTCDPVGGQVQVPCIERNAIASVKAINASRMALRRTTSPRVSLDKVIETMYETGKDMNAKYRETSQGGLAIKVVCS","71233","","L-serine dehydratase (L-serine deaminase)","Cytoplasm","","
InterPro
IPR004644
Family
Iron-sulfur-dependent L-serine dehydratase single chain form
TIGR00720\"[1-454]Tsda_mono: L-serine ammonia-lyase
InterPro
IPR005130
Domain
Serine dehydratase alpha chain
PF03313\"[172-450]TSDH_alpha
InterPro
IPR005131
Domain
Serine dehydratase beta chain
PF03315\"[3-159]TSDH_beta


","BeTs to 10 clades of COG1760COG name: L-serine deaminaseFunctional Class: EThe phylogenetic pattern of COG1760 is ---------drlb-efgh-nuj----Number of proteins in this genome belonging to this COG is","","Residues 2 to 57 match (1e-18) PD:PD428043 which is described as L-SERINE PROTEOME COMPLETE DEHYDRATASE LYASE DEAMINASE GLUCONEOGENESIS 4FE-4S IRON-SULFUR SDH ","","","","","","","","","","","","Mon Dec 2 09:08:19 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00093 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 172 to 450 (E-value = 2e-194) place AA00093 in the SDH_alpha family which is described as Serine dehydratase alpha chain (PF03313)","","","","","Secondary Laboratory Evidence:Su H, Moniakis J, Newman EB. Use of gene fusions of the structural gene sdaA to purifyL-serine deaminase 1 from Escherichia coli K-12. Eur J Biochem. 1993 Feb 1;211(3):521-7. PMID: 8436113 Su H, Newman EB. A novel L-serine deaminase activity in Escherichia coliK-12. J Bacteriol. 1991 Apr;173(8):2473-80. PMID: 2013569 Su HS, Lang BF, Newman EB. L-serine degradation in Escherichia coli K-12: cloning andsequencing of the sdaA gene. J Bacteriol. 1989 Sep;171(9):5095-102. PMID: 2504697","","Mon Dec 2 09:08:19 2002","1","","","" "AA00096","72466","71420","1047","ATGAAGTTAAGAAAATTAACCGCATTCACCGTATTAAGTTTAGCCTGTTCCGTCGCCTATGCGGCAAATTTGCCGAACATTACCATTTTGGCAACCGGCGGAACCATTGCCGGCGGTGGGGAAACGGCGGTCAGTTCTGCCTATAAAGCAGGGCAGTTGACGGTAGAGCGCTTAATTGAAGCGGTGCCGGAAATGAAAAATCTTGCGGAAATTAAAGGCGAACAAGTTGTGAATATCGGTTCACAGGATATGAACGATGAAGTGTGGCTAAAATTAGCCAAAACCATTAATCGGCAATGCGCCGATACGGACGGCTTTGTGATTACGCACGGTACGGACACTATGGAAGAAACCGCGTATTTTCTGGATTTAACTGTGAAATGTGACAAACCGGTGGTATTAGTGGGCGCTATGCGTCCGGCGACGGAGAAAAGCGCTGATGGTCCGTTAAATTTATATAATGCCGTAGTGGTGGCGACAAATAAAAAATCTGCCGGCCGCGGTGTGCTGGTGGCGATGAACGACAAAGTACTGGGTGCCCGCGATGTAACCAAAATGAGCACTACGGCGGTGCAAACCTTTGTAGCGCCGAACTTCGGTCCGTTAGGCTATATTCATAACAGCAAAGTGGATTACGAACGTTCGCCGGAAAGCAAACACACTGCTAATACGCCGTTTGATGTATCGAAACTGGACGCTTTGCCGAAAGTGGGCATTGTATATGCGTATTCCAATATGCCGACGGAACCGTTACAAGCCTTATTGAGCGCGGGGTATCAGGGTGTCATTAGTGCCGGCGTGGGCAATGGCAATGTGAATCAGGCAAATTTGGATTTATTGGAAAAAGCGGCAAAAGACGGCGTGGCAGTGGTGCGTTCTTCCCGCGTGCCGACGGGCTACACCACCCGTGATGCGGAAGTGGATGACAGCAGATACGGCTTCGTGACCTCAGGTTCGTTGAACCCGCAAAAAGCGCGCGTGTTGTTGCAATTAGCATTAACCAAAACCAAAGATGTGAAGGAAATTCAGCAATATTTCGATGATTTT","","","37305","MKLRKLTAFTVLSLACSVAYAANLPNITILATGGTIAGGGETAVSSAYKAGQLTVERLIEAVPEMKNLAEIKGEQVVNIGSQDMNDEVWLKLAKTINRQCADTDGFVITHGTDTMEETAYFLDLTVKCDKPVVLVGAMRPATEKSADGPLNLYNAVVVATNKKSAGRGVLVAMNDKVLGARDVTKMSTTAVQTFVAPNFGPLGYIHNSKVDYERSPESKHTANTPFDVSKLDALPKVGIVYAYSNMPTEPLQALLSAGYQGVISAGVGNGNVNQANLDLLEKAAKDGVAVVRSSRVPTGYTTRDAEVDDSRYGFVTSGSLNPQKARVLLQLALTKTKDVKEIQQYFDDF","71420","","L-asparaginase II precursor","Periplasm","","
InterPro
IPR004550
Family
L-asparaginase, type II
TIGR00520\"[1-349]TasnASE_II: L-asparaginases, type II
InterPro
IPR006034
Family
Asparaginase/glutaminase
PD003221\"[44-346]TASG2_HAEIN_P43843;
PR00139\"[27-38]T\"[104-122]T\"[283-301]TASNGLNASE
PIRSF001220\"[24-347]TL-asparaginase/Glutamyl-tRNA(Gln) amidotransferase subunit D
PTHR11707\"[76-349]TL-ASPARAGINASE
PF00710\"[26-343]TAsparaginase
PS00144\"[29-37]TASN_GLN_ASE_1
PS00917\"[105-115]TASN_GLN_ASE_2
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1170\"[21-235]Tno description
G3DSA:3.40.50.40\"[236-349]Tno description
PIRSF500176\"[24-347]TL-asparaginase/L-glutaminase
PTHR11707:SF4\"[76-349]TL-ASPARAGINASE II
PS51257\"[1-16]TPROKAR_LIPOPROTEIN
signalp\"[1-21]?signal-peptide


","BeTs to 19 clades of COG0252COG name: L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit DFunctional Class: E,JThe phylogenetic pattern of COG0252 is aompkzy--drlb-efghsnu-----Number of proteins in this genome belonging to this COG is","Significant hit ( 3.9e-97) to 5/5 blocks of the IPB000267 family, which is described as \"Asparaginase/glutaminase family\". Interpro entry for IP:IPR000267. IPB000267A 24-40 2.9e-09 IPB000267B 58-96 1.5e-19 IPB000267C 104-148 6.7e-35 IPB000267D 155-196 3.9e-16 IPB000267E 320-346 3.8e-12","Residues 24 to 346 match (9e-134) PD:PD003221 which is described as L-ASPARAGINASE COMPLETE PROTEOME HYDROLASE AMIDOHYDROLASE L-ASPARAGINE L-ASNASE I REPEAT II ","","","","","","","","","","","","Mon Dec 2 09:13:29 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00096 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 35 to 344 (E-value = 3e-174) place AA00096 in the Asparaginase family which is described as Asparaginase (PF00710)","","","","","Scott S, Busby S, Beacham I. Transcriptional co-activation at the ansB promoters:involvement of the activating regions of CRP and FNR whenbound in tandem. Mol Microbiol. 1995 Nov;18(3):521-31. PMID: 8748035 Jennings MP, Scott SP, Beacham IR. Regulation of the ansB gene of Salmonella enterica. Mol Microbiol. 1993 Jul;9(1):165-72. PMID: 8412661 Jennings MP, Beacham IR. Co-dependent positive regulation of the ansB promoter ofEscherichia coli by CRP and the FNR protein: a molecularanalysis. Mol Microbiol. 1993 Jul;9(1):155-64. PMID: 8412660 Harms E, Wehner A, Jennings MP, Pugh KJ, Beacham IR, RohmKH. Construction of expression systems for Escherichia coliasparaginase II and two-step purification of the recombinantenzyme from periplasmic extracts. Protein Expr Purif. 1991 Apr-Jun;2(2-3):144-50. PMID: 1821783 Bonthron DT. L-asparaginase II of Escherichia coli K-12: cloning, mappingand sequencing of the ansB gene. Gene. 1990 Jul 2;91(1):101-5. PMID: 2144836 Jennings MP, Beacham IR. Analysis of the Escherichia coli gene encodingL-asparaginase II, ansB, and its regulation by cyclic AMPreceptor and FNR proteins. J Bacteriol. 1990 Mar;172(3):1491-8. PMID: 2407723 ","","Thu Jan 23 10:38:28 2003","1","","","" "AA00099","72761","73897","1137","ATGTTAGAACAAACTGTTGCCGAACCGGCAAAAAAAGTCAATTTAATGAATTTAACCCGCGCACAAATGCGTGAATTTTTCGCTGAATTAGGCGAAAAACCGTTTCGCGCCGATCAGTTGGTGAAATGGATTTATCATTTCGGCGAAGACAATTTCGACAATATGACCAACCTGAACAAAGCGTTACGGGAAAAATTAAAAACCATGGCGGAAATCAAAGCGCCGGAAGTGGCGGTTGAGCAACGTTCCGCCGACGGCACCATTAAATGGGCGATGCAGGTGGGCGATCAGCAAGTGGAAACCGTGTATATTCCCGAAGCGGATCGCGCCACCTTATGCGTTTCTTCGCAAGTGGGTTGCGCCTTGGCTTGCACCTTCTGTTCCACCGCCCAACAGGGTTTTAACCGCAATTTAACGGTGGCGGAAATTATCGGTCAGGTGTGGCGCGCCTCGAAAATTATCGGTAATTTCGGCGTCACCGGCGTGCGTCCGATTACCAACGTCGTGATGATGGGCATGGGCGAACCCTTGTTAAATGTGGCGAATGTGGTGCCGGCAATGGAAATTATGCTGGATGACTTCGCCTACGGCTTGTCCAAACGCCGCGTGACCTTATCCACCTCCGGCGTGGTACCGGCGTTGGACAATTTAAGCAAAATGATCGATGTGGCGTTGGCGATTTCCCTGCACGCGCCGAACGATGAATTGCGCGATGAAATCGTGCCGTTAAACAAGAAATACAACATTAAAACCCTGATTGATTCGGTGAACCGTTATTTGAGCGTCTCCAACGCCAATCACGGCAAAGTCACCATTGAATATGTGATGCTGGATCACATTAACGATCATGTGGAACACGCCCATCAGCTCGCCGCCGTACTGAAAAATACGCCGTGCAAAATTAACCTGATTCCGTGGAACCCGTTCCCCCAAGCGCCTTATGCGAAAAGTTCCAACACGCGAATTGACCATTTCCAAAAAACCTTGATGGAATACGGTTTAACCGTGATTGTGCGCAAAACCCGCGGCGATGATATTGATGCCGCCTGCGGACAATTAGCCGGCGATGTGATCGACCGTACCAAACGCACCGCACAGAAAAAACACTTCGGGCAAGGCATTGCCGTTCAAATTCAA","","","42885","MLEQTVAEPAKKVNLMNLTRAQMREFFAELGEKPFRADQLVKWIYHFGEDNFDNMTNLNKALREKLKTMAEIKAPEVAVEQRSADGTIKWAMQVGDQQVETVYIPEADRATLCVSSQVGCALACTFCSTAQQGFNRNLTVAEIIGQVWRASKIIGNFGVTGVRPITNVVMMGMGEPLLNVANVVPAMEIMLDDFAYGLSKRRVTLSTSGVVPALDNLSKMIDVALAISLHAPNDELRDEIVPLNKKYNIKTLIDSVNRYLSVSNANHGKVTIEYVMLDHINDHVEHAHQLAAVLKNTPCKINLIPWNPFPQAPYAKSSNTRIDHFQKTLMEYGLTVIVRKTRGDDIDAACGQLAGDVIDRTKRTAQKKHFGQGIAVQIQ","73897","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR004383
Family
Conserved hypothetical protein 48
TIGR00048\"[9-365]TTIGR00048: radical SAM enzyme, Cfr family
InterPro
IPR007197
Domain
Radical SAM
PF04055\"[114-291]TRadical_SAM


","BeTs to 16 clades of COG0820COG name: Predicted Fe-S-cluster redox enzymeFunctional Class: RThe phylogenetic pattern of COG0820 is -------qvdrlbcefghsnuj--twNumber of proteins in this genome belonging to this COG is","","Residues 300 to 353 match (3e-08) PD:PD445749 which is described as PROTEOME COMPLETE AQ_416 ","","","","","","","","","","","","Mon Dec 2 09:21:02 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00099 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 114 to 291 (E-value = 2.2e-14) place AA00099 in the Radical_SAM family which is described as Radical SAM superfamily (PF04055)","","","","","","","","1","","","" "AA00101","73922","74470","549","ATGATCAAATTTCAACAGCACAATCGTGCAATACCGTTTATTTTTCCGTTTTTGCTTTCCGCCTGCGTCACCCAACAAAGTGCGGTGGATTTTGACAAGCAAAAAGCCGCCAAAGCACGCGTGGAACTGGCATTAGGCTATTTACAGCAGCAAGATTCGGCACAAGCCAAGCTGAACCTGGATAAAGCCTTTTCTTACGCTCCCGATTATTATTTAGTGTCAGCGGCATTTGCCTATTTCTATCAACAACAGGGCGACATTGAACAAGCCCGTACCACCTATTTAAACGCGATAAAATTAGATGATAAACAAGGGGATGTGTTCAATAATTACGGTGCATTTCTTTGTGCGCAAGGGGAATTCGACAGTGCCTATGTACAATTTGAACGCGCCTTAAAAAGCTCGAATTATTACCATCAGGCGGACACTTATGAAAACTTGGCGTTATGTGCTTTATCCGCCAAAAATCAGGCGATTTATCGGCAAAATCTCGCATTATTGACGAAAATCTCTCCGAAACGGGCGGCAAAATTACCACAAGGGATAAAA","","","20682","MIKFQQHNRAIPFIFPFLLSACVTQQSAVDFDKQKAAKARVELALGYLQQQDSAQAKLNLDKAFSYAPDYYLVSAAFAYFYQQQGDIEQARTTYLNAIKLDDKQGDVFNNYGAFLCAQGEFDSAYVQFERALKSSNYYHQADTYENLALCALSAKNQAIYRQNLALLTKISPKRAAKLPQGIK","74470","","fimbrial biogenesis and twitching motility protein","Periplasm, Outer membrane, Extracellular","","
InterPro
IPR011990
Domain
Tetratricopeptide-like helical
G3DSA:1.25.40.10\"[33-173]Tno description
InterPro
IPR013026
Domain
Tetratricopeptide region
SM00028\"[37-70]T\"[71-104]T\"[105-138]TTPR
PS50293\"[37-138]TTPR_REGION
InterPro
IPR013360
Family
Pilus biogenesis/stability type IV, PilW
TIGR02521\"[11-179]Ttype_IV_pilW: type IV pilus biogenesis/stab
noIPR
unintegrated
unintegrated
PTHR23083\"[47-133]TTETRATRICOPEPTIDE REPEAT PROTEIN, TPR
PTHR23083:SF23\"[47-133]TO-GLCNAC TRANSFERASE, P110 SUBUNIT-RELATED
PS51257\"[1-22]TPROKAR_LIPOPROTEIN
signalp\"[1-28]?signal-peptide


","No hits to the COGs database.","","Residues 37 to 94 match (3e-08) PD:PD586509 which is described as COMPLETE PROTEOME BIOGENESIS FIMBRIAL PROTEIN TWITCHING PRECURSOR SIGNAL HI0366 MOTILITY ","","","","","","","","","","","","Mon Dec 2 09:25:45 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00101 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00105","74617","75669","1053","ATGAATATGCAAAATACATCAGAAACACAATCCCGCAACGAACAGCAGACCACTTTAGGCGATAAATTCCGCCTTGCCCGCGAAGCCCTTAACCTGACACCGGAGCAAGTGTCAAAAGAGATTTCCCTACGCCCTGCCCTCGTTCGTCTCATCGAAAATAATCAGTTTACTAACGAAACCATTCCCGCCACATTTATGCGCGGTTATGTGCGTAGTTATGCGAAATTTTTGCGTATTCCGGACAGCGAATGGATGAATGTCATTCATTTCGGCAACGAACAGAAAAACGATTTGGGCAAAAACGCCCGCGCCACCCGCTCCGTTAACCAATATTCGTCACACAATAACTGGATCGGTTACCTCAGCGCGTTAGTCATTTTGATCGTGGTCGGCATGACCGGAATGTGGTGGTGGGAAAGCCACCAGCAATCTAACGCGGAACGGGATGTATTAGTCAATTCCTACACGCCGTCCGCACCGGTGACAACGGAAGTGAACACCGCGCCTGCCAAGCCCGCAGGTAACGAGATTCCGGTGCCGCAGCCTACGGACAAAATCGAAAATACCTTAACGGATACCGCACCGAAAGGCACCGGCATCGAAATTGAAACCAAACCGCTCACAGAGACACCGGTTGCAGCCAATACGACGGCGCCTTTCGTTCAAGAATCAAACACTCCGGCAGCAACCGCCAATGTGTTGCAATCGAAAATGGAAAAAATCGGCAGCAATGAGCAGTTAACTAGCGTTCAACCTGAATCGCAAGCCTCCGCCAAGCCACAAAGTGCGGTGGAAAATTCAAGTGTTTCTGCCGTCGCCACAAAGGATAACTTATATATTGAAGTTATCGGCAACTGCTGGATCAGCGTTAAAGATAAAAACCGCAAAGTCTTGGCACAAAAAGAATACAAACAAGGTGATGTGTTGAGTTTCAACGAAGAAGAACCTTATTCGTTAATTATTGGCGCGCCGGGCAACGTAAGAATTACTTATAAAGGTCAAGCCTTCCCGTTGACCGTTGACGGACGTGTGGCAAAATTTAAATTACCTCAA","","","38845","MNMQNTSETQSRNEQQTTLGDKFRLAREALNLTPEQVSKEISLRPALVRLIENNQFTNETIPATFMRGYVRSYAKFLRIPDSEWMNVIHFGNEQKNDLGKNARATRSVNQYSSHNNWIGYLSALVILIVVGMTGMWWWESHQQSNAERDVLVNSYTPSAPVTTEVNTAPAKPAGNEIPVPQPTDKIENTLTDTAPKGTGIEIETKPLTETPVAANTTAPFVQESNTPAATANVLQSKMEKIGSNEQLTSVQPESQASAKPQSAVENSSVSAVATKDNLYIEVIGNCWISVKDKNRKVLAQKEYKQGDVLSFNEEEPYSLIIGAPGNVRITYKGQAFPLTVDGRVAKFKLPQ","75669","","conserved hypothetical protein","Periplasm, Cytoplasm, Extracellular","","
noIPR
unintegrated
unintegrated
tmhmm\"[118-138]?transmembrane_regions


","BeTs to 7 clades of COG1426COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG1426 is --------v--lb-efghs---xit-Number of proteins in this genome belonging to this COG is","","Residues 5 to 83 match (9e-09) PD:PD452808 which is described as COMPLETE PROTEOME DNA-BINDING MEMBRANE YFGA PARAL ","","","","","","","","","","","","Mon Dec 2 09:28:59 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00105 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00106","75684","76784","1101","ATGTTAGAAAAACCAAAGATTCAGCGTAGAGAATCAACGAAAATTTATGTGGGAAAGGTGCCGGTGGGCGGCGATGCGCCGATTGCCGTGCAATCAATGACAAATACGCGCACTACCGATGTGGAAGCCACCGTGGCGCAGATTAAGTCTCTGGAACGGGTGGGCGCGGATATTGTGCGCGTTTCTGTGCCGACCATGGACGCGGCGGAAGCCTTCAAATTAATCAAACAACAAGTCAACGTGCCGCTGGTGGCGGATATTCACTTTGACTATCGCATTGCGTTGAAAGTAGCGGAATACGGCGTGGACTGTTTACGTATCAACCCGGGCAATATCGGGCGAGAAGATCGCATTCATGCCGTGGTGGATTGCGCTAAAGATAAAAATATTCCGATTCGGATCGGCGTCAATGCCGGTTCTCTGGAAAAAGACATTCAGGAAAAATACGGCGAACCGACACCGCAAGCCTTATTGGAATCCGCATTACGTCATGTGGAAATTCTTGATCGTTTGAACTTCGATCAATTTAAAGTGAGTGTTAAAGCCTCCGATGTTTATTTGGCGGTAGAATCCTATCGCCTGCTCGCCAAAGCCATTAAGCAACCCTTACATTTAGGCATTACCGAAGCCGGCGGTGCCCGTGCAGGCGCGGTGAAATCGGCAATCGGTTTGGGAATGCTATTGTCCGAAGGCATCGGCGATACGTTACGGGTATCCTTAGCGGCGGATCCAATGGAAGAAATCAAAGTCGGTTTCGACATTTTGAAATCCTTACGCATTCGTTCGCGCGGGATTAATTTCATCGCCTGCCCGACCTGCTCCCGTCAGGAATTTGATGTTATCGGCACGGTCAACGCCCTTGAACAGCGTTTGGAAGACATTATCACGCCGATGGACGTCTCCATTATCGGCTGCGTGGTAAACGGCCCAGGAGAAGCGCTGGTGTCCGATTTGGGTGTGACCGGCGGCAACAAGAAAAGCGGTTATTATCTTTCCGGAGAACGTCAAAAAGAACGTTTTGACAATGAGGATTTAATCAATCAGCTGGAAGCCAAAATTCGCGCCCGCGTTGCGCAGCAAGATCCGAAAAATCGCATTATT","","","40082","MLEKPKIQRRESTKIYVGKVPVGGDAPIAVQSMTNTRTTDVEATVAQIKSLERVGADIVRVSVPTMDAAEAFKLIKQQVNVPLVADIHFDYRIALKVAEYGVDCLRINPGNIGREDRIHAVVDCAKDKNIPIRIGVNAGSLEKDIQEKYGEPTPQALLESALRHVEILDRLNFDQFKVSVKASDVYLAVESYRLLAKAIKQPLHLGITEAGGARAGAVKSAIGLGMLLSEGIGDTLRVSLAADPMEEIKVGFDILKSLRIRSRGINFIACPTCSRQEFDVIGTVNALEQRLEDIITPMDVSIIGCVVNGPGEALVSDLGVTGGNKKSGYYLSGERQKERFDNEDLINQLEAKIRARVAQQDPKNRII","76784","From Genbank:[gi:1169879] This protein converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate(ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.","1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase","Cytoplasm","","
InterPro
IPR004588
Family
IspG protein
PF04551\"[9-361]TGcpE
TIGR00612\"[9-354]TispG_gcpE: 4-hydroxy-3-methylbut-2-en-1-yl


","BeTs to 16 clades of COG0821COG name: Essential bacterial protein, involved in density-dependent regulation of peptidoglycan biosynthesisFunctional Class: MThe phylogenetic pattern of COG0821 is -------qvdr-bcefghsnuj-it-Number of proteins in this genome belonging to this COG is","","Residues 10 to 350 match (1e-181) PD:PD008743 which is described as ISOPRENE 4-DIPHOSPHATE SYNTHASE BIOSYNTHESIS 1-HYDROXY-2-METHYL-2-E-BUTENYL PROTEOME COMPLETE GCPE E ","","","","","","","","","","","Mon Jan 13 15:15:30 2003","Mon Jan 13 15:15:30 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00106 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 9 to 361 (E-value = 1.5e-247) place AA00106 in the GcpE family which is described as GcpE protein (PF04551)","","","","","Baker,J., Franklin,D.B. and Parker,J. Sequence and characterization of the gcpE gene ofEscherichia coli FEMS microbiology letters. 73 (1-2), 175-180 (1992) PubMed: 1521767 Altincicek B, Kollas AK, Sanderbrand S, Wiesner J, Hintz M,Beck E, Jomaa H. GcpE is involved in the 2-C-methyl-D-erythritol 4-phosphatepathway of isoprenoid biosynthesis in Escherichia coli. J Bacteriol. 2001 Apr;183(8):2411-6. PMID: 11274098 Campos N, Rodriguez-Concepcion M, Seemann M, Rohmer M,Boronat A. Identification of gcpE as a novel gene of the2-C-methyl-D-erythritol 4-phosphate pathway for isoprenoidbiosynthesis in Escherichia coli. FEBS Lett. 2001 Jan 19;488(3):170-3. PMID: 11163766 Seemann M, Bui BT, Wolff M, Tritsch D, Campos N, Boronat A,Marquet A, Rohmer M. Isoprenoid Biosynthesis through the MethylerythritolPhosphate Pathway: The (E)-4-Hydroxy-3-methylbut-2-enylDiphosphate Synthase (GcpE) is a [4Fe-4S] Protein. Angew Chem Int Ed Engl. 2002 Nov 15;41(22):4337-4339. PMID: 12434382 ","","Mon Dec 2 09:52:51 2002","1","","","" "AA00107","76839","78083","1245","ATGAACGATTGCTTACCAACGGAAACCCCTTTGTGGCAGTGGGTTGAAAATAAAGTGCGGTCGGTTTTACAGGCGTATGGTTACGCCGAAATCCGGATGCCGATTGTGGAAAGCACGCCGTTATTCGCCCGCGCTATCGGTGAGGTGACCGATGTAGTAGAAAAAGAAATGTTTACCTTTAACGACCGTGACGACGAAAGTTTAACGCTCCGTCCGGAAGGTACGGCAGGTTGCGTGCGCGCCGGGATTGAGCACGGTTTGTTATATAATCAGGAACAGCGTTTGTGGTACATGGGACCGATGTTCCGTTACGAACGCCCGCAAAAAGGGCGTTATCGTCAATTCCATCAGGTCGGCGTGGAAATTTTCGGCATTCCGAATCCGGAAATTGATGCAGAGATTATCGCTTTAACCGCCCGTTTGTGGAAAGATTTAGGTATTTTTGACCATGTTACCCTTCAACTTAATTCCATCGGCTCCTTGGAAGCACGTAAAAATTATCGCCAGGCGTTGGTGGCTTTCCTGCAAAATCATCTTGATATTTTAGATGAAGACAGTAAACGCCGTTTAACCACCAATCCGTTACGGATTTTAGACAGCAAAGATCAGCGCGTTCAACAAGTATTAAATGATGCGCCGAAATTACACGATTACCTTGATGAAGAATCCCGCGAACATTTTGCACAATTATGCGCCTTGTTGGATAATTTAGGCATCACATACGAAATCAATCAAAAACTGGTACGCGGTTTGGACTACTACAATAAAACCGTGTTTGAATGGGTGACTTCCGCGTTGGGCGCGCAAGGCACGGTATGCGGTGGCGGTCGTTATGACGGCTTGGTGGAACAGCTTGGCGGACACGCCACCTCCGGTGTCGGTTTCGCTATGGGCTTAGAGCGTTTAGTGTTGCTCGTGCAGGAAGTCAATAAACAGATTACGCTACCAAGTGCGGTGGATATTTACATTGTTTATCAAGGTGAAGGCACTACGGTGGCGGCGTTTAGCCTGGCGGAAAAACTCCGCTCGGAATTACCGCACTTACGCACGCTATTGCATTGCAGCGGCGGAAACTTCAAAAAACAATTCAAACGTGCCGATAAAAGCGGTGCAAAATTGGCTTTAGTGATCGGTGAAGATGAAGTGAAAAATCAACAAGTGGTTGTGAAAGAATTGCTACAACATAGCGAACAAGTGGTGGTAGCATTAAGCGACATTACGACTCATATTCAAAATACGTTTAAA","","","47958","MNDCLPTETPLWQWVENKVRSVLQAYGYAEIRMPIVESTPLFARAIGEVTDVVEKEMFTFNDRDDESLTLRPEGTAGCVRAGIEHGLLYNQEQRLWYMGPMFRYERPQKGRYRQFHQVGVEIFGIPNPEIDAEIIALTARLWKDLGIFDHVTLQLNSIGSLEARKNYRQALVAFLQNHLDILDEDSKRRLTTNPLRILDSKDQRVQQVLNDAPKLHDYLDEESREHFAQLCALLDNLGITYEINQKLVRGLDYYNKTVFEWVTSALGAQGTVCGGGRYDGLVEQLGGHATSGVGFAMGLERLVLLVQEVNKQITLPSAVDIYIVYQGEGTTVAAFSLAEKLRSELPHLRTLLHCSGGNFKKQFKRADKSGAKLALVIGEDEVKNQQVVVKELLQHSEQVVVALSDITTHIQNTFK","78083","","histidyl-tRNA synthetase","Cytoplasm","","
InterPro
IPR002314
Domain
tRNA synthetase, class II (G, H, P and S)
PF00587\"[11-178]TtRNA-synt_2b
InterPro
IPR004154
Domain
Anticodon-binding
G3DSA:3.40.50.800\"[316-415]Tno description
PF03129\"[320-413]THGTP_anticodon
InterPro
IPR004516
Family
Histidyl-tRNA synthetase, class IIa
PIRSF001549\"[1-414]THistidyl-tRNA synthetase
InterPro
IPR006195
Domain
Aminoacyl-transfer RNA synthetase, class II
PS50862\"[15-316]TAA_TRNA_LIGASE_II
InterPro
IPR015805
Family
Histidyl-tRNA synthetase
PTHR11476\"[1-415]THISTIDYL-TRNA SYNTHETASE
InterPro
IPR015807
Family
Histidyl-tRNA synthetase 1
TIGR00442\"[1-410]ThisS: histidyl-tRNA synthetase
noIPR
unintegrated
unintegrated
G3DSA:3.30.930.10\"[1-313]Tno description


","BeTs to 26 clades of COG0124COG name: Histidyl-tRNA synthetaseFunctional Class: JThe phylogenetic pattern of COG0124 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 15 to 282 match (2e-09) PD:PD169451 which is described as COMPLETE REGULATORY BIOSYNTHESIS PROTEOME SUBUNIT PHOSPHORIBOSYLTRANSFERASE ATP HISTIDINE PROBABLE ","","","","","","","","","","","","Mon Dec 2 09:58:27 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00107 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 320 to 413 (E-value = 5.9e-17) place AA00107 in the HGTP_anticodon family which is described as Anticodon binding domain (PF03129)","","","","","Gillet S, Hoang CB, Schmitter JM, Fukui T, Blanquet S,Hountondji C. Affinity labeling of Escherichia coli histidyl-tRNAsynthetase with reactive ATP analogues. Identification oflabeled amino acid residues by matrix assisted laserdesorption-ionization mass spectrometry. Eur J Biochem. 1996 Oct 1;241(1):133-41. PMID: 8898898 Freedman,R., Gibson,B., Donovan,D., Biemann,K., Eisenbeis,S.,Parker,J. and Schimmel,P. Primary structure of histidine-tRNA synthetase andcharacterization of hisS transcripts J. Biol. Chem. 260 (18), 10063-10068 (1985) PubMed: 2991272 Eisenbeis,S.J. and Parker,J. The nucleotide sequence of the promoter region of hisS, the structural gene for histidyl-tRNA synthetase Gene 18 (2), 107-114 (1982) PubMed: 6290315 Arnez,J.G., Harris,D.C., Mitschler,A., Rees,B.,Francklyn,C.S. and Moras,D. Crystal structure of histidyl-tRNA synthetase fromEscherichia coli complexed with histidyl-adenylate EMBO J. 14 (17), 4143-4155 (1995) PubMed: 7556055 ","","Mon Jan 13 15:17:13 2003","1","","","" "AA00108","78097","78708","612","ATGGCTTATACCATTGAAGAAGAACAAGAACTGACTGCCATCAAAGCCTGGTGGAATGAAAATTACAAATTTATTATCGTTTGTTTTGTTATTGCGTTTGGTGGCGTATTCGGCTGGAATTACTGGCAGTCTCATCAAATACAAAAAATGCACAAAGCCTCTGCAGAATATGAACAGGCATTGTTTAACTATCAAAAAGATCCGAAAGCACAAGCGGAACAATTTAATCAATTCATTAAAAACAATGAAAAAACCAGCTATGCCGTCTTAGCCTTGCTGGATAAGGCTAAAATCGCAGTGGAAAACAAAGACTTCCCATTGGCAGAAGATGCGCTGAAACAAGCGATGGCGCAATCTAACAATGATATTTTATCTTCCGTCAGTGCGTTACGTTTGGCGTCCGTACAATTCCAGTTGGGGCAATTGGATCCCGCGTTGGAAAGCCTTAAATCCGTCAAAGAACAGGCATGGAACAGCGCAAAAAACCTGTTGGCAGGCGATATTCAATTAGCCAAAGGCGATAAAGAAGCCGCGAAGAAAAGCTACCAACAGGCACAGGAAAATGCCGGTGCGTTGGAGCAACAGCTCATTCAAGTGCGGTTAAATAATTTA","","","23050","MAYTIEEEQELTAIKAWWNENYKFIIVCFVIAFGGVFGWNYWQSHQIQKMHKASAEYEQALFNYQKDPKAQAEQFNQFIKNNEKTSYAVLALLDKAKIAVENKDFPLAEDALKQAMAQSNNDILSSVSALRLASVQFQLGQLDPALESLKSVKEQAWNSAKNLLAGDIQLAKGDKEAAKKSYQQAQENAGALEQQLIQVRLNNL","78708","","conserved hypothetical protein","Periplasm","","
InterPro
IPR011990
Domain
Tetratricopeptide-like helical
G3DSA:1.25.40.10\"[89-187]Tno description
noIPR
unintegrated
unintegrated
PD012704\"[87-157]TYA57_ACTAC_O52728;
signalp\"[1-38]?signal-peptide
tmhmm\"[24-42]?transmembrane_regions


","BeTs to 5 clades of COG2976COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG2976 is --------------efghsn------Number of proteins in this genome belonging to this COG is","","Residues 1 to 38 match (3e-15) PD:PD015452 which is described as TRANSMEMBRANE COMPLETE PROTEOME PM2012 HI0370 ","","","","","","","","","","","","Mon Dec 2 09:59:56 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00108 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00109","78722","79213","492","TTGGTTTCCAAGCCTTTCTGTTATCTCGCTTCAAGGCTTACTATGTCAAGAAATAAACCGAAAATTCCCATTCCGCCGCCACTCATTTTTGTTTTTTGCGCGTTACTGATGAAATTGCTGCCACCCGTTTGGCAATTTCCGACATCCTGGGGATTGGTCATTATTTTCAGTGCCTTAGGTTGCTTCATCGGCGCAGGCAGTGTGCTGCAATTTTTGCTGGCAAAAACCACCGTCAATCCGCTGCAATTAGAAACCGCTTCACAATTAGTGACGACTGGAATTTATAAATTCACCCGCAATCCCATGTATTTAGGATTAGTTTTTATCTTGCTGAGTTGGATGTGTTACTTAGGTTCGTTATCTGCTTTTTTCGGCATTGTATTATTCATTTGGTACATCACCGAGTTTCAGATTAAACGGGAAGAAGAAAGCCTGCGAAACATTTTTGGAGAGCAATTTACACAATATTTCCGTCGTACCCGCAGATGGTTG","","","18977","LVSKPFCYLASRLTMSRNKPKIPIPPPLIFVFCALLMKLLPPVWQFPTSWGLVIIFSALGCFIGAGSVLQFLLAKTTVNPLQLETASQLVTTGIYKFTRNPMYLGLVFILLSWMCYLGSLSAFFGIVLFIWYITEFQIKREEESLRNIFGEQFTQYFRRTRRWL","79213","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
PTHR12714\"[76-160]TPROTEIN-S ISOPRENYLCYSTEINE O-METHYLTRANSFERASE
signalp\"[1-45]?signal-peptide
tmhmm\"[21-41]?\"[47-69]?\"[104-133]?transmembrane_regions


","No hits to the COGs database.","","Residues 89 to 164 match (4e-08) PD:PD010871 which is described as STEROL COMPLETE PROTEOME REDUCTASE TRANSMEMBRANE METHYLTRANSFERASE BIOSYNTHESIS OXIDOREDUCTASE NADP CARBOXYL ","","","","","","","","","","","","Mon Dec 2 10:08:56 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00109 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00110","79899","79225","675","TTGCCTATTCATCAGCTTGATGATGATACGTTGGAAAATTTCCATGCGGAAAATAATCAGCTGCTGCTCAATTCCCTGCAAAAAAATTTCTCCCATCCTCAACAGCAATTTTTCTATATTTGGGGCAATCGCGGCAGTGGTAAAAGCCATTTGTTGAAAGCCATTTGCCATCATTATTTAACCCAACAACGCCCCGCACTTTATGTTCCGTTGAATAAGGCTCAGTATTTCTCCCCGGCAGTGTTGGAAAATCTTGAACGGCAGGACGTCGTGTGTTTGGATGACGTGCAGGAAGTGATAGGCAATGCGGAATGGGAACTGGCGATTTTCGATTTAATTAATCGCATTCGCGAAACCGGAAAAACCCTTTTATTAATGGGCTCCGATCAATCTCCGGCGAATTTGGCGGCGCGCCTGCCGGATCTCCGTTCCCGTTTGACTTGGGGGGAGGTGTATCAATTAATGCCGCTGGACGACGCACAAAAAATTGCCGTGTTGCAAGAGAATGCGCACCAGCGCGGTATCGAATTGCCTGATGAAACGGCAAATTTCCTGTTTAAGCGTTTGGAGCGGGATATGAAAACCTTATTCGAAGCCTTAGAAAAACTGGATCAGGCTTCTTTGCAGGCGCAACGCAAACTAACCATTCCCTTCGTCAAAGAAATCCTGTCTCTA","","","26977","LPIHQLDDDTLENFHAENNQLLLNSLQKNFSHPQQQFFYIWGNRGSGKSHLLKAICHHYLTQQRPALYVPLNKAQYFSPAVLENLERQDVVCLDDVQEVIGNAEWELAIFDLINRIRETGKTLLLMGSDQSPANLAARLPDLRSRLTWGEVYQLMPLDDAQKIAVLQENAHQRGIELPDETANFLFKRLERDMKTLFEALEKLDQASLQAQRKLTIPFVKEILSL","79225","","ATPase involved in DNA replication","Cytoplasm","","
InterPro
IPR001957
Family
Bacterial chromosomal replication initiator protein, DnaA
PR00051\"[35-55]T\"[123-150]TDNAA
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[34-150]TAAA
InterPro
IPR013317
Domain
Chromosomal replication initiator, DnaA
PF00308\"[6-210]TBac_DnaA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[7-154]Tno description


","BeTs to 18 clades of COG0593COG name: ATPase involved in DNA replication initiationFunctional Class: LThe phylogenetic pattern of COG0593 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.6e-08) to 3/4 blocks of the IPB001957 family, which is described as \"Bacterial chromosomal replication initiator protein, DnaA\". Interpro entry for IP:IPR001957. IPB001957A 35-52 0.019 IPB001957B 81-127 4.1 IPB001957C 139-170 0.046","Residues 40 to 223 match (3e-71) PD:PD433007 which is described as COMPLETE PROTEOME DNAA-RELATED REPLICATION XF0590 INSERTION RSC2625 RP631 NMA1279 MLR7968 ","","","","","","","","","","","","Wed Feb 19 15:50:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00110 is paralogously related to AA00001 (9e-17).","","","","","","","","","","","","","","1","","","" "AA00111","79888","80046","159","ATGAATAGGCAAAGGAAGTTGAAAATGTGGCTCGCTCAAATCAAATACCGAAAAATGCTGAAGGAAAGTGCGGTAAGAATAAACGAAATTTTTTCATTTAGAAAGCCATTGGCGGATATTTTTATCCTCGTTTTTATATCCGCCAATGGGATTTTCGTT","","","6356","MNRQRKLKMWLAQIKYRKMLKESAVRINEIFSFRKPLADIFILVFISANGIFV","80046","","hypothetical protein","Cytoplasm","No similarities were found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-1]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Sat Feb 21 11:02:16 2004","Sat Feb 21 11:02:16 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA00111 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sat Feb 21 11:03:07 2004","","","","","","","","","","","","","1","","","" "AA00112","81299","80049","1251","ATGACAACAGCAACACAATTAGACGCATCACAAGCGCGTCAAAGCGTCGGCAAGCAAGCGTTTGTCGGTTTACAAATGTTATTCGTCGCGTTTGGTGCATTGGTCTTAGTGCCTTTGATTACCGGGCTTGACGCCAATACGGCATTACTTACCGCCGGTATCGGAACCTTGCTTTTCCAACTTTGCACCGGCAAACAGGTGCCGATTTTCTTAGCGTCGTCCTTTGCCTTTATCGCACCGATTCAATACGGCGTCGCCACCTGGGGTATTCCTGTCACCATGGGCGGTTTGGAGTGCGCCGGCTTGGTTTATGTGGCGTTAAGCGCACTGGTGAAACTGCGCGGCGCGGCGGCGTTGGAGCGCATTTTCCCGCCGGTGGTGGTCGGTCCGGTGATTATTATCATCGGTATGGGCTTGGCGCCCATCGCCGTGGATATGGCGCTCGGTAAAAACAGCGACTATCAATATAACGATGCGGTGCTGGTTTCCATGGTGACCCTGATTACCACCTTGTGTGTCGCGGTGTTTTCTAAAGGCTTGATGAAATTAATCCCGATTATGTTCGGTATCGCCGTGGGCTATATTTTATGCCTGTTCATGGGCTTAATTAAATTCCAACCTGTATTGGACGCGCCTTGGTTCAGTATGCCGAATCTTACGGCACCGGAGTTTAAACTGGAGGCGATTTTATATTTACTGCCGATTGCTATCGCGCCTGCGGTTGAGCACGTGGGCGGGATTATGGCAATCAGTTCGGTCACGGGCAAAGATTTTATCAAAAAACCGGGCCTGCATCGCACGTTGCTGGGCGACGGTATCGCCACCGGTGCTGCCTCATTATTAGGTGGACCGCCGAATACCACTTATGCGGAAGTGACCGGCGCGGTGATGCTGACCCGTAACTTTAATCCGAATATCATGACTTGGGCGGCAGTTTGGGCGATTGGTATTTCTTTCTGTGGCAAAGTAGGTGCCTTCTTATCCACCATTCCGACCATCGTGATGGGTGGCATCATGATGTTGGTGTTCGGTTCCATTGCGGTAGTAGGCATGAGCACCTTAATTCGCGCCAAAGTGGATGTTACCGAAGCGCGTAATTTGTGTATCATTGCGGTGGTAATGACCTTCGGTATCGGCAATATGTTCGTTGATGTGGGTGGTGTTTCTTTAAAAGGAATCAGCCTGTGCGCCGTGGTGGCGATTATCTTGAATCTGGTATTGCCAAAAGCGAAAAATGACACCCTTCAGGAT","","","43531","MTTATQLDASQARQSVGKQAFVGLQMLFVAFGALVLVPLITGLDANTALLTAGIGTLLFQLCTGKQVPIFLASSFAFIAPIQYGVATWGIPVTMGGLECAGLVYVALSALVKLRGAAALERIFPPVVVGPVIIIIGMGLAPIAVDMALGKNSDYQYNDAVLVSMVTLITTLCVAVFSKGLMKLIPIMFGIAVGYILCLFMGLIKFQPVLDAPWFSMPNLTAPEFKLEAILYLLPIAIAPAVEHVGGIMAISSVTGKDFIKKPGLHRTLLGDGIATGAASLLGGPPNTTYAEVTGAVMLTRNFNPNIMTWAAVWAIGISFCGKVGAFLSTIPTIVMGGIMMLVFGSIAVVGMSTLIRAKVDVTEARNLCIIAVVMTFGIGNMFVDVGGVSLKGISLCAVVAIILNLVLPKAKNDTLQD","80049","","uracil permease","Inner membrane, Cytoplasm","","
InterPro
IPR006042
Family
Xanthine/uracil permease
TIGR00801\"[13-406]Tncs2: uracil-xanthine permease
PS01116\"[330-350]TXANTH_URACIL_PERMASE
InterPro
IPR006043
Family
Xanthine/uracil/vitamin C permease
PTHR11119\"[11-413]TXANTHINE-URACIL / VITAMIN C PERMEASE FAMILY MEMBER
PF00860\"[17-386]TXan_ur_permease
noIPR
unintegrated
unintegrated
PTHR11119:SF3\"[11-413]TXANTHINE-URACIL PERMEASE
signalp\"[1-42]?signal-peptide
tmhmm\"[21-41]?\"[47-67]?\"[88-108]?\"[122-144]?\"[159-177]?\"[183-203]?\"[306-326]?\"[332-352]?\"[367-385]?\"[391-411]?transmembrane_regions


","BeTs to 9 clades of COG2233COG name: Xanthine/uracil permeasesFunctional Class: FThe phylogenetic pattern of COG2233 is ----k---vd-lb-efgh-n------Number of proteins in this genome belonging to this COG is","Significant hit ( 4.1e-32) to 2/2 blocks of the IPB000444 family, which is described as \"Xanthine/uracil permeases family\". Interpro entry for IP:IPR000444. IPB000444A 270-299 3.4e-10 IPB000444B 311-354 1.6e-20","Residues 159 to 216 match (8e-16) PD:PD488820 which is described as PROTEOME COMPLETE PERMEASE URACIL INNER PROBABLE MEMBRANE URACIL/XANTHINE TRANSMEMBRANE TRANSPORTER ","","","","","","","","","","","","Mon Dec 2 10:27:02 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00112 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 17 to 386 (E-value = 1.3e-137) place AA00112 in the Xan_ur_permease family which is described as Permease family (PF00860)","","","","","Andersen,P.S., Frees,D., Fast,R. and Mygind,B. Uracil uptake in Escherichia coli K-12: isolation of uraAmutants and cloning of the gene J. Bacteriol. 177 (8), 2008-2013 (1995) PubMed: 7721693 ","","Mon Dec 2 10:27:02 2002","1","","","" "AA00113","82049","81426","624","ATGAAATTAGTAGAAGTTAAACATCCGTTAGTAAAGCATAAACTAGGTTTAATGCGGGCCGCCGATATTGATACCAAGAAATTTCGTGAATTGGCGATGGAAGTGGGCAGCTTGTTGACCTATGAAGCCACCTCGGATTTAGAAACGGAAAAAGTGATTATTGATGGTTGGTGCGGTCCGGTAGAAATCGATCGTATTAAAGGCAAGAAAGTGACCGTGGTGCCGATTTTGCGTGCCGGTCTTGGCATGATGGACGGCGTGTTGGAGCACGTGCCGAGTGCGCGTATCAGCGTAGTGGGGATGTACCGTAATGAAGAAACGTTAGAGCCGGTGCCGTACTTTCAAAAACTTGCCAGTGATTTAGATGAACGCTTGGCAATCGTGGTGGATCCGATGTTGGCAACGGGCGGTTCCATGATTGCTACCATTGATTTACTTAAACAAAAAGGTTGCCAACATATTAAAGTATTGGTTTTGGTGGCGGCACCGGAAGGGCTTGCCGCATTGGAAAAAGCCCATCCCGATATTGAGTTATATACGGCTTCTATTGACGATCACTTAAATGAAAACGGCTACATCATTCCGGGTTTAGGTGACGCGGGCGACAAGATTTTTGGTACGAAA","","","26592","MKLVEVKHPLVKHKLGLMRAADIDTKKFRELAMEVGSLLTYEATSDLETEKVIIDGWCGPVEIDRIKGKKVTVVPILRAGLGMMDGVLEHVPSARISVVGMYRNEETLEPVPYFQKLASDLDERLAIVVDPMLATGGSMIATIDLLKQKGCQHIKVLVLVAAPEGLAALEKAHPDIELYTASIDDHLNENGYIIPGLGDAGDKIFGTK","81426","","uracil phosphoribosyltransferase","Cytoplasm","","
InterPro
IPR000836
Domain
Phosphoribosyltransferase
PF00156\"[41-179]TPribosyltran
InterPro
IPR005765
Family
Uracil phosphoribosyl transferase
TIGR01091\"[2-208]Tupp: uracil phosphoribosyltransferase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2020\"[6-208]Tno description
PTHR10285\"[1-207]TURIDINE KINASE RELATED
PTHR10285:SF1\"[1-207]TURACIL PHOSPHORIBOSYLTRANSFERASE


","BeTs to 19 clades of COG0035COG name: Uracil phosphoribosyltransferaseFunctional Class: FThe phylogenetic pattern of COG0035 is -om-kzyqvdrlbcefgh-nuj--twNumber of proteins in this genome belonging to this COG is","","Residues 118 to 206 match (4e-09) PD:PD183421 which is described as PROTEOME PHOSPHORIBOSYLTRANSFERASE PYROPHOSPHORYLASE COMPLETE GLYCOSYLTRANSFERASE UPRTASE URACIL TRANSFERASE UMP ","","","","","","","","","","","","Mon Dec 2 10:31:31 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00113 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 41 to 179 (E-value = 7.3e-16) place AA00113 in the Pribosyltran family which is described as Phosphoribosyl transferase domain (PF00156)","","","","","ndersen,P.S., Smith,J.M. and Mygind,B. Characterization of the upp gene encoding uracil phosphoribosyltransferase of Escherichia coli K12 Eur. J. Biochem. 204 (1), 51-56 (1992) PubMed: 1371255 Savacool HK, Switzer RL. Characterization of the interaction of Bacillus subtilis PyrRwith pyr mRNA by site-directed mutagenesis of the protein. J Bacteriol. 2002 May;184(9):2521-8. PMID: 11948166 Martinussen J, Schallert J, Andersen B, Hammer K. The pyrimidine operon pyrRPB-carA from Lactococcus lactis. J Bacteriol. 2001 May;183(9):2785-94. PMID: 11292797 Ghim SY, Kim CC, Bonner ER, D'Elia JN, Grabner GK, SwitzerRL. The Enterococcus faecalis pyr operon is regulated byautogenous transcriptional attenuation at a single site inthe 5' leader. J Bacteriol. 1999 Feb;181(4):1324-9. PMID: 9973361 ","","Wed Jan 22 18:02:59 2003","1","","","" "AA00114","84031","82187","1845","ATGGTAATGGAAAAACTGCACGGAGCTTCAAATAACTGGGCTTCCAAGTTTCTTTTTGGTTTTATTACGGTCACTTTCGTTATTAGTTCTATGGCAGGCTATCTTTACTCCAGAATTGATAGTTCGGCAGCGAAAGTGAACGGCGAAGAAATTTCACAGCAAGCTTTTCAAAATCAATACAATATCGCCTCTCAAAATCTTAGCCCGCAAGAAGCGGATTCTCCGACTGTCGTTGCCAATTTAAAAAGACAGGTTCTATCTTCCCTGATTGATCAGGAATTACTGCGCCAATATGTTAAAGACCTCAAATTAGGCGTCAGCGATGAGCGTATTAAGCAGGAAATCGTCACCACACCGAGCTTCCAAAATAACGGCAAATTTGACAATGTGTTATATCAGCAGTTGTTGCAAAGCAACGGTATCAGCGCCGAAACCTATGCCGGTTATGTGCGCGAAGCCTTGCATTTGGAGCAATTGCAAAGCGGTTTAGGTATTACCGCGTTCACCGTGCCGGTGCAGCAGGAAGCCTTGACAAAACTTTTCTTTCAACGTCGTGATGTGCGTTTAGCAGCACTGTCTTTAGCGGACGAAATTGCCAAACAAACGGTCAGTGCCGAAGAAATTCAAGCTTACTATGACGCCCATAAGGCAGATTTTACCCTGCCGGAATCGGTGAAAGTGCAATATCTTGATTTGTCCGGCGCCAATATGGAGAAAAACATCAATATTAGCAATGTGGAAATTGCGCAATATTATCAGGACAATAAATCCCAATTCATGACTCAAGGGCAACAACGTCTCGCGCATATTGAAGTGAAAACCGAGCAACAGGCACAGGATTTATATCAACAACTGCAAAACGGCGCGGACTTTGCCACTTTAGCGAAGAACCATTCCATTGACCCGATTAGTGCGGAAAAAGGCGGAGATTTAAGTTGGGTAAGTGCGGGTGAATTTCCGAAAGTTTTTGAAGACGCCGCGAATGCCTTGGATGTGGGTAAGTTCAGTCAGCCGGTTAAATTAGATAATAGCTACCACATTATTTTAGTGGAAGAGCGTAAAGATTCGGCGGTGTTGCCGTTGGAGCGCGTGAGGCCTCAAATTGTTGCGCAAATTCGTCAAAATTTAGTGAATAACCAGTTCTTTTCCGTTGAAAAACGCGTGGCAGAAAAAGCCTTTGAAGATTCTTCCTCTTTGAACGCGGCGGCGGAAGCCGGTGGCGTGAAAGTACAGGAAACGGGGTATTTCTCACGTAAAGATATTCCGGCAGCGTTAAATTACCCAAATGTAGTTTCGGCGATTTTTGATTCCGATATTTCTCAGGGCGGTAGCAATTCCGAACCGATGAGCATCGGCGATCAGCATTCGGTTGTTATTCGTGTGTTAGAGCATAAAGCGGAAAGCGTGAAAAGTTTAGACGAAGCGAAAAATGACATTACCGCCCGTCTTAAACGCCAAAAGGCGGAAGCGGTGGTGTTAGCCGAAGCCAACAAGTTAGTGCAGGAATTAACGGCGGGTAAAACCGTGGATAGCCTGAAATTCGGTGCGACACAAAGCTTGGTATTCGCAGAAAATAACGATCCGATGTTGTACAATGCCGTGTTTGCGATGCCGAAACCGACGGAAGGAAAAGCGGTTTACCAAGCAACCAAAGAAACAAAAGGCGACATTGTTGTGATTGCCTTGGATAAGGTTGTTGACGGCGCACTAAGCGAACAGGAGCAACAACAATTTGCCGTGCAACTGGCGCGTGCCGATCAGATTGCGTTGCAGAATAATCTGTTGAATGTGTTACGCGCCAAAGCCAAAATTGAAATAAACGATTCGGTGGTGAATCAGGAGCAA","","","71260","MVMEKLHGASNNWASKFLFGFITVTFVISSMAGYLYSRIDSSAAKVNGEEISQQAFQNQYNIASQNLSPQEADSPTVVANLKRQVLSSLIDQELLRQYVKDLKLGVSDERIKQEIVTTPSFQNNGKFDNVLYQQLLQSNGISAETYAGYVREALHLEQLQSGLGITAFTVPVQQEALTKLFFQRRDVRLAALSLADEIAKQTVSAEEIQAYYDAHKADFTLPESVKVQYLDLSGANMEKNINISNVEIAQYYQDNKSQFMTQGQQRLAHIEVKTEQQAQDLYQQLQNGADFATLAKNHSIDPISAEKGGDLSWVSAGEFPKVFEDAANALDVGKFSQPVKLDNSYHIILVEERKDSAVLPLERVRPQIVAQIRQNLVNNQFFSVEKRVAEKAFEDSSSLNAAAEAGGVKVQETGYFSRKDIPAALNYPNVVSAIFDSDISQGGSNSEPMSIGDQHSVVIRVLEHKAESVKSLDEAKNDITARLKRQKAEAVVLAEANKLVQELTAGKTVDSLKFGATQSLVFAENNDPMLYNAVFAMPKPTEGKAVYQATKETKGDIVVIALDKVVDGALSEQEQQQFAVQLARADQIALQNNLLNVLRAKAKIEINDSVVNQEQ","82187","","peptidyl-prolyl cis-trans isomerase D (PPIase D) (rotamase D)","Periplasm, Outer membrane","","
InterPro
IPR000297
Domain
Peptidyl-prolyl cis-trans isomerase, PpiC-type
PF00639\"[269-352]TRotamase
PS50198\"[262-352]TPPIC_PPIASE_2
PS01096\"[291-312]?PPIC_PPIASE_1
InterPro
IPR013982
Domain
AICARFT/IMPCHase bienzyme, formylation region
SM00798\"[128-308]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.10.50.40\"[258-355]Tno description
PTHR10657\"[273-431]TROTAMASE
signalp\"[1-32]?signal-peptide
tmhmm\"[15-37]?transmembrane_regions


","BeTs to 15 clades of COG0760COG name: Parvulin-like peptidyl-prolyl isomeraseFunctional Class: OThe phylogenetic pattern of COG0760 is ------yqvd-lbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 8.1e-08) to 2/2 blocks of the IPB000297 family, which is described as \"PpiC-type peptidyl-prolyl cis-trans isomerase\". Interpro entry for IP:IPR000297. IPB000297A 288-299 0.0024 IPB000297B 304-314 0.014","Residues 104 to 238 match (2e-09) PD:PD012172 which is described as COMPLETE PROTEOME KINASE ATP-BINDING TRANSFERASE BINDING MEMBRANE SIGNAL DNA PRECURSOR ","","","","","Wed Feb 19 16:25:13 2003","","","","Wed Feb 19 16:25:13 2003","","","Mon Dec 2 10:44:27 2002","","","Tue Mar 2 14:00:52 2004","","yes","Fri Feb 20 15:41:32 MST 1998","AA00114 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Tue Mar 2 14:00:52 2004","","","","","Residues 269 to 352 (E-value = 1.6e-32) place AA00114 in the Rotamase family which is described as PPIC-type PPIASE domain (PF00639)","Tue Mar 2 14:00:52 2004","","","","Muller M, Koch HG, Beck K, Schafer U.Protein traffic in bacteria: multiple routes from the ribosome to and across the membrane.Prog Nucleic Acid Res Mol Biol. 2001;66:107-57. Review.PMID: 11051763 Dartigalongue C, Raina S.A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli.EMBO J. 1998 Jul 15;17(14):3968-80.PMID: 9670013 ","","Tue Feb 18 14:15:31 2003","1","","","" "AA00115","86437","84167","2271","ATGAAAATTCAGCAGGTTATAAAAGAAAATCGCTTGGAATTGTTGTTTCAGCAGGGTTCTTTCGGTATTGAAAAAGAAAGCCAACGCGTGTATGCGGACGGTTCCGTTGTGGTAAGCGCACACCCGAAATGTTTTGGCAGCCGTTCTTACCACCCTTATATCCAAACGGATTTCGCCGAAAGCCAGCTTGAATTAATTACCCCGCCGAATAAAAAAATTGAAGACACTTTACGTTGGTTATCCGCCATTCATGAAGTAGTGTTGCGCACCATGCTGCAAGATGAATACGTGTTTCCGTTAAGTATGCCGGCAGGGTTGCCGCCGGAAGAGCAAATCAAAGTAGCGCAATTGGAGAATCCGGCAGATGTGGCATATCGTGAGCATTTGGTGCAATCCTACGGCAAAAGCAAACAAATGGTGAGCGGTGTTCACTATAATTTCCAACTGGATCCCGCTCTAATCCGGCAGCTTTTTAACGGGCAAAATGAATACCAAAGTGCGGTGGATTTTCAGAATGATTTGTATCTGAAAGTTGCCCGCAATTTCCTGCGTTATCAATGGATTCTCGTTTATTTACTGGCGGCGACGCCGACCGTTGACGCTAATTATTTCCGCGGCGGCACGCCATTAAAACCGGGACAATATGTGCGTAGTCTGCGTTCCAGCCAATATGGCTATGTGAATGATCCGAGCGTCAAAATTTCTTACGACAGCTTGAAGGATTATGTCAATACTTTGGAACACGCGGTAAACAGCGGTCAATTAATCGCGGAAAAAGAGTTTTATTCCAACGTTCGTTTACGTGGCGCGAAGCACGCCCGCGAGCTGCTGCAAAACGGCATTCAATATTTGGAATTTCGTCTGTTCGATTTGAATCCGTTCGAGCCTTATGGTATTGCGCTAAACGATGCGAAATTCGTTCACTATTTTATTTTGCTTATGGCGTGGTTGGACGAAGAATCCACCGAAAGTGCGGTGGATTTAGGCAAAGAAAAATTAGCGCAGGTGGCATGGGAAAATCCGTTGTCGCCGACCGCCTTTCAATCGGAAGGGGAGCGTGTGTTACAGCAATTGTTAGCCATGTTGACGGAAATTCACACCGGCGCGGAAATCACGACGATCGTAAAAGAGAAATTGGCGCAATTTGCGGACCCGACACTTACCCTCGGCGCGCGTTTGGTCAATGCCATTGAGCAACATGGCGGTTATCAAAAATTGGGCGCGGAACTGGCGATTCGTTACAAACAGCAGGCATTTGAGCGTTTTTATGCCTTGTCCGCTTTTGATAATATGGAGCTTTCCACTCAAGCTCTGATGTTCGATGCGATTCAAAAAGGGCTGAAAATTGAAATTCTGGATGAGCGGGATCAATTCCTCAGCCTGCAATTCGGCGATCATTTGGAATATGTGAAAAACGGCAACATGACTTCCCACGACAGCTACATTTCGCCACTGATCATGGAAAATAAAGTGGTGACCAAAAAAGTGTTGGCGAAAGCCGGGTTTAACGTGCCGCAAAGTGTAGAATTCACCAGTGTGGAACAGGCGGTTGCCAATTACGCCTTATTTGCCGGTCGTGCCGTGGTGATTAAACCGAAATCCACCAATTACGGCTTAGGTATCAGCATTTTCCAACAAGGTGTACATGATCGGGAAGATTTTGCCAAAGCCATTGAAATCGCTTTTCGTGAAGATAAAGAAGTGATGGTGGAAGATTATTTAACCGGCACCGAATACCGTTTCTTTGTGCTGGGCGATGAAACCCTGGCGGTGTTATTGCGCGTGCCGGCGAATGTTATCGGCGACGGCGTGCATACGGTGGCGGAATTGGTGGCGCAGAAAAACGATCATCCGTTGCGTGGCGACGGTAGCCGTACGCCGTTGAAGAAAATCGCTTTGGGCGATATTGAGCGGTTACAGTTGAAAGAACAGGGTTTGGCGGTGGACAGTGTGCCGGTAAAAGATCAGCTGGTGCAGTTACGCGCCAATTCCAATATCAGCACCGGCGGCGATTCCATCGATATGACAGATCAAATGCACCCAAGCTATAAGGAACTCGCGGTGGGCATTACCAAAGCCATGGGCGCGGCAGTGTGCGGCGTGGATTTAATTATTCCTGATTTAACCAAACCCGCCGAACCGAACTTACAATCCTGGGGTGTGATTGAAGCCAATTTCAACCCGATGATGATGATGCACATTTTCCCTTACGCCGGACAATCCCGCAGAGTGACACAAAACGTGTTGAAGATGTTATTTCCTGAGTTGAAG","","","85243","MKIQQVIKENRLELLFQQGSFGIEKESQRVYADGSVVVSAHPKCFGSRSYHPYIQTDFAESQLELITPPNKKIEDTLRWLSAIHEVVLRTMLQDEYVFPLSMPAGLPPEEQIKVAQLENPADVAYREHLVQSYGKSKQMVSGVHYNFQLDPALIRQLFNGQNEYQSAVDFQNDLYLKVARNFLRYQWILVYLLAATPTVDANYFRGGTPLKPGQYVRSLRSSQYGYVNDPSVKISYDSLKDYVNTLEHAVNSGQLIAEKEFYSNVRLRGAKHARELLQNGIQYLEFRLFDLNPFEPYGIALNDAKFVHYFILLMAWLDEESTESAVDLGKEKLAQVAWENPLSPTAFQSEGERVLQQLLAMLTEIHTGAEITTIVKEKLAQFADPTLTLGARLVNAIEQHGGYQKLGAELAIRYKQQAFERFYALSAFDNMELSTQALMFDAIQKGLKIEILDERDQFLSLQFGDHLEYVKNGNMTSHDSYISPLIMENKVVTKKVLAKAGFNVPQSVEFTSVEQAVANYALFAGRAVVIKPKSTNYGLGISIFQQGVHDREDFAKAIEIAFREDKEVMVEDYLTGTEYRFFVLGDETLAVLLRVPANVIGDGVHTVAELVAQKNDHPLRGDGSRTPLKKIALGDIERLQLKEQGLAVDSVPVKDQLVQLRANSNISTGGDSIDMTDQMHPSYKELAVGITKAMGAAVCGVDLIIPDLTKPAEPNLQSWGVIEANFNPMMMMHIFPYAGQSRRVTQNVLKMLFPELK","84167","There is one significant hit to gi|20517793 UDP-N-acetylmuramyl tripeptide synthase [Thermoanaerobacter tengcongensis]: residues 416 to 755 are 35% similar to this protein. There are many very weak hits to D-alanine-D-alanine ligase A: expect values range from 2e-04 to 7.1. ","glutamate--cysteine ligase (gamma-glutamylcysteine synthetase) (gamma-ECS)","Cytoplasm","","
InterPro
IPR000115
Domain
Phosphoribosylglycinamide synthetase
PF01071\"[489-638]TGARS_A
InterPro
IPR006335
Family
Glutamate--cysteine ligase related
TIGR01435\"[12-753]Tglu_cys_lig_rel: putative glutamate--cystei
InterPro
IPR007370
Domain
Glutamate--cysteine ligase
PF04262\"[1-337]TGlu_cys_ligase
InterPro
IPR011761
Domain
ATP-grasp fold
PS50975\"[494-753]TATP_GRASP
InterPro
IPR013816
Domain
ATP-grasp fold, subdomain 2
G3DSA:3.30.470.20\"[550-606]Tno description
noIPR
unintegrated
unintegrated
PTHR23135\"[404-662]TMUR LIGASE FAMILY MEMBER
PTHR23135:SF1\"[404-662]TUDP-N-ACETYLMURAMOYLALANYL-D-GLUTAMYL-2,6-DIAMINOPIMELATE--D-ALANYL- D-ALANYL LIGASE


","BeTs to 3 clades of COG2918COG name: Gamma-glutamylcysteine synthetaseFunctional Class: HThe phylogenetic pattern of COG2918 is --------------efgh--------Number of proteins in this genome belonging to this COG is","","Residues 428 to 484 match (1e-21) PD:PD399226 which is described as PROTEOME COMPLETE LIGASE PROBABLE LIN2913 PM1048 ATP-GRASP UNCHARACTERIZED LMO2770 GLUTAMATE-CYSTEINE ","","","","","Wed Feb 19 16:27:45 2003","","","","Wed Feb 19 16:27:45 2003","","Wed Dec 11 10:48:14 2002","Thu Dec 12 17:50:35 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00115 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 337 (E-value = 8.1e-158) place AA00115 in the Glu_cys_ligase family which is described as Glutamate-cysteine ligase (PF04262)","","","","","","","","1","","","" "AA00116","86669","88267","1599","ATGTTTCAATCAAAAAAATTCTCTTTTCTTTACAATGATATATCCTTCTTTCTATTGTTACTGTTATTCGCCTTTCTGTCACATATTGCCCTAGGCATTTTAGATAATTATGCCAATCACATTCTGAGCATTTTGGGCTTGGGCATCCTGCTTTTCACGTTCAAAAAGCACAGCAACCGCTTATTTCTGGTCGCTTTTGTTTTTATTTTTGCCATTTCCTTCGGCTATGTGCCGTCAGGCATATTATACGGGCCGGTCTCCATCGGCGTGATTGCCTCCGTTTATGAAACGAATTTCAGCGAAACTTTGGGCTTTTTTCGCGCCATGCCCATTTCAATTTATTTTTTCACCGCACTTTATGTCGTTTTATTCATCGCATTATTGGTGATTAATCGCCATATCCATAGCAATAAAAAATATCAACCGGCTTACTATTGCCTTTATTTAGCCGCCGTTGTTCTGAGTTTATATACTCCCGTCAATAAACTCATCAACCACACGGATAAAACACAACCCTTTACCACCGCCGAATTTATTAAAGCGTCGGATTTTTACCCGGTCAGTTTTATTTCCAACGCGGTGAAGGTGAACAACACCTATTTAACCCAACGCGATTTATTAAATGACGCCCTAACCAAAACCCCGGAATGGGATATTGTTTACGTCGAACCGAAATACCAAAATTACGTGTTAATTATCGGGGAGAGTATGCGACGGGATTACACCTCGTTATACGGTTATCCGCAAAAAACCACGCCGTTTTTAGAGCAAGTGAACGGCTTGATTTTTAATCTGTATGTGGCGGCGGGCCCGAACACTCAGCCTTCTTTACAACGCACTCTTTATCGTTCCACCAACAATAATGAAGAAACGGTTTACACCGACAACATCATCTCCCTCGCCAAATTGGCGCACTACAAAACCTACTGGCTGTCCAACCAAGGCAAAGTGGGCGAATGGGACACCATGGCATCGCGCATCGGCATTCAAGCGGACGAATCCTTTTTCACCAAAAAAGGCGGCTACGATTCGGGCAATACGCCGGACACGGCATTATTGGAACCATTAAAACAGCTATTAAATAAAGACAAAGATCAAACCAAATTAATCGTGTTGCATTTAATCGGCTCCCACCCGACATTTTGCGCCCACTTAAATGGCGAAGAACCGAAATTCCATTTAGTCAGCCGTGAAATGTCCTGTTATTTGGATACCTTAAAACAAACGGATACCTTATTGTCGGAAATTAATCAGATTCTGAAAGCGCAAAATCAAAGTTATTCGGTAATTTATTTTTCCGATCACGGCTTGGCGCATTTGGGCGAAGGCAAAAATCTGTCCATGTTAAACAATAAAGAATACAAACAAAGTTATGCCGTGCCCTTTATTCGTTTTTCCAGCGACGATACCAAAAGAACCGTCATTAAAAACCCGCAAAGCGCCTTTAATTTTATTAACGGCTTTGCCCAATGGCTCGGCATCAAAGAAACCCATTTGAGCCAGGACGATTTTTTCAATCCGAAACCGCAACCGATTAAAGTGTTTAACTGGCGGGCGCTGGTGGATTACAACTCGCTGAAGGAAGATCCGGCGAAAAAA","","","61466","MFQSKKFSFLYNDISFFLLLLLFAFLSHIALGILDNYANHILSILGLGILLFTFKKHSNRLFLVAFVFIFAISFGYVPSGILYGPVSIGVIASVYETNFSETLGFFRAMPISIYFFTALYVVLFIALLVINRHIHSNKKYQPAYYCLYLAAVVLSLYTPVNKLINHTDKTQPFTTAEFIKASDFYPVSFISNAVKVNNTYLTQRDLLNDALTKTPEWDIVYVEPKYQNYVLIIGESMRRDYTSLYGYPQKTTPFLEQVNGLIFNLYVAAGPNTQPSLQRTLYRSTNNNEETVYTDNIISLAKLAHYKTYWLSNQGKVGEWDTMASRIGIQADESFFTKKGGYDSGNTPDTALLEPLKQLLNKDKDQTKLIVLHLIGSHPTFCAHLNGEEPKFHLVSREMSCYLDTLKQTDTLLSEINQILKAQNQSYSVIYFSDHGLAHLGEGKNLSMLNNKEYKQSYAVPFIRFSSDDTKRTVIKNPQSAFNFINGFAQWLGIKETHLSQDDFFNPKPQPIKVFNWRALVDYNSLKEDPAKK","88267","","conserved hypothetical protein","Outer membrane, Inner membrane, Cytoplasm","","
InterPro
IPR000917
Domain
Sulfatase
PF00884\"[225-509]TSulfatase
InterPro
IPR001952
Family
Alkaline phosphatase
G3DSA:3.40.720.10\"[225-498]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-32]?signal-peptide
tmhmm\"[10-30]?\"[36-54]?\"[63-83]?\"[110-130]?\"[140-160]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 5.7e-27) to 3/3 blocks of the IPB003371 family, which is described as \"Integral membrane protein of unknown function\". Interpro entry for IP:IPR003371. IPB003371A 230-253 1.7e-13 IPB003371B 296-310 0.0024 IPB003371C 349-378 6.3e-07","","","","","","","","","","","","","Mon Dec 2 11:35:30 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00116 is paralogously related to AA01596 (1e-93).","","","","","","Residues 225 to 518 (E-value = 3.9e-66) place AA00116 in the Sulfatase family which is described as Sulfatase (PF00884)","","","","","","","","1","","","" "AA00117","88478","88386","93","GTGCGGTCAGAAAAAACGGTGTTTTTGGTGCCGGGTAAGCCGACGATGCCGCAGAGGCGAATTCACTTCGCAAAAAACGGCGGCTATTTTACC","","","3545","VRSEKTVFLVPGKPTMPQRRIHFAKNGGYFT","88386","","hypothetical protein","Periplasm, Cytoplasm","No similarities were found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sat Feb 21 11:07:02 2004","Sat Feb 21 11:07:02 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00117 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sat Feb 21 11:07:45 2004","","","","","","","","","","","","","1","","","" "AA00119","88527","89090","564","ATGGTCGTTGACCAAACCTCCCGCGGTGAACGCGCCTATGACATTTATTCCCGCCTGCTGAAAGACCGCGTGATTTTTCTCAGCGGCGAAGTGGAAGACAACATGGCAAACCTGATTGTGGCGCAACTGCTTTTCTTAGAATCGGAAGATCCCGATAAAGACATCAACCTATACATCAACTCCCCGGGCGGCTCCGTCACTGCCGGCATGGCGATTTACGACACCATGCAATTTATTAAACCGGATGTTCGCACCCTGTGTATCGGTCAAGCCTGTTCCATGGGTGCATTTTTATTAGCCGGCGGCGCAGCGGGCAAACGCGGCGCATTACCGCATGCCCGCGTGATGATTCATCAACCACTCGGCGGTTTCCGTGGTCAGGCATCGGATATTCAGATTCACGCGCAAGAAATTCTGAAAATCAAAAGCACTCTTAACGAACGCCTGGCGTTCCACACCGGACAACCCATTGAAACCATCGAAAAAGATACCGACCGCGACAATTTTATGTCGGCGCAGGAAGCCAAAAATTACGGCTTAATTGACGAAGTGTTCAGCAAACGC","","","21291","MVVDQTSRGERAYDIYSRLLKDRVIFLSGEVEDNMANLIVAQLLFLESEDPDKDINLYINSPGGSVTAGMAIYDTMQFIKPDVRTLCIGQACSMGAFLLAGGAAGKRGALPHARVMIHQPLGGFRGQASDIQIHAQEILKIKSTLNERLAFHTGQPIETIEKDTDRDNFMSAQEAKNYGLIDEVFSKR","89090","","ATP-dependent Clp protease proteolytic subunit (endopeptidase Clp)","Cytoplasm","","
InterPro
IPR001907
Family
Peptidase S14, ClpP
PR00127\"[14-29]T\"[54-74]T\"[85-102]T\"[106-125]T\"[163-182]TCLPPROTEASEP
PTHR10381\"[51-184]TPROTEASE FAMILY S14 CLPP PROTEASE
PF00574\"[7-188]TCLP_protease
TIGR00493\"[1-187]TclpP: ATP-dependent Clp protease, proteolyt
PS00381\"[85-96]TCLP_PROTEASE_SER
PS00382\"[107-120]TCLP_PROTEASE_HIS
noIPR
unintegrated
unintegrated
G3DSA:3.90.226.10\"[1-188]Tno description


","BeTs to 17 clades of COG0740COG name: Protease subunit of ATP-dependent Clp proteasesFunctional Class: N,OThe phylogenetic pattern of COG0740 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 3e-113) to 4/4 blocks of the IPB001907 family, which is described as \"Clp protease\". Interpro entry for IP:IPR001907. IPB001907A -1-23 2e-06 IPB001907B 39-84 4.3e-42 IPB001907C 85-123 7.6e-31 IPB001907D 141-184 1.6e-30","Residues 7 to 188 match (3e-81) PD:PD001650 which is described as PROTEASE CLP ATP-DEPENDENT PROTEOLYTIC SUBUNIT ENDOPEPTIDASE HYDROLASE SERINE PROTEOME COMPLETE ","","","","","","","","","","","","Mon Dec 2 11:43:37 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00119 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 188 (E-value = 9.7e-138) place AA00119 in the CLP_protease family which is described as Clp protease (PF00574)","","","","","Kroh,H.E. and Simon,L.D. The ClpP component of Clp protease is the sigma 32-dependentheat shock protein F21.5 J. Bacteriol. 172 (10), 6026-6034 (1990) PubMed: 2211522 Arribas,J. and Castano,J.G. A comparative study of the chymotrypsin-like activity of therat liver multicatalytic proteinase and the ClpP from Escherichiacoli J. Biol. Chem. 268 (28), 21165-21171 (1993) PubMed: 8407953 Shin,D.H., Lee,C.S., Chung,C.H. and Suh,S.W. Molecular symmetry of the ClpP component of the ATP-dependentClp protease, an Escherichia coli homolog of 20 S proteasome J. Mol. Biol. 262 (2), 71-76 (1996) PubMed: 8831780 Wang,J., Hartling,J.A. and Flanagan,J.M. The structure of ClpP at 2.3 A resolution suggests a modelfor ATP-dependent proteolysis Cell 91 (4), 447-456 (1997) PubMed: 9390554 Maurizi,M.R., Clark,W.P., Katayama,Y., Rudikoff,S.,Pumphrey,J., Bowers,B. and Gottesman,S. Sequence and structure of Clp P, the proteolytic component ofthe ATP-dependent Clp protease of Escherichia coli J. Biol. Chem. 265 (21), 12536-12545 (1990) PubMed: 2197275 ","","Wed Jan 29 10:00:03 2003","1","","","" "AA00120","89103","90341","1239","ATGGCAAAAGATAAAGAATTACACTGTTCTTTCTGCGGCAAAGAACAAGACGAAGTGAATAAACTTATCGCCGGCACTTCCGGTTACATTTGTAACGAATGTATCGAACTGTGCCACGATATGCTGCTCAACGAAGAACATGGCGAAGAAGCGGAAGCTGAAAGCGCAAAAGAGCAACAGGAATTACCGACGCCCCACCAAATCCGAGCCCATTTGGACGATTATGTCATCGGTCAGGATTATGCCCAAAAAGTGCTGGCGGTGGCGGTGTATAACCACTACAAACGCCTACGCACCAAACATCAGACGAACGATGTGGAACTCGGTAAAAGCAACATTTTGCTTATCGGCCCGACCGGTAGCGGCAAAACCTTATTGGCAGAAACCATGGCGCGTATGTTGAACGTGCCTTTCGCCATGGCGGACGCCACTACCTTAACGGAAGCCGGTTATGTAGGTGAAGACGTGGAAAACGTGTTGCAGAAATTGCTACAAAACTGCGATTACGACATTGAACGCGCGGAACAAGGCATTATCTACATCGACGAAATCGACAAAATCACCCGCAAATCGGAAAATCCGTCCATTACCCGTGATGTCTCCGGCGAAGGCGTACAACAAGCCTTATTAAAACTCATCGAAGGCACCATCGCCTCCATTCCGCCACAAGGCGGACGCAAACACCCGCAACAGGAAATGTTACGCATCGACACCTCCAAAATCCTATTCATTTGCGGCGGTGCGTTTGCGGGCTTGGATAAAGTCATCGAAAAACGCACCAGCGTCGCCACCGCCATCGGTTTCGGCGCCGAAATCAAGAGCGAAAAAGACAAAGCGACACTGACCGACTTATTCAAACAGGTGGAACCGGACGATTTAATGAAATACGGCTTAATCCCGGAATTTATCGGACGTTTGCCGGTGGTGGCGCCATTAAGCGAATTGGACGAAGAAGCCTTGGTACGTATTCTCACCGAACCGAAAAATGCCCTGTGCAAGCAATATCAGGCATTGTTCGGTTTAGAAGAGGTGGCATTGGAATTCACCAACGAAGCCCTAACCGCAATGGCGAAAAAAGCCCTTGCCCGCAAAACCGGCGCCCGCGGCTTACGTTCCATCATCGAAGGCGTCTTGCTTGACACCATGTACGACTTGCCATCCTTGGAAGGCTTGAAAAAAGTCGTGGTCAACGAAAACGTCATCAACGACAACCAATCCCCGGAATTGATTTATTCCAAC","","","45636","MAKDKELHCSFCGKEQDEVNKLIAGTSGYICNECIELCHDMLLNEEHGEEAEAESAKEQQELPTPHQIRAHLDDYVIGQDYAQKVLAVAVYNHYKRLRTKHQTNDVELGKSNILLIGPTGSGKTLLAETMARMLNVPFAMADATTLTEAGYVGEDVENVLQKLLQNCDYDIERAEQGIIYIDEIDKITRKSENPSITRDVSGEGVQQALLKLIEGTIASIPPQGGRKHPQQEMLRIDTSKILFICGGAFAGLDKVIEKRTSVATAIGFGAEIKSEKDKATLTDLFKQVEPDDLMKYGLIPEFIGRLPVVAPLSELDEEALVRILTEPKNALCKQYQALFGLEEVALEFTNEALTAMAKKALARKTGARGLRSIIEGVLLDTMYDLPSLEGLKKVVVNENVINDNQSPELIYSN","90341","There are some weaker hits to ATP-dependent hsl protease ATP-binding subunit hslU. Residues 64-410 are 28% similar to Hslu protein from Rickettsia prowazekii (gi11133244). However, these hits are very few and weak in comparison to the ClpX hits. ","ATP-dependent Clp protease ATP-binding subunit","Cytoplasm","","
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[109-248]TAAA
InterPro
IPR004487
Family
ClpX, ATPase regulatory subunit
PTHR11262:SF4\"[3-410]TATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX
TIGR00382\"[1-410]TclpX: ATP-dependent Clp protease, ATP-bindi
InterPro
IPR010603
Domain
Zinc finger, C4-type
PF06689\"[6-45]Tzf-C4_ClpX
InterPro
IPR013093
Domain
ATPase AAA-2
PF07724\"[108-309]TAAA_2
InterPro
IPR013237
Domain
Phage P4 alpha, zinc-binding
SM00778\"[4-42]Tno description
noIPR
unintegrated
unintegrated
G3DSA:1.10.8.60\"[314-413]Tno description
G3DSA:3.40.50.300\"[54-313]Tno description
PTHR11262\"[3-410]THSL AND CLP PROTEASE


","No hits to the COGs database.","Significant hit ( 5.2e-07) to 3/8 blocks of the IPB001270 family, which is described as \"Chaperonins clpA/B\". Interpro entry for IP:IPR001270. IPB001270E 89-143 0.0028 IPB001270G 298-312 2.5 IPB001270H 360-374 21Significant hit ( 2.4e-05) to 1/5 blocks of the IPB000623 family, which is described as \"Shikimate kinase\". Interpro entry for IP:IPR000623. IPB000623A 113-142 2.4e-05","Residues 76 to 112 match (5e-07) PD:PD189825 which is described as ATP-BINDING PROTEASE SUBUNIT CLP ATP-DEPENDENT CLPX PROTEOME COMPLETE CHAPERONE ZINC-FINGER ","","","","","","","","","","","Tue Mar 9 14:14:53 2004","Mon Dec 2 11:54:57 2002","","Tue Mar 9 14:14:53 2004","Tue Mar 9 14:14:53 2004","Tue Mar 9 14:14:53 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00120 is paralogously related to AA00460 (4e-19) and AA02289 (1e-06).","Tue Mar 9 14:14:53 2004","","","","","Residues 112 to 371 (E-value = 7.3e-26) place AA00120 in the AAA family which is described as ATPase family associated with various cellular activities (AAA) (PF00004)","Tue Mar 9 14:14:53 2004","","","","Gottesman S, Clark WP, de Crecy-Lagard V, Maurizi MR.ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities.J Biol Chem. 1993 Oct;268(30):22618-26.PMID: 8226770Wawrzynow A, Wojtkowiak D, Marszalek J, Banecki B, Jonsen M, Graves B, Georgopoulos C, Zylicz M.The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone.EMBO J. 1995 May;14(9):1867-77.PMID: 7743994","","Tue Mar 9 14:14:53 2004","1","","","" "AA00122","90352","90441","90","GTGCGGTTAAAAAACACAATGGATTTTAACCGCACTTTTTCTTACGTAAAACGCTTTATACCAGCTGTAGCTGCACCATTCGTCCTGTTT","","","3531","VRLKNTMDFNRTFSYVKRFIPAVAAPFVLF","90441","","hypothetical protein","Cytoplasm","No similarities were found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sat Feb 21 11:09:21 2004","Sat Feb 21 11:09:21 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00122 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sat Feb 21 11:10:12 2004","","","","","","","","","","","","","1","","","" "AA00123","90450","90361","90","TTGTTGCTAAAACAGGACGAATGGTGCAGCTACAGCTGGTATAAAGCGTTTTACGTAAGAAAAAGTGCGGTTAAAATCCATTGTGTTTTT","","","3694","LLLKQDEWCSYSWYKAFYVRKSAVKIHCVF","90361","","hypothetical protein","Cytoplasm","No similarities were found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sat Feb 21 11:11:03 2004","Sat Feb 21 11:11:03 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00123 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sat Feb 21 11:11:54 2004","","","","","","","","","","","","","1","","","" "AA00124","90730","90410","321","ATGAATAATATTGATACAAAAATTCGCCACACAACAAAAGGCGATGGTAATGTGTTTGCTGATTTAGGTTTTTCTCAACAGGAAGCGGAGAGATTAAAATCGGCAAGTCAGCAATTAATTGAGAACAAACTTCTTTTACTTAATGTGATGAGTGATTGGATTGCCGATAATAACCTTAAACAAGCGGAAGCAGCTGCCATTTTGGGAGTGAGTCGTCCGCGAGTTTCCGATATGGTGAACAAAAAATTAGAGAAATTTACGTTGGATACCTTGGTGTCTTTTGTTGCTAAAACAGGACGAATGGTGCAGCTACAGCTGGTA","","","11914","MNNIDTKIRHTTKGDGNVFADLGFSQQEAERLKSASQQLIENKLLLLNVMSDWIADNNLKQAEAAAILGVSRPRVSDMVNKKLEKFTLDTLVSFVAKTGRMVQLQLV","90410","The significant alignments in the COGS expect values ranging from 0.022 to 7.7.","conserved hypothetical protein (possible cytoplasmic protein)","Cytoplasm","","No hits reported.","No hits to the COGs database.","","Residues 25 to 106 match (5e-10) PD:PD281317 which is described as COMPLETE PROTEOME CYTOPLASMIC STY3650 STMD1.83 XF1677 Z3231 ","","","","","","","","","","","Wed Dec 11 10:59:39 2002","Wed Dec 11 10:59:39 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00124 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00125","91073","90726","348","ATGAGTAGGCAACAAATAGAAAGGAAACCAATTCATTGGATTGGCTCTAGCTTAGAGGATGTTAAGGCGTTTCCGGATAATATAAAACGGGAATTAGGTTTCGATCTTGACCTCGTACAACAGGGGTTATCGCCTCGGGATTTTAAGGCAATGCAGAACCTGGGTTCCGGTGTAATGGAAATTCGAGTGAGGGATATTTCAGGGGCATATCGTTTGGTTTACATTGCCAAATTAAAGAAAGCGATTTATTGTTTGCATGCCTTTCAAAAGAAAACACAAAAAACATCTTCACAAGATCTTGCCGTAATTAAAGCGCGTTATGCTGCGTTAAAGGAGTTAGACGATGAA","","","13266","MSRQQIERKPIHWIGSSLEDVKAFPDNIKRELGFDLDLVQQGLSPRDFKAMQNLGSGVMEIRVRDISGAYRLVYIAKLKKAIYCLHAFQKKTQKTSSQDLAVIKARYAALKELDDE","90726","","conserved hypothetical protein (possible phage-related protein)","Cytoplasm, Periplasm","","
InterPro
IPR009241
Family
Protein of unknown function DUF891
PF05973\"[55-110]TGp49


","No hits to the COGs database.","","Residues 17 to 110 match (1e-22) PD:PD068960 which is described as PROTEOME COMPLETE PHAGE GP49 ALL1034 Z3230 ","","","","","","","","","","","","Wed Dec 11 11:02:57 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00125 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00126","92035","91193","843","ATGTTGAATAAAATCGATTTATGGCTCATGAATCATCAGCCCGATCCTCAGTTGAAAGGAATCAAACGATTTTTTGTCGAATTCTGGTTTTTCGGTTTAAAAGAAGCCAGAGCCTGCCTGTTTGCCGGCGTGTTTTTTATCGCCATGTTTATTATGCCGAAAAACGGCATCGCCGGCATTCCACGCTATGATTTATTGCTGATTTTTGCTTTAGTCGTGCAATATTTGATGTTTCGATTCAAACTGGAAACACGCGATGAAATCAAATCCATCACCCTGTTTCACTTGGTGGGTTTTGCGTTGGAATTGTTTAAAACCTCCTCTTCCATTCAATCCTGGGCGTATCCCGATTTCGCTTACAGCAAAATCTTCGGCGTGCCTTTATTCACCGGGTTTATGTATGCCGCGGTGGGCAGTTATATTATTCAGGCGTGGCGTTTATTCGGGTTGAAAATTCAAAGCCACCCGCCGTATTTTTTATCTACGCTCACCGCCATTCTGATTTACCTGAATTTTTTCACCCATCATTATATCGGCGATTACCGCTGGTATCTGGCGGCTTTCGCACTTGGGCTTTACGCCCGCACCACGGTCTATTTCACGCCTTACGACAAACCGCGTCGCATGCCGTTATTGCTATCCTTCATGTTGATTGGTTTCTTCATTTGGCTGGCGGAAAATATCGGCACGCTTATCGGCATTTGGCGTTACCCCAATCAAATCGGCGCGTGGTCGTTAGTGCATGCCAGCAAGTGGAGTGCCTGGGCGTTGTTGGTGGTAATGACATTCACCATCGTGGCGAACCTCAAACACATTAAACAAACGATTCGGGTGTCGAGGGAT","","","32822","MLNKIDLWLMNHQPDPQLKGIKRFFVEFWFFGLKEARACLFAGVFFIAMFIMPKNGIAGIPRYDLLLIFALVVQYLMFRFKLETRDEIKSITLFHLVGFALELFKTSSSIQSWAYPDFAYSKIFGVPLFTGFMYAAVGSYIIQAWRLFGLKIQSHPPYFLSTLTAILIYLNFFTHHYIGDYRWYLAAFALGLYARTTVYFTPYDKPRRMPLLLSFMLIGFFIWLAENIGTLIGIWRYPNQIGAWSLVHASKWSAWALLVVMTFTIVANLKHIKQTIRVSRD","91193","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR008535
Family
Protein of unknown function DUF817
PIRSF009141\"[22-281]TPredicted membrane protein
PF05675\"[25-263]TDUF817
noIPR
unintegrated
unintegrated
tmhmm\"[28-50]?\"[60-78]?\"[93-113]?\"[123-145]?\"[155-173]?\"[183-203]?\"[213-233]?\"[252-272]?transmembrane_regions


","No hits to the COGs database.","","Residues 171 to 209 match (5e-12) PD:PD488923 which is described as PROTEOME COMPLETE ATU1921 PM1172 ","","","","","","","","","","","","Mon Dec 2 12:02:42 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00126 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 25 to 263 (E-value = 1e-174) place AA00126 in the DUF817 family which is described as Protein of unknown function (DUF817) (PF05675)","","","","","","","","1","","","" "AA00128","94267","92111","2157","ATGCAAAAAGTATCTCTTCAAATTGGCGGAATGACGTGTCAGTCTTGCGCCAGCCGTATTGAAAAAGTATTGAATAAAAAGGATTTTGTGCAGCAGGCAGGCGTGAATTTTGCCAGCGAAGAGGCGCAGGTGACTTTCGATGAAAAGCAAACTTCCGTTGAGCAACTTATCCAAATTGTTCAAAAAACCGGTTTCAGCGCGCAGTTAAAACCGGCGCAGGCGGATTTGCCGCAAGAGCATAAAATCTCTTGGCGTTTGATTTTATTATGGCTGATTAATGTGCCGTTTTTAATCGGTATGCTGGGCATGATGATCGGGCGCCATGATTGGATGTCGCCGCCTCTATGGCAAATGGTGCTCGCCACGATTGTGCAATTTGGCTTGGCAATCCCTTTTTATCGCAGTGCTTGGGGCAGTATTAAAGGCGGTTTGGCGAATATGGACGTGTTGGTCAGCCTCGGCACGCTCACCATCTATTTTTATTCGGTATTTATGCTGTTTTATGCGCCGCATATAGGGCATGAACACGGCTCGGCAAATATTTATTTTGAAGCTGCCGTGATGGTGTTGGGCTTTGTGAGTTTAGGAAAATTACTGGAAGACCGTACTAAAAAGCACAGCTTGAATAGCCTCGGTTTGTTGTTGCAACTGACACCGAAACAAGTAAGCGTACAACGTAACGGGCAATGGCAAACCGTGCCGTTGAATCAGATCCAAGTGGGCGAGCTGTTACGCGCCAATCAGGGCGAGCGCATTGCGGCGGACGGTTTGGTAGAAGACGGTTCGGGCTGGTGTGATGAAAGCCATTTAACCGGTGAATCCGTTCCTGAAATGAAGAAGCTGGGCAGCAAAGTGTTGGCGGGCGCGATGGTGGCGGATGGTAGTCTGGTTTATCGCACGCAACAACTGGGTAGCCAAACCCTGCTGGGCGACATGATGAACGCTTTGTCGGAAGCGCAGGGCAGTAAAGCGCCTATCGCCCGTTTTGCCGATAAAGTGGCGGCGGTGTTCGTGCCGACGGTGATTGGCATTGCGTTAGTGACTTTTTTGCTCACATGGTGGATTCGGCAAGATGTGGTCATGGCGTTAATTCACGGCGTTGCCGTGTTGGTGATTGCCTGTCCTTGCGCGTTGGGTTTGGCAACGCCGGCGGCGATTATGGTCGGCATGGGCAAAGCGGTGAAACAGGGTATTTGGTTTAAAGATGCCGCCGCGATGGAGGAATCCGCCCATGTGAATGCTGTGGTGTTGGACAAAACCGGCACGCTAACGGAAGGCAAACCACAAGTGGTGGCGTTTTGGCAGGCAAAAAGTGCGGTCAATTCCGAAGATGAAATTTATGCGTTGGTAGCAGCCATTGAACAAAACGCCACGCACCCGTTAGCGAAAGCGATTGTGCAGGCGGCGATGGCGAAAAATGTCGTTTTGCCTGCCGTGCAACATATTCAAACAGACGTCGGACAGGGCATTCAAGGTGAAGTGGAAAATGTCGGCACGGTGAAAGTGGGTAAGCCTTCATATTGTGGTTTAACGCTGCCGGAGGGGCTTGATCCTGTATGGAATATTGCCAGTATTGTGGCGGTTACGCTGAATGACGAGCCTATCGCCGCCTTTGCTTTGGCGGACGCCTTAAAACCGGACAGTCAAAAAGCGATTAACCGTTTGCAGGCGCACGATATTGAGGTGTATATCATGAGTGGCGATAATCCCAATGTGGTGCAATACATCGCCGATCAACTGGGCATTAAAAACGCGCAGGGCAATATGTCGCCAAGAGATAAAGCGGGCGCGGTTAAAGCGCTGCAAGAGCAGGGCAAAGTGGTCGCCATGGCAGGCGATGGCGTGAACGACGCACCGGCATTGACGGCGGCGAATGTCAGTTTTGCTATGCGTGACGGTGCCGATGTGGCGCAACACAGCGCTTCGGCAACCTTAATGCAACATTCGGTGAATCAATTAGTGGATGCCTTGCTGATTTCTCGCGCGACCCTGAAAAACATTAAGCAAAATCTCTTTTTCGCCTTTATTTATAATGTGTTGGGGATTCCGCTGGCGGCGTTCGGGTTACTTAGCCCGGTAATTGCGGGGGCGGCGATGGCGCTAAGTTCCATTTCCGTGTTAAGCAATGCGTTACGTTTGAAAAAAGTGAAAATTGAA","","","77033","MQKVSLQIGGMTCQSCASRIEKVLNKKDFVQQAGVNFASEEAQVTFDEKQTSVEQLIQIVQKTGFSAQLKPAQADLPQEHKISWRLILLWLINVPFLIGMLGMMIGRHDWMSPPLWQMVLATIVQFGLAIPFYRSAWGSIKGGLANMDVLVSLGTLTIYFYSVFMLFYAPHIGHEHGSANIYFEAAVMVLGFVSLGKLLEDRTKKHSLNSLGLLLQLTPKQVSVQRNGQWQTVPLNQIQVGELLRANQGERIAADGLVEDGSGWCDESHLTGESVPEMKKLGSKVLAGAMVADGSLVYRTQQLGSQTLLGDMMNALSEAQGSKAPIARFADKVAAVFVPTVIGIALVTFLLTWWIRQDVVMALIHGVAVLVIACPCALGLATPAAIMVGMGKAVKQGIWFKDAAAMEESAHVNAVVLDKTGTLTEGKPQVVAFWQAKSAVNSEDEIYALVAAIEQNATHPLAKAIVQAAMAKNVVLPAVQHIQTDVGQGIQGEVENVGTVKVGKPSYCGLTLPEGLDPVWNIASIVAVTLNDEPIAAFALADALKPDSQKAINRLQAHDIEVYIMSGDNPNVVQYIADQLGIKNAQGNMSPRDKAGAVKALQEQGKVVAMAGDGVNDAPALTAANVSFAMRDGADVAQHSASATLMQHSVNQLVDALLISRATLKNIKQNLFFAFIYNVLGIPLAAFGLLSPVIAGAAMALSSISVLSNALRLKKVKIE","92111","","cation-transporting ATPase (probable potassium/copper transporter)","Inner membrane, Cytoplasm","","
InterPro
IPR001756
Family
ATPase, P-type copper-transporter
PR00943\"[18-32]T\"[47-67]T\"[186-205]T\"[339-353]T\"[399-414]T\"[588-605]TCUATPASE
InterPro
IPR001757
Family
ATPase, P-type, K/Mg/Cd/Cu/Zn/Na/Ca/Na/H-transporter
PR00119\"[266-280]T\"[416-430]T\"[558-568]T\"[611-630]T\"[634-646]TCATATPASE
PTHR11939\"[1-719]TCATION-TRANSPORTING ATPASE
TIGR01494\"[188-434]T\"[526-699]TATPase_P-type: ATPase, P-type (transporting
PS00154\"[418-424]?ATPASE_E1_E2
InterPro
IPR005834
Domain
Haloacid dehalogenase-like hydrolase
PF00702\"[412-634]THydrolase
InterPro
IPR006121
Domain
Heavy metal transport/detoxification protein
PF00403\"[5-69]THMA
PS50846\"[3-69]THMA_2
PS01047\"[8-37]THMA_1
InterPro
IPR006403
Family
ATPase, P type cation/copper-transporter
TIGR01511\"[128-714]TATPase-IB1_Cu: copper-translocating P-type
InterPro
IPR006416
Family
Heavy metal translocating P-type ATPase
TIGR01525\"[147-713]TATPase-IB_hvy: heavy metal translocating P-
InterPro
IPR008250
Domain
E1-E2 ATPase-associated region
PF00122\"[188-408]TE1-E2_ATPase
noIPR
unintegrated
unintegrated
G3DSA:2.70.150.10\"[155-297]Tno description
G3DSA:3.30.70.100\"[3-79]Tno description
G3DSA:3.40.50.1000\"[531-655]Tno description
PTHR11939:SF39\"[1-719]TCOPPER-TRANSPORTING ATPASE P-TYPE (COPA)
tmhmm\"[87-107]?\"[113-133]?\"[148-168]?\"[178-196]?\"[333-355]?\"[369-389]?\"[667-687]?\"[693-711]?transmembrane_regions


","BeTs to 23 clades of COG2217COG name: Cation transport ATPasesFunctional Class: PThe phylogenetic pattern of COG2217 is aompkzyqvdrlbcefgh-nuj-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.8e-18) to 2/2 blocks of the IPB001757 family, which is described as \"E1-E2 ATPases\". Interpro entry for IP:IPR001757. IPB001757A 415-426 0.00039 IPB001757B 602-631 1e-12Significant hit ( 8.4e-15) to 2/2 blocks of the IPB001934 family, which is described as \"Heavy-metal-associated domain\". Interpro entry for IP:IPR001934. IPB001934A 8-30 5.5e-11 IPB001934B 414-424 0.04","Residues 443 to 495 match (5e-07) PD:PD037880 which is described as ATPASE PROTEOME COMPLETE HYDROLASE PHOSPHORYLATION TRANSMEMBRANE ATP-BINDING CATION-TRANSPORTING P-TYPE METAL-BINDING ","","","","","Wed Feb 19 16:28:41 2003","","","","Wed Feb 19 16:28:41 2003","","","Mon Dec 2 12:48:27 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00128 is paralogously related to AA00130 (1e-09).","","","","","","Residues 412 to 634 (E-value = 1e-26) place AA00128 in the Hydrolase family which is described as haloacid dehalogenase-like hydrolase (PF00702)","","","","","Sardesai AA, Gowrishankar J.Improvement in K+-limited growth rate associated with expression of the N-terminal fragment of one subunit (KdpA) of the multisubunit Kdp transporter in Escherichia coli.J Bacteriol. 2001 Jun;183(11):3515-20.PMID: 11344160 Gassel M, Altendorf K.Analysis of KdpC of the K(+)-transporting KdpFABC complex of Escherichia coli.Eur J Biochem. 2001 Mar;268(6):1772-81.PMID: 11248697","","Sun Feb 16 16:31:27 2003","1","","","" "AA00129","94262","94612","351","TTGCATAACATCCTCTTTTCTCGCAAAGTGCGGTCGTTTTTAAACATGTTTTTACAACGTATTGATGGCGTGCCTCGCACCCTCAATCAAACTTACGCCACCTGCGCATCGAATCCCGCGTCTTCCACCGCTTCAACCAATGCCGCAGGCTGCACTTTACTTTCATCAAAACTGATCACCGCCTGTGCTTTTTCCAAACTCACCTCCGCTTGTACCACGCCGTCCAGCTCGGTCAACACGCGGGTCACGCTTTTCACACAGCCGCCACAAGTCATTCCGTCGATTTTTAATGTTACGTTTTGCATAATTTGCTCCTTCAAGAATAAGTTAAACCTTGCCGATCTTTGTCGG","","","13375","LHNILFSRKVRSFLNMFLQRIDGVPRTLNQTYATCASNPASSTASTNAAGCTLLSSKLITACAFSKLTSACTTPSSSVNTRVTLFTQPPQVIPSIFNVTFCIICSFKNKLNLADLCR","94612","","hypothetical protein","Periplasm, Extracellular","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Dec 2 13:02:58 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00129 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00130","94581","94357","225","TTGAAGGAGCAAATTATGCAAAACGTAACATTAAAAATCGACGGAATGACTTGTGGCGGCTGTGTGAAAAGCGTGACCCGCGTGTTGACCGAGCTGGACGGCGTGGTACAAGCGGAGGTGAGTTTGGAAAAAGCACAGGCGGTGATCAGTTTTGATGAAAGTAAAGTGCAGCCTGCGGCATTGGTTGAAGCGGTGGAAGACGCGGGATTCGATGCGCAGGTGGCG","4.10","-6.11","7906","LKEQIMQNVTLKIDGMTCGGCVKSVTRVLTELDGVVQAEVSLEKAQAVISFDESKVQPAALVEAVEDAGFDAQVA","","","mercuric transport protein (periplasmic mercury ion binding protein) (mercury scavenger protein)","Cytoplasm, Periplasm","Many weak hits to mercuric transport protein periplasmic component precursor (periplasmic mercury ion binding protein) (mercury scavenger protein). Residues 7-74 are 41% similar to mercuric transport protein periplasmic component precursor from Acinetobacter calcoaceticus (249854).AA00130 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus ducreyi gene.AA00130 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus influenzae Rd gene.","
InterPro
IPR000428
Family
Copper ion binding protein
PR00944\"[8-20]T\"[20-33]T\"[33-46]T\"[59-72]TCUEXPORT
InterPro
IPR001757
Family
ATPase, P-type, K/Mg/Cd/Cu/Zn/Na/Ca/Na/H-transporter
PTHR11939\"[1-75]TCATION-TRANSPORTING ATPASE
InterPro
IPR001802
Family
Mercury scavenger protein
PR00946\"[5-16]T\"[16-32]T\"[32-47]T\"[47-61]T\"[61-75]THGSCAVENGER
InterPro
IPR001877
Family
Copper-transporting ATPase 1
PR00942\"[8-33]T\"[34-57]T\"[63-75]TCUATPASEI
InterPro
IPR006121
Domain
Heavy metal transport/detoxification protein
PF00403\"[10-74]THMA
PS50846\"[8-74]THMA_2
PS01047\"[13-42]THMA_1
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.100\"[5-74]Tno description
PTHR11939:SF32\"[1-75]TCOPPER-TRANSPORTING ATPASE P-TYPE


","No hits to the COGs database.","Significant hit ( 1.9e-12) to 2/2 blocks of the IPB001934 family, which is described as \"Heavy-metal-associated domain\". Interpro entry for IP:IPR001934. IPB001934A 13-35 1.1e-11 IPB001934B 62-72 59Significant hit ( 3.4e-12) to 5/6 blocks of the PR00946 family, which is described as \"Mercury scavenger protein signature\". Prints database entry for PR:PR00946. PR00946B 5-16 1.2 PR00946C 16-32 0.63 PR00946D 32-47 0.073 PR00946E 47-61 1.8 PR00946F 61-75 4.8","Residues 6 to 71 match (7e-14) PD:PD000309 which is described as COPPER ATPASE COMPLETE PROTEOME METAL-BINDING HYDROLASE TRANSMEMBRANE ATP-BINDING PHOSPHORYLATION COPPER-TRANSPORTING ","Fri Feb 27 08:28:48 2004","Sat Feb 28 16:42:06 2004","Sat Feb 28 16:42:06 2004","Sat Feb 28 16:42:06 2004","Fri Feb 27 08:28:48 2004","Fri Feb 27 08:28:48 2004","Fri Feb 27 08:28:48 2004","Fri Feb 27 08:28:48 2004","Fri Feb 27 08:28:48 2004","Fri Feb 27 08:28:48 2004","Fri Feb 27 08:28:48 2004","Fri Feb 27 08:28:48 2004","Fri Feb 27 08:37:23 2004","Fri Feb 27 08:37:23 2004","Fri Feb 27 08:37:23 2004","Fri Feb 27 08:37:23 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00130 has similarity to AA00128, a cation-transporting ATPase (probable potassium/copper transporter) (7e-11).AA00130 is paralogously related to AA00128 (6e-11).","Fri Feb 27 08:37:23 2004","Sat Feb 28 16:42:06 2004","pdb1AFI1AFI STRUCTURE OF THE REDUCED FORM OF MERP, THE 62.1 1e-11pdb1K0V1K0V-A COPPER TRAFFICKING: THE SOLUTION STRUCTURE OF 61.3 2e-11pdb1AW01AW0 FOURTH METAL-BINDING DOMAIN OF THE MENKES 57.8 3e-10pdb1CPZ1CPZ-A COPPER CHAPERONE OF ENTEROCOCCUS HIRAE 53.1 7e-09pdb1FVQ1FVQ-A SOLUTION STRUCTURE OF THE YEAST COPPER 48.4 2e-07pdb1JWW1JWW-A NMR CHARACTERIZATION OF THE N-TERMINAL DOMAIN 40.2 5e-05pdb1KQK1KQK-A SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF 39.5 8e-05pdb1AW01AW0 FOURTH METAL-BINDING DOMAIN OF THE MENKES 97.5 3e-22pdb1AFI1AFI STRUCTURE OF THE REDUCED FORM OF MERP, THE 94.0 3e-21pdb1JWW1JWW-A NMR CHARACTERIZATION OF THE N-TERMINAL DOMAIN 93.6 4e-21","","","Residues 10 to 74 (E-value = 1.2e-16) place AA00130 in the HMA family which is described as Heavy-metal-associated domain (PF00403)","Fri Feb 27 08:37:23 2004","","","","Kholodii,G.Y., Gorlenko,Z., Lomovskaya,O.L., Mindlin,S.Z.,Yurieva,O.V. and Nikiforov,V.G.Molecular characterization of an aberrant mercury resistancetransposable element from an environmental Acinetobacter strainPlasmid 30 (3), 303-308 (1993)PubMed: 8302940Wilson JR, Leang C, Morby AP, Hobman JL, Brown NL.MerF is a mercury transport protein: different structures but a common mechanism for mercuric ion transporters?.FEBS Lett. 2000 Apr;472(1):78-82.PMID: 10781809DeSilva TM, Veglia G, Porcelli F, Prantner AM, Opella SJ.Selectivity in heavy metal- binding to peptides and proteins.Biopolymers. 64(4):189-97.PMID: 12115136","","Fri Feb 27 08:37:23 2004","1","Fri Feb 27 08:28:48 2004","","" "AA00131","94661","95044","384","ATGAATATCAGTCAAGCAGCCAAACTCACCGGTTTATCCGCCAAACAAATCCGCGATTACGAAAAACTCGGTTTATTAAACCCCGGCGCAAGAACTCTCGCCGGTTATCGGCATTATGAAGAAAGCGATTTAAAACGCCTGCATTTTATCCGCCACTCGCGAGACGTGGGCTTTTCCCTGCAACAAATCGCCCAACTGTTGCAATTACAAGACAACCCGCAACGCAACAGCCGCGAAGTGAAAAAACTCACCGCGCAACACATTGAAACCTTAAACGACCAAATACAGGCGTTACAAAAAATGGTCACCGAACTGCAACGTTGGCACGACAACTGCCAAGGTAACGACTGCCCGGAATGCTCGATTTTGGAGGGCTTGAGTGAG","","","14680","MNISQAAKLTGLSAKQIRDYEKLGLLNPGARTLAGYRHYEESDLKRLHFIRHSRDVGFSLQQIAQLLQLQDNPQRNSREVKKLTAQHIETLNDQIQALQKMVTELQRWHDNCQGNDCPECSILEGLSE","95044","","transcriptional regulator (MerR family)","Cytoplasm","","
InterPro
IPR000551
Domain
Bacterial regulatory protein, MerR
PR00040\"[2-13]T\"[13-26]T\"[37-57]THTHMERR
PF00376\"[2-39]TMerR
SM00422\"[1-70]THTH_MERR
PS50937\"[1-69]THTH_MERR_2
PS00552\"[4-26]THTH_MERR_1
InterPro
IPR015358
Domain
Transcription regulator MerR, DNA binding
PF09278\"[44-108]TMerR-DNA-bind
noIPR
unintegrated
unintegrated
G3DSA:1.10.1660.10\"[1-126]Tno description


","BeTs to 13 clades of COG0789COG name: Predicted transcriptional regulatorsFunctional Class: KThe phylogenetic pattern of COG0789 is a------q-drlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 9.8e-27) to 2/2 blocks of the IPB000551 family, which is described as \"Bacterial regulatory proteins, MerR family\". Interpro entry for IP:IPR000551. IPB000551A 3-24 3.2e-09 IPB000551B 26-67 4.6e-16","Residues 72 to 127 match (1e-15) PD:PD437081 which is described as REGULATOR COPPER TRANSCRIPTION REGULATION DNA-BINDING PROTEOME COMPLETE TRANSCRIPTIONAL ACTIVATOR EFFLUX ","","","","","","","","","","","","Tue Dec 3 11:09:42 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00131 is paralogously related to AA01078 (2e-13) and AA01113 (3e-05).","","","","","","Residues 2 to 39 (E-value = 3.5e-14) place AA00131 in the MerR family which is described as MerR family regulatory protein (PF00376)","","","","","Adaikkalam,V. and Swarup,S.Molecular characterization of an operon, cueAR, encoding a putative P1-type ATPase and a MerR-type regulatory protein, involved in copper homeostasis in Pseudomonas putidaMicrobiology 148, 2857-2867 (2002)","","Mon Dec 2 13:26:51 2002","1","","","" "AA00132","95359","95078","282","ATGTCCGATTCTCTTACATTGCAGCCCGTTGCTATCATTCACACGCCTTACAAAGGAAAATTTTCCGTGCCGCGCCAACCGAATTTGGTGCAGGACGGCACGGGGATCATTGAGTTATTGCCGCCTTTCAATCAGGCGGAATCTGTGCGCGGTTTGGAACAATTCAGCCATCTCTGGCTGATTTTTCAGTTCGATCAAATCCCGCAGGGCAAATGGCATCCCACCGTGCGCCCGCCACGTTTAAAAGATAAGCGTGAGAGATTTTTTAATTATATTTCTACT","","","10928","MSDSLTLQPVAIIHTPYKGKFSVPRQPNLVQDGTGIIELLPPFNQAESVRGLEQFSHLWLIFQFDQIPQGKWHPTVRPPRLKDKRERFFNYIST","95078","","conserved hypothetical protein (possible regulator protein, VirR family)","Periplasm, Cytoplasm","","
InterPro
IPR001378
Domain
Protein of unknown function UPF0066
PD006705\"[36-81]TY510_HAEIN_P44740;
PF01980\"[19-94]TUPF0066
TIGR00104\"[2-94]TTIGR00104: conserved hypothetical protein T
noIPR
unintegrated
unintegrated
PTHR12818\"[4-89]TUNCHARACTERIZED


","BeTs to 8 clades of COG1720COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG1720 is aom-kz--v-----efgh-n-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 6.6e-07) to 1/3 blocks of the IPB001378 family, which is described as \"Uncharacterized protein family UPF0066 (VIRR)\". Interpro entry for IP:IPR001378. IPB001378A 11-27 7.1e-07","Residues 10 to 66 match (2e-14) PD:PD126622 which is described as COMPLETE PROTEOME FIS 5830415F09RIK RCSF COLF1582 FLJ20206 PAB0452 CG12822 CDNA ","","","","","","","","","","","","Wed Dec 11 11:24:35 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00132 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 19 to 94 (E-value = 2.2e-08) place AA00132 in the UPF0066 family which is described as Uncharacterised protein family UPF0066 (PF01980)","","","","","","","Wed Jan 22 15:22:07 2003","1","","","" "AA00134","95457","96389","933","TTGCGATGTCCTGTTGTGAATGTGGAAATTATGACAAAAAATACAATAAAAATGTGGATTGAAACGGCACGTCCGAAAACCTTGCCATTAGCCTTAGCAACCATTTTAACGGGTTCGGCGCTGGCTTATTGGGCGGGCAGTTTTCATTGGGGCGTGACCGTTTTATGTTTGCTAACCACTTTATTTCTGCAAATTCTCTCCAACTTCGCTAATGATTACGGCGATCACCAAAAAGGTTCCGACACCGCCGAGCGTATCGGTCCGTTGCGCGGCATTCAGCAGGGCGCAATTTCCGCCGCTCAGTTGAAAAACGGGCTATATTTAATGATTGCCTTGAGTTTTGTTTGCGGCGCCATATTAATCGGCACGGCATATCAAAATCTGAGCGACTTAATCGCCTTTTCCGTTCTCGGCGTGCTCGCCATTATTGCCGCCATCACTTACACCGTAGGCAGTAAACCTTACGGCTATTTGGGCTTAGGCGATATTTCCGTGCTGATTTTCTTCGGTTTATTGGGCGTGGGTGGCACTTATTATTTACAGGTTCATACGTTTTCTGCGGAAATTCTGTTGCCTGCCGTCGCCAGTGGTTTATTAGCGACCGCTGTATTAAACATCAACAACTTACGTGACATTGAACAGGATCGCAAAGCAGGCAAGAATACCCTGGTGGTACGCTTGGGCGCACACAACGGGCGCATTTATCATTGCATTCTGCTTGCTGTCGCCGCACTGTTTTACTTCTTATTCACCGCTATGAATTTACGCCATCCGTTGAGTTTTGTGTTTTTGCTGACTTACCCGTTATTATTGAAACACGCCTTCTTCGTTCTATCTCACAAAGAACCGACGGCGCTGCGTCCGATGTTGGAGCAAATGTCGTTATTGGCGTTGCTAATTAACGGGCTATTTAGTTTTGGCTTGCTTCCGGGC","","","33744","LRCPVVNVEIMTKNTIKMWIETARPKTLPLALATILTGSALAYWAGSFHWGVTVLCLLTTLFLQILSNFANDYGDHQKGSDTAERIGPLRGIQQGAISAAQLKNGLYLMIALSFVCGAILIGTAYQNLSDLIAFSVLGVLAIIAAITYTVGSKPYGYLGLGDISVLIFFGLLGVGGTYYLQVHTFSAEILLPAVASGLLATAVLNINNLRDIEQDRKAGKNTLVVRLGAHNGRIYHCILLAVAALFYFLFTAMNLRHPLSFVFLLTYPLLLKHAFFVLSHKEPTALRPMLEQMSLLALLINGLFSFGLLPG","96389","","1,4-dihydroxy-2-naphthoate octaprenyltransferase (menaquinone biosynthetic protein)","Inner membrane, Cytoplasm","","
InterPro
IPR000537
Family
UbiA prenyltransferase
PF01040\"[28-309]TUbiA
InterPro
IPR004657
Family
1,4-dihydroxy-2-naphthoate octaprenyltransferase
TIGR00751\"[24-307]TmenA: 1,4-dihydroxy-2-naphthoate octaprenyl
noIPR
unintegrated
unintegrated
PTHR13929\"[9-309]T1,4-DIHYDROXY-2-NAPHTHOATE OCTAPRENYLTRANSFERASE
signalp\"[1-42]?signal-peptide
tmhmm\"[22-42]?\"[48-66]?\"[105-125]?\"[131-151]?\"[156-178]?\"[184-206]?\"[227-249]?\"[259-279]?\"[294-309]?transmembrane_regions


","BeTs to 8 clades of COG1575COG name: 1,4-dihydroxy-2-naphthoate octaprenyltransferaseFunctional Class: HThe phylogenetic pattern of COG1575 is -o------v-rlbce-gh--------Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Mon Dec 2 14:58:58 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00134 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 28 to 309 (E-value = 6.1e-45) place AA00134 in the UbiA family which is described as UbiA prenyltransferase family (PF01040)","","","","","Tullius,M.V., Munson,R.S. Jr., Wang,J. and Gibson,B.W. Purification, cloning, and expression of a cytidine 5'-monophosphate N-acetylneuraminic acid synthetase from Haemophilus ducreyi J. Biol. Chem. 271 (26), 15373-15380 (1996) PubMed: 8663048 Bozue,J.A., Tullius,M.V., Wang,J., Gibson,B.W. and Munson,R.S. Jr. Haemophilus ducreyi produces a novel sialyltransferase. Identification of the sialyltransferase gene and construction of mutants deficient in the production of the sialic acid-containing glycoform of the lipooligosaccharide J. Biol. Chem. 274 (7), 4106-4114 (1999) PubMed: 9933604 Suvarna,K., Stevenson,D., Meganathan,R. and Hudspeth,M.E. Menaquinone (vitamin K2) biosynthesis: localization and characterization of the menA gene from Escherichia coli J. Bacteriol. 180 (10), 2782-2787 (1998) PubMed: 9573170 ","","Wed Jan 22 16:44:51 2003","1","","","" "AA00135","96443","96940","498","ATGTACATTGATACTTCTGAACTTTGCGATATTTATCTCGACCAGGTCGATGTTGTCGAGCCCATTTTCTCCAGTTTCGGCGGACTCAGTTCCTTCCACGGTAAAGTCACCACCGTGAAATGTTTTGAAAATAACGGACTGATTGCTGAAATTTTAGAAGAAAACGGCGAAGGTCGGGTGTTATTGGTGGATGGCGGCGGTGCGGTGCGCCGTGCGTTAATTGATGCGGAACTCGCCCAATTAGCGGCAGACAACCAGTGGGAAGGCATTATCGTTTACGGTGCGGTACGTCAAATTCAACAGTTGGAAAATATCGACATCGGTATTCATGCGTTGGCTCCGATTCCGGTTGGCGCGGACAATTCTAATCATGGCGAAACCGATATTCCAGTCAACTTCGGCGGCGTCACCTTCTTCCCGGAAGATTTCGTTTATGCCGATTTAACCGGCATTATCCTGTCGCAGGAAGCCTTGGATTTGGAAGATTTCGAGCAGGAT","","","18001","MYIDTSELCDIYLDQVDVVEPIFSSFGGLSSFHGKVTTVKCFENNGLIAEILEENGEGRVLLVDGGGAVRRALIDAELAQLAADNQWEGIIVYGAVRQIQQLENIDIGIHALAPIPVGADNSNHGETDIPVNFGGVTFFPEDFVYADLTGIILSQEALDLEDFEQD","96940","","S-adenosylmethionine: 2-demethylmenaquinone methyltransferase (menaquinone biosynthesis protein)","Cytoplasm","","
InterPro
IPR005493
Family
Dimethylmenaquinone methyltransferase
PF03737\"[1-153]TMethyltransf_6
InterPro
IPR010203
Family
Ribonuclease E inhibitor RraA
TIGR01935\"[5-154]TNOT-MenG: RraA family
InterPro
IPR014339
Family
Ribonuclease E inhibitor RraA, gammaproteobacteria
TIGR02998\"[1-161]TRraA_entero: regulator of ribonuclease acti
noIPR
unintegrated
unintegrated
G3DSA:3.50.30.40\"[1-162]Tno description


","No hits to the COGs database.","","Residues 2 to 153 match (8e-62) PD:PD006785 which is described as METHYLTRANSFERASE TRANSFERASE COMPLETE PROTEOME S-ADENOSYLMETHIONINE:2-DEMETHYLMENAQUINONE MENAQUINONE BIOSYNTHESIS 2.1.-.- PROBABLE PLASMID ","","","","","","","","","","","","Wed Jan 22 16:40:52 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00135 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 153 (E-value = 2.1e-77) place AA00135 in the Methyltransf_6 family which is described as Demethylmenaquinone methyltransferase (PF03737)","","","","","Tyson K, Metheringham R, Griffiths L, Cole J. Characterisation of Escherichia coli K-12 mutants defective informate-dependent nitrite reduction: essential roles for hemN and themenFDBCE operon. Arch Microbiol. 1997 Nov;168(5):403-11. PMID: 9325429","","Mon Dec 2 15:08:11 2002","1","","","" "AA00136","97132","98511","1380","ATGAGCGAAACAACTCAAAATCAAAGTAAGATCAATAGGAGTGTAATTATCTTTATCCTTGCCGTTATTCTATTTTTTATCTTACTCAACACACTGCCATTCGATAGAGACGCCAATAGTGGGTTGGCATTATTGGCTTTAGTTGCCATTTTATGGCTAACGGAAGCCCCACACGTTACTATCACGGCGTTGATTGTTCCTTTGATGGCGATTTTTTTGGGGCTCGTAAAAACAAGTACCGCCCTTGCCACCTTCGCCGATCCGAATATTTTCTTATTTTTCGGCGGATTTGCCTTAGCCACTGCATTACATATTCAGCAATTGGATAAAATGATTGCGAATAAAATCATGACATTGGCAAAAGGAAATTTATTTGTTGCCGTCATCTATTTGTTCTCTGTGACCGCATTTTTATCCATGTGGGTGAGTAATACCGCCACCGCCGCCATGATGTTGCCGCTGGCGATGGGCGTATTAAGTCGTCTTGATCGTAAAGAGCAACATAATACTTATCTGTTCGTGTTGTTAGGAATCGCCTATAGCGCCAGTATCGGCGGTATGGGAACTTTAGTAGGCAGCCCACCGAATAACATCGTGGCAACCCAATTGCACCTCACCTTCGCCGATTGGTTATGGTATGGCTTGCCGATTATGATTATCTTAATGCCAATTATGATCGGGACGCTTTATATTGTGTTCAAACCGAAACTTCACGTTCACTTTGAACAACAATTTGAAAAAGTAGAAATGACCAAACAACGCTGGATTACCCTCGGCATTTTTGTGTTTATTGCCTTAAGCTGGGTTTTCAGTAGTCAAATCAACCCGATTCTTTCCGCAGCATTAGGTTTAGAAGGTAAAATTGCCGGCTTTGATAGTGTCATCGCCTTATCGGCGGCAGTGATTATCTGCGTTAGCGGTGTAGCCAACTGGAAGCAAATTCAGGAAAGCACCGACTGGGGCGTGTTAATGCTGTTCGGTGGCGGTTTAACCTTAAGCGCGGTGCTAAAAAATTCCGGTGCCAGCAAAATTTTAGCGGATGGTATCGTCTTCCTCATTGAAGGCGGAAATTTCTACCTCATCGGCTTATTGGTCGCCGCGTTCATTATTTTCTTAACGGAGTTTACCTCCAACACCGCTAGTGCCGCGTTATTAGTGCCGATTTTCATTTCTATCGCACAATCGCTCGGCATGCCGGAAATCGGTCTTGCCCTTATCATCGGCTTAGGCGCCTCCTGTGCCTTTATGTTGCCGGTGGCAACGCCGCCGAATGCCATTGTGTTCGGTACCGGTGAAGTGAAACAAAGTGAAATGGTCAGAGCGGGTGTTATTCTGAACATCGTCTGTGTTTTTGTCATCGCCACCTTCGGTTATTTATTC","","","51698","MSETTQNQSKINRSVIIFILAVILFFILLNTLPFDRDANSGLALLALVAILWLTEAPHVTITALIVPLMAIFLGLVKTSTALATFADPNIFLFFGGFALATALHIQQLDKMIANKIMTLAKGNLFVAVIYLFSVTAFLSMWVSNTATAAMMLPLAMGVLSRLDRKEQHNTYLFVLLGIAYSASIGGMGTLVGSPPNNIVATQLHLTFADWLWYGLPIMIILMPIMIGTLYIVFKPKLHVHFEQQFEKVEMTKQRWITLGIFVFIALSWVFSSQINPILSAALGLEGKIAGFDSVIALSAAVIICVSGVANWKQIQESTDWGVLMLFGGGLTLSAVLKNSGASKILADGIVFLIEGGNFYLIGLLVAAFIIFLTEFTSNTASAALLVPIFISIAQSLGMPEIGLALIIGLGASCAFMLPVATPPNAIVFGTGEVKQSEMVRAGVILNIVCVFVIATFGYLF","98511","","sodium/sulphate transporter","Inner membrane, Cytoplasm","","
InterPro
IPR001898
Family
Sodium/sulphate symporter
PF00939\"[307-459]TNa_sulph_symp
TIGR00785\"[33-460]Tdass: transporter, divalent anion:Na+ sympo
PS01271\"[411-427]TNA_SULFATE
noIPR
unintegrated
unintegrated
PTHR10283\"[35-456]TCATION TRANSPORTER RELATED
PTHR10283:SF37\"[35-456]TSODIUM/DICARBOXYLATE COTRANSPORTER-RELATED
signalp\"[1-31]?signal-peptide
tmhmm\"[10-30]?\"[36-54]?\"[59-79]?\"[85-103]?\"[118-136]?\"[142-162]?\"[172-192]?\"[211-233]?\"[254-272]?\"[291-311]?\"[321-341]?\"[347-369]?\"[379-399]?\"[405-427]?\"[439-459]?transmembrane_regions


","BeTs to 17 clades of COG0471COG name: Di- and tricarboxylate transportersFunctional Class: PThe phylogenetic pattern of COG0471 is -om-k-yq-d-lbcefghsnu--i--Number of proteins in this genome belonging to this COG is","Significant hit ( 7e-126) to 8/8 blocks of the IPB001898 family, which is described as \"Sodium:sulfate symporter family\". Interpro entry for IP:IPR001898. IPB001898A 52-75 1.1e-08 IPB001898B 91-117 7.5e-14 IPB001898C 135-154 5.7e-16 IPB001898D 174-198 4.8e-15 IPB001898E 205-229 8e-10 IPB001898F 247-273 1.2e-06 IPB001898G 317-346 2.2e-13 IPB001898H 399-447 5.7e-33 IPB001898B 324-350 0.94 IPB001898C 369-388 0.0041 IPB001898G 84-113 0.29","Residues 383 to 452 match (6e-08) PD:PD574152 which is described as TRANSMEMBRANE CHROMOSOME III X K08E5.2 F31F6.6 CG4961 GH13033P B0285.6 R107.1 ","","","","","","","","","","","Wed Dec 11 11:25:44 2002","Mon Dec 2 15:23:29 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00136 is paralogously related to AA01784 (0.0), AA00941 (4e-21), AA00741 (4e-10), AA00615 (2e-08), AA00080 (2e-05) and AA02387 (2e-04).","","","","","","Residues 8 to 459 (E-value = 1.9e-13) place AA00136 in the Na_sulph_symp family which is described as Sodium:sulfate symporter transmembrane region (PF00939)","","","","","","","","1","","","" "AA00137","99117","98587","531","ATGGCAAAGCATAAAAAAGAAGATTTTGACCGGCAGAATGAAGAACAGGAAGAAATCATTTGGGTCAGCAAGAGCGAAATCAAACGGGACGCGGAAGCATTAAAAAAATTGGGTGAAAAATTGGTTGAACTGACCAAAGCCAAATTAGATAAAATTCCATTGGAAGAATCCTTGCTGGAAGCAGTAAATTTGGCGCAGCGCCTGCAAAAAGAAGCGCGTCGCCGCCAGTTACAATATATCGGTAAATTATTGCGTAGTATGGACGTGGAACCGATTCAGGGCGCCTTGGACAAACTGGAAAACAAACATTTGCAACAACAAGCCATGTTACACAAACTGGAATTACTGCGTGACGAGCTTGTGGCAAAGGGCGATAGCGCATTAACGGATTTTCTAGCGGATTATCCCCATGCCGATCGGCAACATTTACGCACTTTGATTCGTGCCGCTAATAAGGAAAAAGAACAAAATAAACCGGCAAAAGCCTATCGTGAAATTTTTCAGTATTTAAAAGAGATTGTGTTGGAAGAT","","","21290","MAKHKKEDFDRQNEEQEEIIWVSKSEIKRDAEALKKLGEKLVELTKAKLDKIPLEESLLEAVNLAQRLQKEARRRQLQYIGKLLRSMDVEPIQGALDKLENKHLQQQAMLHKLELLRDELVAKGDSALTDFLADYPHADRQHLRTLIRAANKEKEQNKPAKAYREIFQYLKEIVLED","98587","","conserved hypothetical protein (possible alpha helix protein)","Cytoplasm","","
InterPro
IPR006839
Family
Protein of unknown function DUF615
PIRSF016183\"[1-177]TUncharacterised conserved protein
PF04751\"[1-177]TDUF615


","BeTs to 6 clades of COG3028COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3028 is --------------efghsn------Number of proteins in this genome belonging to this COG is","","Residues 3 to 171 match (3e-48) PD:PD035713 which is described as COMPLETE PROTEOME COILED MICROTUBULES ATP-BINDING MOTOR COIL YJGA ISOLOG HI1151 ","","","","","","","","","","","","Mon Dec 2 15:39:17 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00137 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 177 (E-value = 1.7e-110) place AA00137 in the DUF615 family which is described as Protein of unknown function (DUF615) (PF04751)","","","","","","","","1","","","" "AA00138","99106","99201","96","ATGCTTTGCCATGTTTTTTCCGATCATTCTACTTACTTAAAAGTGCGGAGCATTTTAGCACAGAATCTGTGGTTCGCCTTAAAAAGAAAAATAAGC","","","3789","MLCHVFSDHSTYLKVRSILAQNLWFALKRKIS","99201","","hypothetical protein","Cytoplasm","No similarities were found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sat Feb 21 11:13:33 2004","Sat Feb 21 11:13:33 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00138 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sat Feb 21 11:14:31 2004","","","","","","","","","","","","","1","","","" "AA00139","99238","100596","1359","ATGCAACAAAAAACACTTGAAAAATCCACCGCACTTTTACGCCAACAGGAACAACAATTACGCGACGCCGTAAGCCTTGCCATTGAAATCGCGCAAAAAGCAGGCGCCACCGCCGAAGTGGGCGTCACCAAATCCGGCGGGCTGTCTGTCTCTACCCGCCTCCGGGAAATTGAAAATGTTGAATTTAACAATGACGGCGCGTTAGGCATTTCCGTTTATCTGGGACAACAAAAAGGCAATGCCTCCACCTCCGATTTAACGCCGGATGCTATCAAAAGCACCGTCGAAGCCGCCCTAGCCATCGCCAAATATACTTCACCGGACGATTGTGCCGGCTTGGCAGATAAAGATCTGATGGCATTTGATGCGCCGGATTTAGCGTTGTATCACGCCGCCGAAATAGAGGTGGATCACGCCATGCAACTCGCGCTGGAAACGGAAAGAGCCGCATTGGAACATGACGCGCGTATCGTCAACAGCGAAGGTGCTTCTTTCAACGCCCATACCGGCGTACGGGTTTATGGCAACAGTTACGGCATGTTGCAAAGCTATTTATCCAGTCGCTATTCCCTTTCCTGCTCGGTGATTGCCGAACATCAGACGCAGTTGGAACGGGATTATGAATACACAGTAGCGCGAGATATGACACAGTTAGCGCAACCGAAATGGGTCGGTGAACATGCCGCGCAAAAAGCCATTGCCCGTTTGCAACCGCAAAAACTCGCGACCCAACAAGCACCGGTCATATTCTTAAATGATGTGGCGACAGGCTTAATTAGCCATTTGACGGCGGCAATCAGTGGCGGCAGTTTATATCGCAAAGCCAGTTTTTTATTGGATCATTTAGACAAACAGGTGTTACCGGATTGGTTTGAGATTGTGGAAAGACCGCACCTGATGGGGCAACTTGCTTCAACACCTTTCGATAGCGAAGGTGTGAAAACGCAGGATATGGACATTATCCGCAACGGCATTTTACAGACTTATTTGCTCACCAGTTACAGCGGTCGCAAACTCGGCATGCAAAGCAACGGGCACGCGGGCGGCATTCATAACTGGTTGGTGAAAGCAAATTCATCGGGAAAACTGACCGCACTTTTACGTCAAATGAATCGCGGTTTGTTGGTTACGGAAGTAATGGGGCAAGGCGTTAATCCGGTTAGTGGCGATTATTCGCGCGGAGCAGCCGGCTTCTGGGTGGAAAACGGCGAGATTCAATACCCGGTGGCAGAAATCACCATTGCCGGTCAATTACCTGAAATGTTGCGCAATATTGTTGCCGTGGGTGATGATATTGAACATCGTTCAAATATTCAGACCGGTTCTATTCTCTTGGAAAATATGAAAATTTCCGGTAAT","","","49129","MQQKTLEKSTALLRQQEQQLRDAVSLAIEIAQKAGATAEVGVTKSGGLSVSTRLREIENVEFNNDGALGISVYLGQQKGNASTSDLTPDAIKSTVEAALAIAKYTSPDDCAGLADKDLMAFDAPDLALYHAAEIEVDHAMQLALETERAALEHDARIVNSEGASFNAHTGVRVYGNSYGMLQSYLSSRYSLSCSVIAEHQTQLERDYEYTVARDMTQLAQPKWVGEHAAQKAIARLQPQKLATQQAPVIFLNDVATGLISHLTAAISGGSLYRKASFLLDHLDKQVLPDWFEIVERPHLMGQLASTPFDSEGVKTQDMDIIRNGILQTYLLTSYSGRKLGMQSNGHAGGIHNWLVKANSSGKLTALLRQMNRGLLVTEVMGQGVNPVSGDYSRGAAGFWVENGEIQYPVAEITIAGQLPEMLRNIVAVGDDIEHRSNIQTGSILLENMKISGN","100596","","antibiotic maturation factor","Cytoplasm","","
InterPro
IPR002510
Family
Peptidase U62, modulator of DNA gyrase
PF01523\"[36-329]TPmbA_TldD


","No hits to the COGs database.","Significant hit ( 6.5e-17) to 1/2 blocks of the IPB002510 family, which is described as \"Putative modulator of DNA gyrase\". Interpro entry for IP:IPR002510. IPB002510B 304-346 6.3e-17","Residues 366 to 441 match (4e-28) PD:PD002987 which is described as COMPLETE PROTEOME TLDD PMBA PROTEASE MATURATION HOMOLOG GYRASE DNA MODULATOR ","","","","","Wed Feb 19 09:31:06 2003","","","","","","","Mon Dec 2 15:49:51 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00139 is paralogously related to AA01687 (1e-14).","","","","","","Residues 36 to 329 (E-value = 6e-84) place AA00139 in the PmbA_TldD family which is described as Putative modulator of DNA gyrase (PF01523)","","","","","Allali N, Afif H, Couturier M, Van Melderen L.The highly conserved TldD and TldE proteins of Escherichia coli are involved in microcin B17 processing and in CcdA degradation.J Bacteriol. 2002 Jun;184(12):3224-31.PMID: 12029038Rodriguez-Sainz,M.C., Hernandez-Chico,C. and Moreno,F. Molecular characterization of pmbA, an Escherichia colichromosomal gene required for the production of the antibiotic peptide MccB17 JOURNAL Mol. Microbiol. 4 (11), 1921-1932 (1990) PubMed: 2082149 Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H., Horiuchi,T., Sekimizu,K. and Miki,T. Evidence for involvement of Escherichia coli genes pmbA, csrA anda previously unrecognized gene tldD, in the control of DNA gyrase by letD (ccdB) of sex factor F J. Mol. Biol. 256 (3), 483-502 (1996) PubMed: 8604133 Allali N, Afif H, Couturier M, Van Melderen L.The highly conserved TldD and TldE proteins of Escherichia coli are involved in microcin B17 processing and in CcdA degradation.J Bacteriol. 2002 Jun;184(12):3224-31.PMID: 1202903","","Thu Feb 13 17:33:47 2003","1","","","" "AA00140","100932","100786","147","GTGTTGATAGAAGACGGTGATTTCTTTACCGAGTTCCCGGATACGGGAGCGGGCTTCTTGTTCGGAAATCAGAATATCAACGTGGTGTTTTTTCATTTAAGGTTACCTTTGGCAGATGAGGATGTCGCTATTCTAACAAAAAAAGAC","","","5482","VLIEDGDFFTEFPDTGAGFLFGNQNINVVFFHLRLPLADEDVAILTKKD","100786","","hypothetical protein","Cytoplasm","No similarities were found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sat Feb 21 11:18:08 2004","Sat Feb 21 11:18:08 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00140 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sat Feb 21 11:19:22 2004","","","","","","","","","","","","","1","","","" "AA00141","100954","101373","420","GTGGTAGGCTTATTGCGCGGTTCCTTTATGTTCATGGCGGATTTGGTGCGCGAACTGCATTTGCCGGTAGAAATTGAATTTATGACGACCTCCAGCTACGGTAGCGGCATGACCACTAATCATGACGTGCGTATCAGCAAAGATTTAGACGGCGACATCAAAGGCAAAGACGTTCTGATTGTGGAAGATATTATAGACACAGGTTACACCTTGGAAAAAGTACGCGAAATTTTGAATTTGCGTGAACCGGCATCCCTGGCGATTTGTACCTTGCTCGACAAACCATCACGCCGTGAAGTGCAGGTGCCGGTGGACTGGGTGGGCTTTACTATTCCCGATGAATTCGTGGTGGGCTACGGTATTGATTATGCCCAACAGCATCGTAATCTGGGCTATATTGGCAAAGTGATTTTGGAAGAA","","","20427","VVGLLRGSFMFMADLVRELHLPVEIEFMTTSSYGSGMTTNHDVRISKDLDGDIKGKDVLIVEDIIDTGYTLEKVREILNLREPASLAICTLLDKPSRREVQVPVDWVGFTIPDEFVVGYGIDYAQQHRNLGYIGKVILEE","101373","","hypoxanthine phosphoribosyl transferase (HPRT)","Cytoplasm","","
InterPro
IPR000836
Domain
Phosphoribosyltransferase
PF00156\"[1-112]TPribosyltran
InterPro
IPR002375
Family
Purine/pyrimidine phosphoribosyl transferase
PS00103\"[58-70]TPUR_PYR_PR_TRANSFER
InterPro
IPR005904
Family
Hypoxanthine phosphoribosyl transferase
TIGR01203\"[1-137]THGPRTase: hypoxanthine phosphoribosyltransf
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2020\"[1-136]Tno description
PTHR22573\"[1-134]TPHOSPHOHEXOMUTASE FAMILY MEMBER
PTHR22573:SF9\"[1-134]THYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE
signalp\"[1-19]?signal-peptide


","BeTs to 12 clades of COG0634COG name: Hypoxanthine-guanine phosphoribosyltransferaseFunctional Class: FThe phylogenetic pattern of COG0634 is -------qvdrlb-efghsn-j---wNumber of proteins in this genome belonging to this COG is","Significant hit ( 7.7e-07) to 1/2 blocks of the IPB002375 family, which is described as \"Purine/pyrimidine phosphoribosyl transferase\". Interpro entry for IP:IPR002375. IPB002375B 55-70 8.3e-07Significant hit ( 7.1e-06) to 1/6 blocks of the IPB000842 family, which is described as \"Phosphoribosyl pyrophosphate synthetase\". Interpro entry for IP:IPR000842. IPB000842D 34-88 6.1e-06","Residues 4 to 133 match (5e-07) PD:PD418029 which is described as TRANSFERASE COMPLETE PROTEOME GLYCOSYLTRANSFERASE PHOSPHORIBOSYLTRANSFERASE PROBABLE HYPOXANTHINE-GUANINE HYPOXANTHINE PURINE/PYRIMIDINE PHOSPHORIBOSYLTRANSFERASE ","","","","","","","","","","","","Mon Dec 2 16:03:55 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00141 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 112 (E-value = 7.1e-22) place AA00141 in the Pribosyltran family which is described as Phosphoribosyl transferase domain (PF00156)","","","","","Showalter,R.E. and Silverman,M.R. TITLE Nucleotide sequence of a gene, hpt, for hypoxanthine phosphoribosyltransferase from Vibrio harveyi JOURNAL Nucleic Acids Res. 18 (15), 4621 (1990) PubMed: 2388850 ","","Mon Dec 2 16:03:55 2002","1","","","" "AA00142","102585","101449","1137","ATGAAAATTATTATTGCGCCGGATTCCTTTAAAGAAAGTTTAACCGCATTGGAAGCGGCAAATGCCATTGAAGCAGGGTTTAAGCGGATTTTTCCGAATGCGGAATGTGTCAAATTACCGATGGCGGACGGGGGCGAAGGGACGGTTCAGTCTTTGGTGGATGCCACCGGCGGTAAACTGGTTGAATGCGATGTCGTGGCACCGTTGGGCAATACCGTACAAAGTTTCTTCGGGCTTTCCGGCGATGGCAAAACGGCGATTATTGAAATGGCGGCGGCATCGGGCTTGCATTTGGTGGCGCCGGAGCAACGTAATCCGTTGCATACCACCAGTTACGGCACCGGTGAGTTGATTAAACGTGCGTTGGCTCTTGGCGTACAGCACATTATTTTAGGCATCGGCGGCAGCGCCACCAATGATGGCGGTGTCGGAATGCTGCAAGCGCTGGGCATTCGGTTTTTAAATTTTCAACAACAGGAAATTGGTTATGGCGGCGCACAGTTAGCGCAACTTGCACAAATTGATATGAACGCTTTGGAGCCGCATTTGGCGCAAGTGCATATTGAAGTGGCGTGCGATGTGAATAATCCGTTGTGTGGTGAACGGGGTGCGTCGGCGATTTTCGGACCGCAAAAAGGCGCCACCCCGGAAATGGTGGCGCAACTGGATGTGGCGTTGGCGCATTTCGCCGAGATTGCCCAACGCGATTGTGGCAAAAATATTCAAGATCAGCCGGGTGCCGGCGCCGCAGGCGGTATGGGCGGCGGCTTATTGCTGTTACCGAATGTGGAATTAAAAGCCGGTGTGCAAATCATGTTGGAAAATTTGCAACTGGCGGACAAAGTGCATGACGCCGATTTGGTGATTACCGGTGAAGGCCGCATGGACGCACAGAGTATTCTCGGTAAAACGCCTATTGGTGTGGCGCGTACGGCGAAGCAGTTCAATAAACCGGTGATTGCCATTGTTGGTTGTCTGCGTGAGGATTATGAAGTGGTGTACGAGCATGGCATTGATGTGGTGTTCCCGATCATTCGCCAGCTGGCACCGTTATCGGAAATTTTGCAGCAGGGCAGGGAGAACCTGGTTTCCGCTGCACAAAATATCGCCCGCCTGTTTGCGTTACAAGGGAAAATT","","","40277","MKIIIAPDSFKESLTALEAANAIEAGFKRIFPNAECVKLPMADGGEGTVQSLVDATGGKLVECDVVAPLGNTVQSFFGLSGDGKTAIIEMAAASGLHLVAPEQRNPLHTTSYGTGELIKRALALGVQHIILGIGGSATNDGGVGMLQALGIRFLNFQQQEIGYGGAQLAQLAQIDMNALEPHLAQVHIEVACDVNNPLCGERGASAIFGPQKGATPEMVAQLDVALAHFAEIAQRDCGKNIQDQPGAGAAGGMGGGLLLLPNVELKAGVQIMLENLQLADKVHDADLVITGEGRMDAQSILGKTPIGVARTAKQFNKPVIAIVGCLREDYEVVYEHGIDVVFPIIRQLAPLSEILQQGRENLVSAAQNIARLFALQGKI","101449","","glycerate kinase","Cytoplasm","","
InterPro
IPR004381
Family
Glycerate kinase
PF02595\"[1-378]TGly_kinase
TIGR00045\"[2-376]TTIGR00045: glycerate kinase
noIPR
unintegrated
unintegrated
G3DSA:3.90.1510.10\"[42-276]Tno description
PTHR21599\"[2-379]TGLYCERATE KINASE


","BeTs to 8 clades of COG1929COG name: Glycerate kinaseFunctional Class: GThe phylogenetic pattern of COG1929 is ----------rlbcefgh-n------Number of proteins in this genome belonging to this COG is","Significant hit (1.1e-125) to 5/5 blocks of the IPB003747 family, which is described as \"Glycerate kinase/DUF168\". Interpro entry for IP:IPR003747. IPB003747A 1-26 7.6e-19 IPB003747B 40-49 2.4e-05 IPB003747C 106-150 4.2e-32 IPB003747D 188-230 1.7e-35 IPB003747E 284-324 3.5e-29","Residues 1 to 150 match (1e-10) PD:PD543597 which is described as RV2205C PROTEOME KINASE COMPLETE TRANSFERASE ","","","","","","","","","","","","Mon Dec 2 16:25:26 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00142 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 378 (E-value = 2.1e-249) place AA00142 in the Gly_kinase family which is described as Glycerate kinase family (PF02595)","","","","","Cusa,E., Obradors,N., Baldoma,L., Badia,J. and Aguilar,J.Genetic analysis of a chromosomal region containing genes requiredfor assimilation of allantoin nitrogen and linked glyoxylatemetabolism in Escherichia coliJ. Bacteriol. 181 (24), 7479-7484 (1999)PubMed: 10601204 ","","Mon Dec 2 16:25:26 2002","1","","","" "AA00143","103856","102585","1272","ATGACGACAGTCTCAGCGTTGGGAGCGGTCATTGCACTTGCGGTGGCGCTCCTCCTGATTTTGAAAAAAGTATCGCCGGCATACGGTATGCTGGCGGGGGCGTTAATCGGCGGTTTGGTCGGCGGTGCCGATTTAGTGCAAACCGTGAGTCTCATGATCGGCGGTGCGCAGGGCATTACCACGGCGGTCATGCGGATTTTAGCCGCCGGTGTGTTGGCGGGCGTGCTGATTGATTCCGGTGCTGCCAACACGATTGCGGAAACCATTACCAATAAGTTGGGGGAAGCCCGTGCTTTGTTGGCATTAGCCTTAGCGACGATGATTTTAACAGCTGTTGGCGTGTTCGTTGATGTGGCGGTGATTACCGTATCACCGATTGCCCTTGCCTTGGCGCGTCGTACCGATTTATCCAAACCGGCGATTTTGCTGGCGATGATCGGTGGTGGTAAAGCGGGGAATATTATGTCGCCGAACCCCAATGCCATCGCAGCTTCCGACACCTTCCACCAGCCGTTAACGTCCGTCATGATGGCGGGGATTATTCCAGCGGTTTTCGGTGTAATTTTAACCTATTTCTTAGCCAAACGTTTGATTCGTAGAGGCTCCAAAGTCACTTCACAAGAAGTCATTGTCGTGGAAAAACACGATTTACCGCATTTCGGCACGGCAATAGTTGCGCCGCTGTGTGCGATTCTATTATTAGCTTTACGTCCGTTATTCGGCATCAAAGTGGATCCCCTGATTGCGTTGCCGGCGGGCGGTTTGGTCGGTGCGTTGTGTATGGGAAAAATTCGCCATGCGAATAATTATGCCATCAGCGGATTGGGCAAAATGGCGCCGGTTGCCATTATGTTGCTTGGTACGGGCGCACTTGCCGGGATTATCGCTAATTCAGGGTTAAAAGATGTGTTAATTCAAGGTTTAGAACATTCCGGGTTACCTTCCTATATTCTGGCACCTATCTCAGGCGTATTAATGTCTTTGGCGACGGCTTCGACCACGGCGGGGACGGCGGTGGCGTCCAACGTGTTTAGCGGCATTTTGTTAGAATTAGGCGTGAGCGGTTTAGCAGCGGCAGCCATGATTCATGCCGGTGCGACAGTATTCGACCATATGCCGCACGGTTCTTTCTTCCATGCCACCGGCGGCAGCGTGAACATGGATATTAAAGAACGCTTGAAACTGATCCCTTATGAAAGTGCGGTGGGTTTAATCATGACGATTGTTTCTACGCTGATTTTCGGCGTGTTTAATTGGTTCTGGGAGGTTTTA","","","44629","MTTVSALGAVIALAVALLLILKKVSPAYGMLAGALIGGLVGGADLVQTVSLMIGGAQGITTAVMRILAAGVLAGVLIDSGAANTIAETITNKLGEARALLALALATMILTAVGVFVDVAVITVSPIALALARRTDLSKPAILLAMIGGGKAGNIMSPNPNAIAASDTFHQPLTSVMMAGIIPAVFGVILTYFLAKRLIRRGSKVTSQEVIVVEKHDLPHFGTAIVAPLCAILLLALRPLFGIKVDPLIALPAGGLVGALCMGKIRHANNYAISGLGKMAPVAIMLLGTGALAGIIANSGLKDVLIQGLEHSGLPSYILAPISGVLMSLATASTTAGTAVASNVFSGILLELGVSGLAAAAMIHAGATVFDHMPHGSFFHATGGSVNMDIKERLKLIPYESAVGLIMTIVSTLIFGVFNWFWEVL","102585","","gluconate permease (GntP family)","Inner membrane, Cytoplasm","","
InterPro
IPR001969
Active_site
Peptidase aspartic, active site
PS00141\"[75-86]?ASP_PROTEASE
InterPro
IPR004680
Family
Divalent ion symporter
PF03600\"[7-358]TCitMHS
noIPR
unintegrated
unintegrated
signalp\"[1-26]?signal-peptide
tmhmm\"[5-25]?\"[31-51]?\"[66-86]?\"[96-130]?\"[139-157]?\"[171-193]?\"[223-241]?\"[247-265]?\"[280-300]?\"[319-339]?\"[344-364]?\"[401-421]?transmembrane_regions


","BeTs to 6 clades of COG2610COG name: H+/gluconate symporter and related permeasesFunctional Class: G,EThe phylogenetic pattern of COG2610 is -----------lb-efgh-n------Number of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-57) to 4/4 blocks of the IPB003474 family, which is described as \"GntP family permease\". Interpro entry for IP:IPR003474. IPB003474A 35-75 3e-14 IPB003474B 142-193 2.5e-17 IPB003474C 269-304 4.6e-07 IPB003474D 357-396 7.9e-15 IPB003474A 54-94 0.055","Residues 277 to 356 match (7e-18) PD:PD583711 which is described as PROTEOME COMPLETE GNTP PERMEASE TRANSMEMBRANE PERMEASE GLUCONATE HI0092 FAMILY ","","","","","","","","","","","","Thu Dec 5 20:40:16 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00143 is paralogously related to AA02668 (8e-18), AA02870 (2e-16), AA01784 (2e-05), AA01459 (1e-04) and AA00741 (8e-04).","","","","","","Residues 1 to 413 (E-value = 1.6e-06) place AA00143 in the GntP_permease family which is described as GntP family permease (PF02447)","","","","","Klemm,P., Tong,S., Nielsen,H. and Conway,T.The gntP gene of Escherichia coli involved in gluconate uptakeJ. Bacteriol. 178 (1), 61-67 (1996)PubMed: 8550444Izu H, Kawai T, Yamada Y, Aoshima H, Adachi O, Yamada M.Characterization of the gntT gene encoding a high-affinity gluconate permease in Escherichia coli.Gene. 1997 Oct 15;199(1-2):203-10.PMID: 9358057","","Thu Dec 5 20:48:01 2002","1","","","" "AA00144","105046","103991","1056","ATGAATATTATTGGTTGTTCGGTGAATGTGATGGATCATCACGGGATTATTATTGCTTCCGGAAATCCCGCCCGTTTGAACCAGTTGCATACCGGTGCGGTGCTTGCTTTACGTCAGAACAGAATGGTGGAAGTGGATGAAAACCTTGCGGAAAAATGGAATTTTGACGCGCACCCGGGGATCAACGTGCCGATTCAATATCTTGGCAATAATATCGGTGTAATTGGTATTTCCGGCGTGCCGGAACAGGTTAAGCCCTATGCAGAATTAGTCAAAATGACGGCGGAATTAATTATTGAACAACATATTTTATTGGAGAAAGAAAGCTGGAATCGACGCTATAAAGAAGAATTTATTTTACAGCTGGTAAAAGGAAATTTATCTCTGGCGGAAATACAACAACAGGCAGCGTTTTTTTCTTTTGCATTAGATATTCCGCGCGTCGTCATTATTATTAAATTATTACATCCCAACGCCGATTCATTACAGCAATTAGTGGGTTATTTAGAACAACCGCAATTTGAACAAGATGTGGCGATTTTATCCTTGGATCAAATTATTATTTTGCAGCCTTTTAATATTTTTGCCCAATTTGGCAAACAGCTAAAAAAATTATTACCGAAGGACTATTCGCAGCAGGATTACAAAATCGCCATCGGTGCACAGCTGGAATGTCCTGCCGGCGAGCAGTTGCATTTATCTTATCGCAGTGCCTTAAGCACCTTGCAGTATGGTTTGAAACATTATCCGCGCAAAACCCTTTACTTTTTCGAACAATATCGACTGCCTGTTTTGTTGGCGGGCATTGCCGATAGCTGGCAGGCGGAAGAATTGTTAAAACCGCTAAAAGCCTTATTTTCGGAAGAGAACGCGTTGCTCTTTAAAACATTGCAACAATATTTTTTATCAAATTGTGATCTTGTTCTCACTGCACAAAAATTGTTCATTCACCCTAACACGTTGCGCTATCGGTTGGCGAAGATTGAACAGATAACCGCATTGTCTTTCAATAAGATAGAGGATCGGTTTAGCCTTTATTTAAGTACCGTACTCATT","","","41869","MNIIGCSVNVMDHHGIIIASGNPARLNQLHTGAVLALRQNRMVEVDENLAEKWNFDAHPGINVPIQYLGNNIGVIGISGVPEQVKPYAELVKMTAELIIEQHILLEKESWNRRYKEEFILQLVKGNLSLAEIQQQAAFFSFALDIPRVVIIIKLLHPNADSLQQLVGYLEQPQFEQDVAILSLDQIIILQPFNIFAQFGKQLKKLLPKDYSQQDYKIAIGAQLECPAGEQLHLSYRSALSTLQYGLKHYPRKTLYFFEQYRLPVLLAGIADSWQAEELLKPLKALFSEENALLFKTLQQYFLSNCDLVLTAQKLFIHPNTLRYRLAKIEQITALSFNKIEDRFSLYLSTVLI","103991","","possible carbohydrate diacid regulator","Cytoplasm","","
InterPro
IPR008599
Domain
Putative sugar diacid recognition
PF05651\"[1-281]TDiacid_rec


","BeTs to 5 clades of COG3835COG name: Sugar diacid utilization regulatorFunctional Class: K,TThe phylogenetic pattern of COG3835 is ------------b-efgh--------Number of proteins in this genome belonging to this COG is","","Residues 230 to 347 match (5e-09) PD:PD007784 which is described as COMPLETE PROTEOME TRANSCRIPTIONAL REGULATOR PLASMID DNA-BINDING REGULATORY GENES ACTIVATOR CDS ","","","","","Tue Feb 18 15:52:37 2003","","","","","","","Thu Dec 5 11:02:28 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00144 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 281 (E-value = 1.6e-110) place AA00144 in the Diacid_rec family which is described as Putative sugar diacid recognition (PF05651)","","","","","Monterrubio,R., Baldoma,L., Obradors,N., Aguilar,J. and Badia,J.A common regulator for the operons encoding the enzymes involved in D-galactarate, D-glucarate, and D-glycerate utilization inEscherichia coliJ. Bacteriol. 182 (9), 2672-2674 (2000)PubMed: 10762278","","Thu Dec 5 10:06:04 2002","1","","","" "AA00145","105404","105186","219","ATGGGTCAAGATAATCGGCGCGGGAATTGCTATGACAATGCGGTGATAGAGAGTTTTTTCAGCACGTTGAAGTCGGCATGTTTTTATTCCCGTCAGTTTAAGGACATTGACGAATTAGAACGGGCGATACATGACTATATTCGTTATTATAACGAGGAGCGCATTAAGCCTAAATTAAACAATTTGAGCCCTGTGCAGTACAGAGCTCAATATTTAACT","","","8474","MGQDNRRGNCYDNAVIESFFSTLKSACFYSRQFKDIDELERAIHDYIRYYNEERIKPKLNNLSPVQYRAQYLT","","","probable degenerate transposase fragment","Cytoplasm, Extracellular","","
InterPro
IPR001584
Domain
Integrase, catalytic core
PF00665\"[6-69]Trve


","BeTs to 9 clades of COG2801COG name: Putative transposaseFunctional Class: LThe phylogenetic pattern of COG2801 is ---p-----drlbcefgh-n-j---wNumber of proteins in this genome belonging to this COG is","","Residues 19 to 70 match (1e-11) PD:PD467292 which is described as COMPLETE TRANSPOSASE PROTEOME PLASMID ORFB ELEMENT TRANSPOSASE-LIKE ISRSO11-TRANSPOSASE TNIBDELTA1 TNIA ","Thu May 29 17:06:36 2003","","","Thu May 29 17:06:36 2003","Thu May 29 17:07:01 2003","","","Thu May 29 17:07:01 2003","Thu May 29 17:07:01 2003","Thu May 29 17:06:36 2003","Thu May 29 17:06:36 2003","Thu May 29 17:22:03 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00145 is paralogously related to AA02342 (7e-24), AA01444 (7e-24), AA01287 (7e-24), AA01268 (7e-24), AA01077 (7e-24), AA00010 (7e-24) and AA02117 (7e-18).","","","","","","","","","","","","","","1","","","" "AA00146","105396","106004","609","TTGACCCATTCAAATGAAGCGGAATGTATCAAATTATTTGCCAATTCCTACCTTGCCTTGCGGGTGACATTCTTCAACGAATTGGATACCTTTGCCGCAACGCACGGGTTCAATACGGCGGAGATTATCGAAGGGGTGTCTCTTGATCCGCGTATCGGCACGCATTACAACAATCCGTCTTTCGGTTACGGCGGTTATTGCCTGCCTAAAGACACCAAGCAATTGCTGGCAAACTATAAAGATATTCCGCAAACCCTGATTAGTGCCATTGTGAAATCCAACTCGGTGCGCAAAGATTTCATTGTCGAGGAAGTGTTGAGAAGAAAGCCATCAGTAGTGGGCGTTCATCGTTTAACCATGAAACACGGTTCCGATAATTTCCGTAGCTCCAGCATTCAATACGTGATCAAACGCATCAAAAAAGCGGGTGTGAAAGTGATTATTTACGAACCGGAATATGCTGAAAAAGACTTTTTTGGCTCGGAAGTGGTGACTGATTTAAACGCGTTCAAGCAACAAGCCGATGTCATTCTCGCCAATCGTATGGCGGATGAAATCCTGGATGTGGCGGATAAAGTCTATACCCGCGATATTAAGGGAACGGATTTA","","","22842","LTHSNEAECIKLFANSYLALRVTFFNELDTFAATHGFNTAEIIEGVSLDPRIGTHYNNPSFGYGGYCLPKDTKQLLANYKDIPQTLISAIVKSNSVRKDFIVEEVLRRKPSVVGVHRLTMKHGSDNFRSSSIQYVIKRIKKAGVKVIIYEPEYAEKDFFGSEVVTDLNAFKQQADVILANRMADEILDVADKVYTRDIKGTDL","106004","","UDP-glucose/GDP-mannose dehydrogenase","Cytoplasm","","
InterPro
IPR014026
Domain
UDP-glucose/GDP-mannose dehydrogenase, dimerisation
PF00984\"[4-97]TUDPG_MGDP_dh
InterPro
IPR014027
Domain
UDP-glucose/GDP-mannose dehydrogenase, C-terminal
PF03720\"[114-196]TUDPG_MGDP_dh_C
InterPro
IPR014028
Domain
UDP-glucose/GDP-mannose dehydrogenase, dimerisation and substrate-binding
PTHR11374\"[1-198]TUDP-GLUCOSE DEHYDROGENASE/UDP-MANNAC DEHYDROGENASE
noIPR
unintegrated
unintegrated
G3DSA:1.10.8.220\"[4-90]Tno description
G3DSA:3.40.50.1870\"[96-202]Tno description


","BeTs to 13 clades of COG1004COG name: Predicted UDP-glucose 6-dehydrogenaseFunctional Class: MThe phylogenetic pattern of COG1004 is aom-k--q--rlbcefghs-ujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-48) to 3/8 blocks of the IPB001732 family, which is described as \"UDP-glucose/GDP-mannose dehydrogenase family\". Interpro entry for IP:IPR001732. IPB001732F -1-53 1.1e-22 IPB001732G 62-71 4e-06 IPB001732H 111-151 4.6e-17","Residues 112 to 202 match (1e-27) PD:PD005757 which is described as DEHYDROGENASE UDP-GLUCOSE OXIDOREDUCTASE NAD 6-DEHYDROGENASE PROTEOME COMPLETE UDPGDH UDP-GLC UDP-GLCDH ","","","","","Wed Feb 19 07:09:55 2003","","","","","","","Tue Dec 3 14:09:32 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00146 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 114 to 201 (E-value = 6e-07) place AA00146 in the UDPG_MGDP_dh_C family which is described as UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain (PF03720)","","","","","Drummelsmith,J., Amor,P.A. and Whitfield,C.Polymorphism, duplication, and IS1-mediated rearrangement in thechromosomal his-rfb-gnd region of Escherichia coli strains withgroup IA and capsular K antigensJ. Bacteriol. 179 (10), 3232-3238 (1997)PubMed: 9150218 Wang,L., Huskic,S., Cisterne,A., Rothemund,D. and Reeves,P.R.The O-antigen gene cluster of Escherichia coli O55:H7 andidentification of a new UDP-GlcNAc C4 epimerase geneJ. Bacteriol. 184 (10), 2620-2625 (2002)PubMed: 11976290Dougherty BA, van de Rijn I.Molecular characterization of hasB from an operon required for hyaluronic acid synthesis in group A streptococci. Demonstration of UDP-glucose dehydrogenase activity.J Biol Chem. 1993 Apr 5;268(10):7118-24.PMID: 8463246 ","","Wed Feb 19 07:09:55 2003","1","","","" "AA00148","107903","106095","1809","ATGACTGAAACTAAAATGACTTTCATGGATTTAGGCTTGCCTGAATTCATCCTTAATGCTGTTTCCGATCTGGGTTTTCAAACTCCTTCTCCGATTCAACAAATTTGCATACCGCACTTATTAGAAGGGCGTGACGTACTGGGTATGGCGCAAACCGGTAGCGGCAAAACAGCGGCATTTGCGTTACCGATTTTGGCGAAAATTGATCCTAATGAAAAACATCCGCAATTATTGGTGATGGCACCGACCCGTGAGCTGGCAATTCAGGTTGCTGACGCCTGCGAACAATTTATGAAATATGCCAAAGGCATCAATATCGTGACCTTATATGGCGGTCAACGTTATGACATTCAATTACGCGCGCTCAAACAAGGCGCACAAGTGGTGGTGGGAACACCGGGACGTATTCTGGATCATATTCGTCGCGGCACATTAAATCTGGCGGAACTCAAAGCCATTGTATTGGATGAAGCGGACGAAATGTTGCGTATGGGCTTTATTGAAGATGTGGAAACCGTGATGGCGGAACTGCCTGAACACCACCAAACCGCCTTATTCTCCGCCACCATGCCGGAACCGATTCGTCGCATTACCAAGCGCTTCATGAAAGATCCGCAGGAAATCAAAATCAAAGCGACTCAGCAAAGTGCGCCGGATATTGCGCAAAGTTGTTGGTATGTGCATGGCTTCCGTAAAAACGATGCCTTATTGCGTTTCCTTGAAGTGGAGGATTTTGATGCAGCGATTATTTTCACCCGTACCAAAACCGGCACTTTGGACGTGACGGAATTACTGGAAAAACACGGTTTCCGTGCCGCCGCATTAAACGGCGACATGACTCAACAATTGCGTGAACAAACCCTTGACCGTTTGCGTAGTGGTAGTTTAGATATTGTTGTTGCTACTGATGTGGCGGCGCGCGGTATTGATATTGAACGTATCAGTCTTGTGGTTAACTACGATATTCCGCTGGATGCCGAATCCTATGTTCACCGTATCGGACGTACCGGCCGTGCAGGACGCTCCGGTCGGGCGTTATTGTTCGTTGAACCACGTGAACGCCGTTTGCTGCGCAATGTTGAGCACCTTATCAAGAAAAACATTGAAGAAGTGGAACTGCCAAATCATGAAGTGCTGCAAGCCTGTCGTCGTAAAAAATTCAAAGACAAAATTACCACTCAGTTGGAACATCATGATTTAGAGCTTTACCGTCAATTGCTGGAAGACATGTTCACGGCAGATCAATCGCAGGAAGACATTGCGGCGGCAATGATGATGTTGTTGCAGGGCAAACAAAAACTGATTCTCCCACCGGATCCGGTCGTAGAGAAAAAAGCCCGTCGTGAACGTGGTGAGCGTGGCGAGCGTGGCGATCGTCGTGAAAATCCGCGTTCGGCGGAGCGTCGCGGGGAACGCAAAGGCTATGGTACGCCGCAACCGATGGATTTATACCGTATCGAAGTCGGGCGTGGCGATGGCGTGGAAGTGCGTCATATCGTCGGCGCCATTGCCAATGAAGGGGATATTAACAGCCGTTATATCGGCCATATCAAACTTTATGACGATTATTCCACCATTGAATTGCCGCAAGGTATGCCGAAAGAATTGTTACAGCAGTTCGGCAAGACCCGCGTGTTGAATAAACAAATGCGTATGTCTTTCATCGGCGAAGCCAAAGGCGAACGAGGCGGCGATAACTTCGGCGGCAAACGTCGCGGCGGACGTTTTGAAGACAACGGCTTTAAAGGCGAGCGTAAATTTAAAGAAAAAACGCACCGCACTTTTAAAGAAAAACGCGAGTTCAGAAAA","","","68594","MTETKMTFMDLGLPEFILNAVSDLGFQTPSPIQQICIPHLLEGRDVLGMAQTGSGKTAAFALPILAKIDPNEKHPQLLVMAPTRELAIQVADACEQFMKYAKGINIVTLYGGQRYDIQLRALKQGAQVVVGTPGRILDHIRRGTLNLAELKAIVLDEADEMLRMGFIEDVETVMAELPEHHQTALFSATMPEPIRRITKRFMKDPQEIKIKATQQSAPDIAQSCWYVHGFRKNDALLRFLEVEDFDAAIIFTRTKTGTLDVTELLEKHGFRAAALNGDMTQQLREQTLDRLRSGSLDIVVATDVAARGIDIERISLVVNYDIPLDAESYVHRIGRTGRAGRSGRALLFVEPRERRLLRNVEHLIKKNIEEVELPNHEVLQACRRKKFKDKITTQLEHHDLELYRQLLEDMFTADQSQEDIAAAMMMLLQGKQKLILPPDPVVEKKARRERGERGERGDRRENPRSAERRGERKGYGTPQPMDLYRIEVGRGDGVEVRHIVGAIANEGDINSRYIGHIKLYDDYSTIELPQGMPKELLQQFGKTRVLNKQMRMSFIGEAKGERGGDNFGGKRRGGRFEDNGFKGERKFKEKTHRTFKEKREFRK","106095","","ATP-dependent RNA helicase","Cytoplasm","","
InterPro
IPR000629
Domain
ATP-dependent helicase, DEAD-box
PS00039\"[154-162]TDEAD_ATP_HELICASE
InterPro
IPR001114
Family
Adenylosuccinate synthetase
SM00788\"[106-349]Tno description
InterPro
IPR001650
Domain
Helicase, C-terminal
PF00271\"[264-340]THelicase_C
SM00490\"[259-340]THELICc
PS51194\"[232-379]THELICASE_CTER
InterPro
IPR005580
Domain
DbpA, RNA-binding
PF03880\"[469-556]TDbpA
InterPro
IPR011545
Domain
DEAD/DEAH box helicase, N-terminal
PF00270\"[30-197]TDEAD
InterPro
IPR014001
Domain
DEAD-like helicases, N-terminal
SM00487\"[25-223]TDEXDc
InterPro
IPR014014
Domain
DEAD-box RNA helicase Q motif
PS51195\"[6-34]TQ_MOTIF
InterPro
IPR014021
Domain
Helicase superfamily 1 and 2 ATP-binding
PS51192\"[37-208]THELICASE_ATP_BIND_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[6-210]T\"[217-380]Tno description
PTHR10967\"[2-483]TDEAD BOX ATP-DEPENDENT RNA HELICASE
PTHR10967:SF51\"[2-483]TATP-DEPENDENT RNA HELICASE


","No hits to the COGs database.","Significant hit ( 1.3e-88) to 5/5 blocks of the IPB000629 family, which is described as \"ATP-dependent helicase, DEAD-box\". Interpro entry for IP:IPR000629. IPB000629A 25-68 1.3e-29 IPB000629B 78-90 8.9e-07 IPB000629C 127-138 6.5e-05 IPB000629D 150-173 6.9e-11 IPB000629E 302-343 4e-31","Residues 65 to 307 match (3e-07) PD:PD035480 which is described as HELICASE MG308 RNA-BINDING PROBABLE PROTEOME COMPLETE ATP-BINDING RNA HOMOLOG H08_ORF409 ","","","","","","","","","","","","Tue Dec 3 14:23:40 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00148 is paralogously related to AA00506 (2e-69), AA00263 (2e-69), AA00927 (4e-19), AA02480 (1e-08), AA02303 (3e-06) and AA01928 (8e-06).","","","","","","Residues 469 to 556 (E-value = 3.1e-42) place AA00148 in the DbpA family which is described as DbpA RNA binding domain (PF03880)","","","","","Peng,H.L., Hsieh,M.J., Zao,C.L. and Chang,H.Y. Nucleotide sequence and expression in Escherichia coli of theKlebsiella pneumoniae deaD gene. J. Biochem. 115(3): 409-414.1994. PubMed: 8056751. Toone,W.M., Rudd,K.E. and Friesen,J.D. deaD, a new Escherichia coli gene encoding a presumedATP-dependent RNA helicase, can suppress a mutation in rpsB, thegene encoding ribosomal protein S2. J. Bacteriol. 173(11): 3291-3302.1991 PubMed: 2045359.","","Tue Dec 3 14:23:40 2002","1","","","" "AA00150","108917","108018","900","ATGACACAACGTCGGTTGTTTAATTTCACGGTATTTCTACCTGGTTTATTTTTCACTTTGCTGCTGTCCGGTTGTGTCGGAACCAATCAAAGCTTTGTGTCTAAAAATTCTGTGGTATTGGCCGATCAAAATCCTGCTCAACATTTTGAACAGGAAGTGATGATTGTTCGGATTAGCCAAGTTTTGCTGGTTGGAAAAATGAGTAATGAAGAACGTGCCGCCCTGCATTTTGAACGGGGTGTGCTTTACGATAGTTTGGGGCTTTGGGCTTTAGCACGTTATGATTTTACTCAGGCTCTTGCACTGCAACCGAAAATGACCGCGGTGTATAACTATTTGGGACTTTATTTATTACTTGATGAAGATTACGATGGGGCTTTGGAAGCATTTAATGCTGTGCTTAGCTTAGATCCCGACTATGAATATACGATGTTAAATCGTGCTTTGGATTTCTATTATGTGGGGCGTTATAACCTTGCCCAGCAGGATTTTCTGAGTTTCTATCAACGCAATAAATCCGATCCCTACCGTGTTTTATGGCTGTATTTGAATGAATTAAGATTCAAGCCCGACGAAGCACAAAAAAATCTGGCTCAACGTGCAATTGGGCTTTCTCATGATTATTGGGGTACCTACATTGTCCAATACTATTTGGGCAAACTTTCAGTACGGGAATTACAGGCTAAAGCGGAGCAGTTTTCCAAGCAAACTTCGACGCAATATGCGGAAATTCTTACTGAAACCTACTTTTATCTGGCAAAACAAAAACTCAATATGGGGCAGGTTGATGAGGCGGAGACCTTATTAAAACTGGCTATTGCAAATCAGGTGTATAACTTTGTGGAGTATCGTTTTGCGGTGTTTGAGCTACTGAAATTAGGACAACAGGTTCAAACGGAA","","","34877","MTQRRLFNFTVFLPGLFFTLLLSGCVGTNQSFVSKNSVVLADQNPAQHFEQEVMIVRISQVLLVGKMSNEERAALHFERGVLYDSLGLWALARYDFTQALALQPKMTAVYNYLGLYLLLDEDYDGALEAFNAVLSLDPDYEYTMLNRALDFYYVGRYNLAQQDFLSFYQRNKSDPYRVLWLYLNELRFKPDEAQKNLAQRAIGLSHDYWGTYIVQYYLGKLSVRELQAKAEQFSKQTSTQYAEILTETYFYLAKQKLNMGQVDEAETLLKLAIANQVYNFVEYRFAVFELLKLGQQVQTE","108018","","conserved hypothetical protein (possible TPR domain protein)","Outer membrane, Cytoplasm","","
InterPro
IPR011990
Domain
Tetratricopeptide-like helical
G3DSA:1.25.40.10\"[31-296]Tno description
InterPro
IPR013026
Domain
Tetratricopeptide region
SM00028\"[73-106]T\"[107-140]T\"[246-279]TTPR
PS50005\"[73-106]T\"[107-140]T\"[246-279]TTPR
PS50293\"[73-174]TTPR_REGION
InterPro
IPR013105
Repeat
Tetratricopeptide TPR_2
PF07719\"[73-106]T\"[107-140]TTPR_2
noIPR
unintegrated
unintegrated
PTHR23083\"[69-164]TTETRATRICOPEPTIDE REPEAT PROTEIN, TPR
PTHR23083:SF20\"[69-164]TTETRATRICOPEPTIDE REPEAT PROTEIN, TPR
PS51257\"[1-25]TPROKAR_LIPOPROTEIN
signalp\"[1-27]?signal-peptide
tmhmm\"[9-27]?transmembrane_regions


","BeTs to 7 clades of COG0457COG name: TPR-repeat-containing proteinsFunctional Class: RThe phylogenetic pattern of COG0457 is aompk-yqvd-lbcefghsnujxit-Number of proteins in this genome belonging to this COG is","","Residues 100 to 167 match (1e-09) PD:PD471788 which is described as COMPLETE REPEAT LIPOPROTEIN PROTEOME DIVISION MEMBRANE HOMOLOG NLPI PM1113 SIGNAL ","","","","","","","","","","","","Tue Dec 3 14:38:12 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00150 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 107 to 140 (E-value = 8.8e-06) place AA00150 in the TPR family which is described as TPR Domain (PF00515)","","","","","","","","1","","","" "AA00151","111131","109005","2127","GTGAATCCAATTGTTAAACAGTTTAAATACGGTCAACATACCGTAACCTTAGAAACCGGTGCGATCGCCCGTCAAGCAACCGCAGCGGTCATGGCAAGCATGGACGATACGACCGTATTCGTGACTGTGGTTGCTAAAAAAGATGTGAAAGAAGGTCAGGATTTCTTCCCATTGACCGTTAATTATCAAGAGCGTACTTATGCCGCCGGTCGCATTCCCGGCGGTTTCTTCAAACGCGAAGGTCGTCCGTCCGAAGGCGAAACCTTAATTGCCCGTTTAATCGACCGTCCGATTCGTCCGTTATTCCCGGAAGGGTTTTTCAACGAAATTCAAGTGGTTGCCACCGTGGTATCGGTAAATCCGCAAATCAGCCCGGATTTAGTGGCAATGATCGGTGCGTCCGCCGCGTTATCTTTATCCGGTGTGCCGTTTAATGGTCCGATCGGTGCAGCGCGTGTGGGTTTTATTAACGGTCAATTCGTGCTAAACCCAACCATGAACGAGCAAAAACAAAGCCGTTTGGATTTAGTGGTGGCGGGTACCGATAAAGCCGTGTTAATGGTGGAATCCGAAGCGGATATTTTAACCGAAGAACAAATGTTGGCGGCGGTGGTTTATGGTCATCAGCAACAACAAGTGGTCATTGAGGCCATCAAAGAACTCGTTGCCGAAGCGGGCAAACCGCGTTGGGATTGGGTTGCGCCTGAACCGAACACGGCGTTAATTAACAAAGTGAAAGCGTTGGCGGAAGCCCGTTTAGGCGATGCCTATCGTATCACCGAAAAACAATCCCGCTATGAGCAAATCGATGCTATTAAAGCGGATGTGATTGCACAAATCACCGCTGAAGACGAAGAGGTTAGCGAGGGTAAAATTATTGATATTTTCACCGCACTTGAAAGTCAAATCGTGCGTGGCCGCATTATCGCAGGCGAACCGCGTATCGATGGCCGTACTGTTGACACCGTGCGTGCATTGGATATTTGCACCGGCGTATTACCGCGTACCCACGGCTCCGCGATTTTTACCCGTGGTGAAACCCAAGCCTTGGCGGTGGCGACTTTAGGTACCGAGCGTGATGCGCAAATTATTGATGAATTGACCGGCGAACGTTCCGATCATTTCCTATTCCACTATAACTTCCCGCCGTACTCCGTGGGTGAAACCGGTATGATCGGTTCACCGAAACGTCGTGAAATCGGTCATGGTCGTTTGGCAAAACGCGGTGTGGCGGCAGTTATGCCAACTTTGGCTGAATTTCCTTATGTGGTTCGTGTGGTATCCGAAATCACCGAATCGAACGGTTCTTCTTCTATGGCGTCCGTATGTGGTGCTTCTCTTGCCTTAATGGATGCCGGTGTGCCGATTAAAGCGGCAGTAGCAGGTATCGCCATGGGTTTGGTGAAAGAAGAGGATAAATTTGTAGTGCTTTCCGATATTCTTGGCGATGAAGATCACTTAGGTGATATGGACTTCAAAGTTGCCGGTACCCGTGAAGGCGTGACTGCGTTGCAAATGGATATCAAAATTGAAGGCATCACTGCAGAAATTATGCAAATTGCCCTGAATCAGGCGAAAAGTGCGCGTATGCACATTCTTGGCGTGATGGAACAAGCGATTCCGGCACCACGTGCGGATATTTCCGATTTTGCACCGCGTATTTACACTATGAAGATCGATCCGAAGAAAATCAAAGATGTTATCGGTAAAGGCGGTGCGGTTATTCGTGTGCTGACCGAAGAAACCGGCACTTCCATTGATATTGATGACGATGGTACGGTGAAAATTGCTGCGGTAGATAAAAATGCAGTGCAGGATGTAATGGCACGCATTGAAGACATCACTGCCGAAGTGGAAGTCGGCGCAACTTACAAAGGTAAAGTCATCCGTTTGGCGGATTTTGGCGCGTTTGTGGCAATCGTCGGTAACAAAGAAGGTTTAGTTCATATTTCACAAATCGCTGAAGAACGTGTGGAAAAAGTGAGCGATTATCTACAAGTAGGACAAGAAGTGATGGTGAAAGTGGTCGAAATCGATCGCCAGGGTCGTATCCGTTTAACTATGAAAGACCTTGTGCCTAAACAAGATACTGTTCAACAACCTGCCGACAACCTTTTTGAACAGGAG","","","81721","VNPIVKQFKYGQHTVTLETGAIARQATAAVMASMDDTTVFVTVVAKKDVKEGQDFFPLTVNYQERTYAAGRIPGGFFKREGRPSEGETLIARLIDRPIRPLFPEGFFNEIQVVATVVSVNPQISPDLVAMIGASAALSLSGVPFNGPIGAARVGFINGQFVLNPTMNEQKQSRLDLVVAGTDKAVLMVESEADILTEEQMLAAVVYGHQQQQVVIEAIKELVAEAGKPRWDWVAPEPNTALINKVKALAEARLGDAYRITEKQSRYEQIDAIKADVIAQITAEDEEVSEGKIIDIFTALESQIVRGRIIAGEPRIDGRTVDTVRALDICTGVLPRTHGSAIFTRGETQALAVATLGTERDAQIIDELTGERSDHFLFHYNFPPYSVGETGMIGSPKRREIGHGRLAKRGVAAVMPTLAEFPYVVRVVSEITESNGSSSMASVCGASLALMDAGVPIKAAVAGIAMGLVKEEDKFVVLSDILGDEDHLGDMDFKVAGTREGVTALQMDIKIEGITAEIMQIALNQAKSARMHILGVMEQAIPAPRADISDFAPRIYTMKIDPKKIKDVIGKGGAVIRVLTEETGTSIDIDDDGTVKIAAVDKNAVQDVMARIEDITAEVEVGATYKGKVIRLADFGAFVAIVGNKEGLVHISQIAEERVEKVSDYLQVGQEVMVKVVEIDRQGRIRLTMKDLVPKQDTVQQPADNLFEQE","109005","","polynucleotide phosphorylase","Cytoplasm","","
InterPro
IPR001247
Domain
Exoribonuclease
PF01138\"[11-143]T\"[322-455]TRNase_PH
PF03725\"[146-210]T\"[458-528]TRNase_PH_C
PF03726\"[241-319]TPNPase
InterPro
IPR003029
Domain
RNA binding S1
PF00575\"[617-689]TS1
SM00316\"[619-689]TS1
PS50126\"[621-689]TS1
InterPro
IPR004087
Domain
KH
SM00322\"[551-616]TKH
InterPro
IPR004088
Domain
KH, type 1
PF00013\"[554-611]TKH_1
PS50084\"[552-611]TKH_TYPE_1
InterPro
IPR012162
Family
Polyribonucleotide nucleotidyltransferase
PIRSF005499\"[2-703]TPolyribonucleotide nucleotidyltransferase
PTHR11252\"[144-693]TPOLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[616-691]Tno description
noIPR
unintegrated
unintegrated
G3DSA:1.10.10.400\"[236-318]Tno description


","BeTs to 17 clades of COG1185COG name: Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase)Functional Class: JThe phylogenetic pattern of COG1185 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 5.9e-06) to 2/9 blocks of the PR00681 family, which is described as \"Ribosomal protein S1 signature\". Prints database entry for PR:PR00681. PR00681A 461-479 54 PR00681H 634-653 5.2e-05","Residues 546 to 608 match (1e-12) PD:PD023173 which is described as NUCLEOTIDYLTRANSFERASE COMPLETE PROTEOME POLYRIBONUCLEOTIDE TRANSFERASE POLYNUCLEOTIDE PHOSPHORYLASE PNPASE RNA-BINDING GUANOSINE ","","","","","","","","","","","","Wed Dec 4 08:18:21 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00151 is paralogously related to AA02528 (1e-10), AA00939 (3e-09) and AA01062 (4e-04).","","","","","","Residues 617 to 689 (E-value = 1.2e-24) place AA00151 in the S1 family which is described as S1 RNA binding domain (PF00575)","","","","","Jarrige A, Brechemier-Baey D, Mathy N, Duche O, Portier C. Mutational analysis of polynucleotide phosphorylase fromEscherichia coli. J Mol Biol. 2002 Aug 16;321(3):397-409. PMID: 12162954 Regnier,P., Grunberg-Manago,M. and Portier,C. Nucleotide sequence of the pnp gene of Escherichia coli encodingpolynucleotide phosphorylase. Homology of the primary structure ofthe protein with the RNA-binding domain of ribosomal protein S1.J. Biol. Chem. 262(1): 63-68.1987. PubMed: 2432069. Evans,S. and Dennis,P.P. . Promoter activity and transcript mapping in the regulatory regionfor genes encoding ribosomal protein S15 and polynucleotidephosphorylase of Escherichia coli. Gene 40(1): 15-22.1985 PubMed: 3005122. Portier,C. and Regnier,P. . Expression of the rpsO and pnp genes: structural analysis of a DNAfragment carrying their control regions. Nucleic Acids Res. 12(15): 6091-6102.1984 PubMed: 6382163.","","Wed Dec 4 08:18:21 2002","1","","","" "AA00153","111425","111892","468","ATGATTATAGGAGATCTTACCCGCGCAGATGTAAAATTAGGCTTACCGCCCGTTATTGCACAAATCTGTGACTATTTAAACGGCTTGGACTTAACCGCGTTAACCAACGGACGCCATAACATTACCGACCAAATTTACATGAACGTTATGGAATTTGACACCGCCCCGGCAGACAGCAAACAAGCGGAACTGCACCACAAATATTTAGATGTACAAGTATTAATCAGCGGCGCCGAAAGTATTGATTACAGCGTGACCCACCCTGATTTAAACCAATACACCGATTACAACGATGCCGACGACTATCAACTTTGCCCGATCATCGAACAGCAAAATACTCTAACCTTAAGGCCGAAAATGTTCGTGGTATTTTATCCGTACGAACCGCACCGCCCGGGTTGTAACGTCAACGGACAAACGGTTAAATTAAAAAAACTGGTGGTGAAAATCCCCGTGGCGTTAATCAAA","","","17587","MIIGDLTRADVKLGLPPVIAQICDYLNGLDLTALTNGRHNITDQIYMNVMEFDTAPADSKQAELHHKYLDVQVLISGAESIDYSVTHPDLNQYTDYNDADDYQLCPIIEQQNTLTLRPKMFVVFYPYEPHRPGCNVNGQTVKLKKLVVKIPVALIK","111892","Similar to YhcH/YiaL/YjgK family, hypothetical proteins from Escherichia col","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR004375
Family
Conserved hypothetical protein 22
PF04074\"[1-153]TDUF386
TIGR00022\"[1-155]TTIGR00022: conserved hypothetical protein
noIPR
unintegrated
unintegrated
G3DSA:2.60.120.370\"[1-155]Tno description


","No hits to the COGs database.","","Residues 1 to 38 match (6e-10) PD:PD537874 which is described as PROTEOME COMPLETE PM1713 ","","","","","","","","","","","Wed Jan 22 15:24:18 2003","Wed Dec 4 08:23:50 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00153 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 153 (E-value = 1.5e-71) place AA00153 in the DUF386 family which is described as Domain of unknown function (DUF386) (PF04074)","","","","","","","","1","","","" "AA00155","112009","111887","123","ATGAAAAACGGCTCACGGATTATTTTACGGTTTTCCGAAATTTATCCACAAACTTATGTACAGTCGGTGAGTAACAAAAAATACCTCAAGAATGGGTTTGAGGTATCTAATGATTTATTTGAT","","","4813","MKNGSRIILRFSEIYPQTYVQSVSNKKYLKNGFEVSNDLFD","111887","","hypothetical protein","Periplasm, Cytoplasm","No similarities were found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sat Feb 21 11:21:08 2004","Sat Feb 21 11:21:08 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00155 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sat Feb 21 11:21:52 2004","","","","","","","","","","","","","1","","","" "AA00156","112162","112073","90","ATGTGGCAAGTCAAATTGAGTGAAAAATTCGTTGGTTATTTGCTAAACAGGATTTGTGCAAAAAATATTAAGGAAAATGAATGGAGCGGC","","","3567","MWQVKLSEKFVGYLLNRICAKNIKENEWSG","112073","","hypothetical protein","Cytoplasm, Extracellular","No similarities were found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sat Feb 21 11:23:04 2004","Sat Feb 21 11:23:04 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00156 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sat Feb 21 11:24:43 2004","","","","","","","","","","","","","1","","","" "AA00157","112259","112384","126","GTGAAATCAGAAGAAAAATTTCCTTTATTCATCAATCAGCTGCTAAAAAAACAACGGCATTTTTCTGTTAATGAAAAATGCCGTTTTATACTGTATATTTATTGTTCAACTCATAAATGTTGCAAA","","","5133","VKSEEKFPLFINQLLKKQRHFSVNEKCRFILYIYCSTHKCCK","112384","","hypothetical protein","Cytoplasm","No similarities were found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sat Feb 21 11:26:40 2004","Sat Feb 21 11:26:40 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences to this sequence are found.AA00157 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sat Feb 21 11:27:55 2004","","","","","","","","","","","","","1","","","" "AA00158","112995","112372","624","TTGCCTAAGGTAAAAAACACCGTAAAATTCCACCGCACTTTTATGGGATCCCGATCGCAAAAAGAAAATCTTATGACGGAAAAACAACGACAAATTAAAGACGGTTGGTTGCTTGATGAAAGACGGGTGCTTTCTCCTCACTTTGACCAACGCCCCGACCCGCAGGACATTTCCCTGTTGATTATTCATTACATCAGTTTGCCGCCGGAACAGTTTGGCGGCGGTTACATTGATGATTTTTTCCAAGGTAAACTGGACGCACAGGCACATCCGTATTTTCAGGAAATCAGTCTGCTGCGGGTGTCGGCACATTGTTTGATTGAGCGCACGGGGCGCATTACGCAATATGTGAATTTTAACGACCGCGCGTGGCACGCGGGACTATCCTATTTTGAAGGACGGGAAAAATGCAATGATTTTGCCATCGGCATTGAATTGGAAGGTAGCAATGAACAGCCGTTTACCACACAGCAATATGACACGCTACAACGCTTAACCCGACAAATTATGCAGGCGTATCCGCGGATTACCAAAGAACGCATTGTAGGGCATTGTGATGTGTCGCCGGGGCGAAAAATCGATCCGGGACAATATTTCGATTGGCAGCGTTATTTGCAACATTTA","","","25333","LPKVKNTVKFHRTFMGSRSQKENLMTEKQRQIKDGWLLDERRVLSPHFDQRPDPQDISLLIIHYISLPPEQFGGGYIDDFFQGKLDAQAHPYFQEISLLRVSAHCLIERTGRITQYVNFNDRAWHAGLSYFEGREKCNDFAIGIELEGSNEQPFTTQQYDTLQRLTRQIMQAYPRITKERIVGHCDVSPGRKIDPGQYFDWQRYLQHL","112372","The primary laboratory evidence is unpublished.","ampD signalling protein (N-acetylmuramyl-L-alanine amidase)","Cytoplasm","","
InterPro
IPR002502
Domain
N-acetylmuramoyl-L-alanine amidase, family 2
PF01510\"[46-207]TAmidase_2
SM00644\"[45-196]TAmi_2
noIPR
unintegrated
unintegrated
G3DSA:3.40.80.10\"[30-208]Tno description


","BeTs to 6 clades of COG3023COG name: Negative regulator of beta-lactamase expressionFunctional Class: MThe phylogenetic pattern of COG3023 is --------------efghsn-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 3e-12) to 3/3 blocks of the IPB002502 family, which is described as \"N-acetylmuramoyl-L-alanine amidase (family 2)\". Interpro entry for IP:IPR002502. IPB002502A 115-127 2.9e-06 IPB002502B 138-147 0.076 IPB002502C 188-206 2.3","Residues 137 to 205 match (7e-28) PD:PD009380 which is described as COMPLETE PROTEOME AMIDASE N-ACETYLMURAMOYL-L-ALANINE AMPD HYDROLASE PROBABLE CELL ANHYDRO-N-ACETYLMURAMYL-TRIPEPTIDE SECRETED ","","","","","","","","","","","Wed Dec 4 08:37:22 2002","Wed Dec 4 08:37:22 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00158 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 46 to 207 (E-value = 1.6e-61) place AA00158 in the Amidase_2 family which is described as N-acetylmuramoyl-L-alanine amidase (PF01510)","","","","","Kopp U, Wiedemann B, Lindquist S, Normark S. Sequences of wild-type and mutant ampD genes of Citrobacterfreundii and Enterobacter cloacae. Antimicrob Agents Chemother. 1993 Feb;37(2):224-8. PubMed: 8383940. (","","Wed Dec 4 08:37:22 2002","1","","","" "AA00160","112976","113494","519","GTGTTTTTTACCTTAGGCAAAATGCCCGCGCCCAATTTGGCACACATTATTTTTTACAAAGGTATTTTTATGAAAATTCAATCCGCGTTTATTTCGCTAAAATTCGTTAAAAAAGGGTTTACATTAATCGAATTAATGATCGTCATCGCTATTGTTGCTATTCTCGCCACCGTAGCCGTACCATCTTATCAAAATTACACTAAAAAAGCGGCGGTTTCCGAATTATTACAAGCCTCCGCCCCATTACGTTCCGAAGTGGAACTCTGTATTTATAACACCGGTAAGGCTGAAAATTGTAGCGGCGGACAAAACGGCATTCAAGCAGATGTTGCAGATGCTTCGAAACAAAAATATGTGAAATCCACTGCGGTCAAAGGCGGCGTCATCACCGTTACCGGCAAAGGCAGTTTGGATAAAATCAGCTACACCCTTACCGCTTCGGGCACGGCTGCCAGCGGGGTCAGCTGGAACGCCGCCTGCGGCAATAATGCCGACATTTTCCCGGCAGGTTTCTGTTCT","","","18943","VFFTLGKMPAPNLAHIIFYKGIFMKIQSAFISLKFVKKGFTLIELMIVIAIVAILATVAVPSYQNYTKKAAVSELLQASAPLRSEVELCIYNTGKAENCSGGQNGIQADVADASKQKYVKSTAVKGGVITVTGKGSLDKISYTLTASGTAASGVSWNAACGNNADIFPAGFCS","113494","","pilA-like biogenesis protein / prepilin peptidase dependent proteinD","Extracellular, Inner membrane","","
InterPro
IPR001082
Family
Fimbrial protein pilin
PD000666\"[61-123]TQ9JRN0_ACTAC_Q9JRN0;
InterPro
IPR001120
PTM
Prokaryotic N-terminal methylation site
PS00409\"[38-58]TPROKAR_NTER_METHYL
InterPro
IPR012902
PTM
Prepilin-type cleavage/methylation, N-terminal
PF07963\"[38-61]TN_methyl
TIGR02532\"[37-60]TIV_pilin_GFxxxE: prepilin-type N-terminal c
noIPR
unintegrated
unintegrated
G3DSA:3.30.700.10\"[39-171]Tno description
tmhmm\"[40-60]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 3.8e-13) to 1/1 blocks of the IPB001120 family, which is described as \"Prokaryotic N-terminal methylation site\". Interpro entry for IP:IPR001120. IPB001120 37-56 4e-13Significant hit ( 3.3e-09) to 1/2 blocks of the PR00813 family, which is described as \"Bacterial general secretion pathway protein G signature\". Prints database entry for PR:PR00813. PR00813A 39-64 3.3e-09Significant hit ( 2.8e-05) to 2/3 blocks of the PR00885 family, which is described as \"Bacterial general secretion pathway protein H signature\". Prints database entry for PR:PR00885. PR00885A 35-49 0.0025 PR00885B 50-64 6.2","Residues 71 to 160 match (5e-13) PD:PD031196 which is described as PEPTIDASE D PREPILIN PROTEOME COMPLETE DEPENDENT METHYLATION HOMOLOG PRECURSOR ","","","","","","","","","","","","Thu Dec 5 10:24:01 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00160 is paralogously related to AA02827 (9e-05).","","","","","","Residues 40 to 173 (E-value = 2.1e-10) place AA00160 in the Pilin family which is described as Pilin (bacterial filament) (PF00114)","","","","Wang,Y., Goodman,S.D., Redfield,R.J. and Chen,C. Natural transformation and DNA uptake signal sequences in Actinobacillus actinomycetemcomitans J. Bacteriol. 184 (13), 3442-3449 (2002) PubMed: 12057937","Doughty,S.W., Ruffolo,C.G. and Adler,B.The type 4 fimbrial subunit gene of pasteurella multocidaVet. Microbiol. 72 (1-2), 79-90 (2000)PubMed: 10699505","Thu Dec 5 10:30:03 2002","Thu Dec 5 10:30:03 2002","1","","","" "AA00161","113524","114930","1407","ATGCAAAATCCGATGGCGCAAGGTTATTTGATTCACAGCCAAAATCACGGGGACTTTACCATTGCGCCCGAGCTATGGCTTAAAAATCAGCAACAACAAACCGTCCTGTTGCGTTATCTCGCCCTGCCCTTAGCAGAAAACGGGCAGACCTTGTGGCTAGGGTTAGACTCGTTAACTAACCTGAGCGCCTGTGAAGCCTTTTCTTTTCTCACCGGCAAAACCATTGAGCCGGTATTAATTGAAAGCCAAACGCTAAAAACCGCATTGCAGGATTTATCCCCGCGCGTCGAAAAAGTCGAAGAAAATCAACCGCTCTTTTATTCCGCACTGTCACAGGAACAGCCGACACAACCGTATGACGAACCGATTATTCGGCTGTTAAATGATATTTTTGAAAGCGCGACGGCACAAAAAGCCTCCGATATTCATCTGGAACCGCAAGCAGACTGCCTGCAAACCCGTTTTCGCATTGACGGCGTGCTGCAGGTGCAAAACACCGTTCCCTTATCCATAGCGAGCCGACTGATTTCTCGTTTAAAATTATTGGCAAAACTGGATATTAGCGAAACCCGCCTGCCGCAAGACGGACGCTTTCAGTTTAAAACGACGTTTTCCGACACGCTGGATTTTCGCCTTTCCACCCTTGCCACCCAATTCGGTGAAAAAGCGGTCCTGCGTTTGCAACAAAATCGTCCCGTGCAACTGGCATTCGGTGAACTGGGCATGACGGAATCACAGCAACAGCGTTTTCGTCGTGCCTTGAGCCAACCACAAGGCTTGATTTTAGTCACCGGTCCGACAGGCAGCGGCAAAAGTATTTCTTTATATACGGCGTTGCAGTACTTAAATACGTCTGAAAAACACATTATGACGGCGGAAGATCCCATTGAAATTCAGCTCCCAGGCATTATTCAAAGCCAAGTGAATCACCCTATCGGCTTGGATTTCAGCCGATTGCTTCGCACCTTTTTACGCCAAGATCCGGACATTATTATGTTAGGTGAAATTCGTGATGAAGAAAGTGCCGCCATGGCATTACGCGCCGCGCAAACGGGGCATTTGGTGCTTTCGACGCTACATACCAACGACGCCCCTTCCGCCATTTCCCGCCTGCAACAACTCGGCATTCAACGCCATGAAATCGACGGCAGTTTGTTGCTGGTGATCGCCCAACGTTTGGTGCGCAAACGCTGCCAAAAGTGCGGTGGAAATGCCACGCGTTTTTGCGATTGCCATCAAGGCTACAAAGGGCGTGTCGGGGTCTATCAATTCCTGCAACCGAATTTACAACATCCGCAGGGCTATGAAACGGATTTCGCCGATTTAGGCCAAAGCGCTTTAGAAAAACTCAAAGACGGCACAACAGATTTAACCGAAATCCAACGGGTGTTAGGACAAACTCATGAT","","","52539","MQNPMAQGYLIHSQNHGDFTIAPELWLKNQQQQTVLLRYLALPLAENGQTLWLGLDSLTNLSACEAFSFLTGKTIEPVLIESQTLKTALQDLSPRVEKVEENQPLFYSALSQEQPTQPYDEPIIRLLNDIFESATAQKASDIHLEPQADCLQTRFRIDGVLQVQNTVPLSIASRLISRLKLLAKLDISETRLPQDGRFQFKTTFSDTLDFRLSTLATQFGEKAVLRLQQNRPVQLAFGELGMTESQQQRFRRALSQPQGLILVTGPTGSGKSISLYTALQYLNTSEKHIMTAEDPIEIQLPGIIQSQVNHPIGLDFSRLLRTFLRQDPDIIMLGEIRDEESAAMALRAAQTGHLVLSTLHTNDAPSAISRLQQLGIQRHEIDGSLLLVIAQRLVRKRCQKCGGNATRFCDCHQGYKGRVGVYQFLQPNLQHPQGYETDFADLGQSALEKLKDGTTDLTEIQRVLGQTHD","114930","primary laboratory evidence unpublished.","pilin B biogenesis protein; fimbrial transcription regulation","Cytoplasm, Outer membrane","","
InterPro
IPR001482
Domain
Bacterial type II secretion system protein E
PD000739\"[232-329]TGSPII_E
PF00437\"[118-397]TGSPII_E
PS00662\"[324-338]TT2SP_E
InterPro
IPR007831
Domain
General secretory system II, protein E, N-terminal
PF05157\"[5-99]TGSPII_E_N
noIPR
unintegrated
unintegrated
G3DSA:3.30.450.90\"[91-229]TG3DSA:3.30.450.90
G3DSA:3.40.50.300\"[230-463]TG3DSA:3.40.50.300
SSF52540\"[100-464]TSSF52540


","BeTs to 13 clades of COG2804COG name: Predicted ATPases involved in pili biogenesis, PilB homologsFunctional Class: NThe phylogenetic pattern of COG2804 is -------qvd-lbcefghsnuj-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.7e-70) to 5/5 blocks of the IPB001482 family, which is described as \"Bacterial type II secretion system protein E\". Interpro entry for IP:IPR001482. IPB001482A 139-161 3.2e-08 IPB001482B 257-279 1.8e-14 IPB001482C 288-298 4.4e-05 IPB001482D 320-364 1.4e-33 IPB001482E 414-423 0.0018","Residues 237 to 401 match (5e-09) PD:PD555210 which is described as E PROTEOME PATHWAY GENERAL COMPLETE SECRETION ","","","","","","","","","","","Wed Dec 4 08:58:48 2002","Thu Jan 23 08:00:02 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00161 is paralogously related to AA00874 (2e-10).","","","","","","Residues 118 to 397 (E-value = 1.8e-126) place AA00161 in the GSPII_E family which is described as Type II/IV secretion system protein (PF00437)","","","","Wang,Y., Goodman,S.D., Redfield,R.J. and Chen,C. Natural transformation and DNA uptake signal sequences in Actinobacillus actinomycetemcomitans J. Bacteriol. 184 (13), 3442-3449 (2002) PubMed: 12057937","Sauvonnet N, Gounon P, Pugsley AP. PpdD type IV pilin of Escherichia coli K-12 can Be assembled intopili in Pseudomonas aeruginosa. J Bacteriol. 2000 Feb;182(3):848-54. PMID: 10633126 Lowther WT, Weissbach H, Etienne F, Brot N, Matthews BW. The mirrored methionine sulfoxide reductases of Neisseriagonorrhoeae pilB. Nat Struct Biol. 2002 May;9(5):348-52. PMID: 11938352 Olry A, Boschi-Muller S, Marraud M, Sanglier-Cianferani S, VanDorsselear A, Branlant G. Characterization of the methionine sulfoxide reductase activitiesof PILB, a probable virulence factor from Neisseria meningitidis. J Biol Chem. 2002 Apr 5;277(14):12016-22. PMID: 11812798 ","Wed Dec 4 08:58:48 2002","Fri Dec 6 14:39:55 2002","1","","","" "AA00162","114926","116146","1221","ATGATTAAATTGAAACTGTTTCAACGGCGCGCCGTTAATCGACTACAGCAAAAACAAAAAGGCTTAATCGTGGCGGAAACGGAGGCGATGGCACAACAACAGCTGCTTTCATGCGGGTTGCAAAACATCAAATTACAACAAAACTGGCAATTTAGCCACAAACCGAAAAATGCCGACATCTGCACGCTGCTTTCCCAACTGGCGACGCTGTTACAAGCCGCCGTGCCGCTGAAAAACAGCCTGCAAATTTTATTGCAAAATTGTACCAATATTGCGTTGAATCGCTGGCTACGCTGCTTGCTACAGGAGATTGAAAGCGGCTTAGCATTTTCTCAAGCATTGGAACAACAAGGTTTATACTTAACCTATCAGGAACGCCAACTGATTCAGGTGGGTGAAATGACAGGCAAACTTGCCGCCGTTTGTCATGAAATCGCACAACATAAACAACAGGCGCTGGCGTTGCAGCGTAAAATTCAGAAAATCCTGCTTTATCCGTTGCTGGTGCTCGGAATCTCATTGATTTTGACCGCACTTTTATTGCTGTTCATCGTGCCGCAATTTGCCGCCATGTATGACAACAGCAACGCGCAACTGCCCGTGTTCACGCAGGTTTTACTAGCCCTTTCCCAAGGCTTGCAGGGTTATTGGTTCGCGCTGCTCATGTTTATTGCGCTGACCGTGGCGTTAATTCGCTTTCGCCTCAAACATTCGCCTTGGCTTAACCGACAAAAAAACCGGCTGATTAACAGTATTCCGCTACTTAATCGTATCGTACAACTCTCCCGTTTAGTGGGATTCAGTCACAGCTTGTTTTTGATGTTACAGGCAGGTATTCCGCTGAATCAGGCGCTACAATCTTTCCTACCGAAACAACAAAGCTGGCAAACTAAACCGCAGCAGCAAGGGGATTGGCTGCTTATTGCGGGAGTGCAATCGGCACTGCATTGGATTCAACAAGGCTATCCGTTCTCCGCCAGCGTAAGCGGACAAATCTTCCCGCCGGCGGCACAACAAATGCTGCAAGTCGGCGAACAAAGCGGTCAATTGCCGAAAATGCTGCAATTTATCGCCAACGATCATCAGCAACAATTGGATCACCAAATCGATCTACTGTCACAAATGCTGGAACCGTTGTTGATGGTAATTATCGGCGGGCTGATCGGCTTGATTATGCTCGGTATGTATTTACCGATTTTCAACATGGGCTCGCTGGTACAA","","","45933","MIKLKLFQRRAVNRLQQKQKGLIVAETEAMAQQQLLSCGLQNIKLQQNWQFSHKPKNADICTLLSQLATLLQAAVPLKNSLQILLQNCTNIALNRWLRCLLQEIESGLAFSQALEQQGLYLTYQERQLIQVGEMTGKLAAVCHEIAQHKQQALALQRKIQKILLYPLLVLGISLILTALLLLFIVPQFAAMYDNSNAQLPVFTQVLLALSQGLQGYWFALLMFIALTVALIRFRLKHSPWLNRQKNRLINSIPLLNRIVQLSRLVGFSHSLFLMLQAGIPLNQALQSFLPKQQSWQTKPQQQGDWLLIAGVQSALHWIQQGYPFSASVSGQIFPPAAQQMLQVGEQSGQLPKMLQFIANDHQQQLDHQIDLLSQMLEPLLMVIIGGLIGLIMLGMYLPIFNMGSLVQ","116146","unpublished primary laboratory evidence.","pilin C biogenesis protein/protein transport protein","Inner membrane, Cytoplasm","","
InterPro
IPR001992
Family
Bacterial type II secretion system protein
PF00482\"[63-186]T\"[267-398]TGSPII_F
PS00874\"[158-186]TT2SP_F
InterPro
IPR003004
Family
Bacterial general secretion pathway protein F
PR00812\"[59-71]T\"[158-186]T\"[371-385]T\"[387-406]TBCTERIALGSPF
noIPR
unintegrated
unintegrated
tmhmm\"[162-184]?\"[213-233]?\"[380-400]?transmembrane_regions


","BeTs to 10 clades of COG1459COG name: General secretory pathway protein FFunctional Class: NThe phylogenetic pattern of COG1459 is -------qvd-lbcefghsn-j-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 2.2e-41) to 3/3 blocks of the IPB001992 family, which is described as \"Bacterial type II secretion system protein\". Interpro entry for IP:IPR001992. IPB001992A 63-77 4.4e-05 IPB001992B 146-200 9e-25 IPB001992C 333-350 1.2e-08 IPB001992A 267-281 0.045","Residues 150 to 213 match (1e-08) PD:PD373915 which is described as COMPLETE PROTEOME ASSEMBLY PILC TRANSMEMBRANE TYPE MEMBRANE INNER PILUS FIMBRIAL ","","","","","","","","","","","Wed Dec 4 09:05:50 2002","Wed Dec 4 09:04:09 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00162 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 265 to 398 (E-value = 7.9e-22) place AA00162 in the GSPII_F family which is described as Bacterial type II secretion system protein F domain (PF00482)","","","","Wang,Y., Goodman,S.D., Redfield,R.J. and Chen,C. Natural transformation and DNA uptake signal sequences in Actinobacillus actinomycetemcomitans J. Bacteriol. 184 (13), 3442-3449 (2002) PubMed: 12057937","Sauvonnet N, Gounon P, Pugsley AP. PpdD type IV pilin of Escherichia coli K-12 can Be assembled intopili in Pseudomonas aeruginosa. J Bacteriol. 2000 Feb;182(3):848-54. PMID: 10633126 ","Wed Dec 4 09:04:09 2002","Wed Dec 4 09:04:09 2002","1","","","" "AA00163","116146","116832","687","ATGATGTGGCTACTTTTTTTGCTTGGTGGCGCACTATGCGGGTGGCGTGTTCATCGTTATGTAGAACATTTCGCCGATAACCTCAGCCGCGAGGTTCATGCCGCCTACACGGAAATTTACCCGCAAAACCCACCGCACTTTACAGCGGAAAAGTCGATTCTGAAACCGCTTAAACGGCATTTTTCCGCGCCCCTTTACAGCCTTTTATTCACCTTGCTGTTCATTATTTGTTATGCCATCAATGAACCGTTACAAGCCCTATGCTTTGCCCTTTATGGCGCCTTATTAATTGCCATTTCCCTAGTGGATTGGCACTATCGCTTGATTTCACCCGCCTTATGCCAAGCCTTGTTTACCCTCGGTTTAGGCGCGGCATACTGGCAAATCGGCACATTAACATTGGAGCAAAGCCTGCAAAGTGCGGTTGTTTTTTTCGGTGTTTTTTATGCCATCTACCACGCCGCAAAATGGTACTACCGACAAGAAGCTCTCGGACGCGGCGATTATTGGTTGGCACTGGGCTTAGGCGTTTTTCTCCCGGCACACCAATTTCCTGTTTTTTTATTCCTCGCCTGCTTTTTCGGCTTACTTTATGCTGCCTACGCCAAATACCAACATCGCACACTCAACGCCGTGCCTTTCGGTCCCTTTATGTCCCTAGCCGGCGTGGTCTGTTTATTGCTTAAT","","","26004","MMWLLFLLGGALCGWRVHRYVEHFADNLSREVHAAYTEIYPQNPPHFTAEKSILKPLKRHFSAPLYSLLFTLLFIICYAINEPLQALCFALYGALLIAISLVDWHYRLISPALCQALFTLGLGAAYWQIGTLTLEQSLQSAVVFFGVFYAIYHAAKWYYRQEALGRGDYWLALGLGVFLPAHQFPVFLFLACFFGLLYAAYAKYQHRTLNAVPFGPFMSLAGVVCLLLN","116832","","type IV prepilin peptidase; type II secretion pathway related protein","Inner membrane, Cytoplasm","","
InterPro
IPR000045
Domain
Peptidase A24A, prepilin type IV
PF01478\"[90-200]TPeptidase_A24
noIPR
unintegrated
unintegrated
PIRSF001215\"[1-229]TTcpJ


","BeTs to 11 clades of COG1989COG name: Signal peptidase, cleaves prepilin-like proteinsFunctional Class: NThe phylogenetic pattern of COG1989 is aom-kz-qvd-lbcefghsnuj----Number of proteins in this genome belonging to this COG is","","Residues 162 to 227 match (8e-25) PD:PD002186 which is described as PEPTIDASE LEADER ENZYME PREPILIN TYPE PROTEOME 3.4.99.- COMPLETE PROCESSING PREPILIN-LIKE ","","","","","Wed Feb 19 07:22:10 2003","","","","","","","Wed Feb 19 07:22:10 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00163 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 90 to 200 (E-value = 9.8e-20) place AA00163 in the Peptidase_A24 family which is described as Type IV leader peptidase family (PF01478)","","","","Wang,Y., Goodman,S.D., Redfield,R.J. and Chen,C.Natural transformation and DNA uptake signal sequences inActinobacillus actinomycetemcomitansJ. Bacteriol. 184 (13), 3442-3449 (2002)PubMed: 12057937","A gene cluster closely related to type II secretion pathway operons of gram-negative bacteria is located on the large plasmid of enterohemorrhagic Escherichia coli O157 strainsFEMS Microbiol. Lett. 148 (2), 265-272 (1997)PubMed: 9084155","Wed Dec 4 09:26:37 2002","Thu Dec 5 13:21:04 2002","1","","","" "AA00164","116885","117505","621","ATGACTTATGTGGTCGGGTTAACCGGTGGGATCGGCAGTGGCAAAAGCACCGTTGCCGATTTGTTTGCCGAACTTGGTGTGTCGGTGATTGATGCGGATGTGGTGGCGCGTCAGGTGGTAGAAAAAGGCTCGCCGTTATTGGCAGAAATCGCTGAACATTTCGGCGAGGAAATTTTGCTTGCCGACGGTTCACTCAATCGCACCGCCTTACGGGAGAAGGTGTTTGCCGATGAATCGCAAAAACAGTGGCTGAATCAGTTGTTGCACCCCGCCATTCGTCGCGAAATGTTAAAACAGTTGGCAGTGCAACGTGCGCCTTATTGTCTTTTTGTGGTGCCCTTATTAATTGAAAATAAATTGACCGCACTTTGCCAACGGATTTTAGTAGTGGATGTGAGTGAACAAACCCAGCTAGAACGGGCAAATCGGCGGGATAACAATCAGTTGGCGCTTATTAAAAATATTATGCAATCGCAAGTCAGCCGTGCGGAACGCTTAAAGTACGCCGATGATGTCATTAATAATGACGAGGATTTAGCCCGAAACCTGCCTCAACTGAAGCAAAAAGTGCTAGACTTGCACCACCTCTATTTACAATTTGCGGAGATATTTAATGAGCGA","","","23342","MTYVVGLTGGIGSGKSTVADLFAELGVSVIDADVVARQVVEKGSPLLAEIAEHFGEEILLADGSLNRTALREKVFADESQKQWLNQLLHPAIRREMLKQLAVQRAPYCLFVVPLLIENKLTALCQRILVVDVSEQTQLERANRRDNNQLALIKNIMQSQVSRAERLKYADDVINNDEDLARNLPQLKQKVLDLHHLYLQFAEIFNER","117505","unpublished primary lab evidence.","dephospho-CoA kinase (dephosphocoenzyme A kinase)","Cytoplasm","","
InterPro
IPR001977
Family
Dephospho-CoA kinase
PD003329\"[3-99]TDepp_CoAkinase
PTHR10695\"[77-179]TDepp_CoAkinase
PF01121\"[3-181]TCoaE
TIGR00152\"[4-188]TDepp_CoAkinase
PS51219\"[4-204]TDPCK
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[2-199]TG3DSA:3.40.50.300
SSF52540\"[1-190]TSSF52540


","BeTs to 21 clades of COG0237COG name: Dephospho-CoA kinaseFunctional Class: HThe phylogenetic pattern of COG0237 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 3.7e-68) to 4/4 blocks of the IPB001977 family, which is described as \"Uncharacterized protein family UPF0038\". Interpro entry for IP:IPR001977. IPB001977A 5-34 2.8e-21 IPB001977B 54-92 9e-24 IPB001977C 105-120 3.2e-05 IPB001977D 140-177 7.2e-14Significant hit ( 3.4e-05) to 1/6 blocks of the PR00988 family, which is described as \"Uridine kinase signature\". Prints database entry for PR:PR00988. PR00988A 2-19 3.6e-05","Residues 100 to 180 match (3e-11) PD:PD582583 which is described as KINASE A COMPLETE PROTEOME ATP-BINDING TRANSFERASE DEPHOSPHOCOENZYME COENZYME BIOSYNTHESIS DEPHOSPHO-COA ","","","","","Mon Feb 17 07:05:56 2003","","","","","","Wed Dec 4 09:49:43 2002","Mon Feb 17 07:05:56 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00164 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 181 (E-value = 2.1e-102) place AA00164 in the CoaE family which is described as Dephospho-CoA kinase (PF01121)","","","","","O'Toole N, Barbosa JA, Li Y, Hung LW, Matte A, Cygler M.Crystal structure of a trimeric form of dephosphocoenzyme A kinase from Escherichia coli.Protein Sci. 2003 Feb;12(2):327-36.PMID: 12538896Obmolova,G., Teplyakov,A., Bonander,N., Eisenstein,E., Howard,A.J.and Gilliland,G.L.Crystal structure of dephospho-coenzyme A kinase from HaemophilusinfluenzaeJ. Struct. Biol. 136 (2), 119-125 (2001)PubMed: 11886213Mishra P, Park PK, Drueckhammer DG.Identification of yacE (coaE) as the structural gene for dephosphocoenzyme A kinase inEscherichia coli K-12.J Bacteriol. 2001 May;183(9):2774-8.PMID: 11292795 Obmolova,G., Teplyakov,A., Bonander,N., Eisenstein,E., Howard,A.J.and Gilliland,G.L.Crystal structure of dephospho-coenzyme A kinase from HaemophilusinfluenzaeJ. Struct. Biol. 136 (2), 119-125 (2001)PubMed: 11886213","","Mon Feb 17 07:05:56 2003","1","","","" "AA00165","117498","117707","210","ATGAGCGATGAAACCTTTACCGTGCCCTGCCCTATTTGCTACAAAGCAGTGGTTTGGTCGGAGCAAAGCCCTTATCGTCCGTTTTGCAGCAAACGCTGTCAATTAATTGATTTAGGCGAATGGGCGGCGGAAGAAAAAGCCATTCCATGCGAAACCGCCGATTTTGCGGCAGACGGTTTGTTAAACGAAGACAATGATTGGGTAAAACAC","","","8654","MSDETFTVPCPICYKAVVWSEQSPYRPFCSKRCQLIDLGEWAAEEKAIPCETADFAADGLLNEDNDWVKH","117707","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR005584
Family
Protein of unknown function DUF329
PF03884\"[6-65]TDUF329
noIPR
unintegrated
unintegrated
G3DSA:3.30.50.10\"[4-66]Tno description


","No hits to the COGs database.","","Residues 7 to 48 match (2e-08) PD:PD568745 which is described as PROTEOME COMPLETE PILUS CC2340 MSL6451 ASSEMBLY RSC2830 R00616 NON-ESSENTIAL ","","","","","","","","","","","","Wed Dec 4 09:57:37 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00165 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 6 to 68 (E-value = 6.3e-33) place AA00165 in the DUF329 family which is described as Domain of unknown function (DUF329) (PF03884)","","","","","","","","1","","","" "AA00166","117695","117979","285","TTGGGTAAAACACTAATGCACATTCAACACGAGCAAAATGCGGAACAGGGTGCCTTCTTTATTTTAGACGAGCAACAACGGCGCATTGCCGAACTCACCTATTTTTTCATTGATGACAACACCATTAACGCTGACCACACCTATGTGTCGGAAGCGCTGCGCGGGCAAGGCGTGGCGGATAAGCTATATCAGGCGTTAGTGGAATTTATTCGGGAAAAGCAACTCAAGCTCAAACCGACCTGTAGCTACATTGCAAAAAAATGGCAGCGCGACCGGGCGCATGGT","","","11093","LGKTLMHIQHEQNAEQGAFFILDEQQRRIAELTYFFIDDNTINADHTYVSEALRGQGVADKLYQALVEFIREKQLKLKPTCSYIAKKWQRDRAHG","117979","","conserved hypothetical protein (possible acetyltransferase)","Cytoplasm","","
noIPR
unintegrated
unintegrated
G3DSA:3.40.630.30\"[7-94]Tno description


","BeTs to 5 clades of COG2388COG name: Predicted acetyltransferaseFunctional Class: RThe phylogenetic pattern of COG2388 is a----z---d-l--efgh---j----Number of proteins in this genome belonging to this COG is","","Residues 19 to 94 match (7e-07) PD:PD029192 which is described as PROTEOME COMPLETE PA1749 MSL3681 YJDJ HEMATOPOIESIS LIN0181 DR1844 2.3.1.- ZINC ","","","","","","","","","","","","Wed Dec 4 10:02:13 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00166 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00167","118379","119749","1371","ATGTCATTAGAAGGCGTTTTATCTGCAATAAATACTTTCGTATGGGGACCGCCCCTACTCATTTTATTATCCGGCACGGGATTATATTTAACCCTGCGTCTGGGCTTCATTCAAATCATCCAATTGCCGCGCGCATTGCGCTATTTATTTAAACGGGATTCCGGTTTGCAGCAAAAAGGCGACGTGTCCTCTTTCGCCGCGCTATGCACCGCCCTTGCCGCCACCATCGGCACGGGAAATATCGTGGGCGTTGCCACTGCCGTACAGGCGGGCGGACCGGGTGCGATTTTCTGGATGTGGTTGGTGGCATTGCTCGGCATGGCGACCAAATACGCCGAATGTTTACTGGCGGTGAAATATCGCGTGAGGGATAAAAACGGCTTTATGGCGGGCGGTCCGATGTATTACATTGAGCGCGGTCTCGGCTTAGGCTGGCTGGCGAAGCTGTTTGCCGTGTTCGGCGTGCTGGTGGCATTTTTCGGCATCGGTACTTTCCCGCAAGTAAACGCCATCACCCACGCTATGAACGACACCTTCAGCATTCCGATTCCTGCCACGGCGGCGGTTATCACTATTTTAGTGGGCTTGATTATTCTCGGTGGGGTAAAACGTATCGCCTTGGTGTCCTCTTACATCGTGCCGTTTATGGCGTTATCTTATGTCGCCACTTCCATCGTCATTATGCTGTTAAATTTAGAAAAAATTCCGACCGCACTTCAGTTAATCGTTCATAGCGCTTTCAATCCGGAAGCAGCATTGGGCGGCGCGCTGGGCTTTAGCGTCATGAAAGCCATTCAATCGGGCGTGGCGCGGGGGATTTTCTCTAATGAATCGGGCTTAGGAAGTGCACCTATTGCCGCCGCTGCCGCGCAAACCAAAGAACCGGTGCGTCAAGGGTTGATTTCCATGACCGGCACGTTCCTTGATACGATCATTGTCTGCACCATGACGGGCATTGTGTTAGTACTTACCGGCGCATGGCAATCGCCCGGCATGGAAGGCGCCGCCGTCACCAATTTCGCTTTTTCAAGCGGCTTAAACTCCTCTGTCGGCGCGACTATTGTGACCATTGGCTTGTTATTTTTCGCTTTTACCACGATTCTCGGCTGGTGTTATTACGGCGAACGCTGTTTTGTGTATTTGGTCGGTATCAAAGGCATTAAACTTTACCGCGCCGTTTTCATTGCGTTGGTCGGCTGCGGGGCGTTTATTCAGTTAAATCTCATTTGGATTCTGGCGGATATCGTCAACGGTCTAATGGTTTTCCCGAATTTGGTGGCGTTAATCGGCTTACGTAAAGTGGTGATTGAGGAAACCAAAGATTATTTTACCCGTTTGAAAACCAACCAACGCGACCTGGATGAAATGGCG","","","49558","MSLEGVLSAINTFVWGPPLLILLSGTGLYLTLRLGFIQIIQLPRALRYLFKRDSGLQQKGDVSSFAALCTALAATIGTGNIVGVATAVQAGGPGAIFWMWLVALLGMATKYAECLLAVKYRVRDKNGFMAGGPMYYIERGLGLGWLAKLFAVFGVLVAFFGIGTFPQVNAITHAMNDTFSIPIPATAAVITILVGLIILGGVKRIALVSSYIVPFMALSYVATSIVIMLLNLEKIPTALQLIVHSAFNPEAALGGALGFSVMKAIQSGVARGIFSNESGLGSAPIAAAAAQTKEPVRQGLISMTGTFLDTIIVCTMTGIVLVLTGAWQSPGMEGAAVTNFAFSSGLNSSVGATIVTIGLLFFAFTTILGWCYYGERCFVYLVGIKGIKLYRAVFIALVGCGAFIQLNLIWILADIVNGLMVFPNLVALIGLRKVVIEETKDYFTRLKTNQRDLDEMA","119749","","possible amino-acid transporter (sodium-alanine symporters)","Inner membrane, Cytoplasm","","
InterPro
IPR001463
Family
Sodium:alanine symporter
PR00175\"[91-113]T\"[183-201]T\"[211-230]T\"[306-324]T\"[352-374]T\"[411-431]TNAALASMPORT
PF01235\"[42-456]TNa_Ala_symp
TIGR00835\"[15-442]TagcS: amino acid carrier protein
PS00873\"[91-106]TNA_ALANINE_SYMP
noIPR
unintegrated
unintegrated
signalp\"[1-34]?signal-peptide
tmhmm\"[19-41]?\"[62-82]?\"[96-118]?\"[142-162]?\"[181-201]?\"[211-231]?\"[241-261]?\"[307-327]?\"[349-371]?\"[392-412]?\"[418-436]?transmembrane_regions


","BeTs to 12 clades of COG1115COG name: Na+/alanine symporterFunctional Class: EThe phylogenetic pattern of COG1115 is ----k----d-lb-efgh-nu--it-Number of proteins in this genome belonging to this COG is","Significant hit (1.3e-119) to 5/5 blocks of the IPB001463 family, which is described as \"Sodium:alanine symporter family\". Interpro entry for IP:IPR001463. IPB001463A 63-113 1.5e-43 IPB001463B 185-232 2.2e-22 IPB001463C 268-299 1.3e-22 IPB001463D 360-372 2.8e-05 IPB001463E 409-449 5.1e-21 IPB001463D 361-373 3.5e-05","Residues 58 to 142 match (2e-31) PD:PD284669 which is described as COMPLETE PROTEOME AMINO ACID PERMEASE AMINO-ACID TRANSMEMBRANE TRANSPORTER PROBABLE MEMBRANE ","","","","","","","","","","","","Wed Dec 4 10:40:33 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00167 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 42 to 456 (E-value = 1.7e-237) place AA00167 in the Na_Ala_symp family which is described as Sodium:alanine symporter family (PF01235)","","","","","","","","1","","","" "AA00168","119980","120300","321","ATGACATTAAATATCACAAGCAAACAAATGGATATCACCCCTGCAATCCGCGCCCACGTTGAAGAACGACTCAGCAAACTGAAAAAATGGCATACCCAACTGATAAATCCTCACTTTATTTTAAATAAAACCCCTAAGGGCTTCTCTGTTGATGCTTCCATCGGCACCCCGTTCGGCAATCTGATTGCCAGTGCCGAAGAGGAAGATATGTACAAAGCCATCAACGACGTAGAAGAAAAATTGGAGAGACAGCTCAACAAGCTACAGCATAAGAGTGAATCCCGCCGCGCAGAAGAACGCTTAAAAGATTCGTTTAATGAA","","","12359","MTLNITSKQMDITPAIRAHVEERLSKLKKWHTQLINPHFILNKTPKGFSVDASIGTPFGNLIASAEEEDMYKAINDVEEKLERQLNKLQHKSESRRAEERLKDSFNE","120300","","possible sigma 54 modulation protein","Cytoplasm","","
InterPro
IPR003489
Domain
Sigma 54 modulation protein/ribosomal protein S30EA
PF02482\"[2-95]TRibosomal_S30AE
TIGR00741\"[1-99]TyfiA: ribosomal subunit interface protein
InterPro
IPR013194
Domain
Histone deacetylase interacting
SM00761\"[20-98]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.30.160.100\"[1-107]Tno description


","BeTs to 10 clades of COG1544COG name: Ribosome-associated protein Y (PSrp-1)Functional Class: JThe phylogenetic pattern of COG1544 is -------qvdrlbcefghs--jxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 4.7e-28) to 2/2 blocks of the IPB003489 family, which is described as \"Sigma 54 modulation protein / S30EA ribosomal protein\". Interpro entry for IP:IPR003489. IPB003489A 1-26 2.1e-12 IPB003489B 51-91 3.1e-14","Residues 1 to 91 match (3e-36) PD:PD003440 which is described as COMPLETE PROTEOME MODULATION SIGMA54 PROBABLE SIGMA-54 RIBOSOMAL PROTEIN ORF95 LIGHT ","","","","","","","","","","","","Wed Dec 4 10:47:49 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00168 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 95 (E-value = 2.9e-41) place AA00168 in the Ribosomal_S30AE family which is described as Sigma 54 modulation protein / S30EA ribosomal protein (PF02482)","","","","","O'Neill E, Sze CC, Shingler V.Novel effector control through modulation of a preexisting binding site of the aromatic-responsive sigma(54)-dependent regulatorDmpR.J Biol Chem. 1999 Nov 5;274(45):32425-32.PMID: 10542286van Heeswijk WC, Rabenberg M, Westerhoff HV, Kahn D.The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli.Mol Microbiol. 1993 Aug;9(3):443-57.PMID: 8412694","","Wed Feb 5 14:13:36 2003","1","","","" "AA00169","120452","121003","552","ATGTTAAAAAAAGTTATTTTTTCTGTAGTTACATTACTATTAGTCGGATGTGCAGACGATCCTATAACACCAATCCCGGGAGAATTTGCCGGCGCCGATTATCTACTATCTGACATTGATGCAAAACGTTGGGCTTTTGATAGTAAGCAAGCAGAACAGTGTATTTACCCTAATTTAACCCGAATACAAAAAGAACATTTTTCTCGGGAAGATACTTATATTTATTCTCAATACATACTCTTATATCCATTAGAAAACATCATCGGAGAAAAATACTTAAAAATAATTCAAAATGATGAAAAATCTATGTTATACGCTACTTATCAATATAAGAAATTTAAATTTGAAGAAGTTGAGTATTTAGATCATTTTAAATGCCAAACCTTACGCACTAATGCCCGTGATGATTTAGATGTAGTTAAAGGTAAATATAAGAATGGTATGATTGAAGAAAAGAAAACCGAAGGTGGAGAGAATTCGGATCAAGGGGTTGCTACCAGTGAAAATAGATTCTTCTTTGATATCATAAAATGGGGTACTACATTGCTACTC","","","21430","MLKKVIFSVVTLLLVGCADDPITPIPGEFAGADYLLSDIDAKRWAFDSKQAEQCIYPNLTRIQKEHFSREDTYIYSQYILLYPLENIIGEKYLKIIQNDEKSMLYATYQYKKFKFEEVEYLDHFKCQTLRTNARDDLDVVKGKYKNGMIEEKKTEGGENSDQGVATSENRFFFDIIKWGTTLLL","121003","","conserved hypothetical protein","Cytoplasm, Outer membrane, Inner membrane","","
noIPR
unintegrated
unintegrated
PD104362\"[13-184]TY966_HAEIN_P44085;
PS51257\"[1-17]TPROKAR_LIPOPROTEIN
signalp\"[1-18]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Dec 4 10:48:45 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00169 is paralogously related to AA00864 (0.001).","","","","","","","","","","","","","","1","","","" "AA00170","121467","121378","90","GTGAACCAATCGCTAGACGAAAAAACGCAGGAAGAACTGACCGCACTTCAATCAAAACTTGATCGTGGTACAGTACAACGACAACCACCT","","","3392","VNQSLDEKTQEELTALQSKLDRGTVQRQPP","121378","","hypothetical protein","Cytoplasm, Extracellular","No similarities were found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sat Feb 21 11:04:48 2004","Sat Feb 21 11:04:48 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA00170 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sat Feb 21 11:05:50 2004","","","","","","","","","","","","","1","","","" "AA00171","121933","121625","309","ATGGATAGAACAATGTTAGAACAACAACGCAATCCGGCTGAAGCGTTAACGGTTTCAGTATTAAATTCTCAGTCACAAGTAACCAATAAACCTCTGCGTGATTCGGTAAAACAGGCTTTAAGAAACTACTTGTCTCAATTAGACGGTCAAGATGTGAATGAGCTTTATGAATTGGTCTTGGCAGAAGTTGAACATCCGATGTTAGATATGGTGATGCAATATACCCGTGGTAATCAGACCCGTGCGGCGACAATGCTTGGTATTAACCGCGGTACATTGCGTAAAAAATTAAAAAAATACGGTATGGGT","","","11724","MDRTMLEQQRNPAEALTVSVLNSQSQVTNKPLRDSVKQALRNYLSQLDGQDVNELYELVLAEVEHPMLDMVMQYTRGNQTRAATMLGINRGTLRKKLKKYGMG","121625","","DNA-binding protein","Periplasm, Cytoplasm","","
InterPro
IPR002197
Domain
Helix-turn-helix, Fis-type
PR01590\"[66-83]T\"[83-103]THTHFIS
PF02954\"[60-100]THTH_8
InterPro
IPR005412
Family
DNA-binding protein Fis
PR01591\"[14-31]T\"[31-47]T\"[47-62]T\"[62-74]TDNABINDNGFIS
PIRSF002097\"[5-103]TDNA-binding protein Fis
noIPR
unintegrated
unintegrated
G3DSA:1.10.1680.10\"[6-103]Tno description


","BeTs to 6 clades of COG2901COG name: Factor for inversion stimulation Fis, transcriptional activatorFunctional Class: K,LThe phylogenetic pattern of COG2901 is --------------efghsn------Number of proteins in this genome belonging to this COG is","","Residues 8 to 58 match (1e-11) PD:PD420095 which is described as DNA-BINDING FIS COMPLETE PROTEOME ACTIVATOR TRANSCRIPTION REGULATION HIN RECOMBINATIONAL BINDING ","","","","","","","","","","","","Wed Dec 4 10:52:31 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00171 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 60 to 100 (E-value = 6.1e-17) place AA00171 in the HTH_8 family which is described as Bacterial regulatory protein, Fis family (PF02954)","","","","","Beach,M.B. and Osuna,R. Identification and characterization of the fis operon in enteric bacteria J. Bacteriol. 180 (22), 5932-5946 (1998) PubMed: 9811652 Johnson,R.C., Ball,C.A., Pfeffer,D. and Simon,M.I. Isolation of the gene encoding the Hin recombinational enhancer binding protein Proc. Natl. Acad. Sci. U.S.A. 85 (10), 3484-3488 (1988) PubMed: 2835774 Koch,C., Vandekerckhove,J. and Kahmann,R. Escherichia coli host factor for site-specific DNA inversion: cloning and characterization of the fis gene Proc. Natl. Acad. Sci. U.S.A. 85 (12), 4237-4241 (1988) PubMed: 2837762 Osuna,R., Lienau,D., Hughes,K.T. and Johnson,R.C. Sequence, regulation, and functions of fis in Salmonella typhimurium J. Bacteriol. 177 (8), 2021-2032 (1995) PubMed: 7536730 ","","Wed Dec 4 10:52:31 2002","1","","","" "AA00172","122964","121918","1047","ATGATAGCCCACCTTGTCGGTTGGCAAGGGCATTTGGTCAAGTTGCCGGAAAGTAGTGGGGTCGCGGTGCGCATTGGTTCTTATCAATTAAAAAATCGCATTTTATTGGCTCCTATGGCGGGTGTTACCGATTTGCCTTTTCGGCGAATTTGCGCCAATTATGGTGCAGGTTTGACCTTCTCCGAAATGATGTCAACCAATCCACAGGTATGGTATACCGAGAAATCGAAACTGCGCTTGGCGCATCACCAAGAAGCAGGGATTAATGCCGTACAAATCGCGGGTTCCGATCCTGATGGAATGGCGCAAGCCGCTCAAGTGAATGTGGAATACGGCGCTCAGATTATCGATATTAATATGGGCTGTCCAGCAAAAAAGGTGAATCGTAAAATGGCGGGTTCCGCCCTTTTGCAATATCCTGACTTGGTTCGACGGATTCTTGAGGCTGTGGTGAAAGCAGTTAAGGTTCCGGTAACCTTGAAGATTCGCACAGGTTGGGATATGGAAAATCGAAATTGTGTAGAAATCGCCAAAATCGCAGAACAAAGCGGAATTCAAGCGCTCACCGTGCATGGTCGTACGCGCGCCTGTAAATTTGAAGGTGTGGCGGAATACGATTCCATTAAAGCGGTGAAGCAAAATGTTTCCCTTCCGGTGATTGCCAACGGCGATATAACTTCTGCCGAACAAGCCAAATTCGTTCTCGATTACACGGGGGCGGACGGCATAATGATCGGACGTGGTGCATTGGGGCGACCTTGGTTGTTTCAAACGGTGGTCGGCTTAATTGAGCAACATTCGATCGTTGCGGAACCAAGTTTAGAAGAAAAATGTAGTGTGATTTTGCAGCATATCCGCGATCTTCATCGATTTTACGGCGAAGAAAAAGGGTATCGCATCGCACGCAAGCATATCACTTGGTACTTACAGGATATTCACCCCGATTCTGTTTTTAAGCAACGTTTTAATGCGCTAACCTCCGCTAAAGAGCAATTACACGCGTTAGAACAATTTTTTAAGTTAATATTTACATGGATAGAACAATGT","","","39122","MIAHLVGWQGHLVKLPESSGVAVRIGSYQLKNRILLAPMAGVTDLPFRRICANYGAGLTFSEMMSTNPQVWYTEKSKLRLAHHQEAGINAVQIAGSDPDGMAQAAQVNVEYGAQIIDINMGCPAKKVNRKMAGSALLQYPDLVRRILEAVVKAVKVPVTLKIRTGWDMENRNCVEIAKIAEQSGIQALTVHGRTRACKFEGVAEYDSIKAVKQNVSLPVIANGDITSAEQAKFVLDYTGADGIMIGRGALGRPWLFQTVVGLIEQHSIVAEPSLEEKCSVILQHIRDLHRFYGEEKGYRIARKHITWYLQDIHPDSVFKQRFNALTSAKEQLHALEQFFKLIFTWIEQC","121918","","conserved hypothetical protein (possible regulator protein / nitrogen fixation protein)","Cytoplasm","","
InterPro
IPR001269
Family
Dihydrouridine synthase, DuS
PIRSF006621\"[23-349]TtRNA-dihydrouridine synthase
PF01207\"[35-343]TDus
PS01136\"[116-134]TUPF0034
InterPro
IPR004652
Family
Dihydrouridine synthase TIM-barrel protein nifR3
TIGR00737\"[25-343]TnifR3_yhdG: putative TIM-barrel protein, ni
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[28-271]Tno description
noIPR
unintegrated
unintegrated
G3DSA:1.10.1200.80\"[273-342]Tno description
PTHR11082\"[61-339]TTRNA-DIHYDROURIDINE SYNTHASE
PTHR11082:SF9\"[61-339]TTRNA-DIHYDROURIDINE SYNTHASE-RELATED


","BeTs to 18 clades of COG0042COG name: Predicted TIM-barrel enzymes, possibly dehydrogenases, nifR3 familyFunctional Class: RThe phylogenetic pattern of COG0042 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 5.7e-75) to 6/6 blocks of the IPB001269 family, which is described as \"Uncharacterized protein family UPF0034\". Interpro entry for IP:IPR001269. IPB001269A 35-55 7.7e-12 IPB001269B 105-137 9.7e-21 IPB001269C 156-167 9.9e-07 IPB001269D 184-207 6.2e-11 IPB001269E 216-225 0.00012 IPB001269F 238-255 9e-13","Residues 31 to 107 match (8e-08) PD:PD292851 which is described as THYRO1001703 MGC:14981 FOR FINGER ZINC Y37E11B.5 BDF1-SFP1 CG10463 ","","","","","","","","","","","","Wed Dec 4 10:57:54 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00172 is paralogously related to AA00384 (1e-15), AA01053 (2e-10) and AA01054 (2e-06).","","","","","","Residues 35 to 343 (E-value = 7.8e-152) place AA00172 in the Dus family which is described as Dihydrouridine synthase (Dus) (PF01207)","","","","","","","","1","","","" "AA00173","123108","123197","90","TTGAAGGGGGAAAACAAAAAGTGCGGTGATTTTTTTCACTGTTTTTCAGCGCTTGAAAACACCGCTAAAAACCACCGCACTTTTATGTCA","","","3444","LKGENKKCGDFFHCFSALENTAKNHRTFMS","123197","","hypothetical protein","Cytoplasm","No similarities were found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sat Feb 21 11:29:26 2004","Sat Feb 21 11:29:26 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00173 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sat Feb 21 11:30:08 2004","","","","","","","","","","","","","1","","","" "AA00174","124093","123212","882","ATGGCTTGGATTCAAATTCGCCTGAACAGTACTAACGAAAAGGCAGAGCAACTCAGTGATTTCTTAGAAGAAATCGGATCGGTATCAGTGACTTTTATGGACAGTCAGGACACGCCGATTTTTGAGCCGCTGCAGGGGGAAACCCGTTTGTGGGGTAATACGGATGTGATTGCTTTGTTTGATGCGGAAACCGACATGAACGCGGTGGTGACGCAGCTTAAACAGGCAAAGTATTTGGACAATCATGCCGCTTATAAAATCGAGCAAATCGAAGATAAAGATTGGGAACGTGAATGGATGGATAATTTCCACCCGATGCAATTCGGCAAGCGCTTGTGGATTTGTCCGAGTTGGCGTGAAGTGCCTGATCCTAACGCAGTAAACGTGATGCTTGATCCGGGGCTGGCGTTCGGTACGGGAACCCACCCGACTACGGCGTTATGCCTGGAGTGGCTGGACGGCTTAGGTTTGCAAGGCAAAACTGTGATTGATTTCGGTTGCGGTTCCGGCATTCTTGCCATTGCGGCGTTGAAACTGGGGGCAAAAAGTGCGGTGGGTATTGACATCGATCCGCAGGCGATTCTGGCAAGTCGCAATAATGCAGAGCAAAACGGCGTCGCCGATCGTTTGCAGCTGTGTTTGTCTGATGAAAGACCATCGGATTTAAACGCCGATGTAGTGGTGGCGAACATTCTCGCCGGTCCGTTAAAAGAGCTTTATCCCGTGATTAGCCAATTGGTGAAACCGAACGGTGATTTGGGTTTATCGGGTATTCTGGCAACCCAGGCGCAGTCCGTGTGCAATGTTTATGCCGAGGGTTTTGTGTTGGCGCTGGTGGCAGAACGTGAAGAATGGTGTCGGATTACGGGCAAGCTGAAATGT","","","32262","MAWIQIRLNSTNEKAEQLSDFLEEIGSVSVTFMDSQDTPIFEPLQGETRLWGNTDVIALFDAETDMNAVVTQLKQAKYLDNHAAYKIEQIEDKDWEREWMDNFHPMQFGKRLWICPSWREVPDPNAVNVMLDPGLAFGTGTHPTTALCLEWLDGLGLQGKTVIDFGCGSGILAIAALKLGAKSAVGIDIDPQAILASRNNAEQNGVADRLQLCLSDERPSDLNADVVVANILAGPLKELYPVISQLVKPNGDLGLSGILATQAQSVCNVYAEGFVLALVAEREEWCRITGKLKC","123212","","ribosomal protein L11 methyltransferase","Cytoplasm","","
InterPro
IPR004498
Family
Ribosomal protein L11 methyltransferase
PIRSF000401\"[1-294]TRibosomal protein L11 methyltransferase
TIGR00406\"[3-286]TprmA: ribosomal protein L11 methyltransfera
InterPro
IPR010456
Family
Ribosomal L11 methyltransferase
PF06325\"[2-293]TPrmA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[137-230]Tno description
PTHR18895\"[143-293]TMETHYLTRANSFERASE
PTHR18895:SF3\"[143-293]TRIBOSOMAL PROTEIN L11 METHYLTRANSFERASE (L11 MTASE)


","BeTs to 13 clades of COG2264COG name: Ribosomal protein L11 methylaseFunctional Class: JThe phylogenetic pattern of COG2264 is -------qvd-lbcefghsnuj----Number of proteins in this genome belonging to this COG is","","Residues 160 to 206 match (2e-08) PD:PD015722 which is described as METHYLTRANSFERASE TRANSFERASE PROTEOME COMPLETE DHHB 3-DEMETHYLUBIQUINONE-9 3-METHYLTRANSFERASE UBIQUINONE RIBOSOMAL L11 ","","","","","","","","","","","","Wed Dec 4 11:05:08 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00174 is paralogously related to AA00508 (2e-04).","","","","","","Residues 2 to 293 (E-value = 4.8e-166) place AA00174 in the PrmA family which is described as Ribosomal protein L11 methyltransferase (PrmA) (PF06325)","","","","","Vanet,A., Plumbridge,J.A. and Alix,J.H. Cotranscription of two genes necessary for ribosomal protein L11methylation (prmA) and pantothenate transport (panF) inEscherichia coli K-12. J. Bacteriol. 175 (22), 7178-7188 (1993) PubMed: 8226664. Vanet,A., Plumbridge,J.A., Guerin,M.F. and Alix,J.H. Ribosomal protein methylation in Escherichia coli: the gene prmA,encoding the ribosomal protein L11 methyltransferase, isdispensable. Mol. Microbiol. 14 (5), 947-958 (1994) PubMed: 7715456 ","","Wed Dec 4 11:05:08 2002","1","","","" "AA00175","124649","124062","588","ATGAAAAAAACAGATCAGCAAAGTTTAGAAAATGCTTACCGCTTGTTTGAAACGGGTGATATTCATCAAATGGAAGTAGGAACTACGCGGGGATTGCAGCAGATTCATCGCTATTTATTTCAAGATTTGTATGAGTTTGCCGGCGTGATTCGGGAACAAAATATTTCCAAGGGAAATTTTCGTTTTGCCAACTCGCTTTATTTAAAGGAGGCGTTAGGGAAAATAGAGCAAATGCCCGAAAGCAGTTTTGAAGAAATTATTAACAAATATGTGGAAATGAATATTGCGCATCCGTTTTGGGAAGGAAATGGACGTTCAACCCGTATTTGGTTAGATTTAATTTTAAAGAAAAACTTAGGCAAAGTGGTTAATTGGCAAAATGTAGATAAAACGTTGTATTTACAAGCTATGGAGCGCAGTCCGATTAATGATTTGGAAATTCGCTTTTTATTACAAAGTAATTTGACTGATGATGTGAATAACCGTGAGATGATTTTTAAAGGTATTGAGCAATCTTATTATTACGAAGGTTACGGGGAAATAATAAGGAATAAGTATGGCTTGGATTCAAATTCGCCTGAACAGTAC","","","23456","MKKTDQQSLENAYRLFETGDIHQMEVGTTRGLQQIHRYLFQDLYEFAGVIREQNISKGNFRFANSLYLKEALGKIEQMPESSFEEIINKYVEMNIAHPFWEGNGRSTRIWLDLILKKNLGKVVNWQNVDKTLYLQAMERSPINDLEIRFLLQSNLTDDVNNREMIFKGIEQSYYYEGYGEIIRNKYGLDSNSPEQY","124062","","cell filamentation protein","Cytoplasm","","
InterPro
IPR003812
Family
Filamentation induced by cAMP protein Fic
PF02661\"[32-143]TFic
noIPR
unintegrated
unintegrated
PTHR13504\"[92-117]TFAMILY NOT NAMED
PTHR13504:SF8\"[92-117]Tgb def: Hypothetical cytosolic protein


","No hits to the COGs database.","Significant hit ( 1.3e-40) to 2/2 blocks of the IPB003812 family, which is described as \"Fic (filamentation induced by cAMP) protein\". Interpro entry for IP:IPR003812. IPB003812A 35-66 4.4e-22 IPB003812B 90-111 3.3e-17","Residues 97 to 162 match (5e-20) PD:PD017327 which is described as PROTEOME COMPLETE PLASMID PFHB2 SURFACE P76 FILAMENTATION CELL WSV406 AA38 ","","","","","","","","","","","","Thu Feb 20 07:51:03 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00175 is paralogously related to AA01132 (4e-04).","","","","","","Residues 32 to 143 (E-value = 5.3e-37) place AA00175 in the Fic family which is described as Fic protein family (PF02661)","","","","","Kawamukai,M., Matsuda,H., Fujii,W., Utsumi,R. and Komano,T.Nucleotide sequences of fic and fic-1 genes involved in cellfilamentation induced by cyclic AMP in Escherichia coliJ. Bacteriol. 171 (8), 4525-4529 (1989)PubMed: 2546924Utsumi,R., Nakayama,T., Iwamoto,N., Kohda,K., Kawamukai,M.,Tanabe,H., Tanaka,K., Takahashi,H. and Noda,M.Mutational analysis of the fic promoter recognized by RpoS (sigma38) in Escherichia coliBiosci. Biotechnol. Biochem. 59 (8), 1573-1575 (1995)PubMed: 7549107 ","","Wed Dec 4 11:28:56 2002","1","","","" "AA00176","126104","124671","1434","GTGAATTTAGGCATCATTTTTCCGTTAGTGATTTACTTGGCGTTTGTATTCGGCGCGGCGATTTACGCTTATGTTAAACGCCAAAAAAGCGGCGATTTTCTTTCCGAATATTATGTGGGCAACCGCTCTATGACGGGCTTTGTGCTCGCCATGACCACCGCCTCCACTTATGCCAGTGCCAGTTCTTTCATCGGCGGACCGGGTGCCGCGTATAAATACGGCTTGGGTTGGGTGTTGCTTGCCATGATTCAAGTGCCGGCAGTGTGGTTGGCGCTCGGTGCTTTGGGGAAAAAATTCGCATTACTTTCCCGCAAAACCAACGCTTTAACAATCAACGATCTGCTTCTGTATCGCTACAAAAACAAATATTTAGTGTGGATTGCCTGTGTGGCGTTGCTTATCGCCTTTTTTGCCGCCATGACCGTGCAGTTTATCGGCGGCGCCCGTTTATTGGAGACTACCATCGGCATTCCTTATACCCAAGCCTTGTTGATTTTTGCCCTGACAGTGGGGATTTATACCTATGTCGGCGGCTTCCGCGCGGTGGTACTGACGGATACCATCCAAGGCACAGTGATGATTTTAGGCACCATTGTGTTATTGGTCGGTGTGATTTATCAGGTGGGCGGCATAGAAAGTGCGGTCAAAAAATTAACTGAAATCGACCCAAGTCTGGTTAGCCCGTACGGACCGAACGACATGCTGGATTTTCAATTCATGGCGTCCTTCTGGATTTTGGTGTGCTTTGGTGTGGTCGGCTTGCCGCACACGGCGGTACGTTGCATGGCATTTAAAGACAGCAAAGCCTTGCACAGCGGTATGCTTATTGGCACTATTGTGTTGACGGTGGTTATGTTAGGTATGCACTTGGCGGGCGCATTAGGTCGTGTTGTAGTGCCGGCTTTAACAGTGTCGGACAAAGTCATTCCAAGCCTAATGTTACAAGTGTTACCGCCTATCGTCGCGGGCATTTTCCTTGCCGCGCCGATGTCGGCAATCATGTCTACGGTGGATGCGCAGCTGATTCAATCTTCTTCCATTTTCGTGAAGGATTTATATTTAGCAACAAAACCACAGGCGGCGCAAAATCAAAAACGTATCGGGCGAATCTCCTCAATAATTACGTTAATTTTGACCGCACTTTTAATCTTCGCCTCCCTCAATCCGCCGGATATGATCATTTGGCTGAATCTGTTTGCCTTCGGTGGGTTGGAAGCGGCATTTTTGTGGGCCATCATATTCGGCTTATATTGGGATAAAGCCAATGCCTACGGCGCGATCAGCTCCATGTTAGCAGGCTTAATCTCATTTATTTTGCTCACCCAATTCGGCATTAAATTATTCGGCTTCAACCCTATTGTCCCGGCGCTGGTGTTCGGTTTGGCGGCGTTTTTGGTGGGAAATAAAATAGGAGGAATTGCTGATAAAGTGCGG","","","51317","VNLGIIFPLVIYLAFVFGAAIYAYVKRQKSGDFLSEYYVGNRSMTGFVLAMTTASTYASASSFIGGPGAAYKYGLGWVLLAMIQVPAVWLALGALGKKFALLSRKTNALTINDLLLYRYKNKYLVWIACVALLIAFFAAMTVQFIGGARLLETTIGIPYTQALLIFALTVGIYTYVGGFRAVVLTDTIQGTVMILGTIVLLVGVIYQVGGIESAVKKLTEIDPSLVSPYGPNDMLDFQFMASFWILVCFGVVGLPHTAVRCMAFKDSKALHSGMLIGTIVLTVVMLGMHLAGALGRVVVPALTVSDKVIPSLMLQVLPPIVAGIFLAAPMSAIMSTVDAQLIQSSSIFVKDLYLATKPQAAQNQKRIGRISSIITLILTALLIFASLNPPDMIIWLNLFAFGGLEAAFLWAIIFGLYWDKANAYGAISSMLAGLISFILLTQFGIKLFGFNPIVPALVFGLAAFLVGNKIGGIADKVR","124671","","pantothenate permease","Inner membrane, Cytoplasm","","
InterPro
IPR001734
Family
Na+/solute symporter
PTHR11819\"[6-401]TSODIUM/SOLUTE SYMPORTER
PF00474\"[37-433]TSSF
TIGR00813\"[37-433]Tsss: transporter, solute:sodium symporter (
PS50283\"[2-447]TNA_SOLUT_SYMP_3
PS00456\"[156-181]TNA_SOLUT_SYMP_1
PS00457\"[415-435]?NA_SOLUT_SYMP_2
InterPro
IPR011849
Family
Sodium/pantothenate symporter
TIGR02119\"[3-474]TpanF: sodium/pantothenate symporter
noIPR
unintegrated
unintegrated
PTHR11819:SF14\"[6-401]TSODIUM/PANTOTHENATE SYMPORTER
signalp\"[1-18]?signal-peptide
tmhmm\"[4-24]?\"[45-65]?\"[75-95]?\"[123-145]?\"[159-179]?\"[188-208]?\"[239-259]?\"[274-294]?\"[308-328]?\"[367-387]?\"[393-413]?\"[428-448]?\"[454-474]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 2.2e-35) to 3/3 blocks of the IPB001734 family, which is described as \"Sodium:solute symporter family\". Interpro entry for IP:IPR001734. IPB001734A 47-63 0.071 IPB001734B 156-196 1.5e-19 IPB001734C 404-433 5.6e-11","Residues 425 to 471 match (6e-08) PD:PD249036 which is described as PROTEOME COMPLETE SYMPORTER SODIUM/PANTOTHENATE PERMEASE PANTOTHENATE SYMPORT SODIUM TRANSMEMBRANE MEMBRANE ","","","","","","","","","","","","Thu Jan 23 09:20:31 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00176 is paralogously related to AA00680 (1e-40).","","","","","","Residues 37 to 433 (E-value = 3.7e-190) place AA00176 in the SSF family which is described as Sodium:solute symporter family (PF00474)","","","","","Vanet A, Plumbridge JA, Alix JH. Cotranscription of two genes necessary for ribosomal protein L11methylation (prmA) and pantothenate transport (panF) in Escherichia coli K-12. J Bacteriol. 1993 Nov;175(22):7178-88. PMID: 8226664 Reizer J, Reizer A, Saier MH Jr. The Na+/pantothenate symporter (PanF) of Escherichia coli ishomologous to the Na+/proline symporter (PutP) of E. coli and the Na+/glucose symporters of mammals. Res Microbiol. 1990 Nov-Dec;141(9):1069-72. No abstract available.PMID: 1965458 Jackowski S, Alix JH. Cloning, sequence, and expression of the pantothenate permease(panF) gene of Escherichia coli. J Bacteriol. 1990 Jul;172(7):3842-8. PMID: 2193919 ","","Thu Jan 23 09:20:31 2003","1","","","" "AA00177","126373","126104","270","ATGGATTTACAACAACGCTATAAACAAGCCACGAAAGAAGCGCGGTGGTCGCTGGGTTTAACGCTGCTTTATGTGGTCGGTTGGTGCTTATGCGCGTATTTGCCAAAAGGTACGCACGGTCCTATGGGTTTTCCGTTGTGGTTTGAACTTGCCTGTATTTATCTGCCGATTCTGTTTATTGTGGTGGCATATTGGCTGATTAAAATTGTATTTCAGGATATTCCGTTGGATGTGGAATCCCAAACGCAAAACATGACGGAGAATAAACAG","","","11070","MDLQQRYKQATKEARWSLGLTLLYVVGWCLCAYLPKGTHGPMGFPLWFELACIYLPILFIVVAYWLIKIVFQDIPLDVESQTQNMTENKQ","126104","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR010398
Family
Protein of unknown function DUF997
PF06196\"[8-82]TDUF997
noIPR
unintegrated
unintegrated
PD745092\"[6-78]TYHDT_HAEIN_P46455;
signalp\"[1-31]?signal-peptide
tmhmm\"[15-35]?\"[45-67]?transmembrane_regions


","No hits to the COGs database.","","Residues 6 to 78 match (7e-26) PD:PD028397 which is described as PROTEOME COMPLETE TRANSMEMBRANE MEMBRANE INNER PM1090 YHDT HI0974.1 ORF STY3561 ","","","","","","","","","","","","Wed Dec 4 11:41:24 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00177 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 82 (E-value = 1.2e-44) place AA00177 in the DUF997 family which is described as Protein of unknown function (DUF997) (PF06196)","","","","","","","","1","","","" "AA00179","127785","126400","1386","ATGGTCTACGCCGAAGAGAGACCGGAACCGAGAAATAATTTGCCGGAAGAGCGTATTCAAGTGGCGAAGCCTCAGCTTGCGCAACCGCAGCCGGTGCAAACAGAGAGTAGCGATAATAAGCACACCCTTTCCATCACCAAAGAAGAGCTGGCAAAGCATCCTGACTTAATTATTCGCGGGTTGATTCCGGCGGTGCTGCAGAATAATACGGAGGCGGTGGAACTGCTGTTGCCGTTATACCAGAATCTGCCACAGCAGGATCCATTTTTATTAGCTTGGGCGGAGGCCATTATAGCGACCAAACAAGGGAATTATTCCCGTGCGGTGCAGGAATATCGCATTTTGTTTGCACAACGTCCCGATATTTTGCAGTTGTGTTATCAATTAGCGCACGCGTTATTTTTGAATAATGATAACGAAGCAGCAAAAGATCAGTTCCAAAAACTCCGTGCGGAAGTGAATGATGAACAATCGCAGCACGTGATCGATCAGTATTTAACGGCGATCAACCAACGTGATCAATGGAGAATCAGCGGCGGTATTAGTTTTTTAAATGAATCGAACGTCAGTAATGCACCAAAAGCGGGTACACGTATCGGTGGCTGGCAGGCGTGGCAACGCGAATCGGCACACGGGCTTTCTTATTATCTCAGTAGTGAAAAGAAATGGTCGCTGCCAAAAAATGTTTTCGCCAAATTTATTTGGGACGGACAAGGCAAATATTATTGGGATAACAAGAAATATAACGAATTCAACGCCCGTATCGGGGCAGGCTTGGGCTATCAAACGGCAAATACCGAAGTGGTGTTGTTGCCTTTCGCCGAACGTCGTTGGTATTCCGGCGGATCTTCCGGCAGTGATGCTATGAAGCAATTTTCTAAAAACTCCGGCGTACGTTTTGAATTAAGCCATTGGTTTCATAAAATGTGGCAAATTTCCACCGCACTTGAGTATGGCGAACAGCGTTATGTGAAGCGCAAACATTTAAGCGGCAATAATTATTTGTGGTCGAACACTTTGTTATTCCTGCCTTACAGCGGGCAATATTGGTTTGCCGGGGTGGATTACAACCGCGAAAATACCCGTGATAGCGATAATGCCTATCAGCGTAAAAATCTTCGTTTGGGCTGGGTGCAGGAATGGCCGTTGGGCATTTCTACCCGCATTTCCCTTGCCTATGCCAGACGAACTTATAACAACATTGATTTCTTTAGCATTCGCCAAAAAAACAACGAATATCAAGCCGCACTTACTGTATGGCATCGTAACCTGTACTTTTTGGGCATCACTCCTAAACTAACATGGTCGTATCAAAAAAACGACAGCAATCATCCGTTTTATCGTTATGATAAAAACCGGATTTATTTAGAAATGAGTAAAACTTTT","","","56067","MVYAEERPEPRNNLPEERIQVAKPQLAQPQPVQTESSDNKHTLSITKEELAKHPDLIIRGLIPAVLQNNTEAVELLLPLYQNLPQQDPFLLAWAEAIIATKQGNYSRAVQEYRILFAQRPDILQLCYQLAHALFLNNDNEAAKDQFQKLRAEVNDEQSQHVIDQYLTAINQRDQWRISGGISFLNESNVSNAPKAGTRIGGWQAWQRESAHGLSYYLSSEKKWSLPKNVFAKFIWDGQGKYYWDNKKYNEFNARIGAGLGYQTANTEVVLLPFAERRWYSGGSSGSDAMKQFSKNSGVRFELSHWFHKMWQISTALEYGEQRYVKRKHLSGNNYLWSNTLLFLPYSGQYWFAGVDYNRENTRDSDNAYQRKNLRLGWVQEWPLGISTRISLAYARRTYNNIDFFSIRQKNNEYQAALTVWHRNLYFLGITPKLTWSYQKNDSNHPFYRYDKNRIYLEMSKTF","126400","","conserved hypothetical protein (possible outer membrane protein)","Outer membrane, Extracellular","","
InterPro
IPR007655
Family
Protein of unknown function DUF560
PF04575\"[415-462]TDUF560


","BeTs to 3 clades of COG3699COG name: Predicted outer membrane proteinFunctional Class: MThe phylogenetic pattern of COG3699 is -----------------h-n------Number of proteins in this genome belonging to this COG is","","Residues 90 to 399 match (8e-09) PD:PD155809 which is described as (see also SP:O85083_MORCA_O85083).","","","","","","","","","","","","Wed Dec 4 11:42:47 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00179 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 415 to 462 (E-value = 6e-28) place AA00179 in the DUF560 family which is described as Protein of unknown function (DUF560) (PF04575)","","","","","","","","1","","","" "AA00180","128128","127907","222","ATGTCCGCTGATTCTCAAGTAATTAATATGAATGCAACTATTTCTAATAACAGTTTTGAGGGAAAAGCTACATCTAAGCATTTATCTGGCGAGGCTACCGTGGAGGGTAAATTCTATGGTAATAATGCCGAAGCATTGGCTGGCGCATTTCATAGATCAGGAGACAAACCTTGGTATGGTGCGTTTGGTGCAAAAAAAGATGACAGTGCTAAACCTAATCCA","","","7776","MSADSQVINMNATISNNSFEGKATSKHLSGEATVEGKFYGNNAEALAGAFHRSGDKPWYGAFGAKKDDSAKPNP","127907","","conserved hypothetical protein","Outer membrane, Periplasm, Extracellular","This sequence is weakly related to gi32033879, a predicted tonB fragment from Actinobacillus pleuropneumoniae serovar 1 str. 4074. See also gi16272910 from H. influenzae.","
InterPro
IPR001677
Family
Transferrin binding protein
PF01298\"[11-72]TLipoprotein_5


","No hits to the COGs database.","Significant hit ( 8.8e-05) to 1/5 blocks of the IPB001677 family, which is described as \"Transferrin binding protein\". Interpro entry for IP:IPR001677. IPB001677E 22-48 8.7e-05 IPB001677B 34-57 0.2","","","","","","","","","","","","","Sat Feb 21 11:34:24 2004","Sat Feb 21 11:34:24 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No sequeneces are paralogously related to this sequence.AA00180 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sat Feb 21 11:34:24 2004","","","","","","","","","","","","","1","","","" "AA00181","128915","128709","207","GTGCGGTCAGAAAAAACAAAGTTTTTCAATGTGTTAAAGAACGTTTTAGGGATAGGTAAGCAAAGAAATGAACTTATGAATAAAATATTCCGGTTTTTTTTCGCACTTTTATTAATTTTCAATAAACGTATTTTGTTTATTGTGTTAAACTGCCCAAGCAGTTTATGCGATTACGTCCACTTAAAAATTTCAAGCAGTTATAAAATT","","","8140","VRSEKTKFFNVLKNVLGIGKQRNELMNKIFRFFFALLLIFNKRILFIVLNCPSSLCDYVHLKISSSYKI","128709","","hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-56]?signal-peptide
tmhmm\"[32-52]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Dec 4 11:45:11 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00181 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00182","130295","128952","1344","ATGTTAGAAAAAGTTGTCATTGCCAATCGCGGTGAAATCGCACTGCGAATTTTGCGCGCTTGCAAAGAATTAGGCATTAAAACCGTCGCCGTACATTCCACCGCAGACCGTGAATTGAAACACGTTCTGCTTGCCGATGAAACCGTATGTATCGGTCCGGCCCAATCGGCAAAAAGTTATTTAAATATCCCGGCGATTATTGCCGCCGCCGAAGTGACCGGCGCCGACGCTATTCACCCGGGCTATGGTTTCCTTTCCGAAAATGCCGATTTCGCCGAGCAGGTGGAAAGTTCAGATTTCATTTTTATCGGTCCGACCGCTGATGTGATTCGTTTAATGGGTGATAAAGTATCCGCCATTAACGCCATGAAAAAAGCCGGTGTGCCTTGCGTGCCGGGTTCTGACGGTCCGTTAAGTTCCGACATCGCGAAAAATAAAGAAATCGCCAAACGTATCGGCTACCCGATTATTATCAAAGCCTCCGGTGGCGGTGGTGGTCGTGGTATGCGCGTGGTGCGTAGTGAAGATACTTTGGAAGAATCTATTGCCATGACCAAAGCGGAAGCCAAAGCCGCTTTTAACAACGACATGGTTTACATGGAAAAATATTTGGAAAACCCACGCCATGTGGAAATCCAAGTATTAGCCGACACCCACGGCAACGCAGTATATCTTGCAGAACGTGATTGCTCCATGCAGCGTCGCCACCAAAAAGTGGTGGAAGAAGCACCGGCCCCGGGCATTGCCGAAGAAGTGCGTCGCGACATCGGTTCCCGCTGTGCGAAAGCCTGCGTAGAAATCGGTTACCGTGGTGCGGGTACTTTTGAGTTCTTGTATGAAAACGGCGAATTCTATTTCATTGAAATGAACACCCGTATTCAGGTAGAGCACCCGGTGACCGAAATGATCACCGGTGTGGATTTGGTGAAAGAACAATTACATATCGCTTCCGGCTTGCCGATTTCCTTTAAACAGGAAGATATTAAAGTGAAAGGGCACGCTATTGAGTGTCGTATTAACGCGGAAGATCCGAAAACCTTCCTGCCTTCGCCGGGCAAAGTGGTGCATTTACACTCGCCGGGTGGATTGGGTGTGCGTTGGGATTCCCATATTTACGCCGGTTATACGGTTCCGCCGCACTATGATTCTATGATCGCGAAGCTCATCACTTACGGTGATGTCCGTGAAGTGGCGATTCGTCGTATGCAAAATGCGCTATCGGAAACTATCATTGACGGTATTAAAACCAATATCCCGTTACATGATCTTATTTTAGACGATGAAAACTTCCAAAAAGGTGGCACTAATATCCACTATTTGGAGAAAAAATTAGGTATGCACGAA","","","49328","MLEKVVIANRGEIALRILRACKELGIKTVAVHSTADRELKHVLLADETVCIGPAQSAKSYLNIPAIIAAAEVTGADAIHPGYGFLSENADFAEQVESSDFIFIGPTADVIRLMGDKVSAINAMKKAGVPCVPGSDGPLSSDIAKNKEIAKRIGYPIIIKASGGGGGRGMRVVRSEDTLEESIAMTKAEAKAAFNNDMVYMEKYLENPRHVEIQVLADTHGNAVYLAERDCSMQRRHQKVVEEAPAPGIAEEVRRDIGSRCAKACVEIGYRGAGTFEFLYENGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQLHIASGLPISFKQEDIKVKGHAIECRINAEDPKTFLPSPGKVVHLHSPGGLGVRWDSHIYAGYTVPPHYDSMIAKLITYGDVREVAIRRMQNALSETIIDGIKTNIPLHDLILDDENFQKGGTNIHYLEKKLGMHE","128952","","biotin carboxylase (subunit of acetyl-CoA carboxylase)","Cytoplasm","","
InterPro
IPR004549
Family
Acetyl-CoA carboxylase, biotin carboxylase
TIGR00514\"[1-448]TaccC: acetyl-CoA carboxylase, biotin carbox
InterPro
IPR005479
Domain
Carbamoyl-phosphate synthase L chain, ATP-binding
PF02786\"[115-329]TCPSase_L_D2
PS00866\"[154-168]TCPSASE_1
PS00867\"[286-293]?CPSASE_2
InterPro
IPR005481
Domain
Carbamoyl-phosphate synthetase large chain, N-terminal
PF00289\"[1-113]TCPSase_L_chain
InterPro
IPR005482
Domain
Biotin carboxylase, C-terminal
PF02785\"[336-441]TBiotin_carb_C
InterPro
IPR011761
Domain
ATP-grasp fold
PS50975\"[120-317]TATP_GRASP
InterPro
IPR011764
Domain
Biotin carboxylation region
PS50979\"[1-445]TBC
InterPro
IPR013816
Domain
ATP-grasp fold, subdomain 2
G3DSA:3.30.470.20\"[86-444]Tno description
InterPro
IPR013817
Domain
Pre-ATP-grasp fold
G3DSA:3.40.50.20\"[1-85]Tno description
noIPR
unintegrated
unintegrated
PTHR18866\"[4-442]TCARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE


","BeTs to 20 clades of COG0439COG name: Biotin carboxylaseFunctional Class: IThe phylogenetic pattern of COG0439 is aom---yq-drlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.9e-96) to 7/8 blocks of the IPB001882 family, which is described as \"Biotin-requiring enzymes attachment site.\". Interpro entry for IP:IPR001882. IPB001882A 75-95 1.3e-14 IPB001882B 104-132 1.7e-15 IPB001882C 153-170 1e-12 IPB001882D 209-244 9.2e-29 IPB001882E 267-281 1.5e-06 IPB001882F 292-301 4.7e-06 IPB001882G 332-350 0.00098Significant hit ( 6.6e-17) to 1/1 blocks of the IPB000901 family, which is described as \"Carbamoyl-phosphate synthase\". Interpro entry for IP:IPR000901. IPB000901 149-172 6.7e-17","Residues 117 to 161 match (9e-16) PD:PD581279 which is described as CARBOXYLASE BIOTIN PROTEOME COMPLETE ACETYL-COA LIGASE A ACC SUBUNIT ATP-BINDING ","","","","","","","","","","","","Wed Dec 4 11:48:42 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00182 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 336 to 441 (E-value = 5.6e-64) place AA00182 in the Biotin_carb_C family which is described as Biotin carboxylase C-terminal domain (PF02785)","","","","","Kondo,H., Shiratsuchi,K., Yoshimoto,T., Masuda,T., Kitazono,A., Tsuru,D., Anai,M., Sekiguchi,M. and Tanabe,T. Acetyl-CoA carboxylase from Escherichia coli: gene organizationand nucleotide sequence of the biotin carboxylase subunit Proc. Natl. Acad. Sci. U.S.A. 88 (21), 9730-9733 (1991) PubMed: 1682920 Li,S.J. and Cronan,J.E. Jr. The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase J. Biol. Chem. 267 (2), 855-863 (1992) PubMed: 1370469 Waldrop,G.L., Rayment,I. and Holden,H.M. Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase Biochemistry 33 (34), 10249-10256 (1994) PubMed: 7915138 Thoden,J.B., Blanchard,C.Z., Holden,H.M. and Waldrop,G.L. Movement of the biotin carboxylase B-domain as a result of ATP binding J. Biol. Chem. 275 (21), 16183-16190 (2000) PubMed: 10821865 Lamhonwah,A.M., Barankiewicz,T.J., Willard,H.F., Mahuran,D.J.,Quan,F. and Gravel,R.A.Isolation of cDNA clones coding for the alpha and beta chains ofhuman propionyl-CoA carboxylase: chromosomal assignments and DNApolymorphisms associated with PCCA and PCCB genesProc. Natl. Acad. Sci. U.S.A. 83 (13), 4864-4868 (1986)PubMed: 3460076 ","","Wed Dec 4 12:10:29 2002","1","","","" "AA00183","130805","130341","465","ATGGACATTCGTAAAATTAAAAAATTAATCGAACTCGTCGAAGAATCGGGCATTATGGAGCTTGAGATCTCCGAAGGTGAGGAATCGGTTCGTATTAATCGCGGTTCTCCGGCTTCCGTTCAATATACCGTGCCAATGGCGGCACCGGCTGCGCCTGTTGCCGCACCGACCCCATCCGCACCGGCAGCAAGTCCTGCCCCGGCTGCAGCGCCTGCGGCTTCCGAAGAAGTTGCCGGACATAAAATCCGTTCTCCGATGGTGGGAACTTTCTATCGCAGCCCAAGCCCTGAAGCGAAGGCTTTTGTTGACGTGGGTCAAACTGTGAAAGTGGGCGACGCCCTTTGTATCGTTGAAGCGATGAAAATGATGAACCGCATTGAAGCGGATAAAGCAGGTGTAGTTAAAGCTATTCTGGTAAATGATGGTGATCCTGTTGAATTTGATGAGCCGTTGATTATTATCGAA","","","16264","MDIRKIKKLIELVEESGIMELEISEGEESVRINRGSPASVQYTVPMAAPAAPVAAPTPSAPAASPAPAAAPAASEEVAGHKIRSPMVGTFYRSPSPEAKAFVDVGQTVKVGDALCIVEAMKMMNRIEADKAGVVKAILVNDGDPVEFDEPLIIIE","130341","","acetyl-CoA carboxylase, biotin carboxyl carrier protein","Cytoplasm","","
InterPro
IPR000089
Domain
Biotin/lipoyl attachment
PF00364\"[80-154]TBiotin_lipoyl
PS50968\"[80-154]TBIOTINYL_LIPOYL
InterPro
IPR001249
Family
Acetyl-CoA biotin carboxyl carrier
PR01071\"[84-97]T\"[101-115]T\"[116-129]TACOABIOTINCC
TIGR00531\"[1-155]TBCCP: acetyl-CoA carboxylase, biotin carbox
InterPro
IPR001882
Binding_site
Biotin-binding site
PS00188\"[111-128]TBIOTIN
noIPR
unintegrated
unintegrated
G3DSA:2.40.50.100\"[76-155]Tno description
PTHR18866\"[92-155]TCARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE
PTHR18866:SF13\"[92-155]TPROPIONYL-COENZYME A CARBOXYLASE, ALPHA POLYPEPTIDE


","BeTs to 19 clades of COG0511COG name: Biotin carboxyl carrier proteinFunctional Class: IThe phylogenetic pattern of COG0511 is ao--k-yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-30) to 3/3 blocks of the PR01071 family, which is described as \"Acetyl-CoA biotin carboxyl carrier protein signature\". Prints database entry for PR:PR01071. PR01071A 84-97 2.7e-11 PR01071B 101-115 6e-06 PR01071C 116-129 3.9e-10Significant hit ( 1.4e-10) to 1/8 blocks of the IPB001882 family, which is described as \"Biotin-requiring enzymes attachment site.\". Interpro entry for IP:IPR001882. IPB001882H 92-137 1.3e-10Significant hit ( 2.6e-06) to 1/1 blocks of the IPB003016 family, which is described as \"2-oxo acid dehydrogenases acyltransferase component lipoyl binding site\". Interpro entry for IP:IPR003016. IPB003016 103-137 2.5e-06","Residues 82 to 155 match (3e-29) PD:PD000268 which is described as COMPLETE PROTEOME BIOTIN PYRUVATE DIHYDROLIPOAMIDE CARBOXYLASE TRANSFERASE DEHYDROGENASE LIPOYL COMPONENT ","","","","","","","","","","","","Thu Jan 23 11:13:38 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00183 is paralogously related to AA02195 (6e-12) and AA01986 (9e-08).","","","","","","Residues 80 to 154 (E-value = 5.3e-36) place AA00183 in the Biotin_lipoyl family which is described as Biotin-requiring enzyme (PF00364)","","","","","Li,S.J. and Cronan,J.E. Jr. The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase The Journal of biological chemistry. 267 (2), 855-863 (1992) PubMed: 1370469 Li,S.J. and Cronan,J.E. Jr. Growth rate regulation of Escherichia coli acetyl coenzyme A carboxylase, which catalyzes the first committed step of lipid biosynthesis Journal of bacteriology. 175 (2), 332-340 (1993) PubMed: 7678242 Sutton,M.R., Fall,R.R., Nervi,A.M., Alberts,A.W., Vagelos,P.R. andBradshaw,R.A. Amino acid sequence of Escherichia coli biotin carboxyl carrier protein (9100) The Journal of biological chemistry. 252 (11), 3934-3940 (1977) PubMed: 324999 Kondo,H., Shiratsuchi,K., Yoshimoto,T., Masuda,T., Kitazono,A., Tsuru,D., Anai,M., Sekiguchi,M. and Tanabe,T. Acetyl-CoA carboxylase from Escherichia coli: gene organizationand nucleotide sequence of the biotin carboxylase subunit Proceedings of the National Academy of Sciences of the United States of America. 88 (21), 9730-9733 (1991) PubMed: 1682920 Athappilly,F.K. and Hendrickson,W.A. Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing Structure (Camb) 3 (12), 1407-1419 (1995) PubMed: 8747466 Yao,X., Wei,D., Soden,C. Jr., Summers,M.F. and Beckett,D. Structure of the carboxy-terminal fragment of the apo-biotin carboxyl carrier subunit of Escherichia coli acetyl-CoAcarboxylase Biochemistry. 36 (49), 15089-15100 (1997) PubMed: 9398236 Roberts,E.L., Shu,N., Howard,M.J., Broadhurst,R.W., Chapman-Smith,A., Wallace,J.C., Morris,T., Cronan,J.E. Jr. and Perham,R.N. Solution structures of apo and holo biotinyl domains from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy Biochemistry. 38 (16), 5045-5053 (1999) PubMed: 10213607 ","","Wed Dec 4 12:22:11 2002","1","","","" "AA00184","130822","130971","150","ATGCAAATTTCAACCGCACTTTTCGTGAAAAAAGTGCGGTCCGGATTAAGTTTAAATTTTTGCCCGAGAGATTACCTGAAAATAATCATTTTGGCGACAAAATTCTGTTATTTTTCGTCAATTTTCGCTGAATTTCGCTTTTTTGCCAGA","","","5871","MQISTALFVKKVRSGLSLNFCPRDYLKIIILATKFCYFSSIFAEFRFFAR","130971","","hypothetical protein","Cytoplasm","No significant similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sat Feb 21 11:36:08 2004","Sat Feb 21 11:36:08 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00184 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sat Feb 21 11:36:52 2004","","","","","","","","","","","","","1","","","" "AA00185","131405","130932","474","ATGTCATCAAAATACAATATCTTGCTGTTAAACGGTCCGAATTTGAATATGTTAGGTGTGCGTGAGCCGAGCCATTACGGGCATTTATCTTTAGGCATGATCGAAGCCAAAATGCACCAGCTGGCAGGGCTGCAAGGCGTCGCATTAACCTGCTTTCAAGCCAATAGCGAAGAAAAATTAATCGAACAAATCCATCAAAGTTTTCAAAAAGTGGATTTTATTATCATTAATCCTGCCGCTTATACGCATACCAGCGTTGCCTTGCGAGACGCGTTATTGGCGGTGGCGATTCCTTTTGTGGAAGTGCATTTGTCCAACATTCACAAACGCGAACCGTTCCGTCACCATTCCTATTTCAGCGATGTGGCGGAAAGCGTGATTTGCGGCTGTGGCGCTCAGGGTTACGAATTTGCCCTGCAATTCGCGTTAAATTATCTGGCAAAAAAGCGAAATTCAGCGAAAATTGACGAAAAA","","","17623","MSSKYNILLLNGPNLNMLGVREPSHYGHLSLGMIEAKMHQLAGLQGVALTCFQANSEEKLIEQIHQSFQKVDFIIINPAAYTHTSVALRDALLAVAIPFVEVHLSNIHKREPFRHHSYFSDVAESVICGCGAQGYEFALQFALNYLAKKRNSAKIDEK","130932","","3-dehydroquinate dehydratase II","Cytoplasm","","
InterPro
IPR001874
Family
Dehydroquinase, class II
PD004527\"[19-144]TAROQ_PASMU_P57903;
G3DSA:3.40.50.9100\"[5-146]Tno description
PTHR21272\"[5-152]TFAMILY NOT NAMED
PF01220\"[5-148]TDHquinase_II
TIGR01088\"[6-146]TaroQ: 3-dehydroquinate dehydratase, type II
PS01029\"[10-27]TDEHYDROQUINASE_II


","BeTs to 12 clades of COG0757COG name: 3-dehydroquinate dehydratase IIFunctional Class: EThe phylogenetic pattern of COG0757 is --------vdr-bcefghs-uj----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.5e-77) to 3/3 blocks of the IPB001874 family, which is described as \"Dehydroquinase class II\". Interpro entry for IP:IPR001874. IPB001874A 7-41 4.3e-19 IPB001874B 42-82 2.1e-19 IPB001874C 98-139 9.4e-37","Residues 19 to 139 match (8e-50) PD:PD004527 which is described as DEHYDRATASE 3-DEHYDROQUINATE PROTEOME COMPLETE LYASE 3-DEHYDROQUINASE II TYPE DHQASE AROMATIC ","","","","","","","","","","","","Fri May 20 10:04:47 2005","","Fri May 20 10:04:47 2005","Fri May 20 10:04:47 2005","Fri May 20 10:04:47 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA00185 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Fri May 20 10:04:47 2005","","","","","Residues 7 to 148 (E-value = 3.8e-93) place AA00185 in the DHquinase_II family which is described as Dehydroquinase class II (PF01220)","Fri May 20 10:04:47 2005","","","","Gourley DG, Shrive AK, Polikarpov I, Krell T, Coggins JR,Hawkins AR, Isaacs NW, Sawyer L. The two types of 3-dehydroquinase have distinct structures butcatalyze the same overall reaction. Nat Struct Biol. 1999 Jun;6(6):521-5. PMID: 10360352 Florova G, Denoya CD, Morgenstern MR, Skinner DD, Reynolds KA. Cloning, expression, and characterization of a type II3-dehydroquinate dehydratase gene from Streptomyceshygroscopicus. Arch Biochem Biophys. 1998 Feb 15;350(2):298-306. PMID: 9473305 Boam DJ, Price NC, Kelly SM, Krell T, Coggins JR. Evidence that the active site in type II dehydroquinase fromStreptomyces coelicolor is near the single tryptophan. Biochem Soc Trans. 1997 Feb;25(1):348; replaces 93S. PMID: 9147947 Bottomley JR, Clayton CL, Chalk PA, Kleanthous C. Cloning, sequencing, expression, purification and preliminarycharacterization of a type II dehydroquinase from Helicobacterpylori. Biochem J. 1996 Oct 15;319 ( Pt 2):559-65. PMID: 8912695 ","","Wed Dec 4 12:27:31 2002","1","","","" "AA00186","132505","131507","999","ATGACGAATCGAAGTTATAATCTTTACCGCTATGCCATTCCTGTAGATTCCCAACTGATTTTACGTAATCGTTTTTTGAAAAAACGCGAGGGGTTGTTGGTGAAAGTCTGTTGCGGTGAACATAAAGGCTGGGGCGAAATTGCGCCGTTGCCGGAATTTAGCCAAGAAACTTTAGACGAGGCGCAGGCGCAGGCAATTGAATGGCTGAAAAAATGGGATGAAGCGCGCCGTTGCAATGTGAAACTGGAACTCACGCCGGATTTATATCCTTCCGTGGCGTTCGGTTTAAGTTGTGCGTTAATGGAAATGAAAGGCAGGTTGGATGACGAGGGAAACTATCAGGTGGCGCCGTTGTGTTATGGCGATCCGGATGAGTTGTATGAACCGCTGGATCGGATGCAGGGCGAAAAGGTCGCCAAGATTAAAGTGGGGATGTATGAAGCCAACCGCGACGGCATGATTGCGGATATGTTGTTGGAGGCTATTCCCGATTTGCAACTTCGTTTGGATGCCAACCGCAGCTGGACGCCCGCTAAAGCACAGCTTTTCGCCAAATATGTGAAACCCGGGCATCGTGCGCGCATCCAGTTTTTGGAAGAACCGTGCAAAACCCGTGAGGAAAGCCGTCAATTCGCCGCCGAAACAGGCATTAATATCGCCTGGGATGAAAGCGTGCGTGAACCTGGTTTTTGCGTGGAAAAAGAACCGCACTTGGCGGCGATTGTAATTAAACCGACCTTGGTGGGATCTATCGAGCACTGCACCGCATTGATTGAACAAGCGCACGTGCTGGGAATTAAAGCGGTGATCAGTTCCAGTATCGAAAGCAGCTTCGGTTTAACCCAACTGGCGCGCATGGCGCAGCAATATACGCCGAATGTCACACCGGGGCTGGATACGTTAAGTTTAATGGATTATCAATTGGTGAGACGCTGGCCGGGTTCCGATTTGCCTTTGGTGGGATTGGATTCCGAATTTGTTAGCGAAGTTAAAGTAGAT","","","37564","MTNRSYNLYRYAIPVDSQLILRNRFLKKREGLLVKVCCGEHKGWGEIAPLPEFSQETLDEAQAQAIEWLKKWDEARRCNVKLELTPDLYPSVAFGLSCALMEMKGRLDDEGNYQVAPLCYGDPDELYEPLDRMQGEKVAKIKVGMYEANRDGMIADMLLEAIPDLQLRLDANRSWTPAKAQLFAKYVKPGHRARIQFLEEPCKTREESRQFAAETGINIAWDESVREPGFCVEKEPHLAAIVIKPTLVGSIEHCTALIEQAHVLGIKAVISSSIESSFGLTQLARMAQQYTPNVTPGLDTLSLMDYQLVRRWPGSDLPLVGLDSEFVSEVKVD","131507","","o-succinylbenzoate-CoA synthase; OSB synthase","Cytoplasm","","
InterPro
IPR010196
Family
O-succinylbenzoic acid (OSB) synthetase, gamma proteobacteria and archaea
TIGR01927\"[9-315]TmenC_gamma/gm+: o-succinylbenzoic acid (OSB
InterPro
IPR013342
Domain
Mandelate racemase/muconate lactonizing enzyme, C-terminal
PF01188\"[123-218]TMR_MLE
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.120\"[106-303]Tno description
PTHR10992\"[197-262]TALPHA/BETA HYDROLASE RELATED
PTHR10992:SF10\"[197-262]TO-SUCCINYLBENZOATE SYNTHASE


","BeTs to 11 clades of COG1441COG name: O-succinylbenzoate synthase and related enzymesFunctional Class: HThe phylogenetic pattern of COG1441 is ao-p-z--vdrlbcefgh---j----Number of proteins in this genome belonging to this COG is","Significant hit ( 4.4e-07) to 3/5 blocks of the IPB001354 family, which is described as \"Mandelate racemase/muconate lactonizing enzyme family\". Interpro entry for IP:IPR001354. IPB001354A 38-48 1.2e+02 IPB001354C 157-198 0.0069 IPB001354D 238-283 0.15","Residues 13 to 184 match (2e-55) PD:PD104362 which is described as PROTEOME COMPLETE PM1073 HI0966 ","","","","","","","","","","","","Thu Jan 23 09:24:02 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00186 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Koike-Takeshita A, Koyama T, Ogura K. Identification of a novel gene cluster participating inmenaquinone (vitamin K2) biosynthesis. Cloning and sequencedetermination of the 2-heptaprenyl-1,4-naphthoquinonemethyltransferase gene of Bacillus stearothermophilus. J Biol Chem. 1997 May 9;272(19):12380-3. PMID: 9139683 Sharma V, Hudspeth ME, Meganathan R. Menaquinone (vitamin K2) biosynthesis: localization andcharacterization of the menE gene from Escherichia coli. Gene. 1996 Feb 2;168(1):43-8. PMID: 8626063 ","","Wed Dec 4 12:39:17 2002","1","","","" "AA00187","132815","132489","327","ATGTCAAAGTTTGGATTAAGCGATAAATCTATTGAGCAGATCCATTCGATTTTGAGAAAATATCCTGAGATTGAAACGGCAGTTATTTATGGTTCCAGAGCGAAGGGAAACTATAGGGAAGGTTCCGATGTTGATTTAACCTTAAAAGGTGAAAATCTTACTTATTCTGTATTGTTGAAGATTGCGGGCGAATTGGATGATTCTGATTCGCCGTATTTATTTGATTTATCTATTTATCATCAACTGTCAAATCCTGATTTCATTGAACATATTGATCGAGTAGGTCAAGTCTTTTATCAAAGAGAAAACGATGACGAATCGAAGTTA","","","12474","MSKFGLSDKSIEQIHSILRKYPEIETAVIYGSRAKGNYREGSDVDLTLKGENLTYSVLLKIAGELDDSDSPYLFDLSIYHQLSNPDFIEHIDRVGQVFYQRENDDESKL","132489","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR002934
Domain
DNA polymerase, beta-like region
PF01909\"[11-99]TNTP_transf_2
noIPR
unintegrated
unintegrated
G3DSA:3.30.460.10\"[4-104]Tno description


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Dec 4 12:40:51 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00187 is paralogously related to AA01096 (9e-05).","","","","","","Residues 7 to 99 (E-value = 4.3e-06) place AA00187 in the NTP_transf_2 family which is described as Nucleotidyltransferase domain (PF01909)","","","","","","","","1","","","" "AA00188","133216","132800","417","ATGCAGCAAGATGATGTTCGTTGGAAACAACGCTTTGAAAATTATAAGAGGGCGTTAAATCAACTTGAAACCGCACTTCATGAGTATGCAGATACCAACCTTGATATTATTAAGGAGGGCATTATTCAGCGTTTTGAGTTTACCCATGAACTGGCATGGAAATTAATGCAGGATATTTTACAGGCGGAAGGTGTTGTGGATATTTTGGGTTCCCGTACCGCCACTCGCATGGCGTTTAATCGTGGATTGATTCAACAAGGTGATATATGGCTTGAAATGGTGAAAAGTCGAAATATCACCGTGCATACCTATGATGAAAAAATTCTGGCGCAAGAGTTTAGTAAAATTATGACACTTTATTTACCCCTTTTTCTTCAATTTAAACAACGGGTTGAACAATTATGTCAAAGTTTGGAT","","","16537","MQQDDVRWKQRFENYKRALNQLETALHEYADTNLDIIKEGIIQRFEFTHELAWKLMQDILQAEGVVDILGSRTATRMAFNRGLIQQGDIWLEMVKSRNITVHTYDEKILAQEFSKIMTLYLPLFLQFKQRVEQLCQSLD","132800","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR010235
Family
Nucleotidyltransferase substrate binding protein, HI0074
PF08780\"[17-132]TNTase_sub_bind
TIGR01987\"[11-133]THI0074: nucleotidyltransferase substrate bi
noIPR
unintegrated
unintegrated
G3DSA:1.20.120.330\"[5-129]Tno description


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Dec 4 12:41:34 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00188 is paralogously related to AA01097 (2e-08).","","","","","","","","","","","","","","1","","","" "AA00189","134113","133259","855","ATGCAAAATCCGAAAGATGATGTGTTTTATGCGCCGGTAGAGTGGATCGATCACAGCGCGGGCTACACCGATATTCGTTACCACAAATCCACCGATGGCATTGCCAAAATCACCATCAACCGCCCGGAAGTGCGCAATGCGTTCCGTCCGCAAACCGTGAAAGAAATGATTAACGCTTTTGCCGACGCGCGTTTCGACGAAAAAATCGGCGTCATCGTGTTGACCGGTGAAGGCGAAAAAGCGTTCTGTTCCGGTGGCGACCAAAAAGTACGCGGCGACTACGGCGGCTATAAAGACGACAGCGGTGTGCATCATCTGAATGTATTGGATTTCCAACGTGATATTCGCACCTGCCCGAAACCGGTAGTGGCAATGGTGGCGGGTTACGCCATCGGCGGCGGTCATGTGTTACACATGATGTGCGATCTCACCATTTCCGCCGATAACGCCATTTACGGGCAAACCGGTCCGAAAGTGGGTTCTTTCGACGGCGGCTGGGGAGCAAGCTACATGGCGCGTATCATCGGTCAGAAAAAAGCGCGCGAAATCTGGTTTCTGTGCCGTCAGTACAACGCGCAGGAAGCCTTGGATATGGGCTTGGTGAACACCGTTGTGCCTTATGCCGAGTTGGAAAAAGAAACCGTTCGCTGGTGTCGTGAAATGTTACGCAACAGCCCGATTGCCTTACGTTGCCTAAAAGCGGCGTTAAATGCGGATTGCGACGGTCAATCCGGCCTGCAGGAACTCGCCGGCAATGCCACCATGTTGTTCTACATGACCGAAGAAGGGCAGGAAGGGCGCAACGCCTTCAACGAAAAACGCGCCCCGGATTTCAGCAAGTTCAAACGTAATCCT","","","31736","MQNPKDDVFYAPVEWIDHSAGYTDIRYHKSTDGIAKITINRPEVRNAFRPQTVKEMINAFADARFDEKIGVIVLTGEGEKAFCSGGDQKVRGDYGGYKDDSGVHHLNVLDFQRDIRTCPKPVVAMVAGYAIGGGHVLHMMCDLTISADNAIYGQTGPKVGSFDGGWGASYMARIIGQKKAREIWFLCRQYNAQEALDMGLVNTVVPYAELEKETVRWCREMLRNSPIALRCLKAALNADCDGQSGLQELAGNATMLFYMTEEGQEGRNAFNEKRAPDFSKFKRNP","133259","","dihydroxynaphthoic acid synthase (naphthoate synthas)","Cytoplasm","","
InterPro
IPR001753
Domain
Enoyl-CoA hydratase/isomerase
PF00378\"[35-206]TECH
PS00166\"[123-143]TENOYL_COA_HYDRATASE
InterPro
IPR010198
Family
Naphthoate synthase
TIGR01929\"[22-281]TmenB: naphthoate synthase
noIPR
unintegrated
unintegrated
G3DSA:3.90.226.10\"[16-279]Tno description
PTHR11941\"[28-278]TENOYL-COA HYDRATASE-RELATED


","No hits to the COGs database.","Significant hit ( 7.7e-54) to 5/5 blocks of the IPB001753 family, which is described as \"Enoyl-CoA hydratase/isomerase\". Interpro entry for IP:IPR001753. IPB001753A 37-48 1e-06 IPB001753B 73-87 3e-06 IPB001753C 121-142 9.9e-14 IPB001753D 164-205 1.3e-20 IPB001753E 269-274 2.1","Residues 1 to 32 match (9e-10) PD:PD236894 which is described as SYNTHETASE MENAQUINONE DIHYDROXYNAPHTHOIC PROTEOME COMPLETE ACID NAPHTHOATE DHNA SYNTHASE LYASE ","","","","","","","","","","","","Wed Dec 4 12:44:39 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00189 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 35 to 206 (E-value = 1.9e-73) place AA00189 in the ECH family which is described as Enoyl-CoA hydratase/isomerase family (PF00378)","","","","","Sharma,V., Suvarna,K., Meganathan,R. and Hudspeth,M.E. Menaquinone (vitamin K2) biosynthesis: nucleotide sequence andexpression of the menB gene from Escherichia coli. J. Bacteriol. 174(15): 5057-5062, 1992. PubMed: 1629162.","","Wed Dec 4 12:44:39 2002","1","","","" "AA00190","134992","134228","765","ATGGCTCGTCGTCCTTTAGTTATGGGTAACTGGAAATTAAACGGTAGCAAAGCGTTCACCAGAGAATTAATTACCGGTTTGAAGGAAGAATTGCATGGTGTGACCGGTTGTAATGTGGCAATTGCTCCGCCGGTGATGTATTTGGCGGAAGCGGAAGCTGCGCTGGTTGGCAGTCAAATTGTTTTAGGTGCACAAAACGTTGATGTGAACGTGAAAGGTGCATTCACCGGCGATATTTCTACCGAAATGTTAAAAGATTTCGGCGCGAAATATATCATTATTGGTCACTCCGAACGTCGTACTTATCATAAAGAAAGCGATGAATTCGTGGCGAAAAAATTCGGTGCGTTAAAAGAAGCGGGCTTGGTGCCGGTGTTATGTATCGGTGAATCCGAAGCGGAAAACGAAGCAGGAAAAACCGAAGAAGTGTGCGCCCGTCAAATTGACGCGGTGATTAACCTGTTAGGCGTGGAAGCCTTCAATGGCGCGGTGATTGCCTACGAACCGATTTGGGCAATCGGCACCGGGAAATCTGCCACTCCGGCGCAAGCGCAAGCGGTACACGCGTTCATTCGCGGTCATATCGCGAAAAAATCCCAAGCGGTTGCCGATCAAGTTATTATTCAATACGGCGGTTCCGTAAACGATGCCAACGCGGCGGAATTGTTCACCCAACCGGATATTGACGGTGCATTGGTGGGCGGCGCGTCCTTAAAAGCCCCGGCATTTGCGGTTATCGTAAAAGCAGCGGCAAAAGCGAAAAAC","","","26758","MARRPLVMGNWKLNGSKAFTRELITGLKEELHGVTGCNVAIAPPVMYLAEAEAALVGSQIVLGAQNVDVNVKGAFTGDISTEMLKDFGAKYIIIGHSERRTYHKESDEFVAKKFGALKEAGLVPVLCIGESEAENEAGKTEEVCARQIDAVINLLGVEAFNGAVIAYEPIWAIGTGKSATPAQAQAVHAFIRGHIAKKSQAVADQVIIQYGGSVNDANAAELFTQPDIDGALVGGASLKAPAFAVIVKAAAKAKN","134228","","triosephosphate isomerase","Cytoplasm","","
InterPro
IPR000652
Family
Triosephosphate isomerase
PD001005\"[2-234]TTPIS_HAEIN_P43727;
PTHR21139\"[1-251]TTRIOSEPHOSPHATE ISOMERASE
PF00121\"[5-247]TTIM
TIGR00419\"[6-241]Ttim: triosephosphate isomerase
PS00171\"[166-176]TTIM
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[3-253]Tno description


","No hits to the COGs database.","Significant hit (6.3e-101) to 5/5 blocks of the IPB000652 family, which is described as \"Triosephosphate isomerase\". Interpro entry for IP:IPR000652. IPB000652A 6-16 0.00026 IPB000652B 73-113 8.8e-32 IPB000652C 121-147 4.7e-15 IPB000652D 164-188 2.7e-21 IPB000652E 207-238 2.2e-23","Residues 3 to 238 match (5e-114) PD:PD001005 which is described as ISOMERASE TRIOSEPHOSPHATE TIM SHUNT GLYCOLYSIS PENTOSE BIOSYNTHESIS GLUCONEOGENESIS FATTY ACID ","","","","","","","","","","","","Wed Dec 4 12:48:18 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00190 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 251 (E-value = 2.3e-156) place AA00190 in the TIM family which is described as Triosephosphate isomerase (PF00121)","","","","","Pichersky,E., Gottlieb,L.D. and Hess,J.F. 1984. Nucleotide sequence of the triose phosphate isomerase gene ofEscherichia coli. Mol. Gen. Genet. 195(1-2):314-320. PubMed: 6092857. Tao H, Gonzalez R, Martinez A, Rodriguez M, Ingram LO, Preston JF,Shanmugam KT. Engineering a homo-ethanol pathway in Escherichia coli: increasedglycolytic flux and levels of expression of glycolytic genesduring xylose fermentation. J Bacteriol. 2001 May;183(10):2979-88. PMID: 11325924 ","","Wed Dec 4 12:48:18 2002","1","","","" "AA00191","135159","135605","447","TTGCCCATGATTAAAATTTTCAAAGCTGAACAATGGAACGTAGAAACCCTCCTGCCGTTATTTGAAGCCTACCGTCTTTCCCACGGCATGGCGGAAAACCCGGAACGGACGTTCACTTTTCTTTCCAATCGTATTCGCTTCGGTGAAAGCATTTTTTTCCTCGCGCTCGATCAATCACAACAGGCAGTCGGTTTTATTCAGCTTTACCCCCGCCTTTCCTCCCTTCAATTACAACGTTACTGGCAATTAACGGATATTTTCGTGCGCGACGGCAATCAAACGAACGACATTTACACCGCACTTATCGCCAAAGCCAAAGAATTTGTCAGCTACACCCAATCCACCCGCTTGGTGATAGAACAGGACAGACAACAACACCATTTGCTGGAACAGGAAGGCTTCCGCTTAAATCCGAAGAAATCGGTGTTTGAATTGAATTTGGCAGGT","","","17486","LPMIKIFKAEQWNVETLLPLFEAYRLSHGMAENPERTFTFLSNRIRFGESIFFLALDQSQQAVGFIQLYPRLSSLQLQRYWQLTDIFVRDGNQTNDIYTALIAKAKEFVSYTQSTRLVIEQDRQQHHLLEQEGFRLNPKKSVFELNLAG","135605","","conserved hypothetical protein (possible acetyltransferase, GNAT family)","Cytoplasm","","
noIPR
unintegrated
unintegrated
G3DSA:3.40.630.30\"[4-108]Tno description


","BeTs to 5 clades of COG0454COG name: Histone acetyltransferase HPA2 and related acetyltransferasesFunctional Class: K,RThe phylogenetic pattern of COG0454 is aompkzyqvdrlbcefghsnuj-i-wNumber of proteins in this genome belonging to this COG is","","Residues 96 to 147 match (8e-12) PD:PD415492 which is described as PROTEOME COMPLETE HI0677 PM1312 ","","","","","","","","","","","","Wed Dec 4 12:52:34 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00191 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00194","137049","135685","1365","ATGTCCGAGATTATTTGGGATTTAGCATTAATTCAGAAATATAACCAATCCGGTCCGCGTTATACCTCTTATCCGACGGCGCTGGAATTTAGCGAAAATTACACCAATGACGATTTCACTGCAGCGGCGCAACGTTACCCCGAGCGCCCGCTGTCCTTATATGTTCACATTCCGTTTTGCCACAAACTTTGCTATTTCTGTGCTTGTAATAAACTCATCACACGCCATCAGCACAAAGCGGATATTTATTTGGATTTTCTGGAAAGGGAAATACAAGTGCGGTCGAAATTATTTGCAGATCGCGTGACAACCCAAGTACACTGGGGCGGTGGCACGCCGACCTATTTAACGGAAGCGCAATCTTCCCGTTTGATGCAAATGCTACGCGATCATTTCAATATCGCCGACAACGCGGAAATCAGCATTGAAATGGATCCCCGTGAAATCGAACTTTCCATGCTTGAACACTTGCGCCACATCGGTTTCAACCGTATCAGCATGGGCGTACAGGATTTCAACAAAGAGGTGCAAAAAGCGGTCAATCGAGAGCAGGATGAGGATTTTGTCAACGCGCTGTTGGTGCGCGCCCGCGAGCTGGGTTTTCAATCCACCAATCTGGATTTAATTTATGGCTTGCCGTTCCAAACCGTTGATGGTTTTATGTTCACGTTGCAAAAAGTGATTGAACTCAACCCCGATCGTCTAAGCGTATTCAACTACGCCCATTTGCCGAGCCGTTTTGCCGGACAGGCGAAAATCAAGGATTGGCAGTTGCCGAAACCGGAAGCGAAACTGGAAATTCTGCAAAAAACCATCGAAACGCTGGGCAACGCCGGTTACAAATTTATCGGCATGGATCATTTCGCTAAACCCGATGACGAACTTGCCATTGCGCAACAAAAAGGCGTGCTACACCGCAATTTCCAAGGCTACACCACGCAGGAAGAATGTGATTTGCTGGGCTTGGGTGTGTCGGCAATCAGCCTGCTCGGCGATACTTACGCACAAAATCAAAAGGACTTAAAAGCCTATTATACGGCGGTGGACATGCACGGCATTGCGTTGCATAAAGGCTTAGCCATGACCAAAGAAGATTGTCTGCGTCGTGATGTGATTAAACAATTGATTTGTAACTTTAAACTCGCTTACGCGCCGATTGAACAACAATATCATATTCATTTTAAACAATATTTCGCCGAGGATTTAGCACTGCTGGCGCCTTTAGCCGCCGACGGTTTGCTGGACATCGGCGAAGCACAAATCACCGTTTCCGCCAAAGGGCGTTTGTTGATTCGCAATATTTGTTTGTATTTCGACACGTATTCCCGCGCACAAGCAAAACAACAACAGTTTTCGCGGATTATT","","","52757","MSEIIWDLALIQKYNQSGPRYTSYPTALEFSENYTNDDFTAAAQRYPERPLSLYVHIPFCHKLCYFCACNKLITRHQHKADIYLDFLEREIQVRSKLFADRVTTQVHWGGGTPTYLTEAQSSRLMQMLRDHFNIADNAEISIEMDPREIELSMLEHLRHIGFNRISMGVQDFNKEVQKAVNREQDEDFVNALLVRARELGFQSTNLDLIYGLPFQTVDGFMFTLQKVIELNPDRLSVFNYAHLPSRFAGQAKIKDWQLPKPEAKLEILQKTIETLGNAGYKFIGMDHFAKPDDELAIAQQKGVLHRNFQGYTTQEECDLLGLGVSAISLLGDTYAQNQKDLKAYYTAVDMHGIALHKGLAMTKEDCLRRDVIKQLICNFKLAYAPIEQQYHIHFKQYFAEDLALLAPLAADGLLDIGEAQITVSAKGRLLIRNICLYFDTYSRAQAKQQQFSRII","135685","","oxygen-independent coproporphyrinogen III oxidase","Cytoplasm","","
InterPro
IPR004558
Family
Oxygen-independent coproporphyrinogen III oxidase HemN
TIGR00538\"[4-455]ThemN: oxygen-independent coproporphyrinogen
InterPro
IPR006638
Domain
Elongator protein 3/MiaB/NifB
SM00729\"[50-270]TElp3
InterPro
IPR007197
Domain
Radical SAM
PF04055\"[54-227]TRadical_SAM
InterPro
IPR010723
Domain
HemN, C-terminal
PF06969\"[309-429]THemN_C
noIPR
unintegrated
unintegrated
PTHR13932\"[40-455]TCOPROPORPHYRINIGEN III OXIDASE


","BeTs to 18 clades of COG0635COG name: Coproporphyrinogen III oxidase and related Fe-S oxidoreductasesFunctional Class: HThe phylogenetic pattern of COG0635 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit (1.9e-151) to 8/8 blocks of the IPB003401 family, which is described as \"Oxygen-independent coproporphyrinogen III oxidase\". Interpro entry for IP:IPR003401. IPB003401A 19-27 1.1e-05 IPB003401B 52-67 1.2e-13 IPB003401C 103-116 2e-07 IPB003401D 139-184 9.1e-33 IPB003401E 200-244 2e-32 IPB003401F 287-327 7.2e-36 IPB003401G 357-378 9.2e-12 IPB003401H 432-441 0.0072","Residues 280 to 330 match (4e-07) PD:PD558830 which is described as PROTEOME COPROPORPHYRINOGEN III OXIDASE COMPLETE ","","","","","Tue Feb 18 14:36:18 2003","","","","","","","Wed Dec 4 12:58:16 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00194 is paralogously related to AA02371 (1e-21).","","","","","","Residues 309 to 429 (E-value = 2.1e-48) place AA00194 in the HemN_C family which is described as HemN C-terminal region (PF06969)","","","","","Kusaba A, Ansai T, Akifusa S, Nakahigashi K, Taketani S, Inokuchi H, Takehara T.Cloning and expression of a Porphyromonas gingivalis gene for protoporphyrinogen oxidaseby complementation of a hemG mutant of Escherichia coli.Oral Microbiol Immunol. 2002 Oct;17(5):290-5.PMID: 12354210Layer G, Verfurth K, Mahlitz E, Jahn D.Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli.J Biol Chem. 2002 Sep 13;277(37):34136-42.PMID: 12114526 Troup,B., Hungerer,C. and Jahn,D.Cloning and characterization of the Escherichia coli hemN geneencoding the oxygen-independent coproporphyrinogen III oxidaseJ. Bacteriol. 177 (11), 3326-3331 (1995)PubMed: 7768836Xu,K. and Elliott,T.Cloning, DNA sequence, and complementation analysis of theSalmonella typhimurium hemN gene encoding a putativeoxygen-independent coproporphyrinogen III oxidaseJ. Bacteriol. 176 (11), 3196-3203 (1994)PubMed: 8195073Roper JM, Raux E, Brindley AA, Schubert HL, Gharbia SE, Shah HN,Warren MJ. The enigma of cobalamin (Vitamin B12) biosynthesis inPorphyromonas gingivalis. Identification and characterization of afunctional corrin pathway. J Biol Chem. 2000 Dec 22;275(51):40316-23. PMID: 11007789 ","","Tue Feb 18 14:33:54 2003","1","","","" "AA00195","137502","137071","432","ATGTGGAAAATCCTTTTACTCATTGCGGCCGTGTGTATTGTTGCGGGCATGATCGGCTATGCTGTGTATTTATTGCTCGCGTTACAAAAACAGAAAAAAGCCTTGCAACTTGCCCGCCAAAATCGCATCAATCGCATTAAAGAAAGCCTGGAAATTATCGCCAAAGCCATGTTGAACGGCGATTGTAATTTGTCGGAAGGCGTGCTGCGTTTGAAAATGTTGCTGGAACCTGTGGGCATGGCGCTTAAAAATTATCCTGCCATGTGGCAATTGTATGAAATGGTGGAAGGTATGCCCACCCACAATGCGCGTAAAGAATTGAAAAAGAACGAAAGAATGCGCCTGGATTTGCGCCGCGAAAGCGCTGAAGCGGAACTTGAAAGTAAAATTAAATTGGAACTGCATCGGCTGTTGACCGATATTCAAACATTA","","","16570","MWKILLLIAAVCIVAGMIGYAVYLLLALQKQKKALQLARQNRINRIKESLEIIAKAMLNGDCNLSEGVLRLKMLLEPVGMALKNYPAMWQLYEMVEGMPTHNARKELKKNERMRLDLRRESAEAELESKIKLELHRLLTDIQTL","137071","","conserved hypothetical protein","Cytoplasm, Periplasm","","
noIPR
unintegrated
unintegrated
PD033591\"[5-142]TQ9CK04_PASMU_Q9CK04;
signalp\"[1-21]?signal-peptide
tmhmm\"[5-27]?transmembrane_regions


","No hits to the COGs database.","","Residues 5 to 142 match (8e-31) PD:PD033591 which is described as PROTEOME COMPLETE PASTEURELLA TRANSMEMBRANE COPROPORPHYRINOGEN III HI0725 OXIDASE VC0115 HAEMOLYTICA ","","","","","","","","","","","","Wed Dec 4 13:05:33 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00195 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00196","138075","137518","558","ATGTCCCGTCAGAAAAAGACCCGCCGCCTTACGGATATTATGCCGGCGCGCAAAGCCGATAAAAAATCGGAGCAACCCTATTCAGGTCGCAAAGCCACACGTTATGAACTCGACGCGAAAGCGCGTGAAGAGAAGAAAAAGCGCAAACACAAAGGTTTGAGTTCGGGCTCCCGTCACAGTGCGGCGGAGAGTAAAAACGCCGAACAGGTAAAAGAAGCGCAGGATCCGCGTCTCGGTAGCCGCAAAAAAGTGCCGTTAATAGTGGAATTTGTGAATAAACCGCAAAAAGCGCAAGCCGTTTCCGCCACGAAAGCCGAGCCTAAAGCAAAATTGGATCCGATGCTGGAATTGGAACAGTTGGAAAATAATGAATGCTTACATCAGTTGTTGGATCAATTAGATGAAGGCAAGAAACTGTCTGCCGAGGATCAGCAATTTGTGGATGAATGTTTGGCGCGCGTCGAGCAATTAATGACCGAATTGGGTATTGCGGAAGACGAGGAAAACGACGAAGATTTATACCGCACTTTCGAGCGAATCGACATCAATCAATTCAAA","","","21394","MSRQKKTRRLTDIMPARKADKKSEQPYSGRKATRYELDAKAREEKKKRKHKGLSSGSRHSAAESKNAEQVKEAQDPRLGSRKKVPLIVEFVNKPQKAQAVSATKAEPKAKLDPMLELEQLENNECLHQLLDQLDEGKKLSAEDQQFVDECLARVEQLMTELGIAEDEENDEDLYRTFERIDINQFK","137518","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR007336
Family
Protein of unknown function DUF414
PF04220\"[8-186]TDUF414
noIPR
unintegrated
unintegrated
PD016292\"[29-164]TYI35_PASMU_Q9CK03;


","BeTs to 3 clades of COG3078COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3078 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 29 to 164 match (5e-28) PD:PD016292 which is described as PROTEOME COMPLETE YIHI PASTEURELLA COPROPORPHYRINOGEN III HI0724 OXIDASE YPO0020 VC0114 ","","","","","","","","","","","","Wed Dec 4 13:06:18 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00196 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 186 (E-value = 5.8e-92) place AA00196 in the DUF414 family which is described as Protein of unknown function, DUF414 (PF04220)","","","","","","","","1","","","" "AA00198","138703","138179","525","ATGACCGAATCCCAAACCCAGCTCGACGAAAAATTTATGCACCATGCCCTAATGTTGGCGGGCAAAGCCGAAGCTTTGGGGGAAATCCCCGTGGGGGCTGTGTTAGTGAGTGAAGCGGGGGAAATTATCGGTGAAGGCTGGAATTTATCCATTATCCATTCCGATCCCACCGCACACGCGGAAATTGTCACGCTGCGTCAAGGAGGGCAGAAGTTGCAAAATTACCGTCTGCTTAACACCACCTTATATGTGACCCTTGAGCCTTGCACCATGTGCGCCGGGGCGATTTTACACAGCCGTATTAAACGCTTGGTGTTCGGCGCTGCCGATTACAAAACCGGCGCGGTGGGTTCTCGTTTTCATTTTTTCGATGATTACAAAATGAATCACGCTATCGAAATCACCGGTGGCGTACTGCAACAGGAATGCAGCGAAAAACTCAGCGCCTTCTTCCAAAAACGCCGCGCACAGCAAAAGGAAGCGAAATTGGCACGTCAGGCGACTGTCGAAATGCCTTCCAGCGCC","","","19248","MTESQTQLDEKFMHHALMLAGKAEALGEIPVGAVLVSEAGEIIGEGWNLSIIHSDPTAHAEIVTLRQGGQKLQNYRLLNTTLYVTLEPCTMCAGAILHSRIKRLVFGAADYKTGAVGSRFHFFDDYKMNHAIEITGGVLQQECSEKLSAFFQKRRAQQKEAKLARQATVEMPSSA","138179","","conserved hypothetical protein (Cytosine deaminase-related enzyme)","Cytoplasm","","
InterPro
IPR000169
Active_site
Peptidase, cysteine peptidase active site
PS00639\"[13-23]?THIOL_PROTEASE_HIS
InterPro
IPR002125
Domain
CMP/dCMP deaminase, zinc-binding
PF00383\"[6-108]TdCMP_cyt_deam_1
PS00903\"[59-96]TCYT_DCMP_DEAMINASES
noIPR
unintegrated
unintegrated
G3DSA:3.40.140.10\"[9-170]Tno description
PTHR11079\"[9-171]TCYTOSINE DEAMINASE
PTHR11079:SF9\"[9-171]TCYTIDINE/DEOXYCYTIDYLATE DEAMINASE-RELATED


","BeTs to 14 clades of COG0590COG name: Cytosine/adenosine deaminasesFunctional Class: F,JThe phylogenetic pattern of COG0590 is ------yq-drlbcefghsn-jxi--Number of proteins in this genome belonging to this COG is","","Residues 5 to 54 match (7e-13) PD:PD523072 which is described as PROTEOME COMPLETE ZINC HI0906 HYDROLASE ","","","","","","","","","","","","Wed Dec 4 13:10:33 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00198 is paralogously related to AA01790 (1e-08).","","","","","","Residues 7 to 108 (E-value = 2.6e-39) place AA00198 in the dCMP_cyt_deam family which is described as Cytidine and deoxycytidylate deaminase zinc-binding region (PF00383)","","","","","","","","1","","","" "AA00199","138804","138715","90","TTGAATGCAATTTTCGTCGGTCTCTCTCCCGAAAGCGGGCGAGAGGAAAATAAAAAACATTTTAAAATACAACCGCACTTTAACTCTAAC","","","3421","LNAIFVGLSPESGREENKKHFKIQPHFNSN","138715","","hypothetical protein","Cytoplasm","No significant similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sat Feb 21 11:38:09 2004","Sat Feb 21 11:38:09 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00199 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sat Feb 21 11:38:52 2004","","","","","","","","","","","","","1","","","" "AA00200","139829","139032","798","GTGGAAAACGAACGCACCGGCAAACGCTGCTTAACGGTGATTAACGCCAACCTGACCTACGACGTGGTAAACAATCAATTTCCGTTGATTACCACCCGTAAAAGCTATTGGAAAGCCGCCATCGCCGAATTTTTAGGCTATATTCGCGGCTACGATAATGCCGCCGATTTTCGCAAGCTCGGTACTAAAACCTGGGATGCCAACGCTAACGAAAACCAGGCGTGGTTAAACAATCCGCACCGTAAAGGTACCGATGATATGGGGCGCGTGTACGGCGTACAGGGCAGAAGCTGGCGCAAACCTAACGGCGAGCATTTGGATCAGCTACGCAAAATTGTCAACAACCTGAGCAAAGGTATCGACGATCGCGGCGAGATTTTGACATTCTACAACCCGGGCGAATTTGATCTGGGCTGCCTGCGTCCTTGTATGCACACCCACACTTTTTCCCTGCTTGACGACACTTTATATCTCACCAGCTACCAACGCTCCTGTGATGTGCCGCTCGGCTTGAATTTCAACCAAATCCAAGTGTTCACGTTTCTTGCTTTGATGGCGCAAATTACCGGCAAAAAAGCAGGGCAGGCGTTTCATCAAATCGTCAACGCGCACATTTACGAAGACCAGCTGGAACTTATGCGCGATGTGCAATTAAAACGCGAACCGTTCCCGTCGCCGACGCTGGAAATTAATCCGGACATCAAATCCCTGGCAGACCTGGAAACCTGGGTCACTATGGACGATTTTAAAGTCACGGGCTACCAATGCCACGAACCGATTAAATATCCGTTTTCCGTG","","","35266","VENERTGKRCLTVINANLTYDVVNNQFPLITTRKSYWKAAIAEFLGYIRGYDNAADFRKLGTKTWDANANENQAWLNNPHRKGTDDMGRVYGVQGRSWRKPNGEHLDQLRKIVNNLSKGIDDRGEILTFYNPGEFDLGCLRPCMHTHTFSLLDDTLYLTSYQRSCDVPLGLNFNQIQVFTFLALMAQITGKKAGQAFHQIVNAHIYEDQLELMRDVQLKREPFPSPTLEINPDIKSLADLETWVTMDDFKVTGYQCHEPIKYPFSV","139032","","thymidylate synthase","Cytoplasm","","
InterPro
IPR000398
Domain
Thymidylate synthase, C-terminal
PD001180\"[170-266]TTYSY_HAEIN_P44420;
PR00108\"[27-48]T\"[112-131]T\"[156-182]T\"[194-211]TTHYMDSNTHASE
G3DSA:3.30.572.10\"[1-266]Tno description
PF00303\"[1-266]TThymidylat_synt
PS00091\"[123-151]TTHYMIDYLATE_SYNTHASE
noIPR
unintegrated
unintegrated
PTHR11549\"[61-266]TDIHYDROFOLATE REDUCTASE
PTHR11549:SF2\"[61-266]TBIFUNCTIONAL DIHYDROFOLATE REDUCTASE-THYMIDYLATE SYNTHASE


","BeTs to 14 clades of COG0207COG name: Thymidylate synthaseFunctional Class: FThe phylogenetic pattern of COG0207 is a-m---y--drlb-efghsn-j---wNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.6e-79) to 5/6 blocks of the IPB000398 family, which is described as \"Thymidylate synthase\". Interpro entry for IP:IPR000398. IPB000398B 27-53 7.3e-14 IPB000398C 85-98 1.6e-05 IPB000398D 106-147 6.9e-19 IPB000398E 148-202 1.2e-25 IPB000398F 243-266 3.6e-10","Residues 1 to 266 match (3e-146) PD:PD001180 which is described as SYNTHASE THYMIDYLATE TRANSFERASE METHYLTRANSFERASE NUCLEOTIDE BIOSYNTHESIS TSASE TS COMPLETE PROTEOME ","","","","","","","","","","","","Wed Dec 4 13:13:09 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00200 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 266 (E-value = 5.2e-120) place AA00200 in the Thymidylat_synt family which is described as Thymidylate synthase (PF00303)","","","","","Myllykallio H, Lipowski G, Leduc D, Filee J, Forterre P, Liebl U. An alternative flavin-dependent mechanism for thymidylatesynthesis. Science. 2002 Jul 5;297(5578):105-7. PMID: 12029065 Viswanathan M, Lacirignola JJ, Hurley RL, Lovett ST. A novel mutational hotspot in a natural quasipalindrome inEscherichia coli. J Mol Biol. 2000 Sep 22;302(3):553-64. PMID: 10986118 Fu X, Xu JG. Development of a chromosome-plasmid balanced lethal system forLactobacillus acidophilus with thyA gene as selective marker. Microbiol Immunol. 2000;44(7):551-6. PMID: 10981827 ","","Wed Dec 4 13:13:09 2002","1","","","" "AA00201","140674","139880","795","ATGAATTCAGATTATCTTATATTGCCCCATTTCGACCCCGCCATTTTTGAATTCGGTCCTATCGGCCTGCGCTGGTACGGCTTGATGTACCTGCTCGGGTTTATTTTTGCCCGCTGGTTAGGCGTGCGTCGCGCCAAACGACCGAACAGCGGCTGGACCGTAGAGCAAGTGGATTCCCTGTTATTTAACGGTTTCATGGGCGTATTTCTGGGCGGGCGTATCGGCGATGTGTTCTTCTATAATCTCGACCATTTTCTGCAAGATCCGCTGTATTTATTCCGCGTTTGGGAAGGTGGTATGTCCTTCCACGGTGGCTTAATCGGTGTGATTATCGCCATGATCCTCACCTCCAAAGCGCAGAAACGCAATTTCTGGGCGACGGCGGATTTTGTGGCGCCGTTAATTCCTTTCGGCTTGGGTATGGGGCGCATCGGTAATTTCATCAATCTGGAATTATGGGGACGCCAAACGGATGTGCCTTGGGCGATGATTTTCCCGACGGATCCTCTACTGTTGCCTCGCCACCCGTCGCAATTGTACGAAGCCTTTTTGGAAGGGCTGGTGTTGTTCCTGATTCTCAATTGGTTTATTCGCAAACCGCGCCCGATGGGGGCGGTAGCGGGTTTATTCCTTATCGGTTACGGCTGCTTCCGCTTTATTATCGAATATGTACGCGAGCCGGACGTGGAGCTGTTCCTTGACGTCATCACGCGGGGGCAATTGCTTTGCCTGCCGATGATTCTCGGCGGCATGTTAATCATACTTTGGGCATACAAAAAAAGTGCGGTGAAAAAA","","","30338","MNSDYLILPHFDPAIFEFGPIGLRWYGLMYLLGFIFARWLGVRRAKRPNSGWTVEQVDSLLFNGFMGVFLGGRIGDVFFYNLDHFLQDPLYLFRVWEGGMSFHGGLIGVIIAMILTSKAQKRNFWATADFVAPLIPFGLGMGRIGNFINLELWGRQTDVPWAMIFPTDPLLLPRHPSQLYEAFLEGLVLFLILNWFIRKPRPMGAVAGLFLIGYGCFRFIIEYVREPDVELFLDVITRGQLLCLPMILGGMLIILWAYKKSAVKK","139880","","prolipoprotein diacylglyceryl transferase","Inner membrane, Cytoplasm","","
InterPro
IPR001640
Family
Prolipoprotein diacylglyceryl transferase
PF01790\"[11-260]TLGT
TIGR00544\"[1-265]Tlgt: prolipoprotein diacylglyceryl transfer
PS01311\"[142-154]TLGT
noIPR
unintegrated
unintegrated
signalp\"[1-37]?signal-peptide
tmhmm\"[22-40]?\"[61-81]?\"[95-115]?\"[130-150]?\"[179-197]?\"[202-221]?\"[240-258]?transmembrane_regions


","BeTs to 18 clades of COG0682COG name: Prolipoprotein diacylglyceryltransferaseFunctional Class: MThe phylogenetic pattern of COG0682 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 5e-48) to 4/4 blocks of the IPB001640 family, which is described as \"Prolipoprotein diacylglyceryl transferase\". Interpro entry for IP:IPR001640. IPB001640A 19-33 4.3e-08 IPB001640B 98-108 2.3e-07 IPB001640C 129-154 1.1e-16 IPB001640D 174-192 2.1e-11","Residues 26 to 240 match (3e-97) PD:PD005412 which is described as TRANSFERASE PROLIPOPROTEIN PROTEOME COMPLETE DIACYLGLYCERYL LIPOPROTEIN 2.4.99.- TRANSMEMBRANE PROBABLE MEMBRANE ","","","","","","","","","","","","Wed Dec 4 13:15:07 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00201 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 11 to 260 (E-value = 1.1e-134) place AA00201 in the LGT family which is described as Prolipoprotein diacylglyceryl transferase (PF01790)","","","","","Zhu P, Klutch MJ, Bash MC, Tsang RS, Ng LK, Tsai CM. Genetic diversity of three lgt loci for biosynthesis oflipooligosaccharide (LOS) in Neisseria species. Microbiology. 2002 Jun;148(Pt 6):1833-44. PMID: 12055303 Leskela S, Wahlstrom E, Kontinen VP, Sarvas M. Lipid modification of prelipoproteins is dispensable for growthbut essential for efficient protein secretion in Bacillussubtilis: characterization of the Lgt gene. Mol Microbiol. 1999 Feb;31(4):1075-85. PMID: 10096076","","Wed Dec 4 13:15:07 2002","1","","","" "AA00202","141480","140686","795","ATGTTAACCTTTTTTCTCTTCTGCTTACTTGCCGGTTGTATTGCCGGCTTTTTAGCCGGTTTATTCGGCATCGGCGGTGGGCTGGTGATTGTGCCGATGTTGGTGTATTTATTGCCTATCGTCGGTGTGCCCGATTCGCTGCTCATGCCAACCGCACTTGGTACTTCTTTTGCCACCATTGTGATTACCGCCTTTTCCTCCGCGCAACGGCACCACAAACTGGGCAACGTTGTGTGGTCAACTTTAAAATATTTTGCGCCCGCCTTAATGATCAGCGCTTTTGTCTCCAGTCAATATATCAGCAAATTACCGCACGAAATTTCCAGTAAATTATTCGCCTGTTTAGTGATGTATTTAGCGGCAAAAATGGTGCTTTCCATTAAACAAAAACACATTGATCCCAATAAGAAAATCACCCCGTTAGCCTCCATTATCGGTGGTGGTCTCATCGGCATGGCAGCCAGCGTGGCGGGTATCGGTGGTGGCGGGTTTATCGTGCCATTTTTAAACTCGCGCAATGTGGATATTAAAAAAGCCATCGGTACTTCCGCGTTCTGCGGAATGTTAATGGGCATTGCCGGCATGTTAAGTTTTATGGTGAGCGGCTGGAACGCACCGGGTATGCCGCCGTATTCCATCGGTTTTGTGTATTTGCCGGCGGTGTTGAGTATTACCGTGACCTCATTTTTTACCTCCAAACTCGGCGCCAGTGCCACCAATAAACTGCCGGTGCCGACCTTGAAGAAAGCCTTTGCCGCCTTTTTAATTGTGGTGGCGATAAATATGTTGTTGAAA","","","27789","MLTFFLFCLLAGCIAGFLAGLFGIGGGLVIVPMLVYLLPIVGVPDSLLMPTALGTSFATIVITAFSSAQRHHKLGNVVWSTLKYFAPALMISAFVSSQYISKLPHEISSKLFACLVMYLAAKMVLSIKQKHIDPNKKITPLASIIGGGLIGMAASVAGIGGGGFIVPFLNSRNVDIKKAIGTSAFCGMLMGIAGMLSFMVSGWNAPGMPPYSIGFVYLPAVLSITVTSFFTSKLGASATNKLPVPTLKKAFAAFLIVVAINMLLK","140686","","conserved hypothetical protein (possible membrane protein)","Inner membrane, Extracellular","","
InterPro
IPR002781
Family
Protein of unknown function DUF81
PF01925\"[6-263]TDUF81
noIPR
unintegrated
unintegrated
signalp\"[1-15]?signal-peptide
tmhmm\"[5-36]?\"[46-66]?\"[81-101]?\"[107-125]?\"[140-160]?\"[179-201]?\"[216-236]?\"[242-264]?transmembrane_regions


","BeTs to 19 clades of COG0730COG name: Predicted permeasesFunctional Class: RThe phylogenetic pattern of COG0730 is aompkz-qvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 7.5e-06) to 1/1 blocks of the IPB002781 family, which is described as \"Domain of unknown function DUF81\". Interpro entry for IP:IPR002781. IPB002781 16-26 7.9e-06 IPB002781 151-161 0.17","Residues 6 to 124 match (6e-25) PD:PD001246 which is described as PROTEOME COMPLETE TRANSMEMBRANE MEMBRANE INTEGRAL PLASMID PROBABLE PERMEASE ORF YRKJ ","","","","","","","","","","","","Wed Dec 4 13:20:41 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00202 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 6 to 263 (E-value = 7.6e-61) place AA00202 in the DUF81 family which is described as Domain of unknown function DUF81 (PF01925)","","","","","","","","1","","","" "AA00204","142082","141486","597","GTGATCGACTCCGATGGCTACCGTCCGAATGTAGGCATTGTTATTTGCAACAATAAGGGGCAAGTGCTGTGGGCGAAGAGATACGGACAAAACTCCTGGCAATTTCCGCAGGGCGGAATTAATTGTAGTGAAACGCCCGAGCAGGCGATGTATCGCGAATTGTTTGAGGAGGTGGGTTTAACACGCAAAGATGTGCGGGTGCTGCATGCTTCCAAACATTGGTTACGTTATAAGTTGCCGAAACGTTTGTTGCGTTCTGATTCTAAACCAATGTGTATCGGACAAAAACAACGTTGGTTTTTACTGGAACTCATCGGCGACAGCAAAAATATCAATATGCAATGCAGCAAAATCCCGGAATTCGACGGTTGGCGTTGGGTCAGTTTTTGGTATCCGGTGCGTCAGGTGGTGTCTTTCAAAAAAGAAGTATATCGCAAGGCCATGAAGGAATTCGCCTCGGTGTTATTTGATGAAAATAACAAAGGGTTATTGCAACCGAAGGAACTAAGTGCGTCGGAAGAAAATAGGCGCGTTTCCCCGTCGAAAAAACACAACAATTCCAAACATTCAAAACGCCCATCATATAAATACAAAGGA","","","23415","VIDSDGYRPNVGIVICNNKGQVLWAKRYGQNSWQFPQGGINCSETPEQAMYRELFEEVGLTRKDVRVLHASKHWLRYKLPKRLLRSDSKPMCIGQKQRWFLLELIGDSKNINMQCSKIPEFDGWRWVSFWYPVRQVVSFKKEVYRKAMKEFASVLFDENNKGLLQPKELSASEENRRVSPSKKHNNSKHSKRPSYKYKG","141486","","(di)nucleoside polyphosphate hydrolase; possible invasion protein","Periplasm, Cytoplasm","","
InterPro
IPR000086
Domain
NUDIX hydrolase
PR00502\"[33-47]T\"[47-62]TNUDIXFAMILY
G3DSA:3.90.79.10\"[3-155]Tno description
PF00293\"[7-150]TNUDIX
PS00893\"[38-59]TNUDIX
noIPR
unintegrated
unintegrated
PTHR22769\"[13-70]TMUTT/NUDIX HYDROLASE


","BeTs to 21 clades of COG0494COG name: NTP pyrophosphohydrolases including oxidative damage repair enzymesFunctional Class: L,RThe phylogenetic pattern of COG0494 is aomp-zyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 2.8e-10) to 1/1 blocks of the IPB000086 family, which is described as \"NUDIX hydrolase\". Interpro entry for IP:IPR000086. IPB000086 33-59 2.8e-10","","","","","","","","","","","","","Tue Dec 10 16:46:39 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00204 is paralogously related to AA02850 (3e-05), AA01085 (1e-04) and AA01160 (2e-04).","","","","","","Residues 7 to 150 (E-value = 4.3e-24) place AA00204 in the NUDIX family which is described as NUDIX domain (PF00293)","","","","","Conyers,G.B. and Bessman,M.J.The gene, ialA, associated with the invasion of human erythrocytesby Bartonella bacilliformis, designates a nudix hydrolase active on inucleoside 5'-polyphosphatesJ. Biol. Chem. 274 (3), 1203-1206 (1999)PubMed: 9880487Steele-Mortimer O, Brumell JH, Knodler LA, Meresse S, Lopez A, Finlay BB.The invasion-associated type III secretion system of Salmonella enterica serovar Typhimurium is necessary for intracellularproliferation and vacuole biogenesis in epithelial cells.Cell Microbiol. 2002 Jan;4(1):43-54.PMID: 11856172 ","","Tue Dec 10 16:46:39 2002","1","","","" "AA00205","142302","142718","417","ATGAAAAAAACCATAATCCTCAACGCCCAACTCTCTCATTGCATTGCCACGCTGGGACACACCGACGGTTTAACCCTCTGCGACGCGGGTCTGCCGATCCCCACCCAAGTTGAACGTATCGATCTCGCCTTAACCAAAAACATCCCAAGTTTCCTCGCCTGCTTAGATGCCATCGTCAGCGAAATATTTGTAGAACGGGTGTTACTGGCGCAGAAAATCCAAGAAAAAAGTCCCGAAATTCTGACCGCACTTTTAGCCCGCCTGAACAAACTGGAACAGCAACAAGGCAACCGAATCGCCATAGAATACGTTAGCCACGAGGCGTTCAAACACGCCACCGCGCGAAGCAAAGCTATCGTACGCAGCGGCGAATGCTCGCCATACGCCAATATTATTTTGTATTCCGGCGTGCCGTTT","","","27360","MKKTIILNAQLSHCIATLGHTDGLTLCDAGLPIPTQVERIDLALTKNIPSFLACLDAIVSEIFVERVLLAQKIQEKSPEILTALLARLNKLEQQQGNRIAIEYVSHEAFKHATARSKAIVRSGECSPYANIILYSGVPF","142718","","ribose ABC transporter protein / high affinity D-ribose transport protein","Cytoplasm, Inner membrane","","
InterPro
IPR007721
Family
RbsD or FucU transport
PF05025\"[1-139]TRbsD_FucU


","No hits to the COGs database.","","Residues 1 to 139 match (8e-51) PD:PD021156 which is described as PROTEOME COMPLETE RIBOSE RBSD PERMEASE HIGH AFFINITY ABC MEMBRANE-ASSOCIATED TRANSPORTER ","","","","","","","","","","","","Wed Dec 4 13:27:05 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00205 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 139 (E-value = 4.1e-77) place AA00205 in the RbsD_FucU family which is described as RbsD / FucU transport protein family (PF05025)","","","","","","","","1","","","" "AA00207","142732","144237","1506","ATGCAGCAACCTCTGTTAAAAATCAGCGGCGTTGATAAATCCTTTCCCGGCGTGAAAGCCTTAAGCAACGCCGGTTTGTCCGTGTATGCCGGGCACGCCATGGCGTTAATGGGAGAAAATGGCACGGGCAAATCCACCCTGATGAAAGTGCTCACCGGCATTTACGACAAAGACACGGGAAGCATTGAATATTTAGGAAAACAAGTGGCGTTTAAAGGTCCGAAAGATTCTCAGGAAGCGGGCATCAGCATTATTCATCAAGAACTCAATTTGGTAGGCAATTTAACCATTGCAGAGAATATTTTTCTCGGACGGGAATTTACCAAACCTTGGGGCGCCATTGATTGGCAACGCATGTATCGGGAAGCGGATAAGTTGTTGGCACGTCTGGGTGTCACCCACAGCAGCCAAACCCTTTGCGCTACGCTTTCCATCGGCGAACAGCAAATGGTGGAGATCGCCAAAGCCCTTAGTTTTGAATCCAAAGTCATTGTTATGGACGAACCCACCGACGCGCTCACCAACACCGAAACGGAAGCCTTATTTAAGGTAACCCGTGAGCTCAAGGCGGAAAATCGCGGCATTGTGTATATTTCCCACCGAATTAAAGAAATTTTTCAGATTTGCGATAATGTCACCGTGTTGCGCGACGGTCAGTTTATCGGCGAAAGTGCGGTGGAAAATTTAGATGAAAATCGTCTTATCGAAATGATGGTGGGTCGTCGTTTAGAAGAACAATATCCGCGTCTGGAACGGGCACCCGGCGAAGTGCGCTTGACGGTAAACCATCTCAGCGGCAGCGGCGTACATGATGTCTCCTTTGCATTGCGCAGCGGCGAGATTCTCAGTATTTCCGGCTTAATGGGCACCGGTCGCAGCGAATTAATGAAAGTGCTTTACGGTGCGCTGCCGCGAGAATCCGGTGAAGTGCGGTTAAATCAACGGGCGATTTTGAATCGTACGCCACAGGAAGGCTTACGTAACGGCATTGTGTATATTTCCGAAGACCGCAAAGGCGACGGGCTGATTTTAGGTATGTCGGTCAAAGAAAATATGTCCCTTACCGCGTTAGATTATTTCGCCAAAACCTTTCATATCGACCGGGCGGCGGAACGCATGGCAGTGGATGATTTTATCATGTTATTCAACATAAAAACGCCAAGCCGGGAGCAACCCATCGGGCTTCTTTCCGGCGGCAATCAACAAAAAGTCTCCATCGCCAAAGGCTTGATGACCCGTCCGCAGGTGCTGATTTTAGATGAGCCAACGCGTGGCGTAGATGTAGGCGTAAAAAAAGAAATTTATCAGCTCATTAATCAATTCAAAGGAGAAGGCATGAGCATTATTTTGGTCTCTTCCGAAATGCCCGAAGTGTTGGGCATGAGCGATCGCATTCTGGTGATGCGGGAAGGACATATCAGCGCCGAATTTCAGCGGGCTGACGCCACACAAGAAAAATTATTGGCAGCCGCCATCGAAAAACTCAATTCACAAGAGGCGATAATA","","","55418","MQQPLLKISGVDKSFPGVKALSNAGLSVYAGHAMALMGENGTGKSTLMKVLTGIYDKDTGSIEYLGKQVAFKGPKDSQEAGISIIHQELNLVGNLTIAENIFLGREFTKPWGAIDWQRMYREADKLLARLGVTHSSQTLCATLSIGEQQMVEIAKALSFESKVIVMDEPTDALTNTETEALFKVTRELKAENRGIVYISHRIKEIFQICDNVTVLRDGQFIGESAVENLDENRLIEMMVGRRLEEQYPRLERAPGEVRLTVNHLSGSGVHDVSFALRSGEILSISGLMGTGRSELMKVLYGALPRESGEVRLNQRAILNRTPQEGLRNGIVYISEDRKGDGLILGMSVKENMSLTALDYFAKTFHIDRAAERMAVDDFIMLFNIKTPSREQPIGLLSGGNQQKVSIAKGLMTRPQVLILDEPTRGVDVGVKKEIYQLINQFKGEGMSIILVSSEMPEVLGMSDRILVMREGHISAEFQRADATQEKLLAAAIEKLNSQEAII","144237","","D-ribose ABC transporter, ATP-binding protein / galactoside ABC transporter, ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR000169
Active_site
Peptidase, cysteine peptidase active site
PS00639\"[30-40]?THIOL_PROTEASE_HIS
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[143-184]T\"[396-438]TQ6LH11_PHOPR_Q6LH11;
PF00005\"[31-218]T\"[279-471]TABC_tran
PS50893\"[6-242]T\"[245-495]TABC_TRANSPORTER_2
PS00211\"[396-410]?ABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[30-249]T\"[278-472]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[3-245]T\"[252-499]Tno description
PTHR19222\"[6-301]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF12\"[6-301]TSUGAR ABC TRANSPORTER


","BeTs to 7 clades of COG1129COG name: ABC-type sugar (aldose) transport system, ATPase componentFunctional Class: GThe phylogenetic pattern of COG1129 is -----z--v--lb-efgh---j--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 8.3e-24) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 20-66 1.6e-11 IPB001140B 393-431 2.7e-07 IPB001140C 448-477 0.096","Residues 321 to 391 match (5e-07) PD:PD541106 which is described as ATP-BINDING COMPLETE ABC PROTEOME TRANSPORTER TRANSPORTER SUGAR NUCLEOTIDE BINDING/ATPASE PLASMID ","","","","","Mon Feb 17 11:21:22 2003","","","","","","","Fri Dec 6 14:14:59 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00207 is paralogously related to AA00751 (1e-114), AA01456 (1e-109), AA02786 (1e-101), AA02225 (9e-64), AA00933 (3e-52), AA02140 (4e-32), AA00934 (6e-30), AA02320 (1e-24), AA02080 (2e-21), AA00415 (1e-19), AA02440 (2e-19), AA01524 (9e-19), AA01779 (3e-18), AA01051 (7e-18), AA00799 (7e-18), AA01645 (1e-17), AA02550 (1e-17), AA00700 (3e-17), AA02573 (8e-17), AA01568 (1e-16), AA02718 (2e-16), AA02353 (7e-16), AA02484 (1e-15), AA02898 (2e-15), AA01656 (2e-15), AA01422 (3e-15), AA00858 (4e-15), AA01961 (1e-14), AA01867 (1e-14), AA01510 (2e-14), AA01616 (2e-14), AA01393 (4e-14), AA02899 (6e-14), AA01820 (6e-14), AA01757 (1e-13), AA02805 (2e-13), AA01684 (2e-13), AA02606 (2e-13), AA02609 (2e-12), AA01569 (3e-12), AA02152 (1e-11), AA02226 (5e-11), AA01947 (1e-10), AA02331 (1e-10), AA01509 (1e-09), AA01824 (2e-09), AA02324 (3e-09), AA02642 (8e-09), AA00591 (3e-08), AA00061 (2e-07), AA02146 (4e-07), AA01555 (8e-07), A02145 (2e-04) and AA01291 (3e-04).","","","","","","Residues 279 to 471 (E-value = 2.3e-32) place AA00207 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Bell,A.W., Buckel,S.D., Groarke,J.M., Hope,J.N., Kingsley,D.H. andHermodson,M.A.The nucleotide sequences of the rbsD, rbsA, and rbsC genes ofEscherichia coli K12J. Biol. Chem. 261 (17), 7652-7658 (1986)PubMed: 3011793 Buckel,S.D., Bell,A.W., Rao,J.K. and Hermodson,M.A.An analysis of the structure of the product of the rbsA gene ofEscherichia coli K12J. Biol. Chem. 261 (17), 7659-7662 (1986)PubMed: 3086314 Tatusov,R.L., Mushegian,A.R., Bork,P., Brown,N.P., Hayes,W.S.,Borodovsky,M., Rudd,K.E. and Koonin,E.V.Metabolism and evolution of Haemophilus influenzae deduced from awhole-genome comparison with Escherichia coliCurr. Biol. 6 (3), 279-291 (1996)PubMed: 8805245","","Mon Feb 17 06:35:56 2003","1","","","" "AA00208","144237","145130","894","ATGACTGAACAACAAAATATAAAGTTAGGTAAATTTTTACTGGAACAACGCTCAATTATCGCCTTATTGGTGCTTATTGGCGTCGTGTCGGCGATTAATCCCGATTTTTTCAGCGTGGATAATATTCTCAACATTTTGCGCCAAACCTCGGTAAACGCCATTATCGCCGTCGGCATGACTTTCGTGATTTTAATTGCCGGCATTGATTTATCCGTAGGTTCCATTCTCGCACTGACAGGGGCTTTCGCGGCAAGTATGGTGGGCGCGGAATTGCCGGTGTTATTGGTGATTCCGCTGGTTTTACTCATCGGCACGTTGCTCGGCGGCATCAGCGGCGTGATCGTCGCCAAAGGAAAAGTGCAGGCGTTTATTGCCACCCTAGTAACCATGACGTTATTACGCGGCGTCGCCATGGTTTATACGGACGGTCGCCCGATTAGTACCGGTTTTTCCGATACCGCTGATGCCTTCGCGTTTCTCGGCACCGGCTATTTATTCGTCATCCCGCTTCCGATTTGGTTAATGGCAATCGTGTTTTTAGTGTCTTGGTATGTGCTGAAACACACCAAAATAGGACGCTACATTTACGCCCTCGGCGGCAACGAAGCGGCAACCCGGCTGTCCGGCATCAACGTTAACAAAGTGAAAATTTTCGTATTTGCCGTCAGCGGCTTTCTATCCGCCCTTTCCGGACTTATCGTCACGTCCCGCCTCTCTTCCGCCCAACCCACTGCGGGTGTGTCTTACGAATTAGATGCCATCGCAGCGGTTGTGGTGGGCGGAACCAGTTTAATGGGCGGCAAAGGTCGGGTCATGGGCACACTCATCGGCGCGCTGATTATCGGATTTTTAAATAATGCACTGAATTTACTGATATTTCCTCTTACTATCAAA","","","31187","MTEQQNIKLGKFLLEQRSIIALLVLIGVVSAINPDFFSVDNILNILRQTSVNAIIAVGMTFVILIAGIDLSVGSILALTGAFAASMVGAELPVLLVIPLVLLIGTLLGGISGVIVAKGKVQAFIATLVTMTLLRGVAMVYTDGRPISTGFSDTADAFAFLGTGYLFVIPLPIWLMAIVFLVSWYVLKHTKIGRYIYALGGNEAATRLSGINVNKVKIFVFAVSGFLSALSGLIVTSRLSSAQPTAGVSYELDAIAAVVVGGTSLMGGKGRVMGTLIGALIIGFLNNALNLLIFPLTIK","145130","","D-ribose ABC transporter, permease protein / Galactoside transport system permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR001851
Family
Bacterial inner-membrane translocator
PF02653\"[41-294]TBPD_transp_2
noIPR
unintegrated
unintegrated
signalp\"[1-31]?signal-peptide
tmhmm\"[20-38]?\"[48-68]?\"[70-89]?\"[95-115]?\"[120-140]?\"[166-186]?\"[217-239]?\"[273-293]?transmembrane_regions


","BeTs to 7 clades of COG1172COG name: Ribose/xylose/arabinose/galactoside ABC-type transport systems, permease componentsFunctional Class: GThe phylogenetic pattern of COG1172 is --------v-rlb-efgh---j--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 2.4e-11) to 2/2 blocks of the IPB001851 family, which is described as \"Binding-system dependent bacterial transporters (araH, livH/limM families)\". Interpro entry for IP:IPR001851. IPB001851A 191-205 0.00031 IPB001851B 250-261 2.6e-05","Residues 20 to 77 match (5e-07) PD:PD522318 which is described as COMPLETE PROTEOME PERMEASE TRANSPORTER ABC L-ARABINOSE SUGAR SYSTEM TRANSMEMBRANE MEMBRANE ","","","","","","","","","","","","Wed Dec 4 16:19:34 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00208 is paralogously related to AA02785 (3e-53), AA01457 (2e-52), AA00753 (7e-44), AA00936 (4e-36), AA02224 (7e-34), AA02220 (1e-32) and AA00935 (3e-18).","","","","","","Residues 41 to 297 (E-value = 9.1e-59) place AA00208 in the BPD_transp_2 family which is described as Branched-chain amino acid transport system / permease component (PF02653)","","","","","Bell,A.W., Buckel,S.D., Groarke,J.M., Hope,J.N., Kingsley,D.H. and Hermodson,M.A. The nucleotide sequences of the rbsD, rbsA, and rbsC genes of Escherichia coli K12 J. Biol. Chem. 261 (17), 7652-7658 (1986) PubMed: 3011793 Hogg,R.W., Voelker,C. and Von Carlowitz,I.Nucleotide sequence and analysis of the mgl operon of Escherichiacoli K12Mol. Gen. Genet. 229 (3), 453-459 (1991)PubMed: 1719366 ","","Wed Dec 4 16:19:34 2002","1","","","" "AA00209","145223","146092","870","ATGAAAAAACTAACCACATTAGCCACCGCACTTTTATTGAGTTTCAGCACCTCAGCACTGGCGCAGGACACGATCGCCCTCACCGTTTCCACACTGGACAACCCGTTTTTCGTATCCTTAAAAGAAGGTGCGCAGAAAAAAGCCGATGAACTGGGCTACAAACTGGTGGTGCTGGATTCTCAAAATGACCCGGCGAAGGAGCTGGCAAACGTAGAAGATTTACTGGTGCGCGGCGCGAAAGTGTTGCTGATTAACCCGACCGATTCGGAAGCGGTAAGCAATGCCGTCGCCATCGCCAATCGCAATAAAATTCCGGTTATCACCTTAGACCGTGGTGCGGCAAAAGGCGAAGTGGTGAGCCATATCGCATCCGACAACGTTGCCGGCGGCAAAATGGCAGGCGATTTTATCGCGCAAAAACTTGGTGCCAATGCCAAAGTCATTCAATTAGAAGGCTTGGCGGGCACTTCCGCCGCCCGTGAACGGGGCGAGGGCTTCAAGCAAGCGGTTGCCGAACATAAATTTGATGTACTTGCCAATCAACCGGCTGATTTTGACCGCACGAAAGGCTTAAATGTGATGGAAAATCTGCTTGCCACCAAAGGCACGGTTCAAGCCGTATTCGCTCAAAATGATGAAATGGCATTAGGCGCATTGCGCGCGTTATCCGCCGCCAATAAAAAAGTCCTCGTGGTTGGCTTTGACGGCACCGATGACGGCATGAAAGCGGTAAAAAGCGGAAAAATGGCGGCAACAATCGCTCAACAACCGGCGTTAATCGGCGAACTTGGCGTGGTGACGGCAGACAAATTGCTTAAAGGCGAAAAAGTAGAAGCCAAAATTCCGGTAGATCTCAAAGTCATCAGCGAA","","","30304","MKKLTTLATALLLSFSTSALAQDTIALTVSTLDNPFFVSLKEGAQKKADELGYKLVVLDSQNDPAKELANVEDLLVRGAKVLLINPTDSEAVSNAVAIANRNKIPVITLDRGAAKGEVVSHIASDNVAGGKMAGDFIAQKLGANAKVIQLEGLAGTSAARERGEGFKQAVAEHKFDVLANQPADFDRTKGLNVMENLLATKGTVQAVFAQNDEMALGALRALSAANKKVLVVGFDGTDDGMKAVKSGKMAATIAQQPALIGELGVVTADKLLKGEKVEAKIPVDLKVISE","146092","","D-ribose ABC transporter, periplasmic-binding protein","Periplasm, Cytoplasm","","
InterPro
IPR001761
Domain
Periplasmic binding protein/LacI transcriptional regulator
PF00532\"[22-226]TPeripla_BP_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2300\"[124-267]Tno description
signalp\"[1-21]?signal-peptide


","BeTs to 7 clades of COG1879COG name: Periplasmic sugar-binding proteinsFunctional Class: GThe phylogenetic pattern of COG1879 is --------v-rlb-efgh---j--t-Number of proteins in this genome belonging to this COG is","","Residues 24 to 195 match (2e-07) PD:PD553319 which is described as PERIPLASMIC Y4MI PROBABLE ABC PLASMID SUGAR BINDING SIGNAL PRECURSOR TRANSPORTER ","","","","","","","","","","","","Fri Dec 6 14:13:17 2002","","Wed May 12 16:29:29 2004","","Wed May 12 16:29:29 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00209 is paralogously related to AA00932 (2e-34), AA02787 (2e-29), AA02788 (1e-26), AA01455 (5e-20), AA00750 (1e-17), AA00749 (9e-12), AA02003 (2e-10), AA02673 (2e-09), AA02219 (3e-08) and AA02006 (6e-08).","Wed May 12 16:29:29 2004","","","","","Residues 22 to 289 (E-value = 1.1e-09) place AA00209 in the Peripla_BP_1 family which is described as Periplasmic binding proteins and sugar binding domain of the LacI family (PF00532)","Wed May 12 16:29:29 2004","",""," James D, Shao H, Lamont RJ, Demuth DR.,The Actinobacillus actinomycetemcomitans ribose binding protein RbsB interacts with cognate and heterologous autoinducer 2 signals.Infect Immun. 2006 Jul;74(7):4021-9.PMID: 16790775","Buckenmeyer,G.K. and Hermodson,M.A.The amino acid sequence of D-ribose-binding protein from Salmonellatyphimurium ST1J. Biol. Chem. 258 (21), 12957 (1983)PubMed: 6415058Groarke,J.M., Mahoney,W.C., Hope,J.N., Furlong,C.E., Robb,F.T.,Zalkin,H. and Hermodson,M.A.The amino acid sequence of D-ribose-binding protein fromEscherichia coli K12J. Biol. Chem. 258 (21), 12952-12956 (1983)PubMed: 6313683","","Wed Dec 4 16:40:02 2002","1","","","" "AA00211","146095","146223","129","ATGCGTCGCCACACAAAAAGTGCGGTCGTTTTTACAAACGTTTTTGAAGAGCGCGCTGTGCGTTCTTTTTTTCAGGAGGGATTATGTGCGCTAAACTCGTTGTGCTCGGCAGCGTTAACGCCGATCATA","","","4797","MRRHTKSAVVFTNVFEERAVRSFFQEGLCALNSLCSAALTPII","146223","","hypothetical protein","Cytoplasm","No significant similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 12:09:36 2004","Sun Feb 22 12:09:36 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00211 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 12:10:21 2004","","","","","","","","","","","","","1","","","" "AA00212","146196","147107","912","GTGCTCGGCAGCGTTAACGCCGATCATATGATTCGTGTCCCGCGTTTTGCTCGCGCCGGTGAAACGTTACGCGGCTCCGGTTACCGCATTGCTTACGGCGGCAAAGGTGCTAATCAGGCGGTAGCTGCCGCACGGTTAAAAGATCCAAACACGCAGGTGGATTTTATCGCCTGCCTTGGTAACGATGACATAGGTCGTACCATGAAAGCCGCTTTTGCAAAAGACGGCATTAACACGGCGACCATAACTCAAGTTGAGCAGGAAATGACGGGGGTCGCTATGATTCAAGTGGCGGACAACGGCGAAAACAGCATTGTAATTAACGCCGGTGCCAATGCCTGTCTGGACGAACATCTCGTTTCCTGTTATGCCGCGCATATTCAACAAGTGGATGCCTTGTTAATGCAGCTGGAAACCCCTCTTTCGGCAATTTGTAAAGCGGCGCAAATCGCCAAACAAAACGGTACAAAAGTGATTCTTAATCCTGCGCCGGCGCAAGCATTACCGGAAGAATTGCTCCGGCAGTTATATATGATTACACCAAATGAAACGGAAGCGGAAATCCTGACGGACATTAAAGTGGAAGATAAAATCTCGGCAGCACAGGCGGCAAAAAGATTCCATCAACTAGGCGTGCAAATCGTGCTTATTACCCTGGGTGCCAAAGGGGTTTATTTCAGTGAAAATGGTCAGGGGCAAATTATCGGCGGTTTTCGCGTAAAAGCGAAAGACACCACGGCAGCAGGCGATACCTTCAATGGTGCCTTGGCGGTTGCGTTACTGGAAGGAAAAACATTGACGAATGCCATTCGCTTCGCCCACGCAGCGGCGGCAATCAGCGTCACCCGCGAAGGTGCGCAGCCCTCAATTCCGAGCCGTGCGGAAGCCTTGGATTTTCTTGAAAAGCAGGGA","","","32713","VLGSVNADHMIRVPRFARAGETLRGSGYRIAYGGKGANQAVAAARLKDPNTQVDFIACLGNDDIGRTMKAAFAKDGINTATITQVEQEMTGVAMIQVADNGENSIVINAGANACLDEHLVSCYAAHIQQVDALLMQLETPLSAICKAAQIAKQNGTKVILNPAPAQALPEELLRQLYMITPNETEAEILTDIKVEDKISAAQAAKRFHQLGVQIVLITLGAKGVYFSENGQGQIIGGFRVKAKDTTAAGDTFNGALAVALLEGKTLTNAIRFAHAAAAISVTREGAQPSIPSRAEALDFLEKQG","147107","","ribokinase","Cytoplasm","","
InterPro
IPR002139
Family
Ribokinase
PR00990\"[1-22]T\"[28-47]T\"[103-116]T\"[171-186]T\"[215-226]TRIBOKINASE
InterPro
IPR002173
Family
Carbohydrate kinase, PfkB
PS00584\"[244-257]?PFKB_KINASES_2
InterPro
IPR011611
Domain
PfkB
PF00294\"[1-293]TPfkB
InterPro
IPR011877
Family
Ribokinase, bacterial
TIGR02152\"[1-298]TD_ribokin_bact: ribokinase
noIPR
unintegrated
unintegrated
G3DSA:3.40.1190.20\"[1-303]Tno description
PTHR10584\"[1-301]TSUGAR KINASE RELATED
PTHR10584:SF29\"[1-301]TRIBOKINASE


","BeTs to 17 clades of COG0524COG name: Sugar kinases, ribokinase familyFunctional Class: GThe phylogenetic pattern of COG0524 is aompkzy-vdrlbcefghs--j----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-12) to 2/2 blocks of the IPB002173 family, which is described as \"PfkB family of carbohydrate kinases\". Interpro entry for IP:IPR002173. IPB002173A 32-47 5.4e-06 IPB002173B 243-257 6.5e-05","Residues 100 to 300 match (3e-15) PD:PD432502 which is described as (see also SP:Q9AI19_ECOLI_Q9AI19).","","","","","Wed Feb 19 08:49:02 2003","","","","","","","Wed Dec 4 16:54:11 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00212 is paralogously related to AA02384 (1e-16), AA02797 (4e-10), AA00333 (2e-07) and AA02584 (4e-07).","","","","","","Residues 1 to 293 (E-value = 2.2e-77) place AA00212 in the PfkB family which is described as pfkB family carbohydrate kinase (PF00294)","","","","","Hope,J.N., Bell,A.W., Hermodson,M.A. and Groarke,J.M.Ribokinase from Escherichia coli K12. Nucleotide sequence andoverexpression of the rbsK gene and purification of ribokinaseJ. Biol. Chem. 261 (17), 7663-7668 (1986)PubMed: 3011794Sigrell,J.A., Cameron,A.D., Jones,T.A. and Mowbray,S.L.Structure Of Escherichia Coli Ribokinase In Complex With RiboseAnd Nucleotide Determined To 1.8 A Resolution: Insights Into A NewFamily Of Kinase Structures Structure London), 183 (1998)","","Wed Dec 4 16:54:11 2002","1","","","" "AA00213","147417","147211","207","ATGTCTAAATTAAACGGCACCGTAAAATGGTTTAACTCCATAAAAGGCTTTGGTTTTATCGCTCCCACGGATGGTTCAAAAGATGTATTCGTACATTTCTCCGGCATCGTCGGTAACAATTTCCGTACTTTAAACGAAGGCGACCATGTGGCGTATAACGTACAGAATTCCCAACGCGGACCGACAGCAATTGAAGTTGAAGTGGTT","","","7526","MSKLNGTVKWFNSIKGFGFIAPTDGSKDVFVHFSGIVGNNFRTLNEGDHVAYNVQNSQRGPTAIEVEVV","147211","","cold shock protein (negative regulator of cspA transcription)","Cytoplasm, Extracellular","","
InterPro
IPR002059
Domain
Cold-shock protein, DNA-binding
PD000621\"[22-69]TQ9CMZ5_PASMU_Q9CMZ5;
PR00050\"[6-21]T\"[27-36]T\"[42-60]TCOLDSHOCK
PF00313\"[3-69]TCSD
PS00352\"[17-36]TCOLD_SHOCK
InterPro
IPR011129
Domain
Cold shock protein
SM00357\"[5-69]TCSP
InterPro
IPR012156
Family
Cold shock, CspA
PIRSF002599\"[4-69]TCold shock protein, CspA type
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[3-69]Tno description
noIPR
unintegrated
unintegrated
PTHR11544\"[1-63]TCOLD SHOCK DOMAIN CONTAINING PROTEINS


","BeTs to 13 clades of COG1278COG name: Cold shock proteinsFunctional Class: KThe phylogenetic pattern of COG1278 is -o-----qvdrlb-efghsn-jx---Number of proteins in this genome belonging to this COG is","Significant hit ( 4.6e-23) to 2/2 blocks of the IPB002059 family, which is described as \"Cold-shock DNA-binding domain\". Interpro entry for IP:IPR002059. IPB002059A 6-20 2.2e-08 IPB002059B 28-66 3.7e-13","Residues 22 to 69 match (2e-09) PD:PD580670 which is described as TRANSCRIPTION COLD DNA-BINDING REGULATION ACTIVATOR PROTEOME COMPLETE SHOCK SHOCK-LIKE FAMILY ","","","","","","","","","","","","Mon Feb 17 06:18:41 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00213 is paralogously related to AA02273 (4e-10).","","","","","","Residues 3 to 69 (E-value = 2.5e-33) place AA00213 in the CSD family which is described as 'Cold-shock' DNA-binding domain (PF00313)","","","","","Lee,S.J., Xie,A., Jiang,W., Etchegaray,J.P., Jones,P.G. andInouye,M.Family of the major cold-shock protein, CspA (CS7.4), ofEscherichia coli, whose members show a high sequence similaritywith the eukaryotic Y-box binding proteinsMol. Microbiol. 11 (5), 833-839 (1994)PubMed: 8022261Yamanaka,K., Mitani,T., Ogura,T., Niki,H. and Hiraga,S.Cloning, sequencing, and characterization of multicopy suppressorsof a mukB mutation in Escherichia coliMol. Microbiol. 13 (2), 301-312 (1994)PubMed: 7984109Goldstein,J., Pollitt,N.S. and Inouye,M.Major cold shock protein of Escherichia coliProc. Natl. Acad. Sci. U.S.A. 87 (1), 283-287 (1990)PubMed: ","","Mon Feb 17 06:18:41 2003","1","","","" "AA00214","149309","147867","1443","ATGAAATTAGAGGCATTATTTGATTTGGATCCAAATGTGAAAGTGCGTACCCGTTTTGCGCCAAGCCCGACCGGTTATTTACATGTCGGCGGTGCCAGAACCGCACTTTATTCTTGGTTATATGCAAAACATAACCATGGTGAATTTGTGTTGCGTATCGAAGATACTGATTTGGAACGCTCCACCCCAGAAGCGACGCAAGCTATTTTAGAAGCGATGGAATGGCTGGATTTGGCATGGGAACATGGTCCGTATTATCAAACCAAACGTTTTGATCGTTACAATCAGGTGATTGATCAAATGATTGAACAAGGCTTGGCATACCGTTGCTACTGCACTAAAGAACGCTTGGATGCGTTGCGTCATACACAAGAGAAAAATAAAGAAAAACCGCGTTATGACCGTCATTGCTTGCATGATCACGCCTATCACTCTGCTGACGAACCGCACGTTGTGCGTTTTAAAAATCCGACGGAAGGTTCCGTGGTTTTTGATGACGCTGTGCGCGGACGCATTGAAATCAGCAACAGCGAATTGGACGATTTGATTATCCGTCGCACCGACGGATCACCGACCTACAATTTCTGCGTGGTGGTGGATGACTGGGACATGGGCATTACCCATGTTGTGCGGGGCGAAGACCACATTAACAACACCCCACGTCAAATTAACATCTTAAAAGCGCTCGATGCACCGATTCCGGTGTATGCCCACGTTTCCATGATTAACGGCGATGACGGGCAAAAACTTTCCAAACGCCATGGCGCGGTGAGCGTCATGCAATATCGCGACGAAGGTTATCTGCCGGAAGCGCTCATCAACTATTTGGTACGCTTAGGCTGGGGACACGGCGATCAGGAAATCTTCACCCGTGAAGAAATGATTGAATTGTTCGATTTGCATTCCGTCAGCAAATCCGCCAGTGCGTTTAATACGGAAAAATTATTGTGGTTGAACCATCATTATATTCGTGAATTACCGGCAGACTATGTAGCGAAACATCTGGCATGGCAATATCAGGATCTTGGTATTGACACCGCCAACGGTCCGGCATTAACGGAAATTGTTGCCATGTTGGCGGATCGCTGCAAAACTTTACGGGAAATGGCGCTGGCAAGCCGTTATTTCTTTGAAGAATTCGACGAATTTGATGAAGCAGCGGCTAAAAAACATTTCAAAGCCGGTTCCGTAGAGACCCTCGAAAAAGTAAAAGAAAAACTGACCGCACTTTCCGGCTGGGATTTACATTCCACTCATGAAGCCATTGAACAAACCGCCGCCGAATTAGAGGTCGGCATGGGCAAAGTGGGGATGCCTTTGCGTGTTGCCGTTACCGGTGCGGGACAATCGCCGTCAATGGATGTCACCCTGGTCGGCATCGGACGCGAACGCGTATTAAACCGCATTCAACGTGCCATTGATTTTATTAAAGCGCAAAACGCT","","","54886","MKLEALFDLDPNVKVRTRFAPSPTGYLHVGGARTALYSWLYAKHNHGEFVLRIEDTDLERSTPEATQAILEAMEWLDLAWEHGPYYQTKRFDRYNQVIDQMIEQGLAYRCYCTKERLDALRHTQEKNKEKPRYDRHCLHDHAYHSADEPHVVRFKNPTEGSVVFDDAVRGRIEISNSELDDLIIRRTDGSPTYNFCVVVDDWDMGITHVVRGEDHINNTPRQINILKALDAPIPVYAHVSMINGDDGQKLSKRHGAVSVMQYRDEGYLPEALINYLVRLGWGHGDQEIFTREEMIELFDLHSVSKSASAFNTEKLLWLNHHYIRELPADYVAKHLAWQYQDLGIDTANGPALTEIVAMLADRCKTLREMALASRYFFEEFDEFDEAAAKKHFKAGSVETLEKVKEKLTALSGWDLHSTHEAIEQTAAELEVGMGKVGMPLRVAVTGAGQSPSMDVTLVGIGRERVLNRIQRAIDFIKAQNA","147867","","glutamyl-tRNA synthetase","Cytoplasm","","
InterPro
IPR000924
Family
Glutamyl-tRNA synthetase, class Ic
PR00987\"[18-30]T\"[32-43]T\"[47-60]T\"[191-201]T\"[207-215]TTRNASYNTHGLU
PTHR10119\"[18-477]TGLUTAMYL/GLUTAMINYL-TRNA SYNTHETASE
PF00749\"[14-317]TtRNA-synt_1c
InterPro
IPR001412
Family
Aminoacyl-tRNA synthetase, class I
PS00178\"[21-32]TAA_TRNA_LIGASE_I
InterPro
IPR004527
Family
Glutamyl-tRNA synthetase bacterial/mitochondrial
TIGR00464\"[14-478]TgltX_bact: glutamyl-tRNA synthetase
InterPro
IPR008925
Domain
Class I aminoacyl-tRNA synthetase, anticodon-binding
G3DSA:1.10.10.350\"[377-474]Tno description
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620\"[14-243]Tno description
noIPR
unintegrated
unintegrated
G3DSA:1.10.1160.10\"[244-327]Tno description
PTHR10119:SF1\"[18-477]TGLUTAMYL-TRNA SYNTHETASE 1, 2, 3 (GLUTAMATE--TRNA LIGASE 1, 2, 3)


","No hits to the COGs database.","","Residues 267 to 308 match (7e-10) PD:PD491026 which is described as SYNTHETASE PROTEOME COMPLETE LIGASE GLUTAMYL-TRNA AMINOACYL-TRNA GLURS ATP-BINDING GLUTAMATE--TRNA BIOSYNTHESIS ","","","","","","","","","","","","Wed Feb 12 10:21:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00214 is paralogously related to AA02082 (2e-12).","","","","","","Residues 14 to 317 (E-value = 3.6e-185) place AA00214 in the tRNA-synt_1c family which is described as tRNA synthetases class I (E and Q), catalytic domain (PF00749)","","","","","Breton,R., Sanfacon,H., Papayannopoulos,I., Biemann,K. and Lapointe,J. Glutamyl-tRNA synthetase of Escherichia coli. Isolation andprimary structure of the gltX gene and homology with otheraminoacyl-tRNA synthetases J. Biol. Chem. 261 (23), 10610-10617 (1986) PubMed: 3015933 Brun,Y.V., Sanfacon,H., Breton,R. and Lapointe,J. Closely spaced and divergent promoters for an aminoacyl-tRNA synthetase gene and a tRNA operon in Escherichia coli. Transcriptional and post-transcriptional regulation of gltX, valU and alaW J. Mol. Biol. 214 (4), 845-864 (1990) PubMed: 2201777 ","","Wed Dec 4 17:47:31 2002","1","","","" "AA00216","149997","150782","786","ATGAATAAACCAATTAAAAATCAGACCGCACTTTTCATTTCTAACGGCTTGTTACGTTTAGCCGGCAATATTGTCAAAATCCTAAGTTACCCGTTCCACGCGATTTTTCCGAAAAAGCGCTTTACCATTCCGGAATTCAGCCCGGCAAGACACCCAACCAATAAGCCCGGCAAAATCAATAAAGTCATCTGGCAAACCAACTACAGCAACCAAGTTACCTTACCGATTTATTGTAACTATTTGGTCAATCGCCTGTTTTCGCCCGGTTATGATTACCGTTATGTGAGCACCGAAGCGCGCGGCGATTATATTGAAAAAAATGCCGATGCCCGCACATTCGCCGCGTATAGCAAACTTACCGACGGCGCGGCGCAGGCGGATTTCTGGCGTTTATTCACGCTCTACCACGACGGTGGTATTTACATGGACATCGACGGCCATTTGGTCGGCAATTTGGATAAGATGATTGATCCCGAAGACAACGAAGTACTCATTACGCGCCGTGGTCGTTACACCAATTTCTTTTTAGCCAGTCGCAAAAGCAATCCGTTTTTGAAAGAAACTCTGGACATTATTATTGATAATATCGAAAACCGTCGTATTGACGGCGGCGTGTTTGTCCTCACCGGTCCCGATACGCTCAATAAAGCGCTGGAAAACAAAGATGTCAACACCCGCCGCGATAAATTGACCTGCGCACAAGGCACCTTTGCCAACGAATATTTTCAATATATGGATAAAAAACGCGGCAAATGGATTCACGCGAAAAACGAAGATTTATTAAAA","","","30221","MNKPIKNQTALFISNGLLRLAGNIVKILSYPFHAIFPKKRFTIPEFSPARHPTNKPGKINKVIWQTNYSNQVTLPIYCNYLVNRLFSPGYDYRYVSTEARGDYIEKNADARTFAAYSKLTDGAAQADFWRLFTLYHDGGIYMDIDGHLVGNLDKMIDPEDNEVLITRRGRYTNFFLASRKSNPFLKETLDIIIDNIENRRIDGGVFVLTGPDTLNKALENKDVNTRRDKLTCAQGTFANEYFQYMDKKRGKWIHAKNEDLLK","150782","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR007577
Domain
Glycosyltransferase sugar-binding region containing DXD motif
PF04488\"[90-173]TGly_transf_sug


","BeTs to 3 clades of COG3774COG name: Mannosyltransferase OCH1 and related enzymesFunctional Class: MThe phylogenetic pattern of COG3774 is ------y---------gh--------Number of proteins in this genome belonging to this COG is","","Residues 185 to 262 match (2e-25) PD:PD274959 which is described as PROTEOME COMPLETE PM1116 VC0234 ","","","","","","","","","","","","Wed Dec 4 17:50:32 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00216 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 90 to 173 (E-value = 9.5e-22) place AA00216 in the Gly_transf_sug family which is described as Glycosyltransferase sugar-binding region containing DXD motif (PF04488)","","","","","","","","1","","","" "AA00217","150885","150796","90","TTGTTATTTGTGAAATCGGTTAAAAAATATATCACAGAAACAAAAAAGGCGATCAACAAAAATCTGCTTTTTGTGACCGCACTTTTTGCT","","","3424","LLFVKSVKKYITETKKAINKNLLFVTALFA","150796","","hypothetical protein","Cytoplasm","No significant similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 12:11:21 2004","Sun Feb 22 12:11:21 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00217 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 12:12:11 2004","","","","","","","","","","","","","1","","","" "AA00218","150898","152271","1374","ATGGCACTTTGGGGTGGACGCTTCACGCAAGCTGCGGATAAGCGTTTTAAAAACTTTAACGACTCATTACGCTTTGACTACCGTTTGGCAGAGCAAGACATCGAAGGCTCAATCGGCTGGTCGAAAGCGTTGGTATCCGTGGGCATTTTAGATGTGCAGGAACAACAACAATTAGAACAGGCATTGCACGAATTATTAGTTGAAGTGCGGTCAAATCCGCAAGCGATTTTACAAGATGACGCGGAAGACATCCACAGCTGGGTGGAAAGTAAGCTCATTGATAAGGTAGGCAATTTAGGCAAAAAACTGCACACCGGGCGCAGCCGCAACGACCAAGTGGCACTCGACATCAAAATGTGGTGTAAACAACGGGTTGCCGAATTGCAGCATTCTATCCGTGACTTACAGCGTAAATTGGTGCTCACCGCAGAAAACAATCAGGATGCCGTGATGCCAGGCTACACCCACCTGCAACGCGCCCAACCGATCACCTTTGCCCATTGGTGCATGGCGTATGTGGAAATGCTGGATCGCGATTATTCCCGTTTAGCTGATGCCTACCGTCGCATGAACAGCTGCCCGCTCGGTAGCGGCGCCCTTGCCGGCACGGCATATCCTATCGATCGCGAACGGTTCGCCAAGGATCTGGATTTCGCCTTCGCCACCCGTAACAGCTTGGACAGCGTATCCGATCGCGATCACATTGTGGAACTGCTCTCCGCCGCGTCCCTTAGCATGGTGCATTTATCCCGTTTCGCCGAAGACATGATTATTTTCAGCAGCGGCGAATCCAACTTTGTGGAACTCTCCGATCGCGTAACGTCCGGTTCTTCCCTGATGCCGCAAAAGAAAAATCCCGATGCCTGCGAATTGATTCGCGGTAAAGCGGGGCGCGTAATCGGCGCCCTAAACGGCATGCTGATGACACTGAAAGGTTTGCCGTTAGCCTACAACAAAGATATGCAGGAAGACAAAGAAGGCATTTTCGATGCGTTGGATACTTGGCAAGATTGCTTAGATATGGCGTCTTTGGTGTTGGATGATATTAAAGTGAACGTGGAACGCACCCGCGAATCCGCGCTAAAAGGCTACTCTAACGCCACCGAATTGGCAGATTACTTGGTCGCTAAAGGCGTGCCGTTCCGCGATTCCCACCACATTGTGGGCGAGACCGTGGTATATGCCATTAAGCAACACAAGGCGTTAGAAGAATTGACTATTCCGGAATTCCGTCAATTCTGCGAAAAAGTGTCGGACGATGTGTACGATATTCTGTCTCTGCAATCCTGTTTAGACAAACGTGCCGCCAAAGGCGGGGTTTCACCGTTGCGCATTGCCGAAGCCATTGCTGACGCAAAAGCCCGATTTGCGTCG","","","51340","MALWGGRFTQAADKRFKNFNDSLRFDYRLAEQDIEGSIGWSKALVSVGILDVQEQQQLEQALHELLVEVRSNPQAILQDDAEDIHSWVESKLIDKVGNLGKKLHTGRSRNDQVALDIKMWCKQRVAELQHSIRDLQRKLVLTAENNQDAVMPGYTHLQRAQPITFAHWCMAYVEMLDRDYSRLADAYRRMNSCPLGSGALAGTAYPIDRERFAKDLDFAFATRNSLDSVSDRDHIVELLSAASLSMVHLSRFAEDMIIFSSGESNFVELSDRVTSGSSLMPQKKNPDACELIRGKAGRVIGALNGMLMTLKGLPLAYNKDMQEDKEGIFDALDTWQDCLDMASLVLDDIKVNVERTRESALKGYSNATELADYLVAKGVPFRDSHHIVGETVVYAIKQHKALEELTIPEFRQFCEKVSDDVYDILSLQSCLDKRAAKGGVSPLRIAEAIADAKARFAS","152271","","argininosuccinate lyase","Cytoplasm","","
InterPro
IPR000362
Domain
Fumarate lyase
PR00149\"[103-121]T\"[148-164]T\"[232-259]T\"[276-292]TFUMRATELYASE
PF00206\"[6-301]TLyase_1
PS00163\"[276-285]TFUMARATE_LYASES
InterPro
IPR003031
Domain
Delta crystallin
PR00145\"[102-124]T\"[143-163]T\"[194-210]T\"[232-256]T\"[276-292]T\"[311-330]TDCRYSTALLIN
InterPro
IPR009049
Domain
Argininosuccinate lyase
TIGR00838\"[3-457]TargH: argininosuccinate lyase
noIPR
unintegrated
unintegrated
G3DSA:1.20.200.10\"[120-390]Tno description
PTHR11444\"[1-457]TASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE
PTHR11444:SF3\"[1-457]TARGININOSUCCINATE LYASE


","No hits to the COGs database.","Significant hit ( 7.8e-17) to 2/2 blocks of the IPB000362 family, which is described as \"Fumarate lyase\". Interpro entry for IP:IPR000362. IPB000362A 153-166 1.2e-08 IPB000362B 276-286 1.5e-06","Residues 176 to 421 match (2e-57) PD:PD548333 which is described as LYASE ADENYLOSUCCINATE PROTEOME COMPLETE BIOSYNTHESIS PURINE ASL ADENYLOSUCCINASE CYCLOISOMERASE ISOMERASE ","","","","","","","","","","","","Wed Dec 4 17:53:18 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00218 is paralogously related to AA01717 (2e-10) and AA01277 (6e-09).","","","","","","Residues 6 to 301 (E-value = 9.7e-123) place AA00218 in the Lyase_1 family which is described as Lyase (PF00206)","","","","","Parsot,C., Boyen,A., Cohen,G.N. and Glansdorff,N. Nucleotide sequence of Escherichia coli argB and argC genes: comparison of N-acetylglutamate kinase and N-acetylglutamate-gamma-semialdehyde dehydrogenase with homologousand analogous enzymes Gene 68 (2), 275-283 (1988) PubMed: 2851495 Troshina O, Hansel A, Lindblad P. Cloning, characterization, and functional expression inEscherichia coli of argH encoding argininosuccinate lyase in the cyanobacterium Nostoc sp. strain PCC 73102. Curr Microbiol. 2001 Oct;43(4):260-4. PMID: 11683360 Auchincloss AH, Loroch AI, Rochaix JD. The argininosuccinate lyase gene of Chlamydomonas reinhardtii:cloning of the cDNA and its characterization as a selectable shuttle marker. Mol Gen Genet. 1999 Feb;261(1):21-30. PMID: 10071206 ","","Mon Jan 27 14:50:40 2003","1","","","" "AA00221","152576","153925","1350","ATGTCTGGTTCGGTCCCTTCCTTAGAAGCATTTTTAGCTAAAGTCGAACAACGCGATGGTAACCAACCTGAATTTTTACAAGCTGTTCGTGAAGTGTTTACTTCCATCTGGCCATTTCTTGAACAAAATCCGAAATATTGTTCCGAAGCCTTATTAGAACGTCTTGTAGAACCTGAACGCGCCATTCAGTTTCGCGTAGCATGGACGGACGATAAAGGTCAAGTGCAAGTCAACCGCGCATTCCGTATTCAATTTAACAGTGCCATCGGTCCGTTCAAAGGCGGCATGCGTTTTCACCCTTCCGTAAACCAATCCATTTTAAAATTCTTAGGGTTTGAACAAATCTTCAAAAACGCCCTAACCACCTTACCGATGGGCGGCGCCAAAGGCGGTTCCGACTTCGATCCGAAAGGCAAAAGCGATGCGGAAGTCATGCGTTTCTGTCAAGCGCTTATGGCGGAACTTTATCGCCATATCGGTCCGGACACCGACATACCGGCAGGAGACATCGGTGTGGGCGGTCGTGAAGTAGGTTATTTAACCGGCATGATGAAAAAACTCTCTAACCAAACCGGCTGCGTATTCACCGGTAAAGGCTTAACCTTCGGCGGTAGCTTAATTCGTCCGGAAGCCACCGGTTACGGCTTGGTTTATTTCGTACAAGCCATGCTGGCGGAAAAAGGTCAGGATTTAAAAGGCAAAACCGTGGCGGTTTCAGGTTCCGGCAACGTGGCGCAATATGCCATCGAAAAAGCGTTGGAATTAGGCGCAAAAGTCATTAGCTGTTCCGACTCTTCGGGCACGGTTGTGGATGAAGAAGGCTTCACCACCGAAAAATTAGCCGCACTGATGGAAATCAAAAATGTGAAACGCGGTCGCGTTAAAGATTACGCCGATCAGTTCGGATTGAAATATGTGGCAGGCGCGCGCCCATGGCACTTAAAAGTGGATGTTGCTCTGCCTTGCGCAACCCAAAACGAATTGGCATTGAGCGACGCGCAAACCCTTATCGCCAACGACGTACAAGTGGTGGCGGAAGGCGCCAATATGCCAACCACCATCGACGCCACCAATGCCTTCATTGACGCCGGCGGCGTATTATTCGGACCGGGCAAAGCAGCGAATGCAGGTGGTGTGGCAACTTCCGGCTTAGAAATGTCGCAAAATGCACAACGTTTAAGCTGGACCCGCGAAGAAGTGGACACGAAATTACACAGCATCATGCTGGATATTCACGCTAACTGTAAAAAATACGGCTCCAACGCCCAAGGCAACATCAACTATGTGGTGGGCGCCAACATCGCCGGTTTCGTGAAAGTCGCCGATGCCATGTTGGCACAAGGGGTGTAT","","","48308","MSGSVPSLEAFLAKVEQRDGNQPEFLQAVREVFTSIWPFLEQNPKYCSEALLERLVEPERAIQFRVAWTDDKGQVQVNRAFRIQFNSAIGPFKGGMRFHPSVNQSILKFLGFEQIFKNALTTLPMGGAKGGSDFDPKGKSDAEVMRFCQALMAELYRHIGPDTDIPAGDIGVGGREVGYLTGMMKKLSNQTGCVFTGKGLTFGGSLIRPEATGYGLVYFVQAMLAEKGQDLKGKTVAVSGSGNVAQYAIEKALELGAKVISCSDSSGTVVDEEGFTTEKLAALMEIKNVKRGRVKDYADQFGLKYVAGARPWHLKVDVALPCATQNELALSDAQTLIANDVQVVAEGANMPTTIDATNAFIDAGGVLFGPGKAANAGGVATSGLEMSQNAQRLSWTREEVDTKLHSIMLDIHANCKKYGSNAQGNINYVVGANIAGFVKVADAMLAQGVY","153925","","NADP-specific glutamate dehydrogenase","Cytoplasm, Periplasm","","
InterPro
IPR006095
Family
Glu/Leu/Phe/Val dehydrogenase
PR00082\"[115-129]T\"[194-216]T\"[236-256]T\"[374-385]TGLFDHDRGNASE
PTHR11606:SF2\"[21-450]TGLUTAMATE DEHYDROGENASE
PS00074\"[123-136]TGLFV_DEHYDROGENASE
InterPro
IPR006096
Domain
Glu/Leu/Phe/Val dehydrogenase, C-terminal
PF00208\"[203-448]TELFV_dehydrog
InterPro
IPR006097
Domain
Glu/Leu/Phe/Val dehydrogenase, dimerisation region
PF02812\"[58-188]TELFV_dehydrog_N
InterPro
IPR014362
Family
Glutamate dehydrogenase
PIRSF000185\"[20-450]TGlutamate dehydrogenase
noIPR
unintegrated
unintegrated
G3DSA:1.10.285.10\"[6-55]Tno description
G3DSA:3.40.192.10\"[60-202]Tno description
G3DSA:3.40.50.720\"[203-448]Tno description
PTHR11606\"[21-450]TGLUTAMATE DEHYDROGENASE


","No hits to the COGs database.","Significant hit (4.7e-118) to 7/7 blocks of the IPB001625 family, which is described as \"Glutamate/leucine/phenylalanine/valine dehydrogenase\". Interpro entry for IP:IPR001625. IPB001625A 80-100 3.4e-12 IPB001625B 110-146 5.5e-28 IPB001625C 159-184 2.3e-14 IPB001625D 195-215 5.7e-14 IPB001625E 233-260 9.8e-19 IPB001625F 344-356 8.8e-07 IPB001625G 365-389 5.4e-16","Residues 15 to 78 match (3e-10) PD:PD427241 which is described as DEHYDROGENASE GLUTAMATE DEPENDENT NAD ","","","","","","","","","","","","Wed Dec 4 18:03:02 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00221 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 203 to 448 (E-value = 4.3e-136) place AA00221 in the GLFV_dehydrog family which is described as Glutamate/Leucine/Phenylalanine/Valine dehydrogenase (PF00208)","","","","","Okwumabua O, O'Connor M, Shull E.A polymerase chain reaction (PCR) assay specific for Streptococcus suis based on the gene encoding the glutamatedehydrogenase.FEMS Microbiol Lett. 2003 Jan 21;218(1):79-84.PMID: 12583901Goss TJ, Janes BK, Bender RA.Repression of glutamate dehydrogenase formation in Klebsiella aerogenes requires two binding sites for the nitrogen assimilationcontrol protein, NAC.J Bacteriol. 2002 Dec;184(24):6966-75.PMID: 12446647Bansal,A., Dayton,M.A., Zalkin,H. and Colman,R.F.Affinity labeling of a glutamyl peptide in the coenzyme bindingsite of NADP+-specific glutamate dehydrogenase of Salmonellatyphimurium by 2-[(4-bromo-2,3-dioxobutyl)thio]-1,N6-ethenoadenosine 2',5'-bisphosphateJ. Biol. Chem. 264 (17), 9827-9835 (1989)PubMed: 2656714","","Fri Nov 21 12:54:50 2003","1","","","" "AA00223","154417","155868","1452","ATGTCAGCAAAATGCCCTTTCGATCATAACTCTGCCACATTGACTACCGCTGCCGGCGCGCCGGTGGTGGATAATGACAACACCATGAGTGCCGGCCCCCGCGGCCCGTTACTGTTACAAGATGTTTGGTATCAAGAAAAACTAGCCCACTTTGCCCGCGAGCGCATTCCTGAGCGTGTGGTGCACGCCAAGGGTTCCGCCGCATTCGGTACATTCACCGTCACTCACGACATCACCCAATACACCAAAGCTGCGCTGTTCAGCGAAGTGGGCAAACAAACGGAAGTGCTGTTGCGCTTTTCCACCGTTGCCGGCGAACGCGGTGCTGCCGACGCGGAACGTGATGTACGCGGTTTTTCGTTGAAATTCTACACCGAACAAGGCAACTGGGACTTAGTGGGCAATAACACGCCGGTGTTCTTCATCCGTGACCCGCTCAAATTCCCGGATTTCATTCACACTCAAAAACGCAACCCGCAAACCAACTTACGCGACGCTACCGCCGCATGGGATTTCTGGTCGCGTCATCCTGAATCCATGCACCAAATTATGATTCTGTTCAGCGATCGTGGTATTCCGGCAAGCCTGCGCAATATGAACGGTTACGGCAGCCACACTTACAGCTTTATCAATGCGGACAACGAACGCTTTTGGGTGAAATTCCACTTCAAAACCCAACAAGGTCATAAATTTTTAACCAACGCAGAAGCGGCGAAGGTGGTGGGTGAAGATCGTGAATCCAGCCAACGTGATTTATATGATGCCATTGCCAACGGCAATTTCCCCCGTTGGAACGTGCGAATTCAAATCATGCCGGAAGCCGATGCAGAAAAACACAATTACAGTTTTGACTTAACCAAAGTATGGCCGCACAAAGATTATCCGTTGATTGATGTAGGCGTATTGGAACTGAATCGCAATCCACAAAACTATTTTGCTGAAGTGGAACAAGCCGCCTTCGCGCCGAACAACAACGTGCCCGGCATCGGCTTCTCGCCCGATCGTATGTTGCAGGGTCGTTTATTCTCTTATCAAGATGCACAACGCTACCGCTTGGGCGTAAACCACCACCAAATTCCGGTGAATGCACCAAAATGCCCGTATCACACCACCCACCGTGACGGTGCAATGCGCGTAGATCACAACGGCGGCACACACCCGAACTATGCTCCAAACCGCTTTGACACCTATGTGCCAACCCACGATCAAGGTCCGTCATTGCAACTGGAACGTGAAGGCGCGCACTTTAATTTCCGTGATTACGACGAAGATTACTACTCACAACCTGCCGCGCTTTACGCCATTATGGACGCCGCCCAACGCGACCGCCTCGCCGGCAACTTCGCCGCCAGCCTGGCAGAAGTCACCGACGATGCCATCGTGGAACACCAGTTGGTACACTTTGAACGCGTTAATACGGAATTGGCAAACGCCATTCGCACAAAACTTGCT","","","54950","MSAKCPFDHNSATLTTAAGAPVVDNDNTMSAGPRGPLLLQDVWYQEKLAHFARERIPERVVHAKGSAAFGTFTVTHDITQYTKAALFSEVGKQTEVLLRFSTVAGERGAADAERDVRGFSLKFYTEQGNWDLVGNNTPVFFIRDPLKFPDFIHTQKRNPQTNLRDATAAWDFWSRHPESMHQIMILFSDRGIPASLRNMNGYGSHTYSFINADNERFWVKFHFKTQQGHKFLTNAEAAKVVGEDRESSQRDLYDAIANGNFPRWNVRIQIMPEADAEKHNYSFDLTKVWPHKDYPLIDVGVLELNRNPQNYFAEVEQAAFAPNNNVPGIGFSPDRMLQGRLFSYQDAQRYRLGVNHHQIPVNAPKCPYHTTHRDGAMRVDHNGGTHPNYAPNRFDTYVPTHDQGPSLQLEREGAHFNFRDYDEDYYSQPAALYAIMDAAQRDRLAGNFAASLAEVTDDAIVEHQLVHFERVNTELANAIRTKLA","155868","Mutants in this gene show increased sensitivity to hydrogen peroxide (Thomson et al., 1999).","catalase (hydroperoxidase; iron heme axial ligand)","Periplasm, Cytoplasm","","
InterPro
IPR002226
Family
Catalase
PD000510\"[15-445]TCatalase
PR00067\"[28-51]T\"[91-109]T\"[112-129]T\"[131-149]T\"[295-322]T\"[327-353]TCATALASE
PTHR11465\"[90-483]TCatalase
PS00437\"[340-348]TCATALASE_1
PS00438\"[51-67]TCATALASE_2
InterPro
IPR011614
Domain
Catalase, N-terminal
G3DSA:2.40.180.10\"[2-483]TCatalase_N
PF00199\"[15-398]TCatalase
noIPR
unintegrated
unintegrated
SSF56634\"[7-484]TSSF56634


","BeTs to 10 clades of COG0753COG name: CatalaseFunctional Class: PThe phylogenetic pattern of COG0753 is ------y--d--b-efgh-nuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 7e-182) to 5/5 blocks of the IPB002226 family, which is described as \"Catalase\". Interpro entry for IP:IPR002226. IPB002226A 36-87 6.6e-40 IPB002226B 101-153 3.1e-48 IPB002226C 177-208 9e-24 IPB002226D 235-288 1.4e-25 IPB002226E 313-364 2.6e-40","Residues 352 to 433 match (1e-07) PD:PD490371 which is described as CATALASE OXIDOREDUCTASE HEME IRON PEROXIDE HYDROGEN PEROXIDASE COMPLETE PEROXISOME NADP ","","","","","Sun Feb 16 16:26:52 2003","","","","","","Sun Feb 16 16:26:52 2003","Sun Feb 16 16:26:52 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00223 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 15 to 398 (E-value = 2.8e-279) place AA00223 in the Catalase family which is described as Catalase (PF00199)","","","","Thomson,V.J., Bhattacharjee,M.K., Fine,D.H., Derbyshire,K.M. andFigurski,D.H.Direct selection of IS903 transposon insertions by use of abroad-host-range vector: isolation of catalase-deficient mutants of Actinobacillus actinomycetemcomitansJ. Bacteriol. 181 (23), 7298-7307 (1999)PubMed: 10572134","Bishai,W.R., Smith,H.O. and Barcak,G.J.A peroxide/ascorbate-inducible catalase from Haemophilus influenzae is homologous to the Escherichia coli katE gene productJ. Bacteriol. 176 (10), 2914-2921 (1994)PubMed: 8188593 Cummings,N.J. and Connerton,I.F.The Bacillus subtilis 168 chromosome from sspE to katAMicrobiology 143 (Pt 6), 1855-1859 (1997)PubMed: 9202460Lee JK, Movahedi S, Harding SE, Waites WM.The effect of acid shock on sporulating Bacillus subtilis cells.J Appl Microbiol. 2003;94(2):184-90.PMID: 12534809Chauvatcharin N, Vattanaviboon P, Switala J, Loewen PC, Mongkolsuk S.Cloning and Characterization of katA, Encoding the Major Monofunctional Catalase fromXanthomonas campestris pv. phaseoli and Characterization of the Encoded Catalase KatA.Curr Microbiol. 2003 Feb;46(2):83-87.PMID: 12520360","Sun Feb 16 16:26:52 2003","Fri Nov 21 12:57:03 2003","1","","","" "AA00226","156511","156416","96","GTGTCTGAAATGCCTCATTCAACCTTTTATTATCAACAGGCAGGATTAGAGCCGGGTAAATTTGTGTATTACAACCAAAAACGAATTAAACCGATT","","","3802","VSEMPHSTFYYQQAGLEPGKFVYYNQKRIKPI","156416","","hypothetical protein","Cytoplasm, Extracellular","No significant similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 12:13:41 2004","Sun Feb 22 12:13:41 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00226 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 12:14:26 2004","","","","","","","","","","","","","1","","","" "AA00227","156702","156547","156","TTGAAGTGGCTTGAAACAAGCGACTTTTCACCACAAGCCTTTAAAAAACTGAAACGGGAACCTGCCCTTGCAAAAGAGGAGATTGATAATCTAAAAAAGTTAGTGGAATTAGACAATCAAAAACGACGGCAGAAAAAAGAAAAGTCATCGAAAAGT","","","6168","LKWLETSDFSPQAFKKLKREPALAKEEIDNLKKLVELDNQKRRQKKEKSSKS","156547","","hypothetical sequence","Periplasm, Cytoplasm","No significant similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 12:15:16 2004","Sun Feb 22 12:15:16 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogously related to AA00348, a hypothetical.AA00227 is paralogously related to AA01404 (2e-21), AA00631 (2e-15), AA02115 (8e-12), AA01289 (8e-12), AA01075 (8e-12), AA00008 (8e-12), AA00535 (1e-11) and AA02340 (2e-10).","Sun Feb 22 12:16:21 2004","","","","","","","","","","","","","1","","","" "AA00229","160371","157003","3369","ATGGTAGCGGTGGGCTTGACGGATTTCACCAATTTTTGTGGCTTGGTACGCTTTTACGGCGAGGCGTTGTCTTCCGGTGTGAAGCCGATTATCGGGACGGATGTGTTGGTACAAAGCGCATTATGCGGCGATGAAAAATTTCGTTTAACCTTGCTGGCGAAGAATAACGAAGGTTATAAAAACATTACGTTGCTGCTTTCCAAAGCTTATGAACGCGGTTATGCCGATTTGCCTTATATCGATCAGCAGTGGCTGGTGGAACACCGCGCCGGGGTGATTGTGCTGTCCGGCGGGGTAAACGGCGATGTGGGCAAGAAATTGCTCAGAAGCAACCCCGATGAACTAAAAAGTGCGGTGGATTTTTACCGTGAATTTTTCCCCGATCATTTCTATTTAACCCTCACCCGTACCGGTCGCCCTGACGAAGAACGCTATATTAAAGCGGCGCTGGAACTGGCGGAGCAGCAACAGTTGCCGGTAGTGGCAACTAATGATGTATGCTTTTTGCAGGCGGAGGATTTTGAAGCCCATGAAATTCGCGTGGCGATTCATGACGGTTTTACCTTGGACGACCCGAAACGCCCGAAACTTTATACGTCACAACAATATTTTCGCTCCGAACAGGAAATGTGCGATTTGTTCGCCGACGTGCCGAGCGCGTTGGAAAATACGGTGTTAATTGCGCAGCGTTGTAATGTCACCATTCGTTTGGGCGAATATTTCTTGCCACAATTTCCGACCGGTGATTTAACTACGGAAGATTATCTGGTTAAGCGCGCCAAAGACGGCTTGGAAGAACGCTTAAAAGTGTTGTTCCCCGATGAGAAGGTGCGTGCCGAACGCCGCCCGGAATATGATGAACGGCTACAGGTTGAACTGGATGTGATTAACCAAATGGGCTTCCCGGGCTATTTTTTGATCGTGATGGAGTTTATTCAATGGTCGAAAGATAATGACATTCCGGTAGGACCCGGGCGTGGTTCCGGGGCGGGATCTTTGGTGGCATATGCGCTAAAAATTACCGATTTGGATCCGTTGGAATTCGATTTGCTCTTTGAGCGTTTCCTCAATCCGGAACGGGTTTCCATGCCTGACTTCGACGTGGATTTCTGCATGGACGGACGCGACCGCGTGATTGACCATGTGGCGGAAATGTACGGGCATGGTGCGGTGTCGCAAATCATTACCTTCGGTACTATGGCGGCGAAAGCGGTAATTCGCGATGTGGGGAGGGTGCTGGGGCAACCTTACGGCTTTGTGGATCGCATTTCCAAACTGGTGCCGCCTGATCCGGGCATGACCTTGGCTAAGGCCTTTGAAGCAGAACCGAAATTACAGGAAATTTATGACGCGGATGAAGAAGTGCGTGCCATTATCGACATGGCGCGCAAACTGGAAGGTGTCACGCGTAACGCCGGTAAACACGCCGGCGGGGTGGTGATTTCGCCGACCCTGATCACGGATTTCTCGCCACTGTATTGCGATTCGGAAGGCAAACATCCGGTCACCCATTTCGATAAAAATGACGTGGAATACGCCGGTTTGGTGAAGTTTGACTTCCTCGGTTTACGCACGTTGACCATCATAAAATGGGCGCTGGATATGATTAATGCCCGCATGGAAAAAGAAGGCAAGCTGTTGGTGGACATCAGCGCCATTCCGTTGGACGACCAACAATCCTTCGATGTGTTACTGAATGCGGAAACCACGGCGGTGTTTCAGTTGGAATCGCGCGGTATGAAAGATTTGATTAAACGCCTGAAGCCGGACTGTTTTGAAGACATTATCGCGTTGGTGGCGTTGTTCCGTCCAGGTCCGTTGCAATCAGGCATGGTGGATAATTTTATCGACCGCAAACACGGACGCGAGGAAGTGTCTTACCCAGATGCCAATTATCAGCATGAATCCCTCAAACCGATTTTGGAACCGACCTACGGCATTATTTTGTATCAGGAACAGGTGATGCAAATCGCTCAAGTGTTGGCAGGCTATACTTTGGGTGGCGCGGACTTGTTGCGCCGTGCCATGGGGAAGAAAAAACCGGAAGAAATGGCGAAGCAGCGTTCCGTGTTTGAAGAAGGCGCGGTGAAAAACGGCGTGGACGGCGGACTTGCCATGAAGATCTTCGACTTGGTGGAAAAATTCGCCGGTTACGGTTTTAACAAATCCCACTCCGCCGCCTATGCGTTGGTGTCTTATCAAACCCTGTGGCTGAAAGCCCATTATCCGGCGGAATTTATGGCAGCGGTGATGACCTCGGAAATGGATAACACGGACAAAATTGTGGGCTTATACGACGAATGTATGCGTATGGGCTTGAAAGTGGTTCCGCCCGACATTAACACCGGTAAACACCATTTCAGCGTGAATGAAAACGGTGAAATCGTGTACGGAATCGGCGCCATTAAAGGCGTGGGTGAAGGCCCTATTGCGGCGTTGGTGGAAGCGCGGGAAAAAGACGGGATCTTTAAAAATCTGTTCGACTTATGTGCCCGCGTAGATTTAAAGAAAATCAACCGTCGTACTTTTGAAAGCCTGATTAAATCCGGTGCTTTTGATAAACTCGGACCGCATCGCGCCGCGTTACAGCAAAACTTGGAAGATGCGTTGCGCGCTTCCGATCAACACGCGAAAGACGAAGCCTTGGGGCAGGTGGATATGTTCGGCGTGCTGACGGAAACTAATGAGGAAGTGGAAAACTCCTATGCCAACATCGCACCTTGGACGGAAAAGACCATTTTGGACGGCGAACGGGAAACTTTAGGGTTGTATCTCAGCAGCCACCCGGTAACCCGTTATTTGAAAGAACTAGCCCATTACAGCCCCGTTCGCTTAAAAGAGCTGGTGCCGAATTATCGCGGGCAAATGAGCACCGCCAGCGGTTTGGTGATTAACACTCGCGTTGCGGTGACGAAAAAAGGCAACCATATCGGCATCGCTACCATTGACGATCGCTCCGGCCGGTTGGATTTAACCTTATTTGGCGAAGCCTTGGAAAAATTCGGCGAGAAACTGCAAAAAGACACGGTGATTGTGGTTTCCGGGCAAGTAAGTTTTGACGACTTCTCGCAGGGTTTGCGTATGTCAGTGCGTGATTTAATGACCATCGACGAAGCCCGTGCCCGTTATGCCAAAAGCCTTGCGATTTGCTTGTCGCAAGAACAAATCACGCCGCAATTCATTAAACAATTTAAAAGCATTTTACAGCCTTACAGCGGCAATTCGCTGCCGGTGCATATTTACTACCAAAGCCCGCAGGGCAGAGCGCTGGTTAAAATGGGCGTGCAATGGTCGGTCAACCCGACGGACGAACTGCTCACCGAACTGGCGGCACTGTTCGGTGAAAGTGCGGTGGAATTGGAGTTTGAA","","","129484","MVAVGLTDFTNFCGLVRFYGEALSSGVKPIIGTDVLVQSALCGDEKFRLTLLAKNNEGYKNITLLLSKAYERGYADLPYIDQQWLVEHRAGVIVLSGGVNGDVGKKLLRSNPDELKSAVDFYREFFPDHFYLTLTRTGRPDEERYIKAALELAEQQQLPVVATNDVCFLQAEDFEAHEIRVAIHDGFTLDDPKRPKLYTSQQYFRSEQEMCDLFADVPSALENTVLIAQRCNVTIRLGEYFLPQFPTGDLTTEDYLVKRAKDGLEERLKVLFPDEKVRAERRPEYDERLQVELDVINQMGFPGYFLIVMEFIQWSKDNDIPVGPGRGSGAGSLVAYALKITDLDPLEFDLLFERFLNPERVSMPDFDVDFCMDGRDRVIDHVAEMYGHGAVSQIITFGTMAAKAVIRDVGRVLGQPYGFVDRISKLVPPDPGMTLAKAFEAEPKLQEIYDADEEVRAIIDMARKLEGVTRNAGKHAGGVVISPTLITDFSPLYCDSEGKHPVTHFDKNDVEYAGLVKFDFLGLRTLTIIKWALDMINARMEKEGKLLVDISAIPLDDQQSFDVLLNAETTAVFQLESRGMKDLIKRLKPDCFEDIIALVALFRPGPLQSGMVDNFIDRKHGREEVSYPDANYQHESLKPILEPTYGIILYQEQVMQIAQVLAGYTLGGADLLRRAMGKKKPEEMAKQRSVFEEGAVKNGVDGGLAMKIFDLVEKFAGYGFNKSHSAAYALVSYQTLWLKAHYPAEFMAAVMTSEMDNTDKIVGLYDECMRMGLKVVPPDINTGKHHFSVNENGEIVYGIGAIKGVGEGPIAALVEAREKDGIFKNLFDLCARVDLKKINRRTFESLIKSGAFDKLGPHRAALQQNLEDALRASDQHAKDEALGQVDMFGVLTETNEEVENSYANIAPWTEKTILDGERETLGLYLSSHPVTRYLKELAHYSPVRLKELVPNYRGQMSTASGLVINTRVAVTKKGNHIGIATIDDRSGRLDLTLFGEALEKFGEKLQKDTVIVVSGQVSFDDFSQGLRMSVRDLMTIDEARARYAKSLAICLSQEQITPQFIKQFKSILQPYSGNSLPVHIYYQSPQGRALVKMGVQWSVNPTDELLTELAALFGESAVELEFE","157003","","DNA polymerase III, alpha subunit","Cytoplasm","","
InterPro
IPR004013
Domain
PHP, C-terminal
PF02811\"[1-170]TPHP
InterPro
IPR004365
Domain
Nucleic acid binding, OB-fold, tRNA/helicase-type
PF01336\"[957-1036]TtRNA_anti
InterPro
IPR004805
Family
DNA polymerase III, alpha subunit
TIGR00594\"[1-994]Tpolc: DNA polymerase III, alpha subunit
InterPro
IPR011708
Domain
Bacterial DNA polymerase III, alpha subunit
PF07733\"[202-699]TDNA_pol3_alpha


","BeTs to 18 clades of COG0587COG name: DNA polymerase III alpha subunitFunctional Class: LThe phylogenetic pattern of COG0587 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 4.1e-18) to 2/3 blocks of the IPB003141 family, which is described as \"PHP domain N-terminal region\". Interpro entry for IP:IPR003141. IPB003141B 352-367 4.7e-12 IPB003141C 718-728 0.00019","Residues 19 to 60 match (4e-14) PD:PD337666 which is described as PROTEOME COMPLETE HYDROLASE NADH MUTT PYROPHOSPHATASE REPEAT 3.6.1.- MAGNESIUM MANGANESE ","","","","","","","","","","","","Tue Dec 9 12:56:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00229 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 957 to 1036 (E-value = 7.1e-12) place AA00229 in the tRNA_anti family which is described as OB-fold nucleic acid binding domain (PF01336)","","","","","Li,S.J. and Cronan,J.E. Jr. Growth rate regulation of Escherichia coli acetyl coenzyme A carboxylase, which catalyzes the first committed step of lipid biosynthesis J. Bacteriol. 175 (2), 332-340 (1993) PubMed: 7678242 Fijalkowska,I.J. and Schaaper,R.M. Antimutator mutations in the alpha subunit of Escherichia coli DNApolymerase III: identification of the responsible mutations and alignment with other DNA polymerases Genetics 134 (4), 1039-1044 (1993) PubMed: 8375647 O\"Donnell,M. Accessory protein function in the DNA polymerase III holoenzyme from E. coli Bioessays 14 (2), 105-111 (1992) PubMed: 1575709 Tomasiewicz,H.G. and McHenry,C.S. Sequence analysis of the Escherichia coli dnaE gene J. Bacteriol. 169 (12), 5735-5744 (1987) PubMed: 3316192","","Tue Dec 9 12:56:16 2003","1","","","" "AA00231","160675","162459","1785","ATGGATCTCAATTTTCATTTTATCAATCGCATTCGCCATCAGGCAAAAACGCTGGCAAATCGCACCGCACTTTGCTATTTCAAAGACAATAACCGGCTGGATATTTCCTGGGCGGAGCTGCAACAGCAAGTGGATCACATCTCTTTGGCACTTTTAGCCAATCATATTGATATTCAAGATAAAATCGGTATTTTCGCGCACAATATGCCGCGTTGGACAATCACCGACATTGGTATATTACAGGTGCGTGCGGTGACGGTACCGATTTATGCCACCAACACCGCAAAACAGGCGCAATTCATTATTAACAACGCCGATATGAAGATCATTTTCGCCGGCGATCAGGAACAATACGATCAGGTGATCGACATCGCCGATGAATGCCCTAAGCTTATAAAAATCGTGGCGATGAAAAGCACCATCAATTTGCACGAACACGCCAAAGCCTGTCATTGGCAGGATTTTATTGAAATGGCGGACGAACAATATCGACCGCAATTACAACAGCGGCTGGATGGCAAATCTTTGGCGGATTTATTCACCCTGATTTACACCTCCGGCACCACCGGTGAGCCGAAAGGCGTGATGCTGGATTATGCCAATCTGGCGCACCAGCTGAAGGCGCACGATCAGGCGTTGCAAATAGATGATAGCGATGTGTCCCTTTCCTTCCTGCCGTTATCTCATATTTTTGAGCGGGCTTGGGTGGCGTATGTGCTCCATCGCGGTGCCACTAACTGTTACATTGAAGATACCAACCAAGTGCGGTCGGCATTGACGGAGATTCGTCCGACATTGATGTGTACCGTGCCACGTTTTTACGAGAAGATTTACACAGCGATTCTGGACAAAGTGCATAACGCACCGAAACTGCGCCAATGGATTTTCAATTGGGCAATTGCCGTCGGGCGTAAACGTTTCGATACCCTTGCCAAGCAACAGAAAATCGGCTTCCCATTAAAACAACAATATGCCCTCGCCGATAAATTGGTGCTCGGTAAACTGCGCGCCTTACTCGGCGGACGCATTCGTATGATGCCGTGCGGCGGCGCCAAATTGGAACCGACCATCGGCTTGTTTTTCCACAGTATCGGCTTAAACATCAAACTGGGTTACGGCATGACGGAAACCACCGCCACCGTTTCCTGCTGGAATGATTTCAGTTTTAATGCCAATTCTATCGGTACTTTGATGCCGGGCGCAGAAGTGAAAATCGGCGAAAACAATGAAATTCTGGTGCGTGGCGGCATGGTGATGAAAGGTTATTATAAAAAACCGCAGGAAACCGCCGACACCTTCACCCCTGACGGTTTCCTGAAAACCGGTGACGCCGGCGAATTCGATGCCGACGGCAATTTATACATCACCGATCGCATCAAAGAACTGATGAAAACCTCCAACGGCAAATATATCGCGCCACAGGTGCTGGAAAGTAAAATCGGCAAAGATAAATTCATCGAACAAATCGCCGTCATCGCCGACGCGAAAAAATACGTCTCCGCCCTTATCGTGCCTTGCTATGCGTCACTGGAAGATTATGCCAAGCAGGTCAACATCAAATATCAGGATCGTTTGGAATTGTTAAGAAATTCGGAGATTATTCAAATGTTAGAACGCCGAATTAATGAATTGCAAAAAGAATTGGCGGGCTGGGAAAAAATTAAACGTTTCACCCTTTTGCCCCAAGCCTTCAGCACACAATTGGAAGAAATCACACCGACGTTGAAATTACGACGAAAAGTGATTTTACAGCGTTATAAAGAGCTGATTGAGGCGATGTATAAC","","","67841","MDLNFHFINRIRHQAKTLANRTALCYFKDNNRLDISWAELQQQVDHISLALLANHIDIQDKIGIFAHNMPRWTITDIGILQVRAVTVPIYATNTAKQAQFIINNADMKIIFAGDQEQYDQVIDIADECPKLIKIVAMKSTINLHEHAKACHWQDFIEMADEQYRPQLQQRLDGKSLADLFTLIYTSGTTGEPKGVMLDYANLAHQLKAHDQALQIDDSDVSLSFLPLSHIFERAWVAYVLHRGATNCYIEDTNQVRSALTEIRPTLMCTVPRFYEKIYTAILDKVHNAPKLRQWIFNWAIAVGRKRFDTLAKQQKIGFPLKQQYALADKLVLGKLRALLGGRIRMMPCGGAKLEPTIGLFFHSIGLNIKLGYGMTETTATVSCWNDFSFNANSIGTLMPGAEVKIGENNEILVRGGMVMKGYYKKPQETADTFTPDGFLKTGDAGEFDADGNLYITDRIKELMKTSNGKYIAPQVLESKIGKDKFIEQIAVIADAKKYVSALIVPCYASLEDYAKQVNIKYQDRLELLRNSEIIQMLERRINELQKELAGWEKIKRFTLLPQAFSTQLEEITPTLKLRRKVILQRYKELIEAMYN","162459","","long-chain-fatty-acid--CoA ligase","Cytoplasm, Inner membrane","","
InterPro
IPR000873
Domain
AMP-dependent synthetase and ligase
PR00154\"[177-188]T\"[189-197]TAMPBINDING
PF00501\"[36-491]TAMP-binding
PS00455\"[182-193]TAMP_BINDING
noIPR
unintegrated
unintegrated
G3DSA:2.30.38.10\"[391-456]Tno description
G3DSA:3.40.50.980\"[2-200]Tno description
PTHR11968\"[34-305]T\"[341-513]T\"[531-595]TATP-DEPENDENT AMP-BINDING ENZYME FAMILY MEMBER
PTHR11968:SF10\"[34-305]T\"[341-513]T\"[531-595]TLONG-CHAIN-FATTY-ACID COA LIGASE


","BeTs to 12 clades of COG1022COG name: Long-chain acyl-CoA synthetases (AMP-forming)Functional Class: IThe phylogenetic pattern of COG1022 is ao---zyq--r--c-fgh------t-Number of proteins in this genome belonging to this COG is","Significant hit ( 8.7e-10) to 2/2 blocks of the IPB000873 family, which is described as \"AMP-dependent synthetase and ligase\". Interpro entry for IP:IPR000873. IPB000873A 184-199 2.1e-06 IPB000873B 219-229 0.15","Residues 72 to 111 match (1e-09) PD:PD102940 which is described as LIGASE COMPLETE PROTEOME LONG-CHAIN-FATTY-ACID-COA LONG-CHAIN-FATTY-ACID--COA FATTY ACID COA CHAIN LONG-CHAIN ","","","","","","","","","","","","Thu Dec 5 11:44:37 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00231 is paralogously related to AA02598 (1e-18), AA02108 (4e-16) and AA02512 (1e-10).","","","","","","Residues 36 to 491 (E-value = 1.1e-80) place AA00231 in the AMP-binding family which is described as AMP-binding enzyme (PF00501)","","","","","Campbell JW, Morgan-Kiss RM, E Cronan J.A new Escherichia coli metabolic competency: growth on fatty acids by a novel anaerobic beta-oxidation pathway.Mol Microbiol. 2003 Feb;47(3):793-805.PMID: 12535077Shockey,J.M., Fulda,M.S. and Browse,J.A.Arabidopsis Contains Nine Long-Chain Acyl-Coenzyme A SynthetaseGenes That Participate in Fatty Acid and Glycerolipid MetabolismPlant Physiol. 129 (4), 1710-1722 (2002)Fulda,M., Heinz,E. and Wolter,F.P.Brassica napus cDNAs encoding fatty acyl-CoA synthetasePlant Mol. Biol. 33 (5), 911-922 (1997)PubMed: 9106514DiRusso CC, Heimert TL, Metzger AK.Characterization of FadR, a global transcriptional regulator of fatty acid metabolism in Escherichia coli. Interaction with the fadB promoter is prevented by long chain fatty acyl coenzyme A.J Biol Chem. 1992 Apr 25;267(12):8685-91.PMID: 1569108","","Mon Feb 17 14:43:17 2003","1","","","" "AA00233","162479","162592","114","GTGCGGTGGAAAAATAATGTGTTTTTTCACCGCACTTTTTATATTAATTTCTCTTTATTATTCGTCTTTCAAGTGAATTTTAATAAAAAATTTCAAAAAAGACCTTATTTTTTG","","","4917","VRWKNNVFFHRTFYINFSLLFVFQVNFNKKFQKRPYFL","162592","","hypothetical protein","Cytoplasm","No significant similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-27]?signal-peptide
tmhmm\"[7-27]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 12:18:02 2004","Sun Feb 22 12:18:02 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00233 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 12:18:59 2004","","","","","","","","","","","","","1","","","" "AA00234","162807","168701","5895","ATGAATAAAGTCTTTAAAGTAATCTGGTGTAAAACATCTCAGACATGGATTGCCGTATCTGAACTATCTAAAGCTTTTTCCCTTTCTACCACTACAGATATACCTAAAAAAACTAAAATATTCATTGCTGCAGCCCCGTTATTATTTCTCTCCTTTAATACCAACGCTTACATTGCTATAGGTTCTGTTGAAAACAATTCTGTGAAATCCGAGGGGGCAGAAGCCTCCCCAAACAAGAGAAAGGGAAGCCAAGCATTAAATTATTACAACCCCGGTAGTAAATCATATGATGATAAAGACAAACCGAGCAATCCTGAAAGAAGATACAGCAATGGGGAGGCATATGGTATCGCTATCGGTAAAAATACCGATGTTCGTGACTCAAGTAAGGATTCAAATGGTATCGCCTTAGGCGATTATTCTAAAGCTACCGGTGGGCTTGCCATGGCCTTAGGTTCATTTTCCAGAGCAGAAAAAAATGGCGGTATTGCAATCGGTATAGCTTCCAGATCATCAGGAATTAATTCTCTTGCGATGATGCGTCAATCTGCAGCAACCGGGGATTATTCTACTGCCATTGGTTCTGTCGCATGGGCTGCAGGTCAATCAAGCTTCGCACTGGGGGCTTCTGCTACTGCTAAAGGCAACCAATCCATTGCAATTGGCAGCTTGGAACAAAAAATATCTCCGAATGGTTCTGGTGTGCCAATCACAAAATACAACGGGTTAGACAACACACAAACCAATGGTAACCGTTCCATGGCATTGGGTACGGCAGCTAAAACCAATGGTGATGATTCATTTGCTATTGGTTATAAAGCACACACCGGTGAGTTTAAAGTGGAACATGACAACTATCTAAAAGAGAATGTTACCTCTCCGGATCTGTCTAAAAAAGCTGATAAAGCCATTGCTGTCGGTACGAGTGCCCTTGCGCAAAAAGAATCTGCTATCGCATTTGGCTACCAAGCTAATGCTTCCGGCATTAATGCAATTTCTCTTGGCGCAAATGCAAAAGCATCTCAAGATAACGTTGTAGCAATAGGTAAATATGCTACAGCCACTGAATCTGGTTCAATGGCCATTGGTCAGGGAGCTAAATCTACCTTTAAAAACTCATTGGCATTAGGTACAGGTACCATTGTCAACAGTGTCGATGGCGGGCAATCTAAATTTACTGCACAAAATTATGATGCTAATAATGGTGTTGTAGCTGTTGCAAACGCCGGTAAAGAGCGTCGAATTATTAATGTTGCCGGTGGTCGTAATGATACTGATGCAGTGAATATTGCCCAGTTAAAATTCGTGAATGATAACTTAGCCAAGTCCATCGCAGGCGCCGGTTATAACGGCTATGAAACAGACGGACATACTTACAAAGCACCGGTATTTAGTATTAAAAATACCAACTATCACGATGTCAAAACAGCTGTTGAAGCGGCACAAACCAATTATGTAAGTGTAAATAGCACTAATACAGCAGCCGATAGTAATTACGACAATAAAGGGGCTAAAGCAGTAGGTTCTATTGCGTTAGGCGAAAAAGCCACAACAGGAACGGCGGCAATGAACTCTATTGCCATTGGTTTAAACAGCAATGTTAGCGGCCAAAATACCGTTGCATTGGGTGCCAATATCACCGCGACAACCAACGGTTCCGTCATTTTAGGAAATTCCTCCACCACGGAAGGTTCACATCCTGTTTCAAATGTTAGCAGTGCGACTGTTAACGGATATACCTACTCAGGTTTTACCGGCACGGTAAAAGAGTCGGGACATTTTGTGAGCATTGGTTCAAAAGGCAATGAGCGTCAAATTAAAAATGTGGCAGCAGGTAATGTTGCGGCAAACTCAACCGATGCCGTTAATGGCTCTCAATTATTTGCTGTCGCCAGTCGTGTAGAACAAGGTTGGCAAATCACTTCCGGCGTAGAAAATGGTGGTACTCAAAATGGCGCAGCCTCAACAGCAACAATCAAACCGAGTAACCAAGTGAAGCTACTGGCAGGAAAGAATTTAGCAGTCAAACAAAACGGCACTAACTTCACCTTCTCAACCCAAGAAAATGTCACGTTCACTAATGTTACGACCCAAGATCTAACTGCAACAGGCAACACCACTGTTAAGAACTTCAGCGTTCAAAATGGCGGAACCATCAATATGGGAAATAATCGCATTACCGGTGTCGCTGAAGGCACTCAAGATGACGACGCGGTTAACTTTAAACAATTAAAAAGCCTTCTTGGTGGCTCCGCATCAACGGAAATTGTTGAGAAAAAAGCAGCTCAAGCCGGAGATGAAAACCTGGCGGATATTAGCGTAGCAAATGGTAAAAACGCCGGCGATATGGGTGCGAAATACGAAGTATCTGTATCCAAAAAAGCCGTACAAAGTGCCGCAAAAGAAGCGGTTAAAGTGACAGGTTCGGCACCGATTAATGTAAACAAAACAGATGTAAATGGCGTTGATACTTATGCCGTAACCTTTAATGGCACAGAAGCGGCGAAATCTATCCCATTAACTTATAAAGCTAACGGTAGCGGTGATAAAACCGTCATGTTGGATAAAGGATTAAACTTTACCAATGGTATGATGACAACCGCTTCCGTGGCAAATGACGGTGTGGTGAAATATGACGTCAATTTATCCACCATTAAAGTAGAAGATGGCAAGGCTGCCGTAGCCGGTACACCGGGCACAAATGGCGCCAACGGCACTGATGGCAAAGATGGCGTAGCGACGGTTAAAAATGTGGTAGAGGCGTTAAATAATGCCGCATGGACAATAACTGCCTCTAAATCTGACGGCGAAGTCGTCAGCAATGCATCTAATTCCGTTAAAAATGGGGATACGGTGACTTATGATGCCGGCAAAAACATCAAAATTACTCAAAGAGATAAAAAATTCTCTTTTGCCACCAAAGATAATGTTGAATTTACTTCTGTGACCACGGGCAATACCAAATTAACCGGTAATGGTGTAGAAATCACCAACGGCCCTAAACTTACCCAATCAGGTGTGGATGCAGGCGGTAAGAAAATCACCAATGTAGCAGATGGCGTTATTGCAGCTAACAGCAAAGATGCCGTGAATGGCGGTCAATTATTCGCTGAAACTGCAAAAGCCAAAACTACGGTTGAGAAAGGTGATGATAATATTCAAATCACATCAGAAACTGCAACGGACGGACATATTAACTATAAAGTGGCATTAAATCCTAGCTTGACCGTCGGACCAAGAACAAATGGTCACCCGATCACCATTGATGGTAATAACGGCTATATTACCGGTTTAACCAATACAAGCTGGACGGGCGCGCCAACAACCGGTCGTGCAGCAACGGAAGATCAATTATCTATAGTCGATAAAAAATTCGATAATAAGGTTTCTTTAGGCGGTGACAACGGTAGTACCACAGAGAAATCCTTGTCTCACAACGGCGGAATCAAATTTAATATCAAAGGCGGAGACAGCCAAAAATATGTGACGACATCAGGATCCGGCGATGATGTCACGGTGGATCTTGCCCAAACCACAAAAAATAAGATCGACAATGCGGCAGATAAAGATCTCGCCAACATTACCGATAATGGTAAAAAAGTTATTACCGCTTTAGGCGCTGTAGTGAAAGCGGCTGATTCTACGATTACGGTAACTGACGAAACCGATAATACGACAGGACAAAAAACCTACAAAATCAAAGCCAATATTCCAACACCGGAAAAAACAGCAATGGCTCCCGGCAACAATACAACCATTGAAGGTGATGGCTCAGCCGCCAATCCGTTTAAAGTGAATCTGAAAGATGATTTAGCGCTAGGTCAAAAAGACGCTAACGGCGTAACCGGTAAAGATTCTTCCATTAAAGTGAACGGCAAAGATGGCTCCGGTGTGGCGATTAACGGTAAAGACGGTTCCATTGCATTAAATGGCAAAGACGGTGCGAATCCTGTCACCATCAAAACGGCGCAAGGTCCTGCCGGTGTGAATGAAACCAATCCCAAAGACCGTTTAATGGTGAATAACGACGCTGTTGCAACCCTTAAAGACGGCTTAAAATTCGCCGGAGATAACAGCACCGAAGTCATCACTAAAACCTTAAATCAAAAACTGGAAATTGTGGGTGGTGCAGATAAAAACAAATTATCTGACAACAATATCGGCGTAAATGCCAATAACGGCAAACTGGAAGTGAAATTAGCCAAAGAGTTGAATGAGTTAACCAGTGCGCAATTCAAGAATGGCGACAACACAACGGTTATCAATGGCAATGGCATAACAATTACCCCGAAAGATCCGACAAAGGCGGTCAGCTTAACGGATAAAGGACTAAACAATGGTGGTAATCAAATTGTGAACATTGACAGCGGATTAAAACAAGCCGACGGTTCAACAGTTGCTTTAAAAGACGCCTCAGGTGATACCTTAAAAAATGCGGCGAATATCGGCGATTTACAAAAATCCATTAACGACATTACCGACGCAAGTAAAAACGGCGGCTTCGGTTTAAGCGATGACAATGGCGCAACCGCTAAAGCCAACTTAGGTGAAACCGTGAAAGTGAAAGGCGATGGCAGTGTTATTACAAAAGTAGTTACCGATAATGGTAAACCGACCTTACAAGTGGGTTTAAGCAACGACATCACTGTAGGAGACGATGCGCAAGCGGGCACCATTAGCGTCAAAGGGGAAAACGGTAAGGATGGCGTATCCATCAACGGCAAAGAGGCTTCCGTCACTTTTGCTAAAGACGGACAACCGGGTATGTCTATTGCCGCTACGCGTAGCGCTGATGGTAAAGACGCGTTGACGCTCAAAGGCAAAGACGGTAAAGATGGCATTTCGTTCCAGGAAGATGGTCGTATTACTCAGGTTGCCGATGGGGTAAATGACAAAGATGCGGTGAACAAATCCCAATTGGATAGAAGTATTGCTCAAGCTAAATCCGGTGTTAGTGCCGGCAAAAACATTACTGTAACGCCTCAAAAGAATGCCGACGGAAGCACCACGTACACCGTTGAAACCCAAAACGATGTTGAATTCAGCACGGTGAAAACCGGTGATACCACCCTGGATAGCAACGGTGTCAATATCAATGGCGGACCAAGTGTCACCAAGGACGGCATTCACGCCAATGATAAGAAAATCACCGGTGTAAAAGACGGTGAAATTTCAGCCCATAGTAAAGAGGCGGTGAACGGTAGCCAATTACATCAAACCAACCAAAATGTGACGAATTTAGCCAACAATGTGGACAAAGGGCTGAATTTCCAAGGAGACAATCAAGAAGTCACAGTTAATCGTAAATTAGGCGATCAACTTAACATTCGCGGCGGTGCGGATCCGAAGAAATTAACACAAAATAATATCGGCGTGACCGCAGATAAAAACGGCACCATGACCGTTCAGCTGGCGAAGGAAGTTAATCTCGGCGCAGATGGCAGCCTTACTGTAGGCAATACCACGGTCAATAACGACGGTGTTACGATTAAAGACGGTCCAAGCATGACAAGCCACGGCATCAACGCCGGCGGCAAACGAATTGCTAACGTTGCGAAAGGGAAAGCACCGACGGATGCAGTAAATATGAGTCAGCTTCAAGACGTCGGCAGTGCCATTAATAATCGCATTGATAACATTGATAAGCGCGTGAAAAAAATGGATAAACGTCGCAAAGCCGGCACCGCTTCCGCCCTCGCTACGGCGGGTTTGATGCAGCCGCATAGAGACGGGCAATCCGCCTTAGTCGCCGCTGTCGGTCAATATCAAAGCGAAACCGCTGTAGCTGTGGGTTACTCACGCATTTCCGATAACGGAAAATACGGCGTGAAAGTTTCTTTCAGCACCAACTCACAAGGTGAAGTTGGCGGTACGGCAGGCGCGGGCTATTTCTGG","","","201783","MNKVFKVIWCKTSQTWIAVSELSKAFSLSTTTDIPKKTKIFIAAAPLLFLSFNTNAYIAIGSVENNSVKSEGAEASPNKRKGSQALNYYNPGSKSYDDKDKPSNPERRYSNGEAYGIAIGKNTDVRDSSKDSNGIALGDYSKATGGLAMALGSFSRAEKNGGIAIGIASRSSGINSLAMMRQSAATGDYSTAIGSVAWAAGQSSFALGASATAKGNQSIAIGSLEQKISPNGSGVPITKYNGLDNTQTNGNRSMALGTAAKTNGDDSFAIGYKAHTGEFKVEHDNYLKENVTSPDLSKKADKAIAVGTSALAQKESAIAFGYQANASGINAISLGANAKASQDNVVAIGKYATATESGSMAIGQGAKSTFKNSLALGTGTIVNSVDGGQSKFTAQNYDANNGVVAVANAGKERRIINVAGGRNDTDAVNIAQLKFVNDNLAKSIAGAGYNGYETDGHTYKAPVFSIKNTNYHDVKTAVEAAQTNYVSVNSTNTAADSNYDNKGAKAVGSIALGEKATTGTAAMNSIAIGLNSNVSGQNTVALGANITATTNGSVILGNSSTTEGSHPVSNVSSATVNGYTYSGFTGTVKESGHFVSIGSKGNERQIKNVAAGNVAANSTDAVNGSQLFAVASRVEQGWQITSGVENGGTQNGAASTATIKPSNQVKLLAGKNLAVKQNGTNFTFSTQENVTFTNVTTQDLTATGNTTVKNFSVQNGGTINMGNNRITGVAEGTQDDDAVNFKQLKSLLGGSASTEIVEKKAAQAGDENLADISVANGKNAGDMGAKYEVSVSKKAVQSAAKEAVKVTGSAPINVNKTDVNGVDTYAVTFNGTEAAKSIPLTYKANGSGDKTVMLDKGLNFTNGMMTTASVANDGVVKYDVNLSTIKVEDGKAAVAGTPGTNGANGTDGKDGVATVKNVVEALNNAAWTITASKSDGEVVSNASNSVKNGDTVTYDAGKNIKITQRDKKFSFATKDNVEFTSVTTGNTKLTGNGVEITNGPKLTQSGVDAGGKKITNVADGVIAANSKDAVNGGQLFAETAKAKTTVEKGDDNIQITSETATDGHINYKVALNPSLTVGPRTNGHPITIDGNNGYITGLTNTSWTGAPTTGRAATEDQLSIVDKKFDNKVSLGGDNGSTTEKSLSHNGGIKFNIKGGDSQKYVTTSGSGDDVTVDLAQTTKNKIDNAADKDLANITDNGKKVITALGAVVKAADSTITVTDETDNTTGQKTYKIKANIPTPEKTAMAPGNNTTIEGDGSAANPFKVNLKDDLALGQKDANGVTGKDSSIKVNGKDGSGVAINGKDGSIALNGKDGANPVTIKTAQGPAGVNETNPKDRLMVNNDAVATLKDGLKFAGDNSTEVITKTLNQKLEIVGGADKNKLSDNNIGVNANNGKLEVKLAKELNELTSAQFKNGDNTTVINGNGITITPKDPTKAVSLTDKGLNNGGNQIVNIDSGLKQADGSTVALKDASGDTLKNAANIGDLQKSINDITDASKNGGFGLSDDNGATAKANLGETVKVKGDGSVITKVVTDNGKPTLQVGLSNDITVGDDAQAGTISVKGENGKDGVSINGKEASVTFAKDGQPGMSIAATRSADGKDALTLKGKDGKDGISFQEDGRITQVADGVNDKDAVNKSQLDRSIAQAKSGVSAGKNITVTPQKNADGSTTYTVETQNDVEFSTVKTGDTTLDSNGVNINGGPSVTKDGIHANDKKITGVKDGEISAHSKEAVNGSQLHQTNQNVTNLANNVDKGLNFQGDNQEVTVNRKLGDQLNIRGGADPKKLTQNNIGVTADKNGTMTVQLAKEVNLGADGSLTVGNTTVNNDGVTIKDGPSMTSHGINAGGKRIANVAKGKAPTDAVNMSQLQDVGSAINNRIDNIDKRVKKMDKRRKAGTASALATAGLMQPHRDGQSALVAAVGQYQSETAVAVGYSRISDNGKYGVKVSFSTNSQGEVGGTAGAGYFW","168701","","collagen adhesin","Outer membrane, Extracellular","This sequence corresponds to GI:33578091 in GenBank. Nearest neighbor in the NR database is GI:32034569 from A.pleuropneumoniae.","
InterPro
IPR000425
Family
Major intrinsic protein
PS00221\"[1070-1078]?MIP
InterPro
IPR005594
Domain
YadA-like, C-terminal
PF03895\"[1887-1965]TYadA
InterPro
IPR008635
Domain
Haemagluttinin motif
PF05662\"[413-433]T\"[604-627]T\"[724-744]T\"[1012-1035]T\"[1449-1468]T\"[1620-1640]T\"[1714-1737]T\"[1846-1866]THIM
InterPro
IPR008640
Repeat
Hep_Hag
PF05658\"[143-170]T\"[171-198]T\"[199-226]T\"[248-275]T\"[300-325]T\"[326-353]T\"[354-381]T\"[504-533]THep_Hag
noIPR
unintegrated
unintegrated
G3DSA:2.150.10.10\"[108-237]T\"[301-439]T\"[457-633]TG3DSA:2.150.10.10
SSF101967\"[122-277]T\"[299-439]T\"[464-633]T\"[679-750]T\"[908-1041]T\"[1515-1646]TSSF101967
SSF101999\"[972-1091]T\"[1416-1545]T\"[1680-1805]T\"[1821-1933]TSSF101999


","No hits to the COGs database.","","Residues 925 to 1035 match (4e-09) PD:PD544283 which is described as SURFACE PROTEOME COMPLETE CELL ","","","","","","","","","","","","Tue Feb 8 14:48:01 2005","Tue Feb 8 14:49:46 2005","Tue Feb 8 14:48:01 2005","","Tue Feb 8 14:48:01 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA00234 is paralogously related to AA02485 (1e-10).","Tue Feb 8 14:48:01 2005","","","","","Residues 1887 to 1965 (E-value = 8.5e-24) place AA00234 in the YadA family which is described as YadA-like C-terminal region (PF03895)","Tue Feb 8 14:48:01 2005","","","Mintz KP.Identification of an extracellular matrix protein adhesin, EmaA, which mediates the adhesion of Actinobacillus actinomycetemcomitans to collagen.Microbiology. 2004 Aug;150(Pt 8):2677-88.PMID: 15289564","","Tue Feb 8 14:49:46 2005","","1","","","" "AA00235","168736","168828","93","GTGCGGTGGAAAAATAATGTGTTTCTTCACCGCACTTTTTTATTTTCGCCCTCTCATTTCTCCCCGAATGAAATTCCTAACGAAACCAATCAC","","","3748","VRWKNNVFLHRTFLFSPSHFSPNEIPNETNH","168828","","hypothetical protein","Cytoplasm, Extracellular","No significant similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 12:20:34 2004","Sun Feb 22 12:20:34 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00235 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 12:21:23 2004","","","","","","","","","","","","","1","","","" "AA00236","168958","171081","2124","ATGGGTACATTCTTTGTCATTAAGCGTGATGGTTCACGCATTAGCTTTGAACTTCAACGTATCGTAAACGCCATAAAAAAGGCAGCGCAGGCGGTCGGTATTACGGATGATCGTTATTGCTATGCCGTGGCGCAGAAAGTCAGTGATGACATTTTCAGCCATTACCAACAGGAAATCGACATTAGTCACATTCAAAAAATCGTGGAAAATCACCTGATGGCTAGCCAATACCCGCAAGTGGCACGCGCTTATATTGAATATCGCCACGATCGTGATTTGGCGCGTGAAAAACGCAGTCAATTAACCCGGGAAATTGAGGGATTAATTGAACAAAGCAACGTGGAATTACTGAACGAAAACGCCAATAAAGACGCCAAAGTGATCCCGACCCAACGGGATTTGCTGGCGGGTATCGTGGCGAAACATTATGCCAAACGTTACATTCTGCCGCGCGATGTGGTGGCAGCCCATGAGAAAGGCGAAATCCATTATCACGATTTGGACTATTCGCCCTTCTTCCCGATGTTTAACTGTATGTTGGTGGATTTAAAAGGCATGCTGACCCAAGGCTTTAAAATGGGCAATGCGGAAATCGAACCGCCGAAATCCATCGGCACCGCCACCGCCGTGACTGCGCAAATTATCGCGCAGGTAGCAAGTCACATTTACGGCGGCACCACTATTAACCGTATTGACGAAGTGTTGGCGCCTTACGTTCAACTCAGTTACGACAAACATCTGAAAAATGCCGCGCAGTGGAATGTGCCCGATGCGCAAGGATACACGCAGGCACTTATCGAAAAAGATTGTTTCGACGCCTTCCAATCCCTTGAATATGAAGTGAATACCTTGCACACCGCCAATGGTCAAACCCCATTCGTGACCTTCGGTTTCGGTTTGGGCACAAGCTGGCAGGCGCGCTTGATTCAAAAAGCGATTTTGCAAAACCGAATTCGCGGTTTAGGCAAAAACCACAAAACACCGGTGTTCCCGAAACTGGTTTTCACCCAACGCAAGGGCGTAAATCTGGAACCTAATGATCCGAATTACGACATCAAACAGCTTGCCTTGGAATGCGCCAGCAAACGTATGTATCCGGATATTCTGAATTACGATCAAGTGGTCAAAGTCACCGGTTCCTTCAAAGCCCCGATGGGCTGCCGTAGCTTCTTGGGCGCGTACGAAGAAAATGGTGAACAAATCCACGACGGACGTAACAACCTCGGCGTGGTGAGCCTCAACCTGCCGCGTATCGCCATTGAAGCCAAAGGGGATGAAAAACGCTTCTATGAAATTTTGGATCAACGTTTAGCCTTGGCGAAAAAAGCACTCATGACCCGCATTGCCCGCTTAGAACACACCAAAGCCCGTGTGGCACCGATTTTATACATGGAAGGCGCCTGTGGCGTGCGTTTAAAAGCGGACGACAACGTGGCACAAATCTTCAAAAACGGACGCGCCTCCATTTCCCTCGGTTACATCGGCATTTATGAAACCGTCAATGCGCTCTATCACCAAGGACACATTTACGATAACGACATGCTACGCGAAAAAGGTCGTGCCATCGTGGAATACCTCAGCAACGCCACCAAACAATGGCGCGCCGAAACGGGTTATGCCTTCAGTTTGTATTCCACTCCAAGCGAAAACCTGTGCGATCGCTTCTGCCGTTTAGATACCAAACAATTCGGCGTCATCGACGGCGTGACCGACAAAGGCTACTACACCAACAGCTACCATTTGGACGTGGAGAAAAAAGTCAATCCATACGACAAACTGGACTTTGAAATGGCGTACCCGCCACTTGCCAGCGGCGGTTTCATTTGCTACGGCGAATACCCAAACATCCAGCACAACCTCAAAGCACTGGAAGACGTGTGGAATTACAGCTACGACCGCGTGCCTTACTACGGCACCAACACGCCTATCGACGAATGCTACGAATGCGGTTTCACCGGCGAATTTGAATGCACCAGCAAAGGCTTCACCTGCCCGAAATGCGGCAACCACGACAGCGAAAAAGTCTCCGTCACCCGACGGGTTTGCGGCTACCTAGGAAGCCCAGACGCCAGACCGTTTAATGCGGGGAAACAGGAAGAAGTGAAGCGCAGAGTTAAGCATATG","","","80266","MGTFFVIKRDGSRISFELQRIVNAIKKAAQAVGITDDRYCYAVAQKVSDDIFSHYQQEIDISHIQKIVENHLMASQYPQVARAYIEYRHDRDLAREKRSQLTREIEGLIEQSNVELLNENANKDAKVIPTQRDLLAGIVAKHYAKRYILPRDVVAAHEKGEIHYHDLDYSPFFPMFNCMLVDLKGMLTQGFKMGNAEIEPPKSIGTATAVTAQIIAQVASHIYGGTTINRIDEVLAPYVQLSYDKHLKNAAQWNVPDAQGYTQALIEKDCFDAFQSLEYEVNTLHTANGQTPFVTFGFGLGTSWQARLIQKAILQNRIRGLGKNHKTPVFPKLVFTQRKGVNLEPNDPNYDIKQLALECASKRMYPDILNYDQVVKVTGSFKAPMGCRSFLGAYEENGEQIHDGRNNLGVVSLNLPRIAIEAKGDEKRFYEILDQRLALAKKALMTRIARLEHTKARVAPILYMEGACGVRLKADDNVAQIFKNGRASISLGYIGIYETVNALYHQGHIYDNDMLREKGRAIVEYLSNATKQWRAETGYAFSLYSTPSENLCDRFCRLDTKQFGVIDGVTDKGYYTNSYHLDVEKKVNPYDKLDFEMAYPPLASGGFICYGEYPNIQHNLKALEDVWNYSYDRVPYYGTNTPIDECYECGFTGEFECTSKGFTCPKCGNHDSEKVSVTRRVCGYLGSPDARPFNAGKQEEVKRRVKHM","171081","","anaerobic ribonucleoside-triphosphate reductase","Cytoplasm","","
InterPro
IPR001150
Domain
Formate C-acetyltransferase glycine radical
PF01228\"[583-689]TGly_radical
PS51149\"[585-708]TGLY_RADICAL_2
PS00850\"[678-686]TGLY_RADICAL_1
InterPro
IPR005144
Domain
ATP-cone
PF03477\"[4-95]TATP-cone
PS51161\"[4-95]TATP_CONE
InterPro
IPR012833
Domain
Ribonucleoside-triphosphate reductase, anaerobic
TIGR02487\"[118-707]TNrdD: anaerobic ribonucleoside-triphosphate
noIPR
unintegrated
unintegrated
G3DSA:3.20.70.20\"[124-690]Tno description
PTHR21075\"[6-708]TANAEROBIC RIBONUCLEOSIDE-TRIPHOSPHATE REDUCTASE


","BeTs to 7 clades of COG1328COG name: Oxygen-sensitive ribonucleoside-triphosphate reductaseFunctional Class: FThe phylogenetic pattern of COG1328 is --m-k---v--l--efgh--------Number of proteins in this genome belonging to this COG is","Significant hit ( 3.5e-31) to 2/2 blocks of the IPB001150 family, which is described as \"Pyruvate formate-lyase, glycine radical\". Interpro entry for IP:IPR001150. IPB001150A 355-365 0.05 IPB001150B 657-706 9.7e-28","Residues 268 to 303 match (5e-14) PD:PD039550 which is described as REDUCTASE ANAEROBIC PROTEOME COMPLETE RIBONUCLEOSIDE-TRIPHOSPHATE OXIDOREDUCTASE RADICAL IRON-SULFUR ORGANIC RIBONUCLEOTIDE ","","","","","Wed Feb 19 14:35:34 2003","","","","Wed Feb 19 14:35:34 2003","","","Wed Feb 19 08:40:54 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00236 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 583 to 689 (E-value = 8.5e-55) place AA00236 in the Gly_radical family which is described as Glycine radical (PF01228)","","","","","Sun,X., Harder,J., Krook,M., Jornvall,H., Sjoberg,B.M. andReichard,P.A possible glycine radical in anaerobic ribonucleotide reductasefrom Escherichia coli: nucleotide sequence of the cloned nrdD geneProc. Natl. Acad. Sci. U.S.A. 90 (2), 577-581 (1993)PubMed: 8421692Sun,X., Eliasson,R., Pontis,E., Andersson,J., Buist,G.,Sjoberg,B.M. and Reichard,P.Generation of the glycyl radical of the anaerobic Escherichia coliribonucleotide reductase requires a specific activating enzymeJ. Biol. Chem. 270 (6), 2443-2446 (1995)PubMed: 7852304Masalha,M., Borovok,I., Schreiber,R., Aharonowitz,Y. and Cohen,G.Analysis of transcription of the Staphylococcus aureus aerobicclass Ib and anaerobic class III ribonucleotide reductase genes inresponse to oxygenJ. Bacteriol. 183 (24), 7260-7272 (2001)PubMed: 11717286Fontecave M, Mulliez E, Logan DTDeoxyribonucleotide synthesis in anaerobic microorganisms: the class III ribonucleotide reductase.Prog Nucleic Acid Res Mol Biol. 2002;72:95-127. Review.PMID: 12206460 Masalha M, Borovok I, Schreiber R, Aharonowitz Y, Cohen G.Analysis of transcription of the Staphylococcus aureus aerobic class Ib and anaerobic class III ribonucleotide reductase genes in response to oxygen.J Bacteriol. 2001 Dec;183(24):7260-72.PMID: 11717286","","Wed Feb 19 08:40:54 2003","1","","","" "AA00237","171229","171074","156","TTGCAATTTTTAGGAAATTTTCGTCTGTTTGCGCGTAGCGAGTTCGAAAATTTCCGTGAAGAAAATTGCAACCAAGCGAAGAACAGCGGCTTATCCGGGGTGTGTTCTTTGCTACTTTCTTGCACAAGCAAGAAAGTAGGAGTAACTACATATGCT","","","5762","LQFLGNFRLFARSEFENFREENCNQAKNSGLSGVCSLLLSCTSKKVGVTTYA","171074","","hypothetical protein","Cytoplasm, Extracellular","No significant similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 12:22:14 2004","Sun Feb 22 12:22:14 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","Np paralogous sequences are found to this sequence.AA00237 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 12:22:56 2004","","","","","","","","","","","","","1","","","" "AA00239","171478","171353","126","TTGCATTTTGTCCTTTGTTCCATTGAATTTGCTTTACGGGAATTTTGTAAACTTGCTACGCTCAAACAGTACAAAATTCCCTACAAATTCAATTTCACAAAGGCGGTAAAGAAGGGAACCCAACGT","","","4992","LHFVLCSIEFALREFCKLATLKQYKIPYKFNFTKAVKKGTQR","171353","","hypothetical protein","Cytoplasm","No significant similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 12:25:49 2004","Sun Feb 22 12:25:49 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogously related to AA0029, a hypothetical.AA00239 is paralogously related to AA00042 (4e-12).","Sun Feb 22 12:26:52 2004","","","","","","","","","","","","","1","","","" "AA00240","171652","171530","123","ATGGTTTTTGTTGATATATCGGATTTCGCCGATGGCGAGTTACTTTTCTTTGCGTCGTCAAAGAAAAGTAACCAAAAGAAAGGCGCCCCTGCTTTGCCTTGTTTATTCGCAACTCAGCACAGC","","","4429","MVFVDISDFADGELLFFASSKKSNQKKGAPALPCLFATQHS","171530","","hypothetical protein","Periplasm, Cytoplasm","No significant similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 12:23:46 2004","Sun Feb 22 12:23:46 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is weakly paralogous to AA0029, a hypothetical.AA00240 is paralogously related to AA00042 (2e-07).","Sun Feb 22 12:24:44 2004","","","","","","","","","","","","","1","","","" "AA00241","171686","172150","465","ATGAACTACCTCCAATACTACCCCGTCGACATCGTCAACGGCGAAGGCACTCGCTGCACCCTTTTCGTCAGCGGCTGTACGCACGCCTGCAAAGGTTGCTACAACCAAAAAAGCTGGTCGTTTAGTGCGGGCGTGCCGTTTGGTATTGAAATGGAAGAACAAATTCTCAAGGATCTCAAAGACACCCGCATTAAACGCCAAGGTTTGACCCTATCCGGCGGTGATCCGCTTCATCCGCGCAATGTAGAAACGCTGTTGCCGTTAGTGCAACGGGTGAAACGGGAATGCCCCGATAAAGACATTTGGGTATGGACCGGGTACAAATTAGATGAATTGGACGACTATCAACGCCAAATGCTGCCTTATATCGACGTGCTAATTGACGGCAAATTCATTCAGGCGCAAGCGGATCCGAGCCTGATTTGGCGCGGTTCGGCGAATCAAGTGATTCACCGGTTTAAGATC","","","17838","MNYLQYYPVDIVNGEGTRCTLFVSGCTHACKGCYNQKSWSFSAGVPFGIEMEEQILKDLKDTRIKRQGLTLSGGDPLHPRNVETLLPLVQRVKRECPDKDIWVWTGYKLDELDDYQRQMLPYIDVLIDGKFIQAQADPSLIWRGSANQVIHRFKI","172150","","formate acetyltransferase activating enzyme (anaerobic ribonucleoside-triphosphate reductase activating protein)","Cytoplasm","","
InterPro
IPR001989
Domain
Radical-activating enzyme
PS01087\"[14-35]TRADICAL_ACTIVATING
InterPro
IPR012837
Family
Ribonucleoside-triphosphate reductase activating, anaerobic
TIGR02491\"[2-154]TNrdG: anaerobic ribonucleoside-triphosphate


","BeTs to 6 clades of COG0602COG name: Organic radical activating enzymesFunctional Class: OThe phylogenetic pattern of COG0602 is aompk--q---lbcefghsnujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 6.2e-22) to 3/3 blocks of the IPB001989 family, which is described as \"Radical activating enzymes\". Interpro entry for IP:IPR001989. IPB001989A 12-39 1.8e-13 IPB001989B 68-79 0.00035 IPB001989C 125-130 0.75","Residues 100 to 150 match (5e-07) PD:PD091895 which is described as PROTEOME COMPLETE ANAEROBIC REDUCTASE ACTIVATING RIBONUCLEOSIDE-TRIPHOSPHATE RIBONUCLEOTIDE ACTIVATOR PROTEIN NRDG ","","","","","","","","","","","","Thu Dec 5 12:30:24 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00241 is paralogously related to AA02982 (7e-06).","","","","","","","","","","","Fontecave M, Mulliez E, Logan DT.Deoxyribonucleotide synthesis in anaerobic microorganisms: the class III ribonucleotidereductase.Prog Nucleic Acid Res Mol Biol. 2002;72:95-127. Review.PMID: 12206460 Torrents E, Eliasson R, Wolpher H, Graslund A, Reichard P.The anaerobic ribonucleotide reductase from Lactococcus lactis. Interactions between thetwo proteins NrdD and NrdG.J Biol Chem. 2001 Sep 7;276(36):33488-94.PMID: 11427536 Sun,X., Harder,J., Krook,M., Jornvall,H., Sjoberg,B.M. and Reichard,P. A possible glycine radical in anaerobic ribonucleotide reductase from Escherichia coli: nucleotide sequence of the cloned nrdD gene Proc. Natl. Acad. Sci. U.S.A. 90 (2), 577-581 (1993) PubMed: 8421692 Sun,X., Eliasson,R., Pontis,E., Andersson,J., Buist,G., Sjoberg,B.M. and Reichard,P. Generation of the glycyl radical of the anaerobic Escherichia coli ribonucleotide reductase requires a specific activating enzyme J. Biol. Chem. 270 (6), 2443-2446 (1995) PubMed: 7852304 ","","Mon Feb 17 08:26:24 2003","1","","","" "AA00244","172872","172183","690","GTGCAAAAGATTTTGATTGTTGCTGTGTTGCAGCGGGATTTCAAAACGATTGAAAAAATGACCGCACTTTATCCCGGGCAGTTGTATTACGGCTTAGGGTTGCATCCTTTGTATATCCAAGAGCATCAAATCGACGATTTGGGTTTGCTGGATCAGGCATTGGCAAGTCGTCCGGCAAATTGTACGGCGGTGGCGGAAATCGGTTTGGAGCGTGCCTTGCCTGAACTCTTAACGGAAGCATTATGGCGCAAGCAATGTGATTTCTTGGAAGCGCAGTTGCACTTGGCGAAAAAACACAACCTGCCGGTAAATCTGCATTCCCGTAAATCTCATGAGCAACTGTTTTCCTTTTTAAGACGCATCGCCGTGCCAAAATGTGGTGTGGTGCATGGTTTTGCGGGCAGTTATGATCAGGCGAAACGCTTTGTGGATTTAGGTTACAAAATCGGCGTAGGCGGCACCATTACTTATGAACGCGCCAATAAAACCCGTCAAACCATCGCCAAATTGCCTTTAAACGCGTTGCTGTTGGAAACGGATTCGCCCGATATGCCGGTGTTTGGTTTTCAAGGGCAGCCTAATCGCCCGGAACGCGTGGTGCAGGTGTTCAATGCCTTGTGTGAATTAAGAAGCGAAACGCCGGCGCAAATCGCCGAGACCATTTGGCACAACAGCGTGGCAAAATTCGCT","","","29504","VQKILIVAVLQRDFKTIEKMTALYPGQLYYGLGLHPLYIQEHQIDDLGLLDQALASRPANCTAVAEIGLERALPELLTEALWRKQCDFLEAQLHLAKKHNLPVNLHSRKSHEQLFSFLRRIAVPKCGVVHGFAGSYDQAKRFVDLGYKIGVGGTITYERANKTRQTIAKLPLNALLLETDSPDMPVFGFQGQPNRPERVVQVFNALCELRSETPAQIAETIWHNSVAKFA","172183","","conserved hypothetical protein (possible deoxyribonuclease, possible hydrolase)","Cytoplasm","","
InterPro
IPR001130
Family
TatD-related deoxyribonuclease
PTHR10060\"[1-229]TTATD DNASE-RELATED
PF01026\"[1-230]TTatD_DNase
PS01091\"[166-182]TTATD_3
InterPro
IPR012278
Family
Mg-dependent DNase, TatD
PIRSF005902\"[1-230]TMg-dependent DNase, TatD type
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.140\"[1-229]Tno description


","BeTs to 23 clades of COG0084COG name: Mg-dependent DNaseFunctional Class: LThe phylogenetic pattern of COG0084 is --m-kzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-25) to 4/5 blocks of the IPB001130 family, which is described as \"Uncharacterized protein family UPF0006\". Interpro entry for IP:IPR001130. IPB001130B 28-36 0.35 IPB001130C 61-71 0.078 IPB001130D 85-108 3e-10 IPB001130E 170-190 3.5e-07","Residues 85 to 182 match (2e-08) PD:PD577746 which is described as PROTEOME COMPLETE CDA11 SSO0046 ST2051 ST0937 PAE2003 CG3358 ","","","","","","","","","","","","Wed Feb 19 15:39:25 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00244 is paralogously related to AA00301 (4e-24).","","","","","","Residues 1 to 229 (E-value = 3.3e-60) place AA00244 in the TatD_DNase family which is described as TatD related DNase (PF01026)","","","","","","","Wed Feb 19 15:39:25 2003","1","","","" "AA00245","173252","172974","279","TTGCATAAAATTATTTATTCAGAAAACGCCGTTCAGGATTTTGAGCATATTGTTTTTGATTTAACCGAATATGCCGGATTTAGCAGTGCTATAACTATTTTTGAAGATATTAAACAAGCGATTGAATTGCTTGCCTATATGCCTCTGATGGGAGTTGTCGGTAGTGTTGAGGGAACTCGTGAAATTTATGTCAGAGGCTATCGAATTGTTTATCGTGTTTCTTCTGCAGAAATTCAAATCAGCACCATCATTCATTGTAAAAGACTTTATCCCAATTTC","","","10675","LHKIIYSENAVQDFEHIVFDLTEYAGFSSAITIFEDIKQAIELLAYMPLMGVVGSVEGTREIYVRGYRIVYRVSSAEIQISTIIHCKRLYPNF","172974","","hypothetical protein","Cytoplasm","","
InterPro
IPR007712
Family
Plasmid stabilization system
PF05016\"[4-90]TPlasmid_stabil


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Dec 5 12:53:56 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00245 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 87 (E-value = 5.9e-06) place AA00245 in the Plasmid_stabil family which is described as Plasmid stabilisation system protein (PF05016)","","","","","","","","1","","","" "AA00246","173400","173248","153","ATGATGACACAGGAATATAAGCAGTTTTTGCAACAAAAAGTGGCAAAATCTGATGAAGATTTTAAAAATAATCGCGTATTTGAGCCTGAACAAGTGTACCAACGCGTGATTCAAGCGGCGGTAAAAGCTAAAGAAGGAATGAAGGACGTTGCA","","","6006","MMTQEYKQFLQQKVAKSDEDFKNNRVFEPEQVYQRVIQAAVKAKEGMKDVA","173248","","hypothetical protein","Cytoplasm, Extracellular","No significant similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 12:28:34 2004","Sun Feb 22 12:28:34 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00246 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 12:28:34 2004","","","","","","","","","","","","","1","","","" "AA00247","174006","173497","510","ATGGTTACACTATATACAAATTTCGGCGATATTAAAATTGCCTTAAATCACGAGAAAGCACCGGTAACGGCGGAAAATTTCTTAACTTATTGTAAAAACGGTTTTTATGATAACACAATTTTCCACCGCGTGATTGACGGTTTTATGATTCAAGGCGGCGGTATGGAAAGCGGTATGCGCGAAAAAGCCACCAACGCGCCGATTAAAAATGAAGCCAATAACCGTTTAAGTAACAAACGCGGCACCATCGCCATGGCGCGCACCTCCGATCCGCATTCCGCGACAGCGCAATTCTTCATTAATGTTGCCGATAACAACTTCCTGGATTACCGCGCAAAAGAGTTGCACGGGCGCGAAGTGGTGCAAGAATGGGGTTATGCGGTATTCGGCGAAGTGGTTGAAGGCATGGATGTGGTCGATAAAATCAAAGGCGTTAAAACCGGCAACAAAGGTTTTCATCAAGACGTGCCGAATGAGGATGTGGTGATTACTTCGGTTACTGTGGATGAG","","","18908","MVTLYTNFGDIKIALNHEKAPVTAENFLTYCKNGFYDNTIFHRVIDGFMIQGGGMESGMREKATNAPIKNEANNRLSNKRGTIAMARTSDPHSATAQFFINVADNNFLDYRAKELHGREVVQEWGYAVFGEVVEGMDVVDKIKGVKTGNKGFHQDVPNEDVVITSVTVDE","173497","","peptidyl-prolyl cis-trans isomerase B","Cytoplasm, Periplasm","","
InterPro
IPR002130
Domain
Peptidyl-prolyl cis-trans isomerase, cyclophilin-type
PR00153\"[15-30]T\"[41-53]T\"[124-139]TCSAPPISMRASE
G3DSA:2.40.100.10\"[1-170]Tno description
PF00160\"[1-169]TPro_isomerase
PS50072\"[1-168]TCSA_PPIASE_2
PS00170\"[36-53]TCSA_PPIASE_1
noIPR
unintegrated
unintegrated
PTHR11071\"[1-168]TCYCLOPHILIN
PTHR11071:SF29\"[1-168]TPEPTIDYL-PROLYL CIS-TRANS ISOMERASE B, PPIB


","BeTs to 16 clades of COG0652COG name: Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin familyFunctional Class: OThe phylogenetic pattern of COG0652 is -om---y--drlbcefghsnuj--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.5e-32) to 3/3 blocks of the IPB002130 family, which is described as \"Cyclophilin-type peptidyl-prolyl cis-trans isomerase\". Interpro entry for IP:IPR002130. IPB002130A 9-30 2.6e-07 IPB002130B 36-74 7.3e-14 IPB002130C 84-121 2.4e-08","Residues 1 to 166 match (5e-80) PD:PD000341 which is described as ISOMERASE ROTAMASE CIS-TRANS PEPTIDYL-PROLYL CYCLOPHILIN PPIASE CYCLOSPORIN B PROTEOME COMPLETE ","","","","","","","","","","","","Thu Dec 5 12:56:14 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00247 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 169 (E-value = 1.1e-52) place AA00247 in the Pro_isomerase family which is described as Cyclophilin type peptidyl-prolyl cis-trans isomerase (PF00160)","","","","","Hayano,T., Takahashi,N., Kato,S., Maki,N. and Suzuki,M. Two distinct forms of peptidylprolyl-cis-trans-isomerase are expressed separately in periplasmic and cytoplasmic compartmentsof Escherichia coli cells Biochemistry 30 (12), 3041-3048 (1991) PubMed: 2007139 Kawamukai,M., Matsuda,H., Fujii,W., Utsumi,R. and Komano,T. Nucleotide sequences of fic and fic-1 genes involved in cell filamentation induced by cyclic AMP in Escherichia coli J. Bacteriol. 171 (8), 4525-4529 (1989) PubMed: 2546924 ","","Thu Dec 5 12:56:14 2002","1","","","" "AA00248","174008","174109","102","GTGCTTTTCCTCTACGAATTAAAGAGCGTCATTATTTCACAATCCGCCCCAAATCGCCATAAAGTGCGGTGCGTTTTCAAAAAGATTTGGATCCCAATATGT","","","4012","VLFLYELKSVIISQSAPNRHKVRCVFKKIWIPIC","174109","","hypothetical protein","Cytoplasm","No significant similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 12:29:52 2004","Sun Feb 22 12:29:52 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00248 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 12:29:52 2004","","","","","","","","","","","","","1","","","" "AA00249","174106","175482","1377","ATGTTAAAACTTTTCAATACCCTAACCCGCGAAAAAGAAATTTTTAAACCGATTCACGCCGGCAAAATCGGAATGTATGTGTGTGGCGTGACCGTGTACGATCTCTGCCACATCGGGCACGGGCGTACGTTCGTGTGTTTCGATGTAATCGCCCGTTATTTGCGTTATTTAGGCTACGATTTAACCTATGTGCGTAATATTACCGACGTGGATGACAAAATTATTAAACGTGCCTTGGAAAATAAAGAAACCTGCGATCAGTTGGTGGATCGCATGGTGGTGGAAATGTATAAAGATTTTGACGCGCTGAATATTTTGCGTCCGGATTTTGAACCGCGCGCCACCCACCATATTCCTGAAATCATTGACATTGTACAGAAATTAATCCAACGCGGACACGCCTACGTAGCGGACAACGGCGATGTAATGTTTGATGTGGAAAGCTTCAAAGATTACGGCAAATTGTCCCGTCAGGATTTGGAACAATTACAAGCGGGCGCGCGCATTGAAATTAACGAAATCAAGAAAAATCCAATGGATTTCGTGTTATGGAAAATGTCTAAACCGAATGAACCGAGCTGGGACTCGCCTTGGGGCAAAGGGCGCCCAGGCTGGCACATCGAATGCTCCGCCATGAACAGCAAACAATTAGGCGAGCATTTTGACATTCACGGTGGCGGCTCCGACCTCATGTTCCCACATCACGAAAACGAAATCGCCCAATCCTGCTGTGCCCACGGCAATCAATATGTGAACTATTGGCTACACTCCGGCATGATCATGGTGGATAAAGAAAAAATGTCGAAATCCCTCGGCAATTTCTTCACCATTCGCGACGTATTAAACCACTACGACGCGGAAAGCGTGCGCTATTTCTTATTGACCGCGCACTACCGCAGCCAATTAAATTACAGCGAAGAAAACCTTAACCTCGCTCACGGCGCATTAGAACGGCTCTACACCGCATTACGCGGCACAGATAAAAGTGCGGTGGCTTTTGGCGGTGAAAATTTTGTGGATGCCTTCCGTGAAGCCATGGATGATGATTTCAACACGCCGAATGCCCTTTCCGTACTGTTTGAAATGGCGCGTGAACTGAACAAGCTGAAGACCGAAGACATGGCAAAAGCCAACGGCTTAGCCGCACGCTTACGCGAACTCGCCGCCATTCTCGGTCTGCTTCAACTGGATCCGGAGCAATTCCTGCAAGCCGGTTCCGATGAAGATGAAGTGGCGAAAATCGAAGCGCTTATTAAGCAACGCAACGAATCCCGAGCCACCAAAGACTGGGCAGCCGCTGACGCCGCGCGCAATGCCTTAACGGAAATGGGCATCATATTGGAAGACGGACCGAACGGCACCACCTGGCGTAAGCAA","","","53587","MLKLFNTLTREKEIFKPIHAGKIGMYVCGVTVYDLCHIGHGRTFVCFDVIARYLRYLGYDLTYVRNITDVDDKIIKRALENKETCDQLVDRMVVEMYKDFDALNILRPDFEPRATHHIPEIIDIVQKLIQRGHAYVADNGDVMFDVESFKDYGKLSRQDLEQLQAGARIEINEIKKNPMDFVLWKMSKPNEPSWDSPWGKGRPGWHIECSAMNSKQLGEHFDIHGGGSDLMFPHHENEIAQSCCAHGNQYVNYWLHSGMIMVDKEKMSKSLGNFFTIRDVLNHYDAESVRYFLLTAHYRSQLNYSEENLNLAHGALERLYTALRGTDKSAVAFGGENFVDAFREAMDDDFNTPNALSVLFEMARELNKLKTEDMAKANGLAARLRELAAILGLLQLDPEQFLQAGSDEDEVAKIEALIKQRNESRATKDWAAADAARNALTEMGIILEDGPNGTTWRKQ","175482","","cysteinyl-tRNA synthetase (cysteine--tRNA ligase)","Cytoplasm","","
InterPro
IPR002308
Family
Cysteinyl-tRNA synthetase, class Ia
TIGR00435\"[2-459]TcysS: cysteinyl-tRNA synthetase
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620\"[19-309]Tno description
InterPro
IPR015273
Domain
Cysteinyl-tRNA synthetase, class Ia, DALR
PF09190\"[341-402]TDALR_2
InterPro
IPR015803
Domain
Cysteinyl-tRNA synthetase, class Ia, N-terminal
PR00983\"[25-36]T\"[61-70]T\"[191-209]T\"[222-243]TTRNASYNTHCYS
PF01406\"[14-314]TtRNA-synt_1e
InterPro
IPR015804
Domain
Cysteinyl-tRNA synthetase, class Ia, C-terminal
PTHR10890\"[190-416]TCYSTEINYL-TRNA SYNTHETASE


","No hits to the COGs database.","Significant hit ( 1.6e-06) to 2/2 blocks of the IPB001412 family, which is described as \"Aminoacyl-transfer RNA synthetases class-I\". Interpro entry for IP:IPR001412. IPB001412A 30-40 6.8 IPB001412B 263-273 0.00011","Residues 9 to 98 match (4e-11) PD:PD256578 which is described as LIGASE SYNTHETASE CYSTEINYL-TRNA CYSTEINE--TRNA PROTEOME COMPLETE AMINOACYL-TRNA CYSRS ATP-BINDING BIOSYNTHESIS ","","","","","","","","","","","","Wed Feb 12 10:23:17 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00249 is paralogously related to AA00717 (5e-04).","","","","","","Residues 14 to 314 (E-value = 2.7e-223) place AA00249 in the tRNA-synt_1e family which is described as tRNA synthetases class I (C) catalytic domain (PF01406)","","","","","Eriani,G., Dirheimer,G. and Gangloff,J.Cysteinyl-tRNA synthetase: determination of the last E. coliaminoacyl-tRNA synthetase primary structureNucleic Acids Res. 19 (2), 265-269 (1991)PubMed: 2014166Hou,Y.M., Shiba,K., Mottes,C. and Schimmel,P. Sequence determination and modeling of structural motifs for the smallest monomeric aminoacyl-tRNA synthetase Proc. Natl. Acad. Sci. U.S.A. 88 (3), 976-980 (1991) PubMed: 1992490 ","","Thu Dec 5 13:14:46 2002","1","","","" "AA00250","176595","175636","960","ATGGGAACACCTTTTAAAATGGAGCGCGGCGTTAAATATCGCGATGCCGCCAAAACCTCCATTATTCCGGTGAAAAATATCGATCCTGAGCAAGAACTGCTCAAAAAGCCGGAATGGATGAAAATTAAAATTCCGGCAAACGGTGCGCGCATTCAAAGTATCAAATCCGGTATGCGTCGCCATGGCTTGCATTCCGTCTGCGAAGAAGCCTCCTGCCCGAACCTGCACGAATGTTTCAACCACGGTACGGCAACTTTTATGATTCTTGGTGCTATTTGCACCCGCCGTTGTCCGTTCTGCGACGTGGCGCATGGTAAACCGTTGGCGCCGGATCCGGAAGAACCGCGTAAATTAGCGGAAACCATTCAGGATATGAAATTGCGTTATGTGGTGATTACCTCCGTTGACCGCGATGATTTACCGGATCGCGGTGCCGGGCATTTTGCCGATTGCGTTCGGGAAATCCGCGCCCTGAATCCGAATATTAAAATTGAAATTTTAGTGCCGGATTTCCGTGGTCGCATTGAACTGGCATTGGAAAAATTAAAAGACAATCCGCCCGATGTGTTCAATCATAATCTGGAAAACGTACCGCGCTTATACCGCGAAATCCGCCCGGGCGCTGATTATCAATGGTCACTGCGTTTGTTGAAGGAATTTAAAGCCATGTTCCCGCATATTCCGACCAAATCCGGACTTATGGTGGGATTAGGCGAAACCAATGACGAGATCTTGGAAGTGATGCAGGATCTGCGGGATCACGGTGTGACGATGCTGACGTTGGGGCAATATTTACAACCGAGTCGTCACCACCTTCCGGTTGCCCGCTATGTTCCACCGACAGAATTCGATATGTTCCGCGACAAAGCCCAAAACATGGGCTTCGAACACGCCGCCTGCGGCCCATTCGTCCGTTCTTCTTATCACGCCGATTTACAAGCAAGCGGCGGCTTGGTGAAA","","","36256","MGTPFKMERGVKYRDAAKTSIIPVKNIDPEQELLKKPEWMKIKIPANGARIQSIKSGMRRHGLHSVCEEASCPNLHECFNHGTATFMILGAICTRRCPFCDVAHGKPLAPDPEEPRKLAETIQDMKLRYVVITSVDRDDLPDRGAGHFADCVREIRALNPNIKIEILVPDFRGRIELALEKLKDNPPDVFNHNLENVPRLYREIRPGADYQWSLRLLKEFKAMFPHIPTKSGLMVGLGETNDEILEVMQDLRDHGVTMLTLGQYLQPSRHHLPVARYVPPTEFDMFRDKAQNMGFEHAACGPFVRSSYHADLQASGGLVK","175636","From Genbank:[gi:13431630] This protein is involved in the synthesis of alpha-(+)-lipoic acid. It may be involved in the sulfur insertion chemistry in lipoate biosynthesis.","lipoate biosynthesis protein A","Cytoplasm","","
InterPro
IPR003698
Family
Lipoate synthase
PIRSF005963\"[16-320]TLipoyl synthase
PTHR10949\"[32-311]TLIPOIC ACID SYNTHETASE
TIGR00510\"[21-320]TlipA: lipoic acid synthetase
InterPro
IPR006638
Domain
Elongator protein 3/MiaB/NifB
SM00729\"[83-291]TElp3
InterPro
IPR007197
Domain
Radical SAM
PF04055\"[87-251]TRadical_SAM
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[46-287]Tno description


","BeTs to 16 clades of COG0320COG name: Lipoate synthaseFunctional Class: HThe phylogenetic pattern of COG0320 is -o---zyq-dr-bcefghsn-jxi--Number of proteins in this genome belonging to this COG is","Significant hit (2.9e-158) to 7/7 blocks of the IPB003698 family, which is described as \"Lipoate synthase\". Interpro entry for IP:IPR003698. IPB003698A 35-45 5.3e-05 IPB003698B 65-102 2.8e-32 IPB003698C 114-156 4.2e-34 IPB003698D 164-173 6.8e-06 IPB003698E 187-205 8.1e-13 IPB003698F 229-278 5.2e-43 IPB003698G 280-310 7.4e-18","Residues 63 to 112 match (6e-07) PD:PD556651 which is described as ACID LIPOIC SYNTHASE-LIKE ","","","","","","","","","","","Mon Jan 13 15:25:17 2003","Thu Dec 5 13:20:07 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00250 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 87 to 251 (E-value = 2.9e-26) place AA00250 in the Radical_SAM family which is described as Radical SAM superfamily (PF04055)","","","","","Jordan SW, Cronan JE Jr. A new metabolic link. The acyl carrier protein of lipid synthesisdonates lipoic acid to the pyruvate dehydrogenase complex inEscherichia coli and mitochondria. J Biol Chem. 1997 Jul 18;272(29):17903-6. PMID: 9218413 Morris TW, Reed KE, Cronan JE Jr. Lipoic acid metabolism in Escherichia coli: the lplA and lipBgenes define redundant pathways for ligation of lipoyl groups toapoprotein. J Bacteriol. 1995 Jan;177(1):1-10. PMID: 8002607","","Thu Dec 5 13:20:07 2002","1","","","" "AA00251","177298","176663","636","ATGCAACCCGAATTAATTGTACGACAACTCGGCATTCGTGATTATGAGGACGTTTGGCACGAGATGCAGGCGTTTACCGATAATCGTACGGAGCAGACTCCTGATGAAATTTGGTTGGTGCAGCATCTATCTGTGTTCACCCAAGGTCAGGCGGGCAAGCCGGAACATCTATTGCAACAAAGTGCAATTCCGGTGGTGCAGTCCGATCGTGGTGGGCAGATTACCTATCACGGTTTGGGGCAGCAAATTATGTATGTGCTGATTGATGTGAAACGCCACGAGAATCTAAATGTGCGCCAATTAGTAACCGCACTTGAGCAATCAGTGGTGAAAACCTTGGCGGATTACGGCATTGAAGGCTATGCGAAACCTGATGCGCCGGGCGTTTATATTGACGGCAAAAAAATCTGCTCCCTCGGTTTGCGTATTCGCCACGGTCGGTCGTTCCATGGCTTGGCATTTAACATCAACATGGATTTGACCCCGTTTCATCAAATCAATCCTTGCGGTTACGCGGGTTTGGAAATGTGTCAGCTGGCAGATTTTATTCCCGCACCAGAGGCGGACTGCGACAAGGTTTCCCCACAATTAGTTCAACATTTCGCCGTGCAATTAGGGTATAATGTAACAAATTGT","","","23826","MQPELIVRQLGIRDYEDVWHEMQAFTDNRTEQTPDEIWLVQHLSVFTQGQAGKPEHLLQQSAIPVVQSDRGGQITYHGLGQQIMYVLIDVKRHENLNVRQLVTALEQSVVKTLADYGIEGYAKPDAPGVYIDGKKICSLGLRIRHGRSFHGLAFNINMDLTPFHQINPCGYAGLEMCQLADFIPAPEADCDKVSPQLVQHFAVQLGYNVTNC","176663","From Genbank:[gi:12230907] This protein is involved in the attachment of lipoyl groups to proteins, by creating an amide linkage that joins the free carboxyl group of lipoic acid to the epsilon-amino group of a specific lysine residue in lipoylated proteins.","lipoate biosynthesis protein B","Cytoplasm","","
InterPro
IPR000544
Domain
Lipoate-protein ligase B
PD006086\"[35-103]TLIPB_HAEIN_P44464;
TIGR00214\"[25-206]TlipB: lipoyltransferase
PS01313\"[70-85]TLIPB
InterPro
IPR004143
Domain
Biotin/lipoate A/B protein ligase
PF03099\"[48-132]TBPL_LipA_LipB
noIPR
unintegrated
unintegrated
PTHR10993\"[13-184]TLIPOATE-PROTEIN LIGASE B


","No hits to the COGs database.","Significant hit ( 1.9e-45) to 3/3 blocks of the IPB000544 family, which is described as \"Lipoate-protein ligase B\". Interpro entry for IP:IPR000544. IPB000544A 35-53 6.3e-08 IPB000544B 70-85 4.9e-11 IPB000544C 135-170 1.2e-23","Residues 129 to 183 match (2e-17) PD:PD006665 which is described as LIGASE B LIPOATE LIPOATE-PROTEIN PROTEOME BIOSYNTHESIS COMPLETE 6.-.-.- PROBABLE PRECURSOR ","","","","","","","","","","","Mon Jan 13 15:27:32 2003","Mon Jan 13 15:27:32 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00251 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 48 to 162 (E-value = 2.5e-29) place AA00251 in the BPL_LipA_LipB family which is described as Biotin/lipoate A/B protein ligase family (PF03099)","","","","","Jordan SW, Cronan JE Jr. A new metabolic link. The acyl carrier protein of lipidsynthesis donates lipoic acid to the pyruvate dehydrogenasecomplex in Escherichia coli and mitochondria. J Biol Chem. 1997 Jul 18;272(29):17903-6. PMID: 9218413 Morris TW, Reed KE, Cronan JE Jr. Lipoic acid metabolism in Escherichia coli: the lplA and lipBgenes define redundant pathways for ligation of lipoyl groups toapoprotein. J Bacteriol. 1995 Jan;177(1):1-10. PMID: 8002607","","Thu Dec 5 13:25:04 2002","1","","","" "AA00252","177586","177347","240","TTGCTGGAATTCCCATGTGATTTCACTTTTAAAGTGGTGGGTGCCGCCCGTCCCGATTTAGTGGATGATGTGGTTCAGGTGGTGCATAAAACCATCAAAGACGATTACAACCCGAGCATGAAAGAGAGTGGCAAAGGCACTTATCATTCCGTGTCCATCACCGTGCGCGCTGAAAATATCGAACAAATTGAAAAACTGTATAAAGAATTGGCGGAAATCGACGGCGTGAGAATGGTGCTT","","","11192","LLEFPCDFTFKVVGAARPDLVDDVVQVVHKTIKDDYNPSMKESGKGTYHSVSITVRAENIEQIEKLYKELAEIDGVRMVL","177347","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR007454
Family
Protein of unknown function DUF493
PF04359\"[1-80]TDUF493


","BeTs to 5 clades of COG2921COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG2921 is --------------efghsn------Number of proteins in this genome belonging to this COG is","","Residues 1 to 80 match (5e-21) PD:PD028950 which is described as PROTEOME COMPLETE BU488 CYTOPLASMIC YPO2600 HI0028 PA3998 NMA1380 STY0687 VC0945 ","","","","","","","","","","","","Thu Dec 5 13:26:49 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00252 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 80 (E-value = 8e-39) place AA00252 in the DUF493 family which is described as Protein of unknown function (DUF493) (PF04359)","","","","","","","","1","","","" "AA00253","177571","177696","126","ATGGGAATTCCAGCAAGTCTTTTAATTTTTGTTGTGGAATGTCGGCTAAATTTACCGTTTTTTTATCTGTCATTGCATTCTCCTAAAAAAGTGAACCGCACTTTCATGAAAAAGTGCGGTCAGTGT","","","4813","MGIPASLLIFVVECRLNLPFFYLSLHSPKKVNRTFMKKCGQC","177696","","hypothetical protein","Cytoplasm","No significant similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 12:31:47 2004","Sun Feb 22 12:31:47 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00253 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 12:31:47 2004","","","","","","","","","","","","","1","","","" "AA00254","178834","177719","1116","ATGGCGGCGGAAGACGTACAATTTAACATCGCCGTGCCGGAAATTAATGCACAAACCTACGTCTTAATGGATTACAACTCCGGTGCCGTGTTGGCGTCCCTTAACCCTGATCAGCGCCAATATCCGGCATCATTGACCAAAATGATGACCAGCTATGTGGTCGGGCAGGCGATTAAGCAAGGTAAAATCCGTAATACGGATATGGTCACCATCGGCGAAAGCTCCTGGGGGCATAAATTCCCCGGTTCTTCCAAAATGTTCTTAAACTTAAATCAACAAGTTTCCGTTGCGGATTTACATCGCGGCATCATCATTGTTTCGGGTAATGACGCCTGCGTGGCAATGGCGGAGCATGTTTCCGGCACGGTGATGAACTTCGTTGATACCATGAATAAATATGTGGAACAGTTCGGTTTAAAAAATACCTATTTCACCACGGTGCACGGTTTAGATGAAGATAACCAATACTCTTCCGCCCGCGATATGGCGATTATCGGCGCGCGTATTATTCGTGATTTACCGGAAGAATATAAAATTTACGCCGAAAAAGATTTTACCTTTAACAAAATCAAACAGCCTAATCGCAACGGCTTGTTATGGGACAAAACCATTAACGTTGACGGTATGAAAACCGGTCACACGGATAAAGCGGGGTACAACCTGGTGGCTTCCGCCATCAGCCCGAACAATATGCGTTTGATTTCTGTGGTGATGGGCGTGCCGACTTATAAAGGTCGCGAAGTGGAAAGCAAAAAATTATTGCAATGGGGTTTTGCTAATTTTGAGACCTTCAAAACCTTGGATTCAGGCAAATCCATTTCCGAACAACGGGTGTATTACGGCGATGAAAGTAACATCCAATTAGGCGTGTTACAAGATGCTTTCATCACCATTCCGAAAGGCAAAAGCGCCGAGCTCAAAGCCCGTTACGAATTAGAGAAAAAATACCTTGAAGCGCCCCTTGCCAAAGGGCAAGTTGTGGGCAAGGTGGTGTATCAATTAGACGGCAAAGACATCGCCAGTGTAAACTTACAAGTGATGCAAGAAGTGAAAGAAGGCGGTATCTTCGGCAAAATCTGGGACTGGCTGGTGCTGACCATCAAAAGTTTATTTGAC","","","43911","MAAEDVQFNIAVPEINAQTYVLMDYNSGAVLASLNPDQRQYPASLTKMMTSYVVGQAIKQGKIRNTDMVTIGESSWGHKFPGSSKMFLNLNQQVSVADLHRGIIIVSGNDACVAMAEHVSGTVMNFVDTMNKYVEQFGLKNTYFTTVHGLDEDNQYSSARDMAIIGARIIRDLPEEYKIYAEKDFTFNKIKQPNRNGLLWDKTINVDGMKTGHTDKAGYNLVASAISPNNMRLISVVMGVPTYKGREVESKKLLQWGFANFETFKTLDSGKSISEQRVYYGDESNIQLGVLQDAFITIPKGKSAELKARYELEKKYLEAPLAKGQVVGKVVYQLDGKDIASVNLQVMQEVKEGGIFGKIWDWLVLTIKSLFD","177719","","penicillin-binding protein 5","Periplasm, Inner membrane, Cytoplasm","","
InterPro
IPR001967
Family
Peptidase S11, D-alanyl-D-alanine carboxypeptidase A
PR00725\"[43-54]T\"[99-116]T\"[126-139]TDADACBPTASE1
PF00768\"[6-242]TPeptidase_S11
InterPro
IPR012907
Domain
Peptidase S11, D-Ala-D-Ala carboxypeptidase A, C-terminal
PF07943\"[261-352]TPBP5_C
noIPR
unintegrated
unintegrated
G3DSA:3.40.710.10\"[4-261]Tno description
PTHR21581\"[10-371]TD-ALANYL-D-ALANINE CARBOXYPEPTIDASE


","BeTs to 11 clades of COG1686COG name: D-alanyl-D-alanine carboxypeptidaseFunctional Class: MThe phylogenetic pattern of COG1686 is ----------rlb-efghsn-jxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 6.3e-23) to 3/3 blocks of the PR00725 family, which is described as \"D-Ala-D-Ala carboxypeptidase 1 (S11) family signature\". Prints database entry for PR:PR00725. PR00725A 43-54 6e-07 PR00725B 99-116 2.9e-07 PR00725C 126-139 2.3e-05","Residues 184 to 256 match (1e-07) PD:PD589240 which is described as COMPLETE PROTEOME CARBOXYPEPTIDASE BINDING PENICILLIN TRANSMEMBRANE FRACTION A PENICILLIN-BINDING D-ALANYL-D-ALANINE ","","","","","","","","","","","","Fri Jan 10 14:08:32 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00254 is paralogously related to AA02103 (2e-07).","","","","","","Residues 6 to 242 (E-value = 6e-133) place AA00254 in the Peptidase_S11 family which is described as D-alanyl-D-alanine carboxypeptidase (PF00768)","","","","","McDonough MA, Anderson JW, Silvaggi NR, Pratt RF, Knox JR, KellyJA. Structures of two kinetic intermediates reveal speciesspecificity of penicillin-binding proteins. J Mol Biol. 2002 Sep 6;322(1):111-22. PMID: 12215418 Fusetti F, Dijkstra BW. Purification and light-scattering analysis of penicillin-bindingprotein 4 from Escherichia coli. Microb Drug Resist. 1996 Spring;2(1):73-6. PMID: 9158725","","Thu Dec 5 13:30:42 2002","1","","","" "AA00256","179794","178940","855","ATGAATCTAGAGCAAGCTGTAAAATATATGATAATTTTGTTTTCATTTTGCACCGCACTTTCCGTGCAAGCCGAAACAAAAAAATTATACGGCATTCAGGGACCGTCGTTGACTTACCGTCCGATGTCCGATAAAGCGCAGACTTATAATGTAAAAGGGGAAACTTACACCACGAAGCCGCACCAAACGGCAAAAAATTATTCCAAACAGGGGATTGCCAGCTATTACCATCATAAATTTAACGGGCGGAAAACTTCCAACGGCGATATTTACGATTCCACTTTATATACGGCGGCACATAAAACTTTGCCTTTGAATTCCTACGCAGTGGTCACCAATATGTATAACCAACGCAAAGTCATTGTGCGAATCAACGACCGTGGGCCCTTTGCTAAAGATCGTATTATTGATTTGTCCCACGCGGCGGCAAAAGAGATCGGTATTGTAAATTACGGTATGGGATTGGTTAAGGTGGAAGCGTTGCATGTGGACGCTAACGGTGAGCTTTCCGGCGCAGGCACCTCCACATTGGCGAAAGCAAGTAGAACAGAAGAAGGGCTAAAACGCCTGGTGGATAATGAAATCGCTTCCACGCCGGCGCCGCGACAAAATCGTAAAGTGGCAAGTGCCGAACGCTATGAAATTAAAATGGTCAATGTCGCCAGCAAGAAAAACGCCGAGCAGATCATTCAGGATTTAGCGTTAAATAATGTGAAAACGGAAATTGCCGCACATGGTCAAAAATACCATATTCATTTGGGACCTTTTAATTCAAAACAGGAAATCAACGAATTGAAAACACAATTAAGACGGTTAAATCATTCTGAACCGTTGATTGTGTATTCTTATAATCAA","","","31909","MNLEQAVKYMIILFSFCTALSVQAETKKLYGIQGPSLTYRPMSDKAQTYNVKGETYTTKPHQTAKNYSKQGIASYYHHKFNGRKTSNGDIYDSTLYTAAHKTLPLNSYAVVTNMYNQRKVIVRINDRGPFAKDRIIDLSHAAAKEIGIVNYGMGLVKVEALHVDANGELSGAGTSTLAKASRTEEGLKRLVDNEIASTPAPRQNRKVASAERYEIKMVNVASKKNAEQIIQDLALNNVKTEIAAHGQKYHIHLGPFNSKQEINELKTQLRRLNHSEPLIVYSYNQ","178940","","rare lipoprotein A precursor","Periplasm, Extracellular","","
InterPro
IPR005132
Domain
Rare lipoprotein A
PF03330\"[68-158]TDPBB_1
InterPro
IPR007730
Domain
Sporulation/cell division region, bacteria
PF05036\"[209-281]TSPOR
InterPro
IPR012997
Domain
Rare lipoprotein A, bacterial
TIGR00413\"[71-279]TrlpA: rare lipoprotein A
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.1070\"[204-284]Tno description
signalp\"[1-24]?signal-peptide


","BeTs to 12 clades of COG0797COG name: LipoproteinsFunctional Class: MThe phylogenetic pattern of COG0797 is -------q-----cefghsnujx-t-Number of proteins in this genome belonging to this COG is","","Residues 11 to 72 match (2e-07) PD:PD063651 which is described as RLPA-LIKE PROTEOME COMPLETE SIGNAL PRECURSOR ","","","","","","","","","","","","Thu Dec 5 13:44:51 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00256 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 66 to 161 (E-value = 1.8e-51) place AA00256 in the DPBB_1 family which is described as Rare lipoprotein A (RlpA)-like double-psi beta-barrel (PF03330)","","","","","Takase,I., Ishino,F., Wachi,M., Kamata,H., Doi,M., Asoh,S.,Matsuzawa,H., Ohta,T. and Matsuhashi,M.Genes encoding two lipoproteins in the leuS-dacA region of theEscherichia coli chromosomeJ. Bacteriol. 169 (12), 5692-5699 (1987)PubMed: 3316191","","Thu Dec 5 13:43:57 2002","1","","","" "AA00257","180964","179846","1119","ATGAAAATGAATGATCGTAATATTTGGCTGGAACTGTGGCGGCGTCTGCATATCGATTTGTGGCTGTTTATCGGGTTGGTGGTGGTTACCGGCTACGGCATGTTGGTGTTATATAGCGCTTCCGGTGCCAATGAAGCCATGTTTCGTAGCCGTATTGTGCAGGTGGCGCTCGGGTTTGTCGTAATGTTGGTCATGGCGCAATTTCCGCCGAAATTTTACCAGCGCATTGCGCCGTATTTATTTGGAATCGGCATCGTATTGCTTATTTTGGTGGATCTTATCGGCGCAACCAGTAAGGGGGCACAGCGTTGGCTGGATTTGGGCGTGGTACGTTTTCAGCCGTCCGAGATCGTAAAATTGGCAGTGCCGCTGATGGTGGCGGTGTATTTGGGCAATCGCCCACAACCCATTAAGTTAAAGGAAACGTTTATCGCACTGATCACCATTATTGTACCGACCTTACTCGTGGCGATTCAACCCGATTTGGGCACCGCAATTTTGGTTAGCGGTTCCGGCTTATTTGTGATATTTTTAGCCGGCATGAGCTGGTGGCTCATTTTAATTGCCGTGGTTGCGCTTGCGGGATTTATTCCGGTTATGTGGTTCTATTTAATGCACGACTATCAACGTGCCCGTGTGTTGACCTTATTTGATCCGGAAAAAGATTTATTGGGCGCGGGCTACCATATTTGGCAATCCAAAATTGCGATCGGTTCCGGTGGGTTATGGGGCAAAGGCTGGTTACAGGGAACGCAATCCCAGCTGGAGTTTTTACCCGAGCCGCACACGGATTTTATTTTCGCCGTGTTGAGTGAAGAATATGGCATGATTGGCTTTTTGGTTTTATTAGCCATTTATTTATTTATTGTTGCGCGCGGTTTAATGATTGGCGTTAATGCGCAAAGCGCTTTCGGGCGTATTTTAGTGGGGGCATTAACGTTAATTTTCTTCGTTTATGTCTTTGTTAACATCGGCATGGTAAGCGGCATTTTGCCTGTTGTGGGCGTGCCTTTACCATTGGTGAGTTATGGCGGTACATCCTATGTGGCAATTATGGCGGGCTTCGGTTTAATCATGTCAATTCATACTCACAAAGAACACTTTCTGAAAGGAACTAAC","","","43235","MKMNDRNIWLELWRRLHIDLWLFIGLVVVTGYGMLVLYSASGANEAMFRSRIVQVALGFVVMLVMAQFPPKFYQRIAPYLFGIGIVLLILVDLIGATSKGAQRWLDLGVVRFQPSEIVKLAVPLMVAVYLGNRPQPIKLKETFIALITIIVPTLLVAIQPDLGTAILVSGSGLFVIFLAGMSWWLILIAVVALAGFIPVMWFYLMHDYQRARVLTLFDPEKDLLGAGYHIWQSKIAIGSGGLWGKGWLQGTQSQLEFLPEPHTDFIFAVLSEEYGMIGFLVLLAIYLFIVARGLMIGVNAQSAFGRILVGALTLIFFVYVFVNIGMVSGILPVVGVPLPLVSYGGTSYVAIMAGFGLIMSIHTHKEHFLKGTN","179846","From Genbank:[gi:133265] This is one of the proteins responsible for the rod shape of E.coli. It is required for the expression of the enzymatic of PBP2 which is thought to synthesize peptidoglycan in the step of initiation of cell elongation.","rod-shape-determining protein","Inner membrane, Cytoplasm","","
InterPro
IPR001182
Family
Cell cycle protein
PF01098\"[20-367]TFTSW_RODA_SPOVE
PS00428\"[323-347]TFTSW_RODA_SPOVE
InterPro
IPR011923
Family
Rod shape-determining protein RodA
TIGR02210\"[19-366]TrodA_shape: rod shape-determining protein R
noIPR
unintegrated
unintegrated
signalp\"[1-31]?signal-peptide
tmhmm\"[20-40]?\"[76-96]?\"[143-177]?\"[183-203]?\"[224-244]?\"[277-297]?\"[307-327]?\"[341-361]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.5e-58) to 4/4 blocks of the IPB001182 family, which is described as \"Cell cycle proteins\". Interpro entry for IP:IPR001182. IPB001182A 100-117 1e-07 IPB001182B 227-248 1.3e-13 IPB001182C 257-278 2.3e-14 IPB001182D 322-347 1.3e-18","Residues 55 to 109 match (2e-09) PD:PD495342 which is described as CELL PROTEOME DIVISION COMPLETE FTSW TRANSMEMBRANE MEMBRANE INNER SHAPE PEPTIDOGLYCAN ","","","","","","","","","","","Mon Jan 13 16:42:29 2003","Mon Jan 13 16:42:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00257 is paralogously related to AA00837 (5e-47).","","","","","","Residues 20 to 367 (E-value = 1.1e-164) place AA00257 in the FTSW_RODA_SPOVE family which is described as Cell cycle protein (PF01098)","","","","","Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y.and Matsuhashi,M. Structural similarity among Escherichia coli FtsW and RodAproteins and Bacillus subtilis SpoVE protein, which function incell division, cell elongation, and spore formation,respectively. J. Bacteriol. 171(11): 6375-6378, 1989. PubMed: 2509435.Matsuzawa,H., Asoh,S., Kunai,K., Muraiso,K.,Takasuga,A. and Ohta,T. Nucleotide sequence of the rodA gene, responsible for the rod shape of Escherichia coli: rodA and the pbpA gene, encoding penicillin-binding protein 2, constitute the rodA operon J. Bacteriol. 171 (1), 558-560 (1989) PubMed: 2644207 ","","Mon Jan 13 16:43:20 2003","1","","","" "AA00258","182912","180954","1959","ATGAGTTTAAAAATATTATTAAATCAGCCGCAATACGATCCGATTCGTGACAAAAAAGCCGAGCGCAACTTATTTGCCCGTCGCGCTTTGGTGTCATTTATCGGCGTGTTGGTGTTGTCGGTGGTGTTAATTTTAAACTTGTATGATTTGCAGGTGGTCAATTATGACGGTTATCAAACCCGTTCCAACGGCAATCGTATTAAGTTGTTGCCGCTGCCGCCGACTCGCGGGTTGATTTATGATCGCAACGGCAAACTGCTGGCGGAAAATCTGACCTTTTTCGGGCTTTATATCGTGCCTGAAAAGGTGGAAAATTTAGACCGCACTTTTGAGGAGCTGAGGGTGTTGGTAGGCTTAACTGATGAAGATATTGCGAATTTTAACAAGGAACGGCGTCGCTCCTCCCGTTATATGCCGATTATGCTGAAACGAAATCTAACGGAAGAGCAAATTGCCCGTTTTGCGGTGAATCAATACAATTTCCAGAGTTTGGATGTGAAACCCTACTTTAAGCGCCATTATTTATACGGCGAACCGCTGACCCATGTTTTGGGCTATGTGTCAAAAATTAACGATCGTGATGTAGAACGCTTGAAAAAAGAGGAAAAGTACGCCAATTATTCCGGCACGCACGACTGGGGCAAACTCGGCATTGAGCGCTATTATGAAGATGCTTTACACGGCACCACAGGCTTTGAAGAAGTAGAAGTGAACAGTCGCGGTAAAGTGATCCGCAAATTGCGCGCACAACCCGCCATTGCCGGCAAAAGCATTCACTTGACCATTGACTTAAATTTACAGCTTTACGTTACCGATTTATTGGCGGGACACAAAGGCGCCGTGGTAGTGATGGATCCGAAAGACAACAGTATTTTAGCCATGGTTTCCGTACCGAGTTATGACAATAATCTTTTTGTGGATGGTATTTCCGGGGCGGATTACCGTCGCTTGCTCAATGACTCAAATCGCCCGCTTTATAGCCGCGTGACCCAAGGCGCCTATCCGCCGGCATCAACCGTGAAACCGTTCATCGCTGTTTCCGCATTGCAGGAAAATGTGATTACGCCGAACATGACCATTTATGATCCCGGCTATTGGATGTTGCCGAACAGTACCAAGCGTTTTCGTGACTGGCGTAAAGGCGGGCACGGCATGATCAATCTAAACAAGGCCATTACCGAATCCTCCGATACGTATTTTTATCAAACTGCCTATAACCTCGGCATCGATCGCCTGTCCGATTGGATGAAACGCTTTGGTTTCGGTGTCCCGACGGGGATTGATATTCAGGAAGAAACCAGTGCCAATATGCCGACCCGTGAATGGAAGCAAAAACGCTATAAAAAAGCCTGGGTGCAGGGCGATACAATTTCCGTAGGCATTGGGCAGGGGTACTGGACGGCGACGCCGTTACAGCTGGCAAAAGCCACCAGCATTTTAGTGAATAACGGCAAGGTAAACACACCGCACTTAATGAAGAGCGTGGAAGGTTCGGTAGTAGAACCCTATAAAGATCCGTTGTTGTACGAAGATATTACCGAACCGAAACAGTATTTCTGGGATGAGGCGAAACGCGGTATGTACAACGTGGTAAACGGTGCCGGCGGAACGGGGCGTAAAGCTTTTATCGGCACGCCTTATCGTGTCGCCGGTAAATCCGGTACGGCACAGGTGTTCAGTTTGAAAGAAAATCAAACGTATAACGCCGGCAGCTTGAAAAAAGAATTGCACGATCACGCGTGGTTTACCGCTTTCGCACCTTATGATAACCCACAAATCGTGGTGTCGATGATTTTGGAAAATGCCGGCGGCGGTTCCAGTAATGCGGCGCCGATCGTCAGAAAAATTATGGATTATTATTTTAAACAAAATACCCCGCAAGCCGTGATGTCGCTATTCGATGAGCCTGAATCGCCGGAATCGGAACCCGCAACAGGAGACGAACCGAATGAAAATGAA","","","74022","MSLKILLNQPQYDPIRDKKAERNLFARRALVSFIGVLVLSVVLILNLYDLQVVNYDGYQTRSNGNRIKLLPLPPTRGLIYDRNGKLLAENLTFFGLYIVPEKVENLDRTFEELRVLVGLTDEDIANFNKERRRSSRYMPIMLKRNLTEEQIARFAVNQYNFQSLDVKPYFKRHYLYGEPLTHVLGYVSKINDRDVERLKKEEKYANYSGTHDWGKLGIERYYEDALHGTTGFEEVEVNSRGKVIRKLRAQPAIAGKSIHLTIDLNLQLYVTDLLAGHKGAVVVMDPKDNSILAMVSVPSYDNNLFVDGISGADYRRLLNDSNRPLYSRVTQGAYPPASTVKPFIAVSALQENVITPNMTIYDPGYWMLPNSTKRFRDWRKGGHGMINLNKAITESSDTYFYQTAYNLGIDRLSDWMKRFGFGVPTGIDIQEETSANMPTREWKQKRYKKAWVQGDTISVGIGQGYWTATPLQLAKATSILVNNGKVNTPHLMKSVEGSVVEPYKDPLLYEDITEPKQYFWDEAKRGMYNVVNGAGGTGRKAFIGTPYRVAGKSGTAQVFSLKENQTYNAGSLKKELHDHAWFTAFAPYDNPQIVVSMILENAGGGSSNAAPIVRKIMDYYFKQNTPQAVMSLFDEPESPESEPATGDEPNENE","180954","From GenBank (gi:1172028):PBP2 is responsible for the determination of the rod shape of the cell. Its synthesize cross linked peptiglycan from the lipid intermediates. ","penicillin binding protein 2","Inner membrane, Outer membrane, Periplasm","","
InterPro
IPR001460
Domain
Penicillin-binding protein, transpeptidase
PF00905\"[279-618]TTranspeptidase
InterPro
IPR005311
Domain
Penicillin-binding protein, dimerisation domain
PF03717\"[71-248]TPBP_dimer
noIPR
unintegrated
unintegrated
G3DSA:3.40.710.10\"[261-628]Tno description
signalp\"[1-40]?signal-peptide
tmhmm\"[29-49]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.3e-12) to 3/3 blocks of the IPB001460 family, which is described as \"Penicillin binding protein transpeptidase domain\". Interpro entry for IP:IPR001460. IPB001460A 76-84 0.0021 IPB001460B 260-268 3.6 IPB001460C 469-484 2.7e-05","Residues 172 to 267 match (3e-08) PD:PD560094 which is described as PREDICTED PENICILLIN-BINDING ","","","","","","","","","","","Tue Apr 1 14:38:43 2003","Fri Jan 10 14:00:37 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00258 is paralogously related to AA00844 (2e-20) and AA01304 (1e-05).","","","","","","Residues 279 to 618 (E-value = 6.1e-110) place AA00258 in the Transpeptidase family which is described as Penicillin binding protein transpeptidase domain (PF00905)","","","","","Laible G, Hakenbeck R, Sicard MA, Joris B, Ghuysen JM. Nucleotide sequences of the pbpX genes encoding thepenicillin-binding proteins 2x from Streptococcus pneumoniae R6and a cefotaxime-resistant mutant, C506. Mol Microbiol 1989 Oct;3(10):1337-48. PubMed: 2615650 Wijayarathna CD, Wachi M, Nagai K. Isolation of ftsI and murE genes involved in peptidoglycansynthesis from Corynebacterium glutamicum. Appl Microbiol Biotechnol. 2001 May;55(4):466-70. PMID: 11398928 Ubukata K, Shibasaki Y, Yamamoto K, Chiba N, Hasegawa K, TakeuchiY, Sunakawa K, Inoue M, Konno M. Association of amino acid substitutions in penicillin-bindingprotein 3 with beta-lactam resistance in beta-lactamase-negativeampicillin-resistant Haemophilus influenzae. Antimicrob Agents Chemother. 2001 Jun;45(6):1693-9. PMID: 11353613","","Tue Apr 1 14:38:43 2003","1","","","" "AA00259","183392","182928","465","GTGAAAATTCAGTTAATTGCCGTTGGAACCAAAATGCCGGGGTGGGTGACTACGGGCTTTGAGGAATATCAACGCCGCTTTCCGAAAGAGATGCCTTTTGAACTCATTGAAATTCCTGCCGGTAAACGGGGTAAAAATGCCGACATCAAACGTATTTTGGAACAGGAAGGCAAAGCCATGTTGGCGGCTGCCGGAAAAGGCAAGGTGGTGACACTGGACATTCCAGGTAACCCCTGGACCACGGAACAGCTGGCTCAACAATTAGAAGGCTGGAAAAATGACGGGCGCGATGTTTGTTTGCTCATCGGCGGGCCGGAAGGCTTGGCACTGGAATGTAAAGCCGCCGCCGAACAAAGTTGGTCACTTTCACCGCTTACTTTGCCGCATCCGTTGGTGCGCGTGGTGGTGGCGGAAAGCCTGTATCGCGCGTGGTCGCTCACTGCCAATCATCCATATCATCGAGAA","","","19713","VKIQLIAVGTKMPGWVTTGFEEYQRRFPKEMPFELIEIPAGKRGKNADIKRILEQEGKAMLAAAGKGKVVTLDIPGNPWTTEQLAQQLEGWKNDGRDVCLLIGGPEGLALECKAAAEQSWSLSPLTLPHPLVRVVVAESLYRAWSLTANHPYHRE","182928","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003742
Family
Protein of unknown function DUF163
PF02590\"[1-153]TDUF163
TIGR00246\"[1-155]TTIGR00246: conserved hypothetical protein T
noIPR
unintegrated
unintegrated
G3DSA:3.40.1280.10\"[1-155]Tno description
PIRSF004505\"[1-154]TPredicted methyltransferase, bacterial type


","No hits to the COGs database.","Significant hit ( 5.8e-63) to 2/2 blocks of the IPB003742 family, which is described as \"DUF163\". Interpro entry for IP:IPR003742. IPB003742A 1-44 4.4e-24 IPB003742B 101-154 7.8e-38","Residues 1 to 154 match (2e-69) PD:PD010975 which is described as PROTEOME COMPLETE FRAME X OPEN ORFX READING YBEA UU180 YYDA ","","","","","","","","","","","","Thu Dec 5 14:18:57 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00259 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 153 (E-value = 2.6e-79) place AA00259 in the DUF163 family which is described as Uncharacterized ACR, COG1576 (PF02590)","","","","","","","","1","","","" "AA00260","183760","183455","306","ATGTCATTAGTCGATTTCGTGGTGAATAAACTGGATAATTTAAAAGCCACCGATATTTTATCGTTAAACGTGAAGGGAAAATCCTCCGTCACCGATACCATGATCCTTTGCACCGGCACCTCTTCCCGCCATGTGTCTTCTTTGGCGCAAAAATTAATTACCGAATGCAAACTTGCCGGTATCGACGTGTTCGGCGATGAAGGCAAGGAAACCGCCGATTGGGTGGTAGTGGATTTGGGTGACGCCATCGTACATATCATGCAGGCAGAAAGCCGCGAAATGTATCAGCTGGAAAAACTTTGGGCA","","","11170","MSLVDFVVNKLDNLKATDILSLNVKGKSSVTDTMILCTGTSSRHVSSLAQKLITECKLAGIDVFGDEGKETADWVVVDLGDAIVHIMQAESREMYQLEKLWA","183455","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR004394
Family
Iojap-related protein
PTHR21043\"[1-102]TIOJAP SUPERFAMILY ORTHOLOG
PF02410\"[1-102]TDUF143
TIGR00090\"[3-101]TTIGR00090: iojap homolog


","No hits to the COGs database.","Significant hit ( 1.4e-30) to 2/2 blocks of the IPB003456 family, which is described as \"Domain of unknown function DUF143\". Interpro entry for IP:IPR003456. IPB003456A 18-45 3.9e-11 IPB003456B 74-101 4.9e-18","Residues 34 to 101 match (4e-27) PD:PD008103 which is described as COMPLETE PROTEOME IOJAP IOJAP-RELATED SUPERFAMILY ORTHOLOG YBEB YQEL TP0738 SIMILAR ","","","","","","","","","","","","Thu Dec 5 14:20:52 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00260 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 102 (E-value = 3.6e-48) place AA00260 in the DUF143 family which is described as Domain of unknown function DUF143 (PF02410)","","","","","","","","1","","","" "AA00263","185155","183830","1326","GTGTCTAATTTTTGGGGATTTTCCCTGTTCGTGCTATGCTTAGCGCCAATTTTTTACGATAAATTTGAGACTATGCAACAGAATTATTTAAGTTCGGCACGTTTCGCCGATTTAGCCCTACATCCTTTGGTGTTACAGGCGTTGAACGACAAAGGATTTGATTTTTGTACGCCGATTCAGGCGCTCTCGCTGCCCATTACGTTACGAGGCAAAGATGTTGCCGGACAGGCACAAACCGGCACCGGAAAAACAATCGCGTTTTTGTCCGCACTTTTCCATCATTTATTAACCTACCCGAAACAAACGGAAGCCAATCAACCGCGCGCTTTGATTCTGGCACCAACCCGCGAATTGGCGGTGCAAATTGAACACGACGCGCAGATTTTCTTAAAAACAACCAAATTTAAGACCGCACTTGCCTACGGCGGTGACGGCTATGACAAGCAACTCAAAGCCATTGAAAACGGCGTGGACGTGCTTATCGGCACCACGGGGCGCGTAATTGATTATGTGAAACAGGGCGTGATTCGTTTGGATCAGATTCAAACGGTGGTGCTGGACGAAGCGGATCGTATGTTCGATTTGGGTTTTATCCGTGACATTCGCTATTTGTTACGCAAATGCCCGCCGCCACAACAACGCTTGACCATGTTGTTCTCCGCCACCTTGTGTTACAAAGTGCGTGAACTGGCTTTTGAAGATATGAATAGCCCGGAATATGTGGAAATCGAACCTGAACAAAAAACCGGGCAGCAAATTAAAGAAGAATTATTTTATCCGTCCAATCGGGACAAAATGCCGTTGTTGCTGACGCTCTTGGAAGAAGAATGGCCGGAGCGCTGTATTGTGTTTGCCAACACCAAACATAAATGCGAGGAAATTTGGGGCTATTTGGCGGCGGACGGGCATCGCGTGGGCTTATTAACCGGCGATGTGGCGCAGAAAAAACGGCTTTCCTTATTGAAAAAATTTACCGACGGCGATTTGGATATTTTAGTGGCGACGGACGTGGCGGCGCGCGGGCTGCATATTGCGGAAGTGACTCATGTGTTCAATTACGATTTGCCGGACGATCGGGAAGATTATGTGCACCGTATCGGGCGTACCGGACGTGCCGGCGAAAGCGGCATTTCCATCAGCTTCGCCTGCGAGCAATACGCCATGAATTTGCCGGCGATTGAAGAATATATCGGACACAGCATTACCGTGAGCCAATACGATCCGAACGCGTTATTACAGGATTTGCCGAAGCCTTATCGATTAAAACGGCAAACCAATTTCAGCGCACAGAATAACAATCGCCGCAAACCGTTTCGCGCAAAACGC","","","50188","VSNFWGFSLFVLCLAPIFYDKFETMQQNYLSSARFADLALHPLVLQALNDKGFDFCTPIQALSLPITLRGKDVAGQAQTGTGKTIAFLSALFHHLLTYPKQTEANQPRALILAPTRELAVQIEHDAQIFLKTTKFKTALAYGGDGYDKQLKAIENGVDVLIGTTGRVIDYVKQGVIRLDQIQTVVLDEADRMFDLGFIRDIRYLLRKCPPPQQRLTMLFSATLCYKVRELAFEDMNSPEYVEIEPEQKTGQQIKEELFYPSNRDKMPLLLTLLEEEWPERCIVFANTKHKCEEIWGYLAADGHRVGLLTGDVAQKKRLSLLKKFTDGDLDILVATDVAARGLHIAEVTHVFNYDLPDDREDYVHRIGRTGRAGESGISISFACEQYAMNLPAIEEYIGHSITVSQYDPNALLQDLPKPYRLKRQTNFSAQNNNRRKPFRAKR","183830","","ATP-dependent RNA helicase","Cytoplasm, Periplasm","","
InterPro
IPR000629
Domain
ATP-dependent helicase, DEAD-box
PS00039\"[185-193]TDEAD_ATP_HELICASE
InterPro
IPR001650
Domain
Helicase, C-terminal
PF00271\"[297-373]THelicase_C
SM00490\"[292-373]THELICc
PS51194\"[265-412]THELICASE_CTER
InterPro
IPR011545
Domain
DEAD/DEAH box helicase, N-terminal
PF00270\"[57-230]TDEAD
InterPro
IPR014001
Domain
DEAD-like helicases, N-terminal
SM00487\"[52-253]TDEXDc
InterPro
IPR014014
Domain
DEAD-box RNA helicase Q motif
PS51195\"[33-61]TQ_MOTIF
InterPro
IPR014021
Domain
Helicase superfamily 1 and 2 ATP-binding
PS51192\"[64-241]THELICASE_ATP_BIND_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[20-251]Tno description
PTHR10967\"[35-401]TDEAD BOX ATP-DEPENDENT RNA HELICASE
PTHR10967:SF51\"[35-401]TATP-DEPENDENT RNA HELICASE
signalp\"[1-19]?signal-peptide


","No hits to the COGs database.","Significant hit ( 4.7e-79) to 5/5 blocks of the IPB000629 family, which is described as \"ATP-dependent helicase, DEAD-box\". Interpro entry for IP:IPR000629. IPB000629A 52-95 2.8e-21 IPB000629B 110-122 1.8e-08 IPB000629C 158-169 0.0033 IPB000629D 181-204 6.4e-11 IPB000629E 335-376 1.1e-29","Residues 109 to 206 match (7e-07) PD:PD555560 which is described as HELICASE ATP-DEPENDENT ATP-BINDING RNA ","","","","","","","","","","","","Thu Dec 5 14:25:46 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00263 is paralogously related to AA00148 (2e-69), AA00506 (2e-61), AA01928 (3e-07) and AA00927 (1e-06).","","","","","","Residues 297 to 373 (E-value = 9.9e-33) place AA00263 in the Helicase_C family which is described as Helicase conserved C-terminal domain (PF00271)","","","","","Py,B., Higgins,C.F., Krisch,H.M. and Carpousis,A.J. A DEAD-box RNA helicase in the Escherichia coli RNA degradosome.Nature 381 (6578), 169-172.1996. PubMed: 8610017. Peng,H.L., Hsieh,M.J., Zao,C.L. and Chang,H.Y. Nucleotide sequence and expression in Escherichia coli of theKlebsiella pneumoniae deaD gene. J. Biochem. 115(3): 409-414.1994. PubMed: 8056751. Toone,W.M., Rudd,K.E. and Friesen,J.D. deaD, a new Escherichia coli gene encoding a presumedATP-dependent RNA helicase, can suppress a mutation in rpsB, thegene encoding ribosomal protein S2. J. Bacteriol. 173(11): 3291-3302.1991 PubMed: 2045359.Nishi,K., Morel-Deville,F., Hershey,J.W., Leighton,T. and Schnier,J. An eIF-4A-like protein is a suppressor of an Escherichia coli mutant defective in 50S ribosomal subunit assembly Nature 336 (6198), 496-498 (1988) PubMed: 2461520Kalman,M., Murphy,H. and Cashel,M. rhlB, a new Escherichia coli K-12 gene with an RNA helicase-likeprotein sequence motif, one of at least five such possible genesin a prokaryote. New Biol. 3(9): 886-895.1991 PubMed: 1931833.","","Thu Dec 5 14:29:23 2002","1","","","" "AA00264","185192","185362","171","GTGGACCTGAAAAACGCCCGCAAAAACCACCGCACTTTTCTGCAATCCGGGGTTGGATCAAACAAACACAGAAAAAAAACGTTAAAAACTAGACAGTGCCTAAATTTAATGCTAAGTTACGCACCAATTTCAAATTGGCCTCCATTCATTTATTTCTTAAACATTCAACTC","","","6683","VDLKNARKNHRTFLQSGVGSNKHRKKTLKTRQCLNLMLSYAPISNWPPFIYFLNIQL","185362","","hypothetical protein","Cytoplasm","No significant similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
tmhmm\"[33-53]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 12:33:10 2004","Sun Feb 22 12:33:10 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00264 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 12:33:10 2004","","","","","","","","","","","","","1","","","" "AA00265","185447","186643","1197","ATGGGTTTGGAAAATTTAGCCCGTTTACGCAAACAAGACATTATTTTTGCGATTTTGAAACAGCACGCCAAAGGTGGGGAAGATATTTTCGGCGGCGGCGTGTTGGAAATTTTGCCGGACGGTTTCGGTTTCCTGCGTTCCGACGACAGTTCCTATTTAGCCGGCCCGGATGATATTTATGTCAGCCCGAGCCAAATTCGTCGTTTCAATTTACAGACCGGGGACAAAATCGAAGGGAAAATTCGACCGCCTAAAGAAGGCGAACGCTACTTTGCCCTCCTTAAAGTTGACCAAGTCAACGACGACAAACCGGAAGTATCCCGCAGCAAAATCCTTTTCGAAAACTTAACCCCATTACACGCCAACTCCCGTTTAAGAATGGAACGCGGCAACGGTTCTACCGAAGATTTAACCGCCCGTATTTTAGATTTGGCCTCCCCGATTGGTAAAGGTCAGCGTGGTTTGATCGTGGCGCCGCCAAAAGCGGGTAAAACCATGTTGCTGCAAAATATCGCACAAAGTATCACGCACAATTACCCTGATGTCGAACTTATCGTCTTGCTGATTGATGAACGTCCGGAAGAGGTAACGGAAATGCAACGTTCCGTGAAAGGCGAAGTCATCGCGTCCACCTTCGACGAACCGGCGACCCGTCACGTCCAAGTGGCGGAAATGGTTATTGAAAAAGCCAAACGTGCCGTCGAACACAAAAAAGACGTAGTGATTTTACTCGATTCCATCACTCGTTTAGCGCGCGCTTACAACACCGTAACCCCGGCTTCCGGCAAAATTTTATCCGGTGGTGTGGACGCCAACGCTCTACATCGCCCAAAACGCTTTTTTGGTGCGGCACGTAACGTAGAAGAAGGCGGTAGCTTAACCATTATCGCCACCGCGCTGGTGGATACCGGTTCGAAAATGGACGAAGTAATCTTCGAAGAATTTAAAGGCACCGGTAACATGGAATTGCATCTTTCGCGTAAAATCGCGGAAAAACGCGTGTTCCCGGCAATTGACTTCAACCGTTCAGGCACCCGTAAAGAAGACTTGCTTACTACCCCTGACGAGTTACAAAAAATGTGGATCCTGCGCAAAATCCTTAACCCAATGGGCGAAGTGGAAGCCATGGAATTCCTTATCGACAAACTCGCCGTAGCAAAAACCAACGAAGAATTTTTTGAGATTATGAAACGCTCA","","","46857","MGLENLARLRKQDIIFAILKQHAKGGEDIFGGGVLEILPDGFGFLRSDDSSYLAGPDDIYVSPSQIRRFNLQTGDKIEGKIRPPKEGERYFALLKVDQVNDDKPEVSRSKILFENLTPLHANSRLRMERGNGSTEDLTARILDLASPIGKGQRGLIVAPPKAGKTMLLQNIAQSITHNYPDVELIVLLIDERPEEVTEMQRSVKGEVIASTFDEPATRHVQVAEMVIEKAKRAVEHKKDVVILLDSITRLARAYNTVTPASGKILSGGVDANALHRPKRFFGAARNVEEGGSLTIIATALVDTGSKMDEVIFEEFKGTGNMELHLSRKIAEKRVFPAIDFNRSGTRKEDLLTTPDELQKMWILRKILNPMGEVEAMEFLIDKLAVAKTNEEFFEIMKRS","186643","Brennan,C.A. and Platt,T. Mutations in an RNP1 consensus sequence of Rho protein reduce RNAbinding affinity but facilitate helicase turnover.1991 J. Biol. Chem. 266(26): 17296-17305. PubMed: 91373347. Dombroski,A.J., Brennan,C.A., Spear,P. and Platt,T. Site-directedalterations in the ATP-binding domain of rho protein affect itsactivities as a termination factor. J. Biol. Chem. 263(35): 18802-18809.1988. PubMed: 8906670. Matsumoto,Y., Shigesada,K., Hirano,M. and Imai,M. Autogenous regulation of the gene for transcription terminationfactor rho in Escherichia coli: localization and function of itsattenuators. J. Bacteriol. 166(3): 945-958.1986 PubMed: 86223816.","transcription termination factor","Cytoplasm","","
InterPro
IPR000194
Domain
ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding
PF00006\"[137-345]TATP-synt_ab
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[150-335]TAAA
InterPro
IPR004665
Family
Transcription termination factor Rho
TIGR00767\"[1-398]Trho: transcription termination factor Rho
InterPro
IPR011112
Domain
Rho termination factor, N-terminal
PF07498\"[1-27]TRho_N
InterPro
IPR011113
Domain
Rho termination factor, RNA-binding
PF07497\"[29-106]TRho_RNA_bind
InterPro
IPR011129
Domain
Cold shock protein
SM00357\"[32-98]TCSP
noIPR
unintegrated
unintegrated
G3DSA:1.10.720.10\"[1-27]Tno description
G3DSA:3.40.50.300\"[109-399]Tno description
PTHR15184\"[1-376]TATP SYNTHASE
PTHR15184:SF2\"[1-376]TTRANSCRIPTION TERMINATION FACTOR RHO


","No hits to the COGs database.","Significant hit ( 1e-12) to 2/2 blocks of the IPB002059 family, which is described as \"Cold-shock DNA-binding domain\". Interpro entry for IP:IPR002059. IPB002059A 31-45 0.029 IPB002059B 58-96 1e-08 IPB002059B 181-219 0.11Significant hit ( 2.8e-06) to 2/5 blocks of the IPB000194 family, which is described as \"ATP synthase alpha and beta subunit, N-terminal\". Interpro entry for IP:IPR000194. IPB000194B 137-174 3.3e-05 IPB000194E 292-339 36","Residues 140 to 199 match (5e-24) PD:PD526659 which is described as ATP HYDROLASE ION HYDROGEN SYNTHASE ATP-BINDING SYNTHESIS CF1 BETA SUBUNIT ","","","","","","","","","","","Wed Jul 11 17:24:25 2007","Thu Dec 5 14:31:52 2002","","Wed Jul 11 17:24:25 2007","Wed Jul 11 17:24:25 2007","Wed Jul 11 17:24:25 2007","yes","Fri Feb 20 15:41:32 MST 1998","AA00265 is paralogously related to AA01482 (2e-07) and AA01486 (0.001).","Wed Jul 11 17:24:25 2007","","","","","Residues 181 to 351 (E-value = 1.6e-39) place AA00265 in the ATP-synt_ab family which is described as ATP synthase alpha/beta family, nucleotide-binding domain (PF00006)","Wed Jul 11 17:24:25 2007","","","","","","","1","","","" "AA00266","188006","186774","1233","ATGACAACAAACGTAAATAGCTATGGCTGGAAAGCCTTGCTGGGTTCCGCCGTGGGTTATGCCATGGACGGTTTCTATCTTCTCATTCTCGGTTTCATGTTAAGCGCTATTTCCGCCGATTTAGGTTTAACCCCGGCACAGGGCGGTTCTTTGGTCACCTGGACCTTAGTCGGCGCGGTAGTCGGTGGCATCTTATTCGGTGCGTTAAGTGACAAATACGGGCGCGTGCGCGTGCTCATGTGGACGATTATCCTATTCGCCGTGTTCACCGGTTTATGTGCCTTAGCGCAAGGGTATTGGGATTTGCTCATTTACCGCACCATCGCCGGAATCGGCTTGGGCGGCGAATTCGGTATTGGCATGACATTGGCGGCGGAAGCCTGGCCGGCGCGTCATCGCGCCAAAGCGGCATCTTATGTGGCGCTCGGCTGGCAAGTCGGCGTGCTGGGGGCGGCGTTGCTGACACCGGTATTATTACCGCATATCGGCTGGCGCGGAATGTTTGTGGTGGGTATCTTCCCGGCATTTGTCGCCTGGTATTTACGCGCTCACTTACATGAACCTGAAATTTTTGTGCAAAAACAAACCGCACTTTCTGAGCGCAAAGCGGAAAAAAGCGGTTGGTTTTCCAAGTTGGAATCGTTCAAATTACTGGTGAAAGATAAAGCCACCATCAAAATCAGTTTAGGCGTTGTGGTGCTGACTTCCGTACAAAATTTCGGGTATTACGGCATCATGATTTGGATGCCGAATTTTCTCTCCAAGCAACTGAGTTTCAGCTTAACAAAATCCGGCATTTGGACAGCGGTCACCGTGTGCGGCATGATGGTCGGCATCTGGATTTTCGGACGTTTGGCGGATCATATCGGGCGCAAACCGAGTTTTCTGTTATTCCAAGCCGGTGCCGTGGTGAGTATTTTCGCCTATTCTCAATTAGCGGACCCGACGGCGACGCTGATTGCCGGCGCATTTTTAGGGATGTTTGTGAACGGCATGATGGGCGGTTACGGTGCCTTAATGGCGGAAGCCTACCCAACTCAAGCGCGCGCTACCGCACAAAATGTGCTATTTAACTTAGGGCGCGCCGTCGGCGGATTCGGACCGATTGTGGTCGGTGCGATCGTCTGCGCATATTCATTCCAAACCGCCATTGCCTTATTGGCAGTGATTTATGTGATTGATATGTTGGCGACCGTGTTCCTGGTACCGGAATTAAAGGGCAAAGCGTTAAAT","","","44036","MTTNVNSYGWKALLGSAVGYAMDGFYLLILGFMLSAISADLGLTPAQGGSLVTWTLVGAVVGGILFGALSDKYGRVRVLMWTIILFAVFTGLCALAQGYWDLLIYRTIAGIGLGGEFGIGMTLAAEAWPARHRAKAASYVALGWQVGVLGAALLTPVLLPHIGWRGMFVVGIFPAFVAWYLRAHLHEPEIFVQKQTALSERKAEKSGWFSKLESFKLLVKDKATIKISLGVVVLTSVQNFGYYGIMIWMPNFLSKQLSFSLTKSGIWTAVTVCGMMVGIWIFGRLADHIGRKPSFLLFQAGAVVSIFAYSQLADPTATLIAGAFLGMFVNGMMGGYGALMAEAYPTQARATAQNVLFNLGRAVGGFGPIVVGAIVCAYSFQTAIALLAVIYVIDMLATVFLVPELKGKALN","186774","","conserved hypothetical protein (probable metabolite transport protein)","Inner membrane, Extracellular","","
InterPro
IPR005829
Family
Sugar transporter superfamily
PS00217\"[108-133]?SUGAR_TRANSPORT_2
InterPro
IPR007114
Family
Major facilitator superfamily
PS50850\"[12-406]TMFS
InterPro
IPR011701
Family
Major facilitator superfamily MFS_1
PF07690\"[16-376]TMFS_1
noIPR
unintegrated
unintegrated
PTHR11600\"[4-411]TSUGAR TRANSPORTER
PTHR11600:SF25\"[4-411]TMETABOLITE TRANSPORT PROTEIN-RELATED
signalp\"[1-38]?signal-peptide
tmhmm\"[10-30]?\"[49-69]?\"[79-99]?\"[103-125]?\"[140-160]?\"[166-181]?\"[227-247]?\"[266-286]?\"[295-313]?\"[319-339]?\"[359-379]?\"[383-403]?transmembrane_regions


","BeTs to 20 clades of COG0477COG name: Permeases of the major facilitator superfamilyFunctional Class: G,E,P,RThe phylogenetic pattern of COG0477 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 6.4e-09) to 1/2 blocks of the IPB003662 family, which is described as \"General substrate transporters\". Interpro entry for IP:IPR003662. IPB003662A 102-134 6.3e-09 IPB003662A 318-350 0.017","Residues 326 to 362 match (2e-10) PD:PD447732 which is described as PROTEOME TRANSMEMBRANE COMPLETE INNER HI1104 SPY1340 MEMBRANE METABOLITE ","","","","","","","","","","","","Thu Dec 5 14:36:27 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00266 is paralogously related to AA02864 (2e-10), AA01731 (5e-07), AA01463 (2e-06), AA00062 (6e-04) and AA00691 (0.001).","","","","","","Residues 11 to 410 (E-value = 1.7e-18) place AA00266 in the Sugar_tr family which is described as Sugar (and other) transporter (PF00083)","","","","","","","","1","","","" "AA00267","188093","188203","111","GTGCGCCAGTCTACTGCTTTCAGGGAAAATTTCAATAAGCAAAGCACAGAAAGTGCGGTCGGTTTTGAATGTGTTTTTTACGGCGGGAATGTAGAATCACCAGAAAAAATT","","","4139","VRQSTAFRENFNKQSTESAVGFECVFYGGNVESPEKI","188203","","hypothetical protein","Periplasm, Cytoplasm","No significant similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 12:34:30 2004","Sun Feb 22 12:34:30 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00267 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 12:34:30 2004","","","","","","","","","","","","","1","","","" "AA00268","188471","188244","228","ATGAGCATTGAAGAACGCGTAAAAAAAATCATCGTTGAACAATTAGGCGTGAAAGAAGAAGATGTAAAACCTGAAGCGTCTTTCGTTGAAGATTTAGGTGCGGATTCTTTAGATACTGTTGAATTGGTGATGGCTTTAGAAGAAGAATTCGATATCGAAATTCCGGATGAAGAAGCTGAAAAAATCACAACAGTTCAATCAGCGATTGATTACGTTCAAAACAATCAA","","","8566","MSIEERVKKIIVEQLGVKEEDVKPEASFVEDLGADSLDTVELVMALEEEFDIEIPDEEAEKITTVQSAIDYVQNNQ","188244","","acyl carrier protein (ACP)","Cytoplasm","","
InterPro
IPR003231
Family
Acyl carrier protein (ACP)
PD000887\"[31-76]TACP_PASMU_Q9CJS5;
TIGR00517\"[1-76]Tacyl_carrier: acyl carrier protein
InterPro
IPR006162
PTM
Phosphopantetheine attachment site
PS00012\"[31-46]TPHOSPHOPANTETHEINE
InterPro
IPR006163
Domain
Phosphopantetheine-binding
PF00550\"[5-72]TPP-binding
PS50075\"[3-73]TACP_DOMAIN
InterPro
IPR009081
Family
Acyl carrier protein-like
G3DSA:1.10.1200.10\"[3-72]Tno description
noIPR
unintegrated
unintegrated
PTHR20863\"[2-76]TACYL CARRIER PROTEIN/ZINC FINGER PROTEIN 593-RELATED
PTHR20863:SF5\"[2-76]TACYL CARRIER PROTEIN


","BeTs to 18 clades of COG0236COG name: Acyl carrier proteinFunctional Class: I,QThe phylogenetic pattern of COG0236 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 7.3e-06) to 1/1 blocks of the IPB003880 family, which is described as \"Phosphopantetheine attachment site\". Interpro entry for IP:IPR003880. IPB003880 35-44 8.7e-06","Residues 3 to 76 match (2e-15) PD:PD000887 which is described as ACYL CARRIER PHOSPHOPANTETHEINE BIOSYNTHESIS ACP FATTY ACID COMPLETE PROTEOME CHLOROPLAST ","","","","","","","","","","","","Thu Dec 5 14:38:06 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00268 is paralogously related to AA01195 (1e-05) and AA01194 (2e-04).","","","","","","Residues 5 to 72 (E-value = 1.4e-24) place AA00268 in the PP-binding family which is described as Phosphopantetheine attachment site (PF00550)","","","","","Hoang TT, Sullivan SA, Cusick JK, Schweizer HP. beta-Ketoacyl acyl carrier protein reductase (FabG) activity ofthe fatty acid biosynthetic pathway is a determining factor of3-oxo-homoserine lactone acyl chain lengths. Microbiology. 2002 Dec;148(Pt 12):3849-56. PMID: 12480888 Keating MM, Gong H, Byers DM. Identification of a key residue in the conformational stability ofacyl carrier protein. Biochim Biophys Acta. 2002 Dec 16;1601(2):208-14. PMID: 12445484 Florova G, Kazanina G, Reynolds KA. Enzymes involved in fatty acid and polyketide biosynthesis inStreptomyces glaucescens: role of FabH and FabD and their acylcarrier protein specificity. Biochemistry. 2002 Aug 20;41(33):10462-71. PMID: 12173933 McAllister KA, Peery RB, Meier TI, Fischl AS, Zhao G. Biochemical and molecular analyses of the Streptococcuspneumoniae acyl carrier protein synthase, an enzyme essential forfatty acid biosynthesis. J Biol Chem. 2000 Oct 6;275(40):30864-72. PMID: 10903317","","Tue Jan 7 10:25:46 2003","1","","","" "AA00269","189473","188748","726","ATGCAGGGCAAAATTGCACTCGTGACAGGCGCAACACGCGGTATCGGTCGTGCGGTGGCGGAAGAATTGGCATCGAAAGGTGCGTTTGTGATCGGCACGGCAACTTCTGAAAAAGGCGCAGAAACGATTTCCGCCTATTTAGGTGAAAAAGGCAGAGGCTTGGTATTAAACGTTGCCGATCAAGCCTCTATCGAAGGCGTATTGGAGCGCATCAAAAAAGAATTCGGCGACATTGATATTTTAGTCAACAACGCCGGGATTACCCGTGACAATCTGTTAATGCGTATGAAAGATGAAGAATGGTTCGATATTTTACAAACCAATTTAAGCTCCGTTTATCATCTTTCCAAAGCCATGTTACGCAGCATGATGAAAAAACGCTTCGGACGTATCATCAACATCGGTTCCGTCGTAGGTTCCTCCGGTAACCCGGGGCAAAGTAACTACTGCGCGGCAAAAGCCGGTTTAGTCGGTTTTAGTAAAGCCTTGGCGAAAGAAGTGGCCTCCCGCGGGATTACCGTAAACGTTGTGGCACCGGGCTTTATCGCAACAGATATGACCGAAGTATTAAGCGAAGAATTAAAAAACAACCTGCTGACCCAAATTCCGGCGGGACGTTTGGGCAAACCGAAAGACATTGCTAAAGCCGTGGCATTTTTAGCCTCCGACGATGCGGCATACATCAACGGTATAACGTTGCACGTTAATGGCGGAATGTACATGAGC","","","25610","MQGKIALVTGATRGIGRAVAEELASKGAFVIGTATSEKGAETISAYLGEKGRGLVLNVADQASIEGVLERIKKEFGDIDILVNNAGITRDNLLMRMKDEEWFDILQTNLSSVYHLSKAMLRSMMKKRFGRIINIGSVVGSSGNPGQSNYCAAKAGLVGFSKALAKEVASRGITVNVVAPGFIATDMTEVLSEELKNNLLTQIPAGRLGKPKDIAKAVAFLASDDAAYINGITLHVNGGMYMS","188748","","3-oxoacyl-(acyl-carrier-protein) reductase/short-chain alcohol dehydrogenase","Cytoplasm","","
InterPro
IPR002198
Family
Short-chain dehydrogenase/reductase SDR
PR00080\"[76-87]T\"[129-137]T\"[149-168]TSDRFAMILY
PTHR19410\"[1-237]TSHORT-CHAIN DEHYDROGENASES/REDUCTASE FAMILY MEMBER
PF00106\"[4-168]Tadh_short
PS00061\"[136-164]TADH_SHORT
InterPro
IPR002347
Family
Glucose/ribitol dehydrogenase
PR00081\"[5-22]T\"[76-87]T\"[123-139]T\"[149-168]T\"[170-187]T\"[203-223]TGDHRDH
InterPro
IPR011284
Family
3-oxoacyl-(acyl-carrier-protein) reductase
TIGR01830\"[6-240]T3oxo_ACP_reduc: 3-oxoacyl-(acyl-carrier-pro
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[1-241]Tno description
PTHR19410:SF87\"[1-237]T3-OXOACYL-[ACYL-CARRIER-PROTEIN] REDUCTASE


","BeTs to 22 clades of COG1028COG name: Dehydrogenases with different specificities (related to short-chain alcohol dehydrogenases)Functional Class: Q,RThe phylogenetic pattern of COG1028 is ao-pkzyqvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.7e-19) to 1/1 blocks of the IPB002198 family, which is described as \"Short-chain dehydrogenase/reductase (SDR) superfamily\". Interpro entry for IP:IPR002198. IPB002198 129-164 1.6e-19","Residues 7 to 238 match (1e-07) PD:PD563725 which is described as PROTEOME DEHYDROGENASE CHAIN COMPLETE SHORT ","","","","","","","","","","","","Thu Dec 5 14:44:14 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00269 is paralogously related to AA01179 (1e-40), AA02383 (3e-21), AA01109 (4e-19), AA02205 (2e-16), AA00912 (9e-15) and AA01738 (3e-09).","","","","","","Residues 6 to 239 (E-value = 8.2e-90) place AA00269 in the adh_short family which is described as short chain dehydrogenase (PF00106)","","","","","Rawlings,M. and Cronan,J.E. Jr. The gene encoding Escherichia coli acyl carrier protein lieswithin a cluster of fatty acid biosynthetic genes J. Biol. Chem. 267 (9), 5751-5754 (1992) PubMed: 1556094 Ren Q, Sierro N, Witholt B, Kessler B. FabG, an NADPH-dependent 3-ketoacyl reductase of Pseudomonasaeruginosa, provides precursors for medium-chain-length poly-3-hydroxyalkanoate biosynthesis in Escherichia coli. J Bacteriol. 2000 May;182(10):2978-81. PMID: 10781572 ","","Thu Dec 5 14:43:48 2002","1","","","" "AA00270","190421","189501","921","ATGGTTTTCCCGGGACAAGGTTCTCAAGCTGTGGGTATGCTTGCCGAATTGGCGGTGGAATATCCTGTGGTGCAGGACACTTTCAAACAGGCATCCGAGGCGTTGGGCTATGATTTATGGCAATTGGTACAACAAGGTCCGGCAGAAGAGTTGAATAAAACCTGGCAAACCCAGCCTGCGCTTTTAGCTGCGTCCGTAGCAATTTATCGTGTGTGGCAGGAAAAATATCCGCAATTAAAACCGGAAGTCATGGCGGGACACAGTTTGGGTGAATATTCCGCGTTGGTATGTGCCGGCGTGTTGGATTTCCAGGATGCAGTTAAATTGGTGGAATTGCGCGGTAAACTCATGCAACAAGCTGTACCGGAAGGCACCGGCGCCATGTATGCCATTATCGGGCTAGATAATGAAGCGATTATTAATGCTTGTAAACAGGCGGAACAAGGGGAAGTGGTGTCTGCAGTGAACTTTAATTCACCGGGACAAGTGGTCATTGCCGGTACGAAAGCGGCGGTAGAACGTGCGGCAGCATTGTGTAAAGAAGCCGGCGCTAAGCGTGCGTTACCGTTAGCGGTGAGCGTGCCTTCCCATTGTGCATTAATGAAACCGGCGGCGGATCAATTATCCGTTTCCTTAGAAAGTATTACCTTAAAGGCACCGAGTGTTGCCGTATTAAATAATGTGGACGTGAAAGGGGAAAGCGAGGCGGAAGCCATTCGTCACGCCTTGGTTCGCCAGCTTTATAGCCCGGTGCGTTGGACTGAAACCGTGCAGAAAATGGCGGGCAACGGCGTGGAAGTGTTAGTGGAAATCGGTCCGGGCAAAGTGTTAAACGGGCTAACTAAACGTATTGTGGATTCATTGCAGGCGGTTTCGGTGAACGATGTGAAATCCCTCGATTCAATTGAAGAATTATTCGCA","","","33283","MVFPGQGSQAVGMLAELAVEYPVVQDTFKQASEALGYDLWQLVQQGPAEELNKTWQTQPALLAASVAIYRVWQEKYPQLKPEVMAGHSLGEYSALVCAGVLDFQDAVKLVELRGKLMQQAVPEGTGAMYAIIGLDNEAIINACKQAEQGEVVSAVNFNSPGQVVIAGTKAAVERAAALCKEAGAKRALPLAVSVPSHCALMKPAADQLSVSLESITLKAPSVAVLNNVDVKGESEAEAIRHALVRQLYSPVRWTETVQKMAGNGVEVLVEIGPGKVLNGLTKRIVDSLQAVSVNDVKSLDSIEELFA","189501","","malonyl coA-acyl carrier protein transacylase","Cytoplasm","","
InterPro
IPR000005
Domain
Helix-turn-helix, AraC type
PS00041\"[145-190]?HTH_ARAC_FAMILY_1
InterPro
IPR001227
Domain
Acyl transferase region
G3DSA:3.40.366.10\"[1-305]Tno description
InterPro
IPR004410
Family
Malonyl CoA-acyl carrier protein transacylase
TIGR00128\"[1-288]TfabD: malonyl CoA-acyl carrier protein tran
InterPro
IPR014043
Domain
Acyl transferase
PF00698\"[2-273]TAcyl_transf_1
noIPR
unintegrated
unintegrated
PTHR10982\"[1-305]TMALONYL COENZYME A-ACYL CARRIER PROTEIN TRANSACYLASE-RELATED
PTHR10982:SF4\"[1-305]TMALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE


","No hits to the COGs database.","Significant hit ( 2.8e-06) to 2/2 blocks of the IPB001227 family, which is described as \"Acyl transferase domain\". Interpro entry for IP:IPR001227. IPB001227A 81-93 3.7e-05 IPB001227B 275-282 37","Residues 186 to 288 match (1e-34) PD:PD338968 which is described as PHOSPHOPANTETHEINE SYNTHASE TRANSFERASE POLYKETIDE COMPLETE PROTEOME TRANSACYLASE CARRIER MALONYL I ","","","","","","","","","","","Thu Dec 5 15:18:51 2002","Wed Jan 22 16:17:42 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00270 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 307 (E-value = 7.7e-13) place AA00270 in the Acyl_transf_1 family which is described as Acyl transferase domain (PF00698)","","","","","Rawlings,M. and Cronan,J.E. Jr. The gene encoding Escherichia coli acyl carrier protein lieswithin a cluster of fatty acid biosynthetic genes J. Biol. Chem. 267 (9), 5751-5754 (1992) PubMed: 1556094 Serre,L., Verbree,E.C., Dauter,Z., Stuitje,A.R. andDerewenda,Z.S. The Escherichia coli malonyl-CoA:acyl carrier proteintransacylase at 1.5-A resolution. Crystal structure of a fatty acid synthase component J. Biol. Chem. 270 (22), 12961-12964 (1995) PubMed: 7768883 ","","Thu Dec 5 15:19:39 2002","1","","","" "AA00271","190404","190529","126","TTGTCCCGGGAAAACCATTGCAAATTTTTTCATACTTTTTTCCTACTTAAAAATGTGAGAAAAACCGACCGCACTTTAAAGTGTCAATCCGCATCAATACCTAAAAAGTGCGGTCATAAAATTCAT","","","4981","LSRENHCKFFHTFFLLKNVRKTDRTLKCQSASIPKKCGHKIH","190529","","hypothetical protein","Periplasm, Cytoplasm","No significant similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 12:35:52 2004","Sun Feb 22 12:35:52 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00271 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 12:35:52 2004","","","","","","","","","","","","","1","","","" "AA00272","191493","190546","948","ATGTTTAGCAAAATTTTATCTACCGGTAGTTATTTACCAAAAAATATTCGCACCAATGTCGATTTAGAAAAAATGGTAGATACTTCAGATGAATGGATTGTGACCCGTTCCGGTATTCGCGAACGTCGCATTGCCGATCCGAATGAAACCGTATCAACCATGGGCGTTGAAGCAGCGAAAAAAGCGATTGAAGCCGCAAACATTGACCCGCAGGAAATCGATCTTGTGTTGGTCGCTACAACCAGCAACTCTCATGCCTATCCGAGCGCTGCTTGCCAGATTCAGGGGATGCTGGAGATTGATGATGCCATTTCCTTCGACATTGCCGCCGCTTGCACCGGATTTGTGTATGCCTTAGGTGTCGCGGATCAATTTATTCGCACCGGTAAAGTAAAAAATGCGCTGGTGGTCGGTTCCGATTTAAACTCCCGCAAATTAGATGAAACGGATCGTAGCACTGTGGTGTTATTCGGTGATGGTGCCGGCGCGCTGATTTTACAGGCTTCCGAACAGGAAGGCATTATTTCCACCCATTTGCATGCCTCTGCGGACAAGCACGCCGCCTTGGTGCTGCCGCAACCGGAACGAGGTGAAGCCAAATCAGGCTATATTGAGATGCAGGGTAACGAAACCTTTAAACTTGCCGTGCGCGAGCTTTCCAATGTAGTGGAAGAAACCCTTGCCGCCAATAATTTAGATAAAAAAGATATTGATTGGTTAGTGCCTCATCAGGCAAATTTACGTATTATCACGGCGACGGCGAAAAAACTGGAAATGGATATGTCGCAAGTGGTGGTGACGCTGGATCGTTATGCCAATAACAGTGCGGCAACGGTGCCGGTGGCGCTGGATGAAGCGGTGCGTGACGGACGTATTCAACGCGGGCAGCTGCTCCTGCTGGAAGCCTTCGGCGGTGGTTGGACTTGGGGATCCGCCCTGGTTAGGTTT","","","35452","MFSKILSTGSYLPKNIRTNVDLEKMVDTSDEWIVTRSGIRERRIADPNETVSTMGVEAAKKAIEAANIDPQEIDLVLVATTSNSHAYPSAACQIQGMLEIDDAISFDIAAACTGFVYALGVADQFIRTGKVKNALVVGSDLNSRKLDETDRSTVVLFGDGAGALILQASEQEGIISTHLHASADKHAALVLPQPERGEAKSGYIEMQGNETFKLAVRELSNVVEETLAANNLDKKDIDWLVPHQANLRIITATAKKLEMDMSQVVVTLDRYANNSAATVPVALDEAVRDGRIQRGQLLLLEAFGGGWTWGSALVRF","190546","","3-oxoacyl-[acyl-carrier-protein] synthase III","Cytoplasm","","
InterPro
IPR004655
Family
Beta-ketoacyl-acyl carrier protein synthase III (FabH)
TIGR00747\"[1-316]TfabH: 3-oxoacyl-(acyl-carrier-protein) synt
InterPro
IPR013747
Domain
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C-terminal
PF08541\"[227-316]TACP_syn_III_C
InterPro
IPR013751
Domain
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III
PF08545\"[106-183]TACP_syn_III
noIPR
unintegrated
unintegrated
G3DSA:3.40.47.10\"[5-177]T\"[216-316]Tno description


","BeTs to 15 clades of COG0332COG name: 3-oxoacyl-acyl-carrier-protein synthase IIIFunctional Class: IThe phylogenetic pattern of COG0332 is -------q-drlbcefghsnujxi--Number of proteins in this genome belonging to this COG is","","Residues 112 to 316 match (9e-07) PD:PD559491 which is described as PROTEOME III COMPLETE SYNTHASE 3-OXOACYL-ACYL-CARRIER-PROTEIN ","","","","","","","","","","","","Thu Dec 5 15:12:12 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00272 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Tsay,J.T., Oh,W., Larson,T.J., Jackowski,S. and Rock,C.O.Isolation and characterization of the beta-ketoacyl-acyl carrierprotein synthase III gene (fabH) from Escherichia coli K-12. J. Biol. Chem. 267(10):6807-6814, 1992. PubMed: 1551888. Oh,W. and Larson,T.J. Physical locations of genes in the rne (ams)-rpmF-plsX-fab regionof the Escherichia coli K-12 chromosome. J. Bacteriol. 174(23):7873-7874, 1992. PubMed: 1447160. Zhang,Y. and Cronan,J.E. Jr. Transcriptional analysis of essential genes of the Escherichiacoli fatty acid biosynthesis gene cluster by functionalreplacement with the analogous Salmonella typhimurium genecluster. J. Bacteriol. 180(13):3295-3303, 1998. PubMed: 9642179.","","Thu Dec 5 15:12:12 2002","1","","","" "AA00273","192559","191543","1017","TTGAGTCGTCTAACCCTTGCGTTAGATGCGATGGGCGGGGACATAGGTCCCCGTATTACTATCCCTGCATCCATTTTAGCCTTGGAACGTGATCCAGCGCTTTTCCTCGTATTATTTGGCGATCGCCAACAAATTCTTCCGCTTTTATCCGCCGCTTCAAACACTGTTCGTCAACGTTGTGACATCATTCATTGCGCCCGCGTAATTGATAATCGCCAAGGTATTTCCTATGCGTTACGTCACAGTAAAGATACTTCAATGCGTTTAGCTATTGAAGTGGTACAAAAGGATACCGCGCAGGCTTGTGTCAGTGCCGGCGATACCGCCTCATTAATGGGGTTGTCAAAAATTTTATTACAGCCCCTTGAAGGCATTCATCGCCCCGCGCTTATCTCCGCGATTCCGACCATCACCGGTGAACGTACTATCATGCTTGATTTGGGCGCCAATCTGGAATGTGACGCGGAAAACCTATACCAGTTTGCGCTGATGGGGGCTATTTTTGCCGAGAATACGCTGGATTTGGTTTATCCTCGCATTGCGTTGTTGAATATCGGTATTGAAGCAGTGAAAGGGTATAAATCCCTGCGTGATGCCGCTGATTTACTGCAAAAAGATACCGCACTTAATTATATAGGGTTCATTGAAGGGAACTGCCTGTTAAACGGCATGGCGGATGTGATTGTCAGTGACGGTTTTGCCGGTAATATTGCCTTAAAAACCCTGGAGGGGGCGGCGAAGAATGTGATTTCCTTACTGAAAAGTGAGAAGAAAAATAGTATATTAAGCACGGTTTTCAGTTGTTTAATTCGGTCTTTATTCAAAGACAGATACCAACGACTAAAAAAAATCAACCCCGATCAATATAATGGCGCATCTTTGATTGGTTTGACTTCCGTGGTAGTAAAAAGTCACGGCAGCGCGAACCAAGAAGCTTTTGCCAATGCCATTGCCGATGCGGCGTTACAAGCCCGTCGTCAAATTCCGCAAAAAATTTTAGCGGGATTAAATAAGAAT","","","36555","LSRLTLALDAMGGDIGPRITIPASILALERDPALFLVLFGDRQQILPLLSAASNTVRQRCDIIHCARVIDNRQGISYALRHSKDTSMRLAIEVVQKDTAQACVSAGDTASLMGLSKILLQPLEGIHRPALISAIPTITGERTIMLDLGANLECDAENLYQFALMGAIFAENTLDLVYPRIALLNIGIEAVKGYKSLRDAADLLQKDTALNYIGFIEGNCLLNGMADVIVSDGFAGNIALKTLEGAAKNVISLLKSEKKNSILSTVFSCLIRSLFKDRYQRLKKINPDQYNGASLIGLTSVVVKSHGSANQEAFANAIADAALQARRQIPQKILAGLNKN","191543","","fatty acid/phospholipid synthesis protein","Inner membrane, Cytoplasm","","
InterPro
IPR003664
Family
Fatty acid synthesis plsX protein
PD006974\"[57-137]TPLSX_PASMU_P57976;
PF02504\"[4-331]TFA_synthesis
TIGR00182\"[4-339]TplsX: fatty acid/phospholipid synthesis pro
InterPro
IPR012281
Family
Phospholipid biosynthesis protein, PlsX type
PIRSF002465\"[4-339]TPhospholipid biosynthesis protein, PlsX type


","BeTs to 13 clades of COG0416COG name: Fatty acid/phospholipid biosynthesis enzymeFunctional Class: IThe phylogenetic pattern of COG0416 is -------qvd-lbcefgh-nuj-i-wNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.6e-64) to 5/5 blocks of the IPB003664 family, which is described as \"Fatty acid synthesis plsX protein\". Interpro entry for IP:IPR003664. IPB003664A 4-27 9.1e-08 IPB003664B 105-135 6.4e-09 IPB003664C 178-192 4.5e-06 IPB003664D 211-244 8.8e-19 IPB003664E 283-320 5.8e-17","Residues 27 to 145 match (7e-39) PD:PD006974 which is described as FATTY BIOSYNTHESIS SYNTHESIS ACID/PHOSPHOLIPID ACID PLSX PHOSPHOLIPID COMPLETE PROTEOME ","","","","","","","","","","","","Thu Dec 5 15:22:08 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00273 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 331 (E-value = 3.6e-112) place AA00273 in the FA_synthesis family which is described as Fatty acid synthesis protein (PF02504)","","","","","Oh,W. and Larson,T.J. 1992. Physical locations of genes in the rne (ams)-rpmF-plsX-fab regionof the Escherichia coli K-12 chromosome. J. Bacteriol. 174(23):7873-7874. PubMed: 1447160. Zhang,Y. and Cronan,J.E. Jr. Transcriptional analysis of essential genes of the Escherichiacoli fatty acid biosynthesis gene cluster by functionalreplacement with the analogous Salmonella typhimurium genecluster. J. Bacteriol. 180(13):3295-3303. PubMed: 9642179.","","Thu Dec 5 15:22:08 2002","1","","","" "AA00274","192756","192589","168","ATGGCTGTTCAACAAAATAAAAAATCCCGTTCACGTCGTGATATGCGTCGTTCTCATGATGCGTTAACCACAGCTGCAGTCTCTGTTGATAAAGCAAGTGGTGAAACTCATTTGCGTCACCATGTAACCGCTGACGGTTACTATCGTGGTCGTAAAGTGATTAACAAG","","","6375","MAVQQNKKSRSRRDMRRSHDALTTAAVSVDKASGETHLRHHVTADGYYRGRKVINK","","","50S ribosomal protein L32","Cytoplasm, Extracellular","","
InterPro
IPR002677
Family
Ribosomal L32p protein
PF01783\"[2-56]TRibosomal_L32p
TIGR01031\"[2-55]TrpmF_bact: ribosomal protein L32


","BeTs to 8 clades of COG0333COG name: Ribosomal protein L32Functional Class: JThe phylogenetic pattern of COG0333 is ------yqvd-lbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 7.9e-09) to 1/1 blocks of the IPB002677 family, which is described as \"Ribosomal L32p protein family\". Interpro entry for IP:IPR002677. IPB002677 2-18 8.9e-09","Residues 2 to 54 match (3e-10) PD:PD357045 which is described as RIBOSOMAL 50S L32 PROTEOME COMPLETE L32-1 ","Thu May 29 13:07:59 2003","","","Thu May 29 13:09:12 2003","Thu May 29 13:09:12 2003","","","Thu May 29 13:09:12 2003","Thu May 29 13:09:12 2003","Thu May 29 13:07:59 2003","Thu May 29 13:07:59 2003","Thu May 29 13:17:13 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00274 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 56 (E-value = 7.5e-26) place AA00274 in the Ribosomal_L32p family which is described as Ribosomal L32p protein family (PF01783)","","","","","","","","1","","","" "AA00275","193297","192776","522","ATGCAAAAGGTAAAGCTACCCCTAACTGTTGATCCGGTAAAAGACGCGCAACGAAGATTGGATTATCAGGGTTATTACTCCGTTAGTCAATTAAGCCGCCTTGCCGAATCGGTCAGTAAAGTGCTCAGCGATGCACAGGTTACATTATCGTTCTTTATTGATCCGCAAAAATTAGTTGTTATGCAAGGTCATGCCTGCGTTGATGTCAAGTTGACTTGTCACCGTTGTGGTGAACCGTTTACACAAACCGTTGATTGTGAATTTTGCTACAGTCCGGTAGCTAGTTTTGATCAAATTGATGTATTGCCGGAGATCTATGAGCCAATTGAATTCAATGAATTCGGTGAAATAGATTTACTCGGTGCGATTGAAGATGAACTCATTTTAAGTTTGCCGATTGTACCAATGCATTCATCTGAACACTGTGAAGTGTCCGTGGCGGAACAGGTTTTTGGCGAATTGCCGCAAGAGCTGGCGAAAAGACCGAACCCGTTCGCTGTATTAGCTAATTTAAAGCAAAAA","","","19516","MQKVKLPLTVDPVKDAQRRLDYQGYYSVSQLSRLAESVSKVLSDAQVTLSFFIDPQKLVVMQGHACVDVKLTCHRCGEPFTQTVDCEFCYSPVASFDQIDVLPEIYEPIEFNEFGEIDLLGAIEDELILSLPIVPMHSSEHCEVSVAEQVFGELPQELAKRPNPFAVLANLKQK","192776","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003772
Family
Protein of unknown function DUF177
PF02620\"[15-173]TDUF177


","BeTs to 7 clades of COG1399COG name: Predicted metal-binding, possibly nucleic acid-binding proteinFunctional Class: RThe phylogenetic pattern of COG1399 is -------qvdr-bcefghsn------Number of proteins in this genome belonging to this COG is","","Residues 7 to 172 match (1e-71) PD:PD035384 which is described as COMPLETE PROTEOME YCED G30K XF1815 NMA0545 VC2026 HI0159 YPO1594 NMB1910 ","","","","","","","","","","","","Thu Dec 5 15:23:20 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00275 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 15 to 173 (E-value = 3e-53) place AA00275 in the DUF177 family which is described as Uncharacterized ACR, COG1399 (PF02620)","","","","","","","","1","","","" "AA00276","194010","193372","639","ATGGGAAAAGTATTGTTTGTTTCAGGCATTGATACCGATATTGGCAAATCCGTTGCCACAGGTTATTACGCTAGATACTTAATGCAATTGGGGTATTCGGTAATCACTCAGAAAATGGTGCAAACAGGTTGTTGCGATATTTCATCAGATATTTTAATTCACCGCAAAATTCAAGGTGTTGAATTAGCAGATGAAGATCGCAAAGGGGAAACCTGCTGCTATTTATTTGATTATCCTTGTTCACCCTATTTAGCTGCATGTTTGCAAAATACCTATATTGATGAAAAAACGATTGAAAAATACACCGCACTCTTAGCGCAAAAATATGATTATGTTTTGCTGGAAGGAGCAGGCGGTTTGATGGTCCCTTATGCCGAGGGAAAGACAACCTTGGATTATATTACGGCACATAATTATCCGTTAATCTTGGTGACTTCCGGTAGATTGGGTAGCATTAATCATACATTGCTCAGTTTAGAAGTATGCGCGCATCAAAATATTAACGTGGATACATTGATTTATAATCTTTATCCGCCTACGGATAAATTGATTACACAAGATACGCAACAATATTTCAAAAGCTATTTAGCCAAACGCTTTCCGACGACAAAATTTATGTTGATGCAAAAAATTGATTTT","","","24048","MGKVLFVSGIDTDIGKSVATGYYARYLMQLGYSVITQKMVQTGCCDISSDILIHRKIQGVELADEDRKGETCCYLFDYPCSPYLAACLQNTYIDEKTIEKYTALLAQKYDYVLLEGAGGLMVPYAEGKTTLDYITAHNYPLILVTSGRLGSINHTLLSLEVCAHQNINVDTLIYNLYPPTDKLITQDTQQYFKSYLAKRFPTTKFMLMQKIDF","193372","","dethiobiotin synthase","Cytoplasm","","
InterPro
IPR004472
Family
Dethiobiotin synthase
PIRSF006755\"[2-213]TDethiobiotin synthetase
TIGR00347\"[6-175]TbioD: dethiobiotin synthase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[2-196]Tno description
PTHR21343\"[4-179]TDETHIOBIOTIN SYNTHETASE


","BeTs to 15 clades of COG0132COG name: Dethiobiotin synthetaseFunctional Class: HThe phylogenetic pattern of COG0132 is --m---yq--r-bcefghsnuj-i--Number of proteins in this genome belonging to this COG is","","Residues 1 to 78 match (6e-25) PD:PD583611 which is described as SYNTHETASE DETHIOBIOTIN COMPLETE PROTEOME SYNTHASE BIOSYNTHESIS LIGASE BIOTIN DTBS ATP-BINDING ","","","","","","","","","","","","Thu Dec 5 15:27:01 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00276 is paralogously related to AA02231 (1e-10).","","","","","","","","","","","Sakurai N, Akatsuka H, Kawai E, Imai Y, Komatsubara S. Complete sequence and organization of the Serratia marcescensbiotin operon. Microbiology. 1996 Nov;142 ( Pt 11):3295-303. PMID: 8969526 Bower S, Perkins JB, Yocum RR, Howitt CL, Rahaim P, Pero J. Cloning, sequencing, and characterization of the Bacillussubtilis biotin biosynthetic operon. J Bacteriol. 1996 Jul;178(14):4122-30. PMID: 8763940 ","","Thu Dec 5 15:27:01 2002","1","","","" "AA00277","194750","194013","738","ATGCAATGTTTCAATGCCGCATTAGAAACCTATGAAAAAAATGCCATTGCTCAACAACATATTGCCAATGATTTATTGAAATTATTATTGGAAAAAGGTGGAAGCCGTTTTCATCGAGTGCTGGAAATTGGTTGCGGCACAGGTAATTTTACCCGTTTATTGATGCAAAATATTGAGGCAGAGCATTGGGATTGTAATGATTTGTGCGATGTTTCCGCTCAATTAATGCAGAATCTGCCACTTCGGAACTATAATTTTTACCAAGGATGTGGCGAATCTTTGGTCTTATCTGCTCAATATGATTTGATCGTTTCCGCCTCAACCATTCAATGGTTTTCCGATCCATTGGCTTTTTTGTACCGATGTTCGACACACTTAATACCAAACAGTATGATTTTATTGAGTACATTTGCGCCGACGAATTTGCCTGAAATCAGGGCACTAAGCCAAATCGGTTTGGATTACCCTAATCTGGCACAATGGCGGGAAACATTAATGGCGAATTTTCATATTATTCACTTATCCCAAAAGGAAATTCGGCTAGAATTTGATTCCGCACTTTCAGTGCTGAGACATTTAAAAGATACCGGCGTCACAGCAACGAATAATCGAATTTGGAATCGTGAGAAAGTTGCTCGCTTTTGTGAGCAATATCATCAACATTACATCAATGAACAGGGTAAAGTTTCATTAACTTATGTGCCGATCTTCATGTTGGCACGAAAAAAAGAGAATGCA","","","29640","MQCFNAALETYEKNAIAQQHIANDLLKLLLEKGGSRFHRVLEIGCGTGNFTRLLMQNIEAEHWDCNDLCDVSAQLMQNLPLRNYNFYQGCGESLVLSAQYDLIVSASTIQWFSDPLAFLYRCSTHLIPNSMILLSTFAPTNLPEIRALSQIGLDYPNLAQWRETLMANFHIIHLSQKEIRLEFDSALSVLRHLKDTGVTATNNRIWNREKVARFCEQYHQHYINEQGKVSLTYVPIFMLARKKENA","194013","","biotin synthesis protein","Cytoplasm","","
InterPro
IPR011814
Family
Biotin biosynthesis protein BioC
TIGR02072\"[3-242]TBioC: biotin biosynthesis protein BioC
InterPro
IPR013216
Domain
Methyltransferase type 11
PF08241\"[41-134]TMethyltransf_11
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[39-150]Tno description
PTHR10108\"[38-168]TMETHYLTRANSFERASE
PTHR10108:SF26\"[38-168]TMETHLYTRANSFERASE, UBIE/COQ5 FAMILY


","BeTs to 18 clades of COG0500COG name: SAM-dependent methyltransferasesFunctional Class: Q,RThe phylogenetic pattern of COG0500 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 2 to 80 match (4e-13) PD:PD407453 which is described as PROTEOME COMPLETE BIOTIN SYNTHESIS BIOC BIOC NMA2011 TRANSFERASE METHYLTRANSFERASE BIOSYNTHESIS ","","","","","","","","","","","","Thu Dec 5 15:29:01 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00277 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Secondary Laboratory Evidence:Sakurai N, Akatsuka H, Kawai E, Imai Y, Komatsubara S. Complete sequence and organization of the Serratia marcescensbiotin operon. Microbiology. 1996 Nov;142 ( Pt 11):3295-303. PMID: 8969526 Bower S, Perkins JB, Yocum RR, Howitt CL, Rahaim P, Pero J.Cloning, sequencing, and characterization of the Bacillussubtilis biotin biosynthetic operon. J Bacteriol. 1996 Jul;178(14):4122-30. PMID: 8763940","","Thu Dec 5 15:29:01 2002","1","","","" "AA00278","195418","194771","648","ATGCAATATCAATTAATTAACGTAAACCTGACACGTCGGCATTTAATCGTGTATTTCACCGGATGGGGTATGACACCATTGGTCATCCAACATTTAACATTACCGAAAGAACATGATTTGCTGGTTTGTTATGACTATCGGGATTTATCGCTTAATTTTGATTTTTCCTGTTATGAAAGTGTACGCTTAGTAGCATGGTCTATGGGTGTTTGGGTGGCTGAACATGTGATGGGGCAAACACCATTACTTTCCGCCACTGCAATTAATGGCACGGGGCTCCCTATGCACAATGAATATGGCATCCCTTGTGCCGTATTTAAAGGCACTTTGGAAGCTTTTGATGAGGTCAATCAACATAAATTTGAACGCCGAATGTGTGGTGACAAAAGTACATTACTACAATATCAATCGCTGGAAGGGCAGCGTTCAATTGAAGAAACACATGCCGAATTGACCGCACTTTATGAAGCATTGTTGACAAACCGGCAAAATGTCCCTCTGCACTGGACGAAAGCCATTATTGGCACGCAAGATCGTATTTTTCCTGTGCAGAATCAGCGTAATTACTGGCATTCTCGTTGTACGATGGTTGAAATGCTGGGTGGGCATTATTTGTTCCCATTACTACAAACATGGGCGCAATTATGG","","","25107","MQYQLINVNLTRRHLIVYFTGWGMTPLVIQHLTLPKEHDLLVCYDYRDLSLNFDFSCYESVRLVAWSMGVWVAEHVMGQTPLLSATAINGTGLPMHNEYGIPCAVFKGTLEAFDEVNQHKFERRMCGDKSTLLQYQSLEGQRSIEETHAELTALYEALLTNRQNVPLHWTKAIIGTQDRIFPVQNQRNYWHSRCTMVEMLGGHYLFPLLQTWAQLW","194771","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR007398
Family
Protein of unknown function DUF452
PF04301\"[1-215]TDUF452
noIPR
unintegrated
unintegrated
PD112097\"[14-212]TQ9CJT9_PASMU_Q9CJT9;
tmhmm\"[15-33]?transmembrane_regions


","BeTs to 4 clades of COG2830COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG2830 is -----------------h-nu-----Number of proteins in this genome belonging to this COG is","","Residues 14 to 212 match (4e-56) PD:PD112097 which is described as COMPLETE PROTEOME NMB0473 CJ0305C HI1552 NMA2012 PM1902 ","","","","","","","","","","","","Thu Dec 5 15:30:19 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00278 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 215 (E-value = 1.8e-97) place AA00278 in the DUF452 family which is described as Protein of unknown function (DUF452) (PF04301)","","","","","","","","1","","","" "AA00279","196574","195402","1173","ATGAATAGGTCGGATTATTTTTCCACACAACTGGACATATTACGGCAAAAAGATCAATATCGCCGTTTCCCGCAAATTCACCATAACGGTAAGTTTGTTGAGCAAAATGGACATCAGATGCTCAATTTGGCTTCTAATGATTATCTGGGGTTAGCCGGTGATGTATCGTTACAACAAGCTTTTCTTAAAAAATACATTGAAAAACTACCGCACTTTACCTCCTCTTCGTCGCGCTTGCTAACCGGCAATTTCCCCGAATATGAAGCCCTTGAACAATTAATGGCAAATGCGTTTCGGCGGGAGGCATGTTTGCTGTTTAATAGCGGTTATCACGCCAATATTGGTATTTTACCGGCAGTAGCCAATAAACAAACCTTGATCGTCGCTGACAAATTGGTACATGCCAGCATTATTGATGGTATTCGCCTGAGCAATTCCCCGTTTTTGCGGTATCGTCATAACGATTACGATCACTTGTATAACATTTTACACAAACAGTATCTTCATTATGAACGCATTATTGTGGTGACGGAAAGTGTGTTCAGTATGGATGGGGATCTCGCAGACTTATCACAATTGGTTGCATTTAAAAAGCAATTTGACAATGTTATGTTGTATGTGGATGAAGCACATGGCATTGGTGTTTATGGCGAACGGGGTCTGGGTGTTGCCGAACAGACAAATTGCCTACCTGACATTGATTTTTTGGTAGGGACTTTTGGTAAAGCGTTTGCTTCCATGGGCGCTTATGTGGTTTGTGATCGAGTCATTAAAGATTATTTAATTAACACTATGCGCCCTTTGATCTTCAGCACAGCGTTACCGCCATTCAATGTGGCATGGACCACATTTCTCTTCGAAAAACAACCGCACTTTCAGGCTAAACGACAACATCTCATGCAATTAAGTGCGCGATTACGGCAGGTTCTCGCAGAGCAATTCAATATGCCAATGCCAAGTGAAAGCCATATAGTACCTTATATTTTAGGCGAAAATCAGCGCACTATAAAAATAGCGCACCGCCTTCAACAATGTGGATATTATTGCTTACCTATTCGGCCGCCTACCGTTCCTGTCGGAACATCTCGCATTCGTTTGTCTTTAACAGCCGATATGACCCATGATGAAATTGAACAATTTATAGAACAGTTATTTTATGCAATATCAATTAAT","","","44848","MNRSDYFSTQLDILRQKDQYRRFPQIHHNGKFVEQNGHQMLNLASNDYLGLAGDVSLQQAFLKKYIEKLPHFTSSSSRLLTGNFPEYEALEQLMANAFRREACLLFNSGYHANIGILPAVANKQTLIVADKLVHASIIDGIRLSNSPFLRYRHNDYDHLYNILHKQYLHYERIIVVTESVFSMDGDLADLSQLVAFKKQFDNVMLYVDEAHGIGVYGERGLGVAEQTNCLPDIDFLVGTFGKAFASMGAYVVCDRVIKDYLINTMRPLIFSTALPPFNVAWTTFLFEKQPHFQAKRQHLMQLSARLRQVLAEQFNMPMPSESHIVPYILGENQRTIKIAHRLQQCGYYCLPIRPPTVPVGTSRIRLSLTADMTHDEIEQFIEQLFYAISIN","195402","","8-amino-7-oxonoanoate synthase","Cytoplasm","","
InterPro
IPR001917
Binding_site
Aminotransferase, class-II
PS00599\"[239-248]?AA_TRANSFER_CLASS_2
InterPro
IPR004839
Domain
Aminotransferase, class I and II
PF00155\"[38-384]TAminotran_1_2
InterPro
IPR015421
Domain
Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10\"[72-287]Tno description
noIPR
unintegrated
unintegrated
PTHR13693\"[28-390]TCLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE
PTHR13693:SF4\"[28-390]T8-AMINO-7-OXONONANOATE SYNTHASE


","BeTs to 19 clades of COG0156COG name: 7-keto-8-aminopelargonate synthetase and related enzymesFunctional Class: HThe phylogenetic pattern of COG0156 is --mpk-yq-dr-bcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-28) to 6/7 blocks of the IPB003408 family, which is described as \"Aminolevulinic acid synthase domain\". Interpro entry for IP:IPR003408. IPB003408A 1-31 0.22 IPB003408C 109-163 4.1e-07 IPB003408D 184-225 0.055 IPB003408E 242-287 7.3e-05 IPB003408F 296-332 0.0073 IPB003408G 338-372 0.19Significant hit ( 6.6e-13) to 3/3 blocks of the IPB001917 family, which is described as \"Aminotransferases class-II\". Interpro entry for IP:IPR001917. IPB001917A 71-82 1.8e+02 IPB001917B 129-140 0.0007 IPB001917C 203-217 7.9e-07","Residues 73 to 154 match (7e-07) PD:PD587846 which is described as TRANSFERASE WCBT F43H9.2B ACYL-COA ","","","","","","","","","","","","Thu Dec 5 15:31:48 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00279 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 78 to 385 (E-value = 4.1e-44) place AA00279 in the Aminotran_1_2 family which is described as Aminotransferase class I and II (PF00155)","","","","","Sakurai N, Akatsuka H, Kawai E, Imai Y, Komatsubara S. Complete sequence and organization of the Serratia marcescensbiotin operon. Microbiology. 1996 Nov;142 ( Pt 11):3295-303. PMID: 8969526 Bower S, Perkins JB, Yocum RR, Howitt CL, Rahaim P, Pero J.Cloning, sequencing, and characterization of the Bacillussubtilis biotin biosynthetic operon. J Bacteriol. 1996 Jul;178(14):4122-30. PMID: 8763940","","Thu Dec 5 15:31:48 2002","1","","","" "AA00280","197856","196570","1287","ATGAATCAACAACAGCTATTAAAATTTGATCGTGAACATATTTGGCATCCCTATGCAGCACTTCCACCAACTACACCGATTTATGCAGTAGAACGCGCAGAGGGCGTAATGATTATGCTTAAAGATGGACGTCAGCTGATTGACGGAATGTCGTCTTGGTGGGCAGCGTTACATGGTTATAATCACCCTCGTCTGAATGCAGCGGCAAATAAACAGTTGGCGCAAATGAGCCACATTATGTTCGGTGGGTTAACTCACGAACCGGCTATTAAACTGACACAAAAATTGTTACCTTTATTACCTTCGGGATTAGAACAAATCTTTTTTGCCGATAGTGGTTCCATTGCCGTTGAAGTGGCGATGAAGATGGCTATTCAGTATCAACATGCAAAAGGTGAAACTCAGCGATATAAATTTGCAACCATTCGTTCAGGTTATCATGGTGATACTTGGCATGCCATGTCGGTATGCGATCCGGTGACGGGGATGCATAGCCTGTTTGCCAAAAGTTTGCCGGTGCAGTATTTCCTTCCACAGCCTCAAACTTCTTTTGGGCAACCATGGTGTGAAGAAGATATTGCACCATTGGCGGATTTATTGGAAAAACGAGGTGCAGAATTAGCCGCACTTATTCTTGAACCGGTAGTGCAGGGGGCAGGAGGAATGTATTTTTATTCGCCAATGTATTTAGTCCGGGCCCAACAACTTTGTCAACAATACGGCGTATTGCTAATTTTTGATGAGATTGCTACCGGTTTTGGTCGCACAGGAAAATTATTTGCGGCAGAATATGCCGACATTTCACCTGACATTATGTGTATCGGTAAGGCGTTAACCGGCGGTTATTTAACGCTGTCGGCAACCATTACAACCCGTGTTATTGCGCAAACTATTTGTCGTGGTGAAGCACAATGTTTTATGCATGGACCGACGTTTATGGCAAATCCATTAGCTTGTGCCATTGCTACAGCATCAATTGATTTATTGCTGGAAAACGATTGGCAGGGCAATGTAAAACGTATTGAACAACAACTGAAAGCCGAATTGCAGATTGCGGAAAATTTTAATGCGGTGAAAGCTGTACGGGTACTGGGTGCTATTGGTGTTTTGGAAATGTATGAACCGGTCAATTTAACCTCATTGCAGGTGCGTTTAGTGGCACATGGCGTCTGGGTTCGCCCGTTTGGCAGATTAGTGTACTTAATGCCACCTTTTATTATCAGTCCGTCACAATTATCTGCATTAACTTCCGGTATGTTGGCGGCAATCAGAGAGGAATACTATGAA","","","47531","MNQQQLLKFDREHIWHPYAALPPTTPIYAVERAEGVMIMLKDGRQLIDGMSSWWAALHGYNHPRLNAAANKQLAQMSHIMFGGLTHEPAIKLTQKLLPLLPSGLEQIFFADSGSIAVEVAMKMAIQYQHAKGETQRYKFATIRSGYHGDTWHAMSVCDPVTGMHSLFAKSLPVQYFLPQPQTSFGQPWCEEDIAPLADLLEKRGAELAALILEPVVQGAGGMYFYSPMYLVRAQQLCQQYGVLLIFDEIATGFGRTGKLFAAEYADISPDIMCIGKALTGGYLTLSATITTRVIAQTICRGEAQCFMHGPTFMANPLACAIATASIDLLLENDWQGNVKRIEQQLKAELQIAENFNAVKAVRVLGAIGVLEMYEPVNLTSLQVRLVAHGVWVRPFGRLVYLMPPFIISPSQLSALTSGMLAAIREEYYE","196570","","adenosylmethionine-8-amino-7-oxononanoate; 7,8-diamino-perlargonic acid ATase","Inner membrane, Cytoplasm","","
InterPro
IPR005814
Family
Aminotransferase class-III
PTHR11986\"[16-429]TAMINOTRANSFERASE CLASS III
PF00202\"[29-374]TAminotran_3
PS00600\"[244-281]TAA_TRANSFER_CLASS_3
InterPro
IPR005815
Family
Adenosylmethionine--8-amino-7-oxononanoate aminotransferase
PTHR11986:SF8\"[16-429]TADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE
TIGR00508\"[1-426]TbioA: adenosylmethionine-8-amino-7-oxononan
InterPro
IPR015421
Domain
Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10\"[62-332]Tno description


","BeTs to 15 clades of COG0161COG name: Adenosylmethionine-8-amino-7-oxononanoate aminotransferaseFunctional Class: HThe phylogenetic pattern of COG0161 is --m---yq-dr-b-efghsnuj-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.3e-52) to 4/4 blocks of the IPB000954 family, which is described as \"Aminotransferase class-III pyridoxal-phosphate\". Interpro entry for IP:IPR000954. IPB000954A 40-69 2.8e-11 IPB000954B 218-257 4.3e-22 IPB000954C 266-281 1.1e-06 IPB000954D 308-326 3.2e-08","Residues 157 to 211 match (4e-07) PD:PD594221 which is described as AMINOTRANSFERASE PHOSPHATE ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE BIOTIN ACID 78-DIAMINO-PELARGONIC TRANSFERASE DAPA BIOA PYRIDOXAL ","","","","","","","","","","","","Thu Jan 23 09:26:43 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00280 is paralogously related to AA02425 (3e-23).","","","","","","Residues 17 to 427 (E-value = 8.4e-161) place AA00280 in the Aminotran_3 family which is described as Aminotransferase class-III (PF00202)","","","","","Sakurai N, Akatsuka H, Kawai E, Imai Y, Komatsubara S. Complete sequence and organization of the Serratia marcescensbiotin operon. Microbiology. 1996 Nov;142 ( Pt 11):3295-303. PMID: 8969526 Bower S, Perkins JB, Yocum RR, Howitt CL, Rahaim P, Pero J.Cloning, sequencing, and characterization of the Bacillussubtilis biotin biosynthetic operon. J Bacteriol. 1996 Jul;178(14):4122-30. PMID: 8763940","","Thu Dec 5 15:33:09 2002","1","","","" "AA00281","198079","198945","867","ATGAACAAATCCACTTATTGGCAGCGCCTGAAAGTTGCCTTTCAATATGTTATGCCACAACTGTATTTAACCCAATTGGCGGGCTGGTTCGCCAAGCAAAAATGGGGCGCAGTCACTCATTTCGTAATTAAACTCTTCGCCAAGAAATACAATGTGGACATGAGCGAAGCGAAAAAAGAAAACTTCAGCGACTACGAAAATTTCAACCAATTTTTTATTCGCGAATTAAAAGACGGTGCCCGAAAAATAAATGAAAATCCTACCGCACTTTGCTTGCCGGCAGATGGTCGTGTGAGCCAAATCGGGCATATTGACGACGAATTATTATTGCAAGCCAAAGGGCATTTTTTCAGCTTGTCCGATTTATTGGCGGGCGATGAGGAATTGGTCAACACCTTTAAAAACGGCGAATTCGCCACCATCTATTTATCTCCTCGCGATTACCACCGCGTGCATATGCCGTGCGATGCCACCCTGCGCAAAATGATTTATGTGCCCGGCGCCTTGTTCTCGGTGAACCCGTTCCTGGCGGAACACGTGTCTAACTTATTTGCCCGTAATGAACGGGTGATTTGCCTGTTTGATACCGAATTCGGCCCTATGGTGCAGATTCTGGTGGGCGCCACGATCACCGCCAGCATGAGCACCGTTTGGGCGGGCGTGATTAATCCGCCGCGCGCCGATGAAGTGAAAGTCTGGACGTATCAAGAGGAAAATGCGGTAAAATTGACCAAAGGTCAGGAAATGGGCGCATTTCAGTTAGGTTCTACGGTCATCAACCTTTTCCCGGCTAATCGCGTGACCTTAACAGAACATTTGCAGGTGGACGAACCCGTCAGAGTGGGTGAAATATTAGCCACGATCAAT","","","32807","MNKSTYWQRLKVAFQYVMPQLYLTQLAGWFAKQKWGAVTHFVIKLFAKKYNVDMSEAKKENFSDYENFNQFFIRELKDGARKINENPTALCLPADGRVSQIGHIDDELLLQAKGHFFSLSDLLAGDEELVNTFKNGEFATIYLSPRDYHRVHMPCDATLRKMIYVPGALFSVNPFLAEHVSNLFARNERVICLFDTEFGPMVQILVGATITASMSTVWAGVINPPRADEVKVWTYQEENAVKLTKGQEMGAFQLGSTVINLFPANRVTLTEHLQVDEPVRVGEILATIN","198945","","phosphatidylserine decarboxylase proenzyme","Cytoplasm","","
InterPro
IPR001005
Domain
SANT, DNA-binding
PS00037\"[233-241]?MYB_1
InterPro
IPR003817
Family
Phosphatidylserine decarboxylase-related
PF02666\"[68-287]TPS_Dcarbxylase
InterPro
IPR005221
Family
Phosphatidylserine decarboxylase
PTHR10067\"[28-288]TPHOSPHATIDYLSERINE DECARBOXYLASE
TIGR00163\"[54-289]TPS_decarb: phosphatidylserine decarboxylase


","BeTs to 12 clades of COG0688COG name: Phosphatidylserine decarboxylaseFunctional Class: IThe phylogenetic pattern of COG0688 is aom---y--dr-b-efghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.3e-41) to 5/5 blocks of the IPB003817 family, which is described as \"Phosphatidylserine decarboxylase\". Interpro entry for IP:IPR003817. IPB003817A 65-79 0.00018 IPB003817B 90-98 0.31 IPB003817C 142-154 1.3e-08 IPB003817D 164-190 1.9e-13 IPB003817E 246-262 2.7e-07","","","","","","","","","","","","","Thu Dec 5 15:34:53 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00281 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 68 to 287 (E-value = 1.8e-98) place AA00281 in the PS_Dcarbxylase family which is described as Phosphatidylserine decarboxylase (PF02666)","","","","","Li,Q.X. and Dowhan,W. Structural characterization of Escherichia coliphosphatidylserine decarboxylase The Journal of biological chemistry. 263 (23), 11516-11522 (1988)PubMed: 3042771 Li,Q.X. and Dowhan,W. Studies on the mechanism of formation of the pyruvate prosthetic group of phosphatidylserine decarboxylase from Escherichia coli The Journal of biological chemistry. 265 (7), 4111-4115 (1990) PubMed: 2406271 Dowhan,W. and Li,Q.X. Phosphatidylserine decarboxylase from Escherichia coli Methods in enzymology. 209, 348-359 (1992) PubMed: 1495415 ","","Thu Dec 5 15:34:53 2002","1","","","" "AA00282","198974","199603","630","ATGACGGCAGCGTTTTTTAATCAAGTGAAATTGGACGATACACAAGCCAAAGGCAGCTACGGTATCGGCTTGCAAATCGGTCAGCAATTATTGGACAGCCAATTAGCGGTAAAAACGGAAGCCGTGGCAAAAGGAATTTACGATGTGTTAAATCAACACGCGCCGGTATTGGATTTCAACGAAATCAGCCAAGCGCTGCAACAATTACAACAACAAGCGGCAGAAGCACAACAGGCGCAATTCAAAGAAATTGAAGCGGCTGGCAAAGCCTTCTTGGAAGCCAATAAACAAAAAGACGGTGTGAAAATGACCGATTCCGGTTTGCAATATGAAGTGCTGATTGAAGGCGACGGCAAAGTGCCTTCCGCCACGGACAAAGTCAGCGTACACTACACCGGCACGCTACCGGACGGCACCGTATTCGACAGCTCCGTAACACGCGGTCAACCGGCGGAGTTCCCGGTTAACGGCGTGATTAAAGGTTGGGTCGAAGCCCTCTCCATGATGCCGGTCGGTTCCAAATGGCGTTTGGCGATTCCGCATGAATTGGCTTACGGCGAACGTGGTGCTGGCGCAGCCATTCCGCCATTCAGCCCGTTAGTGTTTGAAGTGGAATTATTGGATATTCTA","","","22589","MTAAFFNQVKLDDTQAKGSYGIGLQIGQQLLDSQLAVKTEAVAKGIYDVLNQHAPVLDFNEISQALQQLQQQAAEAQQAQFKEIEAAGKAFLEANKQKDGVKMTDSGLQYEVLIEGDGKVPSATDKVSVHYTGTLPDGTVFDSSVTRGQPAEFPVNGVIKGWVEALSMMPVGSKWRLAIPHELAYGERGAGAAIPPFSPLVFEVELLDIL","199603","","peptidyl-prolyl cis-trans isomerase; macrophage infectivity potentiator","Outer membrane, Periplasm","","
InterPro
IPR000774
Domain
Peptidyl-prolyl cis-trans isomerase, FKBP-type, N-terminal
PD001516\"[88-122]TQ765B0_BBBBB_Q765B0;
PF01346\"[2-112]TFKBP_N
InterPro
IPR001179
Domain
Peptidyl-prolyl cis-trans isomerase, FKBP-type
PTHR10516\"[111-209]TFK506 BINDING PROTEIN
PF00254\"[116-207]TFKBP_C
PS50059\"[124-210]TFKBP_PPIASE
noIPR
unintegrated
unintegrated
G3DSA:3.10.50.40\"[70-209]Tno description
PTHR10516:SF17\"[111-209]TFKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE


","BeTs to 11 clades of COG0545COG name: FKBP-type peptidyl-prolyl cis-trans isomerases 1Functional Class: OThe phylogenetic pattern of COG0545 is ------y--d---cefghsn-j-it-Number of proteins in this genome belonging to this COG is","Significant hit ( 9.3e-70) to 4/4 blocks of the IPB000774 family, which is described as \"Domain amino terminal to FKBP-type peptidyl-prolyl isomerase\". Interpro entry for IP:IPR000774. IPB000774A 78-118 3.2e-20 IPB000774B 129-156 3.8e-20 IPB000774C 157-186 6.6e-19 IPB000774D 194-209 1.8e-06Significant hit ( 1.4e-13) to 1/1 blocks of the IPB001179 family, which is described as \"FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase)\". Interpro entry for IP:IPR001179. IPB001179 153-186 1.4e-13","Residues 101 to 151 match (3e-07) PD:PD407729 which is described as INFECTIVITY MACROPHAGE POTENTIATOR ISOMERASE ROTAMASE CIS-TRANS MEMBRANE PEPTIDYL-PROLYL OUTER MIP ","","","","","","","","","","","","Thu Jan 23 08:55:07 2003","","","Tue Mar 2 14:01:53 2004","","yes","Fri Feb 20 15:41:32 MST 1998","AA00282 is paralogously related to AA01517 (2e-38).","Tue Mar 2 14:01:53 2004","","","","","Residues 116 to 207 (E-value = 2.2e-44) place AA00282 in the FKBP_C family which is described as FKBP-type peptidyl-prolyl cis-trans isomerase (PF00254)","Tue Mar 2 14:01:53 2004","","","","","","","1","","","" "AA00283","200075","199674","402","ATGATGCGGTGGCGACGGCGGAAATTAAAGTGGGATAACGATAATTTATCAGCGCTGGTGGCGATTTTGGTGCAGGCGGATCGTTTGGAAAACCGTAAACAATGGCTGTTCACCGCGCCGTCGGCAGGCGTACTGACCATTGATGAAGGCGCACAAAGTGCGGTGTTAATTCAGCATAAATCTTTACTGCAGGCAGGCATTGTGAGTGTCAGCGGGCGTTTCTCACGCGGTGAAGTGGTGCGCATTCGGAATGCACAAGGCAAGGACATTGCCCTCGGCATGCCGCGCTATAACAGCGATGCGCTGGAACTGATTAAAGGCAAACAATCGCAGGATATTGAACAACAGCTGGGCTATGAGTACGGCGCGGTGGCTATTCATCGGGACGATATGATCGTGTTA","","","15072","MMRWRRRKLKWDNDNLSALVAILVQADRLENRKQWLFTAPSAGVLTIDEGAQSAVLIQHKSLLQAGIVSVSGRFSRGEVVRIRNAQGKDIALGMPRYNSDALELIKGKQSQDIEQQLGYEYGAVAIHRDDMIVL","199674","","glutamate 5-kinase (gamma-glutamyl kinase)","Cytoplasm, Periplasm","","
InterPro
IPR002478
Domain
PUA
PF01472\"[43-117]TPUA
SM00359\"[43-126]TPUA
PS50890\"[42-120]TPUA


","BeTs to 14 clades of COG0263COG name: Glutamate 5-kinaseFunctional Class: EThe phylogenetic pattern of COG0263 is ------yqvdrlbcefghsnuj--t-Number of proteins in this genome belonging to this COG is","","Residues 26 to 132 match (4e-07) PD:PD489889 which is described as KINASE BIOSYNTHESIS PROTEOME GLUTAMATE GK COMPLETE PROLINE GAMMA-GLUTAMYL 5-KINASE TRANSFERASE ","","","","","","","","","","","","Thu Dec 5 15:52:41 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00283 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 43 to 117 (E-value = 8.1e-21) place AA00283 in the PUA family which is described as PUA domain (PF01472)","","","","","Deutch,A.H., Rushlow,K.E. and Smith,C.J.Analysis of the Escherichia coli proBA locus by DNA and proteinsequencingNucleic Acids Res. 12 (15), 6337-6355 (1984)PubMed: 6089111Sleator RD, Gahan CG, Hill C.Mutations in the listerial proB gene leading to proline overproduction: effects on salttolerance and murine infection.Appl Environ Microbiol. 2001 Oct;67(10):4560-5.PMID: 11571156 Sleator RD, Gahan CG, Hill C.Identification and disruption of the proBA locus in Listeria monocytogenes: role of prolinebiosynthesis in salt tolerance and murine infection.Appl Environ Microbiol. 2001 Jun;67(6):2571-7.PMID: 11375165 Massarelli I, Forlani G, Ricca E, De Felice M.Enhanced and feedback-resistant gamma-glutamyl kinase activity of an Escherichia coli transformant carrying a mutated proB gene of Streptococcus thermophilus.FEMS Microbiol Lett. 2000 Jan 1;182(1):143-7.PMID: 10612746 ","","Mon Feb 17 11:07:45 2003","1","","","" "AA00286","200320","200105","216","GTGCCATTGCCGCCGGTCGCCATTAATTATTTAAATCACCCGCAATTGCCGCCCACCGTGGCGTCCAAACAATTGCTGGCGGCGGAGGAGCAGAGCCAGCTGATTCAAACCTGGGAAAAACTGTTTGCCATTTATGATATTCGCATCGGGCAAATGTTGCTGACCCGCGCCGATATTGAAGATCGCGAACGTTTCCTGAATGCACGCGTTGCTGGA","","","8165","VPLPPVAINYLNHPQLPPTVASKQLLAAEEQSQLIQTWEKLFAIYDIRIGQMLLTRADIEDRERFLNARVAG","200105","","glutamate 5-kinase (gamma-glutamyl kinase)","Cytoplasm","","No hits reported.","BeTs to 14 clades of COG0263COG name: Glutamate 5-kinaseFunctional Class: EThe phylogenetic pattern of COG0263 is ------yqvdrlbcefghsnuj--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.5e-13) to 1/4 blocks of the IPB001057 family, which is described as \"Glutamate 5-kinase\". Interpro entry for IP:IPR001057. IPB001057B 24-59 1.4e-13","Residues 9 to 69 match (1e-24) PD:PD102733 which is described as KINASE GLUTAMATE GAMMA-GLUTAMYL 5-KINASE TRANSFERASE PROTEOME COMPLETE GK BIOSYNTHESIS PROLINE ","","","","","","","","","","","","Thu Dec 5 15:58:01 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00286 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Deutch,A.H., Rushlow,K.E. and Smith,C.J. Analysis of the Escherichia coli proBA locus by DNA and protein sequencing Nucleic Acids Res. 12 (15), 6337-6355 (1984) PubMed: 6089111Sleator RD, Gahan CG, Hill C. Mutations in the listerial proB gene leading to proline overproduction: effects on salt tolerance and murine infection. Appl Environ Microbiol. 2001 Oct;67(10):4560-5. PMID: 11571156 Sleator RD, Gahan CG, Hill C. Identification and disruption of the proBA locus in Listeriamonocytogenes: role of proline biosynthesis in salt tolerance and murine infection. Appl Environ Microbiol. 2001 Jun;67(6):2571-7. PMID: 11375165 Massarelli I, Forlani G, Ricca E, De Felice M. Enhanced and feedback-resistant gamma-glutamyl kinase activity of an Escherichia coli transformant carrying a mutated proB gene ofStreptococcus thermophilus. FEMS Microbiol Lett. 2000 Jan 1;182(1):143-7. PMID: 10612746 ","","Mon Feb 17 11:11:20 2003","1","","","" "AA00287","200567","200298","270","ATGCTTAATAGAATAAGCACTAAAGTGCGGTGGGATTTTTGGATAAATTTCAGGATTTATGCTAGGTTAAGTGCATTTTTGAGAGAAGTCAGTATGCAACAGAATAATAAAACCATTGTGGTGAAATTCGGCACCAGCACGCTCACGCAGGGCTCGCCGAAATTGAATTTAGCCTACATGATGGAAATTGTTCGTCAGTTGGCACAATTACATCAGGCAGGTTTTCGCCTGGTGATCGTGACCTCGGGTGCCATTGCCGCCGGTCGCCAT","","","10294","MLNRISTKVRWDFWINFRIYARLSAFLREVSMQQNNKTIVVKFGTSTLTQGSPKLNLAYMMEIVRQLAQLHQAGFRLVIVTSGAIAAGRH","200298","","glutamate 5-kinase (gamma-glutamyl kinase)","Cytoplasm, Inner membrane","","
InterPro
IPR001048
Domain
Aspartate/glutamate/uridylate kinase
PF00696\"[37-89]TAA_kinase


","BeTs to 15 clades of COG0263COG name: Glutamate 5-kinaseFunctional Class: EThe phylogenetic pattern of COG0263 is ------yqvdrlbcefghsnuj--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 3e-12) to 1/4 blocks of the IPB001057 family, which is described as \"Glutamate 5-kinase\". Interpro entry for IP:IPR001057. IPB001057A 60-85 3e-12","Residues 65 to 90 match (1e-07) PD:PD102733 which is described as KINASE GLUTAMATE GAMMA-GLUTAMYL 5-KINASE TRANSFERASE PROTEOME COMPLETE GK BIOSYNTHESIS PROLINE ","","","","","","","","","","","","Thu Dec 5 16:04:00 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00287 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Deutch,A.H., Rushlow,K.E. and Smith,C.J. Analysis of the Escherichia coli proBA locus by DNA and protein sequencing Nucleic Acids Res. 12 (15), 6337-6355 (1984) PubMed: 6089111Sleator RD, Gahan CG, Hill C. Mutations in the listerial proB gene leading to proline overproduction: effects on salt tolerance and murine infection. Appl Environ Microbiol. 2001 Oct;67(10):4560-5. PMID: 11571156 Sleator RD, Gahan CG, Hill C. Identification and disruption of the proBA locus in Listeriamonocytogenes: role of proline biosynthesis in salt tolerance and murine infection. Appl Environ Microbiol. 2001 Jun;67(6):2571-7. PMID: 11375165 Massarelli I, Forlani G, Ricca E, De Felice M. Enhanced and feedback-resistant gamma-glutamyl kinase activity of an Escherichia coli transformant carrying a mutated proB gene ofStreptococcus thermophilus. FEMS Microbiol Lett. 2000 Jan 1;182(1):143-7. PMID: 10612746 ","","Mon Feb 17 11:11:46 2003","1","","","" "AA00288","200625","201407","783","ATGGAAAGAGAAAACATCACACCCGACTATCAACGGGAAGTCACGCGATTATGCGTGCAAACGGCGCTGTTATTACTACAACATGGCGCGGAAAGCACCGTCGTGTCGCAAATGGCGCAACGGCTCGGTTTTGCACTGGGGGTAAAAAGTGTAGAATGCGCCCTCACCGCCAACGCCGTGGTTATCACCACCTTGGCTAACAACCATTGCATCACCACCGCCCGTAAAAGCACCGACAAGGGCATTAATATGCAAATGGTCACCGACGTGCAACGCATTGTCATCTCTGCCGAACATAAAATCTACGACATTCAGCTGGTCAGGAAAAAACTCTCGCAACCCAAGCCGCTAAAATATAACCGCTATTTTGTGGTCTTGATGATCGGCTTATCCTGCGCCTCTTTTGCCCATTTATCCGGCGGCAATGCGCTGATTTCGCTCATCACCTTTTTAGCCGCCTCCGTCGCCATGTTCGTGCGGCAGGAATTGTCCAAACGGCACTACAACCCGGTCATTGTGTTTGCCGTCACCGCTTTCGTCGCCTCGCTCATCGCCGGCATCAGTCTGAAATATCAGCTCGGCAACGACCCACAAATCGCCTTGGCGTCCAGCGTATTATTGCTGGTGCCTGGCTTTCCGTTAATCAATTCTTTGGCGGATATTCTGAAAGGCTATGTGAACATGGGAATCGGGCGTTGGGCGATCGCTACCATTCTCACTTTCGGCGCTTGTCTCGGCATTGTCTTCGCCTTGAGCGTACTCAACATCACCACGTGGGGGCAT","","","28376","MERENITPDYQREVTRLCVQTALLLLQHGAESTVVSQMAQRLGFALGVKSVECALTANAVVITTLANNHCITTARKSTDKGINMQMVTDVQRIVISAEHKIYDIQLVRKKLSQPKPLKYNRYFVVLMIGLSCASFAHLSGGNALISLITFLAASVAMFVRQELSKRHYNPVIVFAVTAFVASLIAGISLKYQLGNDPQIALASSVLLLVPGFPLINSLADILKGYVNMGIGRWAIATILTFGACLGIVFALSVLNITTWGH","201407","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR006162
PTM
Phosphopantetheine attachment site
PS00012\"[45-60]?PHOSPHOPANTETHEINE
InterPro
IPR010619
Family
Protein of unknown function DUF1212
PF06738\"[21-211]TDUF1212
noIPR
unintegrated
unintegrated
signalp\"[1-32]?signal-peptide
tmhmm\"[117-137]?\"[143-161]?\"[171-189]?\"[199-219]?\"[234-254]?transmembrane_regions


","BeTs to 5 clades of COG2966COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG2966 is ------------b-e-gh--u-----Number of proteins in this genome belonging to this COG is","","Residues 176 to 253 match (3e-28) PD:PD036297 which is described as PROTEOME COMPLETE MEMBRANE VC0438 SP1731 YJJP STRUCTURAL TRANSMEMBRANE INTEGRAL PM1895 ","","","","","","","","","","","","Thu Dec 5 16:04:50 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00288 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 21 to 211 (E-value = 1.3e-63) place AA00288 in the DUF1212 family which is described as Protein of unknown function (DUF1212) (PF06738)","","","","","","","","1","","","" "AA00290","201412","201873","462","ATGGATTGGTTATTTTTGTTACTGGACGATATGTTTTTCGCCGCTATTCCGGCGGTAGGCTTTGCGTTGGTCTTTAATGTGCCGCCGAAAGCGTTGAAATACTGCGCCTTGCTCGGTGCTTTGGGACACGTCACCCGCACCATTTTAATTCAGTGCAACATCCACATCGTTTTTGCCACCCTGGTCGGCGCGGCGCTCATCGGCTTCATCGGCGTACATTTATCCCACCGTTATTTGGCACACCCGAAAGTGTTCACCGTCGCCGCCATTATCCCGATGATTCCTGGCGTGCAGGCATATAAGGCGATGATCGCCATCGTGCAAATTCACCATTACGGCTTCTCCGACGCCTTATTTGAGCAGATGATCGCCTCCTTCATCAGCACCACGTTTATTCTCGGTGCGCTGGTTTTCGGCTTGGCATTACCTGGCTTACTGTTCTATCGGGAAAAACCTGTGGTA","","","16811","MDWLFLLLDDMFFAAIPAVGFALVFNVPPKALKYCALLGALGHVTRTILIQCNIHIVFATLVGAALIGFIGVHLSHRYLAHPKVFTVAAIIPMIPGVQAYKAMIAIVQIHHYGFSDALFEQMIASFISTTFILGALVFGLALPGLLFYREKPVV","201873","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide
tmhmm\"[5-25]?\"[54-74]?\"[84-104]?\"[123-143]?transmembrane_regions


","BeTs to 5 clades of COG3610COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3610 is ------------b-e-gh--u-----Number of proteins in this genome belonging to this COG is","","Residues 48 to 154 match (2e-32) PD:PD032003 which is described as PROTEOME COMPLETE MEMBRANE TRANSMEMBRANE VC0439 SP1730 YJJB CPE1931 SAV0744 P-14 ","","","","","","","","","","","","Thu Dec 5 16:05:34 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00290 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00291","201965","201855","111","TTGCCGATGACATGGTTTTTGGTCATGGCGACAATCAGGCTTAAACGCATTGTATTTCCTAATGTATTTAACGGGTTAAAGTGCGGTTACTATACCACAGGTTTTTCCCGA","","","4325","LPMTWFLVMATIRLKRIVFPNVFNGLKCGYYTTGFSR","201855","","hypothetical protein","Cytoplasm","No significant similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-20]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 12:37:55 2004","Sun Feb 22 12:37:55 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00291 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 12:37:55 2004","","","","","","","","","","","","","1","","","" "AA00292","201940","202398","459","ATGACCAAAAACCATGTCATCGGCAAAGATAACCAAATGCCATGGCACCTGCCCGCCGACCTCGCCTGGTTTCGCCAAAATACCACCGGCAAACCCGTCATCATGGGACGCAAAACCTTTGAAAGCATCGGTCGCCCATTACCGAAACGTACCAACATCGTGCTTTCCCGCCAACCTTTCGTGCACGACGGCATTATTTGGAAAGACAGCCTGGAAAGTGCGGTGGATTTTGTCATCGATTCCGACGAAATCATGCTCATCGGCGGCGGTCAGCTGTTCAAGCAATATTTACCGCAGGCGACCCGCCTTTACCTCACCGAAATCCAAACTGAACTGGAAGGCGACACCTTCTTCCCGCCTATTGATTGGAACCACTGGAACATTGAATTTGAACAATACCGCCCCGCCGACGAACAAAATCCTTACGATTGTCGTTTTATGATTTTGGTGCGGAAAGGG","","","18776","MTKNHVIGKDNQMPWHLPADLAWFRQNTTGKPVIMGRKTFESIGRPLPKRTNIVLSRQPFVHDGIIWKDSLESAVDFVIDSDEIMLIGGGQLFKQYLPQATRLYLTEIQTELEGDTFFPPIDWNHWNIEFEQYRPADEQNPYDCRFMILVRKG","202398","","dihydrofolate reductase","Cytoplasm","","
InterPro
IPR001796
Domain
Dihydrofolate reductase region
PR00070\"[6-16]T\"[20-28]T\"[33-44]T\"[83-97]TDHFR
PF00186\"[1-151]TDHFR_1
PS00075\"[6-28]TDHFR
InterPro
IPR012259
Family
Dihydrofolate reductase
PIRSF000194\"[1-151]TDihydrofolate reductase
PTHR11549:SF1\"[6-132]TDIHYDROFOLATE REDUCTASE
noIPR
unintegrated
unintegrated
G3DSA:3.40.430.10\"[2-146]Tno description
PTHR11549\"[6-132]TDIHYDROFOLATE REDUCTASE


","BeTs to 13 clades of COG0262COG name: Dihydrofolate reductaseFunctional Class: HThe phylogenetic pattern of COG0262 is ------y-vdrlb-efghsn-j-i-wNumber of proteins in this genome belonging to this COG is","Significant hit ( 4.5e-41) to 5/6 blocks of the IPB001796 family, which is described as \"Dihydrofolate reductase\". Interpro entry for IP:IPR001796. IPB001796B 14-28 1e-07 IPB001796C 31-43 3.6e-08 IPB001796D 45-57 2.7e-08 IPB001796E 84-93 0.098 IPB001796F 103-119 1.6e-08","Residues 2 to 152 match (1e-68) PD:PD000692 which is described as DIHYDROFOLATE REDUCTASE OXIDOREDUCTASE NADP METABOLISM ONE-CARBON PROTEOME COMPLETE SYNTHASE RESISTANCE ","","","","","","","","","","","","Thu Dec 5 16:07:08 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00292 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 151 (E-value = 3.9e-58) place AA00292 in the DiHfolate_red family which is described as Dihydrofolate reductase (PF00186)","","","","","Herrington MB, MacRae TJ, Panagopoulos D, Wong SH. A mutation in the folA promoter delays adaptation to minimalmedium by Escherichia coli K-12. J Basic Microbiol. 2002;42(3):172-80. PMID: 12111744 Zywno-van Ginkel S, Dooley TP, Suling WJ, Barrow WW. Identification and cloning of the Mycobacterium avium folAgene, required for dihydrofolate reductase activity. FEMS Microbiol Lett. 1997 Nov 1;156(1):69-78. PMID: 9368362 ","","Thu Dec 5 16:07:08 2002","1","","","" "AA00295","202511","202407","105","GTGGGTGTTGTATCCGCCCGAATTGTTCTGCTTTTAAGAGACAGTTTGGTGTCTCCTCTGCATTCCCTTTTTAAAAACGCTGCGAAAATCCACCGCACTTTTCTG","","","3854","VGVVSARIVLLLRDSLVSPLHSLFKNAAKIHRTFL","202407","","hypothetical protein","Cytoplasm","No significant similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 12:39:06 2004","Sun Feb 22 12:39:06 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00295 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 12:39:06 2004","","","","","","","","","","","","","1","","","" "AA00296","203774","202524","1251","GTGTCTTCTGCTGAAATTTCCCTGGCGGGGGCGCGTCGGATTAAATTGCAAAACATGGTCAACGAAGGTAACACGAAAGCCGCCATGGTGCTCAAACTGCAAGAGCAACCGGGGCGCTTCATTACTGTGGTGCAAATCGGCTTGAATATGGTCGCCGTGTTAGGCGGGGTGATCGGCGAAGCGACCATTCGGGTGCACTTGCAACACGTTATTCATCAATATACCGATGCTGCGTGGGTGGAAAGCGCCGCTTCCTGGATTGCGTTTTTTATCGTGACCGCTTCCTTTATTTTGCTGGCGGATCTCATGCCTAAACGCCTGGCAATGACCAACCCCGAAGTGGTGGCATTGCGCACGGTGCGGATTATGCAAATCTGCATTTTCTTATTGAAACCTATTGTGTGGGTGTTCGATTCCGTCGCCAATTTCATTTTCCGTATTTTTAAAGTATCTACCGTGCGCGAAGAAAGTATGACCTCCGAAGACATCGTGGCAGTGGTGGATGCCGGCGCGGAGGCAGGCGTGTTAAAAGCGCAGGAACATTATCTCATCGAGAATATTTTCGATATGCAGCAACGCACGGTCACCTCCACCATGACCACCCGCGAAAATATCATTTTTTTAGACCGCACTTTTACCCGCCAGCAAGTGCTGGACACGCTCACGAAAAATTCCCATTCCAAACTGCTTATTTGCGATCAGGGCTTGGATCATATTTTAGGTTATGTGGAATCGCACAGTTTGCTGACACTGTTCCTGAAAGAGGAACAGGTGCAGCTCACCGACAATCGTTTGTTGCGCAAACCGCTGTTCGTGCCTGATACTTTGTCTTTGTATGAGGTGCTCGAATTATTTAAATCCACCGGCGAAGATTTTGCCGTTATCGTCAACGAATATGCGCTGGTGGTGGGCATTGTTACCTTAAACGATGTGATGAGTATCGTCATGGGCGAGTTGGTATCCAGCGAAGAAGAACAGATTATCCGCCGCGACGAAGATTCTTGGTTGGTGGACGGCGCCACACCGCTGGAAGATGTGAAACGCGCCTTGGATATTGAAGTCTTCCCGCACGATGAAAATTACGAAACCATCGCCGGTTTTATGATGTATATGCTACGTAAAATCCCGAAAAAAACCGATTTTGTGTTATACGGCCGCTACAAATTTGAAATCATCGACACCGAGAACTTTAAAATCGATCAACTGATGGTGTCTTTTAGGAGGGATTTGGAGGAAAGTAATCATAAGGAT","","","49490","VSSAEISLAGARRIKLQNMVNEGNTKAAMVLKLQEQPGRFITVVQIGLNMVAVLGGVIGEATIRVHLQHVIHQYTDAAWVESAASWIAFFIVTASFILLADLMPKRLAMTNPEVVALRTVRIMQICIFLLKPIVWVFDSVANFIFRIFKVSTVREESMTSEDIVAVVDAGAEAGVLKAQEHYLIENIFDMQQRTVTSTMTTRENIIFLDRTFTRQQVLDTLTKNSHSKLLICDQGLDHILGYVESHSLLTLFLKEEQVQLTDNRLLRKPLFVPDTLSLYEVLELFKSTGEDFAVIVNEYALVVGIVTLNDVMSIVMGELVSSEEEQIIRRDEDSWLVDGATPLEDVKRALDIEVFPHDENYETIAGFMMYMLRKIPKKTDFVLYGRYKFEIIDTENFKIDQLMVSFRRDLEESNHKD","202524","","conserved hypothetical protein (possible hemolysin / transport protein)","Inner membrane, Cytoplasm","","
InterPro
IPR000644
Domain
Cystathionine-beta-synthase
PF00571\"[199-316]TCBS
SM00116\"[204-253]T\"[268-316]TCBS
InterPro
IPR002550
Domain
Protein of unknown function DUF21
PF01595\"[2-180]TDUF21
InterPro
IPR005170
Domain
Transporter-associated region
PF03471\"[328-408]TCorC_HlyC
noIPR
unintegrated
unintegrated
PTHR22777\"[20-416]THEMOLYSIN-RELATED


","No hits to the COGs database.","","Residues 280 to 345 match (1e-08) PD:PD268257 which is described as COMPLETE PROTEOME TRANSMEMBRANE CBS DOMAIN HEMOLYSIN SMC00240 MLR2581 XF1280 INTEGRAL ","","","","","","","","","","","","Fri Dec 6 08:39:27 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00296 is paralogously related to AA01123 (8e-26) and AA00729 (2e-19).","","","","","","Residues 328 to 408 (E-value = 5.9e-21) place AA00296 in the CorC_HlyC family which is described as Transporter associated domain (PF03471)","","","","","","","","1","","","" "AA00298","203943","203764","180","TTGGTTCGACAGCGAAAACTAACGTTCCTTTTTCCTTTCTTCGGTGCGGTTGAAAAACGTTTTAGAAACCGACCGCACTTTATCTTTATTTACATCAATGAATTGAAATCTTATGAGTTTATTTACCGCGATTTTAGTTTTAATTTTATTAATTATCATCAGTGCCGTTGTGTCTTCTGC","","","7609","LVRQRKLTFLFPFFGAVEKRFRNRPHFIFIYINELKSYEFIYRDFSFNFINYHQCRCVFC","203764","","hypothetical protein","Cytoplasm","No significant similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-19]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 12:40:41 2004","Sun Feb 22 12:40:41 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00298 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 12:40:41 2004","","","","","","","","","","","","","1","","","" "AA00299","204396","204494","99","GTGAAAAACCAAAATCACCGTAATGAAAAAATATTTAAAAAATTTACGCATTATTCCGTCCTTTTTCCGACTCGTTTGAACCTCATTGTACCTGAATTT","","","4041","VKNQNHRNEKIFKKFTHYSVLFPTRLNLIVPEF","204494","","hypothetical protein","Cytoplasm","No significant similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 12:42:13 2004","Sun Feb 22 12:42:13 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00299 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 12:42:13 2004","","","","","","","","","","","","","1","","","" "AA00300","204413","203925","489","GTGATTTTGGTTTTTCACCTGTTTTTGTTCGCCACCGTGCACTATGTGTTCCCGCGCTATGATGTGACGCAGGTCACCGGCGTGGAAGTGAAACGGATGGATAAAGACGGGTTAATTACTAAAACCAATCCGGCGGACGGACCGACCCGCGACGTGTATTTTATCAACACCCAACATCCGGACGGCAAAGTGCGGGTATATCGTAACGAAGACACCGGCTGGGGCTTCCCGTTCTATTTTAAATTCGGTTCCGCGAATTTGCAGGCGGAGGCGCAGGCATTGGGTAACGAACAGAAAACCGTACAAATGAAATACTACGGCTGGCGCATTACCGTATTTAACGAATTTCCGAATGCTTTGTCGGTAGAAGCTCTGGCAGAAGGCGAATCGCCAAACCATCCGATTTTCGCCTATATTTTCTACGTGATTTTGCTGTTCACCTTATTCTTCTCTGTGCAATTTGTGCGCGGTTGGTTCGACAGCGAAAAC","","","20382","VILVFHLFLFATVHYVFPRYDVTQVTGVEVKRMDKDGLITKTNPADGPTRDVYFINTQHPDGKVRVYRNEDTGWGFPFYFKFGSANLQAEAQALGNEQKTVQMKYYGWRITVFNEFPNALSVEALAEGESPNHPIFAYIFYVILLFTLFFSVQFVRGWFDSEN","203925","","conserved hypothetical protein","Periplasm, Cytoplasm","","
InterPro
IPR011088
Family
Protein of unknown function DUF1523
PF07509\"[1-163]TDUF1523
noIPR
unintegrated
unintegrated
PD035441\"[1-162]TQ9CKE6_PASMU_Q9CKE6;
signalp\"[1-18]?signal-peptide
tmhmm\"[135-155]?transmembrane_regions


","No hits to the COGs database.","","Residues 1 to 162 match (2e-61) PD:PD035441 which is described as COMPLETE PROTEOME PM1676 TRANSMEMBRANE HI0453 SECRETED ","","","","","","","","","","","","Fri Dec 6 08:45:21 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00300 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00301","205260","204481","780","ATGTTTATTGTGGATTCCCATTGCCATTTGGATGCGTTGGATTACGAAAAATTACATGAAAATATCGCCGATGTAGTGGCAAAAGCTAACGCCCGCGATGTGAAGCATTTATTGGCAATCGGCGTAACGTTAAGCCGTTTCGAGAAAGCCTATCCCGAATTGGTTAAATTTGATAACGTCTCTTTGGCGTGCGGCGTGCACCCTTTGGATTTTGAGGAAGAACCTTACGACGCCGCCCGTTTGCTACATTTGGCGCAGGATCCGAAAGTGGTCGCCATCGGCGAAATCGGCTTGGATTATTATTACAGCGCAGAAAACAAGGCGCAGCAACAGGCGGTGTTTGCCAGCCAGATTGAAGTTGCCAATCAGTTAAATAAGCCGGTGATTATTCACACCCGCGAAGCCCGCGAGGACACCATGAGCCTGTTGCGCGACAATCATGCGGAAAAGTGCGGTGGCGTTTTGCATTGTTTTACGGAAAATTACGACATGGCAAAACAAGCCTTGGATTTGGGCTTTTATATTTCTATTTCAGGCATCGTTACCTTTAAAAATGCCGAGGAAATTCGCGATGTGGTGCGTAAATTGCCATTAGATTGTTTACTGGTGGAAACCGATTCGCCGTATTTGGCGCCGGTGCCTTATCGCGGCAAACAAAATCAACCGGCTTACACCCGTGAAGTGTGCGAATATGTGGCGGCGTTGAAAGGCGTTTCGGTGCAGGAAATGGCGCAAATCACTACGCAAAACTTCGAGCGTTTATTTAAAATTCAGGTACAA","","","29316","MFIVDSHCHLDALDYEKLHENIADVVAKANARDVKHLLAIGVTLSRFEKAYPELVKFDNVSLACGVHPLDFEEEPYDAARLLHLAQDPKVVAIGEIGLDYYYSAENKAQQQAVFASQIEVANQLNKPVIIHTREAREDTMSLLRDNHAEKCGGVLHCFTENYDMAKQALDLGFYISISGIVTFKNAEEIRDVVRKLPLDCLLVETDSPYLAPVPYRGKQNQPAYTREVCEYVAALKGVSVQEMAQITTQNFERLFKIQVQ","204481","","conserved hypothetical protein (possible deoxyribonuclease)","Cytoplasm","","
InterPro
IPR001130
Family
TatD-related deoxyribonuclease
PTHR10060\"[28-257]TTATD DNASE-RELATED
PF01026\"[1-256]TTatD_DNase
TIGR00010\"[3-257]TTIGR00010: hydrolase, TatD family
PS01090\"[127-137]TTATD_2
PS01091\"[192-208]TTATD_3
PS01137\"[3-11]TTATD_1
InterPro
IPR012278
Family
Mg-dependent DNase, TatD
PIRSF005902\"[3-259]TMg-dependent DNase, TatD type
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.140\"[3-255]Tno description


","BeTs to 23 clades of COG0084COG name: Mg-dependent DNaseFunctional Class: LThe phylogenetic pattern of COG0084 is --m-kzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 3.1e-45) to 5/5 blocks of the IPB001130 family, which is described as \"Uncharacterized protein family UPF0006\". Interpro entry for IP:IPR001130. IPB001130A 3-11 0.00022 IPB001130B 60-68 0.43 IPB001130C 90-100 4.2e-07 IPB001130D 110-133 1e-11 IPB001130E 196-216 1.6e-14","Residues 56 to 151 match (1e-07) PD:PD419989 which is described as 1500010M24RIK ","","","","","Tue Feb 18 16:18:38 2003","","","","","","","Tue Feb 18 16:18:38 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00301 is paralogously related to AA00244 (5e-24).","","","","","","Residues 1 to 257 (E-value = 1.4e-118) place AA00301 in the TatD_DNase family which is described as TatD related DNase (PF01026)","","","","","Carter,J.R., Franden,M.A., Aebersold,R. and McHenry,C.S. Identification, isolation, and characterization of thestructural gene encoding the delta\" subunit of Escherichia coli DNA polymerase III holoenzyme Journal of bacteriology. 175 (12), 3812-3822 (1993) PubMed: 8509334 Dong,Z., Onrust,R., Skangalis,M. and O\"Donnell,M. DNA polymerase III accessory proteins. I. holA and holB encodingdelta and delta\" The Journal of biological chemistry. 268 (16), 11758-11765(1993) PubMed: 8505303 ","","Tue Feb 18 16:18:38 2003","1","","","" "AA00302","206265","205267","999","GTGGGTTTCTCTTTCAAGATGATCGCGTTATACCCTTGGCTTACGCCCGTTTATCAGAAAATCACGCAGGCTTTTGAGGAAGGGCTGGGGCATCATGCGTTGCTGATTCGTGCCGATGAAGGTTTGGGCGCAGAACAGCTTTGCCGCCTTTTGGCGCAACGTTTGATGTGCTTAACGCCAAAGAGCGCGGAACCTTGCGGTGAATGCCATGCCTGTCATTTGATGCAGGCGAACAGTCACCCTGATTTCCAGCATATTGCGCCCATTGAAAATAAAGACATCGGTGTAGATCAAATTCGTGCCATGAATGAACAGGCAAGTCAGCACGCGCAACAAAACGGCAATAAAGTGATTTATATTGAACAGGCGCATCGCCTGACGGAATCTGCCGCCAATGCTATTTTGAAAACCTTGGAAGAACCCCGCCCGAACACCTATTTCATTTTGCAGAATGATATGCAAAAGGCGCTGTTGCCCACCATTTATAGCCGTTGCCAAGTGTGGAATCTTCTGCCGCCGGCGACGGATACTGCGTTGCACTGGTTGCAGGCACAAACGTCTGTCGAAACGCCGGAAATTCTGACCGCACTTTTGGTAAATTATGGTCGCCCGCTGTTGGCGCTTGCCATGTTGACGCAGCATCTGCCGGAACAACGGCGCGAGTTTTTACGTCAATTCTGGTTGTTTTATCGTCGTCGTTCGCCGTTGGAATTGTTGCCGTTTTTTAATAAAGAGATTCTGTTGCAACAACTGGATTGGCTGTTGGCGTTTTTGAGTGATAGTCTGAAAAATAAATTGGCTATTCAGGAAAACTGGATTTGTCGGGATATTGAACGGGGCGTGATTCAATTCAGCCAAGGGCTGTCCGCTCCGGCATTGTTAAAAGCGACGCAGATCGTCGGCAAAGTGCGGTCGGATTTGGCGGCGAATAATGCGTTAAATCAGGAATTAATTTTATTGGACGGGCTGACCCGTTTAATTACCGAAGTGTTTGAAGGA","","","37980","VGFSFKMIALYPWLTPVYQKITQAFEEGLGHHALLIRADEGLGAEQLCRLLAQRLMCLTPKSAEPCGECHACHLMQANSHPDFQHIAPIENKDIGVDQIRAMNEQASQHAQQNGNKVIYIEQAHRLTESAANAILKTLEEPRPNTYFILQNDMQKALLPTIYSRCQVWNLLPPATDTALHWLQAQTSVETPEILTALLVNYGRPLLALAMLTQHLPEQRREFLRQFWLFYRRRSPLELLPFFNKEILLQQLDWLLAFLSDSLKNKLAIQENWICRDIERGVIQFSQGLSAPALLKATQIVGKVRSDLAANNALNQELILLDGLTRLITEVFEG","205267","There are also many weaker but still significant hits to DNA polymerase III gamma and tau subunits.","DNA polymerase III, delta' subunit","Cytoplasm","","
InterPro
IPR004622
Domain
DNA polymerase III, delta prime subunit
TIGR00678\"[18-207]TholB: DNA polymerase III, delta' subunit
InterPro
IPR015199
Domain
DNA polymerase III, delta subunit, C-terminal
PF09115\"[216-330]TDNApol3-delta_C
noIPR
unintegrated
unintegrated
G3DSA:1.20.272.10\"[214-330]Tno description
G3DSA:3.40.50.300\"[8-173]Tno description
PTHR11669\"[92-193]TREPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT
signalp\"[1-19]?signal-peptide


","BeTs to 15 clades of COG0470COG name: ATPase involved in DNA replicationFunctional Class: LThe phylogenetic pattern of COG0470 is aompkzyqvdrlbcefghsnu-xitwNumber of proteins in this genome belonging to this COG is","","Residues 17 to 120 match (4e-10) PD:PD035127 which is described as DNA POLYMERASE COMPLETE PROTEOME III GAMMA TAU SUBUNIT SUBUNITS TRANSFERASE ","","","","","","","","","","","Fri Dec 6 08:59:09 2002","Fri Dec 6 08:59:09 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00302 is paralogously related to AA02501 (9e-16).","","","","","","","","","","","Dong,Z., Onrust,R., Skangalis,M. and O\"Donnell,M. 1993. DNA polymerase III accessory proteins. I. holA and holB encodingdelta and delta\". J. Biol. Chem. 268(16): 11758-11765. PubMed: 8505303. Carter,J.R., Franden,M.A., Aebersold,R. and McHenry,C.S. Identification, isolation, and characterization of thestructural gene encoding the delta' subunit of Escherichia coli DNApolymerase III holoenzyme J. Bacteriol. 175 (12), 3812-3822 (1993) PubMed: 8509334 Onrust,R. and O'Donnell,M. DNA polymerase III accessory proteins. II. Characterization of delta and delta' J. Biol. Chem. 268 (16), 11766-11772 (1993) PubMed: 8505304 O'Donnell,M. Accessory protein function in the DNA polymerase III holoenzyme from E. coli Bioessays 14 (2), 105-111 (1992) PubMed: 1575709 Guenther,B., Onrust,R., Sali,A., O'Donnell,M. and Kuriyan,J. Crystal structure of the delta' subunit of the clamp-loadercomplex of E. coli DNA polymerase III Cell 91 (3), 335-345 (1997) PubMed: 9363942 ","","Fri Dec 6 08:59:09 2002","1","","","" "AA00303","206876","206247","630","ATGGTAGGCAAATTTATTGTCATTGAAGGCTTGGAAGGCGCAGGCAAAAGCACCGCTCATCAATGCGTTGTGGATACGTTAAAAACGTTAGGTGTTGGGGAAGTCATCTCTACCCGCGAGCCGGGCGGCACACCGTTGGCGGAAAAGCTACGCCATCTCATTAAACATGAAAACGAAGAGCCGGTGACCGATAAAGCGGAATTACTCATGCTGTATGCGGCGCGCGTGCAGTTGGTGGAAAATGTGATCAAGCCTGCTTTGGCACAAGGCAAATGGGTGGTGGGCGATCGCCATGATATGTCCTCACAGGCTTATCAGGGCGGTGGTCGTCAGTTGGGCAAGGATCTTTTAAGTAGCTTAAAGCAAACCGTATTGGGCGATTTTGAACCGGATTTGACCCTTTATTTAGACATTGATCCGGAGATCGGCTTAGCGCGCGCGCGCGTACGGGGTGAACTGGATCGTATCGAACAGCAAAATCTGGATTTTTTCCACCGCACCCGCGCCCGTTATCTGGAACTGGTGAAAGACAATCCGAAGGCGGTGATCATTGACGCGGCGCAACCTGTTGAGCAGGTGCGGGCGGACATTCAAAGTGCGGTCAAAAATTGGTGGGTTTCTCTTTCAAGA","","","23329","MVGKFIVIEGLEGAGKSTAHQCVVDTLKTLGVGEVISTREPGGTPLAEKLRHLIKHENEEPVTDKAELLMLYAARVQLVENVIKPALAQGKWVVGDRHDMSSQAYQGGGRQLGKDLLSSLKQTVLGDFEPDLTLYLDIDPEIGLARARVRGELDRIEQQNLDFFHRTRARYLELVKDNPKAVIIDAAQPVEQVRADIQSAVKNWWVSLSR","206247","","thymidylate kinase (DTMP)","Cytoplasm","","
InterPro
IPR000062
Domain
Thymidylate kinase
PF02223\"[8-197]TThymidylate_kin
TIGR00041\"[1-197]TDTMP_kinase: thymidylate kinase
PS01331\"[94-106]TTHYMIDYLATE_KINASE
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[1-210]Tno description
PIRSF000737\"[4-208]TThymidylate kinase
PTHR10344\"[1-209]TTHYMIDYLATE KINASE


","No hits to the COGs database.","Significant hit ( 3.6e-39) to 4/4 blocks of the IPB000062 family, which is described as \"Thymidylate kinase\". Interpro entry for IP:IPR000062. IPB000062A 5-18 1.4e-08 IPB000062B 62-75 0.011 IPB000062C 83-106 5.3e-13 IPB000062D 130-146 3.8e-10","Residues 4 to 188 match (1e-09) PD:PD555116 which is described as KINASE TMP TRANSFERASE ","","","","","","","","","","","","Fri Dec 6 09:01:17 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00303 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 197 (E-value = 2.3e-80) place AA00303 in the Thymidylate_kin family which is described as Thymidylate kinase (PF02223)","","","","","Reynes,J.P., Tiraby,M., Baron,M., Drocourt,D. and Tiraby,G.1996. Escherichia coli thymidylate kinase: molecular cloning,nucleotide sequence, and genetic organization of thecorresponding tmk locus. J. Bacteriol. 178(10): 2804-2812.PubMed: 8631667.","","Fri Dec 6 09:01:17 2002","1","","","" "AA00305","207921","206881","1041","ATGAAAAAATTTTGTTTATTTCTTTTGTTTTTACTTGTTCTTCTTGCCGGCGCAGGATTTTGGGGATACCGGCAGTTGCAACAGTTTGTGCAGCAACCGGTGAATGTGCAAAAAGACCGGCTATTCACCGTGGAACGCGGCACCACGGGTAGCAAACTGGTGACTTTGCTGCAAAACGAACATCTTTTAGAAAATGCCGCACTCCTGCCTTGGGTGTTGAAAATTTATCCGGAATTTAACAAGGTGAAAGCGGGCACTTATGCCTTGGATAACGTCAAAACTGTGGAAGATTTGCTGAAGCTTCTCAATTCCGGTAAAGAAGCGCAATTTAACGTGCAGTTCATTGAAGGCAATACCTTTAAAACCTGGCGAAAACGCTTGGAAAACGCACCGCACTTAAAGCAAACCCTAAAAGATAAATCCGAGCAGGAAATTTTTCACTTATTGGCAATTCCCGATGTGGCGCAAGAGGTGTACGAATGGCTGAAAATCGAAGGCTGGTTGTATCCCGACACCTATAATTACACGCCGAATTCCACCGATTTGGAGCTTCTGCAACGTTCCGCCGAACGCATGAAAAAAGCCCTGGATAAAGCATGGCAGGAGCGTGATAAAGATCTGCCGTTGGCGAACCCTTACGAAATGCTGATCCTCGCGTCCATCGTGGAAAAAGAAACCGGCATTGCTGCAGAACGCCCACAAGTGGCGTCGGTATTCATTAATCGGTTAAAAGCCAAAATGAAGCTGCAAACCGATCCGACCGTCATTTACGGCATGGGCGACGACTACAACGGCAATATTCGCAAAAAAGATTTGGAAACGCCAACGCCTTATAACACCTATGTGATTGACGGCTTGCCGCCGACACCGATTGCGATGCCGAGTGAAGAGGCGTTACAGGCGGTGGCACATCCGGCGCAAACGGCGTTTTATTATTTCGTGGCAGACGGCACGGGGGGACACAAATTCAGTCGTAATTTAAACGAACATAACAAAGCGGTGCAGCAATATTTGCGCTGGTACCGCGAACAAAACGGAAAA","","","39919","MKKFCLFLLFLLVLLAGAGFWGYRQLQQFVQQPVNVQKDRLFTVERGTTGSKLVTLLQNEHLLENAALLPWVLKIYPEFNKVKAGTYALDNVKTVEDLLKLLNSGKEAQFNVQFIEGNTFKTWRKRLENAPHLKQTLKDKSEQEIFHLLAIPDVAQEVYEWLKIEGWLYPDTYNYTPNSTDLELLQRSAERMKKALDKAWQERDKDLPLANPYEMLILASIVEKETGIAAERPQVASVFINRLKAKMKLQTDPTVIYGMGDDYNGNIRKKDLETPTPYNTYVIDGLPPTPIAMPSEEALQAVAHPAQTAFYYFVADGTGGHKFSRNLNEHNKAVQQYLRWYREQNGK","206881","","conserved hypothetical protein","Periplasm, Cytoplasm","","
InterPro
IPR003770
Family
Aminodeoxychorismate lyase
PF02618\"[40-340]TADC_lyase
TIGR00247\"[1-347]TTIGR00247: conserved hypothetical protein T
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide
tmhmm\"[5-23]?transmembrane_regions


","BeTs to 14 clades of COG1559COG name: Predicted periplasmic solute-binding proteinFunctional Class: RThe phylogenetic pattern of COG1559 is -------q-drlb-efghsnujx-t-Number of proteins in this genome belonging to this COG is","","Residues 17 to 146 match (4e-39) PD:PD332386 which is described as PROTEOME COMPLETE KINASE LYASE AMINODEOXYCHRORISMATE YCEG EXPORTED THYMIDYLATE PM1672 VC2017 ","","","","","","","","","","","","Fri Dec 6 09:05:07 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00305 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 40 to 340 (E-value = 3.6e-158) place AA00305 in the ADC_lyase family which is described as Aminodeoxychorismate lyase (PF02618)","","","","","","","","1","","","" "AA00306","208398","208063","336","ATGAAAAAAATCGAAGCGATTATAAAACCGTTTAAACTGGACGATGTGCGTGAAGCCTTGTCGGACATTGGCATTACCGGCATGACGGTGACTGAGGTGCGCGGTTTCGGGCGGCAAAAAGGGCATACGGAATTGTATCGCGGTGCCGAATATATGGTGGATTTTCTACCGAAAGTGAAAATGGAAGTTGTGGTGCCCAATGATTTGTTAGACCGATGCTTGGACGCCATTATTGATACAGCACAAACGGGCAAAATCGGTGATGGCAAGATTTTTGTGTACGAGGTGGAACGGGTGATTCGTATCCGCACGGGCGAAGAAAATGAGGATGCCATT","","","12627","MKKIEAIIKPFKLDDVREALSDIGITGMTVTEVRGFGRQKGHTELYRGAEYMVDFLPKVKMEVVVPNDLLDRCLDAIIDTAQTGKIGDGKIFVYEVERVIRIRTGEENEDAI","208063","","nitrogen regulatory protein p-II","Cytoplasm","","
InterPro
IPR002187
Family
Nitrogen regulatory protein P-II
PD001194\"[9-100]TGLNB_HAEIN_P43795;
PR00340\"[2-17]T\"[23-41]T\"[52-75]T\"[83-103]TPIIGLNB
G3DSA:3.30.70.120\"[1-112]Tno description
PF00543\"[4-105]TP-II
PS00638\"[83-96]TPII_GLNB_CTER
InterPro
IPR002332
PTM
P-II protein urydylation site
PS00496\"[46-51]?PII_GLNB_UMP


","BeTs to 15 clades of COG0347COG name: Nitrogen regulatory protein PIIFunctional Class: EThe phylogenetic pattern of COG0347 is a-m----qvdrlbcefghsn-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 3.3e-73) to 2/2 blocks of the IPB002187 family, which is described as \"Nitrogen regulatory protein P-II\". Interpro entry for IP:IPR002187. IPB002187A 6-55 9.4e-42 IPB002187B 60-108 1.6e-30","Residues 1 to 112 match (1e-47) PD:PD001194 which is described as NITROGEN REGULATORY FIXATION PROTEOME COMPLETE P-II TRANSCRIPTION REGULATION PII GLNB-LIKE ","","","","","","","","","","","","Fri Dec 6 09:06:45 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00306 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 106 (E-value = 2.1e-57) place AA00306 in the P-II family which is described as Nitrogen regulatory protein P-II (PF00543)","","","","","Zhang Y, Pohlmann EL, Ludden PW, Roberts GP. Functional characterization of three GlnB homologs in thephotosynthetic bacterium Rhodospirillum rubrum: roles in sensingammonium and energy status. J Bacteriol. 2001 Nov;183(21):6159-68. PMID: 11591658 Reyes-Ramirez F, Little R, Dixon R. Role of Escherichia coli nitrogen regulatory genes in thenitrogen response of the Azotobacter vinelandii NifL-NifAcomplex. J Bacteriol. 2001 May;183(10):3076-82. PMID: 11325935 ","","Fri Dec 6 09:06:45 2002","1","","","" "AA00308","209232","208477","756","ATGATTCCTGCAGAGCGACAAAAATTATTACTCAATTTAATTAACCAAAAAGGTATTGTGAGCATTTCAAAATTAATGGAATCGCTCAATGTTTCACACATGACAATTCGTCGTGATATTCAAAAATTAGAAGAGATGGGGAAGGTTGTCTCAGTATCCGGTGGTGTGAAAATACATGAACATTTGTCCTTTGAGCCTACACATCAGGACAAATCGTTATTATTTCATGATCAGAAAGAAAAAATCGGCGAGCAGGCGGCAAAGTTGATTCCATCTAATACTACGATTTATTTGGATGCCGGCACGACAACGTTGGAAATTGCCTATCGTATTATTGAACGCGATGATTTATTAGTCATAACCAATGATTTCTCCATTACACATTTTTTAATGACCAGCGGCAAATGCCAATTAATCCATATTGGCGGTTCGGTGAATAAACTCAATCACTCTTCGGTAGGGGAACTGGCTGGGCAGTTTTTACGTCAGCTGTCGGTTGACATTGCTTTTATCTCTACCTCTTCTTGGACATTGACGGGCTTAACTACGCCGGATGAAATGAAGCTACCGGTGAAAAAAACGATAATTGAGTCAAGCAATAAGCGGATCTTAGTCTCAGACTCTTCAAAATACGGCAAAGTTGCCACCTTCAAAATTGCAGCCTTAAGCGTTTTCAATACGATTATTTGTGATAAGAATTTATTGCCTAATACAAAAGAAGCAATCCATGATATGGATATTGAATTGTTGCTGGTA","","","28009","MIPAERQKLLLNLINQKGIVSISKLMESLNVSHMTIRRDIQKLEEMGKVVSVSGGVKIHEHLSFEPTHQDKSLLFHDQKEKIGEQAAKLIPSNTTIYLDAGTTTLEIAYRIIERDDLLVITNDFSITHFLMTSGKCQLIHIGGSVNKLNHSSVGELAGQFLRQLSVDIAFISTSSWTLTGLTTPDEMKLPVKKTIIESSNKRILVSDSSKYGKVATFKIAALSVFNTIICDKNLLPNTKEAIHDMDIELLLV","208477","","glycerol-3-phosphate regulon repressor","Cytoplasm","","
InterPro
IPR001034
Domain
Bacterial regulatory protein, DeoR N-terminal
PR00037\"[24-38]T\"[38-56]THTHLACR
PF08220\"[6-62]THTH_DeoR
SM00420\"[6-58]THTH_DEOR
PS51000\"[3-58]THTH_DEOR_2
PS00894\"[6-40]THTH_DEOR_1
InterPro
IPR014036
Domain
Bacterial regulatory protein, DeoR
PF00455\"[76-231]TDeoR


","BeTs to 8 clades of COG1349COG name: Transcriptional regulators of sugar metabolismFunctional Class: K,GThe phylogenetic pattern of COG1349 is -------qvd-lb-efgh-n-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.5e-35) to 5/5 blocks of the IPB001034 family, which is described as \"Bacterial regulatory protein, DeoR family\". Interpro entry for IP:IPR001034. IPB001034A 20-55 1.1e-15 IPB001034B 79-103 1.3e-10 IPB001034C 120-130 0.35 IPB001034D 142-154 25 IPB001034E 203-213 0.047Significant hit ( 7.4e-06) to 1/1 blocks of the IPB000524 family, which is described as \"Bacterial regulatory proteins, GntR family\". Interpro entry for IP:IPR000524. IPB000524 19-59 7e-06","Residues 36 to 112 match (5e-09) PD:PD236511 which is described as COMPLETE PROTEOME TRANSCRIPTION TRANSCRIPTIONAL DNA-BINDING REGULATION REPRESSOR REGULATOR OPERON FAMILY ","","","","","","","","","","","","Fri Dec 6 09:18:51 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00308 is paralogously related to AA02048 (2e-27), AA01698 (5e-18), AA00973 (2e-16), AA00585 (6e-11), AA01546 (2e-10) and AA00586 (9e-08).","","","","","","Residues 6 to 231 (E-value = 9.1e-62) place AA00308 in the DeoR family which is described as Bacterial regulatory proteins, deoR family (PF00455)","","","","","Zeng,G., Ye,S. and Larson,T.J. Repressor for the sn-glycerol 3-phosphate regulon of Escherichiacoli K-12: primary structure and identification of theDNA-binding domain. J. Bacteriol. 178(24): 7080-7089, 1996. PubMed: 8955387. Choi,Y.L., Kawase,S., Nishida,T., Sakai,H., Komano,T.,Kawamukai,M., Utsumi,R., Kohara,Y. and Akiyama,K. Nucleotide sequence of the glpR gene encoding the repressor forthe glycerol-3-phosphate regulon of Escherichia coli K12. Nucleic Acids Res. 16(15): 7732, 1988. PubMed: 3045764.","","Fri Dec 6 09:18:51 2002","1","","","" "AA00309","209425","210327","903","ATGACAAACAAATCATATTCTGTTGCTATTGTTGGGCTGGGTGCAATGGGCATGGGGGCGGCTCAGTCTTGTATAAGAGCCGGATTGACGACCTATGGTGTAGATCTTAACCCAAAAGCACTTGAAAAATTAAAAACTGATGGCGCACACGCAACCAGCCAAAGTGCGGTCGATTTTGCGGATAAATTAGATGCAGTTTTGTTGCTTGTAGTAAATGCTGTGCAAGTCAATTCGGTGCTATTTGGTGAAAATGGTTTAGCGGCTAAGTTAAATAAAGGAACCGCTGTCATGGTTTCCTCAACCATTTCTGCCCAAGATGCGAAAGCGATTTCACAAAAATTAACAGATTTGGGGTTAGTTATGTTAGATGCGCCGGTTTCCGGTGGCGCGGCAAAAGCAGCATTGGGTGAGATGACAGTAATGGCATCAGGTTCTGCACAGGCTTTTGAAAAATTACAACCGGTGTTAGATGCCGTTGCGGGTAAAGTGTATAACATCGGTGAAGAAATCGGTTTAGGCGCAACCGTGAAAATCATCCACCAGCTGCTTGCCGGTGTGCATATTGCCGCAGGTGCAGAAGCGATGGCGCTTGCAGCCAAAGCAGGGATTCCACTTAATCTGATGTACGATGTGGTGACTAACGCAGCAGGTAATTCATGGATGTTTGAAAATCGTATGAAACACGTGGTGGAAGGAGATTATTCTCCGCTTTCTATGGTAGATATTTTTGTGAAAGATTTAGGTCTCGTAAACGATACGGCGAAATCTTTGCACTTCCCACTTCACCTCGCAAGTACCGCCTATTCAATGTTTACTGAAGCGAGTAATGCAGGCTATGGCAAAGAAGATGACAGCGCTGTGATTAAAATTTTCAGTGGTATCGAATTACCGAAAAAAGGAGCG","","","32869","MTNKSYSVAIVGLGAMGMGAAQSCIRAGLTTYGVDLNPKALEKLKTDGAHATSQSAVDFADKLDAVLLLVVNAVQVNSVLFGENGLAAKLNKGTAVMVSSTISAQDAKAISQKLTDLGLVMLDAPVSGGAAKAALGEMTVMASGSAQAFEKLQPVLDAVAGKVYNIGEEIGLGATVKIIHQLLAGVHIAAGAEAMALAAKAGIPLNLMYDVVTNAAGNSWMFENRMKHVVEGDYSPLSMVDIFVKDLGLVNDTAKSLHFPLHLASTAYSMFTEASNAGYGKEDDSAVIKIFSGIELPKKGA","210327","","3-hydroxyisobutyrate dehydrogenase; 2-hydroxy-3-oxopropionate reductase","Cytoplasm","","
InterPro
IPR002204
Family
Hydroxyacid dehydrogenase/reductase
PIRSF000103\"[6-299]T3-hydroxyisobutyrate dehydrogenase
PTHR22981\"[16-295]T3-HYDROXYISOBUTYRATE DEHYDROGENASE-RELATED
PS00895\"[10-23]?3_HYDROXYISOBUT_DH
InterPro
IPR006115
Domain
6-phosphogluconate dehydrogenase, NAD-binding
PF03446\"[5-168]TNAD_binding_2
InterPro
IPR013328
Domain
Dehydrogenase, multihelical
G3DSA:1.10.1040.10\"[171-291]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[1-168]Tno description
PTHR22981:SF7\"[16-295]T3-HYDROXYISOBUTYRATE DEHYDROGENASE
PS51257\"[1-24]TPROKAR_LIPOPROTEIN
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.7e-46) to 5/5 blocks of the IPB002204 family, which is described as \"3-hydroxyisobutyrate dehydrogenase\". Interpro entry for IP:IPR002204. IPB002204A 8-21 7.7e-05 IPB002204B 79-102 9.5e-09 IPB002204C 122-139 1.2e-07 IPB002204D 168-203 2.1e-16 IPB002204E 245-254 0.016Significant hit ( 3.2e-06) to 1/6 blocks of the IPB002135 family, which is described as \"3-hydroxyacyl-CoA dehydrogenase\". Interpro entry for IP:IPR002135. IPB002135A 10-35 3.2e-06","Residues 218 to 291 match (4e-07) PD:PD476046 which is described as PROTEOME COMPLETE OXIDOREDUCTASE REDUCTASE DEHYDROGENASE SEMIALDEHYDE PROBABLE PLASMID NAD TARTRONATE ","","","","","Thu Feb 13 15:26:22 2003","","","","","","","Thu Feb 13 15:26:22 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00309 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Steele,M.I., Lorenz,D., Hatter,K., Park,A. and Sokatch,J.R.Characterization of the mmsAB operon of Pseudomonas aeruginosa PAOencoding methylmalonate-semialdehyde dehydrogenase and3-hydroxyisobutyrate dehydrogenaseJ. Biol. Chem. 267 (19), 13585-13592 (1992)PubMed: 1339433Njau RK, Herndon CA, Hawes JW.Novel beta -hydroxyacid dehydrogenases in Escherichia coli and Haemophilus influenzae.J Biol Chem. 2000 Dec 8;275(49):38780-6.PMID: 10978349 ","","Thu Feb 13 15:26:22 2003","1","","","" "AA00310","210333","211574","1242","ATGTTAGGTGTAATTGCTGATGATTTCACCGGCGCAAGCGATATTGCCAGTTTCTTAGTTGAAAATGGCTTGCATACGGTACAAATGAATGGCGTGCCAAACGCGCCATTAACAGAAAAAGTGGATGCCATTGTCATCGGTTTAAAATCTCGTTCCAACCCGGTGAATGAAGCTATTGAACAATCATTGCAGGCGCTTCACTGGCTACAAAAGAGCGGTTGTTCTAAGTTCTATTTTAAATATTGTTCCACCTTTGATAGCACACCAAAAGGCAATATTGGTCCTGTAACGGATGCCTTGTTAGAAGCACTTGATGATGATTTTACCGTAATCACGCCGGCTTTGCCTGTCAATGGCAGAACGATCTTTAACGGTTATTTATTCGTCGGTAATGTGTTGCTTAATGAATCCGGCATGCGTGATCACCCGATTACACCGATGAAAGACGCCAATCTTATACGTTTAATGGATGCGCAAGCAAAAGGTAAAACCGGTTTAGTGAGTTATGCAGATGTGATTCAAGGTGCTGAGCACCTGAAGGCTTGTTTCACCCGGTTGAAGCAAGCCGGCTTCCGCTACGCTGTTGTGGATGCCGTGGATAATAGTCAACTTGCTGTTTTGGCAGAAGCCGTCAGTGAATTGAAATTAGTCACAGGTGGTTCCGGTTTAGGGGCTTATATGGCAGCAAGATTAAGTGGCGGCAAAAAAGCCACAGATGCTTTTGTACCGAAAAAAGGACGAAGCGTGATTCTTTCCGGTTCTTGTTCTGTGATGACGAATAAACAAGTGAATGCCTATAAAGAAAAAGCCACCGCCATTTATTTAGATGTGGAAAAAGCTATTGCGGAATCTAATTATGCGGAAACGTTGTTTGATCAAGTGCAACCTCATTTTTCTGAACCGCTTGCACCAATGGTTTATGCCACCGTGCCACCGGAACAACTGAAACAAATTCAAAGCCGATTTGGTGGTGAACGGGCAAGCCATGCTATTGAGAAAACCTTTGCAAACTTAGCGCAGTTACTAAAAGAAAAAGCCAAGGTGGAAAACTTTATTACTGCGGGTGGAGAAACTTCAAGCATTGTGGTGCAACAACTTGGCTTCACCGGTTTTCAAATTGGCAAACAAATTGCGCCGGGCGTGCCTTGGTTAAAAGTATTGGGAGAATCGACCGCACTTGCATTGAAATCAGGCAACTTCGGCAAAGAAACCTTCTTCGCTGATGCACAAGGAATGATGTTA","","","44516","MLGVIADDFTGASDIASFLVENGLHTVQMNGVPNAPLTEKVDAIVIGLKSRSNPVNEAIEQSLQALHWLQKSGCSKFYFKYCSTFDSTPKGNIGPVTDALLEALDDDFTVITPALPVNGRTIFNGYLFVGNVLLNESGMRDHPITPMKDANLIRLMDAQAKGKTGLVSYADVIQGAEHLKACFTRLKQAGFRYAVVDAVDNSQLAVLAEAVSELKLVTGGSGLGAYMAARLSGGKKATDAFVPKKGRSVILSGSCSVMTNKQVNAYKEKATAIYLDVEKAIAESNYAETLFDQVQPHFSEPLAPMVYATVPPEQLKQIQSRFGGERASHAIEKTFANLAQLLKEKAKVENFITAGGETSSIVVQQLGFTGFQIGKQIAPGVPWLKVLGESTALALKSGNFGKETFFADAQGMML","211574","","conserved hypothetical protein","Periplasm","","
InterPro
IPR010737
Family
Type III effector Hrp-dependent outers
PF07005\"[159-375]TDUF1537


","BeTs to 3 clades of COG3395COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3395 is ------------bce--h---j----Number of proteins in this genome belonging to this COG is","","Residues 1 to 407 match (2e-15) PD:PD466045 which is described as PROTEOME COMPLETE PLASMID RB0380 MLL7005 ","","","","","","","","","","","","Fri Dec 6 10:05:18 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00310 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 159 to 375 (E-value = 5.3e-115) place AA00310 in the Hop family which is described as Type III effector Hrp-dependent outer proteins (Hop) (PF07005)","","","","","","","","1","","","" "AA00311","211574","212203","630","ATGAGTGATGGTGAATTAAAAAAAATCATGGTGCGGCTTGGACATTCTTTTTATGAACGTGGCTACACCGTCGGTGGCGCAGGAAATCTCTCCACCCGGCTGGATGGGAATCGAATTTTAGTCACGCCTACCGGTTCTTCACTTGGACGTTTAGAGGAAGCGCGACTTTCCATATTAGATATGGAGGGCAACCTGTTAGAAGGTGATAAACCATCCAAAGAATCCGTCTTTCATTTGGCCATGTATCGCAAAAATCCGGAGTGCAAGGCCATTGTCCACCTTCATTCTAGTTACTTAACTGCGCTTTCTTGTTTAGAAAACCTTGATCCACAAAATGCTATAAAAGCCTTTACGCCTTATTACGTAATGCGAGTCGGAAGCTTACCGGTGATTCCTTATTACCGCCCGGGTTCACCGCGCATAGCGGAAGAATTAGAGGCACGCGCGTTGTCAGGTAAAGCCTTTTTATTGGCAAATCATGGCGTAGTGGTCACGGGTAAGGATTTACTCGATGCCGCCGACAATACCGAAGAATTGGAAGAAGCCGCGAAACTGTTCTTCCTATTGCAAGGGCAACCGATTCGTTATCTCAATGACGATGAAGTGAATGAATTGAAAAACAGGGGGAAA","","","23239","MSDGELKKIMVRLGHSFYERGYTVGGAGNLSTRLDGNRILVTPTGSSLGRLEEARLSILDMEGNLLEGDKPSKESVFHLAMYRKNPECKAIVHLHSSYLTALSCLENLDPQNAIKAFTPYYVMRVGSLPVIPYYRPGSPRIAEELEARALSGKAFLLANHGVVVTGKDLLDAADNTEELEEAAKLFFLLQGQPIRYLNDDEVNELKNRGK","212203","","L-fuculose-phosphate aldolase","Cytoplasm","","
InterPro
IPR000169
Active_site
Peptidase, cysteine peptidase active site
PS00639\"[158-168]?THIOL_PROTEASE_HIS
InterPro
IPR001303
Domain
Class II aldolase/adducin, N-terminal
G3DSA:3.40.225.10\"[10-205]Tno description
PF00596\"[8-201]TAldolase_II
noIPR
unintegrated
unintegrated
PTHR22789\"[76-208]TFUCULOSE PHOSPHATE ALDOLASE


","No hits to the COGs database.","Significant hit ( 3e-25) to 4/4 blocks of the IPB001303 family, which is described as \"Class II Aldolase and Adducin N-terminal domain\". Interpro entry for IP:IPR001303. IPB001303A 23-32 23 IPB001303B 35-60 8.5e-05 IPB001303C 78-96 1.5e-09 IPB001303D 155-172 2.4e-06","Residues 1 to 174 match (7e-07) PD:PD125085 which is described as PROTEOME COMPLETE ALDOLASE RHAMNULOSE-1-PHOSPHATE LYASE SUGAR-PHOSPHATE RHAMNOSE LMO2847 LIN2979 METABOLISM ","","","","","","","","","","","","Fri Dec 6 10:17:59 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00311 is paralogously related to AA01703 (9e-08).","","","","","","Residues 8 to 201 (E-value = 1e-61) place AA00311 in the Aldolase_II family which is described as Class II Aldolase and Adducin N-terminal domain (PF00596)","","","","","Joerger AC, Mueller-Dieckmann C, Schulz GE.Structures of l-fuculose-1-phosphate aldolase mutants outlining motions during catalysis.J Mol Biol. 2000 Nov 3;303(4):531-43.PMID: 11054289 Joerger AC, Gosse C, Fessner WD, Schulz GE.Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis.Biochemistry. 2000 May 23;39(20):6033-41.PMID: 10821675Dreyer MK, Schulz GE.Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure.J Mol Biol. 1996 Jun 14;259(3):458-66.PMID: 8676381Chen YM, Zhu Y, Lin EC.The organization of the fuc regulon specifying L-fucose dissimilation in Escherichia coli K12 as determined by gene cloning.Mol Gen Genet. 1987 Dec;210(2):331-7.PMID: 3325779 ","","Mon Feb 17 14:26:11 2003","1","","","" "AA00312","212209","212982","774","ATGCCAAAATTTGCTGCTAATTTAACCATGATGTTCAACGAAGTGCCATTTATTGATCGTTTTGAAGCGGCGGCTAACGCCGGCTTTAAGTATGTCGAGTTTCTCTGGCCTTACGATTACAGTGTTGAAACCATCAGGCAAGAACTGGATAAACATGGTTTAAAGGTCGTTTTATTTAATACTCCGGCAGGCGATGTTTCCAAAGGGGAATGGGGCGTTTCTGCTATTCCCGGGCGTGAGGAACAAAGCCATCAACACATTGATATGGCATTGGAATACGCGCTAGGTCTTGGTTGCCCGAATGTCCATATTATGGCAGCGGTGGTACCGGAAGGGGCGGATAAGTCAGAATATCAACAAATCTTTATTCAGAATATTCGTTATGCATCAGAAAAATTTAAACCGCATGGTGTGAATATTTTACTTGAAGCATTAAGTCCGGAAGTGAAACCGCACTATTTGCTAAAAAGCCAATATGACACCTTAGACATTGTAGAGCGTGTTGAACGCGATAATGTGTTTGTTCAATTAGATTACTTCCATGCTCAAAATGTAGACGGCAATTTATCCCGTTTGACCGACAAATTAAATGGCAAATTTGCGCATGTACAAATTGCTTCCGTACCGGATCGTCATGAACCGGATGAAGGCGAAATCAATTATGAATACCTCTTTAATAAATTAGATGAGATTGGTTACCAAGGTTTCGTAGGCTGTGAGTACAAACCACGGGGTGAAACCTCAAGCGGTCTAGGTTGGTTTGAACAGTATAAA","","","29433","MPKFAANLTMMFNEVPFIDRFEAAANAGFKYVEFLWPYDYSVETIRQELDKHGLKVVLFNTPAGDVSKGEWGVSAIPGREEQSHQHIDMALEYALGLGCPNVHIMAAVVPEGADKSEYQQIFIQNIRYASEKFKPHGVNILLEALSPEVKPHYLLKSQYDTLDIVERVERDNVFVQLDYFHAQNVDGNLSRLTDKLNGKFAHVQIASVPDRHEPDEGEINYEYLFNKLDEIGYQGFVGCEYKPRGETSSGLGWFEQYK","212982","","conserved hypothetical protein (possible hydroxypyruvate isomerase)","Cytoplasm","","
InterPro
IPR012307
Domain
Xylose isomerase-like TIM barrel
PF01261\"[21-219]TAP_endonuc_2
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.150\"[1-257]Tno description
PTHR12110\"[1-258]THYDROXYPYRUVATE ISOMERASE


","No hits to the COGs database.","","Residues 3 to 70 match (7e-08) PD:PD546250 which is described as (see also SP:Q96S83_HUMAN_Q96S83).","","","","","","","","","","","","Fri Dec 6 10:41:59 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00312 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 219 (E-value = 5.1e-07) place AA00312 in the AP_endonuc_2 family which is described as AP endonuclease family 2 (PF01261)","","","","","","","","1","","","" "AA00313","213117","212962","156","ATGGAGACCGGGATGCCAATTAGAATAAGTATTTCATTAGACATACAAAACTCCTTAGCTATGGATATAAAAAGTGCGGTCAATTTTCATGACGTTTTAAAAACTCTCAAAAAAACAACCGCACTTCATCACTTATTTATACTGTTCAAACCAACC","","","5863","METGMPIRISISLDIQNSLAMDIKSAVNFHDVLKTLKKTTALHHLFILFKPT","212962","","hypothetical protein","Cytoplasm","No significant similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 13:59:29 2004","Sun Feb 22 13:59:29 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","Noparalogous sequences are found to this sequence.AA00313 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 13:59:29 2004","","","","","","","","","","","","","1","","","" "AA00314","213139","214386","1248","TTGTATGAGGAAATAGCCGGTTATCGTGAAAAATCTTTTCCGGTTAAAGAGTTAGCTAAAAATACCAACCGTCTAAAAGCATTTTCATTGGAAAAAAGTGGTGGTTTACAATGGGATCATACTTATGGAAACTTTACTGACGGTTCAGCAAGACGAGCGGCTTTAGTAGAGGGTACTCATTTAGGTGTGATGGTTTCATCACATACCAATAAAGAGGCAATTTTATGGTTTAATCAAGCTTTACAACAAGGACAACAAGATGCCGATTGGATTGAACCTGAACAACAGACATATTGGTATAAAGAGATTGCAGGATTATTTGCGTTATCTTTTGCGGTTATTTCTGCGTTATGTTTAGCGGCAGGCTTACTGAAGAATCCTTATTTCTCTGCCGTGACACAAATGCCGTCAAGAAAAGTTGAATTGCCTTCAGGTAAATGGGTTCATTTCGCTATGTGCAATATTATTGCGACAATGATATTGTATCCATTGTTCACGCAATGGGGAGGCGCTAATGAACCTATTGCATCAATGATTTCTTTCATGCCATTGGAGATGGGAAATGGAATTGTCTTATGGTTAGTCGTCAGTGCAATTGTTAATTATCTCTTATTCTTTCTATGGTCCCATAAAAAATCTATTTCTTGGCAGGAATTTGGTATTTTAGCTGGCAAACCAAATATAACGACCTCTCAATTAATCGGGCACTATTTGATTTTAGCTGCCATATTAGTTAGTTATTTGTATGGGATTGCCTATGTCGTTCATTCTTACTGGCAAGTTGAATTGCGCTTTTTATGGCCGGCATTTAAACCTCTTACACCAGAGCGCTTTGCTTTGTTTCCGATTTACTGGTTATTTATTTTATTCTTCTTTTACTCATTTAATGGGTTAGTTGTCACTGTACAAATGCGTATGAAACAGGCAAAAAATTTCACAATAACCTTGATTGGCTGGACAATTAAAACGAGCTTTTTCGCGGTAAGTGGATTGGTACTTTTATGGTTATTTCACTTTATACCGGATTTTATGCAATTGGGACCGGGCTTTGATTTAATTGGACTTCCACAATTCGGTGGTCGCTGGATAATGATGTTATCAGTGATTATTCCACAATTTATTGTGTTGATTTTAATTAGCCATTGGTGTTATTTAAAAACAGGTTATGTGTATTTAGGCGTTTTTTTAACTTCAATATTAATGACATGGATTATTGTTGGCGGGCAGGTTATAGGGCGTTTCCTTGCC","","","47402","LYEEIAGYREKSFPVKELAKNTNRLKAFSLEKSGGLQWDHTYGNFTDGSARRAALVEGTHLGVMVSSHTNKEAILWFNQALQQGQQDADWIEPEQQTYWYKEIAGLFALSFAVISALCLAAGLLKNPYFSAVTQMPSRKVELPSGKWVHFAMCNIIATMILYPLFTQWGGANEPIASMISFMPLEMGNGIVLWLVVSAIVNYLLFFLWSHKKSISWQEFGILAGKPNITTSQLIGHYLILAAILVSYLYGIAYVVHSYWQVELRFLWPAFKPLTPERFALFPIYWLFILFFFYSFNGLVVTVQMRMKQAKNFTITLIGWTIKTSFFAVSGLVLLWLFHFIPDFMQLGPGFDLIGLPQFGGRWIMMLSVIIPQFIVLILISHWCYLKTGYVYLGVFLTSILMTWIIVGGQVIGRFLA","214386","There are some very weak hits to NADH dehydrogenas. Is 'Kmt1 protein' a definition?********","conserved hypothetical protein (possible Kmt1 protein)","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
tmhmm\"[104-124]?\"[145-165]?\"[189-209]?\"[233-253]?\"[280-300]?\"[315-337]?\"[359-379]?\"[389-407]?transmembrane_regions


","No hits to the COGs database.","","Residues 1 to 161 match (3e-47) PD:PD389702 which is described as PROTEOME KMT1 COMPLETE ","","","","","","","","","","","Wed Jan 22 15:57:51 2003","Fri Dec 6 10:54:23 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00314 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00316","214585","215400","816","ATGACATACCAGGTTATCGCGTTTGATCTTGACGGTACTTTGCTAAACCGTCAAGGCAGTATTCTTCCCGCTAGCAAACACGCCATTCAACTGGCACGAAAACAAGGCATGAAAGTAGTTTTTGTCACCGGGCGTCATCACACCGCCGTCAAACCTTATTATCATGAAGTGAACTTGGACACGCCGATTATTTGCTGCAACGGAACTTACCTTTACTACCCACAAACCGATGAAGTGAAATTCGCCAACCCGCTTTCCGCCGCACAATGCCATAAAGTGCTCGACATTGCAGATCAATTCGACACCCACTTGCTGATGTATAGCCGCGATGCCATGAACTACACCCGCTTAAATCCGCACATGGAAAAATTCACCCAATGGGCAATGAGCTGCCCGCCTGCCGTGCGCCCAGACGTACGTCTGGTAACGGATTTCAAGGTAATTATTAATAACTCGAAAGAAAATATCTGGAAATTCGTGATTAGCTCGCCTGATCGTCAGGCTATGGAAAGTGCGGTCAAATCCTTGCCTGAATCGGAGTTCAGCTGTGAATGGTCATGGATTGATCGCGTGGATGTTGCCAACAACGGCAACAGTAAAGGTGCACGTCTGCTTGATTTATTAAAGTTATGGAATATTGATCCGCAAAACGTTATCGCCTTCGGCGACAATCATAACGACATCAGTATGCTTACCGCCGTAGGACTCAGCGTTGCCATGGGAAACGCAGAAGATGCCGTAAAAGCACAGGCAAAACGGGTTATCGGTTCAAATGATAGCGACGGCATCGCCCGGTTTATTGAAGAAATACTTGGC","","","30490","MTYQVIAFDLDGTLLNRQGSILPASKHAIQLARKQGMKVVFVTGRHHTAVKPYYHEVNLDTPIICCNGTYLYYPQTDEVKFANPLSAAQCHKVLDIADQFDTHLLMYSRDAMNYTRLNPHMEKFTQWAMSCPPAVRPDVRLVTDFKVIINNSKENIWKFVISSPDRQAMESAVKSLPESEFSCEWSWIDRVDVANNGNSKGARLLDLLKLWNIDPQNVIAFGDNHNDISMLTAVGLSVAMGNAEDAVKAQAKRVIGSNDSDGIARFIEEILG","215400","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR000150
Family
Cof protein
TIGR00099\"[5-267]TCof-subfamily: Cof-like hydrolase
PS01228\"[5-16]TCOF_1
PS01229\"[221-243]TCOF_2
InterPro
IPR006379
Family
HAD-superfamily hydrolase, subfamily IIB
TIGR01484\"[5-240]THAD-SF-IIB: HAD-superfamily hydrolase, subf
InterPro
IPR013200
Domain
HAD superfamily hydrolase-like, type 3
PF08282\"[6-267]THydrolase_3
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1000\"[1-271]Tno description


","BeTs to 18 clades of COG0561COG name: Predicted hydrolases of the HAD superfamilyFunctional Class: RThe phylogenetic pattern of COG0561 is aompkzy-vdrlbce-gh-n-j-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 8.2e-30) to 3/3 blocks of the IPB000150 family, which is described as \"Cof protein\". Interpro entry for IP:IPR000150. IPB000150A 2-16 1.4e-06 IPB000150B 36-45 0.0069 IPB000150C 219-251 3.5e-17","Residues 191 to 269 match (3e-07) PD:PD186741 which is described as COMPLETE PROTEOME TRANSFERASE ACID FIXI NUCLEOTIDYLTRANSFERASE SYNTHETASE YRBI COF FAMILY ","","","","","","","","","","","","Fri Dec 6 10:55:55 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00316 is paralogously related to AA00482 (1e-20), AA01431 (1e-14) and AA01216 (1e-11).","","","","","","Residues 3 to 244 (E-value = 2.2e-10) place AA00316 in the Hydrolase family which is described as haloacid dehalogenase-like hydrolase (PF00702)","","","","","","","","1","","","" "AA00317","218170","215612","2559","ATGAAACAATATCTGCAACTTAAAGCAGAGAATCCGGATATTTTGTTATTTTATCGTATGGGCGATTTTTACGAGCTATTTTACGACGATGCAAAACGCGCCTCCGCCTTGTTGGATATTTCCCTGACCAAGCGCGGGCAATCCGCCGGACAGCCGATTCCTATGGCGGGCGTGCCTTATCATGCGGTGGAAGGCTATTTGGCGAAATTGGTGCAACTGGGTGAGTCGGTGGCGATTTGCGAGCAGGTCGGCGATCCGAATACCGCAAAAGGCCCTGTAGAACGCCAAATCGTGCGCATTGTCACACCGGGCACCGTGAGCGATGAAGCCCTCTTGCCGGAACGGCAGGATAATCTTATTGCCGCCGTGTATCAGGAAAAAGATCATTTCGGTTTAGCCACGCTGGATATGACCTCCGGCCGTTTTCAAGTGTGCGAGCCGCAATCCCCAGCAGATTTACAAACTGAATTACAACGCATTGAGCCGGTGGAATTGCTTTATTGTGAAGATTTTGCCGATTTTCAGCTAATTGAGCACGCCAAAGGTTTGCGTCGCCGTCCTATTTGGGAATTTGAGCTGAAAACCGCTATTCAACAGCTTTGCCATCAATTTAATACCAAGGATTTACGCGGCTTCGGCGTGGAAAAAGCGATTTTAGGCTTATGCGCCGCCGGTTGTTTATTGCAGTACGCGCGCGAAACTCAACGCACCGCGTTGCCGCATATTCAGAGCATTTATCTGGTTCAACACAGCGAAAACATTCAACTGGACGCCGCAACCCGTCGCAACTTGGAACTCACCCAAAATCTGTCGGGGGGCACGGAAAATACGCTGGCAGCGGTGTTAGATAAATGCGTTACGCCAATGGGAAGCCGCTTGCTCAAACGTTGGATTCACCAACCGATTTGCGATGTGGCGAAACTCATGCAACGCCAACAGGCCATCGGTACGATTTTAGAACAGGATTTAGCGGCGGATTTGCAACCCTATTTACAACAGGTGGGCGACATTGAACGCATTCTGGCGCGCGTGGCGTTACGCACCGCCCGCCCGCGTGATTTAACCCGTTTACGCACCGCTTTGGAGCAGATTCCTTATATTAAAAATCTGTTGGCTGAAAAAACGTCCGCCAAAATGACTGCACTTTACCAACAACTGGGTGATTTTTCCGTGCAATTCGATCTCTTACAACGGGCGATCATTGAAAGCCCACCGGTCTTAATTCGCGACGGTGGTGTTATCGCGCCGGGCTATCATGCGGAATTGGATGAATGGCGTGCGTTAGCTGATGGTGCCACCCGTTATTTAGAAGAATTGGAACAGCGTGAGCGGGAAAGCACGGGGATTGATTCGCTAAAAATCGGTTTCAATGCGGTGCACGGCTATTACATTCAAATCAGTCAAGGACAGGCGCACAAAGCGCCGATTCATTATGTGCGTCGCCAAACCCTGAAAAATGCCGAACGCTATATTATTCCCGAACTTAAAACCTATGAAGATAAAGTGCTGAAGGCAAAAGGCGCTTCCTTGGCGTTGGAAAAACAACTATATGATGAAATCTTTGCTCAATTGTTACCGCACTTAAGCCGTCTGCAACTAGCCGGTTTAGCATTAGCCGAATTAGATGTGCTGACCAACTTAGCGGAGCGGGCGGAGAATTTGAATTATGTGGCGCCGACGTTCTCAGAACAAACCGGCATTCATATTCAAAACGGACGCCATCCGGTGGTAGAACAAGTGCTGAAAGAACCGTTTATCGCCAACCCGACGGAGCTTACCGAACAGCAACATTTCCTCATCATTACCGGGCCGAACATGGGCGGTAAAAGCACCTATATGCGCCAAACTGCATTGATTACGCTGATGGCGTACATGGGCAGTTTTGTACCGGCGGACAGCGCCGTTATCGGGCCGATTGATCGCATTTTTACCCGCATCGGTGCCTCCGATGATTTGGCTTCCGGACGCTCAACCTTTATGGTAGAAATGACGGAAATGGCGAATATTTTGCATCAGGCAACGGAGAAAAGTTTGGTGTTAATTGATGAAATCGGGCGTGGAACCTCCACTTATGATGGGTTGTCTCTGGCTTGGGCATGTGCCGAGTGGCTGGCGAAAAAAATCCGTTCACTGACCCTGTTCGCCACGCACTATTTTGAATTAACTATTCTACCGGAACAAGTCAATGGTATCGGCAACATTCACTTGGATGCCATGGAACACAACGACACCATCGCATTTATGCACGCCGTTCAGCATGGCGCCGCAAGCAAAAGCTATGGCTTGGCAGTGGCGGCTTTAGCCGGTGTTCCGCAACAAGTGATCAAGTTAGCGAAGCAAAAACTTGCCCAACTGGAAAAATTGTCAAACCAAAACACCAATCAGCAAATTCAAGATCTGCGTTTATTGAACCAACGCCAAGGTGAGTTAGCTTTTGAAAGTGCAGAAGATGAGAATAAAGATATGCTGTTGCATATGTTACAAGAATTGGATCCTGACGAATTAAGCCCGAAACAGGCATTGGCTTATTTATATCAGCTGAAAAAAATGGTGAAAAAT","","","97085","MKQYLQLKAENPDILLFYRMGDFYELFYDDAKRASALLDISLTKRGQSAGQPIPMAGVPYHAVEGYLAKLVQLGESVAICEQVGDPNTAKGPVERQIVRIVTPGTVSDEALLPERQDNLIAAVYQEKDHFGLATLDMTSGRFQVCEPQSPADLQTELQRIEPVELLYCEDFADFQLIEHAKGLRRRPIWEFELKTAIQQLCHQFNTKDLRGFGVEKAILGLCAAGCLLQYARETQRTALPHIQSIYLVQHSENIQLDAATRRNLELTQNLSGGTENTLAAVLDKCVTPMGSRLLKRWIHQPICDVAKLMQRQQAIGTILEQDLAADLQPYLQQVGDIERILARVALRTARPRDLTRLRTALEQIPYIKNLLAEKTSAKMTALYQQLGDFSVQFDLLQRAIIESPPVLIRDGGVIAPGYHAELDEWRALADGATRYLEELEQRERESTGIDSLKIGFNAVHGYYIQISQGQAHKAPIHYVRRQTLKNAERYIIPELKTYEDKVLKAKGASLALEKQLYDEIFAQLLPHLSRLQLAGLALAELDVLTNLAERAENLNYVAPTFSEQTGIHIQNGRHPVVEQVLKEPFIANPTELTEQQHFLIITGPNMGGKSTYMRQTALITLMAYMGSFVPADSAVIGPIDRIFTRIGASDDLASGRSTFMVEMTEMANILHQATEKSLVLIDEIGRGTSTYDGLSLAWACAEWLAKKIRSLTLFATHYFELTILPEQVNGIGNIHLDAMEHNDTIAFMHAVQHGAASKSYGLAVAALAGVPQQVIKLAKQKLAQLEKLSNQNTNQQIQDLRLLNQRQGELAFESAEDENKDMLLHMLQELDPDELSPKQALAYLYQLKKMVKN","215612","","DNA mismatch repair protein","Cytoplasm","","
InterPro
IPR000432
Domain
DNA mismatch repair protein MutS, C-terminal
PD001263\"[646-744]TQ6Q134_HAEIN_Q6Q134;
PF00488\"[556-788]TMutS_V
SM00534\"[596-783]TMUTSac
PS00486\"[677-693]TDNA_MISMATCH_REPAIR_2
InterPro
IPR005748
Family
MutS 1 protein
TIGR01070\"[1-849]TmutS1: DNA mismatch repair protein MutS
InterPro
IPR007695
Domain
DNA mismatch repair protein MutS, N-terminal
PF01624\"[1-110]TMutS_I
InterPro
IPR007696
Domain
MutS III
PF05192\"[251-553]TMutS_III
SM00533\"[273-580]TMUTSd
InterPro
IPR007860
Domain
MutS II
PF05188\"[118-243]TMutS_II
InterPro
IPR007861
Domain
MutS IV
PF05190\"[417-508]TMutS_IV
noIPR
unintegrated
unintegrated
G3DSA:1.10.1420.10\"[251-438]Tno description
G3DSA:3.30.420.110\"[118-249]Tno description
G3DSA:3.40.1170.10\"[1-103]Tno description
G3DSA:3.40.50.300\"[556-788]Tno description
PTHR11361\"[601-807]TDNA MISMATCH REPAIR MUTS RELATED PROTEINS
PTHR11361:SF34\"[601-807]TDNA MISMATCH REPAIR PROTEIN MUTS


","No hits to the COGs database.","Significant hit (1.7e-111) to 6/6 blocks of the IPB000432 family, which is described as \"DNA mismatch repair protein MutS family, C-terminal domain\". Interpro entry for IP:IPR000432. IPB000432A 21-31 1.7e-05 IPB000432B 290-311 1.8e-10 IPB000432C 600-631 4.4e-28 IPB000432D 640-688 1.5e-42 IPB000432E 712-722 3.5e-05 IPB000432F 747-778 3.4e-13","Residues 789 to 851 match (4e-13) PD:PD479137 which is described as DNA REPAIR DNA-BINDING MUTS COMPLETE ATP-BINDING MISMATCH PROTEOME ","","","","","","","","","","","","Fri Dec 6 11:02:42 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00317 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 556 to 788 (E-value = 5.6e-166) place AA00317 in the MutS_V family which is described as MutS domain V (PF00488)","","","","","Joshi A, Rao BJ. MutS recognition: multiple mismatches and sequence contexteffects. J Biosci. 2001 Dec;26(5):595-606. PMID: 11807290Schlensog,V. and Bock,A.The Escherichia coli fdv gene probably encodes mutS and is locatedat minute 58.8 adjacent to the hyc-hyp gene clusterJ. Bacteriol. 173 (23), 7414-7415 (1991)PubMed: 1938937","","Fri Dec 6 11:02:42 2002","1","","","" "AA00318","219109","218297","813","GTGCAGGAATCAGTTACATTTGAGCCTTTCCTTGATATTTTTAGTAAGAACGCATTACCTGATATTTTGAAAAAAGGCTTTTTCGCCGAATTAATCGGTTTAGATGAACGACATTTTTTAACGGATAAAGAGGAAATACCACTTCAGTTACAACAAACAGGTAAACATTATTATGCAGTAATTGACACCTCAAAAGTTGTTGCTTATCCCTCCGCCTTAAAAGGTTCGGGACAAATAGCTAATCTCTATAAGGGAAAAACAGGCGAAACATTAGAAGATGCAGCACCCTATTTATTTGAATTCGATCCCGGCAATAGCGGGAGCATTATGTTCCTGCAAAAATTATTCAGGAAAATGGAAAGTCGGGTTTTAAGCCACTGGGAAACTAATCCTGTCATTTTTATCCGTAGTGATAAGGATTTTGATATGGTTTATCACCATCTCAGAAAATTTACACACCTGTATAACCCTGAAGAAGAAATATGGTATTTCTTCCGTTTTTACGACCCAAAAGTGCTAAGCGCCTGCTTGCCATATGATGAACGTCAACCGGCAGACCGTCGAATGGAGCATATTACATCGGTATTTAATAAAGCCACCGCCATTTTTGGTGACGCTAGGCGATCTCCAACAGGTTTTAAATATCATTATATAATTTTCATCTTATTTGGTTCCCTAACTCCCAGAATAAGATGGTTTTTTTATCTTACTCCCCATACAATAGCTCTTTCCCTTAGTAGTCGTTTTTTATTAAAGCTGTGGATATGTTATACAATGTATTTTCAGCGTCTACAAAAAACCTATATTAAGACA","","","31977","VQESVTFEPFLDIFSKNALPDILKKGFFAELIGLDERHFLTDKEEIPLQLQQTGKHYYAVIDTSKVVAYPSALKGSGQIANLYKGKTGETLEDAAPYLFEFDPGNSGSIMFLQKLFRKMESRVLSHWETNPVIFIRSDKDFDMVYHHLRKFTHLYNPEEEIWYFFRFYDPKVLSACLPYDERQPADRRMEHITSVFNKATAIFGDARRSPTGFKYHYIIFILFGSLTPRIRWFFYLTPHTIALSLSSRFLLKLWICYTMYFQRLQKTYIKT","218297","","hypothetical protein","Cytoplasm, Inner membrane","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Fri Dec 6 11:21:09 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00318 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00321","219412","219194","219","TTGGGTGACACAATACCGTTTTGCCCCAACAACTCGACAAACGAACAATTTACCGGTTATGTGCTTGGTTTAATGTCGGACAGAGAAAGTTATCAACAAGCTGTTGAAACGTTTCTATCGACACAAAATTTATCCGGGCATTTTCAACTTGCCGCGCTACCTATTCAAATTTGGTTTACCCGACATGACTTTTCTGCCCCGTTATGGCGATTAGCACAG","","","8303","LGDTIPFCPNNSTNEQFTGYVLGLMSDRESYQQAVETFLSTQNLSGHFQLAALPIQIWFTRHDFSAPLWRLAQ","219194","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Fri Dec 6 11:21:40 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00321 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00323","220282","219527","756","ATGAACATCCAGCTCCTCTGTGAAACAAAAACACCGGAAAAACCAACCGCACTTTTTACCGACGCCGGTTTAACGCACGATCCGCATAGTCCCTTGGCGTTGGTGTGGACGGAAGCGGACGGCGTGGAACGCCTGGAATTGCGCAAATTGGATGAACCGAAACTTGGCGCGGTGTTTGTGGATTTTGTCGGCGGCGCGATGGCGCATCGGCGCAAATTCGGCGGAGGACGCGGCGAAGCGGTGGCAAAAGCGGTGGGCGTTAAACAAGACAAACTCCCCACCGTCATCGACGCCACCGCAGGATTGGGGCGCGATGCCTTTGTGCTGGCGACGCTCGGTTGCCAAGTAAAGTTGGTTGAACGCCACCCGGTGGTTCGCCTGTTACTGCAAGACGGTTTGCAACGTGCTTATGCCGACGAAGAAATCGGCAGCTGGATGCAACGCAATATGCAGCTATTGCCTTATCAACACATCAATGAACTCAACCCCGAAACGGATTGTGCTGATGTGGTGTATCTTGACCCCATGTACCCGCATAAAACCAAAAACGCGTTAGTCAAAAAAGAAATGCGCGTCTTCCAACACCTCGTGGGCGCAGATCTAGATGCCGATGAACTGCTCTCCCCCGCGTTACAACTTGCCCGTCAACGGGTGGTGGTCAAACGCCCGGACTACGCCGATTTTCTCGCCCGAAAAACACCGCACTTTTCCCGCGAAACCAAAAACCATCGCTTTGATGTGTATGTGAAACATGGG","","","28237","MNIQLLCETKTPEKPTALFTDAGLTHDPHSPLALVWTEADGVERLELRKLDEPKLGAVFVDFVGGAMAHRRKFGGGRGEAVAKAVGVKQDKLPTVIDATAGLGRDAFVLATLGCQVKLVERHPVVRLLLQDGLQRAYADEEIGSWMQRNMQLLPYQHINELNPETDCADVVYLDPMYPHKTKNALVKKEMRVFQHLVGADLDADELLSPALQLARQRVVVKRPDYADFLARKTPHFSRETKNHRFDVYVKHG","219527","","conserved hypothetical protein (possible SAM-dependent methyltransferase)","Cytoplasm","","
InterPro
IPR007536
Family
Protein of unknown function DUF548
PF04445\"[13-251]TDUF548


","BeTs to 8 clades of COG0500COG name: SAM-dependent methyltransferasesFunctional Class: Q,RThe phylogenetic pattern of COG0500 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Fri Dec 6 11:29:02 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00323 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 13 to 251 (E-value = 2.8e-156) place AA00323 in the DUF548 family which is described as Protein of unknown function (DUF548) (PF04445)","","","","","","","","1","","","" "AA00324","221381","220287","1095","ATGCTTTATTTACCTGTTGAACGTTACTCCGTGCTACTTGCAGAAAAGCAAAAAAAACTGACCGCACTTTTCGCCCCGTTTAATGCCCCCGAATTACAGGTTTTTGCCTCACCGACACAGCATTTCCGTATGCGTGCGGAATTTCGTATTTGGCATGAACAGGACGATTTCTATCACATCATGTTCGATCAGCAAAGCAAGCAACGTTATCGTGTGGATCGCTTTCCCATTGCCAACGAATTGATTAACCGCATGATGACGGCATTATTACCGTTGCTGAAACAACAAATGGTGTTGCACCACAAGCTGTTCCAAATTGATTATCTCAGCACCCAAAGCGGGCAAATTATCGTCAGTCTGTTATATCACAAAACCTTAGACGACGCGTGGCAGACTGCCGCACAAACCCTACGCACCCAACTGCAGCAACAAGGCTTCAACGTGCAGCTTATCGGGCGCGCCAGTAAGCAAAAAATCTGCCTGGAACAGGATTATGTGGACGAAATCCTCAGCGTGCACGGCAAGCAGTACATTTATCGCCAAGTGGAAAACAGTTTCACCCAGCCGAACGCGGCGGTGAATAGCAAAATGCTGGAATGGGCGGTGGATTGCACCCGCAACAGCCACGGGGATTTGCTGGAACTGTATTGCGGCAACGGCAATTTTTCCATCACCTTGGCGCAAAATTTCCGCCAAGTCCTCGCCACAGAAATCGCCAAACCGTCCGTGGTGGCGGCACAATTTAACATTGTCGCCAACAAGGTGGAAAATTTACAGATTATCCGTATGTCCGCTGAAGAATTCACCCAAGCCATGCAAGGCGTGCGCGCGTTTAACCGGCTCAAAGGCATTGATTTGACTGCCTACCAATGCAACACGATTTTCGTCGATCCGCCGCGTGCCGGATTGGATAACCAAACCCTGAAATTAGTGCAGCAGTACGAGCGTATTTTGTACATTTCCTGCAACCCGCACACCCTGTGCGACAATCTGCAAACCCTCTGCCAAACCCACCGCATTGAAAAAGCCGCGCTGTTCGATCAATTTCCTTATACGGAACACATGGAAGCGGGCGTGTGGTTGGTGAGGAAGTCA","","","42346","MLYLPVERYSVLLAEKQKKLTALFAPFNAPELQVFASPTQHFRMRAEFRIWHEQDDFYHIMFDQQSKQRYRVDRFPIANELINRMMTALLPLLKQQMVLHHKLFQIDYLSTQSGQIIVSLLYHKTLDDAWQTAAQTLRTQLQQQGFNVQLIGRASKQKICLEQDYVDEILSVHGKQYIYRQVENSFTQPNAAVNSKMLEWAVDCTRNSHGDLLELYCGNGNFSITLAQNFRQVLATEIAKPSVVAAQFNIVANKVENLQIIRMSAEEFTQAMQGVRAFNRLKGIDLTAYQCNTIFVDPPRAGLDNQTLKLVQQYERILYISCNPHTLCDNLQTLCQTHRIEKAALFDQFPYTEHMEAGVWLVRKS","220287","","tRNA (Uracil-5-)-methyltransferase (tRNA(M-5-U54)-methyltransferase)","Cytoplasm","","
InterPro
IPR010280
Family
(Uracil-5)-methyltransferase
PF05958\"[8-364]TtRNA_U5-meth_tr
PS01230\"[297-326]TTRMA_1
PS01231\"[346-356]TTRMA_2
InterPro
IPR011869
Family
tRNA (uracil-5-)-methyltransferase
TIGR02143\"[8-364]TtrmA_only: tRNA (uracil-5-)-methyltransfera
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[155-268]Tno description
PTHR11061\"[30-365]TRNA M5U METHYLTRANSFERASE FAMILY
PTHR11061:SF2\"[30-365]TRNA M5U METHYLTRANSFERASE


","No hits to the COGs database.","Significant hit ( 3.5e-49) to 4/4 blocks of the IPB001566 family, which is described as \"RNA methyltransferase trmA family\". Interpro entry for IP:IPR001566. IPB001566A 212-253 4.2e-20 IPB001566B 294-304 0.00012 IPB001566C 317-326 1.3e-06 IPB001566D 338-361 2.3e-13","Residues 318 to 357 match (6e-16) PD:PD004091 which is described as METHYLTRANSFERASE TRANSFERASE PROTEOME COMPLETE TRNA PROCESSING URACIL-5--METHYLTRANSFERASE RRNA RNA TRNAM-5-U54- ","","","","","","","","","","","","Fri Dec 6 11:32:27 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00324 is paralogously related to AA01071 (5e-20) and AA02992 (1e-09).","","","","","","Residues 8 to 364 (E-value = 1.1e-267) place AA00324 in the tRNA_U5-meth_tr family which is described as tRNA (Uracil-5-)-methyltransferase (PF05958)","","","","","Gustafsson,C., Lindstrom,P.H., Hagervall,T.G., Esberg,K.B. and Bjork,G.R. The trmA promoter has regulatory features and sequence elementsin common with the rRNA P1 promoter family of Escherichia coli J. Bacteriol. 173 (5), 1757-1764 (1991) PubMed: 1999392 Gustafsson,C. and Warne,S.R. Physical map of the oxyR-trmA region (minute 89.3) of the Escherichia coli chromosome J. Bacteriol. 174 (23), 7878-7879 (1992) PubMed: 1447162 ","","Fri Dec 6 11:32:27 2002","1","","","" "AA00325","221780","221454","327","ATGGCTGAGAGTTTTAGCGTCACACGTCGTTTTTTCGATGACAAAAATTACCCGCGCGGCTTCGCCCGTCACGGCGACTACACCATCAAAGAAGCACAGGCTTTAGAGCAATACGGACAAGCATTCCGTGCTTTGGATTCAGGCGAGCGTAAACCTGCAACGGCAGAAGAAAAAGCCTTCGTGGCGTTCTGTCGTGGTAAACGTGAAGCGGAAACCTTCTTTGAGAAGACCTGGAATAAATATCGCAGCCATATTTCTGCCAGCAAACGCCTCTACACCTTATCCGGCGTGGTGAGTGTAGATAATCTGGACGACTACTCGGCAGAC","","","12535","MAESFSVTRRFFDDKNYPRGFARHGDYTIKEAQALEQYGQAFRALDSGERKPATAEEKAFVAFCRGKREAETFFEKTWNKYRSHISASKRLYTLSGVVSVDNLDDYSAD","221454","","conserved hypothetical protein","Cytoplasm, Extracellular","","
InterPro
IPR007335
Family
Protein of unknown function DUF413
PF04219\"[1-109]TDUF413
noIPR
unintegrated
unintegrated
PD030670\"[1-109]TQ9CK33_PASMU_Q9CK33;


","No hits to the COGs database.","","Residues 1 to 109 match (2e-41) PD:PD030670 which is described as PROTEOME COMPLETE YIFE WITH YPO3903 VCA1021 REGULATOR STY3707 COLI E. ","","","","","","","","","","","","Fri Dec 6 11:33:34 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00325 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 109 (E-value = 1.3e-66) place AA00325 in the DUF413 family which is described as Protein of unknown function, DUF (PF04219)","","","","","","","","1","","","" "AA00326","222457","221843","615","ATGAAAAAATGGTTATTTTTAGCCCTTACCGCCGCGTTTTCCGTCTCCGTGCAAGCACAGGATTTAACGGAAGGCAAACAATACACCGTAGTGGAAGGTCAACAACGCACCGCCCAGCCTGAAGTGATTGAATTTTTCTCTTTCTATTGCCCGCATTGTTATTCCTTTGAAGCGCAATATCACATCCCGCAAAAAGTTGCCGAAGCCTTGCCGGAAGGCACCTCTTTTAAACAATACCATGTGGATTTCTTAGGTCTTCAGTCGGAAAACCTAACTCGCGCCTGGGCGTTGGCGATGGCGATCAAAGCGGAAGAAAAAGTCAAAATACCATTGTTTAAAGCGGCACAAACCAACACGTTAAAATCTATGGATGACATTCGCCAAATCTTTATTGATAACGGCATTTCTGCCGAACAATTTGACGGCGGCATCAACAGTTTTGCGGTAAGTGGTTTAGTCGCCAAACAGCAAAATTTGGTGGAAAAATACCAACTGCGCGGTGTGCCGGATTTCTACGTGAATGGCAAATATCGCGTAAATACAGAAGGTTTGGCGCGCGATGAAAAGGGTTTCGTTGCCGAATATGTTGAAACCGTAAAAGGTTTATTGCAAAGA","","","23350","MKKWLFLALTAAFSVSVQAQDLTEGKQYTVVEGQQRTAQPEVIEFFSFYCPHCYSFEAQYHIPQKVAEALPEGTSFKQYHVDFLGLQSENLTRAWALAMAIKAEEKVKIPLFKAAQTNTLKSMDDIRQIFIDNGISAEQFDGGINSFAVSGLVAKQQNLVEKYQLRGVPDFYVNGKYRVNTEGLARDEKGFVAEYVETVKGLLQR","221843","","periplasmic oxidoreductase (por) (Thiol:disulfide interchange protein dsbA precursor.)","Periplasm, Cytoplasm","","
InterPro
IPR001853
Family
DSBA oxidoreductase
PF01323\"[41-196]TDSBA
InterPro
IPR006662
Domain
Thioredoxin-related
PS00194\"[42-60]TTHIOREDOXIN
InterPro
IPR010916
Domain
TonB box, N-terminal
PS00430\"[1-20]?TONB_DEPENDENT_REC_1
InterPro
IPR012335
Domain
Thioredoxin fold
G3DSA:3.40.30.10\"[20-205]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-19]?signal-peptide


","BeTs to 7 clades of COG0526COG name: Thiol-disulfide isomerase and thioredoxinsFunctional Class: O,CThe phylogenetic pattern of COG0526 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.8e-51) to 4/4 blocks of the IPB001853 family, which is described as \"DSBA oxidoreductase\". Interpro entry for IP:IPR001853. IPB001853A 19-31 0.081 IPB001853B 42-56 2.6e-13 IPB001853C 92-112 1.2e-07 IPB001853D 139-177 2.7e-24","Residues 41 to 176 match (6e-10) PD:PD005778 which is described as COMPLETE PROTEOME MEMBRANE OUTER THIOL:DISULFIDE 27KDA ISOMERASE INTERCHANGE PERIPLASMIC SIGNAL ","","","","","","","","","","","","Fri Dec 6 11:35:30 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00326 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 41 to 196 (E-value = 4.2e-40) place AA00326 in the DSBA family which is described as DSBA-like thioredoxin domain (PF01323)","","","","","Bardwell,J.C., McGovern,K. and Beckwith,J. Identification of a protein required for disulfide bond formation in vivo Cell. 67 (3), 581-589 (1991) PubMed: 1934062 Kamitani,S., Akiyama,Y. and Ito,K. Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme The EMBO journal. 11 (1), 57-62 (1992) PubMed: 1740115 Zhang,H.Z. and Donnenberg,M.S. DsbA is required for stability of the type IV pilin of enteropathogenic escherichia coli Molecular microbiology. 21 (4), 787-797 (1996) PubMed: 8878041 Zapun,A., Bardwell,J.C. and Creighton,T.E. The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo Biochemistry. 32 (19), 5083-5092 (1993) PubMed: 8494885 Link,A.J., Robison,K. and Church,G.M. Comparing the predicted and observed properties of proteins encoded in the genomeof Escherichia coli K-12 Electrophoresis. 18 (8), 1259-1313 (1997) PubMed: 9298646 Grauschopf,U., Winther,J.R., Korber,P., Zander,T., Dallinger,P. and Bardwell,J.C.Why is DsbA such an oxidizing disulfide catalyst? Cell. 83 (6), 947-955 (1995) PubMed: 8521518 Akiyama,Y., Kamitani,S., Kusukawa,N. and Ito,K. In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product The Journal of biological chemistry. 267 (31), 22440-22445 (1992) PubMed: 1429594 Martin,J.L., Bardwell,J.C. and Kuriyan,J. Crystal structure of the DsbA protein required for disulphide bond formation in vivo Nature. 365 (6445), 464-468 (1993) PubMed: 8413591 Guddat,L.W., Bardwell,J.C., Zander,T. and Martin,J.L. The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding Protein science : a publication of the Protein Society. 6 (6), 1148-1156 (1997) PubMed: 9194175 ","","Fri Dec 6 11:35:30 2002","1","","","" "AA00327","222742","222479","264","ATGAAATGTCATCGCCTGAATGAAGTGTTGGAACTTTTGCAACCGTACTGGTCTAAAGACTCCGATTTGCATTTAACGCAGATTTTGCAAAAAATCGCTGACGAAGCAGGTTTTGATAAGCCGTTAACCGAATTACCGGACGAAGTGATTATTTATCACTTAAAAATGGCAGGAAAAGACAAATTTGAACCGATTCCCGGGATCAAAAAAGATTATGAAGAAGATTTTAAAGCTGCTTTATTAAAAGCACGTGGAATTATTAAG","","","10176","MKCHRLNEVLELLQPYWSKDSDLHLTQILQKIADEAGFDKPLTELPDEVIIYHLKMAGKDKFEPIPGIKKDYEEDFKAALLKARGIIK","222479","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR009383
Family
Protein of unknown function DUF1040
PF06288\"[1-88]TDUF1040
noIPR
unintegrated
unintegrated
PD029038\"[1-88]TQ9CK35_PASMU_Q9CK35;


","BeTs to 3 clades of COG3084COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3084 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 1 to 88 match (2e-33) PD:PD029038 which is described as PROTEOME COMPLETE YIHD CYTOPLASMIC STY3885 VC0037 HI0845 PM1800 YPO0013A ORF1 ","","","","","","","","","","","","Fri Dec 6 11:37:21 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00327 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 88 (E-value = 5e-55) place AA00327 in the DUF1040 family which is described as Protein of unknown function (DUF1040) (PF06288)","","","","","","","","1","","","" "AA00329","222877","223407","531","ATGGGCGGTGCGGACAAAGGCTTACAGCGATTGCACGGCAAACCGCTGTTTCAGTGGATTTATGAACGGCTGTGTTCGCAGGTGGCGCAGGTTTCGGTGAATACCAATCGCAATCAAGCCGATTATGCCGCTGCCGGCTTGCCGGTATTTGCCGATAATATGGAGGGGTTTCAAGGCCCGTTAAGCGGGATTTTGACGGCGTTGGAACGATCCGACACGGATTTTGTCTTATTTGTACCCTGCGACAGCCCGTTTTTCCCGGAAAATCTGCTGGAAAAGCTCAAAAGTGCGGTCATTTTTCACGGCGTTTCTGTTGCCTATGCCCATGATGGCGAGCGGGAACATCCGACCTTCTGTTTAATGGCGCGCAGTCTGAAAGACAAACTTGCCGCCTATTTAGCTTCGGGCGAGCGCCGAATGCTGCATTTTATGCGCCAAAACGGCGCAGTGAGCGTGGATTTTTCGGAAAATAAACAGGCGTTTGCCAATATCAATACATTCGATGAGTTGCAGCAACTTAACGGACAGGCG","","","21329","MGGADKGLQRLHGKPLFQWIYERLCSQVAQVSVNTNRNQADYAAAGLPVFADNMEGFQGPLSGILTALERSDTDFVLFVPCDSPFFPENLLEKLKSAVIFHGVSVAYAHDGEREHPTFCLMARSLKDKLAAYLASGERRMLHFMRQNGAVSVDFSENKQAFANINTFDELQQLNGQA","223407","","molybdopterin-guanine dinucleotide biosynthesis protein","Cytoplasm","","
InterPro
IPR013482
Family
Molybdopterin-guanine dinucleotide biosynthesis protein A
TIGR02665\"[1-171]Tmolyb_mobA: molybdopterin-guanine dinucleot
noIPR
unintegrated
unintegrated
G3DSA:3.90.550.10\"[1-174]Tno description


","BeTs to 17 clades of COG0746COG name: Molybdopterin-guanine dinucleotide biosynthesis protein AFunctional Class: HThe phylogenetic pattern of COG0746 is aompkz-q-dr-bcefgh-nuj----Number of proteins in this genome belonging to this COG is","","Residues 1 to 170 match (3e-56) PD:PD277375 which is described as BIOSYNTHESIS COMPLETE PROTEOME DINUCLEOTIDE MOLYBDOPTERIN-GUANINE A COFACTOR MOLYBDENUM GTP-BINDING PROBABLE ","","","","","","","","","","","","Fri Dec 6 11:39:45 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00329 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Iobbi-Nivol,C., Palmer,T., Whitty,P.W., McNairn,E. and Boxer,D.H.The mob locus of Escherichia coli K12 required for molybdenum cofactor biosynthesis is expressed at very low levels Microbiology 141 (Pt 7), 1663-1671 (1995) PubMed: 7551035 Eaves,D.J., Palmer,T. and Boxer,D.H. The product of the molybdenum cofactor gene mobB of Escherichia coli is a GTP-binding protein Eur. J. Biochem. 246 (3), 690-697 (1997) PubMed: 9219527 ","","Fri Dec 6 11:39:45 2002","1","","","" "AA00330","223509","224036","528","ATGTTAAAAAAACTTTCCATTCTTGTGTTTGCCTCCCTGTTGAGTGCGTGTTCCCTTTCTTCTATTTCCTCTTATGTGCCGTTTATGGGCGACAAAAAAACTGTCATTAACTTAGACGAAGATAAAATCGATCAAAAATCCTACGCTACCGCTTATGAAGCCACGGTGGAAACCTATCGCGATCGCGTAAACGATAACTACAATGTCAACTCGTTCGCCAGCGGCGCGAAAGACTGGTATTTGGGCGGAATCCTCATTCCGGTTGAACAGATCAAAGAAAAACTGTATAGCCCGCAAGGTCAAGATTCCGATGTGTACGCTTATTACAGCGGCGTGCTTCATGCTGAGGCGTTGCAAGGCAATTTCGCCAAATTGAATCCGAATTGCTGGAGCTACATTGATACGCCGAGCACTACACAAGGTATTTATGATGCCATGTTAGATTTACAAAAAGGCAAAGTGCGGTCAGAACATGATGAATATATTGCGCAAGGTTCCGAGCAGCTGCTCAAACTTTGCACCGGAAAA","","","19622","MLKKLSILVFASLLSACSLSSISSYVPFMGDKKTVINLDEDKIDQKSYATAYEATVETYRDRVNDNYNVNSFASGAKDWYLGGILIPVEQIKEKLYSPQGQDSDVYAYYSGVLHAEALQGNFAKLNPNCWSYIDTPSTTQGIYDAMLDLQKGKVRSEHDEYIAQGSEQLLKLCTGK","224036","","conserved hypothetical protein","Outer membrane, Extracellular","","
noIPR
unintegrated
unintegrated
PS51257\"[1-17]TPROKAR_LIPOPROTEIN
signalp\"[1-20]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","","Residues 25 to 173 match (7e-54) PD:PD415572 which is described as COMPLETE PROTEOME PM1798 SIGNAL PRECURSOR HI0449 ","","","","","","","","","","","","Fri Dec 6 11:40:33 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00330 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00332","224151","225677","1527","ATGTTTAATTTACCTGAAAGTAACATTCATCTGGCGGCGCAAGCCGACAATAAGCAGCAAGCTATTGAAATGGCGGCAAATGCGCTTGAACAGGCGGGTTATGTGGAAAGCGGCTACCTGCAAGGAATGTTAGGACGCGAACAACAAACCTCGACGTTTTTGGGTAACGGCATTGCCATTCCGCACGGTACGTTAGAAACCCGCAGCATGGTGAAAAATACCGGCGTGCAGATTTTCCAATTTCCACAAGGCATTGAATGGGGTGAAGGCAATATCGCTTATGTGGTAATTGGCATTGCCGCGCGCTCCGACGAGCATTTGGCATTGTTGCGCCAACTGACGCACGTGCTGGGGAATGAAGACACCGCCGCCAAACTCGCCACGCTGACCGATGTGAAAAAATTCCGTGCCATTTTAATGGGCGAAGCGGAAGCATTTAAAGTAGCCGCCGAAAACATCAGTTTGGATGTGGACACCGCCAGCCTGTTGACCTTAATCGCCATCAACGCGGGCAAATTGGAACAGCAAAGTGCGGTCAATAATCAATACGTTTCCGAGGTCATCGCCAATCCGGCGTTGCCGTTGGTGCAAGGTTTATGGGTAACCGACGCGGCGGTAGGCAATCAAAAGAACGCGATTGCCTTTAGTCGTGCAAAACAGGCGTTCAGTCTGAATAATAAAGCCGTGCACGGCGTGGTGACGGTCGCCTATGCCAACGATCAAATCAACGAGGCGTTAACCCGTTTATTGGATGCGAAAGTGCAACAAATCTTGTTAAACGGTGACGGCGCGCAAATTGTCGCTGTGTTAAACGGCGTGGCAATTCCTGAAGCGGTAGCGCCAACCGCTTCAAGTGAACCGGCGGTGGCGGGCGGCAGCGTGGTCGGCACTTTCACCATTCGTAACGAACACGGTTTACACGCCCGTCCGAGTGCCATTTTAGTCAACGAAGTGAAGAAATTTACCTCAAAAATCAATGTAGAAAACCTCACGCGCGCTAGTGCACCGGTGAGCGCCAAGAGCCTGATGAAAATCGTAGCGTTGGGCGTGACCCAAGGACATCGTTTACGTTTCGTAGCGGAAGGTGAAGATGCGCAAGCCGCCATGGAAGCCATCGGCAAAGTGATTGCTGCCGGTCTTGGCGAAGGCGTTTCTGCCGTACCGCCGAGTGAACCGGATACTATCGAAGTTATGGGACAAGCTACGCCGGCAGCCTCTGCGTCAAGCCATGAAAGTGCGGTGCAAAATCCGGGTGAATCGGTGGAAGGCATTTTTGAAGTGAAAAACGAACATGGCTTACACGCCCGCCCTGCTGCAGTATTAGTGAGCGAAGTGAAAAAATACAACGCCAATGTGGCGGTGCAAAATCTATCGCGCGATTCACAACTGGTCAGCGCGAAAAGCCTGATGAAAGTGGTGGCGTTGGGTGTCGTGAAAGGCCATCGCCTGCGTTTCGTAGCGACCGGTGAGCAAGCGCAACAAGCCATCGACGGCATCGGCGCCGCGATCAACGCAGGATTGGGAGAA","","","53275","MFNLPESNIHLAAQADNKQQAIEMAANALEQAGYVESGYLQGMLGREQQTSTFLGNGIAIPHGTLETRSMVKNTGVQIFQFPQGIEWGEGNIAYVVIGIAARSDEHLALLRQLTHVLGNEDTAAKLATLTDVKKFRAILMGEAEAFKVAAENISLDVDTASLLTLIAINAGKLEQQSAVNNQYVSEVIANPALPLVQGLWVTDAAVGNQKNAIAFSRAKQAFSLNNKAVHGVVTVAYANDQINEALTRLLDAKVQQILLNGDGAQIVAVLNGVAIPEAVAPTASSEPAVAGGSVVGTFTIRNEHGLHARPSAILVNEVKKFTSKINVENLTRASAPVSAKSLMKIVALGVTQGHRLRFVAEGEDAQAAMEAIGKVIAAGLGEGVSAVPPSEPDTIEVMGQATPAASASSHESAVQNPGESVEGIFEVKNEHGLHARPAAVLVSEVKKYNANVAVQNLSRDSQLVSAKSLMKVVALGVVKGHRLRFVATGEQAQQAIDGIGAAINAGLGE","225677","","PTS system, fructose-specific IIA/FPr component (diphosphoryl transfer protein)","Cytoplasm","","
InterPro
IPR000032
Family
Phosphotransferase system, phosphocarrier HPr protein
PD002238\"[305-383]T\"[432-487]TQ8D7F4_VIBVU_Q8D7F4;
PR00107\"[305-321]T\"[333-348]T\"[348-365]TPHOSPHOCPHPR
G3DSA:3.30.1340.10\"[293-383]T\"[420-509]Tno description
PF00381\"[293-379]T\"[420-506]TPTS-HPr
InterPro
IPR001020
PTM
Phosphotransferase system, HPr histidine phosphorylation site
PS00369\"[305-312]T\"[432-439]TPTS_HPR_HIS
InterPro
IPR002114
PTM
Phosphotransferase system, HPr serine phosphorylation site
PS00589\"[461-476]?PTS_HPR_SER
InterPro
IPR002178
Domain
Phosphotransferase system, phosphoenolpyruvate-dependent sugar EIIA 2
PD001689\"[4-132]TPTFA_HAEIN_P44715;
G3DSA:3.40.930.10\"[4-143]Tno description
PF00359\"[2-142]TPTS_EIIA_2
PS51094\"[2-142]TPTS_EIIA_TYPE_2
PS00372\"[47-63]TPTS_EIIA_TYPE_2_HIS
InterPro
IPR005698
Family
Phosphotransferase system, HPr
TIGR01003\"[297-377]T\"[425-504]TPTS_HPr_family: phosphocarrier, HPr family


","BeTs to 7 clades of COG1762COG name: Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type)Functional Class: G,TThe phylogenetic pattern of COG1762 is ---------d-lb-efgh-n-j-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1e-34) to 2/2 blocks of the IPB001020 family, which is described as \"Histidine phosphorylation site in HPr protein\". Interpro entry for IP:IPR001020. IPB001020A 300-327 7.7e-15 IPB001020B 334-372 1.7e-18 IPB001020A 427-454 2.4e-12Significant hit ( 3.2e-23) to 3/3 blocks of the PR00107 family, which is described as \"Phosphocarrier protein signature\". Prints database entry for PR:PR00107. PR00107A 305-321 5.7e-09 PR00107B 333-348 0.008 PR00107C 348-365 4.3e-08Significant hit ( 2.1e-10) to 2/2 blocks of the IPB002114 family, which is described as \"Serine phosphorylation site in HPr protein\". Interpro entry for IP:IPR002114. IPB002114A 294-324 0.0008 IPB002114B 339-382 8.1e-05 IPB002114A 421-451 0.001 IPB002114B 466-509 0.021Significant hit ( 1.9e-09) to 1/1 blocks of the IPB002178 family, which is described as \"phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2\". Interpro entry for IP:IPR002178. IPB002178 46-63 1.9e-09","Residues 425 to 488 match (1e-19) PD:PD002238 which is described as HPR PHOSPHOTRANSFERASE PHOSPHOCARRIER PROTEOME COMPLETE SYSTEM PHOSPHORYLATION HISTIDINE-CONTAINING SUGAR PTS ","","","","","","","","","","","","Wed Feb 19 14:15:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00332 is paralogously related to AA01599 (7e-10).","","","","","","Residues 420 to 506 (E-value = 1.6e-36) place AA00332 in the PTS-HPr family which is described as PTS HPr component phosphorylation site (PF00381)","","","","","Geerse,R.H., Izzo,F. and Postma,P.W.The PEP: fructose phosphotransferase system in Salmonellatyphimurium: FPr combines enzyme IIIFru and pseudo-HPr activitiesMol. Gen. Genet. 216 (2-3), 517-525 (1989)PubMed: 2546043Reizer,J., Reizer,A., Kornberg,H.L. and Saier,M.H. Jr.Sequence of the fruB gene of Escherichia coli encoding thediphosphoryl transfer protein (DTP) of the phosphoenolpyruvate:sugar phosphotransferase systemFEMS Microbiol. Lett. 118 (1-2), 159-162 (1994)PubMed: 8013873Dobrynina OIu, Erlagaeva RS, Umiarov AM, Bol'shakova TN.[The multifunctional fructose-specific component of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli K12--fruA gene product]Mol Gen Mikrobiol Virusol. 2001;(4):18-22. Russian.PMID: 11816114 Kornberg HL.Routes for fructose utilization by Escherichia coli.J Mol Microbiol Biotechnol. 2001 Jul;3(3):355-9. Review.PMID: 11361065","","Wed Feb 19 14:15:45 2003","1","","","" "AA00333","225683","226621","939","ATGGCAAAAGTCGCAACCATCACCTTAAACTCCGCTTACGATTTGGTCGGGCGTTTAAAACGTATTGAATTGGGCGAAGTGAACACCGTGGAAACCCTCGGTTTTTTCCCGGCGGGCAAAGGCATTAACGTGGCGAAAGTGTTAAAAGATTTGGACGTGGATGTCACCGTGGGCGGGTTCCTTGGCGAAGATAACCAAGGGGATTTCGTCACCCTGTTCGACAAATTGGGGCTACAAGATAAATTCCAACGCGTGCCGGGTAAAACCCGCATTAACGTGAAAATCACCGAAACCGAAGCGGACGTCACGGACTTGAATTTCTTAGGTTATAAAATCAGTGCCGACGCATGGCAACAGTTTGTGACGGATTCTCTCGCCTATTGCAAAGCCTTCGACATCGTCGCCGTGTGCGGCAGCTTGCCACGCGGCGTGACACCGGAACTATTCGCCGACTGGTTAAAACAGTTACATCAGGCGGGCGTAAAAGTGGTGTTGGACAGCAGTAACGCCGCATTGACCGCCGGCTTAACGGCGCAACCTTGGTTGGTTAAACCGAATCATCGTGAGTTGGAAGCCTGGATTGGTCATGCGCTGCCGACCTTGGACGACATTATCGCGGCGGCGAAAAAACTGAAAGCACAAGGCATTGCTAACGTGATTATTTCCATGGGCGCCAACGGTTCGTTGTGGTTGAGCGATACAGCCGTCGTACAGGCGCAACCGCCGAAATGCGAAAACGTGGTCAGCACCGTGGGCGCGGGCGATTCTATGGTGGCGGGCTTGATTTACGGCGTAATTAACGGCTTGCCGCAACAGCAAACGCTTGCCTTCGCCAGCGCGGTATCCGCCTTTGCCGTGTCGCAAAGTAACGTAGGTATTTCAGACCGCAGCTTACTTGAACCGATTTTAAACAATGTCAAAATCACTGTCATTGAGGGA","","","33277","MAKVATITLNSAYDLVGRLKRIELGEVNTVETLGFFPAGKGINVAKVLKDLDVDVTVGGFLGEDNQGDFVTLFDKLGLQDKFQRVPGKTRINVKITETEADVTDLNFLGYKISADAWQQFVTDSLAYCKAFDIVAVCGSLPRGVTPELFADWLKQLHQAGVKVVLDSSNAALTAGLTAQPWLVKPNHRELEAWIGHALPTLDDIIAAAKKLKAQGIANVIISMGANGSLWLSDTAVVQAQPPKCENVVSTVGAGDSMVAGLIYGVINGLPQQQTLAFASAVSAFAVSQSNVGISDRSLLEPILNNVKITVIEG","226621","","1-phosphofructokinase; tagatose-6-phosphate kinase","Cytoplasm","","
InterPro
IPR002173
Family
Carbohydrate kinase, PfkB
PS00584\"[249-262]TPFKB_KINASES_2
InterPro
IPR011611
Domain
PfkB
PF00294\"[7-298]TPfkB
noIPR
unintegrated
unintegrated
G3DSA:3.40.1190.20\"[5-306]Tno description
PTHR10584\"[7-300]TSUGAR KINASE RELATED
PTHR10584:SF37\"[7-300]TPHOSPHOFRUCTOKINASE(PFK1)


","No hits to the COGs database.","Significant hit ( 1.2e-09) to 2/2 blocks of the IPB002173 family, which is described as \"PfkB family of carbohydrate kinases\". Interpro entry for IP:IPR002173. IPB002173A 37-52 0.051 IPB002173B 248-262 8.5e-06","Residues 178 to 229 match (1e-10) PD:PD457578 which is described as KINASE PROTEOME COMPLETE TRANSFERASE 1-PHOSPHOFRUCTOKINASE TAGATOSE-6-PHOSPHATE 1-PHOSPHATE FRUCTOSE FRUCTOSE-1-PHOSPHATE METABOLISM ","","","","","Thu Feb 13 15:15:16 2003","","","","","","","Thu Feb 13 15:15:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00333 is paralogously related to AA00212 (3e-07) and AA02384 (2e-04).","","","","","","Residues 3 to 298 (E-value = 2.4e-63) place AA00333 in the PfkB family which is described as pfkB family carbohydrate kinase (PF00294)","","","","","Orchard,L.M. and Kornberg,H.L.Sequence similarities between the gene specifying1-phosphofructokinase (fruK), genes specifying other kinases inEscherichia coli K12, and lacC of Staphylococcus aureusProc. R. Soc. Lond., B, Biol. Sci. 242 (1304), 87-90 (1990)PubMed: 1981619Kornberg HL.Routes for fructose utilization by Escherichia coli.J Mol Microbiol Biotechnol. 2001 Jul;3(3):355-9. Review.PMID: 11361065Tatusov,R.L., Mushegian,A.R., Bork,P., Brown,N.P., Hayes,W.S., Borodovsky,M., Rudd,K.E. and Koonin,E.V.Metabolism and evolution of Haemophilus influenzae deduced from a whole-genome comparison with Escherichia coliCurr. Biol. 6 (3), 279-291 (1996)MEDLINE; 96398784van Rooijen RJ, van Schalkwijk S, de Vos WM. Molecular cloning, characterization, and nucleotide sequence of the tagatose 6-phosphate pathway gene cluster of the lactose operon of Lactococcus lactisJ. Biol. Chem. 266 (11), 7176-7181 (1991)PubMed: 1901863","","Thu Feb 13 15:15:16 2003","1","","","" "AA00335","226629","228290","1662","ATGCATATTTATTTCACTCCATCCGCCGGTTTCGGCAATGCAAAAGCCTTTTTATTGCGCCAAATGCTCAGCGCGGCGGCGACCCAACATCAAATCGTGGATAACACCGATGCAGCAGAGTTGATTATCGTGCTTGGCGATCAGCTACCGAATAACCCGCAATTTCACGGCAAAAAAGTGTTTTTGGCGAAAATCGACGAGCACTTTAATGCGCCGGAACAGTTGTTAGACACCGCTATTCAACAGGCACAGGATTATGTTCCGCCAACGAAAAGTGCGGTCGTTTCTGACGGTAAAATTAAAAATATCGTAGCAGTGACCGCTTGCCCGACGGGCGTGGCGCATACCTTCATGTCTGCTGAAGCGATTGAAACCTACGCCAAACAACAAGGCTGGCAGGTGAAAGTGGAAACCCGCGGTCAGGTAGGTGCCGGTAATGAAATTACGCCGGAAGAAGTGGCGGCGGCGGATCTTGTCTTTGTGGCGGCGGATATTGATGTGCCGTTAGACAAATTCAAAGGCAAATTAATGTACCGCACTTCCACCGGGCTTGCCTTGAAGAAAACCGCGCAGGAATTTGAAAAAGCCTTCAAAGAAGCCAAAGTGTTTGATGGCGGAGCGGCACAAGTGGGCGCAAAAGCGGAAGAAAGCGGCGAGAAGAAAGGCGTGTACAAACACCTGATGACCGGCGTATCGCACATGTTGCCGTTGGTGGTGGCGGGCGGTTTGCTGATCGCCATTTCCTTCATGTTCGGGATTGAAGCGTTTAAAGACGAAACCATCGCAGGCGGCTTGCCGAAAGCCTTAATGGACATCGGTGGTGGCGCAGCGTTCCACTTAATGATCGCCGTCTTCGCCGGCTATGTGGCGTTTTCTATTGCCGACCGTCCGGGGCTGGCGGTCGGTTTAATCGGCGGTATGCTTGCCACCATGGCGGGCGCGGGGATTTTGGGCGGGATTATCGCCGGTTTCCTTGCGGGTTATGTGGTGAAAAGCTTGAACAACGCCATTAAATTGCCACCAAGTTTAACTTCTTTAAAACCAATTTTGATTTTACCGCTACTTGGCACGCTCATTGTGGGCTTGGCGATGATTTACATCATTAACCCACCGGTTGCCAAAATTATGGCGGCGTTAAGTGATTGGCTGAAATCTATAGGAGATGTAAATGCCATCGTGCTCGGGGTAATTATCGGCAGCATGATGTGTATTGATATGGGCGGTCCGGTAAACAAAGCGGCTTACACCTTCTCGGTAGGTCTGTTGGCGTCACAGATTCACACTCCGATGGCCGCCGCCATGGCTGCCGGTATGGTGCCGCCAATTGGCATGGCAATCGCTACTTGGTTAGCACGTAATAAATTCACCGCCAATCAGTGTGATGCAGGGAAAGCCTCTTTCGTACTGGGATTATGCTTTATCTCTGAAGGGGCGTTGCCGTTCGTGGCAGCAGATCCGCTCCGCGTGATTATCAGTTCCGTGTTAGGCGGCGCTACCGCAGGGGCAATTTCCATGAGCTGCGGCATTGCGCTACAAGCGCCGCACGGCGGTTTATTCGTGATCCCGTTTGTCTCCGAACCGTTGATGTACCTCAGCGCCATCGCTATCGGCTCTGTCGTGACCGGCGTAGTGTATGCGGTGATTAAACCAAAAGCAGAAGCA","","","58767","MHIYFTPSAGFGNAKAFLLRQMLSAAATQHQIVDNTDAAELIIVLGDQLPNNPQFHGKKVFLAKIDEHFNAPEQLLDTAIQQAQDYVPPTKSAVVSDGKIKNIVAVTACPTGVAHTFMSAEAIETYAKQQGWQVKVETRGQVGAGNEITPEEVAAADLVFVAADIDVPLDKFKGKLMYRTSTGLALKKTAQEFEKAFKEAKVFDGGAAQVGAKAEESGEKKGVYKHLMTGVSHMLPLVVAGGLLIAISFMFGIEAFKDETIAGGLPKALMDIGGGAAFHLMIAVFAGYVAFSIADRPGLAVGLIGGMLATMAGAGILGGIIAGFLAGYVVKSLNNAIKLPPSLTSLKPILILPLLGTLIVGLAMIYIINPPVAKIMAALSDWLKSIGDVNAIVLGVIIGSMMCIDMGGPVNKAAYTFSVGLLASQIHTPMAAAMAAGMVPPIGMAIATWLARNKFTANQCDAGKASFVLGLCFISEGALPFVAADPLRVIISSVLGGATAGAISMSCGIALQAPHGGLFVIPFVSEPLMYLSAIAIGSVVTGVVYAVIKPKAEA","228290","","PTS fructose-specific IIBC component","Inner membrane, Cytoplasm","","
InterPro
IPR003352
Domain
Phosphotransferase system, EIIC
PF02378\"[228-497]TPTS_EIIC
InterPro
IPR003353
Domain
Phosphotransferase system, fructose-specific IIB subunit
PF02379\"[102-203]TPTS_IIB_fruc
TIGR00829\"[104-187]TFRU: PTS system, Fru family, IIB component
InterPro
IPR006327
Domain
Phosphotransferase system, fructose IIC component
TIGR01427\"[209-549]TPTS_IIC_fructo: PTS system, Fru family, IIC
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[234-412]Tno description
InterPro
IPR013011
Domain
Phosphotransferase system, EIIB component, type 2
PS51099\"[103-198]TPTS_EIIB_TYPE_2
InterPro
IPR013014
Domain
Phosphotransferase system, EIIC component, type 2
PS51104\"[223-554]TPTS_EIIC_TYPE_2
noIPR
unintegrated
unintegrated
tmhmm\"[235-253]?\"[272-294]?\"[299-330]?\"[349-369]?\"[390-410]?\"[429-451]?\"[489-509]?\"[528-548]?transmembrane_regions


","BeTs to 8 clades of COG1299COG name: Phosphotransferase system, fructose-specific IIC componentFunctional Class: GThe phylogenetic pattern of COG1299 is ---------d-lb-efgh------twNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.3e-36) to 1/1 blocks of the IPB003353 family, which is described as \"PTS system, fructose specific IIB domain\". Interpro entry for IP:IPR003353. IPB003353 103-152 1.3e-36","Residues 1 to 86 match (5e-11) PD:PD030288 which is described as COMPONENT IIBC PTS FRUCTOSE-SPECIFIC SYSTEM COMPLETE PROTEOME TRANSFERASE PHOSPHOTRANSFERASE SUGAR ","","","","","","","","","","","","Wed Feb 19 14:20:13 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00335 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 228 to 496 (E-value = 4.6e-53) place AA00335 in the PTS_EIIC family which is described as Phosphotransferase system, EIIC (PF02378)","","","","","Prior,T.I. and Kornberg,H.L.Nucleotide sequence of fruA, the gene specifying enzyme IIfru ofthe phosphoenolpyruvate-dependent sugar phosphotransferase systemin Escherichia coli K12J. Gen. Microbiol. 134 (Pt 10), 2757-2768 (1988)PubMed: 3076173Dobrynina OIu, Erlagaeva RS, Umiarov AM, Bol'shakova TN. [The multifunctional fructose-specific component of the phosphoenolpyruvate-dependent phosphotransferasesystem of Escherichia coli K12--fruA gene product] Mol Gen Mikrobiol Virusol. 2001;(4):18-22. Russian. PMID: 11816114 Kornberg HL. Routes for fructose utilization by Escherichia coli. J Mol Microbiol Biotechnol. 2001 Jul;3(3):355-9. Review. PMID: 11361065 ","","Wed Feb 19 14:20:13 2003","1","","","" "AA00337","228805","228404","402","TTGATGAATCCTTTTAAAGAAGGGCTTTATGTCAGTAAATCTTACGTGGCGCAGTACGGCATACCGAAAACGCCGAAAGCGTTGGCGGGACATAAACTCATCGGCTATCGCTTCATTTCCTCCAATCGCATTGAACCGCTGGTACTGGATATTGACGGGCAGGACACGGCGTTGGATATGGGTATGCCGTTATTTGTAACGACCCGGAAATCATCGCTGATGCCACTCGCGAAGGCTTGGACATCGGGCGTATTTTTGAAACCAGTCTGCAATTTTTCCCCGACAAAGCTCAATTTATCCCCGTGCTGCAAAAATACTGGCGTCAATCCCCCGCGCTTTATTTGTATTATTTACAACACAGTCAAAAGGCGAAAAAAGAGTAGGTGCTCATTGAATTTTTGT","","","15417","LMNPFKEGLYVSKSYVAQYGIPKTPKALAGHKLIGYRFISSNRIEPLVLDIDGQDTALDMGMPLFVTTRKSSLMPLAKAWTSGVFLKPVCNFSPTKLNLSPCCKNTGVNPPRFICIIYNTVKRRKKSRCSLNFC","228404","","conserved hypothetical protein","Periplasm","","No hits reported.","BeTs to 4 clades of COG0583COG name: Transcriptional regulatorFunctional Class: KThe phylogenetic pattern of COG0583 is a-m----q-drlbcefghsnuj----Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Thu Jan 23 11:57:04 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00337 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00339","228922","228827","96","TTGTTGATTCGTCATCTGGTGTTGCACATTGAGGTGTTAACCAACCTGATTGAAGATGGCTTTGATTTGGGCATTCGTTTCGGTAATCGGCTGAAT","","","3696","LLIRHLVLHIEVLTNLIEDGFDLGIRFGNRLN","228827","","hypothetical protein","Cytoplasm","No significant similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-16]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 14:00:58 2004","Sun Feb 22 14:00:58 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00339 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 14:00:58 2004","","","","","","","","","","","","","1","","","" "AA00340","228937","229485","549","ATGAAAAATGTACTTATCGTTTCAGGTCACCCGGATTCAAACCATTCTGTGGCAAATGTGGAAATTCTACAAGCGGTCGAAAACACGTTACCCGATGTAAAAATCCGTCGCTTAGACAGCCTTTACCCGACCTATAAATTTGATATTGACGCGGAACAATCGGTGATTTTGGAAGCGGACGTGATTGTGTTCCAATTCCCGTTCTCCTGGTATTCCGTACCGAGTAATGAAATTGTGAATCGACAAAGTTTTGTATACGGCTTTGCACACGGTTCAGCGGCAAAAATCGGCGGTAAAAAATTAATTATTTCCACCACCGGCGCACCAAATGAAGTGTATCAAAAAGACGGTTTCTTCAAACACACCGTGGAAGATTACTTGTCGCAATTTGAAACCTTCGCCACCTTATGTGCTTTGGACTATCAAGCGCTGGTCATCACCTGCGGCGTAAGCTATGCGGGACGAGACGAAGCGAAAGTCGCCGCACAAAAAGCCATGGCACCAGATCACGCGGCACGTTTAGTGGCGGTGATTGATAAGGCGACAGCG","","","20076","MKNVLIVSGHPDSNHSVANVEILQAVENTLPDVKIRRLDSLYPTYKFDIDAEQSVILEADVIVFQFPFSWYSVPSNEIVNRQSFVYGFAHGSAAKIGGKKLIISTTGAPNEVYQKDGFFKHTVEDYLSQFETFATLCALDYQALVITCGVSYAGRDEAKVAAQKAMAPDHAARLVAVIDKATA","229485","","NADP(H) oxidoreductase (NAD(P)H dehydrogenase (quinone))","Cytoplasm","","
InterPro
IPR003680
Family
Flavodoxin-like fold
PF02525\"[2-179]TFlavodoxin_2
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.360\"[3-165]Tno description


","BeTs to 8 clades of COG2249COG name: Putative NADPH-quinone reductase (modulator of drug activity B)Functional Class: RThe phylogenetic pattern of COG2249 is ------------b-efgh-nuj---wNumber of proteins in this genome belonging to this COG is","","Residues 42 to 156 match (7e-10) PD:PD022346 which is described as COMPLETE PROTEOME OXIDOREDUCTASE NADPH PHOSPHODIESTERASE QUINONE DEHYDROGENASE REDUCTASE ACYL CARRIER ","","","","","","","","","","","","Fri Dec 6 13:06:12 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00340 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 176 (E-value = 6.9e-14) place AA00340 in the Flavodoxin_2 family which is described as Flavodoxin-like fold (PF02525)","","","","","","","","1","","","" "AA00341","229528","229863","336","ATGTACATCATCAACATCACTGTAAACCCCTCCGTTTCTGAAGAAAAACAAAACGAGTTATTCCCAATCCATGTGGAATGGTTCAAAAAATACTTCCAAGCAGGCAAATTTTTAATGCTCGGTCCTTACATCGACACCGATGCCCATTCAGGCGTCATTTTCGCGAAAACCGAAAGCCGTGAAGCATTCCAAAAAATCTTGGAAGAAGATTGCTACTACCCGGATTTCGCCAAATATGAAATCCGCGAATTCGCCCCGAAAATGATCGCGGCGGATATTAGTAAAGCAAAGTTCAGGATTGGGTTTGGTGATTGCTTTGGAAATGGTAAAACATTA","","","12932","MYIINITVNPSVSEEKQNELFPIHVEWFKKYFQAGKFLMLGPYIDTDAHSGVIFAKTESREAFQKILEEDCYYPDFAKYEIREFAPKMIAADISKAKFRIGFGDCFGNGKTL","229863","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Fri Dec 6 14:44:39 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00341 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00342","229835","229999","165","GTGATTGCTTTGGAAATGGTAAAACATTATGATGACACATTGATGCTTAAAGGCAGCAAAAATTCGAAACAGAGCTGTTGGTGGGGACTTGGCTGCCGCGTGGATAGTACAAATAATGCCCTATCTTTTTTGTCTGTGGGTAATTTATTACCACTGATTATCGTA","","","6063","VIALEMVKHYDDTLMLKGSKNSKQSCWWGLGCRVDSTNNALSFLSVGNLLPLIIV","229999","","hypothetical protein","Cytoplasm","No significant similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 14:02:48 2004","Sun Feb 22 14:02:48 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00342 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 14:02:48 2004","","","","","","","","","","","","","1","","","" "AA00343","230048","230713","666","ATGGCAATGACCGCACAAGCCGCGCCGATTATCAATCTGTTTGAACTGGGCATTCAGCCGGGCAAAAACGCGCAATATGAAGCAGTGGGCGAACAGAACATCAAAACCTCGATGCAAACGGAAAAGGGCACACTGGCAATGCATTCGGTGAAACAAAAAGCTGATGCGAATATGGCGTATATGGTGGAAATTTATGCCGATCAAAACGCCTACGAAATCCACCGCACTTCACCGCAATACAAGGCGTTTTTAACCGCCTCTCCTGAGATTTTAACGGATCACAAAAAGCGCACAGTGCTAACTCCGCAATTTTTAGCCGATAAGAAAGTTGAGCAAACTGCCAACACCCGGACGAATTTAGTCATGGTGGAGGTGAAACCGTCGGAAAATGACAAATTTAAAGCTATTGTGCTGGCTGAAATGGCGCAATCGTTAAAAGTAGAAGACGGCGTCATTGCAATGTATGCCGCCACAGCACAGGAAAATCCGAATAAATGGATGTTCTTTGAAATCTATGCAAACGACGATGCCTATGCGGCACACCGAGAAACACCGCATTTTAAAGATTATTTGAAACAAACCGCCGAGATGTTGGTAGATAAGCAAAGTATCGAGATTCAACCGACATATCTAGGGAACAAAGGTGGTTTGCAGTTTGAAAAACCA","","","26261","MAMTAQAAPIINLFELGIQPGKNAQYEAVGEQNIKTSMQTEKGTLAMHSVKQKADANMAYMVEIYADQNAYEIHRTSPQYKAFLTASPEILTDHKKRTVLTPQFLADKKVEQTANTRTNLVMVEVKPSENDKFKAIVLAEMAQSLKVEDGVIAMYAATAQENPNKWMFFEIYANDDAYAAHRETPHFKDYLKQTAEMLVDKQSIEIQPTYLGNKGGLQFEKP","230713","","conserved hypothetical protein (possible cytosolic protein)","Periplasm","","
InterPro
IPR007138
Domain
Antibiotic biosynthesis monooxygenase
PF03992\"[18-82]T\"[125-189]TABM
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.900\"[4-103]T\"[117-210]Tno description


","No hits to the COGs database.","Significant hit ( 6.5e-09) to 2/2 blocks of the IPB003771 family, which is described as \"DUF176\". Interpro entry for IP:IPR003771. IPB003771A 123-157 4.7e+02 IPB003771B 166-201 4.6e-09","Residues 9 to 95 match (7e-10) PD:PD596213 which is described as PROTEOME COMPLETE PLASMID ATU0206 RA0291 ","","","","","","","","","","","","Fri Dec 6 14:48:13 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00343 is paralogously related to AA02215 (6e-04).","","","","","","Residues 125 to 189 (E-value = 2.6e-09) place AA00343 in the ABM family which is described as Antibiotic biosynthesis monooxygenase (PF03992)","","","","","","","","1","","","" "AA00344","231158","231565","408","ATGGCATTAGAGATTGAGAAAAAGAAAAATGCACCTGAGGCTCCCATTGAAAAAGCTAAGGGATTAAACATTTTTTTATGGTTGCTGACAGTATTGATCATTGCAGTGGCCGCATTTGGTAATATTTATTTCCAAGACCAATATTCTACGCCGATTCGCGTGGTTGCAATTGTTGTCTTGCTGTCAGTCTCTTTAGGTGTCGCAGCGAGCACCAACCAAGGCGGAAAAGCCCTTGGCTTCTTTAAAGATGCCCGTACCGAATTGCGCAAAATTGTCTGGCCGACCCGTCCGGAAGCGACGCAAACCACATTGATGGTTGTTGGTGTCACCGTGTTTGTGTCTTTAATCCTTTGGGGGTTAGATTCAATTATCGTCAGCATTATTACCTTTTTAACCGACTGGAGATTC","","","14992","MALEIEKKKNAPEAPIEKAKGLNIFLWLLTVLIIAVAAFGNIYFQDQYSTPIRVVAIVVLLSVSLGVAASTNQGGKALGFFKDARTELRKIVWPTRPEATQTTLMVVGVTVFVSLILWGLDSIIVSIITFLTDWRF","231565","","preprotein translocase secE subunit","Inner membrane, Cytoplasm","","
InterPro
IPR001901
Family
Protein secE/sec61-gamma protein
PF00584\"[76-132]TSecE
PS01067\"[80-108]TSECE_SEC61G
InterPro
IPR005807
Family
SecE subunit of protein translocation complex
PR01650\"[53-74]T\"[74-94]T\"[98-118]T\"[118-134]TSECETRNLCASE
TIGR00964\"[77-133]TsecE_bact: preprotein translocase, SecE sub
noIPR
unintegrated
unintegrated
signalp\"[1-37]?signal-peptide
tmhmm\"[24-44]?\"[54-72]?\"[111-131]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 2e-20) to 1/1 blocks of the IPB001901 family, which is described as \"Protein secE/sec61-gamma protein\". Interpro entry for IP:IPR001901. IPB001901 80-121 1.8e-20","Residues 80 to 128 match (2e-12) PD:PD293146 which is described as SECE COMPLETE PREPROTEIN PROTEOME SUBUNIT TRANSLOCASE TRANSMEMBRANE TRANSLOCATION INNER MEMBRANE ","","","","","","","","","","","","Fri Dec 6 14:49:34 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00344 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 76 to 132 (E-value = 4.5e-21) place AA00344 in the SecE family which is described as SecE/Sec61-gamma subunits of protein translocation complex (PF00584)","","","","","Secondary Laboratory Evidence:Schatz,P.J., Riggs,P.D., Jacq,A., Fath,M.J. and Beckwith,J.The secE gene encodes an integral membrane protein requiredfor protein export in Escherichia coli. Genes Dev. 3(7): 1035-1044, 1989. PubMed: 2673920. Breyton C, Haase W, Rapoport TA, Kuhlbrandt W, Collinson I.Three-dimensional structure of the bacterialprotein-translocation complex SecYEG. Nature. 2002 Aug 8;418(6898):662-5. PMID: 12167867 Veenendaal AK, Van Der Does C, Driessen AJ. The Core of the Bacterial Translocase Harbors a TiltedTransmembrane Segment 3 of SecE. J Biol Chem. 2002 Sep 27;277(39):36640-5. PMID: 12138117 ","","Wed Jan 22 17:15:57 2003","1","","","" "AA00345","231570","232118","549","ATGACCGAAACCGCAAACAAAAAACGTTGGTATGTATTGCAGGCGTTCTCCGGTTTTGAAGCACGAGTAGCAACCACATTGCGTGAATACATTAAACTTCACAATATGGAAGATCAATTCGGCGAGGTGTTGGTGCCGACGGAAGAGGTTGTTGAAAATGTAGCGGGTAAACGTCGTAAAAGCGAACGTAAATATTTCCCGGGTTATGTGCTGGTACAGATGGAAATGAATGATGACACTTGGCACTTGGTGCGCAGTGTGCCGCGGGTGATGGGCTTTATCGGCGGTACACCAGATAAGCCGGCACCAATCAGCAGTCGTGAAGCGGATATTATTTTAAATCGCTTGGAACAAAGCAACGACAAACCGAAACCAAGAACGACATTCCAGCCGGGCGAAGAAGTGCGTGTAACCGAAGGGCCGTTTATAGATTTCAACGGTACAGTGGAAGAGGTCGATTACGAAAAAGGTCGTTTGAAAGTGTCCGTGTCTATTTTCGGCCGTGCTACGCCGGTTGAACTTGAGTTCGGTCAGGTAGAAAAAAATAAC","","","20940","MTETANKKRWYVLQAFSGFEARVATTLREYIKLHNMEDQFGEVLVPTEEVVENVAGKRRKSERKYFPGYVLVQMEMNDDTWHLVRSVPRVMGFIGGTPDKPAPISSREADIILNRLEQSNDKPKPRTTFQPGEEVRVTEGPFIDFNGTVEEVDYEKGRLKVSVSIFGRATPVELEFGQVEKNN","232118","","transcription antitermination protein","Cytoplasm","","
InterPro
IPR001062
Family
Bacterial transcription antitermination protein NusG
PR00338\"[62-74]T\"[140-155]T\"[158-174]TNUSGTNSCPFCT
PF02357\"[8-107]TNusG
TIGR00922\"[10-182]TnusG: transcription termination/antitermina
PS01014\"[165-174]TNUSG
InterPro
IPR003257
Domain
Bacterial NusG ribosomal protein
PD005267\"[68-174]TNUSG_METJA_Q57818;
InterPro
IPR005824
Domain
KOW
PF00467\"[129-166]TKOW
InterPro
IPR006645
Domain
NGN
SM00738\"[7-116]TNGN
InterPro
IPR006646
Domain
KOW (Kyrpides, Ouzounis, Woese) motif
SM00739\"[128-155]TKOW
InterPro
IPR014722
Domain
Translation protein SH3-like, subgroup
G3DSA:2.30.30.30\"[120-182]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.940\"[7-120]Tno description


","BeTs to 22 clades of COG0250COG name: Transcription antiterminatorFunctional Class: KThe phylogenetic pattern of COG0250 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 4.5e-82) to 4/4 blocks of the IPB001062 family, which is described as \"Bacterial transcription antitermination protein, nusG\". Interpro entry for IP:IPR001062. IPB001062A 10-24 1.6e-07 IPB001062B 46-95 7.5e-36 IPB001062C 129-145 9.3e-08 IPB001062D 147-181 4.1e-27","Residues 113 to 147 match (1e-07) PD:PD575416 which is described as TRANSCRIPTION ANTITERMINATION PROTEOME COMPLETE NUSG TERMINATION ","","","","","","","","","","","","Fri Dec 6 14:56:41 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00345 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 129 to 166 (E-value = 1.2e-10) place AA00345 in the KOW family which is described as KOW motif (PF00467)","","","","","Steiner T, Kaiser JT, Marinkovic S, Huber R, Wahl MC. Crystal structures of transcription factor NusG in light ofits nucleic acid- and protein-binding activities. EMBO J. 2002 Sep 2;21(17):4641-53. PMID: 12198166 Zhou Y, Filter JJ, Court DL, Gottesman ME, Friedman DI. Requirement for NusG for transcription antitermination in vivoby the lambda N protein. J Bacteriol. 2002 Jun;184(12):3416-8. PMID: 12029062 Downing,W.L., Sullivan,S.L., Gottesman,M.E. and Dennis,P.P.Sequence and transcriptional pattern of the essentialEscherichia coli secE-nusG operon. J. Bacteriol. 172(3): 1621-1627.1990 PubMed: 2137819.","","Fri Dec 6 14:56:41 2002","1","","","" "AA00347","232277","232702","426","ATGGCAAAAAAAGTCCAAGCCTACGTTAAGCTGCAAGTTGCAGCCGGTATGGCAAACCCGTCTCCACCGGTCGGTCCCGCATTAGGTCAACAAGGTGTGAATATCATGGAATTCTGTAAAGCATTTAACGCTCGTACCGAGAGCTTAGAAAAAGGTTTACCGATTCCGGTTGTTATCACTGTTTATGCAGACCGTTCATTCACTTTCGTAACCAAAACTCCACCGGCAGCCGTGTTATTGAAAAAAGCGGCAGGCATCAAATCCGGTTCCGGTAAACCGAATAAGGATAAAGTGGGTAAAGTAACTCTAGATCAAATCCGTCAAATCGCTGAAACCAAAGCAGCCGATATGACCGGTGCAACTATCGAAACCAAAATGAAATCAATCGCCGGTACTGCTCGTTCAATGGGCTTAGTGGTAGAGGAG","","","14902","MAKKVQAYVKLQVAAGMANPSPPVGPALGQQGVNIMEFCKAFNARTESLEKGLPIPVVITVYADRSFTFVTKTPPAAVLLKKAAGIKSGSGKPNKDKVGKVTLDQIRQIAETKAADMTGATIETKMKSIAGTARSMGLVVEE","232702","","50S ribosomal protein L11","Periplasm, Cytoplasm","","
InterPro
IPR000911
Family
Ribosomal protein L11
PD001367\"[9-73]TRL11_HAEIN_P44351;
G3DSA:1.10.10.250\"[72-141]Tno description
PIRSF002179\"[7-142]TRibosomal protein L11/L12
PTHR11661\"[1-142]T60S RIBOSOMAL PROTEIN L12
PF00298\"[72-140]TRibosomal_L11
PF03946\"[8-67]TRibosomal_L11_N
SM00649\"[9-141]TRL11
PS00359\"[127-142]TRIBOSOMAL_L11
InterPro
IPR006519
Family
Ribosomal protein L11, bacterial
PTHR11661:SF1\"[1-142]T50S ROBOSOMAL PROTEIN L11
TIGR01632\"[3-142]TL11_bact: ribosomal protein L11
noIPR
unintegrated
unintegrated
G3DSA:3.30.1550.10\"[2-72]Tno description
PIRSF500072\"[1-142]TRibosomal protein L11


","BeTs to 26 clades of COG0080COG name: Ribosomal protein L11Functional Class: JThe phylogenetic pattern of COG0080 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.8e-70) to 3/3 blocks of the IPB000911 family, which is described as \"Ribosomal protein L11\". Interpro entry for IP:IPR000911. IPB000911A 9-41 5.1e-23 IPB000911B 55-93 7.9e-29 IPB000911C 108-141 3.3e-16","Residues 18 to 74 match (1e-07) PD:PD300659 which is described as RIBOSOMAL L11 MITOCHONDRION ","","","","","","","","","","","","Fri Dec 6 14:58:36 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00347 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 72 to 140 (E-value = 4.7e-36) place AA00347 in the Ribosomal_L11 family which is described as Ribosomal protein L11, RNA binding domain (PF00298)","","","","","Dognin,M.J. and Wittmann-Liebold,B. Purification and primary structure determination of theN-terminal blocked protein, L11, from Escherichia coli ribosomes Eur. J. Biochem. 112 (1), 131-151 (1980) PubMed: 7004866 Choli,T. Structural properties of ribosomal protein L11 fromEscherichia coli Biochem. Int. 19 (6), 1323-1338 (1989) PubMed: 2483975 ","","Fri Dec 6 14:58:36 2002","1","","","" "AA00348","232710","233396","687","ATGGCTAAATTGACTAAAAAAATGAAAGCAATCAAAGCTGGCGTGGATTCTACTAAAGCATACGAAATCAACGAAGCTATCGCATTATTAAAGCAATTCGCGACCGCTAAATTCGTTGAAAGCGTTGACGTTGCCGTAAACTTGGGTATCGACCCACGTAAATCCGATCAAAACGTGCGTGGCGCAACTGTATTACCACATGGTACCGGTCGTGAAGTTCGCGTTGCTGTGTTCACTCAAGGTGCAAACGCAGAAGCGGCTAAAGCAGCCGGTGCAGATTTAGTCGGTATGGAAGATTTAGCAGAGCAAATTAAGAAAGGCGAAATGAACTTTGACGTTGTTATCGCTTCTCCTGATGCAATGCGTGTTGTCGGTCAATTAGGTCAAGTATTAGGCCCGCGCGGCTTAATGCCAAACCCGAAAGTGGGTACCGTAACACCAAACGTTGCCGAAGCGGTTAAAAACGCGAAATCCGGTCAAATCCGTTATCGTAACGATAAAAACGGTATCATCCACACCACTATCGGTAAAGCAAACTTCTCCGAAGATCAATTAAAAGAAAACCTTCAAGCGCTGTTAGCCGCTTTAACCAAAGCGAAACCCACAACATCCAAAGGTATCTTCATTAAGAAAGTGAGCCTTTCTACCACGATGGGTGCCGGTGTAGCGATTGATCAAGATTCACTT","","","24139","MAKLTKKMKAIKAGVDSTKAYEINEAIALLKQFATAKFVESVDVAVNLGIDPRKSDQNVRGATVLPHGTGREVRVAVFTQGANAEAAKAAGADLVGMEDLAEQIKKGEMNFDVVIASPDAMRVVGQLGQVLGPRGLMPNPKVGTVTPNVAEAVKNAKSGQIRYRNDKNGIIHTTIGKANFSEDQLKENLQALLAALTKAKPTTSKGIFIKKVSLSTTMGAGVAIDQDSL","233396","","50S ribosomal protein L1","Periplasm, Cytoplasm","","
InterPro
IPR002143
Family
Ribosomal protein L1
PD001314\"[15-224]TRL1_HAEIN_P44342;
PF00687\"[15-221]TRibosomal_L1
PS01199\"[121-139]TRIBOSOMAL_L1
InterPro
IPR005878
Family
Ribosomal protein L1, bacterial and chloroplast form
PTHR23105:SF5\"[21-225]T50S RIBOSOMAL PROTEIN L1P
TIGR01169\"[3-229]TrplA_bact: ribosomal protein L1
noIPR
unintegrated
unintegrated
G3DSA:3.30.190.20\"[2-228]Tno description
PTHR23105\"[21-225]TRIBOSOMAL PROTEIN L7AE FAMILY MEMBER


","No hits to the COGs database.","Significant hit ( 3.1e-86) to 5/5 blocks of the IPB002143 family, which is described as \"Ribosomal protein L1\". Interpro entry for IP:IPR002143. IPB002143A 51-100 1.2e-33 IPB002143B 111-121 0.00046 IPB002143C 127-140 8.4e-11 IPB002143D 157-201 7.5e-26 IPB002143E 208-224 1.7e-06","Residues 6 to 228 match (3e-92) PD:PD001314 which is described as RIBOSOMAL L1 50S PROTEOME COMPLETE RRNA-BINDING L10A 60S L1P CHLOROPLAST ","","","","","","","","","","","","Fri Dec 6 15:00:46 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00348 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 15 to 221 (E-value = 1.1e-128) place AA00348 in the Ribosomal_L1 family which is described as Ribosomal protein L1p/L10e family (PF00687)","","","","","Brauer,D. and Ochsner,I. The primary structure of protein L1 from the large ribosomalsubunit of Escherichia coli. FEBS Lett. 96(2): 317-321.1978. PubMed: 365581.Comment:","","Fri Dec 6 15:00:46 2002","1","","","" "AA00349","233414","233587","174","ATGAAAAATAACCGCACTTTTAAAAGTAAAAGTGCGGTTATTTTTTGCGACGTTTATCACGGGCGAATTGATGATTTTTTATCACCAGGCTTTACAAATGCCGTTTCGGTCGTTATAATCCATGTCCCTTTTAGACCGCAGTTTACTTGCGGTTTAGCATTTCTGGTTGGTGCT","","","6416","MKNNRTFKSKSAVIFCDVYHGRIDDFLSPGFTNAVSVVIIHVPFRPQFTCGLAFLVGA","233587","","hypothetical protein","Cytoplasm","No significant similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 14:04:23 2004","Sun Feb 22 14:04:23 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00349 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 14:04:23 2004","","","","","","","","","","","","","1","","","" "AA00350","233761","234249","489","ATGGCATTAAATCTTCAAGACAAACAAGCAATTGTTGCCGAAGTAAATGAAGCAGCCAAAGGTGCCCTTTCTGCCGTGATCGCGGATTCCCGTGGTGTCACCGTAGATAAAATGACCGAATTGCGTAAATCTGCACGCGAAGCCGGTGTTTCTATGCGCGTTGTTCGTAATACTTTATTACGTCGTGCGGTAGAAGGCACTGAATTCGAGTGTTTGAAAGACGCTTTCACCGGTCCGACACTTATCGCATTCTCTAATGAACATCCTGGTGCTGCAGCACGTTTGTTCAAAGAATTTGCTAAAGCAAACGATAAGTTTGAACTTAAAGGTGCAGCCTTTGAAGGTAAGATCCAAGATGTTGAATTCTTAGCAACATTACCGACTTACGACGAAGCAATTGCACGTTTAATGGGCACAATGAAAGAAGCTGCGGCAGGCAAACTTGTTCGCACTTTTGCGGCATTACGCGACAAATTACAAGAAGCGGCT","","","17619","MALNLQDKQAIVAEVNEAAKGALSAVIADSRGVTVDKMTELRKSAREAGVSMRVVRNTLLRRAVEGTEFECLKDAFTGPTLIAFSNEHPGAAARLFKEFAKANDKFELKGAAFEGKIQDVEFLATLPTYDEAIARLMGTMKEAAAGKLVRTFAALRDKLQEAA","234249","","50S ribosomal protein L10","Cytoplasm","","
InterPro
IPR001790
Family
Ribosomal protein L10
PF00466\"[3-101]TRibosomal_L10
InterPro
IPR002363
Family
Eubacterial ribosomal protein L10
PS01109\"[8-42]TRIBOSOMAL_L10


","BeTs to 19 clades of COG0244COG name: Ribosomal protein L10Functional Class: JThe phylogenetic pattern of COG0244 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-51) to 3/3 blocks of the IPB002363 family, which is described as \"Eubacterial ribosomal protein L10\". Interpro entry for IP:IPR002363. IPB002363A 15-65 2e-28 IPB002363B 88-103 2.7e-07 IPB002363C 105-143 3.6e-13Significant hit ( 4.3e-21) to 3/3 blocks of the IPB001790 family, which is described as \"Ribosomal protein L10\". Interpro entry for IP:IPR001790. IPB001790A 32-63 1.3e-15 IPB001790B 71-92 0.15 IPB001790C 117-132 1.6","Residues 121 to 162 match (7e-11) PD:PD398695 which is described as RIBOSOMAL COMPLETE PROTEOME 50S L10 L8 REGULATION RNA-BINDING TRANSLATION REPRESSOR ","","","","","","","","","","","","Fri Dec 6 15:05:25 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00350 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 101 (E-value = 3.5e-40) place AA00350 in the Ribosomal_L10 family which is described as Ribosomal protein L10 (PF00466)","","","","","Heiland,I., Brauer,D. and Wittmann-Liebold,B. Primary structure of protein L10 from the large subunit of Escherichia coli ribosomes Hoppe-Seyler's Z. Physiol. Chem. 357 (12), 1751-1770 (1976) PubMed: 797648 ","","Fri Dec 6 15:05:57 2002","1","","","" "AA00351","234295","234672","378","TTGATTGTTATGTCATTAACTAACGAACAAATCATTGAAGCGATTGCTTCTAAATCTGTAACCGAAATCGTTGAATTAATCGCAGCGATGGAAGAAAAATTCGGCGTTTCAGCAGCGGCAGCAGTAGCAGCAGCTCCGGCAGGTGGCGCAGTAGCGGCAGCAGAAGAGAAAACTGAATTCGACGTAGTTCTTGCTGAAGCAGGCGCTAACAAAGTAGCGGTAATCAAAGCAGTACGTGGTGCAACCGGTTTAGGCTTGAAAGAAGCTAAAGACTTAGTTGAATCTGCACCGGCTGTATTGAAAGAAGGTATCGCTAAAGCAGAAGCAGAAGCACTTAAGAAAGAATTAGAAGAAGCTGGCGCGAAAGTAGAAATCAAA","4.50","-6.99","12709","LIVMSLTNEQIIEAIASKSVTEIVELIAAMEEKFGVSAAAAVAAAPAGGAVAAAEEKTEFDVVLAEAGANKVAVIKAVRGATGLGLKEAKDLVESAPAVLKEGIAKAEAEALKKELEEAGAKVEIK","","","50S ribosomal protein L7/L12","Cytoplasm, Inner membrane","AA00351 has significant similarity to the Haemophilus ducreyi gene HD1879, a 50S ribosomal protein L7/L12 (2e-53).AA00351 has significant similarity to the Haemophilus influenzae Rd gene 16272584 (2e-55). ","
InterPro
IPR000206
Family
Ribosomal protein L7/L12
TIGR00855\"[4-126]TL12: ribosomal protein L7/L12
InterPro
IPR013823
Domain
Ribosomal protein L7/L12, C-terminal
PD001326\"[67-99]TRL7_PASMU_Q9CK90;
PF00542\"[59-126]TRibosomal_L12
InterPro
IPR014719
Domain
Ribosomal protein L7/L12, C-terminal/adaptor protein ClpS-like
G3DSA:3.30.1390.10\"[53-126]Tno description
noIPR
unintegrated
unintegrated
PTHR11809\"[9-126]TRIBOSOMAL PROTEIN L7/L12


","BeTs to 19 clades of COG0222COG name: Ribosomal protein L7/L12Functional Class: JThe phylogenetic pattern of COG0222 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.6e-67) to 3/3 blocks of the IPB000206 family, which is described as \"Ribosomal protein L7/L12 C-terminal domain\". Interpro entry for IP:IPR000206. IPB000206A 9-40 3.9e-16 IPB000206B 55-70 5.9e-10 IPB000206C 71-123 5.7e-39","Residues 59 to 98 match (9e-09) PD:PD001326 which is described as RIBOSOMAL 50S L7/L12 PROTEOME COMPLETE CHLOROPLAST L12 TRANSIT PEPTIDE PRECURSOR ","Fri Feb 27 08:51:51 2004","Sat Feb 28 16:45:49 2004","Sat Feb 28 16:45:49 2004","Sat Feb 28 16:45:49 2004","Fri Feb 27 08:51:51 2004","Fri Feb 27 08:51:51 2004","Fri Feb 27 08:51:51 2004","Fri Feb 27 08:51:51 2004","Fri Feb 27 08:51:51 2004","Fri Feb 27 08:51:51 2004","Fri Feb 27 08:51:51 2004","Fri Feb 27 08:51:51 2004","Fri Feb 27 08:52:10 2004","Fri Feb 27 08:51:51 2004","Fri Feb 27 08:51:51 2004","Fri Feb 27 08:51:51 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00351 is paralogously related to AA02832, an outer membrane integrity protein (0.001).AA00351 is paralogously related to AA02832 (7e-04).","Fri Feb 27 08:51:51 2004","Fri Feb 27 08:52:10 2004","pdb1CTF1CTF L7(SLASH)*L12 50 S RIBOSOMAL PROTEIN 81.1 6e-17pdb1DD31DD3-A CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L12 80.8 8e-17pdb1CTF1CTF L7(SLASH)*L12 50 S RIBOSOMAL PROTEIN 80.9 7e-17pdb1DD41DD4-C CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L12 53.2 2e-08pdb1DD31DD3-C CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L12 53.2 2e-08pdb1DD31DD3-A CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L12 113.0 8e-27pdb1CTF1CTF L7(SLASH)*L12 50 S RIBOSOMAL PROTEIN 80.9 7e-17pdb1DD41DD4-C CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L12 51.2 6e-08pdb1DD31DD3-C CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L12 51.2 6e-08","","","Residues 59 to 126 (E-value = 3.7e-36) place AA00351 in the Ribosomal_L12 family which is described as Ribosomal protein L7/L12 C-terminal domain (PF00542)","Fri Feb 27 08:51:51 2004","","","","Pettersson,I., Hardy,S.J.S. and Liljas,A. .The ribosomal protein L8 is a complex L7/L12 and L10.FEBS Lett. 64(1): 135-138.1976PubMed: 773698.","","Fri Feb 27 08:52:10 2004","1","Fri Feb 27 08:51:51 2004","","" "AA00353","234728","234291","438","ATGGTTACCCACCAGCCATTTAGCCTGAGAAACAGGACGAAATCGAATCAAAATTATTTGATTTCTACTTTCGCGCCAGCTTCTTCTAATTCTTTCTTAAGTGCTTCTGCTTCTGCTTTAGCGATACCTTCTTTCAATACAGCCGGTGCAGATTCAACTAAGTCTTTAGCTTCTTTCAAGCCTAAACCGGTTGCACCACGTACTGCTTTGATTACCGCTACTTTGTTAGCGCCTGCTTCAGCAAGAACTACGTCGAATTCAGTTTTCTCTTCTGCTGCCGCTACTGCGCCACCTGCCGGAGCTGCTGCTACTGCTGCCGCTGCTGAAACGCCGAATTTTTCTTCCATCGCTGCGATTAATTCAACGATTTCGGTTACAGATTTAGAAGCAATCGCTTCAATGATTTGTTCGTTAGTTAATGACATAACAATCAATTCC","","","14678","MVTHQPFSLRNRTKSNQNYLISTFAPASSNSFLSASASALAIPSFNTAGADSTKSLASFKPKPVAPRTALITATLLAPASARTTSNSVFSSAAATAPPAGAAATAAAAETPNFSSIAAINSTISVTDLEAIASMICSLVNDITINS","234291","","hypothetical protein","Extracellular, Periplasm","No significant similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 14:07:01 2004","Sun Feb 22 14:07:01 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00353 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 14:07:01 2004","","","","","","","","","","","","","1","","","" "AA00354","234922","234830","93","GTGACCCACAATCAACACACAATAATTTGGGCAAATATTGGTGATAATGTATTAGATACCGTTTTAGATGACCGCACTATGAACCTTACTTCT","","","3490","VTHNQHTIIWANIGDNVLDTVLDDRTMNLTS","234830","","hypothetical protein","Cytoplasm","No significant similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 14:08:45 2004","Sun Feb 22 14:08:45 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00354 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 14:08:45 2004","","","","","","","","","","","","","1","","","" "AA00355","234946","238971","4026","ATGGTTTACTCCTATACCGAGAAAAAACGAATTCGTAAAGACTTCGGCAAACGTCCGCAAGTTTTAAATATTCCCTATTTATTAACAATCCAGATCGACTCTTTTGAGAAATTTATTAAAAGAGATCCGGATGGTCAACAAGGCTTAGAAGCCGCTTTCCGCTCCGTCTTCCCAATTGTCAGTACGAACGGAAATACCGAATTACAATATGTCAGCTATCAATTAGGCGAGCCTGTATTTGATGTGCGTGAATGTCAAATTCGCGGCACGACCTATGCGGCACCATTGCGTGTAAAATTGCGTTTAGTCAGCTATGACAAAGACGCAGCACCGGGCACGATCAAAGATATTAAAGAACAAGAAGTTTACATGGGTGAAATCCCGTTGATGACCGATAACGGTACTTTTGTGATTAACGGTACCGAGCGTGTTATCGTGTCTCAATTACACCGCAGTCCGGGTGTATTTTTTGATAGCGACAAAGGCAAAACCCACTCTTCAGGTAAAGTGCTTTATAATGCACGCATTATTCCTTACCGTGGTTCATGGTTGGATTTTGAGTTTGATCCGAAAGATAACTTATACGCACGTATTGACCGCCGTCGTAAATTACCGGCAACCATTATTTTGCGTGCTTTAGGCTACACCACCGAACAAATCTTAGATCTTTTCTTTTATAAAATTACTTTTGAAATCAAAGATAACAAATTGTTGATGACGTTAGTGCCGGAACGCCTACGTGGTGAAACCGCCGCCTTTGATATTGAAACCAAAGGCAAGGTGTATGTAGAACGCGGTCGTCGTATTACCGCCCGTCACATTAAAGCGTTGGAAAAAGATAAAGTCACTCAGGTGGAAGTGCCAACCGAATATATTATCGGGAAAGTTGCCGCGAAAGATTATGTAGATTTAGAAACCGGCGAATTAATTTGCCCGGCGAATATGGAACTTTCTCTTGAATTATTGGCGAAATTGGCACAAGCCGGTTATACCACGCTGGAAACTCTATTTACCAATGACTTGGATTACGGTCCGTATATTTCCGAAACCCTGCGTGTTGATCCGTCGAACGATCGTTTAAGCGCTTTGGTGGAAATTTATCGCATGATGCGTCCGGGCGAACCACCGACAAAAGAAGCGGCGGAAGCGTTATTCGATAATTTATTCTTCTCTTCCGATCGTTATGACTTATCTGCGGTAGGGCGCATGAAATTCAACCGCTCTTTAGGCATTGAAGAAACCACTGGTGGTGGCACCTTAAGCAATGAAGATATTGTCAGTGTGATGAAAAAATTGATTGATATCCGTAATGGCCGTGGTGAAGTGGATGATATTGACCACTTGGGTAACCGTCGTATTCGTTCCGTAGGTGAAATGGCGGAAAATCAATTCCGTATCGGCTTGGTTCGTGTTGAACGCGCGGTAAAAGAACGCTTATCTTTAGGTGATCTGGAAGCTGTTACCCCGCAAGATCTAATCAATGCGAAACCGATTTCCGCCGCGGTGAAAGAATTCTTTGGTTCATCCCAATTGTCTCAATTTATGGACCAAAACAACCCGTTATCGGAAGTGACCCATAAACGCCGTATTTCCGCATTGGGTCCGGGCGGTTTAACCCGTGAACGTGCCGGTTTTGAAGTGCGTGATGTACACGCCACCCACTACGGTCGTGTGTGTCCGATTGAAACCCCTGAAGGTCCGAACATCGGTTTGATCAACTCCCTTTCCGTTTATGCGCGTACTAACGACTACGGTTTCTTAGAAACTCCGTACCGTAAAGTAGTAAATGGTCAGGTGACCGAAGAAATCGAATATTTGTCTGCCATTGAAGAAGGCAAATACGTTATCGCACAGGCGAACTCCAATCTTGATGATGATTTCCGCTTTACCGATGCCTTTGTAACCTGTCGTGGTGAACATGGTGAATCCGGCTTATATAAACCGGAAGAAATTCACTATATGGACGTTTCTACCCAACAAGTGGTTTCCGTAGCGGCGGCATTGATTCCGTTCCTGGAGCATGACGATGCGAACCGTGCTTTGATGGGGGCGAACATGCAACGTCAAGCCGTGCCGACATTGCGTGCGGACAAACCGTTAGTCGGTACAGGTATCGAAAAAGCGGTTGCCCTTGACTCCGGTGTGGCGGTTGTGGCAAAACGCGGCGGTACCATCCAATATGTGGATGCTTCCCGCATCGTGGTGAAAGTCAATGAAGACGAAACTGTCGCGGGCGAAGCCGGTATTGATATTTATAACCTCATTAAATATACCCGTTCGAACCAAAATACCTGTATCAACCAAATTCCTTGTGTGGAACTGGGCGATCCGGTGGAACGCGGTGAAATCTTGGCAGACGGTCCTTCCACCGATTTAGGTGAATTGGCATTAGGTCAAAACATTCGCGTGGCGTTCATGCCGTGGAACGGTTATAACTTCGAAGACTCCATGTTAGTCTCCGAACGTGTGGTTCAACAAGATCGCTTCACCACGATTCACATCCAAGAACTTTCTTGTGTAGCGCGTGATACCAAATTAGGCGCGGAAGAAATTACCGCAGATATTCCTAACGTCGGTGAAGCCGCACTAAGTAAGTTGGACGAATCCGGTATCGTGTATATCGGTGCGGAAGTGAAAGGCGGCGATATTCTGGTAGGTAAAGTGACACCGAAAGGTGAAACCCAATTAACGCCGGAAGAAAAATTATTGCGTGCGATCTTCGGTGAAAAAGCCTCCGATGTGAAAGACTCCTCTCTACGCGTACCAAACAGCGTTTCCGGTACGGTTATCGATGTGCAAGTGTTTACCCGCGATGGTGTGGAAAAAGACAAACGTGCGTTAGAAATTGAAGAAATGCAATTAAAACAAGCGAAAAAAGATTTGAGCGAAGAGTTTGAGATCTTGGAAGCCGGCTTGTTTATGCGCGTACGCAATCTGTTGTTATCCGGCGGTTTCGATGCGAAATCCTTGGATAAATTAGACCGCACTAAATGGTTGGAACAAACTTTAGATAACGAAGAAAAACAACACCAATTAGAGCAGTTGGCGGAACAGCACGAAGAATTACGCAAAGAATTTGAACGTAAATTGGAAATTCAACGCAACAAGATTATCCAAGGCGACGATTTGGCACCGGGCGTGTTAAAAGTGGTTAAAGTGTATCTTGCGGTGAAACGTCAAATTCAACCGGGTGATAAAATGGCGGGTCGTCACGGTAACAAAGGGATTATCTCCAAAATTAACCCGGTGGAAGACATGCCATACGATGAAAACGGTCAACCTGTTGAGATCGTATTGAACCCGCTGGGCGTTCCGTCCCGTATGAATATCGGTCAAATCTTGGAAACTCACTTAGGTTTGGCGGCGAAAGGTATTGGCGATCAAATTAACGCGATGATTAAACAACAACAATCTATCGCGAAATTGCGTGAATACATGCAAAAAGCCTATGACCTTGGCGGCGGTTCACAAAAAGTGGATCTCAGCACCTTTACCGATGAAGAAGTGATGCGTTTGGCGCAAAATCTGCGTAAAGGTTTGCCGGTTGCTACACCGGTATTTGACGGTGCACATGAAAAAGAAATCAAAGGTTTGTTAGAGCTTGGTGGTTTACCGACTTCCGGTCAAATTACCCTTTATGATGGTCGCACAGGTGAAAAATTCGAGCGTCCGGTAACCGTAGGTTATATGTATATGCTCAAATTGAATCACTTGGTTGATGACAAAATGCACGCGCGTTCAACCGGTTCTTATAGTCTTGTTACCCAACAACCGTTGGGCGGTAAGGCGCAGTTCGGTGGTCAACGTTTCGGTGAAATGGAGGTGTGGGCACTTGAGGCTTATGGTGCGGCTTATACCTTACAAGAAATGTTAACCGTGAAATCCGATGACGTGAACGGTCGTACGAAGATGTATAAAAACATCGTCAGCGGCAACCAACAAATGGATCCGGGTACACCGGAATCTTTCAACGTAATCATGAAAGAAATCCGTTCACTTGGTATCAACATCGACTTGGACGAAGAA","","","151905","MVYSYTEKKRIRKDFGKRPQVLNIPYLLTIQIDSFEKFIKRDPDGQQGLEAAFRSVFPIVSTNGNTELQYVSYQLGEPVFDVRECQIRGTTYAAPLRVKLRLVSYDKDAAPGTIKDIKEQEVYMGEIPLMTDNGTFVINGTERVIVSQLHRSPGVFFDSDKGKTHSSGKVLYNARIIPYRGSWLDFEFDPKDNLYARIDRRRKLPATIILRALGYTTEQILDLFFYKITFEIKDNKLLMTLVPERLRGETAAFDIETKGKVYVERGRRITARHIKALEKDKVTQVEVPTEYIIGKVAAKDYVDLETGELICPANMELSLELLAKLAQAGYTTLETLFTNDLDYGPYISETLRVDPSNDRLSALVEIYRMMRPGEPPTKEAAEALFDNLFFSSDRYDLSAVGRMKFNRSLGIEETTGGGTLSNEDIVSVMKKLIDIRNGRGEVDDIDHLGNRRIRSVGEMAENQFRIGLVRVERAVKERLSLGDLEAVTPQDLINAKPISAAVKEFFGSSQLSQFMDQNNPLSEVTHKRRISALGPGGLTRERAGFEVRDVHATHYGRVCPIETPEGPNIGLINSLSVYARTNDYGFLETPYRKVVNGQVTEEIEYLSAIEEGKYVIAQANSNLDDDFRFTDAFVTCRGEHGESGLYKPEEIHYMDVSTQQVVSVAAALIPFLEHDDANRALMGANMQRQAVPTLRADKPLVGTGIEKAVALDSGVAVVAKRGGTIQYVDASRIVVKVNEDETVAGEAGIDIYNLIKYTRSNQNTCINQIPCVELGDPVERGEILADGPSTDLGELALGQNIRVAFMPWNGYNFEDSMLVSERVVQQDRFTTIHIQELSCVARDTKLGAEEITADIPNVGEAALSKLDESGIVYIGAEVKGGDILVGKVTPKGETQLTPEEKLLRAIFGEKASDVKDSSLRVPNSVSGTVIDVQVFTRDGVEKDKRALEIEEMQLKQAKKDLSEEFEILEAGLFMRVRNLLLSGGFDAKSLDKLDRTKWLEQTLDNEEKQHQLEQLAEQHEELRKEFERKLEIQRNKIIQGDDLAPGVLKVVKVYLAVKRQIQPGDKMAGRHGNKGIISKINPVEDMPYDENGQPVEIVLNPLGVPSRMNIGQILETHLGLAAKGIGDQINAMIKQQQSIAKLREYMQKAYDLGGGSQKVDLSTFTDEEVMRLAQNLRKGLPVATPVFDGAHEKEIKGLLELGGLPTSGQITLYDGRTGEKFERPVTVGYMYMLKLNHLVDDKMHARSTGSYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEMLTVKSDDVNGRTKMYKNIVSGNQQMDPGTPESFNVIMKEIRSLGINIDLDEE","238971","","DNA-directed RNA polymerase beta chain (transcriptase beta chain)","Cytoplasm","","
InterPro
IPR007120
Domain
RNA polymerase Rpb2, domain 6
PF00562\"[716-1264]TRNA_pol_Rpb2_6
InterPro
IPR007121
Family
RNA polymerase, beta subunit
PS01166\"[1064-1076]TRNA_POL_BETA
InterPro
IPR007641
Domain
RNA polymerase Rpb2, domain 7
PF04560\"[1266-1342]TRNA_pol_Rpb2_7
InterPro
IPR007642
Domain
RNA polymerase Rpb2, domain 2
PF04561\"[151-454]TRNA_pol_Rpb2_2
InterPro
IPR007644
Domain
RNA polymerase beta subunit
PF04563\"[27-509]TRNA_pol_Rpb2_1
InterPro
IPR007645
Domain
RNA polymerase Rpb2, domain 3
PF04565\"[513-582]TRNA_pol_Rpb2_3
InterPro
IPR010243
Family
DNA-directed RNA polymerase, beta subunit
TIGR02013\"[8-1339]TrpoB: DNA-directed RNA polymerase, beta sub
InterPro
IPR014724
Domain
RNA polymerase Rpb2, OB-fold
G3DSA:2.40.50.150\"[830-961]Tno description
noIPR
unintegrated
unintegrated
G3DSA:2.40.270.10\"[1022-1235]Tno description
G3DSA:2.40.50.100\"[716-787]Tno description
G3DSA:3.90.1100.10\"[10-715]Tno description
PTHR20856\"[489-934]T\"[1042-1145]T\"[1196-1342]TDNA-DIRECTED RNA POLYMERASE I SUBUNIT 2
PTHR20856:SF3\"[489-934]T\"[1042-1145]T\"[1196-1342]TDNA-DIRECTED RNA POLYMERASE BETA CHAIN


","BeTs to 26 clades of COG0085COG name: DNA-directed RNA polymerase beta subunit/140 kD subunit (split gene in Mjan, Mthe, Aful)Functional Class: KThe phylogenetic pattern of COG0085 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit (5.5e-224) to 8/8 blocks of the IPB001572 family, which is described as \"RNA polymerases beta subunit\". Interpro entry for IP:IPR001572. IPB001572A 443-459 6.8e-12 IPB001572B 504-543 1.8e-33 IPB001572C 548-572 4.3e-21 IPB001572D 663-692 9.4e-27 IPB001572E 798-815 2.3e-14 IPB001572F 866-890 9e-19 IPB001572G 1064-1106 1.3e-35 IPB001572H 1231-1284 3.6e-54","Residues 261 to 329 match (3e-07) PD:PD001122 which is described as RNA POLYMERASE DNA-DIRECTED SUBUNIT BETA' CHAIN TRANSFERASE TRANSCRIPTION PROTEOME COMPLETE ","","","","","","","","","","","","Mon Dec 9 13:18:31 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00355 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1266 to 1342 (E-value = 2.3e-48) place AA00355 in the RNA_pol_Rpb2_7 family which is described as RNA polymerase Rpb2, domain 7 (PF04560)","","","","","Morse R, O'Hanlon K, Collins MD. The spectrum of spontaneous rifampin resistance mutations in therpoB gene of Bacillus subtilis 168 spores differs from that ofvegetative cells and resembles that of Mycobacterium tuberculosis. J Bacteriol. 2002 Sep;184(17):4936-40. PMID: 12204372 Ko KS, Lee HK, Park MY, Lee KH, Yun YJ, Woo SY, Miyamoto H, KookYH. Application of RNA polymerase beta-subunit gene (rpoB) sequencesfor the molecular differentiation of Legionella species. J Clin Microbiol. 2002 Jul;40(7):2653-8. PMID: 12089300 Aboshkiwa M, Rowland G, Coleman G. Nucleotide sequence of the Staphylococcus aureus RNA polymeraserpoB gene and comparison of its predicted amino acid sequence withthose of other bacteria. Biochim Biophys Acta 1262(1):73-8.1995 PubMed: . ","","Fri Nov 21 13:21:52 2003","1","","","" "AA00356","239077","243342","4266","GTGAAAGACTTAGTTAAATTTTTAAAAGCACAATCAAAAACCGCTGAAGATTTTGATGTGATTAAAATCGGTTTAGCCTCACCTGACATGATCCGTTCTTGGTCATACGGTGAAGTTAAAAAGCCTGAAACAATCAACTATCGTACCTTTAAACCGGAACGTGACGGTCTTTTCTGTGCCCGTATTTTCGGACCGGTAAAAGATTACGAATGTTTGTGCGGTAAGTACAAACGCTTAAAACACCGTGGCGTGATTTGTGAAAAATGTGGCGTTGAAGTGACTCAAACCAAAGTACGTCGTGAACGTATGGGGCACATCGAATTAGCCTCTCCGGTGGCGCACATTTGGTTTTTAAAATCCCTGCCGTCCCGTATCGGTTTGTTGTTAGATATGCCATTGCGTGATATTGAACGCGTGCTTTATTTTGAATCTTACATTGTGATCGAACCGGGTATGACCGATCTGGAACGCGGTCAGTTATTAACCGAAGAGCAATATCTTGACGCGGAAGACCGCTGGCAGGATGAGTTCGACGCAAAAATGGGTGCGGAAGCGATCCAAGCGTTATTGCGCGGTATCGATTTAGAAGCGGAATGCGAAAATTTACGTGAAGAATTACAAGAAACCAATTCCGAAACCAAACGGAAGAAAATCACGAAGCGCTTAAAATTATTAGAAGCTTTCCTGCAATCCGGCAACAAACCGGAATGGATGGTGATGACCGTATTGCCGGTACTTCCGCCGGATTTACGTCCGTTAGTGCCGTTAGACGGCGGCCGTTTCGCCACTTCCGATTTGAACGATTTATATCGTCGTGTGATCAACCGTAACAACCGTTTAAAACGTTTATTGGATCTTATCGCACCGGATATTATCGTGCGCAACGAAAAACGCATGTTGCAGGAATCCGTGGACGCGTTATTGGATAACGGTCGTCGCGGTCGTGCCATCACCGGTTCTAACCGTCGTCCGTTAAAATCATTGGCGGATATGATTAAAGGTAAACAAGGTCGCTTCCGTCAAAACTTGTTGGGTAAACGTGTTGACTACTCCGGTCGTTCCGTAATCACCGTGGGTCCATACTTGCACTTACACCAATGTGGTTTGCCGAAGAAAATGGCATTGGAATTATTCCGTCCGTTTATCTACGCGAAATTAGAAAGTCGTGGTTATGCAACAACGATTAAAGCGGCGAAAAAAATGGTGGAACGCGAAGACGCCATCGTTTGGGATATTCTGGCGGAAGTCATTCGCGAACATCCGATTCTGTTGAACCGTGCACCGACACTTCACCGTTTGGGTATTCAAGCCTTTGAACCAATCTTAATCGAAGGTAAAGCAATCCAATTGCACCCGCTTGTCTGTGCGGCGTTTAACGCGGACTTCGACGGTGACCAAATGGCGGTGCACGTTCCGTTGACGCTTGAAGCGCAATTAGAAGCGCGTGCGTTAATGATGTCCACCAATAACATTCTTTCTCCGGCGAACGGCGATCCGATTATCGTTCCGTCACAAGACGTGGTGTTAGGGCTTTACTACATGACCCGCGAAAAAGTGAACGGTAAAGGTGAAGGTATGCTATTGCAAGATCCGCGCGAAGCGGAAAAAGCCTATCGTACCGGTCAGGCAGAATTGCATTCCCGCGTGAAAGTGCGTATTACCGAATATGTGAAAAACGACGCCGGTGAGTTTGAACCGAAAACAACCCTAACCGATACTACCATCGGTCGTGCCATCTTATGGATGATCGCGCCGAAAGGCATGCCGTTTAGCTTGTTTAACCAAACTCTTGGCAAAAAAGCCATTTCTAAGTTAATTAACGAAAGCTATCGTCGCTTAGGCTTAAAAGCCAGCGTCATGTTCGCCGACCAAATCATGTACACCGGTTTTGCTTACGCGGCACGTTCCGGTTCCTCCGTGGGTATCGACGACATGGTGATTCCGGCGAAGAAATACGAAATTATTTCTGCGGCGGAAGAAGAAGTTGCCGAAATTCAGGAACAATTCCAATCCGGTCTTGTGACAGCGGGCGAACGTTATAACAAAGTGATTGATATTTGGGCGGCAGCCAATGAACGCGTTGCCAAAGCCATGATGGAAAACCTGTCTTCGGAAGAAGTGATTAACCGTGAAGGTAAACCGGAAAAACAAGCCTCTTTCAACAGCATCTTTATGATGGCGGATTCCGGTGCCCGTGGTTCCGCAGCACAGATTCGTCAGTTGGCGGGTATGCGTGGTTTGATGGCGCGTCCGGACGGTTCCATTATCGAAACCCCAATCACTGCAAACTTCCGTGAAGGGTTGAACGTTTTACAATACTTTATTTCTACCCACGGTGCGCGTAAAGGTTTGGCGGATACCGCGTTGAAAACCGCGAACTCCGGTTACTTAACCCGCCGTTTGGTTGACGTGGCACAGGATTTAGTGATCATCGAAGATGACTGTGGTACGCACGAAGGTATCGTGATGACCCCGTTAATCGAAGGTGGCGACGAAAAAGTTCCTCTGCGCGAATTGGTATTAGGTCGTGTGGCGGCGGAAGATATCTTAAAACCGGGTACGGAAGACGTATTAATTCCACGCAATACCTTGCTTGATGAAAAACTTTGTGATGTGTTGGATGAAAACTCCGTGGACAGCGTAAAAGTGCGTTCCGTCGTAACCTGTAACACCGATTTAGGCGTTTGTGCGAAATGTTACGGTCGTGACTTGGCGCGCGGTCACCTGATTAACCAAGGTGAAGCGGTAGGTGTTATCGCGGCACAATCTATCGGTGAACCGGGTACACAGTTAACCATGCGTACGTTCCACATCGGTGGTGCGGCATCCGCGGCAGCCAAAGAATCCAGCGTACAAGTGAAAAACAACGGCACATTGCGTTTAGCCAATGCAAAATTCGTGACGAACAACGAAGGTAAATTGGTGCTGACTTCCCGTAATACCGAATTGACCGTTGTGGATAATTTCGGACGTACCAAAGAGCACTATAAAGTGCCTTACGGTGCGATTTTAAGCAAAGGCGATCACCAAGAAGTGAATGCAGGCGAAACCATCGCTAACTGGGATCCGCATACCATGCCGGTTATTTCTGAAGTGGGCGGTTTCGTGAAATTCGTGGACATCGTAGACGGTTTAACCGTCACCCGTCAAACCGACGAACTCACCGGTCTTTCCTCTATCGTGGTACAAGACGTGGGTGAACGTGCCACAGCCGGTAAAGATCTGCGCCCTGCAATCAAACTAGTTGATGAGAAAGGGAATGACGTATTGGTGTCGGGCACCGACGTTGCGGCACAATATTTCTTGCCAAGTAAGGCTATCGTGACCTTGGATGACGGCGCGGAAGTGCATGTGGGTGACCCGTTGGCACGTATTCCACAAGAATCTGTCGGAACAAAAGATATTACCGGCGGTCTTCCGCGCGTGGCGGATTTATTTGAAGCGCGTAAACCGAAAGAACCTGCCATCTTGGCGGAAATTTCCGGTATCGTGTCCTTCGGTAAAGAAACCAAAGGTAAACGTCGCTTATTGATTACCCCGACGGAAGGTGAAGTGTACGAAGAAATGATCCCGAAATGGCGTCAACTGAACGTATTCGAAGGTGAAATGGTACAATGCGGCGATTTAATCTCCGACGGTGCGGAAACGCCACATGACATCTTACGTTTACGAGGTGTCCATGCCGTAACCGAATACATCGTTAACGAGGTACAGGAAGTTTACCGCTTACAAGGGGTAAAAATTAACGATAAACACATCGAAGTGATCGTACGCCAAATGTTGCGTAAAGCTATCGTTACCAAAGCCTACGACTCCGAATTCCTCGAAGGGGAACAAGTGGAAGTGGCGCGTGTGAAAATCGTTAACCGCAAACGCGAAGCAGAAGGCAAACCGCCGGTTGAATATGAACGCGAATTATTGGGTATCACCAAAGCGTCCTTGGCAACCGAGTCCTTCATCTCTGCGGCCTCCTTCCAGGAAACCACCCGTGTGTTAACGGAAGCGGCGGTTGCCGGTAAACGCGATGAATTACGTGGCTTGAAAGAAAACGTCATCGTAGGTCGTTTGATCCCGGCGGGTACCGGTTTTGCGTATCACCGAAATCGCCATAAAAACCCGACAGCCATCGCGGATGACGAGGTGCCGGTAAGATTATCGGCGGCGGATGAAGAAGAAATTGCTTCCGAATTCGTGATGACCTCCGAAGATGCGTCAGCAAGTTTAACCGAAATGTTAAACATGGTAGAAGAAGACAATCACGCGGAA","","","159079","VKDLVKFLKAQSKTAEDFDVIKIGLASPDMIRSWSYGEVKKPETINYRTFKPERDGLFCARIFGPVKDYECLCGKYKRLKHRGVICEKCGVEVTQTKVRRERMGHIELASPVAHIWFLKSLPSRIGLLLDMPLRDIERVLYFESYIVIEPGMTDLERGQLLTEEQYLDAEDRWQDEFDAKMGAEAIQALLRGIDLEAECENLREELQETNSETKRKKITKRLKLLEAFLQSGNKPEWMVMTVLPVLPPDLRPLVPLDGGRFATSDLNDLYRRVINRNNRLKRLLDLIAPDIIVRNEKRMLQESVDALLDNGRRGRAITGSNRRPLKSLADMIKGKQGRFRQNLLGKRVDYSGRSVITVGPYLHLHQCGLPKKMALELFRPFIYAKLESRGYATTIKAAKKMVEREDAIVWDILAEVIREHPILLNRAPTLHRLGIQAFEPILIEGKAIQLHPLVCAAFNADFDGDQMAVHVPLTLEAQLEARALMMSTNNILSPANGDPIIVPSQDVVLGLYYMTREKVNGKGEGMLLQDPREAEKAYRTGQAELHSRVKVRITEYVKNDAGEFEPKTTLTDTTIGRAILWMIAPKGMPFSLFNQTLGKKAISKLINESYRRLGLKASVMFADQIMYTGFAYAARSGSSVGIDDMVIPAKKYEIISAAEEEVAEIQEQFQSGLVTAGERYNKVIDIWAAANERVAKAMMENLSSEEVINREGKPEKQASFNSIFMMADSGARGSAAQIRQLAGMRGLMARPDGSIIETPITANFREGLNVLQYFISTHGARKGLADTALKTANSGYLTRRLVDVAQDLVIIEDDCGTHEGIVMTPLIEGGDEKVPLRELVLGRVAAEDILKPGTEDVLIPRNTLLDEKLCDVLDENSVDSVKVRSVVTCNTDLGVCAKCYGRDLARGHLINQGEAVGVIAAQSIGEPGTQLTMRTFHIGGAASAAAKESSVQVKNNGTLRLANAKFVTNNEGKLVLTSRNTELTVVDNFGRTKEHYKVPYGAILSKGDHQEVNAGETIANWDPHTMPVISEVGGFVKFVDIVDGLTVTRQTDELTGLSSIVVQDVGERATAGKDLRPAIKLVDEKGNDVLVSGTDVAAQYFLPSKAIVTLDDGAEVHVGDPLARIPQESVGTKDITGGLPRVADLFEARKPKEPAILAEISGIVSFGKETKGKRRLLITPTEGEVYEEMIPKWRQLNVFEGEMVQCGDLISDGAETPHDILRLRGVHAVTEYIVNEVQEVYRLQGVKINDKHIEVIVRQMLRKAIVTKAYDSEFLEGEQVEVARVKIVNRKREAEGKPPVEYERELLGITKASLATESFISAASFQETTRVLTEAAVAGKRDELRGLKENVIVGRLIPAGTGFAYHRNRHKNPTAIADDEVPVRLSAADEEEIASEFVMTSEDASASLTEMLNMVEEDNHAE","243342","","DNA-directed RNA polymerase, beta' chain","Cytoplasm","","
InterPro
IPR000722
Domain
RNA polymerase, alpha subunit
G3DSA:2.40.40.30\"[347-489]Tno description
PF00623\"[345-487]TRNA_pol_Rpb1_2
InterPro
IPR001907
Family
Peptidase S14, ClpP
PS00381\"[935-946]?CLP_PROTEASE_SER
InterPro
IPR006592
Domain
RNA polymerase, N-terminal
SM00663\"[236-515]TRPOLA_N
InterPro
IPR007066
Domain
RNA polymerase Rpb1, domain 3
PF04983\"[490-645]TRNA_pol_Rpb1_3
InterPro
IPR007080
Domain
RNA polymerase Rpb1, domain 1
G3DSA:3.90.1120.10\"[14-346]Tno description
PF04997\"[15-343]TRNA_pol_Rpb1_1
InterPro
IPR007081
Domain
RNA polymerase Rpb1, domain 5
PF04998\"[767-1322]TRNA_pol_Rpb1_5
InterPro
IPR007083
Domain
RNA polymerase Rpb1, domain 4
PF05000\"[674-765]TRNA_pol_Rpb1_4
InterPro
IPR012754
Family
DNA-directed RNA polymerase, subunit beta-prime
TIGR02386\"[20-1368]TrpoC_TIGR: DNA-directed RNA polymerase, bet
noIPR
unintegrated
unintegrated
PTHR19376\"[15-1393]TDNA-DIRECTED RNA POLYMERASE
PTHR19376:SF4\"[15-1393]TDNA-DIRECTED RNA POLYMERASE BETA CHAIN


","BeTs to 26 clades of COG0086COG name: DNA-directed RNA polymerase beta' subunit/160 kD subunit (split gene in archaea and Syn)Functional Class: KThe phylogenetic pattern of COG0086 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit (2.4e-104) to 6/6 blocks of the IPB000722 family, which is described as \"RNA polymerase, alpha subunit\". Interpro entry for IP:IPR000722. IPB000722A 89-117 3.7e-19 IPB000722B 235-252 6.5e-13 IPB000722C 333-350 1.5e-13 IPB000722D 422-440 5.6e-12 IPB000722E 458-472 1.4e-11 IPB000722F 476-515 1.6e-28Significant hit ( 1.6e-45) to 6/12 blocks of the IPB000684 family, which is described as \"Eukaryotic RNA polymerase II heptapeptide repeat\". Interpro entry for IP:IPR000684. IPB000684A 88-134 0.076 IPB000684B 333-387 2.1e-15 IPB000684C 433-480 3.1e-05 IPB000684E 767-818 1.9e-08 IPB000684F 893-932 0.00023 IPB000684K 1340-1374 0.047","Residues 530 to 592 match (1e-07) PD:PD542603 which is described as BETA' PROBABLE PROTEOME POLYMERASE DNA-DIRECTED CHAIN COMPLETE NUCLEOTIDYLTRANSFERASE RNA TRANSFERASE ","","","","","","","","","","","","Fri Nov 21 13:23:58 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00356 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 767 to 1322 (E-value = 1.2e-159) place AA00356 in the RNA_pol_Rpb1_5 family which is described as RNA polymerase Rpb1, domain 5 (PF04998)","","","","","Ovchinnikov,Yu.A., Monastyrskaya,G.S., Gubanov,V.V., Guryev,S.O., Salomatina,I.S., Shuvaeva,T.M., Lipkin,V.M. and Sverdlov,E.D. The primary structure of E. coli RNA polymerase, Nucleotide sequence of the rpoC gene and amino acid sequence of the beta'-subunit Nucleic Acids Res. 10 (13), 4035-4044 (1982) PubMed: 6287430 Squires,C., Krainer,A., Barry,G., Shen,W.F. and Squires,C.L. Nucleotide sequence at the end of the gene for the RNA polymerase beta' subunit (rpoC) Nucleic Acids Res. 9 (24), 6827-6840 (1981) PubMed: 6278450 ","","Fri Nov 21 13:23:58 2003","1","","","" "AA00357","243923","243474","450","ATGGTAAGTAAAGCCAATGACGATTCAAGTCTATCACATACCAAATGGAACTGTAAGTATCACATCGTCTTCACCCCGAAATATAGAAGAAAAGCCATTTACGGAAGGCTTAGAGCGGATATAGGTAGCATATTAAGGCAATTATGTGACTATAAAAATGTGGAAATAATAGAAGCACACGCAATGAAAGAGCATATTCATATGCTTCTAAAAATTCCGCCGAAATTATCGGTATCAAGTTTTATGGGGTATTTAAAGGGAAAATCATTTGAAAGGCACGCAAACCTAAAATACAACTATGGTAACCGACATTTTTGGTCGAAAGGCTATTATGTAAGCACGGTAGGGCTAAATACAAAGACAGTGGAGGAGTATATAAGGAATCAGGAAAAGGAAGACATGATTCAGGATAATTTATCGAAGAAAGGATATGTGGACCCCTTTAAGGGG","","","17582","MVSKANDDSSLSHTKWNCKYHIVFTPKYRRKAIYGRLRADIGSILRQLCDYKNVEIIEAHAMKEHIHMLLKIPPKLSVSSFMGYLKGKSFERHANLKYNYGNRHFWSKGYYVSTVGLNTKTVEEYIRNQEKEDMIQDNLSKKGYVDPFKG","243474","","transposase (probable IS200-like )","Cytoplasm","","
InterPro
IPR002686
Family
Transposase IS200-like
PD003831\"[12-68]TQ93PB3_BBBBB_Q93PB3;
PF01797\"[23-122]TTransposase_17


","No hits to the COGs database.","","Residues 16 to 69 match (4e-07) PD:PD590305 which is described as TRANSPOSASE PROTEOME COMPLETE ORFA PLASMID TRANSPOSASE PROBABLE VNG6182H IS605 A ","","","","","","","","","","","","Mon Dec 9 14:05:40 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00357 is paralogously related to AA01226 (2e-69), AA01244 (4e-50) and AA02040 (8e-30).","","","","","","Residues 23 to 122 (E-value = 2.3e-59) place AA00357 in the Transposase_17 family which is described as Transposase IS200 like (PF01797)","","","","Yamada,T.Molecular analysis of a new insertion sequence from Actinobacillus(Haemophilus) actinomycetemcomitans FDC Y4Microbiology 142 (Pt 9), 2449-2452 (1996)PubMed: 8828211"," ","Mon Dec 9 14:05:02 2002","Tue Jan 7 14:08:04 2003","1","","","" "AA00358","244369","244115","255","ATGACTGATAAAATTCGTAGCGTGCAAGGTCGTGTTGTAAGTGACAAGATGGAGAAATCTTTCGTTGTTGCTATTGAACGCAAGGTTAAACACCCACTTTATGGCAAGTTTATCCGTCGCACAACCAAACTACATGTGCACGATGAAAACAACGAAGCTAAATTAGGTGATTTAGTAGAAGTTCGCGAATGTCGTCCAATTTCTAAAACTAAATCATGGACTTTAGTTCGTGTAGTTGAGAAAGCAGTAATTGCT","","","9813","MTDKIRSVQGRVVSDKMEKSFVVAIERKVKHPLYGKFIRRTTKLHVHDENNEAKLGDLVEVRECRPISKTKSWTLVRVVEKAVIA","244115","","30S ribosomal protein S17","Cytoplasm","","
InterPro
IPR000266
Family
Ribosomal protein S17
PD001295\"[6-76]TRibosomal_S17
PR00973\"[24-47]T\"[56-66]T\"[66-73]TRIBOSOMALS17
PTHR10744\"[6-85]TRibosomal_S17
PF00366\"[10-78]TRibosomal_S17
PS00056\"[56-68]TRIBOSOMAL_S17
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[3-80]TOB_NA_bd_sub
noIPR
unintegrated
unintegrated
SSF50249\"[4-82]TNucleic_acid_OB


","No hits to the COGs database.","Significant hit ( 2.5e-34) to 2/2 blocks of the IPB000266 family, which is described as \"Ribosomal protein S17\". Interpro entry for IP:IPR000266. IPB000266A 10-46 1.2e-21 IPB000266B 56-73 2.6e-11","Residues 6 to 79 match (7e-08) PD:PD010443 which is described as RIBOSOMAL S11 40S RRNA-BINDING COMPLETE 30S PROTEOME S17P S17 PROBABLE ","","","","","","","","","","","","Mon Dec 9 14:07:33 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00358 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 10 to 78 (E-value = 1e-39) place AA00358 in the Ribosomal_S17 family which is described as Ribosomal protein S17 (PF00366)","","","","Hayashida,H., Hotokezaka,H., Ohara,N., Kimura,M., Takagi,O. andYamada,T.Molecular analysis of a new insertion sequence from Actinobacillus(Haemophilus) actinomycetemcomitans FDC Y4Microbiology 142 (Pt 9), 2449-2452 (1996)PubMed: 96425869","Yaguchi,M. and Wittmann,H.G. The primary structure of protein S17 from the small ribosomalsubunit of Escherichia coli. FEBS Lett. 87(1): 37-40.1978. PubMed: 344065.Abe,R., Yamashita,A. and Isono,K.Cloning and characterization of the ribosomal protein genes in thespc operon of a prokaryotic endosymbiont of the pea aphid, Acyrthosiphon kondoiDNA Res. 1 (3), 103-114 (1994)PubMed: 7584036","Mon Dec 9 14:09:54 2002","Mon Dec 9 14:12:41 2002","1","","","" "AA00359","244560","244372","189","ATGAAAGCTCAAGAACTACGTACAAAAAGTGTTGAAGAGCTGAATGCTGAATTGGTTAACTTGTTAGGTGAGCAATTCAAGTTGCGTATGCAAGCAGCCACCGGTCAGCTTCAACAAACCCATCAGTTAAAACAAGTGCGTCGTAGTATTGCACAAATTAAAACTGTTCTAACCGAAAAGGCGGGTGAG","","","7145","MKAQELRTKSVEELNAELVNLLGEQFKLRMQAATGQLQQTHQLKQVRRSIAQIKTVLTEKAGE","244372","","50S ribosomal protein L29","Cytoplasm","","
InterPro
IPR001854
Family
Ribosomal protein L29
PF00831\"[3-60]TRibosomal_L29
TIGR00012\"[5-60]TL29
PS00579\"[39-53]TRIBOSOMAL_L29
SSF46561\"[1-60]TRibosomal_L29
noIPR
unintegrated
unintegrated
G3DSA:1.10.287.310\"[1-60]TG3DSA:1.10.287.310


","BeTs to 18 clades of COG0255COG name: Ribosomal protein L29Functional Class: JThe phylogenetic pattern of COG0255 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 8.3e-30) to 2/2 blocks of the IPB001854 family, which is described as \"Ribosomal protein L29\". Interpro entry for IP:IPR001854. IPB001854A 5-35 2.3e-16 IPB001854B 39-60 5.1e-12","Residues 1 to 63 match (7e-07) PD:PD490783 which is described as RIBOSOMAL 50S L29 PROTEOME COMPLETE ","","","","","","","","","","","","Mon Dec 9 14:18:47 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00359 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 60 (E-value = 1.2e-29) place AA00359 in the Ribosomal_L29 family which is described as Ribosomal L29 protein (PF00831)","","","","Hayashida,H., Hotokezaka,H., Ohara,N., Kimura,M., Takagi,O. andYamada,T.Molecular analysis of a new insertion sequence from Actinobacillus(Haemophilus) actinomycetemcomitans FDC Y4Microbiology 142 (Pt 9), 2449-2452 (1996)PubMed: 96425869","Bitar,K.G. The primary structure of the ribosomal protein L29 fromEscherichia coli Biochim. Biophys. Acta 386 (1), 99-106 (1975) PubMed: 1092361 Arnold,R.J. and Reilly,J.P. Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry Anal. Biochem. 269 (1), 105-112 (1999) PubMed: 10094780 ","Fri Feb 7 15:28:27 2003","Mon Dec 9 14:15:42 2002","1","","","" "AA00361","244970","244563","408","ATGTTGCAACCAAAACGTACAAAATTCCGTAAAGTTCACAAAGGCCGTAACCGTGGTATCGCGGGCGGTACAGAAGTTAGCTTCGGTACTTTCGGTTTAAAAGCAGTTGGTCGTGGTCGTTTAACTGCGCGTCAAATTGAAGCCGCTCGTCGTGCTATGACTCGTGCAGTAAAACGTCAAGGTAAAATCTGGATTCGTGTATTCCCGGATAAACCAATTACTGAAAAACCATTAGAAGTCCGTATGGGTAAAGGTAAAGGTAACGTTGAGTACTGGGTAGCCTTAATCCAACCGGGTAAAGTTCTCTATGAAATGGATGGTGTGTCTGAAGAAATCGCAAGAGAAGCATTTGCACTAGCAGCTGCCAAATTGCCGGTTAAGACCACTTTCGTAACTAAGACGGTGATG","","","15167","MLQPKRTKFRKVHKGRNRGIAGGTEVSFGTFGLKAVGRGRLTARQIEAARRAMTRAVKRQGKIWIRVFPDKPITEKPLEVRMGKGKGNVEYWVALIQPGKVLYEMDGVSEEIAREAFALAAAKLPVKTTFVTKTVM","244563","","50S ribosomal protein L16","Cytoplasm","","
InterPro
IPR000114
Family
Ribosomal protein L16
PR00060\"[23-35]T\"[41-52]T\"[57-86]T\"[87-116]TRIBOSOMALL16
PF00252\"[1-131]TRibosomal_L16
TIGR01164\"[2-126]TrplP_bact
PS00586\"[58-69]TRIBOSOMAL_L16_1
PS00701\"[81-92]TRIBOSOMAL_L16_2
noIPR
unintegrated
unintegrated
PTHR12220\"[1-131]TPTHR12220
SSF54686\"[3-134]TSSF54686


","BeTs to 19 clades of COG0197COG name: Ribosomal protein L16/L10EFunctional Class: JThe phylogenetic pattern of COG0197 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 5.4e-65) to 2/2 blocks of the IPB000114 family, which is described as \"Ribosomal protein L16\". Interpro entry for IP:IPR000114. IPB000114A 1-19 4e-14 IPB000114B 59-113 8.8e-50","Residues 33 to 127 match (1e-07) PD:PD587820 which is described as RIBOSOMAL MITOCHONDRION L16 MITOCHONDRIAL 60S 50S ","","","","","","","","","","","","Mon Dec 9 14:24:00 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00361 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 131 (E-value = 8.2e-92) place AA00361 in the Ribosomal_L16 family which is described as Ribosomal protein L16 (PF00252)","","","","Hayashida,H., Hotokezaka,H., Ohara,N., Kimura,M., Takagi,O. andYamada,T.Molecular analysis of a new insertion sequence from ActinobacillusHaemophilus) actinomycetemcomitans FDC Y4Microbiology 142 (Pt 9), 2449-2452 (1996)PubMed: 96425869","Brosius,J. and Chen,R. The primary structure of protein L16 located at thepeptidyltransferase center of Escherichia coli ribosomes. FEBS Lett. 68(1): 105-109. PubMed: 786730.Zurawski,G. and Zurawski,S.M.Structure of the Escherichia coli S10 ribosomal protein operonNucleic Acids Res. 13 (12), 4521-4526 (1985)PubMed: 3892488Baxter,R.M. and Zahid,N.L16, a bifunctional ribosomal protein and the enhancing effect ofL6 and L11Eur. J. Biochem. 155 (2), 273-277 (1986)PubMed: 3956484 ","Mon Dec 9 14:24:00 2002","Mon Jan 13 17:26:54 2003","1","","","" "AA00362","245691","244987","705","ATGGGTCAAAAAGTACATCCACATGGTATTCGCCTGGGTATTGTAAAACCTTGGAGCTCTACTTGGTTTGCGAATACACAAGACTTCGCCGATAATCTTGAAGGCGATTTCAAAGTACGTCAATTCTTAAATAAAGAATTAGCGAATGCTTCAGTTTCACGTATTACTATTGAACGTCCTGCAAAGAGCATTCGTGTGACTATTCACACAGCCCGCCCTGGTATCGTAATTGGTAAGAAAGGTGAAGATGTTGAGAAATTGCGTAACGCAGTGGCAAAAATTGCCGGTGTTCCTGCACAAATCAATATTGCTGAAGTGAAAAAACCTGAATTAGATGCAAAATTAGTTGCAGATAGCATCGCTTCACAATTAGAACGTCGTGTAATGTTCCGTCGTGCTATGAAAAAAGCGGTACAAAATGCAATGCGTTTAGGCGCTAAAGGTATCAAAGTTGAAGTTAGCGGTCGTTTAGGCGGTGCAGAAATTGCTCGTTCTGAATGGTATCGTGAAGGTCGTGTACCTCTACATACATTGCGTGCGGACATCGACTATAACACTGCTGAAGCTCATACAACATACGGCGTAATCGGCGTTAAAGTATGGATCTTCAAAGGTGAGATTCTTGGTGGAATGGCTGCGCTAGCGCAACCGGAACAACAACCTACCGACAAGCCTAAAAAGGTTCCGCGCGGTAAAGGTCGTAAG","","","27184","MGQKVHPHGIRLGIVKPWSSTWFANTQDFADNLEGDFKVRQFLNKELANASVSRITIERPAKSIRVTIHTARPGIVIGKKGEDVEKLRNAVAKIAGVPAQINIAEVKKPELDAKLVADSIASQLERRVMFRRAMKKAVQNAMRLGAKGIKVEVSGRLGGAEIARSEWYREGRVPLHTLRADIDYNTAEAHTTYGVIGVKVWIFKGEILGGMAALAQPEQQPTDKPKKVPRGKGRK","244987","","30S ribosomal protein S3","Cytoplasm","","
InterPro
IPR001351
Domain
Ribosomal protein S3, C-terminal
G3DSA:3.30.1140.32\"[108-207]TRibosomal_S3_C
PF00189\"[119-202]TRibosomal_S3_C
PS00548\"[163-197]TRIBOSOMAL_S3
SSF54821\"[107-207]TRibosomal_S3_C
InterPro
IPR004044
Domain
KH, type 2
PF07650\"[63-117]TKH_2
PS50823\"[39-107]TKH_TYPE_2
InterPro
IPR004087
Domain
KH
SM00322\"[60-125]TKH
InterPro
IPR004088
Domain
KH, type 1
PS50084\"[61-105]FKH_TYPE_1
InterPro
IPR008282
Domain
Ribosomal protein S3, N-terminal
PF00417\"[1-62]TRibosomal_S3_N
InterPro
IPR009019
Domain
KH, prokaryotic type
G3DSA:3.30.300.20\"[17-107]TKH_prok
SSF54814\"[2-106]TKH_prok
noIPR
unintegrated
unintegrated
PTHR11760\"[90-210]TPTHR11760
PTHR11760:SF10\"[90-210]TPTHR11760:SF10


","BeTs to 26 clades of COG0092COG name: Ribosomal protein S3Functional Class: JThe phylogenetic pattern of COG0092 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 4.2e-43) to 2/2 blocks of the IPB001351 family, which is described as \"Ribosomal protein S3\". Interpro entry for IP:IPR001351. IPB001351A 2-23 3.8e-12 IPB001351B 148-184 1.1e-29","Residues 2 to 38 match (8e-17) PD:PD337063 which is described as RIBOSOMAL S3 30S CHLOROPLAST PROTEOME COMPLETE TRNA-BINDING PROBABLE BS2 CYANELLE ","","","","","","","","","","","","Mon Dec 9 14:27:34 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00362 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 119 to 202 (E-value = 2.9e-55) place AA00362 in the Ribosomal_S3_C family which is described as Ribosomal protein S3, C-terminal domain (PF00189)","","","","Hayashida,H., Hotokezaka,H., Ohara,N., Kimura,M., Takagi,O. and Yamada,T.Molecular analysis of a new insertion sequence from Actinobacillus(Haemophilus) actinomycetemcomitans FDC Y4Microbiology 142 (Pt 9), 2449-2452 (1996)PubMed: 96425869","Secondary Laboratory Evidence:Brauer,D. and Roming,R. The primary structure of protein S3 from the small ribosomalsubunit of Escherichia coli. FEBS Lett. 106(2): 352-357. 1979. PubMed: 387449.","Fri Feb 7 14:49:22 2003","Mon Dec 9 14:27:34 2002","1","","","" "AA00363","246040","245711","330","ATGGAAACAATTGCAAAACATCGTTACGCTCGCACTTCAGCGCAAAAAGCTCGCTTAGTTGCGGATTTAATCCGTGGTAAGAAAGTTGCTCAAGCATTAGAAATTCTTACTTACACTAATAAAAAAGCCTCAGCTTTAGTGAAGAAAGTTCTTGAGTCAGCTATTGCAAATGCCGAGCACAATGACGGTGCAGATATCGATGATCTTAAAGTTGCGAAGATTTTCGTAGATGAAGGTCCAAGCATGAAACGTGTTATGCCACGTGCTAAAGGTCGTGCAGATCGTATTTTAAAACGTACAAGCCACATTACTGTGGTTGTGTCAGATCGT","","","12164","METIAKHRYARTSAQKARLVADLIRGKKVAQALEILTYTNKKASALVKKVLESAIANAEHNDGADIDDLKVAKIFVDEGPSMKRVMPRAKGRADRILKRTSHITVVVSDR","245711","","50S ribosomal protein L22","Cytoplasm","","
InterPro
IPR001063
Family
Ribosomal protein L22/L17
PD001032\"[29-109]TRibosomal_L22
G3DSA:3.90.470.10\"[1-109]TRibosomal_L22
PF00237\"[5-109]TRibosomal_L22
PS00464\"[83-107]TRIBOSOMAL_L22
SSF54843\"[1-110]TRibosomal_L22
InterPro
IPR005727
Family
Ribosomal protein L22, bacterial and organelle form
PTHR13501\"[13-107]TRibosom_L22_bac
TIGR01044\"[5-107]TrplV_bact


","BeTs to 25 clades of COG0091COG name: Ribosomal protein L22Functional Class: JThe phylogenetic pattern of COG0091 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-61) to 3/3 blocks of the IPB001063 family, which is described as \"Ribosomal protein L22p / L17e\". Interpro entry for IP:IPR001063. IPB001063A 5-35 3.3e-17 IPB001063B 36-61 3.4e-13 IPB001063C 64-107 9.5e-29","Residues 11 to 107 match (7e-10) PD:PD411961 which is described as RIBOSOMAL PUTATIVE 25606-24374 PROTEIN-MITOCHONDRIAL COPPER-BINDING PROTEIN-LIKE 50S CHLOROPLAST RPS3-PSD1 L22 ","","","","","","","","","","","","Mon Dec 9 14:31:18 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00363 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 109 (E-value = 8.3e-59) place AA00363 in the Ribosomal_L22 family which is described as Ribosomal protein L22p/L17e (PF00237)","","","","","Wittmann-Liebold,B. and Greuer,B. Amino acid sequence of protein L22 from the large subunit ofthe Escherichia coli ribosome. FEBS Lett. 121(1): 105-112.1980. PubMed: 7007072.","Mon Jan 13 17:32:20 2003","Mon Dec 9 14:31:18 2002","1","","","" "AA00365","246326","246054","273","ATGCCACGTTCTCTCAAGAAAGGTCCTTTCCTTGACCTACACTTGTTGAAGAAGGTAGAGAAGGCGGTGGAAAGCGGGGATAAAAAACCAATTAAAACCTGGTCCCGTCGTTCAATGATCATTCCATCAATGATCGGATTGACCATCGCAGTCCATAATGGTCGTCAGCACGTTCCTGTTTATGTTTCTGATGAAATGATCGGTCATAAATTAGGCGAATTTGCACCGACTCGTACTTACCGCGGTCATGCTGCGGACAAGAAAGCTAAGAAG","","","10242","MPRSLKKGPFLDLHLLKKVEKAVESGDKKPIKTWSRRSMIIPSMIGLTIAVHNGRQHVPVYVSDEMIGHKLGEFAPTRTYRGHAADKKAKK","246054","","30S ribosomal protein S19","Cytoplasm, Periplasm","","
InterPro
IPR002222
Family
Ribosomal protein S19/S15
PD001012\"[10-83]TRS19_HAEIN_P44385;
PR00975\"[33-52]T\"[53-65]T\"[65-80]TRIBOSOMALS19
G3DSA:3.30.860.10\"[1-90]Tno description
PTHR11880\"[1-89]TRIBOSOMAL PROTEIN S19P FAMILY MEMBER
PF00203\"[3-83]TRibosomal_S19
PS00323\"[53-77]TRIBOSOMAL_S19
InterPro
IPR005732
Family
Ribosomal protein S19, bacterial and organelle form
TIGR01050\"[1-91]TrpsS_bact: ribosomal protein S19


","No hits to the COGs database.","Significant hit ( 1.2e-47) to 2/2 blocks of the IPB002222 family, which is described as \"Ribosomal protein S19\". Interpro entry for IP:IPR002222. IPB002222A 3-15 1e-05 IPB002222B 34-83 1.1e-40","Residues 2 to 83 match (1e-38) PD:PD001012 which is described as RIBOSOMAL S19 30S RRNA-BINDING PROTEOME COMPLETE CHLOROPLAST MITOCHONDRION 40S S15 ","","","","","","","","","","","","Mon Dec 9 14:35:53 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00365 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 83 (E-value = 6.7e-54) place AA00365 in the Ribosomal_S19 family which is described as Ribosomal protein S19 (PF00203)","","","","","Yaguchi,M. and Wittmann,H.G. Primary structure of protein S19 from the small ribosomalsubunit of Escherichia coli FEBS Lett. 88 (2), 227-230 (1978) PubMed: 348496 ","Mon Jan 13 17:56:19 2003","Mon Jan 13 17:33:18 2003","1","","","" "AA00366","247173","246355","819","ATGGCTATCGTTAAATGTAAGCCGACCTCCGCTGGTCGTCGTCATGTTGTTAAAGTTGTTAACCCTGAATTGCACAAAGGTAAACCTTTCGCTGCGCTTTTAGATACTAAATCTAAAACCGGTGGTCGTAACAACTATGGTCGTATTACTACTCGTCACATCGGTGGCGGTCATAAGCAACACTATCGTTTAATTGATTTCAAACGTAATAAATTAGACATTCCTGGTGTTGTTGAGCGTTTAGAATACGATCCGAATCGTTCTGCAAATATCGCTTTAGTGCTTTATAAAGACGGTGAACGTCGTTATATCTTAGCGCCTAAAGGCTTGGCTGCAGGTGATCAAATCCAAGCGGGTGCGCATGCACCAATTAAAGTTGGTAATGCATTACCAATGCGCAATATTCCGGTTGGTTCTACCGTACATAACGTTGAATTAAAACCTGGTAAAGGCGGTCAAATTGCCCGCTCTGCAGGTAGCTATGTACAGATCATCGCCCGTGAAGGTAACTATGTTACTTTACGTCTTCGCTCCGGTGAAATGCGTAAAGTATTAGCTGAGTGTTCTGCAACCATCGGTGAAGTAGGTAACTCAGAGCATATGCTTCGCGTATTGGGTAAAGCAGGTGCTAATCGCTGGAGAGGTGTACGCCCTACAGTTCGTGGTACTGCAATGAACCCGGTAGATCACCCACATGGTGGTGGTGAAGGTCGTAACTTTGGTAAACACCCGGTAACACCTTGGGGCGTTCAAACCAAAGGTAAGAAAACTCGCCATAACAAACGTACTGATAAATATATCGTACGTCGTCGTGGTAAA","","","29949","MAIVKCKPTSAGRRHVVKVVNPELHKGKPFAALLDTKSKTGGRNNYGRITTRHIGGGHKQHYRLIDFKRNKLDIPGVVERLEYDPNRSANIALVLYKDGERRYILAPKGLAAGDQIQAGAHAPIKVGNALPMRNIPVGSTVHNVELKPGKGGQIARSAGSYVQIIAREGNYVTLRLRSGEMRKVLAECSATIGEVGNSEHMLRVLGKAGANRWRGVRPTVRGTAMNPVDHPHGGGEGRNFGKHPVTPWGVQTKGKKTRHNKRTDKYIVRRRGK","246355","","50S ribosomal protein L2","Periplasm, Cytoplasm, Extracellular","","
InterPro
IPR002171
Family
Ribosomal protein L2
PTHR13691\"[93-271]TRibosomal_L2
PF00181\"[42-118]TRibosomal_L2
PF03947\"[124-251]TRibosomal_L2_C
PS00467\"[218-229]TRIBOSOMAL_L2
InterPro
IPR005880
Family
Ribosomal protein L2, bacterial and organelle form
PTHR13691:SF5\"[93-271]TRibosom_L2_bac
TIGR01171\"[3-273]TrplB_bact
InterPro
IPR008991
Domain
Translation protein SH3-like
SSF50104\"[127-267]TTransl_SH3_like
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[38-114]TOB_NA_bd_sub
InterPro
IPR014722
Domain
Translation protein SH3-like, subgroup
G3DSA:2.30.30.30\"[118-197]TRibosomal_L2
noIPR
unintegrated
unintegrated
SSF50249\"[38-126]TNucleic_acid_OB


","BeTs to 26 clades of COG0090COG name: Ribosomal protein L2Functional Class: JThe phylogenetic pattern of COG0090 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 3e-121) to 5/5 blocks of the IPB002171 family, which is described as \"Ribosomal protein L2\". Interpro entry for IP:IPR002171. IPB002171A 47-69 2.7e-15 IPB002171B 74-113 6.7e-28 IPB002171C 127-164 5e-29 IPB002171D 174-213 3.4e-25 IPB002171E 218-238 4.7e-19","Residues 49 to 74 match (5e-07) PD:PD467076 which is described as RIBOSOMAL L2 CHLOROPLAST 50S COMPLETE PROTEOME RRNA-BINDING MITOCHONDRION RPL2 MITOCHONDRIAL ","","","","","","","","","","","","Mon Dec 9 14:38:36 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00366 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 124 to 251 (E-value = 1.3e-83) place AA00366 in the Ribosomal_L2_C family which is described as Ribosomal Proteins L2, C-terminal domain (PF03947)","","","","","Marty I, Meyer Y. cDNA nucleotide sequence and expression of a tobaccocytoplasmic ribosomal protein L2 gene. Nucleic Acids Res 1992 Apr 11;20(7):1517-22 PMID: 1579444","Mon Jan 13 17:33:50 2003","Mon Dec 9 14:38:36 2002","1","","","" "AA00367","247496","247197","300","ATGAGTCAAGAACGTTTGCTAAAAGTGCTTAAAGCACCGCATATCTCTGAGAAAGCAACAAATAACGCTGAGAAGTCAAACACTATCGTTTTCAAAGTAGCTTTAGATGCAAATAAAGTAGAAATTACTAACGCAGTAGAGCAACTTTTTGAAGTGAAAGTGGATTCCGTTCGTACCGTAGTGGTGAAAGGTAAAACTAAACGCCGTGGTGCTAAGATCGGACGTCGCAGTGACTGGAAAAAAGCTTATGTTACACTTCAAGAAGGACAATCTTTGGACTTCGTTGAAGGTGCAGCAGAG","","","11125","MSQERLLKVLKAPHISEKATNNAEKSNTIVFKVALDANKVEITNAVEQLFEVKVDSVRTVVVKGKTKRRGAKIGRRSDWKKAYVTLQEGQSLDFVEGAAE","247197","","50S ribosomal protein L23","Cytoplasm","","
InterPro
IPR001014
Family
Ribosomal L23 protein
PS00050\"[80-95]TRIBOSOMAL_L23
InterPro
IPR012677
Domain
Nucleotide-binding, alpha-beta plait
G3DSA:3.30.70.330\"[3-99]Ta_b_plait_nuc_bd
InterPro
IPR012678
Domain
Ribosomal L23 and L15e, core
SSF54189\"[3-99]TL23_L15e_core
InterPro
IPR013025
Domain
Ribosomal protein L25/L23
PD001141\"[11-97]TRibosomal_L23
PF00276\"[7-98]TRibosomal_L23
noIPR
unintegrated
unintegrated
PTHR11620\"[8-61]TPTHR11620


","BeTs to 23 clades of COG0089COG name: Ribosomal protein L23Functional Class: JThe phylogenetic pattern of COG0089 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 7.5e-17) to 1/1 blocks of the IPB001014 family, which is described as \"Ribosomal L23 protein\". Interpro entry for IP:IPR001014. IPB001014 27-59 7.2e-17","Residues 71 to 98 match (2e-08) PD:PD591663 which is described as PROTEOME COMPLETE RPL23 RIBOSOMAL L23 ","","","","","","","","","","","","Mon Dec 9 14:40:19 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00367 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 98 (E-value = 1e-37) place AA00367 in the Ribosomal_L23 family which is described as Ribosomal protein L23 (PF00276)","","","","Hayashida,H., Hotokezaka,H., Ohara,N., Kimura,M., Takagi,O. andYamada,T.Molecular analysis of a new insertion sequence from Actinobacillus(Haemophilus) actinomycetemcomitans FDC Y4Microbiology 142 (Pt 9), 2449-2452 (1996)PubMed: 96425869","Wittmann-Liebold,B. and Greuer,B. Primary structure of protein L23 from the Escherichia coliribosome FEBS Lett. 108 (1), 69-74 (1979) PubMed: 391594 Arnold,R.J. and Reilly,J.P. Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry Anal. Biochem. 269 (1), 105-112 (1999) PubMed: 10094780 ","Mon Dec 9 14:41:17 2002","Mon Dec 9 14:41:17 2002","1","","","" "AA00368","248095","247496","600","ATGGAATTACAAGTTGTAGGTGCTAACGCACTCACTGTTTCTGAAACTACCTTCGGCCGTGAGTTTAACGAAGCATTGATTCACCAAGTTGTTGTTGCTTATGCAGCAGGTGCCCGTCAAGGTTCTCGTGCACAAAAAACTCGTGCTGAAGTGTCCGGTTCAGGTAAAAAACCTTGGCGTCAAAAAGGTACAGGTCGCGCTCGTTCAGGTGATATTAGATCACCAATTTGGCGTTCCGGTGGTGTCACTTTCGCAGCGAAACCACAAGATCACAGCCAAAAAGTGAACAAGAAAATGTACCGTGGTGCAATTAAGAGCATTCTTTCCGAGCTTGTTCGTCAAGATCGTTTAGTTGTTGTTGATAAATTTGAAATTGATGCACCAAAAACCAAAGTATTAGTACAAAAATTAAAAGAATTAGCACTGGAAGATGTGTTAATCATCACAGCAAGTTTAGATGAAAATCTATTCTTAGCAGCGCGTAACTTATATAAAGTAGATGTTCGTGATGCTCAAGGTATTGATCCGGTAAGTTTGATCGCTTTCGATAAAGTGGTTGTTACTGTGGATGCTGTGAAGCAAATTGAGGAGATGTTAGCA","","","21985","MELQVVGANALTVSETTFGREFNEALIHQVVVAYAAGARQGSRAQKTRAEVSGSGKKPWRQKGTGRARSGDIRSPIWRSGGVTFAAKPQDHSQKVNKKMYRGAIKSILSELVRQDRLVVVDKFEIDAPKTKVLVQKLKELALEDVLIITASLDENLFLAARNLYKVDVRDAQGIDPVSLIAFDKVVVTVDAVKQIEEMLA","247496","","50S ribosomal protein L4","Cytoplasm","","
InterPro
IPR002136
Family
Ribosomal protein L4/L1e
PF00573\"[10-198]TRibosomal_L4
SSF52166\"[1-199]TRibosomal_L4/L1E
InterPro
IPR013005
Family
Ribosomal protein L4/L1e, bacterial like
PTHR10746\"[12-200]TRibos_L4_L1E_bac
InterPro
IPR015498
Family
Ribosomal protein L4
PTHR10746:SF2\"[12-200]TRibosomal_L4
noIPR
unintegrated
unintegrated
G3DSA:3.40.1370.10\"[74-200]TG3DSA:3.40.1370.10


","No hits to the COGs database.","","Residues 45 to 85 match (2e-12) PD:PD385768 which is described as CHLOROPLAST RIBOSOMAL CHROMOSOME FROM L4 DNA-DIRECTED RNA MATURASE-LIKE POLYMERASE ORF519 ","","","","","","","","","","","","Mon Dec 9 14:43:27 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00368 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 10 to 198 (E-value = 3.9e-56) place AA00368 in the Ribosomal_L4 family which is described as Ribosomal protein L4/L1 family (PF00573)","","","","","Arnold,R.J. and Reilly,J.P. Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry Anal. Biochem. 269 (1), 105-112 (1999) PubMed: 10094780 ","Mon Jan 13 17:35:46 2003","Mon Dec 9 14:43:27 2002","1","","","" "AA00369","248740","248114","627","ATGATTGGTTTAGTCGGTCGTAAAGTCGGTATGACCCGTATCTTTAATGAAGACGGCGTGTCAGTACCGGTTACCGTTATCGAAATCGAAGCCAACCGCGTAACTCAAGTTAAAACTCTTGAAAACGATGGCTATACTGCAGTTCAAGTTACAACCGGTTCTAAAAAAGCGAGCCGTGTGACTAAGCCTGAAGCGGGTCATTTCGTGAAAGCCGGTGTTGAAGCCGGTCGCGGTTTATGGGAATTTCGTACTGAAGGTGAAGAATTCACTTTAGGTCAAGAAATTAATGTTGACATCTTTTTTGCAGATGTTAAAAAAGTCGATGTTACCGGTACATCTAAAGGTAAAGGCTTCCAAGGTGGTGTTAAACGTTGGAACTTCCGCACTCAAGATGCTACCCACGGTAACTCTTTATCACATCGTGTCCTTGGTTCTATTGGTCAAAACCAAACTCCGGGCCGTGTGTTTAAAGGCAAAAAAATGGCAGGACACTTAGGTAATGAGCGTGTAACCGTTCAATCACTTGAAGTTGTTCGTGTAGATGCTGAGCGTAAATTGCTATTAGTGAAAGGCGCCGTTCCTGGTGCTACCGGTAGTGATGTTATCGTTAAGCCGGCAGTTAAAGCA","","","22457","MIGLVGRKVGMTRIFNEDGVSVPVTVIEIEANRVTQVKTLENDGYTAVQVTTGSKKASRVTKPEAGHFVKAGVEAGRGLWEFRTEGEEFTLGQEINVDIFFADVKKVDVTGTSKGKGFQGGVKRWNFRTQDATHGNSLSHRVLGSIGQNQTPGRVFKGKKMAGHLGNERVTVQSLEVVRVDAERKLLLVKGAVPGATGSDVIVKPAVKA","248114","","50S ribosomal protein L3","Cytoplasm, Extracellular","","
InterPro
IPR000597
Family
Ribosomal protein L3
PD001374\"[113-166]TRL3_HAEIN_P44344;
PF00297\"[8-204]TRibosomal_L3
PS00474\"[101-124]TRIBOSOMAL_L3
noIPR
unintegrated
unintegrated
G3DSA:4.10.960.10\"[114-165]Tno description
PTHR11229\"[1-208]T50S RIBOSOMAL PROTEIN L3


","No hits to the COGs database.","Significant hit ( 6.4e-21) to 1/1 blocks of the IPB000597 family, which is described as \"Ribosomal protein L3\". Interpro entry for IP:IPR000597. IPB000597 99-135 6.1e-21","Residues 122 to 180 match (8e-08) PD:PD504290 which is described as RIBOSOMAL L3 50S ","","","","","","","","","","","","Mon Dec 9 14:45:23 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00369 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 204 (E-value = 1.8e-96) place AA00369 in the Ribosomal_L3 family which is described as Ribosomal protein L3 (PF00297)","","","","","Muranova,T.A., Muranov,A.V., Markova,L.F. and Ovchinnikov,Y.A.The primary structure of ribosomal protein L3 from Escherichiacoli 70 S ribosomes FEBS Lett. 96 (2), 301-305 (1978) PubMed: 365579 Zurawski,G. and Zurawski,S.M.Structure of the Escherichia coli S10 ribosomal protein operonNucleic Acids Res. 13 (12), 4521-4526 (1985)PubMed: 3892488","","Mon Jan 13 17:37:14 2003","1","","","" "AA00370","249068","248760","309","ATGCAGAACCAAAGAATCCGTATCCGTCTTAAAGCGTTTGATCATCGTTTGATCGATCAATCCACGGCGGAGATCGTTGAAACAGCTAAACGTACCGGTGCACAAGTGCGTGGTCCGATTCCTTTACCAACTCGTAAAGAGCGTTTCACAGTATTGATTTCTCCACACGTAAACAAAGATGCACGTGACCAATATGAAATCCGTACTCACAAACGTTTAGTTGATATTGTTGAGCCAACAGAAAAAACTGTTGATGCGTTGATGCGTTTAGACTTGGCTGCCGGCGTTGACGTGCAGATCAGCCTAGGT","","","11750","MQNQRIRIRLKAFDHRLIDQSTAEIVETAKRTGAQVRGPIPLPTRKERFTVLISPHVNKDARDQYEIRTHKRLVDIVEPTEKTVDALMRLDLAAGVDVQISLG","248760","","30S ribosomal protein S10","Cytoplasm","","
InterPro
IPR001848
Family
Ribosomal protein S10
PD001272\"[13-100]TRS10_HAEIN_P44378;
PR00971\"[5-18]T\"[40-55]T\"[61-75]TRIBOSOMALS10
G3DSA:3.30.70.600\"[3-100]Tno description
PTHR11700\"[1-102]T30S RIBOSOMAL PROTEIN S10 FAMILY MEMBER
PF00338\"[5-100]TRibosomal_S10
PS00361\"[29-44]TRIBOSOMAL_S10
InterPro
IPR005731
Family
Ribosomal protein S10, bacterial form
PTHR11700:SF2\"[1-102]T30S RIBOSOMAL PROTEIN S10
TIGR01049\"[4-102]TrpsJ_bact: ribosomal protein S10


","BeTs to 26 clades of COG0051COG name: Ribosomal protein S10Functional Class: JThe phylogenetic pattern of COG0051 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 5.7e-36) to 1/1 blocks of the IPB001848 family, which is described as \"Ribosomal protein S10\". Interpro entry for IP:IPR001848. IPB001848 14-68 4.7e-36","Residues 5 to 100 match (3e-40) PD:PD001272 which is described as RIBOSOMAL 30S S10 PROTEOME COMPLETE S10P 40S S20 CHLOROPLAST S22 ","","","","","","","","","","","","Mon Dec 9 14:49:17 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00370 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 100 (E-value = 7.5e-61) place AA00370 in the Ribosomal_S10 family which is described as Ribosomal protein S10p/S20e (PF00338)","","","","","Shibata Y, Kuramitsu HK. Isolation and preliminary characterization of the Streptococcus mutans rpsJ gene.Oral Microbiol Immunol. 1996 Dec;11(6):407-11.PMID: 9467374Olins,P.O. and Nomura,M. Regulation of the S10 ribosomal protein operon in E. coli: nucleotide sequence at the start of the operon Cell 26 (2 Pt 2), 205-211 (1981) PubMed: 7037196 ","","Mon Jan 13 17:38:26 2003","1","","","" "AA00371","250214","249321","894","ATGGATATTCGACATTTACGCTATTTCGTTTCAATCGTGGATAACGACTTCAATCTGAGCAGGGCTTCATTGAATCTCTACGTTTCTCAGCCCGCGCTGAGCATGATGATCAGCGATTTTGAAAATAAGGAAGGGGTGCAGTTGTTTAAACGGGCGCAGGGGAAAATTGTCGGATTAACTTATGTGGGCGAAAATTACTACCGTGATGCCAAAGAGGTTATAAAAAAATATAATGAAATGCACTCAAATCTGCATAAGTCGATCGAGCAGATAAAGGGGCATATTTCAATCGGCATACCGCCGTTGATCCTGTCCGTCGTTTTTTCCGAAGTCATGCCGAAACTGATTCTGAACAATCCGGAGATTAATTTCACGATTAAGGAATTGGGCGCTTATTTATTAAAAAGCGATCTGTTGTTGGAAAATATCGATTTCGCCGTTCTGTTAAATCCGGAGAGAATTTCTAAAAACATCATAGAATCTTACGAAATACACCGTTCGGAACTCTCCCTGTTCTTATCGCCAAAGCATCATTTATCCGCAAAAGAGAACATTACATGGCGCGATCTGCACGGCGAAAAGATAGTGATTTTTGATCAGACGTTTATGATTCATCATCAATTGGTCGAATCTTTTGAACGGCATAATGTCTATCCGAATATCGTCTTGAAATCGAGTTCGTGGGACTTTTTGTTATACTCGGTAAAAATTAACGAAAGCCTATTAACGATTTTGCCCTTGCCGATGTACGAACAATATAAATCGACGGAATTCATTTGCCGGAGAATGGAAGAAGCCATTCCTTGGAGTGTAACCTTGTGCCGCTTAAAGAAAAATTGCTATACCAATGTTGAAGAATACATTTTCGATTCGCTGTTAAAGGCGTTTAAACCG","","","35437","MDIRHLRYFVSIVDNDFNLSRASLNLYVSQPALSMMISDFENKEGVQLFKRAQGKIVGLTYVGENYYRDAKEVIKKYNEMHSNLHKSIEQIKGHISIGIPPLILSVVFSEVMPKLILNNPEINFTIKELGAYLLKSDLLLENIDFAVLLNPERISKNIIESYEIHRSELSLFLSPKHHLSAKENITWRDLHGEKIVIFDQTFMIHHQLVESFERHNVYPNIVLKSSSWDFLLYSVKINESLLTILPLPMYEQYKSTEFICRRMEEAIPWSVTLCRLKKNCYTNVEEYIFDSLLKAFKP","249321","","transcriptional regulator","Cytoplasm","","
InterPro
IPR000215
Family
Proteinase inhibitor I4, serpin
PS00284\"[196-206]?SERPIN
InterPro
IPR000847
Domain
Bacterial regulatory protein, LysR
PF00126\"[3-64]THTH_1
PS50931\"[1-59]THTH_LYSR
InterPro
IPR005119
Domain
LysR, substrate-binding
PF03466\"[88-297]TLysR_substrate
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[1-89]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[168-269]Tno description


","BeTs to 11 clades of COG0583COG name: Transcriptional regulatorFunctional Class: KThe phylogenetic pattern of COG0583 is a-m----q-drlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 7.1e-09) to 1/1 blocks of the IPB000847 family, which is described as \"Bacterial regulatory protein, LysR family\". Interpro entry for IP:IPR000847. IPB000847 18-51 6.9e-09","Residues 179 to 288 match (1e-24) PD:PD415097 which is described as COMPLETE PROTEOME LYSR FAMILY TRANSCRIPTION TRANSCRIPTIONAL REGULATION REGULATOR DNA-BINDING REGULATOR ","","","","","Wed Feb 19 07:39:20 2003","","","","","","","Wed Feb 19 07:39:20 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00371 is paralogously related to AA01999 (2e-13), AA01513 (1e-11), AA00940 (3e-11), AA01794 (2e-05) and AA02539 (1e-04).","","","","","","Residues 88 to 297 (E-value = 5.7e-15) place AA00371 in the LysR_substrate family which is described as LysR substrate binding domain (PF03466)","","","","","Sung,Y.C. and Fuchs,J.A.The Escherichia coli K-12 cyn operon is positively regulated by amember of the lysR familyJ. Bacteriol. 174 (11), 3645-3650 (1992)PubMed: 1592818","","Mon Dec 9 15:04:02 2002","1","","","" "AA00372","250488","251138","651","ATGACTAAAAAAAGAATTGATCTATCAGATGTAAAAAATCATTTACATGATGGAATGAGCATTATGTTCGGTGGCTTTATGGGTATCGGCACACCGGAAAAGCTGGTTAAGGAAATTCTTGATTCGGGCGTTAAAGATCTCACCCTGATCGGTAACGATACCGCATTCGTCGATACCGGCGTCGGGCCGTTAATCACCAACAATCGGGTGAAACGGGTTATCGCCTCGCATATCGGCACCAATCCGGAAACCGGCAAAAAAATGATTGCCGGCGAAATTGACGTCGAACTGGTTCCGCAAGGCACGTTAGCCGAACGGGTTCGGGCGGGCGGCGCTGGATTAGGCGGCATTCTCACACCGACCGGCGTCGGCACCGTGGTGGAGGAAGGCAAACAGAAAATTCAGATAAACGGCGTCGAACACCTGATTGAATTACCGTTAAAAGCCGACCTTGCCATTGTTCGGGCAAAAAAAGCCGATGAAGCCGGCAACCTTGTCTATGAATTATCCGCACAAAACTTCAATCCTCTCATTGCACTCGCCTCCAAAACCGTCATTGTCCAAGCCGACCAAGTCGTAAAAACCGGCGATATTTCACCGGACGCCGTCGTCACCCCCGCCGCACTGGTGGACTATATCGTTTACCCGGAA","","","22898","MTKKRIDLSDVKNHLHDGMSIMFGGFMGIGTPEKLVKEILDSGVKDLTLIGNDTAFVDTGVGPLITNNRVKRVIASHIGTNPETGKKMIAGEIDVELVPQGTLAERVRAGGAGLGGILTPTGVGTVVEEGKQKIQINGVEHLIELPLKADLAIVRAKKADEAGNLVYELSAQNFNPLIALASKTVIVQADQVVKTGDISPDAVVTPAALVDYIVYPE","251138","","acetate CoA-transferase (alpha subunit)","Cytoplasm","","
InterPro
IPR004163
Binding_site
Coenzyme A transferase binding site
PS01273\"[17-32]TCOA_TRANSF_1
InterPro
IPR004165
Family
Coenzyme A transferase
PTHR13707\"[25-214]TKETOACID-COENZYME A TRANSFERASE
PF01144\"[5-216]TCoA_trans
InterPro
IPR012792
Domain
3-oxoacid CoA-transferase, subunit A
TIGR02429\"[1-216]TpcaI_scoA_fam: 3-oxoacid CoA-transferase, A
noIPR
unintegrated
unintegrated
G3DSA:3.40.1080.10\"[2-214]Tno description
PTHR13707:SF3\"[25-214]TBUTYRATE-ACETOACETATE COA-TRANSFERASE-RELATED


","BeTs to 11 clades of COG1788COG name: Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunitFunctional Class: IThe phylogenetic pattern of COG1788 is ao-p-z---drlb-ef-h--uj----Number of proteins in this genome belonging to this COG is","Significant hit ( 3.6e-19) to 1/1 blocks of the IPB001618 family, which is described as \"Coenzyme A transferase\". Interpro entry for IP:IPR001618. IPB001618 140-193 3.2e-19","Residues 32 to 195 match (7e-07) PD:PD477798 which is described as TRANSFERASE SUBUNIT PROTEOME COMPLETE A COA-TRANSFERASE GLUTACONATE B GCT COA-TRANSFERASE ","","","","","Mon Feb 17 06:13:33 2003","","","","","","","Sun Feb 16 17:05:58 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00372 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 216 (E-value = 1.1e-83) place AA00372 in the CoA_trans family which is described as Coenzyme A transferase (PF01144)","","","",""," Korolev S, Koroleva O, Petterson K, Gu M, Collart F, Dementieva I, Joachimiak A. Related Articles, Links Autotracing of Escherichia coli acetate CoA-transferase alpha-subunit structure using 3.4 A MAD and 1.9 A native data. Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2116-21. PMID: 12454473 Takahashi N, Sato T, Yamada T. Related Articles, Links Metabolic pathways for cytotoxic end product formation from glutamate- and aspartate-containing peptides by Porphyromonas gingivalis. J Bacteriol. 2000 Sep;182(17):4704-10. PMID: 10940008 Fischer,R.J., Helms,J. and Durre,P.Cloning, sequencing, and molecular analysis of the sol operon ofClostridium acetobutylicum, a chromosomal locus involved insolventogenesisJ. Bacteriol. 175 (21), 6959-6969 (1993)PubMed: 8226639Petersen,D.J., Cary,J.W., Vanderleyden,J. and Bennett,G.N.Sequence and arrangement of genes encoding enzymes of theacetone-production pathway of Clostridium acetobutylicum ATCC824Gene 123 (1), 93-97 (1993)PubMed: 8423010","","Sun Feb 16 17:05:58 2003","1","","","" "AA00373","251153","251815","663","ATGAACGCAAAAGAATTAATCGCACGCCGTATCGCAATGGAACTCAACGACGGTGATATCGTAAATTTAGGCATCGGCTTACCGACCCAAGTGGCGAATTATTTGCCCGACGACGTCGATATTACATTGCAATCGGAAAACGGTTTCATGGGATTAACCGCATTGGATCCCGAGTATCCGAATCCCAATCTGGTCAACGCGGGCGGACAACCTTGCGGCATTAAAGCGGGCGGCGCCACCTTCGACAGCGCATTCTCTTTCGCCTTGATTCGCGGCGGTCACGTGGATGCCTGCGTGTTAGGCGGTCTGGAAGTGGATCAACAAGGCAACCTCGCCAACTGGATGGTGCCGGGCAAAATGGTGCCGGGCATGGGCGGTGCAATGGATTTAGTGACCGGTTCCCGCAAAGTGATCATCGGCATGGAACACTGTGCCAAATCGGGAAGTTCCAAGATTCTGAAACAATGCACCTTACCGTTAACGGCGCGCAATAAAGTCACCATGGTCGTTACCGAATTGGCGGTATTCCGCTTTATCGACGATCAGTTAGTGCTTAAAGAACACGCACCCGATGTCGATTTAGACACGATTCGAGGCAAAACGGAAGCGGATTTCATTGTCGCCGACGATTTCAAAGAAATGCATATCAGCCAAAAAGGAATG","","","23617","MNAKELIARRIAMELNDGDIVNLGIGLPTQVANYLPDDVDITLQSENGFMGLTALDPEYPNPNLVNAGGQPCGIKAGGATFDSAFSFALIRGGHVDACVLGGLEVDQQGNLANWMVPGKMVPGMGGAMDLVTGSRKVIIGMEHCAKSGSSKILKQCTLPLTARNKVTMVVTELAVFRFIDDQLVLKEHAPDVDLDTIRGKTEADFIVADDFKEMHISQKGM","251815","","CoA-transferase (beta)","Cytoplasm","","
InterPro
IPR004165
Family
Coenzyme A transferase
PTHR13707\"[1-218]TKETOACID-COENZYME A TRANSFERASE
PF01144\"[4-200]TCoA_trans
InterPro
IPR012791
Domain
3-oxoacid CoA-transferase, subunit B
TIGR02428\"[2-207]TpcaJ_scoB_fam: 3-oxoacid CoA-transferase, B
noIPR
unintegrated
unintegrated
G3DSA:3.40.810.20\"[5-211]Tno description


","BeTs to 10 clades of COG2057COG name: Acyl CoA:acetate/3-ketoacid CoA transferase, beta subunitFunctional Class: IThe phylogenetic pattern of COG2057 is -o-p-z---drlb-ef-h--uj----Number of proteins in this genome belonging to this COG is","Significant hit ( 2.6e-33) to 1/1 blocks of the IPB001618 family, which is described as \"Coenzyme A transferase\". Interpro entry for IP:IPR001618. IPB001618 86-139 2.4e-33","Residues 4 to 207 match (6e-89) PD:PD004976 which is described as TRANSFERASE COMPLETE PROTEOME SUBUNIT B COA-TRANSFERASE A SUCCINYL-COA:3-KETOACID-COENZYME BETA 3-OXOADIPATE ","","","","","Mon Feb 17 06:13:09 2003","","","","","","","Mon Dec 9 16:19:49 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00373 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 200 (E-value = 2.4e-55) place AA00373 in the CoA_trans family which is described as Coenzyme A transferase (PF01144)","","","","","Fischer,R.J., Helms,J. and Durre,P.Cloning, sequencing, and molecular analysis of the sol operon ofClostridium acetobutylicum, a chromosomal locus involved insolventogenesisJ. Bacteriol. 175 (21), 6959-6969 (1993)PubMed: 8226639Petersen,D.J., Cary,J.W., Vanderleyden,J. and Bennett,G.N.Sequence and arrangement of genes encoding enzymes of theacetone-production pathway of Clostridium acetobutylicum ATCC824Gene 123 (1), 93-97 (1993)PubMed: 8423010Cary,J.W., Petersen,D.J., Papoutsakis,E.T. and Bennett,G.N.Cloning and expression of Clostridium acetobutylicum ATCC 824acetoacetyl-coenzyme A:acetate/butyrate:coenzyme A-transferase inEscherichia coliAppl. Environ. Microbiol. 56 (6), 1576-1583 (1990)PubMed: 2383002","","Mon Feb 17 06:04:03 2003","1","","","" "AA00374","251821","253161","1341","ATGATTAGCCGCGTATCTCGTTTTATGACCGCACTGGTCAGCAAATATCTGCCGGATCCGCTAATCTTCGCCGTGTTGCTTACCTTTATCACCTTCGTGTGTGCGTTATGTTTAACGGACAGCACGCCTGTTGACCTGGTCAACATGTGGGGTGACGGGTTCTGGAATCTGCTCGCTTTCGGTATGCAAATGGCGTTGATTGTGGTGACGGGAAATGCCTTGGCGACTTCGCCGCAAATCAAGTCCTTCCTGACTACCATGGCATCGCTGGCAAAAACACCGGCACAAGGCGTGGTGCTCGTCACCTTCATGGGTTCTATCGCCTGTATTATCAACTGGGGCTTCGGCTTAGTGGTCGGCGCGATGTTCGCCAAAGAAGTGGCGCGGCGGGTGAAAGGCAGCGACTACGCCTTGTTAATCGCCTGCGCCTATATCGCCTTTATGACATGGGGCGGCGGTTTGTCGGGTTCCATGCCGTTACTGGCGGCGACCCCGGGAAATCCGGTGGCGCACATTATGGTGACGGAAAGCAATCCGCAAGGCATTATTCCGGCGACCGAAACGCTGTTCTCAAGCTATAACCTCTTTATCACTGGCTGTCTGATACTCTGTTTGCCGTTTATCACCTACATGATGATGCCGAAAAGCGGCGAAGTGAAAAGTATCGATCCGACATTGCTCGCGCCAGATCCCGAATTTACCAAAAAACTGGATCAGAACGCGACGGTAGCGGAGAAAATGGAAGAAAGCCGGCTGCTCGCCTACGCCATCGGTGCGTTGGGTTACGGCTATCTTGCCATGTATTTCCATAAAAACGGCTTCAATCTCACCATTAACAACGTCAACCTCATTTTCCTGATTACCGGCATCGTATTACACGGTTCGCTGATGGCGTATATGCGCGCGATTCTGAATGCCACCCGCAGCACCGCCGGCATTCTCATTCAATTCCCGTTCTACGCTGGCGTGCAATTAATGATGGAACATTCGGGGCTCGGCGGACTCATCACCGAATTCTTTATTAACATCGCCAATAAAGACACCTTCCCGGTGCTGACCTTCTTCAGCTCCGCATTAATCAACTTCGCCGTGCCGTCCGGCGGCGGGCACTGGGTGATTCAAGGGCCGTTCGTCATTCCGGCGGCACAGGCATTGGGCGCAGATCTGGGCAAATCCACTATGGCAATTGCCTACGGTGAACAATGGATGAACATGGCGCAACCGTTCTGGGCGTTACCGGCGTTGGGCATCGCAGGTCTTGGGGTACGGGATATTATGGGATTCTGTATGACCGCACTTATCTTCACCACCCCGATCTTTTTCATCGGATTATATTTCTTT","","","48247","MISRVSRFMTALVSKYLPDPLIFAVLLTFITFVCALCLTDSTPVDLVNMWGDGFWNLLAFGMQMALIVVTGNALATSPQIKSFLTTMASLAKTPAQGVVLVTFMGSIACIINWGFGLVVGAMFAKEVARRVKGSDYALLIACAYIAFMTWGGGLSGSMPLLAATPGNPVAHIMVTESNPQGIIPATETLFSSYNLFITGCLILCLPFITYMMMPKSGEVKSIDPTLLAPDPEFTKKLDQNATVAEKMEESRLLAYAIGALGYGYLAMYFHKNGFNLTINNVNLIFLITGIVLHGSLMAYMRAILNATRSTAGILIQFPFYAGVQLMMEHSGLGGLITEFFINIANKDTFPVLTFFSSALINFAVPSGGGHWVIQGPFVIPAAQALGADLGKSTMAIAYGEQWMNMAQPFWALPALGIAGLGVRDIMGFCMTALIFTTPIFFIGLYFF","253161","","short-chain fatty acids transporter","Inner membrane, Cytoplasm","","
InterPro
IPR006160
Family
Short chain fatty acid transporter
PD018634\"[26-170]TATOE_HAEIN_P44051;
PF02667\"[1-447]TSCFA_trans
InterPro
IPR006161
Family
Conserved hypothetical protein 336
TIGR00366\"[4-435]TTIGR00366: conserved hypothetical protein T
noIPR
unintegrated
unintegrated
signalp\"[1-35]?signal-peptide
tmhmm\"[19-39]?\"[54-76]?\"[95-115]?\"[136-156]?\"[190-210]?\"[252-270]?\"[280-300]?\"[425-445]?transmembrane_regions


","BeTs to 7 clades of COG2031COG name: Short chain fatty acids transporterFunctional Class: IThe phylogenetic pattern of COG2031 is a----z-----lb-ef-h--u-----Number of proteins in this genome belonging to this COG is","","Residues 378 to 444 match (6e-26) PD:PD286414 which is described as PROTEOME COMPLETE SHORT-CHAIN ACIDS FATTY TRANSPORTER MEMBRANE TRANSMEMBRANE INNER AF1538 ","","","","","Wed Feb 19 08:25:18 2003","","","","","","","Mon Dec 9 16:35:50 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00374 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00377","253182","254360","1179","ATGGAAAATATCGTTATCGTCAGCGCGGTCAGAACGCCGATCGGCAGCTTTAACGGCAGTCTTGCCGCCGTCAGTGCGGTTGATCTGGGCGCTACCGTGATCAAAGAAGTGATCAAGCGCGCAGACATCGACAGCGCCTTGGTCAACGAAGTGATTATGGGTAATGTGCTGCAAGCCGGTATCGGACAAAACCCTGCCCGTCAAGCTGCACTCAAAGCGGGCGTGGCGAAGGGAATTCCGTCCTACACTGTCAATAAAGTCTGCGGTTCGGGCTTAAAAAGCGTGGCGTTGGGCGTGCAAGCCATTGCCAGCGGCGACGCCGACATCGTGGCGGCCGGCGGCATGGAAAGTATGAGCCAAGCGCCGTACATTCTGGATCATAAAATCCGTTCCGGCGTCAGAATGGGCAATCTGCCGTTGCGCGACAGCATGATCGAAGACGGTCTGACGTGCGCCATAAACCATTACCACATGGGCATTACGGCGGAAAATATCGCCGAACAATACGGTATCAGCCGTGAGGAACAGGATCAGCTTGCGCTGCGTTCGCAAACCCTTGCCTCTCAAGCGGTGCAAAACGGCGTATTCGACAAAGAAATCGTATCTGTCACCGTGAAAACCCGCAAAGGCGACATCGTTGTCTCCCGCGACGAATACCCGAAACCCGACACCACAGCGGAAGGGCTGGCGAAGTTAAGACCGGCATTCAAAAAAGACGGCACCGTCACCGCCGGTAACGCCTCCGGTATTAACGACGGCGCCGCCGCGTTATTGTTAATGAGCGAAAGCAAAGCGAACGCATTAGGACTGAAACCGCTCGCCCGTATCCGCGGTTACGCCAGTGCAGGAGTCGATCCTGCCGTGATGGGATTGGGGCCGGTGCCGGCAACCCAGAAAGCGCTGCGCAAAGCGGGATTGACGCTCGACGATATTGACCTGATCGAAGCGAACGAAGCCTTCGCCTCGCAATTCCTCGGCGTCGGCAGAGAACTGCATTTCAATATGGAGAAAACCAATATCCACGGTGGTGCCATCTCGCTGGGTCACCCTATCGGCGCCAGCGGCGCCAGAATTCTGGTGACGCTGCTGCACAATCTCATTGAGAAAGACAAAAAGCTCGGTCTGGCGACCCTGTGTATCGGCGGCGGGGAAGGCATTTCAGTGATTGTCGAACGGATC","","","40817","MENIVIVSAVRTPIGSFNGSLAAVSAVDLGATVIKEVIKRADIDSALVNEVIMGNVLQAGIGQNPARQAALKAGVAKGIPSYTVNKVCGSGLKSVALGVQAIASGDADIVAAGGMESMSQAPYILDHKIRSGVRMGNLPLRDSMIEDGLTCAINHYHMGITAENIAEQYGISREEQDQLALRSQTLASQAVQNGVFDKEIVSVTVKTRKGDIVVSRDEYPKPDTTAEGLAKLRPAFKKDGTVTAGNASGINDGAAALLLMSESKANALGLKPLARIRGYASAGVDPAVMGLGPVPATQKALRKAGLTLDDIDLIEANEAFASQFLGVGRELHFNMEKTNIHGGAISLGHPIGASGARILVTLLHNLIEKDKKLGLATLCIGGGEGISVIVERI","254360","","acetyl-CoA acetyltransferase (Beta-ketothiolase,3-ketoacyl-CoA thiolase)","Cytoplasm, Periplasm","","
InterPro
IPR002155
Family
Thiolase
PTHR18919\"[64-393]TACETYL-COA C-ACYLTRANSFERASE
PF00108\"[1-263]TThiolase_N
PF02803\"[270-392]TThiolase_C
TIGR01930\"[6-391]TAcCoA-C-Actrans: acetyl-CoA acetyltransfera
PS00098\"[84-102]TTHIOLASE_1
PS00099\"[374-387]TTHIOLASE_3
PS00737\"[339-355]TTHIOLASE_2
noIPR
unintegrated
unintegrated
G3DSA:3.40.47.10\"[1-276]Tno description
PIRSF000429\"[1-393]TAcetyl-CoA acetyltransferase
PTHR18919:SF9\"[64-393]TACETYL-COA ACETYLTRANSFERASE


","BeTs to 19 clades of COG0183COG name: Acetyl-CoA acetyltransferasesFunctional Class: IThe phylogenetic pattern of COG0183 is aompkzy--drlbcefgh--ujx-t-Number of proteins in this genome belonging to this COG is","Significant hit (2.1e-117) to 5/5 blocks of the IPB002155 family, which is described as \"Thiolase\". Interpro entry for IP:IPR002155. IPB002155A 62-108 4.9e-29 IPB002155B 158-203 1e-27 IPB002155C 240-260 5.5e-17 IPB002155D 286-323 1.3e-26 IPB002155E 338-357 3.1e-12","Residues 80 to 125 match (1e-07) PD:PD000145 which is described as PHOSPHOPANTETHEINE SYNTHASE TRANSFERASE POLYKETIDE PROTEOME COMPLETE TYPE I MODULAR MULTIFUNCTIONAL ","","","","","Thu Feb 13 15:57:52 2003","","","","","","","Thu Feb 13 15:57:52 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00377 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 270 to 392 (E-value = 1.7e-74) place AA00377 in the Thiolase_C family which is described as Thiolase, C-terminal domain (PF02803)","","","","","Stim-Herndon,K.P., Petersen,D.J. and Bennett,G.N.Characterization of an acetyl-CoA C-acetyltransferase (thiolase)gene from Clostridium acetobutylicum ATCC 824Gene 154 (1), 81-85 (1995)PubMed: 7867955 Winzer,K., Lorenz,K., Zickner,B. and Durre,P.Differential regulation of two thiolase genes from Clostridiumacetobutylicum DSM 792J. Mol. Microbiol. Biotechnol. 2 (4), 531-541 (2000)PubMed: 11075929Liebergesell,M. and Steinbuchel,A.Cloning and molecular analysis of the poly(3-hydroxybutyric acid)biosynthetic genes of Thiocystis violaceaAppl. Microbiol. Biotechnol. 38 (4), 493-501 (1993)PubMed: 7763384Peoples OP, Sinskey AJ.Poly-beta-hydroxybutyrate biosynthesis in Alcaligenes eutrophusH16. Characterization of the genes encoding beta-ketothiolase andacetoacetyl-CoA reductaseJ. Biol. Chem. 264 (26), 15293-15297 (1989)PubMed: 2670935Peoples,O.P. and Sinskey,A.J.Poly-beta-hydroxybutyrate (PHB) biosynthesis in Alcaligeneseutrophus H16. Identification and characterization of the PHBpolymerase gene (phbC)J. Biol. Chem. 264 (26), 15298-15303 (1989)PubMed: 2670936 ","","Thu Feb 13 15:57:52 2003","1","","","" "AA00378","254928","254464","465","ATGCGAAAGAAACTGTTTGATAACATTGATACGCGCATTCTTAAGGCATTGCAGCGCAACGGAAGATTGCCAAATAACGAGCTTGCCAAAGAAGTTGGCTTATCCAATTCCGCCTGTCTGCGTCGGGTGAACCAGTTGGAAGAAAGCGGTGTTATTGATGGTTATGCAGCGTTATTACATCCCAAAAAACTGAATTGCAATTTGTTGGTTTATGTACAGGGCACGTTTTTTGAAGAAGATCCGGAACTCAAAGAGCGGTTCATTTTTGAAGTGAAATTAATTCCGCAAATTACTGAATGTCATCTGATGGCGGGCAGTTACGATTTCATTTTAAAAATGTGGGTTTCCGATTTGGAAGAATTCAACAGTATAAAAAATAAATATCTCACCAAAGACATCGGAATTAAAACCTTAAAATCCGAAGTGTCGCTGAAAACGGTTAAATCCACGACGGAATTGCCGTTG","","","20799","MRKKLFDNIDTRILKALQRNGRLPNNELAKEVGLSNSACLRRVNQLEESGVIDGYAALLHPKKLNCNLLVYVQGTFFEEDPELKERFIFEVKLIPQITECHLMAGSYDFILKMWVSDLEEFNSIKNKYLTKDIGIKTLKSEVSLKTVKSTTELPL","254464","","leucine-responsive regulatory protein (transcription regulator)","Cytoplasm","","
InterPro
IPR000485
Family
Bacterial regulatory proteins, AsnC/Lrp
PR00033\"[6-22]T\"[22-33]T\"[33-52]THTHASNC
PF01037\"[80-146]TAsnC_trans_reg
SM00344\"[6-115]THTH_ASNC
PS50956\"[6-67]THTH_ASNC_2
PS00519\"[24-50]THTH_ASNC_1
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[6-57]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.920\"[59-155]Tno description


","BeTs to 15 clades of COG1522COG name: Transcriptional regulatorsFunctional Class: KThe phylogenetic pattern of COG1522 is aompkz---dr-b-efgh-n-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.8e-35) to 3/3 blocks of the IPB000485 family, which is described as \"Bacterial regulatory proteins, AsnC family\". Interpro entry for IP:IPR000485. IPB000485A 6-27 6.6e-09 IPB000485B 34-74 2.9e-12 IPB000485C 84-125 2.4e-11","Residues 79 to 148 match (7e-10) PD:PD161972 which is described as PROTEOME COMPLETE TRANSCRIPTION TRANSCRIPTIONAL DNA-BINDING REGULATION REGULATOR REGULATORY ASNC FAMILY ","","","","","","","","","","","","Tue Dec 10 08:13:21 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00378 is paralogously related to AA02734 (4e-28) and AA00387 (9e-11).","","","","","","Residues 30 to 133 (E-value = 1.1e-29) place AA00378 in the AsnC_trans_reg family which is described as AsnC family (PF01037)","","","","","Willins,D.A., Ryan,C.W., Platko,J.V. and Calvo,J.M. Characterization of Lrp, and Escherichia coli regulatory proteinthat mediates a global response to leucine J. Biol. Chem. 266 (17), 10768-10774 (1991) PubMed: 2040596 Friedberg,D., Platko,J.V., Tyler,B. and Calvo,J.M. The amino acid sequence of Lrp is highly conserved in fourenteric microorganisms J. Bacteriol. 177 (6), 1624-1626 (1995) PubMed: 7883720 Haney,S.A., Platko,J.V., Oxender,D.L. and Calvo,J.M. Lrp, a leucine-responsive protein, regulates branched-chainamino acid transport genes in Escherichia coli J. Bacteriol. 174 (1), 108-115 (1992) PubMed: 1729203 D'Ari,R., Lin,R.T. and Newman,E.B. The leucine-responsive regulatory protein: more than aregulator? Trends Biochem. Sci. 18 (7), 260-263 (1993) PubMed: 8212136 ","","Tue Dec 10 08:13:21 2002","1","","","" "AA00379","256548","255022","1527","ATGGAAGCGTCTACTCAAAAAAAGACCTTTAATTTCCCATCGGCATTTACGATTTTATTCTTTATTCTCATCCTTGCTGTGGGACTCACCTGGGTTATTCCGTCAGGTTCATATTCTAAATTGACTTATAGTATGACTGACAAAATGTTTGTAGTGAAGACCTATGGCGAACAAGATAAAACCTATCCTGCCACCGAAGAAACATTAAATAACCTCAATATCAAAATTAAACTTTCCAATTTCACCGAAGGCATCATTAAGAAACCTATCGCCATTCCCGGCACTTATCAACGAATTGAACAGCACTACAAAGGCATCAAAGATATTCCGATCAGCATGGTGGAAGGAACCATTGAAGCGGTGGATGTGATGGTCTTTATTTTCGTGCTGGGCGGTATGATAGGGGTTATTAACAAAACGGGTTCATTTAATGCCGGCTTAATGGCATTGGCGCGGCGCACCAAGGGTAACGAATTCATGATTGTGTTCAGCGTTTCCGTGCTTATGGTGTTAGGCGGTACCACTTGTGGTATCGAAGAAGAAGCTGTGGCGTTTTATCCTATTTTGGTACCGGTATTTTTAGCTTTGGGATACGATGCAATCGTTTGCGTCGGTGCGATTTTCTTAGCCGCCTCCATGGGGACGGCGTTCTCTACCATTAATCCATTCTCAGTAGTTATCGCCTCCAACGCCGCCGGGATTCAATTTACCGAGGGTATCGGATTCCGCACCATTGGCTTAATCTTAGGTTCGGCGTGTGTGATTGCTTATCTTTATTGGTACTGTAAAAAAGTGAAAGCCGATCCGAGTTTTTCATATACTTATGAGGATAGAGAAGAGTTTCGTCATCGTTATATGAAGAATTTTGATCCGAATGTGGTGGTGGAATTTACCCTCAGAAGAAAATTTATCCTGATTTTATTCTGTATCGCGTTCCCAATGATGATCTGGGGCGTGATGGCGGGCGGTTGGTGGTTCCCGCAAATGGCGGCATCTTTCTTATCCATCACCATTATCATCATGTTTATCAGTGGGTTGAAAGAAAAAGACATTGTGGAATCCTTTACCGAAGGGGCATCGGAATTGGTCGGCGTGTCGCTCATTATCGGCTTGGCGCGCGGAGTAAACCTTGTCTTAGAGCAAGGCATGATTTCCGACACGATTTTAGATTATATGTCTAACTTGGTGAGTGGAATGCCGGGCAGTATCTTTATCCTGGGTCAGTTGATCGTTTTCGTCTTCCTCGGACTGATTGTGCCGTCTTCCTCCGGTTTAGCGGTGCTTTCCATGCCGATTATGGCGCCGCTTGCCGACGCCGTTGGTATTCCACGCGACATCGTGGTTTCCGCCTACAACTGGGGGCAATATGCCATGTTGTTCCTGGCGCCGACCGGCTTGGTGTTGGTGACTTTGCAAATGTTGCATATTCCGTTCAATAAGTGGGTGAAGTTTGTTTTACCGATGATCGGTTGTTTGTTGGTTATCGGCGCGACATTGTTGGTCATCCAGGTTTCTTTATATAGTGTT","","","55820","MEASTQKKTFNFPSAFTILFFILILAVGLTWVIPSGSYSKLTYSMTDKMFVVKTYGEQDKTYPATEETLNNLNIKIKLSNFTEGIIKKPIAIPGTYQRIEQHYKGIKDIPISMVEGTIEAVDVMVFIFVLGGMIGVINKTGSFNAGLMALARRTKGNEFMIVFSVSVLMVLGGTTCGIEEEAVAFYPILVPVFLALGYDAIVCVGAIFLAASMGTAFSTINPFSVVIASNAAGIQFTEGIGFRTIGLILGSACVIAYLYWYCKKVKADPSFSYTYEDREEFRHRYMKNFDPNVVVEFTLRRKFILILFCIAFPMMIWGVMAGGWWFPQMAASFLSITIIIMFISGLKEKDIVESFTEGASELVGVSLIIGLARGVNLVLEQGMISDTILDYMSNLVSGMPGSIFILGQLIVFVFLGLIVPSSSGLAVLSMPIMAPLADAVGIPRDIVVSAYNWGQYAMLFLAPTGLVLVTLQMLHIPFNKWVKFVLPMIGCLLVIGATLLVIQVSLYSV","255022","","possible membrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR004669
Family
C4-dicarboxylate anaerobic carrier
PF03606\"[12-505]TDcuC
noIPR
unintegrated
unintegrated
PTHR10283\"[66-509]TCATION TRANSPORTER RELATED
PTHR10283:SF43\"[66-509]Tgb def: Arginine/ornithine antiporter
signalp\"[1-30]?signal-peptide
tmhmm\"[15-35]?\"[118-138]?\"[159-178]?\"[182-202]?\"[207-227]?\"[241-261]?\"[303-323]?\"[329-347]?\"[359-379]?\"[398-418]?\"[423-443]?\"[449-469]?\"[484-504]?transmembrane_regions


","BeTs to 4 clades of COG1288COG name: Uncharacterized membrane proteinFunctional Class: SThe phylogenetic pattern of COG1288 is -----------lb-e--h---j--t-Number of proteins in this genome belonging to this COG is","","Residues 256 to 319 match (9e-13) PD:PD543284 which is described as PROTEOME COMPLETE SAV1171 ","","","","","","","","","","","","Tue Jan 21 12:46:52 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00379 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 12 to 505 (E-value = 5.9e-242) place AA00379 in the DcuC family which is described as C4-dicarboxylate anaerobic carrier (PF03606)","","","","","","","","1","","","" "AA00380","257597","256668","930","ATGAGAATCGTCATTGCATTGGGCGGTAATGCGCTGTTACGGCGCGGCGAACCGCTGACGGCGGAAAATCAACGCTTAAACGTGCGTATCGCTTGTGAGCAAATCGCCAAAATTTATCCGAATAATGAATTGGTGATTGCCCATGGGAATGGGCCACAAGTGGGTTTGCTGGCGCTGCAAGGGGCAGCTTATAAAGATGTTCCGACCTATCCGTTGGATGTGTTGGGCGCGGAATCCGTGGGCATGATCGGTTACATGATTCAACAGGAATTGGGTAACTTAGTGCCGTTTGAAGTGCCGTTTGCTACATTGCTTTCCCAAGTGGAAGTGGACATTAACGACCCGGCATTTAAGAACCCGACCAAACCGATTGGTCCGGTGTATTCCAAAGAAGAAGCGGAACGTCTGGCGAAAGAAAAAAATTGGTCTATCGCACAAGATGGCGATAAATATCGTCGCGTTGTGCCAAGCCCGTTACCAAAACGAATTTTTGAAATTCGTCCGGTGAAATGGTTGCTGGAAAAGGGCAGTATTGTCATTTGCGCCGGTGGTGGCGGTATTCCGACTTATTATGATGAACAACACAATCTGCAAGGGGTTGAAGCGGTTATCGACAAAGATTTATGCTCCGCATTGTTGGCGGAAAATCTGGACGCGGATTTGTTCATTATTGCCACCGATGTATCTGCTGTGTTTGTAGATTGGGGCAAACCGACACAAAAAGCGATTGCTTTGGCTCCGCCTGATGAAATTGAAAAATTAGCTTTTGCTGCCGGTTCCATGGGACCGAAGGTGCAAGCGGCGGTAAATTTTGCACGTCATACGGGAAAAGATGCAGTCATCGGATCACTTTCTGACATTGTTGATATTGTGAAAGGCAAGGCCGGTACACGCATTACCAATAAGGCGAAAGAGATCTCTTATTATTCA","","","33786","MRIVIALGGNALLRRGEPLTAENQRLNVRIACEQIAKIYPNNELVIAHGNGPQVGLLALQGAAYKDVPTYPLDVLGAESVGMIGYMIQQELGNLVPFEVPFATLLSQVEVDINDPAFKNPTKPIGPVYSKEEAERLAKEKNWSIAQDGDKYRRVVPSPLPKRIFEIRPVKWLLEKGSIVICAGGGGIPTYYDEQHNLQGVEAVIDKDLCSALLAENLDADLFIIATDVSAVFVDWGKPTQKAIALAPPDEIEKLAFAAGSMGPKVQAAVNFARHTGKDAVIGSLSDIVDIVKGKAGTRITNKAKEISYYS","256668","","carbamate kinase","Cytoplasm","","
InterPro
IPR001048
Domain
Aspartate/glutamate/uridylate kinase
G3DSA:3.40.1160.10\"[2-301]Tno description
PF00696\"[1-283]TAA_kinase
InterPro
IPR003964
Family
Bacterial carbamate kinase
PR01469\"[41-60]T\"[71-89]T\"[103-122]T\"[151-170]T\"[174-192]T\"[205-220]T\"[256-271]TCARBMTKINASE
PIRSF000723\"[1-301]TCarbamate kinase
TIGR00746\"[1-301]TarcC: carbamate kinase


","BeTs to 9 clades of COG0549COG name: Carbamate kinaseFunctional Class: EThe phylogenetic pattern of COG0549 is -o-pkz-----l-cef-h-------wNumber of proteins in this genome belonging to this COG is","Significant hit ( 3.3e-14) to 2/4 blocks of the IPB001057 family, which is described as \"Glutamate 5-kinase\". Interpro entry for IP:IPR001057. IPB001057C 203-236 1.4e-07 IPB001057D 251-283 5.9e-05","Residues 2 to 299 match (1e-157) PD:PD004953 which is described as KINASE CARBAMATE COMPLETE PROTEOME TRANSFERASE ARGININE METABOLISM KINASE-LIKE PLASMID SYNTHETASE ","","","","","Sun Feb 16 16:06:08 2003","","","","","","","Tue Dec 10 08:42:01 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00380 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 283 (E-value = 6.8e-99) place AA00380 in the AA_kinase family which is described as Amino acid kinase family (PF00696)","","","","","Baur,H., Luethi,E., Stalon,V., Mercenier,A. and Haas,D.Sequence analysis and expression of the arginine-deiminase andcarbamate-kinase genes of Pseudomonas aeruginosaEur. J. Biochem. 179 (1), 53-60 (1989)PubMed: 2537202D'Hooghe,I., Vander Wauven,C., Michiels,J., Tricot,C., de Wilde,P., Vanderleyden,J. and Stalon,V.The arginine deiminase pathway in Rhizobium etli: DNA sequenceanalysis and functional study of the arcABC genesJ. Bacteriol. 179 (23), 7403-7409 (1997)PubMed: Alcantara C, Cervera J, Rubio V.Carbamate kinase can replace in vivo carbamoyl phosphate synthetase. Implications for the evolution of carbamoyl phosphate biosynthesis.FEBS Lett. 2000 Nov 10;484(3):261-4.PMID: 11078889 ","","Thu Feb 20 09:18:14 2003","1","","","" "AA00381","258611","257610","1002","ATGGCTTTCAATCTTAAAAACAGACATTTATTAAGTTTGGTAAATCATTCAGAACGTGAAATTAACTATTTGTTGGATTTATCCCGAGACTTAAAAAGAGCGAAATATGCCGGAACCGAACAACAAAAATTGAAAGGGAAAAATATTGCGTTAATTTTTGAAAAAACCTCCACCCGCACCCGTTGCGCCTTTGAAGTCGCTGCCTATGACCAAGGCGCTCAAGTCACTTACATCGATCCGAATTCCTCCCAAATCGGTCACAAAGAAAGCATGAAAGACACCGCCCGTGTGTTGGGCAGAATGTATGACGCCATTGAATATCGCGGCTTCAAACAAGAAATCGTCGATGAATTGGCGGCGTATGCCGGCGTGCCGGTGTTTAACGGGTTAACCGATGAATTCCATCCGACCCAAATGCTGGCGGACGTGTTAACCATGATTGAAAACTGCGATAAACCGTTGAGCGAAATCAGCTATGTGTATATCGGCGATGCGCGCAACAACATGGGGAATTCCTTATTATTAATCGGTGCCAAACTGGGCATGGACGTACGCATTTGCGGGCCGAAAGCCTTATTGCCGGATGCGGAATTGGTAGAAATGTGCGAAGGCTTTGCAAAACAAAGCGGTGCTCGTATTACCGTCACCGACGACATTGATAAAGCGGTGAAAGGTGTGGATTTCGTGCATACCGACGTGTGGGTTTCCATGGGTGAACCGTTAGAAACCTGGGGCGAACGGATTAAATTATTGTTGCCGTATCAAGTGACCCCTGAATTAATGAAACGCACTGGCGATCCGCGGGTGAAATTCATGCACTGCTTGCCGGCGTTTCACAACAGCGAAACCAAAGCAGGTCGTCAAATCGCGGAAAAATACCCGGAACTGGCAAACGGTATTGAAGTCACCGAAGATGTGTTCGAATCCCCGATGAACGTGGCGTTTGAGCAAGCGGAAAACCGTATGCACACCATTAAAGCCGTACTTTACTCCAGCTTAATC","","","38249","MAFNLKNRHLLSLVNHSEREINYLLDLSRDLKRAKYAGTEQQKLKGKNIALIFEKTSTRTRCAFEVAAYDQGAQVTYIDPNSSQIGHKESMKDTARVLGRMYDAIEYRGFKQEIVDELAAYAGVPVFNGLTDEFHPTQMLADVLTMIENCDKPLSEISYVYIGDARNNMGNSLLLIGAKLGMDVRICGPKALLPDAELVEMCEGFAKQSGARITVTDDIDKAVKGVDFVHTDVWVSMGEPLETWGERIKLLLPYQVTPELMKRTGDPRVKFMHCLPAFHNSETKAGRQIAEKYPELANGIEVTEDVFESPMNVAFEQAENRMHTIKAVLYSSLI","257610","","ornithine carbamoyltransferase","Cytoplasm","","
InterPro
IPR002292
Family
Ornithine carbamoyltransferase
PR00102\"[51-65]T\"[84-97]T\"[124-138]T\"[229-239]T\"[312-323]TOTCASE
TIGR00658\"[8-334]Torni_carb_tr: ornithine carbamoyltransferas
InterPro
IPR006130
Family
Aspartate/ornithine carbamoyltransferase
PR00100\"[53-72]T\"[135-146]T\"[267-276]T\"[298-321]TAOTCASE
PIRSF000416\"[8-333]TOrnithine/aspartate carbamoyltransferase
PS00097\"[53-60]TCARBAMOYLTRANSFERASE
InterPro
IPR006131
Domain
Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding region
PF00185\"[154-332]TOTCace
InterPro
IPR006132
Domain
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding
PF02729\"[8-149]TOTCace_N
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1370\"[138-333]Tno description
PIRSF500170\"[8-330]TOrnithine carbamoyltransferase
PTHR11405\"[136-280]T\"[300-334]TCARBAMOYLTRANSFERASE RELATED
PTHR11405:SF1\"[136-280]T\"[300-334]TORNITHINE CARBAMOYLTRANSFERASE


","BeTs to 23 clades of COG0078COG name: Ornithine carbamoyltransferaseFunctional Class: EThe phylogenetic pattern of COG0078 is aompkzyqvdrlbcefghsnuj--twNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.6e-57) to 4/4 blocks of the IPB002029 family, which is described as \"Aspartate and ornithine carbamoyltransferase family\". Interpro entry for IP:IPR002029. IPB002029A 46-73 2.8e-16 IPB002029B 83-108 4.9e-15 IPB002029C 125-163 4.5e-14 IPB002029D 265-286 6.8e-08","Residues 109 to 329 match (2e-07) PD:PD124910 which is described as PROTEOME COMPLETE TRANSFERASE CARBAMOYL YGEW ","","","","","","","","","","","","Mon May 23 14:17:21 2005","","Mon May 23 14:17:21 2005","Mon May 23 14:17:21 2005","Mon May 23 14:17:21 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA00381 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon May 23 14:17:21 2005","","","","","Residues 154 to 333 (E-value = 1.3e-86) place AA00381 in the OTCace family which is described as Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain (PF00185)","Mon May 23 14:17:21 2005","","","","Tonon T, Bourdineaud JP, Lonvaud-Funel A. The arcABC gene cluster encoding the arginine deiminase pathwayof Oenococcus oeni, and arginine induction of a CRP-like gene. Res Microbiol. 2001 Sep;152(7):653-61. PMID: 11605985 Shi D, Gallegos R, DePonte J 3rd, Morizono H, Yu X, Allewell NM,Malamy M, Tuchman M. Crystal structure of a transcarbamylase-like protein from theanaerobic bacterium Bacteroides fragilis at 2.0 A resolution. J Mol Biol. 2002 Jul 19;320(4):899-908. PMID: 12095263","","Tue Dec 10 08:44:39 2002","1","","","" "AA00382","258733","258945","213","TTGCGTCAGTGTAAAGATTTTGAACTTATGTCTAACAAAGGGGAATTTATTGGTATAAAATTCGGTTTTACGCAGAAATTAATCATAAAACACCACAACAGCCTAACATTTCACGATAAAAATGAACGCTTTCATCACCTCATTCCGCCACTTCGTGCTAAAAGTGCGGTATGTTTTACACAAGAAATTACGCCAAAGCCACCGCCTGTCGCA","","","8210","LRQCKDFELMSNKGEFIGIKFGFTQKLIIKHHNSLTFHDKNERFHHLIPPLRAKSAVCFTQEITPKPPPVA","258945","","hypothetical protein","Cytoplasm","No significant similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 14:10:24 2004","Sun Feb 22 14:10:24 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00382 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 14:10:24 2004","","","","","","","","","","","","","1","","","" "AA00383","259034","260242","1209","TTGGAGTGGAACGCCCAATGGACACAACAACATCCCTTCGCCGCTTGGGTTGTGATGCCCTGCGGGTTAGCCGCATTGGCGTGGTTCGTGCTGAAATACACGCCCTATGTGGGCGGCAGTGGCATTCCGCAGGTCATCGCCTCTCTCAGTTTGCCCCATAACAGTGACAAAACCCGTTTAGTCGCATTTGCACAAACCTTATGGAAAATTCCCCTCACCTTTTTAGCTATGCTGTTCGGCGCTTCCGTAGGGAGGGAAGGCCCGTCTGTGCAAGTGGGCGCGGCGGTGATGTTATGGTGGGGCAATCTTTGTCGTCAATACGGCGTGGCATTCAAAGGACTTAGTGCCAATGAACTGATGGCAACGGGCGCGGCGGGCGGGTTGGCGGCAGCATTTAACGCGCCGTTAGCCGGAGTGATTTTCGCCATTGAAGAACTTGGACGCGGCGTATTATTACGTTGGGAGCGGCGGGTGCTGCTGGGTGTATTGGCGGCGGGTTTCATTTTGGTTGCGATCGACGGCAACAACCCGTATTTTCCTAAATACCACGGCGTCACCGACATTCCTTATTTGTATTTATGGGTTTTGTTGTGTGGCGTGGTTTGCGGGGTGTTCGGCGGCATTTTCGCCCGCCTGCTGGCAAAAGGCGTTGGCGGCGTCTTGCCGAATTTATGCCGTGGCTGGGTGCGCAATCATCCCATTTATACCGCCTTCATTTTGGGCTTAATTCTGACCGCACTTGGGCTGTACACCAACGGGCAAACCTACGGCACAGGCTATCATGTGGTGACCCAAGCCCTCGACGGACAAGCCATGCAAACCGACATCGGCATCATGAAATTATTCGCCACAGTGGGTACTTACTGGACGGGCATCGCGGGCGGCATCTTCACGCCGTCTCTGACCATCGGCGCGGGGCTTGGCGTGCAAGTGGCAACCCTCACCGACGGCTTAATTGACCAACGTCTGCTGGTGCTGCTGTGTATGGCGGCATTTCTGGCGGGCGCCACCCAATCGCCGGTCACCGCCAGCGTCATCGTAATGGAAATGACCGGCTGCCAGCCCGTGCTGATTTGGCTATTGATTTGCTGCCTGATTTCCTCCATTATTTCACGCCAATTTAATCCGAAGCCGTTCTATCATTTTGCGGCGGGGCGCTTCCGCCATCGGATTCAAGAAGAAATGCAACAAGACATGAAGGACAACTCG","","","50236","LEWNAQWTQQHPFAAWVVMPCGLAALAWFVLKYTPYVGGSGIPQVIASLSLPHNSDKTRLVAFAQTLWKIPLTFLAMLFGASVGREGPSVQVGAAVMLWWGNLCRQYGVAFKGLSANELMATGAAGGLAAAFNAPLAGVIFAIEELGRGVLLRWERRVLLGVLAAGFILVAIDGNNPYFPKYHGVTDIPYLYLWVLLCGVVCGVFGGIFARLLAKGVGGVLPNLCRGWVRNHPIYTAFILGLILTALGLYTNGQTYGTGYHVVTQALDGQAMQTDIGIMKLFATVGTYWTGIAGGIFTPSLTIGAGLGVQVATLTDGLIDQRLLVLLCMAAFLAGATQSPVTASVIVMEMTGCQPVLIWLLICCLISSIISRQFNPKPFYHFAAGRFRHRIQEEMQQDMKDNS","260242","","chloride channel protein","Inner membrane, Cytoplasm","","
InterPro
IPR001807
Family
Chloride channel, voltage gated
PR00762\"[35-52]T\"[69-88]T\"[125-144]T\"[292-312]T\"[322-338]T\"[340-359]TCLCHANNEL
PTHR11689\"[4-401]TCHLORIDE CHANNEL
InterPro
IPR014743
Domain
Chloride channel, core
PF00654\"[19-375]TVoltage_CLC
noIPR
unintegrated
unintegrated
G3DSA:1.10.3080.10\"[11-400]Tno description
PTHR11689:SF14\"[4-401]TVOLTAGE-GATED CLC-TYPE CHLORIDE CHANNEL ERIC
signalp\"[1-39]?signal-peptide
tmhmm\"[12-30]?\"[123-143]?\"[158-176]?\"[190-210]?\"[231-251]?\"[288-308]?\"[323-341]?\"[351-371]?transmembrane_regions


","BeTs to 15 clades of COG0038COG name: Chloride channel protein EriCFunctional Class: PThe phylogenetic pattern of COG0038 is aompkzyq-drlbce-gh-n-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.3e-18) to 5/7 blocks of the PR00762 family, which is described as \"Chloride channel signature\". Prints database entry for PR:PR00762. PR00762A 35-52 0.18 PR00762B 69-88 3 PR00762C 125-144 3.1e-08 PR00762D 292-312 0.032 PR00762F 340-359 71","Residues 255 to 316 match (7e-08) PD:PD438031 which is described as INNER CHLORIDE PROTEOME PLASMID CHLORIDE-CHANNEL COMPLETE PROTEIN-RELATED MEMBRANE CHANNEL ","","","","","Mon Feb 17 11:24:08 2003","","","","","","","Sun Feb 16 16:42:04 2003","","Thu Mar 18 10:00:25 2004","Thu Mar 18 10:00:25 2004","Thu Mar 18 10:00:25 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00383 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Mar 18 10:00:25 2004","","","","","Residues 19 to 375 (E-value = 4.6e-22) place AA00383 in the Voltage_CLC family which is described as Voltage gated chloride channel (PF00654)","Thu Mar 18 10:00:25 2004","","","","","","","1","","","" "AA00384","260248","261228","981","ATGCCTCAAAACCCACCGCACTTTTATCGCGGACGCTTCGCCGTGGCACCCATGTTGGACTGGACGACGCGCCATTGCCGTTATTTCCACCGCCAATTTTCCCGCCATGCCTTGCTTTACACGGAAATGGTGACGACACAAGCCATCATCCACGCCAAATATGATCATCTCGATTTTGACCCGGCGGAACAGCCTGTGGCGTTACAACTGGGCGGCAGCGACCCTGCCCAACTCAAACATTGCGCCCAATTGGCGGAACAACGGGGCTATCAGGAAATTAACCTGAACGTGGGCTGCCCGTCCGATCGCGTGCAAAACGGCATGTTCGGCGCCTGTTTAATGGCAAAGGCGGAGCTGGTCGCCGAGTGCGTACAACAAATGCAAGAAGCGGTGCGCATTCCGGTGACGGTGAAAACCCGTATCGGCATCGACGATTTCGACAGCTACGACTTTCTTTGCGATTTCATTGAAAAAGTGCAACAAGCAGGCTGCCGAGAATTTATCGTACACGCGCGCAAAGCCTGGCTTTCCGGCTTAAGCCCGAAACAAAACCGCGAAATTCCGCCGCTGGATTACGAACGGGTGTATCAACTGAAACGGGATTTTCCCCACTTGCTCATCAGCATTAACGGCGGCATTAAAACCATTGACGAAATGCAACAGCATTTGCAGCGGGTGGACGGCGTGATGGTGGGGCGCGAAGCCTATCAAAATCCGTCGTTGCTTGGCTACATCGATCAGGCATTGTTCAATGCCAACGCCCCAATTGTCACCCCACGCGAAGCCGTGGAAAAAATGCTCCCTTACATTGAACAACAACTCAGCCGGGGCGTGTATCTCAACCACATCGTGCGCCATATACTCAGCGCTTTCCAACACTGTAAAGGCGCCCGCCAATGGCGCCGCTATTTAAGCGAAAACGCCTATAAAGAAGGCGCCGGTATTGAGGTAGTAGAAACCGCTTTGGGGTTTGTGGAAGCA","","","37388","MPQNPPHFYRGRFAVAPMLDWTTRHCRYFHRQFSRHALLYTEMVTTQAIIHAKYDHLDFDPAEQPVALQLGGSDPAQLKHCAQLAEQRGYQEINLNVGCPSDRVQNGMFGACLMAKAELVAECVQQMQEAVRIPVTVKTRIGIDDFDSYDFLCDFIEKVQQAGCREFIVHARKAWLSGLSPKQNREIPPLDYERVYQLKRDFPHLLISINGGIKTIDEMQQHLQRVDGVMVGREAYQNPSLLGYIDQALFNANAPIVTPREAVEKMLPYIEQQLSRGVYLNHIVRHILSAFQHCKGARQWRRYLSENAYKEGAGIEVVETALGFVEA","261228","","conserved hypothetical protein (possible nitrogen fixation protein)","Cytoplasm","","
InterPro
IPR001269
Family
Dihydrouridine synthase, DuS
PIRSF006621\"[1-326]TtRNA-dihydrouridine synthase
PF01207\"[14-326]TDus
PS01136\"[93-111]TUPF0034
InterPro
IPR004653
Family
Dihydrouridine synthase TIM-barrel protein yjbN
TIGR00742\"[11-327]TyjbN: TIM-barrel protein, yjbN family
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[7-257]Tno description
noIPR
unintegrated
unintegrated
PTHR11082\"[41-322]TTRNA-DIHYDROURIDINE SYNTHASE
PTHR11082:SF9\"[41-322]TTRNA-DIHYDROURIDINE SYNTHASE-RELATED


","No hits to the COGs database.","Significant hit ( 6.4e-51) to 6/6 blocks of the IPB001269 family, which is described as \"Uncharacterized protein family UPF0034\". Interpro entry for IP:IPR001269. IPB001269A 14-34 3.8e-07 IPB001269B 82-114 1.3e-15 IPB001269C 133-144 9.2e-06 IPB001269D 163-186 5.7e-07 IPB001269E 204-213 1.6 IPB001269F 224-241 7.3e-07","Residues 84 to 172 match (5e-13) PD:PD335770 which is described as PROTEOME BB0225 COMPLETE CAB87804.1 ","","","","","","","","","","","","Thu Feb 20 07:53:11 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00384 is paralogously related to AA00172 (9e-16) and AA01054 (4e-04).","","","","","","Residues 14 to 326 (E-value = 6.2e-140) place AA00384 in the Dus family which is described as Dihydrouridine synthase (Dus) (PF01207)","","","","","","","","1","","","" "AA00386","262279","261290","990","ATGAAAAAGACATTTATTTTACAGCAACAAGAAATCAGCTTTGTGAAAAACACATTCACACAAAATCTTATTGAACAACTTGGCATTATTGAAGTTCAGGGACCTATCTTAAGCCAAGTGGGTAATGGTATGCAAGATAACTTATCCGGTATTGAAAAAGCGGTACAGGTTCACGTCAAACAAATTCCGGGCGTGGTTTTTGAAGTTGTGCATTCCTTGGCAAAATGGAAACGTCACACCCTTGCCCGCTTCCATTTTAAAGAAAACGAAGGCTTATTCGTGCACATGAAAGCTTTGCGCCCTGATGAAGATTCTCTCGACCCGACGCACTCGATTTATGTGGATCAATGGGACTGGGAAAAAGTGATTCCGGAAGGTCGTCGCAATTTTGCCTATTTGAAAGAAACCGTGAATGCCATTTATCGCGCCATTCGTTTAACCGAATTGGCGGTGGAAGCCCGCTTTGACATCCCGTCAATTTTGCCGAAACACATCACTTTTGTGCATACCGAAGATTTGGTGCAACGCTATCCAAACCTCAGCGGCAAAGAGCGTGAAAACGCCATCTGTAAGGAATACGGCGCGGTCTTTTTAATCGGTATCGGCGGCAACTTATCCGACGGCAAACCGCACGACGGTCGTGCACCGGATTACGACGACTGGACCACCGAGTCGGAAAACGGCTACAAAGGGTTAAACGGTGACATTTTGGTGTGGAACGAACAACTCGGCACCGCCTTTGAGCTTTCTTCCATGGGAATTCGCGTAGATGAAGCGGCATTACGTTTGCAAGTGGGCTTAACCGGCGACGAAGACCGTTTAACCATGGATTGGCACCAAGAGTTGCTGCAAGGTAAATTGCCATTGACCATCGGTGGCGGTATCGGTCAATCCCGCATGGCAATGTTCCTGCTGCGCAAAAAACACATCGGCGAAGTGCAATCCAGCGTCTGGCCGGAAGAAATGCTGGAACAATATCAGCATATCCTC","","","37559","MKKTFILQQQEISFVKNTFTQNLIEQLGIIEVQGPILSQVGNGMQDNLSGIEKAVQVHVKQIPGVVFEVVHSLAKWKRHTLARFHFKENEGLFVHMKALRPDEDSLDPTHSIYVDQWDWEKVIPEGRRNFAYLKETVNAIYRAIRLTELAVEARFDIPSILPKHITFVHTEDLVQRYPNLSGKERENAICKEYGAVFLIGIGGNLSDGKPHDGRAPDYDDWTTESENGYKGLNGDILVWNEQLGTAFELSSMGIRVDEAALRLQVGLTGDEDRLTMDWHQELLQGKLPLTIGGGIGQSRMAMFLLRKKHIGEVQSSVWPEEMLEQYQHIL","261290","","aspartate--ammonia ligase (asparagine synthetase A)","Cytoplasm","","
InterPro
IPR004618
Family
Aspartate--ammonia ligase
PD024629\"[9-320]TASNA_HAEIN_P44338;
PIRSF001555\"[1-330]TAspartate-ammonia ligase
PF03590\"[3-246]TAsnA
TIGR00669\"[1-330]TasnA: aspartate--ammonia ligase
InterPro
IPR006195
Domain
Aminoacyl-transfer RNA synthetase, class II
PS50862\"[13-319]TAA_TRNA_LIGASE_II
noIPR
unintegrated
unintegrated
G3DSA:3.30.930.10\"[1-330]Tno description


","BeTs to 4 clades of COG2502COG name: Asparagine synthetase AFunctional Class: EThe phylogenetic pattern of COG2502 is -----------l--e--h------twNumber of proteins in this genome belonging to this COG is","","Residues 9 to 325 match (4e-172) PD:PD024629 which is described as LIGASE COMPLETE PROTEOME SYNTHETASE ASPARAGINE A ASPARTATE--AMMONIA ASPARTATE-AMMONIA ASNA 3D-STRUCTURE ","","","","","","","","","","","","Tue Dec 10 09:04:47 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00386 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 246 (E-value = 5e-188) place AA00386 in the AsnA family which is described as Aspartate-ammonia ligase (PF03590)","","","","","Nakamura,M., Yamada,M., Hirota,Y., Sugimoto,K., Oka,A. andTakanami,M. 1981. Nucleotide sequence of the asnA gene codingfor asparagine synthetase of E. coli K-12. Nucleic Acids Res.9(18): 4669-4676. PubMed: 6117826Sugiyama,A., Kato,H., Nishioka,T. and Oda,J.Overexpression and purification of asparagine synthetase fromEscherichia coliBiosci. Biotechnol. Biochem. 56 (3), 376-379 (1992)PubMed: 1369484","","Tue Dec 10 09:08:54 2002","1","","","" "AA00387","262445","262894","450","ATGCACAATATTGATAATTTAGATCAGCAAATATTGCGCGTGTTAACGCGGGATGCCCGCACGCCTTATGCGGAAATGGCGAAAAACTTCGGCGTGAGTCCCGGCACGATTCATGTGCGGGTGGAAAAAATGCGTCAATCCGGTGTAATTGAAGGCACCAAAGTGCGCATTAACGAACGCAAGCTGGGTTATGATGTGTGTGGTTTTATCGGCATTATTCTGAAATCCGCCAAAGATTATGACAAAGTGATCAAAAAGCTGGAAACCATCGATGAAGTGGTGGAAGCGTATTACACCACCGGCAACTACTCCATTTTTATTAAAGTTATGACGCACACCATCGCCGAATTACATTTTGTGTTATCGGCAAAAATTCAGTTAATTGATGAAATTCAATCCACAGAAACCTTAATTTCCATGCAAAATCCGATTTTGCGTGACATTAAACCT","","","17094","MHNIDNLDQQILRVLTRDARTPYAEMAKNFGVSPGTIHVRVEKMRQSGVIEGTKVRINERKLGYDVCGFIGIILKSAKDYDKVIKKLETIDEVVEAYYTTGNYSIFIKVMTHTIAELHFVLSAKIQLIDEIQSTETLISMQNPILRDIKP","262894","","transcription regulatory protein","Cytoplasm","","
InterPro
IPR000485
Family
Bacterial regulatory proteins, AsnC/Lrp
PR00033\"[4-20]T\"[20-31]T\"[31-50]THTHASNC
PF01037\"[68-142]TAsnC_trans_reg
SM00344\"[4-111]THTH_ASNC
PS50956\"[4-65]THTH_ASNC_2
PS00519\"[22-48]THTH_ASNC_1
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[4-55]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.920\"[56-150]Tno description


","No hits to the COGs database.","Significant hit ( 7.4e-39) to 3/3 blocks of the IPB000485 family, which is described as \"Bacterial regulatory proteins, AsnC family\". Interpro entry for IP:IPR000485. IPB000485A 4-25 6.4e-09 IPB000485B 32-72 1.3e-15 IPB000485C 80-121 2e-11","Residues 82 to 146 match (7e-08) PD:PD276850 which is described as PROTEOME COMPLETE TRANSCRIPTIONAL REGULATOR FAMILY TRANSCRIPTION REGULATOR ASNC REGULATORY PLASMID ","","","","","","","","","","","","Tue Dec 10 09:10:44 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00387 is paralogously related to AA00378 (9e-11) and AA02734 (4e-09).","","","","","","Residues 28 to 129 (E-value = 5.5e-16) place AA00387 in the AsnC_trans_reg family which is described as AsnC family (PF01037)","","","","","Poggio S, Domeinzain C, Osorio A, Camarena L. The nitrogen assimilation control (Nac) protein represses asnCand asnA transcription in Escherichia coli. FEMS Microbiol Lett. 2002 Jan 10;206(2):151-6. PMID: 11814655 de Wind,N., de Jong,M., Meijer,M. and Stuitje,A.R.. Site-directed mutagenesis of the Escherichia coli chromosomenear oriC: identification and characterization of asnC, aregulatory element in E. coli asparagine metabolism. Nucleic Acids Res. 13(24): 8797-8811, 1985 PubMed: 3909107. Kolling,R. and Lother,H. AsnC: an autogenously regulated activator of asparaginesynthetase A transcription in Escherichia coli. J. Bacteriol. 164(1): 310-315, 1985. PubMed: 2864330. Kolling,R., Gielow,A., Seufert,W., Kucherer,C. and Messer,W. AsnC, a multifunctional regulator of genes located around thereplication origin of Escherichia coli, oriC. Mol. Gen. Genet. 212(1): 99-104, 1988. PubMed: 2836709.","","Tue Dec 10 09:10:44 2002","1","","","" "AA00388","262931","263686","756","ATGTCAGACGTATTTCACCTCGGCTTAACCAAAGCCATGTTAGACGGCGCCAAATTAGCCATTGTGCCCGGTGCACCGGAACGGGTTGAACGTATCGCCCGCTTATTAAATCGCCCGAAATTCCTTGCCGCCACCCGCGAATTCACTTCTTGGCTCGGTTATATTGACGAACACGCCGTGGTGGTTTGCTCCACCGGTATCGGCGGACCTTCCGTTTCTATTGCCGTGGAAGAATTGGCACAACTGGGCGTACGTACTTTCTTGCGTATCGGTACCACCGGTGCCATTCAACCGCACATTAATGTCGGCGATTTATTAATCACCACCGGCGCGGTACGTTTAGATGGCGCCAGCCGTCACTTTGCGCCGTTGGAATATCCGGCAGTCGCCGACTTTGCATGCACCAATGCGTTGTATAACGTAGCGACAGAAGACGCGGGCAACCACGTCCATGTGGGCATCACCGCCTCGTCAGACACCTTCTATCCGGGGCAAGAACGTTACGACACCTTTACCGGCAAAATCTATCGCCACTTCCAAGGCTCACTCAAACAATGGCAGGAATTGCACGTGATGAATTATGAAATGGAATCCGCCACCTTGTTCACCATGTGTTCCGCCTTGGGTCTGCGGGCAGGCATGATAGCCGGTGCCATTGTTAATCGTACCCAACAGGAAATTCCGAACGAAGAAACCATTAAATCCACCGAAGAAAAAGCCATTCATGCAGTGGTGAAAGCAGCGGGATTATTGGTT","","","27270","MSDVFHLGLTKAMLDGAKLAIVPGAPERVERIARLLNRPKFLAATREFTSWLGYIDEHAVVVCSTGIGGPSVSIAVEELAQLGVRTFLRIGTTGAIQPHINVGDLLITTGAVRLDGASRHFAPLEYPAVADFACTNALYNVATEDAGNHVHVGITASSDTFYPGQERYDTFTGKIYRHFQGSLKQWQELHVMNYEMESATLFTMCSALGLRAGMIAGAIVNRTQQEIPNEETIKSTEEKAIHAVVKAAGLLV","263686","","uridine phosphorylase; possible 5'-methylthioadenosine phosphorylase; purine nucleoside phosphorylase","Cytoplasm","","
InterPro
IPR000845
Family
Nucleoside phosphorylase
PF01048\"[18-248]TPNP_UDP_1
PS01232\"[64-79]TPNP_UDP_1
InterPro
IPR010058
Family
Uridine phosphorylase
TIGR01718\"[4-252]TUridine-psphlse: uridine phosphorylase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1580\"[4-252]Tno description
PTHR21234\"[4-252]TPURINE NUCLEOSIDE PHOSPHORYLASE
PTHR21234:SF7\"[4-252]TPURINE NUCLEOSIDE PHOSPHORYLASE


","BeTs to 6 clades of COG2820COG name: Uridine phosphorylaseFunctional Class: FThe phylogenetic pattern of COG2820 is -o---z----rl--e-gh------t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-49) to 4/4 blocks of the IPB000845 family, which is described as \"Purine and other phosphorylases, family 1\". Interpro entry for IP:IPR000845. IPB000845A 23-34 0.0036 IPB000845B 46-80 3e-18 IPB000845C 152-162 0.00055 IPB000845D 190-226 1e-19","Residues 67 to 220 match (2e-08) PD:PD167674 which is described as COMPLETE PROTEOME AMP NUCLEOSIDASE HYDROLASE GLYCOSIDASE PROBABLE ALLOSTERIC PLASMID NUCLEOSIDASE-RELATED ","","","","","","","","","","","","Thu Jan 23 11:16:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00388 is paralogously related to AA00488 (6e-14).","","","","","","Residues 18 to 248 (E-value = 2.8e-94) place AA00388 in the PNP_UDP_1 family which is described as Phosphorylase family (PF01048)","","","","","Walton,L., Richards,C.A. and Elwell,L.P. Nucleotide sequence of the Escherichia coli uridinephosphorylase udp) gene Nucleic Acids Res. 17 (16), 6741 (1989) PubMed: 2674901 AUTHORS Cacciapuoti,G., Porcelli,M., Bertoldo,C., De Rosa,M. and Zappia,V.Purification and characterization of extremely thermophilic andthermostable 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. Purine nucleoside phosphorylase activity and evidence for intersubunit disulfide bondsJ. Biol. Chem. 269 (40), 24762-24769 (1994)PubMed: 7929153","","Thu Jan 23 11:16:14 2003","1","","","" "AA00390","264887","263829","1059","ATGATTGAAATGTTAAAAAATTGGTATCGGAGACGATTTAGCGACCCGCAAGCTATGGGGTTGTTCGCTATTTTATTCTTCGGTTTCGTCGCAATTTATTTTTTTAGTGATTTAATTGCGCCGCTGTTGGTAGCGATTGTGTTAGCGTACCTGTTGGAATGGCCTGTGCGCTTACTAAATGAAAAGTTGAAGTGCCCGCGTTTGCTTGCTACCGGCTTGGTTATTGGCAGCTTTACCGGCTTGGTGTTTTTGGTGGTTTTAGTGTTGATTCCGAATTTGTGGACACAAATGGTCAATTTATTAAGTGATTTGCCGCATATGTTTAATCGGTTTAATGAATGGCTGCTATCTTTGCCGGTACGCTATCCCGATATGATTGACGCACAAACCGTGGAATCTATTTTCGGCACGGTGAAAGAGAAAATTCTGGGCTTGGGCGAATCGGCGTTGAAACTGTCTTTGGCGTCAATTATGAACTTGGTGACGCTGGGGATTTATGCGTTTTTAGTGCCGTTAATGGTGTTTTTCCTGTTGAAAGATAAGCGTCAGTTAATGGACGGTGTGAGCCGTTTTTTACCGCGTAATCGCACTTTAGCGTCAAAAGTGTGGGTGGAAATGCAACAGCAAATTGCCAATTATATTCGCGGAAAATTGGTGGAAATTTTGGTCGTTACCATAGTGACTTATGCGATTTTCCTGATTTTCGGGTTGAATTACCCGTTATTGTTGGCGGTAGCGGTCGGGCTTTCTGTGTTGGTGCCTTACATCGGCGCTGTGTTGGTGGCGATTCCGGTGGTGTTGGTGGCAATTTTCCAATTCGGTGATACGCACACGTTTTGGTACATCGTCATCGCCTTTGTGGTGTCACAGTTATTGGACGGAAATCTGCTGGTGCCGTTTTTGTTCTCCGAAGCGGTCAATCTGCACCCGTTGGTGATCATCATTGCCGTTTTGATTTTCGGTGGCTTGTGGGGATTCTGGGGCGTATTTTTTGCCATTCCGCTGGCGACTTTGGTGAAAGCGGTGGTGAACGCTTGGCCTTCCAATGAAGCGGTGGAA","","","39657","MIEMLKNWYRRRFSDPQAMGLFAILFFGFVAIYFFSDLIAPLLVAIVLAYLLEWPVRLLNEKLKCPRLLATGLVIGSFTGLVFLVVLVLIPNLWTQMVNLLSDLPHMFNRFNEWLLSLPVRYPDMIDAQTVESIFGTVKEKILGLGESALKLSLASIMNLVTLGIYAFLVPLMVFFLLKDKRQLMDGVSRFLPRNRTLASKVWVEMQQQIANYIRGKLVEILVVTIVTYAIFLIFGLNYPLLLAVAVGLSVLVPYIGAVLVAIPVVLVAIFQFGDTHTFWYIVIAFVVSQLLDGNLLVPFLFSEAVNLHPLVIIIAVLIFGGLWGFWGVFFAIPLATLVKAVVNAWPSNEAVE","263829","","permease","Inner membrane, Cytoplasm","","
InterPro
IPR002549
Family
Protein of unknown function UPF0118
PTHR21716\"[94-346]TTRANSMEMBRANE PROTEIN
PF01594\"[18-347]TUPF0118
noIPR
unintegrated
unintegrated
signalp\"[1-95]?signal-peptide
tmhmm\"[15-33]?\"[39-59]?\"[68-90]?\"[155-177]?\"[221-241]?\"[251-271]?\"[280-302]?\"[308-330]?transmembrane_regions


","BeTs to 13 clades of COG0628COG name: Predicted permeaseFunctional Class: RThe phylogenetic pattern of COG0628 is aom-k--qvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 6.8e-20) to 1/2 blocks of the IPB002549 family, which is described as \"Domain of unknown function DUF20\". Interpro entry for IP:IPR002549. IPB002549B 299-336 6.6e-20","Residues 94 to 148 match (9e-08) PD:PD590328 which is described as PROTEOME COMPLETE PERMEASE MEMBRANE PERM TRANSMEMBRANE FAMILY ","","","","","Tue Feb 18 14:19:09 2003","","","","","","","Tue Dec 10 09:30:09 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00390 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 18 to 347 (E-value = 7.1e-94) place AA00390 in the UPF0118 family which is described as Domain of unknown function DUF20 (PF01594)","","","","","","","","1","","","" "AA00391","264961","265308","348","ATGTCCATTATTATCTATCACAACCCATCCTGCTCCAAAAGCTGTGAAACCCTGGCATTATTGGAAAGCCATCAAATTCAACCACAAATCGAGCTTTATTTGCAGAAAACCTATTCCGTTGCGGAGCTGCAAGCCATCGCCGATAAATTAGGCATTAGCGACATCCGCCAAATGATGCGCACCAAAGATGATCTGTATAAAAAACTCGGTTTAGATAACCCGACACTGGGTCAACAGGACTTGCTACAAGCTATTGCGCAACATTCCGCGTTATTAGAGCGCCCTATCGTGATTAACGGCGACAAAGCCAAAATCGGACGCCCGCCGGAAAGCGTACTGGCAATTCTG","","","12907","MSIIIYHNPSCSKSCETLALLESHQIQPQIELYLQKTYSVAELQAIADKLGISDIRQMMRTKDDLYKKLGLDNPTLGQQDLLQAIAQHSALLERPIVINGDKAKIGRPPESVLAIL","265308","","arsenate reductase","Cytoplasm","","
InterPro
IPR006659
Family
Arsenate reductase
TIGR00014\"[3-116]TarsC: arsenate reductase
InterPro
IPR006660
Family
Arsenate reductase and related
PF03960\"[6-115]TArsC
InterPro
IPR012335
Domain
Thioredoxin fold
G3DSA:3.40.30.10\"[1-116]Tno description


","BeTs to 6 clades of COG1393COG name: Arsenate reductase and related proteins, glutaredoxin familyFunctional Class: PThe phylogenetic pattern of COG1393 is ---------drlb-efghsnuj---wNumber of proteins in this genome belonging to this COG is","","Residues 2 to 116 match (4e-40) PD:PD004262 which is described as COMPLETE PROTEOME REDUCTASE ARSENATE ARSENICAL OXIDOREDUCTASE RESISTANCE PLASMID MODIFIER PUMP ","","","","","","","","","","","","Tue Dec 10 10:06:22 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00391 is paralogously related to AA00822 (3e-05).","","","","","","Residues 6 to 116 (E-value = 8.9e-44) place AA00391 in the ArsC family which is described as ArsC family (PF03960)","","","","","Stolz JF, Basu P, Oremland RS.Microbial transformation of elements: the case of arsenic and selenium.Int Microbiol. 2002 Dec;5(4):201-7.PMID: 12497186 Mukhopadhyay R, Rosen BP.Arsenate reductases in prokaryotes and eukaryotes.Environ Health Perspect. 2002 Oct;110 Suppl 5:745-8.PMID: 12426124 ","","Sat Feb 15 07:18:57 2003","1","","","" "AA00395","265711","265418","294","ATGACAGCAAAAACAGAAGTTTTATTTAACAACACATGGAACGTCAGAATCAGCGACCCGGGTGAAGAGGGCGCGCAAAGTCATTTTTTTGAAACCATTTATATTACGTTAGAAGCGCATATTAACGGAAACGACACCACATACGAATTTACCCGCAAAGTGGAAGACCAAATTAAGATTAAAAAAACATTCACCGATTTGGACAAATTATTCATTTATTTAAGCGAACAAATTTCCCCGGTGGCGTTGGGGCATTTGGGCATTAAAATCGGGAATTTGAGGTTGACAAATGAA","","","13839","MTAKTEVLFNNTWNVRISDPGEEGAQSHFFETIYITLEAHINGNDTTYEFTRKVEDQIKIKKTFTDLDKLFIYLSEQISPVALGHLGIKIGNLRLTNE","265418","","conserved hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
PD050153\"[52-93]TQ9CLT1_PASMU_Q9CLT1;


","No hits to the COGs database.","","Residues 52 to 93 match (8e-09) PD:PD050153 which is described as PROTEOME COMPLETE HI0234 PM1128 ","","","","","","","","","","","","Tue Dec 10 10:15:19 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00395 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00396","266012","265731","282","ATGGCAAAACAAAAATATGCCTTGCAAACCCCGCCTCAAAACGTGCAAGGGACGCTGACGTATCAGCATCAACGCGGGGTGATCAAAGATAATGCCATTCAGGCGTTATTACACGACAAACTCTTTCGTCAACGCATTGAGCGTAACAAGAAAGGCAAAGGCAGTTATCAGCGTAAAGCGAAACACGCAAATCGTTATTACGAAAAGCCCGATAATAATATTTCTCTGATCAGAGATGTTATTATCGGGCTTTTTTCTTTCTATTTATTTTGTGCAATATAT","","","11056","MAKQKYALQTPPQNVQGTLTYQHQRGVIKDNAIQALLHDKLFRQRIERNKKGKGSYQRKAKHANRYYEKPDNNISLIRDVIIGLFSFYLFCAIY","265731","","conserved hypothetical protein","Periplasm, Extracellular","","
InterPro
IPR005589
Family
Protein of unknown function DUF331
PD027616\"[21-65]TQ8ZLM4_SALTY_Q8ZLM4;
PF03889\"[23-71]TDUF331
noIPR
unintegrated
unintegrated
tmhmm\"[74-92]?transmembrane_regions


","BeTs to 5 clades of COG3036COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3036 is --------------efgh-n------Number of proteins in this genome belonging to this COG is","","Residues 21 to 65 match (2e-12) PD:PD027616 which is described as PROTEOME COMPLETE CYTOPLASMIC YPO0237 HI0235 PM1129 VCA0185 YHDL NMB1382 ","","","","","","","","","","","","Tue Dec 10 10:22:45 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00396 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 23 to 71 (E-value = 1.5e-27) place AA00396 in the DUF331 family which is described as Domain of unknown function (PF03889)","","","","","","","","1","","","" "AA00397","266209","267549","1341","TTGAGAAAATTTATGAGCACGCCCCCCAATATCGGCTTTGTCAGCCTTGGTTGTCCGAAAAATTTAGTGGATTCGGAACGCATTTTGACGGAATTGCGTTCCAATGGTTATAACATCATTCCGAGCTATGAAAACGCCGATTTGGTGATCGTCAACACCTGCGGTTTTATTGACAGCGCGGTGCAGGAATCGTTGGAAGCCATCGGCGAGGCGTTGGAAGAAAACGGCAAAGTGATTGTGACCGGCTGCCTTGGTGCCAAAGAAGACCAAATTCGCCAGGTGCATCCGAAAGTGTTGGAAATTTCGGGTCCGCACAGTTATGAAACCGTGATGAATCAGGTGCACAAATATGTGCCGAAACCGCAATATAGCCCTTATGAAAGCCTTGTGCCGGCGCAAGGGGTGAAACTGACGCCGAAGCATTATGCGTATTTGAAAATTTCCGAAGGCTGCGACCATCGCTGCACCTTCTGCATTATTCCGTCCATGCGCGGCGATTTGGACAGTCGCCCGATTACGCAAGTGTTAGACGAAGCGAAGCGCCTGGTGGACGCGGGGGTGAAAGAATTGCTGATCGTGTCGCAGGATACCTCGGCGTATGCCCTCGATCAAAGCAAAGAAAATCAAAACAAAACCGTGTTCTGGAACGGCATGCCGATTAAAAATAACCTCATCAGCTTATGCCGCCAGCTGGGCAATCTCGGCGTTTGGGTGCGTTTGCATTATGTTTATCCGTATCCGCACGTAGACGATCTGATTCCGCTCATGGCAGAAGGCAAATTATTGCCTTATTTGGATATTCCGTTGCAGCACGCCAGCCCGAAAATTCTCAAAACAATGAAAAGACCCGGCAAAATCGACCGCACTTTAGAACGCATTCAGCAATGGCGTGAAATTTGCCCGGAACTCACCTTGCGCTCCACCTTTATTGTGGGCTTCCCGGGCGAGACGGAAGAAGATTTCCAAATGTTGTTGGATTTCCTCAAAGCCGCCCAACTGGATCGCGTAGGCTGCTTCAAATTCAGCCCGGTAGAAGGCGCGCCGGCGACGGATATGCCGGATCAGGTGCCGGAAGAAGTGAAAGAAGAACGCTTCCACCGTTTCATGCAAGTACAACAAGAAATCTCTGCCGCACGCTTACAACAAAAAATCGGCAAAACCCTGTCGGTGATTGTGGATGAAGTGAACATGAAAGGCGTGATCGGTCGTTCCATGGCGGATGCGCCGGAAATCGACGGCGTGGTGTATGTGGAAAATCAAAGCCAAAGTGCGGTCAACATCGGCGACGTTATTTCCGTGACGATCACCGACGCCGACGAATATGATTTATGGGGAACCTGC","","","50112","LRKFMSTPPNIGFVSLGCPKNLVDSERILTELRSNGYNIIPSYENADLVIVNTCGFIDSAVQESLEAIGEALEENGKVIVTGCLGAKEDQIRQVHPKVLEISGPHSYETVMNQVHKYVPKPQYSPYESLVPAQGVKLTPKHYAYLKISEGCDHRCTFCIIPSMRGDLDSRPITQVLDEAKRLVDAGVKELLIVSQDTSAYALDQSKENQNKTVFWNGMPIKNNLISLCRQLGNLGVWVRLHYVYPYPHVDDLIPLMAEGKLLPYLDIPLQHASPKILKTMKRPGKIDRTLERIQQWREICPELTLRSTFIVGFPGETEEDFQMLLDFLKAAQLDRVGCFKFSPVEGAPATDMPDQVPEEVKEERFHRFMQVQQEISAARLQQKIGKTLSVIVDEVNMKGVIGRSMADAPEIDGVVYVENQSQSAVNIGDVISVTITDADEYDLWGTC","267549","","Fe-S oxidoreductase; MiaB-like RNA modifying enzyme (2-methylthioadenine synthetase)","Cytoplasm","","
InterPro
IPR002792
Domain
Deoxyribonuclease/rho motif-related TRAM
PS50926\"[381-447]TTRAM
InterPro
IPR005839
Family
Protein of unknown function UPF0004
PTHR11918\"[7-212]T\"[229-415]TRADICAL SAM PROTEINS
TIGR00089\"[10-445]TTIGR00089: RNA modification enzyme, MiaB fa
PS01278\"[145-165]TUPF0004
InterPro
IPR005840
Family
Conserved hypothetical protein 1125
TIGR01125\"[10-445]TTIGR01125: MiaB-like tRNA modifying enzyme
InterPro
IPR006638
Domain
Elongator protein 3/MiaB/NifB
SM00729\"[141-370]TElp3
InterPro
IPR007197
Domain
Radical SAM
PF04055\"[145-328]TRadical_SAM
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[148-360]Tno description
InterPro
IPR013848
Domain
Protein of unknown function UPF0004, N-terminal
PF00919\"[10-103]TUPF0004


","No hits to the COGs database.","Significant hit ( 3e-91) to 7/7 blocks of the IPB001861 family, which is described as \"Uncharacterized protein family UPF0004\". Interpro entry for IP:IPR001861. IPB001861A 13-32 4.2e-07 IPB001861B 46-56 0.0002 IPB001861C 69-92 0.00091 IPB001861D 143-193 8.7e-30 IPB001861E 225-254 0.00014 IPB001861F 265-285 2.7e-08 IPB001861G 301-344 1.1e-24 IPB001861E 227-256 0.0032","Residues 239 to 422 match (8e-18) PD:PD094241 which is described as COMPLETE PROTEOME CJ1006C HP0734 JHP0270 HP0285 CJ1454C ","","","","","Mon Feb 17 11:19:30 2003","","","","","","","Mon Feb 17 08:15:43 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00397 is paralogously related to AA02873 (2e-36).","","","","","","Residues 145 to 328 (E-value = 1.7e-27) place AA00397 in the Radical_SAM family which is described as Radical SAM superfamily (PF04055)","","","","","Pierrel F, Bjork GR, Fontecave M, Atta M.Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein.J Biol Chem. 2002 Apr 19;277(16):13367-70.PMID: 11882645 Urbonavicius J, Qian Q, Durand JM, Hagervall TG, Bjork GR.Improvement of reading frame maintenance is a common function for several tRNA modifications.EMBO J. 2001 Sep 3;20(17):4863-73.PMID: 11532950","","Mon Feb 17 08:15:43 2003","1","","","" "AA00398","267587","268078","492","ATGACTTTTTGGATAAAAATCATGTCACTAGTTAAAATTCTTTTTGTCTGTTTAGGCAATATTTGTCGTTCTCCCATGGCAGAGTACGTAATGCGCGAGAAAGTAAAACAAGCCAATGTACAAAAGCATATCATTACTGCCAGCGCAGGCACGTCCGGCTGGCATGACGGCGAAGATATGCACTGTGGTACCGCCGATATATTGGATCGGCATAAAATTTCTTCCAACGGCTTTGTCAGCCGTAAAGTGCGGTCAACAGATTGGACGGATTTTGATTATATTATCGCCATGGATAACCACAACCTGCGCGATTTAGAGCGGTTGTTCGGTTCTCATCCGAAAAAGCTGTTTCAAATCACCGCACTTTGCCCGACATTAGGCACCGACCATATTCCCGATCCTTGGTACACCAAAGATTTTAATCAGACCTACACATTGTTGGATCAATGCTGCGACGCTTTATTGGCAAAAATTCGACGGGAACATCATTTG","","","21136","MTFWIKIMSLVKILFVCLGNICRSPMAEYVMREKVKQANVQKHIITASAGTSGWHDGEDMHCGTADILDRHKISSNGFVSRKVRSTDWTDFDYIIAMDNHNLRDLERLFGSHPKKLFQITALCPTLGTDHIPDPWYTKDFNQTYTLLDQCCDALLAKIRREHHL","268078","","protein-tyrosine-phosphatase (PTPase)","Cytoplasm","","
InterPro
IPR000106
Family
Low molecular weight phosphotyrosine protein phosphatase
PR00719\"[13-30]T\"[90-105]T\"[131-146]TLMWPTPASE
PTHR11717\"[17-164]TLOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE
PF01451\"[11-157]TLMWPc
SM00226\"[11-157]TLMWPc
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.270\"[4-159]Tno description
PTHR11717:SF7\"[17-164]TLOW MOLECULAR WEIGHT PROTEIN-TYROSINE-PHOSPHATASE
signalp\"[1-19]?signal-peptide


","No hits to the COGs database.","Significant hit ( 2.4e-24) to 3/5 blocks of the PR00719 family, which is described as \"LMW phosphotyrosine protein phosphatase signature\". Prints database entry for PR:PR00719. PR00719A 13-30 7.7e-14 PR00719C 90-105 8.1e-07 PR00719E 131-146 2.4","Residues 106 to 160 match (2e-11) PD:PD500034 which is described as PROTEOME COMPLETE HYDROLASE ","","","","","","","","","","","","Tue Dec 10 10:50:25 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00398 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 11 to 157 (E-value = 7.3e-29) place AA00398 in the LMWPc family which is described as Low molecular weight phosphotyrosine protein phosphatase (PF01451)","","","","","Camici,G., Manao,G., Cappugi,G., Modesti,A., Stefani,M. andRamponi,G.The complete amino acid sequence of the low molecular weightcytosolic acid phosphataseJ. Biol. Chem. 264 (5), 2560-2567 (1989)PubMed: 2644264Morona JK, Morona R, Miller DC, Paton JC.Streptococcus pneumoniae capsule biosynthesis protein CpsB is a novel manganese-dependent phosphotyrosine-proteinphosphatase.J Bacteriol. 2002 Jan;184(2):577-83.PMID: 11751838Preneta R, Jarraud S, Vincent C, Doublet P, Duclos B, Etienne J, Cozzone AJ.Isolation and characterization of a protein-tyrosine kinase and a phosphotyrosine-protein phosphatase from Klebsiella pneumoniae.Comp Biochem Physiol B Biochem Mol Biol. 2002 Jan;131(1):103-12.PMID: 11742763","","Wed Feb 19 14:00:58 2003","1","","","" "AA00399","268208","268423","216","ATGTTTCCGGAATTCAGAGAGTTAATTACAAAACTCAAAACCGAAAATGCTTATTTTGCCAATCTATTTGATAAACATAACGAACTGGACCAACGTATTAAAAACATTGAATCCCATATTGAATTGGGTACGCACAATGAAGTGGAAATGTTGAAAAAGGAAAAATTACGTCTGAAAGATCAGATGTATGACATGCTGAAAAAAGCTGATGCTAAA","","","8694","MFPEFRELITKLKTENAYFANLFDKHNELDQRIKNIESHIELGTHNEVEMLKKEKLRLKDQMYDMLKKADAK","268423","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR007420
Family
Protein of unknown function DUF465
PF04325\"[19-68]TDUF465


","BeTs to 5 clades of COG2841COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG2841 is --------------ef-h-nu-----Number of proteins in this genome belonging to this COG is","","Residues 1 to 68 match (2e-14) PD:PD057627 which is described as PROTEOME COMPLETE HP1242 PM1568 NMA1258 CJ0449C ","","","","","","","","","","","","Tue Dec 10 11:13:15 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00399 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 19 to 68 (E-value = 7.4e-13) place AA00399 in the DUF465 family which is described as Protein of unknown function (DUF465) (PF04325)","","","","","","","","1","","","" "AA00401","269094","268501","594","ATGAAAGTTGCAAAAAATGTTGTGGTAAGCATTGCTTATCAAGTTCGTACCGAAGATGGCGTGTTGGTGGATGAAGCCCCGGCAAACCAACCGTTACAGTATTTACAAGGCCATAATAACTTAGTTATCGGCTTGGAAAATGCGTTAGAAGGCAAATCCGTCGGTGATAAATTTGAAGTCCGCGTGAAACCGGAAGAAGGTTACGGCGAGTATAATGAAAATATGGTACAACGCGTACCAAAAGATGTGTTTGTCGGCGTTGATGATTTAGAAGAGGGTATGCGTTTTATTGCTGATACCGACATGGGGCCGTTGCCGGTGGTGATTACCGAAGTGTGCGATACCGATGTGGTAGTTGACGGCAACCACATGTTAGCCGGTCAGGAATTACATTTCACCGTCGAAGTGGTTGATACTCGCGAAGCGACTTTAGAAGAAATCGCACACGGTCACTTACACCAAGAAGGTGGTTGCTGCGGTGGTCATGGTGATGACAGTGATGAAGAAGGTCACGGCTGCGGTTGCGGCGGTCATCACCATCATCATGACCACCATCATCATGGCGAAAGTGGTTGCGGCTGTGGCGGCAAACAC","","","21410","MKVAKNVVVSIAYQVRTEDGVLVDEAPANQPLQYLQGHNNLVIGLENALEGKSVGDKFEVRVKPEEGYGEYNENMVQRVPKDVFVGVDDLEEGMRFIADTDMGPLPVVITEVCDTDVVVDGNHMLAGQELHFTVEVVDTREATLEEIAHGHLHQEGGCCGGHGDDSDEEGHGCGCGGHHHHHDHHHHGESGCGCGGKH","268501","","FKBP-type peptidyl-prolyl cis-trans isomerase slyD (PPiase)","Cytoplasm","","
InterPro
IPR001179
Domain
Peptidyl-prolyl cis-trans isomerase, FKBP-type
PTHR10516\"[2-156]TFK506 BINDING PROTEIN
PF00254\"[2-137]TFKBP_C
PS50059\"[6-82]TFKBP_PPIASE
noIPR
unintegrated
unintegrated
G3DSA:3.10.50.40\"[2-88]Tno description
PTHR10516:SF31\"[2-156]TFKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE


","BeTs to 17 clades of COG1047COG name: FKBP-type peptidyl-prolyl cis-trans isomerases 2Functional Class: OThe phylogenetic pattern of COG1047 is aompkz---d----efghsnu---t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.7e-08) to 1/1 blocks of the IPB001179 family, which is described as \"FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase)\". Interpro entry for IP:IPR001179. IPB001179 36-69 1.7e-08","Residues 1 to 70 match (1e-09) PD:PD585838 which is described as ISOMERASE PEPTIDYL-PROLYL FKBP-TYPE COMPLETE PROTEOME CIS-TRANS PROBABLE ISOMERASE TRANS SLYD ","","","","","","","","","","","","Tue Dec 10 11:17:53 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00401 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 137 (E-value = 1.5e-05) place AA00401 in the FKBP_C family which is described as FKBP-type peptidyl-prolyl cis-trans isomerase (PF00254)","","","","","Roof,W.D., Horne,S.M., Young,K.D. and Young,R. slyD, a host gene required for phi X174 lysis, is related to the FK506-binding protein family of peptidyl-prolyl cis-trans-isomerases J. Biol. Chem. 269 (4), 2902-2910 (1994) PubMed: 8300625 Hottenrott,S., Schumann,T., Pluckthun,A., Fischer,G. and Rahfeld,J.U. The Escherichia coli SlyD is a metal ion-regulatedpeptidyl-prolyl cis/trans-isomerase J. Biol. Chem. 272 (25), 15697-15701 (1997) PubMed: 9188461 ","","Tue Dec 10 11:17:53 2002","1","","","" "AA00402","269908","269192","717","ATGAAATTCAAAGATTTAGTTTTATTGCTATTGCCCTTAAGCGTCGCTTTAACTGCCAACGCCGAAGCTAAGGTTACCGACGAACCGGAAAAAAACGTTATTTCTTTTAACACTGAAGTCACGAAAGAAGTGGATTATGACGTAATGGAAGTCACTCTTTTCGTGAAACAGGAAAATAAAAATCTAAAAGAATTGAACCAAGCGATTAACGAGAAAGTGAATGCTGCATTGGATGTGATTAAAAAACAAAGTGCGGTGCAAATTAAGAAAAATACGCGTAACACACAAGTGCGTTATGACAACAAAGGCAAACAATCCGGTTGGATTGAACGTGCCGATTTAGTGTTGGAAAGTAAGGATTTTGTAGTCTTATCCCAAGTCATTTCCGATTTAAACGAGACGTTCGCTATTGCTGATGTCATGCAAAAATTATCTAACGAAGCCGCAGTGAAATTTGAAGATGAAATGCTGAAAAGCGCGTTGGCACAGTTCCAACATAAAGCGCAGTTAATTCAGACTTCTCTTAATGCTAAAGGGTATGAAGTAATCAGTCTGGGGTTGGATAACAGAAATGAAATACCGTATTTTGGGGGGCGTATGATACCGGTGGCTAAAATGAAGTCTTTCGCTTCAGAGGTTGCTGACGAAGTGAGTCTTGACAGTAATGATAAAGCAGAATTAAAGACCTCGGTGAGTGCACAAATTAGGTTACTGAAC","","","26726","MKFKDLVLLLLPLSVALTANAEAKVTDEPEKNVISFNTEVTKEVDYDVMEVTLFVKQENKNLKELNQAINEKVNAALDVIKKQSAVQIKKNTRNTQVRYDNKGKQSGWIERADLVLESKDFVVLSQVISDLNETFAIADVMQKLSNEAAVKFEDEMLKSALAQFQHKAQLIQTSLNAKGYEVISLGLDNRNEIPYFGGRMIPVAKMKSFASEVADEVSLDSNDKAELKTSVSAQIRLLN","269192","","conserved hypothetical protein (possible periplasmic protein)","Outer membrane, Periplasm, Cytoplasm","","
InterPro
IPR007497
Family
Protein of unknown function DUF541
PF04402\"[30-232]TDUF541
noIPR
unintegrated
unintegrated
signalp\"[1-23]?signal-peptide


","BeTs to 3 clades of COG3471COG name: Predicted periplasmic/secreted proteinFunctional Class: SThe phylogenetic pattern of COG3471 is ---------------f-h-n------Number of proteins in this genome belonging to this COG is","","Residues 34 to 187 match (2e-30) PD:PD339927 which is described as PROTEOME COMPLETE PA4495 PM1566 PERIPLASMIC PEPTIDE SIGNAL RSC2404 NMB0848 ","","","","","","","","","","","","Tue Dec 10 11:21:24 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00402 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 30 to 232 (E-value = 5.7e-19) place AA00402 in the DUF541 family which is described as Protein of unknown function (DUF541) (PF04402)","","","","","","","","1","","","" "AA00404","270393","269962","432","ATGACAAATTTAGATGAATTACAGGCGGAAACCCGCGAGATCATTACCGATTTATTAAATGACGGTAGCGATCCAAATGCGCTTTATATTATTGAACATCATATCTCTCATCATAATTTTGATAAATTGGAAAAAATCGCTATGGACGCCTTTAAATCCGGTTATGAAGTGTCCGAGGCGGAGGAATTTGAGGAAGAGAACGGCAGGGTGATTTTCTGTTGCGATATTATCAGTGAAGTGGAATTAAAGCCCGAACTCATTGATGCGCAACAAAAAGAGTTGTTGCCGTTAATCGCCAAATACCAAGGCGGTTATGACGGTTGGGGCACTTATTTTGAAGATCCGGATGCCGATGATGACGAATATGGCGATGACGGTGAATTTTTTGACGAAGATGATGCCTTAGATGATGACGATGAGTTCGTTAAACGT","","","16550","MTNLDELQAETREIITDLLNDGSDPNALYIIEHHISHHNFDKLEKIAMDAFKSGYEVSEAEEFEEENGRVIFCCDIISEVELKPELIDAQQKELLPLIAKYQGGYDGWGTYFEDPDADDDEYGDDGEFFDEDDALDDDDEFVKR","269962","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR009671
Family
Protein of unknown function DUF1260
PF06877\"[6-112]TDUF1260
noIPR
unintegrated
unintegrated
PD020474\"[2-110]TYJGD_HAEIN_P44831;
G3DSA:3.30.70.970\"[4-122]Tno description


","BeTs to 3 clades of COG3076COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3076 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 4 to 110 match (2e-35) PD:PD020474 which is described as PROTEOME COMPLETE YJGD VC0424 ORF PM1565 HI0700 YPO3445 ","","","","","","","","","","","","Tue Dec 10 11:22:16 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00404 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 113 (E-value = 2.6e-80) place AA00404 in the DUF1260 family which is described as Protein of unknown function (DUF1260) (PF06877)","","","","","","","","1","","","" "AA00406","270883","270491","393","ATGAGTTTCATTAAAGAATTTCGTGAATTTGCCATGCGTGGCAATGTTGTTGATATGGCAGTCGGTGTAATCATCGGTGGCGCTTTCGGTAAAATTGTCAGTTCATTGGTGGCTGATGTTTTTATGCCGGTATTAGGTATTTTAACCGGTGGCATGGACTTTAAAGATTTGAAATTCGTCTTGGAACCGGCAAACGGTGATATTCCTGCCGTGACGTTAAACTATGGCGTATTTATTCAAAACGTATTTGATTTTGTTATTATTGCGTTTGCCATTTTCATGATGATTAAGGCGCTAAACAAACTGAAAAAACCGGAAGTGGTGGAAGAAGCGCCGGCAGAGCCTTCAACGGAAGAAAAATTATTAACTGAGATTCGTGATCTCCTCAAAAAA","","","14414","MSFIKEFREFAMRGNVVDMAVGVIIGGAFGKIVSSLVADVFMPVLGILTGGMDFKDLKFVLEPANGDIPAVTLNYGVFIQNVFDFVIIAFAIFMMIKALNKLKKPEVVEEAPAEPSTEEKLLTEIRDLLKK","270491","","large-conductance mechanosensitive channel","Inner membrane, Cytoplasm","","
InterPro
IPR001185
Family
Large-conductance mechanosensitive channel
PD007253\"[6-48]TQ749E9_GEOSL_Q749E9;
PR01264\"[6-20]T\"[84-92]T\"[93-102]TMECHCHANNEL
PF01741\"[3-131]TMscL
TIGR00220\"[3-131]TmscL: large conductance mechanosensitive ch
PS01327\"[13-26]TMSCL
noIPR
unintegrated
unintegrated
tmhmm\"[21-41]?\"[76-96]?transmembrane_regions


","BeTs to 9 clades of COG1970COG name: Large-conductance mechanosensitive channelFunctional Class: MThe phylogenetic pattern of COG1970 is ---------drlbcefghs--j----Number of proteins in this genome belonging to this COG is","Significant hit ( 2.9e-63) to 3/3 blocks of the IPB001185 family, which is described as \"Large-conductance mechanosensitive channel mscL\". Interpro entry for IP:IPR001185. IPB001185A 5-42 1.1e-34 IPB001185B 75-105 9.4e-20 IPB001185C 118-129 2.8e-06","Residues 5 to 50 match (8e-11) PD:PD540937 which is described as CHANNEL MECHANOSENSITIVE COMPLETE PROTEOME LARGE-CONDUCTANCE TRANSMEMBRANE CONDUCTANCE IONIC LARGE STRUCTURAL ","","","","","","","","","","","","Tue Dec 10 11:36:35 2002","","Thu Mar 18 10:03:14 2004","Thu Mar 18 10:03:14 2004","Thu Mar 18 10:03:14 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00406 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Mar 18 10:03:14 2004","","","","","Residues 3 to 131 (E-value = 7e-80) place AA00406 in the MscL family which is described as Large-conductance mechanosensitive channel, MscL (PF01741)","Thu Mar 18 10:03:14 2004","","","","Sukharev,S.I., Blount,P., Martinac,B., Blattner,F.R. and Kung,C.A large-conductance mechanosensitive channel in E. coli encoded bymscL aloneNature 368 (6468), 265-268 (1994)PubMed: 7511799","","Tue Dec 10 11:36:35 2002","1","","","" "AA00407","272369","270996","1374","ATGAAAATAATTATTTTAGGCGCCGGGCAAGTGGGTTCCACCCTGGCGGCGAATTTGGTCAGCGAAGATAATGATATTACGTTAATTGATGATGAATCTATGCGTTTGGAGCATTTGCAGGACAAGCATGATTTGCGCGTGATGCAAGGCTTGGCATCATCTCCGAAAGTGTTGCGCGAGGCAGGTGCGCCTGATGCGGATTTATTGATTGCGGTCACCGGTTCCGATGAAATTAACATGGTGGCTTGCCAAATTGCTTATACGCTATTTAATACGCCCACTAAAATCGCGCGTATTCGTAACGGCGAATATTTGAAAGAAAAAGAGAAATTATTTAATCCTGACGTACTTCCTATTGATCATATTATTTCGCCGGAGAATCTGGTCACCAAGGATATTGTGCGTTTGATAGAATATCCCGGCGCGTTGCAGGTGGCGCATTTAGCCAAAGACAAAATCAGTTTGGTCGTGGTGAAGGCGTATTACGGCGGACCTTTGGTGGGCTATCCGATTTCCACGTTGAAGGAACATATTCCTCATGTGGATTGTCGCGTAGTGTCCATTTTACGGCAGGATAAAGCCATTCGTCCGCAAGGTTCAACCATTATTGAAGCGGGCGATGAAGTGATGTTTATTTGCGCGACGGCGTACATCAAAGCAGTCATGAGCGAATTGCAACGCCTGGAAAAACCTTACAAACGCATTATGATTGTGGGCGGCGGTAATGTCGGCACCGGCGTGGCGAAGCAATTGGAAGATCACTGCACGGTGAAACTCATCGAACGCAATACCGAGCGTGCTGCGGTGTTAGCGGAGAAATTATCGAAAACCCTGGTGTTTAACGGTGACGCCTCCGACCAATCCTTGCTGTTTGAAGAACATATTGAAAATATTGATGTTTTTCTTTCCCTTTCCAGTGATGATGAAGCCAATATTATGTCCGCGCTGTTGGCAAAACGGCTCGGTGCGAAGAAAGCCATGGTGTTGATTCAGCGTATGGCATACATCAGTTTGATTCAAGGCGGCACTATTGATATTGCCATTTCGCCTCAACAAGCGACGATTTCTGCCTTGCTCGGACATGTGCGTAAAGGCGATGTGGCAAATGTAGTTTCTCTGCGTCACGGCTTGGCGGAAGCCTTGGAAATCATTGTACATGGCGATGAAACTACCTCTAATGTTATTGGTCGTCTTATCGGCGACTTAAAATTACCCACCGGTGCAATTATCGGCGCAATTCTGCGCGGGAATGAAGTCATTATCGGCAATAATCAACTTGTTATTCAGGAAGAGGATCATGTGGTCGTGTATTTAAGCGATAAGAAATATATTTCCGACCTGGAAAAATTATTCCAGCCAAGTGCATTTTTTATC","","","49976","MKIIILGAGQVGSTLAANLVSEDNDITLIDDESMRLEHLQDKHDLRVMQGLASSPKVLREAGAPDADLLIAVTGSDEINMVACQIAYTLFNTPTKIARIRNGEYLKEKEKLFNPDVLPIDHIISPENLVTKDIVRLIEYPGALQVAHLAKDKISLVVVKAYYGGPLVGYPISTLKEHIPHVDCRVVSILRQDKAIRPQGSTIIEAGDEVMFICATAYIKAVMSELQRLEKPYKRIMIVGGGNVGTGVAKQLEDHCTVKLIERNTERAAVLAEKLSKTLVFNGDASDQSLLFEEHIENIDVFLSLSSDDEANIMSALLAKRLGAKKAMVLIQRMAYISLIQGGTIDIAISPQQATISALLGHVRKGDVANVVSLRHGLAEALEIIVHGDETTSNVIGRLIGDLKLPTGAIIGAILRGNEVIIGNNQLVIQEEDHVVVYLSDKKYISDLEKLFQPSAFFI","270996","","trk system potassium uptake protein","Cytoplasm, Periplasm, Inner membrane","","
InterPro
IPR003148
Domain
TrkA-N
PF02254\"[3-125]T\"[235-350]TTrkA_N
PS51201\"[2-131]T\"[234-354]TRCK_N
InterPro
IPR006036
Family
TrkA potassium uptake protein
PR00335\"[2-16]T\"[19-33]T\"[49-59]T\"[60-70]T\"[73-87]TKUPTAKETRKA
InterPro
IPR006037
Domain
TrkA-C
PF02080\"[155-226]T\"[383-452]TTrkA_C
PS51202\"[143-227]T\"[368-453]TRCK_C
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[1-143]T\"[229-368]Tno description
signalp\"[1-16]?signal-peptide


","BeTs to 17 clades of COG0569COG name: K+ transport systems, NAD-binding componentFunctional Class: PThe phylogenetic pattern of COG0569 is aom-kz-qvdrlbcefgh-nu---twNumber of proteins in this genome belonging to this COG is","Significant hit ( 4.1e-32) to 5/5 blocks of the PR00335 family, which is described as \"TrkA potassium uptake protein signature\". Prints database entry for PR:PR00335. PR00335A 2-16 4.1e-08 PR00335B 19-33 5.9e-05 PR00335C 49-59 0.11 PR00335D 60-70 0.0067 PR00335E 73-87 1.3e-07 PR00335A 234-248 0.19Significant hit ( 2e-05) to 2/2 blocks of the IPB003148 family, which is described as \"KTN NAD-binding domain\". Interpro entry for IP:IPR003148. IPB003148A 4-16 0.029 IPB003148B 50-66 0.35","Residues 4 to 102 match (6e-07) PD:PD435267 which is described as CHANNEL PROTEOME COMPLETE POTASSIUM IONIC TRANSMEMBRANE ION CHANNEL RELATED PLASMID ","","","","","","","","","","","","Tue Dec 10 11:38:48 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00407 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 383 to 452 (E-value = 1.7e-12) place AA00407 in the TrkA_C family which is described as TrkA-C domain (PF02080)","","","","","Schlosser,A., Hamann,A., Bossemeyer,D., Schneider,E. andBakker,E.P. NAD+ binding to the Escherichia coli K(+)-uptake protein TrkA andsequence similarity between TrkA and domains of a family ofdehydrogenases suggest a role for NAD+ in bacterial transport.Mol. Microbiol. 9(3): 533-543.1993. PubMed: 8412700. Bossemeyer,D., Borchard,A., Dosch,D.C., Helmer,G.C., Epstein,W.,Booth,I.R. and Bakker,E.P. K+-transport protein TrkA of Escherichia coli is a peripheralmembrane protein that requires other trk gene products forattachment to the cytoplasmic membrane. J. Biol. Chem. 264(28): 16403-16410. 1989. PubMed: 2674131.Nakamura,T., Matsuba,Y., Yamamuro,N., Booth,I.R. and Unemoto,T.Cloning and sequencing of a K+ transport gene (trk A) from themarine bacterium Vibrio alginolyticusBiochim. Biophys. Acta 1219 (3), 701-705 (1994)PubMed: 7948029 Nakamura,T., Yamamuro,N., Stumpe,S., Unemoto,T. and Bakker,E.P.Cloning of the trkAH gene cluster and characterization of the TrkK(+)-uptake system of Vibrio alginolyticusMicrobiology 144 (Pt 8), 2281-2289 (1998)PubMed: 9720051","","Tue Dec 10 11:47:26 2002","1","","","" "AA00408","273748","272396","1353","ATGAAAACGAGCAAAGCAAAAACGTCGGCGGAAACCACCGCACTTTCCGCCCGCACGGCAGCGGTACAAATTCTTTTTCAGGTGCTGGAACAGGGGAAATCACTTTCATCCCTGTTGCCTGATGCTCAGGTGGTCATCAAAGCGCAGGATCTGCCGTTGTTACAGGAAATTTGCTTTGGCGTATGCCGTGTGTTGCCCCGTTTGGAACAGATTATTGCACAATTGGTTGATAAACCATTGTGCGGTAAAAAGCGTATTGTGCATTGCTTGCTGTTGGTCGGTTTGTATCAGATTTTATACACCCGTATTCCCGTTTATGCCGCCGTGGATGAAATAGTGAACACCGCTAAAAATCTGCAATTACAAAGTTTTCAGGGCTTGGTGAACGCCGTGTTACGTCGTTTTTTGCGTGAACAAGAAAGCATGCTGGCAAAAGTTGATAAACATTGGCAAACGCTACATCCCGACTGGTTGGTAAATAAGCTGAAAAAAGTGTACCCGAATTGGCGTGAGATTATCGAAGCTAATAACCAAAAACCGCCTATGTGGTTGCGGGTCAACACACAAAAAAACAGCCTGGAAACGTACCGCACTTTATTGACGGCACAGCAAATGGACGCGCAGATCACGTCCCATCCGCAGGCACTGGGATTAACGCAGCCGACTTCCGTGCAGTATTTGCCGTTATTTGCCGAAGGCGGCGTGACGGTGCAGGATCTCCATGCCCAATGGGCGGCGTTGTTGTTACAGCCGCAAAACGGTGAACTGATTTTAGACGCCTGTGCGGCACCGGGCGGCAAAACCACCCATATTTTGGAACTGGCACCGCAGGCGGAAGTCGTGGCTTTGGATGTGGAAGAAAACCGTTTACAGCGGGTAAAAGAAAATCTGGCGCGTATGCAGCAGCAGGCGACCATCGTATGCGGTGATGCGGCAAATCCGCGGGCATGGTTGACGAAATTGGGGAAAAGTGCGGTGCGTTTTGACCGCATTTTATTAGACGCACCTTGTTCCGCCACCGGTGTGATTCGTCGTCATCCGGATATTAAATGGCTGCGTAAAGAAGCGGATATCGAACCGTTGGTTGAACTACAAGAGCAAATTTTGCAGGCATTATGGCCGTATTTGAAACCGAGCGGGGTTTTGTTATACGCCACCTGTTCCGTGCTGGCAGAGGAAAACGCCCGGCAAATTGAACGATTTTTACAACACACACCGGACGCGCAACCTACGGCATTGAATTTGCCGGAAGAGGTGTTGGCGCGCAACCAAAGTGCGGTCGGTTTTCAGTTTATTCCACAAACGGATGGCGGCGACGGTTTTTATTACGCGAAATTGGTTAAACGCGAAAGC","","","50531","MKTSKAKTSAETTALSARTAAVQILFQVLEQGKSLSSLLPDAQVVIKAQDLPLLQEICFGVCRVLPRLEQIIAQLVDKPLCGKKRIVHCLLLVGLYQILYTRIPVYAAVDEIVNTAKNLQLQSFQGLVNAVLRRFLREQESMLAKVDKHWQTLHPDWLVNKLKKVYPNWREIIEANNQKPPMWLRVNTQKNSLETYRTLLTAQQMDAQITSHPQALGLTQPTSVQYLPLFAEGGVTVQDLHAQWAALLLQPQNGELILDACAAPGGKTTHILELAPQAEVVALDVEENRLQRVKENLARMQQQATIVCGDAANPRAWLTKLGKSAVRFDRILLDAPCSATGVIRRHPDIKWLRKEADIEPLVELQEQILQALWPYLKPSGVLLYATCSVLAEENARQIERFLQHTPDAQPTALNLPEEVLARNQSAVGFQFIPQTDGGDGFYYAKLVKRES","272396","","SUN protein (FMU protein)","Cytoplasm","","
InterPro
IPR001678
Domain
Bacterial Fmu (Sun)/eukaryotic nucleolar NOL1/Nop2p
PF01189\"[172-447]TNol1_Nop2_Fmu
PS01153\"[328-339]TNOL1_NOP2_SUN
InterPro
IPR004573
Family
Fmu, rRNA SAM-dependent methyltransferase
TIGR00563\"[18-450]TrsmB: ribosomal RNA small subunit methyltra
InterPro
IPR006027
Domain
NusB/RsmB/TIM44
G3DSA:1.10.940.10\"[11-155]Tno description
PF01029\"[15-139]TNusB
InterPro
IPR006174
Domain
rRNA subunit methyltransferase
PD005242\"[175-243]TRSMB_PHOLL_Q7MYI0;
noIPR
unintegrated
unintegrated
G3DSA:1.10.287.730\"[155-180]Tno description
G3DSA:3.30.70.1170\"[181-237]Tno description
G3DSA:3.40.50.150\"[238-449]Tno description
PTHR22807\"[219-450]TNOP2(YEAST)-RELATED NOL1/NOP2/FMU(SUN) DOMAIN-CONTAINING
PTHR22807:SF12\"[219-450]TRIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE B (SUN)


","BeTs to 19 clades of COG0144COG name: tRNA and rRNA cytosine-C5-methylasesFunctional Class: JThe phylogenetic pattern of COG0144 is aom-kzy-vdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 9.9e-56) to 6/6 blocks of the IPB001678 family, which is described as \"NOL1/NOP2/sun family\". Interpro entry for IP:IPR001678. IPB001678A 238-249 0.77 IPB001678B 257-271 4.5e-11 IPB001678C 278-301 3.6e-06 IPB001678D 328-345 1.1e-12 IPB001678E 377-403 8.5e-12 IPB001678F 432-448 2.7e-05Significant hit ( 8.1e-15) to 3/3 blocks of the IPB000139 family, which is described as \"Antitermination protein NusB\". Interpro entry for IP:IPR000139. IPB000139A 18-29 7.5 IPB000139B 86-98 0.0016 IPB000139C 103-135 8e-08","Residues 18 to 161 match (4e-08) PD:PD038046 which is described as COMPLETE PROTEOME SUN FMU BH2507 450AA FMV LONG ","","","","","","","","","","","","Tue Dec 10 12:24:03 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00408 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 172 to 447 (E-value = 5.3e-119) place AA00408 in the Nol1_Nop2_Sun family which is described as NOL1/NOP2/sun family (PF01189)","","","","","Meinnel,T., Guillon,J.M., Mechulam,Y. and Blanquet,S.The Escherichia coli fmt gene, encoding methionyl-tRNA(fMet)formyltransferase, escapes metabolic controlJ. Bacteriol. 175 (4), 993-1000 (1993)MEDLINE :93163064","","Tue Dec 10 12:24:03 2002","1","","","" "AA00409","274704","273751","954","ATGAAACCACTCAATATTATCTTTGCCGGTACGCCGGACTTCGCTGCACGGCATTTACAAGCCTTACTCAATTCTTCCCATAACGTGATTGCGGTTTATACTCAACCGGACAAACCCGCCGGTCGGGGAAAGAAATTGCAATCCAGCCCGGTGAAACAGTTAGCCGAGCAACATCAAATTCCCGTCTATCAACCGAAATCTTTACGTAAAGCGGAAACACAAGCAGAATTGACCGCACTTCAGGCGGATGTCATGGTCGTTGTGGCGTACGGTTTGATTTTGCCACAAGTGGTGCTGGATGCACCGAAGTATGGCTGTCTCAATGTGCACGGTTCTCTGTTGCCGCGTTGGCGCGGTGCGGCGCCGATTCAGCGGGCGATTTGGGCCGGTGATGCACAAACCGGAGTAACCACTATGCAAATGGATGCAGGCTTGGATACAGGCGATATGTTGCACAAAGTTTATTGTGACATTACTTTGCAGGAAACTTCCGCCGGTCTATATGCCAAGCTGGCAGAAATTGCTCCCGCTGCGCTGGTTGAGGTGTTGGATCATTTAACCGACGGCACTTTTACCGCCGAACGCCAGGATGACGCGCAAAGTAGTTATGCCGAAAAATTATCAAAAGAGGAAGCAAAACTGAATTGGCAATTATCGGCGGCACAACTGGAACGCAATATCCGCGCCTTTAACCCTTGGCCTATTGCCTATCTGGAATTAACCGACGGGGCAGGCAATCCGCAAACCCTGAAGGTTTATCAAGCCGCTGTGCTGCCGCATACCAATAAAGCCCCCGGAACGATTTTATCGGCGGATAAGCACGGCATTCAAATTGCGACGGTTGACGGCGTATTGAATTTGTTACAGTTACAACCGTCAGGCAAGAAACCTATGTCCGCACAGGATTTGTTAAACGGGCGTGCCGACTGGTTTCAGGTCGGCAAGGCATTGCCA","","","34583","MKPLNIIFAGTPDFAARHLQALLNSSHNVIAVYTQPDKPAGRGKKLQSSPVKQLAEQHQIPVYQPKSLRKAETQAELTALQADVMVVVAYGLILPQVVLDAPKYGCLNVHGSLLPRWRGAAPIQRAIWAGDAQTGVTTMQMDAGLDTGDMLHKVYCDITLQETSAGLYAKLAEIAPAALVEVLDHLTDGTFTAERQDDAQSSYAEKLSKEEAKLNWQLSAAQLERNIRAFNPWPIAYLELTDGAGNPQTLKVYQAAVLPHTNKAPGTILSADKHGIQIATVDGVLNLLQLQPSGKKPMSAQDLLNGRADWFQVGKALP","273751","","methionyl-tRNA formyltransferase","Periplasm, Cytoplasm","","
InterPro
IPR001555
Active_site
Phosphoribosylglycinamide formyltransferase, active site
PS00373\"[135-158]TGART
InterPro
IPR002376
Domain
Formyl transferase, N-terminal
G3DSA:3.40.50.170\"[1-208]Tno description
PF00551\"[1-183]TFormyl_trans_N
InterPro
IPR005793
Domain
Formyl transferase, C-terminal
PF02911\"[208-308]TFormyl_trans_C
InterPro
IPR005794
Family
Methionyl-tRNA formyltransferase
TIGR00460\"[4-317]Tfmt: methionyl-tRNA formyltransferase
InterPro
IPR015518
Family
Methionine tRNA Formyltransferase-like
PTHR11138\"[68-311]TMETHIONYL-TRNA FORMYLTRANSFERASE
noIPR
unintegrated
unintegrated
G3DSA:3.10.25.10\"[209-318]Tno description


","No hits to the COGs database.","Significant hit ( 4.6e-07) to 1/1 blocks of the IPB001555 family, which is described as \"Phosphoribosylglycinamide formyltransferase active site\". Interpro entry for IP:IPR001555. IPB001555 107-119 4.8e-07","Residues 209 to 306 match (1e-08) PD:PD036500 which is described as TRANSFERASE COMPLETE PROTEOME METHIONYL-TRNA FORMYLTRANSFERASE METHYLTRANSFERASE BIOSYNTHESIS PROBABLE FORMYL YFBG ","","","","","","","","","","","","Tue Dec 10 12:41:31 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00409 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 208 to 308 (E-value = 9.6e-39) place AA00409 in the Formyl_trans_C family which is described as Formyl transferase, C-terminal domain (PF02911)","","","","","Guillon,J.M., Mechulam,Y., Schmitter,J.M., Blanquet,S. andFayat,G. Disruption of the gene for Met-tRNA(fMet) formyltransferase severely impairs growth of Escherichia coli J. Bacteriol. 174 (13), 4294-4301 (1992) PubMed: 1624424 Meinnel,T., Guillon,J.M., Mechulam,Y. and Blanquet,S. The Escherichia coli fmt gene, encoding methionyl-tRNA(fMet) formyltransferase, escapes metabolic control J. Bacteriol. 175 (4), 993-1000 (1993) PubMed: 8432722 Schmitt,E., Blanquet,S. and Mechulam,Y. Structure of crystalline Escherichia coli methionyl-tRNA(f)Met formyltransferase: comparison with glycinamide ribonucleotide formyltransferase EMBO J. 15 (17), 4749-4758 (1996) PubMed: 8887566 ","","Tue Dec 10 12:41:31 2002","1","","","" "AA00410","275282","274773","510","ATGACAGCTTTAAATGTACTTATTTACCCGGAAGAGCACCTTAAAGTGGTTTGCGATCCGGTCGTGGAAGTCAATGACAACACGCGTAAGATTATTGATAATATGTTTGATACCATGTATCAGGAAGGCGGTATCGGCCTAGCGGCACCGCAGGTGGATATTTTACAGCGTATTATCACTATTGATATTGAGGGTGACAAACAAAACCAGTTAGTGTTGATTAACCCTGAAATTTTGGAATCGGAAGGTGAAACCGGAATTGAAGAGGGTTGTTTGTCGATTCCCGGATTTCGTGCGTTAGTGCCACGTAAAGAGAAAGTGACTGTAAAAGCGCTGGATCGTCATGGTAAAGAATTCACCTTAAAAGCCGATGGTCTGTTGGCAATTTGTATTCAGCATGAAATTGATCATTTAAACGGTATTCTTTTTGTGGATTATCTCTCTCCATTGAAACGTCAGCGGATTAAAGAAAAGCTGATTAAAATGAAAAAGCAGATGGAAAAGCAAAAA","","","20615","MTALNVLIYPEEHLKVVCDPVVEVNDNTRKIIDNMFDTMYQEGGIGLAAPQVDILQRIITIDIEGDKQNQLVLINPEILESEGETGIEEGCLSIPGFRALVPRKEKVTVKALDRHGKEFTLKADGLLAICIQHEIDHLNGILFVDYLSPLKRQRIKEKLIKMKKQMEKQK","274773","","peptide deformylase (PDF) (Polypeptide deformylase)","Cytoplasm","","
InterPro
IPR000181
Family
Formylmethionine deformylase
PD003844\"[19-142]TDEF_HAEIN_P44786;
PR01576\"[33-62]T\"[89-100]T\"[101-119]T\"[120-149]TPDEFORMYLASE
G3DSA:3.90.45.10\"[2-169]Tno description
PIRSF004749\"[3-169]TPeptide deformylase
PTHR10458\"[7-168]TPOLYPEPTIDE DEFORMYLASE
PF01327\"[3-153]TPep_deformylase
TIGR00079\"[3-161]Tpept_deformyl: peptide deformylase


","BeTs to 18 clades of COG0242COG name: N-formylmethionyl-tRNA deformylaseFunctional Class: JThe phylogenetic pattern of COG0242 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 4.3e-66) to 3/3 blocks of the IPB000181 family, which is described as \"Formylmethionine deformylase\". Interpro entry for IP:IPR000181. IPB000181A 21-61 1.4e-21 IPB000181B 73-88 0.00016 IPB000181C 101-147 1.6e-37","Residues 45 to 140 match (3e-07) PD:PD483466 which is described as DEFORMYLASE POLYPEPTIDE PROTEOME PDF COMPLETE ZINC PEPTIDE DEFORMYLASE-LIKE FORMYLMETHIONINE BIOSYNTHESIS ","","","","","","","","","","","","Tue Dec 10 12:44:29 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00410 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 153 (E-value = 3.4e-86) place AA00410 in the Pep_deformylase family which is described as Polypeptide deformylase (PF01327)","","","","","Mazel,D., Pochet,S. and Marliere,P. Genetic characterization of polypeptide deformylase, adistinctive enzyme of eubacterial translation. EMBO J. 13(4): 914-923. 1994. PubMed: 8112305. Meinnel,T. and Blanquet,S. Enzymatic properties of Escherichia coli peptide deformylase. J.Bacteriol. 177(7): 1883-1887.1995. PubMed: 7896716. Meinnel,T., Guillon,J.M., Mechulam,Y. and Blanquet,S. The Escherichia coli fmt gene, encoding methionyl-tRNA(fMet) formyltransferase, escapes metabolic control J. Bacteriol. 175 (4), 993-1000 (1993) PubMed: 8432722 ","","Tue Dec 10 12:45:04 2002","1","","","" "AA00411","275938","276348","411","ATGCTTTCAGCACTTATCTCTCCCGCACTTAGCTACCCGGCTATGCGTCTGGCGACACAACCGGAACACCAGCGGTGCGTCCACTCCGGTCCTCTCGTACTAGGAGCAGCCCCAACCAATTCTCCTACGCCCACGGCAGATAGGGACCGAACTGTCTCACGACGTTCTAAACCCAGCTCGCGTACCACTTTAAATGGCGAACAGCCATACCCTTGGGACCTACTTCAGCCCCAGGATGTGATGAGCCGACATCGAGGTGCCAAACACCGCCGTCGATATGAACTCTTGGGCGGTATCAGCCTGTTATCCCCGGAGTACCTTTTATCCGTTGAGCCGATGGCCCTTCCATGCAGGAACCACCGGATCACTATGACCTACTTTCGTACCTGCCCGACCTGTCCGTATAACAGT","","","15384","MLSALISPALSYPAMRLATQPEHQRCVHSGPLVLGAAPTNSPTPTADRDRTVSRRSKPSSRTTLNGEQPYPWDLLQPQDVMSRHRGAKHRRRYELLGGISLLSPEYLLSVEPMALPCRNHRITMTYFRTCPTCPYNS","276348","","hydrolase","Periplasm","This sequence is similar to gi|27363940, a predicted cell-wall hydrolase from V.vulnificus. See also gi|11282815 from Chlamydia muridarum.","
noIPR
unintegrated
unintegrated
PD293281\"[1-104]TQ8CME1_BBBBB_Q8CME1;


","No hits to the COGs database.","","Residues 1 to 111 match (2e-31) PD:PD293281 which is described as PROTEOME COMPLETE TC0114 ","","","","","","","","","","","","Sun Feb 22 15:37:33 2004","Sun Feb 22 15:37:33 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequnce is paralogous to AA1779, AA1489, AA0832, AA0404, AA0273 and AA1024, conserved hypothetical proteins.AA00411 is paralogously related to AA02296 (1e-61), AA01262 (1e-61), AA00620 (1e-61) and AA01567 (4e-12).","Sun Feb 22 15:37:33 2004","","","","","","","","","","","","","1","","","" "AA00412","279514","279314","201","ATGGCGTATACAGAGGGTAACCAACCAGCGATGGGGAGTGAATCTCAGAAAGTGCGTCTAAGTTCGGATTGGAGTCTGCAACTCGACTCCATGAAGTCGGAATCGCTAGTAATCGCGAATCAGAATGTTGCGGTGAATACGTTCCCGGGCCTTGTACACACCGCCCGTCACACCATGGGAGTGGGTTGTACCAGAAGTGGA","","","7166","MAYTEGNQPAMGSESQKVRLSSDWSLQLDSMKSESLVIANQNVAVNTFPGLVHTARHTMGVGCTRSG","279314","","conserved hypothetical protein","Periplasm","This sequence is similar to gi27359373, a conserved hypothetical protein from Vibrio vulnificus. See also gi23015882, a hypothetical protein from Magnetospirillum magnetotacticum.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 15:44:46 2004","Sun Feb 22 15:44:46 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00412 is paralogously related to AA02297 (7e-35), AA01566 (7e-35), AA01261 (7e-35), AA00621 (7e-35) and AA02421 (2e-27).","Sun Feb 22 15:40:55 2004","","","","","","","","","","","","","1","","","" "AA00413","280282","280614","333","ATGCTATTAACACACCAACCTTCCTCAATACCGAAAGAACTTTACAACCCGAAGGCCTTCTTCATTCACGCGGCATGGCTGCGTCAGGGTTGCCCCCATTGCGCAATATTCCCCACTGCTGCCTCCCGTAGGAGTCCGGGCCGTGTCTCAGTCCCGGTGTGGCTGGCCATCCTCTCAGACCAGCTAGCGATCGTCGGCTTGGTAGGCCCTTACCCCACCAACTACCTAATCACACTTGGGTTCATCTCATGGCATGCGGCCATAAAGTCCCGCACTTTNGTCTCCCGACCCTACGCGGTATTAGCGACAGTTTCCCGTCGTTATCCCCCTCCA","","","12162","MLLTHQPSSIPKELYNPKAFFIHAAWLRQGCPHCAIFPTAASRRSPGRVSVPVWLAILSDQLAIVGLVGPYPTNYLITLGFISWHAAIKSRTXVSRPYAVLATVSRRYPPP","280614","","conserved hypothetical protein","Periplasm, Inner membrane","This sequence is similar to gi|27360487, a conserved hypothetical protein from Vibrio vulnificus. See also gi|10039641 from Chlorobium tepidum.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 15:44:19 2004","Sun Feb 22 15:44:19 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00413 is paralogously related to AA02422 (9e-63), AA02298 (9e-63), AA00622 (9e-63), AA01565 (1e-29) and AA01260 (4e-13).","Sun Feb 22 15:44:19 2004","","","","","","","","","","","","","1","","","" "AA00414","281593","281039","555","ATGAAAAAAGCGGTTTTTTTGGATCGTGACGGTACGCTCAATATTGACTATGGTTATGTGCACGAAATTAATCATTTTCGTTTTATTGACGGCAGTATTGAAGCATTAAAAAAATTAAAAAACATGGGTTATTTATTGGTGTTGGTCACAAATCAATCGGGAATTGCCCGAGGCTATTTTACGGAGCAACAATTTTTGCAACTGACGGAATGGATGGATTGGTCGTTGGCTGATCGTGGTGTCGATTTAGATGGAATTTATTACTGCCCGCATCATCCTGAGGCAAAAATTACTGAATTTAAGCAAGATTGTGATTGTCGTAAACCAAAATCAGGCATGTTATTGCAAGGGATTAAAGAACTGAATATTGATCCGAGCAGATCTATTATGATCGGCGATAAAACAGAAGATCTTTTGGCGGGGAAAGGGGCGAAAATAGGTACGACTATCTTAGTACGTACGGGTAAAGAGGTCACGTCGGAGGGAGAAAAGGAAGCCGATTATGTGCTGGATTCTATCGCGGATCTGCCCAGGCTAATTTCTGCACAAAAGATC","","","20844","MKKAVFLDRDGTLNIDYGYVHEINHFRFIDGSIEALKKLKNMGYLLVLVTNQSGIARGYFTEQQFLQLTEWMDWSLADRGVDLDGIYYCPHHPEAKITEFKQDCDCRKPKSGMLLQGIKELNIDPSRSIMIGDKTEDLLAGKGAKIGTTILVRTGKEVTSEGEKEADYVLDSIADLPRLISAQKI","281040","","possible histidinol-phosphatase","Cytoplasm","","
InterPro
IPR004446
Domain
Histidinol phosphatase-related protein
TIGR00213\"[2-178]TGmhB_yaeD: D,D-heptose 1,7-bisphosphate pho
InterPro
IPR005834
Domain
Haloacid dehalogenase-like hydrolase
PF00702\"[30-154]THydrolase
InterPro
IPR006543
Domain
Histidinol-phosphate phosphatase
TIGR01656\"[3-155]THistidinol-ppas: histidinol-phosphate phosp
InterPro
IPR006549
Domain
HAD-superfamily hydrolase, subfamily IIIA
TIGR01662\"[3-155]THAD-SF-IIIA: hydrolase, HAD-superfamily, su
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1000\"[3-181]Tno description
PTHR23133\"[1-184]TIMIDAZOLEGLYCEROL-PHOSPHATE DEHYDRATASE HIS7
PTHR23133:SF3\"[1-184]THIS7-RELATED


","BeTs to 12 clades of COG0241COG name: Histidinol phosphatase and related phosphatasesFunctional Class: EThe phylogenetic pattern of COG0241 is --mp------r--cefghsnuj----Number of proteins in this genome belonging to this COG is","","Residues 136 to 184 match (5e-11) PD:PD380208 which is described as PROTEOME COMPLETE PM1727 HI0621.1 ","","","","","","","","","","","","Thu May 19 15:20:45 2005","","Thu May 19 15:20:45 2005","","Thu May 19 15:20:45 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA00414 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu May 19 15:20:45 2005","","","","","","","","","","Kneidinger,B., Graninger,M., Puchberger,M., Kosma,P. and Messner,P.Biosynthesis of nucleotide-activated D-glycero-D-manno-heptoseJ. Biol. Chem. 276 (24), 20935-20944 (2001)PubMed: 11279237Chiariotti L, Nappo AG, Carlomagno MS, Bruni CB.Gene structure in the histidine operon of Escherichia coli. Identification and nucleotide sequence of the hisB gene.Mol Gen Genet. 1986 Jan;202(1):42-7.PMID: 3007936","","Tue Dec 10 17:00:31 2002","1","","","" "AA00415","281790","282824","1035","ATGATTAAGCTACAGAATGTAAGTAAAATTTTCGACGTTTCAGGCAAAAAACTGACCGCACTTGATAACGTTTCTTTAGATATTCCGAAAGGATATATCTGTGGTGTTATCGGCGCATCCGGTGCCGGCAAGAGCACCTTAATTCGTTGCGTTAACCTGTTGGAAAAACCGACCATGGGAGCCGTGATCATTGACGGCAACGATCTCACCCAACTCAGCGATGCGGAACTCGTGTTAGAACGCCGTAATATCGGCATGATCTTTCAACATTTTAATTTATTAAGCTCCCGTACCGTCTTCGGCAATGTCGCCCTGCCTTTAGAATTAGAAAATACGCCAAAAGAAAATATTGAAAGCAAAGTCAACGAATTACTTTCTTTAGTCGGCTTAAGTGATAAAAGAAATGTTTATCCGTCGAATTTATCCGGCGGTCAAAAGCAACGCGTCGCCATTGCCCGCGCACTCGCCAGTAATCCGAAAGTGTTATTGTGCGACGAAGCTACCAGCGCGCTGGATCCGGCAACCACACAATCCATTTTAAAATTGTTAAAAGAAATCAACCGCACTTTAGGTATCACAATCCTGTTAATCACGCACGAAATGGATGTGGTCAAACGCATTTGCGATTCGGTGGCGATTATCGATCAAGGAAAATTAGTGGAACAAGGTTCCGTCAGTGATATTTTCTCCAATCCGAAAACCGAACTGGCACAACAATTTATTCGTTCTACCTTCAACGTCAATTTACCTGACGAGTATCTAGATAATCTGTTACAAACGCCAAAACACGCAAAATCCTACCCGATTATTAAATTTGAATTTACCGGCCGCTCCGTAGATGCGCCTTTGTTATCGCAGACCTCAAAAAAATTCGGGGTGGAATTAAGCATTTTAACATCACAAATTGAATATGCCGGCGGGGTGAAATTCGGTTTTACCGTGGCGGAAGTGGAAGGTGATGAAGACGCCATTACCCAAGCAAAAATCTATTTAATGGAAAATAACGTACGCGTTGAGGTGCTAGGCTATGTGGAA","","","37713","MIKLQNVSKIFDVSGKKLTALDNVSLDIPKGYICGVIGASGAGKSTLIRCVNLLEKPTMGAVIIDGNDLTQLSDAELVLERRNIGMIFQHFNLLSSRTVFGNVALPLELENTPKENIESKVNELLSLVGLSDKRNVYPSNLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTQSILKLLKEINRTLGITILLITHEMDVVKRICDSVAIIDQGKLVEQGSVSDIFSNPKTELAQQFIRSTFNVNLPDEYLDNLLQTPKHAKSYPIIKFEFTGRSVDAPLLSQTSKKFGVELSILTSQIEYAGGVKFGFTVAEVEGDEDAITQAKIYLMENNVRVEVLGYVE","282825","","D-methionine ABC transporter, ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[140-183]TMETN_HAEIN_P44785;
PF00005\"[31-217]TABC_tran
PS50893\"[2-241]TABC_TRANSPORTER_2
PS00211\"[141-155]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[30-217]TAAA
InterPro
IPR012692
Family
D-methionine ABC transporter, ATP-binding
TIGR02314\"[1-344]TABC_MetN: D-methionine ABC transporter, ATP
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[1-244]Tno description
PTHR19222\"[2-307]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF34\"[2-307]TMETHIONINE ABC TRANSPORTER


","BeTs to 12 clades of COG1135COG name: Uncharacterized ABC-type transport system ATPase componentFunctional Class: RThe phylogenetic pattern of COG1135 is ---------d-lbcefghsnuj-it-Number of proteins in this genome belonging to this COG is","Significant hit ( 6.7e-42) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 20-66 9.8e-15 IPB001140B 138-176 2.9e-24 IPB001140C 194-223 4.7","Residues 84 to 217 match (2e-07) PD:PD588333 which is described as ATP-BINDING PROTEOME COMPLETE COMPONENT POSSIBLE COBALT ABC SUBUNIT ABC- PROTEIN ","","","","","","","","","","","","Tue Dec 10 13:31:31 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00415 is paralogously related to AA01524 (4e-43), AA00700 (3e-40), AA01422 (2e-39), AA02718 (4e-38), AA01616 (8e-37), AA00858 (1e-36), AA01645 (7e-35), AA02353 (2e-34), AA02080 (4e-34), AA02324 (2e-32), AA02899 (3e-32), AA02805 (6e-31), AA02440 (1e-30), AA01779 (2e-29), AA01568 (1e-28), AA01051 (1e-28), AA01656 (5e-28), AA02140 (2e-26), AA01961 (6e-26), AA01867 (6e-26), AA02898 (2e-25), AA02320 (2e-24), AA01947 (3e-21), AA01393 (3e-21), AA01569 (5e-21), AA01510 (6e-21), AA01684 (5e-20), AA02786 (7e-20), AA00207 (9e-20), AA00799 (4e-19), AA02152 (1e-18), AA00751 (1e-18), AA02550 (2e-18), AA00933 (3e-18), AA01824 (5e-18), AA01820 (1e-17), AA02606 (2e-17), AA02609 (9e-17), AA02331 (2e-16), AA01456 (3e-16), AA01509 (8e-16), AA02642 (1e-15), AA02573 (6e-15), AA02484 (2e-14), AA02225 (2e-14), AA01757 (5e-14), AA01555 (3e-11), AA00591 (2e-09), A02145 (6e-08), AA02146 (8e-07), AA00934 (1e-06), AA00061 (3e-06) and AA01291 (4e-05).","","","","","","Residues 31 to 217 (E-value = 1.2e-68) place AA00415 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Allikmets,R., Gerrard,B., Court,D. and Dean,M. Cloning and organization of the abc and mdl genes of Escherichia coli: relationship to eukaryotic multidrug resistance Gene 136 (1-2), 231-236 (1993) PubMed: 7904973 ","","Tue Dec 10 13:25:15 2002","1","","","" "AA00416","282817","283491","675","ATGTGGAATGATTTTTTAACGCAACTTACGCCCCAAATGTGGCAAACAGTGTGGGTTTCCACTTATGAAACCGTGTATATCAGCTTTGCTTCCACGTTTCTGGCGGTGATCGTCGGTTTACCCTTCGGTGTGCTGACATTCCTGACCGGAAAAGGCGAAATTTTACAAAATGCCCGCTTAAATCTGATACTCAACATCGTGATTAATATCGGACGTTCAATTCCATTCATTATTCTGTTAATTATTTTGTTGCCATTTACCCGTTTTGTGTTGAACACCACCCTCGGCACCACTGCCGCCATTATTCCGCTGAGTATTTGTGCCATGCCGTTTGTGGCGCGTTTAACCGCCAACGCCTTGGTTGAAATTCCAAAAGGCTTAACGGAAGCAGCAAAAGCCATGGGCGCCACCAATTGGCAGATTATCCGTAAATTCTATTTGCCGGAAGCTTTGCCAACACTCATTAACGGCATCACCCTGACGCTGGTCACCCTTGTGGGCTATTCCGCCATGGCAGGTATCGTCGGCGGCGGTGGCTTAGGCAGCCTTGCCATTAACTACGGTGAATATCGCAATATGACCTATGTAAAATGGGTCGCCACCATTATTATTGTGGTATTCGTCATGATTTCACAAAAACTTGGCGATGACTTGGCAAAACGTGTCGATCATCGT","","","24653","MWNDFLTQLTPQMWQTVWVSTYETVYISFASTFLAVIVGLPFGVLTFLTGKGEILQNARLNLILNIVINIGRSIPFIILLIILLPFTRFVLNTTLGTTAAIIPLSICAMPFVARLTANALVEIPKGLTEAAKAMGATNWQIIRKFYLPEALPTLINGITLTLVTLVGYSAMAGIVGGGGLGSLAINYGEYRNMTYVKWVATIIIVVFVMISQKLGDDLAKRVDHR","283492","","D-methionine transport system permease protein (ABC transport system)","Inner membrane, Cytoplasm","","
InterPro
IPR000515
Family
Binding-protein-dependent transport systems inner membrane component
PF00528\"[21-224]TBPD_transp_1
PS50928\"[21-215]TABC_TM1
InterPro
IPR001734
Family
Na+/solute symporter
PS00456\"[157-182]?NA_SOLUT_SYMP_1
noIPR
unintegrated
unintegrated
signalp\"[1-39]?signal-peptide
tmhmm\"[26-48]?\"[63-83]?\"[93-113]?\"[150-184]?\"[190-210]?transmembrane_regions


","BeTs to 12 clades of COG2011COG name: Permease component of an uncharacterized ABC transporterFunctional Class: RThe phylogenetic pattern of COG2011 is ---------d-lb-efghsnuj-it-Number of proteins in this genome belonging to this COG is","Significant hit ( 4.4e-08) to 1/1 blocks of the IPB000515 family, which is described as \"Binding-protein-dependent transport systems inner membrane component\". Interpro entry for IP:IPR000515. IPB000515 129-148 4.5e-08","Residues 189 to 225 match (2e-09) PD:PD382802 which is described as COMPLETE PROTEOME ABC PERMEASE TRANSMEMBRANE TRANSPORTER TRANSPORTER MEMBRANE INTEGRAL PROBABLE ","","","","","","","","","","","","Tue Dec 10 13:33:28 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00416 is paralogously related to AA02352 (6e-16), AA02719 (2e-08), AA01950 (2e-08), AA01525 (2e-07), AA01780 (6e-07), AA02720 (4e-06), AA01644 (2e-05), AA00854 (5e-04), AA01650 (0.001) and AA02897 (0.001).","","","","","","Residues 21 to 224 (E-value = 9.1e-25) place AA00416 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component (PF00528)","","","","","","","","1","","","" "AA00417","283529","284368","840","ATGAACTTGAAAAAATTATTAGGCGTCGCAACATTAGCCTCCGTATTCGCCTTAACGGCTTGTAATGAAGAGAAAAAACCGGAAGCCGCACCGGCAGACAAACCGGCGGCAGAAGCCCCGGCAACAATCAAAGTGGGCGTGATGGCAGGACCGGAACACCAAGTGGCTGAAATCGCAGCGAAAGTGGCAAAAGAAAAATACAACTTAGACGTAGAATACGTTTTATTCAATGACTACGCCTTGCCAAACACTGCAGTGTCTAAAGGTGATTTAGACGTTAACGCAATGCAACATAAACCGTATTTAGACAAAGATTCCCAAGCGAAAGGATTGAACAACTTAGTGATCGTGGGTAATACCTTCGTTTACCCGTTAGCCGGCTATTCAAAAAAAATCAAAAATGTAAATGATTTACAAGACAGCGCTGTAGTTGCAGTACCAAATGATCCGAGTAATCTTGCCCGTGCGTTGATTCTATTGGAAAAACAAGGGTTAATTAAATTAAAAGATCCGACCAACCTGTTCTCCACTTCTATAGATATCATTGAAAATCCGAAAAATTTACAAATCAAAGAAGTGGATACCTCCGTTGCGGCACGTGCCTTAGATGACGTTGATTTGGCGGTAGTGAATAACAACTACGCCGGTCAAGTAGGCTTAAATGCGCAAGATCACGGCGTATTTGTGGAAGATAAAGATTCACCGTATGTAAATATTATCGTGGCACGGACCGATAACAAAGACAGCAAAGCCGTACAGACTTTCGTGAAAGCCTACCAAACCCCGGAAGTGGAACAAGAAGCGAAAAAACACTTTAAAGACGGCGTGGTAAAAGGCTGG","","","30326","MNLKKLLGVATLASVFALTACNEEKKPEAAPADKPAAEAPATIKVGVMAGPEHQVAEIAAKVAKEKYNLDVEYVLFNDYALPNTAVSKGDLDVNAMQHKPYLDKDSQAKGLNNLVIVGNTFVYPLAGYSKKIKNVNDLQDSAVVAVPNDPSNLARALILLEKQGLIKLKDPTNLFSTSIDIIENPKNLQIKEVDTSVAARALDDVDLAVVNNNYAGQVGLNAQDHGVFVEDKDSPYVNIIVARTDNKDSKAVQTFVKAYQTPEVEQEAKKHFKDGVVKGW","284369","","outer membrane lipoprotein precursor (probable D-methionine-binding lipoprotein)","Outer membrane, Periplasm","","
InterPro
IPR004478
Family
Lipoprotein YaeC
TIGR00363\"[12-280]TTIGR00363: lipoprotein, YaeC family
InterPro
IPR004872
Family
NLPA lipoprotein
PF03180\"[43-280]TLipoprotein_9
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[42-184]Tno description
PS51257\"[1-21]TPROKAR_LIPOPROTEIN
signalp\"[1-21]?signal-peptide


","BeTs to 12 clades of COG1464COG name: ABC-type uncharacterized transport systems, periplasmic componentFunctional Class: RThe phylogenetic pattern of COG1464 is ---------d-lb-efghsnuj-it-Number of proteins in this genome belonging to this COG is","","Residues 43 to 277 match (1e-89) PD:PD006353 which is described as LIPOPROTEIN COMPLETE PROTEOME MEMBRANE OUTER PRECURSOR SIGNAL GNA1946 FAMILY PERIPLASMIC ","","","","","","","","","","","","Wed Jan 22 17:44:16 2003","","Mon Mar 15 09:58:58 2004","","Mon Mar 15 09:58:58 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00417 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Mar 15 09:58:58 2004","","","","","Residues 43 to 280 (E-value = 4.9e-133) place AA00417 in the Lipoprotein_9 family which is described as NLPA lipoprotein (PF03180)","Mon Mar 15 09:58:58 2004","","","","Chanyangam,M., Smith,A.L., Moseley,S.L., Kuehn,M. and Jenny,P. Contribution of a 28-kilodalton membrane protein to the virulenceof Haemophilus influenzae Infect. Immun. 59 (2), 600-608 (1991) PubMed: 1987077 ","","Tue Dec 10 13:41:06 2002","1","","","" "AA00419","284477","284971","495","ATGAAAGTCACCAGTTTAGCCATTGAAAACGGGCATTTCGCCGACAAATACGGAAAACGGGGCAGTCAATTCAGCCCAAACGGTATGCCTACCTACTCCATTCCTTTTGAAATCACCGATGCGCCCGCCGACACGAAATCCTTCGCCGTGGTGCTGGAAGACAAAGATGCCATCACGGCTTCAGGCTTTGTCTGGATCCACTGGTTAATTGCCGATTTAGCACGCACTTCCGTGCGGGAAAATGCAAGCCAAACCGCCACGGATTTTGTACAAGGGGCAAACAGCTGGGCAAGCGTGCTAGGCAAATTCGACATTAAAGAAGCCTCCGCCTACGGCGGCATGGCGCCGCCAAATTCCAATCATCGGTATGAACTATATGTGTATGCACTTGATACCAAACTGAACCTACCACAGGGCTTTCGCTTCAATGACTTACATTACGCCATGCAGGGGCATATTTTGGCTGAAGCCTATTTGGTGGGCTGGTATAACGTT","","","19295","MKVTSLAIENGHFADKYGKRGSQFSPNGMPTYSIPFEITDAPADTKSFAVVLEDKDAITASGFVWIHWLIADLARTSVRENASQTATDFVQGANSWASVLGKFDIKEASAYGGMAPPNSNHRYELYVYALDTKLNLPQGFRFNDLHYAMQGHILAEAYLVGWYNV","284972","","conserved hypothetical protein (possible phosphatidylethanolamine-binding protein)","Extracellular, Cytoplasm","","
InterPro
IPR005247
Family
YbhB and YbcL
TIGR00481\"[13-163]TTIGR00481: conserved hypothetical protein T
InterPro
IPR008914
Family
PEBP
PF01161\"[8-165]TPBP
noIPR
unintegrated
unintegrated
G3DSA:3.90.280.10\"[1-163]Tno description


","BeTs to 15 clades of COG1881COG name: Phospholipid-binding proteinFunctional Class: RThe phylogenetic pattern of COG1881 is aompk-yq--r-b-e-ghsnuj-i-wNumber of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Tue Dec 10 13:48:34 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00419 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 165 (E-value = 5e-06) place AA00419 in the PBP family which is described as Phosphatidylethanolamine-binding protein (PF01161)","","","","","","","","1","","","" "AA00420","285093","285566","474","ATGTTAGATATTGTTTTATACGAACCGGAAATTCCGCAAAACACAGGAAATATCATTCGTTTATGCGCCAACACCGGATTTCGGTTACATTTAATCGAGCCCTTGGGCTTCACCTGGGACGACAAGAGACTACGCCGTTCCGGCTTGGATTATCACGAATTCGCGGAAATCAAAAAGCACAAAACGTTTGAAGCATTTTTACAAAGCGAACAACCCAAACGCCTGTTTGCACTCACCACCAAAGGCACACCGGCGCACAGCGAAGTGAAATTCTTACTGGGTGATTATTTACTATTTGGCCCCGAAACCCGTGGCATTCCAATGGACATTTTAAACAGTATGCCGCCGGAACAAAAAATCCGCATCCCCATGACAGCCAACAGTCGCAGCATGAATCTCTCCAACTCCGTTGCCGTCACCGTGTACGAAGCCTGGCGCCAGCTGGGTTATGAGGGCGCGGTGAATATAAACCGA","","","18092","MLDIVLYEPEIPQNTGNIIRLCANTGFRLHLIEPLGFTWDDKRLRRSGLDYHEFAEIKKHKTFEAFLQSEQPKRLFALTTKGTPAHSEVKFLLGDYLLFGPETRGIPMDILNSMPPEQKIRIPMTANSRSMNLSNSVAVTVYEAWRQLGYEGAVNINR","285567","","tRNA/rRNA methyltransferase","Cytoplasm","","
InterPro
IPR001537
Domain
tRNA/rRNA methyltransferase, SpoU
PD001243\"[1-149]TYIBK_HAEIN_P44868;
PF00588\"[1-142]TSpoU_methylase
InterPro
IPR004440
Family
RNA methyltransferase TrmH, group 2
TIGR00185\"[1-154]TrRNA_methyl_2: RNA methyltransferase, TrmH
noIPR
unintegrated
unintegrated
G3DSA:3.40.1280.10\"[1-152]Tno description
PTHR12029\"[2-151]TRNA METHYLTRANSFERASE
PTHR12029:SF11\"[2-151]T23S RRNA METHYLTRANSFERASE


","BeTs to 13 clades of COG0219COG name: Predicted rRNA methylase (SpoU class)Functional Class: JThe phylogenetic pattern of COG0219 is ---------drlbcefghsnuj-i-wNumber of proteins in this genome belonging to this COG is","Significant hit ( 1e-22) to 3/3 blocks of the IPB001537 family, which is described as \"tRNA/rRNA methyltransferase (SpoU)\". Interpro entry for IP:IPR001537. IPB001537A 4-28 2.2e-12 IPB001537B 97-105 0.095 IPB001537C 130-143 3.4e-05","Residues 94 to 151 match (2e-07) PD:PD091729 which is described as F2P16.25 ","","","","","","","","","","","Mon Mar 15 10:01:20 2004","Tue Dec 10 13:51:53 2002","","Wed Apr 13 08:46:02 2005","Wed Apr 13 08:46:02 2005","Mon Mar 15 10:01:20 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00420 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Mar 15 10:01:20 2004","","","","","Residues 1 to 142 (E-value = 9.6e-57) place AA00420 in the SpoU_methylase family which is described as SpoU rRNA Methylase family (PF00588)","Mon Mar 15 10:01:20 2004","","","","Koonin EV, Rudd KE.SpoU protein of Escherichia coli belongs to a new family of putative rRNA methylases.Nucleic Acids Res. 1993 Nov;21(23):5519.PMID: 8265370","","Wed Apr 13 08:46:02 2005","1","","","" "AA00422","286540","285668","873","ATGACCGAACAACGTCCTTATCAATGGCCTGATCCGTTTTTTTTATATCCGGATCAAGGTAAAAAATCTTATCGTATGAAGCGTTTTCGCTATCATTTACGTTCGCTGTTACACTGGCAAACTATTAAAAAATTTGAGCGTTTTGTAAACCAAAATCCGTTGTTGGTGATGTTGCTCAATGCGCGCCCGGGTTTTAGTTACCCCTTGGTTCATCGCTTTTTGGATAAGCGTTTTAACTCACGGCAGCGTTTTGAAGAAATGTGCGCCAACCTGACATTTTTACCGGAAAAACTAACCGCACTTCACCTCCCACCTTTATGGCAACAGCCGATTTGTTTCGGCGAAGTGATTCCCGATTTTGAATTATATTTAACGATAAACGATTATCAGGCGATGGAAGGTTATTGGGCGTTGGAGTTGCGCTATAAGCCGACGCAGGAATTGGTTTATTTGCTGACCTTCGGGCGGGTACAAAAAGCCTTACTGATCGCCGTGATTCAAGGTCCGAACTTTGAAGGTTCAAAGGAAATGGTGAAATCACTGACCAAAAAATGTCACGGTTTACGTCCGGCCTATTTGATGGTGGAAGCCATGAAAGCCTTCACTCATGTTCTGGGCTATACCGCTTTGTGGGGAATTCCGCATAAATATCAAAACAAATCCCGTATCGTGCAAAGCAAACGTTATGTGGTGGATTATGATGCGATTTTTGCCGAATCTGCAGGAACGTTAAAAGAATATTGGGAATTGCCGTTACATTTTGAAACCAAGAATATGAATGATATTCCGAGCAACAAACGCTCGATGTATCGCAAGCGTTACGCCATGTTGGCACAATTGCAGGAAAATATGGCGGAAGCACTGAAAGTGCAG","","","34670","MTEQRPYQWPDPFFLYPDQGKKSYRMKRFRYHLRSLLHWQTIKKFERFVNQNPLLVMLLNARPGFSYPLVHRFLDKRFNSRQRFEEMCANLTFLPEKLTALHLPPLWQQPICFGEVIPDFELYLTINDYQAMEGYWALELRYKPTQELVYLLTFGRVQKALLIAVIQGPNFEGSKEMVKSLTKKCHGLRPAYLMVEAMKAFTHVLGYTALWGIPHKYQNKSRIVQSKRYVVDYDAIFAESAGTLKEYWELPLHFETKNMNDIPSNKRSMYRKRYAMLAQLQENMAEALKVQ","285669","","LapB membrane protein","Cytoplasm","","
InterPro
IPR007488
Family
Protein of unknown function DUF535
PF04393\"[15-288]TDUF535


","BeTs to 5 clades of COG2990COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG2990 is --------------e-gh-nuj----Number of proteins in this genome belonging to this COG is","","Residues 28 to 280 match (3e-15) PD:PD017199 which is described as PROTEOME COMPLETE VIRULENCE VIRK PLASMID LOCALIZATION PROPER SURFACE AT REQUIRED ","","","","","","","","","","","","Tue Feb 4 16:22:57 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00422 is paralogously related to AA02531 (3e-33).","","","","","","Residues 15 to 288 (E-value = 4.1e-130) place AA00422 in the DUF535 family which is described as Protein of unknown function (DUF535) (PF04393)","","","","","Highlander,S.K., Wickersham,E.A., Garza,O. and Weinstock,G.M. Expression of the Pasteurella haemolytica leukotoxin is inhibitedby a locus that encodes an ATP-binding cassette homolog. Infect. Immun. 61(9): 3942-3951.1993. PubMed: 8359916.","","Tue Dec 10 13:55:06 2002","1","","","" "AA00423","286673","287284","612","ATGTCGTATATTAAACTGAATTATCACAAAACCCATTTTTTAACCAGTTCGCCTAATCTGAAAAGTTTGCCGGAAGACACCGGCATTGAAATCGCCTTTGCCGGTCGCTCCAACGCGGGGAAATCCACAGCGCTGAACGCCTTAACCAATCAAAAAAACCTTGCCCGCACCTCTAAAACGCCGGGACGCACCCAGCTCATTAATTTATTTGAAGTGGAACCGCAATGTAAATTGGTGGATTTGCCGGGCTATGGTTATGCCGCCGTACCGGAGCAAATGAAATTGCAATGGCAGCAGGCACTGGGCGAGTACTTACAAAAACGCGAATGCCTTGCCGGTATCGTGATTTTGATGGATATTCGTCATCCGCTTAAAGATTTGGATCAGCAAATGATTGAATGGGCAGTGGCATCTCAATTGCCGGTGTTATTGCTATTAACCAAAGCGGACAAATTAAGCCAAAGCGAACGCAGTAAACAGATGAAAATGGTGCGTGAAGCGATTTTACCGTTCCGGGGCGACATTCAGGTAGAAGCCTTTTCTGCGTTAAAACGAACCGGTATCGATCGTCTGGCGGCAACATTAGACGGGTGGTTTGCACCGGTTTTTGCC","","","27201","MSYIKLNYHKTHFLTSSPNLKSLPEDTGIEIAFAGRSNAGKSTALNALTNQKNLARTSKTPGRTQLINLFEVEPQCKLVDLPGYGYAAVPEQMKLQWQQALGEYLQKRECLAGIVILMDIRHPLKDLDQQMIEWAVASQLPVLLLLTKADKLSQSERSKQMKMVREAILPFRGDIQVEAFSALKRTGIDRLAATLDGWFAPVFA","287285","","GTP-binding protein","Periplasm, Cytoplasm","","
InterPro
IPR002917
Domain
GTP-binding protein, HSR1-related
PF01926\"[29-150]TMMR_HSR1
InterPro
IPR005225
Domain
Small GTP-binding protein domain
TIGR00231\"[26-197]Tsmall_GTP: small GTP-binding protein domain
InterPro
IPR005289
Domain
GTP-binding
TIGR00650\"[34-83]TMG442: GTP-binding conserved hypothetical p
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[3-199]Tno description
PTHR11649\"[23-166]TMSS1/TRME-RELATED GTP-BINDING PROTEIN
PTHR11649:SF13\"[23-166]TGTP-BINDING PROTEIN ENGB-RELATED


","No hits to the COGs database.","Significant hit ( 1.1e-06) to 1/1 blocks of the IPB000765 family, which is described as \"GTP1/OBG family\". Interpro entry for IP:IPR000765. IPB000765 29-72 9.9e-07","Residues 31 to 106 match (7e-17) PD:PD000414 which is described as GTP-BINDING PROTEOME COMPLETE PROBABLE TRNA ENGA REPEAT IRON GTPASE HOMOLOG ","","","","","","","","","","","","Tue Dec 10 13:56:49 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00423 is paralogously related to AA00689 (7e-05).","","","","","","","","","","","Dassain,M., Leroy,A., Colosetti,L., Carole,S. and Bouche,J.P. A new essential gene of the 'minimal genome' affecting cell division Biochimie 81 (8-9), 889-895 (1999) PubMed: 10572302 ","","Tue Dec 10 13:56:49 2002","1","","","" "AA00424","287263","287463","201","GTGGTTTGCACCGGTTTTTGCCTAAAAAAGACGATTTCTGCGATCCCGATCGCAAAAAAGTGCGGTATGAATTTCTTTCATTTCACACTTTTTTTATGTTGTCGCTCCGCATTCCCTGTTCAGTATTACGGAGCCAAACATGTCTTTAGCCATCGTTTACAGCCGCGCATCCATGGGCGTTCAGGCGCCGTTGGTCACCAT","","","7505","VVCTGFCLKKTISAIPIAKKCGMNFFHFTLFLCCRSAFPVQYYGAKHVFSHRLQPRIHGRSGAVGHH","287463","","hypothetical protein","Cytoplasm, Extracellular","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 15:46:35 2004","Sun Feb 22 15:46:35 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00424 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 15:46:35 2004","","","","","","","","","","","","","1","","","" "AA00425","287435","288133","699","ATGGGCGTTCAGGCGCCGTTGGTCACCATTGAAGTGCATTTAAGTAACGGTAAACCCGGTTTCACTCTCGTCGGCTTGCCGGAAAAAACCGTCAAAGAAGCCCAAGATCGGGTGCGTAGCGCCTTACTCAACGCCGAATTCAGATACCCCGCCAAACGCGTTACCGTCAATCTCGCCCCCGCCGATTTACCCAAAGAAGGAGGACGCTTCGATTTGCCCATTGCCATCGGCATGCTTGCCGCTTCCGGTTATATTGATACGGAAAAACTGAAACAATTTGAATTTATCGGCGAGCTTGCCCTCACCGGGCAATTACGCGCAGTGCACGGCGTCATCCCCGCCATTCTGGCGGCAAAACAGGCGAAACGAAAATGCATTGTCGCGCAAGGGAATGCTAATGAAGCTTCACTGGTTTCCGATCAGGAAACTTATTACGCCTATTCTTTATTGGAAGTAGTGCAATTTCTCAATAATCAGGACGAATTACCGCTTGCCGGTGAAATACCACAACAAAGTGCGGTGGATTTTTGCCATGAAAATCCGAAAGATCTCACCGATATTATCGGTCAACAACACGCCAAACGCGCTCTCATGATCGCAGCCGCCGGGCAACACAATCTGTTATTTCTCGGTCCGCCCGGCACCGGGAAAACCATGCTTGCCAGCCGTTTAACCGGATTATTACCGGAAATGACCGAC","","","26288","MGVQAPLVTIEVHLSNGKPGFTLVGLPEKTVKEAQDRVRSALLNAEFRYPAKRVTVNLAPADLPKEGGRFDLPIAIGMLAASGYIDTEKLKQFEFIGELALTGQLRAVHGVIPAILAAKQAKRKCIVAQGNANEASLVSDQETYYAYSLLEVVQFLNNQDELPLAGEIPQQSAVDFCHENPKDLTDIIGQQHAKRALMIAAAGQHNLLFLGPPGTGKTMLASRLTGLLPEMTD","288134","The C-terminal region of competence protein M, comM, is AA00448.From GenBank [gi:9457884]: In Haemophilus Influenzae, ComM is induced during competence developement, but is not needed for DNA uptake. It may be involved in a recombination step. It belongs to the Mg-chelatase subunits D.I family, ComM subfamily.","N-terminal region of competence protein M","Cytoplasm","","
InterPro
IPR000523
Domain
Magnesium chelatase, ChlI subunit
PF01078\"[183-233]TMg_chelatase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[179-232]Tno description
PTHR23073\"[206-224]T26S PROTEASE REGULATORY SUBUNIT
PTHR23073:SF3\"[206-224]TAAA-FAMILY ATPASE


","BeTs to 15 clades of COG0606COG name: Predicted ATPase with chaperone activityFunctional Class: OThe phylogenetic pattern of COG0606 is --m----qvdr--cefghsnuj--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 5.1e-05) to 1/8 blocks of the PR00819 family, which is described as \"CbxX/CfqX superfamily signature\". Prints database entry for PR:PR00819. PR00819B 206-221 5.3e-05","Residues 127 to 168 match (6e-09) PD:PD595695 which is described as PROTEOME COMM COMPLETE COMPETENCE ","","","","","","","","","","","Fri Jan 7 17:09:33 2005","Thu Mar 20 16:55:09 2003","","Fri Jan 7 17:09:33 2005","Fri Jan 7 17:09:33 2005","Fri Jan 7 17:09:33 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA00425 is paralogously related to AA02728 (4e-04).","Fri Jan 7 17:09:33 2005","","","","","Residues 9 to 233 (E-value = 3.7e-15) place AA00425 in the Mg_chelatase family which is described as Magnesium chelatase, subunit ChlI (PF01078)","Fri Jan 7 17:09:33 2005","","","","Gwinn ML, Ramanathan R, Smith HO, Tomb JF.A new transformation-deficient mutant of Haemophilus influenzae Rd with normal DNA uptake.J Bacteriol. 1998 Feb;180(3):746-8.PMID: 9457884","","Fri Jan 31 13:33:51 2003","1","","","" "AA00426","288167","288265","99","TTGGTACAAAACGAACTGAATTTTCATAACTGGAAACAACGTCCTTTCCGTGCGCCCCATCACAGTGCTTCCACGCCGGCATTGGTCGGCGGCGGCTGT","","","3652","LVQNELNFHNWKQRPFRAPHHSASTPALVGGGC","288265","","conserved hypothetical protein","Cytoplasm, Extracellular","This sequence is similar to gi42630075, hypothetical protein Hflu1004401 from Haemophilus influenzae. See also gi16273042, a competence protein from Haemophilus influenzae Rd KW20.","
InterPro
IPR000523
Domain
Magnesium chelatase, ChlI subunit
PF01078\"[1-32]TMg_chelatase


","No hits to the COGs database.","","Residues 1 to 32 match (1e-11) PD:PD586207 which is described as COMPLETE PROTEOME COMM COMPETENCE CHELATASE FAMILY MG2 ORF PROBABLE YIFB ","","","","","","","","","","","","Fri Feb 27 06:59:56 2004","Fri Feb 27 06:59:56 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00426 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 15:49:38 2004","","","","","","","","","","","","","1","","","" "AA00427","288370","290016","1647","ATGTCATATTTCAACGAAAATAAATTAGAGAAAGTTCGCTGGCGTTGTTCGCTTAATTTAGAAAAGTATTTTGAAAAACCTCTTCGCGGTTTTTACAATAAAGAGCATGAGTATGTTGCCACTTGGTATGAAAATCGTCTTTCTCTAGATAAATCTAAAACACTCGTTGAAGTCACTTTTATCAATTTAACCAATCCTACCTATATAAACAAGAAAACAGGTGAAGAATGTCAAAGTTTCTTTCGGATTGCTTTGCCTATCAATTACCTGCATAAAGTTCCATTCGGCAGCATCTGGAAAAACGGTGAATCAGAATGTAAGTTCAAACTTAAAGAGTTTAAAGTTACCTTTTCAAAGAGCAAAGGATTGGCTTATAAGGCGCTTTGGACGGATAAGGAATCACCACATCCATTTGAAGCGGATAAATATGTTCATTCGTCTTATTTGAGAACATTTAAAGGGGACGGAAATCGGTTACTTGTTATTAAGCCTGAAGGTGATAGTAAGTCTTATATCGTTCATCCACTACATTTCTTTATGGCTCACTACGGCTATTCTAGCGAGTTAAAACGTATATTGATTACGGATAACTGGAGCAAGGTTGAGAAGAAGTTACGTCTGAATGAGTTTTTCAAAGAAAAGGGTGTATTCGTACCAAATAACCTTTCCACGAAAGATGCGGTATTTCTTTATCACTTGAAATATGATGCTTATACGAAAAAGGTGGTGAAAAGTGTAATGGCTGACGTTATTCTTTCCAAAGGTAAAGAAAAACCGAATTACCTCATTCCTTGCTGGCACGACAAACCAATCATGCTTTCATTCTATGGTATTGAGTTAGGAAATTCAGTGCTTTGCTGCCAAATTACAGGGATTAGCCAACCACAAGGCGAGCCAATTAACCTTTATTACCATTCTGCAATAAAAACAAATAAAGGTGGTAAAGGACAAAAAGACGGAGAACCTCAATACAGAACGCGAAAACAAGAGCGAGAACATGAACTTGAAAAGCTCGATATTGCATTAGATAACGTGAATAACCTTGTAACGGCTGATGTTATTGAACATCTGAAATTACTTGGTGAAGAGCGAACAATTAACCGTATTCAGCTTGTTCAAGAAGCTGAAAAAGGTGGCAAAGTTAAATTCTTAAATTATGATGAACCAGAAAATTACGGTGTAGGTGAGAAACAAGGGAAAACAGGTAATACAGGTATGGCTAACTGCTTCTATGATATTCCTAGTAATCAAGAAATTGAAGGTAAATCACGCCTCAATACCGTTTGGGAACACGCTAAACGCCTACGCAACGAACAAGGTGCGAAGGTCTATTGGTACACACCTAAACTAGGGTTTAACGAAAGCGATAAGTTTACGTTAGTTTCATTAGACGAAATCCTTGATTCTCTGGAACAATACTATCCAGCCGCAGCGTTAATATTGCGAGTAGATGTGCAACAAAGAACATTTTTTGTACTAAGTTTCCCTGCTCGAAATGAAAAAGAGAACTCAGGTTTTAGTAGTGTTGTTTACGAAACTCAAAATATTCAACAATTCTTGTCAAGCGAAGGTGACGTTTATAGCCGAAATGATAATCTATTTAAGTTATTTATTGAAATCATATCAAGCGGGGGCGTAAATAGCGAT","","","63590","MSYFNENKLEKVRWRCSLNLEKYFEKPLRGFYNKEHEYVATWYENRLSLDKSKTLVEVTFINLTNPTYINKKTGEECQSFFRIALPINYLHKVPFGSIWKNGESECKFKLKEFKVTFSKSKGLAYKALWTDKESPHPFEADKYVHSSYLRTFKGDGNRLLVIKPEGDSKSYIVHPLHFFMAHYGYSSELKRILITDNWSKVEKKLRLNEFFKEKGVFVPNNLSTKDAVFLYHLKYDAYTKKVVKSVMADVILSKGKEKPNYLIPCWHDKPIMLSFYGIELGNSVLCCQITGISQPQGEPINLYYHSAIKTNKGGKGQKDGEPQYRTRKQEREHELEKLDIALDNVNNLVTADVIEHLKLLGEERTINRIQLVQEAEKGGKVKFLNYDEPENYGVGEKQGKTGNTGMANCFYDIPSNQEIEGKSRLNTVWEHAKRLRNEQGAKVYWYTPKLGFNESDKFTLVSLDEILDSLEQYYPAAALILRVDVQQRTFFVLSFPARNEKENSGFSSVVYETQNIQQFLSSEGDVYSRNDNLFKLFIEIISSGGVNSD","290017","","hypothetical protein","Cytoplasm, Outer membrane","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Tue Dec 10 14:07:45 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00427 is paralogously related to AA00017 (5e-71).","","","","","","","","","","","","","","1","","1","" "AA00428","290106","289996","111","ATGATACCGTTCCAAACCCAATTATTATTTGTCTTTTTAGCCTCCTTATGTCTAAATAACGACATTTTCCCGTCTTTAGAATCAACGTTAATCGCTATTTACGCCCCCGCT","","","4098","MIPFQTQLLFVFLASLCLNNDIFPSLESTLIAIYAPA","289996","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 15:51:43 2004","Sun Feb 22 15:51:43 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00428 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 15:51:43 2004","","","","","","","","","","","","","1","","1","" "AA00429","290707","291951","1245","ATGTCAAATAATAAATGTATTACTGTTATTGGTGGTGTATATATTGAGCGGTACGCTTGGCCACATTGGGATGAATTATACGGTTCTGGAGGAAGGGCTCTATCAGTCTTACAGTCCCTAGGCTGTGCTACAAAGCTATATTCTTGTTTAAATAAAGATAGTGCTAACATTTTACAAGCGAGAGCTGGAATCTATAAAACTTCCTTCGAAATATGCTCTTCTTTAAAAGAAAGTTATCGCCCGATAAAATTTCACTATTTACACGGGCTATCCACTCCTCAAATTAGCGCAATAACAACTGAATTTGCTCAACAAAATGAAATTATAGAAGACAATATTCTTGTATTTGGAATGCTTGAAGGTAATCCTACTATTTCTGGGAACAAAGTTGTTTATGACCCTCAAAATCCGATTTCTCCCAAGGACTTCTCTGAAAATGGTTCAACTGCAAACGAACTTGCTATTGTTTTAAATACAAATGAGGCATATAAATTAATAAAAAATAGAAATTTATCCCTAGATGAAATTGCTTATGAATTAATTAAAAACAAGGCTAAAGTAGTCATAATCAAGCAAGGAGTTAGAGGAGTTAATATTTATCAAAAACTAAATGATAGATATATTAAGAAGGATAGTGTTCCTTGTTATTTTACAAAAAACGTATGGAAAATCGGTTCTGGTGATTGTTTCTCTGCCCATTTTGCATATCAATGGATATATGAAGGGAAAACACCTACTGAAGCTGCAGAGTTAGCTTCTAAAGCTACAGCCTATTACTGTGAAACAAGAGGATATCCAAGCTTTGAGGAATTTACTAACTGGAAAAATCGAGTACAACCCATAACACATAGACATTCTGAGAAAAAAGTAACTGTATATTTAGCTGGTCCTTTTTTTACTCTTTCACAGATATGGCTTATTAATGAAACTAGAAGGTTATTGAGTGAGATGGGACTGATAGTATTTTCACCATATCATGAAATTGGAACTGGAGATGCTATAATGGTCGTACCTAAAGATATAGATGGAATAAATAATTCAGATATTATATTTGCCATCTTTGATGGAAAAGATTCTGGGACTATTTTTGAAATAGGATACGCTACAGCAAAGAATAAACCTGTTATTGTCTATAATGAAAATGAAAAATCAGAAGACTTAAAGATGATGGAAGGGACAGATTGTATAGTTATTAAAGACTATGTAAGTGCTATTTACCGCACCCTATGGGAAAGCCAAAAATTA","","","46891","MSNNKCITVIGGVYIERYAWPHWDELYGSGGRALSVLQSLGCATKLYSCLNKDSANILQARAGIYKTSFEICSSLKESYRPIKFHYLHGLSTPQISAITTEFAQQNEIIEDNILVFGMLEGNPTISGNKVVYDPQNPISPKDFSENGSTANELAIVLNTNEAYKLIKNRNLSLDEIAYELIKNKAKVVIIKQGVRGVNIYQKLNDRYIKKDSVPCYFTKNVWKIGSGDCFSAHFAYQWIYEGKTPTEAAELASKATAYYCETRGYPSFEEFTNWKNRVQPITHRHSEKKVTVYLAGPFFTLSQIWLINETRRLLSEMGLIVFSPYHEIGTGDAIMVVPKDIDGINNSDIIFAIFDGKDSGTIFEIGYATAKNKPVIVYNENEKSEDLKMMEGTDCIVIKDYVSAIYRTLWESQKL","291952","","conserved hypothetical protein","Outer membrane, Cytoplasm","","
InterPro
IPR007710
Family
Nucleoside 2-deoxyribosyltransferase
PF05014\"[292-403]TNuc_deoxyrib_tr
noIPR
unintegrated
unintegrated
G3DSA:3.40.1190.20\"[155-264]Tno description
G3DSA:3.40.50.1810\"[283-397]Tno description
PTHR10584\"[172-264]TSUGAR KINASE RELATED
PTHR10584:SF25\"[172-264]T2-KETO-3-DEOXYGLUCONOKINASE


","BeTs to 5 clades of COG0524COG name: Sugar kinases, ribokinase familyFunctional Class: GThe phylogenetic pattern of COG0524 is aompkzy-vdrlbcefghs--j----Number of proteins in this genome belonging to this COG is","","Residues 292 to 395 match (9e-08) PD:PD104029 which is described as PROTEOME COMPLETE BB0426 ","","","","","","","","","","","","Tue Dec 10 14:08:31 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00429 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 292 to 403 (E-value = 1.3e-20) place AA00429 in the Nuc_deoxyrib_tr family which is described as Nucleoside 2-deoxyribosyltransferase (PF05014)","","","","","","","","1","","1","" "AA00430","292570","293250","681","ATGAAAAAATGGACTGATTTAGGCATACCCACTCCCAAAAAAAGCATTATCCCGTATATGCCAATTACTTGGGATGAGGAAACTGCATATTCACTCTATCAATATGTGCAAATTGAAGAAAAAATTGACTTTCAACAAGTAATTCTTAGTAGATGTTCTAATTATACTTTTTCAGAGATACAACTTAGAGATATTGCTAATATTTTATACCTAACCAATATCGTGAAATCTTTATCTAACAGTGAATATGGTTTTTTATTATCCAAAAGGCCTATTCCATCAGCAGGAGCGATACATCCTATTCATATCTTCTTAATATCGCATCTTCACAAAAATTTGTTAAGATTTGACCCTTTTAGCTTTACCCTGAATGCTGTTCAATCAGAAATTAATATAAATACGATAAGAAACGAGGTAAATACCATAGTGGATGTTCAAGATGGAACAATAGTATTACTGGGAGCTGAATACGGGAAAACAGCTGCGAAATATGACAACCCAGATAGTCTAATCTGGAGAGATTCAGGCATCCTACTATGTGGATTACATATGGCTGCTACATACCTAAACATGTCATTCTGCCCCTTAGGAATTACTGGCGAGCCATGGGTAAGCAAACTATCAGAACAATCTAATTTGTTTGGAGTGGGAGTTGCTATTTTCGGTAGAAATACTGTCCCA","","","26411","MKKWTDLGIPTPKKSIIPYMPITWDEETAYSLYQYVQIEEKIDFQQVILSRCSNYTFSEIQLRDIANILYLTNIVKSLSNSEYGFLLSKRPIPSAGAIHPIHIFLISHLHKNLLRFDPFSFTLNAVQSEININTIRNEVNTIVDVQDGTIVLLGAEYGKTAAKYDNPDSLIWRDSGILLCGLHMAATYLNMSFCPLGITGEPWVSKLSEQSNLFGVGVAIFGRNTVP","293251","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Tue Dec 10 14:10:18 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00430 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","1","" "AA00431","294018","293194","825","ATGAAACAAATAGCAGCTGTTTTTTCAGATAGTTCTTGTATGCAGTTATTATCCCTCCCCGCCCCAGAGAATGAGGTTCTTCCAGGTGTAGTTTGGGGGAAAATTGAACAATTTCCTTCTCCAGCCTATTGGTATTACCGAGTATTATCTAACCGAGAATTAAATAACACTCCCAAATACCGGCTGGGAGAATCATTTATTGAAGAAGTATGCGCTTGTCTTTTAGGTGGGTATGGTATACCTGCATATGTTGGTTTGGCTGCGTTTCACTACCTCAAATCTCAGAATGTATTTTCTGATATGCCAACAGATAAAGAAGTTATTTTTAACTTGCTGTCTAAACCATTACAAATTAATGGAAAAAAAGTTAAATATCGTTTTGCAAAACAAAAATCATATTATCTCGCTGAAGCTCTAAAATTTCTGAAAGAAACCAACCCACCATTTGGTAATGGTAAACAATTAAGAAATTGGTTATTACAAATACAAGGAATTGGTTATAAAACGGCGTCTTGGATAGCAAGAAATTGGCTTGATGCTGATGATGTTGCTATCTTAGATGTCCATATATTAAGAGCGGGAAGGATAGCGAAGTTTTTTGATACTAATTTAACAGTTGAAAAAAATTATTTAAAGTTAGAGGAGCAGTTTTTAGAATTTGCCCAAGCACTTGGGGTGCGTACTTCAGAATTGGATGCTACTATTTGGTATGATATGATGCTGACAACAAATATATTTAGAAAAAGAAAGAGTACTCAGGCACTATCATGGGACAGTATTTCTACCGAAAATAGCAACTCCCACTCCAAACAAATTAGATTGTTC","","","31536","MKQIAAVFSDSSCMQLLSLPAPENEVLPGVVWGKIEQFPSPAYWYYRVLSNRELNNTPKYRLGESFIEEVCACLLGGYGIPAYVGLAAFHYLKSQNVFSDMPTDKEVIFNLLSKPLQINGKKVKYRFAKQKSYYLAEALKFLKETNPPFGNGKQLRNWLLQIQGIGYKTASWIARNWLDADDVAILDVHILRAGRIAKFFDTNLTVEKNYLKLEEQFLEFAQALGVRTSELDATIWYDMMLTTNIFRKRKSTQALSWDSISTENSNSHSKQIRLF","293195","","conserved hypothetical protein","Outer membrane, Cytoplasm","","No hits reported.","BeTs to 5 clades of COG1059COG name: Thermostable 8-oxoguanine DNA glycosylaseFunctional Class: LThe phylogenetic pattern of COG1059 is a-mp---qv-----------------Number of proteins in this genome belonging to this COG is","","Residues 59 to 237 match (3e-10) PD:PD022835 which is described as LYASE DNA 8-OXOGUANINE GLYCOSYLASE GLYCOSIDASE HYDROLASE APYRIMIDINIC ENDONUCLEASE PROTEOME N-GLYCOSYLASE/DNA ","","","","","","","","","","","","Tue Dec 10 14:10:54 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00431 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","1","" "AA00432","294693","294037","657","ATGACATATCCAGGTGGAAAAGGTAAATGTTTCCAAAAAATCATTAATTTAATGCCTCCGCATGACGTATATATTGAAACTCATCTTGGTAGTGGTGCAGTACTACGAAATAAAAAACCAGCACTAAAAAATATTGGAATAGATCTAGATTTTGATGTTATTCAATCATGGATTGGTTATTCTCCTGAAAATCATAAGTTTTTTAATAATGATGCATTGGCGTTTCTAACTAAGTACCTGTTTACTGGGAAAGAGTTAGTATATTGTGATCCTCCATATGTTCTTTCAACTAGAAGAAGACAAAAAATATATAAATATGAATACACTGATGAGCAGCATGGGGAGTTATTGGATTTATTATGCAAAATTCCTTGCATGGTTATGATTTCTGGATATGAAAATGAGTTATATGATGAGAAATTATCGCTTTGGAGAAAAGAAAAATTTTTTTCTAAAACTCACAATGGAGTGAGAGAGGAATGTGTGTGGCTTAATTTCCCCCCTGCTGACAAACTACATGATGCTTCTTTTTTAGGAGCTAATTTTCGAGAAAGATATACTATCAAAAAACGCCTTAATCGTTTGATTCAAAAATTTGAGTTAATGGATCCGATTGAGCGAGATTATATTTTGGAAATACTTAATAAAAAATATATC","","","26461","MTYPGGKGKCFQKIINLMPPHDVYIETHLGSGAVLRNKKPALKNIGIDLDFDVIQSWIGYSPENHKFFNNDALAFLTKYLFTGKELVYCDPPYVLSTRRRQKIYKYEYTDEQHGELLDLLCKIPCMVMISGYENELYDEKLSLWRKEKFFSKTHNGVREECVWLNFPPADKLHDASFLGANFRERYTIKKRLNRLIQKFELMDPIERDYILEILNKKYI","294038","From GenBank [gi:19352339]:The nearest neighbor, upf31.0 is from uncultured bacteria plasmid B4 ","conserved hypothetical protein; possible methyltransferase","Cytoplasm","","
InterPro
IPR002052
Domain
N-6 Adenine-specific DNA methylase
PS00092\"[87-93]?N6_MTASE
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[1-168]Tno description


","No hits to the COGs database.","Significant hit ( 1.9e-07) to 3/4 blocks of the PR00505 family, which is described as \"D12 class N6 adenine-specific DNA methyltransferase signature\". Prints database entry for PR:PR00505. PR00505A 3-19 0.41 PR00505B 24-38 17 PR00505D 84-96 0.009","Residues 86 to 168 match (2e-11) PD:PD357763 which is described as PROTEOME METHYLTRANSFERASE COMPLETE TRANSFERASE LMO2316 METHYLASE LIN0088 ","","","","","","","","","","","Thu Mar 20 09:43:58 2003","Thu Mar 20 09:45:10 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00432 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Tauch A, Schlüter A, Bischoff N, Goesmann A, Meyer F, Pühler A.The 79,370-bp conjugative plasmid pB4 consists of an IncP-1beta backbone loaded with a chromate resistance transposon, the strA- strB streptomycin resistance gene pair, the oxacillinase gene bla(NPS-1), and a tripartite antibiotic efflux system of the resistance-nodulation-division family.Mol Genet Genomics. 2003 Feb;268(5):570-84.PMID: 12589432Thorsted PB, Shah DS, Macartney D, Kostelidou K, Thomas CM.Conservation of the genetic switch between replication and transfer genes of IncP plasmids but divergence of the replication functions which are major host-range determinants.Plasmid. 1996 Sep;36(2):95-111.PMID: 8954881","","Thu Mar 20 09:43:58 2003","1","","1","" "AA00434","294965","300937","5973","ATGACATTACGCTCGGATTCCAAAACACTTGTTGCCTCATCAGGAAGCACCAAAAGTGCGGTTGAAAAAACAGCTAAATCCTCTTCCGGCATTTCCATTCCTACGCTTAATGATGTTGCCTCCCTTGCCGGTAAAATCAAGCCGGTGGCGGCAATTACCGGTGATAAGAAACTGACAAAACGAGCGGCACGGGTTCAGGAACGGGTGGCTCAGGTACAACAGGGTGTGGCGATTGGCAAAGAGGTGATTCAACGGGTTCAACAATGGGGCAAAAAGCCGCCACTCGTCGGTATCGGCGGTGAAGTCGGTGGTACACCGTCCGTTCAGGATGCCTTATCAGCTTTACTTGGGCGTTCTCCAAGCGGTCTGCAATTCACTTTTCACTCGGCGGGCGTATCGTCTGACAGCTTTGAAGTATTAGGTTTTGATTTATGGGATGGTTACAGCGAGCCTTTTACGCTACATCTTGAACTCAGCAGTAAGAATGATGCCATTCCCTTTGTCGCCGTGTTGGACAATGAGGCTTATCTCACGTTCTGGCAAGATGGCGAACAGGTAAGACGCCTCACCGGTATTGTCAACCAATTTGAACAAGGTGACAGCGGTTTTCATAACACCTTCTATCGTTTGCAACTGCGCCCTACCCTTTGGCGTTTGGGACTGCGTTCAAATTCCCGCATCTTCCAACAAAAAGACCTGCAAACCATTCTCGCTACCCTGCTTGATGAAAATAAAGTCACCGACTATCGCTTTATGCTATGTGACTCCCACCCCGAGCGCGAGTTCTGTGTGCAATACCGTGAAACCGACTTAGCCTTCTTTGAACGCTTGGCGGCGGAAGAAGGGCTGTTCTATTACTTTGATGAACAAAGCCGGTTGGTTATCAGTGATGATGCCTCCACATTAAACAACGAAAAAGCCATCACCTTAAACTACAACCCCAATAAAAACGCCCAACTACAAGAAAACACGCTTAGTCGCTTTGCCCACAGTGAACGGGTGCGGGTGTCTCAGGCGGTGTTAAAAGACTACACCTTTAAAAAGCCTCTGTGGGAAGCCACTTTCACGGAAGAAGCCAAAGACCTTGAGGCGCAACGTGCCATGTATGAGCATTATGACTTTCCGGGGCGCTTTAAAGACGGACGGGGTAAACAATATAGCCGTTATCGGTTGGAGAGCTTACGTCGTGATGCCCATAGCGGACGCGGGGAGAGTAACAGTCCGTTGTTAATGGCGGGTGGTTTAATTAACTTACAGAGTCATCCTAATGCCGCCTTTAATACCTTATGGCAATTAAGCCAGGTGCACTATCATGCCGAACAGGCGCAGGGGGCTCAGGGGGAAGCCGGTGAACGCGGCACCCATTTAACCGCCGCCTTTGAATGCTTACCACGCCACCAGACCTGGCGTCCCTTACAACGCACCAAGCCGTTGGTAGAAGGACCGCAGCCGGCTATTGTGACCGGTCCGAAGGGGGAGGAGATTTATACCGATAACTTTGGACGGGTGCGGTTACAATTCTTATGGGACAGGGAAGGCAAGTATGATGACCACAGTTCTTGTTGGGTGCGGGTAACCCAACCTTGGGCGGGTAAAGGCTGGGGGATGGTGGCGATTCCTCGGGTCGGTCATGAGGTGATGGTAGACTTTTTAGAAGGCGACCCCGACCAGCCGATAGTCACCGGGCGAACCTACCATGCGAATATGCCGTTGCCGGCCAAATTACCACAAAACAAAACCCAGATGCATCTGATGTCACAGACCTATAAGGGCGGTGGTTATAATGGGATGATGATGGAAGATGAGCAGGGTAAACAACGCTTGGACTTCCAGGCTCAGCGGGATATGAATACCTTAGTGCTCAATGACCGTGCCACTAATGTGGGCGGGAATCACAAAGAAACCGTCAAAGGCGAACAGAAAGTTAGTGTCGGCAAAGCCCGTTATAAAGAAGTGGCGGGAGAGGAAACCCAAACCATTGACGAGGCGCAAATCATTACTGTAGGCAAGGATTATCAGTTAATCGCCAATAACGGTCCGGTGTCAATGACATCCAAGGCGGATAATGTGATATTTGAGACCGCCGGTGCACGTCTTACCCTATTTAAGAACGGGAATATTCAACTGGAAGGGAAGTCGGTGTGTATTAATGGTAAGCTCATTGACTTGAATCCGGGTGGGGCGGCGACATCGAGTGCTGAAGCTGATTCTGCGCCGGCTTCGGATGACGGTGGCGACGGAGGTGCTCGTGGCGGTGGTGCTGGTGGCGGTTCTGGAGGTGGCGGTGGTGGCGCTTCTGGTGGTAACGATTCTAGTGGTGCTGAGACTGAGAATTCTGACAATAACACAGATGATAGTGGCTTTAACGGAGGAGTTGGAGCTTTTGCTGGAGCCGGAGCAAATGGTTCGGCCAATACAAACGAATCCATTCCTTGTAAAGCAGCTACCGCAGTGGGTCGACCGGTCAACCCTATTCTTGGATTAAAATTACTTACTAATGAAGTGGATTTCGCCTTTGCGGGATTAATGCCATTAGTTTGGTCTCGTAGTTATTATTCCGACCAAATGGGCACAGGTTGGCTAGGACAAGGTTGGTCAGTACCGGGCTGTCAGCGTATTGAACGACAAACACGCGGCTTGGTTTATATTGATGAACAAGGTCGCGAACTGTTACTTCCTGCACTAACCGCAGGAAGCCAAGAAATTTATCATCAGGCTGAACAAATTTGGATTCAATACAATGAATCAGGCGAAATTATTATCGCCTCTTTAGATAAACGTCTATCTCTTGTATTCCGTTCATTATCCGAAACATATCAAGCTTATGTATTATCCGCAATTCAAGATGCCTTCGGTAATCAACAGCGCTTTGATTATGATACTCAAACGGGACTACTCCAAAAGGTTACTGACGGTAACGGACGAGAATTTTATTTTGCATTTGAAAATCTCACTCAAGACAAAACTGACACGAGTCCACTATGGCGTTTAGTCTCTATTGAGCATCAAAAAGACCAGCAACGAATCCCATTGGTACATTATCGCTATAATACAGAAGGCGATTTGGTTGAAGTATTAGACTCACAAAAGACCATTGTCCGTACATTCGGTTATCATAACCATATCATGGTGTCACACCGTAATGCGTCAGGTTTAGAATCTTACTATAAATATGATGTATACGGCCCTAAAGGCAAAGTTTTACGCAATACAACCAACTTGGATGAAAGCTGGCAGTTTGAATATCATCCGACTTATACACAAATCACTGACAGCCTGGGGCGGATTGAACAGTATCATTTTGACAATAACCAAGAAATCGTGAAACGAGTGTTTGCTGACGGCTCCCAAGCTATCATGGAAAGAGATAATCTCGGACGCTTATTAAGTCAAACCGATAGTGCTGGCAAAACAACAAGCTATGTCTACAATGAACAGGGACAAGTGATAAAAATCACACGCCCAGACCAATTGGCACAGCAATATCAATACGATAATAACGGTCGCTTAGTTGCCCAAACAGATGTCATGGGCAATCAAAGTCATTATGTCTATGATAGTATCGGGAACCTCACTATAGCAACCAATGCGTTAGGTGAGAGCGTCAAGTTCGAATATAGCAATAAGGGCTTACGCACAGCCATGATTGACCCATTAGGCAACCGTACCACCTTTAACTATAACGCCGACAATCAGTTAGCAAGCCGTGTTGACTGCTCCGGCAATATAACTCAATTGGAATACAACGATGATGGTTTACTCACCACCGTCATTGACGCATTGGGTCAAAAAACACACTACATCTATAACAATAATCATCAGCTCATTCAAACAACCTATGCAGACGGTAGCCAAGAACAGTTTACTTATGATACCGCAGGACGTTTAATCACCTATACCGACGGCAAAGGTAACCAAACCGAATATGAGTATAGCGTCGATGATTTACCGGTTAGCCGTAAAAATGCCTTGGGTCACACGTTTGCTTACACCTACGACAACGCCAGACGCTTAGTTCAACTCACCAATGAAAACCTTGTCACCTATCGCTTCGATTATGACCCGATGAACCGTTTAACCGCCGAAATCGGCTTTGACAACCGCAAAACCGTTTATCATTACAACGAAAAAGGTGAACTGGCCACCCAACAGGAATTCGGTACGGATAACCATAAACAGGTGTTGCGTACCACCGAATTTAAACGAGATAAACTGGGTCGAGTCATTGCCGAACAGATTCAACAGTTTGACGGTCAAACCCAACAAACGAGCTATCACTATGACCAACTCGGCAGACTAAGTCAGTTAGAGGATGAGCAAACGACAATACACTTTACTTACGACAATGTAGGCAGAGTCATTGAACATCATTTATCAGATAAAAACGACCACAGCCAAGTGATGCGTTATACCTATGACGCTAACGGCAACCGATTGAAAACCAAATTGCCGAATGGTGAACAGATTGATTATCACTACTATGGTAGCGGGCACTTATCCACAATCAAATTCAACGACCGCTTAATCAGCGACATCACCCGAGATAAACTGCACCGTGAAGTCTCGCGTACACAAGGCAAACTGGTCAAATTGGACGCTATCGGCAGATTAGAAGAACAGTTAGCGACGCTGGAGCAGCAAACAACCCAACAAGCCCTTGTCAATCGAACTTATCGTTATAACGAGGTGGGCAACCTAATACAAAGCCGTGATTTACGCATGGGCAATCAGGATTACTATTACGACAAACTCGGTCAACTGACCATGACCGGCAATGAAGTCTTCGCCTTTGACCCGGCGCATAACCTGATTGAGCGGGAAAGCGAGAAACATCTAAACAACCAACTACACGAATACCAAGGCATCACTTATTACTATGACGAGTTTGGCAACTTAAGCCAACGTAAACGCAATAACGGTGAAGTACAAACCTATTCCTACAATGCTAAAGACCGGCTGATTAAAGCGGTGATTCAAAGACCGAATCAAAAGGCGGAAACCTGGCATTATCAATACGATGTGCTTGGCAGACGAATGATAAAAGTGCGGTCGGAAAACGGCGCGTTTCTAGCACACACAATGACTGAATTTATGTGGGATGGTAGCCATCTGGTGCAAGAAATCAATCGTGAAAATGACCGCACTTTCAGCTATATTTACCGCAGCCCACAAAGCTACGAGCCGTTGGCGCAGGTGTGCACGGACAACAAACAAAACCATACACAAACGCGCTACTTCCATTGCGACCAGATTGGTGTGCCACGGGAATTAACGGATGAGAACGGCAATCTTTGTTGGTATGGTGATTACCTCGGCTGGGGCAAACTACGTAACAGCCACAACCTCATGGCGAACGTACATCAACCGTTCCGCCTACAAAACCAGTATGCTGATGAAGAAACCAGCTTACATTACAACTTCTTCCGCTACTATGACCCGTATATTGGGCGTTTTACACAGCAGGATCCGATTGGGCTTGCCGGAGGGAATAACCTATATAGGTTTGAGGGCGCGGTACAGAATCAAACCGATCCACTGGGATTATTTGCACCAGTACTTGCGGCACCTTGGATTTTGGAAGGATTAGCCTATGCCGGTACAGCTATGGCGGGCATTCTTATTGGCGTAGGTATAATGGATGCTAAGGAAGAGTATGATAAGGCTCAGGCTCAATCTGCCGCAGAAATTGAAGCGTCTAAATGTGAAAAAGAACGCAAAAGACGTTGTAAGAAGTGGGGGACTGGAACACCAGCTCAGGCTAGAAATATAGTTAATATTAATCGTAGAGGACCTAAGGGGATAAAAAGAATTGATAGACCTGAAGAATCAGTTCCTGGCTCCCAATATCATGCCCATGCTTACAATGATGCAGCACTTAATGTAGATGGAACGGTACATGATAAACATCGTGGAATGCCACCATTCTCTAAAGATGATAAAGATTTTCTATTTTGTTACGGCTGGAAAGGAGTA","","","224387","MTLRSDSKTLVASSGSTKSAVEKTAKSSSGISIPTLNDVASLAGKIKPVAAITGDKKLTKRAARVQERVAQVQQGVAIGKEVIQRVQQWGKKPPLVGIGGEVGGTPSVQDALSALLGRSPSGLQFTFHSAGVSSDSFEVLGFDLWDGYSEPFTLHLELSSKNDAIPFVAVLDNEAYLTFWQDGEQVRRLTGIVNQFEQGDSGFHNTFYRLQLRPTLWRLGLRSNSRIFQQKDLQTILATLLDENKVTDYRFMLCDSHPEREFCVQYRETDLAFFERLAAEEGLFYYFDEQSRLVISDDASTLNNEKAITLNYNPNKNAQLQENTLSRFAHSERVRVSQAVLKDYTFKKPLWEATFTEEAKDLEAQRAMYEHYDFPGRFKDGRGKQYSRYRLESLRRDAHSGRGESNSPLLMAGGLINLQSHPNAAFNTLWQLSQVHYHAEQAQGAQGEAGERGTHLTAAFECLPRHQTWRPLQRTKPLVEGPQPAIVTGPKGEEIYTDNFGRVRLQFLWDREGKYDDHSSCWVRVTQPWAGKGWGMVAIPRVGHEVMVDFLEGDPDQPIVTGRTYHANMPLPAKLPQNKTQMHLMSQTYKGGGYNGMMMEDEQGKQRLDFQAQRDMNTLVLNDRATNVGGNHKETVKGEQKVSVGKARYKEVAGEETQTIDEAQIITVGKDYQLIANNGPVSMTSKADNVIFETAGARLTLFKNGNIQLEGKSVCINGKLIDLNPGGAATSSAEADSAPASDDGGDGGARGGGAGGGSGGGGGGASGGNDSSGAETENSDNNTDDSGFNGGVGAFAGAGANGSANTNESIPCKAATAVGRPVNPILGLKLLTNEVDFAFAGLMPLVWSRSYYSDQMGTGWLGQGWSVPGCQRIERQTRGLVYIDEQGRELLLPALTAGSQEIYHQAEQIWIQYNESGEIIIASLDKRLSLVFRSLSETYQAYVLSAIQDAFGNQQRFDYDTQTGLLQKVTDGNGREFYFAFENLTQDKTDTSPLWRLVSIEHQKDQQRIPLVHYRYNTEGDLVEVLDSQKTIVRTFGYHNHIMVSHRNASGLESYYKYDVYGPKGKVLRNTTNLDESWQFEYHPTYTQITDSLGRIEQYHFDNNQEIVKRVFADGSQAIMERDNLGRLLSQTDSAGKTTSYVYNEQGQVIKITRPDQLAQQYQYDNNGRLVAQTDVMGNQSHYVYDSIGNLTIATNALGESVKFEYSNKGLRTAMIDPLGNRTTFNYNADNQLASRVDCSGNITQLEYNDDGLLTTVIDALGQKTHYIYNNNHQLIQTTYADGSQEQFTYDTAGRLITYTDGKGNQTEYEYSVDDLPVSRKNALGHTFAYTYDNARRLVQLTNENLVTYRFDYDPMNRLTAEIGFDNRKTVYHYNEKGELATQQEFGTDNHKQVLRTTEFKRDKLGRVIAEQIQQFDGQTQQTSYHYDQLGRLSQLEDEQTTIHFTYDNVGRVIEHHLSDKNDHSQVMRYTYDANGNRLKTKLPNGEQIDYHYYGSGHLSTIKFNDRLISDITRDKLHREVSRTQGKLVKLDAIGRLEEQLATLEQQTTQQALVNRTYRYNEVGNLIQSRDLRMGNQDYYYDKLGQLTMTGNEVFAFDPAHNLIERESEKHLNNQLHEYQGITYYYDEFGNLSQRKRNNGEVQTYSYNAKDRLIKAVIQRPNQKAETWHYQYDVLGRRMIKVRSENGAFLAHTMTEFMWDGSHLVQEINRENDRTFSYIYRSPQSYEPLAQVCTDNKQNHTQTRYFHCDQIGVPRELTDENGNLCWYGDYLGWGKLRNSHNLMANVHQPFRLQNQYADEETSLHYNFFRYYDPYIGRFTQQDPIGLAGGNNLYRFEGAVQNQTDPLGLFAPVLAAPWILEGLAYAGTAMAGILIGVGIMDAKEEYDKAQAQSAAEIEASKCEKERKRRCKKWGTGTPAQARNIVNINRRGPKGIKRIDRPEESVPGSQYHAHAYNDAALNVDGTVHDKHRGMPPFSKDDKDFLFCYGWKGV","300938","In E.coli, \"vgr, encodes a large protein distinguished by 18 to 19 repetitions of a Val-Gly dipeptide occurring with a eight-residueperiodicity.\" (Wang et al., 1998).","VgrG-like protein (Rhs accessory genetic element)","Extracellular, Outer membrane","","
InterPro
IPR001826
Family
RHS protein
PF03527\"[1743-1780]TRHS
InterPro
IPR006530
Repeat
YD repeat
PF05593\"[1016-1053]T\"[1122-1159]T\"[1164-1201]T\"[1206-1243]T\"[1248-1285]T\"[1290-1327]T\"[1353-1394]T\"[1402-1441]T\"[1472-1503]T\"[1560-1593]T\"[1626-1663]TRHS_repeat
TIGR01643\"[1101-1142]T\"[1143-1184]T\"[1185-1226]T\"[1227-1268]T\"[1269-1310]T\"[1311-1352]T\"[1353-1394]T\"[1427-1467]T\"[1472-1513]T\"[1626-1667]TYD_repeat_2x: YD repeat (two copies)
InterPro
IPR006533
Family
Rhs element Vgr protein
PF04524\"[482-560]TDUF586
TIGR01646\"[137-615]Tvgr_GE: Rhs element Vgr protein


","No hits to the COGs database.","Significant hit ( 1.2e-13) to 3/5 blocks of the PR00394 family, which is described as \"RHS protein signature\". Prints database entry for PR:PR00394. PR00394C 1768-1783 1.4e+02 PR00394D 1793-1813 6.4e-05 PR00394E 1816-1835 1.8e-06","Residues 1051 to 1155 match (8e-08) PD:PD003925 which is described as COMPLETE PROTEOME PLASMID RHS-RELATED CORE TRANSMEMBRANE EXTENSION RHS WITH REPEAT ","","","","","Wed Feb 19 14:43:44 2003","","","","Wed Feb 19 14:43:59 2003","","Wed Mar 19 17:46:30 2003","Tue Dec 10 16:01:04 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00434 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1290 to 1327 (E-value = 5.7e-05) place AA00434 in the RHS_repeat family which is described as RHS Repeat (PF05593)","","","","","Wang,Y.D., Zhao,S. and Hill,C.W.Rhs elements comprise three subfamilies which diverged prior toacquisition by Escherichia coliJ. Bacteriol. 180 (16), 4102-4110 (1998)PubMed: 9696756","","Wed Feb 19 06:50:09 2003","1","","1","" "AA00435","300944","301456","513","ATGCAGGGCTTAACATTATTAAATAAATTAGCAAAACTTGAAAAATCTTATCAAGAAAAGAATATTATAGATTTTTTAAAATATCCTGTTGAATTTGAGGAAATACCAATTATTACCCAAAAGGGAAGAGAAGATATTTTTCTAGAGACTTTCTCTAAAAAGGATTTTGATGTTTTCTTTTTAAATGTGGCTTTGTTTTATCTTAATAATATCAAGCTGATGGCGAGAAAGGTGTTAAGTGAGGAAGAAAGGAAAGATCTTTTTTTCTGTATAACATATCCTGATTTAGAATTATCTGACTTATATGGTTTTAACATACCAAATATATGTATTTCAAAAACAAAATATAAAGAAAAATTTGAGGAAAAACCGCAAGTAAATTTAGATCAGATGTTATGGCTAAAAAATTCCTTAGAACAACTTGGATATATCGATACATTTAAGATTGTTTATTCTAAATCTGATGATGGTTTTGGTGGTGAATTCTTTAGAGTATTTTTATTAAATAAAGAA","","","20324","MQGLTLLNKLAKLEKSYQEKNIIDFLKYPVEFEEIPIITQKGREDIFLETFSKKDFDVFFLNVALFYLNNIKLMARKVLSEEERKDLFFCITYPDLELSDLYGFNIPNICISKTKYKEKFEEKPQVNLDQMLWLKNSLEQLGYIDTFKIVYSKSDDGFGGEFFRVFLLNKE","301457","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Dec 11 12:13:46 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00435 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","1","" "AA00436","301878","302159","282","ATGAAACATGCTACCCATAAAAATATAATTCTTAGTGATCTTGTTTATTGGAAAAACTCGTCTCCTTTAGATAAAGGTATCGTGGTTTGTTTGATCGATGAAGGCGTATTTTTAGATGGATACGACTTTTCTTGCTTAAAAGACTCAGGAGGTGGGATAATGATGTTGTTTGATTCTACAGGACTTGTTCAAATCATGGGGGATGATAAAAATATAGATATTGAATTTATTTCTCACTTAACGACTTCAGAGATTAATAATTTTTTGAAGAGTATTTTTTCT","","","10445","MKHATHKNIILSDLVYWKNSSPLDKGIVVCLIDEGVFLDGYDFSCLKDSGGGIMMLFDSTGLVQIMGDDKNIDIEFISHLTTSEINNFLKSIFS","302159","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 15:53:23 2004","Sun Feb 22 15:53:23 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00436 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 15:53:23 2004","","","","","","","","","","","","","1","","1","" "AA00437","303135","302284","852","ATGCCTAAAAATATTACTTACGCTTTTCATAATGAATTAGTGATGTTACCACTCGATGTTATTATTTCTTCTCACCCTATAGATAATAAACTTGAGAAAAGTGTTAAGTTTCAGAGTATTTTTTCTTCTATTCAGGAAATTGGTATTATTGAGCCACTTGTTGTTTATCCTGACAACGGACAGTACCTATTACTTGATGGACATTCTCGACTTCATGCATTAAAAATGTTAGGTATGACGGAAACATTATGTATGCTTGCTACTGATGATGAAGGTTTCACCTATAACAAGCAAATTAATCGACTTACCGCGATTCAAGAACATAATATGATAATGAAAGCTATTGAGCGTGGTGTATCTGATGAAGCAATTTCAAGAACACTTAATATAGATATAAAAATTCTTCGTCAGAAAATGGCAATGTTGAAAGGGATTACTCAAGAAGTCTCCGAGAAGCTTGCTAATAAACCCGTTGGTAAAGAAATTTTCCGAATTTTACGAAAAATGAAACCAGAACGGCAAATTGAGGTAGCTGATATGATGTTAGCTAGTAATAAATTTACTGTAACGTATGCTAATATGATGTTACTCAGCTCTCGTAAAGAAGAATTGGTTGAATCACACAAGCCTAAAGCTACATCAGAACTTGCTGACATAGCCATTATGCAGAAGGAAATGGAGCGCCTAAAGGAAAACTATAAAATTTCTGAGGAAAAATTAGCTGATCTAAAACTTAGTCTAATTGTAGCCAAAGGCTATGTAAACAGACTTCTTAACAATGTCGTTATCTCAGAATTTCTTGAGAATGATAAGAATGATATTTATCTTGCTCTGAAAGAAGTTTGTGAGAAA","","","32518","MPKNITYAFHNELVMLPLDVIISSHPIDNKLEKSVKFQSIFSSIQEIGIIEPLVVYPDNGQYLLLDGHSRLHALKMLGMTETLCMLATDDEGFTYNKQINRLTAIQEHNMIMKAIERGVSDEAISRTLNIDIKILRQKMAMLKGITQEVSEKLANKPVGKEIFRILRKMKPERQIEVADMMLASNKFTVTYANMMLLSSRKEELVESHKPKATSELADIAIMQKEMERLKENYKISEEKLADLKLSLIVAKGYVNRLLNNVVISEFLENDKNDIYLALKEVCEK","302285","","conserved hypothetical protein; possible parB-like nuclease","Cytoplasm","","
InterPro
IPR003115
Domain
ParB-like nuclease
PF02195\"[14-81]TParBc
SM00470\"[14-105]TParB
InterPro
IPR011111
Domain
RepB plasmid partition
PF07506\"[98-270]TRepB
InterPro
IPR013253
Family
Kinetochore Spc7
SM00787\"[12-275]Tno description


","No hits to the COGs database.","","Residues 144 to 267 match (6e-08) PD:PD416533 which is described as PROTEOME COMPLETE MLL8115 MSR9757 PLASMID ","","","","","","","","","","","Wed Mar 19 16:27:14 2003","Wed Mar 19 16:36:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00437 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 14 to 105 (E-value = 1.2e-06) place AA00437 in the ParBc family which is described as ParB-like nuclease domain (PF02195)","","","","","","","","1","","1","" "AA00438","303976","303131","846","ATGGATATTCAAACTATTCCGATAGAAGATATTCGGATTATCAATCCAAGAACGCGTAATCGAAAAATCTTCGCAGATCTTGTAGAAAATATTGCGTCTGTTGGTTTAAAACGACCAATTACAGTCTCAAAGACGTCTGATGGTTATAACTTACTATGTGGTCAGGGGCGTTTAGAAGCCTGCAAACATCTGGGCGAAAAAGTTATTCCCTGTCGAGTTATTGAAGTGAGTCAAGAAGAAAGTTATCTCATTAGTCTGGCAGAAAATATTGCAAGGCGCAAACATACTAATATGGAATTACTTTCTGGAATTCGTATTTTAAGTGAACGTGGGTATCGAACATCTGACATAGCAAGGAAAGTTGGCTTTGATACGACTTATATAAGCGGAATTATTCATCTTCTTAAGGTAGGTGAAGAAAGATTGATTAATGGCGTAGAAAAAGGTTACTTGCCTATTACTGTGGCTATCTCTATTGCACGAGCGGATGATAAGGAGACTCAGAAACAACTTACGGAATTATATGAAAACGGTACATTAAAGCAGTCAGATATTACGAAAATTCGTAATATTATGCATCGTCGGAAATTAATAGGTAAAAGAGCAAATACTGCTATAAAAAACTCAGTTTATAGCCAGAAAAGTATCATAAATATTTATAAAGAGGAGACTGACCGACAACAGAGAATGATTAAGCAAGCTGAGTTCGATGAAAGCCAATTATTTGTCTTAATTTCCTGTCTTAAAAAGTTATTTAATGATAAGGTTTTTCTGCTTCTCCTGAAATCTGAAAAACTTAATGATATACCAAAAGATTTGAGTGAGCGTTTAAGGGGGAACTATGCC","","","32275","MDIQTIPIEDIRIINPRTRNRKIFADLVENIASVGLKRPITVSKTSDGYNLLCGQGRLEACKHLGEKVIPCRVIEVSQEESYLISLAENIARRKHTNMELLSGIRILSERGYRTSDIARKVGFDTTYISGIIHLLKVGEERLINGVEKGYLPITVAISIARADDKETQKQLTELYENGTLKQSDITKIRNIMHRRKLIGKRANTAIKNSVYSQKSIINIYKEETDRQQRMIKQAEFDESQLFVLISCLKKLFNDKVFLLLLKSEKLNDIPKDLSERLRGNYA","303132","","probable chromosomal partitioning protein (ParB-like family)","Cytoplasm","","
InterPro
IPR003115
Domain
ParB-like nuclease
PF02195\"[4-90]TParBc
SM00470\"[4-90]TParB
InterPro
IPR011111
Domain
RepB plasmid partition
PF07506\"[91-257]TRepB


","BeTs to 13 clades of COG1475COG name: Predicted transcriptional regulatorsFunctional Class: KThe phylogenetic pattern of COG1475 is aom-kz-q-drlb-efg-snujxit-Number of proteins in this genome belonging to this COG is","","Residues 120 to 277 match (4e-25) PD:PD545486 which is described as PROTEOME PARTITIONING PLASMID COMPLETE ","","","","","","","","","","","","Wed Feb 19 15:46:42 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00438 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 90 (E-value = 3.3e-16) place AA00438 in the ParBc family which is described as ParB-like nuclease domain (PF02195)","","","","","Lee PS, Lin DC, Moriya S, Grossman AD.Effects of the Chromosome Partitioning Protein Spo0J (ParB) on oriC Positioning and Replication Initiation in Bacillus subtilis.J Bacteriol. 2003 Feb;185(4):1326-37.PMID: 12562803Hao JJ, Yarmolinsky M.Effects of the P1 plasmid centromere on expression of P1 partition genes.J Bacteriol. 2002 Sep;184(17):4857-67.PMID: 12169611","","Wed Feb 19 15:46:42 2003","1","","1","" "AA00439","305498","303921","1578","ATGGAATATAAAAATCTTGCTGTTGCTTATATCCGTATGTCTACGGAGCATCAGGAATTTTCACCGGATATACAACGTCGCTTCATTCAAAAATATGCTAAGGAACAAGGGCTTATACTCACTAGGGAATACCTAGATGAGGGAAGGAGTGGATTAAGCGCAGAAAAACGTCCTCAGTTTTTATCACTCATTAATTTTGTACAATCCGGTAATGCTGATTTTTCACATATTCTTGTTTATGACATTAGCCGATGGGGGCGCTTTCTAAATATTGATGAATCTGCACATTATGAACAAATTTGTTCAAAAATGGGGATTAAAGTGCATTACTGTGCAGAACCTTTTAAGGGAAACGACATTGGTTCTCAAATTTTTAAAGCGGTAAAACGTTGGTCTGCCGGAGAATACTGTCGTGAGCTAGGTGAAAAAGTTTTTAATGGGCAGAAGAATTTGATTGAGCGCGGATTTCGTCAAGGTGGACCAGCTGGATTTGGGTTAAGACGCCTATTATTAAGTGCTGATGGTTCGCCAAAATTTGAACTAAAAACGGGTGACAGGAAGAGTTTGCAGTCGGATCGTGTCATTCTTATTGCGGGTCCTGAATTTGAACAGAAAATTATTTTACAAATCTATCACGATTTTATTTACAGACATAAAACGGAACGACAAATTGCAGATAGTTTAAATGCCCAAGTTATTTTAACAGATAGAAATACACGGTGGACTAAAGGTGTAGTCCATCAGATTCTAATTAATGAAAAATATGTAGGGCACAATGTTTGGAATAAATCTTGTACATCAAAGACGGGGAAGTTACGTGGTAAAAATCCAGAGTCTCAATGGGTAAGAGTTGAAAATGCTTTTGAAGCAATTATCCCACAACCCTTATTTAATGCAGCACAAGCCATTATTCACCAACGCTCAATAAAACTGACTGATGAGGAGATGTTGGACAAACTTCGAACATTGCTGAAAGTAAAGGGAAAGTTATCTGGTTTAATTATTGATGAAGCAGAAGATTGTCCATCAAGTAGCGCATATAGTAGTCGATTCGGTAGTCTGATCCGAACTTACGCAATGATTCACTATGAACCGGAGCGTGATTACCACTATGTTGAAATTAATCGATTAATGCGTCAACAATATAAGAAAATAGTTCAACAGGTACTTAATGAAATTATTGCATTAGGTGGACGTGTATCTATCGCTCCTAATGATCTTCTAAAAATCAATGAAGAATTTACCGCCTCTCTGGTTGTAAGCCCTTGCCGACCAACTACAAGGGGTAATAAACGCTGGATGATTCGTTTTGATACCGGGCTTGAACCTGATTTAACTATTGCAGTTCGTCTTGACGAAGATGCAGAAAACATTATTGATTATTATTTATTTCCAATGAAGGGGAGAGAAAGTAATAAATTGAGATTGGCTGAAAGCAACCCGGCTGAACTTGATATTTATCGATTTTCTAACTTGGATCGTTTCTTCATTATGGTAGAACGTATCTTATTAGGAGTTCATTATGGATATTCAAACTATTCCGATAGAAGATATTCGGATTATCAATCCAAGAACGCG","","","60862","MEYKNLAVAYIRMSTEHQEFSPDIQRRFIQKYAKEQGLILTREYLDEGRSGLSAEKRPQFLSLINFVQSGNADFSHILVYDISRWGRFLNIDESAHYEQICSKMGIKVHYCAEPFKGNDIGSQIFKAVKRWSAGEYCRELGEKVFNGQKNLIERGFRQGGPAGFGLRRLLLSADGSPKFELKTGDRKSLQSDRVILIAGPEFEQKIILQIYHDFIYRHKTERQIADSLNAQVILTDRNTRWTKGVVHQILINEKYVGHNVWNKSCTSKTGKLRGKNPESQWVRVENAFEAIIPQPLFNAAQAIIHQRSIKLTDEEMLDKLRTLLKVKGKLSGLIIDEAEDCPSSSAYSSRFGSLIRTYAMIHYEPERDYHYVEINRLMRQQYKKIVQQVLNEIIALGGRVSIAPNDLLKINEEFTASLVVSPCRPTTRGNKRWMIRFDTGLEPDLTIAVRLDEDAENIIDYYLFPMKGRESNKLRLAESNPAELDIYRFSNLDRFFIMVERILLGVHYGYSNYSDRRYSDYQSKNA","303922","","conserved hypothetical protein (possible recombinase)","Cytoplasm","","
InterPro
IPR006119
Domain
Resolvase, N-terminal
PF00239\"[7-89]TResolvase
InterPro
IPR011109
Family
Recombinase
PF07508\"[201-307]TRecombinase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1390\"[7-133]Tno description


","BeTs to 3 clades of COG1961COG name: Site-specific recombinases, DNA invertase Pin homologsFunctional Class: LThe phylogenetic pattern of COG1961 is ---pk----drlb-efg-s--j----Number of proteins in this genome belonging to this COG is","","Residues 88 to 502 match (3e-103) PD:PD416944 which is described as RECOMBINASE PROTEOME COMPLETE PLASMID HOMOLOG SITE-SPECIFIC ","","","","","","","","","","","","Wed Feb 19 13:48:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00439 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","1","" "AA00440","305540","305845","306","ATGTTGCACACAACGGGTAAGATTTTACCCAAAAATTTCAGAGAAGATTTTATCATCGAACTTCGGCAAGAAATGCATGAACAGTTCTGGTCAACACTTGAGTTATCGAAGAAATTAGGTGTATGCGAAAGAACAGTAAAAGCGTGGTTAAGAAATGAAAGGTTCCCCAACGGTATTTACCTTATAAAATTAATGTATCTCTCTGCACATATTCGAAAATATGTTTGGCAAATATCTGGTTCAGGAAAGCAATATATTGATATAGATATGATGAAACTAATTATTTCGAATTTATTAAATAAGCTA","","","12198","MLHTTGKILPKNFREDFIIELRQEMHEQFWSTLELSKKLGVCERTVKAWLRNERFPNGIYLIKLMYLSAHIRKYVWQISGSGKQYIDIDMMKLIISNLLNKL","305845","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 15:55:01 2004","Sun Feb 22 15:55:01 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00440 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 15:55:01 2004","","","","","","","","","","","","","1","","1","" "AA00442","307741","306329","1413","ATGAAAATCACCAAGATCCGTTCTCAAAAGAGAAATAGTTGCTCTATTTGTGGCAAAGCTCAAGTAACACGCAAGTTCCAAAAAGAATATTATTGCGCGAATTGCTACGCACAATGGTTTAAACAAAAAACTTGTAAGCGATGCGGACAACTCAAACGTATTCACCGTGATGGCAAACTTTGTCTTGAATGCGAAAAATTAACGGATTGTGTACGCTGTGGTAAAGAAGCTGGTACATTTGAAATCGGTATGATAAGTCGTTACGGTGCGGTATGTTGTTCTTGCACTCGTTATTTTCGAGAGGAAATAGAATGCTCAGAATGTGGTAAAATGACACGCGATAGATACCGTTCACCCGTGACGAATGAATCGGTCTGTTTGCAGTGCTATCGTCGATATACTTTTGCAACTTGTAAGAATTGTCGTCGTTATCGTAAGGTTCATAACCAAGAGAAACAGTTGTGCAAGAAATGTGACGAACAGTTACTTTCAACTTGCCCGAAATGCAAAGGTGAAATGCCATCAGGCTATGGCAATGTTTGCCCCGATTGTGCAAGACGAACCCTGTTATTCAAAATGATTCGGTTGAATATTCATATCTTTCGCAATAAAGCAATAAAAACCGCCTATAAGAAATTCATTTTCTGGTATATGCGAAAGTGTGGTATCGGCGTTGCTTTGCGTAAAGGCTCAGATTTTATGCGCTTCTTCATTGATTGTGATGATATTTGGCAGAAAATTCCTGATTATGCGGAATTGGTAACACACTTTAAACCAAATGGGTTACGTGCCAATTTAACTGTATTACGCTGGTTGCTTGATACGAATCAAGTTGCCGTTGATAAAACGCTAAAAGATGATTTAGCGGAATTAGAACGCATACAGGCTCTTTTTAACAAACTTAAAGAATCTATACCTTGTATCGCAAGCTATTATCAGAAATTACAACGGCGATGTGATGAGGGTAAAACCTCACTTAAATCAGTACGATTAGCCTTGCAGCCTGCGATAGACTTAATCAGTACTAACGAGATTACGGACTACCCAACACAAGACCAACTAAACCAGTATCTTGTGGAAAAATCAGGTCAAACGGCAGCTATAACAGGCTTTATCAATCATTTAAAATCGGAGTACCACCGAGAGCTTGAAATCGACCGTAAACTGATTCAGCAAATTAGAGCTAAACAGCTTAAAAAACATTGTTCTCAGCGATTAATTGAACTCTATAAACAAGCTTATTTAACTGAAAAAGAACAAATGGAGCTAGTTTCCGTTGTGTTATATAGTTTACACAACATTACAATTAAAACGCCAAAACGAAAGAACATCATCAAAATTGATCAAGTTGCCTATTATCGTTACGAAAATAGGGATTATTTTTTACCACAGGACATTTATAAGCATATAACC","","","56773","MKITKIRSQKRNSCSICGKAQVTRKFQKEYYCANCYAQWFKQKTCKRCGQLKRIHRDGKLCLECEKLTDCVRCGKEAGTFEIGMISRYGAVCCSCTRYFREEIECSECGKMTRDRYRSPVTNESVCLQCYRRYTFATCKNCRRYRKVHNQEKQLCKKCDEQLLSTCPKCKGEMPSGYGNVCPDCARRTLLFKMIRLNIHIFRNKAIKTAYKKFIFWYMRKCGIGVALRKGSDFMRFFIDCDDIWQKIPDYAELVTHFKPNGLRANLTVLRWLLDTNQVAVDKTLKDDLAELERIQALFNKLKESIPCIASYYQKLQRRCDEGKTSLKSVRLALQPAIDLISTNEITDYPTQDQLNQYLVEKSGQTAAITGFINHLKSEYHRELEIDRKLIQQIRAKQLKKHCSQRLIELYKQAYLTEKEQMELVSVVLYSLHNITIKTPKRKNIIKIDQVAYYRYENRDYFLPQDIYKHIT","306330","","conserved hypothetical protein (possible zinc finger protein)","Cytoplasm","","
noIPR
unintegrated
unintegrated
PTHR18973\"[98-162]TLIM DOMAIN CONTAINING PROTEIN
PTHR18973:SF93\"[98-162]TPINCH


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Mar 12 12:35:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00442 is paralogously related to AA00031 (8e-43).","","","","","","","","","","","","","","1","","1","" "AA00443","308856","307741","1116","ATGGGTACAACCAACGCAGGGCTTACGAAAAATTATCGGATAAAATCAAGGATTATTCGAACACCGCTTTACCTCAATGAAAGCATCAGTTCGTGGCTCATTCGTGCCGCCTTAGATTGTGGTACAGAGCCGATTACATTTACTGGATTTTATTGGGATAAGTGGCGACTATGGATATATGATTTAGATAGAGGGTTTGAACCGATTGCACCGCAGATTTATGAAGATATTAGGGCGTTATCGTTTAATCAACAGGTAAACTTAGTCAACCATTCGCTTTATTCCGTATTGAGACCGATTAATGGCGAAAGCACCCTTATTAAAGGTCAAGCGAAGTGGGTGATTTCAAGAGGTTCGCGTAATCGCACTTTTCGTGTCGGTCAATCTTATTGTCCTTGTTGTTTAGGGGAAACACCTTATTTGCGTAATGAATGGCGTTTTGCGTGGCATTTTGGTTGTTCGAAACATCAAGTTTTACTTGAATCTAAATGCCCTTGTTGTGGCGAACTGTATCAACCTCATTTGCTTTCCGCAGAAAAACGACACTTAAATTACTGTCATCAATGTGGTGAGAAATTACAGGTTGTTACAACACCGCTTAATGAAGTAGAAATTGCAACAATGGAAACACTTAATAACGTATTTATGACTAACTCAGGTGAATGTTTCAGGAAACGTGTGAATGCACAAGTGTACTTTGCTATATTGCGTTACTTCATCAATCTTATTCGGCGTGCTACGGTCGTAAAATCTACTCACGCTTTTGCAAAATTTGTGGAAGAATGTGGTATTTCTCAAGCGGAAATATGCCAAACCAAAACCGCCCTTGCATTTGAGCAGCTTCCTGTTGAAGAGCGCAAGAATCTATTGGTAAACGCGATTAAAATTCTAAAATTACCAAGTAAGGATTTTATTCAAGCTATTCAACAAAGCGGTATAACACAAAAGGCGTTCGACTTTGAAAAGTATCCTATGGAGCTTGATATACTCTTTAAATATGCACCTGAAGGCAAAACTGTAAGCCGTAAAACAGTAACCAATAAACCTAAGACCGATTCTGTTTTAAGTCTAAACCGTCAATGGGAGCGCTTAAAACGACGGCTAAAAATCACAGCA","","","43045","MGTTNAGLTKNYRIKSRIIRTPLYLNESISSWLIRAALDCGTEPITFTGFYWDKWRLWIYDLDRGFEPIAPQIYEDIRALSFNQQVNLVNHSLYSVLRPINGESTLIKGQAKWVISRGSRNRTFRVGQSYCPCCLGETPYLRNEWRFAWHFGCSKHQVLLESKCPCCGELYQPHLLSAEKRHLNYCHQCGEKLQVVTTPLNEVEIATMETLNNVFMTNSGECFRKRVNAQVYFAILRYFINLIRRATVVKSTHAFAKFVEECGISQAEICQTKTALAFEQLPVEERKNLLVNAIKILKLPSKDFIQAIQQSGITQKAFDFEKYPMELDILFKYAPEGKTVSRKTVTNKPKTDSVLSLNRQWERLKRRLKITA","307742","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Dec 11 12:52:06 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00443 is paralogously related to AA00033 (1e-109).","","","","","","","","","","","","","","1","","1","" "AA00444","309707","308817","891","ATGGAAAAACAATATGAGTATGTTCACGAAAAATTCCGTCATTTAGTGATTGCAAGCAATCAGGAACGGATTGAGTTTTTAGATGAACCACGTTGGGTAGGTTATGCCGTTGCAAATAAGATCATTGATAATTTGGTTTCCTTAATGAATAAGCCGAAACGCCCTCGCATGTTCAATTTGTTGGTAGTCGGTGATTCTAACAATGGTAAAACGACGCTTATTCGACACTTTTATGATTTGTACGGCATACCTTTCGTGGACAGCCAGTCGGACGGTATACGCCCCATTATTTTGGCAGAAGCACCGCCGAGTGCAAATGAAAAAGAGCTTTATATCTCGTTACTGGAGCGTTTTTATGTTCCATATCGACCAACGGATAGCGTAGCTAAATTGCGTTATCAGACGATTCACTTATTCCGTGAGTACAAGGTGAAAATGCTGATTATTGACGAATTCCATTCGTTGCTTGTGGGGACACCGCGTTTGCAACGCCAAGTGATGAATGCGATTAAGATGCTATGTAATGAGTTGCAGATTCCGATTGTAGGCGTAGGCACAAAAGATGCAATTCGTGTTTTACACACCGATCCGCAACACGCCAGTCGTTTTGATGTAGCAGAGTTGCCAACATGGAAATTAGATAAGGATTTTCAAAAATTACTCTTCCAATTTCAAGGTATTTTGCCATTGAAAAAATGCTCTAATCTACAATCGCCAGAGTTAGCGACAAAAATTCATACGATTTCAGGGGGTAATTTAGGGAATGTACATCGTTTATTAACCGCGTGCGCCATTGAAGCGATTACAACAGGAACAGAGCAAATTACATTAGATATTATCGAGCATAATTCATGGGTACAACCAACGCAGGGCTTACGAAAAATTATCGGA","","","34073","MEKQYEYVHEKFRHLVIASNQERIEFLDEPRWVGYAVANKIIDNLVSLMNKPKRPRMFNLLVVGDSNNGKTTLIRHFYDLYGIPFVDSQSDGIRPIILAEAPPSANEKELYISLLERFYVPYRPTDSVAKLRYQTIHLFREYKVKMLIIDEFHSLLVGTPRLQRQVMNAIKMLCNELQIPIVGVGTKDAIRVLHTDPQHASRFDVAELPTWKLDKDFQKLLFQFQGILPLKKCSNLQSPELATKIHTISGGNLGNVHRLLTACAIEAITTGTEQITLDIIEHNSWVQPTQGLRKIIG","308818","","NTP binding protein","Cytoplasm","","
InterPro
IPR008868
Family
Bacterial TniB
PF05621\"[22-275]TTniB


","No hits to the COGs database.","Significant hit ( 9e-05) to 2/5 blocks of the PR00449 family, which is described as \"Transforming protein P21 RAS signature\". Prints database entry for PR:PR00449. PR00449A 58-79 0.0003 PR00449D 177-190 1.6e+02","Residues 22 to 124 match (1e-08) PD:PD016330 which is described as PLASMID TNIB ATP-BINDING NTP-BINDING COMPLETE PROTEOME DELTA2 TNIBDELTA1 TNIBDELTA2 ","","","","","Tue Feb 18 09:58:46 2003","","","","","","","Wed Dec 11 13:05:52 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00444 is paralogously related to AA00034 (1e-164).","","","","","","Residues 6 to 296 (E-value = 5.5e-32) place AA00444 in the TniB family which is described as Bacterial TniB protein (PF05621)","","","","","Mindlin,S., Kholodii,G., Gorlenko,Z., Minakhina,S., Minakhin,L.,Kalyaeva,E., Kopteva,A., Petrova,M., Yurieva,O. and Nikiforov,V.Mercury resistance transposons of gram-negative environmentalbacteria and their classificationRes. Microbiol. 152 (9), 811-822 (2001)PubMed: 11763242Kholodii GY, Mindlin SZ, Bass IA, Yurieva OV, Minakhina SV, Nikiforov VG.Four genes, two ends, and a res region are involved in transposition of Tn5053: a paradigm for a novel family of transposons carrying either a mer operon or an integron.Mol Microbiol. 1995 Sep;17(6):1189-200.PMID: 8594337","","Tue May 20 15:24:48 2003","1","","1","" "AA00446","311626","309710","1917","ATGACTAAAGGATTTATTTATCCTCGCTATCACGGTCGATTAGAGCGTGGTCGTCTCATTTTGCAAAAAGGCAACGTTTATGTAAATCGTGAAGATGGCGAACAATATGAACTGATTGAGTATTTAGATGAAGATGCACAAGTGATGATCCGAAATCTTCATACTCGCCAAAGTAAAATTTCCAGTATTCATCAGCTTGAGAATTTAAAAGTGAATGAACGCGAAGATGTTTCTGTTGATTTAAGCGCAATCAGCGATGAATACTGGGAAAAAGCGTTAGAAAAATACGAAATGATTAAGCCGTTGCTTAATTATGAACAACATTGCCCTGCTTCTGTAAAAGAACGAGCAAAAGAAGTTGGAGTGAGTGATCGAAGTTTATATCGTTGGATTCAAGCTTACAACTCTCTCGGCTCTATCGCTGGTTTAGTCAGTCGTAAGCGTGGCTGGGCGGAAGGTAATTCGCGTTTAAGCAAAGAACAAGATGAGTTGGTGACAGCGGTTATCAATGAGTTTTATCTACATAAACAACGCCCAACGATTGAGCAGACGATCCGTGAAGTGCAGCGTGTCGCCAGTCAAAAAGGGCTTGATAGCCCAAGCCGTCGCACAATCCGACAACGTATTTTGCGTATTTCAGAAGAAGAAAGATTGCGTAAACGCGGGCAGAAAGAGAAAGCGAAAAATAAATTTACGCCGAAGCCAAACAGTTTCCCTAACGTAGATTTTCCTTTAAGTGTTATTCAAATCGACCATACGCCTGTTGATTTAATTATTGTAGATAACCAGTATCGTAAGCCGATTGGCAGACCTTACCTAACGTTGGCAATGGATGTATATAGCCGAATGATTACTGGGTACTATCTATCACTTGATGCACCGTCGGTAACATCGGTTGCAATGTGTATTGCTCGCAGCATTTTGCCGAAAGAACGCCTATTACTAGATCATAATGTAAAAGGTGAATGGGCGGTATTCGGTTATCCGAATAAAATCCACGTGGATAATGGAGCAGACTTCCGTTCATTGGATTTATCCAAATCTTGTGAGGCACACGGTATTGCCCTTGAGTTCCGCCCTGTTGGTCGTCCTGAATTTGGCGGACACATTGAGCGTGTAATCGGTACGTTTATGAAAGAAGTTCACGGTTTGAGTGGTACAACATTCTCAAATACGAAAGAGAAAGATACCTATCAATCGGAAGCAGAAGCGGTAATGACCTTAGATGAATTTGAAACGTGGCTGATTAACTATATTGTAAACGTGTATCACAAACGCACCCACTCTGCGCTAGGTATGTCGCCTGTTCAAAAATGGCGATTGGGGATTTTTGGTGATAAAGATCATGTCGGTTGTGGTTATCCGCAAATGCCTGTTGATGAACAAACGTTATTACTCGATTTCTTACCAAGCGAAAAACGAACTATTCAGCATAATGGCGTAACGATTGATGGTTTACGTTACTACGATGTGGCACTCAATATGTACATCAATGATTCCGATGAAAACGGTAAGAGCAAGGAATTTTTATTCCGTCGAGATCCTCGTAATATCGGCAAGATTTGGTTCTATGATCCGAAGTTGAAACATTATTTCCCGATTCCGTTTGCCGACCAGTCTTTACCTGATATGAGCATTTGGGAATACAAACAAGTTCGTCATTTCTTGAAAGATAAAGATGAAAAACTCATTCACTCGCAGCAGATCCACGATGCATTAACTGAAATGCGTGAATTGGTTGAACAGTCTGCACAGCGGATGAAGAAAGCTCGGAGACAGGCTCAACGGCAGAAAGTCCACGCGAAAAGTAAGGTAGTGATCCCAACAAGTTTACCCGAAAGCAAACCAACAGAAACAGTCAAAACACCTGCTTCTAACTTGCTTTTAGATAATGATTTCACGTTTGGAGATATTGAA","","","75653","MTKGFIYPRYHGRLERGRLILQKGNVYVNREDGEQYELIEYLDEDAQVMIRNLHTRQSKISSIHQLENLKVNEREDVSVDLSAISDEYWEKALEKYEMIKPLLNYEQHCPASVKERAKEVGVSDRSLYRWIQAYNSLGSIAGLVSRKRGWAEGNSRLSKEQDELVTAVINEFYLHKQRPTIEQTIREVQRVASQKGLDSPSRRTIRQRILRISEEERLRKRGQKEKAKNKFTPKPNSFPNVDFPLSVIQIDHTPVDLIIVDNQYRKPIGRPYLTLAMDVYSRMITGYYLSLDAPSVTSVAMCIARSILPKERLLLDHNVKGEWAVFGYPNKIHVDNGADFRSLDLSKSCEAHGIALEFRPVGRPEFGGHIERVIGTFMKEVHGLSGTTFSNTKEKDTYQSEAEAVMTLDEFETWLINYIVNVYHKRTHSALGMSPVQKWRLGIFGDKDHVGCGYPQMPVDEQTLLLDFLPSEKRTIQHNGVTIDGLRYYDVALNMYINDSDENGKSKEFLFRRDPRNIGKIWFYDPKLKHYFPIPFADQSLPDMSIWEYKQVRHFLKDKDEKLIHSQQIHDALTEMRELVEQSAQRMKKARRQAQRQKVHAKSKVVIPTSLPESKPTETVKTPASNLLLDNDFTFGDIE","309711","","transposase","Cytoplasm","","
InterPro
IPR001584
Domain
Integrase, catalytic core
PF00665\"[240-440]Trve
PS50994\"[240-443]TINTEGRASE
noIPR
unintegrated
unintegrated
G3DSA:3.30.420.10\"[243-381]Tno description


","BeTs to 4 clades of COG1425COG name: Predicted transposaseFunctional Class: LThe phylogenetic pattern of COG1425 is a--p-----dr---efgh-n-j----Number of proteins in this genome belonging to this COG is","","Residues 117 to 189 match (9e-09) PD:PD483826 which is described as PROTEOME COMPLETE TRANSPOSASE PLASMID ","","","","","","","","","","","","Wed Dec 11 13:22:19 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00446 is paralogously related to AA00036 (0.0).","","","","","","Residues 240 to 440 (E-value = 2.9e-18) place AA00446 in the rve family which is described as Integrase core domain (PF00665)","","","","","Kahn,K. and Schaefer,M.R. Characterization of transposon Tn5469 from the cyanobacterium Fremyella diplosiphon J. Bacteriol. 177 (24), 7026-7032 (1995) PubMed: 8522506 Schaefer,M.R. and Kahn,K. Cyanobacterial transposons Tn5469 and Tn5541 represent a novel noncomposite transposon family J. Bacteriol. 180 (22), 6059-6063 (1998) PubMed: 9811670 ","","Wed Dec 11 13:22:19 2002","1","","1","" "AA00447","312281","311622","660","ATGAAAACAGAACCCATTTTCCAACAGGTTCGTAAGATCAAACCAACACGCCTTAGCGTATCAGGTTTACTCCCTTTTAAAGATGGAGTAAGCATTCCTTACGAATCTACGCTTGAGCGAGATCTCTTGCTTTATTTTACTTATATGCCTGCGGTAGAGGAAATCATTTCTCAACCTGTTCGCATTCTGTTTGTGAAAAATAGAATGACTTATCCTTACACGCCTGATTTCTTTATTCGCTTCAATGATGGACGACCATCGCTTTTGATTGAAGTAAAACCGAAATCAAAATGGCAGGAACATTGGCGTGATTGGAAAGAAAAATGGAAAGCAGCAATGGCATTCAGCAAAAAGAACAAGTGCATCTTCCATATTTATGATGAAGATAGAATTCGTCACCTTGCGTTATTCAACATTAACGCGGTTCAACGTTACAAACGATTACAGTGCGATCCTGAAGATATTGGAGCGATACTTACTCAAGTTAAGTTACACGGTGGTACCACGATAGATTTTCTGCTCTCTCGCCTTTTTACAGGTTCACTTTATCGAACCAAAGGGTTACAGATTATATATCACTTATTAGCAACCAAGCAGCTTACTTGCAACTGGTTTGAACCATTATCTGAATTTACCGAAGTTTGGGGGTATTCAAATGAC","","","26061","MKTEPIFQQVRKIKPTRLSVSGLLPFKDGVSIPYESTLERDLLLYFTYMPAVEEIISQPVRILFVKNRMTYPYTPDFFIRFNDGRPSLLIEVKPKSKWQEHWRDWKEKWKAAMAFSKKNKCIFHIYDEDRIRHLALFNINAVQRYKRLQCDPEDIGAILTQVKLHGGTTIDFLLSRLFTGSLYRTKGLQIIYHLLATKQLTCNWFEPLSEFTEVWGYSND","311623","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR014832
Domain
TnsA endonuclease C terminal
PF08721\"[130-204]TTnsA_C
InterPro
IPR014833
Domain
TnsA endonuclease N terminal
PF08722\"[50-128]TTnsA_N


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Dec 11 13:28:58 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00447 is paralogously related to AA00037 (1e-100).","","","","","","","","","","","","","","1","","1","" "AA00448","312408","313118","711","TTGCCGATTATGCCACTTATTTGTAACTTTGACAGCGGCACGATCCCCAAACCGGGCGAAATTTCCCTCGCTCACAATGGCATTCTTTTCTTAGATGAGTTGCCCGAATTTGAACGCAAAGTGCTGGACGCGCTGCGTCAACCATTGGAAAGTGGCGAAATTATTATTTCCCGCGCCAACGCCAAGATTCAATTTCCGGCAAAATTTCAACTGATTGCCGCGATGAATCCCAGCCCGACAGGGCATTATCAAGGCACGCATAATCGCACCTCACCACAACAAGTTATGCGTTATCTGAATCGGTTATCCGGCCCTTTTTTAGATCGCTTCGATTTATCCATTGAAGTGCCCTTATTACCACAAGGCAGCTTACAAAATAGCGGCGATCGTGGCGAATCCAGCGCAACGGTGCGAGAAAAAGTCCTGAAAACCCGTGCCATTCAACTTCAGCGCGCCGGCAAAATTAATGCCCATTTAAATAGCAAAGAAATCGAACGGGACTGCAAACTAACCGACAAAGACGCACAGTTCCTGGAAAATGCCCTGACTAAACTGGGGCTTTCCGTACGAGCGTACCACCGCATACTGAAAGTGCCCCGCACCATTGCCGATTTAGATGGAGAACAACACATCAACCAGCGCCATCTGGCCGAAGCTCTGGGTTATCGGGCAATGGACAGGTTGTTGCAAAAATTGGCGAAAAACTCGGCG","","","26517","LPIMPLICNFDSGTIPKPGEISLAHNGILFLDELPEFERKVLDALRQPLESGEIIISRANAKIQFPAKFQLIAAMNPSPTGHYQGTHNRTSPQQVMRYLNRLSGPFLDRFDLSIEVPLLPQGSLQNSGDRGESSATVREKVLKTRAIQLQRAGKINAHLNSKEIERDCKLTDKDAQFLENALTKLGLSVRAYHRILKVPRTIADLDGEQHINQRHLAEALGYRAMDRLLQKLAKNSA","313119","The N-terminal region of competence protein M, comM, is AA00425. From GenBank [gi:9457884]: In Haemophilus Influenzae, ComM is induced during competence developement, but is not needed for DNA uptake. It may be involved in a recombination step. It belongs to the Mg-chelatase subunits D.I family, ComM subfamily.","C-terminal region of competence protein M","Cytoplasm","","
InterPro
IPR000523
Domain
Magnesium chelatase, ChlI subunit
PF01078\"[13-124]TMg_chelatase
InterPro
IPR002078
Domain
RNA polymerase sigma factor 54, interaction
PS00676\"[19-34]TSIGMA54_INTERACT_2
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[10-117]Tno description


","BeTs to 14 clades of COG0606COG name: Predicted ATPase with chaperone activityFunctional Class: OThe phylogenetic pattern of COG0606 is --m----qvdr--cefghsnuj--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 2.5e-10) to 1/1 blocks of the IPB001208 family, which is described as \"MCM family\". Interpro entry for IP:IPR001208. IPB001208 16-61 2.3e-10","Residues 32 to 85 match (1e-22) PD:PD587240 which is described as COMPLETE PROTEOME COMM COMPETENCE CHELATASE FAMILY MG2 ORF PROBABLE YIFB ","","","","","","","","","","","Fri Jan 7 17:08:50 2005","Thu Mar 20 17:01:20 2003","","Fri Jan 7 17:08:50 2005","Fri Jan 7 17:08:50 2005","Fri Jan 7 17:08:50 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA00448 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Fri Jan 7 17:08:50 2005","","","","","","","","","","Gwinn ML, Ramanathan R, Smith HO, Tomb JF.A new transformation-deficient mutant of Haemophilus influenzae Rd with normal DNA uptake.J Bacteriol. 1998 Feb;180(3):746-8.PMID: 9457884","","Fri Jan 7 17:08:50 2005","1","","","" "AA00449","313969","313136","834","TTGGTTACGATGAAATTGATGAGCGTAAAAACGCTGATTTTTCTTACCGCACTTCTATGGTTGCCGGTTGCTTATTCTGCCAAACTTGCCATTGTGATTGATGATTTGGGCTATCACCCGAAAGAAGATGCACAAATTCTTGCTTTGCCGAAAGCGGTTTCCGTAGCAATTATTCCCGCTGCGCCTTATGCCAAACAGCGCAACCAACAGGCACACCAGCAGGGGCGCGACATTTTGATTCACATGCCTATGGAAACTGTCAGCAAAATGAAAATTGAAGGCGGCGGTTTGCATTTAGGCATGAACCAGGAGGAAGTGAATCATCGTGTACAAACGGCAAAAAAGATTGTATCTCACGCCATTGGTATGAATAACCACATGGGTAGCGCCGCCACGGCGGATGTGCCGTTAATGACCAAATTAATGACCGCACTTCGAGAGCGTCATTTATTTTTTCTGGACAGCCGTACCATCGGGCGCAGTGTGGCGGGTAAAATTGCCAAAGCGCAGGGCGTGCTGGCGTTGGATAGACATATTTTTTTAGATGACAGCAATGATCTCGCCGACGTGCAACGTCAGTTTCGCGCCGCCGTACAATACGCGCAAAAGCACGGCACTGCCATTGCTATCGGGCATCCGCGTAAGAATACCATTGCCGTCTTGCAAGCCGGCATTATAAACCTGCCGTCGGATGTGCAGTTGGTCTCTATGGGCAGTTTATGGCGTAATGAAAAGGTTATTCCGCCGAAACCGTTTATTTTCTTATTTAGTGAAGCCGCTGCACCGACTTCCGTCCCACCTTATGAAAATGTGCCCTTACTGCGTGGTGTGCCT","","","30431","LVTMKLMSVKTLIFLTALLWLPVAYSAKLAIVIDDLGYHPKEDAQILALPKAVSVAIIPAAPYAKQRNQQAHQQGRDILIHMPMETVSKMKIEGGGLHLGMNQEEVNHRVQTAKKIVSHAIGMNNHMGSAATADVPLMTKLMTALRERHLFFLDSRTIGRSVAGKIAKAQGVLALDRHIFLDDSNDLADVQRQFRAAVQYAQKHGTAIAIGHPRKNTIAVLQAGIINLPSDVQLVSMGSLWRNEKVIPPKPFIFLFSEAAAPTSVPPYENVPLLRGVP","313137","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR006837
Family
Protein of unknown function DUF610, YibQ
PF04748\"[31-242]TPolysacc_deac_2
noIPR
unintegrated
unintegrated
signalp\"[1-26]?signal-peptide


","No hits to the COGs database.","","Residues 224 to 278 match (4e-17) PD:PD123972 which is described as PROTEOME COMPLETE PM1508 HI0755 SIGNAL PRECURSOR ","","","","","","","","","","","","Wed Dec 11 13:32:42 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00449 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 31 to 242 (E-value = 5.4e-113) place AA00449 in the Polysacc_deac_2 family which is described as Divergent polysaccharide deacetylase (PF04748)","","","","","","","","1","","","" "AA00450","315216","313960","1257","ATGTGGCAATTATATGAGATAAAACGTAGGAGGAAATTCCTTGTGGGCAGAGTACGTATAAAAACACTTGGAATTTTCACCGCACTTTTATGTGCCGCGCCTTCCGTTTTTGCCGCGCAGCAGGATTTGTCGAAAATCCACCAGCAGATTAAGCAACAGGAACAAAAAATTGCTTCGCAGAAAGCCGAGCAACAAAAGTTGCAATCCACTCTGAAAACACAAGAAAACCAAATCAATAACGTGATCGGGCAGTTGCGTCAAACGGAATCGGATTTGAAAGCAATCCGTAAAAATATTAGCGATACCGATAAGCAAATCAAGCAATTACAAAAGCAGGAAAAAGAACAAAAAGCGAAACTGGCGAAGCAGTTGGATGCTGCTTATCGTTCCGGCGTCAATCCTTCCGTGGCGGAGCGGATATTGTCCGATAAGGGGCAAAATGCGGAGCGTATGAAAGCGTATTACGCCCATTTGAATCGGGCGCGCATGAAGCTCATTGCAGAGTTACAGGATACCCGGGCGCAGTTGGCGAAACAAAAAGAAGCTATCGCCGAGCAACAGAAAACCCAACAATCGCAGCTTGCGGATCAGAAAAAGCAACAGCAGGCATTGCAGAAAGTTCAGCAGGAGCGCCAATCGACTTTGAGTCAGCTCAATCATAATCTGACCCGTGACGAAAGCAAGCTGGAAGCACTGAAAGCCAATGAAAACGCTTTGCGTCAGGAAATTCAACGGGCGGAACAGGCGGTGAAACAACAAGAGCAACGTGAGCGCGAAGCGTTGGCGCAAAAACAACGGGCGGAGGAGACCAAAACCCATAAACCGTACAAGCCGACGGAGCAGGAAAAACGTTTGTTAAGCAGCACGTCGGGCTTAGGCGCACCGCAGAAACAATATGGTTTTCCGGTGGCGGGCAAAGTTGTCAACCGCTTTGGTTCGACCCAAATGGGCGAACTCCGCTGGAAAGGCATCGTCATTGCCGCCGGCAGCGGCACGCCGGTAAAAGCCATTGCCGACGGGCGGGTGATTTTAGCCAACTGGTTGCAGGGCTATGGCTTGATGGTGATTGTGAAACATGGCGACAGCGATTTAAGTTTGTATGGGTATAATCAATCCCTGGCGGTGAAAGAAGGGCAGTTGGTGAAAGCCGGACAAAAAATCGGCGAAGTGGGGAGCAGTGGCGGGCAGTCAAAAACTGCACTGTATTTTGAAATTCGTCGCAAGGGCGTTGCGGTCAATCCGGTAGGTTGGTTACGA","","","52034","MWQLYEIKRRRKFLVGRVRIKTLGIFTALLCAAPSVFAAQQDLSKIHQQIKQQEQKIASQKAEQQKLQSTLKTQENQINNVIGQLRQTESDLKAIRKNISDTDKQIKQLQKQEKEQKAKLAKQLDAAYRSGVNPSVAERILSDKGQNAERMKAYYAHLNRARMKLIAELQDTRAQLAKQKEAIAEQQKTQQSQLADQKKQQQALQKVQQERQSTLSQLNHNLTRDESKLEALKANENALRQEIQRAEQAVKQQEQREREALAQKQRAEETKTHKPYKPTEQEKRLLSSTSGLGAPQKQYGFPVAGKVVNRFGSTQMGELRWKGIVIAAGSGTPVKAIADGRVILANWLQGYGLMVIVKHGDSDLSLYGYNQSLAVKEGQLVKAGQKIGEVGSSGGQSKTALYFEIRRKGVAVNPVGWLR","313961","","outer membrane antigenic lipoprotein b precursor","Outer membrane, Periplasm, Inner membrane, Extracellular","","
InterPro
IPR002886
Family
Peptidase M23B
PTHR21666:SF7\"[10-94]T\"[263-419]TM23/M37 PEPTIDASE FAMILY MEMBER
PF01551\"[319-414]TPeptidase_M23
noIPR
unintegrated
unintegrated
PTHR21666\"[10-94]T\"[263-419]TPEPTIDASE-RELATED
signalp\"[1-38]?signal-peptide
tmhmm\"[20-38]?transmembrane_regions


","BeTs to 16 clades of COG0739COG name: Membrane proteins related to metalloendopeptidasesFunctional Class: MThe phylogenetic pattern of COG0739 is -------qvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.3e-30) to 2/2 blocks of the IPB002886 family, which is described as \"Peptidase family M23/M37\". Interpro entry for IP:IPR002886. IPB002886A 321-346 2.4e-10 IPB002886B 354-394 7.5e-19","Residues 350 to 408 match (2e-07) PD:PD507385 which is described as NLPD ","","","","","","","","","","","","Wed Dec 11 13:34:39 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00450 is paralogously related to AA01407 (5e-19), AA02347 (8e-10), AA01822 (1e-09), AA02832 (6e-07), AA01922 (2e-04), AA02511 (0.001) and AA00769 (0.001).","","","","","","Residues 335 to 417 (E-value = 5.5e-35) place AA00450 in the Peptidase_M37 family which is described as Peptidase family M23/M37 (PF01551)","","","","","","","","1","","","" "AA00451","315208","315408","201","TTGCCACATAACCTGCCTTCCCTTTTCATAAACCGCGCTAAATATACCATTAATAAGGCAGATTATCCCACAAAAACGTTTGAAAAACCGACCGCACTTTGCCTCAAATTCCCGTTGACTGAGCTGCCCGTGCACTCCGAAATACGCGCCTGCTTATTTAAAAGAAAACGGTATTCCTCAAAGAATACCGTTTTTCATTTT","","","7865","LPHNLPSLFINRAKYTINKADYPTKTFEKPTALCLKFPLTELPVHSEIRACLFKRKRYSSKNTVFHF","315409","","hypothetical protein","Periplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Dec 11 13:36:02 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00451 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00452","317083","315428","1656","ATGTCAGTACTTTTTGATACCGCACAAAATTGGTTAAACCAAGATCCGGATGTGGAAACACACGCAGAATTGACCGCACTTTTAAGTGCTGCGAAAGGCGGTGATGCTAAGGCACAAGCCGAACTCGCCGAACGCTTTAGCGGGCGCTTACAATTCGGCACCGCAGGTTTACGTGGTCGCCTGCAAGCAGGTTCCATGGGCATGAACCGCGTGTTGGTGGCGCAAGCCGCCGGAGGTTTGGCATTATTCTTAAAAGAATACGACAAGCAACCTTCGATCGTGATTGGTTATGACGGACGTAAAAATTCCGATGTATTTGCGCGTGATACCGCCGAAATCATGGCAGGCGCGGGCATTAAAGCCTATTTATTACCGCGCAAATTGCCAACGCCGGTGTTGGCCTATGCCATTCAATATTTCGACACCACCGCCGGCGTGATGGTCACCGCCAGCCATAACCCGCCGGAAGATAACGGTTATAAAGTGTATTTAGGCAAAGCCAACGGCGGTGGACAAATCGTTTCCCCGGCAGATAAACAAATCGCCGCACTTATTGATAAAGTCGCTGCCGGCAGTATTAAGGATTTACCGCGCAGTCAGGATTATGCGGTGTTAGACGACACCGTGGTGGATGCCTATATCGCCAAAACCGCTTCACTTGCCAAAGAACCGCAAACGGATATTAACTATGTTTATACCGCGATGCACGGTGTGGGTTATGAAGTGTTGAGCAAAACCTTGACAAAAGCGGGTTTGCCTCAACCGCATATTGTCGCCGAACAAGTGTGGCCGGACGGCACATTTCCGACTGTTAATTTCCCGAATCCGGAAGAAAAAGGTGCATTGGATTTGGCAATTAAGGTGGCGAAAGAAAACAACGCCGAATTTATTATCGCCAATGACCCCGACGCCGACCGTTTAGCCGTGGCAATCCCTGACGCCGAAGGCAACTGGAAACCGCTGCACGGCAACGTAGTAGGTTGTTTCCTTGGCTGGTATTTGGCGAAACAATATCAAGCTCAAGGCAAAAAAGGCGTATTGGCGTGTTCTCTCGTGTCTTCGCCGGCGTTGGCGGAAATCGCTAAGCGCTATGGTTTCGGATCGGAAGAAACCCTCACCGGCTTCAAATATATCGGCAAAGTACAGGGCTTATTATTTGGCTTTGAAGAAGCCCTTGGCTACTTGGTTGACCCGGATAAAGTGCGCGACAAAGACGGTATCTCCGCCGCCATTGTGTTCTTGGATTTAGTGCGCCATCTGAAAAAACAAGGCAAGACTTTGGCGGATTATGCGGCAGAATTCATCAGTGAATTCGGTGCGTATGTGAGCGGGCAAATTTCCATTCGCGTCAGTGATCTTTCCGAAATCGGCAAATTAATGACCGCACTTCGCAACAATCCGCCAAGCCAAATCGGTGGTTTCAATGTGGCGCAATTTATCGACCACACCAAAACCGACCGCCAAAGTGACATTCTGGTCTTTGTACTTGAAAACGGCAGCCGTTTAATTGCCCGTCCGTCCGGTACCGAACCGAAAATCAAGTTCTACCTCGACGCCCGCGGCACTGACCCGAAAAATGCCGACCAAGTCCTAGCCGACTTCGACGCCGCCGTCCGCGCTATTTTGCGCCAAGAGGCTTATGGGAAACAGGATTGT","","","60702","MSVLFDTAQNWLNQDPDVETHAELTALLSAAKGGDAKAQAELAERFSGRLQFGTAGLRGRLQAGSMGMNRVLVAQAAGGLALFLKEYDKQPSIVIGYDGRKNSDVFARDTAEIMAGAGIKAYLLPRKLPTPVLAYAIQYFDTTAGVMVTASHNPPEDNGYKVYLGKANGGGQIVSPADKQIAALIDKVAAGSIKDLPRSQDYAVLDDTVVDAYIAKTASLAKEPQTDINYVYTAMHGVGYEVLSKTLTKAGLPQPHIVAEQVWPDGTFPTVNFPNPEEKGALDLAIKVAKENNAEFIIANDPDADRLAVAIPDAEGNWKPLHGNVVGCFLGWYLAKQYQAQGKKGVLACSLVSSPALAEIAKRYGFGSEETLTGFKYIGKVQGLLFGFEEALGYLVDPDKVRDKDGISAAIVFLDLVRHLKKQGKTLADYAAEFISEFGAYVSGQISIRVSDLSEIGKLMTALRNNPPSQIGGFNVAQFIDHTKTDRQSDILVFVLENGSRLIARPSGTEPKIKFYLDARGTDPKNADQVLADFDAAVRAILRQEAYGKQDC","315429","","phosphomannomutase; phosphoglucomutase","Periplasm, Cytoplasm","","
InterPro
IPR005841
Family
Phosphoglucomutase/phosphomannomutase
PS00710\"[145-154]TPGM_PMM
InterPro
IPR005843
Domain
Phosphoglucomutase/phosphomannomutase C-terminal
PF00408\"[459-540]TPGM_PMM_IV
InterPro
IPR005844
Domain
Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain I
PF02878\"[49-192]TPGM_PMM_I
InterPro
IPR005845
Domain
Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain II
PF02879\"[211-318]TPGM_PMM_II
InterPro
IPR005846
Domain
Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain III
PF02880\"[322-434]TPGM_PMM_III
noIPR
unintegrated
unintegrated
G3DSA:3.40.120.10\"[39-200]T\"[229-310]T\"[320-443]Tno description
PTHR22573\"[110-544]TPHOSPHOHEXOMUTASE FAMILY MEMBER
PTHR22573:SF2\"[110-544]TPHOSPHOGLUCOMUTASE


","BeTs to 26 clades of COG1109COG name: PhosphomannomutaseFunctional Class: GThe phylogenetic pattern of COG1109 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 6.1e-06) to 1/1 blocks of the IPB001485 family, which is described as \"Phosphoglucomutase and phosphomannomutase family\". Interpro entry for IP:IPR001485. IPB001485 145-154 6.3e-06","Residues 388 to 441 match (2e-07) PD:PD394215 which is described as PHOSPHOMANNOMUTASE COMPLETE PROTEOME PHOSPHORYLATION ISOMERASE FIS PMM CDNA PLACE1001781 NTONG1000264 ","","","","","","","","","","","","Wed Jan 29 13:44:36 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00452 is paralogously related to AA00636 (5e-15) and AA01013 (3e-07).","","","","","","Residues 211 to 318 (E-value = 4.8e-06) place AA00452 in the PGM_PMM_II family which is described as Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II (PF02879)","","","","","Regni C, Tipton PA, Beamer LJ. Crystal structure of PMM/PGM: an enzyme in the biosyntheticpathway of P. aeruginosa virulence factors. Structure (Camb). 2002 Feb;10(2):269-79. PMID: 11839312","","Wed Dec 11 13:38:49 2002","1","","","" "AA00453","317389","318069","681","ATGGAATTAGTTTTTATTCGTCACGGCTTCAGTGAATGGAATGCAAAAAACTTATTTACCGGTTGGCGTGATGTGAATTTAACCGAACGTGGTGTGGAAGAAGCCAAAGCGGCAGGAAAAAAGTTATTAGACGCCGGTTTTGAATTCGACATCGCCTTCACTTCCGTCCTGACCCGTGCCATTAAAACCTGTAACATCGTCTTGGAAGAATCCCACCAATTATGGATCCCGCAAGTGAAAAACTGGCGCTTAAACGAACGTCACTACGGCGAATTACAAGGCTTAGACAAAAAAGCCACCGCCGAAAAATATGGTGACGAACAAGTTCACATCTGGCGCCGTTCCTACGACACATTACCACCATTACTTGATCCGAAAGATCCAAATTCCGCTCACAACGACCGTCGCTACGCCCATTTACCGGATGATGTGATTCCGGACGGTGAGAACCTGAAAGTCACGTTAGCGCGCGTGCTTCCGTTCTGGGATGACCAAATCGCCCTTGCCCTCTTAAGCGGTAAGCGCGTTTTAGTGGTTGCTCACGGTAACTCTTTACGTGCATTGGCAAAACACATTGAAGGCATTTCCGACGCAGACATTATGGATTTAGAAATCCCGACCGGTCAGCCGTTGGTTTACAAATTAGATGATAATCTGAAAGTGGTTGAGAAATTCTATTTG","","","25921","MELVFIRHGFSEWNAKNLFTGWRDVNLTERGVEEAKAAGKKLLDAGFEFDIAFTSVLTRAIKTCNIVLEESHQLWIPQVKNWRLNERHYGELQGLDKKATAEKYGDEQVHIWRRSYDTLPPLLDPKDPNSAHNDRRYAHLPDDVIPDGENLKVTLARVLPFWDDQIALALLSGKRVLVVAHGNSLRALAKHIEGISDADIMDLEIPTGQPLVYKLDDNLKVVEKFYL","318070","","phosphoglyceromutase","Cytoplasm","","
InterPro
IPR005952
Family
Phosphoglycerate mutase 1
PTHR11931\"[1-222]TPHOSPHOGLYCERATE MUTASE
TIGR01258\"[1-227]Tpgm_1: phosphoglycerate mutase
InterPro
IPR013078
Domain
Phosphoglycerate mutase
PF00300\"[2-188]TPGAM
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1240\"[1-227]Tno description
PIRSF001490\"[1-225]TCofactor-dependent phosphoglycerate mutase


","BeTs to 8 clades of COG0588COG name: Phosphoglycerate mutase 1Functional Class: GThe phylogenetic pattern of COG0588 is ------y---rl--e--hsn-j-it-Number of proteins in this genome belonging to this COG is","Significant hit ( 3.5e-43) to 4/4 blocks of the IPB001345 family, which is described as \"Phosphoglycerate mutase family\". Interpro entry for IP:IPR001345. IPB001345A 3-32 1.4e-15 IPB001345B 52-64 0.0016 IPB001345C 76-107 2.4e-13 IPB001345D 146-164 3.7e-06","","","","","","","","","","","","","Wed Dec 11 13:40:47 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00453 is paralogously related to AA02057 (6e-10) and AA00942 (4e-04).","","","","","","Residues 1 to 224 (E-value = 3.3e-129) place AA00453 in the PGAM family which is described as Phosphoglycerate mutase family (PF00300)","","","","","Durany N, Carreras J, Valenti M, Camara J, Carreras J.Inactivation of phosphoglycerate mutase and creatine kinase isoenzymes in human serum.Mol Pathol. 2002 Aug;55(4):242-9.PMID: 12147715 Galperin MY, Jedrzejas MJ.Conserved core structure and active site residues in alkaline phosphatase superfamily enzymes.Proteins. 2001 Dec 1;45(4):318-24.PMID: 11746679 ","","Wed Dec 11 13:47:57 2002","1","","","" "AA00454","318651","318160","492","ATGGAAATGTCAACTACTCAACGTTTGATTTTAGCTAATCAATATAAGTTAATGAGCCTACTCGATTGTGATAATGCCGCTAAATATCAACGTTTGGAAACCATTGTAAAAGGCGGCTTTGCTTTAGAATTAAACACTTTGGAAAATGATTTCACCAACATTTCGGAACGCGAATGTCAAATAGTGTTAGATACTTTGGAAATGTATAAAGCACTTCAAATTTCTTACAACAATTTAGAGAACAAATCCGAATTAAGCGAACATCGTTTACAGTTCGTCGGTTATTGCGCCATTCGTGAGAAGAAATACCTAAGCTACCTGCGTTTCATCACCGGCGTAGAAGGGAAATATCAGGAATTTATGCGTTGCGAACACGGCTGCGATTCCCAAACCCCTATGTGGGACAAATATTCCCGTATGCTCGAAGTCTGGCGCGCTTGCCCGCATGAATATCATTTAAGCATGGTGGAAATTCAAAATATTCTGAATGCT","","","19604","MEMSTTQRLILANQYKLMSLLDCDNAAKYQRLETIVKGGFALELNTLENDFTNISERECQIVLDTLEMYKALQISYNNLENKSELSEHRLQFVGYCAIREKKYLSYLRFITGVEGKYQEFMRCEHGCDSQTPMWDKYSRMLEVWRACPHEYHLSMVEIQNILNA","318161","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR005587
Family
YfbU
PD035118\"[1-164]TYF00_PASMU_Q9CKV5;
PIRSF006272\"[1-164]TUncharacterised conserved protein
PF03887\"[1-164]TYfbU
noIPR
unintegrated
unintegrated
G3DSA:1.10.287.680\"[1-52]Tno description
G3DSA:1.10.3190.10\"[53-164]Tno description


","BeTs to 3 clades of COG3013COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG3013 is --m-----------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 1 to 164 match (2e-70) PD:PD035118 which is described as PROTEOME COMPLETE CYTOPLASMIC YPO2563 VC1871 PM1500 MJECS11 STY2565 YFBU ORF ","","","","","","","","","","","","Wed Dec 11 14:43:24 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00454 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 164 (E-value = 1.7e-92) place AA00454 in the YfbU family which is described as YfbU domain (PF03887)","","","","","","","","1","","","" "AA00455","319445","318672","774","ATGAAGCCATTTTTAATTAAACAGAGTGTCATTATGAAAACACAGAAACTTTTAGCCGCCTTATTGCTCGGTTCCGTCGTGCTGGCCGGCTGTTCATCCACCATCGATCCGGAAACCGGTGAACGCAAAGATGCGTTAGAAGGGTTTAACCGTAAAATGTGGGATTTCAACTATAATGTTGCCGATCCCTATGTGTTAAAGCCACTTGCCAAAGGCTGGAAAGAATATGTGCCAAGCCCGGTGCGCACCGGTGTGATTAATGTAGCGGATAATCTGGATGAACCGGCAAGTTTCGCCAACCGTTTGGTGCAGGGTGAATTCAAGCAAGCGCTGATTCACTTCAACCGTTTCTGGATTAATACGATTTTCGGTTTGGGCGGTTTAATTGACGTGGCAAGTTATAGCGATCCGCTGAAAAAACAAGGCGATAACCGTTTCGGCGATACCTTGGGCAGCTACGGCGTCGGCACCGGACCTTATGTGATGTTACCGTTATACGGACCGGCAACGCCACGCCAAGACATAGGCAACCTGGCGGATACCACTTACCCGATGCTTTTCCTGCTTGGTCCTTGGGGCTTTTTAAAAGCGGGTCTGCAAAGTATTGATACACGTGCTAAACTGATAGACAAAGAAGCCTTATTGGATCAGGCACAAGATCCGTATGTCGCTTTTCGTGAGGCTTATTTCCAAAATTTAGACCAGCGTATTAATGAGAGCAAAGGAAAACAAGCAGATTCAGAGTTATCACAAGATATACTCAATCAAATCAAT","","","29019","MKPFLIKQSVIMKTQKLLAALLLGSVVLAGCSSTIDPETGERKDALEGFNRKMWDFNYNVADPYVLKPLAKGWKEYVPSPVRTGVINVADNLDEPASFANRLVQGEFKQALIHFNRFWINTIFGLGGLIDVASYSDPLKKQGDNRFGDTLGSYGVGTGPYVMLPLYGPATPRQDIGNLADTTYPMLFLLGPWGFLKAGLQSIDTRAKLIDKEALLDQAQDPYVAFREAYFQNLDQRINESKGKQADSELSQDILNQIN","318673","","lipoprotein precursor","Periplasm, Outer membrane, Inner membrane","","
InterPro
IPR007428
Family
VacJ-like lipoprotein
PR01805\"[44-57]T\"[62-78]T\"[113-130]T\"[151-168]TVACJLIPOPROT
PF04333\"[38-238]TVacJ
noIPR
unintegrated
unintegrated
PS51257\"[1-31]TPROKAR_LIPOPROTEIN
signalp\"[1-33]?signal-peptide
tmhmm\"[15-35]?transmembrane_regions


","No hits to the COGs database.","","Residues 44 to 231 match (2e-84) PD:PD023788 which is described as LIPOPROTEIN PROTEOME COMPLETE VACJ PRECURSOR MEMBRANE OUTER SIGNAL HOMOLOG PROBABLE ","","","","","","","","","","","","Wed Dec 11 14:45:28 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00455 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 38 to 238 (E-value = 5.3e-115) place AA00455 in the VacJ family which is described as VacJ like lipoprotein (PF04333)","","","","","","","","1","","","" "AA00458","320944","319514","1431","ATGGTGTTTGAGCCCTTGGTGCTGAATACGGAATTCGGTCCACAGCCGTATTTGGCGGAAAGTTGGAGTATCTCGCCGGATGGCAAAACCTATATTTTCAAATTACGCAAAGATGTCAAATTCAGCGACGGCGAACCATTCAATGCTCAGGCGGTGAAGCTGAACATCGATGCCGTACTGGATAATTATACCCGTCATGCATGGTTGGAGCTGGTGCAACAAATCGACAGCGTGCGCGTTATTGACGATTACACCATTGAACTGAAACTCAAAAACGCCTATTACCCGACCCTCACCGAACTGAGCTTAACCCGCCCGTTTCGTTTTATTTCACCGAAATCGTTCATTGACGGCAAAACCAAAGACGGCGTGAAAGAATACGCCGGCACCGGTCCTTGGATGTTGGCGGCGCATGAAGAAAATCAATACGCCCGTTTTACCGTAAACCCGCATTATTGGGGCAAAAAGCCACAATTAAATGCTGTAGTGTGGAATGTCATATCTGATCGCCAAGCCATGTTGGCGGCATTGGAAAACGGCGATATTCAGTTAATTTTCGGTTCCGACGGCGACATGGTTAACATGGATGCCTTTGATAAGCTGAAATCCTCTAAAACGCTTTCCACTCTGTTAAGCGAACCCACCGCCACCCGTTTCATCATACTAAACAGCGGACGGGAAATTACCGGTGAATTGCCGGTGCGTGAAGCGTTGGAACACGCCGTCAACAAGCAAGGTATTGCGCAAACGGTGTTTGCCAATTCGGAAAGTGTGGCGCAGACGCTGATGTCAAAAAATGTCCCTTACAGTGATGTGGAAGTGAAAACCTTCGATTACGATATAGCTAAAGCTCGCCAACTATTGGATTTTGCAGGCTGGAAATTGCCGGCAGGGAAATCCGTGCGAGAAAAGCAAGATAAAGTCTTGTCATTGTTGTTTTCTTATAACGCCGATAATGCGGCGGAAAAAGAAATTGCCGAACTTATCCAGACGGATTTAAAAAACATCGGTGTGGATTTACGCATTGTTGGCGAAGAAAAAACGGCATATCTGGAACGGCAAAAAACCGGCGACTTTGATGTGCAATATTCCCTTTCCTGGGGCAAGCCTTATGAACCGGCGTCTTACATTTCTTCTTTCCGCAGCCCCGCCCATGCCGATTATCAGGCACAAAAAGGGCTGAAAAACAAACCGGAAATAAACCTAATTATCGGCGAATTATTGATCACGCCCGATGAAACGCTACGCAAGAAACTTTATGTGAATTTATGGAGGACACTGGCGGATCAGGCGGTTTATCTGCCGTTGACCTATGCCCGCACCAAAGCGGTATTCGCTAATGAATTAAAAGGTGTAGGGTTTAATCAGTCGCAATATGAAATCCCTTTTGAGCGAATGTATTTTTCGTCCGCACAAGCCCCCGCGACCAAA","","","60117","MVFEPLVLNTEFGPQPYLAESWSISPDGKTYIFKLRKDVKFSDGEPFNAQAVKLNIDAVLDNYTRHAWLELVQQIDSVRVIDDYTIELKLKNAYYPTLTELSLTRPFRFISPKSFIDGKTKDGVKEYAGTGPWMLAAHEENQYARFTVNPHYWGKKPQLNAVVWNVISDRQAMLAALENGDIQLIFGSDGDMVNMDAFDKLKSSKTLSTLLSEPTATRFIILNSGREITGELPVREALEHAVNKQGIAQTVFANSESVAQTLMSKNVPYSDVEVKTFDYDIAKARQLLDFAGWKLPAGKSVREKQDKVLSLLFSYNADNAAEKEIAELIQTDLKNIGVDLRIVGEEKTAYLERQKTGDFDVQYSLSWGKPYEPASYISSFRSPAHADYQAQKGLKNKPEINLIIGELLITPDETLRKKLYVNLWRTLADQAVYLPLTYARTKAVFANELKGVGFNQSQYEIPFERMYFSSAQAPATK","319515","","nickel-binding periplasmic protein","Periplasm","","
InterPro
IPR000914
Family
Bacterial extracellular solute-binding protein, family 5
PF00496\"[13-388]TSBP_bac_5
PS01040\"[19-41]TSBP_BACTERIAL_5
InterPro
IPR011980
Family
Nickel ABC transporter, periplasmic nickel-binding
TIGR02294\"[1-467]Tnickel_nikA: nickel ABC transporter, peripl
noIPR
unintegrated
unintegrated
G3DSA:3.10.105.10\"[217-438]Tno description
G3DSA:3.90.76.10\"[2-131]Tno description


","BeTs to 19 clades of COG0747COG name: ABC-type dipeptide/oligopeptide/nickel transport systems, periplasmic componentsFunctional Class: E,PThe phylogenetic pattern of COG0747 is ao-pkz-qvdrlbcefgh--uj-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 3.7e-13) to 2/3 blocks of the IPB000914 family, which is described as \"Bacterial extracellular solute-binding protein, family 5\". Interpro entry for IP:IPR000914. IPB000914A 16-23 0.3 IPB000914B 27-44 3.6e-10","Residues 309 to 378 match (3e-07) PD:PD001762 which is described as COMPLETE PROTEOME PERIPLASMIC OLIGOPEPTIDE BINDING ABC PRECURSOR SIGNAL PEPTIDE OLIGOPEPTIDE-BINDING ","","","","","Wed Feb 19 16:29:47 2003","","","","Wed Feb 19 16:29:47 2003","","","Tue Jan 21 13:18:02 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00458 is paralogously related to AA01573 (2e-28), AA01607 (5e-11) and AA02891 (8e-11).","","","","","","Residues 1 to 468 (E-value = 1.3e-71) place AA00458 in the SBP_bac_5 family which is described as Bacterial extracellular solute-binding proteins, family 5 (PF00496)","","","","","Navarro,C., Wu,L.F. and Mandrand-Berthelot,M.A.The nik operon of Escherichia coli encodes a periplasmic binding-protein-dependent transport system for nickelMol. Microbiol. 9 (6), 1181-1191 (1993)PubMed: 7934931","","Tue Jan 21 13:18:02 2003","1","","","" "AA00459","321149","320991","159","TTGATTTTAGGCATGATAGTTGTATCATGCCTTTTGTTTATAGATGGAGAGATTCATGAAAAAAATAACTTTAATTCTGACCGCACTTTTCACCGCCTTGCCAAGCTGGGCGAATATGCAAAACAACGAATTGGATTACGCCAGCACGAAAGATATTCG","","","6214","LILGMIVVSCLLFIDGEIHEKNNFNSDRTFHRLAKLGEYAKQRIGLRQHERYS","320991","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-16]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 15:57:45 2004","Sun Feb 22 15:57:45 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00459 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 15:57:45 2004","","","","","","","","","","","","","1","","","" "AA00460","322491","321163","1329","ATGTCTGAAATGACTCCGCGTGAAATAGTCTCTGAATTAGATCAACATATTATCGGGCAGAGCGAAGCGAAAAGAGCAGTGGCGATCGCCTTGAGAAATCGCTGGCGCAGAATGCAGTTGCAGGAGCCGATGCGTTATGAAGTGACACCGAAAAATATTTTAATGATTGGTCCGACCGGGGTGGGAAAAACCGAAATCGCCCGTCGCTTGGCAAAGTTAGCCAATGCTCCGTTCATTAAAGTGGAAGCCACCAAATTTACCGAAGTAGGCTATGTGGGGAAAGAAGTGGATTCCATTATCCGCGACTTAACCGACAGCGCTATGAAACTGGTGCGTCAGACGGAAATTGAAAAAAATCGCGTGAAAGCGGAAGAAGCGGCGGAAGAACGTATTTTAGACGCCTTATTGCCGGCGGCGAAAAACCAATGGGGCGAAATGGAAAACCGCGATGCGCAAAATAATACGCGCCAGATTTTCCGTAAGAAATTACGTGAAGGTGAGCTTGATGATAAAGAAGTGGAGATTGATGTCGCCGGTGTGCCGATGGGCGTGGAAATTATGGCGCCTCCGGGCATGGAAGACATGACCAGCCAGCTGCAGTCCATGTTCCAGAATCTGTCCAGCGGGCAAACCAAAAAGCGCAAAATGAAAATTAAGGATGCGTTAAAAACCTTAGTTGATGACGAGGCGGCGAAATTGGTGAATCCGGAAGAGCTGAAACAAAAAGCTATTGATGCGGTGGAACAAAACGGTATCGTGTTTATTGATGAAATTGATAAAATCTGTAAGAAAGGCGAATATAGCGGGGCGGATGTGTCCCGTGAAGGTGTGCAGCGCGACTTGCTACCACTGGTGGAAGGTTCTACCGTTAACACCAAGCACGGCATAGTGAAAACCGATCATATTCTGTTTATTGCCTCCGGCGCATTCCAAGTGGCGCGCCCGTCCGATTTGATCCCGGAATTACAGGGGCGTTTGCCGATTCGCGTGGAATTGTCGGCACTCACCGCCGGTGATTTTGAGCGCATTCTGACCGAACCGAATGCCTCTTTAACGGAGCAATACAAAGCATTAATGGCGACGGAAGGCGTGAACATTGAATTCACCCAAGATGCCATTAAGAAAATCGCCGAGGCGGCATTCCGCGTGAATGAGAAAACCGAGAACATCGGCGCCCGCCGGTTGCATACGGTGATGGAACGTTTGATGGATAAAATTTCCTTCAACGCCAGCGATATGGACGGACAAACTGTCAGCATTGACGCGGCGTATGTTAGCGAAGCGCTCGGCGATGTCATCGAAAACGAAGATTTAAGCCGCTTTATTCTT","","","49511","MSEMTPREIVSELDQHIIGQSEAKRAVAIALRNRWRRMQLQEPMRYEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYVGKEVDSIIRDLTDSAMKLVRQTEIEKNRVKAEEAAEERILDALLPAAKNQWGEMENRDAQNNTRQIFRKKLREGELDDKEVEIDVAGVPMGVEIMAPPGMEDMTSQLQSMFQNLSSGQTKKRKMKIKDALKTLVDDEAAKLVNPEELKQKAIDAVEQNGIVFIDEIDKICKKGEYSGADVSREGVQRDLLPLVEGSTVNTKHGIVKTDHILFIASGAFQVARPSDLIPELQGRLPIRVELSALTAGDFERILTEPNASLTEQYKALMATEGVNIEFTQDAIKKIAEAAFRVNEKTENIGARRLHTVMERLMDKISFNASDMDGQTVSIDAAYVSEALGDVIENEDLSRFIL","321164","","ATP-dependent ClpY-related protease; heat shock protein","Cytoplasm","","
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[49-332]TAAA
InterPro
IPR004491
Family
Heat shock protein HslU
PTHR11262:SF3\"[3-221]T\"[303-443]TATP-DEPENDENT HSL PROTEASE ATP-BINDING SUBUNIT HSLU
TIGR00390\"[4-443]ThslU: heat shock protein HslVU, ATPase subu
InterPro
IPR013093
Domain
ATPase AAA-2
PF07724\"[49-100]T\"[170-329]TAAA_2
noIPR
unintegrated
unintegrated
G3DSA:1.10.8.60\"[335-443]Tno description
G3DSA:3.40.50.300\"[2-333]Tno description
PTHR11262\"[3-221]T\"[303-443]THSL AND CLP PROTEASE


","BeTs to 12 clades of COG1220COG name: ATP-dependent protease, ATPase subunitFunctional Class: OThe phylogenetic pattern of COG1220 is -------qv---b-efghs-ujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 4.7e-05) to 1/5 blocks of the IPB000623 family, which is described as \"Shikimate kinase\". Interpro entry for IP:IPR000623. IPB000623A 53-82 4.7e-05Significant hit ( 6e-05) to 2/8 blocks of the IPB001984 family, which is described as \"ATP-dependent serine proteases, Lon family\". Interpro entry for IP:IPR001984. IPB001984C 50-86 0.00022 IPB001984E 382-405 1.3e+02","Residues 350 to 434 match (8e-15) PD:PD336058 which is described as ATP-BINDING PROTEASE SUBUNIT CLP ATP-DEPENDENT PROTEOME COMPLETE CLPX CHAPERONE ZINC-FINGER ","","","","","","","","","","","","Thu Jan 23 07:56:33 2003","","","Tue Mar 2 14:02:23 2004","","yes","Fri Feb 20 15:41:32 MST 1998","AA00460 is paralogously related to AA00120 (4e-19), AA02289 (5e-07) and AA01211 (3e-06).","Tue Mar 2 14:02:23 2004","","","","","Residues 52 to 382 (E-value = 8.7e-08) place AA00460 in the AAA family which is described as ATPase family associated with various cellular activities (AAA) (PF00004)","Tue Mar 2 14:02:23 2004","","","","ochtler,M., Hartmann,C., Song,H.K., Bourenkov,G.P.,Bartunik,H.D. and Huber,R. he structures of HsIU and the ATP-dependent protease HsIU-HsIVNature 403 (6771), 800-805 (2000) PubMed: 10693812 Sousa MC, Kessler BM, Overkleeft HS, McKay DB. Crystal structure of HslUV complexed with a vinyl sulfoneinhibitor: corroboration of a proposed mechanism of allostericactivation of HslV by HslU. J Mol Biol. 2002 May 3;318(3):779-85. PMID: 12054822 Ramachandran R, Hartmann C, Song HK, Huber R, Bochtler M. Functional interactions of HslV (ClpQ) with the ATPase HslU(ClpY). Proc Natl Acad Sci U S A. 2002 May 28;99(11):7396-401. PMID: 12032294 Chuang,S.E., Burland,V., Plunkett,G. III., Daniels,D.L. andBlattner,F.R. Sequence analysis of four new heat-shock genes constitutingthe hslTS/ibpAB and hslVU operons in Escherichia coli. Gene. 134(1): 1-6, 1993. PubMed: 8244018. Rohrwild,M., Coux,O., Huang,H.C., Moerschell,R.P., Yoo,S.J.,Seol,J.H., Chung,C.H. and Goldberg,A.L. HslV-HslU: A novel ATP-dependent protease complex inEscherichia coli related to the eukaryotic proteasome. Proc. Natl. Acad. Sci. U.S.A. 93 (12), 5808-5813, 1996. PubMed: 8650174 ","","Wed Dec 11 15:15:47 2002","1","","","" "AA00461","323039","322515","525","ATGACAACGATTGTAAGTGTACGTCGCAACGGTAAAGTGGTTGTCGGCGGGGATGGACAGGTTTCTCTGGGCAATACGGTGATGAAGGGTAACGCGCGCAAGGTGCGTCGTTTGTATAACGGTAAAGTGTTGGCGGGATTTGCCGGCGGCACGGCGGATGCCTTTACGCTATTTGAATTATTTGAACGTAAACTGGAAATGCACCAAGGGCACTTGCTGAAAAGTGCGGTGGAATTGGCGAAAGATTGGCGCACCGACCGCGCATTGCGGAAGTTGGAAGCCATGCTGATTGTGGCAGATGAAAAAGAAAGTCTGATTATCACCGGTATCGGCGATGTGGTGCAACCGGAAGAAGATCAGATTCTTGCCATCGGTTCCGGCGGTAACTACGCTTTATCCGCCGCTCGTGCGTTGGTGGAAAACACCGATTTATCCGCTCGCGAAATTGTGGAAAAATCACTGAAAATTGCCGGTGAGATTTGCGTGTTCACCAACACTAATTTCACCATTGAAGAATTACCGAAT","","","19119","MTTIVSVRRNGKVVVGGDGQVSLGNTVMKGNARKVRRLYNGKVLAGFAGGTADAFTLFELFERKLEMHQGHLLKSAVELAKDWRTDRALRKLEAMLIVADEKESLIITGIGDVVQPEEDQILAIGSGGNYALSAARALVENTDLSAREIVEKSLKIAGEICVFTNTNFTIEELPN","322516","","heat shock protein; protease","Cytoplasm","","
InterPro
IPR001353
Family
20S proteasome, A and B subunits
PF00227\"[1-173]TProteasome
noIPR
unintegrated
unintegrated
G3DSA:3.60.20.10\"[2-175]Tno description


","BeTs to 13 clades of COG0638COG name: Proteasome protease subunitFunctional Class: OThe phylogenetic pattern of COG0638 is aompkzyqv-r-b-efghs-ujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-07) to 2/3 blocks of the IPB000243 family, which is described as \"Proteasome B-type subunit\". Interpro entry for IP:IPR000243. IPB000243A 1-40 8.1e-06 IPB000243B 107-136 5.3","Residues 2 to 173 match (5e-75) PD:PD008385 which is described as PROTEASE COMPLETE PROTEOME HSLV HYDROLASE 3.4.25.- ATP-DEPENDENT HEAT SHOCK 3.4.99.- ","","","","","","","","","","","","Thu Jan 23 07:57:26 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00461 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 173 (E-value = 8.3e-44) place AA00461 in the Proteasome family which is described as Proteasome A-type and B-type (PF00227)","","","","","Ramachandran R, Hartmann C, Song HK, Huber R, Bochtler M. Functional interactions of HslV (ClpQ) with the ATPase HslU(ClpY). Proc Natl Acad Sci U S A. 2002 May 28;99(11):7396-401. PMID: 12032294 Seong IS, Kang MS, Choi MK, Lee JW, Koh OJ, Wang J, Eom SH,Chung CH. The C-terminal tails of HslU ATPase act as a molecular switchfor activation of HslV peptidase. J Biol Chem. 2002 Jul 19;277(29):25976-82. PMID: 12011053","","Wed Dec 11 15:20:10 2002","1","","","" "AA00463","323254","323958","705","ATGAAAAACCTCGTTAAATTATCCCTCATCGCCATGCTAACAGCCGCAACCCTTCCGGCAATGGCGGCAAAAAGTGAACCCTATACCCACCAAGGCACCAACGCCCGAGAAATGTTGGTAGAACAACCGATTCACTGGATTTCCGTTGACCAATTGAAAAAAGAATTGGAAGGCAAAGCACCGATGAATGTGAGCTTTGATATTGACGACACCGTATTATTCAGCAGCCCGTGTTTTTATCACGGACAACAAAAATACTCACCGGGTAAACAGGATTATTTGAAAAATCAGGATTTCTGGAACGAAGTAAACGCCGGTTGTGACCAATATTCCATTCCGAAACAAATTGCGGTGGATTTAATCAATATGCACCAAGAGCGCGGCGACCAAATTTATTTCATCACCGGTCGTACCGCCGGGGACAAAGACGGCGTGCCCCCGGTGTTACAAAAAGCCTTTAGTATCAAAAACATGCATCCGGTTGAATTCATGGGCGGACGTGATCGCACCACCAAATACAACAAAACCCCGGGCATTATCGAACACAAAGTCACCATTCACTACGGCGACAGCGACGATGACATTCTTGCCGCCAAAGAAGCCGGCGTTCGTGGCATCCGCCTCATGCGCGCCGCCAACTCCACATATCAACCGATGCCAACCCTCGGTGGCTACGGCGAAGAAGTGTTAATTAACTCAAGCTAC","","","26274","MKNLVKLSLIAMLTAATLPAMAAKSEPYTHQGTNAREMLVEQPIHWISVDQLKKELEGKAPMNVSFDIDDTVLFSSPCFYHGQQKYSPGKQDYLKNQDFWNEVNAGCDQYSIPKQIAVDLINMHQERGDQIYFITGRTAGDKDGVPPVLQKAFSIKNMHPVEFMGGRDRTTKYNKTPGIIEHKVTIHYGDSDDDILAAKEAGVRGIRLMRAANSTYQPMPTLGGYGEEVLINSSY","323959","","class B acid phosphatase","Periplasm","","
InterPro
IPR005519
Family
Acid phosphatase (Class B)
PF03767\"[55-143]TAcid_phosphat_B
InterPro
IPR010025
Family
HAD-superfamily phosphatase, subfamily IIIB, AphA
TIGR01672\"[1-235]TAphA: HAD superfamily (subfamily IIIB) phos
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1000\"[24-235]Tno description
signalp\"[1-22]?signal-peptide


","No hits to the COGs database.","","Residues 2 to 235 match (1e-111) PD:PD017140 which is described as PHOSPHATASE ACID B PROTEOME COMPLETE CLASS HYDROLASE PERIPLASMIC SIGNAL PRECURSOR ","","","","","Mon Feb 17 07:12:16 2003","","","","","","","Wed Dec 11 15:32:16 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00463 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 11 to 219 (E-value = 2.5e-11) place AA00463 in the Acid_phosphat_B family which is described as HAD superfamily, subfamily IIIB (Acid phosphatase) (PF03767)","","","","","Thaller,M.C., Schippa,S., Bonci,A., Berlutti,F., Selan,L. andRossolini,G.M.Genetic rearrangements in the tyrB-uvrA region of theenterobacterial chromosome: a potential cause for different class B acid phosphatase regulation in Salmonella enterica and Escherichia coliFEMS Microbiol. Lett. 181 (1), 17-23 (1999)PubMed: 10564784Thaller,M.C., Schippa,S., Bonci,A., Cresti,S. and Rossolini,G.M.Identification of the gene (aphA) encoding the class B acidphosphatase/phosphotransferase of Escherichia coli MG1655 and characterization of its productFEMS Microbiol. Lett. 146 (2), 191-198 (1997)PubMed: 9011040Thaller,M.C., Lombardi,G., Berlutti,F., Schippa,S. andRossolini,G.M.Cloning and characterization of the NapA acidphosphatase/phosphotransferase of Morganella morganii:identification of a new family of bacterialacid-phosphatase-encoding genesMicrobiology 141 (Pt 1), 147-154 (1995)PubMed: 7894706","","Sun Feb 16 16:45:44 2003","1","","","" "AA00464","324165","324052","114","TTGACATTTGGAATTCTCCGTTTTGCTGAAAACAACATTGATAGAGACGGATTAGGCGTTGAACGCTTCTACGTCCCGGGTCGCAACTCTGCCGCTTCTATCGAAATCTGCTTC","","","4244","LTFGILRFAENNIDRDGLGVERFYVPGRNSAASIEICF","324052","","conserved hypothetical protein","Cytoplasm","This sequence is weakly similar to gi|15602606, an unknown from P.multocida.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:00:13 2004","Sun Feb 22 16:00:13 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00464 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:00:13 2004","","","","","","","","","","","","","1","","","" "AA00465","324660","324346","315","ATGTTATCGAAAGCACGTTTAGAGCAAATCACCGAAATGGAAGCCATTTTGAGCGAATCCAATGATTTTCTTGCTGAAGCGGAAACGTTTTTTGAAAAATGGCAGGCGTTTTTACCAAAAATGGAAGCCTTAGAACGTTATTATTTTGACGGCGATTGGCGCGAGGATTATGAAGCCTATGGGCGTGGCGATATTCCGAAAGAGTTGCCTTGCGGCGTATTGGGTGAAGATCCGATTTTTAATGCGAGTGTGACACAACGGGATTTAGCGGTACGGTGGCTGAAATTAATCAGCCGGATTTTAGACAACAATAAG","","","12281","MLSKARLEQITEMEAILSESNDFLAEAETFFEKWQAFLPKMEALERYYFDGDWREDYEAYGRGDIPKELPCGVLGEDPIFNASVTQRDLAVRWLKLISRILDNNK","324347","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Dec 11 15:33:12 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00465 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00467","324938","324705","234","ATGCCGGAAAAGCAAAACGTGTATGATAAAGTGGTTTTTTTATGCTTTATCAAAAACTGTGCGGTAACTCCTGCAGTCTGGAATGAAACCGTAGTTACAGGGCAAGTCTTAGATTTAGGCTGTGGTTGTGGTGAGCGTCTTAAACTGTATTTGGAACCGAGGGAACTAAACAATTTGAGTCTGTGCAGTACAGAGCCCAATATTTTCTCTGTCCAAGTTGTAGGAGGGCACTTT","","","8659","MPEKQNVYDKVVFLCFIKNCAVTPAVWNETVVTGQVLDLGCGCGERLKLYLEPRELNNLSLCSTEPNIFSVQVVGGHF","324705","","hypothetical protein","Cytoplasm, Outer membrane","No sequence similarities are found in the NR database.","No hits reported.","BeTs to 5 clades of COG0500COG name: SAM-dependent methyltransferasesFunctional Class: Q,RThe phylogenetic pattern of COG0500 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Sun Feb 22 16:01:51 2004","Sun Feb 22 16:01:51 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00467 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:01:51 2004","","","","","","","","","","","","","1","","","" "AA00468","326184","324943","1242","ATGACGACTGCAAAACGCCCTTCGTTACTTGGCGGCGCGATGATTATCACCGGTACGGCGATCGGTGCGGGAATGCTCGCCAATCCCACCTCCACCGCCGGCATTTGGTTTGCCGGTTCCATCGTCATCTTAATTTACACCTGGTTCTGCATGACCACATCAGGCTTGATGATTTTAGAAGCTAACTTACATTATCCCACCGGCGCCAGTTTCGACACTATCGTCACCGATTTGTTGGGTAGAGGCTGGAATGTCATTAACGGTTTGTCCGTGGCATTCGTACTGTATATTTTAACGTATGCCTATATCACCTCAGGTGGCAGCATTACAGAAAGTTTCCTCAATCAATTGGGTGAAAACGTAGAAGTCGGGCGCAGCGCAGGTTCGCTGATTTTCTGCATTGTTTTGGCAGCGTTTGTATGGCTCTCCACAAAAGCCGTTGATCGCTTCAGTACCGTGCTTATCGCCGGCATGGTGATTTCCTTTTTTCTGTCCACCGCCGGATTATTAAGCTCTGTGAAAATCGACGTTTTATTTAACACCGTCGCACAAGGCGAACAGCAATATTTACCTTATATTTTGACCGCACTTCCCGTGTGTTTGGTGTCTTTCGGCTTCCACGGCAACGTGCCGAGCCTGGTGAAATATTACGATCGTGACGGCAACCGCGTGATGAAATCCATTTTCCTCGGCACCGGTTTGGGGCTTGTCGTTTACATTTTATGGCAACTTGCCATTCAAGGTAACTTACCGCGCGCCGAGTTCGCCCCGGTCATCGCCAAGGGCGGTGACGTCGCGGCGTTACTGGAAGCGTTGAGCAAATACATTCAAACGGATTACATCGGTATTATTCTGAATTTCTTCGCCTATATGGCAATCGCCAGTTCCTTCCTCGGCGTCACCTTAGGCTTGTTCGATTACATCGCCGATCTATGTAAATTCGATGACAGCCGTTTAGGACGCACCAAAACCACATTGGTTACCTTCCTGCCACCTCTATTGCTGAGCTTGCAATTTCCTTTCGGTTTCGTGCTTGCCATCGGTTACGCTGGTTTGGCAGCCACCATTTGGGCGGCAATTGTGCCCGCGTTATTGGCAAAAGCCAGCCGCAAAAAATTCCCGAACGCGACATATCGCGTGCATGGCGGCAACTTCATGATTTATTTCGTGATCCTGTTCGGGTTATTGAATATCTTCGTGCAAGTGGCATTGCAATTCGGCTGGCTCTCGGATTTCAAAGGA","","","44696","MTTAKRPSLLGGAMIITGTAIGAGMLANPTSTAGIWFAGSIVILIYTWFCMTTSGLMILEANLHYPTGASFDTIVTDLLGRGWNVINGLSVAFVLYILTYAYITSGGSITESFLNQLGENVEVGRSAGSLIFCIVLAAFVWLSTKAVDRFSTVLIAGMVISFFLSTAGLLSSVKIDVLFNTVAQGEQQYLPYILTALPVCLVSFGFHGNVPSLVKYYDRDGNRVMKSIFLGTGLGLVVYILWQLAIQGNLPRAEFAPVIAKGGDVAALLEALSKYIQTDYIGIILNFFAYMAIASSFLGVTLGLFDYIADLCKFDDSRLGRTKTTLVTFLPPLLLSLQFPFGFVLAIGYAGLAATIWAAIVPALLAKASRKKFPNATYRVHGGNFMIYFVILFGLLNIFVQVALQFGWLSDFKG","324944","","tryptophan-specific transport protein / tyrosine-specific transport protein","Inner membrane, Cytoplasm","","
InterPro
IPR002091
Family
Aromatic amino acid permease
PR00166\"[14-37]T\"[41-60]T\"[86-106]T\"[153-173]T\"[192-214]T\"[231-250]T\"[292-311]T\"[326-344]T\"[347-366]TAROAAPRMEASE
PF03222\"[5-401]TTrp_Tyr_perm
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[254-411]Tno description
InterPro
IPR013059
Family
Tryptophan/tyrosine transporter
TIGR00837\"[11-394]TaraaP: aromatic amino acid transport protei
InterPro
IPR013061
Family
Tryptophan/tryrosine permease
PS00594\"[21-37]TAROMATIC_AA_PERMEASE_1
noIPR
unintegrated
unintegrated
signalp\"[1-55]?signal-peptide
tmhmm\"[9-27]?\"[33-51]?\"[84-104]?\"[123-143]?\"[153-173]?\"[189-207]?\"[228-246]?\"[288-308]?\"[323-343]?\"[349-369]?\"[384-404]?transmembrane_regions


","BeTs to 6 clades of COG0814COG name: Amino acid permeasesFunctional Class: EThe phylogenetic pattern of COG0814 is ------y-------efgh-nu--i--Number of proteins in this genome belonging to this COG is","Significant hit (7.9e-144) to 6/6 blocks of the IPB002091 family, which is described as \"Aromatic amino acids permease\". Interpro entry for IP:IPR002091. IPB002091A 12-55 1.3e-31 IPB002091B 73-110 9.1e-24 IPB002091C 198-213 8.5e-12 IPB002091D 228-270 1.9e-22 IPB002091E 288-312 2.3e-16 IPB002091F 320-370 6.9e-32","Residues 29 to 87 match (2e-13) PD:PD551562 which is described as PROTEOME COMPLETE TRYPTOPHAN-SPECIFIC PERMEASE TRYPTOPHAN MEMBRANE INNER TNAB TRANSMEMBRANE AMINO-ACID ","","","","","","","","","","","","Wed Dec 11 15:42:01 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00468 is paralogously related to AA01245 (7e-62), AA01704 (8e-60), AA02973 (1e-59) and AA00092 (1e-05).","","","","","","Residues 5 to 401 (E-value = 1e-221) place AA00468 in the Trp_Tyr_perm family which is described as Tryptophan/tyrosine permease family (PF03222)","","","","","Heatwole,V.M. and Somerville,R.L. Cloning, nucleotide sequence, and characterization of mtr, thestructural gene for a tryptophan-specific permease ofEscherichia coli K-12 J. Bacteriol. 173 (1), 108-115 (1991) PubMed: 1987112 Sarsero,J.P., Wookey,P.J. and Pittard,A.J. Regulation of expression of the Escherichia coli K-12 mtr geneby TyrR protein and Trp repressor J. Bacteriol. 173 (13), 4133-4143 (1991) PubMed: 2061290 Heatwole,V.M. and Somerville,R.L. The tryptophan-specific permease gene, mtr, is differentially regulated by the tryptophan and tyrosine repressors inEscherichia coli K-12 J. Bacteriol. 173 (11), 3601-3604 (1991) PubMed: 1904443 Sarsero,J.P. and Pittard,A.J. Membrane topology analysis of Escherichia coli K-12 Mtrpermease by alkaline phosphatase and beta-galactosidasefusions J. Bacteriol. 177 (2), 297-306 (1995) PubMed: 7814318 Wookey,P.J. and Pittard,A.J. DNA sequence of the gene (tyrP) encoding the tyrosine-specifictransport system of Escherichia coli. J. Bacteriol. 170(10): 4946-4949.1988. PubMed: 3049553. Sarsero,J.P., Wookey,P.J., Gollnick,P., Yanofsky,C. andPittard,A.J. . A new family of integral membrane proteins involved intransport of aromatic amino acids in Escherichia coli. J. Bacteriol. 173(10): 3231-3234.1991 PubMed: 2022620.","","Wed Dec 11 15:39:44 2002","1","","","" "AA00469","326346","326870","525","ATGGGCTTAGAAAGAGTACCGGCAGGTAAAGCATTACCTGATGATATTTATGTCGTCATCGAAATCCCTGCAAACTCAGATCCGATTAAATACGAAGTTGACAAAGAAACCGGCACATTATTTGTGGACCGTTTCATGGCAACGGCAATGTTCTATCCTGCCAACTATGGTTATGTGAACAACACCCTTTCTTCCGACGGCGACCCGGTTGACGTTTTAGTGCCGACTCCGTATCCGTTACAACCGGGTTCGGTCATTCGTTGCCGTCCTGTAGGTGTGTTAAAGATGACCGATGAAGCCGGCGGCGATGCGAAAGTGGTTGCCGTACCGCACACCAAATTGAGCAAAGAATATGATCACATTCAAGATGTAGGCGATTTACCTGCATTGTTAAAAGCACAAATCCAGCACTTCTTCGAAAGCTATAAAGCTTTAGAAACAGGTAAATGGGTGAAAGTGGAAGGCTGGGAAGGCGTTGAAGCCGCCCGTCATGAAATCCTTGATTCATTTGAACGTGCAAAAAAA","","","19351","MGLERVPAGKALPDDIYVVIEIPANSDPIKYEVDKETGTLFVDRFMATAMFYPANYGYVNNTLSSDGDPVDVLVPTPYPLQPGSVIRCRPVGVLKMTDEAGGDAKVVAVPHTKLSKEYDHIQDVGDLPALLKAQIQHFFESYKALETGKWVKVEGWEGVEAARHEILDSFERAKK","326871","","inorganic pyrophosphatase, chain A","Cytoplasm","","
InterPro
IPR008162
Family
Inorganic pyrophosphatase
PD002014\"[30-141]TIPYR_HAEDU_Q7VPC0;
G3DSA:3.90.80.10\"[2-175]Tno description
PTHR10286\"[36-172]TINORGANIC PYROPHOSPHATASE
PF00719\"[17-175]TPyrophosphatase
PS00387\"[66-72]?PPASE


","BeTs to 22 clades of COG0221COG name: Inorganic pyrophosphataseFunctional Class: CThe phylogenetic pattern of COG0221 is -ompkzyq-dr-bcefghsnujxi-wNumber of proteins in this genome belonging to this COG is","Significant hit ( 6.5e-37) to 2/2 blocks of the IPB001596 family, which is described as \"Inorganic pyrophosphatase\". Interpro entry for IP:IPR001596. IPB001596A 43-96 4e-31 IPB001596B 132-143 0.00019","Residues 6 to 38 match (5e-09) PD:PD095158 which is described as HYDROLASE INORGANIC PYROPHOSPHATASE PROTEOME COMPLETE MAGNESIUM PPASE PYROPHOSPHATE PHOSPHO- SOLUBLE ","","","","","","","","","","","","Wed Dec 11 15:43:47 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00469 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 17 to 175 (E-value = 5.6e-58) place AA00469 in the Pyrophosphatase family which is described as Inorganic pyrophosphatase (PF00719)","","","","","Samygina VR, Popov AN, Rodina EV, Vorobyeva NN, Lamzin VS,Polyakov KM, Kurilova SA, Nazarova TI, Avaeva SM. The structures of Escherichia coli inorganic pyrophosphatasecomplexed with Ca(2+) or CaPP(i) at atomic resolution andtheir mechanistic implications. J Mol Biol. 2001 Nov 30;314(3):633-45. PMID: 11846572 Hyytia T, Halonen P, Salminen A, Goldman A, Lahti R, CoopermanBS. Ligand binding sites in Escherichia coli inorganicpyrophosphatase: effects of active site mutations. Biochemistry. 2001 Apr 17;40(15):4645-53. PMID: 11294631","","Wed Jan 22 17:53:37 2003","1","","","" "AA00470","326949","327719","771","ATGTCTAGATTAGGCAAAATGCTCGTATTAGTTTCAACTATCGGCATCTTAACCGCTTGTGCGGATTCTGCTTCCATTAACCAAGAAGCGGCTACGGGCTACGCACAAATGATCAGCCAGGCGCAAGCACACAGGCAAGTGGATAACAAATCAAAAACTGCACAGCGTGTACGCAAAATCTTTAACAAGATGGTGCCGTATGCCAATGCCGAAAACAAAACAGGACAAGCCTTTGACTGGCAAATTTCTGTCATCAAGTCCAAAGAACTTAACGCTTGGGCGATGCCCGGCGGGAAAATGGCGTTTTACACCGGTTTAGTAGATAACTTACGTTTAACCGATGATGAAATCGCCACCGTAATGGGACATGAAATGGCACATGCCTTAAAAGAACATGGTAAGAAAAAAGCCAATATCGGTCAATTCACCGATGTTGTCGCCAGTGTTGCACAAGAAGCGTTAGCCACGAAAATCGGCGCTGACAGCAGTTCAATGGTAGTGGGCTTAGCCAAAGACTGGGGCTTGGACAAACCGTATTCCCGTAGCGCGGAAACCGAAGCCGATGAAGTCGGTTTAATATTAATGGCAAAATCCGGTTACAACCCTGAAGCGGCACCGAAATTGTGGGACAAAATGCAAAAAGCCTCAACCGGCTCTCAAGGTATCTTAGACAAATTAAGTTCAACTCACCCAAGCGACAAAGATCGCCAAGAGAACTTAGTACGCTTAATGCCTGAAGCGGTTGCCTTATACAAACAAAGCAGAAAACGC","","","28003","MSRLGKMLVLVSTIGILTACADSASINQEAATGYAQMISQAQAHRQVDNKSKTAQRVRKIFNKMVPYANAENKTGQAFDWQISVIKSKELNAWAMPGGKMAFYTGLVDNLRLTDDEIATVMGHEMAHALKEHGKKKANIGQFTDVVASVAQEALATKIGADSSSMVVGLAKDWGLDKPYSRSAETEADEVGLILMAKSGYNPEAAPKLWDKMQKASTGSQGILDKLSSTHPSDKDRQENLVRLMPEAVALYKQSRKR","327720","","conserved hypothetical protein (possible Zn-dependent protease with chaperone function)","Periplasm, Outer membrane","","
InterPro
IPR001915
Family
Peptidase M48, Ste24p
PF01435\"[65-245]TPeptidase_M48
InterPro
IPR006025
Binding_site
Peptidase M, neutral zinc metallopeptidases, zinc-binding site
PS00142\"[120-129]?ZINC_PROTEASE
noIPR
unintegrated
unintegrated
PTHR22726\"[7-254]TOMA1 HOMOLOG, ZINC METALLOPEPTIDASE
PS51257\"[1-20]TPROKAR_LIPOPROTEIN
signalp\"[1-23]?signal-peptide


","No hits to the COGs database.","","Residues 79 to 232 match (8e-31) PD:PD002296 which is described as PROTEOME COMPLETE PROTEASE SHOCK HEAT HTPX HYDROLASE 3.4.24.- METALLOPROTEASE ZINC ","","","","","","","","","","","","Wed Dec 11 15:47:55 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00470 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 65 to 245 (E-value = 2.1e-59) place AA00470 in the Peptidase_M48 family which is described as Peptidase family M48 (PF01435)","","","","","","","","1","","","" "AA00471","328402","329043","642","ATGAATCAGTCATTATTATCCCCGTTCGGCACCGCTGAAGAACGTGTCAAAGCCGCCATCGACGCCTTCAAACAAGGCGACGGCGTCCTTGTGTTAGACGATGAGAATCGCGAAAACGAAGGCGATTTAATCTTCCCCGCCGAAACCATTACCGCCGCCCAAATGGCAAAACTTATCCGCTACGGCAGCGGCATCGTGTGTTTATGTATCACCGACGAATTGTGCAAACAACTGGATTTACCTCCGATGGTAAACCACAACACCAGCGTGAATAAAACTGCCTTTACCGTCACCATTGAAGCTGCCGAAGGGGTTTCCACCGGGGTGTCCGCCGCCGACCGCGTGACCACCATTAAAGCCGCCATTGCCGACGGCGCCAAACCGAGCGATTTACACCGCCCGGGACACGTTTTCCCATTACGTGCCGCCCCGAACGGTGTACTACAACGCAACGGTCACACAGAAGCGGCGGTGGATTTGGCACGTTTAGCAGGCTATAAAGAAGCGGGCGTGATCTGCGAAATCACCAACGACGACGGCACCATGGCAAGAGCGCCGGAACTGGTGGAATTCGTGAAACAACAGGGTTATGCGATTGTGACTATTGAAGACTTGATTACATACCGTCAGAAATATCACTGC","","","22998","MNQSLLSPFGTAEERVKAAIDAFKQGDGVLVLDDENRENEGDLIFPAETITAAQMAKLIRYGSGIVCLCITDELCKQLDLPPMVNHNTSVNKTAFTVTIEAAEGVSTGVSAADRVTTIKAAIADGAKPSDLHRPGHVFPLRAAPNGVLQRNGHTEAAVDLARLAGYKEAGVICEITNDDGTMARAPELVEFVKQQGYAIVTIEDLITYRQKYHC","329044","","3,4-dihydroxy-2-butanone 4-phosphate synthase; GTP cyclohydrase II","Cytoplasm","","
InterPro
IPR000422
Domain
3,4-Dihydroxy-2-butanone 4-phosphate synthase
PD003034\"[9-212]TRIBB_PASMU_P57940;
PF00926\"[16-211]TDHBP_synthase
TIGR00506\"[12-209]TribB: 3,4-dihydroxy-2-butanone 4-phosphate
noIPR
unintegrated
unintegrated
G3DSA:3.90.870.10\"[2-211]Tno description
PTHR21327\"[43-211]TGTP CYCLOHYDROLASE II-RELATED
PTHR21327:SF1\"[43-211]TGTP CYCLOHYDROLASE II


","No hits to the COGs database.","Significant hit ( 1.2e-84) to 4/4 blocks of the IPB000422 family, which is described as \"3,4-Dihydroxy-2-butanone 4-phosphate synthase\". Interpro entry for IP:IPR000422. IPB000422A 19-66 6.6e-29 IPB000422B 91-102 0.00012 IPB000422C 107-118 5.7e-06 IPB000422D 130-180 2.4e-41","","","","","","","","","","","","","Thu Jan 23 09:28:38 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00471 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 16 to 211 (E-value = 1.3e-126) place AA00471 in the DHBP_synthase family which is described as 3,4-dihydroxy-2-butanone 4-phosphate synthase (PF00926)","","","","","Fuller,T.E. and Mulks,M.H. Characterization of Actinobacillus pleuropneumoniae riboflavinbiosynthesis genes J. Bacteriol. 177 (24), 7265-7270 (1995) PubMed: 8522537 ","","Wed Dec 11 15:51:35 2002","1","","","" "AA00473","330137","329136","1002","ATGAGCAAACCTATCGTGTTCAGCGGTGTACAGCCATCGGGTGAATTGACTATCGGTAACTACCTCGGTGCGTTACGTCAGTGGGTAAAAATGCAGGATGATTACGAATGCCTGTTTTGTATCGTGGATCAGCACGCCATCACCGTGCGCCAGGATCCGGCGGCATTACGCAAAGCGACCTTAGACGTGTTGGCGCTCTATTTAGCCTGCGGCATCGACCCGGCGAAATCCACCATTTTCATTCAATCCCATGTGCCGGAACACGCGCAACTGGCTTGGGTGTTAAATTGCTACACCTATTTCGGCGAAATGAGCCGCATGACCCAATTTAAAGATAAATCCACCCGTTATGCGGAAAATGTCAACGTGGGTTTGTTCACTTATCCGGTGTTAATGGCGGCGGATATTTTGCTTTACCAAGCCAATCAAGTGCCGGTGGGCGAAGACCAAAAACAACATTTGGAAATCACCCGCGACATCGCCCAACGTTTTAACGCCTTATACGGACCGCACTTTGCCGTGCCGGAAGTGTTTATCCCGAAAGCGGGCGCGCGCGTGATGTCATTGTTGGAACCGGAAAAGAAAATGTCCAAATCCGACGAAAACCGCAACAACGTCATCGGCTTATTGGAAGACCCGAAAGCGGTCGCCAAGAAAATCAAACGCGCAGTGACCGACTCCGACGAGCCGCCGGTGATTCGTTATGATGTGAAAAACAAAGCAGGCGTGTCAAATTTGCTGGATATTCTGTCCGGTGTCAGCGGCAAAACTATCGCAGAACTTGAACAGGAATTTGAAGGCAAAATGTATGGTCACTTAAAAGGCGCGGTGGCAGAAGAAGTCTCCGCCATATTGACCACCCTGCAGGAACGCTACCACCATTTCCGCAACAATGAGGTATTACTGCACCAAATCGCCAAAGAAGGCGCAAAAAAAGCTCAAGCCCGCGCGCGAGCAACACTGGCGAAAGTGTATGAAACCGTCGGGTTTATTGCGGCGAAG","","","39831","MSKPIVFSGVQPSGELTIGNYLGALRQWVKMQDDYECLFCIVDQHAITVRQDPAALRKATLDVLALYLACGIDPAKSTIFIQSHVPEHAQLAWVLNCYTYFGEMSRMTQFKDKSTRYAENVNVGLFTYPVLMAADILLYQANQVPVGEDQKQHLEITRDIAQRFNALYGPHFAVPEVFIPKAGARVMSLLEPEKKMSKSDENRNNVIGLLEDPKAVAKKIKRAVTDSDEPPVIRYDVKNKAGVSNLLDILSGVSGKTIAELEQEFEGKMYGHLKGAVAEEVSAILTTLQERYHHFRNNEVLLHQIAKEGAKKAQARARATLAKVYETVGFIAAK","329137","","tryptophanyl-tRNA synthetase","Cytoplasm","","
InterPro
IPR002305
Domain
Aminoacyl-tRNA synthetase, class Ib
PF00579\"[3-286]TtRNA-synt_1b
InterPro
IPR002306
Family
Tryptophanyl-tRNA synthetase, class Ib
PR01039\"[16-32]T\"[66-85]T\"[142-163]T\"[195-205]TTRNASYNTHTRP
PTHR10055\"[9-332]TTrp_tRNA-synt_1b
TIGR00233\"[2-330]TtrpS
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620\"[3-220]TRossmann-like_a/b/a_fold
noIPR
unintegrated
unintegrated
SSF52374\"[3-332]TSSF52374


","BeTs to 24 clades of COG0180COG name: Tryptophanyl-tRNA synthetaseFunctional Class: JThe phylogenetic pattern of COG0180 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 96 to 142 match (2e-09) PD:PD247980 which is described as LIGASE SYNTHETASE AMINOACYL-TRNA TRYPTOPHAN--TRNA PROTEOME COMPLETE ATP-BINDING TRYPTOPHANYL-TRNA TRPRS BIOSYNTHESIS ","","","","","","","","","","","","Wed Dec 11 15:55:58 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00473 is paralogously related to AA01936 (3e-04).","","","","","","Residues 3 to 286 (E-value = 1.1e-122) place AA00473 in the tRNA-synt_1b family which is described as tRNA synthetases class I (W and Y) (PF00579)","","","","","Barstow,D.A., Sharman,A.F., Atkinson,T. and Minton,N.P. Cloning and complete nucleotide sequence of the Bacillus stearothermophilus tryptophanyl tRNA synthetase gene Gene 46 (1), 37-45 (1986) PubMed: 3026925 Winter,G.P. and Hartley,B.S. The amino acid sequence of tryptophanyl tRNA synthetase from Bacillus stearothermophilus FEBS Lett. 80 (2), 340-342 (1977) PubMed: 891985 Doublie,S., Bricogne,G., Gilmore,C. and Carter,C.W. Jr. Tryptophanyl-tRNA synthetase crystal structure reveals an unexpected homology to tyrosyl-tRNA synthetase Structure 3 (1), 17-31 (1995) PubMed: 7743129 Ilyin,V.A., Temple,B., Hu,M., Li,G., Yin,Y., Vachette,P. and Carter,C.W. Jr. 2.9 A crystal structure of ligand-free tryptophanyl-tRNA synthetase: domain movements fragment the adenine nucleotide binding site Protein Sci. 9 (2), 218-231 (2000) PubMed: 10716174 ","","Wed Dec 11 15:55:58 2002","1","","","" "AA00474","331784","330315","1470","TTGTGGAATTGTTGGTTTTTTCATATAAATCGGAATTTATGCTTAGTTTATCGGGGCTTGTTTGTTAGAATAGCCGGCATTTTATCAAGTTTAAGCGAGAGTGGGCAATTTATGCCGGATGAAAAGAAAAAAGGCGGTTTTTGGTCTTGGTTCGGATTAGGTAAAAATAAACAGGAAGAATCCGAAGAACCGAAGGAACAAGCATCACAAGAAAAAACGAGTCATTACGTTCAAGAATCACAACCTGAAGCGCAAGAAACAGCGGAAAAAAACACCGCACTTCCGGAGGAAGCAGAGACCGAAAATACATTAACGGAAGATACATCGATGGTGCACGCTTCACAGCCTGTGCCATCAGATGAAACGCCAGTTGACGTTGGTGTTGAATCTAATCCGGTCATTGAAGAAACGATTGCAAATTCGACCGCACTTTTAGACGACGAAACGGAAGCACAAGCCGAAAGTGCGGTGGAAATTTCCAATGAATCTCACGAAGAAGACAGCGCCGTTGCCGACATGGTGGAAACGCAGGAAAAACCAAGTGAAGGCGGCTTTTTCAGTCGCTTATTAAAAGGCTTGGTGAAAACCAAACAAAATATCGGTGCGGGCTTCCGTAGCTTTTTCTTAGGCAAAAAAATCGACGACGACTTGTTCGAGGAATTGGAAGAACAGTTACTTATCGCCGACATCGGCGTGCCGACCACCACCAAAATTATCAATAATCTGACCCAACACGCTACCCGCCAACAGTTGCAAAATGCGGATTCACTGTATCAACAGCTAAAATTGGAAATGGGCGAAATCCTGAAACCGGTGGCGCAACCGTTGCACATCGACGGCAGCAAAAAGCCTTATGTGATTTTGATGGTGGGCGTAAACGGCGTGGGCAAAACCACCACCATCGGCAAGTTGGCGCGCAAATTCCAAATGGAAGGCAAATCCGTCATGTTGGCGGCGGGCGATACCTTCCGCGCGGCGGCAGTGGAGCAGTTGCAGGTGTGGGGCGAACGCAATCACATTCCGGTGGTGGCGCAAAGCACCGGCTCCGATTCCGCCTCGGTGATTTTTGATGCCATGCAATCGGCGGCGGCGCGTAATATCGACATTCTGATCGCCGACACCGCAGGGCGTCTGCAAAATAAAAATAACCTGATGGACGAGTTGAAAAAAATTGTCCGCGTCATGAAAAAATACGACGAAAGCGCCCCGCACGAAATTATGCTCACATTGGATGCAGGCACCGGTCAAAACGCCATCAGCCAAGCCAAATTGTTCAATGAAGCGGTGGGCTTAACCGGCATCAGCCTGACCAAACTGGACGGTACCGCCAAAGGCGGCGTGATTTTCGCCATCGCCGACCAATTCAACCTGCCGATCCGCTACATTGGCGTCGGCGAAAAAATTGAAGATTTACGCGAATTCAACGCAGAAGAATTTATTGAGGCTTTATTTGCTCATGAGGAGGAAGAT","","","53972","LWNCWFFHINRNLCLVYRGLFVRIAGILSSLSESGQFMPDEKKKGGFWSWFGLGKNKQEESEEPKEQASQEKTSHYVQESQPEAQETAEKNTALPEEAETENTLTEDTSMVHASQPVPSDETPVDVGVESNPVIEETIANSTALLDDETEAQAESAVEISNESHEEDSAVADMVETQEKPSEGGFFSRLLKGLVKTKQNIGAGFRSFFLGKKIDDDLFEELEEQLLIADIGVPTTTKIINNLTQHATRQQLQNADSLYQQLKLEMGEILKPVAQPLHIDGSKKPYVILMVGVNGVGKTTTIGKLARKFQMEGKSVMLAAGDTFRAAAVEQLQVWGERNHIPVVAQSTGSDSASVIFDAMQSAAARNIDILIADTAGRLQNKNNLMDELKKIVRVMKKYDESAPHEIMLTLDAGTGQNAISQAKLFNEAVGLTGISLTKLDGTAKGGVIFAIADQFNLPIRYIGVGEKIEDLREFNAEEFIEALFAHEEED","330316","","cell division protein Y (GTP-binding signal recognition particle)","Cytoplasm, Inner membrane","","
InterPro
IPR000897
Domain
GTP-binding signal recognition particle SRP54, GTPase
PD000819\"[287-377]TFTSY_HAEIN_P44870;
PF00448\"[283-485]TSRP54
PS00300\"[458-471]TSRP54
InterPro
IPR001114
Family
Adenylosuccinate synthetase
SM00788\"[286-473]Tno description
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[283-463]TAAA
InterPro
IPR004390
Family
Cell division transporter substrate-binding protein FtsY
TIGR00064\"[212-484]TftsY: signal recognition particle-docking p
InterPro
IPR013822
Domain
GTP-binding signal recognition particle SRP54, helical bundle
G3DSA:1.20.120.140\"[191-274]Tno description
PF02881\"[189-270]TSRP54_N
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[277-487]Tno description
PTHR11564\"[257-488]TGTPASE CONTAINING FAMILY OF SIGNAL RECOGNITION PARTICLE PROTEINS
PTHR11564:SF6\"[257-488]TCELL DIVISION PROTEIN FTSY
signalp\"[1-29]?signal-peptide


","No hits to the COGs database.","Significant hit ( 1.8e-79) to 5/5 blocks of the IPB000897 family, which is described as \"GTP-binding signal recognition particle (SRP54) domain\". Interpro entry for IP:IPR000897. IPB000897A 286-305 1.4e-15 IPB000897B 317-331 3.1e-09 IPB000897C 368-388 7.1e-11 IPB000897D 403-445 2e-26 IPB000897E 458-485 7.4e-12","","","","","","","","","","","","","Wed Dec 11 15:59:05 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00474 is paralogously related to AA01117 (1e-37).","","","","","","Residues 283 to 485 (E-value = 1.3e-126) place AA00474 in the SRP54 family which is described as SRP54-type protein, GTPase domain (PF00448)","","","","","Gill,D.R. and Salmond,G.P. The identification of the Escherichia coli ftsY gene product:an unusual protein Mol. Microbiol. 4 (4), 575-583 (1990) PubMed: 2161989 Luirink,J., ten Hagen-Jongman,C.M., van der Weijden,C.C., Oudega,B., High,S., Dobberstein,B. and Kusters,R. An alternative protein targeting pathway in Escherichia coli: studies on the role of FtsY EMBO J. 13 (10), 2289-2296 (1994) PubMed: 8194520 Montoya,G., Svensson,C., Luirink,J. and Sinning,I. Crystal structure of the NG domain from the signal-recognitionparticle receptor FtsY Nature 385 (6614), 365-368 (1997) PubMed: 9002525 ","","Wed Dec 11 15:59:05 2002","1","","","" "AA00475","331761","332342","582","ATGAAAAAACCAACAATTCCACAAGGCACGAAAGGCGAGGTGCGCATTATCGCCGGGTTATGGCGCGGGCGAAAATTGCCGGTGCTGTCTTACCAAGGGCTACGCCCCACTGGCGATCGCGTGAAAGAAACCTTGTTTAACTGGCTGATGCCTTACATTGCCGGCAGTGAATGTTTGGATTGTTTCGCGGGCAGCGGTTCCCTCGGCTTTGAAGCCCTTTCCCGCCAAGCGTCGAAAGTGACCTTTCTCGAATTGGAAAAAGCGGTGGCGCACCAGTTAACGAAAAATATTCAAACCCTGAAATGTGCCGACCGCGCGCAAGTGGTAAATCAAAACAGTTTGCAGTTTTTAAATCACCCGCAAAATCAACCGCACTTTGATGTGGTTTTTCTCGATCCGCCCTTCCATTTTGATTTGGCGGAACAAGCCATTGCGCTGTTGGCGCAACATCATTGGCTGCGTCCGCAAGCCTTGGTTTATGTGGAAACGGAAAAAGGCAAAGATCTTCAAGTACCCGCAACTTGGGCGTTATTGAAAGAAAAAGACAGTGGGCGGGTGAGCTATCGGTTGTATCAGGCGGCA","","","21852","MKKPTIPQGTKGEVRIIAGLWRGRKLPVLSYQGLRPTGDRVKETLFNWLMPYIAGSECLDCFAGSGSLGFEALSRQASKVTFLELEKAVAHQLTKNIQTLKCADRAQVVNQNSLQFLNHPQNQPHFDVVFLDPPFHFDLAEQAIALLAQHHWLRPQALVYVETEKGKDLQVPATWALLKEKDSGRVSYRLYQAA","332343","","conserved hypothetical protein (possible N6-adenine-specific methylase)","Cytoplasm","","
InterPro
IPR002052
Domain
N-6 Adenine-specific DNA methylase
PS00092\"[129-135]?N6_MTASE
InterPro
IPR004398
Family
Conserved hypothetical protein 95
PF03602\"[14-192]TCons_hypoth95
TIGR00095\"[1-194]TTIGR00095: putative methyltransferase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[50-170]Tno description


","BeTs to 16 clades of COG0742COG name: N6-adenine-specific methylaseFunctional Class: LThe phylogenetic pattern of COG0742 is --------vdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","","Residues 56 to 100 match (2e-07) PD:PD016907 which is described as COMPLETE PROTEOME METHYLTRANSFERASE TRANSFERASE TRNA 2.1.1.- HEMK PROCESSING RNA RRNA ","","","","","","","","","","","","Thu Feb 20 09:00:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00475 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 14 to 192 (E-value = 1.9e-86) place AA00475 in the Cons_hypoth95 family which is described as Conserved hypothetical protein 95 (PF03602)","","","","","","","","1","","","" "AA00478","332632","333594","963","ATGACCCACATTATCGTTGCAACGCACGGTAAGTTTTCGGAAGAAATCGTCAATTCCGCCGCGATGGTGTTTGGCGAAGATGAAAACTGCCATGTTGTTACTTTCCTGCCGGGTGAAGGCGGTGAGCATTTGGTTGAAAAATATAATGCCATTATCGCCACCTTGCCGGAAAACGAGCCGGTGCTGTTTTTGGTGGATTTATTCGGCGGCAGCCCGTATAACGCGGCGGCGCGGGTAGCGACCGGACGGGAAAATACGGATATTGTGACCGGTATTAGCTTGCCGATGTTACTGGAAGTGTTGGATGCGAAAAACGGCGCAAGCCTGCCGGAATTGGTGGAAACCGCCAAGGAAGTGGGCGTGGCGGCGGTGAAATCCTTCCGTCAGCCGAAAGAAGACGCAAACCCTGCCACCCCACCGGCGCAAGCCGCCAAACCTGCCGAAGCGGAAAAACCGACCGCACTTTCCGGCAATATGAACATTTCTTTACTGCGTATCGACAGCCTTTTGATTCACGGTCAAGTGGCAACCTCTTGGGCAAAAGCGGTGAAATGCGAAGCGATTTTTGCGGTAAATGATGATGTGGCGAACGATCCGCTGCGTCGTGATTTACTGCTACAGGTTGCACCGCCACACTTGAAAGCCTATGTAATTCCGGTGGAAAAAGCCATTAAGGTGTATCACAACCCGAAATACGCGGGCAAAAATATTCTTTGGTTGGTGACCAATCCGTCCGACATCGTGCGTTTAATTGACGGCGGTGTGAAAGTGGAGAAAGTCAACGTGGGCGGTATGACGTACCGCGAGGGCAACAAATTGCTTTCCCAAGCGGTTGCCGTTAACCCGACCGACGTGGAAGCCTTCAAACAATTGTTGGATAAAGGCGTTGAACTGAGCCTGCAACAAGTGGCCGCCAATCCGAAAGTGATGTTGACCCATAAAGAACTTGATGCCGTTAAATTC","","","34533","MTHIIVATHGKFSEEIVNSAAMVFGEDENCHVVTFLPGEGGEHLVEKYNAIIATLPENEPVLFLVDLFGGSPYNAAARVATGRENTDIVTGISLPMLLEVLDAKNGASLPELVETAKEVGVAAVKSFRQPKEDANPATPPAQAAKPAEAEKPTALSGNMNISLLRIDSLLIHGQVATSWAKAVKCEAIFAVNDDVANDPLRRDLLLQVAPPHLKAYVIPVEKAIKVYHNPKYAGKNILWLVTNPSDIVRLIDGGVKVEKVNVGGMTYREGNKLLSQAVAVNPTDVEAFKQLLDKGVELSLQQVAANPKVMLTHKELDAVKF","333595","Erni,B., Zanolari,B. and Kocher,H.P. The mannose permease of Escherichia coli consists of threedifferent proteins. Amino acid sequence and function in sugartransport, sugar phosphorylation, and penetration of phagelambda DNA. J. Biol. Chem. 262(11):5238-5247, 1987. PubMed: 2951378 Lortie,L.A., Pelletier,M., Vadeboncoeur,C. and Frenette,M. The gene encoding IIABLMan in Streptococcus salivarius is partof a tetracistronic operon encoding aphosphoenolpyruvate:mannose/glucose phosphotransferase system.Microbiology 146:677-685,2000. Nunn,R.S., Markovic-Housley,Z., Genovesio-Taverne,J.C., Flukiger,K., Rizkallah,P.J., Jansonius,J.N., Schirmer,T. and Erni,B. Structure of the IIA domain of the mannose transporter from Escherichia coli at 1.7 angstroms resolution Journal of molecular biology. 259 (3), 502-511 (1996) PubMed: 8676384Markovic-Housley,Z., Balbach,J., Stolz,B. and Genovesio-Taverne,J.C. Predicted topology of the N-terminal domain of the hydrophilic subunit of the mannose transporter of Escherichia coli FEBS letters. 340 (3), 202-206 (1994) PubMed: 8131846.Gschwind,R.M., Gemmecker,G., Leutner,M., Kessler,H.,Gutknecht,R., Lanz,R., Flukiger,K. and Erni,B. Secondary structure of the IIB domain of the Escherichia coli mannose transporter, a new fold in the class of alpha/betatwisted open-sheet structures FEBS letters. 404 (1), 45-50 (1997) PubMed: 9074635","mannose-specific phosphotransferase element","Cytoplasm","","
InterPro
IPR004701
Domain
Phosphotransferase system, fructose subfamily IIA component
G3DSA:3.40.50.510\"[1-134]Tno description
PF03610\"[2-117]TEIIA-man
PS51096\"[1-124]TPTS_EIIA_TYPE_4
InterPro
IPR004720
Domain
Phosphotransferase system, sorbose subfamily IIB component
PD008332\"[167-304]TQ9CMJ0_PASMU_Q9CMJ0;
G3DSA:3.40.35.10\"[159-313]Tno description
PF03830\"[160-310]TPTSIIB_sorb
TIGR00854\"[160-310]Tpts-sorbose: PTS system, mannose/fructose/s
PS51101\"[157-321]TPTS_EIIB_TYPE_4
InterPro
IPR013789
Domain
Phosphotransferase system, fructose subfamily IIA component, subgroup
TIGR00824\"[1-116]TEIIA-man: PTS system, mannose/fructose/sorb


","No hits to the COGs database.","","Residues 4 to 120 match (5e-24) PD:PD328938 which is described as PROTEOME COMPLETE PTS COMPONENT SYSTEM IIA TRANSFERASE SYSTEM IIAB PHOSPHOTRANSFERASE ","","","","","","","","","","","Wed Jul 11 17:30:37 2007","Wed Dec 11 17:22:43 2002","","Wed Jul 11 17:26:42 2007","","Wed Jul 11 17:26:42 2007","yes","Fri Feb 20 15:41:32 MST 1998","AA00478 is paralogously related to AA01465 (8e-73).","Wed Jul 11 17:26:42 2007","","","","","Residues 160 to 310 (E-value = 1.1e-67) place AA00478 in the PTSIIB_sorb family which is described as PTS system sorbose subfamily IIB component (PF03830)","Wed Jul 11 17:26:42 2007","","","","","","","1","","","" "AA00479","333615","334409","795","ATGACAACAATGGAAATTATTTTAGTCACACTGGTCGCCGCCATTTACGGTATGGGAAGTGTGTTGGACGAACGTCAAACCCACCGTCCGTTAGTCGCCTGTACCCTGATCGGACTGGTGCTCGGTGATTTACAAACCGGTATTATCGTGGGTGGTACGTTAGAATTGGTCGCCCTCGGCTGGATGAACGTGGGCGCGGCAATGGCGCCTGATGCGGCGCTTGCCAGTGTGATCGCAGCGATTTTGGTGATCAAAGGCGGTCAGGACAAAGGCAGCGCATTAGCTATCGCCATTCCTGTGGCGGCAGCCGGTCAGGTGTTAACCATTTTCGTGCGTACGCTCACCATATTCCTGCAACACAAAGCGGACGATTACGCGACACAAGCTAACTTCCGCGGCATTGAATTCTGTCACTTCGCCGGGCTTTCCTTACAAGCCTTGCGCGTTGCCATTCCGACCTTCTTCGTTGCCTTAGTTGCCGGCACCGACACCGTTACTCACGCGTTGAACTCCATTCCGGAAGTGGTCACCCGCGGGTTACAAATCGCCGGGGGCTTCATTGTGGTGGTCGGTTACGCCATGGTGATCAACATGATGCGCGCCGGTGCGTTAATGCCGTTCTTCTTCCTTGGCTTCGTCATTGCCTCCTTCTCCGGTTACAACCTGGTGGGCTTGGGTATTTTAGGTACCTGTTTGGCAATTCTCTACATTCAATTAAATCCGCGTTTCAATCAGGTGGCATTGCTACCAAGCAGCGCAAAACGCGAATTAGCCGATGATGAACTTGAAGGACTT","","","27805","MTTMEIILVTLVAAIYGMGSVLDERQTHRPLVACTLIGLVLGDLQTGIIVGGTLELVALGWMNVGAAMAPDAALASVIAAILVIKGGQDKGSALAIAIPVAAAGQVLTIFVRTLTIFLQHKADDYATQANFRGIEFCHFAGLSLQALRVAIPTFFVALVAGTDTVTHALNSIPEVVTRGLQIAGGFIVVVGYAMVINMMRAGALMPFFFLGFVIASFSGYNLVGLGILGTCLAILYIQLNPRFNQVALLPSSAKRELADDELEGL","334410","","mannose-specific phosphotransferase system IIC","Inner membrane, Cytoplasm","","
InterPro
IPR004700
Family
Phosphotransferase system, sorbose-specific IIC subunit
PF03609\"[1-236]TEII-Sor
TIGR00822\"[1-265]TEII-Sor: PTS system, mannose/fructose/sorbo
PS51106\"[1-235]TPTS_EIIC_TYPE_4
noIPR
unintegrated
unintegrated
signalp\"[1-19]?signal-peptide
tmhmm\"[36-58]?\"[64-84]?\"[94-114]?\"[176-196]?\"[206-240]?transmembrane_regions


","No hits to the COGs database.","","Residues 112 to 235 match (2e-10) PD:PD535992 which is described as SYSTEM PROTEOME IIC COMPLETE PTS TRANSFERASE PHOSPHOTRANSFERASE ENZYME ","","","","","","","","","","","","Wed Dec 11 17:38:19 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00479 is paralogously related to AA01466 (6e-89).","","","","","","Residues 1 to 236 (E-value = 8.4e-130) place AA00479 in the EII-Sor family which is described as PTS system sorbose-specific iic component (PF03609)","","","","","Erni,B., Zanolari,B. and Kocher,H.P. The mannose permease of Escherichia coli consists of threedifferent proteins. Amino acid sequence and function in sugartransport, sugar phosphorylation, and penetration of phage lambdaDNA. J. Biol. Chem. 262(11):5238-5247,1987. PubMed: 2951378. Wehmeier,U.F. and Lengeler,J.W. Sequence of the sor-operon for L-sorbose utilization fromKlebsiella pneumoniae KAY2026. Biochim. Biophys. Acta 1208(2):348-351,1994. PubMed: 7947968. Martin-Verstraete,I., Debarbouille,M., Klier,A. and Rapoport,G. Levanase operon of Bacillus subtilis includes a fructose-specificphosphotransferase system regulating the expression of the operon.J. Mol. Biol. 214(3):657-671,1990. PubMed: 2117666.","","Wed Dec 11 17:38:19 2002","1","","","" "AA00480","334426","335259","834","ATGACTGAACAAAATAAACTCGCTTTAACGAAAAAAGATATTCGTAGCACTTACTGGCGCTCAACCTTCTTATTGGGTTCCTTTAACTTTGAACGGATGCAGGCGATGGGCTTCTGTGTTTCCATGATTCCTGCGATCAAACGCCTGTACAGCAAAAAAGAAGATCAAGCGGCGGCGTTAAAACGCCACTTAGAATTCTTCAACACCCAACCTTGGGTTGCCTCTTCCATCATCGGGGTTACCGCCGCCATGGAACAAGAACGCGCCAATGGGGCAAAAGACATTGACGATGCGGCAATCAGCGGGGTGAAAGTAGGTCTTATGGGTCCGCTCGCTGGTGTGGGCGATCCGATTTTCTGGGGGACATTACGTCCTGTGCTTGCCGCCCTCGGCGCAGGGTTGGCGATTACCGGCAGCCGGTTAGGACCGCTATTGTTCTTCATCGGCATTAACCTGTGTCGTGCGTTAACCCGTTGGTACGGCTTCAAATACGGTTACGAAAAAGGAACGGAAATCGTGAACGATATGGGCGGCGGTCGCTTACAAAAACTGACGCAGGGGGCGTCGATCCTAGGTCTCTTTGTCATGGGCTCGTTGGTGTCGAAATGGACCAGCATTAACATTCCGCTGGAACTGTCACGCTATAGAAACCAAATGGGCGATGAAGTGGTCACTACCGTACAAAGCGTATTAAACGACTTGCTCCCGGGCTTGGCGGCATTGTTGCTCACTTTCTTGTGTATGTATTTGCTACGCAAAAAAATCAACGCCATGTATATCATCTTCGCGCTGTTTGGCGTGGGTATCATCGGCTACCATTTCGGTGTGTTAGCG","","","32001","MTEQNKLALTKKDIRSTYWRSTFLLGSFNFERMQAMGFCVSMIPAIKRLYSKKEDQAAALKRHLEFFNTQPWVASSIIGVTAAMEQERANGAKDIDDAAISGVKVGLMGPLAGVGDPIFWGTLRPVLAALGAGLAITGSRLGPLLFFIGINLCRALTRWYGFKYGYEKGTEIVNDMGGGRLQKLTQGASILGLFVMGSLVSKWTSINIPLELSRYRNQMGDEVVTTVQSVLNDLLPGLAALLLTFLCMYLLRKKINAMYIIFALFGVGIIGYHFGVLA","335260","","mannose-specific phosphotransferase system IID","Inner membrane, Cytoplasm","","
InterPro
IPR004704
Family
Phosphotransferase system, mannose/fructose/sorbose family IID component
PF03613\"[7-277]TEIID-AGA
TIGR00828\"[7-277]TEIID-AGA: PTS system, mannose/fructose/sorb
PS51108\"[7-277]TPTS_EIID
noIPR
unintegrated
unintegrated
tmhmm\"[106-124]?\"[130-150]?\"[190-210]?\"[229-251]?\"[256-276]?transmembrane_regions


","No hits to the COGs database.","","Residues 141 to 212 match (7e-15) PD:PD242695 which is described as PROTEOME COMPLETE PTS IID SYSTEM COMPONENT MANNOSE-SPECIFIC PERMEASE TRANSFERASE PHOSPHOTRANSFERASE ","","","","","","","","","","","","Wed Dec 11 17:40:43 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00480 is paralogously related to AA01467 (6e-95).","","","","","","Residues 7 to 277 (E-value = 2.8e-161) place AA00480 in the EIID-AGA family which is described as PTS system mannose/fructose/sorbose family IID component (PF03613)","","","","","Erni,B., Zanolari,B. and Kocher,H.P. The mannose permease of Escherichia coli consists of threedifferent proteins. Amino acid sequence and function in sugartransport, sugar phosphorylation, and penetration of phage lambdaDNA. J. Biol. Chem. 262(11):5238-5247, 1987. PubMed: 2951378. Martin-Verstraete,I., Debarbouille,M., Klier,A. and Rapoport,G. Levanase operon of Bacillus subtilis includes a fructose-specificphosphotransferase system regulating the expression of the operon.J. Mol. Biol. 214(3):657-671,1990. PubMed: 2117666.","","Wed Dec 11 17:40:43 2002","1","","","" "AA00482","335372","336544","1173","ATGAAACTCAAAGACCTCATCAAAGCGCCGCCCGCCGAGGGCTACATCAAAAATTCATCGAATTTAGTGACCGCACTTTTTATTCTGGCGGGCGTGCTTTACTACCCCACCAACGGCTACGGCGCGGTGATTGCCCTTGCGGTGGCGCTTATCGTCCTCATCGGCCAGAAAATGCTTATCGGGCAAGCCAATAAAGATTTCGCCGAAATGCAATTTGCCGAAAAACAATTTCCGCAAACGAAGAATTTGGATTATGTGCGTTTCATTCACGCCCGCGCCACACAAATTTTAAAAGATAACAAAGTGTTATCGGAAAAAGGCAAAAAGGAACTCCATCGTCTGCTCAAGTTTGCTGACACTACCTTGGCGGAAAATGCCGAACAGACCACACCGCAATACAAAGCCGTATTCAGCGACATCGACGGTACGCTACTCAACAACCAACACCAAATCACCCTGAAAACGGAAGATGCTATCAAAAACATGCTCAAACGGGGCATTCCGTTTATTCCCGTTTCCGCACGCCCGCCTTACGCCATTACGCCTTATACGGAACAGCTTGGCGCACAACACGGCATGATTTGTTACAGCGGCGCGTTAATTTTAGATAAAAATCTGACCGCACTTTATAGCGTGATTCTCGAACCGCAGGATCTGCAAAAACTGAACGAACTGCTGGCGGATTTCGCCCGCCTTTCCATCAGTTACTACGCCGGGTTGGATTGGTTCTGTAATGATGTCAACAATGATTGGATTAAACAGGAAAGCGCCATCACCGGCTTAACCGCGGCAGCGATGCCGGACAACCTTACGGAAGTGCATAAACTCTTAATCATGGGCGACGCCGACGAAATCCAAGCGGTGGAACCCGTGCTGAAACAGGCACTGCCAAATTTAAGTATTCACCGTTCCAAAAACGAATATTTGGAAATCATGAACGCCGCCGCTACCAAAGCCAAAGCAATTCAATTTATGGAACAGTATCTCGGCATCACGGCGGATCAGGTCATCGCGTTCGGCGATAATTTCAACGATTTGGATATGTTGCAATACGCCGGTTTAAGCGTCGCCATGGGCAACGCCCCCGACGCCGTCAAACAAGCAGCAAAAGAAGTCACCGCCAATAATAACGAAGGCGGCATTGCTTTGGTACTCAATCGGGTGTTTGGTAAG","","","43086","MKLKDLIKAPPAEGYIKNSSNLVTALFILAGVLYYPTNGYGAVIALAVALIVLIGQKMLIGQANKDFAEMQFAEKQFPQTKNLDYVRFIHARATQILKDNKVLSEKGKKELHRLLKFADTTLAENAEQTTPQYKAVFSDIDGTLLNNQHQITLKTEDAIKNMLKRGIPFIPVSARPPYAITPYTEQLGAQHGMICYSGALILDKNLTALYSVILEPQDLQKLNELLADFARLSISYYAGLDWFCNDVNNDWIKQESAITGLTAAAMPDNLTEVHKLLIMGDADEIQAVEPVLKQALPNLSIHRSKNEYLEIMNAAATKAKAIQFMEQYLGITADQVIAFGDNFNDLDMLQYAGLSVAMGNAPDAVKQAAKEVTANNNEGGIALVLNRVFGK","336545","","hydrolase (haloacid dehalogenase-like) (HAD superfamily)","Periplasm, Cytoplasm","","
InterPro
IPR000150
Family
Cof protein
TIGR00099\"[135-385]TCof-subfamily: Cof-like hydrolase
PS01228\"[135-146]?COF_1
PS01229\"[339-361]TCOF_2
InterPro
IPR006379
Family
HAD-superfamily hydrolase, subfamily IIB
TIGR01484\"[135-358]THAD-SF-IIB: HAD-superfamily hydrolase, subf
InterPro
IPR013200
Domain
HAD superfamily hydrolase-like, type 3
PF08282\"[136-385]THydrolase_3
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1000\"[132-389]Tno description
PTHR10000\"[307-371]TPHOSPHOSERINE PHOSPHATASE
signalp\"[1-41]?signal-peptide
tmhmm\"[15-35]?\"[41-61]?transmembrane_regions


","BeTs to 18 clades of COG0561COG name: Predicted hydrolases of the HAD superfamilyFunctional Class: RThe phylogenetic pattern of COG0561 is aompkzy-vdrlbce-gh-n-j-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.5e-31) to 3/3 blocks of the IPB000150 family, which is described as \"Cof protein\". Interpro entry for IP:IPR000150. IPB000150A 132-146 1.7e-07 IPB000150B 166-175 3.1 IPB000150C 337-369 1.1e-20","Residues 309 to 382 match (9e-11) PD:PD186741 which is described as COMPLETE PROTEOME TRANSFERASE ACID FIXI NUCLEOTIDYLTRANSFERASE SYNTHETASE YRBI COF FAMILY ","","","","","","","","","","","","Thu Dec 12 09:20:43 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00482 is paralogously related to AA00316 (2e-20), AA01431 (2e-14), AA01216 (2e-12) and AA02939 (3e-04).","","","","","","Residues 133 to 362 (E-value = 5.6e-07) place AA00482 in the Hydrolase family which is described as haloacid dehalogenase-like hydrolase (PF00702)","","","","","","","","1","","","" "AA00485","336634","336768","135","ATGCGTAAATTGCGTTTGCCTGTTTCATTTCGTAAAATGATTCACCCATTTACTTCATTCAGTGTGAGAATTTTCACATCACGCCGGTTCTGGGATATTTTAACCACGATGAAGTTAGATGCTTTAACCTACCAA","","","5519","MRKLRLPVSFRKMIHPFTSFSVRIFTSRRFWDILTTMKLDALTYQ","336768","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:03:29 2004","Sun Feb 22 16:03:29 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00485 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:03:29 2004","","","","","","","","","","","","","1","","","" "AA00486","336923","338086","1164","TTGCGTACTGTTTTCGGTGCACTGGCAATCCAAATTGCTATTGGTGCTTTCGTGCTTTATGTGGATAAAGGACGTGAAGCGTTAAAAGCTGCTTCCGATTTTATCGGGAAAATCATTGGATTCGGGAATGAGGGGATTAGTTTTGTGTTCGGTGGTCTGACCGATCCGAGCCAAAGTTTTGGCTTTATCTTCGCCGTGAAAGTGCTACCTGTCATTATCTTCTTCTCCGCATTAATTTCACTCCTTTACTATATCGGCATCATGCAATGGATTATTAAGCTTATCGGTGGTGGATTACAAAAATTATTAGGTACCTCAAAAGCTGAGTCCATGTCTGCCGCAGCAAATATTTTCGTCGGTCAAACAGAAGCACCATTAATCGTCAAGCCATTCATTGGTCGCATGACGCAATCCGAATTATTCACAGTTATGGTCGGCGGTGTGGCGTCTATTGCAGGTTCCGTTATGGCAGGCTATGCAGGTATGGGCGTGCCGCTGACTTACTTGATCGCAGCATCCTTCATGGCAGCACCGGGTGGTTTATTGTTTGCCAAAATCATGTTTCCACAAACGGAAAAAAGCGACGACGCATTAAAAGAAGATGCAAATGTGGAAAAACCGTCCAACGCCATTGAGGCCTTGGCAAACGGTGCACGTGATGGCATGCATTTAGCAATGAATGTGGGCGCAATGCTGATTGCTTTCGTTTCTGTTATCGCCTTAATTAACTGGATTTTAAGCAGTTTTGGTGGATTCTTTGGCGAACCGGATTTAACCTTACAAGTGATTTTAGGATGGATCTTTAAACCTCTGGCCTATTTAATCGGGATTCCTTGGAATGAATCAGCTGTAGCAGGTCAAATGATCGGTCTGAAATTAGCGGTCAATGAATTCGTCGGCTACCTGGAATTCACTAAATATTTGCAACCTGATGCGGCAATAGTATTAAGCGATAAAACCAAAGCGATTATCACCTTCGCCCTTTGTGGTTTCGCCAACTTCAGCTCCATCGCGATTTTAATCGGTGGCTTGGGCGGAATGGCACCAAATCGCCGTAGTGATGTTGCCCGCTTAGGTTTAAAAGCAGTGGTTGCCGGTTCATTATCCAACTTAATGAGCGCAACCATTGCCGGTTTATTTATTGGTTTAAGTGGTGCCGTGCTA","","","45583","LRTVFGALAIQIAIGAFVLYVDKGREALKAASDFIGKIIGFGNEGISFVFGGLTDPSQSFGFIFAVKVLPVIIFFSALISLLYYIGIMQWIIKLIGGGLQKLLGTSKAESMSAAANIFVGQTEAPLIVKPFIGRMTQSELFTVMVGGVASIAGSVMAGYAGMGVPLTYLIAASFMAAPGGLLFAKIMFPQTEKSDDALKEDANVEKPSNAIEALANGARDGMHLAMNVGAMLIAFVSVIALINWILSSFGGFFGEPDLTLQVILGWIFKPLAYLIGIPWNESAVAGQMIGLKLAVNEFVGYLEFTKYLQPDAAIVLSDKTKAIITFALCGFANFSSIAILIGGLGGMAPNRRSDVARLGLKAVVAGSLSNLMSATIAGLFIGLSGAVL","338087","","nucleoside transporter","Inner membrane, Cytoplasm","","
InterPro
IPR002668
Domain
Na+ dependent nucleoside transporter
PF01773\"[1-54]TNucleos_tra2_N
InterPro
IPR008276
Family
Concentrative nucleoside transporter
PD003768\"[1-240]TYEIM_HAEIN_P44742;
PTHR10590\"[2-381]TSODIUM/NUCLEOSIDE COTRANSPORTER
TIGR00804\"[1-380]TnupC: nucleoside transporter, NupC family
InterPro
IPR011642
Domain
Nucleoside recognition
PF07670\"[65-166]TGate
InterPro
IPR011657
Domain
Na+ dependent nucleoside transporter, C-terminal
PF07662\"[169-381]TNucleos_tra2_C
noIPR
unintegrated
unintegrated
signalp\"[1-15]?signal-peptide
tmhmm\"[4-24]?\"[45-65]?\"[71-91]?\"[140-160]?\"[164-184]?\"[228-248]?\"[322-342]?\"[363-383]?transmembrane_regions


","BeTs to 5 clades of COG1972COG name: Nucleoside permeaseFunctional Class: FThe phylogenetic pattern of COG1972 is -----------lb-e-gh--uj----Number of proteins in this genome belonging to this COG is","Significant hit (2.5e-138) to 5/6 blocks of the IPB002668 family, which is described as \"Na+ dependent nucleoside transporter\". Interpro entry for IP:IPR002668. IPB002668B 63-95 6.2e-26 IPB002668C 154-191 9.5e-24 IPB002668D 209-250 2e-21 IPB002668E 263-305 3.3e-25 IPB002668F 315-362 1.8e-37","Residues 1 to 379 match (2e-123) PD:PD003768 which is described as NUCLEOSIDE COMPLETE PROTEOME TRANSPORTER COTRANSPORTER CONCENTRATIVE TRANSMEMBRANE SODIUM/NUCLEOSIDE SODIUM-COUPLED FAMILY ","","","","","","","","","","","","Thu Dec 12 09:27:05 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00486 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 381 (E-value = 2.3e-215) place AA00486 in the Nucleoside_tra2 family which is described as Na+ dependent nucleoside transporter (PF01773)","","","","","Craig,J.E., Zhang,Y. and Gallagher,M.P.Cloning of the nupC gene of Escherichia coli encoding a nucleosidetransport system, and identification of an adjacent insertionelement, IS 186Mol. Microbiol. 11 (6), 1159-1168 (1994)PubMed: 8022285","","Thu Dec 12 09:31:02 2002","1","","","" "AA00488","338215","338931","717","ATGACTCCACATATTAACGCACCTGCCGGTGCATTTGCCGATGCCGTATTAATGCCGGGCGACCCGCTCCGTGCAAAATATATCGCTGAAACCTTTTTAGACGATGTGAAAGAAGTGACTAATGTACGCAATATGTTGGGATTCACAGGCACTTATAAAGGCCGTCGCATTTCCGTCATGGCGCACGGTATGGGAATTCCGTCTTGCTCCATTTATGCGAAAGAGCTGATCACTGAGTACGGCGTAAAAAAACTCATCCGTGTGGGTTCCTGTGGTGCCGTACGTATGGATGTTAAAGTGCGTGACGTGGTTATCGGCGTCGGCGCCTGTACCGATTCCAAAGTGAATCGTATCCGTTTTAAAGACAATGATTTCGCTGCTATCGCCGATTTCGGTTTAACTCAGGCGGCTGTGCAAGCGGTAAAAACGTTGGGCGTAAAAGCACGTGTCGGCAATTTATTCTCCGCCGATTTATTCTATACCCCGGATATGGCAATGTTCGACGTGATGGAAAAATACGGTATTCTCGGCGTGGAAATGGAAGCGGCGGGTATTTATGGCGTAGCGGCAGAATACGGCGCCCGTGCATTAACTATCTGCACCGTTTCCGACCATATTCGTACACACGAACAAACCAGTGCGGAAGAACGTCAATTAACCTTTAATGAAATGATTAAAATCGCATTAGAAGCCATATTAATTGACGACAAAGAAGCA","","","25955","MTPHINAPAGAFADAVLMPGDPLRAKYIAETFLDDVKEVTNVRNMLGFTGTYKGRRISVMAHGMGIPSCSIYAKELITEYGVKKLIRVGSCGAVRMDVKVRDVVIGVGACTDSKVNRIRFKDNDFAAIADFGLTQAAVQAVKTLGVKARVGNLFSADLFYTPDMAMFDVMEKYGILGVEMEAAGIYGVAAEYGARALTICTVSDHIRTHEQTSAEERQLTFNEMIKIALEAILIDDKEA","338932","","purine nucleoside phosphorylase","Cytoplasm","","
InterPro
IPR000845
Family
Nucleoside phosphorylase
PF01048\"[14-232]TPNP_UDP_1
InterPro
IPR004402
Family
Purine nucleoside phosphorylase
TIGR00107\"[4-235]TdeoD: purine nucleoside phosphorylase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1580\"[1-232]Tno description
PTHR21234\"[1-238]TPURINE NUCLEOSIDE PHOSPHORYLASE
PTHR21234:SF7\"[1-238]TPURINE NUCLEOSIDE PHOSPHORYLASE


","BeTs to 8 clades of COG0813COG name: Purine-nucleoside phosphorylaseFunctional Class: FThe phylogenetic pattern of COG0813 is -----z---d-lb-e-gh--uj--twNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.9e-66) to 4/4 blocks of the IPB000845 family, which is described as \"Purine and other phosphorylases, family 1\". Interpro entry for IP:IPR000845. IPB000845A 19-30 3.4e-07 IPB000845B 43-77 3.2e-26 IPB000845C 150-160 0.00022 IPB000845D 174-210 1.5e-24","Residues 2 to 47 match (1e-18) PD:PD411638 which is described as PHOSPHORYLASE NUCLEOSIDE PURINE COMPLETE PROTEOME GLYCOSYLTRANSFERASE TRANSFERASE PNP INOSINE II ","","","","","","","","","","","","Thu Dec 12 09:40:57 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00488 is paralogously related to AA00388 (6e-14) and AA01750 (3e-07).","","","","","","Residues 14 to 232 (E-value = 3.3e-105) place AA00488 in the PNP_UDP_1 family which is described as Phosphorylase family (PF01048)","","","","","Larsen,J.E., Albrechtsen,B. and Valentin-Hansen,P. Analysis of the terminator region after the deoCABD operon ofEscherichia coli K-12 using a new class of single copy numberoperon-fusion vectors. Nucleic Acids Res. 15(13): 5125-5140, 1987. PubMed: 3299264. Sukhodolets VV, Trenina MA. [Study of RecA-independent homologous recombination and achromosomal rearrangement in the Escherichia coli straincarrying an extended tandem duplication] Genetika. 2002 Feb;38(2):171-81. Russian. PMID: 11898608 Lee J, Filosa S, Bonvin J, Guyon S, Aponte RA, Turnbull JL. Expression, purification, and characterization of recombinantpurine nucleoside phosphorylase from Escherichia coli. Protein Expr Purif. 2001 Jul;22(2):180-8. PMID: 11437593 ","","Thu Dec 12 09:40:57 2002","1","","","" "AA00489","338952","339092","141","TTGAACGTGAAAGTGCGGTCAAAAATTTCGATGTTTCGTAGCAAAGACTTAATTTTTGTATTTGCTACGATTTTATTTATGAAAATGTTAATTATTGGTAATAAAAATGTTATATTTTCTACCATTTTTTTATCATTTATA","","","5468","LNVKVRSKISMFRSKDLIFVFATILFMKMLIIGNKNVIFSTIFLSFI","339092","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-33]?signal-peptide
tmhmm\"[15-33]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:04:50 2004","Sun Feb 22 16:04:50 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00489 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:04:50 2004","","","","","","","","","","","","","1","","","" "AA00490","339201","341621","2421","ATGAAGCGACCGTCTTATCTATTTAAGATGGTATTTATGAGTGGAATTTCGCTCTCAACAATACCATTTGCACACGCCAATCAATCTCCAATTGATCTTGAACGGGAAAAAATTATTATCTTTTCCAGACAGGGAGATAGCGAATTAAAACAAGCTATTCCCCAATTAGAAAAACTCTTTGAACGCACTAAAGATCTCAAAGTCCGTGATGACTTAATCGCCCTTTATTTGCGTAATAATCAATCTATACACGCCTTAAAGGTATGCGAATCCTGCACACCAACGCAATTTTCCGAAAGTGAGTTGGAAAATCTGGGAAAAGCTGCCCGTAATGAAAAACAATTCCAACGTTCTTTTGAACTGTATTCACAGTTAGCAAAAAAATATCCGCAAAATCCCAATGGGTTATTAGGCAAAGTCTTAGTGGCAACCGAATTAAAAAATTATACGGTGGCAAAAGACGCTCTCATTAACTACAAAAAACGTTTTGGTGAAAATACAGCCTATTGGGATGCCAACAGTTATTTATTGGATTTTACCCAATCCGATATGGCAAAATTGGGTCGTTGGCAACGTGAATTGTCAAGAAATCCGAAAAATACTCATCTTGCCGGTAATCTTTATCGGCTTGCCTCAAAATACAACATTCATCCGTTGCAGAAAAAATTACAATCGGAATATCCGGATTTGTTTAGTGAAAAAGATTTGCTTTGGTACGAGCATGATAAAATCATCGCATCAGCAAAAAATGCCAAAAATAATCGAAAGCATTTAAAAAATTCATTCGCAGGATTGACCGCACTTTTACGGAAAATTGATCCGGCACATCCGCTTTATCAACAAACATTAATGGATCGATTTATATTAGGTGTGCAATTACATGAATTTGATGCCGTTCGTGATGATTATGCCACTTTAAAAGCGTTACCGACCCCGTCGGCTTATTTACGTGAAGCTTTTGCTGATTATGAACTGGCACATGCGTCACCACATAAAGCCTTGGCAACATATCAATCTCTTGCACAGTCCGCTTTAGATAAGAAAGCACCGGTAAGTGATGAGCTTTTGTTAAAAATGTTTTCTGCCGCCAGTGACGCAGGTGAATTCGCTTTGGCACAGCACTATTTAGAACAGATTAACAGCTCACCTTATGTAAATGATTACACTCATACATCACGCGTTCCGAATCCGTCATATGATGAGCGTTATTTCGGTTTGGCACGCTTGGCATTATGGCGTGGCAATGCAGGTTTAGCGCAGAAAATGATTGATGAACGTGCATTGGATAAAACCCCTGGGGATGGTTGGGTACTATTGCAAAAAGCCGAGTTGGAACGTAATCGTTATAATTTTGATGAGGCTAAAGAATGGGCGCATAAAGCGGGCGTTTTCTTTATTGAATCCGACCAAAAATATGTTCGTCATGCTTTAATTGAAATCGCATTACGTCAAAATGATTTACCGACGGCGAAACGTTTGATTCAGGAAATGAGCCCTGAAGAAATGGATTCAGTCAAACCCTTGATGGAGCGTTATGAATTGGCGCATAAAGGGCGTATTGTAGGAAGTGTTAATCTACAGCACCGCACTTCTGCACCGACAAAACAACATAATGAATCCACTCAAGATTACGCGATTTACACACCAAAAACCGCAGAGGGGCACGATCTTTATGTGCGTTATACGGAAAGCCGCGTACCGGTGGATGGCAATTCACTCAATGCACAATTTATTGGTGCGGGTACCGAACTGAATTTCTATCCGCTTAATGTGCGTATAGAAGCCGGTAAAGGCATTAAACTCAGCAAACGCGGTTATGTGACATCCGATTTAAGTTATGAGTTAAATCAGCGTTGGGCATTTAATTTGCGCGGACATATTAACGGCACCGATGTTCCGTCAAGAGCAGCTGCGCAAAATGTTTATACCAAAGGTGGCGGCGCGTCTGTAGTTTACACTTATTCTGATCTGTTCCAATTAGGCGGTGGTGTTTATTTTTCCCGCTTTAGTGACAGTAATTTAAGACATGATGCTAATTTATGGCTGAATACAAAAACCTTTAAGCATGATCGCTGGGCGCTAACCAACAATTTCCGTGTGGATTATACGCGAAATAAAACCGTTCAATCCGCGGATTATTACAACCCGATAAAAGCAGTCAGTTACGAAGTGGGCGGTGATTTGAGTTATTACCAGCCGTTTGATTATGCGCTGATTCTGACCCATCACTTGAAAGGCAACTTTGGTGCTTATAAACAGCAGGCACAACAGCGTAGTAAAACCTGGTCAGTGAGTTACGGGCATGAATGGCGTATTGGTAAACAATATGGCTTTTTATATGAAATCGGACGTAAAAAGAATATTTATGACGGTAATCCCGAATTTAATAACTTTGGTAACCTCTCTTTCTCACTTTATTAT","","","92568","MKRPSYLFKMVFMSGISLSTIPFAHANQSPIDLEREKIIIFSRQGDSELKQAIPQLEKLFERTKDLKVRDDLIALYLRNNQSIHALKVCESCTPTQFSESELENLGKAARNEKQFQRSFELYSQLAKKYPQNPNGLLGKVLVATELKNYTVAKDALINYKKRFGENTAYWDANSYLLDFTQSDMAKLGRWQRELSRNPKNTHLAGNLYRLASKYNIHPLQKKLQSEYPDLFSEKDLLWYEHDKIIASAKNAKNNRKHLKNSFAGLTALLRKIDPAHPLYQQTLMDRFILGVQLHEFDAVRDDYATLKALPTPSAYLREAFADYELAHASPHKALATYQSLAQSALDKKAPVSDELLLKMFSAASDAGEFALAQHYLEQINSSPYVNDYTHTSRVPNPSYDERYFGLARLALWRGNAGLAQKMIDERALDKTPGDGWVLLQKAELERNRYNFDEAKEWAHKAGVFFIESDQKYVRHALIEIALRQNDLPTAKRLIQEMSPEEMDSVKPLMERYELAHKGRIVGSVNLQHRTSAPTKQHNESTQDYAIYTPKTAEGHDLYVRYTESRVPVDGNSLNAQFIGAGTELNFYPLNVRIEAGKGIKLSKRGYVTSDLSYELNQRWAFNLRGHINGTDVPSRAAAQNVYTKGGGASVVYTYSDLFQLGGGVYFSRFSDSNLRHDANLWLNTKTFKHDRWALTNNFRVDYTRNKTVQSADYYNPIKAVSYEVGGDLSYYQPFDYALILTHHLKGNFGAYKQQAQQRSKTWSVSYGHEWRIGKQYGFLYEIGRKKNIYDGNPEFNNFGNLSFSLYY","341622","","possible outer membrane protein (hemin-binding protein / haemin storage protein)","Outer membrane, Periplasm, Extracellular","","
noIPR
unintegrated
unintegrated
signalp\"[1-26]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","BeTs to 4 clades of COG0457COG name: TPR-repeat-containing proteinsFunctional Class: RThe phylogenetic pattern of COG0457 is aompk-yqvd-lbcefghsnujxit-Number of proteins in this genome belonging to this COG is","","Residues 226 to 798 match (2e-10) PD:PD044048 which is described as PROTEOME COMPLETE MEMBRANE HMSH OUTER STORAGE YCDS HAEMIN TRANSMEMBRANE SYSTEM ","","","","","","","","","","","","Thu Dec 12 10:17:09 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00490 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Lillard,J.W. Jr., Fetherston,J.D., Pedersen,L., Pendrak,M.L. andPerry,R.D.Sequence and genetic analysis of the hemin storage (hms) system ofYersinia pestisGene 193 (1), 13-21 (1997)PubMed: 9249062","","Thu Dec 12 10:17:09 2002","1","","","" "AA00491","341640","343553","1914","ATGAAAATTTTACAAAAATTATTACAAATTATTGTCGTTTCATTTGTGTTTATCACCGGTGTAGCATCTGCTCAGGATAGATACGGCGTGCTGGCGTATCACTCAGTAGTGGATGATACGGCCGCAAAAGAAGAAAAACAGTATTTCCCGCAAACCATTTCCGCCAATTTGTTAATTAGCCATTTTAACTGGTTAAAAGATAACGGTTATAACGTGGTGAGCTGGCAGCAGATTATTGATGCGGAAAACGGCAAAAGTACTTTGCCGGAAAAAGCGGTGGTGCTTTCTTTTGATGATGGCTATGCCACCATGTATAACGTGATTTATCCGATTCTAAAGGCCTATAATTATCCCGCTGTGTTTGCCCCGGTAAGCAGTTGGTTGGATACGCCGGTAAACCAATTAATTCCTTATGCCAACATCAAACTTCCACGTAACGTTTTTGTTACTTGGGAGCAGGTGCGTGAAATGGAACAAAGTGGCTTGGTGGAAATCGCCTCCCACACGGATAATTTACACCATGGTGTGCGTGCCAATCCGGCGGGCAGCCAACTTCCGGCGGTGGTAGCACCGGAATATAAAAATAATCGATACGAGAGCAAAACGGAGTATAAAAATCGTTTAGTTCAGGATTTTTCCCGCTCATCAAAAAGCATTCAACGTCAAATCGGTAAGAAACCGCGTATTATGGTATGGCCTTACGGGCAATTTAATGACGTTGCCATAGACGCGGCAAAGCAATCGGGAATGACGCATCACTTTGCTTTAGGGCAGAAAATTATTAATAAAATTGGTGATAGATACGTCGGTCGTTTATTAATTGACACGGAAACCGGTTTCTCCACCATTAAAAATTTCCTTGATGGTGTGGATGATGAAAGTAAATTGATGCGCATAGTCCATATTGATCTCGACTCTCTTTATGACGCCGATAAAAAACAACAGGCAAAGAATTTTGATAAATTAATTGAGCGTATGTATCGTTATGGTATTACTACGGTTTATCTGAAAGCGTTTTCCGATCCGGACGGCGATGGCGTTGCCGATGCGTTGTATTTCCCGAATCGTTATTTACCGGTGCGGGATGATATTTTCAGTCAAATTGCCTGGCAGCTCAGAACTCGTGCCAACGTGAAGGTATATGCGTGGATGCCGGTTTTGGCGTTTGACTTGCGCAATCATGTTAAAGAGGCAACCTATGTGGTAGATCACCGCACAAACCAACCGGCAAAAGATAAATACTTACGCCTTTCGCCGTATGACCGAAAGAATGTGGAGATGATTAAGTCTATTTATAATGATTTATCATTCTATGCAAAATTTGACGGAATTTTATTCCATGATGATGCGTTTTTAACGGATTTTGAAGGCGTAGAAAGCCATAGTGAAGGTGATGGCGTGACTGCCGCTGCAAAACAAAAAACGTTAGATTTAATTGGTGTGACTGATGAGCTGACGAACGCGCTGAAACCTTATTTCCTAAGTAGTACGCCCGCCCTAAAAACCGTGCGTAGCTTGCATGCGTCGGTGATTACCAATCCGAAAGCGGAAGAATGGTTTGCACAAAATCTGACTACCTTAACTAAACACTATGATACTACGGCAATTATGGCGATGCCTTACATGGAACATCATCAGACAATTTCCGCCAAACAAGCGGAAAAATGGTTTGCTGCCCTGATTCAGCGGGTCAAAGCACAGGCACCGTTAAATAAAGTGTTATTTGAATTCCAGTCGGTGAATTTGAAAACCAAACAGCCAATTCCTGAAACAGAATTGATTAGCTGGATTGAATTGTTGCAACGCAACGGTATCTATAGTTACGGCTACTATCCGGATAATTTTGTTGCCGATCAGCCGAATATGCAAAAAATGAGACGTTATATGTCTCTGAATACTCAAGCAGGTAAACCA","","","72934","MKILQKLLQIIVVSFVFITGVASAQDRYGVLAYHSVVDDTAAKEEKQYFPQTISANLLISHFNWLKDNGYNVVSWQQIIDAENGKSTLPEKAVVLSFDDGYATMYNVIYPILKAYNYPAVFAPVSSWLDTPVNQLIPYANIKLPRNVFVTWEQVREMEQSGLVEIASHTDNLHHGVRANPAGSQLPAVVAPEYKNNRYESKTEYKNRLVQDFSRSSKSIQRQIGKKPRIMVWPYGQFNDVAIDAAKQSGMTHHFALGQKIINKIGDRYVGRLLIDTETGFSTIKNFLDGVDDESKLMRIVHIDLDSLYDADKKQQAKNFDKLIERMYRYGITTVYLKAFSDPDGDGVADALYFPNRYLPVRDDIFSQIAWQLRTRANVKVYAWMPVLAFDLRNHVKEATYVVDHRTNQPAKDKYLRLSPYDRKNVEMIKSIYNDLSFYAKFDGILFHDDAFLTDFEGVESHSEGDGVTAAAKQKTLDLIGVTDELTNALKPYFLSSTPALKTVRSLHASVITNPKAEEWFAQNLTTLTKHYDTTAIMAMPYMEHHQTISAKQAEKWFAALIQRVKAQAPLNKVLFEFQSVNLKTKQPIPETELISWIELLQRNGIYSYGYYPDNFVADQPNMQKMRRYMSLNTQAGKP","343554","According to Lillard et al., 1997, this is an outer membrane protein.","haemin storage system","Periplasm, Cytoplasm, Extracellular","","
InterPro
IPR002509
Domain
Polysaccharide deacetylase
PF01522\"[86-253]TPolysacc_deac_1
noIPR
unintegrated
unintegrated
signalp\"[1-24]?signal-peptide


","No hits to the COGs database.","","Residues 30 to 287 match (3e-11) PD:PD387882 which is described as PROTEOME ADHESION COMPLETE INTERCELLULAR ICAB ","","","","","","","","","","","Mon Feb 17 13:28:57 2003","Tue Jan 21 13:20:56 2003","","Thu Mar 18 09:19:55 2004","","Thu Mar 18 09:19:55 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00491 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Mar 18 09:19:55 2004","","","","","Residues 86 to 253 (E-value = 3.3e-27) place AA00491 in the Polysacc_deac_1 family which is described as Polysaccharide deacetylase (PF01522)","Thu Mar 18 09:19:55 2004","","","","Lillard,J.W. Jr., Fetherston,J.D., Pedersen,L., Pendrak,M.L. andPerry,R.D.Sequence and genetic analysis of the hemin storage (hms) system ofYersinia pestisGene 193 (1), 13-21 (1997)PubMed: 9249062","","Thu Dec 12 10:15:10 2002","1","","","" "AA00492","343718","344797","1080","ATGATTAGCCTCATGGTGCCTTGTTATAACGAGGGCAATAATCTTGATGAATCCATACCGCACTTGCTTCAGCTGAGATACCCGAATTACGAACTCATTTTTATTAATGACGGCAGTAAGGATAACACTGCTGAAGTCATTGATCGCTGGGCGGCGAAAGAACCTCGAATCACTGCATTGCACCAAGAAAATCAAGGCAAAGCCAGTGCATTGAATCATGGTTTAACGGTTGCCAAGGGAAAATACGTTGCCTGTATCGACGGTGATGCGGTATTGGATTACTACGCGCTGGACTACATGGTTCAAGCCTTAGAGCAAGATCCGAAATATGCTGCTACCACAGGTAATCCGCGTGTACGTAACCGTAGTACTATTTTGGGGCGTTTACAGGTATCCGAGTTCAGCTCCATCATCGGTCTAATTAAGCGGGCACAAGGTCTAATGGGCACAATCTTTACCGTTTCCGGCGTGTGTTGTTTATTCCGTAAAGATGTCATGGAAGAAATCGGTGGATGGAGTACTAACATGATCACCGAAGACATTGATATTAGCTGGAAAATTCAAATTGCCGGTTACAACATCATGTACGAACCACGCGCACTCTGCTGGGTGCTTATGCCGGAAAGCATAAAAGGGCTTTATAAACAGCGTTTGCGTTGGGCACAAGGCGGTGCGGAAACTATCATGAAGTATTTTTCGAAAATATGGCATTGGCGGAATCGTCGCTTGTGGCCAATGTATATTGAGTATTTTGCTACCGTTATTTGGGCATTTCTTTGGGTGTTACTTGCTGTTATTGCCTTAATTCAAAAATATATATTTGACATCAGTATTGAAAATATGGGGCTGTTTGAAACTAACATTTCCATTATGTTCTTCGCTTTCTTTTTACAATGTCTGTTAAGTTTGTATATTGATTCACGATATGAACGCAACTTACTACGTTATGGTTTATCTTGTATTTGGTATCCTTATGTCTATTGGCTATTAAATACCGTGACGTTATTGGTTGGTATTCCTAAGGCGATTTTCCGAAACAAATCAAAATTTGCCGTATGGACCAGCCCGGATAGAGGAGTA","","","47521","MISLMVPCYNEGNNLDESIPHLLQLRYPNYELIFINDGSKDNTAEVIDRWAAKEPRITALHQENQGKASALNHGLTVAKGKYVACIDGDAVLDYYALDYMVQALEQDPKYAATTGNPRVRNRSTILGRLQVSEFSSIIGLIKRAQGLMGTIFTVSGVCCLFRKDVMEEIGGWSTNMITEDIDISWKIQIAGYNIMYEPRALCWVLMPESIKGLYKQRLRWAQGGAETIMKYFSKIWHWRNRRLWPMYIEYFATVIWAFLWVLLAVIALIQKYIFDISIENMGLFETNISIMFFAFFLQCLLSLYIDSRYERNLLRYGLSCIWYPYVYWLLNTVTLLVGIPKAIFRNKSKFAVWTSPDRGV","344798","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR001173
Domain
Glycosyl transferase, family 2
PF00535\"[3-170]TGlycos_transf_2
noIPR
unintegrated
unintegrated
G3DSA:3.90.550.10\"[1-210]Tno description
PTHR22916\"[8-334]TGLYCOSYLTRANSFERASE
tmhmm\"[246-266]?\"[287-305]?\"[324-344]?transmembrane_regions


","BeTs to 6 clades of COG1215COG name: Glycosyltransferases, probably involved in cell wall biogenesisFunctional Class: MThe phylogenetic pattern of COG1215 is a-mpk-yq---lbcef-----j----Number of proteins in this genome belonging to this COG is","","Residues 2 to 106 match (2e-17) PD:PD023980 which is described as TRANSFERASE PROTEOME COMPLETE GLYCOSYLTRANSFERASE GLYCOSYL BIOSYNTHESIS POLYSACCHARIDE SPORE SUGAR COAT ","","","","","","","","","","","","Wed Jan 22 14:40:52 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00492 is paralogously related to AA02636 (1e-07), AA02499 (4e-06) and AA02640 (5e-04).","","","","","","Residues 3 to 170 (E-value = 4e-36) place AA00492 in the Glycos_transf_2 family which is described as Glycosyl transferase (PF00535)","","","","","","","","1","","","" "AA00493","344803","345093","291","ATGTCGTCGTCAGATGAACTGCAAAAACTCATGGTGATTGATAAAAGTGATCGTTTATCTTTCAAAATGTTAGTGAAAAACTTTATTTTGGATCTCCTCACTTGGGGATTATGGATTTACAGTATTGCGTTTATCATCAAATACGCCAAAGGGATCTTTACTCAGCCCGTGCTGGAACAATTTTTCTTTCACGACGTGATTGTAATCATGTTTAGTGCGGCGATTATCCTTGTTATCATTACATTCTTTTGGTCGATTATTTCAGCAGGAAGAAGGAGAAAAAAGAAAAAA","","","11393","MSSSDELQKLMVIDKSDRLSFKMLVKNFILDLLTWGLWIYSIAFIIKYAKGIFTQPVLEQFFFHDVIVIMFSAAIILVIITFFWSIISAGRRRKKKK","345094","","hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-43]?signal-peptide
tmhmm\"[28-48]?\"[67-87]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Dec 12 10:22:23 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00493 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00495","345199","345062","138","GTGGAAAATCCAAATGTTTTTTCAACCGCACTTTTTTATGTTGCTTTACAAGTTAAATGTGTTGATAGCGTTAAACCATTTCATCAAAATGAGAAATCTTTTCTTATTTTTTCTTTTTTCTCCTTCTTCCTGCTGAAA","","","5359","VENPNVFSTALFYVALQVKCVDSVKPFHQNEKSFLIFSFFSFFLLK","345062","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:06:19 2004","Sun Feb 22 16:06:19 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00495 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:06:19 2004","","","","","","","","","","","","","1","","","" "AA00497","346539","345217","1323","ATGGGTATTTTTAGTGTCCAGCCGGATTTGCCGGTGACCAAAAGCAAGGAAGAAATTGACAAAACGTACCGTTATTGGCGTATGCACCTGATGATTACCAGCTACATCGGCTATGCTGTATTTTATTTTACGCGGAAAAGTTTTAATTTTGTGATGCCGGCGATGTTAACAGATTTGGGCTTACAAAAAACGGATATTGGGATCATGGGCACTGCGTTTTACTTGACCTACGGCGTATCAAAATTTTTGTCTGGTGTGTTAGGTGACCGTTCAAACCCGCGCTATTTTATGGGCATCGGGTTGATGATGACCGGGGTGGTGAACATTTTCTTCGGCTTGAGCTCTTCAGTGTTTATGTTTATTACCCTTTGGATGATTAATGCGTTTTTCCAAGGCTGGGGCTGGCCGCCTTGTTCTAAGATTTTGAACACTTGGTATTCGCGCAATGAACGCGGTTTGTGGTGGGCAATTTGGAATACCTCGCACAACCTCGGCGGTGCGCTGATTCCGTTGCTCGCCGGTGCGGTAACGCTCTATTGGGGCTGGCGTTACGGCATGATTGTACCGGGGATTATTGCCTGTGTCGTCGGTTTTGCCATATGCTTCTTGTTGCGTGATCGCCCGACCTCCATAGGTTTGCCGACCGTGGGGGAATGGCGCAATGATGTGGCGGAAAAAGAACATGAAAGCGAAGGTGTGGGTTTATCCGACTGGGAAATTTTAAAAACCTATGTGTTCAAAAACACGATTATTTGGGCGCTCGCATTCTCTTGGTGTTTCATTTATATGGTTCGCACCGGGATTAACGACTGGGGCAATTTGTATTTAACGGAAACCCATGGCTACGACTTGTTAAAAGCCAATTCGGCGGTGTCCTTCTTTGAAATCGGCGGTTTCTTGGGTGCGTTATTTGCCGGTTGGGGATCTGATAAATTCTTCCACGGCAACCGCACTCAAATGAATATTATTTATGTGTTGGGCATTATTGCTGTGTCCCTCGCGCTATGGTTTATTCCGAGCGATAATTATTTCGTAATGAGCACCTTGTTCTTCTTAATGGGCTTCTTTATTTTCGGGCCACAATTCCTTATCGCCATGGCGGCAGCGGAAAACTCCCACAAATACGCCTCCGGTTCCGCCACCGGCTTTGTGAGCTTATTCGCATATATCGGTGCCGCTGCTGCCGGTGTACCGTTGGCGTGGATTATTAAATCCTTACACTGGAATGGCTTCTTCGGCAGCCTGTTTATTGTATCCTTGGGCTGTGCGTTATTACTGGTGTTGGTGTATTTCTTACAACGCCGTAAAAATGAAATGAAAGCA","","","52624","MGIFSVQPDLPVTKSKEEIDKTYRYWRMHLMITSYIGYAVFYFTRKSFNFVMPAMLTDLGLQKTDIGIMGTAFYLTYGVSKFLSGVLGDRSNPRYFMGIGLMMTGVVNIFFGLSSSVFMFITLWMINAFFQGWGWPPCSKILNTWYSRNERGLWWAIWNTSHNLGGALIPLLAGAVTLYWGWRYGMIVPGIIACVVGFAICFLLRDRPTSIGLPTVGEWRNDVAEKEHESEGVGLSDWEILKTYVFKNTIIWALAFSWCFIYMVRTGINDWGNLYLTETHGYDLLKANSAVSFFEIGGFLGALFAGWGSDKFFHGNRTQMNIIYVLGIIAVSLALWFIPSDNYFVMSTLFFLMGFFIFGPQFLIAMAAAENSHKYASGSATGFVSLFAYIGAAAAGVPLAWIIKSLHWNGFFGSLFIVSLGCALLLVLVYFLQRRKNEMKA","345218","","hexose phosphate transport system regulatory protein; regulator of uhpT expression","Inner membrane, Cytoplasm","","
InterPro
IPR000849
Family
GlpT transporter
TIGR00881\"[35-412]T2A0104: phosphoglycerate transporter family
PS00942\"[150-166]TGLPT
InterPro
IPR007114
Family
Major facilitator superfamily
PS50850\"[30-437]TMFS
InterPro
IPR011701
Family
Major facilitator superfamily MFS_1
PF07690\"[34-404]TMFS_1
noIPR
unintegrated
unintegrated
PTHR11662\"[15-436]TSODIUM-DEPENDENT PHOSPHATE TRANSPORTERS
PTHR11662:SF13\"[15-436]TGLYCEROL-3-PHOSPHATE TRANSPORTER (HEXOSE TRANSPORTER)
tmhmm\"[23-43]?\"[91-111]?\"[117-135]?\"[155-175]?\"[181-203]?\"[250-268]?\"[287-307]?\"[317-337]?\"[343-365]?\"[380-402]?\"[412-432]?transmembrane_regions


","BeTs to 8 clades of COG2271COG name: Sugar phosphate permeaseFunctional Class: GThe phylogenetic pattern of COG2271 is -----------lb-efgh--u-xi--Number of proteins in this genome belonging to this COG is","Significant hit (1.7e-131) to 7/7 blocks of the IPB000849 family, which is described as \"GlpT family of transporters\". Interpro entry for IP:IPR000849. IPB000849A 23-55 2.4e-17 IPB000849B 65-105 2.9e-25 IPB000849C 131-166 8.9e-22 IPB000849D 186-222 3e-18 IPB000849E 239-276 5.8e-19 IPB000849F 293-310 5.6e-08 IPB000849G 353-385 3.4e-14 IPB000849C 118-153 0.036","Residues 131 to 267 match (6e-12) PD:PD459784 which is described as PLASMID PHOSPHATE PROTEOME COMPLETE SUGAR TRANSPORTER GLYCEROL-3-PHOSPHATASE ","","","","","","","","","","","","Fri Jan 24 13:29:08 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00497 is paralogously related to AA02864 (6e-82), AA01378 (3e-72), AA02792 (6e-59) and AA01731 (5e-05).","","","","","","","","","","","Verhamme DT, Postma PW, Crielaard W, Hellingwerf KJ.Cooperativity in signal transfer through the Uhp system of Escherichia coli.J Bacteriol. 2002 Aug;184(15):4205-10.PMID: 12107138 Hall JA, Maloney PC.Pyridoxal 5-phosphate inhibition of substrate selectivity mutants of UhpT, the sugar 6-phosphate carrier of Escherichia coli.J Bacteriol. 2002 Jul;184(13):3756-8.PMID: 12057975Olekhnovich IN, Kadner RJ.Mutational scanning and affinity cleavage analysis of UhpA-binding sites in the Escherichia coli uhpT promoter.J Bacteriol. 2002 May;184(10):2682-91.PMID: 11976297 Schwoppe C, Winkler HH, Neuhaus HE.Properties of the glucose-6-phosphate transporter from Chlamydia pneumoniae (HPTcp) and the glucose-6-phosphate sensor from Escherichia coli (UhpC).J Bacteriol. 2002 Apr;184(8):2108-15.PMID: 1191434","","Thu Dec 12 11:21:08 2002","1","","","" "AA00499","346710","347339","630","ATGGATTTACACAACATTCGCGCAGAATACCGCAAAAAAGTGCTGTCGCAACTGGAATGCCACGCCAATCCCATCACGCAATTTGAACACTGGCTGGACGACGCCATCAACGCACAAGTGAATGAACCCACTGCCATGAACCTCGCCACCGTCAATGAAAACGGACGACCGAGCAGCCGCATGGTGCTATTAAAAGAAGTAAATGTGCAGGGGTTTGTGTTTTTCACCAACTACCACAGCCGCAAAGGACGCGCCATTGAACAACAGCCCTACGTCGCCTTAACCTTCTTCTGGCCGGAACTGGAACGCTCCGTACGCATCGAAGGCAAAGCGGAAAAAATCTCTGCCGAGCAATCGGACGCTTATTTCGCCAGCCGCCCATACACCAGCCGCATCGGCGCCTGGGCAAGCGAACAAAGTGCGGTCATTTCCGGCTACAAATCTTTACTCGCCAAAGCCGCCCTCATCGCCGCCCAACACCCCCTCAACGTCCCTCGCCCGGAATCCTGGGGCGGCTACCTCGTCACCCCCGACCGCATCGAATTCTGGCAAGGCAGACCCAGCCGCCTGCACGACCGCATTTGTTATTTGCTGGAAAACGGGGAATGGAAAAATGTGAGATTATCGCCG","","","24043","MDLHNIRAEYRKKVLSQLECHANPITQFEHWLDDAINAQVNEPTAMNLATVNENGRPSSRMVLLKEVNVQGFVFFTNYHSRKGRAIEQQPYVALTFFWPELERSVRIEGKAEKISAEQSDAYFASRPYTSRIGAWASEQSAVISGYKSLLAKAALIAAQHPLNVPRPESWGGYLVTPDRIEFWQGRPSRLHDRICYLLENGEWKNVRLSP","347340","","pyridoxamine-5'-phosphate oxidase","Cytoplasm","","
InterPro
IPR000659
Family
Pyridoxamine 5'-phosphate oxidase
PD006312\"[49-144]TPDXH_HAEIN_P44909;
PIRSF000190\"[1-210]TPyridoxamine-phosphate oxidase
PTHR10851\"[5-210]TPYRIDOXAMINE 5'-PHOSPHATE OXIDASE
TIGR00558\"[1-210]TpdxH: pyridoxamine 5'-phosphate oxidase
PS01064\"[180-193]TPYRIDOX_OXIDASE
InterPro
IPR001854
Family
Ribosomal protein L29
PS00579\"[139-153]?RIBOSOMAL_L29
InterPro
IPR011576
Domain
Pyridoxamine 5'-phosphate oxidase-related, FMN-binding core
PF01243\"[32-118]TPyridox_oxidase
InterPro
IPR012349
Domain
FMN-binding split barrel
G3DSA:2.30.110.10\"[5-210]Tno description


","No hits to the COGs database.","Significant hit ( 6.5e-76) to 5/5 blocks of the IPB000659 family, which is described as \"Pyridoxamine 5'-phosphate oxidase\". Interpro entry for IP:IPR000659. IPB000659A 31-51 1.8e-10 IPB000659B 71-114 2.6e-25 IPB000659C 122-148 7.3e-13 IPB000659D 164-193 7.3e-23 IPB000659E 206-210 80","Residues 23 to 210 match (5e-73) PD:PD006312 which is described as OXIDASE PYRIDOXAMINE 5'-PHOSPHATE COMPLETE PROTEOME OXIDOREDUCTASE PYRIDOXINE BIOSYNTHESIS PNP/PMP FMN ","","","","","","","","","","","","Thu Dec 12 10:41:52 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00499 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 32 to 118 (E-value = 5.4e-33) place AA00499 in the Pyridox_oxidase family which is described as Pyridoxamine 5'-phosphate oxidase (PF01243)","","","","","Mittenhuber G. Phylogenetic analyses and comparative genomics of vitamin B6(pyridoxine) and pyridoxal phosphate biosynthesis pathways. J Mol Microbiol Biotechnol. 2001 Jan;3(1):1-20. Review. PMID: 11200221 Di Salvo M, Yang E, Zhao G, Winkler ME, Schirch V. Expression, purification, and characterization of recombinantEscherichia coli pyridoxine 5'-phosphate oxidase. Protein Expr Purif. 1998 Aug;13(3):349-56. PMID: 9693059 Lam HM, Winkler ME. Characterization of the complex pdxH-tyrS operon of Escherichiacoli K-12 and pleiotropic phenotypes caused by pdxH insertionmutations. J Bacteriol. 1992 Oct;174(19):6033-45. PMID: 1356963 ","","Thu Dec 12 10:41:52 2002","1","","","" "AA00500","347291","347416","126","TTGTTATTTGCTGGAAAACGGGGAATGGAAAAATGTGAGATTATCGCCGTAAAAACGTTGGAAAAAAACACCGCACTTTTGGGGAAAGTGCGGTGGGATTTTAAATTGTTTTTTGATAGTGTCGAC","","","4814","LLFAGKRGMEKCEIIAVKTLEKNTALLGKVRWDFKLFFDSVD","347416","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:12:22 2004","Sun Feb 22 16:12:22 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00500 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:12:22 2004","","","","","","","","","","","","","1","","","" "AA00501","348074","347433","642","ATGGGAAATAAAATTTTTATTTCGTATAAATATTCTGACAATGCTGTTAAACAACTTAAAGAACCCAATAATTTGTTTTCATTCTATAGTCAATATAAAACAACTGCTCGTGATTATGTTGATATTATTCAAAATAAATTTGAGCGTGATGATATTCATATCAATAAAGGGGAAAATGATAATGAAAGTCTTGCCGGCTTTAAAACGGAGACTATTCGTTCAAAATTAGCAGAAAAGATTTTTGATAGTTCCGTTACCATTGTTCTTATCTCCCCCAATATAAAAAATTCTTGGAAATCAGAGAAAGATCAATGTATACCTTGGGAAATTGCTTATTCACTAAGAAGTAAGCGACGTCCAGATAACCGAAGCAAGCGTAATGCAATTTTATTGGTCGTTCTACCTGATAGATATGGTTATTATGATTACGTAAATTCATATGGCTTTTATTTTGATATTATTCAAAGAAACTTGAATAACCTGCATACACCATATACTACATATAAACTAAGGAATGGTTGTTCTAATTCATATATGCTTCAATGTAACTGGGATAAGTTTATCTCTAATCCGAATGCTTGGATTGAAGCTGCAATAGAAATTAGAGATAAAGGAAATAATTATAATATTGTAATAAGACCA","","","25222","MGNKIFISYKYSDNAVKQLKEPNNLFSFYSQYKTTARDYVDIIQNKFERDDIHINKGENDNESLAGFKTETIRSKLAEKIFDSSVTIVLISPNIKNSWKSEKDQCIPWEIAYSLRSKRRPDNRSKRNAILLVVLPDRYGYYDYVNSYGFYFDIIQRNLNNLHTPYTTYKLRNGCSNSYMLQCNWDKFISNPNAWIEAAIEIRDKGNNYNIVIRP","347434","","hypothetical protein","Outer membrane, Periplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Dec 12 11:53:24 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00501 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00502","348584","348105","480","ATGAAGAGAAATGTATTTTATAGTTTTCATTATGAAAAAGATGTTTTCCGTGTTCAACAAGTAAGAAACATTGGAAAGCTAGAAGGCAATCCACCAGCGACACCTAATACCTGGGAAGAAATAAAAAGGAAAGGAGATAAAGAAATACAAAAATGGATTGATGAAAATTTATCTGGTAAAAGCTGTCTGGTTGTTCTGATTGGAGAAGATACATCTAAACGAAAATGGGTTAAGTATGAAATTCAAAAAGCTTGGAATGATGGAAAAGGCGTATTGGGTATCTATATTCATAACCTGAAAGATCCAAAAAGTGGTGAATGTAGAAAAGGCGACAATCCATTTGAACAATTTACGTTCGAAAATGGTTCTAAATTATCTAGCATAGTCAAATGTTATAATCCTAAATCTTCGGATGCCTATAATGATATTGCAGATAATATAGAAAAATGGATTGAAGAGGCTATTTCCATTCGTAAAAAA","","","18588","MKRNVFYSFHYEKDVFRVQQVRNIGKLEGNPPATPNTWEEIKRKGDKEIQKWIDENLSGKSCLVVLIGEDTSKRKWVKYEIQKAWNDGKGVLGIYIHNLKDPKSGECRKGDNPFEQFTFENGSKLSSIVKCYNPKSSDAYNDIADNIEKWIEEAISIRKK","348106","","conserved hypothetical protein","Periplasm, Cytoplasm","","
InterPro
IPR015032
Family
Domain of unknown function DUF1863
PF08937\"[49-94]TDUF1863


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Dec 12 11:56:05 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00502 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00503","349849","348590","1260","ATGAATTTAGATATAGACAAAGAAGAAAGCAATCTAGTCTCTTTGGCTCAGTATTATGTCAATAGTAAATGTGGTAAACGTTCAAAAATCAACCAACTCATTTTAGATGAGTTTTCCCAGAGTGCTACATTGACAGAAAATCATAAAATATTAGCTAGACTTCCCATAGATACTTTCTGGACAACCAATTATGACTCTATGATAGAAACAGCATTAAAAGAAGCTGGGAAAGTTGTGGATGTAAAGCACTGCGTAGAACAACTTCCAATATCAATTCATAAAAGAGATGTTGTTGTATATAAAATGCATGGCGATGCTTCTCTGCCAAATCAAACTGTTCTTATCAAGGACGATTATGAGAAATTTCATTTAACAAGAAATGACTTTTTTAATGCTTTGCGTGGAGATCTATTAACAAAAAGATTTTTATTTTTAGGGTTTAGCTTTTCAGATCCTAATATTGATTATATTCTGAGTCGGATTAGAGCGTCATATAGTGAAAATCAAAAAGAGCATTTTTGTATTTTAAGAAAAGTCCAAAAGAATGAGAATGAACCACAAGATGAATTTGAATACAGACAACGGAAGCAACAATTTTTTATTTCAGATTTAGAGCGAGTAGGAATTAGTGCGTTATTAATTGATGATTATTCAGAAATTACAGAAATATTGATGGAAATAGAACAAGCTCAAAAACGTAAAACTATTTTTATCTCAGGGGCAGCAGAAAATTATTCTCCTTATTCTCAGCAAGAAGTTGAACAATTTGTTTCTTCTCTTTCTCAAGAGATTTTAAAACTAGGGTATCGTATTGTTACAGGTTTTGGATTAGGAATAGGTAGCTCAGTTATTTCAGGCGCAATAAAACATCTTACGGAACAAAATTTAAAAATAGATGAGGACTATTTGATACTTCGCCCATTCCCTCAGAATAAAGAAGGGAAAGAATTGTGGTCTGCTTGGCGTGAAGATATGATTTCTTATGCTGGTATCTCTATATTTCTATTCGGAAATAAATTACAGAATGGAAATTTGATTTTATCAAATGGTATGCAGGAGGAATTTGATATTTCCAAAAGGAATGGAAATGTTTTAATCCCTGTTGCTGCTACTGGATATATGGCAAAACAACTCTGGGATAATGAGATGAATAAAGAGTCTGCTAAGGAGGTTGAAAATGAAATGCAAGCACTATCTAAAGAAAATATTTCGCTAGATGAATTAAGATCTAATATTTTGTCAATTTTAAAAAAGGTTAAA","","","53778","MNLDIDKEESNLVSLAQYYVNSKCGKRSKINQLILDEFSQSATLTENHKILARLPIDTFWTTNYDSMIETALKEAGKVVDVKHCVEQLPISIHKRDVVVYKMHGDASLPNQTVLIKDDYEKFHLTRNDFFNALRGDLLTKRFLFLGFSFSDPNIDYILSRIRASYSENQKEHFCILRKVQKNENEPQDEFEYRQRKQQFFISDLERVGISALLIDDYSEITEILMEIEQAQKRKTIFISGAAENYSPYSQQEVEQFVSSLSQEILKLGYRIVTGFGLGIGSSVISGAIKHLTEQNLKIDEDYLILRPFPQNKEGKELWSAWREDMISYAGISIFLFGNKLQNGNLILSNGMQEEFDISKRNGNVLIPVAATGYMAKQLWDNEMNKESAKEVENEMQALSKENISLDELRSNILSILKKVK","348591","","conserved hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","Residues 1 to 123 match (4e-20) PD:PD407727 which is described as USG SIR2-LIKE PROTEOME PLASMID SILENCER COMPLETE ORF25 TRANSCRIPTIONAL ","","","","","","","","","","","","Thu Dec 12 12:18:08 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00503 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00504","351347","350049","1299","ATGAAACGCTATATTTTAGACTTATTACAAAAGTGGAAAACCAAGCCCAATCGTAAGCCATTAATTATTCAAGGTGCTCGACAAGTGGGCAAAACCTGGGCAATGAAACATTTTGGCGAACAGGCTTTTGAACAAGTCGCCTACATTAACTTCGATAATAATCCGCGCATGAAAACCCTCTTCGCAGGCGATTACAATATCGATCGTTTAATCCTCGGGTTAAAAATCGAAAGTGGCGTGGATATTCAAGCGGACAACTCGCTAATCATTTTTGATGAAATCCAAGAAGTGCCACAAGCCCTCTCCTCCCTCAAATATTTTTATGAAAACGCACCGCACTTTTACATTGTCACCGCCGGCTCGTTGCTTGGCGTTTCGCTCCACCATCAAGCCTCTTTTCCTGTGGGGAAAGTGGACTTTCAGCCTATTTACCCCATGGATTTTCGTGAATTTCTACTTGCCATGAGCAAGCCGGATCTCGTGCAATTACTGGAAATGCAGGATTGGGCATTAATTAGCGCAATGAAATCCACATACATTGACTTACTGCGCCAATATTATTTTGTGGGCGGTATGCCGGAAGCGGTCAAAACCTTTGTGGAAACGCAGAATTTGAATGAGGTTCGGCAAATCCAACGCAATTTGTTGATGGCATACGAACAGGATTTTTCCAAACACATTAGCGACGGGCAAACGGTGCAGCGGGTACGTGCATTATGGAACAGCATTCCGGAACAGCTAGCAAAAGAAAACAAAAAATTCGTCTATTCCCAACTGCAAAAAGGAGCGCGCAGTAAAGATTATGAAATCGCCCTGCAATGGTTAAAAGACAGCGGCTTAGTCCATGTCGTGCCACGTATTAAAAAGCCGCATTTACCGCTGAGCGCCTATCAAGACAACGCCTTTAAATTATTCAGCCTTGATGTGGGCTTGCTCGGCGCACAAAGCTATTTAGACTCGACAGTGCTTTTGGAAGGCAACCGCCTATTCACCGAATTCAAAGGTGCACTGACGGAACAATATGTCCTGCAACAACTTTTGGTGCTGCAAGACAATCCCGTTTTCTACTGGGCAACGGAAAAAGGCACGGCAGAAGTAGATTTTGTGCTACAACAAGGACAAAACATCACCCCAATTGAAGTGAAAGCGGAAGAAAATTTAAAGGCAAAGAGTTTAAAAGTCTACGTAGATCAATTCCAACCCAAACGCGCTTTACGGTTTTCAATGGCAGATTATAAGGAACAGGATTGGGTGGTGAATGTGCCGTTGTATGGGGTGACGAGTTTATTTAAAAGCACT","","","49866","MKRYILDLLQKWKTKPNRKPLIIQGARQVGKTWAMKHFGEQAFEQVAYINFDNNPRMKTLFAGDYNIDRLILGLKIESGVDIQADNSLIIFDEIQEVPQALSSLKYFYENAPHFYIVTAGSLLGVSLHHQASFPVGKVDFQPIYPMDFREFLLAMSKPDLVQLLEMQDWALISAMKSTYIDLLRQYYFVGGMPEAVKTFVETQNLNEVRQIQRNLLMAYEQDFSKHISDGQTVQRVRALWNSIPEQLAKENKKFVYSQLQKGARSKDYEIALQWLKDSGLVHVVPRIKKPHLPLSAYQDNAFKLFSLDVGLLGAQSYLDSTVLLEGNRLFTEFKGALTEQYVLQQLLVLQDNPVFYWATEKGTAEVDFVLQQGQNITPIEVKAEENLKAKSLKVYVDQFQPKRALRFSMADYKEQDWVVNVPLYGVTSLFKST","350050","The COG hits are fairly weak, expect values range from 4e-04 to 8.8.","ATPase","Periplasm, Cytoplasm","","No hits reported.","BeTs to 5 clades of COG1373COG name: Uncharacterized ATPases of the AAA superfamilyFunctional Class: RThe phylogenetic pattern of COG1373 is --mpk---v-r------h--uj----Number of proteins in this genome belonging to this COG is","","","","","","","Tue Feb 18 15:49:17 2003","","","","","","Thu Dec 12 12:27:09 2002","Fri Nov 21 14:12:17 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00504 is paralogously related to AA00811 (8e-05).","","","","","","","","","","","","","","1","","","" "AA00505","351793","351701","93","TTGCAGGAACGCTCGTCCTATTATCAAGATGCGCAACACTACAACCTCGCAGGCAACTTCGCCGCTGGTCTGGCAGAGGTCACCGATACGTGG","","","3502","LQERSSYYQDAQHYNLAGNFAAGLAEVTDTW","351701","","hypothetical protein","Cytoplasm, Extracellular","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:13:40 2004","Sun Feb 22 16:13:40 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00505 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:13:40 2004","","","","","","","","","","","","","1","","","" "AA00506","353149","351821","1329","ATGACAAACCTCATCCAATTTGCAGATTTTGATCTCGCGCCCGAATTACTCAACGCCCTTCAGAAAAAAGGTTATCAGCGCCCCACCGCGATCCAGCAGGAAACCATTCCGGCGGCGATGGAAGGCGGTGACGTATTGGGTTCCGCGCCCACCGGCACCGGTAAAACGGCGGCGTTTCTGTTGCCGGCGATTCAGCATTTGCTGGATTACCCACGTCGTAAACCGGGTGCGCCGCGCGTGTTGGTGTTAACGCCGACCCGTGAACTTGCCATGCAGGTAGCGGAACAGGCGAAGGAGCTTGCCTGCTTCACCAAACTCAGTATCGCGACTATTACGGGCGGTGTGGCGTATCAAAATCACGGGGAAATTTTCAATAAAAATCAAGATATTGTAGTTGCCACGCCGGGACGGTTGTTGCAATACATTAAAGAAGAAAATTTTGATTGCCGCACGGTGGAGATTCTTATTTTCGATGAAGCGGACAGAATGTTGCAAATGGGGTTCGGGCAGGATGCGGAAAAAATTGCGGCGGAAACCCGCTGGCGCAAGCAAACCTTGTTGTTCTCCGCAACTCTTGAAGGCGATTTGCTGGAGGATTTTGCCGCACGTACTTTAAACGAACCGGTGAAAATTGAGGCGGAACCGAGCCGCCGTGAACGCAAGAAAATTCAGCAATGGTATTACCACGCCGACAGCCATGAGCATAAATTCAAATTGCTGGCACGCTTCATTGAACAGGAGCAGGTGAGCAAAGGCATTGTGTTCGTGCGTCGCCGCGAAGAAGTGCGCGAACTGGCGGAAAATTTGCGTAAGCGTGGTATTCGCAGCGCCTATCTGGAAGGCGAAATGGCACAAACCCAGCGCAATAATGCCATCGACAAGCTGAAAAACGGCGTGGTAAAAGTGCTGGTTTCCACGGATGTCTCCGCACGTGGCATTGATATTGATGATGTCAGCCACATTATGAATTTCGATTTACCATACAGCGCCGACACGTATTTGCACCGCATCGGGCGCACCGCACGCGCCGGCAAAAAAGGCACCGCGGTGTCTTTTGTGGAAGCTCACGATTACCGCCTGCTCGGCAAAATCAAACGTTATACCGGCGAAATCTTAAAAGCACGCGTCATTGAGGGCTTGGAACCACGCACCAAAGCACCGAAAGACGGCGAAATCAAAACCGTCAGCAAGAAACAAAAAGCGAAGAAACTCGAAAAACGTGAAGCGCGGAAAAAAGCGGATAAGAAAGTCAAACAGCGCCATCAAGATCGTAAAAACATTGGTAAGCGCCGCAAACCGAGCGCTTCAACCACGGCAGCAGCCGTTAAA","","","50045","MTNLIQFADFDLAPELLNALQKKGYQRPTAIQQETIPAAMEGGDVLGSAPTGTGKTAAFLLPAIQHLLDYPRRKPGAPRVLVLTPTRELAMQVAEQAKELACFTKLSIATITGGVAYQNHGEIFNKNQDIVVATPGRLLQYIKEENFDCRTVEILIFDEADRMLQMGFGQDAEKIAAETRWRKQTLLFSATLEGDLLEDFAARTLNEPVKIEAEPSRRERKKIQQWYYHADSHEHKFKLLARFIEQEQVSKGIVFVRRREEVRELAENLRKRGIRSAYLEGEMAQTQRNNAIDKLKNGVVKVLVSTDVSARGIDIDDVSHIMNFDLPYSADTYLHRIGRTARAGKKGTAVSFVEAHDYRLLGKIKRYTGEILKARVIEGLEPRTKAPKDGEIKTVSKKQKAKKLEKREARKKADKKVKQRHQDRKNIGKRRKPSASTTAAAVK","351822","","ATP-dependent RNA helicase protein","Cytoplasm","","
InterPro
IPR000629
Domain
ATP-dependent helicase, DEAD-box
PS00039\"[156-164]?DEAD_ATP_HELICASE
InterPro
IPR001650
Domain
Helicase, C-terminal
PF00271\"[268-344]THelicase_C
SM00490\"[263-344]THELICc
PS51194\"[236-388]THELICASE_CTER
InterPro
IPR011545
Domain
DEAD/DEAH box helicase, N-terminal
PF00270\"[29-200]TDEAD
InterPro
IPR014001
Domain
DEAD-like helicases, N-terminal
SM00487\"[24-226]TDEXDc
InterPro
IPR014014
Domain
DEAD-box RNA helicase Q motif
PS51195\"[5-33]TQ_MOTIF
InterPro
IPR014021
Domain
Helicase superfamily 1 and 2 ATP-binding
PS51192\"[36-210]THELICASE_ATP_BIND_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[2-221]Tno description
PTHR10967\"[7-432]TDEAD BOX ATP-DEPENDENT RNA HELICASE
PTHR10967:SF52\"[7-432]Tgb def: ATP-dependent RNA helicase srmB


","BeTs to 20 clades of COG0513COG name: Superfamily II DNA and RNA helicasesFunctional Class: L,K,JThe phylogenetic pattern of COG0513 is a-mp--yq-drlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is","Significant hit ( 7.8e-83) to 5/5 blocks of the IPB000629 family, which is described as \"ATP-dependent helicase, DEAD-box\". Interpro entry for IP:IPR000629. IPB000629A 24-67 5.2e-28 IPB000629B 81-93 1.1e-06 IPB000629C 129-140 9.1e-06 IPB000629D 152-175 2.4e-10 IPB000629E 306-347 1.3e-26","Residues 14 to 192 match (3e-07) PD:PD578309 which is described as HELICASE PROBABLE ATP-DEPENDENT C22F3.08C ATP-BINDING RNA ","","","","","","","","","","","","Thu Dec 12 12:36:57 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00506 is paralogously related to AA00148 (2e-69), AA00263 (2e-61), AA00927 (3e-15), AA02480 (4e-06) and AA01928 (5e-04).","","","","","","Residues 268 to 344 (E-value = 4.5e-30) place AA00506 in the Helicase_C family which is described as Helicase conserved C-terminal domain (PF00271)","","","","","Du MX, Johnson RB, Sun XL, Staschke KA, Colacino J, Wang QM.Comparative characterization of two DEAD-box RNA helicases in superfamily II: human translation-initiation factor 4A and hepatitis C virus non-structural protein 3 (NS3) helicase.Biochem J. 2002 Apr 1;363(Pt 1):147-55.PMID: 11903057 Py,B., Higgins,C.F., Krisch,H.M. and Carpousis,A.J. A DEAD-box RNA helicase in the Escherichia coli RNA degradosome. Nature 381 (6578), 169-172.1996. PubMed: 8610017. Peng,H.L., Hsieh,M.J., Zao,C.L. and Chang,H.Y. Nucleotide sequence and expression in Escherichia coli of theKlebsiella pneumoniae deaD gene. J. Biochem. 115(3): 409-414.1994. PubMed: 8056751. Toone,W.M., Rudd,K.E. and Friesen,J.D. deaD, a new Escherichia coli gene encoding a presumedATP-dependent RNA helicase, can suppress a mutation in rpsB,the gene encoding ribosomal protein S2. J. Bacteriol. 173(11): 3291-3302.1991 PubMed: 2045359.Kalman,M., Murphy,H. and Cashel,M. rhlB, a new Escherichia coli K-12 gene with an RNA helicase-like protein sequence motif, one of at least five such possible genes in a prokaryote. New Biol. 3(9): 886-895.1991 PubMed: 1931833.","","Thu Dec 12 12:43:54 2002","1","","","" "AA00507","353136","353261","126","ATGAGGTTTGTCATTGGTATTTTTCGTTCATTAGCATTAAAATTGCGCCGAATTATACCGCACTTTGCTATTAAAGTGCGGTTGTTTTTAGTGATGTTTTTTGATGAACAATATGGGATTTCAATT","","","5039","MRFVIGIFRSLALKLRRIIPHFAIKVRLFLVMFFDEQYGISI","353261","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-39]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:15:02 2004","Sun Feb 22 16:15:02 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00507 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:15:02 2004","","","","","","","","","","","","","1","","","" "AA00508","353236","353943","708","TTGATGAACAATATGGGATTTCAATTTAAGCAATTTCGCGTAAATCATGATCGTTGCGCCATGAAAGTGGGCACGGACGGCATTTTATTAGGCGCTTGGGCGAATGTGACGCAGGCAAAACAGATTTTGGATTTGGGCTGCGGTAGTGGGCTGATCGCCTTGATGTTGGCGCAGCGGAGTTCGGCGGAAAGTCGAATTTGCGCCGTGGAAATCGATCCTGCCGCCGCACAACAGGCGCAGGAAAACGTATCGGCATCGCCTTGGAAAGATAAAATTCAGGTGTATCAACAGAATATAGAAACTTTCTGTGCGCAAAGTAAGCACGCTTTTGACTTGATTGTCGCCAACCCACCCTATTTTCAAACAGGCGTGGATTGCCGTAATGAGGCGCGCAATACCGCCCGTTATTTGGCTTCCCAAAGCCATTTGCATTGGTTGGAAACCGCCGCGTCTTGCTTGGCGTCGAAAGGTAAGATCAGTTTTGTATTGCCTTTGGAGGCGGGCGAAACGCTGTTAAAAACCACCGCACTTTATTGCGTTGAGCGTTGTGATGTGACGACCAAACAGGGAAAAATGCCGCAGCGGATGTTATTAACCTTCGCCATGCAACCACAACCTCTGCAACATAGCCGACTGATTATTTATGATGCGCATCATCGCTACCATGATGATTTTGTGGCGTTGACGCGGGAATTTTATTTGAAGTTT","","","26515","LMNNMGFQFKQFRVNHDRCAMKVGTDGILLGAWANVTQAKQILDLGCGSGLIALMLAQRSSAESRICAVEIDPAAAQQAQENVSASPWKDKIQVYQQNIETFCAQSKHAFDLIVANPPYFQTGVDCRNEARNTARYLASQSHLHWLETAASCLASKGKISFVLPLEAGETLLKTTALYCVERCDVTTKQGKMPQRMLLTFAMQPQPLQHSRLIIYDAHHRYHDDFVALTREFYLKF","353944","","SAM-dependent methyltransferase","Cytoplasm, Periplasm","","
InterPro
IPR002052
Domain
N-6 Adenine-specific DNA methylase
PS00092\"[113-119]?N6_MTASE
InterPro
IPR002296
Family
N6 adenine-specific DNA methyltransferase, N12 class
PR00507\"[42-56]T\"[110-122]T\"[140-164]TN12N6MTFRASE
InterPro
IPR013216
Domain
Methyltransferase type 11
PF08241\"[43-116]TMethyltransf_11
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[40-198]Tno description
PTHR18895\"[24-223]TMETHYLTRANSFERASE
PTHR18895:SF4\"[24-223]TRNA METHYLTRANSFERASE


","No hits to the COGs database.","Significant hit ( 1.8e-11) to 3/4 blocks of the PR00507 family, which is described as \"N12 class N6 adenine-specific DNA methyltransferase signature\". Prints database entry for PR:PR00507. PR00507B 42-56 1.4 PR00507C 110-122 1.5e-05 PR00507D 140-164 0.15","Residues 35 to 84 match (6e-10) PD:PD016907 which is described as COMPLETE PROTEOME METHYLTRANSFERASE TRANSFERASE TRNA 2.1.1.- HEMK PROCESSING RNA RRNA ","","","","","","","","","","","","Thu Feb 20 09:41:34 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00508 is paralogously related to AA02818 (4e-05), AA02562 (2e-04), AA00174 (2e-04) and AA00647 (2e-04).","","","","","","","","","","","Morel G, Ban M, Hettich D, Huguet N.Role of SAM-dependent thiol methylation in the renal toxicity of several solvents in mice.J Appl Toxicol. 1999 Jan-Feb;19(1):47-54.PMID: 9989477 Cheng X.Structure and function of DNA methyltransferases.Annu Rev Biophys Biomol Struct. 1995;24:293-318. Review.PMID: 7663118","","Thu Dec 12 12:56:01 2002","1","","","" "AA00511","354542","354024","519","GTGGTGTTCGTCAGTAAAGGAAAAATCAGTAACTATTTGTTCGGCCTTATCTTTGCTTACACTTATTTCTATGTCGCGTGGAAGGCGAATTTCATCGGCGAAATGAACACCGTGCTATACGTTTACCTTCCGGCGCAATTTATCGGCTATTTCACGTGGAAAGCCCATATGCAACAAGAAAAAAGCGGTAGCGAAAGTGTGATTGCTAAATCGCTGACTTTGCAGGGCTGGATTGTGCTCGCTGCTACTGTTAGTGTCGGCACGCTATTATTCGTGCAGGCACTAAAAGCCGCAGGCGGGAGTTCTACCGGCTTAGACGGCTTAACCACCATCATCACCGTCGCTGCACAGTTATTGATGATTTTGCGTTACCGCGAACAATGGCTGTTGTGGATTTTGCTGAACATTATCTCCATTTTGTTATGGGCAGAAACACCGGCAATATACCTCATGTACAGCGCCTATTTGCTTAACTCTTTGTATGGTTATTATAACTGGACGAAGTTGGCAAAACAGGGC","","","25730","VVFVSKGKISNYLFGLIFAYTYFYVAWKANFIGEMNTVLYVYLPAQFIGYFTWKAHMQQEKSGSESVIAKSLTLQGWIVLAATVSVGTLLFVQALKAAGGSSTGLDGLTTIITVAAQLLMILRYREQWLLWILLNIISILLWAETPAIYLMYSAYLLNSLYGYYNWTKLAKQG","354025","","nicotinamide mononucleotide transporter","Inner membrane, Extracellular","","
InterPro
IPR006419
Family
Nicotinamide mononucleotide transporter PnuC
PF04973\"[1-137]TNMN_transporter
TIGR01528\"[1-172]TNMN_trans_PnuC: nicotinamide mononucleotide
noIPR
unintegrated
unintegrated
signalp\"[1-29]?signal-peptide
tmhmm\"[9-29]?\"[35-53]?\"[74-94]?\"[100-122]?\"[132-152]?transmembrane_regions


","BeTs to 3 clades of COG3201COG name: Nicotinamide mononucleotide transporterFunctional Class: HThe phylogenetic pattern of COG3201 is -----------l--ef-h--u-----Number of proteins in this genome belonging to this COG is","","Residues 1 to 122 match (5e-34) PD:PD032505 which is described as COMPLETE PROTEOME TRANSPORTER NICOTINAMIDE MONONUCLEOTIDE PROBABLE TRANSMEMBRANE PM1838 TRANSPORTER HI1077.1 ","","","","","Tue Feb 18 09:42:57 2003","","","","","","","Thu Dec 12 13:14:48 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00511 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 137 (E-value = 4e-49) place AA00511 in the NMN_transporter family which is described as Nicotinamide mononucleotide transporter (PF04973)","","","","","Kurnasov OV, Polanuyer BM, Ananta S, Sloutsky R, Tam A, GerdesSY, Osterman ARibosylnicotinamide Kinase Domain of NadR Protein: Identificationand Implications in NAD Biosynthesis.J Bacteriol. 2002 Dec;184(24):6906-17.PMID: 12446641Penfound T, Foster JW.NAD-dependent DNA-binding activity of the bifunctional NadR regulator of Salmonella typhimurium.J Bacteriol. 1999 Jan;181(2):648-55.PMID: 9882682","","Tue Feb 18 09:42:57 2003","1","","","" "AA00512","354709","354551","159","ATGAACCCAGAGCAACTCCTACAAAAAGCCAAACAGGAACTCTTTTCCGGCTGGAAACCCTTTGAGGTTTTCTGGTTATTACTTTTCATCGCGGCGCAAATTATTGCATTTGTGTTGGATCCGCAATCGCCTCTCGCCATGATTCCGGCATTGCCGGCG","","","5994","MNPEQLLQKAKQELFSGWKPFEVFWLLLFIAAQIIAFVLDPQSPLAMIPALPA","354551","","conserved hypothetical protein","Periplasm, Inner membrane, Cytoplasm","This sequence is weakly similar to gi|42630110, an unknown from H.influenzae. See also gi|15603703 from P.multocida.","
InterPro
IPR006419
Family
Nicotinamide mononucleotide transporter PnuC
PF04973\"[17-51]TNMN_transporter
noIPR
unintegrated
unintegrated
signalp\"[1-36]?signal-peptide
tmhmm\"[21-39]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:18:29 2004","Sun Feb 22 16:18:29 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA0336, a predicted nicotinamide mononucleotide transporter.AA00512 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:18:29 2004","","","","","","","","","","","","","1","","","" "AA00513","355090","355746","657","ATGGCTCTGATTGAATATAACCCACCGCAGGAACCTTGGCTGGATTTGGTGTATCGAGATGATTACATCGCCGTGGTGAATAAACCGAGCGGCTTGCTTTCGGTGCCGGGCAATCAGCCGCAATATTATGACAGCGCCATGTCGCGGGTGAAAGAAAAATACGGTTTTTGCGAACCGGCACACCGGCTGGACATGGCAACCAGTGGCATTCTGCTGTTTGCCTTAAGCAAATCGGCGGATCGCGAATTAAAACGTCAATTTCGCGAACGTGAACCGAAAAAATATTATCAGGCGCTGGTTTGGGGGCATTTGGAACAAGAGCAAGGTATGGTGGAATTGCCGCTCATTTGCGATTGGGAAAACCGCCCACGCCAGAAAATTTGCTTCGAACGGGGAAAAAGAGCGGTCACTTTTTACGACGTTTTGCAGCGTTATCCAAATAACACCACCCGCATAAAACTCACGCCGATTACCGGTCGCTCCCATCAATTACGCCTGCACATGCTGGCGCTCGGACACCCGATTTTAGGCGATAAATTCTACGCCCACCCACAAGCCAAAGCCCTCTCGCCCCGCTTATGCCTGCACGCCGAAAGCCTGCAAATCCGGCACCCGATCACCGGCGAAACCATGGAATTCACCACACTGGTCGGGTTT","","","25400","MALIEYNPPQEPWLDLVYRDDYIAVVNKPSGLLSVPGNQPQYYDSAMSRVKEKYGFCEPAHRLDMATSGILLFALSKSADRELKRQFREREPKKYYQALVWGHLEQEQGMVELPLICDWENRPRQKICFERGKRAVTFYDVLQRYPNNTTRIKLTPITGRSHQLRLHMLALGHPILGDKFYAHPQAKALSPRLCLHAESLQIRHPITGETMEFTTLVGF","355748","","pseudouridylate synthase (pseudouridine synthase)","Cytoplasm","","
InterPro
IPR006145
Domain
Pseudouridine synthase
PD001819\"[61-105]TRLUA_HAEIN_P44782;
PF00849\"[22-170]TPseudoU_synth_2
InterPro
IPR006224
Family
Pseudouridine synthase, Rlu
PS01129\"[60-74]TPSI_RLU
noIPR
unintegrated
unintegrated
PTHR10436\"[8-213]TRIBOSOMAL PSEUDOURIDINE SYNTHASE


","BeTs to 19 clades of COG0564COG name: Pseudouridylate synthases, 23S RNA-specificFunctional Class: JThe phylogenetic pattern of COG0564 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-49) to 4/4 blocks of the IPB000613 family, which is described as \"Pseudouridine synthase\". Interpro entry for IP:IPR000613. IPB000613A 16-36 2.1e-07 IPB000613B 60-99 4.1e-20 IPB000613C 158-182 6.7e-14 IPB000613D 192-205 0.0008Significant hit ( 2.1e-44) to 3/3 blocks of the IPB002990 family, which is described as \"Pseudouridine synthase, Rlu family\". Interpro entry for IP:IPR002990. IPB002990A 16-36 7.8e-07 IPB002990B 60-98 4.3e-20 IPB002990C 158-182 1.2e-14","","","","","","","","","","","","Fri Jan 7 17:18:04 2005","Thu Dec 12 13:25:05 2002","","Fri Jan 7 17:11:44 2005","Fri Jan 7 17:18:04 2005","","yes","Fri Feb 20 15:41:32 MST 1998","AA00513 is paralogously related to AA02913 (6e-29), AA02276 (6e-26), AA01355 (9e-24) and AA02063 (7e-13).","Fri Jan 7 17:11:44 2005","","","","","Residues 22 to 170 (E-value = 5e-57) place AA00513 in the PseudoU_synth_2 family which is described as RNA pseudouridylate synthase (PF00849)","Fri Jan 7 17:11:44 2005","","","","Spedaliere CJ, Hamilton CS, Mueller EGFunctional importance of motif I of pseudouridine synthases: mutagenesis of aligned lysine and proline residues.Biochemistry. 2000 Aug 8;39(31):9459-65.PMID: 10924141Raychaudhuri S, Niu L, Conrad J, Lane BG, Ofengand J.Functional effect of deletion and mutation of the Escherichia coli ribosomal RNA and tRNA pseudouridine synthase RluA.J Biol Chem. 1999 Jul 2;274(27):18880-6.","","Thu Dec 12 13:36:46 2002","1","","","" "AA00514","355898","355749","150","TTGAAAAAGAAAAATATTTGGCAATACAATAAAGACAACCAAAGCAATGAACCCGTTTCACTGCTTTTTATCGCCTCGGAAAAGAAAAGTGCGGTCGGAATTTTAGGTGTTTCACATCGAAAAAACACAGGAAAAATCCACCGCACTTTT","","","5707","LKKKNIWQYNKDNQSNEPVSLLFIASEKKSAVGILGVSHRKNTGKIHRTF","355749","","hypothetical protein","Cytoplasm, Extracellular","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:20:53 2004","Sun Feb 22 16:20:53 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00514 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:20:53 2004","","","","","","","","","","","","","1","","","" "AA00515","355870","356019","150","TTGTATTGCCAAATATTTTTCTTTTTCAATTATTGTCCTTATCATTCCGATCTTTTGAGATTTGCCTTCCATGATGGCGGGCCGGAAGGGGACAGGCTGATGAAGTTGGCGATTAGAACCGGCAATCCGAATCCTTCTGCCACTAAAAAA","","","10282","LYCQIFFFFNYCPYHSDLLRFAFHDGGPEGDRLMKLAIRTGNPNPSATKK","356021","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Dec 12 13:39:10 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00515 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00516","356574","356071","504","ATGCCATTACTTGATAGTTTTAAAGTGGATCACACCCGAATGAAGGCGCCTGCCGTACGTATTGCGAAGATCATGCGCACTCCAAAAGGAGACAATATCACCGTTTTTGATCTTCGTTTCACGATACCTAACAAAGAAAACTTGCCACCGAAAGGTATTCACACCCTTGAACATTTATTTGCCGGTTTTATGCGAGATCACTTAAATGGCAAGGATGTGGAAATTATCGATATTTCCCCGATGGGCTGTCGCACCGGTTTTTATATGTCCTTAATCGGCACTCCAAATGAAACCCAAATCGCACAGGCGTGGGCAGCTTCGATGCAGGATATTCTGAATGTAAAGAAACAAAGCGAAATTCCTGAACTAAATGAGTACCAATGCGGCACTTACACCGAGCATTCTTTGGAAGAAGCACATCAAATCGCACAAAATGTGTTGGATCGCGGTATCGGCGTAAATAAAAATGAAGATTTAACCTTAGACGAAAGCTTATTAAAACAA","","","18959","MPLLDSFKVDHTRMKAPAVRIAKIMRTPKGDNITVFDLRFTIPNKENLPPKGIHTLEHLFAGFMRDHLNGKDVEIIDISPMGCRTGFYMSLIGTPNETQIAQAWAASMQDILNVKKQSEIPELNEYQCGTYTEHSLEEAHQIAQNVLDRGIGVNKNEDLTLDESLLKQ","356073","","autoinducer-2 production protein","Cytoplasm","","
InterPro
IPR003815
Family
LuxS protein
PD013172\"[8-162]TLUXS_HAEIN_P44007;
PR01487\"[5-23]T\"[28-46]T\"[49-67]T\"[77-95]T\"[121-140]TLUXSPROTEIN
PIRSF006160\"[1-162]TAutoinducer-2 production protein LuxS
PF02664\"[2-162]TLuxS
noIPR
unintegrated
unintegrated
G3DSA:3.30.1360.80\"[1-168]Tno description


","BeTs to 9 clades of COG1854COG name: LuxS protein involved in autoinducer AI2 synthesisFunctional Class: TThe phylogenetic pattern of COG1854 is ---------d-lb-e-gh-nu---t-Number of proteins in this genome belonging to this COG is","Significant hit ( 2.4e-81) to 5/5 blocks of the PR01487 family, which is described as \"Bacterial autoinducer-2 (AI-2) production protein LuxS signature\". Prints database entry for PR:PR01487. PR01487A 5-23 1.4e-14 PR01487B 28-46 2.4e-12 PR01487C 49-67 7.7e-17 PR01487D 77-95 3.1e-17 PR01487E 121-140 7.9e-15","Residues 3 to 162 match (8e-76) PD:PD013172 which is described as COMPLETE PROTEOME SYNTHESIS PRODUCTION AUTOINDUCER-2 LUXS AUTOINDUCER AI-2 SENSING QUORUM ","","","","","","","","","","","","Thu Dec 12 13:47:21 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00516 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 162 (E-value = 1e-106) place AA00516 in the LuxS family which is described as LuxS protein (PF02664)","","",""," James D, Shao H, Lamont RJ, Demuth DR.,The Actinobacillus actinomycetemcomitans ribose binding protein RbsB interacts with cognate and heterologous autoinducer 2 signals.Infect Immun. 2006 Jul;74(7):4021-9.PMID: 16790775Fong KP, Chung WO, Lamont RJ, Demuth DR.Intra- and interspecies regulation of gene expression by Actinobacillus actinomycetemcomitans LuxS.Infect Immun. 2001 Dec;69(12):7625-34.PMID: 11705942","Stevenson B, Babb K.LuxS-mediated quorum sensing in Borrelia burgdorferi, the lyme disease spirochete.Infect Immun. 2002 Aug;70(8):4099-105.PMID: 12117917 Ohtani K, Hayashi H, Shimizu T.The luxS gene is involved in cell-cell signalling for toxin production in Clostridium perfringens.Mol Microbiol. 2002 Apr;44(1):171-9.PMID: 1196707Winzer K, Hardie KR, Burgess N, Doherty N, Kirke D, Holden MT, Linforth R, Cornell KA, Taylor AJ, Hill PJ, Williams P.LuxS: its role in central metabolism and the in vitro synthesis of4-hydroxy-5-methyl-3(2H)-furanone.Microbiology. 2002 Apr;148(Pt 4):909-22.PMID: 11932438 Winzer K, Sun YH, Green A, Delory M, Blackley D, Hardie KR, Baldwin TJ, Tang CM.Role of Neisseria meningitidis luxS in cell-to-cell signaling and bacteremic infection.Infect Immun. 2002 Apr;70(4):2245-8.PMID: 11895997 ","Tue Jan 21 16:00:50 2003","Thu Dec 12 13:47:21 2002","1","","","" "AA00518","357273","356791","483","ATGTTAGACCTCTTCAGCTGGGATTGGTGGCAATCCTTATTCGGCGAACATCGGCTTTGGATTATGTTCGCCAGCGCCTTTCTCAGTTCCACCGTGCTGCCCGGCAATTCGGAAATTATTTTTCTTACCATCGCCGCACCGCTTTTATGGTCGGGTTACCATCATTTTTCCATCGAAGTTCAAAGTTTGTTATGGGTTGCGGTTATCGGTAATACACTTGGAAGTCTGACCACTTATGTTTTAGGGCGTTGGTTGCCTGCTTTCAATAAACCGCCGCAGAATGCCGAACTGGCTTGGACATTGGAAAAAACACAACGTTACGGCAGTTTGGTGTTATTTTTCAGCTGGTTGCCAATCATCGGGGATGTATTTTGTGCGGTGGCGGGTTGGTTGCGGTTGAACTGGTTGGCGTGCCTGGTTTTTATCGCGCTGGGCAAAATAGTGCGGTATGTTTTTTTGTTGTTTTTAGGTGTGGCTTTTCTG","","","18373","MLDLFSWDWWQSLFGEHRLWIMFASAFLSSTVLPGNSEIIFLTIAAPLLWSGYHHFSIEVQSLLWVAVIGNTLGSLTTYVLGRWLPAFNKPPQNAELAWTLEKTQRYGSLVLFFSWLPIIGDVFCAVAGWLRLNWLACLVFIALGKIVRYVFLLFLGVAFL","356793","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
PD085709\"[20-160]TQ73IL2_WOLPM_Q73IL2;
signalp\"[1-37]?signal-peptide
tmhmm\"[19-53]?\"[63-83]?\"[108-128]?\"[133-153]?transmembrane_regions


","BeTs to 7 clades of COG1238COG name: Uncharacterized membrane proteinFunctional Class: SThe phylogenetic pattern of COG1238 is --m----q------efghsnujx---Number of proteins in this genome belonging to this COG is","","Residues 105 to 153 match (2e-08) PD:PD541482 which is described as COMPLETE PROTEOME TRANSMEMBRANE MEMBRANE YQAA PROBABLE PM1055 NMB0534 ORF HI0489 ","","","","","","","","","","","","Thu Dec 12 13:49:47 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00518 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00519","357881","357279","603","ATGCTGAGCGAAAAAGAGAAAATGCTGCGTGGTCTCGCCCATCAGCCTTACACCGATGAGCTGGTAGCAATGCGTCTGCGTGCCAAAGAGTTACTGTACCAATTCAATATTCTGACCCGTCCGAGCAATAAAGCGGAAAAAGTGCGGTTGATTTTAGCCTTGTTTGGCAAAGCCGACGCGACAACGCATGTCAATGCGCCCTTTTATTGTGACTACGGCAGCAATATTAAGGTGGGAAAAAACTTTTTCGCCAATTATCACTGCACCATTTTAGATAACGCACCGGTGACCATCGGCAACGATGTGATGTTTGCGCCCAATGTGAGTTTATATACGGTGGGACACCCGCTCGATCCCGAATTGCGCCTTGCCGGCTGGGAGCAGGCGCTTCCGATTACCATCGGCAATAATGTGTGGCTTGGCGGCAATGTTGTGGTTCTGGGCGGTGTGACAATTGGTGATAATGTGGTAATTGCTGGGGGTTCCGTAGTCACTAAAGATATTCCCGCAAACACCGTCGCCGTGGGGTCTCCTTGTCGGGTAGTGCGACAAGTGAATGTGGCAGATCGTGAAAATTATCTGCGTACCTACCGGCCGCAAATC","","","22066","MLSEKEKMLRGLAHQPYTDELVAMRLRAKELLYQFNILTRPSNKAEKVRLILALFGKADATTHVNAPFYCDYGSNIKVGKNFFANYHCTILDNAPVTIGNDVMFAPNVSLYTVGHPLDPELRLAGWEQALPITIGNNVWLGGNVVVLGGVTIGDNVVIAGGSVVTKDIPANTVAVGSPCRVVRQVNVADRENYLRTYRPQI","357281","","O-acetyltransferase","Cytoplasm","","
InterPro
IPR001451
Repeat
Bacterial transferase hexapeptide repeat
PF00132\"[95-112]T\"[131-148]T\"[149-166]THexapep
PS00101\"[140-168]THEXAPEP_TRANSFERASES
noIPR
unintegrated
unintegrated
G3DSA:2.160.10.10\"[47-183]Tno description
PTHR23416\"[132-186]TSIALIC ACID SYNTHASE-RELATED
PTHR23416:SF7\"[132-186]TNEUD PROTEIN


","BeTs to 11 clades of COG0110COG name: Acetyltransferases (the isoleucine patch superfamily)Functional Class: RThe phylogenetic pattern of COG0110 is -om-k-y-vdrlbcefgh-nuj-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 5.1e-23) to 1/1 blocks of the IPB001451 family, which is described as \"Bacterial transferase hexapeptide repeat\". Interpro entry for IP:IPR001451. IPB001451 134-169 4.9e-23 IPB001451 140-175 0.08 IPB001451 128-163 0.1 IPB001451 152-187 0.56","Residues 64 to 112 match (3e-07) PD:PD581880 which is described as PROTEOME COMPLETE THGA LMO0431 ACETYLTRANSFERASE LIN0451 TRANSFERASE ","","","","","Tue Feb 18 10:14:24 2003","","","","","","","Thu Dec 12 14:24:40 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00519 is paralogously related to AA00610 (3e-04) and AA00612 (0.001).","","","","","","","","","","","","","","1","","","" "AA00521","358384","357884","501","ATGGTGGGTCAACATTTTGGCTATCCGTTTGACGGCAATTTATTATATGAACTAGGCGGTGCGCCGGTAAAAACCATCGCGCAGGAAATGATGAAACGCCATGCCATGCCGTTAGAAAGATTGGATGATGTCATCCATTTGAAACGCAAATACGGCAAACAGCTGATTATGCAACACGCCACGCTATTGCCCGCCGCCAGTGTCGTGCGTTCTTTTTACAGCAAAAAACCGTTGGCGTTAGGCACGGGTTCCCATCGTGCCATGACAGAAATTCTATTGGATAAATTTGATTTTGAAAAATACTTTTCCGCCATTGTCACCGCCGAAGATATTCAACATCATAAACCTGCGCCGGACACGTTTTTACGTTGTGCCGAACTGATTAAGGTGAAACCACAACGCTGTTTAGTCTTTGAAGACGGTGATTTGGGCATTCAGGCGGGATTAAGTGCCGGGATGGATGTATTTGATGTGCGCGTAAATAAATTATTGAGAGAAAAC","","","22551","MVGQHFGYPFDGNLLYELGGAPVKTIAQEMMKRHAMPLERLDDVIHLKRKYGKQLIMQHATLLPAASVVRSFYSKKPLALGTGSHRAMTEILLDKFDFEKYFSAIVTAEDIQHHKPAPDTFLRCAELIKVKPQRCLVFEDGDLGIQAGLSAGMDVFDVRVNKLLREN","357886","","phosphatase","Cytoplasm","","
InterPro
IPR005834
Domain
Haloacid dehalogenase-like hydrolase
PF00702\"[65-161]THydrolase
InterPro
IPR006402
Domain
HAD-superfamily hydrolase, subfamily IA, variant 3
TIGR01509\"[5-158]THAD-SF-IA-v3: HAD-superfamily hydrolase, su
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1000\"[76-159]Tno description
PTHR18901\"[4-158]T2-DEOXYGLUCOSE-6-PHOSPHATE PHOSPHATASE 2


","No hits to the COGs database.","","Residues 115 to 156 match (8e-07) PD:PD470828 which is described as PROTEOME COMPLETE HYDROLASE PHOSPHATASE PHOSPHOGLYCOLATE PGP METABOLISM CARBOHYDRATE CHROMOSOME FAMILY ","","","","","","","","","","","","Thu Feb 20 08:56:41 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00521 is paralogously related to AA02446 (1e-06).","","","","","","","","","","","","","","1","","","" "AA00523","358612","358989","378","ATGGATATTCAACAACGGCTGTGGATTTTTCAAACGCGGGAGCTCATTGACGATCATATCGTCGAGACCGTACTCAATGTGCGCCGGCATTTGCAACGCCAATGGCAGGTGGACGTGGAAACGGAACAGGTGAAAATGATGTTGGTGCATATTGCCAGCGCGTTGGGGCGCATTAAACGCGGACATTGCGTTTCGCCGTTGTATGCGGAATTGCTGTTGGAAATGAAAAGTGCGGTGGTTTTTCCGCAAGTTTTGCAGATTCACCAAAATGTGTTGGAACTGATTCCGTTAGATATTCCGGAAGAGGAACAGACATATTTCCTGGCGAACGTATATGGTTTGGTATTGGATCAGCCGCATGTGCTGGCGCGGGTAAGT","","","14729","MDIQQRLWIFQTRELIDDHIVETVLNVRRHLQRQWQVDVETEQVKMMLVHIASALGRIKRGHCVSPLYAELLLEMKSAVVFPQVLQIHQNVLELIPLDIPEEEQTYFLANVYGLVLDQPHVLARVS","358991","","conserved hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
PD076829\"[16-114]TYHFY_HAEIN_P44003;


","No hits to the COGs database.","","Residues 3 to 114 match (1e-08) PD:PD076829 which is described as PROTEOME COMPLETE YHFY ","","","","","","","","","","","","Thu Dec 12 14:29:59 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00523 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00525","359394","359519","126","GTGGGCGGTATGATACGGGTTTATGACAATAAGTCAAATTATTTTTTCCGAAAAGTGCCTGAAATCAACTTGGTTGAGCGATTTCTCAACAAATCCGAACGGGGTTTTTGTCCTTTATTTTCCGCG","","","4925","VGGMIRVYDNKSNYFFRKVPEINLVERFLNKSERGFCPLFSA","359519","","hypothetical protein","Cytoplasm, Extracellular","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:24:11 2004","Sun Feb 22 16:24:11 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paraloogus sequences are found to this sequence.AA00525 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:24:11 2004","","","","","","","","","","","","","1","","","" "AA00527","361523","359511","2013","ATGAAACTCAATCCGCAACAACAACAAGCCGTGGAATACGTCTCCGGCCCTTGCCTGGTGCTAGCCGGCGCCGGTTCCGGCAAAACCCGCGTAATCATCAACAAAATCGCCCATTTAATCGATAAGTGCGGTTATTTTCCGAAGCAAATCGCCGCCGTCACTTTCACCAACAAAGCCGCCCGCGAAATGAAAGAGCGCGTGGCGCAATCCATCGGCAAAGCACAATCCAAAGGGCTGATTGTGTCCACCTTCCACACCTTAGGTTTTGATATTATTAAGTGTGAATACAAACAGTTAGGCTTTAAAGCCAATATGACGCTGTTTGACGAACACGACCAAATGGCGCTGTTAAAAGAACTCACCGCCGATGTGTTGCAGGAAGACAAAGGCGTATTGCGCGAGCTGATTAACCGTATTTCCAACTGGAAGAACGATTTATGCAGTCCGCAACAGGCGCTGGGGTTGGCACGGGATAACAAAGAACAGACCTTCGCCCATTGTTACGATCGCTACAACAAACAACTGCGCGCTTACAACGCCTTGGATTTTGACGATTTGATCATGCTGCCGACGTTGTTGTTCAAACAGAACGCCGAAGTGCGGTTAAAATGGCAGGAGAAAATTCGCTATCTGTTGGTGGACGAATACCAAGACACCAACACCAGCCAATATGAACTGATTAAACTGTTGGTGGGCGAACGCGCCCGTTTTACGGTAGTGGGCGATGACGATCAATCCATTTATTCCTGGCGGGGCGCGCGTCCGCAGAATATGGTGCGGCTGCGCGATGATTTCCCGGCGTTACGGGTGATTAAACTGGAACAAAACTACCGTTCCAGCCAACTAATTTTACACTGCGCCAATATTCTCATTGATAACAATGAGCACGTTTTCGACAAAAAACTGTTTTCCAATTTAGGCGAAGGGGAAAAATTACAAATTATCGAAGCGAAAAATGAAGAGCACGAGGCGGAGCGCGTGGTAGGCGAGCTGATTGCGCATCGATTTATCGGCAAAACCCATTATCGCGATTATGCCATTTTGTATCGCGGCAACCATCAATCGCGCCTGTTGGAAAAAATCCTCATGCAAAACCGCATTCCGTACAAAATTTCCGGCGGCACGTCGTTTTTCTCCCGCACGGAAATTAAAGACATGATGGCGTATTTGCGTTTGGTGGTGAATCAGGACGACGACGCGGCATTTTTGCGTATTGTAAACACGCCGAAGCGGGAAATCGGCACCGCGACGCTGGAAAAACTGGGTTCCTTGGCGCAGGAAAAACATATCAGTTTGTTTGAAGCGATTTTTGATTTTGAGCTGCTTCAACGGGTCACGCCGAAAGCGTATGACGCATTGCAAAAATTCGCCCGCTGGACTGTGGAACTGAATGACGAAATTCAGCGCTCCGAACCGGAACGGGCGGTGCGTTCCATGCTTTCCTCGTTGCACTATGAAGAATATTTGTACGAATACGCCACCAGCCCGAAAGCGGCGGAAATGCAGAGTAAAAACGTGGCGATGCTGTTCGATTGGGTCGCCGGCATGTTGAAAGGCGACGAGTTTAACGAGCCCATGAACCTCAATCAAATTGTCACCCGCTTGACCTTACGGGATATGCTGGAGCGCGGCGAAGAGGAAAATGATGGCGACCAGGTGCAATTGATGACGCTACACGCCTCCAAAGGGCTGGAATTTCCCCATGTGTTTTTAATTGGCATGGAAGAAGGTATTTTGCCGCACCAAACCAGCATTGACAAAGACAATGTGGAAGAAGAGCGTCGTTTGACGTATGTGGGGATTACCCGTGCGCAACAGAATCTGTGGTTTTCCTTGTGTAAGGAACGACGTCAATTCGGCGAGTTAATCCGTCCCGAACCGAGTCGCTTTTTGTTGGAACTGCCGGAAAACGATTTGCAATGGGAGCGGGATAAACCGCCGTTAAGCGCCGAACAGCAACAGGCAAAAACACAAAGCCATATCGCCAATTTACGGGCAATTTTACGCGGAAAA","","","77651","MKLNPQQQQAVEYVSGPCLVLAGAGSGKTRVIINKIAHLIDKCGYFPKQIAAVTFTNKAAREMKERVAQSIGKAQSKGLIVSTFHTLGFDIIKCEYKQLGFKANMTLFDEHDQMALLKELTADVLQEDKGVLRELINRISNWKNDLCSPQQALGLARDNKEQTFAHCYDRYNKQLRAYNALDFDDLIMLPTLLFKQNAEVRLKWQEKIRYLLVDEYQDTNTSQYELIKLLVGERARFTVVGDDDQSIYSWRGARPQNMVRLRDDFPALRVIKLEQNYRSSQLILHCANILIDNNEHVFDKKLFSNLGEGEKLQIIEAKNEEHEAERVVGELIAHRFIGKTHYRDYAILYRGNHQSRLLEKILMQNRIPYKISGGTSFFSRTEIKDMMAYLRLVVNQDDDAAFLRIVNTPKREIGTATLEKLGSLAQEKHISLFEAIFDFELLQRVTPKAYDALQKFARWTVELNDEIQRSEPERAVRSMLSSLHYEEYLYEYATSPKAAEMQSKNVAMLFDWVAGMLKGDEFNEPMNLNQIVTRLTLRDMLERGEEENDGDQVQLMTLHASKGLEFPHVFLIGMEEGILPHQTSIDKDNVEEERRLTYVGITRAQQNLWFSLCKERRQFGELIRPEPSRFLLELPENDLQWERDKPPLSAEQQQAKTQSHIANLRAILRGK","359513","","ATP-dependent DNA helicase","Cytoplasm","","
InterPro
IPR000212
Family
UvrD/REP helicase
PTHR11070\"[14-466]T\"[485-643]TUVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER
PF00580\"[3-485]TUvrD-helicase
InterPro
IPR005752
Family
ATP-dependent DNA helicase RepA
TIGR01074\"[1-669]Trep: ATP-dependent DNA helicase Rep
InterPro
IPR014016
Domain
Helicase superfamily 1, UvrD-related
PS51198\"[1-280]TUVRD_HELICASE_ATP_BIND
InterPro
IPR014017
Domain
UvrD-like DNA helicase, C terminal
PS51217\"[281-563]TUVRD_HELICASE_CTER
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[2-273]T\"[274-643]Tno description


","BeTs to 22 clades of COG0210COG name: Superfamily I DNA and RNA helicasesFunctional Class: LThe phylogenetic pattern of COG0210 is -omp--yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.9e-74) to 7/7 blocks of the IPB000212 family, which is described as \"UvrD/REP helicase\". Interpro entry for IP:IPR000212. IPB000212A 22-32 6.6e-07 IPB000212B 50-67 2e-11 IPB000212C 213-224 2.1e-06 IPB000212D 240-253 1.5e-10 IPB000212E 273-291 6.5e-09 IPB000212F 553-571 2.9e-14 IPB000212G 592-604 6.9e-07","Residues 210 to 291 match (2e-15) PD:PD492605 which is described as HELICASE DNA COMPLETE PROTEOME ATP-DEPENDENT II HYDROLASE 3.6.1.- EXONUCLEASE REPAIR ","","","","","","","","","","","","Thu Dec 12 14:31:43 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00527 is paralogously related to AA02666 (1e-106), AA00021 (2e-14) and AA02266 (3e-10).","","","","","","Residues 3 to 485 (E-value = 2.7e-211) place AA00527 in the UvrD-helicase family which is described as UvrD/REP helicase (PF00580)","","","","","orolev,S., Hsieh,J., Gauss,G.H., Lohman,T.M. and Waksman,G. Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNAand ADP Cell 90 (4), 635-647 (1997) PubMed: 9288744 Gilchrist,C.A. and Denhardt,D.T. Escherichia coli rep gene: sequence of the gene, the encoded helicase, and its homology with uvrD Nucleic Acids Res. 15 (2), 465-475 (1987) PubMed: 3029683 Bialkowska-Hobrzanska,H., Gilchrist,C.A. and Denhardt,D.T. Escherichia coli rep gene: identification of the promoter and N terminus of the rep protein J. Bacteriol. 164 (3), 1004-1010 (1985) PubMed: 2999067 ","","Thu Dec 12 14:31:43 2002","1","","","" "AA00528","361763","361536","228","ATGAAATTTCAACCCGTAAAAACACTCTTTATTTCGACCGCACTTTTTGCTATCAGCGGTTGTGGCACGGTGGTCAAGCTGATCGATCCCACGGAACCTTACAGCGCCTACGCCGGCACCAAGTACGATTTTGACATGGCGAAACGCTGGGGCTTGCCGATTTTAGACCTGCCGCTGTCCTTTTTATTGGATACCGCCCTGTTGCCTTATGCCTGGTCGCAAAGCGAA","","","8447","MKFQPVKTLFISTALFAISGCGTVVKLIDPTEPYSAYAGTKYDFDMAKRWGLPILDLPLSFLLDTALLPYAWSQSE","361538","","conserved hypothetical protein","Cytoplasm, Outer membrane","","
InterPro
IPR010780
Family
Protein of unknown function DUF1375
PF07119\"[7-73]TDUF1375
noIPR
unintegrated
unintegrated
PS51257\"[1-21]TPROKAR_LIPOPROTEIN
signalp\"[1-23]?signal-peptide
tmhmm\"[9-29]?\"[52-72]?transmembrane_regions


","No hits to the COGs database.","","Residues 6 to 74 match (7e-12) PD:PD055756 which is described as PROTEOME COMPLETE HI0650 TRANSMEMBRANE PM1060 ","","","","","","","","","","","","Thu Dec 12 14:38:11 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00528 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 73 (E-value = 5e-29) place AA00528 in the DUF1375 family which is described as Protein of unknown function (DUF1375) (PF07119)","","","","","","","","1","","","" "AA00529","362430","361870","561","ATGAAAAAATTAACGCTTTTAGCGCTTAGCGCAGCTGTTCTTGTGTCAACCTCCGCGGTGGCATCCTCAGATTTTACCGGCTTTGGAATTGGTGTTGGTGTAGGCACAACCAAGTACAAAGACGCAAAACGTATCTCTAACGTTGATTTAATTGCCGATTATGGCATCGACTATGGTAACGATTTCGTAGGTATCATTGAAGGAAAATTGAAGTTAAACAAATCAACGTTACATGATAATAACGCCTCCGGCTACCGTGGCAAACTGAACGAAAAGGCACGTTTGGGCGTAAGTTACTTACAAGGCTATCGCGTAACACCAAGCATTCTTCCTTATGCCAAAGTTGGGGTGCAAACTGCTAAATTTGAAAGTGAGGTTCGTACACGCAACTACTCAGCTACGCATAGTGATACCAAAAACGGTATAGGTTTTGGTGCGGGTGTTAAGGTCAATCTGGTACCGGACTTTGAGCTAAGCTTGGAATATTTAAGGACTCATAACAAATTTGATGGTCAAAAGTTAAGAGGTAATGTATATAGCACCAACGCTACATATCGTTTC","","","20330","MKKLTLLALSAAVLVSTSAVASSDFTGFGIGVGVGTTKYKDAKRISNVDLIADYGIDYGNDFVGIIEGKLKLNKSTLHDNNASGYRGKLNEKARLGVSYLQGYRVTPSILPYAKVGVQTAKFESEVRTRNYSATHSDTKNGIGFGAGVKVNLVPDFELSLEYLRTHNKFDGQKLRGNVYSTNATYRF","361872","","outer membrane protein, Omp 18/16","Outer membrane, Extracellular","","
noIPR
unintegrated
unintegrated
G3DSA:2.40.160.20\"[22-187]Tno description
signalp\"[1-23]?signal-peptide


","No hits to the COGs database.","","","","","","","Tue Feb 18 10:41:32 2003","","","","","","","Tue Feb 18 10:41:32 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00529 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","Komatsuzawa,H., Asakawa,R., Kawai,T., Ochiai,K., Fujiwara,T.,Taubman,M.A., Ohara,M., Kurihara,H. and Sugai,M.Identification of six major outer membrane proteins fromActinobacillus actinomycetemcomitansJOURNAL Gene 288 (1-2), 195-201 (2002)PubMed: 12034509","","Thu Dec 12 14:41:07 2002","","1","","","" "AA00530","362513","362728","216","GTGGATTCTACAGATGAAAGTGCGGTGATTTTTGTCAGTAATTTTAATTGGTTATCAAGCCCGTATTATTCCATGCGCCGCCCCCCGATTTTCGCTATAATGTGTCAATTATTCATCAACATCATGAGATTATTATGGCCCAAATTGCTGCAAATCCCCTCGTTCTGGTGGACGGTTCTTCCTATTTATATCGCGCGTTTCATGCGTTCCCGCCAC","","","8695","VDSTDESAVIFVSNFNWLSSPYYSMRRPPIFAIMCQLFINIMRLLWPKLLQIPSFWWTVLPIYIARFMRSRH","362728","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-47]?signal-peptide
tmhmm\"[23-43]?\"[49-67]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:25:24 2004","Sun Feb 22 16:25:24 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00530 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:25:24 2004","","","","","","","","","","","","","1","","","" "AA00531","362761","365445","2685","ATGTACGGCGTGCTGAATATGCTGAAAAGCCTGATTTCGCAGGTGCAGCCGAGCCATATTGCAGTGGTGTTCGATGCCAAAGGCAAAACTTTCCGTGATGAAATGTTCGAACAATACAAATCCCACCGCCCGCCCATGCCTGATGATTTGCGCAAACAGATTCAACCCTTGCACGACATGATCCGCGCGCTGGGCATTCCGTTGTTGGTAGTAGACGGTGTGGAAGCGGACGACGTGATCGGCACGCTGGCAAGTCAAGCGTCGAAAAACGGGCAAAAAGTGCTCATCAGCACCGGCGACAAAGATATGGCGCAGCTGGTGGACAACAACATTATGTTGATTAACACCATGAACAACAGCCTGCTGGATCGCGCGGGCGTGATTGAAAAATACGGCATTCCGCCGGAATTGATTATTGATTATCTGGCGCTGATGGGCGACAGCTCCGATAACATTCCGGGCGTGGCGGGCGTGGGCGAAAAAACTGCCCTTGGGCTTTTGCAGGGCATCGGCAGCATGGCGCAAATTTATGCCAATCTGGACAAAGTCGCCGAACTGCCGATTCGTGGCGCGAAAAAGCTGGGCAAAAAATTACTCGCCGAAAAAGCCATGGCGGATTTATCTTACGCGCTGGCAACCATTAAAACTGATGTGATGCTAGAATTTTCGCCTCATGAACTCTCCATCGGCGACAGCGATAACGACGCCTTAATCGCGTATTTCGGGCGTTATGAATTTAAACGCTGGCTAGGGGAGGTGATGAATGGCGCCGGTACTGTCACGCAAAGCGCCGAGCAACCCGTAAAAATTAACCACTACCAAGCCACGCCTGCAGCAAAAATCGATGAAAGTGCGGTCGAAAATGCCGTTAAATTTCACATTGATCGCAGCCGTTATGAAAACATTCTCACCGAGGCGGATTTGGCGCGTTGGCTGGAAAAACTGAACGCCGCCAAACTCATCGCCGTGGATACGGAAACCGACGGGCTGGATTATATGTCCGCCAATTTGGTGGGCGTTTCCTTTGCCTTGGAAAATGGCGAAGCGGCGTATTTACCGCTCCATTTGGATTACCTCGGCGCACCGAAAACGCTGGAAAAAAACACCGCACTTTCTGCCCTTAAACCGATTCTGGAAAACCCGAACATCGGCAAAATCGGGCAAAATCTCAAGTTCGACATGACCATTTTCGCCCGCAACGGCATTGATTTGCAGGGCATCGAATTTGACACCATGTTGCTTTCCTACACCCTGGACAGCACCGGGCGACACAATATGGACGACTTGGCGAAGCGCTATCTCGGACATCAAACCATTAGCTTTGAAGACATCGCCGGCAAAGGCAAAAACCAGCTGACCTTCAATCAAATTCCGTTGGAACAGGCGGGCGAATACGCGGCGGAAGATGCCGACGTGACCATGAAGTTGCAACAAGTGTTATGGCAAAAATTACAGCCGCAACCCGGTTTGGTAGAACTCTATCAATCCATCGAACTGCCGCTGCTCGGTGTGTTATCGCGTATGGAACGTTACGGCGTGCTGATTGATTCCGACGCGCTGTTTTTGCAATCCAATGAAATTACCGAAAGATTGACCGCACTTGAAATGCAGGCGCACACTTTGGCGGGACAGCCGTTCAATTTGGCATCCACCAAGCAGTTGCAGGAAATCTTGTTCGACAAACTCGGCTTGCCGGTGCTGCAAAAAACCCCGAAAGGCGTGCCGTCCACTAATGAGGAAGTGCTGGAAGAACTGGCGTACAGCCACGAATTGCCGAAAGTGCTGGTGGAACATCGTGGCTTGAGCAAACTGAAATCCACGTACACCGACAAGTTGCCGCAAATGGTGAATCCGCAAACGGGGCGCGTGCACACCTCCTATCATCAGGCAGTGACGGCGACAGGGCGGCTTTCTTCCAGCGATCCGAATTTACAGAACATTCCGATTCGCAACGAAGCAGGGCGCCGCATTCGCCAAGCCTTTATTGCACGTGATGGCTACAAAATCATCGCCGCCGACTATTCCCAAATTGAGCTGCGCATTATGGCGCATTTGTCCAATGACCAAGGCTTGATCAACGCTTTCGCGCAAGGCAAAGACATTCACCGTTCCACCGCCGCTGAAATTTTCGGTTTGCCACTGGAACAGGTCACGAGCGAACAACGCCGCAACGCGAAAGCCATTAACTTCGGCTTGATTTACGGAATGTCTTCCTTCGGTCTTTCCCGCCAGCTCGGTATTTCCCGCGCCGACGCACAACGCTACATGGATTTATATTTCCAGCGCTACCCGAACGTGCAAACCTTCATACATGACATTCGCGAAAAAGCCAAAGCACAGGGCTATGTGGAAACCCTGTTCGGACGCCGTCTATATTTGCCGGAGATCAATTCTTCCAACGCCATGCGTCGCAAAGGCGCGGAACGGGTGGCGATTAACGCGCCGATGCAAGGCACCGCCGCCGACATCATCAAACGCGCCATGATTAAACTGGATGGCATCACTCGTGATGACCCGGACATTCACATGATTATGCAAGTGCACGATGAACTGGTGTTTGAAGTGCGGTCGGAAAAAATCGCGTTTTTTAGCGATCTCATCAAACAACACATGGAAGCCGCCGCCGAACTGGTGGTGCCACTGATTGTAGATGTGGGCGTAGGTGAAAATTGGGATGAAGCGCAT","","","106741","MYGVLNMLKSLISQVQPSHIAVVFDAKGKTFRDEMFEQYKSHRPPMPDDLRKQIQPLHDMIRALGIPLLVVDGVEADDVIGTLASQASKNGQKVLISTGDKDMAQLVDNNIMLINTMNNSLLDRAGVIEKYGIPPELIIDYLALMGDSSDNIPGVAGVGEKTALGLLQGIGSMAQIYANLDKVAELPIRGAKKLGKKLLAEKAMADLSYALATIKTDVMLEFSPHELSIGDSDNDALIAYFGRYEFKRWLGEVMNGAGTVTQSAEQPVKINHYQATPAAKIDESAVENAVKFHIDRSRYENILTEADLARWLEKLNAAKLIAVDTETDGLDYMSANLVGVSFALENGEAAYLPLHLDYLGAPKTLEKNTALSALKPILENPNIGKIGQNLKFDMTIFARNGIDLQGIEFDTMLLSYTLDSTGRHNMDDLAKRYLGHQTISFEDIAGKGKNQLTFNQIPLEQAGEYAAEDADVTMKLQQVLWQKLQPQPGLVELYQSIELPLLGVLSRMERYGVLIDSDALFLQSNEITERLTALEMQAHTLAGQPFNLASTKQLQEILFDKLGLPVLQKTPKGVPSTNEEVLEELAYSHELPKVLVEHRGLSKLKSTYTDKLPQMVNPQTGRVHTSYHQAVTATGRLSSSDPNLQNIPIRNEAGRRIRQAFIARDGYKIIAADYSQIELRIMAHLSNDQGLINAFAQGKDIHRSTAAEIFGLPLEQVTSEQRRNAKAINFGLIYGMSSFGLSRQLGISRADAQRYMDLYFQRYPNVQTFIHDIREKAKAQGYVETLFGRRLYLPEINSSNAMRRKGAERVAINAPMQGTAADIIKRAMIKLDGITRDDPDIHMIMQVHDELVFEVRSEKIAFFSDLIKQHMEAAAELVVPLIVDVGVGENWDEAH","365447","","DNA polymerase I","Cytoplasm","","
InterPro
IPR001098
Family
DNA-directed DNA polymerase
PF00476\"[515-894]TDNA_pol_A
SM00482\"[654-859]TPOLAc
PS00447\"[722-741]TDNA_POLYMERASE_A
InterPro
IPR002298
Family
DNA polymerase A
PR00868\"[623-645]T\"[646-661]T\"[668-691]T\"[698-711]T\"[722-747]T\"[759-770]T\"[781-792]T\"[813-829]T\"[842-855]TDNAPOLI
TIGR00593\"[2-895]Tpola: DNA polymerase I
InterPro
IPR002421
Domain
5'-3' exonuclease
PF01367\"[133-239]T5_3_exonuc
PF02739\"[1-131]T5_3_exonuc_N
SM00475\"[1-230]T53EXOc
InterPro
IPR002562
Domain
3'-5' exonuclease
PF01612\"[299-485]T3_5_exonuc
SM00474\"[299-485]T35EXOc
InterPro
IPR008918
Domain
Helix-hairpin-helix motif, class 2
SM00279\"[135-170]THhH2
noIPR
unintegrated
unintegrated
G3DSA:1.10.150.20\"[677-820]Tno description
G3DSA:1.20.1060.10\"[511-626]Tno description
G3DSA:3.30.420.10\"[293-510]Tno description
G3DSA:3.40.50.1010\"[1-169]Tno description
PTHR10133\"[1-250]T\"[301-428]T\"[452-895]TDNA POLYMERASE I


","No hits to the COGs database.","Significant hit (4.4e-101) to 9/10 blocks of the IPB001098 family, which is described as \"Replicative DNA polymerase\". Interpro entry for IP:IPR001098. IPB001098B 500-513 0.0036 IPB001098C 542-561 1.1e-10 IPB001098D 622-648 9.8e-24 IPB001098E 673-684 2e-09 IPB001098F 697-707 0.0072 IPB001098G 722-735 7.9e-09 IPB001098H 811-829 1.6e-14 IPB001098I 840-859 2.9e-09 IPB001098J 879-891 1.1e-06","Residues 399 to 544 match (4e-07) PD:PD136802 which is described as DNA POLYMERASE I PROTEOME COMPLETE POLA DNA-BINDING POL I DNA-DIRECTED ","","","","","","","","","","","","Thu Dec 12 14:43:33 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00531 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 515 to 894 (E-value = 1.4e-222) place AA00531 in the DNA_pol_A family which is described as DNA polymerase family A (PF00476)","","","","","Secondary Laboratory Evidence:Joyce,C.M., Kelley,W.S. and Grindley,N.D. Nucleotide sequence of the Escherichia coli polA gene andprimary structure of DNA polymerase I J. Biol. Chem. 257 (4), 1958-1964 (1982) PubMed: 6276402 Joyce,C.M. and Grindley,N.D. Identification of two genes immediately downstream from the polAgene of Escherichia coli J. Bacteriol. 152 (3), 1211-1219 (1982) PubMed: 6183253 Brown,W.E., Stump,K.H. and Kelley,W.S. Escherichia coli DNA polymerase I. Sequence characterization andsecondary structure prediction J. Biol. Chem. 257 (4), 1965-1972 (1982) PubMed: 7035456 Ollis,D.L., Brick,P., Hamlin,R., Xuong,N.G. and Steitz,T.A. Structure of large fragment of Escherichia coli DNA polymerase Icomplexed with dTMP Nature 313 (6005), 762-766 (1985) PubMed: 3883192 ","","Thu Dec 12 14:43:33 2002","1","","","" "AA00533","365463","365582","120","ATGACACATAAAATCGTTCGTAGCGCAGACTTCACCGCCGCCCACGCCCGGGGCGGTTTGGACATTACTGAAATAAACGGCATCAGCGTGCGTTTACATTGGACCGACGAACCTTACAAA","","","4490","MTHKIVRSADFTAAHARGGLDITEINGISVRLHWTDEPYK","365582","","conserved hypothetical protein","Cytoplasm","This sequence is weakly similar to gi|22988710, a hypothetical protein from Burkholderia fungorum. See also gi|23057745 from Pseudomonas fluorescens.","No hits reported.","No hits to the COGs database.","","Residues 6 to 40 match (5e-07) PD:PD596379 which is described as PROTEOME COMPLETE NMA0001 ","","","","","","","","","","","","Sun Feb 22 16:28:31 2004","Sun Feb 22 16:28:31 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00533 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:28:31 2004","","","","","","","","","","","","","1","","","" "AA00534","365654","365559","96","GTGTTCTTTGTAGTGCATTTCTACTACGCCGTCCATTACGGCAAATATTTCTTCGCCGTCATTGGTGTGTCATTTGTAAGGTTCGTCGGTCCAATG","","","3777","VFFVVHFYYAVHYGKYFFAVIGVSFVRFVGPM","365559","","hypothetical protein","Cytoplasm, Extracellular","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-31]?signal-peptide
tmhmm\"[10-30]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:30:06 2004","Sun Feb 22 16:30:06 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00534 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:30:06 2004","","","","","","","","","","","","","1","","","" "AA00535","365835","366179","345","ATGTCCTACTCTTATCAATTTCGTTTAAAAATTATCAAACCGATCACCGAACATGATTTTAGTATTTATAAGGTGTCTAAACTTTATAAGATTCCTCATTCTCAAGTCATTTATTGGTTAAAAGCCTTTCGTGAAAGAGGGCTTGATGGCATAAAATCGCCTTATACTAAACCTAAAACCTCCAAAATTCTGAAACCCAAAATGAAAAAAACGCAGATTGAAGTGGCTGAAACAACCGACTTTTCACCACAAGCCTTTAAAAAACTGAAACGAGAACCCGCCCTTGAAAAAGCGGAGATTGATTATCTAAAAAAGTTAGTGGAATTGGGGCGATCAAAAACAAAT","","","13864","MSYSYQFRLKIIKPITEHDFSIYKVSKLYKIPHSQVIYWLKAFRERGLDGIKSPYTKPKTSKILKPKMKKTQIEVAETTDFSPQAFKKLKREPALEKAEIDYLKKLVELGRSKTN","366181","","hypothetical protein","Periplasm, Cytoplasm","","No hits reported.","BeTs to 3 clades of COG2963COG name: TransposaseFunctional Class: LThe phylogenetic pattern of COG2963 is ---p-----drlb-efgh---j----Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Thu Dec 12 14:52:22 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00535 is paralogously related to AA01267 (3e-28), AA02340 (8e-23), AA02115 (8e-23), AA01289 (8e-23), AA01075 (8e-23), AA00008 (8e-23), AA00631 (6e-16), AA01404 (2e-12), AA00227 (2e-11), AA01445 (9e-11) and AA01549 (3e-06).","","","","","","","","","","","","","Thu Jan 23 12:05:41 2003","1","","","" "AA00536","368102","366291","1812","ATGTTTACACTTAAAAAAACACTTACTCACATTCTTAGTACTACGTTTGTATTTTGTTCAACCTCCGGGTTAGCGGCAAATCCGCCGGAGGATAACCACAAAGCTGTTGAATTGAGCATTCTGCATATTAATGATCATCATTCTTATTTGGAGCCTCACGAAGCCCGCATTTTATTAAACGGTAAAGAAACTAAAGTAAATATTGGCGGTTTTTCCGCAGTTAACAGCAAGCTTAATGAATTACGCAAAAAATATAAAAATCCGCTAGTATTACATGCAGGCGATGCTATTACAGGAACACTTTATTTTACCCTTTTTGGCGGTTCGGCCGATGCAGCGGTAATGAATGCAGGTAATTTTCATTATTTTACACTGGGCAATCATGAGTTTGATGCGGGAAATGAAGGTTTATTAAAATTACTTGAACCACTAAAAATCCCTGTTTTATCTGCTAATGTCATTCCTGATAAAGGTTCTATTTTGTACAATAAATGGAAACCTTATGATATTTTCTCGGTGAATGGAGAAAATATCGGCATTATTGGGTTAGATACAGTAAATAAAACCGTTAATTCATCTTCCCCCGGGAAAGATGTTAAATTTTATGATGAAATTGCAACAGCCCAAATTATGGCGAATGCTTTAAAAGCACAGGGTGTTAACAAAATTATCTTACTTTCCCATGCGGGCAGTGAAAAGAACATAGAAATTGCGCAAAAAGTAAATGATATTGATATTATTGTTACCGGCGATTCACACTATTTATATGGTAATGACGAGTTGCGTGAATTGAAATTGCCGGTGGTATATGAATATCCCTTAGAATTTAAAAGCCCGAATGGTGAACCTGTTTTTGTGATGGAAGCTTGGGCTTATTCCGCCGTAGTGGGCGATTTAGGCGTTAAATTCAGCAAAGATGGGATCGCTTCCATAATCCGAAAAACTCCACATGTATTAATGAGCACAAATAAATTAAAAGTTAAAAACAGTGACGGTAATTGGCAGGAACTTAGTGGAGAAGAACGTCAAAAAGCAATTCAAAGTTTACAAAAGATGAAAAGCATTTCATTGGATTATCATGATAAAAAAACGGATAAACTGATTAGCAAATATCGATATGAAAAGGATCAACTGGCAAAAGAAGTCATCGGTTCAATCGTTGGGCAAGCGATGCCGGGCGGGTCGGATAATCGCATCCCGAATAAAGCAGGTTCTAACCCTGAAGGTTCGGTTGCGACCCGTTTTGTGGCAGAAACGATGTACAACGAATTGAAAAATGTAGATCTGGTTATTCAAAATGCCGGAGGTGTACGTTCAGATATTTTACCCGGTGACGTCACCTTTAATGATGCCTATACCTTTTTACCATTTGGTAATACTTTATTTACTTATAAAATGGAAGGTTCACTGATTAAACAAGCTTTGGAAGATGCTCTGCAATTTGCGTTAGTTGACGGTTCTACCGGCGGCTTCCCTTACGGGGCGGGTGTTCGTTATGAAGCCAATGAAACGCCAAATGCCGACGGTAAACGCTTAGTAAGCGTTGAGGTCTTCAATAAACAAACACAACAATGGGAAGATATTGACGATAATAAACGTTATCTAGTGGGAACCAATTCCTATATTGCCAGCGGTAAAGACGGATATAAAACCTTTGGTCATCTTTTCAATGACCCGAAATACGAAGGTACAGATACCTATCTTCCGGATGCAGAAAGCTTCATTAAATTTATGAAGAAAAATCCGCGTTTTGAGGCCTTCAAAACATCAAATGTAAAATTAAATGTTGTTAGTGAAGCCTTACCTAAAAAA","","","66722","MFTLKKTLTHILSTTFVFCSTSGLAANPPEDNHKAVELSILHINDHHSYLEPHEARILLNGKETKVNIGGFSAVNSKLNELRKKYKNPLVLHAGDAITGTLYFTLFGGSADAAVMNAGNFHYFTLGNHEFDAGNEGLLKLLEPLKIPVLSANVIPDKGSILYNKWKPYDIFSVNGENIGIIGLDTVNKTVNSSSPGKDVKFYDEIATAQIMANALKAQGVNKIILLSHAGSEKNIEIAQKVNDIDIIVTGDSHYLYGNDELRELKLPVVYEYPLEFKSPNGEPVFVMEAWAYSAVVGDLGVKFSKDGIASIIRKTPHVLMSTNKLKVKNSDGNWQELSGEERQKAIQSLQKMKSISLDYHDKKTDKLISKYRYEKDQLAKEVIGSIVGQAMPGGSDNRIPNKAGSNPEGSVATRFVAETMYNELKNVDLVIQNAGGVRSDILPGDVTFNDAYTFLPFGNTLFTYKMEGSLIKQALEDALQFALVDGSTGGFPYGAGVRYEANETPNADGKRLVSVEVFNKQTQQWEDIDDNKRYLVGTNSYIASGKDGYKTFGHLFNDPKYEGTDTYLPDAESFIKFMKKNPRFEAFKTSNVKLNVVSEALPKK","366293","","5'-nucleotidase precursor","Periplasm, Cytoplasm, Extracellular","","
InterPro
IPR004843
Domain
Metallophosphoesterase
PF00149\"[38-255]TMetallophos
InterPro
IPR006146
Domain
5'-Nucleotidase, N-terminal
PS00785\"[38-50]T5_NUCLEOTIDASE_1
PS00786\"[120-131]T5_NUCLEOTIDASE_2
InterPro
IPR006179
Family
5'-Nucleotidase and apyrase
PR01607\"[36-54]T\"[218-235]T\"[237-260]T\"[284-304]T\"[445-468]T\"[527-546]TAPYRASEFAMLY
PTHR11575\"[14-317]T\"[356-552]T5'-NUCLEOTIDASE-RELATED
InterPro
IPR006420
Family
NAD pyrophosphatase/5-nucleotidase NadN
TIGR01530\"[38-582]TnadN: NAD nucleotidase
InterPro
IPR008334
Domain
5'-Nucleotidase, C-terminal
G3DSA:3.90.780.10\"[386-586]Tno description
PF02872\"[382-554]T5_nucleotid_C
noIPR
unintegrated
unintegrated
G3DSA:3.60.21.10\"[30-351]Tno description
PTHR11575:SF7\"[14-317]T\"[356-552]T5-NUCLEOTIDASE-RELATED
signalp\"[1-25]?signal-peptide


","BeTs to 14 clades of COG0737COG name: 5'-nucleotidase/2',3'-cyclic phosphodiesterase and related esterasesFunctional Class: FThe phylogenetic pattern of COG0737 is aom---yqvd-lbce-gh--uj--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1e-57) to 9/9 blocks of the IPB002224 family, which is described as \"5'-Nucleotidase\". Interpro entry for IP:IPR002224. IPB002224A 36-54 1.3e-07 IPB002224B 87-95 0.004 IPB002224C 118-137 3.5e-09 IPB002224D 144-153 0.12 IPB002224E 221-230 0.038 IPB002224F 305-320 2.5 IPB002224G 430-441 0.0026 IPB002224H 444-460 2.8e-07 IPB002224I 526-549 1.6e-09","Residues 367 to 413 match (1e-13) PD:PD142103 which is described as PRECURSOR SIGNAL 5'-NUCLEOTIDASE PROBABLE PROTEOME COMPLETE HYDROLASE LIPOPROTEIN NUCA MEMBRANE ","","","","","Wed Feb 19 16:31:00 2003","","","","Wed Feb 19 16:31:00 2003","","","Wed Feb 19 16:31:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00536 is paralogously related to AA01830 (2e-18).","","","","","","Residues 382 to 554 (E-value = 8.2e-50) place AA00536 in the 5_nucleotid_C family which is described as 5'-nucleotidase, C-terminal domain (PF02872)","","","","","Zagursky,R.J., Ooi,P., Jones,K.F., Fiske,M.J., Smith,R.P. andGreen,B.A.Identification of a Haemophilus influenzae 5'-nucleotidase protein: cloning of the nucA gene and immunogenicity and characterization of the NucA proteinInfect. Immun. 68 (5), 2525-2534 (2000)PubMed: 10768940Kirby TW, Mueller GA, DeRose EF, Lebetkin MS, Meiss G, Pingoud A, London RE.The nuclease A inhibitor represents a new variation of the rare PR-1 fold.J Mol Biol. 2002 Jul 19;320(4):771-82.PMID: 12095254","","Wed Feb 19 16:31:00 2003","1","","","" "AA00537","368839","368132","708","ATGCAAAATATCGAACACACCGGTCAAAACCGGTCGAACCAATCCATACAGGATGTAAAACAGCAATTAGCCGCTGCACTTGCCCGACAAGAACAAAAACAAATTATCGTTTTACAAAAAAAGTTAACGTCTTTGTCTTCCCTATCCCCACAACGTCTTGCGCAACAAATTCGGACTACCGAAAAAATTCTGACCCGTATTTTTAAAACAGAGAAAAATCTGACACCCAAATTTATTGATTACCTGTATTTTGAGCCAATTGAAACGGCTGATGACACCTTAATGCAGGAAATGAAAAAAAATCTTTTGATCTCTTTCTTGGCAAATGAACGCGCTCAAATCTATATTAAAGACATGCCAAACGCTAATCAATTTGTTCAGCTTTTAACAGAAAAAGGAGCAAAGACTACGCAAATATCCGTATTGGCAGAACCTGCTAAAACCATTTTCCAGCGAATCCGCGAACAAATGTACCAAGATTTTCCTAATAAAAAACAGTTTACTATCACTGAAAATCGAGTAAGTGTTATTGCCCCTTCCTCCGTTATTAAGCCACGCCTTGCCTTGGCAGCTGCAATTTTTGATCAGCAGTTTAAAGGGGTTGAAGTTGATGATTTTTCTTACTTGGATCAACCGCGTGAAAATTTGCAACACAATAATGATACAACCCGTTATAAAACCTTTCAGGCAATGTTGGAAGGCTTAGAA","","","30402","MQNIEHTGQNRSNQSIQDVKQQLAAALARQEQKQIIVLQKKLTSLSSLSPQRLAQQIRTTEKILTRIFKTEKNLTPKFIDYLYFEPIETADDTLMQEMKKNLLISFLANERAQIYIKDMPNANQFVQLLTEKGAKTTQISVLAEPAKTIFQRIREQMYQDFPNKKQFTITENRVSVIAPSSVIKPRLALAAAIFDQQFKGVEVDDFSYLDQPRENLQHNNDTTRYKTFQAMLEGLE","368134","","conserved hypothetical protein","Periplasm, Cytoplasm","","No hits reported.","No hits to the COGs database.","","Residues 50 to 235 match (9e-62) PD:PD122097 which is described as PROTEOME COMPLETE HI0205 SIGNAL PRECURSOR ","","","","","","","","","","","","Thu Dec 12 15:03:52 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00537 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00538","369171","369046","126","TTGCTAGATGTGAAAATTGTGTTCATTGTAATAGATTTGCCTGCCGAGGTAAAAGTGCGGTTAAAAATTAATGAGTTTGGAATGCCATATATTATGTTAAAACCTATCCCTATTATTTTAATAAAA","","","4829","LLDVKIVFIVIDLPAEVKVRLKINEFGMPYIMLKPIPIILIK","369046","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:31:36 2004","Sun Feb 22 16:31:36 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00538 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:31:36 2004","","","","","","","","","","","","","1","","","" "AA00539","369184","370107","924","ATGATTATCGTAACAGGCGGCGCGGGCTTTATCGGCAGCAACATCGTCAAAGCATTAAACGACATGGGATGCAAAGATATTTTAGTGGTGGATAACTTAAAAGACGGCACCAAATTCATCAACTTAGTGGATTTAGACATCGCCGACTATTGCGACAAAGAAGACTTCATCGCGTCCATCATCGCCGGCGACGATTTGGGCGACATCGACGCCGTGTTCCACGAAGGCGCGTGCTCCGCCACCACCGAATGGGACGGCAAATACATCATGCACAACAACTACGAATATTCCAAAGAGTTACTGCATTACTGTCTGGATCGCCAAATTCCGTTCCTCTACGCCTCCAGTGCCGCCACCTACGGTGACAAAACCGAATTCCGCGAAGAACGCGAGTTTGAAGGCCCGTTAAATGTGTACGGCTATTCCAAATTTTTATTCGACCAATATGTACGTGCCATTTTGCCGGAAGCGCAATCGCCGGTGTGTGGTTTCCGTTACTTCAACGTGTACGGCCCGCGCGAAGGACACAAAGGCTCCATGGCAAGCGTAGCGTTCCACTTAAACAACCAAATTCTGAAAGGCGAAAACCCGAAACTGTTCGCCGGCAGCGAACACTTCCGCCGTGATTTCGTCTATGTGGGCGATGTAGCAGCAATAAATATCTGGTGCTGGCAAAACAAGGTTTCCGGCATTTTCAACTGCGGCACCGGCAACGCCGAATCCTTCGCCGAAGTGGCAAAAGCCGTTATCAAATTCCACAACAAAGGCGAAGTGGAAACCATCCCGTTCCCGGAACATTTAAAATCCCGCTACCAAGAATACACCCAAGCGGACTTAACCAAACTCCGCGCCACCGGCTACGACAAACCGTTCAAAACCGTGGCGGAAGGCGTCGCGGAATATATGGCGTGGTTAAATCGTAAA","","","34664","MIIVTGGAGFIGSNIVKALNDMGCKDILVVDNLKDGTKFINLVDLDIADYCDKEDFIASIIAGDDLGDIDAVFHEGACSATTEWDGKYIMHNNYEYSKELLHYCLDRQIPFLYASSAATYGDKTEFREEREFEGPLNVYGYSKFLFDQYVRAILPEAQSPVCGFRYFNVYGPREGHKGSMASVAFHLNNQILKGENPKLFAGSEHFRRDFVYVGDVAAINIWCWQNKVSGIFNCGTGNAESFAEVAKAVIKFHNKGEVETIPFPEHLKSRYQEYTQADLTKLRATGYDKPFKTVAEGVAEYMAWLNRK","370109","","ADP-L-glycero-D-manno-heptose-6-epimerase","Cytoplasm","","
InterPro
IPR001509
Family
NAD-dependent epimerase/dehydratase
PF01370\"[2-235]TEpimerase
InterPro
IPR011912
Family
ADP-L-glycero-D-manno-heptose-6-epimerase
PTHR10366:SF29\"[4-308]TADP-L-GLYCERO-D-MANNOHEPTOSE-6-EPIMERASE
TIGR02197\"[2-308]Theptose_epim: ADP-L-glycero-D-manno-heptose
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[1-202]Tno description
PTHR10366\"[4-308]TNAD DEPENDENT EPIMERASE/DEHYDRATASE


","BeTs to 19 clades of COG0451COG name: Nucleoside-diphosphate-sugar epimerasesFunctional Class: M,GThe phylogenetic pattern of COG0451 is aompk-yqvdrlbcefghsnuj--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 4.2e-19) to 5/5 blocks of the IPB001509 family, which is described as \"NAD dependent epimerase/dehydratase family\". Interpro entry for IP:IPR001509. IPB001509A 2-23 4.3e-09 IPB001509B 68-102 0.011 IPB001509C 167-173 5.9 IPB001509D 208-215 0.29 IPB001509E 295-305 1.4e+02Significant hit ( 8.3e-06) to 1/4 blocks of the IPB002225 family, which is described as \"3-Beta hydroxysteroid dehydrogenase/isomerase family\". Interpro entry for IP:IPR002225. IPB002225A -1-29 8.2e-06","Residues 2 to 33 match (1e-08) PD:PD341747 which is described as 4-EPIMERASE COMPLETE PROTEOME UDP-GLUCOSE ISOMERASE GALACTOSE EPIMERASE NAD SUGAR NUCLEOTIDE ","","","","","","","","","","","","Thu Dec 12 15:05:38 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00539 is paralogously related to AA01886 (4e-11) and AA02647 (5e-05).","","","","","","Residues 2 to 308 (E-value = 7e-14) place AA00539 in the Epimerase family which is described as NAD dependent epimerase/dehydratase family (PF01370)","","","","","1: Kneidinger B, Marolda C, Graninger M, Zamyatina A, McArthur F, Kosma P, Valvano MA, Messner P.Biosynthesis pathway of ADP-L-glycero-beta-D-manno-heptose in Escherichia coli.J Bacteriol. 2002 Jan;184(2):363-9.PMID: 11751812Ding,L., Seto,B.L., Ahmed,S.A. and Coleman,W.G. Jr. Purification and properties of the Escherichia coli K-12NAD-dependent nucleotide diphosphosugar epimerase,ADP-L-glycero-D-mannoheptose 6-epimerase. J. Biol. Chem. 269(39): 24384-24390, 1994. PubMed: 7929099.Pegues,J.C., Chen,L.S., Gordon,A.W., Ding,L. and Coleman,W.G.Jr. Cloning, expression, and characterization of the Escherichiacoli K-12 rfaD gene. J. Bacteriol. 172(8): 4652-4660, 1990. PubMed: 2198271. ","","Thu Dec 12 15:07:19 2002","1","","","" "AA00540","370321","370190","132","TTGCCGCCAATTTACCTTCTGCCAAATATATTGTTGTTCCATGCCGCAATTACCTTATTATTCGCCTTAAAATATAAGGCAAATAATATAATTATTTGCCTTATTTGTCATTGCTATTTTCAAAAGTGCGGC","","","5017","LPPIYLLPNILLFHAAITLLFALKYKANNIIICLICHCYFQKCG","370190","","hypothetical protein","Cytoplasm, Periplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide
tmhmm\"[4-23]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:32:48 2004","Sun Feb 22 16:32:48 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00540 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:32:48 2004","","","","","","","","","","","","","1","","","" "AA00541","370280","371404","1125","ATGGAACAACAATATATTTGGCAGAAGGTAAATTGGCGGCAATGGGAATACGACTTGCCACAGTTACTTCCGCTATTAAACCAAGCCCATTATCAACAGGGCTTACTGCTGGGAAGATTGTTGGATATCGGTTTAGGTGAGCGTGAACAGATCTGCCTTCAGGCATTAACCAACAGTGTCCTCAAAAGTAGTGAAATCGAAGGCGAAATGCTCAATGCACAATCCGTGCGTTCTTCCCTGGCTCGCCGTTTAGGCGTTAATATCGGCGGATTAACCGCAACGGATCGTGCCGTCGAAGGCGTCGTAGAAATGACGTTAAATGCCACTGAACAGTTTGATAGCCCACTTACTCTAGAACGGCTGTTCGGCTGGCATGCCGCACTTTTCCCAAGCGGTTATAGCGGAATGGTAAGAATTCGGACGGCACAATTGCGCGATGATAACAATGGTGCAATGCAAGTAATTTCAGGGAGAATCGGGAGACAAAAAATTCATTTTCAGGCACCGCCGGCTGAACAACTTGAAAAGGAATTAATGTTATTTCTAACCTGGCTGAATGATTCGAACCAACTGCTTGATCCTTTTATTAAAACCGGCATCGCTCATCTCTGGTTTTTAACTCTGCACCCTTTTGAAGATGGTAATGGTCGCATTGCACGTGCTATTGCGGATTATTTGCTTGCCAAAGCTGATAGAAACCCACAACGGTTTTACAGCCTGTCTGCCCAAATCCAAAAAGAGCGGTCGAGTTATTATGTGATTTTAGAGCAAACCCAGAAAGGCGAAACCAACTTAACCCAATGGCTGATGTGGTTTTTAGCCTGTTTAATCAATGCCATGAAGCAGGCACAGGAAACCTTGGATAAAGTTTTACTGAAAACCCGATACTGGCAATCCTGGCATCGGTTTTCGCTCAATGAACGGCAAATTAAAGTTCTCAATCTTATGTTAGATGGCTTTGAAGGCAAACTTGGCAATAAAAAATATGCCGCCTTAACCAAAGTGTCGCGGGACACCGCCTTGCGGGATCTCACGGATTTAGTCGCAAAAAATATATTGAAACGCGCGGAAGAAGGCGGGCGGAGCATTCATTATGAATTAACACCCCCGGATTTATCACAAGTT","","","42990","MEQQYIWQKVNWRQWEYDLPQLLPLLNQAHYQQGLLLGRLLDIGLGEREQICLQALTNSVLKSSEIEGEMLNAQSVRSSLARRLGVNIGGLTATDRAVEGVVEMTLNATEQFDSPLTLERLFGWHAALFPSGYSGMVRIRTAQLRDDNNGAMQVISGRIGRQKIHFQAPPAEQLEKELMLFLTWLNDSNQLLDPFIKTGIAHLWFLTLHPFEDGNGRIARAIADYLLAKADRNPQRFYSLSAQIQKERSSYYVILEQTQKGETNLTQWLMWFLACLINAMKQAQETLDKVLLKTRYWQSWHRFSLNERQIKVLNLMLDGFEGKLGNKKYAALTKVSRDTALRDLTDLVAKNILKRAEEGGRSIHYELTPPDLSQV","371406","","conserved hypothetical protein","Cytoplasm, Inner membrane","","
InterPro
IPR003812
Family
Filamentation induced by cAMP protein Fic
PF02661\"[121-261]TFic
noIPR
unintegrated
unintegrated
PTHR13504\"[184-220]TFAMILY NOT NAMED
PTHR13504:SF11\"[184-220]Tgb def: Hypothetical protein ZK593.8


","BeTs to 6 clades of COG3177COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3177 is -o-----q------ef-h-nuj----Number of proteins in this genome belonging to this COG is","","Residues 287 to 367 match (9e-19) PD:PD354797 which is described as PROTEOME COMPLETE PLASMID PA0574 ATU5350 RSC3413 YPO0445 ","","","","","","","","","","","","Thu Dec 12 15:08:32 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00541 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 121 to 261 (E-value = 3.7e-19) place AA00541 in the Fic family which is described as Fic protein family (PF02661)","","","","","","","","1","","","" "AA00543","371427","372467","1041","ATGAATATCCTGATTATCGGCCCGTCTTGGGTCGGCGATATGATGATGTCGCACAGTTTGTATCAACAGCTCAAATTGCAATATCCCCATTGCCACATCGATGTGATAGCGCCTAATTGGTGCAAACCGTTGTTGGCGCGCATGCCGGAGGTGCGGAATGCCATTGAGATGCCACTCGGGCACGGGAAATTTGCGTTGTGTGAGCGTTATCGTTTGGGCAAGGCGTTGCGCAACCAATATGACATGGCGATTGTGTTGCCGAATTCGCTGAAATCGGCGTTTATTCCGTTGTTTGCGAAAATTGCCGTGCGGCGCGGTTGGAAAGGGGAAAGCCGTTATTGGCTGCTCAATGACTTACGCCATAACAAACGGGATTACCCGATGATGGTGCAACGTTATGTGGCGTTGGCGTTTGAAAAAAATGCCGTGCCGAAAGCCGTTGAGATTCCTGTGCTGAAGCCTTATTTAACCGTCGAACCTAGCCGGCAGGCGGCGACCTTAAAAACGTTTGAAAAACCGACCGCACTTTTAGGCAGGCGTCCGATTGTCGGTTTTTGCCCCGGCGCGGAATTCGGTCCGGCGAAGCGTTGGCCGCATTATCATTATGCCGAACTGGCGCGGATGCTTATTGAAAAAGGTTATGCAGTGGAACTTTTCGGCTCGCCGAAAGATGTGGACGCCGGCGAACAAATCCGTAACGCCTTGCCTGTCGAACTGCAGCCTTTCTGCTTGAATCTGGCGGGACAAACCAATCTCAATCAGGCGGTGGATTTAATCGCCAACTGCACCGCCGTCGTCAGTAACGACAGCGGTTTAATGCACATTGCCGCGGCGACCGATCGCCCGTTAGTGGCGCTTTACGGCCCAACCAGCCCCGCTTACACCCCCCCGTTATCGGACAATGCCGAAATCATTCGGTTAATAGAAGGGGATTTGATTAAAGTACGCAAAAGCGCCGACAGCACGGAAGGCTATCATCAGAGTTTGATCGATATTACGCCGCAGCTGGTGTTTGAAAAGTTAATGGGATTACTCAATCAA","","","38915","MNILIIGPSWVGDMMMSHSLYQQLKLQYPHCHIDVIAPNWCKPLLARMPEVRNAIEMPLGHGKFALCERYRLGKALRNQYDMAIVLPNSLKSAFIPLFAKIAVRRGWKGESRYWLLNDLRHNKRDYPMMVQRYVALAFEKNAVPKAVEIPVLKPYLTVEPSRQAATLKTFEKPTALLGRRPIVGFCPGAEFGPAKRWPHYHYAELARMLIEKGYAVELFGSPKDVDAGEQIRNALPVELQPFCLNLAGQTNLNQAVDLIANCTAVVSNDSGLMHIAAATDRPLVALYGPTSPAYTPPLSDNAEIIRLIEGDLIKVRKSADSTEGYHQSLIDITPQLVFEKLMGLLNQ","372469","","ADP-heptose--LPS heptosyltransferase II","Inner membrane, Cytoplasm","","
InterPro
IPR002201
Family
Glycosyl transferase, family 9
PF01075\"[69-326]TGlyco_transf_9
InterPro
IPR011910
Family
Lipopolysaccharide heptosyltransferase II
TIGR02195\"[2-346]Theptsyl_trn_II: lipopolysaccharide heptosyl
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2000\"[1-149]T\"[163-345]Tno description


","BeTs to 9 clades of COG0859COG name: ADP-heptose:LPS heptosyltransferaseFunctional Class: MThe phylogenetic pattern of COG0859 is -------q-----cefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 3.2e-38) to 2/2 blocks of the IPB002201 family, which is described as \"Glycosyltransferase family 9\". Interpro entry for IP:IPR002201. IPB002201A 12-36 2.7e-11 IPB002201B 249-292 1.3e-25","Residues 180 to 297 match (6e-07) PD:PD023978 which is described as TRANSFERASE COMPLETE PROTEOME BIOSYNTHESIS LIPOPOLYSACCHARIDE WAAQ CORE III HEPTOSYLTRANSFERASE RFAQ ","","","","","","","","","","","","Thu Dec 12 15:19:46 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00543 is paralogously related to AA01396 (1e-06), AA01329 (5e-04) and AA01327 (0.001).","","","","","","Residues 69 to 326 (E-value = 4.4e-105) place AA00543 in the Glyco_transf_9 family which is described as Glycosyltransferase family 9 (heptosyltransferase) (PF01075)","","","","","auer,B.A., Lumbley,S.R. and Hansen,E.J. Characterization of a WaaF (RfaF) homolog expressed byHaemophilus ducreyi Infect. Immun. 67 (2), 899-907 (1999) PubMed: 9916106 Pegues,J.C., Chen,L.S., Gordon,A.W., Ding,L. and Coleman,W.G.Jr. Cloning, expression, and characterization of the Escherichiacoli K-12 rfaD gene J. Bacteriol. 172 (8), 4652-4660 (1990) PubMed: 2198271 Chen,L. and Coleman,W.G. Jr. Cloning and characterization of the Escherichia coli K-12 rfa-2 (rfaC) gene, a gene required for lipopolysaccharide inner core synthesis J. Bacteriol. 175 (9), 2534-2540 (1993) PubMed: 8478319 ","","Thu Dec 12 15:19:46 2002","1","","","" "AA00544","372588","373793","1206","ATGCCGGATCGCTCACCTAATATCACGACACATGATCCTTTCGGCAGCTTGTTGGGTTACGCGCCCGGCGGTGTTGCCATTTATTCTTCAGATTACAACACAGCGGATGCGCAGGAATACCCTGACGATGCCGCCTTTCGTAGCTATCTCGGCGGCGAATACATGGGCTACAAATGGCAATGCGTGGAATTCGCCCGTCGCTATCTTTATCTCAATTACGGCATGGTGTTCACCGATGTGGGCATGGCGTATGAAATTTTTTCCTTACGCTTTTTGCGCCAAGTGGTGAATGACGCCCTGTTGCCGTTGCAAGCCTTTGCCAACGGCGGCAAACGGGCGCCGGAATGCGGGGCATTGCTCATTTGGCAGGAAGGCGGCGAATTTAAGCACACCGGGCATGTGGCGGTGATTACTGAAGTATTGGCGGACAAAGTGCGTATCGCCGAGCAAAACGTGATTCACTCCCGCCTGCCAAGCGGTCAACAATGGACACGTGAGCTGCCGATGACGGTTACGGCTGGGAGATACCGCCTGCAAGACACCTTTGATGACACGGAAATTCTCGGCTGGATGATTCAAACGGACAACGAGGAATTTAGTCTGCCGCAACCGATGCCGGCGCCGGAGAAACTCACCATTCATGCAGAACACATTGAAAATCAGGGACAATTCGCCGCCAATTGGCTGAATGAAGACAACCCGCTGGAAGCGGCTTACGTGAAGGCAATGAAGGGACACATCGTCAATCATGGCGATCAATATCGCTATTTTGCCCTTTCCGAAAGCGCACAACATGAGCTGATTCGCGCCACCAATGAGCTGCATTTGATGTATTTGCACGCCACCGACAAGGTGCTGAAAGACGATAAGTTATTGCAATATTTCAATATTCCGAAACTGCTGTGGCCGCGTTTACGCTTATCCTGGCAAAATCGTCGTTATCAAACCATCACCGGCAGAATGGATTTTTGTTTGGATGAACGCGGTTTGAAAGTTTATGAATACAACACCGATTCCGCCTCTTGTCACGCAGAAGCGGGGGCGATTTTGCCCCATTGGGCGGCACTGGCGGGTTTAACCTTAAGGCATGACCCTGGCGAAGGCTTACGCAATGCCTTGGCGGATACCTGGAAACACAGCCACGCCGTTGGTGCACATTATGCAGGATCACGATGCGGAAGAAGAATATCACGCCTTGTTTATGCG","","","45677","MPDRSPNITTHDPFGSLLGYAPGGVAIYSSDYNTADAQEYPDDAAFRSYLGGEYMGYKWQCVEFARRYLYLNYGMVFTDVGMAYEIFSLRFLRQVVNDALLPLQAFANGGKRAPECGALLIWQEGGEFKHTGHVAVITEVLADKVRIAEQNVIHSRLPSGQQWTRELPMTVTAGRYRLQDTFDDTEILGWMIQTDNEEFSLPQPMPAPEKLTIHAEHIENQGQFAANWLNEDNPLEAAYVKAMKGHIVNHGDQYRYFALSESAQHELIRATNELHLMYLHATDKVLKDDKLLQYFNIPKLLWPRLRLSWQNRRYQTITGRMDFCLDERGLKVYEYNTDSASCHAEAGAILPHWAALAGLTLRHDPGEGLRNALADTWKHSHAVGAHYAGSRCGRRISRLVYA","373795","Trypanothione (N1,N8-bis(glutathionyl)spermidine) is synthesized typically in trypanosomes by gspS/","glutathionylspermidine synthetase;amidase","Cytoplasm","","
InterPro
IPR005494
Family
Glutathionylspermidine synthase
PF03738\"[257-338]TGSP_synth
InterPro
IPR007921
Domain
Cysteine, histidine-dependent amidohydrolase/peptidase
PF05257\"[41-178]TCHAP
PS50911\"[36-179]TCHAP


","BeTs to 3 clades of COG0754COG name: Glutathionylspermidine synthaseFunctional Class: EThe phylogenetic pattern of COG0754 is -------------ce--h--uj----Number of proteins in this genome belonging to this COG is","","Residues 15 to 151 match (3e-15) PD:PD331533 which is described as SYNTHETASE TRYPANOTHIONE GSP LIGASE E.COLI PROTEOME COMPLETE AMIDASE RELATED ","","","","","","","","","","","Mon Feb 17 13:09:33 2003","Mon Feb 17 13:09:33 2003","","Thu Mar 18 10:39:49 2004","","Thu Mar 18 10:39:49 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00544 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Mar 18 10:39:49 2004","","","","","Residues 41 to 178 (E-value = 3.1e-26) place AA00544 in the CHAP family which is described as CHAP domain (PF05257)","Thu Mar 18 10:39:49 2004","","","","Bollinger JM, Kwon DS, Huisman GW, Kolter R, Walsh CT.Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase.J Biol Chem. 1995 Jun;270(23):14031-41.PMID: 7775463Amssoms K, Oza SL, Augustyns K, Yamani A, Lambeir AM, Bal G, Van der Veken P, Fairlamb AH, Haemers A.Glutathione-like tripeptides as inhibitors of glutathionylspermidine synthetase. Part 2: substitution of the glycine part.Bioorg Med Chem Lett. 2002 Oct;12(19):2703-5.PMID: 12217358Oza SL, Tetaud E, Ariyanayagam MR, Warnon SS, Fairlamb AH.A single enzyme catalyses formation of Trypanothione from glutathione and spermidine in Trypanosoma cruzi.J Biol Chem. 2002 Sep;277(39):35853-61.PMID: 12121990","","Thu Mar 18 10:39:49 2004","1","","","" "AA00545","373747","374475","729","ATGCAGGATCACGATGCGGAAGAAGAATATCACGCCTTGTTTATGCGTGATACGCTGACGCAGGCGGGTTTTAACACCAAGATTATCCACGGCACAGAAGGGTTGCATTGGGATACGCGCGGACAATTATTGGACGACGAAAATCAACGGGTGCAAAGCGTATGGAAAACCTGGGCATGGGAAACCGTGCTGGAACAATTACGCGAAGATGCCACCGGGCGTGAAGTGGCACCGCCGATTCGCACCGGTTATCCGGAAGATAAAGTGCGGTTGATTGACGTGTTACTTCGTCCGGAAGTGTTGGTGTATGAGCCTTTATGGACGGCAATTCCAAGCAATAAAGCGATTTTGCCGGTGTTGTGGTCGTTGTTCCCGAATCACCGTTATTTGCTGGAAGCCGGTTTTGAACTTACGCCGAAACTCATTGCCAACGGTTATGCGCAAAAACCTATTACCGGTCGCCGTGGCGATAACGTAAAACTTATCGGCGAGTGCAAAACCGTCTTGGATAGCACCAACGGGTGTTTTGCTAAACAAGAAAATATCTACCAGCAATTATGGTGCTTGCCGAAAGTGGAAGATCAATATGTGCAGGTGTGTACGTTTACCGTAGGCGGGCATTATGCCGGCAGTTGTTTGCGCTCCGACCCGACCCGCGTGATTGTGGGCGACAGCGATATGCAACCGTTGCGAATATTGAGCGACAAAGTGTTTACGCAAAAAGCAAAA","","","30378","MQDHDAEEEYHALFMRDTLTQAGFNTKIIHGTEGLHWDTRGQLLDDENQRVQSVWKTWAWETVLEQLREDATGREVAPPIRTGYPEDKVRLIDVLLRPEVLVYEPLWTAIPSNKAILPVLWSLFPNHRYLLEAGFELTPKLIANGYAQKPITGRRGDNVKLIGECKTVLDSTNGCFAKQENIYQQLWCLPKVEDQYVQVCTFTVGGHYAGSCLRSDPTRVIVGDSDMQPLRILSDKVFTQKAK","374477","","glutathionylspermidine synthetase;amidase","Cytoplasm","","
InterPro
IPR005494
Family
Glutathionylspermidine synthase
PF03738\"[99-199]TGSP_synth


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 17 13:10:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00545 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Bollinger,J.M. Jr., Kwon,D.S., Huisman,G.W., Kolter,R. and Walsh,C.T. Glutathionylspermidine metabolism in Escherichia coli.Purification, cloning, overproduction, and characterization ofa bifunctional glutathionylspermidine synthetase/amidase J. Biol. Chem. 270 (23), 14031-14041 (1995) PubMed: 7775463Amssoms K, Oza SL, Augustyns K, Yamani A, Lambeir AM, Bal G, Van der Veken P, Fairlamb AH, Haemers A. Glutathione-like tripeptides as inhibitors of glutathionylspermidine synthetase. Part 2: substitution of theglycine part. Bioorg Med Chem Lett. 2002 Oct 7;12(19):2703-5. PMID: 12217358 Amssoms K, Oza SL, Ravaschino E, Yamani A, Lambeir A, Rajan P, Bal G, Rodriguez J, Fairlamb AH, Augustyns K,Haemers A. Glutathione-like tripeptides as inhibitors of glutathionylspermidine synthetase. Part 1: Substitution of theglycine carboxylic acid group. Bioorg Med Chem Lett. 2002 Sep 16;12(18):2553-6. PMID: 12182858 Oza SL, Tetaud E, Ariyanayagam MR, Warnon SS, Fairlamb AH. A single enzyme catalyses formation of Trypanothione from glutathione and spermidine in Trypanosoma cruzi. J Biol Chem. 2002 Sep 27;277(39):35853-61. PMID: 12121990 Steenkamp DJ. Thiol metabolism of the trypanosomatids as potential drug targets. IUBMB Life. 2002 Apr-May;53(4-5):243-8. Review. PMID: 12121003 Oza SL, Ariyanayagam MR, Fairlamb AH. Characterization of recombinant glutathionylspermidine synthetase/amidase from Crithidia fasciculata. Biochem J. 2002 Jun 15;364(Pt 3):679-86. PMID: 12049631 ","","Mon Feb 17 13:13:11 2003","1","","","" "AA00546","375199","374567","633","ATGTCAGCGAAGAAACCAAATATTTTAGTGCGATTCTGGCGTTGGTTCAGATCGCCTAGCCGTATTGCGGTAGGCACGATTATCGTCTTATCCTTTATCGGCGGTATTTTGTCCTGGGTCGGTTTTAACTACGGCTTGGAACAAACCAACACCGAGCAATTTTGTGCCGGCTGTCACATGAATGATGCGTACCCGGAATATTTGCACAGCGTACATTATCAAACCCGCACCGGCGTGAGCGCCAGCTGTCCGGATTGTCATGTTCCCCATGAATTCGGACCGAAAATGTGGCGTAAAATGGTGGCGGCAAAAGAAGTGTACGCGCATTATATGGGCTTAACTGATACGTTGGAGAAATTCAATGCCCGTCGTCCGCACATGGCGGAAAACGAGTGGGAGCGCATGAAAGCCAACGATTCCCAAGAATGTCGCAACTGCCACAAAATGGATCGTATGGATTTCTCCCAACAAAAAACCGTGGCACAAAGAATGCACAAATTTGCGCAGGAAAACGGCAAAACCTGTATTGATTGCCATAAAGGTATTGCGCACGAGTTGCCGGATATGAGCCGGGTTGCACCGGGTTGGTTGCAAGATACGGAAGTGAAACCGGCAGAAGAACAAGGCAAAAAA","","","24566","MSAKKPNILVRFWRWFRSPSRIAVGTIIVLSFIGGILSWVGFNYGLEQTNTEQFCAGCHMNDAYPEYLHSVHYQTRTGVSASCPDCHVPHEFGPKMWRKMVAAKEVYAHYMGLTDTLEKFNARRPHMAENEWERMKANDSQECRNCHKMDRMDFSQQKTVAQRMHKFAQENGKTCIDCHKGIAHELPDMSRVAPGWLQDTEVKPAEEQGKK","374569","From GenBank (gi:1171647):This protein mediates elecron flow from quinones to the napAB complex. It is a membrane-anchored periplasmic (potential) protein. ","cytochrome C-type protein (denitrification system component)","Periplasm, Inner membrane","","
InterPro
IPR005126
Domain
NapC/NirT cytochrome c, N-terminal
PD004960\"[81-190]TNAPC_HAEIN_P44655;
PF03264\"[18-189]TCytochrom_NNT
InterPro
IPR011031
Domain
Multihaem cytochrome
PS51008\"[50-184]TMULTIHEME_CYTC
InterPro
IPR011885
Family
Periplasmic nitrate reductase c-type cytochrome, NapC/NirT
PIRSF000013\"[6-200]TDenitrification system component NapC/NirT(membrane-bound tetrahaem cytochrome)
TIGR02161\"[8-190]TnapC_nirT: periplasmic nitrate (or nitrite)
noIPR
unintegrated
unintegrated
signalp\"[1-38]?signal-peptide
tmhmm\"[21-41]?transmembrane_regions


","BeTs to 5 clades of COG3005COG name: Nitrate/TMAO reductases, membrane-bound tetraheme cytochrome c subunitFunctional Class: CThe phylogenetic pattern of COG3005 is --------------efgh--u-----Number of proteins in this genome belonging to this COG is","","Residues 20 to 185 match (3e-07) PD:PD104045 which is described as C TETRAHEME CYTOCHROME ","","","","","","","","","","","Fri Jan 24 10:03:01 2003","Thu Dec 12 15:55:36 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00546 is paralogously related to AA02250 (2e-33).","","","","","","Residues 18 to 189 (E-value = 1.7e-104) place AA00546 in the Cytochrom_NNT family which is described as NapC/NirT cytochrome c family, N-terminal region (PF03264)","","","","","Vladymyrova IA.[The influence of different ions on the inhibitory postsynaptic potential of smooth muscle cells].Fiziol Zh. 21(5):624-7.PMID: 1218663Brondijk TH, Fiegen D, Richardson DJ, Cole JA.Roles of NapF, NapG and NapH, subunits of the Escherichia coli periplasmic nitrate reductase, in ubiquinol oxidation.Mol Microbiol. 2002 Apr;44(1):245-55.PMID: 11967083Simon J, Pisa R, Stein T, Eichler R, Klimmek O, Gross R.The tetraheme cytochrome c NrfH is required to anchor the cytochrome c nitrite reductase (NrfA) in the membrane of Wolinella succinogenes.Eur J Biochem. 2001 Nov;268(22):5776-82.PMID: 11722563Potter LC, Cole JA.Essential roles for the products of the napABCD genes, but not napFGH, in periplasmic nitrate reduction by Escherichia coli K-12.Biochem J. 1999 Nov;344 Pt 1:69-76.PMID: 10548535","","Fri Jan 24 10:03:01 2003","1","","","" "AA00547","375662","375216","447","ATGATTAGAAACAACGTATTTGCTTTTAGCGGTGCGCTATTTACGGCATTGTTCGCGACGTCCGTTATGGCGCAACAGCCGACGGAAGGCGCTGGAGATTTTTTCCATAATTCACCGGAAAGTGTCTCGCCGGCATTTCATGATGCACCGAAACAAAGCGAACTGCCTGCCTTAAACTATGTGAATCAACCGCCAATGGTGCCGCATAGTGTGAAAAATTATCAGGTCACCAAAAACGTGAACCAATGCTTAAACTGCCACAGCGTTGAAGCGTCGCGCGTGACCGGTGCAACCCGTATCAGCCCGACGCACTTTATGGATCGCGACGGCAACCTCGGCTCCAGCTCCTCTCCGCGTCGTTATTTCTGCTTACAATGCCACGTTTCTCAATCCGATGTTGAGCCAATCGTGCCAAACGAATTCAAACCGATGAAAGGTTACGGACAG","","","16717","MIRNNVFAFSGALFTALFATSVMAQQPTEGAGDFFHNSPESVSPAFHDAPKQSELPALNYVNQPPMVPHSVKNYQVTKNVNQCLNCHSVEASRVTGATRISPTHFMDRDGNLGSSSSPRRYFCLQCHVSQSDVEPIVPNEFKPMKGYGQ","375218","From GenBank (gi:1171646):This protein is a small subunit of the periplasmic reductase (NAP). It is only expressed at high levels during aerobic growth. The napAB complex receives electrons from the membrane-anchored tetraheme NapC protein, thus allowing electron flow between membrane and periplasm. NapB has essential functions for nitrate assimilation and may have a role in anaerobic metabolism. The midpoint redox potentials of the two heme groups are -25 MV and -175 MV. ","diheme cytochrome c precursor (periplasmic nitrate reductase)","Periplasm","","
InterPro
IPR005591
Family
Nitrate reductase cytochrome c-type subunit (NapB)
PF03892\"[6-148]TNapB
InterPro
IPR011031
Domain
Multihaem cytochrome
PS51008\"[78-132]TMULTIHEME_CYTC
noIPR
unintegrated
unintegrated
signalp\"[1-24]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","","Residues 13 to 148 match (7e-51) PD:PD012898 which is described as CYTOCHROME PERIPLASMIC COMPLETE PROTEOME NAPB PRECURSOR C NITRATE DIHEME C-TYPE ","","","","","","","","","","","Fri Jan 24 09:53:01 2003","Fri Jan 24 09:53:01 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00547 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 6 to 148 (E-value = 8.2e-80) place AA00547 in the NapB family which is described as Nitrate reductase cytochrome c-type subunit (NapB) (PF03892)","","","","","Iobbi-Nivol,C., Crooke,H., Griffiths,L., Grove,J., Hussain,H.,Pommier,J., Mejean,V. and Cole,J.A. A reassessment of the range of c-type cytochromes synthesizedby Escherichia coli K-12 FEMS Microbiol. Lett. 119 (1-2), 89-94 (1994) PubMed: 8039676 Brigé A, Cole JA, Hagen WR, Guisez Y, Van Beeumen JJ.Overproduction, purification and novel redox properties of the dihaem cytochrome c, NapB, from Haemophilus influenzae.Biochem J. 2001 Jun;356(Pt 3):851-8.PMID: 11389694Brondijk TH, Fiegen D, Richardson DJ, Cole JA.Roles of NapF, NapG and NapH, subunits of the Escherichia coli periplasmic nitrate reductase, in ubiquinol oxidation.Mol Microbiol. 2002 Apr;44(1):245-55.PMID: 11967083Brigé A, Leys D, Meyer TE, Cusanovich MA, Van Beeumen JJ.The 1.25 A resolution structure of the diheme NapB subunit of soluble nitrate reductase reveals a novel cytochrome c fold with a stacked heme arrangement.Biochemistry. 2002 Apr;41(15):4827-36.PMID: 11939777Brigé A, Cole JA, Hagen WR, Guisez Y, Van Beeumen JJ.Overproduction, purification and novel redox properties of the dihaem cytochrome c, NapB, from Haemophilus influenzae.Biochem J. 2001 Jun;356(Pt 3):851-8.PMID: 11389694","","Fri Jan 9 14:08:54 2004","1","","","" "AA00549","376581","375703","879","ATGGCGAATTCACCAAAATTTGCAGGCAAAGAGGCGCGGGAAAAACTGGGCTGGTGGCATGCCTATCGCTTCTTGTTTTGGCGTAGGCTCACGCAATTCGGCATCCTGATGATGTTTTTAAGCGGTCCTTACTTTGGTGTGTGGATTTTAAAAGGCAATTACAGCGGAAGTCTGCTTTTCGATGTGATTCCGTTAAGTGATCCGTTAATTACGTTGGAAAGCCTTTCCACGAGGCATTTACCGGGAACCCTGACCCTCATCGGCGCGTTGATTATCTTTACGTTGTATGCGTTGTTAGGTAGCAAAGTTTTCTGCGGCTGGGTTTGTCCGCTGAATGTGGTTACCGATTGCGCCGCCTGGATTCGCCGGAAACTGGGCATTCGCCAAACGGCAAAAATTCCGCGCGGGTTACGTTATGCCATTTTGCTGATGATTTTAGTCGGCAGTGCAGTCAGCGGTTTGTTACTGTGGGAATGGATTAATCCGGTGGCGGCGTTAGGTCGCGCTTTAATTTATAGTTTCGGAGCGACGGCATGGTTGATTTTAGCGGTATTTCTGTTTGATTTATTCATTGTTGAACACGGTTGGTGCGGGCATTTGTGTCCTATTGGCGCAACCTATGGCGTCATTGGTGCGAAAAGTCTGATTCGGATCAAAGTGATTGATCGGGCAAGATGTGACAATTGCATGGATTGCTACAACGTTTGCCCGGAACCCCAAGTGTTGCGTTCGCCATTACACGGAAAAAATAACGAAAGCTTGTTAGTGCTTTCGCAAGATTGCATCAGTTGCGGGCGTTGCATTGATGTCTGCGCTGAAAACGTATTAACTTTTAGCCATCGGTTTAATAACGACATTCCTATCGTCACCCTAAACCAA","","","41381","MANSPKFAGKEAREKLGWWHAYRFLFWRRLTQFGILMMFLSGPYFGVWILKGNYSGSLLFDVIPLSDPLITLESLSTRHLPGTLTLIGALIIFTLYALLGSKVFCGWVCPLNVVTDCAAWIRRKLGIRQTAKIPRGLRYAILLMILVGSAVSGLLLWEWINPVAALGRALIYSFGATAWLILAVFLFDLFIVEHGWCGHLCPIGATYGVIGAKSLIRIKVIDRARCDNCMDCYNVCPEPQVLRSPLHGKNNESLLVLSQDCISCGRCIDVCAENVLTFSHRFNNDIPIVTLNQ","375705","From GenBank (gi:1171650):This protein is involved in electron transfer. ","ferredoxin-type protein","Inner membrane, Periplasm, Cytoplasm","","
InterPro
IPR001450
Domain
4Fe-4S ferredoxin, iron-sulfur binding
PF00037\"[219-242]T\"[254-277]TFer4
PS00198\"[226-237]?4FE4S_FERREDOXIN
InterPro
IPR011886
Family
Ferredoxin-type protein, NapH/MauN family
TIGR02163\"[24-280]TnapH_: ferredoxin-type protein, NapH/MauN f
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.20\"[221-276]Tno description
signalp\"[1-46]?signal-peptide
tmhmm\"[30-50]?\"[80-100]?\"[140-160]?\"[170-192]?transmembrane_regions


","BeTs to 11 clades of COG0348COG name: PolyferredoxinFunctional Class: CThe phylogenetic pattern of COG0348 is a-mp---------cefgh-nuj----Number of proteins in this genome belonging to this COG is","","Residues 222 to 271 match (2e-07) PD:PD000058 which is described as COMPLETE PROTEOME IRON-SULFUR SUBUNIT OXIDOREDUCTASE 4FE-4S ELECTRON FERREDOXIN POLYFERREDOXIN I ","","","","","","","","","","","Fri Jan 24 10:12:08 2003","Thu Dec 12 15:59:53 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00549 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Potter LC, Cole JA. Essential roles for the products of the napABCD genes, butnot napFGH, in periplasmic nitrate reduction by Escherichiacoli K-12. Biochem J. 1999 Nov 15;344 Pt 1:69-76. PMID: 10548535Brondijk TH, Fiegen D, Richardson DJ, Cole JA.Roles of NapF, NapG and NapH, subunits of the Escherichia coli periplasmic nitrate reductase, in ubiquinol oxidation.Mol Microbiol. 2002 Apr;44(1):245-55.PMID: 11967083","","Fri Jan 24 10:12:08 2003","1","","","" "AA00550","377261","376584","678","TTGCGTCCACCTTTCGCCATCGAAAGTGACGAGAAATTTGCCTCCGCCTGCATTCGTTGCGGTCAGTGCGTGCAAGCCTGCCCTTATGATATGTTGCATTTGGCATCGTTGCTATCACCAATGGAAGCGGGGACGCCGTATTTTATCGCGCGCGATAAACCTTGCGAAATGTGTCCGGATATTCCTTGCGCCCATGCGTGTCCGAGCGGTGCGTTAGATCGTGAGGCGCAGGATATTAATCAATCCCGTATGGGGCTGGCGGTGTTGCTGGATCATGAAACCTGCTTGAACTGGCAAGGCTTGCGTTGCGATGTGTGTTATCGGGTTTGTCCGTTGATTGATAAAGCCATTACGCTGGAAAGCCATCGTAATGAGCGCACCGGCAAGCACGCGGTGTTTATTCCGACGGTGCATTCCGATGGCTGTACCGGCTGTGGCAAATGCGAACAAGCGTGTGTCTTGGAAGAAGCGGCAATCAAAGTATTACCGATGCATTTGGCGAAAGGCATGTTAGGCAAACATTATCGTTTGGGTTGGGAAGAAAAGGCGAAAGCCGGACATTCCTTGGCGCCGAAAGATTTGATTTCGATGCCGACCCGTATGCCGGAAGCCACAATGCCGGTAATGGGCGCAGAAGACATTCCGGAGCCGATTCTGGCACCGACATTGGGAGGCAAA","","","31213","LRPPFAIESDEKFASACIRCGQCVQACPYDMLHLASLLSPMEAGTPYFIARDKPCEMCPDIPCAHACPSGALDREAQDINQSRMGLAVLLDHETCLNWQGLRCDVCYRVCPLIDKAITLESHRNERTGKHAVFIPTVHSDGCTGCGKCEQACVLEEAAIKVLPMHLAKGMLGKHYRLGWEEKAKAGHSLAPKDLISMPTRMPEATMPVMGAEDIPEPILAPTLGGK","376586","From GenBank (gi:117164):This protein is involved in electron transfer.","ferredoxin-type protein","Periplasm, Cytoplasm","","
InterPro
IPR001450
Domain
4Fe-4S ferredoxin, iron-sulfur binding
PR00353\"[10-21]T\"[62-73]T4FE4SFRDOXIN
PF00037\"[10-33]T\"[135-160]TFer4
PS00198\"[17-28]T4FE4S_FERREDOXIN
InterPro
IPR004494
Family
MauM/NapG ferredoxin-type protein
TIGR00397\"[1-179]TmauM_napG: MauM/NapG family ferredoxin-type
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.20\"[15-77]Tno description


","No hits to the COGs database.","","Residues 1 to 69 match (4e-25) PD:PD132213 which is described as REDUCTOISOMERASE KETOL-ACID OXIDOREDUCTASE ACID ALPHA-KETO-BETA-HYDROXYLACIL ISOMEROREDUCTASE BIOSYNTHESIS NADP AMINO BRANCHED-CHAIN ","","","","","","","","","","","Fri Jan 24 10:17:27 2003","Thu Dec 12 16:01:12 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00550 is paralogously related to AA00044 (2e-04).","","","","","","Residues 10 to 33 (E-value = 8.7e-06) place AA00550 in the Fer4 family which is described as 4Fe-4S binding domain (PF00037)","","","","","Potter LC, Cole JA. Essential roles for the products of the napABCD genes, butnot napFGH, in periplasmic nitrate reduction by Escherichiacoli K-12. Biochem J. 1999 Nov 15;344 Pt 1:69-76. PMID: 10548535Brondijk TH, Fiegen D, Richardson DJ, Cole JA.Roles of NapF, NapG and NapH, subunits of the Escherichia coli periplasmic nitrate reductase, in ubiquinol oxidation.Mol Microbiol. 2002 Apr;44(1):245-55.PMID: 11967083Reyes F, Gavira M, Castillo F, Moreno-Vivián C.Periplasmic nitrate-reducing system of the phototrophic bacterium Rhodobacter sphaeroides DSM 158: transcriptional and mutational analysis of the napKEFDABC gene cluster.Biochem J. 1998 May;331 ( Pt 3):897-904.PMID: 9560320","","Fri Jan 24 10:17:27 2003","1","","","" "AA00551","377463","377365","99","GTGTTAAAAACCTACCGCACTTTTGTGTCTTCAAGCCAGAAAAGTGCGGTCAGAAAATCAAAAGAAAATGCAAAAACCGACTGTAACGCCCGAACGCCG","","","3684","VLKTYRTFVSSSQKSAVRKSKENAKTDCNARTP","377365","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:34:00 2004","Sun Feb 22 16:34:00 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00551 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:34:00 2004","","","","","","","","","","","","","1","","","" "AA00552","379954","377471","2484","ATGAATTTAAGTCGTCGAGACTTTATGAAAGCCAATGCGGCGATGGCAGCCGCAACGGCGGCCGGGTTAAGTATTCCGGTCAAAAATGTTGAAGCTGCAGAATCCGAAATTAAATGGGATAAAGCGGTTTGCCGTTTCTGCGGTACCGGTTGTGCGGTATTGGTGGGCACCAAAGACGGTCGTGTTGTGGCTTCACAAGGCGATCCGGATGCGGAAGTCAACCGTGGTTTGAACTGCATTAAAGGCTATTTCTTACCGAAAATCATGTACGGTAAAGACCGTTTGACGCAGCCGATGTTGCGCATGAAAGACGGCAAATACGATAAAAACGGTGATTTCACGCCGGTGAGCTGGGACGTGGCGTTTAAGACCATGGCGGAAAAATTTAAAGCTGCAGTGAAAGAATTAGGTCCGAACGGCGTAGGGATGTTCAGTTCCGGGCAGACCACCATTTTTGAAGGCTATGCCAAATCCAAATTGTGGAAAGCCGGTTTCCGTTCTAACAACATCGACCCTAACGCCCGTCACTGTATGGCGTCTGCGGCGGTTGCCTTTATGCGTACTTTCGGCATGGATGAACCGATGGGCTGTTATAACGACATCGAACAAGCCGAAGCCTTCGTACTTTGGGGTTCCAACATGGCGGAAATGCATCCGATTTTGTGGTCCCGTATTACCGATCGTCGTCTATCCAACCAAGATGTGAAAGTCGCCGTGCTTTCTACTTTTGAACATCGTAGTTTTGAATTGGCGGATTATAGCCTCATTTTCAAACCGCACACCGACTTGGTGATTTTGAACTACATTATCAATTATCTGATTCAAAACGATGCCATTAACCGGGATTTCGTCAACAAACATACCAAATTCAAACGCGGCGAAACCGACATTGGTTATGGTTTGCGCCCTGAAAATCCGTTGGAACAAAAAGCGAAAAACGTGAAAACGGCAGGCAAAATGTATGACAGTAACTTTGATGAATTAAAAGCCTTAGTCGCCGAATATACGTTAGACAAAGCCCATGAAATGTCAGGCGTGCCGAAAGATGTGTTGGAAAATTTGGCGAAATTGTATGCCGATCCGAAGAAAAAAGTGGTGTCTTACTGGACCATGGGCTTTAACCAACATACCCGCGGCGTGTGGGCGAACCACCTCATTTATAACATCCATTTGCTGACCGGTAAAATTTCCATTCCGGGCTGCGGTCCGTTCTCGTTAACCGGTCAACCGTCTGCTTGTGGTACGGCGCGCGAAGTGGGAACGTTTATCCACCGCCTGCCGGCAGACTTAGTGGTCACCAATCCGAAACACCGTGAAAAAGCGGAACAAATCTGGAAATTGCCTGCCGGCGTGATTACTGATGTTCTCGGCTTCCATGCGGTCGCTCAAAGTCGTGCGTTAAAAGACGGCAAAATGCGCGTGTTGTGGCAAATGTGTACCAACAATATGCAAGGCGGTCCGAATATTAACAGAGAAACCTTCCCGGGCTGGCGTAATCCGGACAATTTTATTGTGGTGTCCGATCCGTACCCGACGGTGTCCTGTCTAGCCGCCGACTTGATGTTGCCAACGGCAATGTGGGTGGAAAAAGAAGGCGCTTACGGTAACGCGGAGCGTCGTACCCAATTCTGGCGTCAACAAGTAAAAGCGCCGGGAGAAGCCAAATCCGACGTATGGCAATTGGTAGAATTCTCCAAATATTTCACCACCGATGAAATGTGGCCGGCGGAAATTCTGGACAAAAATCCGGAATACAAAGGCAAAACCTTATATGACGTGTTATACCGCAACGGTCAAGTAGATAAATTCCCGTTAAGCGAATTGGCGGAAGGACAATTGAATGATGAGTCCTATCACTTCGGTTTCTACTTGCAAAAAGGCTTATTTGAGGAATACGCCTCCTTCGGTCGCGGTCACGGACATGACTTGGCATCGTTCGATACTTACCACAAAGCACGCGGTTTACGCTGGCCGGTGGTGGACGGCAAAGAAACCTTATGGCGTTATCGCGAAGGCTACGACCCGTATGTCAAAGAAGGGGAAGGTGTGGCGTTCTACGGCTATCCGGATAAAAAAGCGATTATTCTTGCCGTGCCTTATGAGCCGCCTGCGGAATCACCGGACGAAGAATACGATTTGTGGTTATGTACCGGTCGCGTGTTGGAACACTGGCACACCGGCACCATGACCCGTCGTGTACCAGAACTGCACCGCTCCTTCCCGAATAACTTGGTTTGGATGCACCCGACAGACGCGCAAAAGCGCGGGTTACGCCATGGTGATAAAGTCAAAGTCGCTTCACGTCGAGGAGAAATCATTTCGTTCTTAGATACCCGCGGACGTAACAAGGTGCCGGAAGGTTTGATTTACACAACCTTCTTTGATGCCGGTCAGTTGGCGAATAAATTAACCTTGGACGCGACCGACCCGATTTCCAAAGAAACCGACTTCAAAAAATGTGCGGTGAAAGTGGAAAAAGCCGCT","","","93487","MNLSRRDFMKANAAMAAATAAGLSIPVKNVEAAESEIKWDKAVCRFCGTGCAVLVGTKDGRVVASQGDPDAEVNRGLNCIKGYFLPKIMYGKDRLTQPMLRMKDGKYDKNGDFTPVSWDVAFKTMAEKFKAAVKELGPNGVGMFSSGQTTIFEGYAKSKLWKAGFRSNNIDPNARHCMASAAVAFMRTFGMDEPMGCYNDIEQAEAFVLWGSNMAEMHPILWSRITDRRLSNQDVKVAVLSTFEHRSFELADYSLIFKPHTDLVILNYIINYLIQNDAINRDFVNKHTKFKRGETDIGYGLRPENPLEQKAKNVKTAGKMYDSNFDELKALVAEYTLDKAHEMSGVPKDVLENLAKLYADPKKKVVSYWTMGFNQHTRGVWANHLIYNIHLLTGKISIPGCGPFSLTGQPSACGTAREVGTFIHRLPADLVVTNPKHREKAEQIWKLPAGVITDVLGFHAVAQSRALKDGKMRVLWQMCTNNMQGGPNINRETFPGWRNPDNFIVVSDPYPTVSCLAADLMLPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSDVWQLVEFSKYFTTDEMWPAEILDKNPEYKGKTLYDVLYRNGQVDKFPLSELAEGQLNDESYHFGFYLQKGLFEEYASFGRGHGHDLASFDTYHKARGLRWPVVDGKETLWRYREGYDPYVKEGEGVAFYGYPDKKAIILAVPYEPPAESPDEEYDLWLCTGRVLEHWHTGTMTRRVPELHRSFPNNLVWMHPTDAQKRGLRHGDKVKVASRRGEIISFLDTRGRNKVPEGLIYTTFFDAGQLANKLTLDATDPISKETDFKKCAVKVEKAA","377473","From GenBank (gi:2497968):NapA is the large subunit of the periplasmic nitrate reductase (NAP). It is only expressed at high levels during anaerobic growth. The NapANapB complex receives electrons from the memebrane-anchored tetraheme NapC protein, thus allowing electron flow between membrane and periplasm. It has an essential function for nitrate assimilation and may have a role in anaerobic metabolism. ","periplasmic nitrate reductase precursor","Periplasm","","
InterPro
IPR006311
Domain
Twin-arginine translocation pathway signal
TIGR01409\"[3-32]TTAT_signal_seq
InterPro
IPR006655
Family
Prokaryotic molybdopterin oxidoreductase
PS00551\"[42-59]TMOLYBDOPTERIN_PROK_1
InterPro
IPR006656
Domain
Molybdopterin oxidoreductase
PF00384\"[94-567]TMolybdopterin
InterPro
IPR006657
Domain
Molydopterin dinucleotide-binding region
PF01568\"[713-821]TMolydop_binding
InterPro
IPR006963
Domain
Molybdopterin oxidoreductase Fe4S4 region
PF04879\"[37-91]TMolybdop_Fe4S4
InterPro
IPR009010
Domain
Aspartate decarboxylase-like fold
SSF50692\"[674-827]TAsp_decarb_fold
InterPro
IPR010051
Family
Periplasmic nitrate reductase, large subunit
TIGR01706\"[2-827]TNAPA
noIPR
unintegrated
unintegrated
G3DSA:2.40.40.20\"[673-827]TG3DSA:2.40.40.20
G3DSA:3.40.228.10\"[173-409]TG3DSA:3.40.228.10
G3DSA:3.90.55.10\"[28-122]TG3DSA:3.90.55.10
PTHR11615\"[40-301]T\"[318-645]T\"[703-826]TPTHR11615
PTHR11615:SF38\"[40-301]T\"[318-645]T\"[703-826]TPTHR11615:SF38
SSF53706\"[28-724]TSSF53706


","No hits to the COGs database.","Significant hit ( 2.1e-28) to 3/3 blocks of the IPB001467 family, which is described as \"Prokaryotic molybdopterin oxidoreductases\". Interpro entry for IP:IPR001467. IPB001467A 79-101 3.3e-09 IPB001467B 110-132 4.7e-07 IPB001467C 504-529 5.6e-09 IPB001467C 237-262 0.035","Residues 136 to 198 match (4e-08) PD:PD545867 which is described as NITRATE REDUCTASE OXIDOREDUCTASE ","","","","","","","","","","","Fri Jan 24 10:33:30 2003","Thu Dec 12 16:04:35 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00552 is paralogously related to AA02699 (3e-37), AA02251 (6e-18), AA01137 (1e-16), AA02676 (2e-16), AA02698 (8e-12) and AA02675 (1e-04).","","","","","","Residues 713 to 821 (E-value = 1.1e-40) place AA00552 in the Molydop_binding family which is described as Molydopterin dinucleotide binding domain (PF01568)","","","","","Brondijk TH, Fiegen D, Richardson DJ, Cole JA.Roles of NapF, NapG and NapH, subunits of the Escherichia coli periplasmic nitrate reductase, in ubiquinol oxidation.Mol Microbiol. 2002 Apr;44(1):245-55.PMID: 11967083Gavira M, Roldán MD, Castillo F, Moreno-Vivián C.Regulation of nap gene expression and periplasmic nitrate reductase activity in the phototrophic bacterium Rhodobacter sphaeroides DSM158.J Bacteriol. 2002 Mar;184(6):1693-702.PMID: 11872721Stewart V, Lu Y, Darwin AJ.Periplasmic nitrate reductase (NapABC enzyme) supports anaerobic respiration by Escherichia coli K-12.J Bacteriol. 2002 Mar;184(5):1314-23.PMID: 11844760","","Fri Jan 24 10:33:30 2003","1","","","" "AA00553","380272","379991","282","ATGAATAAAACAGACATTTTAACCATGGAAGACGCTAAAGATTGGCACATTGTCGGTCTGGTGGTGCAAGGCAAGCCGCAAAAAATAACAGCCATTCGCACCGCACTTTTGGCGATTCCACATACAGAAATCCCGACCTTTAATGAAAACATCGGCAAAATCGTGGCGGTAATGCAATCTCATGATCCGCATGTTTTGTTGAAGAACATGGAGTTGGTAAAAGAGATTGACGGTGTGATTACCGTGTCGCTGATTTATCATCAACAGGACGAACAGCCAGAA","","","10575","MNKTDILTMEDAKDWHIVGLVVQGKPQKITAIRTALLAIPHTEIPTFNENIGKIVAVMQSHDPHVLLKNMELVKEIDGVITVSLIYHQQDEQPE","379993","From GenBank (gi:1176632):NapD plays a role in the correct assembly of subunits of the periplasmic napAB enzyme.[not from genbank]***The functional class was taken from HD0073. Although it is not an ortholog, HD0073 is an napD gene and is in the vicinity of napABCGH genes.***","NapD component of periplasmic nitrate reductase","Cytoplasm","","
InterPro
IPR005623
Family
NapD
PF03927\"[13-92]TNapD
noIPR
unintegrated
unintegrated
PD328525\"[14-92]TNAPD_HAEIN_P44651;


","BeTs to 4 clades of COG3062COG name: Uncharacterized protein involved in formation of periplasmic nitrate reductaseFunctional Class: PThe phylogenetic pattern of COG3062 is --------------efgh--------Number of proteins in this genome belonging to this COG is","","Residues 14 to 92 match (9e-24) PD:PD328525 which is described as NAPD PROTEOME COMPLETE NITRATE PERIPLASMIC REDUCTASE COMPONENT PLASMID ASSEMBLY SOLUBLE ","","","","","","","","","","","Fri Jan 24 10:38:26 2003","Thu Dec 12 16:16:16 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00553 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Tue Mar 2 14:05:36 2004","","","","","Residues 13 to 92 (E-value = 1.8e-29) place AA00553 in the NapD family which is described as NapD protein (PF03927)","Tue Mar 2 14:05:36 2004","","","","Secondary Laboratory Evidence:Brondijk TH, Fiegen D, Richardson DJ, Cole JA. Roles of NapF, NapG and NapH, subunits of the Escherichiacoli periplasmic nitrate reductase, in ubiquinol oxidation. Mol Microbiol. 2002 Apr;44(1):245-55. PMID: 11967083 Gavira M, Roldn MD, Castillo F, Moreno-Vivin C.Regulation of nap gene expression and periplasmic nitrate reductase activity in the phototrophic bacterium Rhodobacter sphaeroides DSM158.J Bacteriol. 2002 Mar;184(6):1693-702.PMID: 11872721Potter LC, Cole JA.Essential roles for the products of the napABCD genes, but not napFGH, in periplasmic nitrate reduction by Escherichia coli K-12.Biochem J. 1999 Nov;344 Pt 1:69-76.PMID: 10548535Liu HP, Takio S, Satoh T, Yamamoto I.Involvement in denitrification of the napKEFDABC genes encoding the periplasmic nitrate reductase system in the denitrifying phototrophic bacterium Rhodobacter sphaeroides f. sp. denitrificans.Biosci Biotechnol Biochem. 1999 Mar;63(3):530-6.PMID: 10227138Berks BC, Richardson DJ, Reilly A, Willis AC, Ferguson SJ.The napEDABC gene cluster encoding the periplasmic nitrate reductase system of Thiosphaera pantotropha.Biochem J. 1995 Aug;309 ( Pt 3):983-92.PMID: 7639719","","Tue Mar 2 14:05:36 2004","1","","","" "AA00555","380502","380341","162","GTGCGGTGGTTTTTACCGGCGTTTTATCAAGCGGCGTTTTTTCATGCCTGCGTTCTTAAATTTGATCTAAAACAAATTGCGCTGGGAATCCGCCTAAAATACTCATTTGTAGTGATATTAATTCATTCGCAACAAATTAATATGCGGGATCTACAAAAAGAT","","","6424","VRWFLPAFYQAAFFHACVLKFDLKQIALGIRLKYSFVVILIHSQQINMRDLQKD","380341","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-19]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:35:22 2004","Sun Feb 22 16:35:22 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00555 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:35:22 2004","","","","","","","","","","","","","1","","","" "AA00557","380548","382248","1701","TTGAAAATTAAACATTCCGTTTCCACCCGCATTGCCAACTATCTTATTGTGATTATTATCTTTGTCGGCATCATCGGCGCATTAAGTCTGGCGCTGATGGCGGGCAATAAATCCTATGCGGAAGCCATTAACGTGTCCGGTTCATTGCGTATGCAAAGTTATCGCATACTTTATGAAATCGAACATGAACCACAAATGGTGGAAAGCAGCCTGCGCCAATATCGCGTGAGTTTGCATTCAAAATCCCTGGTGGAAATTAACTATCAGTCTTTTGCTTCGCAGGATGTGAAAGATTCCTATCACAATTTGATTAAACGCTGGGAAGTGATGGAACGTCTGGCGCGGGAACAAAATTTCACCGAATATCAAAAGAATATCGCCAATTATGTGGAACAAGTGGATCAATTTGTTTTTACCCTGCAACATTCGGCGGAAGAAAAATGGATTTGGGCGCTGTGCGTGATTATTTTTTCCATGCTGCTTATTGTGATCATGGTGTCTTACGTGAATTGGTACACCCGAAAAGCTGTGGTGCGCCCGCTGGAGCAGCTCACCCGCGCCAGTACGCAGGTGCAAATGGGGCAATTCAAGCATATTCCGCTGGACGTGCGTAAAGAAGACGAACTGGGGCATTTGGCGCGCACTTTCACTAAAATGTCATCGGAGTTGGGTAAACTGTATTCCGGTTTGGAAGCCACAGTGAATGAAAAAACGCAAAAGCTACAACAAACCAACCGCTCTTTAACGACCTTATATCACTGCTCCCAACTTGTGACGACCAATAAAATCGACGGCAAAATTTTGCAACTGGTGCTACAAAATGTCATGATTAGCGAACATTTACGCTATTTGGAACTGGATGTGTTAGACGCGCCGCATTGGAATATATGCTTGGGCGTGAAATATGACCAGCTGGAATCGCAACAAACGGAAATGAATATTGAAGGGGAAAGCCTCGCCGTATTGCGTTGGCAGGCGGGGTTGCCGTGTCCGGATTTGCGCACCATGCAAAATGTGGCTCAAATGCTCAGCCGCTCGCTGTATTTCCAACGCATGCAACGCCAGCAAGAACAGCTATTGTTGATGGAAGAACGTTCCATTATCGCCCGCGAATTGCACGATTCTTTGGCGCAAGTGTTGGCATTTTTGCAAATTCAGCTTACGCTGTTAAAACACAATTTGAACAAAGGCGAAACAGATTCCAAGCAAAAAAGTTTGTCGATTATTAAGCAGTTCGAACAGGCACTCAGCGACGGCTACAGCCAATTACGCGAACTGTTGGCGACGTTCCGTTTAACCGTGCAGGAAGCCAATTTGAAACTGGCATTGGAGCAAGTGATTGATTCCTTGCGCAATCAAACGGACATTCAAATGAGCGTGGATTGCACCTTGCCGTCACAAAGTTTTAACGCGCAGCAATTGGTCAATGCCTTGCAAATTGTGCGTGAAGCGGTGTTAAATGCCATTAAACATTCACAAGGCACACTCATTGAAGTCATCGCGCACACCAATGAAGACGGTGAATATGAACTAGTCGTGCGCGATAACGGAATCGGCATTCCAAGCCTGGAAGAGCCGGATGGACACTACGGGCTCAACATCATGCACGAGCGCAGCATACAACTTAACGCCAAACTGACCATTGCCAACCGCACCGACGGCGGCACGGAAGTGAAAGTCACATTGGCACACACATTAGCT","","","66103","LKIKHSVSTRIANYLIVIIIFVGIIGALSLALMAGNKSYAEAINVSGSLRMQSYRILYEIEHEPQMVESSLRQYRVSLHSKSLVEINYQSFASQDVKDSYHNLIKRWEVMERLAREQNFTEYQKNIANYVEQVDQFVFTLQHSAEEKWIWALCVIIFSMLLIVIMVSYVNWYTRKAVVRPLEQLTRASTQVQMGQFKHIPLDVRKEDELGHLARTFTKMSSELGKLYSGLEATVNEKTQKLQQTNRSLTTLYHCSQLVTTNKIDGKILQLVLQNVMISEHLRYLELDVLDAPHWNICLGVKYDQLESQQTEMNIEGESLAVLRWQAGLPCPDLRTMQNVAQMLSRSLYFQRMQRQQEQLLLMEERSIIARELHDSLAQVLAFLQIQLTLLKHNLNKGETDSKQKSLSIIKQFEQALSDGYSQLRELLATFRLTVQEANLKLALEQVIDSLRNQTDIQMSVDCTLPSQSFNAQQLVNALQIVREAVLNAIKHSQGTLIEVIAHTNEDGEYELVVRDNGIGIPSLEEPDGHYGLNIMHERSIQLNAKLTIANRTDGGTEVKVTLAHTLA","382250","","nitrate/nitrite sensor protein","Inner membrane, Cytoplasm","","
InterPro
IPR003594
Domain
ATP-binding region, ATPase-like
G3DSA:3.30.565.10\"[443-565]Tno description
PF02518\"[472-565]THATPase_c
SM00387\"[473-566]THATPase_c
InterPro
IPR003660
Domain
Histidine kinase, HAMP region
PF00672\"[155-225]THAMP
SM00304\"[175-228]THAMP
PS50885\"[175-228]THAMP
InterPro
IPR005467
Domain
Histidine kinase
PS50109\"[367-566]THIS_KIN
InterPro
IPR011712
Domain
Histidine kinase, dimerisation and phosphoacceptor region
PF07730\"[364-436]THisKA_3
noIPR
unintegrated
unintegrated
signalp\"[1-27]?signal-peptide
tmhmm\"[14-34]?\"[150-172]?transmembrane_regions


","BeTs to 5 clades of COG3850COG name: Signal transduction histidine kinase, nitrate/nitrite-specificFunctional Class: TThe phylogenetic pattern of COG3850 is --------------efgh-n------Number of proteins in this genome belonging to this COG is","","Residues 368 to 445 match (6e-07) PD:PD489117 which is described as KINASE SENSOR PROTEOME COMPLETE TRANSFERASE SENSORY TRANSDUCTION PHOSPHORYLATION TWO-COMPONENT HRPX ","","","","","","","","","","","","Tue Feb 4 17:18:58 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00557 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 472 to 565 (E-value = 5.9e-17) place AA00557 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase (PF02518)","","","","","Rabin,R.S. and Stewart,V. Either of two functionally redundant sensor proteins, NarX andNarQ, is sufficient for nitrate regulation in Escherichia coliK-12 Proc. Natl. Acad. Sci. U.S.A. 89 (18), 8419-8423 (1992) PubMed: 1528845 Chiang,R.C., Cavicchioli,R. and Gunsalus,R.P. Identification and characterization of narQ, a second nitrate sensor for nitrate-dependent gene regulation in Escherichiacoli Mol. Microbiol. 6 (14), 1913-1923 (1992) PubMed: 1508040 ","","Thu Dec 12 16:22:06 2002","1","","","" "AA00558","382266","383288","1023","ATGCAGAATTTACAACCGTTCCATACCTTTTCTATTCCGGCGCAAGCCCAAAAACTGATTGAAATTACCTCCGTTCCTCAACTTAAACAGGTGTGGGACGAATTCCAGCGGGAAAATCTGCCAGTGCTTTTTTTAGGGCAAGGCAGCAATGTGTTGTTTGTGGAAGATTTTGCCGGCGCTGTGCTGATTAATCGTCTGCGTGGTATTGCGCATAAGGAAGACGACCGCTTTCATTATCTACATGTGAATGGCGGCGAAGTGTGGCATGATTTGGTGCAATGGAGTATCGCGCAAGGCATTTACGGCTTGGAAAATCTTGCCCTCATACCGGGCTGTGCCGGTTCCGCCCCGATTCAAAATATCGGTGCCTACGGCGTGGAATTTAAAGACGTGTGCGATTATGTAGAGGTGCTCGATCTCACGTCCGCAGAACAATTCCGTTTGAGCTGCGAAGAATGCGAATTCGGTTATCGGGAAAGCGTGTTTAAACACAAATATGCGCATGGTTATGTGGTCACGGCGGTCGGTTTAAAACTGGCGAAAGACTGGAAACCGGTGTTGAAATACGGCAACTTGGCAAATTTAGACAAAAGTGCGGTCAGTTCGGCGGACGTTTTTGCCGAGGTTTGTGCCGTACGCCAAAGCAAATTGCCCGATCCGAAACAGTTCGGCAATGCGGGTAGCTTCTTTAAGAATCCGGTGGTTTCCGCCCAACAATTTGCCCGCTTAAAAGAAGACTACCCCGCTATACCGCACTTCCCGCAAGCGGACGGCAGCGTCAAATTAGCCGCCGGTTGGCTTATCGATCAATGCGGCTTGAAAGGCTATCAAATCGGCGGCGCGGCAGTACATCAACAACAGGCGCTGGTGATTATTAACAAAGGCAACGCCACCGCGTCCGATGTGGTAGAATTGGCGCATCACATTTATCAATTAGTTGCCCTTCGTTTTGACGTTCGCTTACAGCCCGAAGTGCGTTTTATCGGCAAACAGGGCGAAGTGAATAGTCAACAAACCATCAGT","","","37755","MQNLQPFHTFSIPAQAQKLIEITSVPQLKQVWDEFQRENLPVLFLGQGSNVLFVEDFAGAVLINRLRGIAHKEDDRFHYLHVNGGEVWHDLVQWSIAQGIYGLENLALIPGCAGSAPIQNIGAYGVEFKDVCDYVEVLDLTSAEQFRLSCEECEFGYRESVFKHKYAHGYVVTAVGLKLAKDWKPVLKYGNLANLDKSAVSSADVFAEVCAVRQSKLPDPKQFGNAGSFFKNPVVSAQQFARLKEDYPAIPHFPQADGSVKLAAGWLIDQCGLKGYQIGGAAVHQQQALVIINKGNATASDVVELAHHIYQLVALRFDVRLQPEVRFIGKQGEVNSQQTIS","383290","","UDP-n-acetylenolpyruvoylglucosamine reductase","Cytoplasm","","
InterPro
IPR003170
Family
UDP-N-acetylenolpyruvoylglucosamine reductase
PTHR21071\"[19-341]TUDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE
TIGR00179\"[4-329]TmurB: UDP-N-acetylenolpyruvoylglucosamine r
InterPro
IPR006094
Domain
FAD linked oxidase, N-terminal
PF01565\"[16-149]TFAD_binding_4
InterPro
IPR011601
Domain
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal
PF02873\"[202-329]TMurB_C
noIPR
unintegrated
unintegrated
G3DSA:3.30.43.10\"[2-67]Tno description
G3DSA:3.30.465.10\"[68-217]Tno description
G3DSA:3.90.78.10\"[218-341]Tno description


","No hits to the COGs database.","Significant hit ( 1.4e-87) to 5/5 blocks of the IPB003170 family, which is described as \"UDP-N-acetylenolpyruvoylglucosamine reductase\". Interpro entry for IP:IPR003170. IPB003170A 44-53 0.016 IPB003170B 80-130 3.8e-33 IPB003170C 143-163 6e-07 IPB003170D 224-233 4.2e-05 IPB003170E 265-319 1.5e-34","Residues 200 to 340 match (7e-54) PD:PD004983 which is described as REDUCTASE CELL PROTEOME COMPLETE UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE OXIDOREDUCTASE WALL DIVISION NADP FAD ","","","","","","","","","","","","Thu Dec 12 16:24:18 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00558 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 202 to 329 (E-value = 7.4e-66) place AA00558 in the MurB_C family which is described as UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain (PF02873)","","","","","Pucci,M.J., Discotto,L.F. and Dougherty,T.J. Cloning and identification of the Escherichia coli murB DNA sequence, which encodes UDP-N-acetylenolpyruvoylglucosamine reductase J. Bacteriol. 174 (5), 1690-1693 (1992) Benson,T.E., Marquardt,J.L., Marquardt,A.C., Etzkorn,F.A. and Walsh,C.T. Overexpression, purification, and mechanistic study of UDP-N-acetylenolpyruvylglucosamine reductase Biochemistry 32 (8), 2024-2030 (1993) M:93192262 Benson,T.E., Walsh,C.T. and Hogle,J.M. The structure of the substrate-free form of MurB, an essentialenzyme for the synthesis of bacterial cell walls Structure 4 (1), 47-54 (1996) M:96419135 Benson,T.E., Walsh,C.T. and Hogle,J.M. X-ray crystal structures of the S229A mutant and wild-typeMurB in the presence of the substrateenolpyruvyl-UDP-N-acetylglucosamine at 1.8-A resolution Biochemistry 36 (4), 806-811 (1997) M:97172910 ","","Thu Dec 12 16:24:18 2002","1","","","" "AA00559","383307","383618","312","ATGAATTTTAATGAAATTTTAGCGACATTGCCTGCTATTGACCATTTAAGTGGTATCCATATTTTACATAACGGTACATTGGTTCATGAGATTCCTGCCGTTGCCGGGAAATTAGGTTCATTGCGGGTTTACAATGCGCTCGCCGTAAAATTTAACAGAAAATTAGACCGCACTTCTGCCCAAAAAGGTTTGCAATTATTCGCCGAGTACACGGAAGATGCACATAAACACCCCGGCAAACACCCGAACATTGATTTGTTGTTACGCGTCATCGAACAGGATTTGACCTATCAAATCAAACCGCTAACAGAA","","","11640","MNFNEILATLPAIDHLSGIHILHNGTLVHEIPAVAGKLGSLRVYNALAVKFNRKLDRTSAQKGLQLFAEYTEDAHKHPGKHPNIDLLLRVIEQDLTYQIKPLTE","383620","","conserved hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","Residues 1 to 92 match (3e-28) PD:PD354632 which is described as COMPLETE PROTEOME PLASMID PM1588 NMA0986 NMB0775 RSP0610 ","","","","","","","","","","","","Thu Dec 12 16:25:24 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00559 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00560","383806","384651","846","ATGGATAAAGAAACTCAAACAATGATGCTCGTTCCGCAAGGCAGTATAGAAGCTTATATTCGTGCGGCAAATGAATATCCAATGCTGACCGCCGAAGAAGAAAAGGAATTGGCAGAGCGTTTGTATTACAAAGAAGATATTGAAGCGGCGAAAAAATTAGTGTTGTCTCATTTGCGCTTTGTGATTCACGTCGCGCGCGGTTATTCCGGTTACGGCTTGCCGCAAGCGGATTTAATCCAGGAAGGTAACATCGGCTTAATGAAAGCGGTAAAACGCTTCAACCCGGAAGTAGGCGTGCGCTTGGTTTCTTTCGCTGTGCACTGGATCAAAGCGGAAATTCACGAATATGTGTTGCGCAACTGGCGTATTGTTAAAGTCGCCACCACCAAAGCGCAACGCAAATTGTTCTTCAACCTACGCAAAACTAAGCAACGCTTAGGCTGGTTCAACGAAAACGAAGTGGACATGGTCGCCAATGAACTCGGTGTATCGCCGCAAGATGTCATGGAAATGGAGTCACGCATGACCGGCGCCGATGTGGCATTCGACCTGCCCGGCGATGAGCATGACGAAGAAACCTATGCGCCGGCATTGTATTTGGAAGACAAAAGCTCCAACTTTGCCGCCGAATTGGAAAACGAAAACTACGAAGCACAAGCCACCGATCAGCTTGCCGTCGCGTTAGACAATCTTGATGCACGCAGCCAAGACATTATCAAAGCCCGCTGGTTAGATGAAACCAAAGCTACGTTGCAGGATTTGGCGGCGAAATACAACATTTCCGCCGAACGTGTTCGCCAGTTAGAAACCAATGCCTTGAAAAAACTCAAAAGTGCGGTGGTTTTC","","","32193","MDKETQTMMLVPQGSIEAYIRAANEYPMLTAEEEKELAERLYYKEDIEAAKKLVLSHLRFVIHVARGYSGYGLPQADLIQEGNIGLMKAVKRFNPEVGVRLVSFAVHWIKAEIHEYVLRNWRIVKVATTKAQRKLFFNLRKTKQRLGWFNENEVDMVANELGVSPQDVMEMESRMTGADVAFDLPGDEHDEETYAPALYLEDKSSNFAAELENENYEAQATDQLAVALDNLDARSQDIIKARWLDETKATLQDLAAKYNISAERVRQLETNALKKLKSAVVF","384653","","RNA polymerase sigma-32 factor","Cytoplasm","","
InterPro
IPR000943
Domain
RNA polymerase, Sigma-70 factor
PR00046\"[77-90]T\"[231-243]T\"[250-265]T\"[265-276]TSIGMA70FCT
PS00715\"[77-90]TSIGMA70_1
PS00716\"[250-276]TSIGMA70_2
InterPro
IPR007627
Domain
RNA polymerase sigma-70 region 2
PF04542\"[53-123]TSigma70_r2
InterPro
IPR007630
Domain
RNA polymerase sigma-70 region 4
PF04545\"[227-278]TSigma70_r4
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[213-278]Tno description
InterPro
IPR012759
Family
RNA polymerase sigma factor RpoH, proteobacteria
TIGR02392\"[14-282]TrpoH_proteo: alternative sigma factor RpoH
InterPro
IPR014284
Domain
RNA polymerase sigma-70
TIGR02937\"[48-280]Tsigma70-ECF: RNA polymerase sigma factor, s
noIPR
unintegrated
unintegrated
G3DSA:1.10.601.10\"[15-122]Tno description


","BeTs to 18 clades of COG0568COG name: DNA-directed RNA polymerase sigma subunits (sigma70/sigma32)Functional Class: KThe phylogenetic pattern of COG0568 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.5e-29) to 1/1 blocks of the IPB000943 family, which is described as \"Sigma-70 factor family\". Interpro entry for IP:IPR000943. IPB000943 66-117 2.3e-29","Residues 95 to 126 match (5e-12) PD:PD000270 which is described as FACTOR RNA POLYMERASE SIGMA TRANSCRIPTION DNA-DIRECTED REGULATION DNA-BINDING PROTEOME COMPLETE ","","","","","","","","","","","","Thu Dec 12 16:31:18 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00560 is paralogously related to AA02397 (9e-22).","","","","","","Residues 227 to 278 (E-value = 2.8e-14) place AA00560 in the Sigma70_r4 family which is described as Sigma-70, region 4 (PF04545)","","","","","Solis-Guzman G,Ramirez-Santos J,Souza V,Gomez-Eichelmann MC. Analysis of the regulatory region of the heat-shock generpoH of Escherichia coli strains isolated from non-humanhosts. FEMS Microbiol Lett. 2001 Dec 18;205(2):191-6. PMID: 11750801 Aramaki H, Hirata T, Hara C, Fujita M, Sagara Y. Transcription analysis of rpoH in Pseudomonas putida. FEMS Microbiol Lett. 2001 Dec 18;205(2):165-9. PMID: 11750797 Calendar,R., Erickson,J.W., Halling,C. and Nolte,A. Deletion and insertion mutations in the rpoH gene ofEscherichia coli that produce functional sigma 32 J. Bacteriol. 170 (8), 3479-3484 (1988) PubMed: 2841288 ","","Thu Jan 9 10:49:52 2003","1","","","" "AA00561","385356","384724","633","ATGACAACGGTATCTCAAAGACTCAAGAACGAATTCAAACAACTAGTAGATGGTGAAATCAGTATTAAAAATTTATTCACCGGACATGGTATATTTCATTCAGGAATAATGTTTGCACTTCATCAAAACGATAGCATTTTCTTGCGGGCTGAAGATGAGTTAGTCCCTTACTTAGAAAGTTTAGGTGCTGTAGCTTATTCAATTGATCCCAATAATACGAATAAACTGGCACTCCACCGTTACTATCAACTTCCTCATTCTATTCGTAAAAATAAGCCGTTATTTGAAAAAACCGTTAAATTGTCTATTCAACAGGCAAAATTTAAGAAAGTCGCTGAAGATTTGACAAAAAAAGAGCGAATTAAAGAATTGGCTAATTTTTCCATTAAGCATGAAAGATTGCTGGCTAAAATTAATATTTATACGGTAAGTGAATTTCAGAAGATCGGCGCAATTCACAGCTATGTTAGGTTAAAGAAACTGGGTGTTTCTGCCAACGTAGAATTGTTATGGACTTTATGCGCCGCATTAAAAAATAAGCATGCTTCGTTGCTTACGGAAAAGGAAAAATCGGCAATTTTGACTAAATTAAATGTTTTACTTGCAGCAAATGGTTTGCGGAAAGTAAAGGCC","","","23937","MTTVSQRLKNEFKQLVDGEISIKNLFTGHGIFHSGIMFALHQNDSIFLRAEDELVPYLESLGAVAYSIDPNNTNKLALHRYYQLPHSIRKNKPLFEKTVKLSIQQAKFKKVAEDLTKKERIKELANFSIKHERLLAKINIYTVSEFQKIGAIHSYVRLKKLGVSANVELLWTLCAALKNKHASLLTEKEKSAILTKLNVLLAANGLRKVKA","384726","","DNA transformation protein","Cytoplasm","","
InterPro
IPR007076
Domain
TfoX, N-terminal
PF04993\"[4-108]TTfoX_N
InterPro
IPR007077
Domain
TfoX, C-terminal
PF04994\"[117-197]TTfoX_C


","BeTs to 3 clades of COG3070COG name: Regulator of competence-specific genesFunctional Class: NThe phylogenetic pattern of COG3070 is --------------efgh-n-j----Number of proteins in this genome belonging to this COG is","","Residues 18 to 117 match (2e-13) PD:PD414846 which is described as PROTEOME ACTIVATOR COMPLETE COMPETENCE TFOX TRANSCRIPTION REGULATION INITIATION DNA TRANSFORMATION ","","","","","Mon Feb 17 07:21:12 2003","","","","","","","Thu Dec 12 16:35:23 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00561 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 117 to 197 (E-value = 3.1e-25) place AA00561 in the TfoX_C family which is described as TfoX C-terminal domain (PF04994)","","","","","Zulty,J.J. and Barcak,G.J.Identification of a DNA transformation gene required for com101A+expression and supertransformer phenotype in Haemophilus influenzaeProc. Natl. Acad. Sci. U.S.A. 92 (8), 3616-3620 (1995)PubMed: 7724607Macfadyen LP.Regulation of competence development in Haemophilus influenzae.J Theor Biol. 2000 Dec 7;207(3):349-59.PMID: 11082305Karudapuram S, Barcak GJ.The Haemophilus influenzae dprABC genes constitute a competence-inducible operon thatrequires the product of the tfoX (sxy) gene for transcriptional activation.J Bacteriol. 1997 Aug;179(15):4815-20.PMID: 9244270 ","","Mon Feb 17 07:21:12 2003","1","","","" "AA00562","385520","385398","123","GTGTTATTCTTTGACACCTTTGGTTCTAAAGAACATTTTTTCATTAAAATTTTCCAATTCCTCGATCAAGATCACAAATTTAACATTAAAATAACAATATTTTCTTCATATAAATTTAATTTA","","","5034","VLFFDTFGSKEHFFIKIFQFLDQDHKFNIKITIFSSYKFNL","385398","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:36:46 2004","Sun Feb 22 16:36:46 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00562 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:36:46 2004","","","","","","","","","","","","","1","","","" "AA00563","387828","386647","1182","GTGTCTAAAGAAAAATTTGAACGTACAAAACCGCACGTTAACGTGGGTACAATCGGCCACGTTGACCATGGTAAAACCACTTTAACAGCAGCTATCACTACCGTATTGGCAAAACACTACGGCGGTGCAGCACGTGCATTTGACCAAATCGATAATGCACCTGAAGAAAAAGCGCGTGGTATCACCATCAACACTTCACACGTTGAATATGACACCCCAACCCGTCACTATGCACACGTTGACTGCCCGGGACACGCCGACTATGTGAAAAACATGATTACCGGTGCGGCGCAAATGGACGGTGCTATCTTAGTAGTAGCAGCAACCGACGGTCCTATGCCACAAACTCGTGAGCACATCTTATTAGGTCGCCAAGTAGGTGTTCCTTACATCATCGTATTCTTAAACAAATGCGACATGGTAGATGACGAAGAGTTATTAGAATTAGTTGAAATGGAAGTTCGTGAACTTCTTTCTCAATATGACTTCCCGGGCGATGACACCCCAATCGTACGCGGTTCTGCATTAAAAGCGCTTGAAGGCGATGCCGCATGGGAAGAAAAAATCCTTGAATTAGCAAACCATTTAGATACTTACATCCCGGAACCTGAGCGTGCTATCGACCAACCGTTCCTTCTTCCAATTGAAGATGTGTTCTCTATCTCCGGTCGTGGTACCGTAGTAACGGGTCGTGTTGAGCGCGGTATCATCCGTACCGGTGATGAAGTTGAAATCGTGGGTATCAAACCGACTGCAAAAACCACCGTAACCGGTGTTGAAATGTTCCGTAAATTACTTGACGAAGGTCGTGCGGGTGAAAACATCGGTGCATTATTGCGTGGTACTAAACGTGAAGAAATCGAACGTGGTCAGGTATTGGCGAAACCGGGTTCAATCACCCCGCACACTGACTTCGAATCTGAAGTGTACGTATTGTCCAAAGAAGAAGGTGGTCGTCATACTCCATTCTTCAAAGGTTACCGTCCACAATTCTATTTCCGTACAACTGACGTAACCGGTACTATCGAGTTACCTGAAGGCGTGGAAATGGTTATGCCCGGTGATAACATCAAAATGACCGTATCCTTAATTCACCCAATTGCGATGGACCAAGGTTTACGTTTCGCTATCCGTGAAGGTGGCCGTACAGTGGGTGCCGGCGTGGTAGCTAAAATTATCAAA","","","43279","VSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKHYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAAWEEKILELANHLDTYIPEPERAIDQPFLLPIEDVFSISGRGTVVTGRVERGIIRTGDEVEIVGIKPTAKTTVTGVEMFRKLLDEGRAGENIGALLRGTKREEIERGQVLAKPGSITPHTDFESEVYVLSKEEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMTVSLIHPIAMDQGLRFAIREGGRTVGAGVVAKIIK","386649","","elongation factor Tu","Cytoplasm","","
InterPro
IPR000795
Domain
Protein synthesis factor, GTP-binding
PR00315\"[14-27]T\"[58-66]T\"[78-88]T\"[94-105]T\"[131-140]TELONGATNFCT
PF00009\"[10-204]TGTP_EFTU
PS00301\"[51-66]TEFACTOR_GTP
InterPro
IPR004160
Domain
Translation elongation factor EFTu/EF1A, C-terminal
PF03143\"[299-393]TGTP_EFTU_D3
InterPro
IPR004161
Domain
Translation elongation factor EFTu/EF1A, domain 2
PF03144\"[225-294]TGTP_EFTU_D2
InterPro
IPR004541
Family
Translation elongation factor EFTu/EF1A, bacterial and organelle
PTHR23115:SF31\"[2-328]TELONGATION FACTOR TU (EF-TU)
TIGR00485\"[1-394]TEF-Tu: translation elongation factor Tu
InterPro
IPR005225
Domain
Small GTP-binding protein domain
TIGR00231\"[10-185]Tsmall_GTP: small GTP-binding protein domain
noIPR
unintegrated
unintegrated
G3DSA:2.40.30.10\"[206-335]T\"[339-394]Tno description
G3DSA:3.40.50.300\"[3-205]Tno description
PTHR23115\"[2-328]TTRANSLATION FACTOR


","BeTs to 26 clades of COG0050COG name: GTPases - translation elongation factorsFunctional Class: J,EThe phylogenetic pattern of COG0050 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.3e-56) to 3/3 blocks of the IPB000795 family, which is described as \"GTP-binding elongation factor\". Interpro entry for IP:IPR000795. IPB000795A 14-29 8.8e-14 IPB000795B 80-111 8.2e-26 IPB000795C 115-139 2.4e-14Significant hit ( 2e-13) to 3/6 blocks of the IPB000640 family, which is described as \"Elongation factor G, C-terminus\". Interpro entry for IP:IPR000640. IPB000640A 12-37 1.7e-05 IPB000640B 50-72 0.13 IPB000640C 77-104 0.012Significant hit ( 1.1e-10) to 4/8 blocks of the IPB000178 family, which is described as \"Initiation factor 2\". Interpro entry for IP:IPR000178. IPB000178A 11-49 8.2 IPB000178B 77-109 0.0018 IPB000178C 110-149 0.18 IPB000178E 225-277 4.9","Residues 56 to 89 match (3e-13) PD:PD173400 which is described as FACTOR ELONGATION GTP-BINDING BIOSYNTHESIS PROTEOME COMPLETE TU EF-TU 1-ALPHA EF-1-ALPHA ","","","","","","","","","","","","Thu Dec 12 16:43:46 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00563 is paralogously related to AA00931 (0.0), AA00892 (3e-22), AA02344 (3e-17), AA01922 (6e-14), AA03003 (8e-14), AA00564 (4e-10) and AA01852 (1e-07).","","","","","","Residues 299 to 393 (E-value = 6.2e-62) place AA00563 in the GTP_EFTU_D3 family which is described as Elongation factor Tu C-terminal domain (PF03143)","","","","","","","","1","","","" "AA00564","389994","387895","2100","ATGGCTCGTACAACCCCTATTGAAAGATATCGTAACATTGGTATCAGTGCGCATATTGATGCGGGTAAAACTACTACTACTGAGCGTATCTTGTTCTATACCGGTGTAAGTCACAAAATCGGTGAAGTACACGATGGTGCCGCAACCATGGACTGGATGGAACAGGAACAAGAACGTGGGATTACCATCACCTCTGCGGCAACCACCGCATTCTGGTCAGGTATGTCACAACAATTCCCACAACACCGTATTAACGTTATCGACACCCCGGGACACGTTGACTTTACTGTTGAAGTAGAACGTTCTATGCGTGTTCTTGATGGTGCGGTGATGGTTTACTGTGCGGTTGGTGGTGTTCAACCACAATCCGAAACCGTATGGCGTCAAGCAAACAAATATGAAGTACCACGTATTGCATTCGTTAATAAAATGGACCGCACCGGCGCAAACTTCCTACGCGTGGTTGATCAATTAAAAACCCGTTTAGGTGCCAATGCCGTTCCGCTTCAACTACCAATCGGTTCAGAAGAAAACTTCACCGGTGTTGTTGATTTGATCAAAATGAAAGCGATCAACTGGAACGAAGCTGACCAGGGTATGACGTTTACTTATGAAGATGTTCCTGCTGATATGCACGCCGCTTGCGAAGAATGGCGCCAAAACTTAATTGAAGCGGCAGCAGAAGCTTCAGAAGAATTAATGGAAAAATACCTCGGTGGTGAAGAATTAACTGAAGAAGAAATCAAAGCCGGTCTTCGTCAACGCGTATTAGCAAACGAAATCATTTTGGTAACCTGTGGTTCTGCGTTCAAAAACAAAGGTGTTCAAGCAATGCTTGATGCTGTTGTTGAATACTTGCCGGCGCCAACCGATATTCCTGCGATTAAAGGTATTAACCCGGATGAAACCGAAGGTGAGCGCCATGCAAGCGATGAAGAGCCGTTCTCCTCATTGGCATTCAAAATCGCAACTGATCCATTTGTGGGTAACTTAACCTTCTTCCGTGTGTACTCTGGCGTAATCAATTCCGGAGATACCGTATTGAACTCCGTACGTCAAAAACGTGAACGCTTTGGTCGTATCGTTCAAATGCATGCGAACAAACGTGAAGAAATCAAAGAAGTTCGCGCAGGTGATATTGCGGCGGCAATCGGCTTAAAAGACGTCACCACCGGTGATACATTATGTGCGATTGAAGCGCCAATCATCCTTGAACGTATGGAATTCCCTGAGCCGGTAATCTCTGTTGCGGTAGAACCAAAAACCAAAGCAGACCAAGAAAAAATGGGTATTGCATTAGGCCGTTTAGCACAAGAAGACCCTTCATTCCGAGTGCACACTGATGAAGAATCCGGTGAAACCATTATCTCTGGTATGGGTGAATTACACTTGGATATCATCGTTGACCGTATGAAACGTGAATTCAAAGTGGAAGCTAACATCGGTAAACCACAAGTATCTTACCGTGAAACTATCCGTACTCGCGTTAACGATATGGAAGGTAAACACGCAAAACAATCCGGCGGTCGTGGTCAATACGGTCATGTGGTTATCGACTTGTATCCATTAGAACCGGAAGGTCCGGGTTACGAGTTTGTTAACGAAATTAAAGGTGGTGTAATCCCTGGTGAATATATCCCGGCCGTTGACAAAGGTATTCAAGAACAACTTAAATCCGGTCCGTTAGCAGGTTATCCGGTGGTTGATATCGGTGTTCGTTTACACTTCGGTTCATACCATGATGTGGACTCCTCCGAATTGGCGTTTAAATTAGCGGCATCTTTAGCATTTAAAGCAGCATTCGCTAAAGCAAACCCTGTTCTGCTTGAGCCAATCATGAAAGTTGAAGTAGAAACCCCACCTGAGTACGTAGGTGACGTAATCGGTGACTTAAGCCGTCGTCGTGCAATGGTGAACGGTCAAGAAGCGAACGAATTCGTTGTTAAAATCGATGCAGAAGTTCCGCTTTCAGAAATGTTCGGTTACGCAACTGACTTACGTTCCCAGACTCAAGGTCGTGCTTCCTACTCAATGGAACCATTGAAATATGCTGAAGCACCGAAAAACGTAGCTGAAGCCGTAATTGAAGCTCGTAAAAAA","","","77317","MARTTPIERYRNIGISAHIDAGKTTTTERILFYTGVSHKIGEVHDGAATMDWMEQEQERGITITSAATTAFWSGMSQQFPQHRINVIDTPGHVDFTVEVERSMRVLDGAVMVYCAVGGVQPQSETVWRQANKYEVPRIAFVNKMDRTGANFLRVVDQLKTRLGANAVPLQLPIGSEENFTGVVDLIKMKAINWNEADQGMTFTYEDVPADMHAACEEWRQNLIEAAAEASEELMEKYLGGEELTEEEIKAGLRQRVLANEIILVTCGSAFKNKGVQAMLDAVVEYLPAPTDIPAIKGINPDETEGERHASDEEPFSSLAFKIATDPFVGNLTFFRVYSGVINSGDTVLNSVRQKRERFGRIVQMHANKREEIKEVRAGDIAAAIGLKDVTTGDTLCAIEAPIILERMEFPEPVISVAVEPKTKADQEKMGIALGRLAQEDPSFRVHTDEESGETIISGMGELHLDIIVDRMKREFKVEANIGKPQVSYRETIRTRVNDMEGKHAKQSGGRGQYGHVVIDLYPLEPEGPGYEFVNEIKGGVIPGEYIPAVDKGIQEQLKSGPLAGYPVVDIGVRLHFGSYHDVDSSELAFKLAASLAFKAAFAKANPVLLEPIMKVEVETPPEYVGDVIGDLSRRRAMVNGQEANEFVVKIDAEVPLSEMFGYATDLRSQTQGRASYSMEPLKYAEAPKNVAEAVIEARKK","387897","","elongation factor G","Cytoplasm","","
InterPro
IPR000640
Domain
Translation elongation factor EFG/EF2, C-terminal
G3DSA:3.30.70.240\"[610-698]Tno description
PF00679\"[607-694]TEFG_C
InterPro
IPR000795
Domain
Protein synthesis factor, GTP-binding
PR00315\"[12-25]T\"[58-66]T\"[85-95]T\"[101-112]T\"[137-146]TELONGATNFCT
PF00009\"[8-290]TGTP_EFTU
PS00301\"[51-66]TEFACTOR_GTP
InterPro
IPR004161
Domain
Translation elongation factor EFTu/EF1A, domain 2
PF03144\"[329-396]TGTP_EFTU_D2
InterPro
IPR004540
Family
Translation elongation factor EFG/EF2
TIGR00484\"[1-700]TEF-G: translation elongation factor G
InterPro
IPR005225
Domain
Small GTP-binding protein domain
TIGR00231\"[8-188]Tsmall_GTP: small GTP-binding protein domain
InterPro
IPR005517
Domain
Translation elongation factor EFG/EF2, domain IV
PF03764\"[484-605]TEFG_IV
InterPro
IPR014721
Domain
Ribosomal protein S5 domain 2-type fold
G3DSA:3.30.230.10\"[489-609]Tno description
noIPR
unintegrated
unintegrated
G3DSA:2.40.30.10\"[309-406]Tno description
G3DSA:3.30.70.870\"[408-473]Tno description
G3DSA:3.40.50.300\"[9-239]Tno description
PTHR23115\"[1-164]T\"[248-289]T\"[308-429]TTRANSLATION FACTOR
PTHR23115:SF13\"[1-164]T\"[248-289]T\"[308-429]TTRANSLATION ELONGATION FACTOR G


","BeTs to 26 clades of COG0480COG name: Translation elongation and release factors (GTPases)Functional Class: JThe phylogenetic pattern of COG0480 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit (8.6e-116) to 6/6 blocks of the IPB000640 family, which is described as \"Elongation factor G, C-terminus\". Interpro entry for IP:IPR000640. IPB000640A 10-35 8.3e-20 IPB000640B 50-72 1.9e-17 IPB000640C 84-111 1.1e-22 IPB000640D 118-146 1.1e-22 IPB000640E 278-289 0.0035 IPB000640F 604-638 1.5e-23Significant hit ( 4.3e-29) to 3/3 blocks of the IPB000795 family, which is described as \"GTP-binding elongation factor\". Interpro entry for IP:IPR000795. IPB000795A 12-27 5.7e-07 IPB000795B 87-118 1.8e-15 IPB000795C 459-483 0.0017Significant hit ( 1.6e-13) to 4/8 blocks of the IPB000178 family, which is described as \"Initiation factor 2\". Interpro entry for IP:IPR000178. IPB000178A 9-47 21 IPB000178B 84-116 9.7e-05 IPB000178C 117-156 2e-05 IPB000178E 329-381 3e+02","Residues 11 to 99 match (5e-07) PD:PD249398 which is described as FACTOR ELONGATION G PROTEOME COMPLETE GTP-BINDING LIKE ","","","","","","","","","","","","Thu Dec 12 16:50:12 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00564 is paralogously related to AA01852 (1e-38), AA02344 (8e-24), AA03003 (1e-18), AA00931 (8e-10), AA00563 (8e-10) and AA01922 (1e-06).","","","","","","Residues 607 to 694 (E-value = 4.6e-44) place AA00564 in the EFG_C family which is described as Elongation factor G C-terminus (PF00679)","","","","","engel,J.M., Archer,R.H. and Lindahl,L. The nucleotide sequence of the Escherichia coli fus gene,coding for elongation factor G Nucleic Acids Res. 12 (4), 2181-2192 (1984) PubMed: 6322136 Evers S, Di Padova K, Meyer M, Langen H, Fountoulakis M,Keck W, Gray CP. Mechanism-related changes in the gene transcription andprotein synthesis patterns of Haemophilus influenzae aftertreatment with transcriptional and translational inhibitors. Proteomics. 2001 Apr;1(4):522-44. PMID: 11681206 ","","Thu Dec 12 16:50:12 2002","1","","","" "AA00565","390579","390112","468","ATGCCACGTCGTCGTAGTATTGAACAACGCAAGATTTTACCGGATCCAAAGTTCGGTTCAGAATTACTTGCTAAATTTATCAATGTCATCATGGTAGATGGTAAAAAATCTATCGCAGAATCTATCGTTTATAACGCGTTAGACACTTTAGCGCAACGTACCGGTAAAGAAGCTTTAGAAGCTTTTGAAGCGGCATTAGAAAACGTGCGTCCAACCGTAGAAGTGAAATCCCGTCGTGTCGGTGGTTCTACTTACCAAGTACCGGTTGAAGTTCGCCCGGTTCGTCGTAACGCATTAGGTATGCGTTGGATCGTTGAAGCAGCTCGCAAACGCGGTGATAAATCCATGGCTTTACGTTTAGCTAACGAATTGTCTGACGCTTCCGAAAACAAAGGCGCGGCAGTTAAGAAACGTGAAGACGTTCACCGTATGGCTGAAGCTAACAAAGCGTTTGCTCACTACCGTTGG","","","20196","MPRRRSIEQRKILPDPKFGSELLAKFINVIMVDGKKSIAESIVYNALDTLAQRTGKEALEAFEAALENVRPTVEVKSRRVGGSTYQVPVEVRPVRRNALGMRWIVEAARKRGDKSMALRLANELSDASENKGAAVKKREDVHRMAEANKAFAHYRW","390114","","30S ribosomal protein S7","Cytoplasm","","
InterPro
IPR000235
Family
Ribosomal protein S7
PD000817\"[27-142]TRS7_PASMU_Q9CL85;
G3DSA:1.10.455.10\"[6-156]Tno description
PIRSF002122\"[15-156]TRibosomal protein S7/S5
PTHR11205\"[1-156]TRIBOSOMAL PROTEIN S7
PF00177\"[1-149]TRibosomal_S7
PS00052\"[20-46]TRIBOSOMAL_S7
InterPro
IPR005717
Family
Ribosomal protein S7, bacterial and organelle form
TIGR01029\"[3-156]TrpsG_bact: ribosomal protein S7


","No hits to the COGs database.","Significant hit ( 1.8e-49) to 2/2 blocks of the IPB000235 family, which is described as \"Ribosomal protein S7\". Interpro entry for IP:IPR000235. IPB000235A 53-104 5.7e-32 IPB000235B 123-149 2.6e-16","Residues 27 to 143 match (4e-43) PD:PD000817 which is described as RIBOSOMAL S7 30S RRNA-BINDING CHLOROPLAST PROTEOME COMPLETE S7P 40S S5 ","","","","","","","","","","","","Thu Dec 12 16:51:46 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00565 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 149 (E-value = 3.5e-89) place AA00565 in the Ribosomal_S7 family which is described as Ribosomal protein S7p/S5e (PF00177)","","","","","Reinbolt,J., Tritsch,D. and Wittmann-Liebold,B. The primary structure of ribosomal protein S7 from E. colistrains K and B Biochimie 61 (4), 501-522 (1979) PubMed: 385062 Arnold,R.J. and Reilly,J.P. Observation of Escherichia coli ribosomal proteins and theirposttranslational modifications by mass spectrometry Anal. Biochem. 269 (1), 105-112 (1999) PubMed: 10094780 ","","Thu Dec 12 16:51:46 2002","1","","","" "AA00566","391070","390735","336","GTGAAAAAGGTTGTAAAAAGTAACGTTCCTGCATTAGAGGCTTGCCCGCAGAAACGTGGTGTATGCACCCGTGTGTACACAACTACACCTAAAAAACCGAACTCAGCATTACGTAAAGTATGCCGTATTCGTTTAACCAATGGTTTCGAAGTAACCTCATACATCGGCGGTGAAGGTCACAACCTTCAAGAGCACAGTGTTGTGCTTATCCGTGGTGGTCGTGTTAAAGACTTACCGGGTGTGCGTTATCACACCGTACGCGGCGCATTAGACTGCGCAGGCGTGAAAGATCGTAAACAAGGTCGTTCTAAATACGGCGTTAAACGTCCTAAAGCT","","","13733","VKKVVKSNVPALEACPQKRGVCTRVYTTTPKKPNSALRKVCRIRLTNGFEVTSYIGGEGHNLQEHSVVLIRGGRVKDLPGVRYHTVRGALDCAGVKDRKQGRSKYGVKRPKA","390737","","30S ribosomal protein S12 (streptomycin resistance protein)","Cytoplasm, Extracellular","","
InterPro
IPR005679
Family
Ribosomal protein S12, bacterial and chloroplast form
PR01034\"[15-30]T\"[30-45]T\"[46-65]T\"[65-82]T\"[82-98]T\"[98-110]TRIBOSOMALS12
PTHR11652:SF1\"[6-111]T30S RIBOSOMAL PROTEIN S12
TIGR00981\"[1-112]TrpsL_bact: ribosomal protein S12
InterPro
IPR006032
Family
Ribosomal protein S12/S23
PTHR11652\"[6-111]T30S RIBOSOMAL PROTEIN S12 FAMILY MEMBER
PF00164\"[2-111]TRibosomal_S12
PS00055\"[31-38]TRIBOSOMAL_S12
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[1-111]Tno description


","BeTs to 26 clades of COG0048COG name: Ribosomal protein S12Functional Class: JThe phylogenetic pattern of COG0048 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.3e-28) to 1/1 blocks of the IPB000230 family, which is described as \"Ribosomal protein S12\". Interpro entry for IP:IPR000230. IPB000230 53-88 1.2e-28","Residues 10 to 109 match (1e-46) PD:PD000576 which is described as RIBOSOMAL S12 30S COMPLETE PROTEOME CHLOROPLAST MITOCHONDRION MITOCHONDRIAL 40S S12P ","","","","","","","","","","","","Thu Dec 12 16:58:10 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00566 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 111 (E-value = 1.1e-64) place AA00566 in the Ribosomal_S12 family which is described as Ribosomal protein S12 (PF00164)","","","","","Funatsu,G., Yaguchi,M. and Wittmann-Liebold,B. Primary stucture of protein S12 from the small Escherichiacoli ribosomal subunit FEBS Lett. 73 (1), 12-17 (1977) PubMed: 320034 Kowalak,J.A. and Walsh,K.A. Beta-methylthio-aspartic acid: identification of a novel posttranslational modification in ribosomal protein S12 fromEscherichia coli Protein Sci. 5 (8), 1625-1632 (1996) PubMed: 8844851 Arnold,R.J. and Reilly,J.P. Observation of Escherichia coli ribosomal proteins and theirposttranslational modifications by mass spectrometry Anal. Biochem. 269 (1), 105-112 (1999) PubMed: 10094780 ","","Thu Dec 12 16:58:10 2002","1","","","" "AA00568","391097","391336","240","TTGTTGCCATTAAAAAAACTCCAGTTTAATAAATTCATTAAAAAATGTTGTTTTACAAATCTGTCCATACAAGAACAGACCGCAGATTTTAATCTTCAAACCGCAGGCTGTCAACTTATTATCACTTCCTGCGCGTGTTGCTTGCGGCATGTAAAAACATTTCTGGAAACGACCGCACTTTCCCTCACAACAAAGCCGACAATATTGTCGACTTTTGTTTCTTTGACGAGGTTAACCTTG","","","8952","LLPLKKLQFNKFIKKCCFTNLSIQEQTADFNLQTAGCQLIITSCACCLRHVKTFLETTALSLTTKPTILSTFVSLTRLTL","391336","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:38:13 2004","Sun Feb 22 16:38:13 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paraloogus sequences are found to this sequence.AA00568 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:38:13 2004","","","","","","","","","","","","","1","","","" "AA00569","391642","391331","312","TTGATGATGAATTGCTTGTCCAACAGCGCAAAATTACGTGCCTTTGAATTAGCGGAACAAATTAAAGAAAAATTGGCATTCTTATTTGCCAAACACATGAACGACATTATCAGCGGCGAATTCTCCCGCGTGATGATAGAAGACTGGGCGAAGGGAGATGCCAACTTATTGAAATGGCGTGAAGAAACCGGCAAAACCGCCTTTGAAAACGCACCAAAATACGATGGCAAAATCAGCGAGCAGGAGTATTTCGATAACGGTGAGTTAATGGTCGCGATGGTGAAAGACATGAAACGTATTTCCTTACAAGGT","","","11940","LMMNCLSNSAKLRAFELAEQIKEKLAFLFAKHMNDIISGEFSRVMIEDWAKGDANLLKWREETGKTAFENAPKYDGKISEQEYFDNGELMVAMVKDMKRISLQG","391333","","ketol-acid reductoisomerase","Cytoplasm","","
InterPro
IPR000506
Domain
Acetohydroxy acid isomeroreductase C-terminal
PF01450\"[1-95]TIlvC
noIPR
unintegrated
unintegrated
PTHR21371\"[1-99]TFAMILY NOT NAMED
PTHR21371:SF2\"[1-99]TSUBFAMILY NOT NAMED


","BeTs to 3 clades of COG0059COG name: Ketol-acid reductoisomeraseFunctional Class: E,HThe phylogenetic pattern of COG0059 is a-m-k-yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Fri Dec 13 09:24:34 2002","","Tue May 24 11:19:33 2005","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00569 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Tue May 24 11:19:33 2005","","","","","","","","","","Wernegreen JJ, Richardson AO, Moran NA.Parallel acceleration of evolutionary rates in symbiont genes underlying host nutrition.Mol Phylogenet Evol. 2001 Jun;19(3):479-85.PMID: 11399154 Opel ML, Hatfield GW.DNA supercoiling-dependent transcriptional coupling between the divergently transcribed promoters of the ilvYC operon of Escherichia coli is proportional to promoter strengths and transcript lengths.Mol Microbiol. 2001 Jan;39(1):191-8.PMID: 11123701 Garault P, Letort C, Juillard V, Monnet V.Branched-chain amino acid biosynthesis is essential for optimal growth of Streptococcus hermophilus in milk.Appl Environ Microbiol. 2000 Dec;66(12):5128-33.PMID: 11097879 Wek,R.C. and Hatfield,G.W.Nucleotide sequence and in vivo expression of the ilvY and ilvCgenes in Escherichia coli K12. Transcription from divergentoverlapping promotersJ. Biol. Chem. 261 (5), 2441-2450 (1986)PubMed: 3003115","","Fri Dec 13 09:24:34 2002","1","","","" "AA00570","391845","391753","93","GTGCGGTCAGTTTTAAAATTATTTATTCAAATGAAAAATACACAAAAATTTAACCGCACTTTTTCAAATTCAAAGAGCGAATCTATCCCCGTG","","","3610","VRSVLKLFIQMKNTQKFNRTFSNSKSESIPV","391753","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:39:30 2004","Sun Feb 22 16:39:30 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paraloogus sequences are found to this sequence.AA00570 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:39:30 2004","","","","","","","","","","","","","1","","","" "AA00573","392105","393355","1251","ATGAACTTTAACGATCTCAAAATCTTCACAACCTTCACTCACCCCAAAACTTTGCCAAAACCGCCGGCGCAGTATCATAATATGCCGTCCTCAACGTTGTCCCGCCAAATTCAAGTGAAGAAGAACCAGGGTATGGCACGAGGGCATTGTGTCTATGATGGCGCCGGGCTGCGGGTTGGCGTTGTTGCCGGATGTGGTGATGAAAAACAGTCCATTGAACAATCAGATTTCCACGTTGCAATTAGATGTGCCTATTGCGCCTTTCGAATTAGGCGTGTGCGCCTTAAAACCTGCGTTGGAGCGCCCTTTAGTGCGTGCATTTTGGGATTTGTTGGAGTAAAGTGCGGTCATTATCTAAGGAGTTTTTTCACCATGTTAAAAGGCATCGCATTTTCATTATTTGCCTCCCTACTGTTCGGCTATATGTACTATTTTTCCACACTTCTGTTGCCTTTGAGCGGAACGGATATTTTCGGCTATCGCATTGTGTTCACCCTACCTTTCGTGGCGGCGGCAGTGGTGCTGTTTAAACAGCAAGCGGCACTTGTCGCCCATTTAAAACGCATTCAAAAAAAACCGCACTTTGCGCTGGCGTTTGTGTTTACCGGCGCGCTGATAGGCTTCCAAATGTGGTTGTTTCTGTGGGCACCGAATAACGGCAGCTCGCTCAGTGTTTCTTTCGGCTATTTATTGCTGCCCTTGGTGATGGTGGCAGCAGCGCGTCTTATTTTTAAAGAACGCATTTCGCGCATTAAATTTCTGGCGGTGGTGATTGCCGCCGTGGGTGTGCTGTCGAATATTGTGCTAAAAGGAGAAATTTCTTGGGAAGCCTCGGTGATTTGCGTGGGGTACACCACCTATTTTGTGGTTCGCCGCATCCTGAAAATGACCGATCTGGCGGCATTCTTCCTGGAAATGCTGACCTTATTGCCGTTTTGTGTTTATTTCTCCTGGCAGGTGGATATTGCCCAAGTGCAGCAAAGCAACCCGAATATTTTAACCTTATTGTTGATCCTCGGCTTAATCAGTGGCACTGCGCTCAATTCCTATATTCTTGCCAGCAACCATTTGCCGATGAACCTGCTGGGCTTGTTGGGCTATGTAGAACCTTGCCTGATGGTAGGAATTTCGTTGCTCATCGGCGAAGAAATCGATGCGCAGAGTTACCCGTTGTTTATTTGTTTGGTGATCGCCATGCTATTAATCATCGCCGACGGCGTTTGGCGCACCAAACATAGCCCGACCCGATTA","","","46289","MNFNDLKIFTTFTHPKTLPKPPAQYHNMPSSTLSRQIQVKKNQGMARGHCVYDGAGLRVGVVAGCGDEKQSIEQSDFHVAIRCAYCAFRIRRVRLKTCVGAPFSACILGFVGVKCGHYLRSFFTMLKGIAFSLFASLLFGYMYYFSTLLLPLSGTDIFGYRIVFTLPFVAAAVVLFKQQAALVAHLKRIQKKPHFALAFVFTGALIGFQMWLFLWAPNNGSSLSVSFGYLLLPLVMVAAARLIFKERISRIKFLAVVIAAVGVLSNIVLKGEISWEASVICVGYTTYFVVRRILKMTDLAAFFLEMLTLLPFCVYFSWQVDIAQVQQSNPNILTLLLILGLISGTALNSYILASNHLPMNLLGLLGYVEPCLMVGISLLIGEEIDAQSYPLFICLVIAMLLIIADGVWRTKHSPTRL","393357","","chloramphenicol-sensitive protein RarD","Inner membrane, Cytoplasm","","
InterPro
IPR004626
Family
RarD protein
TIGR00688\"[126-381]TrarD: RarD protein
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[233-409]Tno description
noIPR
unintegrated
unintegrated
tmhmm\"[129-147]?\"[157-176]?\"[197-217]?\"[223-243]?\"[248-266]?\"[272-290]?\"[300-318]?\"[332-352]?\"[361-381]?\"[391-409]?transmembrane_regions


","BeTs to 5 clades of COG2962COG name: Predicted permeasesFunctional Class: RThe phylogenetic pattern of COG2962 is ------------b-efgh---j----Number of proteins in this genome belonging to this COG is","","Residues 265 to 409 match (3e-38) PD:PD012760 which is described as PROTEOME COMPLETE HI0680 HI0223 PM1281 ","","","","","Sun Feb 16 16:37:23 2003","","","","","","","Fri Dec 13 10:45:11 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00573 is paralogously related to AA02980 (6e-04).","","","","","","","","","","","Zhao,G.S., Xia,T.H., Fischer,R.S. and Jensen,R.A.Cyclohexadienyl dehydratase from Pseudomonas aeruginosa. Molecularcloning of the gene and characterization of the gene productJ. Biol. Chem. 267 (4), 2487-2493 (1992)PubMed: 1733946","","Sun Feb 16 16:37:23 2003","1","","","" "AA00574","392253","392441","189","GTGTCTATGATGGCGCCGGGCTGCGGGTTGGCGTTGTTGCCGGATGTGGTGATGAAAAACAGTCCATTGAACAATCAGATTTCCACGTTGCAATTAGATGTGCCTATTGCGCCTTTCGAATTAGGCGTGTGCGCCTTAAAACCTGCGTTGGAGCGCCCTTTAGTGCGTGCATTTTGGGATTTGTTGGAG","4.40","-2.11","6800","VSMMAPGCGLALLPDVVMKNSPLNNQISTLQLDVPIAPFELGVCALKPALERPLVRAFWDLLE","","","regulatory protein","Cytoplasm, Periplasm","Nearest neighbor is 15603148 IlvY [Pasteurella multocida]: residues 3-63 are 60% similar to this protein.AA00574 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus ducreyi gene.AA00574 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus influenzae Rd gene.","No hits reported.","No hits to the COGs database.","","Residues 3 to 62 match (6e-15) PD:PD032660 which is described as COMPLETE ACTIVATOR PROTEOME REGULATION DNA-BINDING ILVY TRANSCRIPTION TRANSCRIPTIONAL AMINO ACID ","Fri Feb 27 09:01:21 2004","Sat Feb 28 16:47:58 2004","Sat Feb 28 16:47:58 2004","Sat Feb 28 16:47:58 2004","Fri Feb 27 09:01:21 2004","Fri Feb 27 09:01:21 2004","Fri Feb 27 09:01:21 2004","Fri Feb 27 09:01:21 2004","Fri Feb 27 09:01:21 2004","Fri Feb 27 09:01:21 2004","Fri Feb 27 09:01:21 2004","Fri Feb 27 09:01:21 2004","Fri Feb 27 09:01:21 2004","Fri Feb 27 09:01:21 2004","Fri Feb 27 09:01:21 2004","Fri Feb 27 09:01:21 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00574 has no significant similarity (blastp p-value < 1e-03) to any other gene in this genome.AA00574 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Fri Feb 27 09:01:21 2004","Fri Feb 27 09:01:21 2004","No hits to the PDB database.","","","No significant hits to the Pfam 7.7 database.","Fri Feb 27 09:01:21 2004","","","","Opel ML, Hatfield GW.DNA supercoiling-dependent transcriptional coupling between the divergently transcribed promoters of the ilvYC operon of Escherichia coli is proportional to promoter strengths and transcript lengths.Mol Microbiol. 2001 Jan;39(1):191-8.PMID: 11123701Rhee KY, Opel M, Ito E, Hung S, Arfin SM, Hatfield GW.Transcriptional coupling between the divergent promoters of a prototypic LysR-type regulatory system, the ilvYC operon of Escherichia coli.Proc Natl Acad Sci U S A. 1999 Dec 7;96(25):14294-9.PMID: 10588699Wek,R.C. and Hatfield,G.W.Nucleotide sequence and in vivo expression of the ilvY and ilvCgenes in Escherichia coli K12. Transcription from divergentoverlapping promotersJ. Biol. Chem. 261 (5), 2441-2450 (1986)PubMed: 3003115","","Fri Feb 27 09:01:59 2004","1","Fri Feb 27 09:01:21 2004","","" "AA00575","394153","393356","798","ATGTTATACGCCGTTTGGGGCAACCCCATCGTTCAAAGCAAATCACCGCAAATTCACCGCATTTTCGCCGAACAAACCACACAAGACGTGCAATATGACGCCATGTTGGGCGATGAACAGGATTTTGAGCGACAATTGCTGGCGTTTTTTGCCAAAGGTGCGGCGGGCTGTAATATCACCTCACCTTTCAAAGAACGGGCATTCAAGCTGGCACAGGCGCACAGTGAACGCTGTTTATTGGCAGAAGCCTGTAATACGCTGAAAAAACGGGATGACGGCAGCCTTTACGCGGACAACACCGACGGCGCCGGTTTAGTGACAGATTTACAGCGGTTACATTGGTTCAAACCGAATCAAACCTTGCTGATTTTAGGCGCTGGTGGCGCCACCAAAGGCGTATTGTTGCCTTTACTACAGGCGCAGCAAAACATTGTGATTGCCAACCGCACGCTATCTAAAGCACAGCAACTGGCGGACAAATTCGCGCCTTACGGTAATGTTCGGGCGGTTGCGCTGGATAAGATTCCCGCACAATCCTTTGATGTGGTGATAAATGCGACTTCATCAGGCTTACACGGCGGCACGGTACAAATTGATGACGCCATTCTACGGATGGCGAAAGCGGTTTACGATATGCAATACGATCGACAACAAGACACACCGTTTTTGGCGCGTTGCCGTGCGTTAGGCGTGCAAAACCGATGTGACGGCTTCGGAATGTTATTGGCGCAAGCAGCGCATTCCTTCTATTTATGGCTCGGCGTGATGCCGAACATCGAACCGCTGTTTGAGGCGTTA","","","29276","MLYAVWGNPIVQSKSPQIHRIFAEQTTQDVQYDAMLGDEQDFERQLLAFFAKGAAGCNITSPFKERAFKLAQAHSERCLLAEACNTLKKRDDGSLYADNTDGAGLVTDLQRLHWFKPNQTLLILGAGGATKGVLLPLLQAQQNIVIANRTLSKAQQLADKFAPYGNVRAVALDKIPAQSFDVVINATSSGLHGGTVQIDDAILRMAKAVYDMQYDRQQDTPFLARCRALGVQNRCDGFGMLLAQAAHSFYLWLGVMPNIEPLFEAL","393358","","shikimate 5-dehydrogenase","Periplasm, Cytoplasm","","
InterPro
IPR006151
Domain
Shikimate/quinate 5-dehydrogenase
PF01488\"[105-223]TShikimate_DH
InterPro
IPR011342
Domain
Quinate/Shikimate 5-dehydrogenase
TIGR00507\"[1-266]TaroE: shikimate 5-dehydrogenase
InterPro
IPR013708
Domain
Shikimate dehydrogenase substrate binding, N-terminal
PF08501\"[5-87]TShikimate_dh_N
noIPR
unintegrated
unintegrated
G3DSA:3.40.192.10\"[2-98]Tno description
G3DSA:3.40.50.720\"[101-244]Tno description
PTHR21089\"[132-266]TSHIKIMATE DEHYDROGENASE


","BeTs to 22 clades of COG0169COG name: Shikimate 5-dehydrogenaseFunctional Class: EThe phylogenetic pattern of COG0169 is aompkzyqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 3.4e-45) to 6/6 blocks of the IPB002907 family, which is described as \"Shikimate / quinate 5-dehydrogenase\". Interpro entry for IP:IPR002907. IPB002907A 5-32 1e-08 IPB002907B 56-87 3.3e-13 IPB002907C 95-104 0.0047 IPB002907D 122-131 0.0056 IPB002907E 178-191 0.003 IPB002907F 237-252 9.8e-06","Residues 160 to 266 match (1e-10) PD:PD268078 which is described as BIOSYNTHESIS 5-DEHYDROGENASE NADP AROMATIC SHIKIMATE AMINO ACID OXIDOREDUCTASE PROTEOME COMPLETE ","","","","","","","","","","","","Fri Dec 13 10:57:28 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00575 is paralogously related to AA01772 (4e-16) and AA01879 (1e-05).","","","","","","Residues 18 to 255 (E-value = 3e-81) place AA00575 in the Shikimate_DH family which is described as Shikimate / quinate 5-dehydrogenase (PF01488)","","","","","Anton,I.A. and Coggins,J.R. Sequencing and overexpression of the Escherichia coli aroEgene encoding shikimate dehydrogenase Biochem. J. 249 (2), 319-326 (1988) PubMed: 3277621 Maclean,J., Campbell,S.A., Pollock,K., Chackrewarthy,S., Coggins,J.R. and Lapthorn,A.J. Crystallization and preliminary X-ray analysis of shikimate dehydrogenase from Escherichia coli Acta Crystallogr. D 56, 512-515 (2000)","","Fri Dec 13 10:57:28 2002","1","","","" "AA00576","394708","394160","549","ATGAATTTACAAGATATTGTTGAACAGTTGAAACGTCAACGCGTGGTGGCGTATCCTACCGAAGCGGTGTTCGGCTTGGGTTGCAACCCGAACAGTCAAAGTGCGGTAGAAAATTTACTTGTTTTGAAGCAACGCCCCGTGTCGAAAGGTTTGATCCTGATTGCGACTGCCTTGGATTTTTTGTTGCCGTTTATTGATGAACGCCCTCTGGCGGAACTGCATTGGCAACGCCTCACCGCGCAATACGCCCGCCCGACCACCTGGGTCGTTCCCGCGAAAAAGACCACGCCGAAATTTCTCACCGGCGATTTTGACAGCATTGCGGTGCGCATCAGTCAGCACCCCGCCGTCAAACTGTTATGCGAACAGGCGGGCTTTGCGCTTACCTCCACCAGCGCCAATTTAAGCGGACAGCCGCCCTGCCGCACGGCGCAGGAAGTCACCCGCCAATTCGGCGCCGATTTTCCGGTGTTGGAGATGCCCGTGGGCGATGCAGTTAACCCGTCGGAAATTCGCGACATTTTCACCAACCAAATTTTTCGTCAAGGA","","","20258","MNLQDIVEQLKRQRVVAYPTEAVFGLGCNPNSQSAVENLLVLKQRPVSKGLILIATALDFLLPFIDERPLAELHWQRLTAQYARPTTWVVPAKKTTPKFLTGDFDSIAVRISQHPAVKLLCEQAGFALTSTSANLSGQPPCRTAQEVTRQFGADFPVLEMPVGDAVNPSEIRDIFTNQIFRQG","394162","","conserved hypothetical protein (possible translation factor)","Periplasm, Cytoplasm","","
InterPro
IPR006070
Domain
SUA5/yciO/yrdC, N-terminal
PF01300\"[7-183]TSua5_yciO_yrdC
PS51163\"[1-183]TYRDC
InterPro
IPR012200
Family
RNA-binding protein, YrdC
PIRSF004931\"[1-183]TRNA-binding protein, YrdC type
noIPR
unintegrated
unintegrated
G3DSA:3.90.870.10\"[3-181]Tno description
PTHR17490\"[13-183]TSUA5


","BeTs to 24 clades of COG0009COG name: Putative translation factor (SUA5)Functional Class: JThe phylogenetic pattern of COG0009 is aompkzyqvdrlbcefghsn-jxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 4.7e-17) to 2/2 blocks of the IPB000666 family, which is described as \"SUA5/yciO/yrdC family\". Interpro entry for IP:IPR000666. IPB000666A 15-43 4.5e-12 IPB000666B 85-102 0.0024","Residues 3 to 181 match (1e-70) PD:PD329321 which is described as COMPLETE PROTEOME SUA5 HYPF HYDROGENASE MATURATION REGULATORY FAMILY FACTOR RELATED ","","","","","","","","","","","","Wed Feb 19 14:40:49 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00576 is paralogously related to AA02682 (2e-06) and AA01997 (1e-04).","","","","","","Residues 7 to 183 (E-value = 6.4e-55) place AA00576 in the Sua5_yciO_yrdC family which is described as yrdC domain (PF01300)","","","","","Teplova M, Tereshko V, Sanishvili R, Joachimiak A, Bushueva T, Anderson WF, Egli M.The structure of the yrdC gene product from Escherichia coli reveals a new fold and suggests a role in RNA binding.Protein Sci. 2000 Dec;9(12):2557-66.PMID: 11206077 Klima R, Coglievina M, Zaccaria P, Bertani I, Bruschi CV.A putative helicase, the SUA5, PMR1, tRNALys1 genes and four open reading frames have been detected in the DNA sequence of an 8.8 kb fragment of the left arm of chromosome VII of Saccharomyces cerevisiae.Yeast. 1996 Sep;12(10B Suppl):1033-40.PMID: 8896267Na JG, Pinto I, Hampsey M.Isolation and characterization of SUA5, a novel gene required for normal growth in Saccharomyces cerevisiae.Genetics. 1992 Aug;131(4):791-801. PMID: 1325384 ","","Wed Feb 19 14:40:49 2003","1","","","" "AA00578","395261","394716","546","ATGCGCGAACCTTTATTCCAAGCCACCAAACAGGAAGAACACTGCCCGCAATGTGGCGCCTTGTTGCAAATCAAACAGGGTAAAAAAGGGCTGTTTCTCGGCTGTTCTGCTTATCCGCAATGCGATTATCTGAAACCGTTGCACGCCGGCAATGAGGTGAAAATCCTCAAAATGCTGGAACAAAGTTGCCCTGAATGTGGGCATCTTTTAGCGTTAAAACAAGGGCATTTCGGGATGTTCATCGGCTGCAGCAATTATCCCGACTGTCATTTTGTGGTGCACGAAGACGCAGAGGAAGAAACGGAAGAACATTTGCCTTGCCCCGAATGCAAAGCAGGGCAATTGGTGGCACGGCGCGGACGTACGGGCAAATCGTTTTATGCCTGCAACCGTTTTCCGCATTGCAAATTTTCTGTGCCGAGCAAGCCGTATGCCGTCCGTTGCCCGCAATGCCACGGCAGTTTAGCCTTATTAAAAAAACAACAGGACGGGCAACGCACTTGGCAATGCGCCAACAAAGCCTGTCGCCATATTTTTATGACCGAG","","","24129","MREPLFQATKQEEHCPQCGALLQIKQGKKGLFLGCSAYPQCDYLKPLHAGNEVKILKMLEQSCPECGHLLALKQGHFGMFIGCSNYPDCHFVVHEDAEEETEEHLPCPECKAGQLVARRGRTGKSFYACNRFPHCKFSVPSKPYAVRCPQCHGSLALLKKQQDGQRTWQCANKACRHIFMTE","394718","","DNA topoisomerase","Cytoplasm, Periplasm","","
InterPro
IPR013498
Domain
DNA topoisomerase, type IA, zn finger
PF01396\"[12-50]T\"[60-98]T\"[104-144]Tzf-C4_Topoisom


","BeTs to 18 clades of COG0551COG name: Zn-finger domain associated with topoisomerase type IFunctional Class: LThe phylogenetic pattern of COG0551 is aompk---v--lb-efghsnu--itwNumber of proteins in this genome belonging to this COG is","","Residues 107 to 175 match (4e-07) PD:PD346735 which is described as TOPOISOMERASE PROTEOME DNA-BINDING COMPLETE ISOMERASE DNA ","","","","","","","","","","","","Fri Dec 13 11:31:34 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00578 is paralogously related to AA02128 (5e-07).","","","","","","Residues 104 to 144 (E-value = 4.1e-11) place AA00578 in the zf-C4_Topoisom family which is described as Topoisomerase DNA binding C4 zinc finger (PF01396)","","","","","Chen CC, Wu HY.Transcription-driven DNA supercoiling and gene expression control.Front Biosci. 2003 Jan 1;8:D430-9.PMID: 12456361 Drolet M, Broccoli S, Rallu F, Hraiky C, Fortin C, Masse E, Baaklini I.The problem of hypernegative supercoiling and R-loop formation in transcription.Front Biosci. 2003 Jan 1;8:D210-21.PMID: 12456359 Trigueros S, Roca J.Failure to relax negative supercoiling of DNA is a primary cause of mitotic hyper-recombination in topoisomerase-deficient yeast cells.J Biol Chem. 2002 Oct 4;277(40):37207-11.PMID: 1215141Zhu Q, Pongpech P, DiGate RJ.Type I topoisomerase activity is required for proper chromosomal segregation in Escherichia coli.Proc Natl Acad Sci U S A. 2001 Aug 14;98(17):9766-71.PMID: 11493711 ","","Fri Dec 13 11:38:39 2002","1","","","" "AA00579","395405","397015","1611","ATGTTTGCATTGGATATTGATTTAAATATGTTATTGGGCATTTGCGCGGCGCTTGGCGTGCTTTGCCTGATTTTGTTATTTGTGGGCGCGCGACGCAAACGCGACAGCGTGGAATTGCAGCAGGATCTCAATAAAAACATCGAAGATTTTAATCAGTTATTGGCGAAATTTGATGCGGTTACCGCACGCAAAAATCAATTGGAACAAGAAGTGGTGAAAGCGCAAACCATGGCGGACGGCCTACAAATTCGCCTCACCGAGCGCGATGAAAAAGTGCTGTATTTGCAAACGGAACTGAACGAAGAACAAGCCCGTCACAGTGCCATTGCGGAACAGATTACCGCCTTAAAAGAACGTTTCGGCGTGGCGTCGGCGCAGGCGGAAGGGTTGCGCAGTCAGTTGGAACAGAGCCAAAGTCTGATTTCACGCCGTGAAGAAGCGTTGGCAAATTTAACGGAAAAATACACCGCACTTTCGCAGGAGCTGGCAGAGCTCAAGACCACCTTAACGGAAAAAGAAAAACATTTTGCCGAACAGCAGCAAAATTTCGAGCAAACCAAACAGCAACTTAATACGGAATTTCAAAATCTCGCCAATCGCATTCTGGAAGAAAAAAGTCAGCGTTTTCAACAAACCAACCAAGCCTCCATGGACAGCCTGTTGAAGCCGTTCCGCGAGCAAATTGAAAGTTTTCAGAAACGGGTGAATGAAATTCATTCGGAGTCCGTTAAAGGCAACGCCGGGTTGGAAGCGGAAATTAAGAAAGTGCTGGAAATCGGCTTGAGTATGTCGCAACAGGCGAATAATCTTACATCCGCGTTAAAAGGCGAAAAGAAAACCCTCGGCAACTGGGGCGAAATGCAGCTGGAGCGCGCGTTGCAATCTGCCGGTTTGCTGGAAGACCAACATTACACCGCGCAGGCGCATTTTAAAAACGAGGAAGGCAAGCGTAATTATCCCGATTTTATTCTCAACCTGCCGGACGACAAACATTTAATCATCGACAGCAAAATGTCCCTTAACGCCTATGAAAGTGCGGTCAGTTCTGAGGATGAAATGGAACGTCAGGCGTTTCTGCATGAAAACATTAAGGCGTTGCGCAATCACATCGATGATTTATCGCGCAAAGATTACAGCAACCTTATCGGCGTACGCAGCCCGAATTTCGTGCTGATGTTCGTTGCCGTGGAACCCGCTTATATTGAAGCGCTAAAAATGGATCCTAGCCTGTTCGGCTACGGCTACGATAAAAATGTCATCATGGTGTCCCACACCACGCTCATGCCGATTTTGCGTACCGTAGCGAACCTGTGGCGGGTAGAACGCGGCAATGCGGAAGCGCGCGAAATCAGCGAAAAAGCCGGCGACATTTATAACCAAATCTGCCTGCTTGCCGAACGTTTGGCAAAAGTGGGCAACAGTCTGTCTGCCGTCAGTTCCCACTACAACAGCACCGTCACCGCGCTGGTCGGGCAGCAAGGCTTAATGGGCAAAGTGGAACGTTTCAAAGCCCTCTCCGCCAAAGCCTCCAAAACCCTGCCGAATATCGAACCGCTGCATCATGATTTTGAAACGGAGCGGTTGTTGGTGACAAAAGAAAATTTAGAAGAA","","","66135","MFALDIDLNMLLGICAALGVLCLILLFVGARRKRDSVELQQDLNKNIEDFNQLLAKFDAVTARKNQLEQEVVKAQTMADGLQIRLTERDEKVLYLQTELNEEQARHSAIAEQITALKERFGVASAQAEGLRSQLEQSQSLISRREEALANLTEKYTALSQELAELKTTLTEKEKHFAEQQQNFEQTKQQLNTEFQNLANRILEEKSQRFQQTNQASMDSLLKPFREQIESFQKRVNEIHSESVKGNAGLEAEIKKVLEIGLSMSQQANNLTSALKGEKKTLGNWGEMQLERALQSAGLLEDQHYTAQAHFKNEEGKRNYPDFILNLPDDKHLIIDSKMSLNAYESAVSSEDEMERQAFLHENIKALRNHIDDLSRKDYSNLIGVRSPNFVLMFVAVEPAYIEALKMDPSLFGYGYDKNVIMVSHTTLMPILRTVANLWRVERGNAEAREISEKAGDIYNQICLLAERLAKVGNSLSAVSSHYNSTVTALVGQQGLMGKVERFKALSAKASKTLPNIEPLHHDFETERLLVTKENLEE","397017","","probable DNA recombination protein","Inner membrane, Cytoplasm","","
InterPro
IPR003798
Domain
RmuC
PF02646\"[214-516]TRmuC
InterPro
IPR013253
Family
Kinetochore Spc7
SM00787\"[28-281]Tno description
noIPR
unintegrated
unintegrated
PTHR18937\"[32-303]TSTRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER
PTHR18937:SF10\"[32-303]TSTRUCTURAL MAINTENANCE OF CHROMOSOMES SMC, BACTERIAL
signalp\"[1-30]?signal-peptide
tmhmm\"[10-30]?transmembrane_regions


","BeTs to 8 clades of COG1322COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG1322 is -----------l--efghsn-jxi--Number of proteins in this genome belonging to this COG is","","Residues 39 to 138 match (9e-09) PD:PD561469 which is described as RECOMBINATION DNA PROTEOME COIL COILED COMPLETE HOMOLOG RMUC ","","","","","","","","","","","","Fri Dec 13 12:10:02 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00579 is paralogously related to AA02511 (1e-04), AA02112 (3e-04) and AA02347 (4e-04).","","","","","","Residues 214 to 516 (E-value = 5.4e-125) place AA00579 in the RmuC family which is described as RmuC family (PF02646)","","","","","Slupska MM, Chiang JH, Luther WM, Stewart JL, Amii L, Conrad A, Miller JH.Genes involved in the determination of the rate of inversions at short inverted repeats.Genes Cells. 2000 Jun;5(6):425-37.PMID: 10886369","","Fri Dec 13 12:02:09 2002","1","","","" "AA00580","397143","397688","546","GTGCAACAAGCGAACCAAGGACAACAAATTAAACCGCGTTATGAGCCGGCGGCAATCAGTAAAATTATTTTCGCCAGCCGTTGGCTGCAACTGCCGATTTATCTCGGGTTGATTATCGTGCAAGGCATTTATGCCTATAAATTTATGAAATCCCTGTGGCATTTAATTGTCAATTTACAGGAAATGGATTCCAACACCGTGATGTTGGCGGTATTGAATCTGATTGATGTTGTCATGATCGCCAATTTGCTGGTGATGGTGATTATCGGCGGGTATGAGATTTTCGTCTCCAAGCTGCGCACGCGTGGGCATCCGGATCAGCCGGAATGGTTGAGCCATGTGAATGCGTCGGTGTTGAAAGTGAAATTGGCGATGTCGATTATCAGCATTTCGTCTATCCATATGTTGCAAACCTTCGTGAATGCGTCAAATATGGATGAAAAAACCATGATGTGGCAGCTGTTTTTACATTTAGGCTTTTTAGCCTCCGCCATTGCCATGGCATATACGGACAAAATCCTTTACGGCACCAGCCATAAAGCACAT","","","21001","VQQANQGQQIKPRYEPAAISKIIFASRWLQLPIYLGLIIVQGIYAYKFMKSLWHLIVNLQEMDSNTVMLAVLNLIDVVMIANLLVMVIIGGYEIFVSKLRTRGHPDQPEWLSHVNASVLKVKLAMSIISISSIHMLQTFVNASNMDEKTMMWQLFLHLGFLASAIAMAYTDKILYGTSHKAH","397690","","conserved hypothetical protein (possible membrane protein)","Inner membrane, Cytoplasm","","
InterPro
IPR005134
Family
Protein of unknown function UPF0114
PD011070\"[19-137]TYC58_PASMU_P57929;
PF03350\"[22-140]TUPF0114
TIGR00645\"[19-182]THI0507: conserved hypothetical protein TIGR
noIPR
unintegrated
unintegrated
signalp\"[1-45]?signal-peptide
tmhmm\"[28-46]?\"[72-92]?\"[113-133]?\"[152-170]?transmembrane_regions


","No hits to the COGs database.","","Residues 23 to 172 match (9e-59) PD:PD011070 which is described as TRANSMEMBRANE PROTEOME COMPLETE PLASMID REPA1-REPA2 YQHA PROBABLE MEMBRANE-ASSOCIATED PIPA PA4574 ","","","","","","","","","","","","Fri Dec 13 12:18:44 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00580 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 18 to 179 (E-value = 4.2e-94) place AA00580 in the UPF0114 family which is described as Uncharacterized protein family, UPF0114 (PF03350)","","","","","","","","1","","","" "AA00581","397745","398026","282","ATGTTACAACAGGATGAAAACGCCGTGCTGGCGGATGTGCGCGATCAGGTGCGCTTCAATTATTCCCACGCACAGGGCGCGGTGAATTTAACGGAACTTACCTGGCCGGATTTTGAAGCCGAATATGATTACGATCAGCCGATTTTGGTCAGTTGTTATCATGGTGTGAGCAGCCGCAGTGTCGCCATGTTTCTATTACAACGCGGCTATGAAAAAGTGTATAGCGTGCGGGGCGGATTCACCGGTTGGGTGGAAGCCAATTTACCGCTGGAAACCGCCTAT","","","12416","MLQQDENAVLADVRDQVRFNYSHAQGAVNLTELTWPDFEAEYDYDQPILVSCYHGVSSRSVAMFLLQRGYEKVYSVRGGFTGWVEANLPLETAY","398028","","thiosulfate sulfurtransferase (rhodanese)","Cytoplasm","","
InterPro
IPR001763
Domain
Rhodanese-like
PF00581\"[1-86]TRhodanese
SM00450\"[1-89]TRHOD
PS50206\"[4-92]TRHODANESE_3
noIPR
unintegrated
unintegrated
G3DSA:3.40.250.10\"[1-90]Tno description


","BeTs to 16 clades of COG0607COG name: Rhodanese-related sulfurtransferasesFunctional Class: PThe phylogenetic pattern of COG0607 is aomp--yq-drlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","","Residues 6 to 90 match (2e-07) PD:PD299733 which is described as PROTEOME COMPLETE SULFURTRANSFERASES BU052 RHODANESE-RELATED YVAB TRANSFERASE YIBN SECRETED ","","","","","","","","","","","","Fri Dec 13 12:29:08 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00581 is paralogously related to AA01507 (1e-10).","","","","","","Residues 1 to 86 (E-value = 8.7e-11) place AA00581 in the Rhodanese family which is described as Rhodanese-like domain (PF00581)","","","",""," Bordo D, Larson TJ, Donahue JL, Spallarossa A, Bolognesi M.Crystals of GlpE, a 12 kDa sulfurtransferase from escherichia coli, display 1.06 A resolutiondiffraction: a preliminary report.Acta Crystallogr D Biol Crystallogr. 2000 Dec;56 Pt 12:1691-3.PMID: 11092948 Ray WK, Zeng G, Potters MB, Mansuri AM, Larson TJ.Characterization of a 12-kilodalton rhodanese encoded by glpE of Escherichia coli and itsinteraction with thioredoxin.J Bacteriol. 2000 Apr;182(8):2277-84.PMID: 10735872 Adams H, Teertstra W, Koster M, Tommassen J.PspE (phage-shock protein E) of Escherichia coli is a rhodanese.FEBS Lett. 2002 May 8;518(1-3):173-6.PMID: 1199704Bhattacharyya AM, Horowitz PM.Rhodanese can partially refold in its GroEL-GroES-ADP complex and can be released to give a homogeneous product.Biochemistry. 2002 Feb 19;41(7):2421-8.PMID: 11841236 Spallarossa A, Donahue JL, Larson TJ, Bolognesi M, Bordo D.Escherichia coli GlpE is a prototype sulfurtransferase for the single-domain rhodanese homology superfamily.Structure (Camb). 2001 Nov;9(11):1117-25.PMID: 11709175","","Wed Feb 19 08:08:53 2003","1","","","" "AA00582","398355","398044","312","ATGAGAAATCCAAATTTGCCCTCGGGCTTCAGCCCTTTCAGCTGGGCGATTGCTATGTTTTGCTTACCGGTTTTGCTTTGGCCATTGGCACTGTTAATTTCACCGAATTTGTTGAAGAACCCGAACCTAAGCGACACTCAAATCCACGCCATGTCGATTTTTCTGTGGGGTTATCCTTTCGCTTTGGGCATCATCGCACGGATTTTTTATAAACTGCATGAGCGCAAAGCCGCGTTGGCGCGTCGCGGTTTAGCCATAAGTGCGGTCATTTTTTACGGCGTTTTAAGCTATGTTGCCGTCGTCGGATTTAAC","","","13634","MRNPNLPSGFSPFSWAIAMFCLPVLLWPLALLISPNLLKNPNLSDTQIHAMSIFLWGYPFALGIIARIFYKLHERKAALARRGLAISAVIFYGVLSYVAVVGFN","398046","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-32]?signal-peptide
tmhmm\"[15-33]?\"[52-70]?\"[85-103]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Fri Dec 13 12:49:57 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00582 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00583","398398","399270","873","ATGCAGCATTTGTTTGGTAGTGAAATTCCCGCGTTAGTCAGTCATTTTCGTGAGCATATTCGCACGAAATATCAGGTGGAGTTGGTTATTGAAGAAAAGACCAACGAACAGGGCGAACCGATTTATCATGTTTTTCTGCCGCAAAATGCACCGCACTTTGAAGCGATTGTGCAGGAATGTGACGGCTTCTTACAAGAATGGCTGAAACGGCAAAATGCACAGGCATGGCAAAATGGCACAAGCCCCGTTCGAGTGCGCGCGGTATCCGCCTCCGACGAGATGCCGCCGCTCAACAGGATTTCCCTTGTAACTTACCTTCAACCGCGAAAAATAACCGTTATTGTGACCGCACTTTGTGCCCTGATTTATCTTTTTATGTTATTCGGTTTTGCCGAACCCATCGTGCTGTTTTCCCATTTCCCCGATGAAGCTGACCAATACGGCGAAATTTGGCGCTATTTCAGTCATACTTTAGTGCATTTGTCCAATATGCACATTCTGTTTAACCTCACATGGTGGTGGATTTTCGGTGGCGCGATTGAACGTCGCTTGGGCAGTTTTAAATTACTGCAAATTTATTTCCTTGCCGGCGCGGTGGGCGGCATTGCGCAAAACATGGTGAGCGGACCGGCATTTTTCGGCTTATCCGGCGTGGTATATGCGGTGCTGGGCTATGTATTTGTGTTGGATAAGCTCAATAAACACACGGATTTTGACGTGCCGGAAGGCTTTTTCAATATGTTGGTTGTCGGGATCTTGCTTGGCTTTGCCGGCCCATTGGTGGATATTAATATTGGCAACACGGCGCATATTTCCGGTTTGTTGGTGGGCGTATTGTTGGCGTTTGCGGATCGAAATATTCGCGTTAAGTCG","","","32825","MQHLFGSEIPALVSHFREHIRTKYQVELVIEEKTNEQGEPIYHVFLPQNAPHFEAIVQECDGFLQEWLKRQNAQAWQNGTSPVRVRAVSASDEMPPLNRISLVTYLQPRKITVIVTALCALIYLFMLFGFAEPIVLFSHFPDEADQYGEIWRYFSHTLVHLSNMHILFNLTWWWIFGGAIERRLGSFKLLQIYFLAGAVGGIAQNMVSGPAFFGLSGVVYAVLGYVFVLDKLNKHTDFDVPEGFFNMLVVGILLGFAGPLVDINIGNTAHISGLLVGVLLAFADRNIRVKS","399272","Beyond its involvement in the Glp regulon, concerned with glycerol utilization, the function of the GlpG protein is unknown.","GlpG protein","Inner membrane, Cytoplasm","","
InterPro
IPR002610
Family
Peptidase S54, rhomboid
PTHR22936\"[94-283]TRHOMBOID-RELATED
PF01694\"[144-289]TRhomboid
noIPR
unintegrated
unintegrated
tmhmm\"[111-131]?\"[150-170]?\"[185-203]?\"[209-229]?\"[244-263]?\"[269-289]?transmembrane_regions


","BeTs to 16 clades of COG0705COG name: Uncharacterized membrane protein (homolog of Drosophila rhomboid)Functional Class: RThe phylogenetic pattern of COG0705 is aompkzyqvdrlbcefghs-uj--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 7.9e-11) to 3/3 blocks of the IPB002610 family, which is described as \"Rhomboid family\". Interpro entry for IP:IPR002610. IPB002610A 160-169 0.11 IPB002610B 214-224 0.01 IPB002610C 269-279 0.014","Residues 1 to 79 match (2e-12) PD:PD396412 which is described as PROTEOME COMPLETE GLPG ","","","","","Tue Feb 18 16:54:33 2003","","","","","","Tue Feb 18 17:50:49 2003","Tue Feb 18 17:56:42 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00583 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 145 to 289 (E-value = 4.5e-39) place AA00583 in the Rhomboid family which is described as Rhomboid family (PF01694)","","","","","Yang B, Larson TJ.Multiple promoters are responsible for transcription of the glpEGR operon of Escherichiacoli K-12.Biochim Biophys Acta. 1998 Mar 4;1396(1):114-26.PMID: 9524241Zeng G, Ye S, Larson TJ.Repressor for the sn-glycerol 3-phosphate regulon of Escherichia coli K-12: primary structure and identification of the DNA-binding domain.J Bacteriol. 1996 Dec;178(24):7080-9.PMID: 8955387","","Tue Feb 18 16:48:03 2003","1","","","" "AA00585","399335","399838","504","ATGAGACAATCTCTTCGTCATCAAAAAATTGTCGAACTGGTGAAGCAAAAAGGGTATTTGAGCACCGATGAATTGGTGGCTTTGTTTGATGTGAGCCCGCAAACCATTCGACGCGATTTAAATGAACTGGCCGAAGCCAACTTCATTCGCCGCCATCATGGAGGTGCCGCTTCGCCTTCCAGCGCCGAAAACAGCGATTATCACGATCGCAAGCACTTTTTTTCTCAAGAAAAAAATCGTATCGCCAAACAGGCGGTTGAGCTCATTCCGAACGGCGCCTCATTGTTTATCGACATCGGTACTACTCTGAAGCCGTTTCTTTCGCTTTACTGGGGCACCAAAGACTGCGTATCGTCACCAATAATCTCAATGCCGCGCATATTCTCATGCAAAATGACTCCTTCGACATTACCATCGCCAGCGGCTCTTTACGCCAAGACGGCGGCATTATCGGCGAATCGACGGTGGAGTTTTTGTCCCAATTCCGTTTGGATTTCGGCGTGT","","","18797","MRQSLRHQKIVELVKQKGYLSTDELVALFDVSPQTIRRDLNELAEANFIRRHHGGAASPSSAENSDYHDRKHFFSQEKNRIAKQAVELIPNGASLFIDIGTTLKPFLSLYWGTKDCVSSPIISMPRIFSCKMTPSTLPSPAALYAKTAALSANRRWSFCPNSVWISAC","399840","","glycerol-3-phosphate regulon repressor","Periplasm, Cytoplasm","","
InterPro
IPR001034
Domain
Bacterial regulatory protein, DeoR N-terminal
PR00037\"[24-38]T\"[38-56]THTHLACR
PF08220\"[6-62]THTH_DeoR
SM00420\"[6-58]THTH_DEOR
PS51000\"[3-58]THTH_DEOR_2
PS00894\"[6-40]THTH_DEOR_1
InterPro
IPR014036
Domain
Bacterial regulatory protein, DeoR
PF00455\"[75-102]TDeoR


","No hits to the COGs database.","Significant hit ( 2.2e-36) to 2/5 blocks of the IPB001034 family, which is described as \"Bacterial regulatory protein, DeoR family\". Interpro entry for IP:IPR001034. IPB001034A 20-55 1.3e-21 IPB001034B 78-102 1.9e-13Significant hit ( 7.7e-06) to 1/1 blocks of the IPB000524 family, which is described as \"Bacterial regulatory proteins, GntR family\". Interpro entry for IP:IPR000524. IPB000524 19-59 7.1e-06","Residues 36 to 102 match (2e-24) PD:PD002333 which is described as PROTEOME COMPLETE TRANSCRIPTIONAL TRANSCRIPTION DNA-BINDING REGULATION REGULATOR REPRESSOR DEOR FAMILY ","","","","","","","","","","","","Fri Dec 13 13:19:30 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00585 is paralogously related to AA01698 (8e-14), AA02048 (3e-12), AA00973 (2e-11), AA00308 (4e-11) and AA01546 (1e-05).","","","","","","Residues 6 to 167 (E-value = 3.1e-14) place AA00585 in the DeoR family which is described as Bacterial regulatory proteins, deoR family (PF00455)","","","","","Secondary Laboratory Evidence:Zeng,G., Ye,S. and Larson,T.J. Repressor for the sn-glycerol 3-phosphate regulon ofEscherichia coli K-12: primary structure and identificationof the DNA-binding domain. J. Bacteriol. 178(24): 7080-7089, 1996. PubMed: 8955387. Choi,Y.L., Kawase,S., Nishida,T., Sakai,H., Komano,T.,Kawamukai,M., Utsumi,R., Kohara,Y. and Akiyama,K. Nucleotide sequence of the glpR gene encoding the repressorfor the glycerol-3-phosphate regulon of Escherichia coliK12. Nucleic Acids Res. 16(15): 7732, 1988. PubMed: 3045764.","","Fri Dec 13 13:19:30 2002","1","","","" "AA00586","399721","400086","366","ATGCAAAATGACTCCTTCGACATTACCATCGCCAGCGGCTCTTTACGCCAAGACGGCGGCATTATCGGCGAATCGACGGTGGAGTTTTTGTCCCAATTCCGTTTGGATTTCGGCGTGTTAGGCATCAGCGCCATTGATTTAGACGGCACATTGCTGGATTACGATTATCATGAAGTGCAGGTTAAGCGGGCAATTATTGATAATTCCCGCAATACCTTGTTAGTCACCGACCATTCTAAATTCAGCCGCCGCGCTATGGTAAAACTGGGTTCAATCACCGATGTGGAATATGTTTTTACCGACATGGACGTACCACCGAGCATTGATGAACTGCTGAAAAACAAAAATGTCAATTTAGTTGTTTGC","","","13570","MQNDSFDITIASGSLRQDGGIIGESTVEFLSQFRLDFGVLGISAIDLDGTLLDYDYHEVQVKRAIIDNSRNTLLVTDHSKFSRRAMVKLGSITDVEYVFTDMDVPPSIDELLKNKNVNLVVC","400088","","glycerol-3-phosphate regulon repressor","Cytoplasm","","
InterPro
IPR014036
Domain
Bacterial regulatory protein, DeoR
PF00455\"[2-101]TDeoR


","BeTs to 6 clades of COG1349COG name: Transcriptional regulators of sugar metabolismFunctional Class: K,GThe phylogenetic pattern of COG1349 is -------qvd-lb-efgh-n-j----Number of proteins in this genome belonging to this COG is","","Residues 18 to 122 match (6e-07) PD:PD538500 which is described as REGULATOR PROTEOME PLASMID DEOR COMPLETE FAMILY TRANSCRIPTIONAL ","","","","","","","","","","","","Fri Dec 13 13:21:29 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00586 is paralogously related to AA00308 (3e-08).","","","","","","Residues 1 to 101 (E-value = 5e-06) place AA00586 in the DeoR family which is described as Bacterial regulatory proteins, deoR family (PF00455)","","","","","Zeng,G., Ye,S. and Larson,T.J. Repressor for the sn-glycerol 3-phosphate regulon ofEscherichia coli K-12: primary structure and identificationof the DNA-binding domain. J. Bacteriol. 178(24): 7080-7089, 1996. PubMed: 8955387. Choi,Y.L., Kawase,S., Nishida,T., Sakai,H., Komano,T.,Kawamukai,M., Utsumi,R., Kohara,Y. and Akiyama,K. Nucleotide sequence of the glpR gene encoding the repressorfor the glycerol-3-phosphate regulon of Escherichia coliK12. Nucleic Acids Res. 16(15): 7732, 1988. PubMed: 3045764.","","Fri Dec 13 13:21:29 2002","1","","","" "AA00587","400115","400216","102","GTGCTGTGGATTTTCACCGCACTTTTTTCTTCTTTATCTCCTGTCTTCGCATTTTTTGAATTTCTTTTTTTTCTTGCTAAAAACTTATTTTTCTATATAAAA","","","4097","VLWIFTALFSSLSPVFAFFEFLFFLAKNLFFYIK","400216","","hypothetical protein","Cytoplasm, Outer membrane","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-17]?signal-peptide
tmhmm\"[4-26]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:40:42 2004","Sun Feb 22 16:40:42 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00587 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:40:42 2004","","","","","","","","","","","","","1","","","" "AA00588","400288","400383","96","TTGATTTTTCTGCAAACACGTTTTAGCAAAAATCTTATTATTGCTTTTATTGTATTCATTTATAAAAAGATCGATAATGAGAATGATTATCAAAAC","","","3905","LIFLQTRFSKNLIIAFIVFIYKKIDNENDYQN","400383","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-15]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:43:39 2004","Sun Feb 22 16:43:39 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00588 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:43:39 2004","","","","","","","","","","","","","1","","","" "AA00589","400474","400346","129","TTGGCAACATTCAGCACGTTTAAAATGCAAAATGTGACCAAATTTAATAAACTTGCTCATTTATTCTCCTTAGGAAAGTTTATTTTTATTAGTTTTGATAATCATTCTCATTATCGATCTTTTTATAAA","","","5145","LATFSTFKMQNVTKFNKLAHLFSLGKFIFISFDNHSHYRSFYK","400346","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:42:20 2004","Sun Feb 22 16:42:20 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00589 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:42:20 2004","","","","","","","","","","","","","1","","","" "AA00590","400458","403157","2700","GTGCTGAATGTTGCCAATGCAGAGGAACAATTAGATCAAATCGACGTTGTTGAAAAAACCATTGCGAACGAGAAAAAACCATTTACCGAGGCGAAAGCTAAAAGTACCCGCGAGAATGTCTTCAAGTCCACAGAAACCGTTGATAATGTGGTACGTAGTATTCCCGGGGCATTTACTCAACAGGATAAAAGTTCTGGCGTACTATCCTTAAACATTCGTGGCGAAACCGGGTTCGGACGGGCGAACACCATGGTTGATGGGGTGACACAAACTTTTTATTCAACCTCTATGGATGCAGGGCGTGCAGGTGGTAATTCGCAGTTTGGTGCGGCAATCGATCCGAATTTTATTGCCGGTATAGATTTAACCAAAGGCAACTTTAGCGGAACCGGCGGGGTAAATTCCTTGTACGGGGCGGCAAATTTCAGAACTTTAGGTGTGAATGATGTGATTCAGGGGGATAAAAACTATGGCTTCCTCACCAAAGGATTAACCGGCGATAACGAAACCAAATATAACTACATGGCAATGGGTGCTGCCCGTAAATGGTTGGATAATGGCGGATATATTGGCGTTCTGTATGGCTATAGCCAAAGAGAGGTTTCACAAAATTATAAGGTCGGCGGTGGTGGCGAACGTATCTCCGATGTAGGTAAAGGGTTTCTTGAACGAAAAAGAAATGAATTTTTCCGTAGCCATCAGTTGAAATTTAACAGTGAGAAAAACGAATGGGAACGTGACTTTTCGATAAAAAATTCAGCGGGTAAGAGTACGTGGGAATATCCCTGGAATAAAAAATATAACGATCCGCAAAAGCTAAAGGAATATATCGCCGAGTTAGGTAAAATCTGGAATGAAAACGAAGTGCCGCAATGGGATTTAACACCGATAGATCCTTCAAGTTTGGTTCAGCGTTCAAAAAGCCATTTAGTGAAAGTGGAATTTTCGGATGATCGACATACCTTAAATTTACAATACCGAACGCTTGATAATCATATCGGTAGTCGAAAAATTGAGAATCAGAATTATCAGTTAAATTACAATTTTAATAATAATGGCTATCTTGATCTCAATGTATTGCTGGCGCATAACGTAGACAAACAAAAGTATCCGAGCGGTTCACGTTTTGGCGGCTGGCAGGTATTGAAATATTTGGAAACCAAAAATACAGCGGATATTGTTGATATTAGTAACAGTTATACCTTTTCGCTGCCAAAAGAAACCGATCTAAAAACGACCTTAGGCGTGAATTTATTTAAAAATCAATATACTAAAAATCGTTTCCCGGAAGAACTCAGTCCTTTTTACGACGGTCCTTCGCAAAAAAGCGGACTATATGACTTCTTAGGTCGTTTCAAAGGCGATAAAGGCATACTTCCGCAAAAATCGACCATTTTACAGCCTTCCGGCGAACAGCGTTTTAATACGGTTTATCTGGATACATCTTTGACTCGTGACATCTTTAAACTTGATTACAGTGTGAATTTTGTGAAGTATAAGTTTAACGGCGAATATACTGCCTATTACAACAGTCCGAGCGATTTTAAAAAGGCATTTGGAGAAGATTCGGAAATTTATAAAAAACACTGCAATCCAAGTTGTGATTTGTATGAACCGGTGTATAAAAAGGGCGGCAAGAAAAGTGCGGTCAATCATTCCGTCGTTTTGAGTGCTGAGCCAAGTGATTATTTTATGCCTTTTATCAGCTATGCCAGAACCCATAGAATGCCGAATATTCAGGAAATGTATTTTTCACAAATCGGCGATTCCGGTGTGAATACCAACTTAAAACCCGAACGTGCGGATACCTATCAAATCGGTTTTAATACGTTCAAAAATAATGTGTTCCTGGATGATGATGTATTGGGTTTAAAAGCCGTGTTTTATCGTAGCCGCAGTTTAAAATACATTCATAATGTTTATGGTAAATGGTGGAATACTCAAGCCGGTTTACCGCCAAGTTGGGTAACGACAACCGGGCTGAGCTATACGATTCAGCACCGAAATTATCAAAAACGCGTTAATAAACGCGGCTTAGAATTAGAGCTTAATTATGATGCGGGTCGGTTCTTTACTAATTTATCTTACGCTTATCAGAAAACCAATCAGCCGACTAACTACAGCGATGCCAGTGAATCACCAAATAACGCATCGAAACAGGATCAAATTAAACAAGGCTATGGTTTAACTAAAATTTCTATGTTGCCGAGAGACTATGGTCGCTTGGAAATCGGTTCGCGCTGGTTTGATCGTAAATTAACCATCGGAAGTGCGGTCAGATATTACGGTAAAAGTAAACGTGCCACTACGGAAGAAAGATACATTGACGGCACGAAACCCGGCAATACCGCTGATCCGCATAATATCGGCAAACGTGTGATTAAAGAAACCGAGACTATTGATAAGCAACCGTTGGTGGTTGATTTCTATGTGGCGTATGAACCCGTCGAAAATTTAGTCATTCGCGCGGATATACAAAATGCCTTTGATAAAAGATATATTGACCCGTTGGATGCCGCAAATGACGCAGCAACCCAACGCTATTTCTCCACCTTTGAGAATCTCAATTCCTATGGAGATGATATAGTTCAGTGTGATTCTAACGGATTATGTAACGGAAGATATGGCGGAAAGACCAATTCTATTCTGAATAATTATGCCAGAGGGAGGACTTTCGTCTTATCGGTGAGTTATAAATTC","","","103196","VLNVANAEEQLDQIDVVEKTIANEKKPFTEAKAKSTRENVFKSTETVDNVVRSIPGAFTQQDKSSGVLSLNIRGETGFGRANTMVDGVTQTFYSTSMDAGRAGGNSQFGAAIDPNFIAGIDLTKGNFSGTGGVNSLYGAANFRTLGVNDVIQGDKNYGFLTKGLTGDNETKYNYMAMGAARKWLDNGGYIGVLYGYSQREVSQNYKVGGGGERISDVGKGFLERKRNEFFRSHQLKFNSEKNEWERDFSIKNSAGKSTWEYPWNKKYNDPQKLKEYIAELGKIWNENEVPQWDLTPIDPSSLVQRSKSHLVKVEFSDDRHTLNLQYRTLDNHIGSRKIENQNYQLNYNFNNNGYLDLNVLLAHNVDKQKYPSGSRFGGWQVLKYLETKNTADIVDISNSYTFSLPKETDLKTTLGVNLFKNQYTKNRFPEELSPFYDGPSQKSGLYDFLGRFKGDKGILPQKSTILQPSGEQRFNTVYLDTSLTRDIFKLDYSVNFVKYKFNGEYTAYYNSPSDFKKAFGEDSEIYKKHCNPSCDLYEPVYKKGGKKSAVNHSVVLSAEPSDYFMPFISYARTHRMPNIQEMYFSQIGDSGVNTNLKPERADTYQIGFNTFKNNVFLDDDVLGLKAVFYRSRSLKYIHNVYGKWWNTQAGLPPSWVTTTGLSYTIQHRNYQKRVNKRGLELELNYDAGRFFTNLSYAYQKTNQPTNYSDASESPNNASKQDQIKQGYGLTKISMLPRDYGRLEIGSRWFDRKLTIGSAVRYYGKSKRATTEERYIDGTKPGNTADPHNIGKRVIKETETIDKQPLVVDFYVAYEPVENLVIRADIQNAFDKRYIDPLDAANDAATQRYFSTFENLNSYGDDIVQCDSNGLCNGRYGGKTNSILNNYARGRTFVLSVSYKF","403159","","outer membrane substrate binding protein; TonB-dependent outer membrane receptor","Outer membrane, Extracellular","","
InterPro
IPR000531
Domain
TonB-dependent receptor
PF00593\"[551-900]TTonB_dep_Rec
InterPro
IPR010917
Domain
TonB-dependent receptor, C-terminal
PS01156\"[883-900]?TONB_DEPENDENT_REC_2
InterPro
IPR012910
Domain
TonB-dependent receptor, plug
PF07715\"[26-139]TPlug
noIPR
unintegrated
unintegrated
G3DSA:2.170.130.10\"[4-144]Tno description
G3DSA:2.40.170.20\"[317-900]Tno description


","BeTs to 8 clades of COG1629COG name: Outer membrane receptor proteins, mostly Fe transportFunctional Class: PThe phylogenetic pattern of COG1629 is -------q-----cefghsnuj----Number of proteins in this genome belonging to this COG is","","Residues 145 to 212 match (7e-09) PD:PD282472 which is described as CJRC PROTEOME OUTER COMPLETE MEMBRANE SIDEROPHORE RECEPTOR ","","","","","Wed Feb 19 14:47:25 2003","","","","Wed Feb 19 14:47:25 2003","","","Tue Feb 18 10:48:04 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00590 is paralogously related to AA02782 (9e-17), AA02157 (5e-06), AA02202 (2e-05) and AA02865 (1e-04).","","","","","","Residues 24 to 900 (E-value = 5.8e-07) place AA00590 in the TonB_dep_Rec family which is described as TonB dependent receptor (PF00593)","","","","","","","","1","","","" "AA00591","405567","403753","1815","ATGAACCGCACTTTTTTGTTATCGGATTATATGATGGATCATACTCAGGAAATTATCACTTCTTTACTTTGGATTGCAAAAACCTTGGCAATTACCGCCGTTGTTTTCAGTTTCAGTATTTTTTTATTAGTGCATCTCACCAGCTGGGGCAAACAATTCTGGATGTTCGCCGGCGGCTATCTTTCGCCGAAGCGCAGCATCAAACCGCTGCTATTTTTCACTTTAATCGTCACCTTGACACTCTTTAGCGTGCGTCTTAGCCTGGTGTACTCTACTTGGTACAACAATCTGTACACCTCGCTCCAGGAATTCAACGAACCGGTGTTTTGGAATCAAATGATCCTCTTTGGCTTTATTGCCGGCTTTTCCGTCCTCTCGACGCTTATTAGCTATTATGTCAGCCAACGCTTTTCCATTAACTGGATTGAATGGCTGAATAGCGAAATGGTAGAAAAATGGATGAGCAATCGCGCTTACTATAAAAGCCAATATACCGGTCATAATCTGGACAACCCCGATCAACGGATTCAACAAGACGTGCAAGCTTACGTCAAAACCACCCTTTCCCTTAGCACCGGCGTGATTAATGCTGTCACCTCCATGATTTCCTACACCATTTTGTTGTGGGGATTGGCGGGTCCAATGAGCGTGCTGGGAGTAAAAATTCCGCACATGATGGTGTTCTTGGTGTTCGCTTACGTGATTTTCACCACGCTCATCGCCTTCTGGCTCGGAAAACCCTTAATCCGCTTGAATTTCGCTAATGAAAAATTAAACGCGAACTATCGTTATTCCTTAATTCGCGTAAAAGAATACGCCGAAAGTATCGCGTTCTATACTGGTGAAAAAGTGGAAAAAAGCCATCTATATAAACAATTTCGCTCGGTTATCGGCAACATGTGGGGCATCGTGTTCCGGACGTTAAAATTCTCCGGGTTCAACTTGGTGGTAAGCCAAATTTCGGTGGTGTTTCCGCTACTCATTCAAGTGGGTCGCTATTTTGAAAAACAAATTAAACTGGGCGACTTAATGCAAACCTTACAGGTTTTCGGGCAGTTACACTCAAATCTCTCCTTTTTCCGTAACACTTACGACAATTTCGCCGAATATAAAGCCACGTTAGACCGTTTAACCGGTTTCAAATACAGCGTCGAAGCGGCACAAAAAGAAAGCAAAACTCACATTTCCGACCACCCGAGCGATGTGATTTTCCAACATCTCAGCGTCAAATCCCCCCTTGGCAAAACGCTGATTAAAGATCTCAATCTCACCCTACCGCAAGGACATTCTTTGCTCATCCAAGGGCAATCGGGCGTAGGTAAAACCACCTTATTACGCACCGTAGCGGGGCTATGGTTATACGCTCAAGGAGAAGTGTTCTGCCCGCAAAACAATACTTTGTTCCTCTCGCAGCGCCCTTATCTGCCACAAGGGGATTTACTCACAGCGCTGTATTATCCGAGCTCCATAGAAAAGGCGGATTTGACAGAGGTCAGCAAGGTGTTACAACAGGTTCAGCTGGCTCATTTACAGGATCGTTTGGCACAGGAACAAGACTGGAGTCGCATTTTATCCCTTGGTGAACAACAACGCCTTGCTTTCGCCCGTTTATTATTGCACAAGCCACAAGTCGCCTTTTTAGACGAAGCCACCGCCAGTCTTGACGAAGGATTGGAAAACGCCATGTATCGTCTCATTCGCCACACATTGCCGAATACGACGATTATCAGCGTAGGGCATCGTTCGGCGTTGGTGCCGTTGCATCAACAGCGTTTAGAATTGCAGGCTGATGGAAGCTGGATATTGACTACCGGT","","","69296","MNRTFLLSDYMMDHTQEIITSLLWIAKTLAITAVVFSFSIFLLVHLTSWGKQFWMFAGGYLSPKRSIKPLLFFTLIVTLTLFSVRLSLVYSTWYNNLYTSLQEFNEPVFWNQMILFGFIAGFSVLSTLISYYVSQRFSINWIEWLNSEMVEKWMSNRAYYKSQYTGHNLDNPDQRIQQDVQAYVKTTLSLSTGVINAVTSMISYTILLWGLAGPMSVLGVKIPHMMVFLVFAYVIFTTLIAFWLGKPLIRLNFANEKLNANYRYSLIRVKEYAESIAFYTGEKVEKSHLYKQFRSVIGNMWGIVFRTLKFSGFNLVVSQISVVFPLLIQVGRYFEKQIKLGDLMQTLQVFGQLHSNLSFFRNTYDNFAEYKATLDRLTGFKYSVEAAQKESKTHISDHPSDVIFQHLSVKSPLGKTLIKDLNLTLPQGHSLLIQGQSGVGKTTLLRTVAGLWLYAQGEVFCPQNNTLFLSQRPYLPQGDLLTALYYPSSIEKADLTEVSKVLQQVQLAHLQDRLAQEQDWSRILSLGEQQRLAFARLLLHKPQVAFLDEATASLDEGLENAMYRLIRHTLPNTTIISVGHRSALVPLHQQRLELQADGSWILTTG","403755","MSD-NBD fusion protein.","ABC transporter, ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR002078
Domain
RNA polymerase sigma factor 54, interaction
PS00675\"[431-444]?SIGMA54_INTERACT_1
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[524-566]TQ9CLX7_PASMU_Q9CLX7;
PF00005\"[428-598]TABC_tran
PS50893\"[402-605]TABC_TRANSPORTER_2
PS00211\"[524-538]?ABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[427-598]TAAA
InterPro
IPR010509
Domain
ABC transporter, N-terminal
PF06472\"[43-334]TABC_membrane_2
InterPro
IPR011527
Domain
ABC transporter, transmembrane region, type 1
PS50929\"[70-369]TABC_TM1F
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[365-595]Tno description
PTHR11384\"[65-603]TATP-BINDING CASSETTE, SUB-FAMILY D MEMBER
PTHR11384:SF3\"[65-603]TATP-BINDING CASSETTE, SUB-FAMILY D, MEMBER 4 (PEROXISOMAL MEMBRANE PROTEIN 69)
signalp\"[1-37]?signal-peptide
tmhmm\"[29-49]?\"[70-90]?\"[114-134]?\"[193-213]?\"[227-245]?\"[310-328]?transmembrane_regions


","BeTs to 6 clades of COG1133COG name: ABC-type long-chain fatty acid transport system, fused permease and ATPase componentsFunctional Class: IThe phylogenetic pattern of COG1133 is ------y---r--ce--h-nuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 9e-24) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 417-463 7e-09 IPB001140B 521-559 2.8e-12 IPB001140C 574-603 24","Residues 120 to 419 match (4e-08) PD:PD492973 which is described as ATP-BINDING PROTEOME COMPLETE ABC ABC-TRANSPORTER TRANSPORTER ","","","","","","","","","","","Wed May 12 16:52:31 2004","Fri Dec 13 13:47:12 2002","","Wed May 12 16:52:31 2004","Wed May 12 16:52:31 2004","Wed May 12 16:52:31 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00591 is paralogously related to AA02606 (5e-18), AA02440 (8e-16), AA02331 (1e-15), AA02805 (2e-15), AA00700 (3e-14), AA02718 (4e-14), AA01684 (1e-13), AA01656 (1e-13), AA01393 (3e-12), AA02609 (7e-12), AA01645 (1e-11), AA01961 (1e-11), AA01616 (3e-11), AA01820 (5e-11), AA01509 (2e-10), AA01422 (3e-10), AA02898 (5e-10), AA01510 (9e-10), AA00858 (9e-10), AA02152 (2e-09), AA01867 (2e-09), AA00415 (3e-09), AA00061 (3e-09), AA01051 (4e-09), AA02140 (6e-09), AA02484 (8e-09), AA02320 (8e-09), AA02550 (2e-08), AA00207 (4e-08), AA02353 (5e-08), AA02080 (8e-08), AA02573 (1e-07), AA00933 (1e-07), AA00799 (2e-07), AA01568 (5e-07), AA02899 (9e-07), AA01757 (2e-06), AA01524 (2e-06), AA02324 (4e-06), AA01824 (4e-06), AA02225 (6e-06), AA01456 (6e-06), AA02786 (1e-05), AA01779 (2e-05), AA00751 (1e-04), AA01555 (6e-04), AA02146 (0.001) and A02145 (0.001).","Wed May 12 16:52:31 2004","","","","","Residues 428 to 598 (E-value = 1.7e-24) place AA00591 in the ABC_tran family which is described as ABC transporter (PF00005)","Wed May 12 16:52:31 2004","","","","","","","1","","","" "AA00592","405676","407346","1671","TTGTTTGAGGTAGATATGAGCGATATTGCAATTACGACGAGCCTATTAGCGTTAGTTGCCGTTATCGGGCTATGGATCGGACATTGGAAAATCAAAGGCGTCGGTTTCGGCGTGGGGGGCGTGCTGTTCGGTGGAATCATCGTGGCGCATTTTACCAATGAATACGGGCTGAAGCTGGATATGCACACGTTGCATTTCGTGCAGGAATTCGGCTTAATTCTGTTTGTTTATACCATCGGGATTCAGGTTGGTCCGGGATTTTTCTCATCGTTGCGCCGTTCAGGATTAAAACTGAACGGTTTTGCATTTTTAATCGTGCTGCTCGGCGGGCTCACTGTGGTAGTGATTCATAAGTTTGCGGGCGTGCCGTTGGATATTATCTTGGGGATTTATTCCGGAGCGGTAACCAATACGCCGTCTCTCGGTACGGGACAACAGATTTTAAGCGAATTGGGCTTTGCTGATGCAAACACCACCATGGGGACAGCATACGCAATGGCTTATCCTTTCGGTATTTGCGGGATTTTGTTATGTATGTGGCTCATTCGCCTGGCGTTTAAAGTGAAAGTGGACGACGAAGAACGTAATTTCCAGCATGAAAGCGGGCAGGATAAAGAATCTTTGGGCTCCATTAACGTAAAAGTAACCAACAAAAACCTGGATGGTTTGCGCTTGGCGGATATTCCGGGTTTTGAAAGTCATGATGTGGTCTGTTCCCGTTTGAAACGTGGTGACGACATCAGCGTGCCGAAAGCCGATACGGAAATTTTTCCGGATGACGTGTTACACTTGGTAGGAGAAACGCCGGCATTGAAAAAAATGCGTTTGGTCATCGGCGAGGAATTGGATTTACCGATTTCCAACATCAGCGGCGAAATTCGTGCCGAACGGGTTGTCGTTACCAGCGAAAAAGTGCTGGGCAAGAAAATCAAATCGCTGGGTATTCACCAAAAATACGGTGTGGTGATTTCCCGTTTGAACCGTGCCGGGGTGGAACTGGTGCCGACCGCCAACACCAGCCTGCAATTCGGTGACGTGTTGCACATGGTCGGGCGCACCGATGTGTTAAATAACGCCATTTCCGTGATCGGTAACGCCGAACAAAAATTACAACAAGTGCAAATGTTACCGGTGTTTATCGGGATCGGCTTGGGTGTGTTGTTGGGCTCCATTCCGTTTTACATTCCCGGTTTTCCGGTGGCATTAAAACTCGGTTTGGCGGGCGGTCCGTTAGTGGTCGCATTGATTTTGGCACGGATCGGTAGTGTGGGAAAACTGTATTGGTTTATGCCGCCGAGCGCCAACCTTGCTTTGCGTGAAATCGGGATCGTTCTGTTCCTGGCGGTGGTCGGGTTAAAATCGGGCGGCAGCTTCCTGGATACCCTGCTTAACGGCAGCGGTTTGGAATGGATGGGCTACGGCGTGATTATTACTTTGGTTCCGCTGCTGATTACTGGCATTGTTGCCCGCTTATACAGCAAGCTCAATTACCTTTCCCTGTGCGGCGTGCTGGCGGGTTCCATGACCGATCCGCCAGCGCTGGCTTTCGCCAATGCTATTAAAGAAGAAAGCGGCGCGGCGGCATTGTCTTATGCCACAGTGTATCCGCTCGCCATGTTCCTGCGGATTATTTCACCGCAGTTATTGGCGTTGCTGTTGTGGAGTTTCGCC","","","59617","LFEVDMSDIAITTSLLALVAVIGLWIGHWKIKGVGFGVGGVLFGGIIVAHFTNEYGLKLDMHTLHFVQEFGLILFVYTIGIQVGPGFFSSLRRSGLKLNGFAFLIVLLGGLTVVVIHKFAGVPLDIILGIYSGAVTNTPSLGTGQQILSELGFADANTTMGTAYAMAYPFGICGILLCMWLIRLAFKVKVDDEERNFQHESGQDKESLGSINVKVTNKNLDGLRLADIPGFESHDVVCSRLKRGDDISVPKADTEIFPDDVLHLVGETPALKKMRLVIGEELDLPISNISGEIRAERVVVTSEKVLGKKIKSLGIHQKYGVVISRLNRAGVELVPTANTSLQFGDVLHMVGRTDVLNNAISVIGNAEQKLQQVQMLPVFIGIGLGVLLGSIPFYIPGFPVALKLGLAGGPLVVALILARIGSVGKLYWFMPPSANLALREIGIVLFLAVVGLKSGGSFLDTLLNGSGLEWMGYGVIITLVPLLITGIVARLYSKLNYLSLCGVLAGSMTDPPALAFANAIKEESGAAALSYATVYPLAMFLRIISPQLLALLLWSFA","407348","","conserved hypothetical protein (membrane/transport protein)","Inner membrane, Cytoplasm","","
InterPro
IPR006037
Domain
TrkA-C
PF02080\"[209-279]T\"[294-364]TTrkA_C
PS51202\"[195-275]T\"[279-365]TRCK_C
InterPro
IPR006512
Domain
YidE/YbjL duplication
PF06826\"[15-184]T\"[377-551]TAsp-Al_Ex
TIGR01625\"[20-170]T\"[382-537]TYidE_YbjL_dupl: YidE/YbjL duplication
noIPR
unintegrated
unintegrated
signalp\"[1-23]?signal-peptide
tmhmm\"[9-29]?\"[34-52]?\"[71-91]?\"[101-121]?\"[162-182]?\"[375-395]?\"[401-421]?\"[442-462]?\"[472-492]?transmembrane_regions


","BeTs to 4 clades of COG2985COG name: Predicted permeaseFunctional Class: RThe phylogenetic pattern of COG2985 is -o------------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 235 to 361 match (2e-47) PD:PD230418 which is described as COMPLETE PROTEOME TRANSMEMBRANE MEMBRANE YIDE YPO4083 PM1071 HI0035 ORFA ","","","","","","","","","","","","Mon Feb 17 15:17:25 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00592 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 377 to 551 (E-value = 1.3e-64) place AA00592 in the Asp-Al_Ex family which is described as Predicted Permease Membrane Region (PF06826)","","","","","","","","1","","","" "AA00595","407334","407471","138","GTGGAGTTTCGCCTAGTAAAAAACGCGATAAAAACCTACCGCACTTTATGCGACGACAGATTTCGCCGTGTAAAGTGCGGTCGGTTTTTGCGGCATTTTCCAATGTTTGCTTCACAGGTTAGGCAAGATCCATTAAAA","","","5626","VEFRLVKNAIKTYRTLCDDRFRRVKCGRFLRHFPMFASQVRQDPLK","407471","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Sun Feb 22 16:45:15 2004","Sun Feb 22 16:45:15 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00595 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sun Feb 22 16:45:15 2004","","","","","","","","","","","","","1","","","" "AA00596","407636","408217","582","ATGGACGTGGAGGTCGGCGTTGTGTTGGGTGGTGGCAATTTATTCCGCGGTGCCAAACTTGCCAAAGCCGGTATGAACCGCGTGGTAGGCGACCACATGGGGATGTTGGCGACGGTGATGAACGGTTTGGCGATGCGTGACGCGCTGCACCGCGCCGATGTCAACGCCAAATTAATGTCCGCCTTTCAGTTAAACGGTATTTGCGATACCTACAACTGGTCCGAAGCCATCAAAATGTTACGCGAAAAACGCGTCGTGATTTTCTCTGCCGGCACCGGCAGCCCTTTCTTTACCACCGATTCCGCCGCTTGTTTACGCGGTATTGAAATTGAAGCGGATGTGGTGTTAAAAGCCACCAAAGTGGATGGCGTGTACGACTGCGATCCGGCCAAAAATACCAATGCCAAACTGTATAAAAACTTAACCTATGCGGAAGTCATCGATAAAGAATTAAAAGTGATGGATCTTGCCGCCTTTACCCTCGCCCGCGACCACGGTATACCAATTCGGGTCTTCAATATGGGTAAACCGGGCGCATTACGCCAAGTCATCCTCGATACCGATGTCGGCACGACCATTTGT","","","22485","MDVEVGVVLGGGNLFRGAKLAKAGMNRVVGDHMGMLATVMNGLAMRDALHRADVNAKLMSAFQLNGICDTYNWSEAIKMLREKRVVIFSAGTGSPFFTTDSAACLRGIEIEADVVLKATKVDGVYDCDPAKNTNAKLYKNLTYAEVIDKELKVMDLAAFTLARDHGIPIRVFNMGKPGALRQVILDTDVGTTIC","408219","From Genbank:[gi:267005] This enzyme catalyzes the phosphorylation of UMP to UDP, with ATP as preferred donor.","uridylate kinase","Cytoplasm","","
InterPro
IPR001048
Domain
Aspartate/glutamate/uridylate kinase
G3DSA:3.40.1160.10\"[1-193]Tno description
PF00696\"[1-173]TAA_kinase
InterPro
IPR011817
Family
Uridylate kinase
TIGR02075\"[1-194]TpyrH_bact: uridylate kinase
noIPR
unintegrated
unintegrated
PTHR21499\"[121-171]TASPARTATE KINASE


","BeTs to 24 clades of COG0528COG name: Uridylate kinaseFunctional Class: FThe phylogenetic pattern of COG0528 is aompkz-qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 6.9e-05) to 1/4 blocks of the IPB001057 family, which is described as \"Glutamate 5-kinase\". Interpro entry for IP:IPR001057. IPB001057C 96-129 6.7e-05","Residues 13 to 86 match (2e-33) PD:PD005760 which is described as KINASE COMPLETE PROTEOME URIDYLATE 2.7.4.- TRANSFERASE MONOPHOSPHATE UMP BIOSYNTHESIS URIDINE ","","","","","","","","","","","Tue Jan 7 11:32:01 2003","Tue Jan 7 11:29:02 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00596 is paralogously related to AA02357 (6e-05).","","","","","","Residues 1 to 173 (E-value = 4.3e-35) place AA00596 in the AA_kinase family which is described as Amino acid kinase family (PF00696)","","","","","Serina,L., Blondin,C., Krin,E., Sismeiro,O., Danchin,A.,Sakamoto,H., Gilles,A.M. and Barzu,O. Escherichia coli UMP-kinase, a member of the aspartokinasefamily,is a hexamer regulated by guanine nucleotides and UTP. Biochemistry 34(15): 5066-5074, 1995. PubMed: 7711027. Yamanaka,K., Ogura,T., Niki,H., Hiraga,S. Identification and characterization of the smbA gene, a suppressor of the mukB null mutant of Escherichia coli. J. Bacteriol. 174(23): 7517-7526, 1992. PubMed: .","","Tue Jan 7 11:32:37 2003","1","","","" "AA00598","408408","408220","189","GTGATTCTACTGGATTTTTGTAAAATTTTGAATCATTTTCTTTTGGAAGCACGGCTTTCAGGCGTAAATTTTTGCTGTATTTTATTTTTTGATGGGCAACAAAGTGCGGTCGAATTTTCATGTGTTTTTTTCATACAAAAAACGGTAGAAAATCATTTCTACCGTTTTTCCTTTTCACGAAACCCCGCT","","","7354","VILLDFCKILNHFLLEARLSGVNFCCILFFDGQQSAVEFSCVFFIQKTVENHFYRFSFSRNPA","408222","","hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Fri Dec 13 13:59:36 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00598 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00600","408445","408999","555","ATGATTAAGCAAATTAAACAAGATGCCGAAGACCGTATGGAAAAAAGCCTGGACGCGTTAAAAGGGCATATTGCAAAAATCCGTACCGGTCGTGCGCAGCCAAGTTTATTGGATGCGATTCAAGTGGATTATTACGGTTCTGCAACACCGTTACGCCAATTAGCCAATGTGGTGGCGGAAGATGCGCGTACGTTGGCGGTGACCGTATTCGATCGTTCTTTGATTCAAGCGGTGGAAAAAGCCATTTTGACTTCCGATTTAGGCTTAAATCCGTCTTCTGCCGGCACCACCATTCGCGTGCCGCTACCACCATTAACGGAAGAACGTCGTCGTGAGTTAATCAAAATCGTGAAAGCGGAAGGCGAACAGGGCAAAGTGGCGATTCGTAACGTGCGCCGTGATGCTAACGATAAAATCAAAGCCTTGTTAAAAGACAAAGAAATCAGCGAAAACGATCAGCACAAAGCGGAAGAGGTGATTCAAAAATTAACCGACAGCTTCATCAAAAAAGTGGATGATGTGTTGGCGGACAAAGAAAAAGAATTACTTGATTTC","","","20665","MIKQIKQDAEDRMEKSLDALKGHIAKIRTGRAQPSLLDAIQVDYYGSATPLRQLANVVAEDARTLAVTVFDRSLIQAVEKAILTSDLGLNPSSAGTTIRVPLPPLTEERRRELIKIVKAEGEQGKVAIRNVRRDANDKIKALLKDKEISENDQHKAEEVIQKLTDSFIKKVDDVLADKEKELLDF","409001","","ribosome recycling factor (ribosome releasing factor)","Cytoplasm","","
InterPro
IPR002661
Family
Ribosome recycling factor
PD004103\"[6-183]TRRF_HAEIN_P44307;
PTHR20982:SF3\"[1-185]TRIBOSOME RECYCLING FACTOR (RIBOSOME RELEASING FACTOR) (RRF)
PF01765\"[19-183]TRRF
TIGR00496\"[10-185]Tfrr: ribosome recycling factor
noIPR
unintegrated
unintegrated
G3DSA:1.10.132.20\"[66-185]Tno description
PTHR20982\"[1-185]TRIBOSOME RECYCLING FACTOR


","No hits to the COGs database.","Significant hit ( 8.9e-60) to 2/2 blocks of the IPB002661 family, which is described as \"Ribosome recycling factor\". Interpro entry for IP:IPR002661. IPB002661A 27-63 1.3e-21 IPB002661B 78-130 4.4e-37","Residues 1 to 183 match (3e-74) PD:PD004103 which is described as RIBOSOME FACTOR RECYCLING PROTEOME COMPLETE RELEASING BIOSYNTHESIS RRF CYCLIN CHLOROPLAST ","","","","","","","","","","","","Fri Dec 13 14:01:56 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00600 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 19 to 183 (E-value = 5.5e-97) place AA00600 in the RRF family which is described as Ribosome recycling factor (PF01765)","","","","","Ohnishi M, Janosi L, Shuda M, Matsumoto H, Hayashi T,Terawaki Y, Kaji A. Molecular cloning, sequencing, purification, andcharacterization of Pseudomonas aeruginosa ribosomerecycling factor. J Bacteriol 181(4):1281-91.1999. PubMed: . Janosi,L., Shimizu,I. and Kaji,A. Ribosome recycling factor (ribosome releasing factor) isessential for bacterial growth. Proc. Natl. Acad. Sci. U.S.A. 91(10): 4249-4253.1994. PubMed: 8183897. Shimizu,I. and Kaji,A. Identification of the promoter region of theribosome-releasing factor cistron (frr). J. Bacteriol. 173(16): 5181-5187. 1991. PubMed: 1860827. Ichikawa,S. and Kaji,A. 1989. Molecular cloning andexpression of ribosome releasing factor. J. Biol. Chem.264(33): 20054-20059. PubMed: 2684966.","","Fri Dec 13 14:01:56 2002","1","","","" "AA00601","409003","409179","177","TTGCTGAACATCGCTAAACACGGACGCAGTGGCTTACCGCGTCTTTTCTTATGCGGGCGCGTTTATTTTATTGCCCGACAACTCTGCAAAGTGCGGTCAAAATTTTATGCAAAACAAACAAAAGGTCGTGATTCTCGGTGCTACAGGTTCTATCGGCAACAGCGCCCTGTCGGTGAT","","","7006","LLNIAKHGRSGLPRLFLCGRVYFIARQLCKVRSKFYAKQTKGRDSRCYRFYRQQRPVGD","409179","","hypothetical protein","Cytoplasm, Extracellular","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 09:32:32 2004","Mon Feb 23 09:32:32 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00601 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 09:32:32 2004","","","","","","","","","","","","","1","","","" "AA00602","409217","410311","1095","GTGGGCGGTTCCAATGCGACGGCGATGTTTGAAAAATGCCTGAAATTTCGACCGCACTTTGTTGCTTTAGCTGATGAATACGCAGCGAAAGTATTGCGCGAAAAATTAACGGCTCATCAGATTCCAACCCAAGTTTTGGCGGGGCAGCAGGCGATTTGTGAATTGAGTGCGCATCCTGATGCAGACATGGTGATGGCGGCGATTGTGGGTGCGGCGGGCTTGTTACCGACCCTATCTGCAGTTAAAGCGGGTAAGAAAGTGTTACTGGCGAACAAAGAGGCGCTGGTGACTTGCGGTCAAATTTTTATTGATGCCGTGAAACAGCATGGCGCGCAATTATTGCCGGTGGACAGCGAACATAACGCCATTTTTCAATCGTTGCCACCACAGGCGCAGCAACAAATCGGTTTTTGCCCGTTGGCGGATTTGGGCATCAGCAAAATCGTGCTGACCGGTTCCGGCGGACCTTTCCGTTATACGGCGTTAAGCGAATTTGACGGCATTACGCCGGAACAAGCGGTAGCGCATCCGAACTGGTCTATGGGCAAGAAAATTTCCGTGGATTCCGCCACCATGATGAACAAAGGCTTGGAATATATTGAAGCCCGCTGGTTGTTTAACGTGTCCGCCGACGAAATGGAAGTGATTATTCACCCGCAATCCATTATTCATTCTATGGTGCGTTATATCGACGGCAGCGTCATCGCGCAAATGGGCAATCCTGATATGCGCACGCCGATCGCCGAAACCATGGCGTATCCGCACCGCACGTTTTCCGGCGTCGCGCCGCTAGATTTCTATCAATTAAACGGGCTGACTTTTTTGGCACCGGACTATCAACGTTATCCTTGCTTGAAACTCGCCATCGAGGCGTTCGCCGCCGGTCAATATGCTACGACGGCAATGAATGCCGCCAATGAAATCGCTGTGCAGGCATTTTTAGATCGCCAAATTAAATTTACCGACATTGCCAAACTTAATCAGGCGGTGGTGGAACAAATTGCACCGCAACAAATCAAACAAATTGATGATGTGTTGGACGTCGATCGCGCAGCGCGTGAGTGCGCGCGTAAACAATTGGCACATTGGTCTCAC","","","46420","VGGSNATAMFEKCLKFRPHFVALADEYAAKVLREKLTAHQIPTQVLAGQQAICELSAHPDADMVMAAIVGAAGLLPTLSAVKAGKKVLLANKEALVTCGQIFIDAVKQHGAQLLPVDSEHNAIFQSLPPQAQQQIGFCPLADLGISKIVLTGSGGPFRYTALSEFDGITPEQAVAHPNWSMGKKISVDSATMMNKGLEYIEARWLFNVSADEMEVIIHPQSIIHSMVRYIDGSVIAQMGNPDMRTPIAETMAYPHRTFSGVAPLDFYQLNGLTFLAPDYQRYPCLKLAIEAFAAGQYATTAMNAANEIAVQAFLDRQIKFTDIAKLNQAVVEQIAPQQIKQIDDVLDVDRAARECARKQLAHWSH","410313","","1-deoxy-D-xylulose 5-phosphate reductoisomerase","Cytoplasm","","
InterPro
IPR003821
Family
1-deoxy-D-xylulose 5-phosphate reductoisomerase
PIRSF006205\"[1-365]T1-deoxy-D-xylulose 5-phosphate reductoisomerase
TIGR00243\"[1-365]TDxr: 1-deoxy-D-xylulose 5-phosphate reducto
InterPro
IPR013512
Domain
1-deoxy-D-xylulose 5-phosphate reductoisomerase, N-terminal
PF02670\"[1-99]TDXP_reductoisom
InterPro
IPR013644
Domain
1-deoxy-D-xylulose 5-phosphate reductoisomerase, C-terminal
PF08436\"[113-206]TDXP_redisom_C


","BeTs to 16 clades of COG0743COG name: 1-deoxy-D-xylulose 5-phosphate reductoisomeraseFunctional Class: IThe phylogenetic pattern of COG0743 is -------qvdr-bcefghsnuj-it-Number of proteins in this genome belonging to this COG is","Significant hit (1.7e-109) to 4/5 blocks of the IPB003821 family, which is described as \"1-deoxy-D-xylulose 5-phosphate reductoisomerase\". Interpro entry for IP:IPR003821. IPB003821B 64-99 1.4e-23 IPB003821C 168-206 1e-34 IPB003821D 213-256 5.5e-34 IPB003821E 301-323 9e-14","Residues 1 to 50 match (1e-13) PD:PD186282 which is described as REDUCTOISOMERASE 5-PHOSPHATE 1-DEOXY-D-XYLULOSE COMPLETE PROTEOME OXIDOREDUCTASE NADP ISOPRENE DXP 1-DEOXYXYLULOSE-5-PHOSPHATE ","","","","","","","","","","","","Fri Dec 13 14:09:18 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00602 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 356 (E-value = 2.2e-203) place AA00602 in the DXP_reductoisom family which is described as 1-deoxy-D-xylulose 5-phosphate reductoisomerase (PF02670)","","","","","Takahashi,S., Kuzuyama,T., Watanabe,H. and Seto,H. A 1-deoxy-D-xylulose 5-phosphate reductoisomerase catalyzingthe formation of 2-C-methyl-D-erythritol 4-phosphate in analternative nonmevalonate pathway for terpenoid biosynthesis Proc. Natl. Acad. Sci. U.S.A. 95 (17), 9879-9884 (1998) PubMed: 9707569 Radykewicz,T., Rohdich,F., Wungsintaweekul,J., Herz,S.,Kis,K., Eisenreich,W., Bacher,A., Zenk,M.H. and Arigoni,D. Biosynthesis of terpenoids: 1-deoxy-D-xylulose-5-phosphate reductoisomerase from Escherichia coli is a class Bdehydrogenase FEBS Lett. 465 (2-3), 157-160 (2000) PubMed: 10631325 Kuzuyama,T., Takahashi,S., Takagi,M. and Seto,H. Characterization of 1-deoxy-D-xylulose 5-phosphate reductoisomerase, an enzyme involved in isopentenyldiphosphate biosynthesis, and identification of its catalytic amino acid residues J. Biol. Chem. 275 (26), 19928-19932 (2000) PubMed: 10787409 ","","Fri Dec 13 14:08:33 2002","1","","","" "AA00603","410423","411052","630","ATGCGCATTTTCGGGCATAAAAACGGCGTGGCGGCGGTGCGTGAGGCGGTGTCTTACGCGCGTAAAATCGGTGTGAAATATTTAACTTTATATGCGTTTAGCAGTGAAAACTGGAATCGCCCCGAGCAGGAAGTCAGTGCGCTGATGAATTTGTTTATGCAGGCGTTGGATTTTGAACTAAAAAAACTGCATAAAAATAATATTCGATTTAAGATTCTGGGCAATGTTGCGCGCTTCAGTGAAGGGTTACAGGAAAAAATTAAGAACGCGGAAAAATTAACGGAAAATAACACCGCACTTACTTTAAATATCGCGGCGAATTACGGCGGTCGTTGGGACATTGTACAGGCGGCACAACAGCTGGCACAAAAAGTACAGACGCAACAACTTGCCGTAACGGAAATTGACGAAGCGTTGTTGCAACAACATTTGGTTACGCAAGACGATCCGGAAGTGGATTTGCTTATTCGCACCAGCGGCGAGCAGCGCATCAGCAATTTTTTATTATGGCAAGCCGCCTATGCCGAATTTTATTTTTCCGATGTGCTTTGGCCGGATTTTAATGAAGCCGAGTTTCATCAGGCGATCCTATCTTATCAACAGCGTCATCGTCGTTTTGGCGGGACGGAA","","","27441","MRIFGHKNGVAAVREAVSYARKIGVKYLTLYAFSSENWNRPEQEVSALMNLFMQALDFELKKLHKNNIRFKILGNVARFSEGLQEKIKNAEKLTENNTALTLNIAANYGGRWDIVQAAQQLAQKVQTQQLAVTEIDEALLQQHLVTQDDPEVDLLIRTSGEQRISNFLLWQAAYAEFYFSDVLWPDFNEAEFHQAILSYQQRHRRFGGTE","411054","From Gen Bank (gi:6175088):This protein generates undecaprenyl pyrophosphate (UPP) from isopentenyl pyrophosphate (IPP). UPP is the precursor of the carrier lipid for peptidoglycan synthesis.","undecaprenyl pyrophosphate synthetase (UPPS)","Cytoplasm","","
InterPro
IPR001441
Family
Di-trans-poly-cis-decaprenylcistransferase
PD003461\"[1-202]TUPPS_PASMU_Q9CJL4;
G3DSA:3.40.1180.10\"[2-207]Tno description
PTHR10291\"[2-208]TDEHYDRODOLICHYL DIPHOSPHATE SYNTHASE
PF01255\"[1-208]TPrenyltransf
TIGR00055\"[1-207]TuppS: undecaprenyl diphosphate synthase
PS01066\"[153-170]TUPP_SYNTHETASE


","No hits to the COGs database.","Significant hit ( 2e-71) to 3/4 blocks of the IPB001441 family, which is described as \"Undecaprenyl pyrophosphate synthetase family\". Interpro entry for IP:IPR001441. IPB001441B 24-51 1.7e-18 IPB001441C 94-121 1.3e-16 IPB001441D 150-187 7.1e-34","Residues 1 to 202 match (1e-66) PD:PD003461 which is described as UNDECAPRENYL SYNTHETASE COMPLETE PYROPHOSPHATE PROTEOME TRANSFERASE SYNTHASE CELL DIPHOSPHATE UPP ","","","","","","","","","","","Mon Jan 13 18:05:45 2003","Fri Dec 13 14:10:52 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00603 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 208 (E-value = 1.6e-120) place AA00603 in the UPP_synthetase family which is described as Putative undecaprenyl diphosphate synthase (PF01255)","","","","","pfel,C.M., Takacs,B., Fountoulakis,M., Stieger,M. andKeck,W. Use of genomics to identify bacterial undecaprenylpyrophosphate synthetase: cloning, expression, andcharacterization of the essential uppS gene. J. Bacteriol. 181(2): 483-492,1999. PubMed: 9882662.","","Fri Dec 13 14:10:52 2002","1","","","" "AA00605","411070","411936","867","GTGCTTAAACAACGGGTTTTATCGGCGATTGTGTTAATTGCCATTGTATTCGCCACGTTATTTTTATTCTCACCTTATTATTTTGCGCTCGCCTTAGGTGTGGTTGTGGTGCTGGGCATTTGGGAATGGACTCAGTTCTTTAATTTCAAACAACCGACATTCTGGCGTTATGCCACCACCGTGTTAAGTGCGGTGTTTTTGTTCCTGTGGATTTATGATGAAGGCAATTATCTGGATGCCGGTCGGGTTTTTGAACATTATGCTCAACCGATTTTATTGGGCGCAGTGATTTGGTGGTTGGTGGCGTTATCTTTTGTGGTGAGTTACCCGAAAAGCAGCAATCTTTGGGCAAAACATTCCGTGCTGCAATTTTTCTTTGCCTTTTTTACGCTGATTCCGTTTTTAATCGGCGTGTTATTGCTACGTTTGGATAATTATGTAGCGCAACCTTATTACGGCATTATGTTGCTGTTGTATGTGTTTATTCTGGTTTGGGTGGCGGATTCCGGGGCGTATTTTGTGGGACGTAAATTCGGTAAACAAAAATTGGCGCCGAAAGTATCGCCAAGTAAATCCTGGCAGGGCGCAATCGGCGGTTTGGTGATGGCGGGCATCGTTTCTGCGATTTTCGTGAATGTTACGCAACAAAGTTTGATTAAAGATATTTCGCCGCCGGCATTTATTGCATTGTCTGTGGTGACGGTAGCCATTTCGATTCTGGGCGATTTAACGGAAAGTATGTTCAAACGCCAAAGCGGCATTAAAGACAGCAGTAACCTGATTCCGGGGCACGGTGGCATTTTGGACAGAATTGACAGCCTGACTGCTGCCGTACCGTTCTTTGCATATTTCTATTTCTTTGTATTG","","","32414","VLKQRVLSAIVLIAIVFATLFLFSPYYFALALGVVVVLGIWEWTQFFNFKQPTFWRYATTVLSAVFLFLWIYDEGNYLDAGRVFEHYAQPILLGAVIWWLVALSFVVSYPKSSNLWAKHSVLQFFFAFFTLIPFLIGVLLLRLDNYVAQPYYGIMLLLYVFILVWVADSGAYFVGRKFGKQKLAPKVSPSKSWQGAIGGLVMAGIVSAIFVNVTQQSLIKDISPPAFIALSVVTVAISILGDLTESMFKRQSGIKDSSNLIPGHGGILDRIDSLTAAVPFFAYFYFFVL","411938","","CDP-diglyceride pyrophosphorylase","Inner membrane, Cytoplasm","","
InterPro
IPR000374
Family
Phosphatidate cytidylyltransferase
PF01148\"[3-288]TCTP_transf_1
PS01315\"[246-272]TCDS
noIPR
unintegrated
unintegrated
PD002096\"[215-267]TQ9CJL3_PASMU_Q9CJL3;
PTHR13773\"[246-272]TPHOSPHATIDATE CYTIDYLYLTRANSFERASE
signalp\"[1-33]?signal-peptide
tmhmm\"[5-25]?\"[31-49]?\"[54-72]?\"[91-109]?\"[121-141]?\"[155-175]?\"[196-214]?\"[224-244]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 3.9e-29) to 2/2 blocks of the IPB000374 family, which is described as \"Phosphatidate cytidylyltransferase\". Interpro entry for IP:IPR000374. IPB000374A 187-199 8.8e-06 IPB000374B 246-273 6.8e-22","Residues 40 to 153 match (8e-26) PD:PD167880 which is described as CYTIDYLYLTRANSFERASE CDP-DIGLYCERIDE SYNTHASE PHOSPHATIDATE SYNTHETASE PROTEOME COMPLETE TRANSFERASE CDP-DAG CDS ","","","","","","","","","","","","Mon Jan 13 18:14:10 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00605 is paralogously related to AA00616 (3e-22).","","","","","","Residues 3 to 288 (E-value = 8e-86) place AA00605 in the CTP_transf_1 family which is described as Cytidylyltransferase family (PF01148)","","","","","Icho,T., Sparrow,C.P. and Raetz,C.R. Molecular cloning and sequencing of the gene forCDP-diglyceride synthetase of Escherichia coli. J. Biol. Chem. 260(22): 12078-12083, 1985. PubMed: 2995358. Nampoothiri KM, Hoischen C, Bathe B, Mockel B, PfefferleW, Krumbach K, Sahm H, Eggeling L. Expression of genes of lipid synthesis and altered lipidcomposition modulates L-glutamate efflux ofCorynebacterium glutamicum. Appl Microbiol Biotechnol. 2002 Jan;58(1):89-96. PMID: 11831479","","Fri Dec 13 14:13:10 2002","1","","","" "AA00606","411948","413279","1332","ATGTCATTTTTGTGGTCGACAGTTTCATTTCTGATTGTTATCGCCGTCTTGGTGGCGGTACACGAATACGGACACTTTTGGGCGGCGAGAAAGTGCGGTGTAAAAGTTCATCGTTTTTCTATCGGCTTCGGCAAAGTGATCTGGTCGCGTACCGATAAACGGGGGACGGAGTTTGCCGTATCAGCGATTCCCCTCGGTGGTTATGTGAAAATGCTGGACGGACGCAATGAAGAGATTCCGCCTGAATTTGCCGCGCAAGCCTTCGATAACAAAACCGTCGCGCAACGTGCGTTCATTATCGCTGCCGGACCTTTAGCCAATTTCTTATTTGCTATTCTGGCGTATTTCGTTATTTACTCCATCGGTGTCCCCAGCATTAAACCAGTGATCGAGGAAGTTCAACCTCATTCCATTGCTGCAAAGGCACAAGTTTCACCAAATACCCAGATTACTGAAGTTGACGGTGTTGTTACGCCGGATTGGGAAACAATTAATCTGTTGCTGGCGACTAAAACGGGCGAAAGCAAGGTGGAATTAACCTTGGTAGAGTTTGGTTCTACCATTGAGCAACACAAAATTTTAGATTTATCTAACTGGACTTTTAATCCCGAAAAAGAAAGTGCTTTCGGCTCACTAGGAATTGTTCCGGTAAGAACCAAAGTGGATATGACTTTGTCTAAAGTCAATAATCATTCCCCTGCGCAAAAGGGAGGGTTGTTGGTCGGTGATAAATTATATTGGTCGGACGGTAAAGAAATTGTCTGGCAGGATTTTATCGAACAGGTTCAACAGGGCAAACCGTTAGCTTTAAAAGTGGAACGCAACGGTGAATGGCTGGAAAAAACCATTACTCCGGAGCTTAATGACAAAAAGCGTTGGTTTGTGGGCATTTCACCGACTTTTTACCCGGTGGCTGATGAATATCGTACCGAATTAAAGTATGATATGCTCGAATCTCTACAGAGGGCGGTTGAAAAGACATTCCAACTCTCTTGGTTAACTATAAAAGTGATCGGTAAATTGCTCATCGGCGAATTATCGTTGAATAACTTGGGTGGTCCGATTTCCATTGCACAGGGCGCAGGTGCATCATCTGAACTAGGTCTGATTTACTATTTAAGCTTTATGGCGTTAATCAGCGTGAATTTAGGTGTGATGAATCTCTTTCCGTTGCCGGTGTTAGACGGCGGGCATTTGGTCTTCCTGGCGCTGGAAGCCCTTAAAGGAAAACCGGTTTCCGAACAGGTCCAGAATATCAGTTATCGAATTGGTGCGGTCTTATTATTGATGTTAATGGGATTCGGACTGATCAATGATTTTTTACGTTTAAAT","","","49303","MSFLWSTVSFLIVIAVLVAVHEYGHFWAARKCGVKVHRFSIGFGKVIWSRTDKRGTEFAVSAIPLGGYVKMLDGRNEEIPPEFAAQAFDNKTVAQRAFIIAAGPLANFLFAILAYFVIYSIGVPSIKPVIEEVQPHSIAAKAQVSPNTQITEVDGVVTPDWETINLLLATKTGESKVELTLVEFGSTIEQHKILDLSNWTFNPEKESAFGSLGIVPVRTKVDMTLSKVNNHSPAQKGGLLVGDKLYWSDGKEIVWQDFIEQVQQGKPLALKVERNGEWLEKTITPELNDKKRWFVGISPTFYPVADEYRTELKYDMLESLQRAVEKTFQLSWLTIKVIGKLLIGELSLNNLGGPISIAQGAGASSELGLIYYLSFMALISVNLGVMNLFPLPVLDGGHLVFLALEALKGKPVSEQVQNISYRIGAVLLLMLMGFGLINDFLRLN","413281","","membrane-associated zinc metalloprotease","Inner membrane, Cytoplasm","","
InterPro
IPR001478
Domain
PDZ/DHR/GLGF
PF00595\"[129-182]T\"[202-273]TPDZ
SM00228\"[114-185]T\"[210-276]TPDZ
InterPro
IPR004387
Family
Peptidase M50, putative membrane-associated zinc metallopeptidase
TIGR00054\"[1-444]TTIGR00054: membrane-associated zinc metallo
InterPro
IPR006025
Binding_site
Peptidase M, neutral zinc metallopeptidases, zinc-binding site
PS00142\"[18-27]?ZINC_PROTEASE
InterPro
IPR008915
Family
Peptidase M50
PF02163\"[9-439]TPeptidase_M50
noIPR
unintegrated
unintegrated
G3DSA:2.30.42.10\"[192-289]Tno description
signalp\"[1-19]?signal-peptide
tmhmm\"[10-28]?\"[97-119]?\"[328-348]?\"[369-389]?\"[418-438]?transmembrane_regions


","BeTs to 20 clades of COG0750COG name: Predicted membrane-associated Zn-dependent proteases 1Functional Class: MThe phylogenetic pattern of COG0750 is aompkz-qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","","Residues 222 to 294 match (4e-14) PD:PD583285 which is described as METALLOPROTEASE ZINC MEMBRANE INNER PROTEOME TRANSMEMBRANE D15 3.4.24.- HYDROLASE COMPLETE ","","","","","Wed Feb 19 07:35:40 2003","","","","","","","Wed Feb 19 07:35:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00606 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 9 to 439 (E-value = 3.7e-72) place AA00606 in the Peptidase_M50 family which is described as Peptidase family M50 (PF02163)","","","","","Dartigalongue,C., Loferer,H. and Raina,S.EcfE, a new essential inner membrane protease: its role in theregulation of heat shock response in Escherichia coliEMBO J. 20 (21), 5908-5918 (2001)PubMed: 11689431","","Fri Dec 13 15:02:08 2002","1","","","" "AA00608","413301","415709","2409","ATGACGATGAAAAAACTTTTAATTGCAAGCTTATTGTTTAGCTCAACCGCCGCGCTTGCCGGACCTTTCGTGGTACAGGACATTCGTGTTGACGGCGTTCAGGCGGGAACCGAAAGTAATATTATCGCAAGTTTGCCGGTTCGTGTCGGGCAAAAAATTAACGATGCCAATATTGCCGGTGTAGTACGTAACTTGTTTTTAACCGGTCAATACGAAGATGTTAAAGCTTCCCAACAAGGTAATACCTTAGTCATTTCCGTGGTGCCGAAAGCAATTATTTCCGATGTGGTGCTGGACGGTAACAAATCCATTCCTAATGATGCATTAAAACAAAATTTAAATGCCAATGGCTTCCAGAAGGGCGATATATTAAATCGTGAAAAACTTGAAGCCTTTCGTAAAAGTTTAGAAGATCATTATCACAGCGTCGGGCGTTATAACGCAAAAGTGGAAACTATCGTAAATCCGCTGCCAAATAACCGCGCTGAAGTGAAAATTCAAATCAAAGAGAACGATGTGGCGTTATTAAAAGGCGTGACCTTTGTGGGTAACCAGGTCTTTGATAGCGACAGATTGCAAGATCAAATGGAACTTCAACCGGATGCCTGGTGGAAGTTATTCGGCAATAAATTCGATTCAACCCAATTCTCCAAAGATTTAGAAACCATTCAAAATTATTATTTGGATCGTGGTTATGCCAAAGCGCAAATCGTTGATAATGATGTTCAGCTAAATGATGAAAAAACCGAAGCACGCGTCACTATTAACGTCTCTGAGGGTGAAAAATATACCGTCAATGGCGCACGTATCGTGGGTGATGTGGGCGGTATGAGCGAGCAGCTGGCACCATTATTGAAGCAAATTCATATCGGCGAAGAATTCCATCGTAGCGATGTGCAAGCCGTTGAAGACAGCATTAAATCCACCTTGGGCGAACGTGGTTACGGTAGCGCACAAGTGAACGTTCAACCTGACTTTAACGATGATGCCAAAACCGTCGGGTTAAGTTTTGTGGTGGATGCGGGCAAACGTTATTCCGTTCGTCAAATTCGTTTTGAAGGCAACACCGTCAGCGCGGACAGCACATTACGTCAGGAAATGCGTCAACAAGAAGGCAGCTGGTTATCTACTGATCTAGTTGAATTGGGTAAAGTGCGGTTAGATCGTACGGGATTTTTTGAAACCGTAGAAAGCCGCACCGAGCCGGTCGAAGGTACCGGCGATGAAGTGGATGTCATTTATAAAGTGAAAGAGCGTAACACCGGTAGTATTAACTTCGGTGTGGGATATGGTACGGAAAGCGGTTTAAGCTACCAAGCAAGTATCAAACAGGATAACTTCCTCGGCATGGGTTCCTCATTAAGCTTGGCGGGTTCCCGTAACGATTACGGCACCAGCGTTAACTTAGGCTATAACGAACCGTACTTCACTAAAGACGGGGTTAGCTTAGGCGGTAATATATTCTTCGAAAATTATGATAACTCCAAAAACTCGACATCCGCGTCCTATGCGCGTACCACTTACGGTGGTAACTTAACATTAGGCTTCCCGGTGAATGAAAATAATGCCTACTATATCGGCTTGGGCTATGCCTATAACAAACTGAAAAATATCACGCCTGAATATAATCGGGCCTTATATTTAGCTTCCTTAAACTATAACGAATGGACCTTCAAATCACACGATTATGATATTTCCTTCGGCTGGAACTACAACAGTTTGAACCGTGGTTTCTTGCCAACCAAAGGGGTGAAAGCCTCTATTGGCGGCAAAGTCACGATTCCGGGTTCCGATAACAAATACTACAAACTGAACGCCGATGTACAAGGTTTCTATCCGCTTAACCGCGATCAAACCTGGGTATTATCCGGACGTTTAGGTGCGGCTTATGCCAACGGCTTCGGTGGTAAGCGTCTGCCGTTCTATCAAACTTACACTGCGGGCGGTATCGGTAGCTTACGTGGTTTCGCCTACAGCGCGATTGGTCCGCAAGCAATTTATATCAATCCGAGGGTGAATGGATGTAGCGGTTCCGGTGTGAATGTCAATTCAAGCTGTTATAACATTGTGAACGGTGATATTGTGGGCGGTAATGCTATGGCAACGGCAAGTGTGGAATTAATCGTGCCGACTCCGTTTGTTGCCGAAAAAAACCAAAACTCCGTGCGCACTTCCTTCTTTGTGGATGCTGCCAGTGTTTGGGATACACATTGGAAGGGTGAAAAAGCCAAATTTACGAATTTGAAATTACCGGATTACGGTGATCCTTCCCGTGTTCGTGCTTCTGCCGGTCTTGCCTTCCAATGGCAATCACCGATTGGTCCGTTAGTTTTCTCTTATGCGAAACCGATTAAGAAATACGAAAATGATGATATTGAGCAATTCCAGTTCAGTATCGGCGGTTCTTTC","","","88289","MTMKKLLIASLLFSSTAALAGPFVVQDIRVDGVQAGTESNIIASLPVRVGQKINDANIAGVVRNLFLTGQYEDVKASQQGNTLVISVVPKAIISDVVLDGNKSIPNDALKQNLNANGFQKGDILNREKLEAFRKSLEDHYHSVGRYNAKVETIVNPLPNNRAEVKIQIKENDVALLKGVTFVGNQVFDSDRLQDQMELQPDAWWKLFGNKFDSTQFSKDLETIQNYYLDRGYAKAQIVDNDVQLNDEKTEARVTINVSEGEKYTVNGARIVGDVGGMSEQLAPLLKQIHIGEEFHRSDVQAVEDSIKSTLGERGYGSAQVNVQPDFNDDAKTVGLSFVVDAGKRYSVRQIRFEGNTVSADSTLRQEMRQQEGSWLSTDLVELGKVRLDRTGFFETVESRTEPVEGTGDEVDVIYKVKERNTGSINFGVGYGTESGLSYQASIKQDNFLGMGSSLSLAGSRNDYGTSVNLGYNEPYFTKDGVSLGGNIFFENYDNSKNSTSASYARTTYGGNLTLGFPVNENNAYYIGLGYAYNKLKNITPEYNRALYLASLNYNEWTFKSHDYDISFGWNYNSLNRGFLPTKGVKASIGGKVTIPGSDNKYYKLNADVQGFYPLNRDQTWVLSGRLGAAYANGFGGKRLPFYQTYTAGGIGSLRGFAYSAIGPQAIYINPRVNGCSGSGVNVNSSCYNIVNGDIVGGNAMATASVELIVPTPFVAEKNQNSVRTSFFVDAASVWDTHWKGEKAKFTNLKLPDYGDPSRVRASAGLAFQWQSPIGPLVFSYAKPIKKYENDDIEQFQFSIGGSF","415711","","protective surface antigen D-15, 85 -kilodalton outermembrane protein","Outer membrane, Extracellular","","
InterPro
IPR000184
Family
Bacterial surface antigen (D15)
PTHR12815\"[447-663]T\"[689-803]TSORTING AND ASSEMBLY MACHINERY (SAM50) PROTEIN
PF01103\"[446-803]TBac_surface_Ag
InterPro
IPR010827
Repeat
Surface antigen variable number
PF07244\"[23-90]T\"[91-171]T\"[174-260]T\"[263-342]T\"[345-419]TSurf_Ag_VNR
noIPR
unintegrated
unintegrated
signalp\"[1-20]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","BeTs to 16 clades of COG0729COG name: Predicted outer membrane proteinFunctional Class: MThe phylogenetic pattern of COG0729 is ------yqvd---cefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit (1.4e-294) to 12/12 blocks of the IPB000184 family, which is described as \"Bacterial surface antigen (D15)\". Interpro entry for IP:IPR000184. IPB000184A 3-27 5.4e-08 IPB000184B 44-76 5.8e-15 IPB000184C 78-114 9.5e-19 IPB000184D 115-157 6.9e-25 IPB000184E 203-246 1.1e-26 IPB000184F 247-286 2.8e-19 IPB000184G 296-340 1.5e-23 IPB000184H 341-384 5.3e-37 IPB000184I 405-441 9e-32 IPB000184J 442-486 5.2e-34 IPB000184K 501-535 9.4e-22 IPB000184L 555-591 3.8e-21","Residues 231 to 435 match (1e-07) PD:PD296020 which is described as PROTEOME COMPLETE OUTER MEMBRANE EXPORTED SIGNAL PRECURSOR CC1603 ATU2615 VC2548 ","","","","","","","","","","","","Tue Jan 14 08:17:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00608 is paralogously related to AA00960 (6e-07).","","","","","","Residues 436 to 803 (E-value = 2.3e-67) place AA00608 in the Bac_surface_Ag family which is described as Surface antigen (PF01103)","","","","","Thomas,K.L., Leduc,I., Olsen,B., Thomas,C.E., Cameron,D.W.and Elkins,C. Cloning, overexpression, purification, and immunobiologyof an 85-kilodalton outer membrane protein from Haemophilus ducreyi Infect. Immun. 69 (7), 4438-4446 (2001) PubMed: 11401984 Manning DS, Reschke DK, Judd RC. Omp85 proteins of Neisseria gonorrhoeae and Neisseria meningitidis are similar to Haemophilus influenzae D-15-Ag and Pasteurella multocida Oma87. Microb Pathog. 1998 Jul;25(1):11-21. PMID: 9705245 Flack FS, Loosmore S, Chong P, Thomas WR. The sequencing of the 80-kDa D15 protective surface antigen of Haemophilus influenzae. Gene. 1995 Apr 14;156(1):97-9. PMID: 7737523 Ruffolo,C.G. and Adler,B. Cloning, sequencing, expression, and protective capacity of the oma87 gene encoding the Pasteurella multocida 87-kilodalton outer membrane antigen. Infect. Immun. 64(8): 3161-3167, 1996. PubMed: 8757848. Loosmore,S.M., Yang,Y.P., Coleman,D.C., Shortreed,J.M., England,D.M. and Klein,M.H. Outer membrane protein D15 is conserved among Haemophilus influenzae species and may represent a universal protective antigen against invasive disease. Infect. Immun. 65(9): 3701-3707, 1997. PubMed: 9284140.","","Fri Dec 13 15:23:34 2002","1","","","" "AA00609","415815","416387","573","ATGAAAAAAATCGTAAAACTTACCGCACTTTCTTTGGCCTTAGCTTTCTCTTCTTTAGCCATGGCTGACGAAAACATTGCATTTATTAGCGCAGAGTACCTTTTCCAAAATCACCCTGATCGCAAAGCGGTAGCAGAAAAATTAGAAGCCGAATTTAAACCGACCGCAGATAAATTAGCAGAAAACAAAAAACAAATTGATACCAAGATCGCCGATATTCAGAAAAAAGTAGAAGCGAAAGTGGCTGCATTACAAAAAGATGCGCCGAAATTGCGTTCTGCCGACATCAAAAAGCGTGAAGATGAAATCAATAAATATGGCAACGACCAGCAAGAGGAAATTAATAAATTAATCGCCGAACATGATCAAAAAGCAAAAGAATTCCAAGAGAACTATGCTAAACGTGAAAATGAGGAAACTGAAAAATTAGTCGCCAGTATTCAAGCCGCGACTAACAATGTCGCGAAACAAAAAAATTATACGTTAGTGCTTGATGATCGTTCCGTTGTCTATGGTATGGATGGTAAAAACATCACCGAAGAAGTGTTAAAAGCAATTCCGGCACAGGCTAAA","","","21476","MKKIVKLTALSLALAFSSLAMADENIAFISAEYLFQNHPDRKAVAEKLEAEFKPTADKLAENKKQIDTKIADIQKKVEAKVAALQKDAPKLRSADIKKREDEINKYGNDQQEEINKLIAEHDQKAKEFQENYAKRENEETEKLVASIQAATNNVAKQKNYTLVLDDRSVVYGMDGKNITEEVLKAIPAQAK","416389","","outer membrane protein","Periplasm, Outer membrane","","
InterPro
IPR005632
Family
Outer membrane chaperone Skp (OmpH)
PF03938\"[9-187]TOmpH
noIPR
unintegrated
unintegrated
G3DSA:3.30.910.20\"[21-187]TG3DSA:3.30.910.20
SSF111384\"[21-187]TSSF111384


","BeTs to 6 clades of COG2825COG name: Outer membrane proteinFunctional Class: MThe phylogenetic pattern of COG2825 is -------qvd----efgh-n---it-Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","Tue Jan 14 09:37:34 2003","Tue Jan 14 09:31:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00609 is paralogously related to AA02832 (2e-04) and AA01922 (0.001).","","","","","","Residues 1 to 187 (E-value = 4.1e-47) place AA00609 in the OmpH family which is described as Outer membrane protein (OmpH-like) (PF03938)","","","","","","","","1","","","" "AA00610","416390","417409","1020","ATGAGAACTTATTCTCTTTCTGAATTAGCACAGCAAATCGGCGCTACCATTCGTGGTAACGCCGATGTTGTTGTTAGCAATATTGCCCCTTTAGACAAGGCAAACGAACGGCAACTGACCTTTATTTCTAATGTCAAATTCCGAGAACTATTGGTGCAGTCGAAAGCGGGAATTTTGGTGGTTTCCGAAGCGGATGTGGAATTTTGCTCTCCGGACAGCAACCTGCTTATTGTTAAAGACCCTTATGTCGCCTATGCCAAACTGGCGCAATATATGGATACCACCCCTAAAGCGGCGAGTGGCATCGCCAAAAGTGCGGTCATTGCTGAAGGCGTTTTTCTTGGTGAAAATGTGTCCATCGGCGCTAATGCGGTGATTGAATCCGGCGTGGAATTGGGGGATAACGTAGTGATAGGCGCCAATTGCTTTGTGGGTAAAAACACAAAAATCGGTGCAAATACCCAACTTTGGGCGAATGTCTCCGTGTATCACGACGTACAAATCGGTCAGCATTGCCTGATTCAATCCGGCGCGGTGATTGGCAGTGACGGTTTCGGTTACGCCAATGAACGCGGCAAATGGATTAAAATCCCGCAGGTGGGGCAGGTAATTATCGGCAATAACGTGGAAATCGGCGCTTGCACCTGTATCGACCGCGGCGCCTTGGATGCCACGGTGATTGAAGATAACGTGATCATCGATAACCTGTGCCAAATCGCCCATAATGTGCATATCGGTACCGGCACGGCAGTGGCGGGCGGTGTGATTATGGCGGGCAGCCTGACGGTCGGTCGCTATTGTTTAATCGGTGGTGCCAGTGTGATTAATGGTCACATGGAAATCTGCGATCAAGTGACGATTACCGGCATGGGCATGGTGATGCGTCCGATTACCGAACCGGGCGTGTATTCTTCCGGTATTCCATTGCAAACCAACAAAGAATGGCGTAAAACCGCTGCATTGACGCTGGGTATTGACGGATTGAATAAGCGCATCAAGGCATTAGAAAAAAAAGTAAAA","","","35872","MRTYSLSELAQQIGATIRGNADVVVSNIAPLDKANERQLTFISNVKFRELLVQSKAGILVVSEADVEFCSPDSNLLIVKDPYVAYAKLAQYMDTTPKAASGIAKSAVIAEGVFLGENVSIGANAVIESGVELGDNVVIGANCFVGKNTKIGANTQLWANVSVYHDVQIGQHCLIQSGAVIGSDGFGYANERGKWIKIPQVGQVIIGNNVEIGACTCIDRGALDATVIEDNVIIDNLCQIAHNVHIGTGTAVAGGVIMAGSLTVGRYCLIGGASVINGHMEICDQVTITGMGMVMRPITEPGVYSSGIPLQTNKEWRKTAALTLGIDGLNKRIKALEKKVK","417411","","UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acetyltransferase","Cytoplasm","","
InterPro
IPR001451
Repeat
Bacterial transferase hexapeptide repeat
PF00132\"[111-128]T\"[129-146]T\"[147-164]T\"[165-182]T\"[202-219]T\"[224-241]T\"[242-259]T\"[266-283]THexapep
PS00101\"[102-130]T\"[132-160]T\"[227-255]THEXAPEP_TRANSFERASES
InterPro
IPR007691
Family
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD
PF04613\"[21-92]TLpxD
TIGR01853\"[8-332]Tlipid_A_lpxD: UDP-3-O-[3-hydroxymyristoyl]
noIPR
unintegrated
unintegrated
G3DSA:2.160.10.10\"[113-310]Tno description
PTHR22572\"[106-183]TSUGAR-1-PHOSPHATE GUANYL TRANSFERASE
PTHR22572:SF7\"[106-183]TEUKARIOTIC TRANSLATION INITIATION FACTOR 2B, EPSILON SUBUNIT


","No hits to the COGs database.","Significant hit ( 5.5e-14) to 1/1 blocks of the IPB001451 family, which is described as \"Bacterial transferase hexapeptide repeat\". Interpro entry for IP:IPR001451. IPB001451 114-149 5.4e-14 IPB001451 126-161 3.7e-08 IPB001451 132-167 3.7e-08 IPB001451 120-155 1.7e-07 IPB001451 108-143 3.1e-07 IPB001451 102-137 1.5e-06 IPB001451 227-262 3.6e-05 IPB001451 245-280 0.00048 IPB001451 138-173 0.0006 IPB001451 263-298 0.0011 IPB001451 96-131 0.0018 IPB001451 144-179 0.002 IPB001451 221-256 0.0029 IPB001451 233-268 0.0056 IPB001451 150-185 0.024 IPB001451 239-274 0.057 IPB001451 156-191 0.31","Residues 102 to 151 match (1e-10) PD:PD565891 which is described as COMPLETE ACYLTRANSFERASE PROTEOME LIPID UDP-N-ACETYLGLUCOSAMINE TRANSFERASE PYROPHOSPHORYLASE BIOSYNTHESIS A REPEAT ","","","","","","","","","","","","Fri Dec 13 15:29:39 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00610 is paralogously related to AA00612 (3e-14), AA01539 (8e-07), AA00519 (7e-04) and AA02000 (0.001).","","","","","","Residues 4 to 104 (E-value = 2.3e-49) place AA00610 in the LpxD family which is described as UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD (PF04613)","","","","","Dicker,I.B. and Seetharam,S. Cloning and nucleotide sequence of the firA gene and the firA200(Ts) allele from Escherichia coli J. Bacteriol. 173 (1), 334-344 (1991) M:91100302 Dicker,I.B. and Seetharam,S. What is known about the structure and function of the Escherichia coli protein FirA? Mol. Microbiol. 6 (7), 817-823 (1992) PubMed: 1602961 Vuorio,R. and Vaara,M. Mutants carrying conditionally lethal mutations in outer membrane genes omsA and firA (ssc) are phenotypically similar, and omsA is allelic to firA J. Bacteriol. 174 (22), 7090-7097 (1992) PubMed: 1429432 Helander,I.M., Lindner,B., Seydel,U. and Vaara,M. Defective biosynthesis of the lipid A component of temperature-sensitive firA (omsA) mutant of Escherichia coliEur. J. Biochem. 212 (2), 363-369 (1993) PubMed: 8444173 Kelly,T.M., Stachula,S.A., Raetz,C.R. and Anderson,M.S. The firA gene of Escherichia coli encodes UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase. The third step of endotoxin biosynthesis J. Biol. Chem. 268 (26), 19866-19874 (1993) PubMed: 8366125 ","","Fri Jan 24 11:47:31 2003","1","","","" "AA00611","417507","417956","450","GTGACTGAACAAAACTCAAGAATTATCGAATCACACGAAATAATGCAATTATTGCCCCATCGTTATCCATTTTTATTAGTTGATCGCGTGATTAACTTTGAAGAAGGTAAATGGTTAACTGCAATTAAGAATATTAGCGTAAACGAGCCCTGTTTTACCGGGCACTTCCCGGATAATCCGATTTTACCGGGGGTGTTAATTCTTGAAGCCTTGGCACAAGCTATGGGCATTTTGGCATTTAAAACCCATGAATTGGTAGGTGGCGAAATTTTCTATTTCGCCGGTGTAGATGAAGCCCGCTTTAAACGTCCGATTATTCCGGGCGATCAAATGGTATTACACGTTGAAGTCATTAAAGAACGTCGCGGTATTACCGCGTTCACGGCAACCGCAACCGTCGATGGTGAAGTGGCTTGCGAAGCGAAGTTAATGTGTGCCCGCCGTGTAGCA","","","16757","VTEQNSRIIESHEIMQLLPHRYPFLLVDRVINFEEGKWLTAIKNISVNEPCFTGHFPDNPILPGVLILEALAQAMGILAFKTHELVGGEIFYFAGVDEARFKRPIIPGDQMVLHVEVIKERRGITAFTATATVDGEVACEAKLMCARRVA","417958","From GenBank (gi:1169597):This protein is involved in saturated fatty acid biosynthesis.","(3R)-hydroxymyristoyl-acyl carrier protein dehydrase","Cytoplasm","","
InterPro
IPR010084
Domain
Beta-hydroxyacyl-(acyl-carrier-protein) dehydratase FabZ
TIGR01750\"[9-147]TfabZ: beta-hydroxyacyl-(acyl-carrier-protei
InterPro
IPR013114
Domain
Beta-hydroxyacyl-(acyl-carrier-protein) dehydratase, FabA/FabZ
PF07977\"[18-142]TFabA
noIPR
unintegrated
unintegrated
PD838104\"[25-144]TFABA_WIGBR_Q8D2Q4;
G3DSA:3.10.129.10\"[10-146]Tno description


","BeTs to 15 clades of COG0764COG name: 3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratasesFunctional Class: IThe phylogenetic pattern of COG0764 is -------qvd-lbcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.7e-78) to 3/3 blocks of the IPB001143 family, which is described as \"Bacterial thioester dehydrase\". Interpro entry for IP:IPR001143. IPB001143A 13-26 2.2e-10 IPB001143B 29-82 3.8e-39 IPB001143C 91-133 1.2e-26","Residues 9 to 37 match (3e-07) PD:PD486284 which is described as LIPID DEHYDRATASE 3R-HYDROXYMYRISTOYL-ACYL CARRIER PROTEOME COMPLETE LYASE A 4.2.1.- ACP ","","","","","","","","","","","Wed Feb 26 09:24:28 2003","Fri Dec 13 15:32:45 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00611 is paralogously related to AA02269 (6e-06) and AA01193 (4e-05).","","","","","","Residues 53 to 141 (E-value = 5.5e-20) place AA00611 in the 4HBT family which is described as Thioesterase superfamily (PF03061)","","","","","Mohan,S., Kelly,T.M., Eveland,S.S., Raetz,C.R. and Anderson,M.S. An Escherichia coli gene (FabZ) encoding (3R)-hydroxymyristoylacyl carrier protein dehydrase. Relation to fabA and suppressionof mutations in lipid A biosynthesis J. Biol. Chem. 269 (52), 32896-32903 (1994) PubMed: 7806516 Heath RJ, Rock CO. Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier proteindehydratases in Escherichia coli fatty acid biosynthesis. J Biol Chem. 1996 Nov 1;271(44):27795-801. PMID: 8910376Clements JM, Coignard F, Johnson I, Chandler S, Palan S, Waller A, Wijkmans J, Hunter MG.Antibacterial activities and characterization of novel inhibitors of LpxC.Antimicrob Agents Chemother. 2002 Jun;46(6):1793-9.PMID: 12019092Steeghs L, Jennings MP, Poolman JT, van der Ley P.Isolation and characterization of the Neisseria meningitidis lpxD-fabZ-lpxA gene cluster involved in lipid A biosynthesis.Gene. 1997 May;190(2):263-70.PMID: 9197543","","Wed Feb 26 09:24:28 2003","1","","","" "AA00612","417980","418765","786","ATGATTCACCCAACTGCAAAAATTCATCCTCAGGCGATCGTTGAAGAAGGCGCTAAAATCGGCGAGAACGTGGTCATCGGTCCTTTTACCATTATCGGTAAAGATGCAAAAATCGGTAAAGGTACCGTTATTCATTCCCATGTTGTGATTAACGGCAACACTAAAATCGGCGAAGATAATGAAATTTATCAGTTCGCCAGTATCGGTGAAGTGAACCAGGACTTGAAATATCAAGGTGAACCGACCCGCGTAGTGATCGGCAACCGTAACCGCATTCGTGAAAGTGTGACTATTCATCGCGGTACGGCACAAGGCGGTGGTGTGACGAAAATCGGCGACGACAATTTACTCATGATTAACGTGCATATTGCGCACGATTGTCTGATAAAAAACCGTTGTATTTTAGCCAATAATGCTACGCTTGCCGGCCATGTGCAACTGGATGATTTTGTTGTTGTGGGAGGCATGTCCGCAATTCACCAATTTGTGGTTATCGGTGCGCATGTGATGTTGGGTGGTGGTTCTATGGTCAGCCAGGATGTCCCGCCGTATGTGATGGCACAAGGTAATCATGCACAACCGTTCGGCGTGAACATTGAAGGTTTGAAACGTCGTGGTTTTGATAAGTTAACCATGCGTACTATTCGTAATGTGTACAAAATGATTTACCGTAGTGGGAAAACATTAGAAGAAGTGATGCCGGAAATTGAGCAAATTGCCGAGACCGAATCGGCCATAAGCTTTTTCGTTGAGTTTTTCAAGCGTTCAAAACGCGGCATTATTCGC","","","31034","MIHPTAKIHPQAIVEEGAKIGENVVIGPFTIIGKDAKIGKGTVIHSHVVINGNTKIGEDNEIYQFASIGEVNQDLKYQGEPTRVVIGNRNRIRESVTIHRGTAQGGGVTKIGDDNLLMINVHIAHDCLIKNRCILANNATLAGHVQLDDFVVVGGMSAIHQFVVIGAHVMLGGGSMVSQDVPPYVMAQGNHAQPFGVNIEGLKRRGFDKLTMRTIRNVYKMIYRSGKTLEEVMPEIEQIAETESAISFFVEFFKRSKRGIIR","418767","From Genbank (gi:1170826):This protein is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysacheride to the outer membrane of the cell.","acyl-(acyl-carrier-protein)-UDP-N-acetylglucosamine","Cytoplasm","","
InterPro
IPR001451
Repeat
Bacterial transferase hexapeptide repeat
PF00132\"[17-34]T\"[35-52]T\"[53-70]T\"[83-100]T\"[108-125]T\"[126-143]T\"[150-167]THexapep
PS00101\"[135-163]?HEXAPEP_TRANSFERASES
InterPro
IPR010137
Family
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
PIRSF000456\"[5-262]TAcyl-[acyl-carrier-protein]:UDP-N-acetylglucosamine O-acyltransferase
TIGR01852\"[8-261]Tlipid_A_lpxA: acyl-[acyl-carrier-protein]--
noIPR
unintegrated
unintegrated
G3DSA:1.20.1180.10\"[197-262]Tno description
G3DSA:2.160.10.10\"[5-197]Tno description
PTHR23416\"[109-199]TSIALIC ACID SYNTHASE-RELATED
PTHR23416:SF7\"[109-199]TNEUD PROTEIN


","No hits to the COGs database.","Significant hit ( 2.8e-12) to 1/1 blocks of the IPB001451 family, which is described as \"Bacterial transferase hexapeptide repeat\". Interpro entry for IP:IPR001451. IPB001451 147-182 2.7e-12 IPB001451 14-49 5.3e-10 IPB001451 20-55 8.2e-09 IPB001451 8-43 1.2e-07 IPB001451 2-37 2.4e-07 IPB001451 26-61 5.3e-07 IPB001451 32-67 4.5e-06 IPB001451 129-164 1.5e-05 IPB001451 38-73 0.035 IPB001451 111-146 0.054 IPB001451 105-140 0.41","Residues 137 to 192 match (1e-09) PD:PD013088 which is described as TRANSFERASE COMPLETE PROTEOME ACETYLTRANSFERASE ACYLTRANSFERASE SERINE REPEAT BIOSYNTHESIS A 2.3.1.- ","","","","","","","","","","","Fri Jan 24 11:27:03 2003","Fri Dec 13 15:36:04 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00612 is paralogously related to AA00610 (2e-14), AA02000 (1e-05) and AA01539 (1e-04).","","","","","","","","","","","Servos,S., Khan,S. and Maskell,D. Cloning and expression of genes encoding lipid A biosynthesis from Haemophilus influenzae type b Gene 175 (1-2), 137-141 (1996) M:97074663 Coleman,J. and Raetz,C.R. First committed step of lipid A biosynthesis in Escherichia coli: sequence of the lpxA gene J. Bacteriol. 170 (3), 1268-1274 (1988) M:88139188 Crowell,D.N., Reznikoff,W.S. and Raetz,C.R. Nucleotide sequence of the Escherichia coli gene for lipid A disaccharide synthase J. Bacteriol. 169 (12), 5727-5734 (1987) M:88058790 Steeghs L, Berns M, ten Hove J, de Jong A, Roholl P, van Alphen L, Tommassen J, van der Ley P.Expression of foreign LpxA acyltransferases in Neisseria meningitidis results in modified lipid A with reduced toxicity and retained adjuvant activity.Cell Microbiol. 2002 Sep;4(9):599-611.PMID: 12390352Souther SG, Vistnes LM.The intestine and the delay phenomenon--A preliminary report.J Surg Res. 1975 Jun;18(6):619-22.PMID: 1127922","","Fri Jan 24 11:27:03 2003","1","","","" "AA00613","418853","420034","1182","ATGTCAGATTTCATTGCAACAAAGGATTCCCCGCTTATCGCCCTCACTGCCGGCGAAGTGTCCGGCGACATTCTCGGCGCCGGTTTGATTAAATCCCTCAAAGTGCGTTATCCCAATGCCTGTTTTATCGGCATCGGCGGACCACGCATGATTGCGGCAGGCTTTGAAAGCCTGTTTGATATGGAAGAACTTTCCGTTATGGGTTTGGTGGAAGTACTTAAGCATCTGCCGCGCCTGCTGAAAATTCGCCGCCGTATTATTCAACAATTATTGGCGTTAAAGCCGGATGTGTTTATCGGCATCGACGCACCGGATTTTAATCTGGATGTGGAGCTTAAACTCAAACAAAACGGCATTAAAACCATTCATTACGTCAGCCCGTCGGTGTGGGCGTGGCGTCAGAAACGCGTGTATAAAATCGGTGCGGCAACCAATTTGGTGCTTGCGTTTTTGCCTTTTGAGAAAGCCTTTTACGATCGCTTTAACGTGCCTTGCCGTTTTATCGGGCACACCATGGCAGACGCCATTCCGTTGAAACCGAATCGCGCGGAAGCCTGCCGTTTGCTCAATCTGGACGAAAACCAACATTATCTTGCTATCCTCGTTGGCAGCCGCAGTAGTGAAGTGGAATTTCTTGCCGAACCTTTTTTGCAAACCGCCCAATTATTGCGCCAACGTTATCCTGATTTACAATTTCTGGTGCCGTTAATTAACGCCAAGCGCCGTCAGCAATTTGAACAAATCAAACAACGCGTGGCACCGGATTTAGATGTTATCCTGTTAGACGGCAATGCCCGCGCCGCCATGATTGCCGCCAAAGCAACCTTACTCGCGTCAGGCACGGCGGCATTAGAGGCGATGTTATGCAAATCACCGATGGTGGTGGGCTATCGCATGAAGCCGTTCACGTATTTCCTGGTGAAATGTTTGGTGAAAATCAAGTATATTTCCCTGCCGAATCTGCTGGCGGATGAAATGTTGGTGCCGGAGCTAATTCAGGCAGAATGTAATCCGACTAATTTGGTGGAAAAACTGTCGGTATATTTGGATACAGATGAAAGTACGGTCAAAAATCGCAACATTTTAATTCAACGTTTCACCGAGTTGCACAAAATGATTCAATGCGATGCCGATCAACAGGCAGCACAGTCGGTGATTGATTTACTGGAGCAGAAAAATGGA","","","44215","MSDFIATKDSPLIALTAGEVSGDILGAGLIKSLKVRYPNACFIGIGGPRMIAAGFESLFDMEELSVMGLVEVLKHLPRLLKIRRRIIQQLLALKPDVFIGIDAPDFNLDVELKLKQNGIKTIHYVSPSVWAWRQKRVYKIGAATNLVLAFLPFEKAFYDRFNVPCRFIGHTMADAIPLKPNRAEACRLLNLDENQHYLAILVGSRSSEVEFLAEPFLQTAQLLRQRYPDLQFLVPLINAKRRQQFEQIKQRVAPDLDVILLDGNARAAMIAAKATLLASGTAALEAMLCKSPMVVGYRMKPFTYFLVKCLVKIKYISLPNLLADEMLVPELIQAECNPTNLVEKLSVYLDTDESTVKNRNILIQRFTELHKMIQCDADQQAAQSVIDLLEQKNG","420036","","lipid-A-disaccharide synthase","Cytoplasm, Inner membrane","","
InterPro
IPR003835
Family
Glycosyl transferase, family 19
PF02684\"[13-385]TLpxB
TIGR00215\"[6-388]TlpxB: lipid-A-disaccharide synthase


","BeTs to 12 clades of COG0763COG name: Lipid A disaccharide synthetaseFunctional Class: MThe phylogenetic pattern of COG0763 is -------q-----cefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 6.2e-48) to 2/2 blocks of the IPB003835 family, which is described as \"Lipid-A-disaccharide synthetase\". Interpro entry for IP:IPR003835. IPB003835A 24-78 8e-33 IPB003835B 120-136 7.2e-14","Residues 13 to 121 match (5e-32) PD:PD231234 which is described as LIPID COMPLETE PROTEOME SYNTHASE LIPID-A-DISACCHARIDE GLYCOSYLTRANSFERASE TRANSFERASE A SYNTHESIS BIOSYNTHESIS ","","","","","","","","","","","","Fri Dec 13 15:37:44 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00613 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 13 to 385 (E-value = 1.3e-195) place AA00613 in the LpxB family which is described as Lipid-A-disaccharide synthetase (PF02684)","","","","","Servos,S., Khan,S. and Maskell,D. Cloning and expression of genes encoding lipid A biosynthesis from Haemophilus influenzae type b Gene 175 (1-2), 137-141 (1996) M:97074663 Crowell,D.N., Reznikoff,W.S. and Raetz,C.R. Nucleotide sequence of the Escherichia coli gene for lipid A disaccharide synthase J. Bacteriol. 169 (12), 5727-5734 (1987) M:88058790 Coleman,J. and Raetz,C.R. First committed step of lipid A biosynthesis in Escherichia coli: sequence of the lpxA gene J. Bacteriol. 170 (3), 1268-1274 (1988) M:88139188 ","","Fri Dec 13 15:37:44 2002","1","","","" "AA00614","420030","420626","597","ATGGATAAATTTACCTATCCCCAAGGCTATGAACTGATTGCCGGTGTAGATGAAGTAGGGCGAGGTCCTTTGGTGGGAGCAGTAGTGACGGCGGCGGTGATTTTGGATCCGAAGCAGCCTATTGAAGGGCTGGCGGATTCCAAAACACTCTCGGAAAAGAAACGGTTATTACTGGCAGAAGAAATTAAGCAAAAAGCGTTGGCATGGGCGCTCGGGCGGGCGGAACCGCATGAAATCGACGAATTGAATATTTTACATGCGTCCATGCTTGCCATGGAGCGGGCGATAAAACACCTGAAAATTCGACCGCACTTTGTGTTGGTGGATGGCAATCGGATTCCGCCGAATCTCATGATTCCCGCGCAAGCCGTTGTCAAAGGGGATGTGTTGGTGCCGGAAATCAGCGCGGCGTCTATTTTGGCAAAAGTGGCGCGCGATCAGGAAATGATAGTGCTGGATAAAAAATATCCGCACTATGCATTTGCTAAGCACAAAGGCTATCCCACCAAGCTACATTTGGAAAAATTAAGGGAATTTGGCGTGCTGCCGGAATACCGCCGCAGTTTTGCACCTGTTAAAAAATTACTAAAATCGCTA","","","23112","MDKFTYPQGYELIAGVDEVGRGPLVGAVVTAAVILDPKQPIEGLADSKTLSEKKRLLLAEEIKQKALAWALGRAEPHEIDELNILHASMLAMERAIKHLKIRPHFVLVDGNRIPPNLMIPAQAVVKGDVLVPEISAASILAKVARDQEMIVLDKKYPHYAFAKHKGYPTKLHLEKLREFGVLPEYRRSFAPVKKLLKSL","420628","","ribonuclease HII (RNase HII)","Cytoplasm","","
InterPro
IPR001352
Family
Ribonuclease HII/HIII
PTHR10954\"[1-192]TRIBONUCLEASE HII
PF01351\"[14-192]TRNase_HII
noIPR
unintegrated
unintegrated
G3DSA:3.30.420.10\"[12-154]Tno description


","No hits to the COGs database.","Significant hit ( 1.8e-34) to 4/4 blocks of the IPB001352 family, which is described as \"Ribonuclease HII\". Interpro entry for IP:IPR001352. IPB001352A 15-29 9e-09 IPB001352B 46-55 0.00034 IPB001352C 126-146 3.8e-11 IPB001352D 166-180 1.9e-05","Residues 66 to 119 match (5e-07) PD:PD544045 which is described as HII PROTEOME COMPLETE RIBONUCLEASE ","","","","","","","","","","","","Fri Dec 13 15:40:04 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00614 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 14 to 192 (E-value = 1.7e-84) place AA00614 in the RNase_HII family which is described as Ribonuclease HII (PF01351)","","","","","Itaya,M. Isolation and characterization of a second RNase H (RNase HII) of Escherichia coli K-12 encoded by the rnhB gene Proc. Natl. Acad. Sci. U.S.A. 87 (21), 8587-8591 (1990) PubMed: 2172991 Ohtani,N., Haruki,M., Morikawa,M., Crouch,R.J., Itaya,M. and Kanaya,S. Identification of the genes encoding Mn2+-dependent RNase HII and Mg2+-dependent RNase HIII from Bacillus subtilis: classification ofRNases H into three families Biochemistry 38 (2), 605-618 (1999) PubMed: 9888800 ","","Fri Dec 13 15:40:04 2002","1","","","" "AA00615","420669","422102","1434","ATGAGTCAAATCTCTCATTTCTTCAATTCATTCCAACCGGAACCGTGGTTATGGGTTGTTTTGTTGCTGATTGCCGCCGTCATTCTTTTCATTCGCAATCACATCCGCATGGACATTGTCGCCGTGTTGGTGATGTTAGCTTTCAGCCTCAGCGGCATTTTGACTGTTGAAGAAGTCTTCGCCGGATTCAGTGATCCGAATATCATCTTAATTGCTTTATTGTTTATCGTCGGGGAAGGTCTGGTGCGTACCGGCGTGGCGTATCAAGTGAGTGAATGGTTACTCAAAGCTTCCCATAACAGCGAATCGCGCGTGCTGGTCTTCATGATGCTGGCGGTAGCGGGGCTCGGCGCATTTATGAGTTCTACCGGCGTGGTGGCGATTTTTATTCCTGTGGTATTAATGATTTGCCAGCAAATGAATATTTCGCCCAAACGCCTGATGATGCCGCTCAGCGTGGCAGGCTTGATTAGCGGTATGCTGACCTTAATCGCCACGGCACCGAACTTAGTGGTAAATGCCGAGTTGGTACGGGAAGCCGGTATGCGCCTGAAATTCTTTGATCTCACGCCCATCGGTTTAGTGATTTTGCTCCTTGGCATCGGTTATATGCTAGTGGCGCGCCGTTGGCTGAAATCCGGCACCAAAGCCGATAATAACAAGCTGGATAAACGTTCCATAAGTGATTTGATCCATGAGTACGGCTTGCAACTGCGGGCGCAACGTTTCGTGGTGAAAAAAGGTTCCGCGATTATCGGTAAAAATCTGGATGAATTGCATTTACGTTCCAAATATGGTTTGAATGTGTTGGCGATTGAACGCTGGAAGCGTTTTCGTCCGCTGTTTATTGCGGCGCTGGGAACGTCTGAAGTGCGTGAAAAAGACATTCTGTTGATGGACATCAGCGATCCCGAATTAGACATAGAAACCTTTTGTACGGAATATAACCTGGAACGGGCAGAAATTCGTGCGCAGTATTTTTCCGAACAAGCCAGTTCCATCGGCATGGCAGAATTGATTTTGGTGCCGAATTCCGATTGTATCGGTAAATCCACCGAACAGTTACGCTTCCGTTCCAAATACGACTTAAATGTGGTGGGTATCAAACGTGATGGCGAGGTGTTGGACGGGCATTTTGTCGAAATGCCGTATAAAGCCGGTGATTTGTTGCTAGTCGTCGGTGACTGGAAACTAATTCAGCAAATGCGTAGCCACAGCAAAGACTTCTTCGTGTTGAATTATCCGAGCGAAATTACCCGTGCCGTACCCGCGCAAAGCCAAGCGCCTTATGCGTTACTCAGCATTGCGGTAATGGTGTTGTTAATGGTTATGGGCGAACCGTTATTTTATCGTGACGATGAAAACAAAGCCGCATTTTTAACCCGTGCCGAGCAGGCGTTGTTAAGTTTGAATGTAACCGAAAAAGGGAGAGCA","","","53605","MSQISHFFNSFQPEPWLWVVLLLIAAVILFIRNHIRMDIVAVLVMLAFSLSGILTVEEVFAGFSDPNIILIALLFIVGEGLVRTGVAYQVSEWLLKASHNSESRVLVFMMLAVAGLGAFMSSTGVVAIFIPVVLMICQQMNISPKRLMMPLSVAGLISGMLTLIATAPNLVVNAELVREAGMRLKFFDLTPIGLVILLLGIGYMLVARRWLKSGTKADNNKLDKRSISDLIHEYGLQLRAQRFVVKKGSAIIGKNLDELHLRSKYGLNVLAIERWKRFRPLFIAALGTSEVREKDILLMDISDPELDIETFCTEYNLERAEIRAQYFSEQASSIGMAELILVPNSDCIGKSTEQLRFRSKYDLNVVGIKRDGEVLDGHFVEMPYKAGDLLLVVGDWKLIQQMRSHSKDFFVLNYPSEITRAVPAQSQAPYALLSIAVMVLLMVMGEPLFYRDDENKAAFLTRAEQALLSLNVTEKGRA","422104","","cation transport protein","Inner membrane, Cytoplasm","","
InterPro
IPR004680
Family
Divalent ion symporter
PF03600\"[20-420]TCitMHS
InterPro
IPR006037
Domain
TrkA-C
PF02080\"[240-316]T\"[336-407]TTrkA_C
PS51202\"[228-317]T\"[324-408]TRCK_C
noIPR
unintegrated
unintegrated
PTHR10283\"[14-168]T\"[255-444]TCATION TRANSPORTER RELATED
PTHR10283:SF12\"[14-168]T\"[255-444]TSODIUM/SULFATE TRANSPORTER
signalp\"[1-29]?signal-peptide
tmhmm\"[15-33]?\"[43-63]?\"[68-86]?\"[105-137]?\"[147-167]?\"[186-206]?\"[430-450]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 4.2e-06) to 3/8 blocks of the IPB001898 family, which is described as \"Sodium:sulfate symporter family\". Interpro entry for IP:IPR001898. IPB001898A 30-53 41 IPB001898C 113-132 12 IPB001898D 147-171 0.003","Residues 396 to 445 match (5e-11) PD:PD407328 which is described as PROTEOME COMPLETE PM1999 ","","","","","","","","","","","","Fri Dec 13 15:50:44 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00615 is paralogously related to AA01784 (4e-10), AA00136 (2e-08), AA00941 (2e-05), AA00080 (1e-04) and AA02387 (6e-04).","","","","","","Residues 336 to 407 (E-value = 1.8e-09) place AA00615 in the TrkA_C family which is described as TrkA-C domain (PF02080)","","","","","","","","1","","","" "AA00616","422105","423031","927","ATGGAAATGTGGAAACTGTTCGGTGGTTTGATGATCACCTTAATTATCGCTTCTTCAATCGGTTACGGTTTAAAACTTAAAGTAGGTTGGTCCACGCCGCACGCTGTGATTGACAACTTAAACACACGCATTAACGCCTGGTGGGTGATGATTTTAATCATCTTCGCCGCTGCCGCCTTGGGTTTTTACGGCATCATCTTTTTATTCTTCGTGATTTCCTTTATGGCATTACGGGAATTTCTCTCGTTGCTTTACATTCGCCGTGGTGACCATTTGGCGCTCGCCGCCTGTTTTTATGTCATCCTGTCCGTGCAATACATTCTGGTGGCAATCGACTGGTTCAGTATGTTCACCATTTTCATTCCGGTGTACGGCTTCCTATTTCTCCCGATCCTCTCCGCCCTGTTGGGCGACACCGCGCATTTCCTGGATCGCTCCACCAAAGTGCAATGGGCGTTGATGATCAGCGTATTTTGTATTTCCCACATTCCTGCCATGCTGACGTTGGATATTGCCGGTTTTGAAGGCAAAAATTTACTGCTGATGATTTTCCTGATTCTGGTGGTGCAGGCGAGCGACGTGTTGCAATATGTGTGGGGCAAATTATTCGGCAAACACAAAATCGCGCCGAAACTGTCGCCATCTAAAACCGTGGAAGGTTTTGTAGGCGGTGTGGTGAGCGCCAGCGTACTAGGCGGTTTACTTTATTGGCTGACGCCGTTTAGCCCGGTGCAAGCGGTGTTAATGAGCTTATTGATTTGCCTGATGGGCTTTTTAGGCGGCTTGGTGATGTCCGCCATGAAACGCAGCATGGGCGTAAAAGACTGGGGCAATATGATTAGCGGGCACGGCGGTATGTTGGATCGCATGGATTCCTTGTGCTTTGCCGCGCCGATTTTCTTCCATGTCGTCAGATATTATTGGACC","","","34460","MEMWKLFGGLMITLIIASSIGYGLKLKVGWSTPHAVIDNLNTRINAWWVMILIIFAAAALGFYGIIFLFFVISFMALREFLSLLYIRRGDHLALAACFYVILSVQYILVAIDWFSMFTIFIPVYGFLFLPILSALLGDTAHFLDRSTKVQWALMISVFCISHIPAMLTLDIAGFEGKNLLLMIFLILVVQASDVLQYVWGKLFGKHKIAPKLSPSKTVEGFVGGVVSASVLGGLLYWLTPFSPVQAVLMSLLICLMGFLGGLVMSAMKRSMGVKDWGNMISGHGGMLDRMDSLCFAAPIFFHVVRYYWT","423033","Synonyms: Phosphatidate cytidylyltransferase (CDP-diglyceride synthetase) (CDP-diglyceride pyrophosphorylase) (CDP-diacylglycerol synthase) (CDS) (CTP:phosphatidatecytidylyltransferase) (CDP-DAG synthase) (CDP-DG synthetase).","phosphatidate cytidylyltransferase","Inner membrane, Cytoplasm","","
InterPro
IPR000374
Family
Phosphatidate cytidylyltransferase
PF01148\"[41-307]TCTP_transf_1
PS01315\"[265-291]TCDS
noIPR
unintegrated
unintegrated
PD002096\"[236-285]TQ9CJK3_PASMU_Q9CJK3;
PTHR13773\"[246-291]TPHOSPHATIDATE CYTIDYLYLTRANSFERASE
signalp\"[1-23]?signal-peptide
tmhmm\"[5-23]?\"[51-71]?\"[92-110]?\"[116-136]?\"[151-173]?\"[179-199]?\"[220-240]?\"[246-266]?transmembrane_regions


","BeTs to 19 clades of COG0575COG name: CDP-diglyceride synthetaseFunctional Class: IThe phylogenetic pattern of COG0575 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 6.3e-26) to 2/2 blocks of the IPB000374 family, which is described as \"Phosphatidate cytidylyltransferase\". Interpro entry for IP:IPR000374. IPB000374A 212-224 3e-06 IPB000374B 265-292 3.6e-18","Residues 180 to 303 match (5e-30) PD:PD002096 which is described as CYTIDYLYLTRANSFERASE PHOSPHATIDATE SYNTHASE CDP-DIGLYCERIDE PROTEOME COMPLETE SYNTHETASE TRANSFERASE NUCLEOTIDYLTRANSFERASE CTP:PHOSPHATIDATE ","","","","","Tue Feb 18 14:33:01 2003","","","","","","Tue Feb 18 14:33:01 2003","Fri Dec 13 16:31:35 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00616 is paralogously related to AA00605 (3e-22).","","","","","","Residues 41 to 307 (E-value = 1.9e-92) place AA00616 in the CTP_transf_1 family which is described as Cytidylyltransferase family (PF01148)","","","","","Weber CH, Park YS, Sanker S, Kent C, Ludwig ML.A prototypical cytidylyltransferase: CTP:glycerol-3-phosphate cytidylyltransferase from bacillus subtilis.Structure Fold Des. 1999 Sep 15;7(9):1113-24.PMID: 10508782 Taguchi K, Fukutomi H, Kuroda A, Kato J, Ohtake H.Cloning of the Pseudomonas aeruginosa gene encoding CDP-diglyceride synthetase.Gene. 1996 Jun 12;172(1):165-6.PMID: 8654980 Icho,T., Sparrow,C.P. and Raetz,C.R.Molecular cloning and sequencing of the gene for CDP-diglyceridesynthetase of Escherichia coliJ. Biol. Chem. 260 (22), 12078-12083 (1985)PubMed: 2995358","","Tue Feb 18 14:33:01 2003","1","","","" "AA00618","423124","423702","579","ATGACCGCACTTTTAAAGATTGGTTTAGTGTCCGTCTCCGATCGGGCGTCACAAGGGATTTATCCGGATCAAGGCATTCCCGAATTGCGCAATTGGCTACAACAGGCGTTGGCGGATTCCTTTGAAGTGGTGGAACGCTTAATTCCCGACGAACAGGCGGAAATCGAACGTACCCTGTGCGAACTGGTGGATGAGCAACATTGTCATTTGGTGCTGACTACCGGCGGCACGGGCCCGGCAAAACGCGACGTGACCCCGGATGCCACCCTTGCCGTCGCCGACCGCGAAATGCCGGGGTTTGGCGAACAAATGCGCCAGGTCAGCCTGCATTTTGTACCGACGGCAATTCTCTCCCGCCAAGTGGGCGTCATTCGCAAAGAAAGCCTCATTTTAAACTTACCCGGACAGCCGAAAGCCATCAAAGAAACGCTGGAAGGGGTAAAAGACAAACAGGGCAACGTTCTGGTCAAAGGGATTTTCAGCGCCGTGCCATACTGTCTGCAACTTATCAACGGCTTATACATAAACACCAAACCCGACGTCATTGTCAGTTTCAGACCCCAATCTGCTTGTCGTGAT","","","21199","MTALLKIGLVSVSDRASQGIYPDQGIPELRNWLQQALADSFEVVERLIPDEQAEIERTLCELVDEQHCHLVLTTGGTGPAKRDVTPDATLAVADREMPGFGEQMRQVSLHFVPTAILSRQVGVIRKESLILNLPGQPKAIKETLEGVKDKQGNVLVKGIFSAVPYCLQLINGLYINTKPDVIVSFRPQSACRD","423704","","molybdopterin biosynthesis protein","Cytoplasm","","
InterPro
IPR001453
Domain
Molybdopterin binding domain
PF00994\"[8-145]TMoCF_biosynth
TIGR00177\"[4-149]Tmolyb_syn: molybdenum cofactor synthesis do
InterPro
IPR008284
Family
Molybdenum cofactor biosynthesis protein
PS01078\"[70-83]TMOCF_BIOSYNTHESIS_1
InterPro
IPR012119
Family
Molybdenum cofactor molybdenum incorporation protein MogA
PIRSF036627\"[5-180]TMolybdenum cofactor molybdenum incorporation protein MogA
noIPR
unintegrated
unintegrated
G3DSA:3.40.980.10\"[5-193]Tno description
PTHR10192\"[4-188]TMOLYBDOPTERIN BIOSYNTHESIS PROTEIN


","BeTs to 17 clades of COG0521COG name: Molybdopterin biosynthesis enzymesFunctional Class: HThe phylogenetic pattern of COG0521 is aompkz-q-dr-b-efgh--uj----Number of proteins in this genome belonging to this COG is","","Residues 3 to 192 match (5e-88) PD:PD405346 which is described as BIOSYNTHESIS COMPLETE PROTEOME COFACTOR MOLYBDENUM MOLYBDOPTERIN MOG B MOAB ENZYME ","","","","","","","","","","","","Fri Dec 13 16:47:32 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00618 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 147 (E-value = 1.9e-39) place AA00618 in the MoCF_biosynth family which is described as Probable molybdopterin binding domain (PF00994)","","","","","Nichols J, Rajagopalan KV.Escherichia coli MoeA and MogA. Function in metal incorporation step of molybdenum cofactor biosynthesis.J Biol Chem. 2002 Jul 12;277(28):24995-5000.PMID: 1200657Langen,H., Takacs,B., Evers,S., Berndt,P., Lahm,H.W., Wipf,B., Gray,C. and Fountoulakis,M. Two-dimensional map of the proteome of Haemophilus influenzae Electrophoresis 21 (2), 411-429 (2000) PubMed: 10675023 Liu,M.T., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H. Crystal structure of the gephyrin-related molybdenumcofactor biosynthesis protein MogA from Escherichia coli J. Biol. Chem. 275 (3), 1814-1822 (2000) PubMed: 10636880 ","","Fri Dec 13 16:54:12 2002","1","","","" "AA00619","424384","424271","114","ATGCTTAAGGAACCCAAAGACAGCAACTTTTCCGACAGCACCACGACTACGTTTACCGTTACGGGCACCACCAAAATAACTTTCATCGGTTTAAATTTCCCCTTCAAACATCAC","","","4273","MLKEPKDSNFSDSTTTTFTVTGTTKITFIGLNFPFKHH","424271","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 09:34:00 2004","Mon Feb 23 09:34:00 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00619 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 09:34:00 2004","","","","","","","","","","","","","1","","","" "AA00620","425322","425753","432","ATGCTTTCAGCACTTATCTCTCCCGCACTTAGCTACCCGGCTATGCGTCTGGCGACACAACCGGAACACCAGCGGTGCGTCCACTCCGGTCCTCTCGTACTAGGAGCAGCCCCAACCAATTCTCCTACGCCCACGGCAGATAGGGACCGAACTGTCTCACGACGTTCTAAACCCAGCTCGCGTACCACTTTAAATGGCGAACAGCCATACCCTTGGGACCTACTTCAGCCCCAGGATGTGATGAGCCGACATCGAGGTGCCAAACACCGCCGTCGATATGAACTCTTGGGCGGTATCAGCCTGTTATCCCCGGAGTACCTTTTATCCGTTGAGCGATGGCCCTTCCATGCAGAACCACCGGATCACTATGACCTACTTTCGTACCTGCCCGACCTGTCCGTCTCGCAGTTAAGCTTGCTTATACCATTGCAC","","","16179","MLSALISPALSYPAMRLATQPEHQRCVHSGPLVLGAAPTNSPTPTADRDRTVSRRSKPSSRTTLNGEQPYPWDLLQPQDVMSRHRGAKHRRRYELLGGISLLSPEYLLSVERWPFHAEPPDHYDLLSYLPDLSVSQLSLLIPLH","425753","","hydrolase","Periplasm","This sequence is similar to gi|27363940, a predicted hydrolase from Vibrio vulnificus. See also gi|29337301 from C. muridarum.","
noIPR
unintegrated
unintegrated
PD293281\"[1-104]TQ8CME1_BBBBB_Q8CME1;


","No hits to the COGs database.","","Residues 1 to 122 match (1e-33) PD:PD293281 which is described as PROTEOME COMPLETE TC0114 ","","","","","","","","","","","","Mon Feb 23 09:38:16 2004","Mon Feb 23 09:38:16 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA1579, AA1489, AA0832, AA0404, AA0273, AA1024, all hypotheticals.AA00620 is paralogously related to AA02296 (8e-83), AA01262 (8e-83), AA00411 (1e-61) and AA01567 (3e-33).","Mon Feb 23 09:38:16 2004","","","","","","","","","","","","","1","","","" "AA00621","429067","428867","201","ATGGCGTATACAGAGGGTAACCAACCAGCGATGGGGAGTGAATCTCAGAAAGTGCGTCTAAGTTCGGATTGGAGTCTGCAACTCGACTCCATGAAGTCGGAATCGCTAGTAATCGCGAATCAGAATGTTGCGGTGAATACGTTCCCGGGCCTTGTACACACCGCCCGTCACACCATGGGAGTGGGTTGTACCAGAAGTGGA","","","7166","MAYTEGNQPAMGSESQKVRLSSDWSLQLDSMKSESLVIANQNVAVNTFPGLVHTARHTMGVGCTRSG","428867","","conserved hypothetical protein","Periplasm","This sequence is similar to gi|27359373, a conserved hypothetical protein from Vibrio vulnificus. See also gi|23015882 from Magnetospirillum magnetotacticum.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 09:42:14 2004","Mon Feb 23 09:42:14 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00621 is paralogously related to AA02297 (7e-35), AA01566 (7e-35), AA01261 (7e-35), AA00412 (7e-35) and AA02421 (2e-27).","Mon Feb 23 09:42:14 2004","","","","","","","","","","","","","1","","","" "AA00622","429832","430164","333","ATGCTATTAACACACCAACCTTCCTCAATACCGAAAGAACTTTACAACCCGAAGGCCTTCTTCATTCACGCGGCATGGCTGCGTCAGGGTTGCCCCCATTGCGCAATATTCCCCACTGCTGCCTCCCGTAGGAGTCCGGGCCGTGTCTCAGTCCCGGTGTGGCTGGCCATCCTCTCAGACCAGCTAGCGATCGTCGGCTTGGTAGGCCCTTACCCCACCAACTACCTAATCACACTTGGGTTCATCTCATGGCATGCGGCCATAAAGTCCCGCACTTTCGTCTCCCGACCCTACGCGGTATTAGCGACAGTTTCCCGTCGTTATCCCCCTCCA","","","12310","MLLTHQPSSIPKELYNPKAFFIHAAWLRQGCPHCAIFPTAASRRSPGRVSVPVWLAILSDQLAIVGLVGPYPTNYLITLGFISWHAAIKSRTFVSRPYAVLATVSRRYPPP","430164","","conserved hypothetical protein","Inner membrane, Cytoplasm","This sequence is similar to gi|27360487, a conserved hypothetical protein from Vibrio vulnificus. See also gi|10039641 from Chlorobium tepidum.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 09:49:49 2004","Mon Feb 23 09:49:49 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00622 is paralogously related to AA02422 (1e-63), AA02298 (1e-63), AA00413 (9e-63), AA01565 (2e-30) and AA01260 (4e-13).","Mon Feb 23 09:49:49 2004","","","","","","","","","","","","","1","","","" "AA00623","430597","430692","96","GTGTTTTCCTTTGAGATAAAAAATTATGGAGATCAAAAAAATGCGGTCAGAAAAACGCTTGAATTTCTGACCGCACTTTTGGCTTTCCGAGTTAAG","","","3729","VFSFEIKNYGDQKNAVRKTLEFLTALLAFRVK","430692","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 09:51:32 2004","Mon Feb 23 09:51:32 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00623 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 09:51:32 2004","","","","","","","","","","","","","1","","","" "AA00625","430905","430705","201","ATGAAAAAACGGGTTCAAATTCTTGGCATCGTGACGTTAGCCGTGGCTTTAACCGGCTGCCATAATTTAAGCAGAACACAAAAGAATACCGCTGTCGGCGCTGCAATCGGTGGTGTTGCCGGTAACGTTATCGGCGGTTCAACCGGTGCCACTTTAGGTGGTGCGGCACTTGGCGGTTTGATTGGAAGCCAAGTGGGCAAA","","","6339","MKKRVQILGIVTLAVALTGCHNLSRTQKNTAVGAAIGGVAGNVIGGSTGATLGGAALGGLIGSQVGK","430707","","hypothetical protein","Periplasm, Outer membrane, Extracellular","","
InterPro
IPR008816
Family
Rickettsia 17 kDa surface antigen
PF05433\"[26-66]TRick_17kDa_Anti
noIPR
unintegrated
unintegrated
PS51257\"[1-20]TPROKAR_LIPOPROTEIN
signalp\"[1-20]?signal-peptide
tmhmm\"[5-25]?\"[31-62]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Fri Dec 13 16:57:59 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00625 is paralogously related to AA00650 (3e-05).","","","","","","","","","","","","","","1","","","" "AA00628","431924","430995","930","ATGGCGAAATTATTAGAGTTATTGGTGAGCGGCGTTGAAAATTCATTGGAAAATCTGACCGCACTTTTAGGCTGTGACGCGCAGCAATTGCAACAGGAAATCCTCCAATTGGAGCAGCAGGGGATATGTTTTGAGGTGGAAAACGGTCATCTTTATTTGATCCCCGAAATGCCGCTATTAGATGAAGCACGTTTGACACAAGCTTTAGCGCCTTATGGCGTAACGCTTAAACCGGTGATTTCCTCGACTAACCAATATTTGTTGGATCACTTGGGACAGTTACAAAAGGGGGATTTATGCTTGGCGGAATATCAAACCACAGGGCGTGGACGCCGTGGCAGACAATGGATTTCACCCTTTGCAGGGCAAATAATCATGAGTTTTTATTGGCAGCTGAATCCAACAAAATCTCTGGATGGATTGAGCTCGGTGATTGGTCTTGCCATTGTTCAAGCATTGGCGGAGTTGGATATGTACGGATTCCAAGTGAAATGGCCGAACGATATTTTAGTTAATGATCGAAAACTGGCGGGTATTCTGGTGGAGATCGTTAATCGCAAAAACGGCATGTTGAATCTGATTGTAGGCATCGGCATGAATATTTCCCTCGGACAGAATAAAAAAATCGATCAACCGTGGGCAGAATTAAGCGAATTTTTCCCGCAGGTTGATCGTGAACAAATTATCATCAAAATGACGAAAACCATTTACCGTTACCTCGAACGTTTTGAACAACACGGCATTGATGCCGAACTGCAACAACAGTGGCTTAATCACGATGCGTATTTCGGCGCGGAGGTCAATGTTATTACGGAAAAAAGTGCGATTTCCGGTACTGAACAAGGCATTGATGCTGCAGGACATTTATGCGTCATTACGGAAAACGGCAGACAATATTTCAACGCCGGAGAAGTGTCCTTACGCAAAAAA","","","34807","MAKLLELLVSGVENSLENLTALLGCDAQQLQQEILQLEQQGICFEVENGHLYLIPEMPLLDEARLTQALAPYGVTLKPVISSTNQYLLDHLGQLQKGDLCLAEYQTTGRGRRGRQWISPFAGQIIMSFYWQLNPTKSLDGLSSVIGLAIVQALAELDMYGFQVKWPNDILVNDRKLAGILVEIVNRKNGMLNLIVGIGMNISLGQNKKIDQPWAELSEFFPQVDREQIIIKMTKTIYRYLERFEQHGIDAELQQQWLNHDAYFGAEVNVITEKSAISGTEQGIDAAGHLCVITENGRQYFNAGEVSLRKK","430997","","biotin operon repressor; biotin acetyl coenzyme A carboxylase synthetase","Cytoplasm","","
InterPro
IPR003142
Domain
Biotin protein ligase, C-terminal
PF02237\"[262-308]TBPL_C
InterPro
IPR004143
Domain
Biotin/lipoate A/B protein ligase
PF03099\"[76-172]TBPL_LipA_LipB
InterPro
IPR004408
Domain
Biotin--acetyl-CoA-carboxylase ligase
TIGR00121\"[73-308]TbirA_ligase: biotin-[acetyl-CoA-carboxylase
noIPR
unintegrated
unintegrated
G3DSA:2.30.30.100\"[262-308]Tno description
G3DSA:3.30.930.10\"[58-261]Tno description
PTHR12835\"[48-300]TBIOTIN PROTEIN LIGASE


","No hits to the COGs database.","Significant hit ( 2.4e-16) to 2/2 blocks of the IPB003142 family, which is described as \"Biotin protein ligase C terminal domain\". Interpro entry for IP:IPR003142. IPB003142A 105-121 1.3e-09 IPB003142B 163-172 4.6e-05","Residues 261 to 309 match (2e-09) PD:PD592185 which is described as BIOTIN LIGASE PROTEOME COMPLETE REPRESSOR BIRA OPERON BIFUNCTIONAL REGULATION DNA-BINDING ","","","","","","","","","","","","Wed Jan 22 17:45:19 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00628 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 262 to 308 (E-value = 9.2e-08) place AA00628 in the BPL_C family which is described as Biotin protein ligase C terminal domain (PF02237)","","","","","Chapman-Smith A, Morris TW, Wallace JC, Cronan JE Jr.Molecular recognition in a post-translational modification of exceptional specificity. Mutants of the biotinylated domain of acetyl-CoA carboxylase defective in recognition by biotin protein ligase.J Biol Chem. 1999 Jan 15;274(3):1449-57.PMID: 9880519Howard,P.K., Shaw,J. and Otsuka,A.J. Nucleotide sequence of the birA gene encoding the biotinoperon repressor and biotin holoenzyme synthetase functions ofEscherichia coli Gene 35 (3), 321-331 (1985) PubMed: 3899863 Buoncristiani,M.R., Howard,P.K. and Otsuka,A.J. DNA-binding and enzymatic domains of the bifunctional biotinoperon repressor (BirA) of Escherichia coli Gene 44 (2-3), 255-261 (1986) PubMed: 3536662 ","","Fri Dec 13 17:04:00 2002","1","","","" "AA00629","432066","433529","1464","ATGGCATTACGCATACAAAAAGAGGCATTGACGTTTGACGACGTTCTTCTCCTGCCCGCTCATTCTACCGTGTTACCGAACACTGCTAATCTTTCCACCCAACTCACTTCCACCATCCGCCTGAACATTCCAATGTTATCCGCCGCCATGGATACTGTGACTGAAGCCAAATTAGCAATTTCATTAGCGCAAGAAGGCGGTATTGGCTTTATTCATAAAAACATGACGATCGAACGCCAGGTGGACCGCGTGCGTAAAGTGAAAAAATTTGAAAGCGGCGTGGTGTCGGATCCGATTACCGTTCCGCCTAATTTAATCATCAGCGAATTAAAAGCCATTGCGCAAAAAAACGGCTTCGCGGGTTATCCCGTGGTAGATGCCGACAACAATTTAGTGGGCATTATTACCGGTCGTGACATTCGTTTCGTATCCAATGTCAATAAAACCGTTGCCGATTTTATGACGCCGAAAGATCGTTTGGTAACCGTTAAAGAAGACGCGCAACGTGAAGAAATTTTCCAACTCATGCACAAACACCGCGTAGAAAAAGTCTTGGTTGTGGATGATAACTTTAAATTGAAAGGCATGATTACCTTAAAAGACTATCAAAAAGCCGAACAAAAACCGAACGCCTGTAAAGACGAATTCGGTCGTTTGCGCGTAGGTGCGGCGGTTGGCGCGGGCGCCAGCAATGAAGAACGTATTGATGCCTTAGTAAAAGCCGGTGTTGACGTACTATTGATCGACTCCTCTCACGGGCATTCCGAAGGCGTATTGCAACGCGTGCGTGAAACCCGCGCGAAATACCCTAACTTACCGATTATTGCGGGCAATATCGCGACAGCCGAAGGTGCCATTGCCTTAGCGGATGCGGGTGCAAGCGCAGTGAAAGTGGGCATCGGCCCGGGGTCAATTTGTACCACCCGTATCGTAACAGGCGTGGGCGTGCCGCAAATTACCGCCATTTCCGACGCCGCAGAAGCATTAAAAGATCGTGGCATTCCAGTCATTGCCGACGGCGGGATTCGTTATTCCAGCGACATCGCCAAAGCCATTGCCGCCGGCGCCAGCTGCGTGATGGTAGGTTCGATGTTTGCCGGCACGGAAGAAGCACCGGGTGAAATTGAATTGTACCAAGGACGTGCGTTCAAATCTTATCGCGGCATGGGCTCCCTCGGCGCCATGGCGAAAGGCTCCAGCGATCGTTATTTCCAATCGGACAACGCGGCGGATAAGCTGGTGCCGGAAGGTATCGAAGGACGCATTCCTTATAAAGGCTTATTGAAAGAAATTATCCATCAACAAATGGGCGGTTTACGCTCCTGCATGGGCTTAACCGGTTGCGCCACCATTGATGAATTACGCACCAAAGCCCAATTTGTGCGCATCAGTGGCGCCGGCATTAAAGAAAGCCATGTACATGATGTGACGATCACTAAAGAAGCACCGAATTACCGCATGAGC","","","52210","MALRIQKEALTFDDVLLLPAHSTVLPNTANLSTQLTSTIRLNIPMLSAAMDTVTEAKLAISLAQEGGIGFIHKNMTIERQVDRVRKVKKFESGVVSDPITVPPNLIISELKAIAQKNGFAGYPVVDADNNLVGIITGRDIRFVSNVNKTVADFMTPKDRLVTVKEDAQREEIFQLMHKHRVEKVLVVDDNFKLKGMITLKDYQKAEQKPNACKDEFGRLRVGAAVGAGASNEERIDALVKAGVDVLLIDSSHGHSEGVLQRVRETRAKYPNLPIIAGNIATAEGAIALADAGASAVKVGIGPGSICTTRIVTGVGVPQITAISDAAEALKDRGIPVIADGGIRYSSDIAKAIAAGASCVMVGSMFAGTEEAPGEIELYQGRAFKSYRGMGSLGAMAKGSSDRYFQSDNAADKLVPEGIEGRIPYKGLLKEIIHQQMGGLRSCMGLTGCATIDELRTKAQFVRISGAGIKESHVHDVTITKEAPNYRMS","433531","","inosine 5' monophosphate dehydrogenase (IMP dehydrogenase)","Cytoplasm","","
InterPro
IPR000644
Domain
Cystathionine-beta-synthase
PF00571\"[92-207]TCBS
SM00116\"[97-145]T\"[159-207]TCBS
InterPro
IPR001093
Family
IMP dehydrogenase/GMP reductase
PTHR11911:SF6\"[1-475]TINOSINE-5-MONOPHOSPHATE DEHYDROGENASE
PF00478\"[8-474]TIMPDH
PS00487\"[296-308]TIMP_DH_GMP_RED
InterPro
IPR005990
Family
IMP dehydrogenase
TIGR01302\"[9-456]TIMP_dehydrog: inosine-5'-monophosphate dehy
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[4-487]Tno description
noIPR
unintegrated
unintegrated
PIRSF000130\"[1-488]TInosine-5'-monophosphate dehydrogenase
PTHR11911\"[1-475]TINOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED


","BeTs to 23 clades of COG0516COG name: IMP dehydrogenase/GMP reductaseFunctional Class: FThe phylogenetic pattern of COG0516 is -ompkzyqvdrlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is","Significant hit (2.2e-104) to 6/6 blocks of the IPB001093 family, which is described as \"IMP dehydrogenase / GMP reductase\". Interpro entry for IP:IPR001093. IPB001093A 10-19 1.6e-05 IPB001093B 36-78 4e-26 IPB001093C 291-322 2.2e-27 IPB001093D 335-374 1.4e-32 IPB001093E 397-406 5.7e-05 IPB001093F 413-424 0.36Significant hit ( 3.5e-07) to 1/6 blocks of the IPB000262 family, which is described as \"FMN-dependent alpha-hydroxy acid dehydrogenases\". Interpro entry for IP:IPR000262. IPB000262F 332-384 3.3e-07Significant hit ( 1.8e-05) to 1/8 blocks of the IPB001295 family, which is described as \"Dihydroorotate dehydrogenase\". Interpro entry for IP:IPR001295. IPB001295H 334-364 1.8e-05 IPB001295H 271-301 0.035","Residues 11 to 71 match (4e-13) PD:PD002050 which is described as PROTEOME COMPLETE DEHYDROGENASE IMP OXIDOREDUCTASE NAD INOSINE-5'-MONOPHOSPHATE BIOSYNTHESIS IMPD ORF ","","","","","","","","","","","","Fri Nov 21 14:22:19 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00629 is paralogously related to AA02749 (4e-04) and AA02171 (8e-04).","","","","","","Residues 154 to 207 (E-value = 6.5e-13) place AA00629 in the CBS family which is described as CBS domain (PF00571)","","","","","Fujio T, Nishi T, Ito S, Maruyama A. High level expression of XMP aminase in Escherichia coli and itsapplication for the industrial production of 5'-guanylic acid. Biosci Biotechnol Biochem. 1997 May;61(5):840-5. PMID: 9178561 Tesfa-Selase F, Drabble WT. Specific binding of DnaA protein to a DnaA box in the guaB gene ofEscherichia coli K12. Eur J Biochem. 1996 Oct 15;241(2):411-6. PMID: 8917437","","Fri Nov 21 14:22:19 2003","1","","","" "AA00631","433818","433988","171","ATGAAAAAAATGCAGATTGAAGTGACTGAAACAACCGACTTTTCACCACAAGCCTTGAAAAAACTCAAACGAGAACCCGCCCTTGCGAGAGCGAAGATTGATTATCTAAAAAAGTTAGTGGAATTGGGCAGTCAAGAACGACAACAGAAAAAAGAAAAGTCACCGCAAAGT","","","6613","MKKMQIEVTETTDFSPQALKKLKREPALARAKIDYLKKLVELGSQERQQKKEKSPQS","433988","","hypothetical protein","Cytoplasm, Extracellular","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 09:53:37 2004","Mon Feb 23 09:53:37 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This seqeunce is paralogous to AA0348, a hypothetical.AA00631 is paralogously related to AA00535 (3e-16), AA00227 (2e-15), AA01404 (1e-14), AA02115 (5e-14), AA01289 (5e-14), AA01075 (5e-14), AA00008 (5e-14) and AA02340 (6e-13).","Mon Feb 23 09:53:37 2004","","","","","","","","","","","","","1","","","" "AA00632","434713","434267","447","ATGAATTATCAAAATCATGCCGCAGTCCAAAATGATCAGTCTTTTTCTTATCAGCCAATGCCGTTTTTTGATGATATGAAACAAAATAACTTGTTCTTTAACAAAAAACTGGATCTTAACTTGTACTGCATCAGACGCCCGCAACAAACCTGCTTTATTCGCGTAACCAATCCGAATATGTTGGCGTGGGGAATTGATGTGGGTGATATGTTGATCGTAGAAAAAAATAATGAGTTATTCGTTGAAGAACTGGTTGTGCTTGAAGTCAATAACGAATTTCATGTGTATGAGTTTATCGCCCATACAAACGGCGAATTCGTTTTCTTATCGCTTGATTCCAAAACCGAAAATATTAAAATCGCCGACTGGCGCAAACTCCCTATCGTCGGCACCGTCACCAATGTGATTCATCAGCTGCAACGCAAAAACACCATGCGTTTTGCCGCG","","","17519","MNYQNHAAVQNDQSFSYQPMPFFDDMKQNNLFFNKKLDLNLYCIRRPQQTCFIRVTNPNMLAWGIDVGDMLIVEKNNELFVEELVVLEVNNEFHVYEFIAHTNGEFVFLSLDSKTENIKIADWRKLPIVGTVTNVIHQLQRKNTMRFAA","434269","","inner membrane protein ImpA","Cytoplasm, Extracellular","","
InterPro
IPR006198
Domain
Peptidase S24, S26A and S26B
PF00717\"[54-123]TPeptidase_S24
InterPro
IPR011056
Domain
Peptidase S24 and S26, C-terminal region
G3DSA:2.10.109.10\"[32-141]Tno description


","No hits to the COGs database.","","Residues 5 to 119 match (2e-21) PD:PD079959 which is described as PROTEOME COMPLETE IMPA HI1546 ","","","","","","","","","","","","Wed Feb 5 13:41:22 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00632 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 14 to 124 (E-value = 9.9e-24) place AA00632 in the Peptidase_S24 family which is described as Peptidase family S24 (PF00717)","","","","Mintz KP, Fives-Taylor PM.impA, a gene coding for an inner membrane protein, influences colonial morphology of Actinobacillus actinomycetemcomitans.Infect Immun. 2000 Dec;68(12):6580-6.PMID: 11083768","Hagege JM, Brasch MA, Cohen SN.Regulation of transfer functions by the imp locus of the Streptomyces coelicolor plasmidogenic element SLP1.J Bacteriol. 1999 Oct;181(19):5976-83.PMID: 10498709 Runyen-Janecky LJ, Hong M, Payne SM.The virulence plasmid-encoded impCAB operon enhances survival and induced mutagenesis in Shigella flexneri after exposure to UV radiation.Infect Immun. 1999 Mar;67(3):1415-23.PMID: 10024589Jung SI, Han MS, Kwon JH, Cheon CI, Min KH, Lee MS.Cloning of the histidine biosynthetic genes of Corynebacterium glutamicum: organization and sequencing analysis of the hisA, impA, and hisF gene cluster.Biochem Biophys Res Commun. 1998 Jun 29;247(3):741-5.PMID: 9647764Doyle N, Strike P.The spectra of base substitutions induced by the impCAB, mucAB and umuDC error-prone DNA repair operons differ following exposure to methyl methanesulfonate.Mol Gen Genet. 1995 Jun 25;247(6):735-41.PMID: 761696","Mon Jan 6 16:48:07 2003","Mon Jan 6 16:48:07 2003","1","","","" "AA00633","435111","435227","117","TTGAATACATTCATGGTTGTAGTAATGAACGTATTCGTGGAGCGTTTTCTCAAGTTGCGCGAAGGTTTCAAACCGCTTGCCATAATAACATTCGGTCTTTATTCGGTCGGCGATTTT","","","4495","LNTFMVVVMNVFVERFLKLREGFKPLAIITFGLYSVGDF","435227","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 09:55:09 2004","Mon Feb 23 09:55:09 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00633 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 09:55:09 2004","","","","","","","","","","","","","1","","","" "AA00634","435322","435891","570","GTGATCGAACCGAAAGAGGTGGCGGATTTTGTCGCCGCATTACCGTTGAAAAAGATTCCCGGCGTGGGCAAAGTGACCTCGGAAAAATTACTGCAAATGGGTCTGGCGACCTGTGCCGATGTGCAAAAATACGATCGCAATGCGCTGTTTAATTTGTTCGGCAAAGTGGGGCAGCACATTTGGGCATATAGCCATGGCATTGATGAACGCCCGGTGCAACCTCATCGGGAGCGTAAATCGGTGGGCGTGGAAACCACGTTATTAGAAAATATTGAGCAGCTTGCCCAAGGAGATGATGTTTTGAAAAAACTGTATTCTCAATTAGTGGCGCGGGTGCAGCGTGCCTGTCCGAATATTCCGCTGGCGCAATTTCGCAAAATCGGGGTGAAGCTAAAATTTGAAGATTTTCAGGTCACTACCTTGGAAAAAAGTGCGGTGGATTTTTCCGAAGAAAATTTTCGCCTGCTGTTGGCGCAAATTTGGCAACGCAAGCAAGGGCGCAGTGTGCGTTTAATCGGCTTGCACGTCACTTTGCCGGAAGAAAAACAATCGGAACAAATGAGCCTATGG","","","23858","VIEPKEVADFVAALPLKKIPGVGKVTSEKLLQMGLATCADVQKYDRNALFNLFGKVGQHIWAYSHGIDERPVQPHRERKSVGVETTLLENIEQLAQGDDVLKKLYSQLVARVQRACPNIPLAQFRKIGVKLKFEDFQVTTLEKSAVDFSEENFRLLLAQIWQRKQGRSVRLIGLHVTLPEEKQSEQMSLW","435893","","DNA polymerase IV (Pol IV)","Cytoplasm","","
InterPro
IPR001126
Domain
UMUC-like DNA-repair protein
PF00817\"[1-115]TIMS
noIPR
unintegrated
unintegrated
G3DSA:1.10.150.20\"[3-55]Tno description
G3DSA:3.30.1490.100\"[75-189]Tno description
PTHR11076\"[1-190]TDNA REPAIR POLYMERASE UMUC / TRANSFERASE FAMILY MEMBER
PTHR11076:SF12\"[1-190]TDNA POLYMERASE IV / KAPPA


","BeTs to 8 clades of COG0389COG name: Nucleotidyltransferase/DNA polymerase involved in DNA repairFunctional Class: LThe phylogenetic pattern of COG0389 is -o----y---rlbcefgh-n-j---wNumber of proteins in this genome belonging to this COG is","Significant hit ( 4.4e-06) to 1/4 blocks of the IPB001126 family, which is described as \"UMUC family (DNA-repair)\". Interpro entry for IP:IPR001126. IPB001126D 11-30 4.5e-06","Residues 141 to 190 match (2e-09) PD:PD046069 which is described as PROTEOME COMPLETE HI1564 DINP ","","","","","Mon Feb 17 07:13:55 2003","","","","","","","Fri Dec 13 17:25:48 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00634 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Lenne-Samuel N, Wagner J, Etienne H, Fuchs RP.The processivity factor beta controls DNA polymerase IV traffic during spontaneous mutagenesis and translesion synthesis in vivo.EMBO Rep. 2002 Jan;3(1):45-9.PMID: 11751576 Boudsocq F, Iwai S, Hanaoka F, Woodgate R.Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4): an archaeal DinB-like DNA polymerase with lesion-bypass properties akin to eukaryotic poleta.Nucleic Acids Res. 2001 Nov 15;29(22):4607-16.PMID: 11713310 Zhou BL, Pata JD, Steitz TA.Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classic polymerase catalytic domain.Mol Cell. 2001 Aug;8(2):427-37.PMID: 1154574","","Mon Feb 17 07:13:55 2003","1","","","" "AA00635","436037","436888","852","TTGCATAGACAAGCAAGTGAATTCCTCATGAAGTTAACCGCCAACAATAAAGTTTTAGACCTTTCTACTCCCCAAATTATGGGGATTCTCAATTTCACCCCCGATTCGTTTTCCGATAGCGGCAAGTTTTTTCAGTTAGACAAAGCGTTAGCACAAGTGGAAAAGATGCTAAGGCTGGGCGCATCGATTATTGACATCGGCGGCGAATCCACCCGACCGATGGCGGATGAAGTCACTTTGGAAGAGGAATTGCAACGTGTTGTGCCTTTAGTCGAGGCAGTGCGTCAACGATTCGATTGCTGGATTTCGGTAGACACATCAAAACCGCAGGTCATGCGTGAAACGGCAAATGCCGGCATGGATTTGATTAACGATATTCGTGCATTGCAGGAACCGCAAGCGTTGGAGACTGCCGCACAGCTGGCGTTGCCGGTGTGCATTATGCATATGCAGGGGCAGCCCCGCACTATGCAGTTAAATCCTCACTATGAGGACGTGGTCGCCGACGTTTTAAAATTTATGCAGCAACGTACGGAACAATGTCTGGCGGCAGGAATCAAACAAGATAACATCATTTGGGATCCGGGCTTCGGGTTTGGCAAAAGCGTGCAACATAATTATCGCTTATTGCAACAACTCTGGGTTTTCTGCCAGCAGGGGTATCCTGTACTGGCGGGCATATCCCGTAAATCAATGATTGGCGCGGTGCTGGATAAACCAGTGGAACAACGAACCGTCGGTAGTGTCAGCGCTGCTTTAATTGCCGCGATGAATGGCGCCCGTATTTTGCGCGTACATGATGTCGGCGAAACTGCCGATGCGTTAAAAATCTGGCAGGCAACCCTAAACAGT","","","31548","LHRQASEFLMKLTANNKVLDLSTPQIMGILNFTPDSFSDSGKFFQLDKALAQVEKMLRLGASIIDIGGESTRPMADEVTLEEELQRVVPLVEAVRQRFDCWISVDTSKPQVMRETANAGMDLINDIRALQEPQALETAAQLALPVCIMHMQGQPRTMQLNPHYEDVVADVLKFMQQRTEQCLAAGIKQDNIIWDPGFGFGKSVQHNYRLLQQLWVFCQQGYPVLAGISRKSMIGAVLDKPVEQRTVGSVSAALIAAMNGARILRVHDVGETADALKIWQATLNS","436890","","dihydropteroate synthase","Cytoplasm","","
InterPro
IPR000489
Domain
Dihydropteroate synthase, DHPS
G3DSA:3.20.20.20\"[19-281]Tno description
PF00809\"[29-237]TPterin_bind
PS50972\"[24-276]TPTERIN_BINDING
PS00792\"[26-41]TDHPS_1
PS00793\"[60-73]TDHPS_2
InterPro
IPR006390
Domain
Dihydropteroate synthase
TIGR01496\"[25-281]TDHPS: dihydropteroate synthase
noIPR
unintegrated
unintegrated
PTHR20941\"[46-280]TFOLATE SYNTHESIS PROTEINS
PTHR20941:SF1\"[46-280]TDIHYDROPTEROATE SYNTHASE


","BeTs to 19 clades of COG0294COG name: Dihydropteroate synthase and related enzymesFunctional Class: HThe phylogenetic pattern of COG0294 is aompkzyqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 3.8e-64) to 5/5 blocks of the IPB000489 family, which is described as \"Dihydropteroate synthase\". Interpro entry for IP:IPR000489. IPB000489A 26-41 1.7e-10 IPB000489B 49-91 8.9e-25 IPB000489C 184-201 1.8e-10 IPB000489D 219-234 8.3e-08 IPB000489E 259-268 9.7e-05","Residues 46 to 232 match (6e-31) PD:PD009873 which is described as METHYLTRANSFERASE COMPLETE TRANSFERASE PROTEOME METHIONINE 5-METHYLTETRAHYDROFOLATE--HOMOCYSTEINE VITAMIN-B12 DEPENDENT SYNTHASE SYNTHASE ","","","","","","","","","","","","Mon Dec 16 08:10:40 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00635 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 29 to 237 (E-value = 9.6e-100) place AA00635 in the Pterin_bind family which is described as Pterin binding enzyme (PF00809)","","","","","Swedberg,G., Fermer,C. and Skold,O. Point mutations in the dihydropteroate synthase gene causing sulfonamide resistance Adv. Exp. Med. Biol. 338, 555-558 (1993) PubMed: 8304179 Dallas,W.S., Gowen,J.E., Ray,P.H., Cox,M.J. and Dev,I.K. Cloning, sequencing, and enhanced expression of the dihydropteroatesynthase gene of Escherichia coli MC4100 J. Bacteriol. 174 (18), 5961-5970 (1992) PubMed: 1522070 Achari,A., Somers,D.O., Champness,J.N., Bryant,P.K., Rosemond,J. and Stammers,D.K. Crystal structure of the anti-bacterial sulfonamide drug target dihydropteroate synthase Nat. Struct. Biol. 4 (6), 490-497 (1997) PubMed: 9187658 ","","Mon Dec 16 08:10:40 2002","1","","","" "AA00636","436920","438254","1335","ATGGCTGAACGTAAATATTTCGGCACCGACGGGGTGCGTGGGAAAGTGGGATCTCATCCGATTACCCCTGATTTTGTGTTAAAACTCGGTTGGGCTGCGGGCAAAGTGCTGGCAAATCATGGCTCCCGCGTGGTGTTAATCGGTAAAGATACGCGTATTTCCGGTTATATGCTGGAATCCGCGCTTGAAGCGGGTTTGGCGGCTGCCGGTTTGTCTGCCGCTTTTACCGGACCAATGCCGACCCCGGCAGTGGCTTATTTAACCCGCACTTTCCGCGCTGAAGCCGGCATTGTAATTTCTGCCTCACATAACCCGTATTACGATAACGGAATCAAGTTTTTCTCTACGCAAGGCACGAAATTGCCGGATGAAGTGGAAGAAGAAATCGAAGCCATGTTAGAACAACCGATGGATTGCGTGGAATCTGCCGAATTAGGGCGTGCCAGCCGAATTAAAGATGCGGCGGGTCGTTATATCGAATTTTGTAAAAGTACATTCCCGGCGCATTTGAGTCTGGAAGGCTACAAGATCGTGGTGGACTGTGCCAACGGTGCGACTTACCACATTGCGCCGAATGTCATGCGCGAGCTGGGCGCGGAAGTCATTGAAATCGGGACGCATCCGAACGGTATGAACATCAATGAAAAATGTGGTGCAACCGACATCGCGGCGTTACAAGCCAAAGTGGTAGAAACCAATGCGGATGTCGGCTTGGCGTATGATGGCGACGGCGACCGCTTAATTATGGTGGATCACCTTGGTAATAAAGTCGATGGAGACCAAGCCTTATTTATTATTGCCCGCGAAGCGTTGCGTGAAGGTCGTTTGCAAGGTGGTGTGGTCGGCACATTAATGAGCAACATGAGCCTTGAATTGGCGTTAAAACAATTAGCGATTCCATTTGTGCGTGCCAATGTGGGCGATCGTTATGTATTGGAAAAAATGCAGGAACGCGGTTGGGGCTTAGGCGGAGAAAACTCCGGTCATATTATCATTGCCGATCGCAACACTACCGGGGATGGCATTATTGCTTCTCTTGCCGTATTGGCTGCGATGGCAAAACATCGTTTGTCCCTTAATGAATTGGCGGGTGCGGTCAAATTATTCCCGCAAGTGCTAATCAATGTACGTTTTGCCGGTGGTGAAAATCCGTTGGAAAGTGGTGCGGTGAAAATGGTTGCTGCCGAGATGGAAAAACGGTTGGCGGGCAAAGGGCGAATTTTGTTGCGTAAATCAGGTACCGAATCGCTTATCCGCATCATGGTGGAATGTGAAGATGGCACTTTGGCACAGCAATGTGCAGAAGAAATTGCAGCAGCAGTAAAAGAAGCCAAC","","","47471","MAERKYFGTDGVRGKVGSHPITPDFVLKLGWAAGKVLANHGSRVVLIGKDTRISGYMLESALEAGLAAAGLSAAFTGPMPTPAVAYLTRTFRAEAGIVISASHNPYYDNGIKFFSTQGTKLPDEVEEEIEAMLEQPMDCVESAELGRASRIKDAAGRYIEFCKSTFPAHLSLEGYKIVVDCANGATYHIAPNVMRELGAEVIEIGTHPNGMNINEKCGATDIAALQAKVVETNADVGLAYDGDGDRLIMVDHLGNKVDGDQALFIIAREALREGRLQGGVVGTLMSNMSLELALKQLAIPFVRANVGDRYVLEKMQERGWGLGGENSGHIIIADRNTTGDGIIASLAVLAAMAKHRLSLNELAGAVKLFPQVLINVRFAGGENPLESGAVKMVAAEMEKRLAGKGRILLRKSGTESLIRIMVECEDGTLAQQCAEEIAAAVKEAN","438256","","MrsA protein (phosphoglucomutase/phosphomannomutase)","Cytoplasm","","
InterPro
IPR005841
Family
Phosphoglucomutase/phosphomannomutase
PR00509\"[95-109]T\"[174-193]T\"[234-249]TPGMPMM
PS00710\"[96-105]TPGM_PMM
InterPro
IPR005843
Domain
Phosphoglucomutase/phosphomannomutase C-terminal
PF00408\"[373-443]TPGM_PMM_IV
InterPro
IPR005844
Domain
Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain I
PF02878\"[4-140]TPGM_PMM_I
InterPro
IPR005845
Domain
Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain II
PF02879\"[156-256]TPGM_PMM_II
InterPro
IPR005846
Domain
Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain III
PF02880\"[258-369]TPGM_PMM_III
InterPro
IPR006352
Family
Phosphoglucosamine mutase
TIGR01455\"[7-443]TglmM: phosphoglucosamine mutase
noIPR
unintegrated
unintegrated
G3DSA:3.40.120.10\"[3-137]T\"[176-250]T\"[251-367]Tno description
PTHR22573\"[62-443]TPHOSPHOHEXOMUTASE FAMILY MEMBER
PTHR22573:SF2\"[62-443]TPHOSPHOGLUCOMUTASE


","No hits to the COGs database.","","Residues 82 to 124 match (5e-18) PD:PD000667 which is described as COMPLETE PROTEOME PHOSPHOMANNOMUTASE ISOMERASE PHOSPHOGLUCOMUTASE PHOSPHORYLATION PHOSPHOMUTASE GLUCOSE PGM MUTASE ","","","","","","","","","","","","Mon Dec 16 08:29:14 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00636 is paralogously related to AA01013 (5e-24) and AA00452 (4e-15).","","","","","","Residues 373 to 443 (E-value = 1.3e-16) place AA00636 in the PGM_PMM_IV family which is described as Phosphoglucomutase/phosphomannomutase, C-terminal domain (PF00408)","","","","","","","","1","","","" "AA00637","438309","438734","426","ATGGTGAATTCTGATAAGGAACGCCGTCTTAATGCGCGCGGTAAGGAACAATCCACTTTGCAAGGAACTTGGTTAAAATCCACCGCACTTGACTTGGATAAAGTGTTGGTCAGCCCTTATACCCGCGCGTTGGAGACCTTTAATCAAATTAATGAAGTTTATGAACAAAAGCTAACCGACAAACTGAAAATTTGGGATGGTATCACGCCTTACGGCGATTCCGGCATTGTGAGCGATTATCTCTCCGTGTTAGCTGAAGAAGGTGTGGAAAATGTGTTAATCATTTCTCATTTGCCTTTAGTTGGCGACATTGTGAAAGAAATGTGCGGTCGAAATCCCGCGAGTTTTTACCCGGCAACCATTGCGGAAATTTATCTCGGTGATGAGTGCGCTGAGGTCATCGGAATTAAATATTTGGATAAATTT","","","17689","MVNSDKERRLNARGKEQSTLQGTWLKSTALDLDKVLVSPYTRALETFNQINEVYEQKLTDKLKIWDGITPYGDSGIVSDYLSVLAEEGVENVLIISHLPLVGDIVKEMCGRNPASFYPATIAEIYLGDECAEVIGIKYLDKF","438736","","phosphohistidine phosphatase","Cytoplasm","","
InterPro
IPR004449
Family
Phosphohistidine phosphatase SixA, subgroup
TIGR00249\"[1-140]TsixA: phosphohistidine phosphatase SixA
InterPro
IPR013078
Domain
Phosphoglycerate mutase
PF00300\"[2-104]TPGAM
InterPro
IPR014595
Family
Phosphohistidine phosphatase SixA
PIRSF035806\"[1-142]TPhosphohistidine phosphatase, SixA type
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1240\"[4-134]Tno description


","BeTs to 10 clades of COG2062COG name: Phosphohistidine phosphatase SixAFunctional Class: TThe phylogenetic pattern of COG2062 is a----z-q--r--cefghs-uj----Number of proteins in this genome belonging to this COG is","","Residues 1 to 47 match (1e-08) PD:PD400100 which is described as COMPLETE PROTEOME HYDROLASE PHOSPHOHISTIDINE PHOSPHATASE 3.1.3.- SIXA DOMAIN PHOSPHOGLYCERATE SH3 ","","","","","","","","","","","","Mon Dec 16 08:36:33 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00637 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Matsubara M, Mizuno T.The SixA phospho-histidine phosphatase modulates the ArcB phosphorelay signal transduction in Escherichia coli.FEBS Lett. 2000 Mar 24;470(2):118-24.PMID: 10734219 Matsubara M, Mizuno T.EnvZ-independent phosphotransfer signaling pathway of the OmpR-mediated osmoregulatory expression of OmpC and OmpF in Escherichia coli.Biosci Biotechnol Biochem. 1999 Feb;63(2):408-14.PMID: 10192921 Hamada K, Kato M, Mizuno T, Hakoshima T.Crystallographic characterization of a novel protein SixA which exhibits phospho-histidine phosphatase activity in the multistep His-Asp phosphorelay.Acta Crystallogr D Biol Crystallogr. 1999 Jan;55 ( Pt 1):269-71.PMID: 10089421Ogino,T., Matsubara,M., Kato,N., Nakamura,Y. and Mizuno,T. An Escherichia coli protein that exhibits phosphohistidine phosphatase activity towards the HPt domain of the ArcB sensor involved in the multistep His-Asp phosphorelay Mol. Microbiol. 27 (3), 573-585 (1998) PubMed: 9489669 ","","Mon Dec 16 08:44:29 2002","1","","","" "AA00639","438961","439503","543","ATGAAAAAATCAGTATTAGCCGCATTAGTGTTAGGCGTAACTTTAAGTGTAACCGGTTGTGATGACAGCAAAACTTCACCACAAGCCGAGCAGGCGAAAACAAGTGTCTCCGAGGCTAAAGATGCTGTAGTAAACGCCGCAAATGATGTTAAGGATGCTACAGTTGAAGCTGCCAAAGATGCACAAAACATGGCAGCCGATAAAATGGCCGAAGTGAAAGATGTCGTATCTGAAAAAATGGATGCCATGGCAACGCAGGCCAGTGAAATGAAAGATGCTGCAGTTGAAGCGGCCAAAGATGCAAAAGATGCAGCGGCAGATAAAATGGCAGAAGTGAAAGATGCCATATCTGAAAAAATGGATGCCATGGCAACACAAGTCAATGAAATGAAAGATACAGCAGCTGAAGCAGTCAAAGATGCAAAAGACGCAGCGGCAGATAAAATGGCCGAAGTGAAAGATGCCGTATCTGAAAAAATGGGTGCCACCGCAACGCAAACTGATGAAATGAAAGACGCGGTAAAAAGCGAAACTGAAAGCAAA","4.40","-13.03","18800","MKKSVLAALVLGVTLSVTGCDDSKTSPQAEQAKTSVSEAKDAVVNAANDVKDATVEAAKDAQNMAADKMAEVKDVVSEKMDAMATQASEMKDAAVEAAKDAKDAAADKMAEVKDAISEKMDAMATQVNEMKDTAAEAVKDAKDAAADKMAEVKDAVSEKMGATATQTDEMKDAVKSETESK","","","conserved hypothetical protein","Inner membrane, Periplasm","Residues 1-179 are 29% similar to 15602307 an unknown protein [Pasteurella multocida]. Residues 1-130 are 29% similar to 23467137 a hypothetical protein [Haemophilus somnus 129PT].AA00639 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus ducreyi gene.AA00639 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus influenzae Rd gene.","
noIPR
unintegrated
unintegrated
PTHR23241\"[24-180]TLATE EMBRYOGENESIS ABUNDANT (PLANTS) LEA-RELATED
PTHR23241:SF11\"[24-180]TLATE EMBRYOGENESIS ABUNDANT (LEA)
PS51257\"[1-20]TPROKAR_LIPOPROTEIN
signalp\"[1-20]?signal-peptide


","No hits to the COGs database.","","","Fri Feb 27 09:13:10 2004","Sat Feb 28 16:46:48 2004","Sat Feb 28 16:46:48 2004","Sat Feb 28 16:46:48 2004","Fri Feb 27 09:13:10 2004","Fri Feb 27 09:13:10 2004","Fri Feb 27 09:13:10 2004","Fri Feb 27 09:13:10 2004","Fri Feb 27 09:13:10 2004","Fri Feb 27 09:13:10 2004","Fri Feb 27 09:13:10 2004","Fri Feb 27 09:13:10 2004","Fri Feb 27 09:13:10 2004","Fri Feb 27 09:13:10 2004","Fri Feb 27 09:13:10 2004","Fri Feb 27 09:13:10 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00639 is weakly paralogous to AA01213, a competence related protein (5e-05).AA00639 is paralogously related to AA01213 (4e-05).","Fri Feb 27 09:13:10 2004","Fri Feb 27 09:13:10 2004","No hits to the PDB database.","","","Residues 96 to 161 (E-value = 2.5e-05) place AA00639 in the LEA_4 family which is described as Late embryogenesis abundant protein (PF02987)","Fri Feb 27 09:13:10 2004","","","","","","","1","Fri Feb 27 09:13:10 2004","","" "AA00640","439502","438933","570","TTGCTTTCAGTTTCGCTTTTTACCGCGTCTTTCATTTCATCAGTTTGCGTTGCGGTGGCACCCATTTTTTCAGATACGGCATCTTTCACTTCGGCCATTTTATCTGCCGCTGCGTCTTTTGCATCTTTGACTGCTTCAGCTGCTGTATCTTTCATTTCATTGACTTGTGTTGCCATGGCATCCATTTTTTCAGATATGGCATCTTTCACTTCTGCCATTTTATCTGCCGCTGCATCTTTTGCATCTTTGGCCGCTTCAACTGCAGCATCTTTCATTTCACTGGCCTGCGTTGCCATGGCATCCATTTTTTCAGATACGACATCTTTCACTTCGGCCATTTTATCGGCTGCCATGTTTTGTGCATCTTTGGCAGCTTCAACTGTAGCATCCTTAACATCATTTGCGGCGTTTACTACAGCATCTTTAGCCTCGGAGACACTTGTTTTCGCCTGCTCGGCTTGTGGTGAAGTTTTGCTGTCATCACAACCGGTTACACTTAAAGTTACGCCTAACACTAATGCGGCTAATACTGATTTTTTCATCGTTACTCCTAAATTAACAATTGAAAGA","","","18959","LLSVSLFTASFISSVCVAVAPIFSDTASFTSAILSAAASFASLTASAAVSFISLTCVAMASIFSDMASFTSAILSAAASFASLAASTAASFISLACVAMASIFSDTTSFTSAILSAAMFCASLAASTVASLTSFAAFTTASLASETLVFACSACGEVLLSSQPVTLKVTPNTNAANTDFFIVTPKLTIER","438933","","hypothetical protein","Inner membrane, Periplasm, Extracellular","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide
tmhmm\"[4-22]?\"[43-63]?\"[69-103]?\"[113-135]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 09:56:35 2004","Mon Feb 23 09:56:35 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00640 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 09:56:35 2004","","","","","","","","","","","","","1","","","" "AA00641","440190","439531","660","ATGGCTCAAGATATTATCGAACTACGAACAGGTCAATTTTCCGCCGTATTTATCAGTATCAACAGTTCAAGCTTAACGGCGATCAAACGTGCGCTGGCAAAAAAAGCTAAAAACGCACCGTCTTTGTTTCAGAATATTGAAGTGATTTTACAGTTCAATCCGGTGTTGGAAAAAGTCAATTTAACCGTGTTGAAAGCCTTACTTGCCGAATACAACATTCATGTCATCGGTGTAGCTGACTGGCAAAACCATCTGCAAAGAGAATTAATCCTCAGCGCCGATTTACCGATTCTCGGCAACATTGATAACCTGTCTGAAATTCTTCCCGAACCGCGCTATCAACCGACTAAAGTTATCGCCCACAACGTGATTGGTAAACAGGTGATCTACGCCAAAAACAGCGATTTAATCATTCACGGTGATGTGGAGCATGGCGCCGAAGTGGCGGCAGACGGCAATATTCACATTTACGGCGAATTATTAGGGCGCGCCATGGCGGGCGTCAACAGCAGTTCAGGATCTATTTATGCACAATATTTAGATGCCGAATTCGTGGCGGTAAATAGCCGTTTTCTGTACAAAGAAAAAATCCCAACTGAATTTTTATATCGTTCAGTCAGGATTTTTGCGGAAAAGGATAAATTAGTTTTTGCCCCGTTT","","","24515","MAQDIIELRTGQFSAVFISINSSSLTAIKRALAKKAKNAPSLFQNIEVILQFNPVLEKVNLTVLKALLAEYNIHVIGVADWQNHLQRELILSADLPILGNIDNLSEILPEPRYQPTKVIAHNVIGKQVIYAKNSDLIIHGDVEHGAEVAADGNIHIYGELLGRAMAGVNSSSGSIYAQYLDAEFVAVNSRFLYKEKIPTEFLYRSVRIFAEKDKLVFAPF","439533","","cell division inhibitor","Cytoplasm","","
InterPro
IPR005526
Domain
Septum formation inhibitor MinC, C-terminal
PF03775\"[113-220]TMinC_C
InterPro
IPR007874
Domain
Septum formation inhibitor MinC, N-terminal
PF05209\"[1-104]TMinC_N
InterPro
IPR013033
Family
Septum formation inhibitor MinC
TIGR01222\"[5-220]TminC: septum site-determining protein MinC
noIPR
unintegrated
unintegrated
G3DSA:2.160.20.70\"[116-220]Tno description


","BeTs to 11 clades of COG0850COG name: Septum formation inhibitorFunctional Class: DThe phylogenetic pattern of COG0850 is -------qvd--bcefghsnuj----Number of proteins in this genome belonging to this COG is","","Residues 173 to 217 match (2e-11) PD:PD499761 which is described as DIVISION PROBABLE SEPTUM PROTEOME COMPLETE SEPTATION MINC CELL SITE-DETERMINING ","","","","","","","","","","","","Mon Dec 16 09:14:43 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00641 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 113 to 220 (E-value = 3.7e-40) place AA00641 in the MinC_C family which is described as Septum formation inhibitor MinC, C-terminal domain (PF03775)","","",""," Haraszthy VI, Jordan SF, Zambon JJ.,Identification of Fur-regulated genes in Actinobacillus actinomycetemcomitans.Microbiology. 2006 Mar;152(Pt 3):787-96.PMID: 16514158","Akerlund T, Gullbrand B, Nordstrom K.Effects of the Min system on nucleoid segregation in Escherichia coli.Microbiology. 2002 Oct;148(Pt 10):3213-22.PMID: 12368455 Johnson JE, Lackner LL, de Boer PA.Targeting of (D)MinC/MinD and (D)MinC/DicB complexes to septal rings in Escherichia coli suggests a multistep mechanism for MinC-mediated destruction of nascent FtsZ rings.J Bacteriol. 2002 Jun;184(11):2951-62.PMID: 12003935 Corbin BD, Yu XC, Margolin W.Exploring intracellular space: function of the Min system in round-shaped Escherichia coli.EMBO J. 2002 Apr 15;21(8):1998-2008.PMID: 11953319","","Mon Dec 16 09:14:43 2002","1","","","" "AA00642","440274","440522","249","ATGTTATGTGCCATTTATAAAAGCCCGAAGGAAGCGGGCATGTATCTTTATATTGAAAAGCGCAGTCATTTTGATGGTGTACCTGAGGCGCTGCTAAAGATATTTGGAAAACCAATTTTTGTCATGTTGTTTAACCTGACTGGCGAAAAGCCGCTGGTGAATGCAGACAAAACGGAGGTTTTGCAAAATATCAGGGAAAAAGGCTTTTATTTGCAAACACCGAAGAAAGATGATTGGCTGTTTAGTCTT","","","9611","MLCAIYKSPKEAGMYLYIEKRSHFDGVPEALLKIFGKPIFVMLFNLTGEKPLVNADKTEVLQNIREKGFYLQTPKKDDWLFSL","440524","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR007840
Family
Protein of unknown function DUF709
PF05166\"[2-83]TDUF709
noIPR
unintegrated
unintegrated
PD030374\"[1-81]TQ9CNI7_PASMU_Q9CNI7;


","BeTs to 4 clades of COG3100COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3100 is --------------efgh--------Number of proteins in this genome belonging to this COG is","","Residues 1 to 81 match (1e-24) PD:PD030374 which is described as PROTEOME COMPLETE CYTOPLASMIC YCGL VC1957 PA1295 YPO2080 HI1446 STY1943 PM0444 ","","","","","","","","","","","","Mon Dec 16 09:19:21 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00642 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 83 (E-value = 2.4e-48) place AA00642 in the DUF709 family which is described as Family of unknown function (DUF709) (PF05166)","","","","","","","","1","","","" "AA00643","440754","440572","183","GTGCAATCTGATTACCAGAAACTCAAAGAGAAGTTAGCCACAGACTCAGCTGAGTTTTTGGCAGAGAGTGAGAAACTGTATCCTTTCCTCAATGTGAGCTTAGCCAATCGGGAGATTGACTCCTTTACAACTGTATGGTGCCTGACTTTCGGCTTAGTCTCGCCAATGCTGGAAAGCGATATT","","","6915","VQSDYQKLKEKLATDSAEFLAESEKLYPFLNVSLANREIDSFTTVWCLTFGLVSPMLESDI","440574","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Dec 16 09:20:37 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00643 is paralogously related to AA02420 (3e-04).","","","","","","","","","","","","","","1","","","" "AA00644","441431","440925","507","ATGTTCAAAAAATTATTGATTATTATCCCTTTACTCGTCTTAACCGCTTGTTCAACCGGCACAGCCTCATACCAACCGGATCAAGATGAAGAACAGCTTAATCAATTAATTGTCTCCCAATTAAAAACCAACAAACCCCGTCAATACTCCGGCATTATGGACAAACGCCTTTCCAAAATTTATCAGGAATGGGCAGGGACCCGTTATCGTTTTGGCGGCACCACAAAAAATGGCATTGATTGTTCCGGCTTTATGCAAACCACCTTTTTAGATGCGTTTGGTGTGACATTGCCGCGTTCGACTTCCGAACAGCGTTATGTCGGTAAAGCGATTCAAAAGAAAGAACTGAAAGTGGGCGATTTGGTTTTTTTCCGTAGAAATAATCATGTAGGCGTATACGTCGGCAACGATCAGTTTATGCATTCCAGTACAAGCCGAGGCGTGATTATTGAGTCCTTAAGCGACAATTACTGGGCGAGAACGTATACCCAATCCCGTCGGGTTCTT","","","19289","MFKKLLIIIPLLVLTACSTGTASYQPDQDEEQLNQLIVSQLKTNKPRQYSGIMDKRLSKIYQEWAGTRYRFGGTTKNGIDCSGFMQTTFLDAFGVTLPRSTSEQRYVGKAIQKKELKVGDLVFFRRNNHVGVYVGNDQFMHSSTSRGVIIESLSDNYWARTYTQSRRVL","440927","","lipoprotein","Outer membrane, Cytoplasm","","
InterPro
IPR000064
Domain
NLP/P60
PF00877\"[66-167]TNLPC_P60
noIPR
unintegrated
unintegrated
PTHR21666\"[18-39]T\"[62-168]TPEPTIDASE-RELATED
PTHR21666:SF1\"[18-39]T\"[62-168]TNLP/P60 FAMILY SECRETED PROTEIN
PS51257\"[1-17]TPROKAR_LIPOPROTEIN
signalp\"[1-23]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","BeTs to 12 clades of COG0791COG name: Cell wall-associated hydrolases (invasion-associated proteins)Functional Class: MThe phylogenetic pattern of COG0791 is ---------drlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.3e-23) to 3/3 blocks of the IPB000064 family, which is described as \"NLP/P60\". Interpro entry for IP:IPR000064. IPB000064A 69-89 2.7e-09 IPB000064B 114-124 0.00079 IPB000064C 129-146 4.1e-07","Residues 66 to 160 match (1e-34) PD:PD001396 which is described as COMPLETE PROTEOME LIPOPROTEIN PRECURSOR SIGNAL SECRETED HYDROLASE MEMBRANE FAMILY REPEAT ","","","","","","","","","","","","Mon Dec 16 09:27:56 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00644 is paralogously related to AA02162 (3e-35).","","","","","","Residues 66 to 167 (E-value = 3.8e-46) place AA00644 in the NLPC_P60 family which is described as NlpC/P60 family (PF00877)","","","","","","","","1","","","" "AA00646","442465","441614","852","ATGCAAAATAAACTCATTCAATTAGGCGATATTCAAATTGCCAACGATAAACCCTTTGTTTTATTCGGCGGCATGAACGTGCTGGAAAGTCGTGACATGGCGATGCGCGTGTGCGAAAAATATGTGGAAGTGACGCAAAAACTGGGCGTACCTTATGTGTTCAAAGCCTCTTTTGATAAGGCGAACCGTTCTTCTATTCATTCTTATCGCGGTCCGGGCATGGAGCAGGGGCTGAAAATTTTTGCCGAGCTCAAACAAACTTTCGGTGTAAAAATCATTACCGATGTACATGAAATTTATCAATGTCAGCCTGTTGCCGAGGTAGTGGATATTATTCAGTTGCCGGCATTTCTTGCCCGTCAAACGGATTTGGTGGAAGCCATGGCGCGCACCGGCGCGGTGATTAATGTGAAAAAACCGCAATTTTTAAGCCCGGGACAAATGGGCAATATCGTGGAAAAAATCGCCGAGTGCGGCAATGATAAAGTGATTCTGTGCGATCGCGGCACGAATTTTGGTTACGATAATTTAGTCGTAGATATGTTGGGTTTCAGCGTCATGAAAAACGTGTCGAAAGGCTGTCCGGTAATTTTTGACGTGACCCATTCATTGCAATGTCGCGATCCGTTCGGTGCGGCTTCCGGCGGACGCCGTGCACAAGTTACCGAACTTGCCCGTTCCGGTCTGGCGGTAGGATTGGCGGGGCTGTTCTTAGAAGCCCATCCGGATCCAAGCAACGCAAAATGTGACGGACCATCGGCGTTACCGCTAGATAAGCTGGAGGCTTTCGTGAATCAAATGAAAGCGATAGATAATTTGGTGAAATCTTTCCCCGAATTGGATACGGCGAAT","","","30985","MQNKLIQLGDIQIANDKPFVLFGGMNVLESRDMAMRVCEKYVEVTQKLGVPYVFKASFDKANRSSIHSYRGPGMEQGLKIFAELKQTFGVKIITDVHEIYQCQPVAEVVDIIQLPAFLARQTDLVEAMARTGAVINVKKPQFLSPGQMGNIVEKIAECGNDKVILCDRGTNFGYDNLVVDMLGFSVMKNVSKGCPVIFDVTHSLQCRDPFGAASGGRRAQVTELARSGLAVGLAGLFLEAHPDPSNAKCDGPSALPLDKLEAFVNQMKAIDNLVKSFPELDTAN","441616","","2-dehydro-3-deoxyphosphooctonate aldolase","Cytoplasm","","
InterPro
IPR006218
Domain
DAHP synthetase I/KDSA
PF00793\"[10-276]TDAHP_synth_1
InterPro
IPR006269
Family
3-deoxy-8-phosphooctulonate synthase
PTHR21057:SF2\"[1-277]T2-DEHYDRO-3-DEOXYPHOSPHOOCTONATE ALDOLASE
TIGR01362\"[17-276]TKDO8P_synth: 3-deoxy-8-phosphooctulonate sy
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[16-284]Tno description
noIPR
unintegrated
unintegrated
PIRSF001364\"[1-279]T2-dehydro-3-deoxyphosphooctonate aldolase
PTHR21057\"[1-277]TPHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE


","BeTs to 11 clades of COG2877COG name: 3-Deoxy-D-manno-octulosonic acid (KDO) 8-phosphate synthaseFunctional Class: MThe phylogenetic pattern of COG2877 is -------q------efghsnujxi--Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Mon Dec 16 09:34:49 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00646 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 10 to 276 (E-value = 1.4e-126) place AA00646 in the DAHP_synth_1 family which is described as DAHP synthetase I family (PF00793)","","","","","Strohmaier,H., Remler,P., Renner,W. and Hogenauer,G. Expression of genes kdsA and kdsB involved in 3-deoxy-D-manno-octulosonic acid metabolism and biosynthesisof enterobacterial lipopolysaccharide is growth phase regulatedprimarily at the transcriptional level in Escherichia coliK-12 J. Bacteriol. 177 (15), 4488-4500 (1995) M:95362678 Woisetschlaeger,M. and Hoegenauer,G. The kdsA gene coding for 3-deoxy-D-manno-octulosonic acid 8-phosphate synthetase is part of an operon in Escherichiacoli Mol. Gen. Genet. 207, 369-373 (1987) M:87286380 ","","Mon Dec 16 09:34:49 2002","1","","","" "AA00647","443374","442478","897","ATGAACTACCAACAATGGCTGCAACAGGCCGTACAAGCGTTAAATCAGGCGAATCCCTCGGAAAATGGCAAAACCGATGCACAGGTGTTATTGCAATTTGTGACGCAAAAGTCTCGCGCTTTTATTCTGGCTTTCGGTGAAACGGCATTGGATGAAAAAACGCTGGAAAAACTGACTGCACTTTTAGCCTGCCGTTTGCAGGGCGAACCCATCGCTTATATTCTCGGTGAAAAAGAGTTTTGGTCGTTGCCGTTAAATGTTTCGGCAGGCACGCTGATTCCACGCCCCGACACGGAAATATTGGTGGAGAAGGCAGTGGCGATTGCCATTGAAAAGCTACAAAAGTGCGGTCAAAATTCGCAGCGTTTTCGCATTCTCGATCTTGGCACCGGCACCGGCGCGATTGCTTTGGCATTGGCTTCGGCGTTAAAACCTATTGCACAAAAACACACGGTTCAGTTGGATATTATTGGCGTTGACCTCACGCCTGAGGTGGTGGTATTGGCGAAATCTAACGGGGAAAAAAATCAATTGAATGTGGCTTTTGTGCAAAGTTGTTGGTTTGAAAATGTTACGGGGACATTTGATTTAATCCTGAGTAACCCGCCGTATATTGATGCCCATGACGAACATTTAACGCAGGGTGATGTGCGTTTTGAACCCTTGTCCGCATTGGTTGCAGCGGAAGAAGGTTACGCGGATTTACGCCATATTATCGCCAATGCGCCGAAATTTATGCGGGAAAACGGCTATTTGTTGGTGGAACATGGTTGGCAGCAAGGGGAAAAAGTGCGGTCGATTTTCCAAGAGAATTTTTGGTCTGCGGTTGAAACTTTGCGGGATTACGGAAATAATGAGCGCGTCACATTAGGTTGTTGGGCGCAAACTGAAAATAAA","","","33206","MNYQQWLQQAVQALNQANPSENGKTDAQVLLQFVTQKSRAFILAFGETALDEKTLEKLTALLACRLQGEPIAYILGEKEFWSLPLNVSAGTLIPRPDTEILVEKAVAIAIEKLQKCGQNSQRFRILDLGTGTGAIALALASALKPIAQKHTVQLDIIGVDLTPEVVVLAKSNGEKNQLNVAFVQSCWFENVTGTFDLILSNPPYIDAHDEHLTQGDVRFEPLSALVAAEEGYADLRHIIANAPKFMRENGYLLVEHGWQQGEKVRSIFQENFWSAVETLRDYGNNERVTLGCWAQTENK","442480","","protoporphyrinogen oxidase","Cytoplasm","","
InterPro
IPR000241
Domain
Putative RNA methylase
PF01170\"[129-204]TUPF0020
InterPro
IPR002052
Domain
N-6 Adenine-specific DNA methylase
PS00092\"[198-204]?N6_MTASE
InterPro
IPR004556
Family
Modification methylase HemK
TIGR00536\"[1-297]ThemK_fam: methyltransferase, HemK family
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[79-291]Tno description
PTHR18895\"[96-288]TMETHYLTRANSFERASE
PTHR18895:SF7\"[96-288]THEMK METHYLTRANSFERASE FAMILY MEMBER


","BeTs to 23 clades of COG2890COG name: Predicted rRNA or tRNA methylaseFunctional Class: JThe phylogenetic pattern of COG2890 is aompk-yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.1e-05) to 2/4 blocks of the PR00507 family, which is described as \"N12 class N6 adenine-specific DNA methyltransferase signature\". Prints database entry for PR:PR00507. PR00507B 125-139 9.2 PR00507C 195-207 0.0012","Residues 235 to 291 match (7e-08) PD:PD582421 which is described as PROTEOME COMPLETE HEMK METHYLTRANSFERASE 2.1.1.- TRANSFERASE PROBABLE HOMOLOG M.XFAHEMK2P ","","","","","Wed Feb 19 16:32:31 2003","","","","","","","Mon Dec 16 09:36:31 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00647 is paralogously related to AA02562 (7e-17), AA02818 (3e-07) and AA00508 (3e-04).","","","","","","","","","","","Nakayashiki,T., Nishimura,K. and Inokuchi,H. Cloning and sequencing of a previously unidentified genethat is involved in the biosynthesis of heme in Escherichia coli Gene 153 (1), 67-70 (1995) M:95189105 ","","Mon Dec 16 09:36:31 2002","1","","","" "AA00649","444415","443417","999","GTGATTAGCGATCAGGACAAATTCAGAGCCTATTCCAAAGAATATGCACAACTTGAGGATGTTGTGAAAAGTTTTAACCGCTGGAATCAGCTCAATTCCAATCTGGAAGAAGCGCAGCTTTTGCTGGACGATCCCGAAATGAAAGAAATGGCGCAAATGGAGATCGAAGAGTCCAAAGCGGAACTTGAACAGGTTGAACAGCATTTACAAATTCTCTTATTGCCGAAAGATCCGAACGACGAATATAACTGTTATCTTGAAATCCGCGCCGGTACCGGTGGTGATGAGGCGGGCATTTTCGCCGGTGATTTATTCCGTATGTACAGCCGTTATGCGGAAACCAAACGTTGGCGTGTTGAAGTGCTCAGTGAAAATGAAAGCGAGCAGGGCGGATTTAAAGAAATTATCGCGTTGGTCAGCGGTGACGGCGTGTATGGTCAGTTAAAATTTGAATCGGGCGGCCACCGCGTGCAGCGAGTGCCGAAAACTGAATCACAAGGGCGTATTCACACCTCTGCCTGTACTGTTGCCGTGATGCCGGAATTGCTGGAATCGGAAATGCCGGAAATTAACCCGGCGGATTTACGCATTGACACCTACCGCGCGTCGGGTGCGGGCGGTCAGCACATCAATAAAACCGATTCCGCGGTGCGTATTACGCATATTCCGACGGGCATGGTGGTGGAATGTCAGGACGAACGTTCACAACATAAAAACAAAGCCAAAGCTTTATCGGTGCTGGCCTCCCGTCTGGTGCAACAGGAACAGGAAAAACTGGCGCAGGAGCAAGCTGACACCCGTCGTAATTTATTGGGTTCCGGCGATCGTTCCGATAAAATCCGCACTTACAATTACCCGCAAGGGCGCGTTACCGATCACCGTATTAACCTGACGATTTACCGCTTAGACGAAGTGATGAACGGCAAAATTGATGGCTTGATTCAACCGATTATCACCGAATATCAAGCGGATCAGTTGGCGGCGTTGTCGGAGCAGAAT","","","42955","VISDQDKFRAYSKEYAQLEDVVKSFNRWNQLNSNLEEAQLLLDDPEMKEMAQMEIEESKAELEQVEQHLQILLLPKDPNDEYNCYLEIRAGTGGDEAGIFAGDLFRMYSRYAETKRWRVEVLSENESEQGGFKEIIALVSGDGVYGQLKFESGGHRVQRVPKTESQGRIHTSACTVAVMPELLESEMPEINPADLRIDTYRASGAGGQHINKTDSAVRITHIPTGMVVECQDERSQHKNKAKALSVLASRLVQQEQEKLAQEQADTRRNLLGSGDRSDKIRTYNYPQGRVTDHRINLTIYRLDEVMNGKIDGLIQPIITEYQADQLAALSEQN","443419","","peptide chain release factor 1 (RF-1)","Cytoplasm","","
InterPro
IPR000352
Domain
Class I peptide chain release factor
PF00472\"[181-294]TRF-1
PS00745\"[201-217]TRF_PROK_I
InterPro
IPR004373
Family
Peptide chain release factor 1
PTHR11075:SF9\"[1-331]TPEPTIDE CHAIN RELEASE FACTOR 1
TIGR00019\"[1-332]TprfA: peptide chain release factor
InterPro
IPR005139
Domain
PCRF
PF03462\"[36-151]TPCRF
InterPro
IPR012086
Family
Protein chain release factor, RF-1/RF-2
PIRSF003056\"[1-332]TProtein chain release factor, RF-1/RF-2
noIPR
unintegrated
unintegrated
PIRSF500105\"[1-332]TPeptide chain release factor 1
PTHR11075\"[1-331]TPEPTIDE CHAIN RELEASE FACTOR


","No hits to the COGs database.","Significant hit ( 1e-143) to 4/4 blocks of the IPB000352 family, which is described as \"Class I peptide chain release factor\". Interpro entry for IP:IPR000352. IPB000352A 77-123 1.2e-36 IPB000352B 130-181 1.1e-40 IPB000352C 194-240 5.3e-47 IPB000352D 267-294 2.8e-16","Residues 1 to 31 match (6e-08) PD:PD587356 which is described as BIOSYNTHESIS PROTEOME CHAIN COMPLETE RELEASE PEPTIDE RF-1 FACTOR ","","","","","","","","","","","","Mon Dec 16 09:37:56 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00649 is paralogously related to AA01744 (1e-50).","","","","","","Residues 183 to 294 (E-value = 4.9e-74) place AA00649 in the RF-1 family which is described as Peptidyl-tRNA hydrolase domain (PF00472)","","","","","Lee,C.C., Kohara,Y., Akiyama,K., Smith,C.L., Craigen,W.J.and Caskey,C.T. 1988. Rapid and precise mapping of the Escherichia coli releasefactor genes by two physical approaches. J. Bacteriol. 170(10): 4537-4541. PubMed: 3049538. Craigen,W.J., Cook,R.G., Tate,W.P. and Caskey,C.T. 1985. Bacterial peptide chain release factors: conserved primarystructure and possible frameshift regulation of releasefactor 2. Proc. Natl. Acad. Sci. U.S.A. 82(11): 3616-3620.PubMed: 3889910.","","Mon Dec 16 09:37:56 2002","1","","","" "AA00650","445090","444638","453","ATGAAAAAAATCGTATTAGCTGTTTTAGTGGGCTTAACTGTTGCCGGTTGTGCTAATCAAGATGTTTATAGTGGCAGTGTGTATTCTTCGGGACAAGCAAAAGAAGCGCGTTCTATTAGTTATGGTACCATCGTTTCAACCCGCCCGGTGAAAATTCAGGCAGATAACCAGGGCGTGATTGGTACTATTGGCGGTGGTGCAATTGGCGGTATTGCCGGATCTGCAATCGGTGGTGGTACAGGTAGAGCGCTTGCAACGGCTGTTGGAGCAATTGCCGGTGCAGTTACCGGCAGTAAGGTTGAAGAAAAAGTCAGCCAAGTTAGCGCCTTGGAAATGGTAATCAAAAAAGATGACGGAAAAGATATTGTTGTAGTGCAAAAAGCCGAACCTAACTTAGTGCCGGGTGCGCGGGTACGTATCGTCGGCGGTTCACGTTTGAACGTTTCTGCACTT","","","14930","MKKIVLAVLVGLTVAGCANQDVYSGSVYSSGQAKEARSISYGTIVSTRPVKIQADNQGVIGTIGGGAIGGIAGSAIGGGTGRALATAVGAIAGAVTGSKVEEKVSQVSALEMVIKKDDGKDIVVVQKAEPNLVPGARVRIVGGSRLNVSAL","444640","","15 kDa peptidoglycan-associated protein","Outer membrane, Cytoplasm, Extracellular","","
InterPro
IPR008816
Family
Rickettsia 17 kDa surface antigen
PF05433\"[58-101]TRick_17kDa_Anti
noIPR
unintegrated
unintegrated
PS51257\"[1-17]TPROKAR_LIPOPROTEIN
signalp\"[1-20]?signal-peptide


","No hits to the COGs database.","","Residues 17 to 129 match (2e-18) PD:PD315349 which is described as LIPOPROTEIN PROTEOME COMPLETE MEMBRANE OUTER PCP PRECURSOR TRANSMEMBRANE SIGNAL PROBABLE ","","","","","","","","","","","","Mon Dec 16 09:42:06 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00650 is paralogously related to AA00625 (9e-05).","","","","","","","","","","","","","","1","","","" "AA00651","445719","445135","585","ATGTCGTTTCGTTTCCCTCATAAAATGTTTGAAAAACAGACCGCACTTTTCACTGATTTTGAAGATTTTGAACAAAAAATTCATACTTTGGCGCAACGGCTTGATTTAAATTTGTCGGAATATGAAATTGACCATCTTTCTTTACGTGTCAATACCGAGCAAGCGGCGCAAGCATGGTTGGCGTTATTGTTAAAGCAAGGTTCGGTGTTACGTGATAATGTAGTGAACGGGCGTGTGATCTATCTTATTCAGCTTAATGAGCCTATATGCTTTGTCGGGCAATGGGTGGATGTGGTGGAGTTGCCGCTGCCGAAAGATAAGCATTACCCGCAAGAAACCTGGGAGCATATTGAGGTGGTTGTGCCGTTTTGGGCGAACGAAACAGCAGATGAATGGGTAGCACGCATAAAAAAATCGTTTTTGCGGAACCAATTTTCAGATCTGACAGTCAAAGCGAGCAAACCAAAAGCAAGCGGTGAAATACTGGATAATTTATCCGTGGCGGTGAGTTTTTTTGATAAAACACACAACCATACTTGCATTAAGTTTCATCCATATAGTATCAAAAAAATCATTAATGCGGTA","","","22681","MSFRFPHKMFEKQTALFTDFEDFEQKIHTLAQRLDLNLSEYEIDHLSLRVNTEQAAQAWLALLLKQGSVLRDNVVNGRVIYLIQLNEPICFVGQWVDVVELPLPKDKHYPQETWEHIEVVVPFWANETADEWVARIKKSFLRNQFSDLTVKASKPKASGEILDNLSVAVSFFDKTHNHTCIKFHPYSIKKIINAV","445137","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR010393
Family
Protein of unknown function DUF991
PF06185\"[8-195]TYecM
noIPR
unintegrated
unintegrated
G3DSA:3.10.180.10\"[3-192]Tno description


","BeTs to 3 clades of COG3102COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3102 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 23 to 194 match (2e-48) PD:PD036173 which is described as PROTEOME COMPLETE CYTOPLASMIC YECM YPO2047 VC2073 HI1581/HI1582 PM0552 STY2116 ORF ","","","","","","","","","","","","Mon Dec 16 09:44:17 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00651 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 195 (E-value = 4.9e-87) place AA00651 in the DUF991 family which is described as Protein of unknown function (DUF991) (PF06185)","","","","","","","","1","","","" "AA00652","445858","447546","1689","ATGCTTGCTGCCGGCGCCGATGCACAATGTAATGCGTTGGTTCGCCAATCGGGCAAGGTGCAATTCGGCGATTATCAAGCCAACGGCATCATGCCTGCTGCCAAAAAATTAGGCATAAACCCGCGTGAATTTGCGCAACTGGTGTTAGCGAAGGCCGAATTGCAAGATATTGCGGAAAAAACCGAAATTGCCGGCCCGGGGTTTATTAATATTTTTCTGAAAGACGGCTGGTTAGCGGAGAATATCGGCAACGCTGTGAAAGATTCGAAATTAGGCATTCACCATCAGGATAAACAAACAGTGGTGGTAGACTATTCTTCCCCGAACGTTGCCAAAGAAATGCACGTGGGGCATTTACGTTCCACCATCATCGGCGACGCTGTAGTGCGTACGTTGGAATTTTTAGGCAATCATGTTATCCGTGCTAACCATGTAGGCGATTGGGGTACACAATTCGGCATGCTAATTGCCTATTTGGAAAAAATGGAAAACGAACACGCCTCTGAAATGGAACTCAGCGATTTGGAAGCCTTTTATCGTGCAGCGAAGAAACATTATGACGAAGATCCGGTATTTGCCGAGAAAGCCCGCAATTATGTAGTGAAACTGCAAAGCGGCGATGAATATTGCCGTACCATGTGGCAAAAGCTGGTAAAAATCACTATGCAACAAAATCAACACAATTACGATCGTTTAAATGTGACCTTAACCGAAAAAGATGTCATGGGTGAAAGCCTGTATAACCCAATGCTGCCGGGCATTGTAGAAGGTCTTAAAAAACAAGGTCTCGCCGTAGAAGACGACGGTGCATGGGTGGTTTATTTAGATGAATTTAAAAATAAAGACGGTGGCCCGATGGGCGTTATCGTGCAGAAAAAAGACGGCGGTTTTCTTTATACCACCACCGATATTGCCGCCGCCAAATATCGCTATGAAACCTTAAAAGCCAACCGTGCATTGGTGTTCTCCGACACCCGCCAAAGCCAACATATGCAACAAGCCTGGCTGATTACCCGCAAGGCCGGTTATGTGCCGGACAGTTTCCAATTAGAACACAAAAATTTTGGCATGATGCTCGGCAAAGACGGCAAGCCATTCAAAACCCGCAGTGGCGACACCGTAAAACTGGCGGATTTATTGGACGAAGCCATTGAACGTGCCGGCGTATTAATATCGCAAAAATCCACCGCACTTTCCGAGCAGGAAAAAGCCGATGTGATCGAGGCGGTAGGTATCGGTTCGGTAAAATACGCAGATTTATCCAAAAACCGTATCACCGATTATGTGTTTGATTGGGACAATATGCTAAGCTTTGAAGGCAACACTGCGCCTTATATGCAATACGCTTACACTCGCATTCGTTCTATCTTTAACCGCAGCCAAATCAGCCCCGGAAAGGTAAAACAGGCGCCATTAACCTTAACGAATGAAAAAGAACGCGCGTTGGCAATCAAATTACTGCAATTTGAAGAAGCCATTCAACTCGCGGCAAAAGACGGTACGCCACACATTCTTTGTGCCTATTTATATGAATTGGCAGGCGTGTTCTCTTCTTTCTACGAGCACTGCCCGATTCTCAATAACGAAGACCAACAGGTAAAACTCAGCCGTTTAAAACTGGCGTTATTAACAGAAAGAACCTTAAAACAAGGATTAGATTTACTGGGCATTAAAACCGTCGAGAGAATG","","","64669","MLAAGADAQCNALVRQSGKVQFGDYQANGIMPAAKKLGINPREFAQLVLAKAELQDIAEKTEIAGPGFINIFLKDGWLAENIGNAVKDSKLGIHHQDKQTVVVDYSSPNVAKEMHVGHLRSTIIGDAVVRTLEFLGNHVIRANHVGDWGTQFGMLIAYLEKMENEHASEMELSDLEAFYRAAKKHYDEDPVFAEKARNYVVKLQSGDEYCRTMWQKLVKITMQQNQHNYDRLNVTLTEKDVMGESLYNPMLPGIVEGLKKQGLAVEDDGAWVVYLDEFKNKDGGPMGVIVQKKDGGFLYTTTDIAAAKYRYETLKANRALVFSDTRQSQHMQQAWLITRKAGYVPDSFQLEHKNFGMMLGKDGKPFKTRSGDTVKLADLLDEAIERAGVLISQKSTALSEQEKADVIEAVGIGSVKYADLSKNRITDYVFDWDNMLSFEGNTAPYMQYAYTRIRSIFNRSQISPGKVKQAPLTLTNEKERALAIKLLQFEEAIQLAAKDGTPHILCAYLYELAGVFSSFYEHCPILNNEDQQVKLSRLKLALLTERTLKQGLDLLGIKTVERM","447548","","arginyl-tRNA synthetase (arginine--tRNA ligase)","Cytoplasm","","
InterPro
IPR001278
Family
Arginyl-tRNA synthetase, class Ic
PR01038\"[100-115]T\"[115-131]T\"[139-152]T\"[289-310]TTRNASYNTHARG
PTHR11956\"[11-563]TARGINYL-TRNA SYNTHETASE
PF00750\"[81-432]TtRNA-synt_1d
TIGR00456\"[1-563]TargS: arginyl-tRNA synthetase
InterPro
IPR001412
Family
Aminoacyl-tRNA synthetase, class I
PS00178\"[108-119]TAA_TRNA_LIGASE_I
InterPro
IPR005148
Domain
Arginyl tRNA synthetase, N-terminal
PF03485\"[1-73]TArg_tRNA_synt_N
InterPro
IPR008909
Domain
DALR anticodon binding
PF05746\"[446-563]TDALR_1
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620\"[97-449]Tno description
noIPR
unintegrated
unintegrated
G3DSA:1.10.730.10\"[450-563]Tno description


","BeTs to 26 clades of COG0018COG name: Arginyl-tRNA synthetaseFunctional Class: JThe phylogenetic pattern of COG0018 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 337 to 440 match (7e-08) PD:PD568879 which is described as LIGASE PROTEOME COMPLETE ARGININE-TRNA ","","","","","","","","","","","","Mon Dec 16 09:46:13 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00652 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 446 to 563 (E-value = 2.5e-56) place AA00652 in the tRNA-synt_1d_C family which is described as DALR anticodon binding domain (PF05746)","","","","","Grundy FJ, Henkin TM. Conservation of a transcription antitermination mechanismin aminoacyl-tRNA synthetase and amino acid biosynthesisgenes in gram-positive bacteria. J Mol Biol. 1994 Jan 14;235(2):798-804. PMID: 8289305 Eriani,G., Dirheimer,G. and Gangloff,J. Isolation and characterization of the gene coding forEscherichia coli arginyl-tRNA synthetase Nucleic Acids Res. 17 (14), 5725-5736 (1989) PubMed: 2668891 ","","Mon Dec 16 09:46:13 2002","1","","","" "AA00653","447822","447920","99","ATGAAAAGTGCGGTCATAAAAAATAATATTTTTTATGACCGCACTTTAATTAAATTAACGAATTTTCGGTTCTTGCCAGACGAGAAATTAATGTCCCAT","","","3967","MKSAVIKNNIFYDRTLIKLTNFRFLPDEKLMSH","447920","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 09:58:02 2004","Mon Feb 23 09:58:02 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00653 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 09:58:02 2004","","","","","","","","","","","","","1","","","" "AA00654","449342","447912","1431","ATGAAAAAATCAGCGTTAGCTTTAGGGGTGGTTGTGGCGTTAGGAGCGACTTGGACCGGTGGTGCTTGGTACACTGGCAAGGTGGCAGAAACGGAATTTGCCCGTCAAGTGGATATTGCCAATAAAGATCTTAACAAATCCGCCTATTCTTTAGGCTTAGATATTCGATTTGATAATGTTTCTTTTGAACGCGGCTTATTCAGCTCTAAAACCAAATATAAAATTCTGGTTTCTGAGCTTGATAATCCCGGTAAAACCTGGACATTGCCGTTTGAAGGCACTTTATACCATGGTCCGTTGCCGTTAAATCAACTTTCCCACTTTAACTTCATGCCAAGTATGTTCTCGAGTGTAGATTTCATAACCAAAAACGAAACCACAACGCCTTGGTTTGACGCCACGAAAGGTAAAACGCCGGTTATGTTGACGACCTCCGTCGGCTATAACCAAAGTGGTTCATCCAAGGTGGAGCTGGTACCTTTTGAGGCACTAATGAAAGACGGTACATTAGCAGCTAACGGTTTTGATGTGAAATTCGGCTTTGTACGCGAAGGCATTAATAAACTGGATTTAGACCTCACCAAACTAGTGTATAGCAAGTCGGATAGTAAAGATTCCATTGAGTTGAATGATGTAAAAATCGACGTGGATTACCGGCGTATTCCGGAGTGGGAATATCTTCCTATCGGTAAAAAATTTTTGTCCGGTGGCGTAATTAAAATTAACGACACAGATGCCGAAGGTAAAACCAATAATGTTGAATTTAAAAACTGGAAAATTGATTTCGATACGGCCAGAAAAGACCAATTTCTGGATTTCGGTGCGAAAATTGCATTTAACGGCATGACTATTCGTGGTATGGGCTTTGGTGATTTGACTATTGATTCTGCTTTTAATCACGTTGACGGTGAAACTTTTAATCAATTAATTCAGGTTTATACCGAGGCGGCGAAAAAGCAGCAAGAAGAATTTGCCGAAGCCAAATTACAGGCAGCGAAGAAATTCCTTGATACTCAACCGCAATTTGTGTTTAGTCCGACATTAACTAATCAAGTCGGTAAAATTGCCTCAAATTTAGATATTTCTATTGCAAGCTCTGATTTTGAAAATTCTATTAGCAAAGGAAAAATCTTCAATCTATTTAATCACTTTATTTTCAAAGTGGATGCGAACAAAGATGCTTTAATCGAAGAAATGGCGAACGCACTGCAATTGAAAAGCCCGGATAGAGAGCAAGCAATGAAAATGGCAGCCACACAAGTGAATGAAGGTGTGAAAAGCGGTGTTCTGCAAGGTGTATTGGTCGAAGACGGTAAACAAGTAAAATTGGATCTCGTATTGGAAAAAGGCCAGCTGAAATTAAATGGTCAGGTGATTTCGGAAGAACAAGTGGCTTCTATGTTATTCTTAGCCGCGATGTCAATGGGACAT","","","52832","MKKSALALGVVVALGATWTGGAWYTGKVAETEFARQVDIANKDLNKSAYSLGLDIRFDNVSFERGLFSSKTKYKILVSELDNPGKTWTLPFEGTLYHGPLPLNQLSHFNFMPSMFSSVDFITKNETTTPWFDATKGKTPVMLTTSVGYNQSGSSKVELVPFEALMKDGTLAANGFDVKFGFVREGINKLDLDLTKLVYSKSDSKDSIELNDVKIDVDYRRIPEWEYLPIGKKFLSGGVIKINDTDAEGKTNNVEFKNWKIDFDTARKDQFLDFGAKIAFNGMTIRGMGFGDLTIDSAFNHVDGETFNQLIQVYTEAAKKQQEEFAEAKLQAAKKFLDTQPQFVFSPTLTNQVGKIASNLDISIASSDFENSISKGKIFNLFNHFIFKVDANKDALIEEMANALQLKSPDREQAMKMAATQVNEGVKSGVLQGVLVEDGKQVKLDLVLEKGQLKLNGQVISEEQVASMLFLAAMSMGH","447914","","conserved hypothetical protein","Periplasm, Cytoplasm","","
InterPro
IPR010352
Family
Protein of unknown function DUF945, bacterial
PF06097\"[1-464]TDUF945
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","","Residues 339 to 476 match (2e-14) PD:PD092471 which is described as PROTEOME COMPLETE HI1235 SIGNAL PRECURSOR PM0735 ","","","","","","","","","","","","Mon Dec 16 09:48:09 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00654 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 464 (E-value = 1.4e-67) place AA00654 in the DUF945 family which is described as Bacterial protein of unknown function (DUF945) (PF06097)","","","","","","","","1","","","" "AA00655","449440","449538","99","ATGAAAAAAATTTCATTTTCCCTTGAAGTTCATATTTTTAACCTTATTCTACGAAAACGAACAGGAAATCGACCGCACTTTTCCTCTGTCAAAAATTTT","","","3928","MKKISFSLEVHIFNLILRKRTGNRPHFSSVKNF","449538","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 09:59:34 2004","Mon Feb 23 09:59:34 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00655 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 09:59:34 2004","","","","","","","","","","","","","1","","","" "AA00657","449628","451526","1899","ATGGGAAAAATTGTTGGTATTGACTTAGGTACAACCAACTCTTGCGTTGCCGTCATGGAAGGTGAAAAACCTCGTGTTATCGAAAACGCAGAAGGCGATCGTACTACTCCGTCAATCATTGCTTATACAAATGACAATGAAACTTTAGTCGGTCAACCGGCAAAACGCCAAGCGGTAACCAACCCGAAAAATACCTTATTCGCCATCAAACGTTTAATCGGCCGTCGTTTTGAAGATGAGGAAGTAAAACGCGATATCGACATTATGCCGTTCGCCATTACCAAAGCAGACAACGGCGATGCGTGGGTTGAAGTGAAAGGAGAAAAATTAGCGCCTCCGCAAATTTCTGCTGAAGTATTGAAAAAAATGAAAAAAGCTGCCGAAGATTATTTGGGCGAACCGGTTACCGAGGCGGTTATTACTGTGCCGGCATACTTTAACGACGCACAACGTCAGGCAACAAAAGATGCAGGTCGTATCGCAGGTTTAGACGTTAAACGTATCATCAACGAACCGACCGCCGCGGCATTAGCTTATGGCTTAGACAAAGGCACCGGCAACAAAACCATCGCGGTATACGACTTAGGTGGCGGTACATTCGACTTATCTATCATCGAAATCGATGAAGTAGGCGGCGAAAAAACCTTTGAAGTATTAGCAACCAACGGTGATACACACTTAGGTGGTGAAGACTTTGATAACCGTATCATCAACTACTTAGTGGATGAGTTCAAAAAAGAACAGGGCATCGACCTACGCAACGACCCGCTTGCAATGCAACGTTTAAAAGAAGCGGCAGAAAAAGCCAAAATCGAGCTTTCTTCCGCCCAACAAACCGATGTAAATCTTCCTTACATTACAGCGGATGCAACCGGTCCTAAACACTTAAACATCAAATTGACTCGTGCAAAATTAGAGTCTTTGGTTGAGGATTTAGTGGCGAAATCCCTTGAGCCTGTACGTATTGCATTAAAAGATGCAGGCAAATCCCCGTCTGAAATCGACGATGTGATTTTAGTCGGCGGTCAAACCCGTATGCCGCTTGTTCAACAAGAAGTTGAAAAATTCTTCGGCAAAGCACCACGTAAAGACGTGAATCCGGATGAAGCGGTCGCTATCGGTGCTGCGGTACAAGGCGGTGTGTTAGCCGGTGATGTGAAAGATGTATTATTGTTAGACGTCACCCCATTATCATTGGGTATCGAAACTATGGGCGGCGTAATGACCACCTTAATTGAGAAAAACACCACGATTCCTACCAAGAAATCACAAGTGTTCTCAACAGCGGAAGATAACCAAAGTGCGGTAACCATTCATGTGTTACAAGGTGAGCGTAAACAAGCGTCAGCCAATAAATCGTTAGGTCAATTCAATCTTGAAGGCATCAATCCGGTTCCACGCGGTATGCCGCAAATTGAAGTGACCTTCGACATCGACGCAGACGGTATTATCCACGTTTCTGCGAAGGATAAAGGCACAGGTAAAGAACAACAAATCACCATTAAAGCCTCTTCCGGTTTAAGCGATGAAGAAATTCAACAAATGGTACGCGACGCTGAAGCAAATGCCGAATCCGACCGTAAATTTGAAGAATTGGTACAAGCCCGCAACCAAGCGGATCACTTAATCCACAGCACACGCAAACAATTGGACGAAGCCGGTGACAAAGTACCTGCAGCAGATCGCGGCACCATCGAAAGCGCATTAAGTGACTTGGAAAAAGCGGCGAAGGGCGAAGATAAAGCAGTTATCGAAGCAAAAATCAAAGCATTAGCCGAAGTTGCACAAAAACTTGCACAAACCGCTCAACCACACGGCGATCCACAACAAGCTCAAAGCAACAGCAAACCAAATGATGATGTTGTTGATGCAGAGTTTGAAGAAGTGAAAGATAACAAG","","","71413","MGKIVGIDLGTTNSCVAVMEGEKPRVIENAEGDRTTPSIIAYTNDNETLVGQPAKRQAVTNPKNTLFAIKRLIGRRFEDEEVKRDIDIMPFAITKADNGDAWVEVKGEKLAPPQISAEVLKKMKKAAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGLDVKRIINEPTAAALAYGLDKGTGNKTIAVYDLGGGTFDLSIIEIDEVGGEKTFEVLATNGDTHLGGEDFDNRIINYLVDEFKKEQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHLNIKLTRAKLESLVEDLVAKSLEPVRIALKDAGKSPSEIDDVILVGGQTRMPLVQQEVEKFFGKAPRKDVNPDEAVAIGAAVQGGVLAGDVKDVLLLDVTPLSLGIETMGGVMTTLIEKNTTIPTKKSQVFSTAEDNQSAVTIHVLQGERKQASANKSLGQFNLEGINPVPRGMPQIEVTFDIDADGIIHVSAKDKGTGKEQQITIKASSGLSDEEIQQMVRDAEANAESDRKFEELVQARNQADHLIHSTRKQLDEAGDKVPAADRGTIESALSDLEKAAKGEDKAVIEAKIKALAEVAQKLAQTAQPHGDPQQAQSNSKPNDDVVDAEFEEVKDNK","451528","","heat shock protein 70","Cytoplasm","","
InterPro
IPR001023
Family
Heat shock protein Hsp70
PR00301\"[3-16]T\"[31-43]T\"[54-62]T\"[138-158]T\"[198-208]T\"[334-350]T\"[365-385]T\"[388-407]T\"[469-485]THEATSHOCK70
PTHR19375\"[1-524]THEAT SHOCK PROTEIN 70KDA
InterPro
IPR012725
Family
Chaperone DnaK
TIGR02350\"[3-604]Tprok_dnaK: chaperone protein DnaK
InterPro
IPR013126
Family
Heat shock protein 70
PD000089\"[69-162]TQ72DW8_DESVH_Q72DW8;
PF00012\"[4-604]THSP70
PS00297\"[7-14]THSP70_1
PS00329\"[192-205]THSP70_2
PS01036\"[337-351]THSP70_3
InterPro
IPR013159
Domain
Chromosomal replication initiator, DnaA C-terminal
SM00760\"[508-572]Tno description
noIPR
unintegrated
unintegrated
G3DSA:2.60.34.10\"[371-561]Tno description
G3DSA:3.30.420.40\"[4-204]Tno description
G3DSA:3.90.640.10\"[228-313]Tno description
PTHR19375:SF1\"[1-524]THEAT SHOCK PROTEIN 70 (HSP70)


","BeTs to 22 clades of COG0443COG name: Molecular chaperoneFunctional Class: OThe phylogenetic pattern of COG0443 is -omp--yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit (8.8e-195) to 6/6 blocks of the IPB001023 family, which is described as \"Heat shock protein hsp70\". Interpro entry for IP:IPR001023. IPB001023A 5-37 1.8e-22 IPB001023B 122-175 1e-48 IPB001023C 190-225 7e-15 IPB001023D 319-358 9.7e-25 IPB001023E 388-436 7.8e-43 IPB001023F 454-501 8.1e-36Significant hit ( 9.7e-14) to 2/3 blocks of the IPB002821 family, which is described as \"Hydantoinase/oxoprolinase\". Interpro entry for IP:IPR002821. IPB002821A 3-16 0.01 IPB002821C 132-181 2.5e-09","Residues 312 to 397 match (6e-07) PD:PD579445 which is described as HEAT SHOCK ATP-BINDING CHAPERONE FAMILY PROTEOME MULTIGENE COMPLETE HOMOLOG HEAT-SHOCK ","","","","","","","","","","","","Mon Dec 16 09:51:25 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00657 is paralogously related to AA00713 (1e-122) and AA01371 (7e-08).","","","","","","Residues 2 to 391 (E-value = 2.8e-05) place AA00657 in the MreB_Mbl family which is described as MreB/Mbl protein (PF06723)","","","","Yoshida,A., Nakano,Y., Yamashita,Y., Yu,H., Ohishi,M. and Koga,T. Isolation and characterization of the dnaKJ operon from Actinobacillus actinomycetemcomitans DNA Seq. 8 (1-2), 93-98 (1997) PubMed: 9522128","Qi HY, Hyndman JB, Bernstein HD. DnaK promotes the selective export of outer membraneprotein precursors in SecA-deficient E. coli. J Biol Chem. 2002 Oct 25 PMID: 12403776 Zavilgelsky GB, Kotova VY, Mazhul' MM, Manukhov IV. Role of Hsp70 (DnaK-DnaJ-GrpE) and Hsp100 (ClpA and ClpB)Chaperones in Refolding and Increased Thermal Stability of Bacterial Luciferases in Escherichiacoli Cells. Biochemistry (Mosc). 2002 Sep;67(9):986-92. PMID: 12387711 Nam SH, Walsh MK. Affinity purification and characterization of theEscherichia coli molecular chaperones. Protein Expr Purif. 2002 Mar;24(2):282-91. PMID: 11858724 Kim SY, Sharma S, Hoskins JR, Wickner S. Interaction of the DnaK and DnaJ chaperone system with anative substrate, P1 RepA. J Biol Chem. 2002 Sep 16 PMID: 12237299 ","Mon Dec 16 09:56:40 2002","Fri Nov 21 14:24:39 2003","1","","","" "AA00658","451758","452012","255","TTGAGCGTAGCGAGTTCGAAAATTTCCGTAAGGAAAATCCTATTGGAAAGAGGAAAAGCGGCTTATCCGGGGTGTGTTTCTTTTGCCTACTTTGCTTTGCACAAGCAAAGAAAAGTAGGTCGCCATCGGCGAAACCCGATACTAATTAACGAAGAAAAATTCCTCAAACAGAGAACAAAACCAAGACCAAAACGGAAACCACCTAATGGCAAAACAAGACTACTACGAACTCCTCGGCATCTCCCGATCCGCCGA","","","9946","LSVASSKISVRKILLERGKAAYPGCVSFAYFALHKQRKVGRHRRNPILINEEKFLKQRTKPRPKRKPPNGKTRLLRTPRHLPIRR","452012","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 10:01:13 2004","Mon Feb 23 10:01:13 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","A very weak similarity is found to AA1627.AA00658 is paralogously related to AA02490 (2e-04).","Mon Feb 23 10:01:13 2004","","","","","","","","","","","","","1","","","" "AA00659","452050","453087","1038","ATGCAGTATCACCCTGACAGAACCAAGGGCGATAAAGAGAAAGAAGAAAAATTCAAAGAAATTCAAGAAGCCTATGAAGTGCTAAACGATAAAGAAAAACGCGCTGCCTATGATCAATATGGGCACGCGGCGTTTGAACAAGGAACTGGCTTTGGTGGCGGCAGTTTTGGCGGTGCGGATTTCGGGGATATTTTCGGCGATATGTTCGGAGATATTTTCGGTGGTGGCGGACGTGGGCGCCAACGCGTCGTGCGTGGTGACGATTTGCGGTACGACATTGAAATTACGCTGGAAGAAGCTGTAAAAGGCACTACAAAAGACATAAAAATTCATACCTTAGCCCCATGTGATACTTGTCACGGCACAGGCGCTGAAGCGGGTTCGAAAGTCGAAACCTGTCCGCATTGCCATGGTGCCGGTCGTTTACGTCGTCAACAGGGCTTCTTTGTAACAGAACAACCTTGTCATTTCTGTCATGGCACCGGTAAGAAAATTGAGAAACCATGTAAAACCTGCCATGGTGACGGCAGAGTCAATAAAGCGAAAAATCTTTCCGTTAAAATCCCGGCGGGCGTGGACACAGGCAATCAACTACGTCTTTCAGGTGAAGGCGCTGCAGGTGAAAACGGCGCCCCGGCAGGCGATTTATATGTGGTGATTCATGTTAAAGAACACCATATTTTTGAACGTGACGGCAGCAACCTCTATTGTGAAGTACCGATCAGTTTTACCATGGCTGCCCTTGGTGGAGAAATTGAAGTGCCGACACTGGATGGTCGTGTGAAGTTAAAAATCCCGGAAGAAACCCAAACCGGAAAATTATTCCGTATGCGCGGGAAAGGTGTCACGTCAACCCGAAGCGGCTACGCAGGGGATTTAACTTGCCGAATTATTGTAGAAACCCCGGTTAAATTAAACGAGGAGCAAAAAGAATTATTACGCAAACTGGAGGAAAGCCTGGAAGGACAAACCAAGCAACGTCCGAAATCCTCCAGCTTCTTAGATGGCGTAAAACGTTTCTTTGATGATCTGACGAAG","","","41362","MQYHPDRTKGDKEKEEKFKEIQEAYEVLNDKEKRAAYDQYGHAAFEQGTGFGGGSFGGADFGDIFGDMFGDIFGGGGRGRQRVVRGDDLRYDIEITLEEAVKGTTKDIKIHTLAPCDTCHGTGAEAGSKVETCPHCHGAGRLRRQQGFFVTEQPCHFCHGTGKKIEKPCKTCHGDGRVNKAKNLSVKIPAGVDTGNQLRLSGEGAAGENGAPAGDLYVVIHVKEHHIFERDGSNLYCEVPISFTMAALGGEIEVPTLDGRVKLKIPEETQTGKLFRMRGKGVTSTRSGYAGDLTCRIIVETPVKLNEEQKELLRKLEESLEGQTKQRPKSSSFLDGVKRFFDDLTK","453089","","heat shock protein","Cytoplasm","","
InterPro
IPR001305
Domain
DnaJ central region
PF00684\"[103-183]TDnaJ_CXXCXGXG
PS51188\"[103-181]TZF_CR
InterPro
IPR001623
Domain
Heat shock protein DnaJ, N-terminal
PF00226\"[1-38]TDnaJ
SM00271\"[1-33]TDnaJ
PS50076\"[1-41]TDNAJ_2
PS00636\"[18-37]TDNAJ_1
InterPro
IPR002939
Domain
Chaperone DnaJ, C-terminal
PF01556\"[196-317]TDnaJ_C
InterPro
IPR003095
Family
Heat shock protein DnaJ
PR00625\"[18-38]T\"[108-127]T\"[133-143]T\"[147-165]T\"[167-182]T\"[186-202]T\"[232-249]TDNAJPROTEIN
InterPro
IPR012724
Family
Chaperone DnaJ
TIGR02349\"[1-320]TDnaJ_bact: chaperone protein DnaJ
InterPro
IPR015609
Family
Molecular chaperone, heat shock protein, Hsp40, DnaJ
PTHR11821\"[1-304]TDNAJ/HSP40
noIPR
unintegrated
unintegrated
G3DSA:1.10.287.110\"[1-47]Tno description
G3DSA:2.10.230.10\"[103-181]Tno description
G3DSA:2.60.260.20\"[225-314]Tno description
PTHR11821:SF79\"[1-304]TCHAPERONE PROTEIN DNAJ


","BeTs to 22 clades of COG0484COG name: Molecular chaperones (contain C-terminal Zn finger domain)Functional Class: OThe phylogenetic pattern of COG0484 is -omp--yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1e-138) to 5/6 blocks of the IPB001305 family, which is described as \"DnaJ central domain (CXXCXGXG)\". Interpro entry for IP:IPR001305. IPB001305B 17-42 1.4e-20 IPB001305C 85-136 2.6e-31 IPB001305D 155-200 7.1e-28 IPB001305E 210-249 1.4e-30 IPB001305F 265-316 6.8e-24 IPB001305D 119-164 0.034 IPB001305F 188-239 0.12Significant hit ( 6.5e-71) to 7/8 blocks of the PR00625 family, which is described as \"DnaJ protein family signature\". Prints database entry for PR:PR00625. PR00625B 18-38 2.3e-14 PR00625C 108-127 9.4e-09 PR00625D 133-143 0.0014 PR00625E 147-165 2.2e-08 PR00625F 167-182 2e-07 PR00625G 186-202 2.2e-07 PR00625H 232-249 9e-12 PR00625D 155-165 0.013 PR00625D 169-179 0.024 PR00625D 116-126 0.029 PR00625E 108-126 0.16 PR00625E 161-179 0.94 PR00625F 131-146 0.003 PR00625F 153-168 0.042 PR00625F 114-129 0.15 PR00625H 86-103 0.016Significant hit ( 8.6e-15) to 1/2 blocks of the IPB001623 family, which is described as \"DnaJ N-terminal domain\". Interpro entry for IP:IPR001623. IPB001623B 17-38 8.7e-15","Residues 89 to 225 match (2e-07) PD:PD311578 which is described as POSSIBLE DNAJ ","","","","","","","","","","","","Mon Dec 16 09:54:41 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00659 is paralogously related to AA00688 (8e-26).","","","","","","Residues 196 to 317 (E-value = 1.1e-79) place AA00659 in the DnaJ_C family which is described as DnaJ C terminal region (PF01556)","","","","Yoshida,A., Nakano,Y., Yamashita,Y., Yu,H., Ohishi,M. and Koga,T.Isolation and characterization of the dnaKJ operon fromActinobacillus actinomycetemcomitansDNA Seq. 8 (1-2), 93-98 (1997)PubMed: 9522128","Zavilgelsky GB, Kotova VY, Mazhul' MM, Manukhov IV.Role of Hsp70 (DnaK-DnaJ-GrpE) and Hsp100 (ClpA and ClpB) Chaperones in Refolding and Increased Thermal Stability ofBacterial Luciferases in Escherichia coli Cells.Biochemistry (Mosc). 2002 Sep;67(9):986-92.PMID: 12387711Nam SH, Walsh MK.Affinity purification and characterization of the Escherichia coli molecular chaperones.Protein Expr Purif. 2002 Mar;24(2):282-91.PMID: 11858724","Mon Dec 16 09:54:41 2002","Mon Dec 16 09:54:41 2002","1","","","" "AA00660","453395","453171","225","ATGAATACAAGACTAGAAATTAAACAATGGGGAAATAGCAAGGCAATTCGCTTACCGAAAGATTTTATTCATACACTAAATCTTGATACGGGTGATTTTTTAGAATTAAACCAAGTGGATAATAAATTTATTTTAACGGTTAATCGAGCGATTAAGAAAGTGGAAACTGCACCCATTGAGTTAGTGCAGGAAGTCCAAGATATTATCACAGCAATCGTTAATGAT","","","8587","MNTRLEIKQWGNSKAIRLPKDFIHTLNLDTGDFLELNQVDNKFILTVNRAIKKVETAPIELVQEVQDIITAIVND","453173","","hypothetical protein","Cytoplasm","","
InterPro
IPR007159
Domain
SpoVT/AbrB-like, predicted transcription regulator
PF04014\"[8-53]TSpoVT_AbrB
noIPR
unintegrated
unintegrated
G3DSA:2.10.260.10\"[3-55]Tno description


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Dec 16 09:57:28 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00660 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00661","454591","453542","1050","ATGAAAAAGACAGTAATCGCATTAGCAATCGCTGCATTAGCAGCAACCGGCACGGCAAGTGCTGTAAAAGTTTATAATCAGGATGGTACGAAAGTTGAGCTTGGTGGTTCAATGCGTATCTTCTTAGGCAAGTTAGGTAAAAATCAACGTGGTGACCTTGTAAATGATGGTTCCCGTATTAAAATTAAAGCGTCTCAAGAATTAGATAACGGCTTATCTGCATTTGTTAGTTATGAGCTTCGTTTCGAAAGAGAAGCTCTTAAAAACAAGCAAAAGGCAAGTAATAATTTTGGTGATCCGACAACTCGTAAATTATTTGTTGGTTTAGGCTTCAAAGATGTGGGTGAGTTAAGTTTTGGTCGCCAGTCTACTAATGCAGATGATGTTTTGGGTGACAGCCTATATTATGGTTCAGGCGATTTAAGTGACTTGACCACTCGTTCTGACAAATCTGTTAAATTCCGGTCTGCAGATTTTAATGGGTTTAGTTTTGGTGTGGATTACTTATTTGGTAATGCAGAGAAGTATAAAGGAACAGCTAATGCGAATCGCTATAAGAATGGTTATGGTGTAGCGGCTTTTTACAATTATGATTTTGCAGAAAATCATAAAATTGACTTTGGTGCTACTTATGCGGTTGACCAATATGATACGTTGACAAGTTCATCAACCAACCGTAAAGAACACAAGTGGTTGCTTGCAACTCACTATCAGCTTGATGCATTGAAGTTAGGCGTAGCATATGGACAATATCATTCTAAAACTAAAGGTGTAGAAGCTGTTAAAACTCGTTATATTTTCTTAGAAGGTAAGTATGACTTGAATGAACTTACAGGTATTCCAACAACCTTTGGTTTACAATGGGAAAGAAAGAGTGCAAAACAAACTTCAGCAGCGCCAAGCCATATTGAAAATCACTATATTGTGAATGTTGATTATGAATTTAATAAACATGTAATTCCTTATGTGTCATATATTCGTGCAACTGATAAAGATGATAAAATCCGTAAAAACGAAAATATTTATGGTGCAGGTTTGCGTGTATTTTTC","","","39405","MKKTVIALAIAALAATGTASAVKVYNQDGTKVELGGSMRIFLGKLGKNQRGDLVNDGSRIKIKASQELDNGLSAFVSYELRFEREALKNKQKASNNFGDPTTRKLFVGLGFKDVGELSFGRQSTNADDVLGDSLYYGSGDLSDLTTRSDKSVKFRSADFNGFSFGVDYLFGNAEKYKGTANANRYKNGYGVAAFYNYDFAENHKIDFGATYAVDQYDTLTSSSTNRKEHKWLLATHYQLDALKLGVAYGQYHSKTKGVEAVKTRYIFLEGKYDLNELTGIPTTFGLQWERKSAKQTSAAPSHIENHYIVNVDYEFNKHVIPYVSYIRATDKDDKIRKNENIYGAGLRVFF","453544","","outer membrane protein","Outer membrane, Extracellular","","
InterPro
IPR001702
Family
Porin, Gram-negative type
PF00267\"[27-350]TPorin_1
InterPro
IPR001897
Domain
Porin, bacterial type
PR00183\"[22-38]T\"[102-124]TECOLIPORIN
InterPro
IPR003229
Domain
Porin, outer membrane
PD000808\"[25-82]TOP28_HAEIN_Q48221;
noIPR
unintegrated
unintegrated
G3DSA:2.40.160.10\"[22-350]Tno description
signalp\"[1-21]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","BeTs to 3 clades of COG3203COG name: Outer membrane protein (porin)Functional Class: MThe phylogenetic pattern of COG3203 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","Significant hit ( 2.7e-13) to 3/7 blocks of the IPB003229 family, which is described as \"Outer membrane protein P2\". Interpro entry for IP:IPR003229. IPB003229A 2-37 8.2e-06 IPB003229B 37-84 0.00058 IPB003229G 335-350 7.1Significant hit ( 3.6e-10) to 5/6 blocks of the IPB001702 family, which is described as \"General diffusion Gram-negative porins\". Interpro entry for IP:IPR001702. IPB001702A 60-79 53 IPB001702B 93-123 0.34 IPB001702C 150-168 0.06 IPB001702D 187-197 1.5e+02 IPB001702F 304-324 0.29","Residues 62 to 350 match (2e-10) PD:PD345115 which is described as MEMBRANE OUTER P2 PORIN SIGNAL PRECURSOR TRANSMEMBRANE OMP ","","","","","","","","","","","","Mon Dec 16 10:00:02 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00661 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 27 to 350 (E-value = 2.7e-06) place AA00661 in the Porin_1 family which is described as Gram-negative porin (PF00267)","","","","Komatsuzawa,H., Asakawa,R., Kawai,T., Ochiai,K., Fujiwara,T.,Taubman,M.A., Ohara,M., Kurihara,H. and Sugai,MIdentification of six major outer membrane proteins fromActinobacillus actinomycetemcomitansGene 288 (1-2), 195-201 (2002)PubMed: 12034509Kokeguchi,S., Kato,K., Nishimura,F., Kurihara,H. and Murayama,Y.Isolation and partial characterization of a 39 kDa major outermembrane protein of Actinobacillus actinomycetemcomitans Y4FEMS Microbiol. Lett. 77, 85-90 (1991)","","Tue Feb 11 16:55:59 2003","","1","","","" "AA00662","455587","454808","780","ATGGGAGGTCAAATTGCGCAATTGATTCGACCGAATACAAAAGTATTGTTCCTTGAAGCACCAAGTTCGCTCACCATGGAAGTGGCGAATATTCCCGCGATGGTGAAGGCTGTGCGGGAAGTCAATCCGGAAATTGTCATTATGATTGATAATACTTGGGCGGGCGGTGTGCTATTTAAAGCCTTAGAACATGATATTGATATTTCCATTCAAGCGGGCACAAAGTATTTGGTAGGGCATTCCGACATCATGATTGGCACGGCGGTATCCAATGCGCGCTGCTGGGATCAGCTACGGGAACATTCCTATTTAATGGGGCAAATGGCGGATGCTGATAGTGCCTATATTACAGCGCGTGGGTTACGCACATTGGGCATTCGCTTGAAGCAACACGAAGAAAGCAGCATAAAAATAGCGCAATGGTTGACGCAACAACCGGAAGTTAAGGCAGTTTATCATCCGGCACTACCGAGCTGTCCCGGGCATGAATTTTTTAAACGGGACTTTCTCGGCGCCAGTGGTTTATTTTCTTTTGAATTAAAACAAAGACTTACGCAACAACAATTGGAGATTTTTATGAATCATTTCCAATTATTTACCATGGCATATTCTTGGGGCGGTTTTGAATCGCTCATTCTTTATAACCAACCGGAAGAGATTGCAAAAATTCGTTCGAATATTCAGAGAAAATTAGAAGGCACATTAATTCGGCTGCATATCGGATTAGAAAATGTTGATGATTTAATTGCAGATTTAAGCGCCGGATTTATGCGTTTAAAA","","","32722","MGGQIAQLIRPNTKVLFLEAPSSLTMEVANIPAMVKAVREVNPEIVIMIDNTWAGGVLFKALEHDIDISIQAGTKYLVGHSDIMIGTAVSNARCWDQLREHSYLMGQMADADSAYITARGLRTLGIRLKQHEESSIKIAQWLTQQPEVKAVYHPALPSCPGHEFFKRDFLGASGLFSFELKQRLTQQQLEIFMNHFQLFTMAYSWGGFESLILYNQPEEIAKIRSNIQRKLEGTLIRLHIGLENVDDLIADLSAGFMRLK","454810","","cystathionine beta-lyase","Cytoplasm","","
InterPro
IPR000277
Family
Cys/Met metabolism pyridoxal-phosphate-dependent enzymes
PTHR11808\"[1-259]TTRANS-SULFURATION ENZYME FAMILY MEMBER
PF01053\"[3-257]TCys_Met_Meta_PP
PS00868\"[67-81]TCYS_MET_METAB_PP
InterPro
IPR006233
Family
Cystathionine beta-lyase, bacterial
PTHR11808:SF8\"[1-259]TCYSTATHIONINE BETA-LYASE
TIGR01324\"[1-259]Tcysta_beta_ly_B: cystathionine beta-lyase
InterPro
IPR015421
Domain
Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10\"[4-121]Tno description
InterPro
IPR015422
Domain
Pyridoxal phosphate-dependent transferase, major region, subdomain 2
G3DSA:3.90.1150.10\"[122-260]Tno description


","BeTs to 17 clades of COG0626COG name: Cystathionine beta-lyases/cystathionine gamma-synthasesFunctional Class: EThe phylogenetic pattern of COG0626 is -o-pkzy-vdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-57) to 5/6 blocks of the IPB000277 family, which is described as \"Cys/Met metabolism pyridoxal-phosphate-dependent enzymes\". Interpro entry for IP:IPR000277. IPB000277B 11-44 5e-09 IPB000277C 50-85 6e-17 IPB000277D 106-146 1.7e-13 IPB000277E 204-220 0.011 IPB000277F 235-252 1.6e-09","Residues 1 to 52 match (2e-07) PD:PD558816 which is described as PROTEOME COMPLETE LYASE PYRIDOXAL PHOSPHATE TRANSFERASE CYSTEINE 4.4.1.- SYNTHASE CYSTATHIONINE ","","","","","","","","","","","","Mon Dec 16 10:07:31 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00662 is paralogously related to AA02917 (2e-36).","","","","","","Residues 2 to 257 (E-value = 5.6e-54) place AA00662 in the Cys_Met_Meta_PP family which is described as Cys/Met metabolism PLP-dependent enzyme (PF01053)","","","","","Aubel D, Germond JE, Gilbert C, Atlan D.Isolation of the patC gene encoding the cystathionine beta-lyase of Lactobacillus delbrueckii subsp. bulgaricus and molecular analysis of inter-strain variability in enzyme biosynthesis.Microbiology. 2002 Jul;148(Pt 7):2029-36.PMID: 12101291 Auger S, Yuen WH, Danchin A, Martin-Verstraete I.The metIC operon involved in methionine biosynthesis in Bacillus subtilis is controlled by transcription antitermination.Microbiology. 2002 Feb;148(Pt 2):507-18.PMID: 11832514 Fernandez M, Kleerebezem M, Kuipers OP, Siezen RJ, van Kranenburg Regulation of the metC-cysK operon, involved in sulfur metabolism in Lactococcus lactis.J Bacteriol. 2002 Jan;184(1):82-90.PMID: 11741847Liu R, Blackwell TW, States DJ.Conformational model for binding site recognition by the E.coli MetJ transcription factor.Bioinformatics. 2001 Jul;17(7):622-33.PMID: 1144888","","Mon Dec 16 10:07:31 2002","1","","","" "AA00663","455994","455680","315","ATGTCAAAAAAATTCTCTTTAGCCACCACATTCGTTCATGCCGGCAGAAAAAAACGTTATACCCACGGTTCCGTCAATCCGGTAGTACAACGCGCTTCATCGTTGGTATTTGATTCTTTAGCGGATAAGAAACACGCCACCATTAATCGTGCCAAAGGTGAATTATTTTATGGCAGACGGGGAACCTTAACCCATTTTGCCTTGCAAGATGCGATGTGTGAATTGGAGGGCGGGGCAGGTTGCTATTTGTATCCGTGCGGTGCGGCTGCCGTGACTAACAGTATTCTTTCTTTTGACAAACCGGTGACCATATCT","","","11368","MSKKFSLATTFVHAGRKKRYTHGSVNPVVQRASSLVFDSLADKKHATINRAKGELFYGRRGTLTHFALQDAMCELEGGAGCYLYPCGAAAVTNSILSFDKPVTIS","455682","","cystathionine beta-lyase","Periplasm, Cytoplasm, Extracellular","","
InterPro
IPR000277
Family
Cys/Met metabolism pyridoxal-phosphate-dependent enzymes
PF01053\"[8-98]TCys_Met_Meta_PP
noIPR
unintegrated
unintegrated
G3DSA:4.10.550.20\"[2-61]Tno description


","BeTs to 14 clades of COG0626COG name: Cystathionine beta-lyases/cystathionine gamma-synthasesFunctional Class: EThe phylogenetic pattern of COG0626 is -o-pkzy-vdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 9.1e-07) to 1/6 blocks of the IPB000277 family, which is described as \"Cys/Met metabolism pyridoxal-phosphate-dependent enzymes\". Interpro entry for IP:IPR000277. IPB000277A 54-75 9.4e-07","Residues 1 to 98 match (8e-38) PD:PD090161 which is described as LYASE COMPLETE PROTEOME CYSTATHIONINE GAMMA-SYNTHASE SULFHYDRYLASE O-SUCCINYLHOMOSERINE BETA-LYASE PYRIDOXAL BIOSYNTHESIS ","","","","","","","","","","","","Mon Dec 16 10:18:38 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00663 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Aubel D, Germond JE, Gilbert C, Atlan D. Isolation of the patC gene encoding the cystathionine beta-lyaseof Lactobacillus delbrueckii subsp. bulgaricus and molecularanalysis of inter-strain variability in enzyme biosynthesis. Microbiology. 2002 Jul;148(Pt 7):2029-36. PMID: 12101291 Auger S, Yuen WH, Danchin A, Martin-Verstraete I. The metIC operon involved in methionine biosynthesis in Bacillussubtilis is controlled by transcription antitermination. Microbiology. 2002 Feb;148(Pt 2):507-18. PMID: 11832514 Fernandez M, Kleerebezem M, Kuipers OP, Siezen RJ, vanKranenburg Regulation of the metC-cysK operon, involved insulfur metabolism in Lactococcus lactis. J Bacteriol. 2002 Jan;184(1):82-90. PMID: 11741847 Liu R, Blackwell TW, States DJ. Conformational model for binding site recognition by the E.coliMetJ transcription factor. Bioinformatics. 2001 Jul;17(7):622-33. PMID: 1144888","","Mon Dec 16 10:12:29 2002","1","","","" "AA00664","456250","456804","555","ATGAAATTTAACATCCCCATTTTTCTGACGCTATTTCGGATTATTTTAATTCCTTTCTTTATCATCGCTTTCTACCTCCCCTTTGATTGGGCGCCATTTTTAACTACTCTAATTTTTTTCATCGCCGGAGTGACCGATTGGTTGGACGGCTATCTAGCACGCAAATGGAAACAAACCACCAGCTTCGGCGCATTTTTGGATCCCGTTGCGGATAAAGTCATGGTGGTTGCCGGGCTTGTATTGGTTGTGGAATACAATCACACTTTTTGGATCACATTGCCGGCCATTGTGGTTATTTCCCGCGAAATTATTATCTCCGCGTTGCGTGAATGGATGGCAGAATTAGGCAGTCGTAGCAAAGTTGCGGTATCTTGGTTGGGAAAAGTCAAAACCACATCACAAATGTTGGCGTTAGGCGGGTTGTTATGGCGTTATAACTTTGCCATGGAAGTAATTGCCATTGTCCTGCTTTATATTGCTGCGATTTTAACCATTTGGTCAATGTTGCAATATCTCACTGCAGCAAAAGACAGCTTGTTGGAAGACTTCCACAAA","","","21146","MKFNIPIFLTLFRIILIPFFIIAFYLPFDWAPFLTTLIFFIAGVTDWLDGYLARKWKQTTSFGAFLDPVADKVMVVAGLVLVVEYNHTFWITLPAIVVISREIIISALREWMAELGSRSKVAVSWLGKVKTTSQMLALGGLLWRYNFAMEVIAIVLLYIAAILTIWSMLQYLTAAKDSLLEDFHK","456806","","phosphatidylglycerophosphate synthase (CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase)","Inner membrane, Cytoplasm","","
InterPro
IPR000462
Family
CDP-alcohol phosphatidyltransferase
PF01066\"[36-174]TCDP-OH_P_transf
PS00379\"[49-71]TCDP_ALCOHOL_P_TRANSF
InterPro
IPR004570
Family
CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
TIGR00560\"[3-182]TpgsA: CDP-diacylglycerol--glycerol-3-phosph
noIPR
unintegrated
unintegrated
PIRSF000847\"[3-183]TCDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
PTHR14269\"[3-182]TCDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE-RELATED
PTHR14269:SF3\"[3-182]TCDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE
signalp\"[1-23]?signal-peptide
tmhmm\"[5-25]?\"[31-51]?\"[151-169]?transmembrane_regions


","BeTs to 22 clades of COG0558COG name: Phosphatidylglycerophosphate synthaseFunctional Class: IThe phylogenetic pattern of COG0558 is aompkzyqv-rlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.8e-20) to 1/1 blocks of the IPB000462 family, which is described as \"CDP-alcohol phosphatidyltransferase\". Interpro entry for IP:IPR000462. IPB000462 46-82 2.7e-20","Residues 38 to 72 match (7e-08) PD:PD483200 which is described as TRANSFERASE COMPLETE CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE PROTEOME SYNTHASE 3-PHOSPHATIDYLTRANSFERASE PHOSPHATIDYLTRANSFERASE TRANSMEMBRANE PHOSPHATIDYLGLYCEROPHOSPHATE 3- ","","","","","","","","","","","","Mon Dec 16 10:46:40 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00664 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 36 to 174 (E-value = 6.9e-42) place AA00664 in the CDP-OH_P_transf family which is described as CDP-alcohol phosphatidyltransferase (PF01066)","","","","","Gopalakrishnan AS, Chen YC, Temkin M, Dowhan W. Structure and expression of the gene locus encoding thephosphatidylglycerophosphate synthase of Escherichia coli. J Biol Chem 1986 Jan 25;261(3):1329-38. PubMed: 3003065. Usui M, Sembongi H, Matsuzaki H, Matsumoto K, Shibuya I. Primary structures of the wild-type and mutant alleles encoding thephosphatidylglycerophosphate synthase of Escherichia coli. J Bacteriol 1994 Jun;176(11):3389-92. PubMed: 8195097. ","","Mon Dec 16 10:46:40 2002","1","","","" "AA00665","457335","457610","276","ATGTGCATTAACCACACTTCTAAAAAACCTTACATTATTACAATCGCCTGTACCAAAGGTGGTTCTGCCAAAAGCACTAATGCTGCTAATATCGGTGCATTTTGTGCAGACCATGGTTTAAGAACCTTACTGATTGATACAGATACACAACCGACACTAAGCTCTTACTATAGTTTAGCTGAAACCGCTCCCGGCGGAATTCATGAGTTTCTATCGCTGCGTGATATCGCCATAGTGCTGCCGAATATCACAAAAAGGGGGATGTCGGCGTTTCGT","","","9826","MCINHTSKKPYIITIACTKGGSAKSTNAANIGAFCADHGLRTLLIDTDTQPTLSSYYSLAETAPGGIHEFLSLRDIAIVLPNITKRGMSAFR","","","plasmid protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[11-74]Tno description


","No hits to the COGs database.","Significant hit ( 5.9e-06) to 1/4 blocks of the IPB003348 family, which is described as \"Anion-transporting ATPase\". Interpro entry for IP:IPR003348. IPB003348A 14-51 5.4e-06","Residues 12 to 59 match (1e-17) PD:PD585548 which is described as PROTEOME COMPLETE RELATED PARTITIONING PLASMID STY4521 CHROMOSOME ","Wed Nov 20 11:26:07 2002","","","Wed Nov 20 11:26:07 2002","Wed Nov 20 11:26:24 2002","","","Wed Nov 20 11:26:24 2002","Wed Nov 20 11:26:24 2002","Wed Nov 20 11:26:07 2002","Wed Nov 20 11:26:07 2002","Wed Jan 15 13:33:08 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00665 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","Mayer,M.P., Bueno,L.C., Hansen,E.J. and DiRienzo,J.M.Identification of a cytolethal distending toxin gene locus and features of a virulence-associated region in Actinobacillus actinomycetemcomitansInfect. Immun. 67 (3), 1227-1237 (1999)PubMed: 10024565","","Wed Jan 15 13:34:12 2003","","1","","2","" "AA00666","457610","457714","105","TTGAAAAGTCGTTTAATTCGCGTCAAAATGATTAAAGTTGACGGCGAGTTAAAATACCAGGAAACGAAAAAAGACAAACCTGCCGATGAAAATGAAGCTTTAGCT","","","4041","LKSRLIRVKMIKVDGELKYQETKKDKPADENEALA","457714","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 10:05:50 2004","Mon Feb 23 10:05:50 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00666 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 10:05:50 2004","","","","","","","","","","","","","1","","2","" "AA00667","458640","458083","558","ATGAAAAAATATTTATTGAGCTTCTTATTAAGCATGATATTGACTTTGACGAGTCATGCAGAATCAAATCCTGATCCGACTACTTATCCTGATGTAGAGTTATCGCCTCCTCCACGTATTAGCTTGCGTAGTTTGCTTACGGCTCAACCAATTAAAAATGACCATTATGATTCACATAATTATTTAAGTACACATTGGGAATTAATTGATTACAAGGGAAAAGAATATGAAAAATTACGTGACGGTGGTACGTTGGTTCAATTTAAAGTGGTCGGTGCAGCAAAATGTTTTGCTTTCCCAGGCGAAGGCACAACTGATTGTAAAGATATTGATCATACTGTGTTTAACCTTATTCCAACTAATACAGGTGCGTTTTTAATCAAAGATGCCCTATTAGGATTTTGTATGACAAGCCATGACTTTGATGATTTGAGGCTTGAACCTTGTGGAATTTCAGTGAGTGGTCGAACCTTTTCGTTGGCGTATCAATGGGGAATATTACCTCCTTTTGGGCCAAGTAAAATTTTAAGACCACCGGTGGGGAGAAATCAGGGTAGC","","","21741","MKKYLLSFLLSMILTLTSHAESNPDPTTYPDVELSPPPRISLRSLLTAQPIKNDHYDSHNYLSTHWELIDYKGKEYEKLRDGGTLVQFKVVGAAKCFAFPGEGTTDCKDIDHTVFNLIPTNTGAFLIKDALLGFCMTSHDFDDLRLEPCGISVSGRTFSLAYQWGILPPFGPSKILRPPVGRNQGS","458085","","cytolethal distending toxin protein C","Periplasm, Cytoplasm","","
InterPro
IPR003558
Family
Cytolethal distending toxin A
PF03498\"[39-178]TCDtoxinA
InterPro
IPR003559
Family
Cytolethal distending toxin C
PIRSF009093\"[1-180]TCytolethal distending toxin, subunit C
noIPR
unintegrated
unintegrated
G3DSA:2.80.10.50\"[21-186]Tno description
signalp\"[1-20]?signal-peptide


","No hits to the COGs database.","","Residues 1 to 186 match (3e-97) PD:PD103788 which is described as C CYTOLETHAL TOXIN DISTENDING ","","","","","","","","","","","","Mon Dec 16 10:52:50 2002","","Tue Feb 8 14:18:26 2005","","Tue Feb 8 14:18:26 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA00667 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Tue Feb 8 14:18:26 2005","","","","","Residues 8 to 140 (E-value = 6.7e-85) place AA00667 in the CDtoxinC family which is described as Cytolethal distending toxin C (PF03499)","Tue Feb 8 14:18:26 2005","",""," Ueno Y, Ohara M, Kawamoto T, Fujiwara T, Komatsuzawa H, Oswald E, Sugai M.,Biogenesis of the Actinobacillus actinomycetemcomitans cytolethal distending toxin holotoxin.Infect Immun. 2006 Jun;74(6):3480-7.PMID: 16714579Tan KS, Ong G, Song KP.Introns in the cytolethal distending toxin gene of Actinobacillus actinomycetemcomitans.J Bacteriol. 2005 Jan;187(2):567-75.PMID: 15629928Belibasakis GN, Johansson A, Wang Y, Chen C, Kalfas S, Lerner UH.The cytolethal distending toxin induces receptor activator of NF-kappaB ligand expression in human gingival fibroblasts and periodontal ligament cells.Infect Immun. 2005 Jan;73(1):342-51.PMID: 15618171Belibasakis GN, Mattsson A, Wang Y, Chen C, Johansson A.Cell cycle arrest of human gingival fibroblasts and periodontal ligament cells by Actinobacillus actinomycetemcomitans: involvement of the cytolethal distending toxin.APMIS. 2004 Oct;112(10):674-85.PMID: 15601319Thelestam M, Frisan T.A. actinomycetemcomitans cytolethal distending toxin.J Immunol. 2004 May;172(10):5813; author reply 5813-4.PMID: 15128757Shenker BJ, Besack D, McKay T, Pankoski L, Zekavat A, Demuth DR.Actinobacillus actinomycetemcomitans cytolethal distending toxin (Cdt): evidence that the holotoxin is composed of three subunits: CdtA, CdtB, and CdtC.J Immunol. 2004 Jan;172(1):410-7.PMID: 14688349Mise K, Akifusa S, Watarai S, Ansai T, Nishihara T, Takehara T.Involvement of ganglioside GM3 in G(2)/M cell cycle arrest of human monocytic cells induced by Actinobacillus actinomycetemcomitans cytolethal distending toxin.Infect Immun. 2005 Aug;73(8):4846-52.PMID: 16040998Kanno F, Korostoff J, Volgina A, Dirienzo JM.Resistance of Human Periodontal Ligament Fibroblasts to the Cytolethal Distending Toxin of Actinobacillus actinomycetemcomitans.J Periodontol. 2005 Jul;76(7):1189-201.PMID: 16018764Kang P, Korostoff J, Volgina A, Grzesik W, Dirienzo JM.Differential effect of the cytolethal distending toxin of Actinobacillus actinomycetemcomitans on co-cultures of human oral cells.J Med Microbiol. 2005 Aug;54(Pt 8):785-94.PMID: 16014433Akifusa S, Heywood W, Nair SP, Stenbeck G, Henderson B.Mechanism of internalization of the cytolethal distending toxin of Actinobacillus actinomycetemcomitans.Microbiology. 2005 May;151(Pt 5):1395-402.PMID: 15870449Ahmed HJ, Svensson LA, Cope LD, Latimer JL, Hansen EJ, Ahlman K,Bayat-Turk J, Klamer D, Lagergard T.Prevalence of cdtABC genes encoding cytolethal distending toxin among Haemophilus ducreyi and Actinobacillus actinomycetemcomitans strains.J Med Microbiol. 2001 Oct;50(10):860-4.PMID: 11599734Shenker,B.J., Hoffmaster,R.H., McKay,T.L. and Demuth,D.R.Expression of the cytolethal distending toxin (Cdt) operon inActinobacillus actinomycetemcomitans: evidence that the CdtBprotein is responsible for G2 arrest of the cell cycle in human TcellsJ. Immunol. 165 (5), 2612-2618 (2000)PubMed: 10946289Shenker,B.J., McKay,T., Datar,S., Miller,M., Chowhan,R. andDemuth,D.Actinobacillus actinomycetemcomitans immunosuppressive protein is a member of the family of cytolethal distending toxins capable ofcausing a G2 arrest in human T cellsJ. Immunol. 162 (8), 4773-4780 (1999)PubMed: 10202019Mayer,M.P., Bueno,L.C., Hansen,E.J. and DiRienzo,J.M.Identification of a cytolethal distending toxin gene locus andfeatures of a virulence-associated region in Actinobacillus actinomycetemcomitansInfect. Immun. 67 (3), 1227-1237 (1999)PubMed: 10024565Sugai,M., Kawamoto,T., Peres,S.Y., Ueno,Y., Komatsuzawa,H., Fujiwara,T., Kurihara,H., Suginaka,H. and Oswald,E.The cell cycle-specific growth-inhibitory factor produced by Actinobacillus actinomycetemcomitans is a cytolethal distending toxinInfect. Immun. 66 (10), 5008-5019 (1998)PubMed: 9746611","Cortes-Bratti X, Chaves-Olarte E, Lagergard T, Thelestam M. The cytolethal distending toxin from the chancroid bacteriumHaemophilus ducreyi induces cell-cycle arrest in the G2 phase. J Clin Invest. 1999 Jan;103(1):107-15. PMID: 9884340 Wising C, Svensson LA, Ahmed HJ, Sundaeus V, Ahlman K, Jonsson IM,Molne L, Lagergard T. Toxicity and immunogenicity of purified Haemophilus ducreyicytolethal distending toxin in a rabbit model. Microb Pathog. 2002 Aug;33(2):49-62. PMID: 12202104 Svensson LA, Henning P, Lagergard T. The cytolethal distending toxin of Haemophilus ducreyi inhibitsendothelial cell proliferation. Infect Immun. 2002 May;70(5):2665-9. PMID: 11953409 Li L, Sharipo A, Chaves-Olarte E, Masucci MG, Levitsky V, Thelestam M, Frisan T. The Haemophilus ducreyi cytolethal distending toxin activates sensorsof DNA damage and repair complexes in proliferating andnon-proliferating cells. Cell Microbiol. 2002 Feb;4(2):87-99. PMID: 11896765 Frisan T, Cortes-Bratti X, Thelestam M. Cytolethal distending toxins and activation of DNA damage-dependent checkpoint responses. Int J Med Microbiol. 2002 Feb;291(6-7):495-9. Review. PMID: 11890549 ","Thu Aug 4 09:06:34 2005","Mon Dec 16 10:59:02 2002","1","","2","" "AA00668","459502","458654","849","ATGCAATGGGTAAAGCAATTAAATGTGGTTTTCTGTACGATGTTATTTAGCTTTTCAAGTTATGCTAACTTGAGTGATTTCAAAGTAGCAACTTGGAATCTGCAAGGTTCTTCAGCTGTAAATGAAAGTAAATGGAATATTAATGTGCGCCAATTATTATCGGGAGAACAAGGTGCAGATATTTTGATGGTACAAGAAGCGGGTTCATTACCAAGTTCGGCAGTAAGAACCTCACGAGTAATTCAACATGGGGGAACGCCAATTGAGGAATATACCTGGAATTTAGGTACTCGCTCCCGTCCAAATATGGTCTATATTTATTATTCCCGTTTAGATGTTGGGGCAAACCGAGTGAACTTAGCTATCGTGTCACGTCGTCAAGCCGATGAAGCTTTTATCGTACATTCTGATTCTTCTGTGCTTCAATCTCGCCCGGCAGTAGGTATCCGCATTGGTACTGATGTATTTTTTACAGTGCATGCTTTGGCCACAGGTGGTTCTGATGCGGTAAGTTTAATTCGTAATATCTTCACTACTTTTACCTCATCACCATCATCACCGGAAAGACGAGGATATAGCTGGATGGTTGTTGGTGATTTCAATCGTGCGCCGGTTAATCTGGAAACTGCATTAAGACAGGAACCCGCCGTGAGTGAAAATACAATTATTATTGCGCCAACAGAACCGACTCATCGGTCCGGTAATATTTTAGATTATGCGATTTTACATGACGCACATTTACCACGTCGAGAGCAAGCACGTGAACGTATCGGCGCAAGTTTAATGTTAAATCAGTTACGCTCACAAATTACATCCGATCATTTTCCTGTTAGTTTTGTTCATGATCGC","","","31511","MQWVKQLNVVFCTMLFSFSSYANLSDFKVATWNLQGSSAVNESKWNINVRQLLSGEQGADILMVQEAGSLPSSAVRTSRVIQHGGTPIEEYTWNLGTRSRPNMVYIYYSRLDVGANRVNLAIVSRRQADEAFIVHSDSSVLQSRPAVGIRIGTDVFFTVHALATGGSDAVSLIRNIFTTFTSSPSSPERRGYSWMVVGDFNRAPVNLETALRQEPAVSENTIIIAPTEPTHRSGNILDYAILHDAHLPRREQARERIGASLMLNQLRSQITSDHFPVSFVHDR","458656","","cytolethal distending toxin protein B","Outer membrane, Periplasm, Extracellular","","
InterPro
IPR003539
Family
Cytolethal distending toxin B
PR01388\"[24-45]T\"[65-85]T\"[99-117]T\"[144-163]T\"[193-208]T\"[261-277]TCDTOXINB
PIRSF018539\"[7-283]TCytolethal distending toxin, subunit B
InterPro
IPR005135
Domain
Endonuclease/exonuclease/phosphatase
PF03372\"[27-281]TExo_endo_phos
noIPR
unintegrated
unintegrated
G3DSA:3.60.10.10\"[23-283]Tno description
signalp\"[1-22]?signal-peptide


","No hits to the COGs database.","Significant hit ( 3e-106) to 6/6 blocks of the PR01388 family, which is described as \"Cytolethal distending toxin B signature\". Prints database entry for PR:PR01388. PR01388A 24-45 2.8e-21 PR01388B 65-85 2.3e-17 PR01388C 99-117 5.8e-17 PR01388D 144-163 2.6e-17 PR01388E 193-208 2.1e-12 PR01388F 261-277 2.9e-14","Residues 10 to 279 match (7e-141) PD:PD013904 which is described as DISTENDING CYTOLETHAL TOXIN B CDTB COMPLETE PROTEOME TOXIN-LIKE PLASMID TOXIN-IIIB ","","","","","Wed Feb 19 06:30:59 2003","","","","","","","Mon Dec 16 11:07:02 2002","","Tue Feb 8 14:57:39 2005","Tue Feb 8 15:02:36 2005","Tue Feb 8 14:57:39 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA00668 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Tue Feb 8 14:57:39 2005","","","","","Residues 27 to 281 (E-value = 1.2e-26) place AA00668 in the Exo_endo_phos family which is described as Endonuclease/Exonuclease/phosphatase family (PF03372)","Tue Feb 8 14:57:39 2005","",""," Ueno Y, Ohara M, Kawamoto T, Fujiwara T, Komatsuzawa H, Oswald E, Sugai M.,Free in PMC Biogenesis of the Actinobacillus actinomycetemcomitans cytolethal distending toxin holotoxin.Infect Immun. 2006 Jun;74(6):3480-7.PMID: 16714579Thelestam M, Frisan T.A. actinomycetemcomitans cytolethal distending toxin.J Immunol. 2004 May;172(10):5813; author reply 5813-4.PMID: 15128757Shenker BJ, Besack D, McKay T, Pankoski L, Zekavat A, Demuth DR.Actinobacillus actinomycetemcomitans cytolethal distending toxin (Cdt): evidence that the holotoxin is composed of three subunits: CdtA, CdtB, and CdtC.J Immunol. 2004 Jan;172(1):410-7.PMID: 14688349 Ahmed HJ, Svensson LA, Cope LD, Latimer JL, Hansen EJ, Ahlman K, Bayat-Turk J, Klamer D, Lagergard T.,Free Full Text Prevalence of cdtABC genes encoding cytolethal distending toxin among Haemophilus ducreyi and Actinobacillus actinomycetemcomitans strains.J Med Microbiol. 2001 Oct;50(10):860-4.PMID: 11599734Shenker,B.J., Hoffmaster,R.H., McKay,T.L. and Demuth,D.R.Expression of the cytolethal distending toxin (Cdt) operon inActinobacillus actinomycetemcomitans: evidence that the CdtBprotein is responsible for G2 arrest of the cell cycle in humanTcellsJ. Immunol. 165 (5), 2612-2618 (2000)PubMed: 10946289Shenker,B.J., McKay,T., Datar,S., Miller,M., Chowhan,R. andDemuth,D.,Actinobacillus actinomycetemcomitans immunosuppressive proteinis a member of the family of cytolethal distending toxinscapable of causing a G2 arrest in human T cellsJ. Immunol. 162 (8), 4773-4780 (1999)PubMed: 10202019Mayer,M.P., Bueno,L.C., Hansen,E.J. and DiRienzo,J.M.Identification of a cytolethal distending toxin gene locus andfeatures of a virulence-associated region in ActinobacillusactinomycetemcomitansInfect. Immun. 67 (3), 1227-1237 (1999)PubMed: 10024565Sugai,M., Kawamoto,T., Peres,S.Y., Ueno,Y., Komatsuzawa,H.,Fujiwara,T., Kurihara,H., Suginaka,H. and Oswald,E.The cell cycle-specific growth-inhibitory factor produced byActinobacillus actinomycetemcomitans is a cytolethal distendingtoxinInfect. Immun. 66 (10), 5008-5019 (1998)PubMed: 9746611","Cortes-Bratti X, Chaves-Olarte E, Lagergard T, Thelestam M. The cytolethal distending toxin from the chancroid bacterium Haemophilus ducreyi induces cell-cycle arrest in the G2 phase. J Clin Invest. 1999 Jan;103(1):107-15. PMID: 9884340 Wising C, Svensson LA, Ahmed HJ, Sundaeus V, Ahlman K, JonssonIM, Molne L, Lagergard T. Toxicity and immunogenicity of purified Haemophilus ducreyi cytolethal distending toxin in a rabbit model. Microb Pathog. 2002 Aug;33(2):49-62. PMID: 12202104 Svensson LA, Henning P, Lagergard T. The cytolethal distending toxin of Haemophilus ducreyi inhibits endothelial cell proliferation. Infect Immun. 2002 May;70(5):2665-9. PMID: 11953409 Li L, Sharipo A, Chaves-Olarte E, Masucci MG, Levitsky V,Thelestam M, Frisan T. The Haemophilus ducreyi cytolethal distending toxin activatessensorsof DNA damage and repair complexes in proliferating and non-proliferating cells. Cell Microbiol. 2002 Feb;4(2):87-99. PMID: 11896765 Frisan T, Cortes-Bratti X, Thelestam M. Cytolethal distending toxins and activation of DNAdamage-dependent checkpoint responses. Int J Med Microbiol. 2002 Feb;291(6-7):495-9. Review. PMID: 11890549","Tue Feb 8 15:02:36 2005","Wed Feb 19 06:30:59 2003","1","","2","" "AA00669","460185","459520","666","ATGAAAAAGTTTTTACCTGGTCTTTTATTGATGGGTTTAGTGGCTTGTTCGTCAAATCAACGAATGAGTGACTATTCTCAGCCTGAATCTCAATCTGATTTAGCACCTAAATCTTCAACAACACAACCCCAACCCCAACCCCTATTATCAAAAGCATCTTCAATGCCATTGAATTTGCTCTCTTCATCCAAGAATGGACAGGTATCGCCGTCTGAACCATCAAACTTTATGACTTTGATGGGACAAAATGGGGCACTGTTGACTGTCTGGGCGCTAGCAAAACGCAATTGGTTATGGGCTTATCCCAATATATATTCGCAGGACTTTGGAAATATTCGTAATTGGAAGATAGAACCTGGTAAACACCGTGAATATTTTCGTTTTGTTAATCAATCTTTAGGTACATGTATTGAAGCTTACGGTAATGGTTTAATTCATGATACTTGTAGTCTGGACAAATTAGCACAAGAGTTTGAGTTATTACCTACTGATAGTGGTGCGGTTGTCATTAAAAGTGTGTCACAAGGACGTTGTGTCACTTATAATCCTGTAAGTCCAACATATTATTCAACAGTTACATTATCAACTTGTGATGGCGCAACAGAACCATTACGTGATCAAACATGGTATCTCGCTCCTCCTGTATTAGAAGCAACAGCGGTTAAT","","","25279","MKKFLPGLLLMGLVACSSNQRMSDYSQPESQSDLAPKSSTTQPQPQPLLSKASSMPLNLLSSSKNGQVSPSEPSNFMTLMGQNGALLTVWALAKRNWLWAYPNIYSQDFGNIRNWKIEPGKHREYFRFVNQSLGTCIEAYGNGLIHDTCSLDKLAQEFELLPTDSGAVVIKSVSQGRCVTYNPVSPTYYSTVTLSTCDGATEPLRDQTWYLAPPVLEATAVN","459522","From Genbank:[gi:13878412] CDT are cytotoxins which induce cell distension, growth arrest in G2/M phase, nucleus swelling, and chromatin fragmentation in HELA cells.","cytolethal distending toxin protein A","Extracellular, Outer membrane, Periplasm","","
InterPro
IPR000772
Domain
Ricin B lectin
PS50231\"[122-211]TRICIN_B_LECTIN
InterPro
IPR003558
Family
Cytolethal distending toxin A
PR01387\"[47-60]T\"[84-101]T\"[106-120]T\"[128-140]T\"[165-179]T\"[188-202]TCDTOXINA
PIRSF036516\"[1-222]TCytolethal distending toxin, subunit A
PF03498\"[76-220]TCDtoxinA
noIPR
unintegrated
unintegrated
G3DSA:2.80.10.50\"[56-222]Tno description
PS51257\"[1-16]TPROKAR_LIPOPROTEIN
signalp\"[1-23]?signal-peptide


","No hits to the COGs database.","Significant hit ( 7.8e-67) to 6/6 blocks of the PR01387 family, which is described as \"Cytolethal distending toxin A signature\". Prints database entry for PR:PR01387. PR01387A 47-60 8e-05 PR01387B 84-101 6.1e-15 PR01387C 106-120 2.9e-12 PR01387D 128-140 1.3e-08 PR01387E 165-179 4.4e-09 PR01387F 188-202 1.7e-09","Residues 1 to 222 match (4e-113) PD:PD013678 which is described as TOXIN A DISTENDING CYTOLETHAL PRECURSOR LIPOPROTEIN SUBUNIT OUTER LECTIN CDT ","","","","","","","","","","","Mon Jan 6 17:52:03 2003","Mon Dec 16 11:09:00 2002","","Tue Feb 8 14:58:07 2005","Tue Feb 8 15:03:00 2005","Tue Feb 8 14:58:07 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA00669 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Tue Feb 8 14:58:07 2005","","","","","Residues 84 to 179 (E-value = 1.8e-73) place AA00669 in the CDtoxinA family which is described as Cytolethal distending toxin A (PF03498)","Tue Feb 8 14:58:07 2005","",""," Ueno Y, Ohara M, Kawamoto T, Fujiwara T, Komatsuzawa H, Oswald E, Sugai M.,Biogenesis of the Actinobacillus actinomycetemcomitans cytolethal distending toxin holotoxin.Infect Immun. 2006 Jun;74(6):3480-7.PMID: 16714579Thelestam M, Frisan T.A. actinomycetemcomitans cytolethal distending toxin.J Immunol. 2004 May;172(10):5813; author reply 5813-4.PMID: 15128757Shenker BJ, Besack D, McKay T, Pankoski L, Zekavat A, Demuth DR.Actinobacillus actinomycetemcomitans cytolethal distending toxin (Cdt): evidence that the holotoxin is composed of three subunits: CdtA, CdtB, and CdtC.J Immunol. 2004 Jan;172(1):410-7.PMID: 14688349Ahmed HJ, Svensson LA, Cope LD, Latimer JL, Hansen EJ, Ahlman K,Bayat-Turk J, Klamer D, Lagergard T.Prevalence of cdtABC genes encoding cytolethal distending toxinamong Haemophilus ducreyi and Actinobacillusactinomycetemcomitans strains.J Med Microbiol. 2001 Oct;50(10):860-4.PMID: 11599734Shenker,B.J., Hoffmaster,R.H., McKay,T.L. and Demuth,D.R.Expression of the cytolethal distending toxin (Cdt) operon inActinobacillus actinomycetemcomitans: evidence that the CdtBprotein is responsible for G2 arrest of the cell cycle in humanT cellsJ. Immunol. 165 (5), 2612-2618 (2000)PubMed: 10946289Shenker,B.J., McKay,T., Datar,S., Miller,M., Chowhan,R. andDemuth,D.Actinobacillus actinomycetemcomitans immunosuppressive proteinis a member of the family of cytolethal distending toxinscapable of causing a G2 arrest in human T cellsJ. Immunol. 162 (8), 4773-4780 (1999)PubMed: 10202019Mayer,M.P., Bueno,L.C., Hansen,E.J. and DiRienzo,J.M.Identification of a cytolethal distending toxin gene locus andfeatures of a virulence-associated region in ActinobacillusactinomycetemcomitansInfect. Immun. 67 (3), 1227-1237 (1999)PubMed: 10024565Sugai,M., Kawamoto,T., Peres,S.Y., Ueno,Y., Komatsuzawa,H.,Fujiwara,T., Kurihara,H., Suginaka,H. and Oswald,E.The cell cycle-specific growth-inhibitory factor produced byActinobacillus actinomycetemcomitans is a cytolethal distendingtoxinInfect. Immun. 66 (10), 5008-5019 (1998)PubMed: 9746611","Cortes-Bratti X, Chaves-Olarte E, Lagergard T, Thelestam M. The cytolethal distending toxin from the chancroid bacterium Haemophilus ducreyi induces cell-cycle arrest in the G2 phase. J Clin Invest. 1999 Jan;103(1):107-15. PMID: 9884340 Wising C,Svensson LA, Ahmed HJ, Sundaeus V, Ahlman K,JonssonIM, Molne L, Lagergard T. Toxicity and immunogenicity of purified Haemophilus ducreyi cytolethal distending toxin in a rabbit model. Microb Pathog. 2002 Aug;33(2):49-62. PMID: 12202104 Svensson LA, Henning P, Lagergard T. The cytolethal distending toxin of Haemophilus ducreyi inhibits endothelial cell proliferation. Infect Immun. 2002 May;70(5):2665-9. PMID: 11953409 Li L, Sharipo A, Chaves-Olarte E, Masucci MG, Levitsky V,Thelestam M, Frisan T. The Haemophilus ducreyi cytolethal distending toxin activatessensorsof DNA damage and repair complexes in proliferating and non-proliferating cells. Cell Microbiol. 2002 Feb;4(2):87-99. PMID: 11896765 Frisan T, Cortes-Bratti X, Thelestam M. Cytolethal distending toxins and activation of DNAdamage-dependent checkpoint responses. Int J Med Microbiol. 2002 Feb;291(6-7):495-9. Review. PMID: 11890549 ","Tue Feb 8 15:03:00 2005","Mon Jan 6 17:40:48 2003","1","","2","" "AA00670","460400","460242","159","ATGTATATGCTTGATACTAACACGGTAAGTTATATTTCCTACTTAACAGATTTATTCATATTTTTATTTCAACAGATTTCAAAAACTATATTGAATCAAAAAACAATTCCTCTTCCTTTTTTATATATTTTATCTAGTTTTATTTTATCAAAAAAAGGA","","","6196","MYMLDTNTVSYISYLTDLFIFLFQQISKTILNQKTIPLPFLYILSSFILSKKG","460242","","hypothetical protein","Cytoplasm","This sequence is similar to gi|4003372, orf2 from A. actinomycetemcomitans. See also gi|9955923.","No hits reported.","No hits to the COGs database.","","Residues 1 to 53 match (1e-11) PD:PD194453 which is described as GENES CDTB CDTC CDTA ORFS ","","","","","","","","","","","","Mon Feb 23 10:12:29 2004","Mon Feb 23 10:12:29 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence. However see gi|4003372 and gi|9955923 from A.a.AA00670 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 10:12:29 2004","","","","","","","","","","","","","1","","2","" "AA00671","460670","460407","264","ATGGAAAGAACTGCGAAATTATTCAGAAACGGACGCAATCAAGCCGTACGGTTACCGGTGGAGTTCGAATTTGATGCTGAACAAGTATACATTCGTAAAGAACAAAATGGAGATATTGTACTTTCATTGACTTCTTCAAGAGAAGCTTCTTGGCAGCGGTTGTTTAAGTTACTTCCCAAAATAAAAAATTGTGATGATTTTCTCAGCAAAGAAGAGCGGAATCAAACGATTACGACCCGTTACCCGTTTCCCGGGATAGGTGAA","","","10349","MERTAKLFRNGRNQAVRLPVEFEFDAEQVYIRKEQNGDIVLSLTSSREASWQRLFKLLPKIKNCDDFLSKEERNQTITTRYPFPGIGE","460409","","virulence plasmid protein","Cytoplasm","","
InterPro
IPR007159
Domain
SpoVT/AbrB-like, predicted transcription regulator
PF04014\"[8-60]TSpoVT_AbrB
noIPR
unintegrated
unintegrated
SSF89447\"[3-75]TSSF89447


","No hits to the COGs database.","","Residues 1 to 88 match (2e-41) PD:PD451173 which is described as PLASMID VIRULENCE ","","","","","","","","","","","","Wed Feb 19 06:35:48 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00671 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 58 (E-value = 1.3e-06) place AA00671 in the SpoVT_AbrB family which is described as SpoVT / AbrB like domain (PF04014)","","","","Mayer MP, Bueno LC, Hansen EJ, DiRienzo JM.Identification of a cytolethal distending toxin gene locus and features of a virulence-associated region in Actinobacillus actinomycetemcomitans.Infect Immun. 1999 Mar;67(3):1227-37.PMID: 10024565Shenker,B.J., Hoffmaster,R.H., McKay,T.L. and Demuth,D.R.Expression of the cytolethal distending toxin (Cdt) operon inActinobacillus actinomycetemcomitans: evidence that the CdtBprotein is responsible for G2 arrest of the cell cycle in human TcellsJ. Immunol. 165 (5), 2612-2618 (2000)PubMed: 20405645","","Wed Feb 19 11:21:16 2003","Mon Dec 16 12:11:25 2002","1","","2","" "AA00672","461098","460757","342","ATGTATGTACCAAAACGTAACGACATTGTTTGGTTGGATTTTGAGCCGAAGAAAGGAAAAGAAATCGGGAAATATCGCCCGGCATTCGTTTTAAGCCATGAAATTTATAATAAATCAACCGGGTTGATTATTTGCTGTCCAATCAGCACGAGTATTCGTGGTGCGGTAACGGAAGTGCCTATCGAAGGATTAGATAGTCCGAGTGTGGTTGCAACTACATTAGTCCAAACATTAGATTGGCGTGAAAGACATATTAAATTTATTAAACAGGCTGAACCACACATTTATGATGAGGTCCTCAAACGGGTAATCCTGTTACTGGGTGGTGAACGTCTTTTGCGA","","","13042","MYVPKRNDIVWLDFEPKKGKEIGKYRPAFVLSHEIYNKSTGLIICCPISTSIRGAVTEVPIEGLDSPSVVATTLVQTLDWRERHIKFIKQAEPHIYDEVLKRVILLLGGERLLR","460759","","conserved hypothetical protein (possible ppGpp-regulated growth inhibitor)","Cytoplasm","","
InterPro
IPR003477
Family
PemK-like protein
PF02452\"[5-108]TPemK
InterPro
IPR011067
Family
Plasmid maintenance toxin/Cell growth inhibitor
G3DSA:2.30.30.110\"[2-108]Tno description


","BeTs to 6 clades of COG2337COG name: Growth inhibitorFunctional Class: TThe phylogenetic pattern of COG2337 is ---------dr-b-e---sn------Number of proteins in this genome belonging to this COG is","Significant hit ( 1.3e-05) to 2/2 blocks of the IPB003477 family, which is described as \"PemK-like protein\". Interpro entry for IP:IPR003477. IPB003477A 26-44 0.00088 IPB003477B 68-96 7.5","Residues 8 to 78 match (6e-10) PD:PD290367 which is described as PROTEOME COMPLETE PEMK-LIKE PLASMID DNA-BINDING PEMK-RELATED MAZF PEMK ","","","","","","","","","","","","Mon Dec 16 12:27:27 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00672 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 108 (E-value = 5.8e-17) place AA00672 in the PemK family which is described as PemK-like protein (PF02452)","","","","","","","Wed Jan 22 16:37:43 2003","1","","2","" "AA00673","461355","461104","252","ATGCAATTGAGACAACAAGCAACGTTAGGTCTGTGGGGAAAGTGTATCGGTTTACGATTAACAGGCAATTTACGTACAGTCCCTCAGTTTTCAGCGGGTGATATTGTGGATATCGAGATTTCTGAAAATGGTTTGTACATTTCAAAAAGCCAAAAAAAACTGACTGAAGCTGATTTATTAAAAGGAATAACGACTTATAACGCTCATGCAGATGAGTTTAACGTCGCTGCTTTACCGCAGGAATTGGACTAT","","","9278","MQLRQQATLGLWGKCIGLRLTGNLRTVPQFSAGDIVDIEISENGLYISKSQKKLTEADLLKGITTYNAHADEFNVAALPQELDY","461106","","hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-17]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Dec 16 12:29:25 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00673 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","2","" "AA00674","462645","461950","696","ATGAAACCCATTTGTGTCGTCCTAAGCGGCGCGGGCATCAGCGCTGAAAGTGGTATTCCCACTTATCGCGCGGAAGACGGTTTATGGGCAGGGCATAAAATTGAAGATGTGTGCACGCCGGAAGCCCTGCAACGGAACCGTAAACAGGTGTTGGCTTTTTATAACGAACGCCGCCGAAATTGCGCCGAAGCCAAACCTAATGCGGCGCACAAGGTGTTGGTGGAATTGGAACGCTCCTATAATGTACAGATCATCACGCAAAACGTGGAAGATTTACACGAACGCGCGGGCAGCACCAACGTGCTGCATCTGCACGGCGAATTAACCAAAGCCCGTAGCAGTTTTGACCCTGATTACATTGTGCCTTGCATGGGTGATCAATCGGTGAACGACAAAGATCCGAACGGACATCCAATGCGCCCGCACATCGTCTTTTTCGGTGAAAGTGTGCCCGTGTTGGAACCGGCCATTGATTTGGTTTCGCAAGCAGACATTGTGCTGGTCATCGGTACATCCCTGCAAGTTTACCCGGCAAACGGTTTGGTCAACGAAGCTCCCAAGAACGCTCAAATTTACCTCATCGACCCAAACCCGAACACAGGGTTTATTCGCCATAACGTCAACGTAGTAAAAATGAAAGCAGGCGAAGGCGTGCCTAAAGTGGTGGCGGAATTATTGGAGAAGGCAAAAAACGGT","","","25402","MKPICVVLSGAGISAESGIPTYRAEDGLWAGHKIEDVCTPEALQRNRKQVLAFYNERRRNCAEAKPNAAHKVLVELERSYNVQIITQNVEDLHERAGSTNVLHLHGELTKARSSFDPDYIVPCMGDQSVNDKDPNGHPMRPHIVFFGESVPVLEPAIDLVSQADIVLVIGTSLQVYPANGLVNEAPKNAQIYLIDPNPNTGFIRHNVNVVKMKAGEGVPKVVAELLEKAKNG","461952","","nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase","Cytoplasm","","
InterPro
IPR003000
Family
Silent information regulator protein Sir2
PTHR11085\"[10-187]TCHROMATIN REGULATORY PROTEIN SIR2
PF02146\"[10-177]TSIR2
PS50305\"[1-230]TSIRTUIN
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1220\"[5-225]Tno description


","BeTs to 14 clades of COG0846COG name: NAD-dependent protein deacetylases, SIR2 familyFunctional Class: HThe phylogenetic pattern of COG0846 is a---kzyqvdrlb-efgh--uj----Number of proteins in this genome belonging to this COG is","Significant hit ( 2.2e-48) to 4/4 blocks of the IPB003000 family, which is described as \"Sir2 family\". Interpro entry for IP:IPR003000. IPB003000A 3-27 5.1e-13 IPB003000B 69-115 1.9e-13 IPB003000C 137-151 1.1e-06 IPB003000D 164-190 8.7e-11 IPB003000B 70-116 0.088","Residues 6 to 201 match (3e-110) PD:PD002659 which is described as PROTEOME COMPLETE SIR2 REGULATORY REGULATION SIRTUIN TYPE TRANSCRIPTION NUCLEAR INFORMATION ","","","","","","","","","","","","Mon Dec 16 12:42:04 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00674 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 10 to 177 (E-value = 5e-78) place AA00674 in the SIR2 family which is described as Sir2 family (PF02146)","","","","","","","","1","","","" "AA00675","463308","462664","645","ATGAAGCTTTATGTTTACGACCATTGCCCGTTTTGCGTGCGCGCCCGCATGATTTTCGGCTTGAAAAATGTTCCCGTTGAACTCGTGACCATCTTAAATGATGACGCGGAAACGCCAATCCGACTGGTCGGCAAAAAAGTGGTGCCGATTTTAGTGAAAGAAAACGGCGAAGCCATGCCGGAAAGTTTGGACATTGTGCGCTATATTGATGAACGCTATGGCGAGAAAATGTTATCGGAAACGGTGCGCCCGGAAGTAGAAGCCTGGTTAAAGCAGGTCGGCAGCTATCAAAATCATCTGGTCATCCCACGCTTTACCCGCCTAGGGCTGCCTGAATATGCCACCCAAAGTGCGGTAGATTATTTCACCGAAAATAAAGAAAAATCCATCGGTGATTTTGCCGAAAATCTTGCGAATACCGACACCTATTTCGCCCGCCTCGCCCCTGACTTAGTGCAACTTGCACATTTAATCCAGTCGGACACTGCACTAAACGGCAGCCTTTCTCTGGAAGACATTCTTGTTTTCCCAATCCTGCGCAACCTCACCTGCGTAAAAGGCATCGTTTTCCCGCCGAAAGTCAACGCCTATGTGGAAACCATGTCCCGTTTGAGCCAAGTGCCGTTGTATTGGGATAAAGCGATT","","","25265","MKLYVYDHCPFCVRARMIFGLKNVPVELVTILNDDAETPIRLVGKKVVPILVKENGEAMPESLDIVRYIDERYGEKMLSETVRPEVEAWLKQVGSYQNHLVIPRFTRLGLPEYATQSAVDYFTENKEKSIGDFAENLANTDTYFARLAPDLVQLAHLIQSDTALNGSLSLEDILVFPILRNLTCVKGIVFPPKVNAYVETMSRLSQVPLYWDKAI","462666","functional class determined from HD0300, not an ortholog, but it has the same definition and is a glx gene.","glutaredoxin 2","Cytoplasm","","
InterPro
IPR004045
Domain
Glutathione S-transferase, N-terminal
PF02798\"[1-71]TGST_N
InterPro
IPR007494
Domain
Glutaredoxin 2, C-terminal
PF04399\"[84-215]TGlutaredoxin2_C
InterPro
IPR010987
Domain
Glutathione S-transferase, C-terminal-like
G3DSA:1.20.1050.10\"[90-215]Tno description
InterPro
IPR011767
Active_site
Glutaredoxin active site
PS00195\"[3-18]TGLUTAREDOXIN
InterPro
IPR011901
Family
Glutaredoxin, GrxB
TIGR02182\"[2-210]TGRXB: Glutaredoxin, GrxB family
InterPro
IPR012335
Domain
Thioredoxin fold
G3DSA:3.40.30.10\"[1-85]Tno description
noIPR
unintegrated
unintegrated
PTHR11260\"[1-210]TGLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING


","BeTs to 3 clades of COG2999COG name: Glutaredoxin 2Functional Class: OThe phylogenetic pattern of COG2999 is --------------e-gh-n------Number of proteins in this genome belonging to this COG is","Significant hit ( 5.8e-06) to 2/2 blocks of the IPB002109 family, which is described as \"Glutaredoxin\". Interpro entry for IP:IPR002109. IPB002109A 1-15 0.00098 IPB002109B 79-98 3","Residues 1 to 215 match (5e-119) PD:PD112015 which is described as PROTEOME GLUTAREDOXIN COMPLETE GRX2 ELECTRON REDOX-ACTIVE CENTER ","","","","","","","","","","","Mon Dec 16 13:03:08 2002","Mon Dec 16 13:03:08 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00675 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 84 to 215 (E-value = 4.2e-96) place AA00675 in the Glutaredoxin2_C family which is described as Glutaredoxin 2, C terminal domain (PF04399)","","","","Mayer,M.P., Bueno,L.C., Hansen,E.J. and DiRienzo,J.M.Identification of a cytolethal distending toxin gene locus andfeatures of a virulence-associated region in ActinobacillusactinomycetemcomitansInfect. Immun. 67 (3), 1227-1237 (1999)PubMed: 10024565","PMID: 12213606 [PubMed - indexed for MEDLINE]Belli G, Polaina J, Tamarit J, De La Torre MA, Rodriguez-Manzaneque MT, Ros J, Herrero E.Structure-function analysis of yeast Grx5 monothiol glutaredoxin defines essential amino acids for the function of the protein.J Biol Chem. 2002 Oct 4;277(40):37590-6.PMID: 12138088 Porras P, Pedrajas JR, Martinez-Galisteo E, Padilla CA, Johansson C, Holmgren A, Barcena JA.Glutaredoxins catalyze the reduction of glutathione by dihydrolipoamide with high efficiency.Biochem Biophys Res Commun. 2002 Aug 2;295(5):1046-51.PMID: 1213559Vlamis-Gardikas,A., Aslund,F., Spyrou,G., Bergman,T. andHolmgren,A.Cloning, overexpression, and characterization of glutaredoxin 2, an atypical glutaredoxin from Escherichia coliJ. Biol. Chem. 272 (17), 11236-11243 (1997)PubMed: 9111025","Mon Dec 16 13:03:08 2002","Mon Dec 16 13:03:08 2002","1","","","" "AA00679","464900","463428","1473","ATGGATTCGGTCGAATTATTGGTCAATGTGACACCCAACGAAACTTGCATTGCCCTTGTAGAAACAGGTATATTAAAAGAAGTACATATTGAACGCCAAGGCAAACGCGGTATTGTGGGAAACATTTATAAAGGGCGCGTGACCCGCGTGCTGCCGGGAATGCAGTCGGCGTTTGTGGACATCGGCTTGGAAAAAGCCGCTTTTTTGCACGCCTCAGACATCGTCTCACACACTGAATGCGTGGATGAAAACGAACAAAAGCAATTTGTGGTAAAAGACATTTCCCAGCTGGTGCACGAGGGGCAGGATATTGTCGTGCAGGTGGTGAAAGATCCTCTCGGCACCAAAGGCGCGCGCCTTACTACGGACATTACGCTGCCTTCCCGCTATTTGGTGTTCATGCCGGAAAACAGCCATGTGGGCGTATCGCAACGCATTGAAAGCGAGGAGGAACGCGCCCGCTTGAAAGAACTGGCGCTGCCGTTATGCGACGAGTTAGGCGGCTTTATTATTCGCACCGCTGCCGAAGGCGCAAGTGAGCTGGATTTACAACAAGACGCGGAATTCCTGAAACGTTTATGGCGCAAAGTGCTGGAACGCCGCGCTAAATACCCGACCCGCTCCATGTTATACGGCGAACTGGCGCTTACCCAGCGCATTTTGCGCGATTTCATCGGCGCCAAATTAGATCGCATTCACATTGACTCCCGTCTCTGTTTCAATGAAGTCAAACAATTCACCGAAGAATTCATCCCGAACCTCACCGACAAACTGATTTTATACGCGGGAAATCAACCGCTCTTTGATGTCTATAGCGTGGAAACGGGCATTCATAACGCGTTGGATAAACGGGTGAATCTCAAATCCGGTGGCTATTTGATTATTGAACAGACAGAAGCCATGACCACCATCGACATTAACACCGGCGCTTTCGTGGGGCATCGCAATCTGGAAGAAACCATTTTCAATACCAACATCGAAGCTACCAAAGCCATCGCCCAACAGCTCCAACTGCGCAATCTCGGTGGTATCATCATTATCGATTTTATCGATATGCAAAAAGAAGAACACCGCACCCGCGTGTTGGAATCCTTGCAGGAAGCCCTTGCCGGCGACCCGGTGAAAACCAATGTCAATGGTTTCACTCAGTTGGGGCTGGTGGAAATGACCCGCAAACGCACCCGCGAAAGTTTGGAGCGCGTGCTATGCGGCGATTGCCCCGCCTGCCAAGGGCGTGGACGGGTGAAAACCGTGGAAACCGTGTGCTATGAAATCATGCGCGAAATCATTCGCGTACACCATGTATTTGCCAGCGAACAATTCGTGGTTTATGCCTCTCACGCCGTCGCCGATTATCTGATTAACGAAGAATCCCACGGCTTACTGGCTGAACTGGAAGTGTTCATCGGCAAACAAATCCAAGTAAAAACTGAAGTGTTTTATACTCAGGAACAGTTTGATGTGGTGGTGATG","","","55473","MDSVELLVNVTPNETCIALVETGILKEVHIERQGKRGIVGNIYKGRVTRVLPGMQSAFVDIGLEKAAFLHASDIVSHTECVDENEQKQFVVKDISQLVHEGQDIVVQVVKDPLGTKGARLTTDITLPSRYLVFMPENSHVGVSQRIESEEERARLKELALPLCDELGGFIIRTAAEGASELDLQQDAEFLKRLWRKVLERRAKYPTRSMLYGELALTQRILRDFIGAKLDRIHIDSRLCFNEVKQFTEEFIPNLTDKLILYAGNQPLFDVYSVETGIHNALDKRVNLKSGGYLIIEQTEAMTTIDINTGAFVGHRNLEETIFNTNIEATKAIAQQLQLRNLGGIIIIDFIDMQKEEHRTRVLESLQEALAGDPVKTNVNGFTQLGLVEMTRKRTRESLERVLCGDCPACQGRGRVKTVETVCYEIMREIIRVHHVFASEQFVVYASHAVADYLINEESHGLLAELEVFIGKQIQVKTEVFYTQEQFDVVVM","463430","","cytoplasmic axial filament (Ribonuclease G)","Cytoplasm","","
InterPro
IPR003029
Domain
RNA binding S1
PF00575\"[36-123]TS1
SM00316\"[38-123]TS1
PS50126\"[40-129]TS1
InterPro
IPR004659
Domain
Ribonuclease E and G
TIGR00757\"[14-427]TRNaseEG: ribonuclease, Rne/Rng family
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[31-129]Tno description
InterPro
IPR013194
Domain
Histone deacetylase interacting
SM00761\"[286-359]Tno description


","BeTs to 13 clades of COG1530COG name: Ribonucleases G and EFunctional Class: JThe phylogenetic pattern of COG1530 is -o--kz-qv-r-bcefghsnujxi--Number of proteins in this genome belonging to this COG is","","Residues 39 to 126 match (2e-07) PD:PD571091 which is described as E ENDONUCLEASE NUCLEASE RIBONUCLEASE CHLOROPLAST HOMOLOG 3.1.4.- RNASE HYDROLASE ","","","","","","","","","","","","Mon Dec 16 13:22:07 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00679 is paralogously related to AA02910 (7e-72).","","","","","","Residues 36 to 123 (E-value = 4.7e-14) place AA00679 in the S1 family which is described as S1 RNA binding domain (PF00575)","","","","Mayer,M.P., Bueno,L.C., Hansen,E.J. and DiRienzo,J.M.Identification of a cytolethal distending toxin gene locus andfeatures of a virulence-associated region in ActinobacillusactinomycetemcomitansInfect. Immun. 67 (3), 1227-1237 (1999)PubMed: 10024565","Okada,Y., Wachi,M., Hirata,A., Suzuki,K., Nagai,K. and Matsuhashi,M.Cytoplasmic axial filaments in Escherichia coli cells: possiblefunction in the mechanism of chromosome segregation and cell divisionJ. Bacteriol. 176 (3), 917-922 (1994)PubMed: 8300545Wachi,M., Umitsuki,G., Shimizu,M., Takada,A. and Nagai,K.Escherichia coli cafA gene encodes a novel RNase, designated asRNase G, involved in processing of the 5' end of 16S rRNABiochem. Biophys. Res. Commun. 259 (2), 483-488 (1999)PubMed: 10362534","Mon Dec 16 13:25:24 2002","Mon Dec 16 13:25:24 2002","1","","","" "AA00680","465039","466556","1518","ATGTTTGGATTAGATCCAACAATTATCACATTTGTTATTTATATCGTCGGCATGCTCGGTATCGGGATTGCCGCTTACTATTACACCCAAAATTTCTCCGACTACATTCTCGGCGGTCGCCGTTTGGGTAGTTTCGTCACCGCCATGTCTGCCGGCGCTTCCGATATGTCCGGCTGGCTGTTAATGGGCTTGCCCGGCGCAGTTTATTTATCCGGTTTGGTTGAAGGGTGGATCGCCATCGGTTTAACCCTCGGTGCGTACCTGAACTGGCTGTTTATCGCCGGTCGTCTGCGCGTTTACACAGAATTCAATAATAACGCTTTAACCCTGCCCGAATATTTTCATCACCGTTTCGGCACGTCCCATAACTTATTGAAGATCGTCTCTGCCACCATTATTCTGGTGTTTTTCACTATTTATTGCGCCTCGGGCGTGGTTGCCAGTGCGAAATTATTCCGCAATCTGTTTTTAATTGACTACTCCACCGCACTTTGGTACGGCGCGCTCGCCACCATCATTTACACCTTCATCGGCGGTTTCCTTGCCGTCAGCTGGACGGACACCATTCAAGCCACGTTAATGATTTTCGCGTTATTGCTCACGCCGGTTTTCGTGGTGATTTCCATTGGCGGCATTGACGAGTTGCAAAACGTCTTACAACAAGCGGAAATTAGCGCGCAAAAAGACTTTACGGATTTATTCCGCGGCACCTCCACCGTCGGCTTGCTAAGTCTTGCCGCTTGGGGCTTGGGCTATTTCGGACAACCGCATATTCTCGCCCGTTTCATGGCTGCAGATTCCGTCCATTCTCTCAACAACGCACGCAAAATCAGCATGACCTGGATGATGCTTTGTTTGGTGGGCGCTATCGCTATCGGCTTCTTCGGCATAATTTATTTTTACGCCGACGCCGGCACTGAATCGGCTGCCCTGGTCAATAAAGAACCGGAGCAGGTTTTCATTGAATTATCCCGCATTCTGTTTAACCCGTGGATTGCCGGCGTGTTGCTATCCGCTATTCTTGCAGCGGTAATGAGTACCTTAAGTGCGCAATTACTCATTTCCTCCACGGCGATTACAGAAGATTTCTACAAAGGCTTCATTCGCCCGAAAGCGTCGGAAAAAGAACTTATCTGGCTTGGTCGCGCCATGGTGTTGGTGATTGCCGGCATTGCTATTTGGATTGCACAAGATGAAAAAAGCCTGGTGTTAAAACTGGTGGAATTCGCTTGGGCGGGCTTCGGCAGTGCTTTTGGACCCGTCGTGTTATTTTCCTTATTCTGGAAACGCATGACATCCTCGGGCGCCATGGCAGGCATGTTGACCGGTGCCATCACCGTGATTGCATGGAAAAAATGGTTGCCGCAAGACACGGAATTGGCTCAGGTTTATGAAATGATTCCGGGCTTTTTACTGGCAACCGTTGCTATTTTCGTGGTTTCGTTGCTGTCGGCAAAACCGGATGCGGAAATTACCGACACCTTTGACAAAGCCCAAAAGGCGTACAAAGAAGCTTTA","","","55292","MFGLDPTIITFVIYIVGMLGIGIAAYYYTQNFSDYILGGRRLGSFVTAMSAGASDMSGWLLMGLPGAVYLSGLVEGWIAIGLTLGAYLNWLFIAGRLRVYTEFNNNALTLPEYFHHRFGTSHNLLKIVSATIILVFFTIYCASGVVASAKLFRNLFLIDYSTALWYGALATIIYTFIGGFLAVSWTDTIQATLMIFALLLTPVFVVISIGGIDELQNVLQQAEISAQKDFTDLFRGTSTVGLLSLAAWGLGYFGQPHILARFMAADSVHSLNNARKISMTWMMLCLVGAIAIGFFGIIYFYADAGTESAALVNKEPEQVFIELSRILFNPWIAGVLLSAILAAVMSTLSAQLLISSTAITEDFYKGFIRPKASEKELIWLGRAMVLVIAGIAIWIAQDEKSLVLKLVEFAWAGFGSAFGPVVLFSLFWKRMTSSGAMAGMLTGAITVIAWKKWLPQDTELAQVYEMIPGFLLATVAIFVVSLLSAKPDAEITDTFDKAQKAYKEAL","466558","","sodium/proline symporter (proline permease)","Inner membrane, Cytoplasm","","
InterPro
IPR001734
Family
Na+/solute symporter
PTHR11819\"[8-411]TSODIUM/SOLUTE SYMPORTER
PF00474\"[35-443]TSSF
TIGR00813\"[35-443]Tsss: transporter, solute:sodium symporter (
PS50283\"[4-457]TNA_SOLUT_SYMP_3
PS00457\"[425-445]TNA_SOLUT_SYMP_2
InterPro
IPR011851
Family
Sodium/proline symporter
TIGR02121\"[5-503]TNa_Pro_sym: sodium/proline symporter
noIPR
unintegrated
unintegrated
PTHR11819:SF12\"[8-411]TSODIUM/PROLINE SYMPORTER
signalp\"[1-24]?signal-peptide
tmhmm\"[9-29]?\"[66-88]?\"[124-144]?\"[163-183]?\"[192-212]?\"[240-260]?\"[281-301]?\"[336-356]?\"[377-397]?\"[407-427]?\"[437-455]?\"[461-483]?transmembrane_regions


","BeTs to 22 clades of COG0591COG name: Na+/proline, Na+/panthothenate symporters and related permeasesFunctional Class: E,H,RThe phylogenetic pattern of COG0591 is aompkzyq-d--bcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 7.2e-46) to 3/3 blocks of the IPB001734 family, which is described as \"Sodium:solute symporter family\". Interpro entry for IP:IPR001734. IPB001734A 136-152 3.3e-05 IPB001734B 157-197 3.3e-21 IPB001734C 414-443 1.2e-16","Residues 320 to 493 match (2e-11) PD:PD275464 which is described as COMPLETE PROTEOME KINASE PERMEASE PROLINE SENSORY TRANSMEMBRANE TRANSDUCTION SENSOR TRANSFERASE ","","","","","","","","","","","","Mon Dec 16 13:27:11 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00680 is paralogously related to AA00176 (1e-40).","","","","","","Residues 35 to 443 (E-value = 2e-188) place AA00680 in the SSF family which is described as Sodium:solute symporter family (PF00474)","","","","","Jung H.The sodium/substrate symporter family: structural and functional features.FEBS Lett. 2002 Oct 2;529(1):73-7. Review.PMID: 12354616Nelson,K. and Selander,R.K. Evolutionary genetics of proline permease gene (putP) andthe control region of the proline utilization operon inpopulations of Salmonella and Escherichia coli J. Bacteriol. 174, 6886-6895 (1992) PubMed: 1400239 ","","Mon Dec 16 13:28:28 2002","1","","","" "AA00682","466462","467535","1074","TTGCTATTTTCGTGGTTTCGTTGCTGTCGGCAAAACCGGATGCGGAAATTACCGACACCTTTGACAAAGCCCAAAAGGCGTACAAAGAAGCTTTATAAGCGAGATAGCAAAATGATCGATTTTCGTCCTTTTTATCAACAAATCGCCACCACCAACCTTTCGCCATGGCTTGAAACGCTGCCCCTGCAACTCAAACAATGGCAGCAACAAACCCATGGCGACTATGCCAAATGGGCAAAAGTCTTGGAATTTCTACCGCACTTGGCAGCATCCCGCATTGACTTGAAAAGTGCGGTCAAATCTGAAAGCGTTTCTCCTCTTTCCGAAGGCGAACGGCAACGTATTGTGCACCACCTCAAACAGCTCATGCCGTGGCGTAAAGGCCCCTATGATTTGCTTGGCATTCATGTGGATTGCGAATGGCGCTCCGATTTCAAATGGGATCGCGTGCTGCCCCATCTTGCACCGTTGCAGGATCGCATTATTTTAGATGTCGGCTGCGGCAGCGGTTATCACATGTGGCGCATGGTGGGTGAAGGGGCGAAAATGGTGGTCGGCATTGATCCGACGGAACTGTTTTTATGCCAATTTGAAGCAGTGCGTAAATTGCTAAACGACGATCGCCGCGCCAATCTGATTCCTCTCGGCATTGAACAAATGCAGCCCCTAGCGGCGTTTGATACGGTGTTTTCCATGGGCGTGCTGTATCACCGCAAATCGCCGTTGGATCATCTTTCCCAACTGCGCGCCCAACTGGTTAAAGGCGGCGAATTAGTGCTGGAAACCTTAGTGGTGGATGGCGACAAAAACACTGTGTTAGTGCCGATGGATCGCTATGCCAAAATGAAAAATGTGTATTTCATTCCTTCCGTTGCCGCGTTAATTCATTGGTTACAAAAAACTGGTTTTAATCATGTGCGTTGTGTGGATGTGGCGGTAACCTCATTGGAAGAACAGCGCAAAACCGACTGGCTGGAAAATGAATCACTGGCGGATTTTCTCGATCCCAATGATTATTGCAGAACCATCGAAGGCTATCCCGCGCCTAAAAGGGCGGTCCTTTTGGCGAATAAA","","","41504","LLFSWFRCCRQNRMRKLPTPLTKPKRRTKKLYKRDSKMIDFRPFYQQIATTNLSPWLETLPLQLKQWQQQTHGDYAKWAKVLEFLPHLAASRIDLKSAVKSESVSPLSEGERQRIVHHLKQLMPWRKGPYDLLGIHVDCEWRSDFKWDRVLPHLAPLQDRIILDVGCGSGYHMWRMVGEGAKMVVGIDPTELFLCQFEAVRKLLNDDRRANLIPLGIEQMQPLAAFDTVFSMGVLYHRKSPLDHLSQLRAQLVKGGELVLETLVVDGDKNTVLVPMDRYAKMKNVYFIPSVAALIHWLQKTGFNHVRCVDVAVTSLEEQRKTDWLENESLADFLDPNDYCRTIEGYPAPKRAVLLANK","467537","","S-adenosylmethionine-dependent methyltransferase","Cytoplasm","","
InterPro
IPR010017
Family
Methyltransferase, putative
PF08003\"[38-358]TMethyltransf_9
TIGR00452\"[38-351]TTIGR00452: methyltransferase, putative
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[129-261]Tno description
PTHR10108\"[140-317]TMETHYLTRANSFERASE
PTHR10108:SF15\"[140-317]T2-HEPTAPRENYL-1,4-NAPHTHOQUINONE METHYLTRANSFERASE


","BeTs to 14 clades of COG0500COG name: SAM-dependent methyltransferasesFunctional Class: Q,RThe phylogenetic pattern of COG0500 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Thu Feb 20 08:39:38 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00682 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00684","467626","468921","1296","ATGGGTAAAAGTGTTGTCGTTCTCGGCGCTCAGTGGGGCGATGAAGGCAAAGGGAAAATCGTTGACCTGCTCACCGATCGCGTGAAATATGTGGTGCGCTACCAAGGTGGTCATAATGCCGGTCATACCTTAATCATCAACGGTGAAAAAACCGTTCTACGTTTAATTCCATCAGGCATCCTGCGCGATAATGTCACCTGTTTAATCGGTAACGGCGTGGTGCTTTCCCCTGCGGCACTCATGCAGGAAATGAGCGAACTGGAAAGTCGTGGCGTGAATGTGCGCGACCGTTTATTAATCTCCGAAGCCTGTCCGTTAATTCTGCCCTATCACGTTGCCATGGATCACGCCCGTGAAGCGGCGTTGGGCAAAAAGGCCATCGGCACCACCGGACGCGGTATCGGCCCTGCCTATGAAGACAAAGTGGCACGTCGCGGTTTACGCGTAGGAGATTTATTCGATCGCGCCGCCTTCGCCGAAAAACTCAAAAATATCCTCGATTACTACAACTTCCAACTGGTCAATTACTACAAAGTCGAACCCGTTGATTATCAAAAAACCTTAGATGACGTGTTCGCCGTTGCCGATATTATCACCGGCATGGTCGCCGACATCACCACCATCTTAGATACCGCACGCAAAAACGGCGACAACATCTTATTTGAAGGCGCGCAAGGCACCATGTTGGACATCGACCACGGCACCTATCCGTATGTAACCAGCTCCAACACCACCGCCGGCGGCGTAGCGACAGGCTCCGGTTTCGGTCCGCGCAATCTGGATTATGTGTTGGGAATCATCAAAGCCTACTGCACCCGCGTGGGCGGCGGTCCGTTCACTACGGAATTATTTGATGAAACAGGTGCTGAAATCGCCCGTAAAGGTAACGAATTCGGCGCGGTTACCGGTCGTCCGCGTCGTTGCGGTTGGTTTGACGCGGTGGCAATTCGTCGCGCTATTCAACTGAACTCCATTTCCGGTTTCTGCATGACCAAATTAGACGTGCTGGACGGTTTCGATGAAGTGAAAATCTGCGTCGGCTACAAAATGCCGAACGGTGACATCGTGGAATACGCCCCGCTCGCCGCGAAAGATTGGGAAGGCGTTGAACCGATTTACGAAACCTTGCCGGGCTGGAAAGAAAACACCTTCGGCATCACCGATGTTAACCAATTGCCGCAAACCTGCCGCGACTACATCAAACGCATCGAAGAAGTCACCGGCGTACCGGTAGCCATTCTTTCCACCGGACCGGATCGCGTACAAACCATGATTCTACAAGACCCATTTGCCGTG","","","47086","MGKSVVVLGAQWGDEGKGKIVDLLTDRVKYVVRYQGGHNAGHTLIINGEKTVLRLIPSGILRDNVTCLIGNGVVLSPAALMQEMSELESRGVNVRDRLLISEACPLILPYHVAMDHAREAALGKKAIGTTGRGIGPAYEDKVARRGLRVGDLFDRAAFAEKLKNILDYYNFQLVNYYKVEPVDYQKTLDDVFAVADIITGMVADITTILDTARKNGDNILFEGAQGTMLDIDHGTYPYVTSSNTTAGGVATGSGFGPRNLDYVLGIIKAYCTRVGGGPFTTELFDETGAEIARKGNEFGAVTGRPRRCGWFDAVAIRRAIQLNSISGFCMTKLDVLDGFDEVKICVGYKMPNGDIVEYAPLAAKDWEGVEPIYETLPGWKENTFGITDVNQLPQTCRDYIKRIEEVTGVPVAILSTGPDRVQTMILQDPFAV","468923","","adenylosuccinate synthase","Cytoplasm","","
InterPro
IPR001114
Family
Adenylosuccinate synthetase
PD001188\"[4-82]TPURA_PASMU_P57889;
PTHR11846\"[1-430]TADENYLOSUCCINATE SYNTHETASE
PF00709\"[4-425]TAdenylsucc_synt
SM00788\"[4-425]Tno description
TIGR00184\"[6-431]TpurA: adenylosuccinate synthetase
PS00513\"[133-144]TADENYLOSUCCIN_SYN_2
PS01266\"[11-18]TADENYLOSUCCIN_SYN_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.440.10\"[5-266]Tno description
G3DSA:3.90.170.10\"[267-432]Tno description


","No hits to the COGs database.","Significant hit (1.4e-169) to 7/7 blocks of the IPB001114 family, which is described as \"Adenylosuccinate synthetase\". Interpro entry for IP:IPR001114. IPB001114A 18-55 2.6e-26 IPB001114B 97-117 2.9e-11 IPB001114C 127-152 1.4e-22 IPB001114D 219-257 1e-38 IPB001114E 263-282 1.6e-13 IPB001114F 295-336 4.1e-32 IPB001114G 373-405 6.2e-18","Residues 157 to 195 match (8e-15) PD:PD551694 which is described as LIGASE SYNTHETASE ADENYLOSUCCINATE PROTEOME IMP--ASPARTATE COMPLETE GTP-BINDING PURINE ADSS AMPSASE ","","","","","","","","","","","","Fri Jan 24 13:22:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00684 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Jayalakshmi R, Sumathy K, Balaram H. Purification and characterization of recombinant Plasmodiumfalciparum adenylosuccinate synthetase expressed inEscherichia coli. Protein Expr Purif. 2002 Jun;25(1):65-72. PMID: 12071700 Hoffman JA, Badger JL, Zhang Y, Kim KS. Escherichia coli K1 purA and sorC are preferentiallyexpressed upon association with human brain microvascularendothelial cells. Microb Pathog. 2001 Aug;31(2):69-79. PMID: 11453702","","Mon Dec 16 13:54:19 2002","1","","","" "AA00686","469279","468992","288","ATGAAACAAAATATTGATATTAAACTGAGTTTTAGTGAAATGTTGAATGTGTGCGCCGGTGAGCGGCAGTGGTTGCTGGCATTGATTGACGAAGGAATTATTTCCGTGGAAGGGCAGCCGGAACAGGCAGTATTTAGTGGCTTTCAAATGGCGCGCGTTCGTCGCGCTCATCGTTTAAGCCATGATTTTGAAGCCAGCGTGCCTGCTTTGAGTTTGATTATGCAACTACTTGATGAGGTGGAGGAATTGCGTAAGCAAACGCGCTCCATTTCGTTGTTAAGCGATCAT","","","10906","MKQNIDIKLSFSEMLNVCAGERQWLLALIDEGIISVEGQPEQAVFSGFQMARVRRAHRLSHDFEASVPALSLIMQLLDEVEELRKQTRSISLLSDH","468994","","hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
PD068243\"[9-86]TQ6FF09_ACIAD_Q6FF09;


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Dec 16 13:58:07 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00686 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00688","470285","469305","981","ATGGCAAAACAAAATTATTACGAGATATTAGGCGTGGATAAAAATGCCGATCTCGATGCAATTAAAAAAGCGTATCGCAAATTGGTGCGCAAATATCATCCCGATGTCAGCAAAGATCCTGACGCGGTGCAAAAAACCGCCGAGGTGAATGAGGCTTATGAAACCTTGAAGGATACGCAGAAACGGGCGGAATACGATGAAATGCTGGCAAACCCGTTTGGGCGCGCAGGGCAAGGTAATCCGCTCGGCGGTGCTTATCAGGGCAATCCGTTTGAAGGCGCGTATGACGATGGCAGTGGCTTCCGCCGTTATGAATTCCATAGTGGTGCGGGCGGTGAGCCGTTCGGTCAGGGGGATTTCCACTTTGAGGATTTATTCTCCGCTTTCGGTCGTCGCGGTCAGCAACAATCACAAACGCGCCAAACCGGTCCGATAAAAGGCGAGGATCAACACGCCGAACTCAGCATTGATATTTCGGCGGCGTATCACGGTGCGGAGCGTTCTTTAAGTCTGAATATGCCGACCATTGACGAGCACGGGAGAATTATTCAGCAAACCAAAACCCTGAATGTGAAAATTCCGAAAGGGATTGCCGAAGGGCAACAAATCCGCTTGTCAGGTCAGGGCTTACCGGGCATCAACGGCGGTACAAACGGTGATTTGTATTTGAAAATCCGTTTCCATGAACAGCCGGATCTCTATGTGAAAAACAAAAAAGACGTTTGTCAGACTATTGATATTTTCCCATGGCAGGCAGCGTTGGGCGGTAAAACCGTGGTATCCACTATTGCCGGAAAAATGCAAATCAATCTGCCGACGAACAGCCAAAGCGGTAAAAGCATTCGTTTGAAAGGCAAAGGTATTCCGGCAAAAGAAGCGGGCGATTTGTATTTGAATATTCGCATTGTGGTACCGACAGTGGAAAATGACGCGGATCGTGCCGCATGGGAACAATTAAGCGCGCATTTTGCCGCGAAGGCG","","","35927","MAKQNYYEILGVDKNADLDAIKKAYRKLVRKYHPDVSKDPDAVQKTAEVNEAYETLKDTQKRAEYDEMLANPFGRAGQGNPLGGAYQGNPFEGAYDDGSGFRRYEFHSGAGGEPFGQGDFHFEDLFSAFGRRGQQQSQTRQTGPIKGEDQHAELSIDISAAYHGAERSLSLNMPTIDEHGRIIQQTKTLNVKIPKGIAEGQQIRLSGQGLPGINGGTNGDLYLKIRFHEQPDLYVKNKKDVCQTIDIFPWQAALGGKTVVSTIAGKMQINLPTNSQSGKSIRLKGKGIPAKEAGDLYLNIRIVVPTVENDADRAAWEQLSAHFAAKA","469307","From GenBank (gi:2506359):CbpA is a DNA-binding protein that preferentially recognizes a curved DNA sequence.","curved DNA-binding protein","Periplasm, Cytoplasm","","
InterPro
IPR001623
Domain
Heat shock protein DnaJ, N-terminal
PF00226\"[5-66]TDnaJ
SM00271\"[4-61]TDnaJ
PS50076\"[5-69]TDNAJ_2
InterPro
IPR002939
Domain
Chaperone DnaJ, C-terminal
PF01556\"[201-320]TDnaJ_C
InterPro
IPR003095
Family
Heat shock protein DnaJ
PR00625\"[16-35]T\"[46-66]T\"[147-164]TDNAJPROTEIN
InterPro
IPR015609
Family
Molecular chaperone, heat shock protein, Hsp40, DnaJ
PTHR11821\"[1-74]T\"[111-307]TDNAJ/HSP40
noIPR
unintegrated
unintegrated
G3DSA:1.10.287.110\"[2-77]Tno description
G3DSA:2.60.260.20\"[137-229]T\"[231-317]Tno description
PTHR11821:SF79\"[1-74]T\"[111-307]TCHAPERONE PROTEIN DNAJ


","No hits to the COGs database.","Significant hit ( 2.1e-39) to 5/6 blocks of the IPB001305 family, which is described as \"DnaJ central domain (CXXCXGXG)\". Interpro entry for IP:IPR001305. IPB001305A 5-37 8.3e-21 IPB001305B 45-70 9.1e-10 IPB001305D 160-205 0.0049 IPB001305E 215-254 32 IPB001305F 268-319 4Significant hit ( 2.7e-29) to 4/8 blocks of the PR00625 family, which is described as \"DnaJ protein family signature\". Prints database entry for PR:PR00625. PR00625A 16-35 1.2e-11 PR00625B 46-66 5.1e-08 PR00625G 191-207 9.4e-06 PR00625H 238-255 78Significant hit ( 1.5e-19) to 2/2 blocks of the IPB001623 family, which is described as \"DnaJ N-terminal domain\". Interpro entry for IP:IPR001623. IPB001623A 21-35 2.5e-10 IPB001623B 45-66 1.3e-07","Residues 190 to 225 match (9e-07) PD:PD404783 which is described as DNA-BINDING PROTEOME COMPLETE CHAPERONE CURVED DNAJ FUNCTIONS METAL-BINDING CLOSELY PROTEIN ","","","","","","","","","","","Tue Jan 21 13:49:00 2003","Tue Jan 21 13:49:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00688 is paralogously related to AA00659 (8e-26) and AA01057 (1e-04).","","","","","","Residues 201 to 320 (E-value = 1.4e-27) place AA00688 in the DnaJ_C family which is described as DnaJ C terminal region (PF01556)","","","","","Ueguchi C, Shiozawa T, Kakeda M, Yamada H, Mizuno T.A study of the double mutation of dnaJ and cbpA, whose gene products function as molecular chaperones in Escherichia coli.J Bacteriol. 1995 Jul;177(13):3894-6.PMID: 7601860Ueguchi,C., Kakeda,M., Yamada,H. and Mizuno,T.An analogue of the DnaJ molecular chaperone in Escherichia coliProc. Natl. Acad. Sci. U.S.A. 91 (3), 1054-1058 (1994)PubMed: 8302830","","Tue Jan 21 13:51:29 2003","1","","","" "AA00689","470573","472102","1530","ATGACAACTCCCGTAGTTGCCTTGGTGGGTCGCCCGAATGTCGGCAAATCCACGCTATTCAATCGTCTGACCCGTACCCGCGACGCCCTCGTCACCGATTTTCCCGGTTTAACCCGCGATCGCAAATATGGTCATGCCCACCTTGCCGGCCATGATTTTATCGTCATTGATACGGGCGGTATCGACGGCACGGAAGAAGGTGTAGAAGAAAAAATGGCGGAGCAATCGCTGCTCGCCATTGAAGAGGCGGATATTGTTCTCTTTTTGGTGGATGCCCGCGCAGGATTAACGTCGGCGGACATTGGCATCGCCAATTATTTACGCCAACGCCAAAACAAAACCACCGTGGTGGTCGCCAATAAAGTGGACGGCATTGATGCGGATTCCCACTGCGCCGAATTTTACCAATTAGGCTTGGGCGACGTTGCCCAAATCGCCGCTTCTCAAGGGCGCGGCGTTGTGAGTTTAATGGAACAGGTACTCAGCCCGCTGGCAGAGCAAATGACGGAAGAAAGTGCAGTGGAAAATCCCGACGTTTCTTCCAATGATGCCGACACTGCCGAATTCGACGAATGGGACGAGGATTTTGATTTTTCAAATGAAGAAGACACCGCACTTTTAGACGAAGAGCTGGCGCAGGAACAGACGCCCGACAAGAAAAATATCAAAATCGCCATTGTAGGGCGCCCGAACGTCGGTAAATCCACGCTGACCAACCGCATTTTAGGCGAAGATCGCGTGGTAGTTTACGACTTGCCTGGCACCACCCGCGACAGCATTTATATTCCCATGGAACGCGACAATCAGGATTACACCCTAATCGACACCGCCGGCGTGCGTAAACGGGGCAAAGTACATTTGGCGGTGGAAAAATTCTCCGTTATCAAAACCCTGCAAGCCATTCAGGATGCCAATGTGGTGCTGCTGGTCATCGACGCGCGCGAAAACATCTCTGATCAGGATTTATCCCTGCTCGGCTTTATTTTAAACGCCGGGCGCTCGCTGGTTATCGTGGTAAATAAATGGGACGGTTTGGATACAGAAGTAAAAAATCGGGTGAAATCGGAACTGGATCGCCGTTTGGATTTCATTGATTTCGCCCGCGTGCATTTTATTTCCGCCTTACACGGCAGCGGCGTCGGCAATTTGTTTGATTCCATCAAAGAAGCCTACGAATGCGCCACGCAAAAGATGACTACCTCCATGCTGACGCGCATTCTGCAAATCGCCACGGAGGAACATCAACCGCCGATGATTAGCGGTCGTCGGGTAAAACTCAAATACGCCCACCCCGGCGGTTACAACCCGCCGATTATTGTAATTCACGGCAACCAAGTGGATAAATTACCGGATTCTTATAAGCGTTATTTGTCCAACCATTTCCGTCGTAGCCTGAAAATCATTGGCTCGCCGATTCGCCTGCAATTCCAGGAAGGCAACAACCCGTTTGCCGGCAGACGCAATAAACTCACACCGAACCAATTACGTAAGCGTAAACGTTTGATGAAGTTTATTAAGAAAGCGAAAAGA","","","56868","MTTPVVALVGRPNVGKSTLFNRLTRTRDALVTDFPGLTRDRKYGHAHLAGHDFIVIDTGGIDGTEEGVEEKMAEQSLLAIEEADIVLFLVDARAGLTSADIGIANYLRQRQNKTTVVVANKVDGIDADSHCAEFYQLGLGDVAQIAASQGRGVVSLMEQVLSPLAEQMTEESAVENPDVSSNDADTAEFDEWDEDFDFSNEEDTALLDEELAQEQTPDKKNIKIAIVGRPNVGKSTLTNRILGEDRVVVYDLPGTTRDSIYIPMERDNQDYTLIDTAGVRKRGKVHLAVEKFSVIKTLQAIQDANVVLLVIDARENISDQDLSLLGFILNAGRSLVIVVNKWDGLDTEVKNRVKSELDRRLDFIDFARVHFISALHGSGVGNLFDSIKEAYECATQKMTTSMLTRILQIATEEHQPPMISGRRVKLKYAHPGGYNPPIIVIHGNQVDKLPDSYKRYLSNHFRRSLKIIGSPIRLQFQEGNNPFAGRRNKLTPNQLRKRKRLMKFIKKAKR","472104","According to Tan et al., 2002, this GTPase rescues rRNA methylation.","GTP-binding protein","Cytoplasm","This sequence is virtually identical to gi|15601970 from P.multocida and to gi|16272103 from H.influnzae (the latter a predicted GTP-binding protein).","
InterPro
IPR002917
Domain
GTP-binding protein, HSR1-related
PF01926\"[4-123]T\"[222-343]TMMR_HSR1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[2-143]T\"[220-363]TAAA
InterPro
IPR005225
Domain
Small GTP-binding protein domain
TIGR00231\"[1-162]T\"[219-389]Tsmall_GTP: small GTP-binding protein domain
InterPro
IPR005289
Domain
GTP-binding
TIGR00650\"[9-43]T\"[227-278]TMG442: GTP-binding conserved hypothetical p
InterPro
IPR006073
Domain
GTP1/OBG
PR00326\"[6-26]T\"[73-91]TGTP1OBG
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[5-171]T\"[196-404]Tno description
PTHR11649\"[1-163]T\"[217-480]TMSS1/TRME-RELATED GTP-BINDING PROTEIN
PTHR11649:SF5\"[1-163]T\"[217-480]TGTP-BINDING PROTEIN ENGA


","BeTs to 18 clades of COG1160COG name: Predicted GTPasesFunctional Class: RThe phylogenetic pattern of COG1160 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.4e-17) to 1/1 blocks of the IPB000765 family, which is described as \"GTP1/OBG family\". Interpro entry for IP:IPR000765. IPB000765 222-265 2.3e-17 IPB000765 4-47 1.1e-15","Residues 479 to 509 match (4e-09) PD:PD554572 which is described as GTP-BINDING PROTEOME COMPLETE ENGA REPEAT PROBABLE FACTOR ","","","","","","","","","","","Mon Feb 17 13:23:08 2003","Mon Dec 16 14:05:41 2002","Wed Feb 25 08:44:37 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is identical to AA00446, a GTP binding protein and less similar but paralogous to AA1971, AA1970, AA1894, AA00281.AA00689 is paralogously related to AA03010 (8e-14), AA03008 (3e-11), AA02886 (1e-05) and AA00423 (2e-04).","Wed Feb 25 08:44:37 2004","","","","","Residues 219 to 413 (E-value = 1.7e-05) place AA00689 in the GTP_EFTU family which is described as Elongation factor Tu GTP binding domain (PF00009)","","","","","Tan J, Jakob U, Bardwell JC.Overexpression of two different GTPases rescues a null mutation in a heat-induced rRNA methyltransferase.J Bacteriol. 2002 May;184(10):2692-8.PMID: 11976298 Caldon CE, Yoong P, March PE.Evolution of a molecular switch: universal bacterial GTPases regulate ribosome function.Mol Microbiol. 2001 Jul;41(2):289-97. Review.PMID: 11489118 Mittenhuber G.Comparative genomics of prokaryotic GTP-binding proteins (the Era, Obg, EngA, ThdF (TrmE), YchF and YihA families) and their relationship to eukaryotic GTP-binding proteins (the DRG, ARF, RAB, RAN, RAS and RHO families).J Mol Microbiol Biotechnol. 2001 Jan;3(1):21-35. Review.PMID: 11200227","","Mon Dec 16 14:05:41 2002","1","","","" "AA00691","473215","472178","1038","ATGATCACCGTTTATGCCTGGATTGTTTCCCTGATGTCGCTGCCGTTTATGTTAATGACAGCAAAACTGGAACGGCGCAGCCTGCTGATTAAACTCTTTATTGTGTTTGTCGCCAGCCATATCCTTTCCGTTGTGGCGTGGGATTTTTGGATTCTGCTGTTATCCCGTATCGGCGTGGCGTTTACCCACGCAATTTTCTGGTCCATTACCACATCCCTTGCGGTGCGGGTGGCACCGAAAGATAAAAAAGCACAGGCGATCGGGTTGCTGGCAATGGGTAGCGCGTTGGCGATGGTGCTAGGCTTGCCCCTTGGACGGGTTATCGGACAGTATTTTGGTTGGCGTGAGGCATTCGGCATTATCGCGTTCCTGGCGTTTGCCGTGTTAGTATTGCTTTATCGCTTCCTGCCGCACTTGGCGAGCCTCAATGCCGGTTCGTTGAAATCCGTTCCTTTGCTGTTTAAACGTCCGCTGCTGGTAGGATTATATGTGCTGACCATTCTGATTATTTCGGCGCATTTCACCGCTTACAGTTATATTGAACCGTTTATTGTGCGTATCGGCGCAATGAGCGATAGCACCGCCACGGCGATCTTATTGATTTTTGGCTTATCGGGCATTACCGCCAGTTTGTTGTTTAACCGCTTTCACCGTTTCGCACCGGCAAAATTTTTGTTGAGCACCATGGCTATTTTAGTCCTTTCTCTGCTGCTGTTATTGCCGTTCAGTCAAAATCAAATCGCCATGTTCCTGTTGGCGTTTATTTGGGGCGTAGGCATTTCCGGTATCGGTTTAAGTTTGCAGGTGCGGGTGTTGCAACTGGCACCTGATGCCACCGATGTGGCAATGGCGATTTATTCGGGGCTTTATAATATCGGTATTGGCGGCGGCGCATTATTAGGCAACCAAGTCATGCAACATCTCGGACTTGCCAACATCGGCTTCTCAGGCGCCTTGTTTGCAGCGCTTGGGTTGATGTTGTTTGTGTCTATCCATTTTCGTTATGGAAAAGCTAGTAGCGAAAATTTAACGCATTTA","","","43437","MITVYAWIVSLMSLPFMLMTAKLERRSLLIKLFIVFVASHILSVVAWDFWILLLSRIGVAFTHAIFWSITTSLAVRVAPKDKKAQAIGLLAMGSALAMVLGLPLGRVIGQYFGWREAFGIIAFLAFAVLVLLYRFLPHLASLNAGSLKSVPLLFKRPLLVGLYVLTILIISAHFTAYSYIEPFIVRIGAMSDSTATAILLIFGLSGITASLLFNRFHRFAPAKFLLSTMAILVLSLLLLLPFSQNQIAMFLLAFIWGVGISGIGLSLQVRVLQLAPDATDVAMAIYSGLYNIGIGGGALLGNQVMQHLGLANIGFSGALFAALGLMLFVSIHFRYGKASSENLTHL","472180","","conserved hypothetical protein (possible multidrug/sugar efflux transporter)","Inner membrane, Cytoplasm","","
InterPro
IPR007114
Family
Major facilitator superfamily
PS50850\"[1-339]TMFS
InterPro
IPR011701
Family
Major facilitator superfamily MFS_1
PF07690\"[1-306]TMFS_1
noIPR
unintegrated
unintegrated
PTHR10074\"[1-341]TMAJOR FACILITATOR SUPERFAMILY MEMBER
PTHR10074:SF29\"[1-341]TMAJOR FACILITATOR FAMILY TRANSPORTER
signalp\"[1-20]?signal-peptide
tmhmm\"[4-19]?\"[28-46]?\"[52-72]?\"[87-107]?\"[117-137]?\"[158-180]?\"[194-214]?\"[219-241]?\"[247-267]?\"[282-302]?\"[308-328]?transmembrane_regions


","No hits to the COGs database.","","Residues 141 to 196 match (8e-11) PD:PD020027 which is described as SUGAR MEMBRANE INNER TRANSPORTER EFFLUX TRANSMEMBRANE PROTEOME COMPLETE PROBABLE B ","","","","","","","","","","","","Wed Feb 19 14:57:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00691 is paralogously related to AA02958 (8e-05) and AA00266 (9e-04).","","","","","","","","","","","Condemine G.Characterization of SotA and SotB, two Erwinia chrysanthemi proteins which modify isopropyl-beta-D-thiogalactopyranoside and lactose induction of the Escherichia coli lac promoter.J Bacteriol. 2000 Mar;182(5):1340-5.PMID: 10671456 ","","Mon Dec 16 14:15:19 2002","1","","","" "AA00692","474575","473376","1200","ATGAAAAAGATCGCAATTATTACTGTGGTCGTCATACTTGCGATCTTTGCATTTTTTGATGTCCAAATTCAGAAACTGGAAACGGTGGTTTCCGCGAAACTGGCGCAACATGAAACCCAATTTCAAGTATTTAGTCTAGGGTTTTTCCCACAACCTTACCTTGCTTTTGAAAACGTTAAACATAACCAAATTAGCATTGAAAAACTGACCGGTAAATTTCCGTTATCCGCGTTGTTTTCTGGGAATGTCAAATTACAGGCGCTGGAAATCCAAAACGCCAAATGGTCTAAAAACGCGCAGAATAGCGCCGATATTCAAATGCGTTTTTCCGATTTCTCCCTTGATAATATTTCTTCCGATGGCATTGTCTTTAGCGGCGATAATTCAGTTACGGTGGAATTGGCAAAACCCTTGTACGGCAACAATAAAATGTTTAATTTTCGTTTTATTAATGGCGTGCTTCAGCGTAGCGACGAGCGAGAATTTACGGCGCAGTTCGATCATGCCGTTTTAAATGAAGAAACTTTAGGCTTTATTCAGGCGGATTTGGATTTATCCCAATACACCAAGCACCTGACCGCAGACATTAATTCTTACTGCCTGCCTGATTCGCCTTGTACCGCACGCTTGGATTATGTCAGTGAGCCGGAAAAAAGTGCGGTCGGTTTTTCCGCTAAAAATTATCCGCTGGAACGCCTGCTAACCTGGCTCACCTTCCCGAAAACCATTACCGGCAATGCCGATGTGGACATCGCCGTGCAATTCGCCCATTCCCAAATTATCGACGGTAAATTCTATTTTGATGCGAGAAACGGCGAATTATTGGGGCTAAATTTGCTGGAACTGGCAGGACGACATTTGCCGATTAACTGGGATGTTTCAGCGTCAAAAGACAGATATAATACTAATACCAAATACGACCGGATGACCAGTAGCTTCCGTTTACAGGGGCATCAACTTGATATTGAAAAAATGATCTTGAAAACCACCGCACTTTTAGGTGAGGGGCGTGGTCGGGTGAATTTGCAATCCATGCAATGCTATGTTGACCTGAACCTTCGTCCAACCGATGAAAAATATACGGACATTGTGCTACCGATTCATTTCTTTAATAGTTGCTATTCGCCGCAATATGAAGTGAATATCGACAAAGCATTTCGCAATAAAATCAAAGAACTTCTTCGACGTAAATTAAAACAA","","","45564","MKKIAIITVVVILAIFAFFDVQIQKLETVVSAKLAQHETQFQVFSLGFFPQPYLAFENVKHNQISIEKLTGKFPLSALFSGNVKLQALEIQNAKWSKNAQNSADIQMRFSDFSLDNISSDGIVFSGDNSVTVELAKPLYGNNKMFNFRFINGVLQRSDEREFTAQFDHAVLNEETLGFIQADLDLSQYTKHLTADINSYCLPDSPCTARLDYVSEPEKSAVGFSAKNYPLERLLTWLTFPKTITGNADVDIAVQFAHSQIIDGKFYFDARNGELLGLNLLELAGRHLPINWDVSASKDRYNTNTKYDRMTSSFRLQGHQLDIEKMILKTTALLGEGRGRVNLQSMQCYVDLNLRPTDEKYTDIVLPIHFFNSCYSPQYEVNIDKAFRNKIKELLRRKLKQ","473378","","conserved hypothetical protein","Outer membrane, Periplasm, Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
PD138521\"[21-399]TY134_HAEIN_P43952;
signalp\"[1-23]?signal-peptide
tmhmm\"[5-23]?transmembrane_regions


","No hits to the COGs database.","","Residues 21 to 399 match (6e-55) PD:PD138521 which is described as PROTEOME COMPLETE TRANSMEMBRANE PM0950 HI0134 ","","","","","","","","","","","","Mon Dec 16 14:17:44 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00692 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00694","475160","474579","582","ATGAGATTATGTGATACCGACATTGAACGTTATCTGGATGAAGGGCTAATCTCCCTCAATCCGCGCCCGTCGAACGATAAAATTAATGGCGCCACAATTGATGTGCGTTTGGGCAATTCCTTCCGCGTATTTCGTGAACATTCCGCCCCTTACATTGATTTGAGCGGTCCGAAAGAAGAAGTGTCGGCGCAGTTGGAATCGGTCATGAGCGATGAAATGATTATCGGTGATGACGAAGCCTTCTTTTTACATCCCGGCGTGCTGGCGCTTGCCACGACTTTGGAATCAGTAAAACTGCCGGCGAATATTATCGGTTGGCTGGACGGGCGTTCTTCTTTGGCGCGTTTGGGGTTGATGGTACACGTCACCGCCCATCGTATCGACCCAGGCTGGGAAGGCAAAATCGTGTTGGAATTTTACAATTCCGGCAAATTACCGTTAGCGTTACGCCCGAATATGATTATCGGCGCCTTGAGTTTCGAAGTGTTAAGCGGACCGGCGGCGCGTCCGTACAGCAGCCGCAAAGACGCAAAATACAAGAACCAACAAAATGCCGTTGCCAGCCGCATTGATGAGGACAAA","","","21421","MRLCDTDIERYLDEGLISLNPRPSNDKINGATIDVRLGNSFRVFREHSAPYIDLSGPKEEVSAQLESVMSDEMIIGDDEAFFLHPGVLALATTLESVKLPANIIGWLDGRSSLARLGLMVHVTAHRIDPGWEGKIVLEFYNSGKLPLALRPNMIIGALSFEVLSGPAARPYSSRKDAKYKNQQNAVASRIDEDK","474581","","dCTP deaminase (deoxycytidine triphosphate deaminas)","Cytoplasm","","
InterPro
IPR003232
Domain
dCTP Deaminase
PD004900\"[71-183]TDCD_ECOL6_Q8X7L4;
InterPro
IPR011962
Family
Deoxycytidine triphosphate deaminase
TIGR02274\"[2-190]TdCTP_deam: deoxycytidine triphosphate deami
noIPR
unintegrated
unintegrated
G3DSA:2.70.40.10\"[1-193]Tno description


","BeTs to 19 clades of COG0717COG name: Deoxycytidine deaminaseFunctional Class: FThe phylogenetic pattern of COG0717 is aompkz-q--r-bcef-hsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 2.3e-55) to 5/5 blocks of the IPB003232 family, which is described as \"dCTP Deaminase\". Interpro entry for IP:IPR003232. IPB003232A 1-9 0.15 IPB003232B 32-44 8.3e-05 IPB003232C 85-123 1.3e-23 IPB003232D 128-141 4.1e-08 IPB003232E 146-174 3.5e-11","Residues 1 to 28 match (9e-08) PD:PD355632 which is described as DEAMINASE HYDROLASE DCTP PROTEOME COMPLETE DEOXYCYTIDINE TRIPHOSPHATE ","","","","","","","","","","","","Mon Dec 16 14:22:06 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00694 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 50 to 189 (E-value = 3.1e-22) place AA00694 in the dUTPase family which is described as dUTPase (PF00692)","","","","","Krogan NJ, Zaharik ML, Neuhard J, Kelln RA. A combination of three mutations, dcd, pyrH, and cdd,establishes thymidine (Deoxyuridine) auxotrophy in thyA+strains of Salmonella typhimurium. J Bacteriol. 1998 Nov;180(22):5891-5. PMID: 9811646 Koonin EV. Pseudouridine synthases: four families of enzymes containinga putative uridine-binding motif also conserved in dUTPasesand dCTP deaminases. Nucleic Acids Res. 1996 Jun 15;24(12):2411-5. PMID: 8710514 Estevenon AM, Kooistra J, Sicard N. An Escherichia coli strain deficient for both exonuclease Vand deoxycytidine triphosphate deaminase shows enhancedsensitivity to ionizing radiation. Mol Gen Genet. 1995 Feb 20;246(4):514-8. PMID: 7891665 ","","Mon Dec 16 14:22:06 2002","1","","","" "AA00695","475820","475173","648","ATGTCAGATACTCAAAATTCATCTTGTATTATTATCGCCATCGCGGGGGCGTCCGCCTCCGGAAAAAGCTCTATTGCGTCCACTGTTCATAGAGAACTGTGCAATGAATTAGGCTGCGAAGAAATCGGCATTATTGCGGAAGACAGTTATTACAAAGATCAAAGCCATCTGGAAATGGCAGAGCGGGTGAAAACCAATTATGACCACCCCAATTCTATGGATCGCGATTTGCTCATTCAACATTTGAAATCCCTCAAGGTCGGCAATGCCGTCGATATTCCTGTTTATAGCTATGTTGAACATACTTGTACCGACGACGTCACCCATTTCACCCCGAAAAGAATCGTGATTTTAGAAGGCATTTTGTTATTAACCGATGAACGTGTGCGTCAGTTGGCGGATATTTCCGTGTTCGTAGATACGCCGCTGGATATTTGCTTTATTCGTCGTTTGCAGCGTGACATGGAAGAGCGAGGGCGTTCTCTGCAATCGGTGATCGACCAATATCGCGCCACCGTGCGCCCGATGTTCCTGCAATTTATCGAACCGTCCAAACAATATGCCGATATTGTAATCCCACGCGGCGGCAAAAACCGCATTGCCATCAATATGTTAAAAGCGCAAATTATGCAGTTATTAAGCCGAAAA","","","24483","MSDTQNSSCIIIAIAGASASGKSSIASTVHRELCNELGCEEIGIIAEDSYYKDQSHLEMAERVKTNYDHPNSMDRDLLIQHLKSLKVGNAVDIPVYSYVEHTCTDDVTHFTPKRIVILEGILLLTDERVRQLADISVFVDTPLDICFIRRLQRDMEERGRSLQSVIDQYRATVRPMFLQFIEPSKQYADIVIPRGGKNRIAINMLKAQIMQLLSRK","475175","","uridine kinase","Cytoplasm, Periplasm","","
InterPro
IPR000764
Family
Uridine kinase
PR00988\"[9-26]T\"[43-54]T\"[88-103]T\"[144-154]T\"[158-169]T\"[180-193]TURIDINKINASE
PTHR10285:SF6\"[17-211]TURIDINE CYTIDINE KINASE I
TIGR00235\"[1-214]Tudk: uridine kinase
InterPro
IPR006083
Family
Phosphoribulokinase/uridine kinase
PF00485\"[11-201]TPRK
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[8-215]Tno description
PTHR10285\"[17-211]TURIDINE KINASE RELATED


","BeTs to 11 clades of COG0572COG name: Uridine kinaseFunctional Class: FThe phylogenetic pattern of COG0572 is -o----y-vd-lbce-gh-----itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 4.7e-51) to 6/6 blocks of the PR00988 family, which is described as \"Uridine kinase signature\". Prints database entry for PR:PR00988. PR00988A 9-26 7.2e-11 PR00988B 43-54 1.8e-05 PR00988C 88-103 8.9e-06 PR00988D 144-154 7.4e-07 PR00988E 158-169 8.5e-06 PR00988F 180-193 3.8e-08Significant hit ( 1.3e-22) to 3/5 blocks of the IPB001324 family, which is described as \"Phosphoribulokinase family\". Interpro entry for IP:IPR001324. IPB001324A 8-29 0.0034 IPB001324C 111-122 0.39 IPB001324D 137-187 5.8e-15","Residues 135 to 214 match (4e-36) PD:PD003826 which is described as KINASE URIDINE MONOPHOSPHOKINASE TRANSFERASE ATP-BINDING CYTIDINE COMPLETE PROTEOME CHLOROPLAST CYCLE ","","","","","","","","","","","","Mon Dec 16 14:23:22 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00695 is paralogously related to AA00930 (7e-06).","","","","","","Residues 11 to 201 (E-value = 2.9e-53) place AA00695 in the PRK family which is described as Phosphoribulokinase / Uridine kinase family (PF00485)","","","","","Schuster S, Zevedei-Oancea I. Treatment of multifunctional enzymes in metabolic pathwayanalysis. Biophys Chem. 2002 Sep 3;99(1):63. PMID: 12223240 Boursaux-Eude C, Margarita D, Gilles AM, Barzu O, SaintGirons I. Borrelia burgdorferi uridine kinase: an enzyme of thepyrimidine salvage pathway for endogenous use ofnucleotides. FEMS Microbiol Lett. 1997 Jun 15;151(2):257-61. PMID: 9228761 ","","Mon Dec 16 14:23:22 2002","1","","","" "AA00696","476129","477166","1038","ATGAAATTAAAATCACTTTCTCTCGCCATTTCCACCGCACTTTTAGCCGGCGGATTACTCGCCTCACAAGCGGCAACCGCCAAAGGGCGCTTGGTGGTGTACTGTAGTGCAACGAACATTTTATGTGAAACCACTACCAAAGCCTTTAGCGAAAAATATGATGTAAAAACCTCCTTCATCCGCAACGGTTCCGGCAGCACCTTCGCCAAAGTGGAAGCAGAAAAAAATAACCCGCAAGCAGATGTTTGGTTCGGCGGTACTTTCGATCCGCAAGCACAAGCTGCCGAACTCGGTTTGATTGAGCCTTATCAATCCAAACACATTGACGAAATCATAGAACGCTTCCGCGATCCGGCAAAAACCAAAGGTCACTACGTCTCCGCCATTTACATGGGGATTTTGGGCTTCGGTGTGAACACCGAACGTCTTGCAAAGTTAGGTATTAAAGACATACCGAAATGCTGGAAAGACCTAACGGATCCACGTTTTAAAGGTGAAGTACAAATTGCCGATCCGCAAAGCGCAGGTACTGCTTACACTGCGTTAGCTACTTTCGTACAATTGTGGGGCACAGAACAAGCCTTTGATTTTTTAAAAGCCTTACATCCGAACGTTTCCCAATACACCAAATCCGGCGTCACCCCATCCCGTAACGCCGCCCGTGGCGAAACCGCAGTAGGAATCGGTTTCTTACACGATTATGCTCTGGAAAAGCGCCAAGGTGCACCGTTGGAATTGGTGGTTCCGTGTGAAGGCACCGGTTATGAATTAGGCGGCGTGAGCATCTTGAAAGGCGCGCGCAACCTCGACAATGCCAAATTGTTCGTGGATTGGGCGTTATCCAAAGAAGGGCAGGAATTGGCATGGAAACAAGGGGATTCCTTACAAATTCTAACTAACACCACCGCAGAACAATCTCCAACAGCGTTTGACCCGAACAAACTCAACCTTATTAATTACGACTTTGAAAAATACGGCGCCAGCGAACAACGAAAAGCCCTGATTGAAAAATGGGTACAAGAGGTAAAATTAGCGAAA","","","39730","MKLKSLSLAISTALLAGGLLASQAATAKGRLVVYCSATNILCETTTKAFSEKYDVKTSFIRNGSGSTFAKVEAEKNNPQADVWFGGTFDPQAQAAELGLIEPYQSKHIDEIIERFRDPAKTKGHYVSAIYMGILGFGVNTERLAKLGIKDIPKCWKDLTDPRFKGEVQIADPQSAGTAYTALATFVQLWGTEQAFDFLKALHPNVSQYTKSGVTPSRNAARGETAVGIGFLHDYALEKRQGAPLELVVPCEGTGYELGGVSILKGARNLDNAKLFVDWALSKEGQELAWKQGDSLQILTNTTAEQSPTAFDPNKLNLINYDFEKYGASEQRKALIEKWVQEVKLAK","477168","","iron(III) ABC transporter, periplasmic iron-compound-binding protein","Periplasm","","
InterPro
IPR006059
Family
Bacterial extracellular solute-binding protein, family 1
PF01547\"[12-286]TSBP_bac_1
InterPro
IPR011587
Domain
Prokaryotic extracellular metal-binding protein
PD008688\"[222-292]TQ8U777_AGRT5_Q8U777;
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[132-272]Tno description
signalp\"[1-29]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","BeTs to 12 clades of COG1840COG name: ABC-type iron/thiamine transport systems, periplasmic componentFunctional Class: HThe phylogenetic pattern of COG1840 is -o--kz---d-lbcefghsnuj--t-Number of proteins in this genome belonging to this COG is","","Residues 119 to 161 match (8e-13) PD:PD583936 which is described as PROTEOME AFUA COMPLETE ABC IRON-COMPOUND-BINDING IRONIII PERIPLASMIC TRANSPORTER ","","","","","","","","","","","","Mon Dec 16 14:32:32 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00696 is paralogously related to AA00698 (1e-133), AA01642 (1e-102), AA01048 (5e-14), AA02286 (5e-13), AA01479 (2e-10) and AA02721 (1e-06).","","","","","","","","",""," Haraszthy VI, Jordan SF, Zambon JJ.,Abstract Identification of Fur-regulated genes in Actinobacillus actinomycetemcomitans.Microbiology. 2006 Mar;152(Pt 3):787-96.PMID: 16514158 James D, Shao H, Lamont RJ, Demuth DR.,The Actinobacillus actinomycetemcomitans ribose binding protein RbsB interacts with cognate and heterologous autoinducer 2 signals.Infect Immun. 2006 Jul;74(7):4021-9.PMID: 16790775Willemsen PT, Vulto I, Boxem M, de Graaff J.Characterization of a periplasmic protein involved in iron utilization of Actinobacillus actinomycetemcomitans.J Bacteriol. 1997 Aug;179(15):4949-52.PMID: 9244288","Chin N, Frey J, Chang CF, Chang YF.Identification of a locus involved in the utilization of iron by Actinobacillus pleuropneumoniae.FEMS Microbiol Lett. 1996 Sep 15;143(1):1-6.PMID: 8807793 ","Mon Dec 16 14:38:27 2002","Mon Dec 16 14:38:27 2002","1","","","" "AA00697","477139","477234","96","ATGGGTACAAGAGGTAAAATTAGCGAAATAGCGCTGAAAAGTGCGGTTAAAAATCCATGTGTTTTTTTAACCGCACTTTTATTCGTAGGGGCAGTT","","","3317","MGTRGKISEIALKSAVKNPCVFLTALLFVGAV","477234","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-0]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 10:21:27 2004","Mon Feb 23 10:21:27 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00697 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 10:21:27 2004","","","","","","","","","","","","","1","","","" "AA00698","477331","478371","1041","ATGAAACTCTCGAAAATCGCATTAACAGTATCCGCATCTGCAACCGTACTTAGTGGCATTTTTTTCTCAACTAATGCCCTCGCTGAAGGGCGATTAGTCGTCTATTGCAGTGCGCAGAATTCAGTGTGTGAAACTCAGGTCCAAGCTTTTGCTAAAAAATACGATGTAAATGCCACTTTTATCCGTAATAGTTCAGGAAGCACCCTAGCCAAAATAAAAGCAGAAACCAATAATCCACAAGCCGATGTATGGTATGGCGGAACGTTTGATCCCCACTCACAGGCAGCTGAAATGGATTTATTAACAGCATATCAATCTCCTTTATTGAAGGAAGTTATGCCGGAATTCAAAGACCCGGGGCGCCGTAAAGGCAACTATAGCTCTGTTGTTTATATGGGAGTTCTGGGTTTTGGTGTTAATACAGAGAAATTAAAGAAACTTGGTATTACTGATGTTCCAAAATGTTGGAAAGATTTATTAGATCCAAGATTCAAAAATGAAATTCAAATTTCAGATCCTCAAAGCGCAGGAACCGCATATACTGCTATTGCCACTTTTGTTCAACTTTGGGGCGAAGATGCTGCATTTAACTATTTAAAAGATCTTGATAAAAATATTTCTCAGTATCCAAAAGCAGGGACGGTTCCCGCACATAATTTAGCCCGTGGGGAAACCACAGTAGGAATTGGATTCTTACAAAATTATTCTTTTGAAAAACAAAATGGCGCGCCAATTGAAGTCATCGTACCTTGCGAAAGTACCGGTTACGAGCTAGGCGGTGTAAGCATTATTAAAAACGCCCGTAATTTAAAAAATGCTCAATTATTTGTTGACTGGGCTATGTCTAAAGAGTCTCAAGAACTCTCTTGGAAAACAGGACAATCTCACCATATTTTAACCAATATAAATGCCGAGGGTTCTCCTTACGCATTAAAATCAAATGAATTGAATTTAATTAAATATGATTTTGATAAATTTGGTTCTTCCGATGTACGGAGTCGTTTGATTGATCGTTGGGTACATGAAGTCAAATTAAATAAA","","","38320","MKLSKIALTVSASATVLSGIFFSTNALAEGRLVVYCSAQNSVCETQVQAFAKKYDVNATFIRNSSGSTLAKIKAETNNPQADVWYGGTFDPHSQAAEMDLLTAYQSPLLKEVMPEFKDPGRRKGNYSSVVYMGVLGFGVNTEKLKKLGITDVPKCWKDLLDPRFKNEIQISDPQSAGTAYTAIATFVQLWGEDAAFNYLKDLDKNISQYPKAGTVPAHNLARGETTVGIGFLQNYSFEKQNGAPIEVIVPCESTGYELGGVSIIKNARNLKNAQLFVDWAMSKESQELSWKTGQSHHILTNINAEGSPYALKSNELNLIKYDFDKFGSSDVRSRLIDRWVHEVKLNK","478373","","iron(III) ABC transporter, periplasmic iron-compound-binding protein","Periplasm, Outer membrane","","
InterPro
IPR006059
Family
Bacterial extracellular solute-binding protein, family 1
PF01547\"[6-287]TSBP_bac_1
InterPro
IPR011587
Domain
Prokaryotic extracellular metal-binding protein
PD008688\"[223-293]TQ8U777_AGRT5_Q8U777;
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[31-308]Tno description
signalp\"[1-28]?signal-peptide


","BeTs to 12 clades of COG1840COG name: ABC-type iron/thiamine transport systems, periplasmic componentFunctional Class: HThe phylogenetic pattern of COG1840 is -o--kz---d-lbcefghsnuj--t-Number of proteins in this genome belonging to this COG is","","Residues 10 to 191 match (5e-10) PD:PD589863 which is described as PROTEOME COMPLETE PERIPLASMIC SOLUTE-BINDING PBP PA3250 PROBABLE ABC TRANSPORTER ","","","","","","","","","","","","Tue Dec 17 07:57:54 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00698 is paralogously related to AA00696 (1e-133), AA01642 (1e-101), AA01048 (9e-12), AA02286 (2e-10), AA02721 (1e-07) and AA01479 (6e-07).","","","","","","Residues 4 to 287 (E-value = 4.9e-07) place AA00698 in the SBP_bac_1 family which is described as Bacterial extracellular solute-binding protein (PF01547)","","",""," Haraszthy VI, Jordan SF, Zambon JJ.,Abstract Identification of Fur-regulated genes in Actinobacillus actinomycetemcomitans.Microbiology. 2006 Mar;152(Pt 3):787-96.PMID: 16514158 James D, Shao H, Lamont RJ, Demuth DR.,The Actinobacillus actinomycetemcomitans ribose binding protein RbsB interacts with cognate and heterologous autoinducer 2 signals.Infect Immun. 2006 Jul;74(7):4021-9.PMID: 16790775Willemsen PT, Vulto I, Boxem M, de Graaff J.Characterization of a periplasmic protein involved in iron utilization of Actinobacillus actinomycetemcomitans.J Bacteriol. 1997 Aug;179(15):4949-52.PMID: 9244288","Chin N, Frey J, Chang CF, Chang YF. Identification of a locus involved in the utilization of iron byActinobacillus pleuropneumoniae. FEMS Microbiol Lett. 1996 Sep 15;143(1):1-6. PMID: 8807793 ","Mon Dec 16 14:48:11 2002","Mon Dec 16 14:48:11 2002","1","","","" "AA00699","478402","480456","2055","ATGAGAAAGCAGTATAATTTTCTCAATTCCAATCTCTTTTGGGTAATGTTAGCAATGGCAGGCTTTATTTTCCTGCCATCATTGGCATTATATTACGGAATATCGGATTCCACTTCGGATGAAATACTTGCCGCAATGGGGTGGAGTCAACCTAATTTAAGTTGGCTATGGTTTGGTTCATTATTCCTTATTCCTATATTTTCTCGTCTATGTAAACAGAAAGGAGCTGTGTATCAGGGAAAAATAGAGTTCATTTTATCCTGTATAATTTTTGGATTTGTGATGGTCTCAGCCACAATTGCAAAAATCAGTTTGGGCTATTCTATTTTTGTTCTCACCATAGCACTAATCGGAGTTTCTACGAATGCACTTGCCAAAATGAAAGTCATGCAAAGTGATAAATTCATCATTGGCTCTTTAATTAGCATTGTCCTATTAATATTCTTTTTTATCGTTTATCCAACATTGGCGATCTTTATGTCAATGTTCTATAAAGGGACAGATTTTGTTCCCGGGCAAGTCATAGATATTATAAAGCAGCCTTATGTTGTCAGAATCATCCTAAACTCACTGTCTGTTGCCGGCACAATAGGCGTACTCGCTACAGCATTTGGTTTGATATTCGCGTTATACACAACAAGAATTGCCAAACGTAGTGCCGTAATAGGTAAAATATTCTCTATATTACCTATTGTCACCCCACCATTTGTAGTTGGATTAGGGGTAACTCTAATGTTAGGACGCTCCGGTTACATTACCCGGTATCTAGTCGAATACTTGGGATTTGATAGTAATTGGTTATATGGGTTCACAGGTATTGTTATTGCCCATACTCTTGCATTAACACCAATGTCTTTTATGATCTTAGAAGGGGCATTAAAGTCTATTCATCCATCTATTGAGGAAGCTTCCTATACGTTAAGAGCTAATCGCTATCAAACTTTCTTTAATATTATTTTCCCATTATTGAAACCGGCATTAGCTAATTCATTCTTAGTCGTTGCGATCCAGTCTATCGCTGACTTTAGTACACCATTAGTTTTAGGTGGTAGTTTTGATGTTATATCATCACAAATTTATTTCTATATAGCCGGTTCCCAACTGGACTACGCCTCTGCAAGTACCTTGGGTACAATATTGTTAGTCTTTTCTTTAGGTATCTTTATCATCCAATATTGGTGGATAGGCAATCGTTCCTATACAACTGTATCAGGTAAATCTTATCGAGGTGATGTACAAGAATTACCAACCACAATGAAATACGCCATTACCTTTATTTTAGGGGGTTGGGTAGTATTTAACATATTATTGTACGGTAGTATTTTCTACGGTAGTTTCACCGTAAACTGGGGTGTAAACTACACTCTAACACTGAAAAATTACATTACCTTATTTGGACAAGGCTTCAGCGATGGAGCATGGCCATCATTGATTCAAACCGTTATCTTCGCAGCTACAGCTGCACCGATCACTGCATTGTTTGGTTTATTAATTGCATACATTACTGTACGAAGAGAATTTAAAGGTAAGAAAACATTAGAGTTTCTCACTTTGCTTTGCTTTGCCGTACCGGGCACGGTAGCCGGTGTATCTTATATTCTTGCCTTTAATGACGCGCCTATTTACATTACAGGTACCAGCCTCATTGTTATTCTATCAATGATCATGCGTAATATGCCTGTAGGTATGCGTGCTGCAATTGCAGGTTTAGGGCAATTAGACAAATCATTAGATGAAGCCTCTTTATCTCTTAAAGGCAGCTCATTCAAAACAATTTGTTTTATTGTTTTCCCGCTATTAAAACCGGCGCTGCTATCTGCGTTAGTAACAAGCTTTGTTCGTGCAATGACAACTGTTAGTGCGATTGTCTTCTTAGTTACTGCAGATACCAGGGTAGCTACCTCATATATCTTAAACCGCGTAGAAGACGGCGAGTATGGTATCGCGATAGCATATGGTTCCCTCTTAATCGTGGTAATGATGGCGATTATTTTATTCTTCGACTGGATTGTCGGTGACACCCGCATTTCCCGTTCCAAAGCGAAAAAAATGAAT","","","75339","MRKQYNFLNSNLFWVMLAMAGFIFLPSLALYYGISDSTSDEILAAMGWSQPNLSWLWFGSLFLIPIFSRLCKQKGAVYQGKIEFILSCIIFGFVMVSATIAKISLGYSIFVLTIALIGVSTNALAKMKVMQSDKFIIGSLISIVLLIFFFIVYPTLAIFMSMFYKGTDFVPGQVIDIIKQPYVVRIILNSLSVAGTIGVLATAFGLIFALYTTRIAKRSAVIGKIFSILPIVTPPFVVGLGVTLMLGRSGYITRYLVEYLGFDSNWLYGFTGIVIAHTLALTPMSFMILEGALKSIHPSIEEASYTLRANRYQTFFNIIFPLLKPALANSFLVVAIQSIADFSTPLVLGGSFDVISSQIYFYIAGSQLDYASASTLGTILLVFSLGIFIIQYWWIGNRSYTTVSGKSYRGDVQELPTTMKYAITFILGGWVVFNILLYGSIFYGSFTVNWGVNYTLTLKNYITLFGQGFSDGAWPSLIQTVIFAATAAPITALFGLLIAYITVRREFKGKKTLEFLTLLCFAVPGTVAGVSYILAFNDAPIYITGTSLIVILSMIMRNMPVGMRAAIAGLGQLDKSLDEASLSLKGSSFKTICFIVFPLLKPALLSALVTSFVRAMTTVSAIVFLVTADTRVATSYILNRVEDGEYGIAIAYGSLLIVVMMAIILFFDWIVGDTRISRSKAKKMN","480458","","iron(III) ABC transporter, permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR000515
Family
Binding-protein-dependent transport systems inner membrane component
PF00528\"[187-400]T\"[473-678]TBPD_transp_1
PS50928\"[187-391]T\"[477-667]TABC_TM1
noIPR
unintegrated
unintegrated
signalp\"[1-29]?signal-peptide
tmhmm\"[12-34]?\"[53-68]?\"[77-97]?\"[103-125]?\"[135-157]?\"[190-210]?\"[225-247]?\"[266-286]?\"[318-340]?\"[346-366]?\"[376-396]?\"[421-441]?\"[456-476]?\"[482-500]?\"[515-535]?\"[539-557]?\"[604-626]?\"[648-670]?transmembrane_regions


","BeTs to 12 clades of COG1178COG name: ABC-type iron/thiamine transport systems, permease componentsFunctional Class: HThe phylogenetic pattern of COG1178 is -o--kz---d--bcefgh-nuj--t-Number of proteins in this genome belonging to this COG is","","Residues 46 to 204 match (3e-21) PD:PD034628 which is described as PERMEASE PROTEOME SYSTEM COMPLETE FERRIC AFUB IRON INNER TRANSMEMBRANE MEMBRANE ","","","","","","","","","","","","Mon Dec 16 14:59:45 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00699 is paralogously related to AA01644 (0.0), AA01050 (9e-27), AA01780 (1e-15), AA01950 (5e-14), AA02719 (1e-12), AA01682 (7e-11), AA02720 (3e-08), AA01866 (6e-08), AA01948 (7e-08), AA01650 (6e-07) and AA01649 (1e-04).","","","","","","Residues 473 to 678 (E-value = 3.8e-09) place AA00699 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component (PF00528)","","",""," James D, Shao H, Lamont RJ, Demuth DR.,The Actinobacillus actinomycetemcomitans ribose binding protein RbsB interacts with cognate and heterologous autoinducer 2 signals.Infect Immun. 2006 Jul;74(7):4021-9.PMID: 16790775","Chin,N., Frey,J., Chang,C.F. and Chang,Y.F.Identification of a locus involved in the utilization of iron byActinobacillus pleuropneumoniaeFEMS Microbiol. Lett. 143 (1), 1-6 (1996)PubMed: 8807793","","Mon Dec 16 15:01:07 2002","1","","","" "AA00700","480475","481518","1044","ATGAACAATGATTTCTTAGTATTAAAAAATATCACCAAATCTTTCGGCAAATCCGTCGTCATTGATAATTTGGATTTAACCATTAAACGTGGCACCATGGTCACCCTGCTCGGTCCGTCCGGTTGCGGTAAAACTACAGTTTTACGCTTGGTTGCAGGCTTGGAAAACCCGACATCCGGTCAAATTTTTATTGACGGCGAAGACGTCACCAAATCCTCCATTCAAAACCGCGATATTTGTATTGTGTTCCAGTCCTACGCCTTATTCCCGCACATGAGCATCGGCGATAACGTGGGCTACGGCTTGCGTATGCAAAACGTGAGCAAAGAAGAACGTAAACAGCGGGTGAAAGAAGCCTTGGAATTGGTGGATCTAGCCGGGTTTGAAGAGCGCTATGTGGATCAGATCTCAGGCGGTCAACAGCAACGTGTGGCACTTGCCCGTGCGCTTGTGCTCAAACCAAAAGTGTTATTGTTCGATGAGCCGCTAAGTAACCTGGATGCCAACTTACGTCGCGCTATGCGTGAAAAAATCCGTGAATTACAACAAAGTCTCGGCATCACTTCGCTTTATGTGACCCACGACCAAACGGAGGCCTTCGCGGTGTCTGATGAAGTTATCGTAATGAACAAAGGCAAAATTATGCAAAAAGCGTCTGCGAAAGATCTTTATCAACGCCCGAACTCGCTATTTCTTGCCAACTTCATGGGTGAATCCAGCATTTTCCCGGCAAAATTGCAAGGTAACACCGTCAATATTGACGGCTATGGGTTAACCCTGAAAGACGCTGCACAATTTCATTTGGCAGATAGTGATTGCCTGGTGGGGATTCGTCCGGAAGCGGTTTATCTTTCCGAAACCGGCAGCGAAGCCCAACGTTGCACCATTAAAAGTGCGGTGTACATGGGTAACCATTGGGAAGTGGTGGCGCAATGGCACGGCAAAGATTTGTTGATTAACAGCCGCCCGGAACACTTCAACCCGACATTGCAGGAAGCTTATATTCAACTTTCCGAACAAGGGGTTTTCCTGTTAAAAAATGAA","","","38762","MNNDFLVLKNITKSFGKSVVIDNLDLTIKRGTMVTLLGPSGCGKTTVLRLVAGLENPTSGQIFIDGEDVTKSSIQNRDICIVFQSYALFPHMSIGDNVGYGLRMQNVSKEERKQRVKEALELVDLAGFEERYVDQISGGQQQRVALARALVLKPKVLLFDEPLSNLDANLRRAMREKIRELQQSLGITSLYVTHDQTEAFAVSDEVIVMNKGKIMQKASAKDLYQRPNSLFLANFMGESSIFPAKLQGNTVNIDGYGLTLKDAAQFHLADSDCLVGIRPEAVYLSETGSEAQRCTIKSAVYMGNHWEVVAQWHGKDLLINSRPEHFNPTLQEAYIQLSEQGVFLLKNE","481520","","iron(III) ABC transporter, ATP-binding protein","Cytoplasm, Outer membrane, Inner membrane","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[135-178]TQ9CM80_PASMU_Q9CM80;
PF00005\"[31-212]TABC_tran
PS50893\"[6-236]TABC_TRANSPORTER_2
PS00211\"[136-150]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[30-213]TAAA
InterPro
IPR013611
Domain
Transport-associated OB
PF08402\"[275-345]TTOBE_2
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[3-239]Tno description
PTHR19222\"[6-244]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF44\"[6-244]TSULFATE-TRANSPORTING ATPASE


","BeTs to 4 clades of COG3841COG name: ABC-type iron transport systems, ATPase componentsFunctional Class: PThe phylogenetic pattern of COG3841 is ------------b-efgh-n----t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-36) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 20-66 2.5e-20 IPB001140B 133-171 5.1e-14 IPB001140C 189-218 23","Residues 77 to 214 match (8e-07) PD:PD032786 which is described as BINDING ABC PROTEOME ATP COMPLETE ATP-BINDING TRANSPORTER TRANSPORTER ","","","","","","","","","","","","Tue Dec 17 08:11:46 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00700 is paralogously related to AA01645 (5e-98), AA02718 (5e-71), AA01656 (3e-59), AA01947 (6e-47), AA01051 (8e-47), AA00415 (3e-40), AA02353 (1e-38), AA01524 (3e-36), AA00858 (5e-36), AA01867 (2e-34), AA02324 (4e-32), AA01824 (9e-30), AA02899 (6e-29), AA01779 (3e-28), AA01422 (2e-27), AA02320 (3e-27), AA02080 (3e-27), AA02140 (6e-27), AA02440 (3e-26), AA01616 (2e-25), AA00799 (9e-25), AA01820 (1e-24), AA01568 (4e-24), AA01684 (2e-23), AA01456 (1e-21), AA02805 (5e-21), AA01961 (5e-21), AA00933 (5e-21), AA01393 (9e-20), AA02152 (4e-19), AA02898 (6e-19), AA02331 (3e-18), AA00751 (5e-18), AA02786 (1e-17), AA00207 (2e-17), AA01509 (5e-17), AA02550 (7e-17), AA02484 (7e-17), AA02609 (8e-16), AA01757 (1e-15), AA02573 (1e-15), AA00061 (5e-15), AA01510 (8e-15), AA00591 (1e-14), AA02606 (2e-14), AA02642 (4e-14), AA02225 (5e-13), AA01569 (1e-10), AA00934 (1e-10), AA01555 (5e-10), A02145 (6e-08), AA02146 (5e-07), AA02226 (2e-06) and AA01291 (8e-05).","","","","","","Residues 31 to 212 (E-value = 2.6e-67) place AA00700 in the ABC_tran family which is described as ABC transporter (PF00005)","","",""," James D, Shao H, Lamont RJ, Demuth DR.,The Actinobacillus actinomycetemcomitans ribose binding protein RbsB interacts with cognate and heterologous autoinducer 2 signals.Infect Immun. 2006 Jul;74(7):4021-9.PMID: 16790775","Kashiwagi K, Innami A, Zenda R, Tomitori H, Igarashi K. The ATPase activity and the functional domain of PotA, acomponent of the sermidine-preferential uptake system inEscherichia coli. J Biol Chem. 2002 Jul 5;277(27):24212-9. PMID: 11976340 Chin,N., Frey,J., Chang,C.F. and Chang,Y.F.Identification of a locus involved in the utilization of iron byActinobacillus pleuropneumoniaeFEMS Microbiol. Lett. 143 (1), 1-6 (1996)PubMed: 8807793Rodriguez,F. and Grandi,G. An operon encoding a novel ABC-type transport system inBacillus subtilis. Microbiology 141(Pt 7): 1781-1784.1995. PubMed: 7551042. ","","Tue Dec 17 08:11:46 2002","1","","","" "AA00702","481800","483908","2109","ATGAGCAAAAAAAGAAAAGTCACGTTAACACTTGCCGCTATCATCGTTGCTATCGGTAGCGGTGCACAAATTTACACCAATCAACAAGTGGAGCAGGTGCTACAAAAATTCCCTTATTCCTTGGATAATCAACTTCGCCTCAATGTAACCGAAACGAATAACAATTTTTTCAGCCGCCATTTAACCTTTAGCCTTGAAAATCCTGATGGCAAAACCACCGATGTGATTTCTGCCAAGCTTACTGCTCTCCCGTTTTTTATCACAGCGGAATCCAAACTGTCCGATCAACTGGTGCACCAATTAAACAAAAATCTCAACATCACTATTGATAAAAATACCATTAACAGTAAATTCTCGCCGATGGGAGATTACCTGCAATCGTATGTGTTAACCGGATTCCGTGACTTCACCAATAAATCACAAAACCTTGCCGTTACCCTAAATTTCAACGCAGAAAACAAAGATGTCAACATTAAAACCGATTTAAGCGGCTTCAATTACGATAAAAACAGCAAACTGGAACAAATTAACGGGCAGTTTCATTTCGTACCTGTGGGTGATAATCAATATGATATTTCCTCCATTGAACTTAACATAAAAAATGCCGAATTAAATTTAATGAACGGTGAAAATACTAAAATTCAGCTTAAAAGTGCGAAATATCAGTTTGATATTAAGAAAAACGAAGAAGCACAACAGCGCGATTTAACCACCAAATTCAGCAGTGATATTCTCCGCGTTGCCAACAAAGAACGCCCCACAGAAGAAAGCCAGACCACCATTAACGGATTATCCCTCAATCTCACCCAACAAGGCGTGAAAAGTGCGGTCGATTTTGCCGATGAATTTAAAAAACTCACCAATGATAACCAAGGCATAAAAAATGCCGTCAATTTTTTGGTTGCCGTGTTGACCCAAAATGAAGAGCTCAAAGGTTCGCTTACCGTAAAATCCGTTGAAGCCCCGAAAAATCAAAAACCTTATTTCAATTTGAATGACACGACCTTCAGCCTCAAAATGGACAATCGTCATCTCGACAATGCAGATATTAATCTGCAACTTAATGTCGGTAACGTCAAACAAACACCGGAAGATCAAAACAAGCAATGGCAGGCGAAAGGCGCCAAAATTATCTATCACTTGGAAAATTACAACTTGGAAAATGAGTTAGCATTCATTCCTTTTTATCTGGATTCCTTCACGGTAAAAACCCCACCGAAAGAAGACAACAAAGTCTTGTTAAAATTGAAAGAGAAATGGGCAAAAGAATCCGGTGGCAATAGCAACGCGGAAATTGCATTGCAATCATTCAATTATGGCAATGTTGTGTCTGGGAACTTATCCGTAAAAAGCCAATCAATGGAAGAAAACCATCAATATCGCGGCGCATCCACACTTTCCATGCAAAAACTGGCACTACCTGAAGCACAAATACAAATTGAAGATCTTGCCGTCAGTCTTCCACTTACCGTCAACAATTACCCGAAACTGGCAGAAGCGCAATTTTGTTCCGGTCTGGCAGCGCCACTGTGTTCTGCCTATTTCACCTCAGAAACCATAGAAAAATATATTGAAAACCAATGGAAAGGATTAGATTTAAGCATAGACAACTCAACAATTACGCTGAATTTGAACACCTATCCTGGTACCAAAGCCTATCCGCTTAAACTGGATATCAACGGCGCGATTAAATCACAACAAGATAACCAAACACCATTGGATACACTCGACCAAAACCTCAGAGGCTCACTCAGTATCACCCTTAATAAGGGCTTAATCGACGATACCAATGAGCAAAGCCTAAAAATCAAAAATGACTCGCCATTCTGGCAACAACTTCAAATGGAAATAAAACCGGAAGACACACTTTCGCCGTTGTTCCTGGAAGACAAGGATAATTACGTAATTAAACTGGAAAAAACCGACAAAGGCACGTTTATTAACGGCAAAACCGAGGAAGAAATCCGGCAGGAAATATTAAAACAAACGGAAGAAGTTGAACCGCAAGAGGAAGCGGAGGAAGTAAAACCGCAAGTGGAAATACCGCCTCAATCAGAGGGTGAAAAACAAGAAGCAGTTCAACCAAATCAAATCGAAAAACCGAACAAC","","","81053","MSKKRKVTLTLAAIIVAIGSGAQIYTNQQVEQVLQKFPYSLDNQLRLNVTETNNNFFSRHLTFSLENPDGKTTDVISAKLTALPFFITAESKLSDQLVHQLNKNLNITIDKNTINSKFSPMGDYLQSYVLTGFRDFTNKSQNLAVTLNFNAENKDVNIKTDLSGFNYDKNSKLEQINGQFHFVPVGDNQYDISSIELNIKNAELNLMNGENTKIQLKSAKYQFDIKKNEEAQQRDLTTKFSSDILRVANKERPTEESQTTINGLSLNLTQQGVKSAVDFADEFKKLTNDNQGIKNAVNFLVAVLTQNEELKGSLTVKSVEAPKNQKPYFNLNDTTFSLKMDNRHLDNADINLQLNVGNVKQTPEDQNKQWQAKGAKIIYHLENYNLENELAFIPFYLDSFTVKTPPKEDNKVLLKLKEKWAKESGGNSNAEIALQSFNYGNVVSGNLSVKSQSMEENHQYRGASTLSMQKLALPEAQIQIEDLAVSLPLTVNNYPKLAEAQFCSGLAAPLCSAYFTSETIEKYIENQWKGLDLSIDNSTITLNLNTYPGTKAYPLKLDINGAIKSQQDNQTPLDTLDQNLRGSLSITLNKGLIDDTNEQSLKIKNDSPFWQQLQMEIKPEDTLSPLFLEDKDNYVIKLEKTDKGTFINGKTEEEIRQEILKQTEEVEPQEEAEEVKPQVEIPPQSEGEKQEAVQPNQIEKPNN","483910","","conserved hypothetical protein","Outer membrane, Periplasm, Extracellular","","
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide
tmhmm\"[9-27]?transmembrane_regions


","No hits to the COGs database.","","Residues 3 to 105 match (8e-32) PD:PD249225 which is described as AMINOPEPTIDASE B PROTEOME COMPLETE PEPTIDASE HYDROLASE 3.4.11.- MANGANESE 3.-.-.- LEUCYL ","","","","","","","","","","","","Tue Dec 17 08:18:27 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00702 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00705","484764","483967","798","ATGAATCCAATGTTAAATATCGCGATTCGTGCAGCACGAAAAGCGGGCAATATTATTGCGAAAAACTATGAGCGTCGTGACGATATCGAAACGATGGAAAAAAGTAAAAATGATTATGTGACGAATGTTGATAAAGCGTCTGAAGCAGCGATTATCGAAGTCATCAAAAAATCCTATCCGGAACATACCATCATTACCGAGGAAAGTGGTGCACTGGAAGGGAGCGATAATGACGTGCAATGGGTGATTGATCCGCTGGATGGCACCACCAATTTCGTGAAAGGCTTACCGCATTTTGCCGTTTCTATTGCCATTCGTGTTAAAGGCCGCACCGAAGTGGGCGTGGTTTATGATCCAATCCTTAACGAACTTTTCACTGCCGTGCGTGGCGAAGGCGCAAAATTAAACGAATTACGTTTACGCGTTGAAAACAAACGCGATTTAAACGGCGCTATTTTAGCCACCGGTTTTCCGTTCAAACAAACCAAATATATGTCGATGCAATTCAACATGATGCAAAGCCTGATTGCCGACGTGGCGGATTTCCGTCGTGCAGGCTCCGCTGCGTTGGATCTTTGCTATGTTGCGGCAGGTCGCGTCGATGGCTATTTTGAGTACGGTATCAAAGCTTGGGATGTGGCGGCAGGCGATTTAATCGTGCGTGAAGCGGGCGGCATCGTCACCGACTACAACGCCGGTCATGCCTATTTGAAATGCGGCCATATCGTGGCAGCCGCTCCGCGGGTTTTAAAAGAAATCCTCGGCAAAATCCAACCTGCTGTTGCCGACGACTTAAAA","","","29541","MNPMLNIAIRAARKAGNIIAKNYERRDDIETMEKSKNDYVTNVDKASEAAIIEVIKKSYPEHTIITEESGALEGSDNDVQWVIDPLDGTTNFVKGLPHFAVSIAIRVKGRTEVGVVYDPILNELFTAVRGEGAKLNELRLRVENKRDLNGAILATGFPFKQTKYMSMQFNMMQSLIADVADFRRAGSAALDLCYVAAGRVDGYFEYGIKAWDVAAGDLIVREAGGIVTDYNAGHAYLKCGHIVAAAPRVLKEILGKIQPAVADDLK","483969","","Inositol-1-monophosphatase (IMPase); extragenic suppressor","Cytoplasm","","
InterPro
IPR000760
Family
Inositol monophosphatase
PD023420\"[40-96]TSUHB_PASMU_Q9CNV8;
PR00378\"[56-72]T\"[76-95]T\"[190-205]T\"[207-225]TINOSPHPHTASE
PTHR20854\"[60-261]TINOSITOL MONOPHOSPHATASE
PF00459\"[1-263]TInositol_P
PS00629\"[81-94]TIMP_1
PS00630\"[211-225]TIMP_2
noIPR
unintegrated
unintegrated
G3DSA:3.30.540.10\"[1-147]Tno description
G3DSA:3.40.190.80\"[154-259]Tno description
PTHR20854:SF4\"[60-261]TMYO INOSITOL MONOPHOSPHATASE


","No hits to the COGs database.","Significant hit ( 2.8e-39) to 3/3 blocks of the IPB000760 family, which is described as \"Inositol monophosphatase\". Interpro entry for IP:IPR000760. IPB000760A 38-68 2.1e-14 IPB000760B 81-92 2.4e-08 IPB000760C 211-229 1.5e-13","Residues 216 to 265 match (2e-07) PD:PD476790 which is described as PROTEOME COMPLETE PHOSPHATASE HYDROLASE INOSITOL-1-MONOPHOSPHATASE I-1-PASE IMPASE INOSITOL-1- MAGNESIUM SUHB ","","","","","","","","","","","","Tue Feb 4 16:29:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00705 is paralogously related to AA02793 (8e-36) and AA01166 (2e-16).","","","","","","Residues 1 to 263 (E-value = 4.8e-113) place AA00705 in the Inositol_P family which is described as Inositol monophosphatase family (PF00459)","","","","","Yano,R., Nagai,H., Shiba,K. and Yura,T., A mutation that enhances synthesis of sigma 32 andsuppresses temperature-sensitive growth of the rpoH15 mutantof Escherichia coli, J. Bacteriol. 172 (4), 2124-2130 (1990) PubMed: 2138605Nigou J, Dover LG, Besra GS.Purification and biochemical characterization of Mycobacterium tuberculosis SuhB, an inositol monophosphatase involved in inositol biosynthesis.Biochemistry. 2002 Apr 2;41(13):4392-8.PMID: 1191408Chen L, Roberts MF.Overexpression, purification, and analysis of complementation behavior of E. coli SuhB protein: comparison with bacterial andarchaeal inositol monophosphatases.Biochemistry. 2000 Apr 11;39(14):4145-53.PMID: 10747806 ","","Tue Feb 4 16:35:31 2003","1","","","" "AA00706","484852","485652","801","TTGACTAAAAATAAAGGGTATTATGTTAGAATAGCTAATATATTAAATCATGTAGTAAAAATAATGTTAAAAAATATTCGGATTGTTTTAATTGAAACCTCACACAGCGGCAACATCGGTTCTGCTGCACGGGCAATGAAGACAATGGGATTAACGGATTTAGTGTTGGTCGCGCCGAAACAAAGCGAGGATGATCAGGCTATCGCCCTTGCCGCCGGTGCGGAAGATGTGGTGAAAAGTGCGGTCACAGCGGAAAGCTTTTCACAAGCGGTCGCCGATTGCTCTTTAGTCATCGGTACCAGCGCAAGATTGCGCCATTTGCAGAATTCGCTTATTGAACCGCGTGAGTGCGGCAAAAAAGCCGTTGCTTACGCAACAAACGGGAAAGTCGCCATTGTGTTCGGGCGCGAACGCGTCGGCTTAACTAATGAAGAATTACTCAAATGCCACTATCATGTGACTATTCCCGCTAATCCCGATTATACCTCACTTAATCTTGCCATGGCGGTGCAATTAATCGCTTATGAAGTCAGAATGGCATATTTGACTCAAACGATTGCATCACCTTCCCAAAATATCCGCAATAACGCGAATATTTACCCGCAGATGGAGGAATTAGAATATTTTTTTAGCCATACGGAGCAGCTTTATCGTTCTGTTGGGTTCATTCAGAATCAGGGCGTTATGCAAAGGCTAAGACGTTTATACAACCGTGCAGGGATAGAAAAAACAGAATTAAACATTCTGCTTGGTATGTTAAGTGCGGTAGAAAAAAACTTAAATCTTGACAGGGATAATAGT","","","29711","LTKNKGYYVRIANILNHVVKIMLKNIRIVLIETSHSGNIGSAARAMKTMGLTDLVLVAPKQSEDDQAIALAAGAEDVVKSAVTAESFSQAVADCSLVIGTSARLRHLQNSLIEPRECGKKAVAYATNGKVAIVFGRERVGLTNEELLKCHYHVTIPANPDYTSLNLAMAVQLIAYEVRMAYLTQTIASPSQNIRNNANIYPQMEELEYFFSHTEQLYRSVGFIQNQGVMQRLRRLYNRAGIEKTELNILLGMLSAVEKNLNLDRDNS","485654","","tRNA/rRNA methyltransferase","Cytoplasm","","
InterPro
IPR001537
Domain
tRNA/rRNA methyltransferase, SpoU
PD001243\"[28-177]TQ8CXU2_LEPIN_Q8CXU2;
PF00588\"[25-175]TSpoU_methylase
InterPro
IPR004384
Family
RNA methyltransferase TrmH, group 1
TIGR00050\"[22-261]TrRNA_methyl_1: RNA methyltransferase, TrmH
noIPR
unintegrated
unintegrated
G3DSA:3.40.1280.10\"[4-181]Tno description


","No hits to the COGs database.","Significant hit ( 2.8e-16) to 3/3 blocks of the IPB001537 family, which is described as \"tRNA/rRNA methyltransferase (SpoU)\". Interpro entry for IP:IPR001537. IPB001537A 28-52 4.5e-07 IPB001537B 132-140 0.33 IPB001537C 163-176 0.00021","Residues 210 to 260 match (9e-13) PD:PD021826 which is described as PROTEOME COMPLETE METHYLTRANSFERASE TRNA/RRNA PM0316 HI0380 2.1.1.- TRANSFERASE ","","","","","","","","","","","","Tue Dec 17 08:31:30 2002","","Wed Apr 13 08:46:38 2005","Wed Apr 13 08:46:38 2005","Wed Apr 13 08:46:38 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA00706 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Apr 13 08:46:38 2005","","","","","Residues 25 to 175 (E-value = 3.4e-39) place AA00706 in the SpoU_methylase family which is described as SpoU rRNA Methylase family (PF00588)","Wed Apr 13 08:46:38 2005","","","","Anantharaman V, Koonin EV, Aravind L.SPOUT: a class of methyltransferases that includes spoU and trmD RNA methylase superfamilies, and novel superfamilies of predicted prokaryotic RNA methylases.J Mol Microbiol Biotechnol. 2002 Jan;4(1):71-5.PMID: 11763972Persson BC, Jager G, Gustafsson C.The spoU gene of Escherichia coli, the fourth gene of the spoT operon, is essential for tRNA (Gm18) 2'-O-methyltransferase activity.Nucleic Acids Res. 1997 Oct 15;25(20):4093-7.PMID: 9321663Koonin EV, Rudd KE.SpoU protein of Escherichia coli belongs to a new family of putative rRNA methylases.Nucleic Acids Res. 1993 Nov 25;21(23):5519. No abstract available.PMID: 8265370 ","","Wed Apr 13 08:46:38 2005","1","","","" "AA00707","485717","486187","471","ATGAAATTAACTTCCAAAGGTCGTTATGCGGTAACCGCAATTTTAGACATTGCTCTTTATGCCAATGATGGTCCTGTGAGCTTGTCTGATATTTCCGAACGACAACATATTTCTTTATCTTACTTAGAACAATTGTTTGCCAAACTGCGTCGGCACAATGTGGTGAAAAGCGTGCGCGGACCGGGCGGCGGTTACAAATTGGGCTTTGCACCAAGTGAGATTTCCATTGCGATGATTATTACTGCCGTCAACGAAAATATTGAAACGACAGCTTGCCTTGGACATGGCAACTGTAGCAACGGTTCCGAATGCCTAACCCATTCCTTATGGGAAAAATTGAGTCAACGCATTGAAGATTTCTTAAGTGAAATTACCTTGGAAGAATTAGTACTCCAACAAAAAGGCAGACAACAGGGCGTTGCCTCCCCTAATAAAAATCAGAATTTTGAAAATTTAGTCGTGGTAAACGGC","","","17186","MKLTSKGRYAVTAILDIALYANDGPVSLSDISERQHISLSYLEQLFAKLRRHNVVKSVRGPGGGYKLGFAPSEISIAMIITAVNENIETTACLGHGNCSNGSECLTHSLWEKLSQRIEDFLSEITLEELVLQQKGRQQGVASPNKNQNFENLVVVNG","486189","","conserved hypothetical protein","Cytoplasm, Outer membrane","","
InterPro
IPR000944
Family
Transcriptional regulator, Rrf2
PD003632\"[1-58]TQ9CNV6_PASMU_Q9CNV6;
PF02082\"[1-121]TRrf2
TIGR00738\"[1-131]Trrf2_super: rrf2 family protein (putative t
PS51197\"[2-131]THTH_RRF2_2


","BeTs to 14 clades of COG1959COG name: Predicted transcriptional regulatorFunctional Class: KThe phylogenetic pattern of COG1959 is -------qvdrlbcefghsnujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 2.2e-26) to 1/1 blocks of the IPB000944 family, which is described as \"Uncharacterized protein family UPF0074\". Interpro entry for IP:IPR000944. IPB000944 14-67 2e-26","Residues 1 to 60 match (7e-11) PD:PD415410 which is described as PROTEOME COMPLETE RRF2 YRZC SLR0846 PLASMID LIN1550 ATU0819 R00571 ATU3423 ","","","","","","","","","","","","Tue Dec 17 08:33:12 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00707 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 121 (E-value = 7.8e-58) place AA00707 in the Rrf2 family which is described as Transcriptional regulator (PF02082)","","","","","","","","1","","","" "AA00708","486244","487455","1212","ATGAAACTACCCATTTATTTAGATTATGCGGCAACCTGTCCGGTAGATGAACGTGTAGCAAAAAAAATGATGGAATATTTAACCATCAACGGTGTTTTCGGTAACCCTGCTTCCCGTTCGCACAAATTCGGCTGGCAAGCGGAAGAAGCGGTCGACGTTGCCCGTAATCAAATTGCCGATTTAATCGGTGCCGATTCCCGTGAAATCGTGTTTACCTCCGGAGCAACGGAATCCGACAACCTCGCCATTAAAGGCGCTGCGCATTTTTATCAAACCAAAGGTAAGCACATTATCACTTGCAAAACCGAGCATAAAGCAGTGCTCGATACCTGCCGTCAATTGGAGCGCGAAGGCTTTGAAGTCACTTACTTGGAACCGGAATCCGACGGTTTAATCGATTTGGAAAAATTCAAAGCGGCATTACGCCCGGACACCATTTTAGCTTCAATCATGCACGTCAATAACGAAATCGGCGTGATTCAAGACATCAAGGCTATCGGTGAACTGTGCCGCGCCAACAAAACTATTTTCCATGTAGATGCAACCCAAAGCGTTGGCAAAGTGGAAATTAATCTTGCCGAATTGCCGGTGGATTTAATGTCCATGTCCGGCCACAAATTATACGGACCAAAAGGCATCGGCGCCTTATATGTGCGTCGGAAACCACGCATTCGTTTAGAAGCCATTATTCACGGCGGCGGACACGAACGCGGTATGCGTTCCGGTACCTTACCGGTACACCAAATCGTCGGCATGGGCGAAGCTTATCGGATTGCTAAAGAAGAAATGGCAACGGAAATTCCTCGCATTAAAGCCCTTCGCGATCGCCTGTACAACGGCTTAAAAAACATCGAAGAAACCTATGTGAACGGTTCTATGGAACACCGCGTCGCCAATAACCTGAACATCAGTTTCAACTATGTAGAAGGTGAATCATTAATAATGGCGTTGCGTGACATCGCGGTTTCCTCCGGTTCCGCTTGTACTTCCGCCAGCCTGGAGCCGTCTTATATCCTACGTGCATTAGGTCGTAACGACGAATTAGCACACAGTTCTATTCGTTTCACCTTAGGTCGTTTCACCACGGAAGAAGAAATCGACTATACCGTAAGCCTGATGAAAGGTGCGGTAGAAAAATTGCGTGAATTATCCCCGCTTTGGGATATGTTCAAAGAAGGCATTGATTTAAACACCATTGAGTGGTCAGCCCAC","","","44957","MKLPIYLDYAATCPVDERVAKKMMEYLTINGVFGNPASRSHKFGWQAEEAVDVARNQIADLIGADSREIVFTSGATESDNLAIKGAAHFYQTKGKHIITCKTEHKAVLDTCRQLEREGFEVTYLEPESDGLIDLEKFKAALRPDTILASIMHVNNEIGVIQDIKAIGELCRANKTIFHVDATQSVGKVEINLAELPVDLMSMSGHKLYGPKGIGALYVRRKPRIRLEAIIHGGGHERGMRSGTLPVHQIVGMGEAYRIAKEEMATEIPRIKALRDRLYNGLKNIEETYVNGSMEHRVANNLNISFNYVEGESLIMALRDIAVSSGSACTSASLEPSYILRALGRNDELAHSSIRFTLGRFTTEEEIDYTVSLMKGAVEKLRELSPLWDMFKEGIDLNTIEWSAH","487457","From GenBank (gi:13432196):This protein catalyzes the removal of elemental sulfur from cysteine to produce alanine, and belongs to the class-V of pyrodixal-phosphate-dependent aminotransferases (NifS/IscS)` subfamily). Pyridoxal phosphatase is a cofactor. nifS is a gene name that matches to cysteine desulfurase frequently in the TIGR database. ","cysteine desulfurase","Cytoplasm","","
InterPro
IPR000192
Family
Aminotransferase, class V
PF00266\"[5-369]TAminotran_5
PS00595\"[197-216]TAA_TRANSFER_CLASS_5
InterPro
IPR010240
Family
Cysteine desulfurase IscS
TIGR02006\"[1-404]TIscS: cysteine desulfurase IscS
InterPro
IPR015421
Domain
Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10\"[5-262]Tno description
noIPR
unintegrated
unintegrated
PTHR11601\"[4-404]TCYSTEINE DESULFURYLASE


","No hits to the COGs database.","Significant hit ( 1.2e-08) to 2/2 blocks of the IPB000192 family, which is described as \"Aminotransferase class-V\". Interpro entry for IP:IPR000192. IPB000192A 5-13 0.022 IPB000192B 205-214 0.00022","Residues 362 to 404 match (3e-07) PD:PD483314 which is described as PHOSPHATE MITOCHONDRIAL MITOCHONDRION DESULFURASE CYSTEINE 4.4.1.- PEPTIDE TRANSIT PRECURSOR LYASE ","","","","","","","","","","","Tue Jan 14 14:13:05 2003","Tue Jan 14 14:05:30 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00708 is paralogously related to AA02579 (2e-21).","","","","","","Residues 15 to 369 (E-value = 4.7e-123) place AA00708 in the Aminotran_5 family which is described as Aminotransferase class-V (PF00266)","","","","","Frazzon J, Fick JR, Dean DR. Biosynthesis of iron-sulphur clusters is a complex andhighly conserved process. Biochem Soc Trans. 2002;30(4):680-5. PMID: 12196163Kambampati,R. and Lauhon,C.T.IscS is a sulfurtransferase for the in vitro biosynthesis of4-thiouridine in Escherichia coli tRNABiochemistry 38 (50), 16561-16568 (1999)PubMed: 10600118","","Tue Dec 17 08:39:12 2002","1","","","" "AA00709","487518","487898","381","ATGACATACAGTAACAAAGTTATCGATCATTACGAAAACCCACGCAACGTCGGTTCAATGGATAGAAAAGACAGCGCCGTCGGCACCGGCATGGTCGGTGCACCGGCCTGTGGTGACGTTATGCAGTTACAAATCCGCGTCAACGACGACGGCATTATTGAAGATGCGAAATTCAAAACCTACGGCTGTGGTTCCGCCATCGCATCCAGCTCCTTAATCACCGAATGGGTGAAAGGCAAATCCCTGGAAGAAGCGGGTGCGATCAAAAACAGCCAAATTGCCGAAGAACTTGAATTACCGCCGGTAAAAGTTCACTGCTCTATTTTGGCAGAAGACGCCATTAAAGCGGCGATTGCCGATTACAAAGCGAAAAAAGGTTCT","","","13516","MTYSNKVIDHYENPRNVGSMDRKDSAVGTGMVGAPACGDVMQLQIRVNDDGIIEDAKFKTYGCGSAIASSSLITEWVKGKSLEEAGAIKNSQIAEELELPPVKVHCSILAEDAIKAAIADYKAKKGS","487900","","metallocluster assembly (NifU protein)","Periplasm, Cytoplasm","","
InterPro
IPR002871
Domain
Nitrogen-fixing NifU-like, N-terminal
PF01592\"[2-127]TNifU_N
InterPro
IPR011339
Family
FeS cluster assembly scaffold IscU
TIGR01999\"[3-126]TiscU: FeS cluster assembly scaffold IscU
noIPR
unintegrated
unintegrated
G3DSA:3.90.1010.10\"[1-125]Tno description
PTHR10093\"[1-126]TIRON-SULFUR CLUSTER ASSEMBLY ENZYME (NIFU HOMOLOG)


","BeTs to 17 clades of COG0822COG name: NifU homologs involved in Fe-S cluster formationFunctional Class: CThe phylogenetic pattern of COG0822 is ao----yqv-rlb-efgh-nujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-65) to 4/4 blocks of the IPB002871 family, which is described as \"NifU-like N terminal domain\". Interpro entry for IP:IPR002871. IPB002871A 3-18 2.9e-11 IPB002871B 30-42 1.1e-07 IPB002871C 49-81 1.4e-27 IPB002871D 99-121 5.4e-15","Residues 4 to 93 match (6e-07) PD:PD388030 which is described as NITROGEN FIXATION NIFU ","","","","","","","","","","","","Tue Dec 17 08:44:53 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00709 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 127 (E-value = 7.6e-77) place AA00709 in the NifU_N family which is described as NifU-like N terminal domain (PF01592)","","","","","Kato S, Mihara H, Kurihara T, Yoshimura T, Esaki N. Gene cloning, purification, and characterization of twocyanobacterial NifS homologs driving iron-sulfur clusterformation. Biosci Biotechnol Biochem. 2000 Nov;64(11):2412-9. PMID: 11193410 Olson JW, Agar JN, Johnson MK, Maier RJ. Characterization of the NifU and NifS Fe-S clusterformation proteins essential for viability in Helicobacterpylori. Biochemistry. 2000 Dec 26;39(51):16213-9. PMID: 11123951","","Tue Dec 17 08:44:53 2002","1","","","" "AA00711","488033","488353","321","ATGTCTATCACTCTCACCGAAAGCGCGGCAGATCGCGTGAAAACATTTTTAGCAAAACGCGGAAAAGGTATCGGCTTGCGCTTAGGCGTCAAAACCTCAGGTTGTTCCGGTTTGTCTTATATGCTGGAATTTGTGGATGCGTTAAACGAAGACGATCAGGTGTTTGAGCAACACGGCGTGAAAGTCATCGTCGATACCAAAAGTTTAGTGTATTTAGACGGCACCCAATTGGATTTCACCAAAGAAGGCTTAAACGAAGGTTTTAAATTCGCTAATCCGAACGTGAAAGACGAATGCGGTTGCGGTGAAAGCTTTAACGTA","","","11627","MSITLTESAADRVKTFLAKRGKGIGLRLGVKTSGCSGLSYMLEFVDALNEDDQVFEQHGVKVIVDTKSLVYLDGTQLDFTKEGLNEGFKFANPNVKDECGCGESFNV","488355","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR000361
Family
HesB/YadR/YfhF
PD002183\"[26-90]TQ9CNV4_PASMU_Q9CNV4;
PTHR10072\"[3-107]THES-B
PF01521\"[3-93]TFe-S_biosyn
TIGR00049\"[3-107]TTIGR00049: iron-sulfur cluster assembly acc
PS01152\"[88-105]THESB
InterPro
IPR011302
Family
Iron-sulphur cluster assembly protein IscA
TIGR02011\"[3-107]TIscA: iron-sulfur cluster assembly protein
noIPR
unintegrated
unintegrated
G3DSA:2.60.300.12\"[3-93]Tno description
PTHR10072:SF27\"[3-107]THES-B


","BeTs to 13 clades of COG0316COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG0316 is ------yq-dr-bcefghsn-jx---Number of proteins in this genome belonging to this COG is","Significant hit ( 1.8e-29) to 2/2 blocks of the IPB000361 family, which is described as \"Hypothetical hesB/yadR/yfhF family\". Interpro entry for IP:IPR000361. IPB000361A 26-46 2.6e-10 IPB000361B 74-105 1e-17","Residues 1 to 107 match (2e-08) PD:PD070482 which is described as ROX1-SPE3 ","","","","","","","","","","","Wed Jan 22 16:47:35 2003","Tue Jan 14 14:02:41 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00711 is paralogously related to AA02430 (3e-17) and AA01221 (2e-04).","","","","","","Residues 2 to 106 (E-value = 5e-60) place AA00711 in the HesB family which is described as HesB-like domain (PF01521)","","","","","","","","1","","","" "AA00712","488368","488886","519","ATGAACAATCCCTTTGCTTTATTTGATTTGCCCGTTGCGTTTCAAGTGGATGCGGCGTTATTAAACGAACGTTATCTGGCGCTGCAAAAATCCCTACATCCGGATAATTTCTCCGCGGCTTCCGCACAGGAACAGCGCCTCGCTATTCAAAAATCGGCGGAAATTAATGATGCCCTGCGCATTTTAAAAGATCCCATCGCACGCGCCGACAGCATTATCGACATCAACACCGGCGAAACGGAAAACGTAGAAGAAAAAAGCACCAATGATATTGCCTTTTTGATGCAGCAAATGGAATGGCGGGAAACCCTGGAAAATATCGAACAGCAAAAAAATGCCAACGAATTAACCGCTTTCAGCCAAGAAATTCAGCAAACCCGCAGCGCCATTTTAACGGAATTATCCACCGCACTTAACGAACAACAATGGCAAACGGCGCGGGCGATTACGGATAAATTACGTTTTATCAAAAAACTCCAAGCCGAAATTGAACGGGTTGAAGAAAATCTATTTGATTTA","","","19791","MNNPFALFDLPVAFQVDAALLNERYLALQKSLHPDNFSAASAQEQRLAIQKSAEINDALRILKDPIARADSIIDINTGETENVEEKSTNDIAFLMQQMEWRETLENIEQQKNANELTAFSQEIQQTRSAILTELSTALNEQQWQTARAITDKLRFIKKLQAEIERVEENLFDL","488888","","chaperone protein hscB, heat shock cognate","Cytoplasm","","
InterPro
IPR001623
Domain
Heat shock protein DnaJ, N-terminal
PF00226\"[3-72]TDnaJ
SM00271\"[2-67]TDnaJ
InterPro
IPR004640
Family
Co-chaperone Hsc20
TIGR00714\"[14-171]ThscB: Fe-S protein assembly co-chaperone Hs
InterPro
IPR012895
Domain
HSCB oligomerisation, C-terminal
PF07743\"[88-165]THSCB_C
noIPR
unintegrated
unintegrated
G3DSA:1.10.287.110\"[2-80]Tno description
G3DSA:1.20.1280.20\"[82-173]Tno description


","BeTs to 7 clades of COG1076COG name: DnaJ-domain-containing proteins 1Functional Class: OThe phylogenetic pattern of COG1076 is ------y------cefgh-nujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 3.2e-05) to 2/2 blocks of the IPB001623 family, which is described as \"DnaJ N-terminal domain\". Interpro entry for IP:IPR001623. IPB001623A 21-35 0.097 IPB001623B 51-72 0.18","Residues 84 to 172 match (4e-18) PD:PD262001 which is described as PROTEOME COMPLETE CHAPERONE HSCB HEAT SHOCK BE ASSEMBLY FE-S HSC20 ","","","","","","","","","","","","Tue Dec 17 08:49:43 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00712 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 75 (E-value = 1e-05) place AA00712 in the DnaJ family which is described as DnaJ domain (PF00226)","","","","","ickery,L.E., Silberg,J.J. and Ta,D.T. Hsc66 and Hsc20, a new heat shock cognate molecularchaperone system from Escherichia coli Protein science : a publication of the Protein Society. 6 (5), 1047-1056 (1997) PubMed: 9144776 Cupp-Vickery,J.R. and Vickery,L.E. Crystal structure of Hsc20, a J-type Co-chaperone fromEscherichia coli Journal of molecular biology. 304 (5), 835-845 (2000) PubMed: 11124030 ","","Tue Dec 17 08:49:43 2002","1","","","" "AA00713","488910","490757","1848","ATGGCATTACTTCAAATTGCAGAGCCCGGTCAAAGCGCCGCACCGCATCAACATAAACTGGCGGTAGGCATTGATCTCGGCACCACCAATTCCCTCATTGCCTCCGTGCGCAATGGCCACAGCGAAATTTTACTCGACGGGCAAGATCGCCCGTTGTTGCCGTCCGTGGTGCATTTTGGCGGCGATGACAAGATTATCGTGGGCTATGAAGCTGCTGAACTTGCGGTGCATGATCCGCAAAATACCGTAATTTCCGTCAAACGTTTAATTGGTCGCAGCCTGGCAGATATTCAACAACGCTACCCTAATTTACCTTATCAATTTGTTGCCAGCGAAAACGGCTTGCCTTTACTGCAAACCACACAAGGCGCCCGCAGCCCCATTGAAATTTCTGCAGAAATACTGAAAAAACTGACCGCACTTGGTGAGCAGCGCTTGGGCGGAAGCCTCGTGGGCGCGGTGATTACCGTCCCCGCCTATTTTGACGACGCACAACGCCAAAGCACCAAAGACGCGGCAAAACTCGCCGGATTAAATGTACTACGTTTACTCAACGAACCCACCGCTGCCGCCATCGCTTACGGTTTGGATAGCGGACAAGAAGGCGTCATTGCGGTGTATGATTTGGGTGGCGGCACATTTGATATTTCAATTTTACGCCTTTCCCGTGGCGTGTTTGAAGTGTTAGCAACCGGCGGCGACACGGCGCTGGGCGGCGACGATTTCGATTTATTATTGGCGAATTGGATTATCGAACAATCCGCGATGAAACCGGAAAACGACAGCCAATACCGCGAACTCATTGAATTAGCCAATCAACTTAAATTAACCCTCAGCCACGAAACGGAAACACAGATCCATTACCGCAATTGGTTGGGCAACATCACCCGCGAACAATTTAACGAACTGATTCAGCCTTTAGTCAAACGTTCGCTGTTAGCTTGCCGTCGCGCCTTAAAAGACGCCGGCGTAGAAGCGGACGAAGTAGTCATGGTGGGTGGCTCCACCCGCGTGCCTTACGTGCGTGAACAAGTGGGTAAGTTTTTCCAAAAACAACCGCTAACTTCCATTGACCCCGACAAAGTAGTGGCATTAGGCGCGGCGATTCAAGCGGATATTCTTGCCGGTAACAAACCGGATTCTGATTTGTTGTTATTGGATGTGATTCCGCTGTCCCTCGGCATTGAGACCATGGGCGGCTTGGTGGAAAAAATCATTCCGCGCAACACCACCATTCCGGTGGCGCGCGCGCAGGAATTTACCACCTTTAAAGACGGGCAAACAGCCATGTCCGTGCATATCGTACAAGGGGAACGGGAAATGGTTACCGACTGTCGCTCCCTTGCCCGTTTCACCCTGCGCGGCATTCCACCAATGGCAGCCGGCGCAGCGCATATTCGCGTGACTTATCAGGTAGATGCGGACGGTTTATTAAGCGTCACTGCCATGGAAAAAACCACCGGCGTGCAATCGTCCATTCAGGTAAAACCGTCTTACGGTTTAACGGACGATGAAATCGCCAATATGTTGAAGGCCTCCATGGAAAATGCCAAAGAGGACATTCAAGCGCGCTTATTGGCGGAACAACGGGTGGAAGCAGAGCGCGTACTGGAAAGCGTGCGTTCGGCACTGGCGCAAGATTATGATTTATTAGATGACGACGAATTAAGTGCGGTCAAAAATACGATTATTTCGTTGGAACAGTTAAAACAACAAGAAGATTACATTGCTATCAAGCAAGGAATCAAAGCATTAGATCTGGCAACGCAGGACTTTGCCGCACGCCGTATGGATAAATCTATTCGCGCCGCGCTGGCAGGTCAATCCGTTGAAGATATTGTAGGAAAA","","","66742","MALLQIAEPGQSAAPHQHKLAVGIDLGTTNSLIASVRNGHSEILLDGQDRPLLPSVVHFGGDDKIIVGYEAAELAVHDPQNTVISVKRLIGRSLADIQQRYPNLPYQFVASENGLPLLQTTQGARSPIEISAEILKKLTALGEQRLGGSLVGAVITVPAYFDDAQRQSTKDAAKLAGLNVLRLLNEPTAAAIAYGLDSGQEGVIAVYDLGGGTFDISILRLSRGVFEVLATGGDTALGGDDFDLLLANWIIEQSAMKPENDSQYRELIELANQLKLTLSHETETQIHYRNWLGNITREQFNELIQPLVKRSLLACRRALKDAGVEADEVVMVGGSTRVPYVREQVGKFFQKQPLTSIDPDKVVALGAAIQADILAGNKPDSDLLLLDVIPLSLGIETMGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMSVHIVQGEREMVTDCRSLARFTLRGIPPMAAGAAHIRVTYQVDADGLLSVTAMEKTTGVQSSIQVKPSYGLTDDEIANMLKASMENAKEDIQARLLAEQRVEAERVLESVRSALAQDYDLLDDDELSAVKNTIISLEQLKQQEDYIAIKQGIKALDLATQDFAARRMDKSIRAALAGQSVEDIVGK","490759","","chaperone protein hscA, heat shock cognate 66","Cytoplasm","","
InterPro
IPR001023
Family
Heat shock protein Hsp70
PR00301\"[20-33]T\"[48-60]T\"[153-173]T\"[212-222]T\"[326-342]T\"[357-377]T\"[382-401]T\"[463-479]THEATSHOCK70
PTHR19375\"[21-518]THEAT SHOCK PROTEIN 70KDA
InterPro
IPR010236
Family
Fe-S protein assembly chaperone HscA
TIGR01991\"[2-613]THscA: Fe-S protein assembly chaperone HscA
InterPro
IPR013126
Family
Heat shock protein 70
PD000089\"[86-177]THSCA_PASMU_Q9CNV2;
PF00012\"[21-598]THSP70
PS00297\"[24-31]THSP70_1
PS00329\"[206-219]THSP70_2
PS01036\"[329-343]THSP70_3
noIPR
unintegrated
unintegrated
G3DSA:2.60.34.10\"[365-555]Tno description
G3DSA:3.30.420.40\"[16-224]Tno description
G3DSA:3.90.640.10\"[238-310]Tno description
PTHR19375:SF1\"[21-518]THEAT SHOCK PROTEIN 70 (HSP70)


","BeTs to 22 clades of COG0443COG name: Molecular chaperoneFunctional Class: OThe phylogenetic pattern of COG0443 is -omp--yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit (2.4e-126) to 6/6 blocks of the IPB001023 family, which is described as \"Heat shock protein hsp70\". Interpro entry for IP:IPR001023. IPB001023A 22-54 7.9e-09 IPB001023B 137-190 1.2e-32 IPB001023C 204-239 1e-20 IPB001023D 311-350 2.5e-08 IPB001023E 382-430 7.9e-29 IPB001023F 448-495 8.4e-21Significant hit ( 7e-10) to 2/3 blocks of the IPB002821 family, which is described as \"Hydantoinase/oxoprolinase\". Interpro entry for IP:IPR002821. IPB002821A 20-33 1 IPB002821C 147-196 2.3e-07","Residues 1 to 97 match (2e-07) PD:PD597597 which is described as COMPLETE PROTEOME HSCA CHAPERONE HEAT ATP-BINDING HOMOLOG SHOCK ","","","","","","","","","","","","Tue Dec 17 08:50:54 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00713 is paralogously related to AA00657 (1e-122) and AA01371 (1e-07).","","","","","","Residues 21 to 598 (E-value = 6.9e-249) place AA00713 in the HSP70 family which is described as Hsp70 protein (PF00012)","","","","","Uehara T, Matsuzawa H, Nishimura A. HscA is involved in the dynamics of FtsZ-ring formation inEscherichia coli K12. Genes Cells. 2001 Sep;6(9):803-14. PMID: 11554926 Campos-Garcia J, G Ordonez L, Soberon-Chavez G. The Pseudomonas aeruginosa hscA gene encodes Hsc66, a DnaKhomologue. Microbiology. 2000 Jun;146 ( Pt 6):1429-35. PMID: 10846221 Kawula,T.H. and Lelivelt,M.J. Mutations in a gene encoding a new Hsp70 suppress rapidDNA inversion and bgl activation, but not proU derepression,in hns-1 mutant Escherichia coli Journal of bacteriology. 176 (3), 610-619 (1994) PubMed: 8300516 Vickery,L.E., Silberg,J.J. and Ta,D.T. Hsc66 and Hsc20, a new heat shock cognate molecularchaperone system from Escherichia coli Protein science : a publication of the Protein Society. 6(5), 1047-1056 (1997) PubMed: 9144776 Lelivelt,M.J. and Kawula,T.H. Hsc66, an Hsp70 homolog in Escherichia coli, is induced bycold shock but not by heat shock J. Bacteriol. 177 (17), 4900-4907 (1995) PubMed: 7665466 ","","Tue Dec 17 08:50:54 2002","1","","","" "AA00715","490772","491110","339","ATGCCAAAAGTGATTTTTTTACCCAATGAAGAGTTTTGCCCGGAAGGCACGGTGGTTGATGCCGCCGCCGGTGACAATTTATTAGAGGTCGCCCATAACGCCGGCGTGGAAATTCACCACGCCTGTGACGGTTCCTGCGCCTGCACCACCTGCCACGTGGTGGTGCGCGAAGGCGGCGATTCATTAAATGAACCATGCGACCAGGAAGAAGATATGTTAGACAAAGCCTGGGGCTTGGAAATAGACAGCCGCTTGTCTTGCCAATGTATCATCGGTGATGAAGATTTAGTGGTGGAAATTCCGAAATATAACATCAACCACGCAAATGAGGCAGCGCAT","","","12824","MPKVIFLPNEEFCPEGTVVDAAAGDNLLEVAHNAGVEIHHACDGSCACTTCHVVVREGGDSLNEPCDQEEDMLDKAWGLEIDSRLSCQCIIGDEDLVVEIPKYNINHANEAAH","491112","","[2Fe-2S] ferredoxin","Cytoplasm, Periplasm","","
InterPro
IPR001041
Domain
Ferredoxin
PF00111\"[10-93]TFer2
PS51085\"[2-104]T2FE2S_FER_2
InterPro
IPR001055
Family
Adrenodoxin
PR00355\"[42-52]T\"[60-74]T\"[83-91]TADRENODOXIN
PS00814\"[42-52]TADX
InterPro
IPR011536
Family
Ferredoxin, 2Fe-2S type
TIGR02007\"[2-111]Tfdx_isc: ferredoxin, 2Fe-2S type, ISC syste
InterPro
IPR012675
Domain
Beta-grasp fold, ferredoxin-type
G3DSA:3.10.20.30\"[1-111]Tno description
noIPR
unintegrated
unintegrated
PTHR23426\"[19-106]TFERREDOXIN/ADRENODOXIN


","BeTs to 12 clades of COG0633COG name: FerredoxinFunctional Class: CThe phylogenetic pattern of COG0633 is ao----yq-dr--cefgh-n-jxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 3.4e-34) to 2/2 blocks of the IPB001055 family, which is described as \"Adrenodoxin\". Interpro entry for IP:IPR001055. IPB001055A 40-52 6.1e-10 IPB001055B 67-103 7.4e-23","Residues 41 to 94 match (3e-08) PD:PD596565 which is described as IRON-SULFUR FERREDOXIN COMPLETE PROTEOME ELECTRON ADRENODOXIN FERREDOXIN 2FE-2S MITOCHONDRIAL FDII ","","","","","","","","","","","","Tue Dec 17 08:53:09 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00715 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 10 to 93 (E-value = 2.6e-15) place AA00715 in the Fer2 family which is described as 2Fe-2S iron-sulfur cluster binding domain (PF00111)","","","","","Ta,D.T. and Vickery,L.E. Cloning, sequencing, and overexpression of a [2Fe-2S] ferredoxin gene from Escherichia coli J. Biol. Chem. 267 (16), 11120-11125 (1992) PubMed: 1317854 Knoell,H.E. and Knappe,J. Escherichia coli ferredoxin, an iron-sulfur protein of the adrenodoxin type Eur. J. Biochem. 50 (1), 245-252 (1974) PubMed: 4375562 Tokumoto U, Nomura S, Minami Y, Mihara H, Kato S, KuriharaT, Esaki N, Kanazawa H, Matsubara H, Takahashi Y. Network of Protein-Protein Interactions among Iron-Sulfur Cluster Assembly Proteins in Escherichia coli. J Biochem (Tokyo). 2002 May;131(5):713-9. PMID: 11983079 Kakuta Y, Horio T, Takahashi Y, Fukuyama K. Crystal structure of Escherichia coli Fdx, an adrenodoxin-type ferredoxin involved in the assembly of iron-sulfur clusters. Biochemistry. 2001 Sep 18;40(37):11007-12. PMID: 11551196 ","","Tue Dec 17 08:53:09 2002","1","","","" "AA00716","491113","491304","192","ATGAAATGGACTGACACGCAGCAAATTGCCGAAACCTTGTATGACAATAACCCGGACTTGGATCCAAAAACCGTGCGTTTTACCGATCTGCACCGCTGGATTTGTGAGCTGGACAATTTTGATGACGATCCGCAAAAATCTAACGAATCCATTTTAGAAGCCATTTTGCTGAAGTGGTTGGAAGAGTACGAG","","","7727","MKWTDTQQIAETLYDNNPDLDPKTVRFTDLHRWICELDNFDDDPQKSNESILEAILLKWLEEYE","491306","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR007479
Family
Protein of unknown function DUF528
PF04384\"[1-64]TDUF528
noIPR
unintegrated
unintegrated
PD014929\"[17-64]TYFHJ_HAEIN_P44668;
G3DSA:1.10.10.600\"[1-64]Tno description


","BeTs to 5 clades of COG2975COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG2975 is --------------efgh-n------Number of proteins in this genome belonging to this COG is","","Residues 1 to 64 match (2e-20) PD:PD014929 which is described as PROTEOME COMPLETE PA3808 BE ASSEMBLY FE-S VC0754 YPO2890 NMA1347 YFHJ ","","","","","","","","","","","","Tue Dec 17 08:57:52 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00716 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 64 (E-value = 1.2e-45) place AA00716 in the DUF528 family which is described as Protein of unknown function (DUF528) (PF04384)","","","","","","","","1","","","" "AA00717","493501","491444","2058","ATGTCGAATAATAAACGTAAAATCCTCGTGACTTGTGCCTTGCCTTATGCCAATGGTCCGATCCATTTAGGGCATATGCTGGAACATATTCAAGCGGATATTTGGGTGCGTTTTCAACGAATGCGCGGCAATGAAATTCACTTTGTTTGTGCCGATGACGCGCATGGCACGCCGATTATGTTAAAAGCCGATCAAATGGGCATCACGCCGGAACAATTGATTGATGATGTGCGCCAAAAACACATGGCGGATTTTGCCGGCTTTAACATCAGTTTTGATAACTACCACTCCACCCATAGCGAAGAAAATCGCGAACTTTCCGAATTAATTTACAACCGCTTGAAAGAAAACGGTTTTATTAAAAGCCGTACCATTTCTCAATTATATGATCCGGAAAAAGGGATGTTTTTGCCCGATCGTTTCGTAAAAGGCACTTGCCCGAAATGTAAATCGCCTGATCAATACGGCGATAACTGTGAAGTGTGCGCGGCAACTTACAGCCCGACGGAATTGATTAGTCCGCGTTCTGTGGTTTCCGGTGCGACGCCGGTGATGAAAGACTCCGAACATTTCTTCTTTGATTTGCCGAGTTTTGAAGCCATGTTGAAAAACTGGCTGGGTTCCGGTTCCTTGCAATCGGAAGTGGTGAATAAAATGCAGGAATGGTTTGAAGCGGGTCTGCAACAGTGGGACATTTCCCGTGACGCGCCGTATTTCGGCTTCCAAATTCCGAATGAGGAAGGCAAATATTTCTATGTGTGGCTGGATGCGCCGATTGGCTATATGGCGTCCTTCAAAAATCTGTGTAAACGCGAAAGCCACATTGATTTTGACGGTTTCTGGCGCAAAGACAGCGACGCGGAACTGTATCATTTCATCGGCAAAGACATTATGTATTTCCACAGCCTGTTCTGGCCGGCAATGCTGGAAGGTGCCGATTTCCGTAAACCGAGCAATATTTTCGTGCACGGCTATGTGACGGTGAACGGTGAGAAAATGTCGAAATCCCGTGGCACTTTCATTCAAGCGGCAACTTATTTGAAGTACTTGGATCCGGAATGTTTGCGCTATTACTACGCGGCGAAACTGAGCAATCGCATTGATGATTTGGATTTGAACTTAGAGGATTTCGTACAGCGCGTGAATACGGATTTGGTGAATAAACTTGTTAATTTGGCTTCCCGTAATGCCGGCTTTATTCAAAAACGTTTCGATGGAAAATTGGCAGCGAGTTTGGACGATCAAGCCTTATTTGATGAATTTATTGCTCAATCGGAACAGATCGCCGCTTATTATGAAAACCGCGAATTCGGCAAAGCCATTCGTGAAATCATGGCGTTAACGGACAAAGCCAATAAATACATTGATGACAAAGTCCCTTGGGTGATTGCCAAAGAAGCAGGCAAAGACGCGGAATTACAAGCGGTTTGCTCTATGGGCATTCAGTTATTCCGCGTGCTTATGGGCTATTTAAAACCGGTGTTGCCGAAACTTGCCGAACGGGCGGAAGCCTTCCTGCAATCTAAATTAACTTGGGCGAATTTGGCGCAACCATTGCTAAATCACCCAATCGCCCCGTTCAAAGCCTTGTTCTCCCGTTTGGACGGCAAACAAATTGAAGCCATGATCGAAGCGTCCAAAGCGGAAAATGCACAGGTCAATGCACCTGCCACGGCGAAAAGTGCGGTCAAAAATACCGGTGAATCTGCGGGCGGCATTGAGCCGATTGCGGAAACTATCACCATTGACGATTTTGCCAAATTGGATTTACGTGTGGCGAAAGTGTTGAAATGCGAAGCCGTGCCGGAATCCAATAAATTATTGCGTTTTGAATTGGATTTAGGCGATCACAAACGCCAAGTGTTCTCCGGTATTAAAGCGGCTTACGACAAACCGGAAGAATTAGAAGGGCGTTTTGTGATTATGGTGGCAAACCTGGCACCGCGCAAAATGAAATTTGGTGTATCCGAAGGCATGATTTTAAGTGCGGGAACGGGCGGTGCCGATTTATTCTTGTTGTCTGCCGACGAAGGCGTGACGGCGGGAATGCAGGTGAAG","","","77354","MSNNKRKILVTCALPYANGPIHLGHMLEHIQADIWVRFQRMRGNEIHFVCADDAHGTPIMLKADQMGITPEQLIDDVRQKHMADFAGFNISFDNYHSTHSEENRELSELIYNRLKENGFIKSRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCAATYSPTELISPRSVVSGATPVMKDSEHFFFDLPSFEAMLKNWLGSGSLQSEVVNKMQEWFEAGLQQWDISRDAPYFGFQIPNEEGKYFYVWLDAPIGYMASFKNLCKRESHIDFDGFWRKDSDAELYHFIGKDIMYFHSLFWPAMLEGADFRKPSNIFVHGYVTVNGEKMSKSRGTFIQAATYLKYLDPECLRYYYAAKLSNRIDDLDLNLEDFVQRVNTDLVNKLVNLASRNAGFIQKRFDGKLAASLDDQALFDEFIAQSEQIAAYYENREFGKAIREIMALTDKANKYIDDKVPWVIAKEAGKDAELQAVCSMGIQLFRVLMGYLKPVLPKLAERAEAFLQSKLTWANLAQPLLNHPIAPFKALFSRLDGKQIEAMIEASKAENAQVNAPATAKSAVKNTGESAGGIEPIAETITIDDFAKLDLRVAKVLKCEAVPESNKLLRFELDLGDHKRQVFSGIKAAYDKPEELEGRFVIMVANLAPRKMKFGVSEGMILSAGTGGADLFLLSADEGVTAGMQVK","491446","","methionyl-tRNA synthetase","Cytoplasm","","
InterPro
IPR001412
Family
Aminoacyl-tRNA synthetase, class I
PS00178\"[15-26]TAA_TRNA_LIGASE_I
InterPro
IPR002304
Domain
Methionyl-tRNA synthetase, class Ia
TIGR00398\"[8-535]TmetG: methionyl-tRNA synthetase
InterPro
IPR002547
Domain
t-RNA-binding region
PF01588\"[590-684]TtRNA_bind
PS50886\"[584-686]TTRBD
InterPro
IPR004495
Domain
Methionyl-tRNA synthetase, beta subunit, C-terminal
TIGR00399\"[540-686]TmetG_C_term: methionyl-tRNA synthetase, bet
InterPro
IPR008224
Family
Methionyl-tRNA synthetase, dimer-forming
PIRSF001528\"[6-686]TMethionyl-tRNA synthetase, dimer-forming
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[583-685]Tno description
InterPro
IPR013237
Domain
Phage P4 alpha, zinc-binding
SM00778\"[143-171]Tno description
InterPro
IPR013253
Family
Kinetochore Spc7
SM00787\"[367-645]Tno description
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620\"[4-388]Tno description
InterPro
IPR014758
Domain
Methionyl-tRNA synthetase, class Ia, N-terminal
PR01041\"[10-23]T\"[42-56]T\"[90-101]T\"[251-262]T\"[291-306]T\"[384-395]TTRNASYNTHMET
InterPro
IPR015413
Domain
tRNA synthetase class I (M)
PF09334\"[8-397]TtRNA-synt_1g
noIPR
unintegrated
unintegrated
G3DSA:1.10.730.10\"[389-526]Tno description
PTHR11946\"[12-558]TISOLEUCYL, LEUCYL, TYROSYL, VALYL AND METHIONYL-TRNA SYNTHETASES
PTHR11946:SF1\"[12-558]TMETHIONYL-TRNA SYNTHETASE


","BeTs to 26 clades of COG0143COG name: Methionyl-tRNA synthetaseFunctional Class: JThe phylogenetic pattern of COG0143 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 8.7e-14) to 2/2 blocks of the IPB002547 family, which is described as \"Putative tRNA binding domain\". Interpro entry for IP:IPR002547. IPB002547A 29-43 0.00087 IPB002547B 645-662 2.7e-08Significant hit ( 8.6e-07) to 2/2 blocks of the IPB001412 family, which is described as \"Aminoacyl-transfer RNA synthetases class-I\". Interpro entry for IP:IPR001412. IPB001412A 15-25 0.0021 IPB001412B 329-339 0.19","Residues 1 to 199 match (1e-10) PD:PD569352 which is described as PROBABLE LIGASE PROTEOME METHIONYL-TRNA SYNTHETASE COMPLETE ","","","","","","","","","","","","Tue Dec 17 09:04:28 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00717 is paralogously related to AA01090 (8e-10), AA02950 (8e-07) and AA00249 (8e-04).","","","","","","Residues 590 to 684 (E-value = 1.5e-40) place AA00717 in the tRNA_bind family which is described as Putative tRNA binding domain (PF01588)","","","","","Deniziak MA, Barciszewski J. Methionyl-tRNA synthetase. Acta Biochim Pol. 2001;48(2):337-50. Review. PMID: 11732605 Crepin T, Schmitt E, Blanquet S, Mechulam Y. Structure and Function of the C-Terminal Domain of Methionyl-tRNA Synthetase. Biochemistry. 2002 Oct 29;41(43):13003-11. PMID: 12390027 Dardel,F., Fayat,G. and Blanquet,S. Molecular cloning and primary structure of the Escherichia coli methionyl-tRNA synthetase gene J. Bacteriol. 160 (3), 1115-1122 (1984) PubMed: 6094501 Dardel,F., Panvert,M. and Fayat,G. Transcription and regulation of expression of the Escherichia coli methionyl-tRNA synthetase gene Mol. Gen. Genet. 223 (1), 121-133 (1990) PubMed: 2259334 ","","Tue Dec 17 09:04:28 2002","1","","","" "AA00718","493674","494783","1110","ATGGCGACGTTATTTTCAGAAAATTTAACGGAACAACAAAAGAAACGGATTGTTCGGTTATTCAAAGACTTTCAACACCCTACCCTGCAAAAAGATCTCATTTCCCTCAATACCTTAAAGAAAGTTGAAAAAGGCGGCGACACCTTACGCATTGAAATCACCATGCCTTTTGCATGGAACACCGCCTTTGCGGACTTAAAAAATGCTTTGACCGCACCGTTAAAACAGATAGCGGACGCAAAAAACGCGAAATGGCAGCTTAACTACCAAATCGCTACCTTAAAACGCGCCAACAATCACCCGGCGGTAAAAGGCGTGAAGAACATTATTGCCGTGAGCTCCGGCAAAGGCGGCGTGGGCAAATCCACCATTTCCGTGAACCTCGCCATCGCCTTGCACCTACAAGGTGCACGCGTGGGCATCTTAGACGCGGATATTTACGGACCGTCCATTCCGCATATGCTCGGCGCACCGCACCAACGCCCGACATCGCCGGACAACAAACACATCACCCCTATTCAAGCACACGGTTTATACGCCAACTCCATCGGCTTTCTCATGGACGAAGATAACGCCACCATTTGGCGCGGCCCGATGGCAAGCAGTGCCTTAAGCCAATTATTACAAGAAACTTTATGGCCGGACTTGGATTACCTCGTCATCGATATGCCTCCGGGCACCGGCGATATTCAGCTCACCTTGTCCCAACAAATTCCGGTCACCGGCGCGGTGGTCGTCACCACACCGCAAGACATTGCGTTATTGGATGCGGTAAAAGGTATCGCCATGTTTGAACGGGTTTCCGTGCCTGTATTGGGCATTGTAGAGAATATGTCCATGCATATTTGTAGCAACTGCGGTCACCAAGAAGCCATCTTCGGCACCGGCGGCGCGGAATGCATCGCGGATAAATACAACATCAAAGTATTGGGTCAGCAACCGTTGCACATCCGCCTCCGTCAAGATCTGGATCGCGGCGAACCGACCGTCATCGCCGCCCCGGACAGCGAAATCGCCCACAGCTTCCTACAATTAGCAGAAAAAGTCGCAAGCGAACTCTACTGGCAAGGCTCCGTAATCCCGAGTGAAATTATGTTCCGAGAAGTGAAT","","","42327","MATLFSENLTEQQKKRIVRLFKDFQHPTLQKDLISLNTLKKVEKGGDTLRIEITMPFAWNTAFADLKNALTAPLKQIADAKNAKWQLNYQIATLKRANNHPAVKGVKNIIAVSSGKGGVGKSTISVNLAIALHLQGARVGILDADIYGPSIPHMLGAPHQRPTSPDNKHITPIQAHGLYANSIGFLMDEDNATIWRGPMASSALSQLLQETLWPDLDYLVIDMPPGTGDIQLTLSQQIPVTGAVVVTTPQDIALLDAVKGIAMFERVSVPVLGIVENMSMHICSNCGHQEAIFGTGGAECIADKYNIKVLGQQPLHIRLRQDLDRGEPTVIAAPDSEIAHSFLQLAEKVASELYWQGSVIPSEIMFREVN","494785","","ABC-related ATP-binding protein; MRP protein","Cytoplasm","","
InterPro
IPR000808
Family
Mrp
PS01215\"[213-229]TMRP
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[106-349]Tno description
PTHR23264\"[146-367]TNUCLEOTIDE-BINDING PROTEIN NBP35(YEAST)-RELATED
PTHR23264:SF4\"[146-367]TMRP-RELATED NUCLEOTIDE-BINDING PROTEIN


","No hits to the COGs database.","Significant hit ( 3e-101) to 4/4 blocks of the IPB000808 family, which is described as \"Mrp family\". Interpro entry for IP:IPR000808. IPB000808A 106-150 1.7e-33 IPB000808B 193-229 6.2e-27 IPB000808C 249-284 3.3e-22 IPB000808D 296-336 4.5e-15Significant hit ( 1.6e-11) to 3/4 blocks of the IPB003348 family, which is described as \"Anion-transporting ATPase\". Interpro entry for IP:IPR003348. IPB003348A 111-148 5.9e-07 IPB003348C 216-236 56 IPB003348D 241-282 0.075Significant hit ( 1.2e-06) to 2/5 blocks of the IPB000392 family, which is described as \"NifH/frxC family\". Interpro entry for IP:IPR000392. IPB000392A 112-127 2.4e-06 IPB000392E 249-277 2.1e+02","Residues 108 to 156 match (6e-11) PD:PD000159 which is described as COMPLETE PROTEOME NITROGENASE PLASMID ATP-BINDING IRON-SULFUR ATPASE REDUCTASE OXIDOREDUCTASE 4FE-4S ","","","","","","","","","","","","Thu Jan 23 11:17:13 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00718 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Van Eenennaam H, Vogelzangs JH, Lugtenberg D, Van Den Hoogen FH, Van Venrooij WJ, Pruijn GJ.Identity of the RNase MRP- and RNase P-associated Th/To autoantigen.Arthritis Rheum. 2002 Dec;46(12):3266-3272.PMID: 12483731 Lin ZP, Johnson DR, Finch RA, Belinsky MG, Kruh GD, Sartorelli AC.Comparative study of the importance of multidrug resistance-associated protein 1 and P-glycoprotein to drug sensitivity in immortalized mouse embryonic fibroblasts.Mol Cancer Ther. 2002 Oct;1(12):1105-14.PMID: 12481434","","Tue Dec 17 10:24:17 2002","1","","","" "AA00719","494889","494767","123","ATGGGGATGAGTGAAAATAGATTGCTAACGCGTGTTCAAAATAAAAGTGCGGTCAATTTAAAAAACATTTTTCAAATCGACCGCACTTTTTATCTATCCCTTCCTAATTCACTTCTCGGAACA","","","4667","MGMSENRLLTRVQNKSAVNLKNIFQIDRTFYLSLPNSLLGT","494767","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database.","
InterPro
IPR000215
Family
Proteinase inhibitor I4, serpin
PS00284\"[24-34]?SERPIN


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 10:26:46 2004","Mon Feb 23 10:26:46 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00719 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 10:26:46 2004","","","","","","","","","","","","","1","","","" "AA00721","496021","494879","1143","ATGAATTATATTAAGAAAATTATTTTATCTCTTTTCCTACTGGGACTATTTAGCGTGTTGAATTGTTGCGTAAAAGGCAATTCCATATATCCGCAAAAAATAAGTACCAAGCAGACCGGATTAATGCTGGACATCGCCCGACATTTTTATTCACCCGAGGTGATTAAATCCTTTATTGATACCATCAGCCTTTCCGGCGGTAATTTTCTGCACCTGCATTTTTCCGACCATGAAAACTATGCGATAGAAAGCCATTTACTTAATCAACGTGCGGAAAATGCCGTGCAGGGCAAAGACGGTATTTATATTAATCCTTATACCGGAAAGCCATTCTTGAGTTATCGGCAACTTGACGATATCAAAGCCTATGCTAAGGCAAAAGGCATTGAGTTGATTCCCGAGCTTGACAGTCCGAATCACATGACGGCGATCTTTAAACTGGTGCAAAAAGACAGAGGGGTCAAGTATCTTCAAGGATTAAAATCACGCCAGGTAGATGATGAAATTGATATTACTAATGCTGACAGTATTGCCTTTATGCAATCTTTAATGAATGAGGTTATTGATATTTTTGGCGACACGAGTCAGCATTTTCATATTGGTGGCGATGAATTTGGTTATTCTGTGGAAAGTAATCATGAGTTTATTACGTATGCCAATAAACTATCCTACTTTTTAGAGAAAAAGGGGTTGAAAACCCGAATGTGGAATGACGGATTAATTAAAAGTACTTTTGAGCAAATCAACCCGAATATTGAAATTACTTATTGGAGCTATGATGGCGATACGCAGGACAAAAATGAAGCTGCCGAGCGTCGTGATATGCGGGTCAGTTTGCCGGAGTTGCTGGCGAAAGGCTTTACTGTCCTGAACTATAATTCCTATTATCTTTACATTGTTCCGAAAGCTTCACCAACCTTCTCGCAAGATGCCGCCTTTGCCGCCAAAGATGTTATAAAAAATTGGGATCTTGGTGTTTGGGATGGACGAAACACCAAAAACCGCGTACAAAATACTCATGAAATAGCCGGCGCAGCATTATCGATCTGGGGAGAAGATGCAAAAGCGCTGAAAGACGAAACAATTCAGAAAAACACGAAAAGTTTATTGGAAGCGGTGATTCATAAGACGAATGGGGATGAG","","","43241","MNYIKKIILSLFLLGLFSVLNCCVKGNSIYPQKISTKQTGLMLDIARHFYSPEVIKSFIDTISLSGGNFLHLHFSDHENYAIESHLLNQRAENAVQGKDGIYINPYTGKPFLSYRQLDDIKAYAKAKGIELIPELDSPNHMTAIFKLVQKDRGVKYLQGLKSRQVDDEIDITNADSIAFMQSLMNEVIDIFGDTSQHFHIGGDEFGYSVESNHEFITYANKLSYFLEKKGLKTRMWNDGLIKSTFEQINPNIEITYWSYDGDTQDKNEAAERRDMRVSLPELLAKGFTVLNYNSYYLYIVPKASPTFSQDAAFAAKDVIKNWDLGVWDGRNTKNRVQNTHEIAGAALSIWGEDAKALKDETIQKNTKSLLEAVIHKTNGDE","494881","","probable beta-N-acetylhexosaminidase (lacto-N-biosidase); dispersin B","Cytoplasm, Periplasm, Extracellular","","
InterPro
IPR001540
Family
Glycoside hydrolase, family 20
PR00738\"[30-47]T\"[59-80]T\"[123-140]T\"[169-187]T\"[193-206]T\"[342-358]TGLHYDRLASE20
PF00728\"[40-377]TGlyco_hydro_20
InterPro
IPR013781
Domain
Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80\"[40-352]Tno description
noIPR
unintegrated
unintegrated
PTHR22600\"[40-353]TBETA-HEXOSAMINIDASE
signalp\"[1-22]?signal-peptide
tmhmm\"[10-30]?transmembrane_regions


","BeTs to 3 clades of COG3525COG name: N-acetyl-beta-hexosaminidaseFunctional Class: GThe phylogenetic pattern of COG3525 is -----------l----g-s--j----Number of proteins in this genome belonging to this COG is","Significant hit ( 7.9e-17) to 5/8 blocks of the PR00738 family, which is described as \"Glycosyl hydrolase family 20 signature\". Prints database entry for PR:PR00738. PR00738C 59-80 0.012 PR00738D 123-140 9.4e-06 PR00738E 169-187 0.98 PR00738F 193-206 0.25 PR00738G 342-358 1.1e+02","Residues 40 to 238 match (1e-15) PD:PD003081 which is described as HYDROLASE BETA-N-ACETYLHEXOSAMINIDASE GLYCOSIDASE PRECURSOR SIGNAL BETA-HEXOSAMINIDASE GLYCOPROTEIN N-ACETYL-BETA- GLUCOSAMINIDASE COMPLETE ","","","","","","","","","","","","Thu Aug 4 11:35:08 2005","","Thu Aug 4 11:35:08 2005","Thu Aug 4 11:40:23 2005","Thu Aug 4 11:35:08 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA00721 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Aug 4 11:35:08 2005","","","","","Residues 40 to 366 (E-value = 1.2e-11) place AA00721 in the Glyco_hydro_20 family which is described as Glycosyl hydrolase family 20, catalytic domain (PF00728)","Thu Aug 4 11:35:08 2005","","","Ramasubbu N, Thomas LM, Ragunath C, Kaplan JB.Structural analysis of dispersin B, a biofilm-releasing glycoside hydrolase from the periodontopathogen Actinobacillus actinomycetemcomitans.J Mol Biol. 2005 Jun;349(3):475-86.PMID: 15878175","Yem,D.W. and Wu,H.C. Purification and properties of beta-N-acetylglucosaminidasefrom Escherichia coli J. Bacteriol. 125 (1), 324-331 (1976) PubMed: 1377 Cheng,Q., Li,H., Merdek,K. and Park,J.T. Molecular characterization of thebeta-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling J. Bacteriol. 182 (17), 4836-4840 (2000) PubMed: 10940025 ","Thu Aug 4 11:40:23 2005","Tue Dec 17 10:53:46 2002","1","","","" "AA00722","496582","496160","423","ATGAGTTTACAACGAACATTATCCATTATTAAACCGGATGCGGTGAAACGCCACTTAGTCGGCGCAATTTTGGCGCGCTTTGAGCAACAGGGTTTTAAAATTGTGGCAGCAAAAATGTTGCATTTAACGCAGGAGCAGGCGGAAGGTTTTTATGTCGAACACCAAGGCAAACCTTTTTTTGTGTCGTTGGTGGAATACATGACATCCGCCCCTGTGTTGGTTAGCGTATTGGAAAAAGAAAACGCCGTGCAGGATTACCGCACTTTAATTGGCAGTACTAACCCTGAGAACGCTGCCAAAGGCACGATTCGCCGTGATTTTGCCTTAAGCCAACAGGAAAACTCCGTACATGGTTCCGACAGTCCGGAAAGTGCTGCCCGTGAAATCGCCTATTTTTTCGTGAGCGATGAGATTAGTCATTAT","","","15758","MSLQRTLSIIKPDAVKRHLVGAILARFEQQGFKIVAAKMLHLTQEQAEGFYVEHQGKPFFVSLVEYMTSAPVLVSVLEKENAVQDYRTLIGSTNPENAAKGTIRRDFALSQQENSVHGSDSPESAAREIAYFFVSDEISHY","496162","","nucleoside diphosphate kinase","Cytoplasm","","
InterPro
IPR001564
Domain
Nucleoside diphosphate kinase
PD001018\"[8-138]TNDK_HAEIN_P43802;
PR01243\"[6-28]T\"[50-69]T\"[70-87]T\"[91-107]T\"[114-133]TNUCDPKINASE
G3DSA:3.30.70.141\"[1-141]Tno description
PF00334\"[4-138]TNDK
SM00562\"[3-140]TNDK
PS00469\"[114-122]TNDP_KINASES
InterPro
IPR012005
Family
Nucleoside-diphosphate kinase
PIRSF000735\"[3-140]TNucleoside diphosphate kinase
noIPR
unintegrated
unintegrated
PTHR11349\"[48-141]TNUCLEOSIDE DIPHOSPHATE KINASE


","BeTs to 24 clades of COG0105COG name: Nucleoside diphosphate kinaseFunctional Class: FThe phylogenetic pattern of COG0105 is aompkzyq-dr-bcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-58) to 3/3 blocks of the IPB001564 family, which is described as \"Nucleoside diphosphate kinase\". Interpro entry for IP:IPR001564. IPB001564A 4-32 6.5e-17 IPB001564B 50-83 7.2e-19 IPB001564C 100-133 2.6e-20","Residues 4 to 138 match (1e-53) PD:PD001018 which is described as KINASE DIPHOSPHATE NUCLEOSIDE NDP TRANSFERASE ATP-BINDING NDK NUCLEOSIDE-2-P COMPLETE PROTEOME ","","","","","","","","","","","","Tue Dec 17 11:00:31 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00722 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 141 (E-value = 9.1e-88) place AA00722 in the NDK family which is described as Nucleoside diphosphate kinase (PF00334)","","","","","Hama,H., Almaula,N., Lerner,C.G., Inouye,S. and Inouye,M. Nucleoside diphosphate kinase from Escherichia coli; its overproduction and sequence comparison with eukaryotic enzymes Gene 105 (1), 31-36 (1991) PubMed: 1657712 Ray,N.B. and Mathews,C.K. Nucleoside diphosphokinase: a functional link between intermediary metabolism and nucleic acid synthesis Curr. Top. Cell. Regul. 33, 343-357 (1992) PubMed: 1323446 Almaula,N., Lu,Q., Delgado,J., Belkin,S. and Inouye,M. Nucleoside diphosphate kinase from Escherichia coli J. Bacteriol. 177 (9), 2524-2529 (1995) PubMed: 7730286 ","","Tue Dec 17 11:00:31 2002","1","","","" "AA00723","497901","496597","1305","ATGTCCATGCAAGTTTTGCTTTCGAACCAACCGGCATCTGCCGCGTGGGGCGAAAAAGCGTTAATCAGTTTCAACGAAGATAAAGCCACCATTCATTTAACCGATTTTTCCGACCGCACTTCCGTACAAAAAGCCGCACGCAAATTACAAAATCAAGGCATTTCCAATGTCACATTAAGTGGCGAACATTGGCAGCTGGAAAATTGCTGGGCGTTTTATCAAGGCTTTTATAATGCTAAGAAACACTTCAAGGTTCAATTCCCGACCTTATCTGCCGCACAACAGCAGGAACTGAATCATCGCATTCAATGCGGCGATTTCGTTCGTGAAATCATTAATTTACCTGCCGCTATTTTAACCCCGGAAGAACTTGCCCAGCGCGCGGCGAAGTTTATCGTTCAAACGGCAGAGCAACAGGGCAAAAAAAGTGCGGTTGGTTTTTCCATCGTTTCTCGTGAGGAGTTGCTTGAGCGCGGTTACCACGGCTTATGGCAGGTGGGAAAAGGCTCGCAAAATCTGCCGGCAATGTTGCAGTTGGATTTCAACCCGACGGGCAGCCCTGATGCGCCCGTGCTGGCGTGTTTGGTAGGCAAAGGCATTACCTTTGACAGCGGCGGTTACAGCATTAAACCGAGCGACGGCATGAGCACCATGCGCACCGACATGGGTGGCGCGGCGTTATTAACGGGTGCGTTGGGGTTGGCAATTTTACGCGGCTTAAATCAGCGGGTGAAATTATTCCTTTGCTGCGCAGAAAATTTGGTCAGCAGTCGTGCCTTTAAATTGGGCGACATTATCCAGTATCGCAACGGCGTGACCGTGGAAATTCTGAACACCGACGCGGAAGGACGCTTAGTGTTGGCGGACGGTTTAATTGACGCCGATGCGCAACAACCGCAATTTATCGTGGATTGCGCCACTTTAACGGGTGCCGCAAAAGTCGCCGTCGGCAACGATTATCACAGTGTGTTGTCTATGGATGATAACTTGGTCGGCGAATTATTCCGTTCTGCCGAGCAGGAACAGGAAGCGTTTTGGCGTTTGCCGTTTGCGGAGCTACATCGCGGACAGATTAAAACCGCCTTCGCCGATATTGCCAACACCGGCACGGTTCCCATCGGCGCAGGTGCCAGCACTGCCACCGCTTTTTTATCCTATTTCGTGAAAAATTATCAACAGCATTGGCTGCACATTGATTGCTCCGCCACCTATCGCAAAACGCCAAGCGATTTATGGGCGACCGGTGCCACCGGTATTGGTGTGCAAACTTTAGCCAATCTATTAATTACTAAAGCAAATCAACAG","","","48123","MSMQVLLSNQPASAAWGEKALISFNEDKATIHLTDFSDRTSVQKAARKLQNQGISNVTLSGEHWQLENCWAFYQGFYNAKKHFKVQFPTLSAAQQQELNHRIQCGDFVREIINLPAAILTPEELAQRAAKFIVQTAEQQGKKSAVGFSIVSREELLERGYHGLWQVGKGSQNLPAMLQLDFNPTGSPDAPVLACLVGKGITFDSGGYSIKPSDGMSTMRTDMGGAALLTGALGLAILRGLNQRVKLFLCCAENLVSSRAFKLGDIIQYRNGVTVEILNTDAEGRLVLADGLIDADAQQPQFIVDCATLTGAAKVAVGNDYHSVLSMDDNLVGELFRSAEQEQEAFWRLPFAELHRGQIKTAFADIANTGTVPIGAGASTATAFLSYFVKNYQQHWLHIDCSATYRKTPSDLWATGATGIGVQTLANLLITKANQQ","496599","","peptidase B (leucyl aminopeptidase)","Cytoplasm, Periplasm","","
InterPro
IPR000819
Domain
Peptidase M17, leucyl aminopeptidase, C-terminal
PR00481\"[193-210]T\"[215-236]T\"[252-273]T\"[274-294]T\"[302-317]TLAMNOPPTDASE
PF00883\"[108-426]TPeptidase_M17
PS00631\"[278-285]TCYTOSOL_AP
InterPro
IPR008330
Family
Peptidase M17, peptidase B
PIRSF036388\"[3-434]TCytosol aminopeptidase, prokaryotic peptidase B
InterPro
IPR011356
Family
Peptidase M17, leucyl aminopeptidase
PTHR11963:SF3\"[55-435]TLEUCINE AMINOPEPTIDASE
noIPR
unintegrated
unintegrated
G3DSA:3.40.630.10\"[107-433]Tno description
PTHR11963\"[55-435]TLEUCINE AMINOPEPTIDASE-RELATED


","BeTs to 17 clades of COG0260COG name: Leucyl aminopeptidaseFunctional Class: EThe phylogenetic pattern of COG0260 is -----z-q-dr-bcefghsnujxi-wNumber of proteins in this genome belonging to this COG is","Significant hit ( 8.4e-81) to 7/7 blocks of the IPB000819 family, which is described as \"Cytosol aminopeptidase\". Interpro entry for IP:IPR000819. IPB000819A 108-117 3.7 IPB000819B 145-183 1.2e-09 IPB000819C 195-210 4.8e-12 IPB000819D 252-294 1.4e-25 IPB000819E 302-317 3.1e-07 IPB000819F 339-386 2.9e-13 IPB000819G 391-405 0.00058","","","","","","","","","","","","","Tue Dec 17 11:04:36 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00723 is paralogously related to AA01778 (1e-47).","","","","","","Residues 108 to 426 (E-value = 1.9e-130) place AA00723 in the Peptidase_M17 family which is described as Cytosol aminopeptidase family, catalytic domain (PF00883)","","","","","Mathew,Z., Knox,T.M. and Miller,C.G. Salmonella enterica serovar typhimurium peptidase B is a leucyl aminopeptidase with specificity for acidic amino acids J. Bacteriol. 182 (12), 3383-3393 (2000) Suzuki,H., Kim,E., Yamamoto,N., Hashimoto,W., Yamamoto,K. and Kumagai,H. Mapping, cloning, and DNA sequencing of pepB gene which encodes peptidase B of Escherichia coli K-12 J. Ferment. Bioeng. 82, 392-397 (1996)Comment:","","Tue Dec 17 11:03:45 2002","1","","","" "AA00724","498096","497947","150","GTGCTACCGCCGGTTTCCGTTGGCGGAATCTTGTACAAAAATTCGGTGCGGATTATACCGTTTTTGTTGATGGCAAGAAAGTTTTTTAAATCAAGAAGCCTGCCGGAATCGGTTTTTTCTTCGATTCATGGTGAGAAAATCCGTAAAAGC","","","5613","VLPPVSVGGILYKNSVRIIPFLLMARKFFKSRSLPESVFSSIHGEKIRKS","497947","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 10:29:07 2004","Mon Feb 23 10:29:07 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00724 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 10:29:07 2004","","","","","","","","","","","","","1","","","" "AA00725","498121","498336","216","ATGTCAAAAGAAGATTCCATTGAAATGCAAGGCACGATTTTAGAAACCTTGCCAAATACCATGTTTCGCGTTGAGTTGGAAAACGGTCACGTGGTAACTGCTCACATTTCCGGCAAAATGCGTAAAAACTACATCCGTATCTTAACCGGCGATAAAGTCACCGTAGAAATGACGCCATACGATTTAAGTAAAGGCCGCATCATTTTCCGCAGCCGT","","","8268","MSKEDSIEMQGTILETLPNTMFRVELENGHVVTAHISGKMRKNYIRILTGDKVTVEMTPYDLSKGRIIFRSR","498338","","translation initiation factor 1","Cytoplasm","","
InterPro
IPR003029
Domain
RNA binding S1
SM00316\"[4-72]TS1
InterPro
IPR004368
Family
Translation initiation factor IF-1
TIGR00008\"[3-71]TinfA: translation initiation factor IF-1
InterPro
IPR006196
Family
S1, IF1 type
PF01176\"[5-70]TeIF-1a
PS50832\"[1-72]TS1_IF1_TYPE
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[1-71]Tno description


","BeTs to 20 clades of COG0361COG name: Translation initiation factor IF-1Functional Class: JThe phylogenetic pattern of COG0361 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 9.9e-05) to 2/2 blocks of the IPB003029 family, which is described as \"S1 RNA binding domain\". Interpro entry for IP:IPR003029. IPB003029A 11-22 2.3 IPB003029B 50-61 0.031","Residues 3 to 70 match (2e-29) PD:PD003406 which is described as INITIATION FACTOR TRANSLATION BIOSYNTHESIS IF-1 CHLOROPLAST PROTEOME COMPLETE IF1 IF-1 ","","","","","","","","","","","","Tue Dec 17 11:05:54 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00725 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 72 (E-value = 4.8e-09) place AA00725 in the S1 family which is described as S1 RNA binding domain (PF00575)","","","","","Sands,J.F., Cummings,H.S., Sacerdot,C., Dondon,L., Grunberg-Manago,M. and Hershey,J.W. Cloning and mapping of infA, the gene for protein synthesis initiation factor IF1 Nucleic Acids Res. 15 (13), 5157-5168 (1987) PubMed: 3037488 Cummings,H.S., Sands,J.F., Foreman,P.C., Fraser,J. and Hershey,J.W. Structure and expression of the infA operon encoding translational initiation factor IF1. Transcriptional control by growth rate J. Biol. Chem. 266 (25), 16491-16498 (1991) PubMed: 1909328 ","","Tue Dec 17 11:05:54 2002","1","","","" "AA00726","499946","498405","1542","ATGAACAAATATTTCACTTATCTTATCGCACTCATTTTCGGCGCTGCCGGCGTGTTTGCCTTTGCACCCTTTTATTATTGGGGCTTGTCTTACATCTCCCTGTTCGGTTTGATTTGGGTGATAAAAACACCGCAAAAATCCACCGCACTTTTGTCTGCCTTTTTATGGGGCTTGAGCTTTTTTACCTTCGGCGTGAACTGGCTGCACGTCAGCATTCACCAATTTGGCGGCGCGCCGTTGGCGTTGAGTTATTTCTTGGTGGTATTGCTGGCAGCGTATTTGTCGTTGTATCCGCTCCTGTTCGCCTATTTAGTACGTCGTTTGCAGGTACAACGGGCGGTACTTTACCCCGTGCTGTGGACGTTTACCGAATTCCTACGCGGTTGGGTGTTTACCGGTTTCCCTTGGCTGCAATTCGGTTATACCCAAATTGACAGCCCCTTTGCCAGAGTAGTGCCGATTTTCGGCGTGACGGGTTTAACCTTCTTCGTGATGTTTATAAGTGCGGTCATTTTTAACATCGTTTCTGCACTGACAACCCCGCCGAAAAAAGCCAATGTGGCGGTGGCGAATGCGTTGATTTTGATGGTTATCGGTGGCGTTGCCGCTTACACGTCGCAACTCAACTATGTAAAAGAGAACGCCGAAAAAGCCCTTAATATTACTTTGGTGCAGGGCAATATTGAGCAAAATCTGAAATGGGATCCCAATTATTTGTATCAAACCATGGAAAATTACGGGCGTTTGATTGGCGATAATCTGGGCAAAACGGATTTGATTATTCTGCCGGAAGTGGCGTTTCCGACCTACGAAAATGACATTCAGCCTTTTTTCCAAGCCTTGCAATCATTGGCGGAAAAAGCGGATACGGAAGTGATGGCGGGCACGCTTTATCAGGATGAAAGCGTGGGTAAATCGCTTAATTCCATTGTGGTGGTGGGCAACAAATCCGCCCCTTATAGTATGCAAACCGAGAACCGTTACAACAAACATCACTTAGTGCCGTTCGGCGAATATGTGCCGCTGGAAAGCATTCTGCGCCCCCTCGGTTCGGTGTTCAATTTGCCGATGTCCGCTTTCCAAAGCGGCGATGCGGTGCAGAAACCGTTACAGGCGAAGAACCTGAACTTCACGGCGGCGATTTGTTACGAGATTATTTTAGGCGCGCAATTACAACAAAATCTTACGGCAAGCAGCGATTTTATCGTCACCATTTCTAACGATGCCTGGTTCGGCAACTCCATCGGTCCATGGCAGCATTTGCAAATGGCGCAAATGCGTGCGCTAGAGTTCGGCAAGCCGGTGATTCGCGCCACTAATACGGGCGTTACTGCCTTTATTGATGCTCAGGGTAAAATCGTGGCGCAGGCACCGCAATTCGTGGAAACGGTGTTAACCCGTAAAATTGCACCGACCGAAGGCAAAACGCCGTATGCCGTGTTTGGCAATATGCCGTTGTATACCTTAAGTGCGGTGTTTTTCTTGTTGCATTTACTGGGAATGTGGCTACAGCGTATCATGCTGAGAAAGGCGCAAAAAGAC","","","58620","MNKYFTYLIALIFGAAGVFAFAPFYYWGLSYISLFGLIWVIKTPQKSTALLSAFLWGLSFFTFGVNWLHVSIHQFGGAPLALSYFLVVLLAAYLSLYPLLFAYLVRRLQVQRAVLYPVLWTFTEFLRGWVFTGFPWLQFGYTQIDSPFARVVPIFGVTGLTFFVMFISAVIFNIVSALTTPPKKANVAVANALILMVIGGVAAYTSQLNYVKENAEKALNITLVQGNIEQNLKWDPNYLYQTMENYGRLIGDNLGKTDLIILPEVAFPTYENDIQPFFQALQSLAEKADTEVMAGTLYQDESVGKSLNSIVVVGNKSAPYSMQTENRYNKHHLVPFGEYVPLESILRPLGSVFNLPMSAFQSGDAVQKPLQAKNLNFTAAICYEIILGAQLQQNLTASSDFIVTISNDAWFGNSIGPWQHLQMAQMRALEFGKPVIRATNTGVTAFIDAQGKIVAQAPQFVETVLTRKIAPTEGKTPYAVFGNMPLYTLSAVFFLLHLLGMWLQRIMLRKAQKD","498407","","apolipoprotein N-acyltransferase, copper","Inner membrane, Cytoplasm","","
InterPro
IPR003010
Domain
Nitrilase/cyanide hydratase and apolipoprotein N-acyltransferase
G3DSA:3.60.110.10\"[219-469]Tno description
PF00795\"[220-407]TCN_hydrolase
PS50263\"[219-514]TCN_HYDROLASE
InterPro
IPR004563
Domain
Apolipoprotein N-acyltransferase
TIGR00546\"[56-453]Tlnt: apolipoprotein N-acyltransferase
noIPR
unintegrated
unintegrated
signalp\"[1-20]?signal-peptide
tmhmm\"[4-26]?\"[47-67]?\"[81-101]?\"[113-133]?\"[152-172]?\"[187-205]?\"[483-503]?transmembrane_regions


","BeTs to 15 clades of COG0815COG name: Apolipoprotein N-acyltransferaseFunctional Class: MThe phylogenetic pattern of COG0815 is -------qvdr--cefgh-nujxit-Number of proteins in this genome belonging to this COG is","","Residues 269 to 327 match (4e-09) PD:PD566401 which is described as N-ACYLTRANSFERASE INNER CUTE PROTEOME TRANSMEMBRANE ALP HOMEOSTASIS APOLIPOPROTEIN 2.3.1.- COMPLETE ","","","","","","","","","","","","Tue Dec 17 11:08:07 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00726 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 220 to 407 (E-value = 1e-36) place AA00726 in the CN_hydrolase family which is described as Carbon-nitrogen hydrolase (PF00795)","","","","","Gupta SD, Lee BT, Camakaris J, Wu HC. Identification of cutC and cutF (nlpE) genes involved in coppertolerance in Escherichia coli. J Bacteriol. 1995 Aug;177(15):4207-15. PMID: 7635807","","Tue Dec 17 11:08:07 2002","1","","","" "AA00729","501237","500344","894","ATGAACGAAGAACACTCGACCAACCAATCTGAAGTTACTAAAAAATCTTTTTTCCAATCCCTTTTCGGACGTTTCTTTCAAGGCGAGCTTAAAAATCGCGATGATTTAGTGGAAGTAATCCGAGATTCCGAACAAAACGATTTAATCGACCAAAATACCCGCGAAATGATTGAAGGCGTAATGGAAATCGCCGAGTTGCGCGTGCGCGATATTATGATTCCGCGCTCTCAAATCGTGTTTATCGAAACCGATCAAGATTTGGATTCCTGTTTGGACACCATCATCGAATCCGCCCACTCGCGCTTCCCGGTAATTGCCGATGCGGACGACCGCGACAATATTGTCGGTATTTTGCACGCCAAAGATTTATTGAAATTCCTGCGCGCCAATGCGGAAGAATTTAATTTGCTGACCATGATTCGCCCGACCATGATCGTGCCGGAAAGCAAACGAGTAGACAGAATGCTGAAGGATTTCCGTTCCGAGCGCTTCCACATGGCGATTGTGGTGGATGAATTCGGCGCGGTGTCGGGTTTGGTGACCATTGAAGATGTGTTGGAACAAATCGTCGGGGATATTGAAGACGAATTCGATGAAGAAGAAGTGGCGGATATTCGCCAGCTTTCCCGCCACACCTATGCCGTGCGGGCATTGACGGACATTGCAGATTTCAATCAACAATTCAATACCCAATACGCCGATGAAGAAGTGGACACCATCGGCGGTTTGGTGATGCAGGCATTCGGCTATTTGCCGAAACGCGGCGAAGAAATTACGCTGGATAACCTGCATTTTAAAGTTACCTCCGCCGACAGCCGCCGCATCATCCAACTCCGTGTCACCGTGCCGGACGAGCATTTGCCGGAGATGGAAAAAGAGGAAGAGGTTGTGGCG","","","34342","MNEEHSTNQSEVTKKSFFQSLFGRFFQGELKNRDDLVEVIRDSEQNDLIDQNTREMIEGVMEIAELRVRDIMIPRSQIVFIETDQDLDSCLDTIIESAHSRFPVIADADDRDNIVGILHAKDLLKFLRANAEEFNLLTMIRPTMIVPESKRVDRMLKDFRSERFHMAIVVDEFGAVSGLVTIEDVLEQIVGDIEDEFDEEEVADIRQLSRHTYAVRALTDIADFNQQFNTQYADEEVDTIGGLVMQAFGYLPKRGEEITLDNLHFKVTSADSRRIIQLRVTVPDEHLPEMEKEEEVVA","500346","","possible hemolysin (TlyC-like)","Cytoplasm","","
InterPro
IPR000644
Domain
Cystathionine-beta-synthase
PF00571\"[72-190]TCBS
SM00116\"[77-128]T\"[142-190]TCBS
InterPro
IPR005170
Domain
Transporter-associated region
PF03471\"[206-284]TCorC_HlyC
noIPR
unintegrated
unintegrated
PTHR22777\"[32-298]THEMOLYSIN-RELATED


","BeTs to 20 clades of COG1253COG name: Hemolysins and related proteins containing CBS domainsFunctional Class: NThe phylogenetic pattern of COG1253 is -o----yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 154 to 227 match (5e-07) PD:PD268257 which is described as COMPLETE PROTEOME TRANSMEMBRANE CBS DOMAIN HEMOLYSIN SMC00240 MLR2581 XF1280 INTEGRAL ","","","","","","","","","","","","Tue Dec 17 11:22:18 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00729 is paralogously related to AA01123 (7e-25) and AA00296 (2e-19).","","","","","","Residues 206 to 284 (E-value = 5.3e-24) place AA00729 in the CorC_HlyC family which is described as Transporter associated domain (PF03471)","","","","","Radulovic S, Troyer JM, Beier MS, Lau AO, Azad AF.Identification and molecular analysis of the gene encoding Rickettsia typhi hemolysin.Infect Immun. 1999 Nov;67(11):6104-8.PMID: 10531273Gibson MM, Bagga DA, Miller CG, Maguire ME.Magnesium transport in Salmonella typhimurium: the influence of new mutations conferring Co2+ resistance on the CorA Mg2+ transport system.Mol Microbiol. 1991 Nov;5(11):2753-62.PMID: 1779764 ","","Tue Dec 17 11:22:05 2002","1","","","" "AA00730","501215","501442","228","TTGGTCGAGTGTTCTTCGTTCATAAAAATTAAAAATATTACCGTCGGATTGACAGGCGAAAAGTATCATATTTGCCCCGAAAGCGCAAAAGGAAGAACAAAAGTGCGGTCGTTTTTTTCTGCGAATTTTGTGCTATGTCACAAAATCATGGCAAAAAAGAAAATCTGCAGAAAACTGAATAAAATCAACAATACACCTTTTGTGTTAGCAAAAACGATGAAACTCAAG","","","8627","LVECSSFIKIKNITVGLTGEKYHICPESAKGRTKVRSFFSANFVLCHKIMAKKKICRKLNKINNTPFVLAKTMKLK","501444","","hypothetical protein","Periplasm, Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Tue Dec 17 11:22:59 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00730 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00732","501483","502487","1005","ATGCAGTTTGAGCGACTATCTACGGCGCATAAAGATCTCAGTGCCATCCGCGAATTTTTAGCCAAAAACGAACTGGATTTAGATGCGCAAATCGAGTATTTCATCGTGGGCTACGACGAGGCGCAACAGATTGCGGTTTGTGGCGGTTTGGCGGGCAACATCATCAAATGCGTCGTCATTGATGAATCCCAGCGCGGCAACGGTGTTGCCTTGCAGCTCGGCACCGAATTAGTCAATCTCGCCTACGAACTCCATCGCCCCCACCTCTTCATTTATACCAAACCCGAATACGAAAAACTCTTTAACGCCTGTGGTTTTTACACCATCTCCGATACTTATCCTTACGTCGTGCTGCTGGAAAACAGCGCCACCCGCTTGCAAAAACAATGCGAAAAATGGCGCGCCATGCGGGTGCCCGGGCAGCACATCGGCGCTATCGTGATGAATGCCAATCCGTTCACGCTGGGGCATCGGTATTTAATCGAACGGGCGCTGCAACAATGCGATCACTTGCATTTATTCGTGGTGGGTGAAGATGCCTCGCAATTTTCTTACGAGGAACGTTTTACATTAATCCAACAAGGCATTGCCGATTTAACCAATATCACCCTTCATTCTGGCTCCGACTACATTATTTCCCGAGCCACCTTTCCCGATTATTTCCTAAAAGACCAAAAAATTACCGACGACAGCTATTTTGCCGTAGATTTGAAATTATTCCGCCGTTATATCGCGCCCGCATTGGGCATTAACCGCCGCTTTGTGGGGACGGAACCGACTTGCGCGGTCACCGCGGAATACAACCGCCAAATGTTCTACTGGCTGATGGAAGCCGAAATGGACGCACCGAAAATCGACGTCATCGAAATCCCGCGTAAAACCATCAACGGGCAAGCCATTTCCGCCTCCGTCGTCAGAAAATTATTAGCCGAAAAGCATTGGACGGCATTGGCGGAATTTGTACCAAGCAGCACGTTAAATTATTTGCAAAAGTGCGGTCGTTTT","","","38250","MQFERLSTAHKDLSAIREFLAKNELDLDAQIEYFIVGYDEAQQIAVCGGLAGNIIKCVVIDESQRGNGVALQLGTELVNLAYELHRPHLFIYTKPEYEKLFNACGFYTISDTYPYVVLLENSATRLQKQCEKWRAMRVPGQHIGAIVMNANPFTLGHRYLIERALQQCDHLHLFVVGEDASQFSYEERFTLIQQGIADLTNITLHSGSDYIISRATFPDYFLKDQKITDDSYFAVDLKLFRRYIAPALGINRRFVGTEPTCAVTAEYNRQMFYWLMEAEMDAPKIDVIEIPRKTINGQAISASVVRKLLAEKHWTALAEFVPSSTLNYLQKCGRF","502489","From GenBank (gi:1168960):This protein acetylates the prothetic group (2(5''-phosphoribosyl)-3'-diphosphocoenzyme-A) of the gamma subunit of citrate lyase. ","citrate lyase ligase","Cytoplasm","","
InterPro
IPR000182
Domain
GCN5-related N-acetyltransferase
PS51186\"[1-131]TGNAT
InterPro
IPR004821
Domain
Cytidyltransferase-related
TIGR00125\"[143-201]Tcyt_tran_rel: cytidyltransferase-related do
InterPro
IPR005216
Family
Citrate lyase ligase
PIRSF005751\"[1-335]TCitrate lyase ligase
TIGR00124\"[3-335]Tcit_ly_ligase: [citrate (pro-3S)-lyase] lig
InterPro
IPR013166
Domain
Citrate lyase ligase, C-terminal
PF08218\"[143-329]TCitrate_ly_lig
SM00764\"[143-329]Tno description
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620\"[140-205]Tno description


","BeTs to 3 clades of COG3053COG name: Citrate lyase synthetaseFunctional Class: CThe phylogenetic pattern of COG3053 is -----------l--e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 3 to 330 match (5e-145) PD:PD016147 which is described as LIGASE LYASE CITRATE PRO-3S-LYASE PROTEOME COMPLETE SYNTHETASE ACETATE:SH-CITRATE ORF5 ACETATE-SH-CITRATE ","","","","","","","","","","","Fri Jan 24 12:00:50 2003","Fri Jan 24 12:00:50 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00732 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Bott M, Dimroth P. Klebsiella pneumoniae genes for citrate lyase and citrate lyase ligase: localization, sequencing, and expression. Mol Microbiol. 1994 Oct;14(2):347-56. PMID: 7830578Martín M, Corrales MA, de Mendoza D, López P, Magni C.Cloning and molecular characterization of the citrate utilization citMCDEFGRP cluster of Leuconostoc paramesenteroides.FEMS Microbiol Lett. 1999 May;174(2):231-8.PMID: 10339813Meyer M, Dimroth P, Bott M.Catabolite repression of the citrate fermentation genes in Klebsiella pneumoniae: evidence for involvement of the cyclic AMP receptor protein.J Bacteriol. 2001 Sep;183(18):5248-56.PMID: 11514506Bekal S, Van Beeumen J, Samyn B, Garmyn D, Henini S, Diviès C, Prévost H.Purification of Leuconostoc mesenteroides citrate lyase and cloning and characterization of the citCDEFG gene cluster.J Bacteriol. 1998 Feb;180(3):647-54.PMID: 9457870","","Fri Jan 24 12:00:50 2003","1","","","" "AA00733","502475","502573","99","GTGCGGTCGTTTTTAAAAACGTTTTTTAATTATCACCCAATAGAAGGAAAAACCTATGAAGATAACGAAAGCAGCCGTTGCCGGCACGCTGGAATCCAG","","","3913","VRSFLKTFFNYHPIEGKTYEDNESSRCRHAGIQ","502573","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 10:40:31 2004","Mon Feb 23 10:40:31 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00733 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 10:40:31 2004","","","","","","","","","","","","","1","","","" "AA00734","502668","502814","147","GTGCGTGCGGTGCTAAACAAATTGAATGTCACCGCGGCGCAAGTGATCATTGAAGACAAGGGCGCCCTTGATTGCGTGTTACAGGCACGAGTGAAAGCGGCGGTGTTACGCGCTACAGACGAAAACATTAACTGGGAGGCGGTGCTA","","","10206","VRAVLNKLNVTAAQVIIEDKGALDCVLQARVKAAVLRATDENINWEAVL","502816","From GenBank (gi:116895):This protein covalently binds the coenzyme of citrate lyase.","citrate lyase, gamma chain (acyl carrier protein)","Cytoplasm, Outer membrane","","
InterPro
IPR006495
Family
Citrate lyase acyl carrier protein CitD
PD015389\"[1-46]TCILG_HAEIN_P44461;
PF04953\"[1-48]TCitD


","BeTs to 3 clades of COG3052COG name: Citrate lyase, gamma subunitFunctional Class: CThe phylogenetic pattern of COG3052 is -----------l--e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 1 to 46 match (1e-10) PD:PD015389 which is described as LYASE CITRATE GAMMA COMPLETE PROTEOME ACYL CARRIER CHAIN SUBUNIT LYASE ","","","","","","","","","","","Fri Jan 24 12:04:43 2003","Fri Jan 24 12:10:01 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00734 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 48 (E-value = 2.7e-09) place AA00734 in the CitD family which is described as Citrate lyase, gamma subunit (PF04953)","","","","","Martin,M., Corrales,M.A., de Mendoza,D., Lopez,P. and Magni,C. Cloning and molecular characterization of the citrate utilization citMCDEFGRP cluster of Leuconostoc paramesenteroides. FEMS Microbiol. Lett. 174(2): 231-238, 1999. PubMed: 10339813. Bott,M. and Dimroth,P. Klebsiella pneumoniae genes for citrate lyase and citrate lyaseligase: localization, sequencing, and expression. Mol. Microbiol. 14(2): 347-356, 1994. PubMed: 7830578. Bekal S, Van Beeumen J, Samyn B, Garmyn D, Henini S, Diviès C, Prévost H.Purification of Leuconostoc mesenteroides citrate lyase and cloning and characterization of the citCDEFG gene cluster.J Bacteriol. 1998 Feb;180(3):647-54.PMID: 9457870","","Fri Jan 24 12:10:01 2003","1","","","" "AA00735","502814","503686","873","ATGAAATTAAGAAGAAGTATGCTGTTCGTGCCGGGTTCAAATGCGGCAATGTTAAGTAACAGTTTTATTTATAAACCGGATTCCATCATGTTCGACCTGGAAGATGCGGTGGCGTTGAAAGAAAAAGATACCGCCCGTTTGTTGGTGGCACACGCCCTGCAACATCCGCTGTACAAAGACATTGAAACCGTAGTGCGTGTGAATCCATTAGATTCTGAATTTGGTTTAGCAGACTTAAACGCCGTAGTGCGTACCGGTGTGGATGTGGTACGGATGCCGAAAACCGAAACGGCGCAAGATATGATCGATATGGATCGCGAAATCACCGAAATCGAAAAAGCCTGCGGACGTGAAGTGGGTTCCACCAAAATGCTCGCTGCCATCGAATCGCCGTTGGGCATCACCCAAGCTAATCAAATCGCCACTGCTTCCAAGCGTTTAATCGGCATTGCCTTGGGCGCAGAAGACTATGTACGCAACCTGAAAACCGAACGCTCGCCGGAAGGTATCGAGCTTTTATTCGCCCGTTGTTCCATTTTACAAGCGGCGCGTGCAGCCGGCATTCAAGCCTTTGATACGGTGTATTCCAACGCCAACAATGAAGAAGGTTTCTTGAAAGAAGCGGCGTTAATTAAACAGCTCGGCTTCGATGGCAAATCCTTGATCAATCCGCGTCAAATTGAATTGTTACACAACTTGTTCGCGCCGACACAAAAAGACGTGGATCAGGCAAAACGCATTATTGAAGCGGCGGAAGAAGCGGAACGCCAAGGGTCCGGCGTGGTTTCATTAAACGGCAAAATGATTGATGCGCCGATTATTGATCGTGCGAAACTCGTGTTAGAACGTGCCAAATCAGGCATTCGTGAAGAG","","","31950","MKLRRSMLFVPGSNAAMLSNSFIYKPDSIMFDLEDAVALKEKDTARLLVAHALQHPLYKDIETVVRVNPLDSEFGLADLNAVVRTGVDVVRMPKTETAQDMIDMDREITEIEKACGREVGSTKMLAAIESPLGITQANQIATASKRLIGIALGAEDYVRNLKTERSPEGIELLFARCSILQAARAAGIQAFDTVYSNANNEEGFLKEAALIKQLGFDGKSLINPRQIELLHNLFAPTQKDVDQAKRIIEAAEEAERQGSGVVSLNGKMIDAPIIDRAKLVLERAKSGIREE","503688","From GenBank (gi:1168952):This protein represents a citryl-ACP lyase. ","citrate lyase, beta chain","Cytoplasm","","
InterPro
IPR005000
Family
HpcH/HpaI aldolase
PF03328\"[5-224]THpcH_HpaI
InterPro
IPR006475
Family
Citrate lyase, bacterial beta subunit
TIGR01588\"[2-288]TcitE: citrate lyase, beta subunit
InterPro
IPR011206
Family
Citrate lyase, beta subunit
PIRSF015582\"[2-290]TCitrate lyase, subunit beta
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.60\"[1-234]Tno description
signalp\"[1-15]?signal-peptide


","BeTs to 8 clades of COG2301COG name: Citrate lyase beta subunitFunctional Class: GThe phylogenetic pattern of COG2301 is -o---z---drl--efgh---j----Number of proteins in this genome belonging to this COG is","","Residues 171 to 291 match (3e-53) PD:PD008620 which is described as LYASE PROTEOME COMPLETE CITRATE BETA SUBUNIT CHAIN LYASE CITRYL-COA CITE ","","","","","","","","","","","Fri Jan 24 12:09:00 2003","Fri Jan 24 12:09:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00735 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Hupperich,M., Henschen,A. and Eggerer,H. Citrate lyase from Klebsiella pneumoniae. The complete primarystructure of the acyl lyase subunit. Eur. J. Biochem. 192(1): 161-166, 1990. PubMed: 2205500. Bott,M. and Dimroth,P. Klebsiella pneumoniae genes for citrate lyase and citrate lyaseligase: localization, sequencing, and expression. Mol. Microbiol. 14(2): 347-356, 1994. PubMed: 7830578. Bekal S, Van Beeumen J, Samyn B, Garmyn D, Henini S, Diviès C, Prévost H.Purification of Leuconostoc mesenteroides citrate lyase and cloning and characterization of the citCDEFG gene cluster.J Bacteriol. 1998 Feb;180(3):647-54.PMID: 9457870Meyer M, Dimroth P, Bott M.Catabolite repression of the citrate fermentation genes in Klebsiella pneumoniae: evidence for involvement of the cyclic AMP receptor protein.J Bacteriol. 2001 Sep;183(18):5248-56.PMID: 11514506","","Fri Jan 24 12:09:00 2003","1","","","" "AA00737","503704","505203","1500","ATGACAACAAGAGAACAACGCATTGCAAAATTCAATGCCAATCGTCCGGTGTATCAGGCAGTACCGAAAGCGGAATCCCTTGCCCGCACGGCGAAAGATCGCAAAATCTGCGATTCGTTGGAAGACGCGATTAAACGCTCCGGCTTAAAAGACGGCATGACCGTGTCCTTCCACCACGCCTTCCGCGCCGGTGACTTCGTGGTCAACATGGTGATGGATAAAATCACCGAAATGGGTTTCAAAAATTTAACCCTCGCTTCCAGTTCATTAATCGATAGTCACTCACCGCTCATCGAACACATCAAAAACGGCGTAGTGACTAAAATCTACTCTTCCGGTCTTCGTGGTGAATTAGCAGAACAAATCTCTCGCGGTTTATTAGACGAACCGGTTAACATTCACTCCCACGGCGGTCGCGTGCATTTGGTGAAATCCGGCGAACTGAAAATCGACGTTGCCTTTTTAGGTGTGCCTTGCTGCGATAAATTCGGTAATGCCAACGGCTTCAGCGGCAAAAGCAAATGTGGCTCACTCGGTTATGCCCGTGTGGATGCGGAATTTGCCGACAAAGTGGTGTTATTAACGGAAGAATTCGCCGACTATCCGCACCACCCGATTAGCATCGGTCAAGACCAAGTGGATCTTATCGTGCAAGTGGATGCCGTGGGCGATCCGAAAAAAATCGGCGGCGGTGCCACCCGCATGACCACCAACCCTCGCGAATTACTTATCGCCCGCAAATGTGCTGAAGTGATTTTTGCCTGCGGTTATTTCAAAGACGGTTTTTCCTTACAAACCGGTACCGGCGGCGCGTCCCTTGCGGTCACCCGCTTCCTTGAAGAAAAAATGGTGCGCGACAACATTAAAGCCGACTTTGCCCTCGGCGGGATCACCGCCAGCATGGTGGATCTGCACGAGAAAGGCTTAATCAAAAAACTGATCGATGTACAAAGCTTCGATGCCATTGCCGCCGAATCCCTGGCGCGCAACCCGAACCACATTGAAGTGTCCGCCAACCAATACTCCAACTACAGCTCCAAAGGGGCTTCCGTAGAACGTTTGGACGTGGTCATTCTTTCCGCCTTGGAAATTGACACTAAATTTAACGTGAACGTACTCACCGGCTCCGACGGCGTGATTCGCGGCGCGTCAGGCGGTCACTGCGACACCGCCTCTTCCGCGCCGGTGGCGATTATCGTTGCGCCATTAGTACGCGGACGTATCCCGACCGTAGTGGAAAACGTGATCACCTGCGTGACCCCGGGCGAAAATATCGACATTTTAGTCACCGACCACGGCGTCGCCGTGAATCCGAAACGTCCGGATCTCATCGAGGCATTAACCGCCGCCGGCATTCCGTTATTCACCATTGAGCAACTGTGTGAACGCGCTTACAGCCTCACCGGCAAACCGAAAGAAATCGAGTTTACCGATAAACCGGTAGCGGTCGTGCGGTATCGCGACGGAACGGTGATTGATACGGTTTATCAGGTGAAAGAA","","","53912","MTTREQRIAKFNANRPVYQAVPKAESLARTAKDRKICDSLEDAIKRSGLKDGMTVSFHHAFRAGDFVVNMVMDKITEMGFKNLTLASSSLIDSHSPLIEHIKNGVVTKIYSSGLRGELAEQISRGLLDEPVNIHSHGGRVHLVKSGELKIDVAFLGVPCCDKFGNANGFSGKSKCGSLGYARVDAEFADKVVLLTEEFADYPHHPISIGQDQVDLIVQVDAVGDPKKIGGGATRMTTNPRELLIARKCAEVIFACGYFKDGFSLQTGTGGASLAVTRFLEEKMVRDNIKADFALGGITASMVDLHEKGLIKKLIDVQSFDAIAAESLARNPNHIEVSANQYSNYSSKGASVERLDVVILSALEIDTKFNVNVLTGSDGVIRGASGGHCDTASSAPVAIIVAPLVRGRIPTVVENVITCVTPGENIDILVTDHGVAVNPKRPDLIEALTAAGIPLFTIEQLCERAYSLTGKPKEIEFTDKPVAVVRYRDGTVIDTVYQVKE","505205","From GenBank (gi:1168950):The protein represents a citrate: acyl-ACP transferase.","citrate lyase, alpha chain (citrase)","Cytoplasm","","
InterPro
IPR006472
Family
Citrate lyase, alpha subunit
PIRSF009451\"[1-500]TCitrate lyase, alpha subunit
PF04223\"[34-498]TCitF
TIGR01584\"[15-500]TcitF: citrate lyase, alpha subunit
noIPR
unintegrated
unintegrated
G3DSA:3.40.1080.10\"[2-230]Tno description
G3DSA:3.40.810.20\"[231-500]Tno description


","No hits to the COGs database.","","Residues 1 to 37 match (3e-10) PD:PD230929 which is described as CITRATE TRANSFERASE LYASE CITRASE PROTEOME SUBUNIT COA- CHAIN COMPLETE ALPHA ","","","","","","","","","","","Fri Jan 24 12:14:09 2003","Fri Jan 24 12:14:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00737 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Bekal S, Van Beeumen J, Samyn B, Garmyn D, Henini S, Diviès C, Prévost H.Purification of Leuconostoc mesenteroides citrate lyase and cloning and characterization of the citCDEFG gene cluster.J Bacteriol. 1998 Feb;180(3):647-54.PMID: 9457870Bott M, Dimroth P.Klebsiella pneumoniae genes for citrate lyase and citrate lyase ligase: localization, sequencing, and expression.Mol Microbiol. 1994 Oct;14(2):347-56.PMID: 7830578","","Fri Jan 24 12:15:57 2003","1","","","" "AA00738","505316","505227","90","GTGACTTATTACGATGGAGCGCGTTTCCCGACGCGTGCCTTCATTTTCTTATTTTTTATCAGCGCGCGTCAGAAGGCGCGTGCTATCGGT","","","3466","VTYYDGARFPTRAFIFLFFISARQKARAIG","505227","","hypothetical protein","Cytoplasm, Outer membrane","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-28]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 10:41:59 2004","Mon Feb 23 10:41:59 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00738 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 10:41:59 2004","","","","","","","","","","","","","1","","","" "AA00740","505400","506809","1410","ATGACAATATCCCTAAAACATTTTTCCACCACTGGAACTGAAATCTCCCTTGAACAGCTTTTATCTGCGCGGAAAGCGCGTGCGTTGCTGCAACAAAAGCTATTGGCGCAGTACGGTCAAACGTTGCTTTGCGTCACGTTGACCGCGGTGGGCGGGGTGAAAAAAAATGCCCTGCTGGATTATGTCTTTGCAAAAACGCTGGAAAAACTCACCGCACTTTTTACGCAGTTAGCCATCACCCCAAGCGCAGAACGGATTCGTCCGTTGGAAACGGGGCATGAAGCGTTTTTTGTGTTGCCGATGGACGCCAAAGCACTGAAAGCGGCAATGATCGAACTGGAAGAAAGCCTTCCTCTCGCCCGTCTTTGGGACTTGGATGTGTTTGATCATGAGGGCAATCTGCTTAGCCGAAGCGATTTCGGTATGCCGCCGCGAACCTGTTTGGTGTGCGGTGCGGATGCCAAAGTCTGTGCCAGATCGCGCGCCCATGGTATTGCGGATATTCTGGCGGAAACGCACAAGCGGGCGCAACAACATGATTTGGCGGAACAAATCGGCAACGCAGTTTGTTCTGCATTAATTCAGGAAGCCCGACTGTCGCCGAAACCCGGCTTGGTGGATGCCATCAATAACGGGGCGCACAAGGACATGAACCTGCAAACCTTCGAGCAAAGTGCGGTCAGTTTGGCACCTTTTTTTACGGCGTTCGTATTAAAAGGGATGCAAACGGCGTCTCTGCCACCATCGCAAATCTTAGCGCAGGTTCGTCCGTTGGGTGTTCTTGCCGAAAAGGCGATGTTTAAAGCAACCCATGGCGTGAATACGCACAAAGGCGCGATTTTTTCCTTTGGTTTGGTATGCGCCGCCATCGGGCGCTTGTTGCAACAGCAGGATTTATCGCAAAGTGCGGTGGTTTTTGAGGTTAAATCCATTTGTGATTTGGTGGCGCAATTTGCGCAAGGCTTAACTGCCGAGCTACAACATTATCCCGACCATTTGCCGATCACCGCCGGCGTGCGATTATTCCGTCAATTCGGTTTAACCGGCGCGCGCGGCGAAGCGGAAAGTGGTTTTCAACAAATTCAAACGTTGTTGCCCCTGTTGGATGAGGATCATCAACAAGATTGGGAACATCGTTTACTCATTCTGTTATTGCATTTAATGGCGACCAATGCCGACACGAACGTAGTACATCGCGGCGGTATGGAAGGATTGCATTTTGTGCAGCAAACAGCGAAAGATCTGCTTGCAGATCAAACCGTTGTGTCGGATAAAGTGAAACTGACACAAGCCTTAATGAAATTTGATGCTGCCTGCATTGCGCGAAATTTAAGCGCAGGCGGTAGCGCCGATTTGTTGGCGCTGATGATTTTCTTTCAAACTTTAAGAGGTAATTCACATGGCATTATC","","","51112","MTISLKHFSTTGTEISLEQLLSARKARALLQQKLLAQYGQTLLCVTLTAVGGVKKNALLDYVFAKTLEKLTALFTQLAITPSAERIRPLETGHEAFFVLPMDAKALKAAMIELEESLPLARLWDLDVFDHEGNLLSRSDFGMPPRTCLVCGADAKVCARSRAHGIADILAETHKRAQQHDLAEQIGNAVCSALIQEARLSPKPGLVDAINNGAHKDMNLQTFEQSAVSLAPFFTAFVLKGMQTASLPPSQILAQVRPLGVLAEKAMFKATHGVNTHKGAIFSFGLVCAAIGRLLQQQDLSQSAVVFEVKSICDLVAQFAQGLTAELQHYPDHLPITAGVRLFRQFGLTGARGEAESGFQQIQTLLPLLDEDHQQDWEHRLLILLLHLMATNADTNVVHRGGMEGLHFVQQTAKDLLADQTVVSDKVKLTQALMKFDAACIARNLSAGGSADLLALMIFFQTLRGNSHGII","506811","From GenBank (gi:14286109):CitG is a bifunctional enzyme that ctalyses formation of 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A, and then the transfer of this prosthetic group precursor to the apo0acyl carrier protein (gamma chain) of the citrate lyase to yields the holo-acyl carrier protein. The N-terminal section belongs to the CITX family, and the C-terminal section belongs to the CITG/.MDCB family.","citrate lyase related biosynthesis protein (2-(5'-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase)","Cytoplasm","","
InterPro
IPR002736
Family
Triphosphoribosyl-dephospho-CoA protein
PF01874\"[191-457]TCitG
InterPro
IPR005551
Family
Apo-citrate lyase phosphoribosyl-dephospho-CoA transferase
PF03802\"[13-183]TCitX


","No hits to the COGs database.","Significant hit ( 8.4e-63) to 4/4 blocks of the IPB002736 family, which is described as \"CitG family\". Interpro entry for IP:IPR002736. IPB002736A 199-216 9.5e-10 IPB002736B 256-288 2.6e-20 IPB002736C 375-416 5.6e-22 IPB002736D 442-459 1.3e-06","Residues 283 to 344 match (1e-17) PD:PD489608 which is described as SYNTHASE 4.2.-.- LYASE APO-ACP 2- 5''-TRIPHOSPHORIBOSYL- 2-5''- 2.7.7.- COA CITXG ","","","","","","","","","","","Tue Jun 17 10:03:08 2003","Tue Jun 17 10:03:08 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00740 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 191 to 457 (E-value = 1.1e-120) place AA00740 in the CitG family which is described as ATP:dephospho-CoA triphosphoribosyl transferase (PF01874)","","","","","Schneider K, Kastner CN, Meyer M, Wessel M, Dimroth P, Bott M. Identification of a gene cluster in Klebsiella pneumoniae whichincludes citX, a gene required for biosynthesis of the citrate lyase prosthetic group. J Bacteriol. 2002 May;184(9):2439-46. PMID: 11948157 Bekal,S., Van Beeumen,J., Samyn,B., Garmyn,D., Henini,S., Divies,C. and Prevost,H. Purification of Leuconostoc mesenteroides citrate lyase and cloning and characterization of the citCDEFG gene cluster. J. Bacteriol.180(3): 647-654, 1998. PubMed: 9457870. Martin,M., Corrales,M.A., de Mendoza,D., Lopez,P. and Magni,C. Cloning and molecular characterization of the citrate utilization citMCDEFGRP cluster of Leuconostoc paramesenteroides. FEMS Microbiol. Lett. 174(2): 231-238, 1999. PubMed: 10339813. ","","Tue Dec 17 11:34:14 2002","1","","","" "AA00741","506799","508136","1338","ATGGCATTATCTAAAAATGCAAAACTGGCGATCTTGGTAGCCATACCGTTGGTCACCTTTATTTTGCCGGCGCCGGAGGGACTTTCTCTGATCGCCTGGCGTTTACTTGGGGTTTATATCGCCACCATCGTCGGCTTGGTGTTAAAACCGTACGGCGAACCGGTAATCTTGCTGGCGGCGGTTGCGGTGTCCGGCGCGATTATCGGTAATACTAGCGGTGCAGCAGAATTTCTGAAAGCCGGCGACATTCTCAACGGTTATAAATCAGGCACCACGTGGTTGATTTTTACCGCCTTCACATTAAGCTCCGCGTTCGTTATCACCGGTCTCGGTAAACGTATTGCTTATCACATGATCGGCGCCATGGGTAGCACCACATTACGTTTGGGTTATGTGACCATGTTCCTGGATTTACTGCTCTCCCCTGCAACGCCGTCCAACACCGCGCGTTCGGGCGGGATTATCTTCCCTATCATCAACAGTGTGGCCGTGGCATTAGGTTCCGACCCGGAAAAAAGCCCGAAAAAAGCCGGTCGCTATTTGATGATGAACGTGTACATGGTGGTAAAAACTACATCTTATATTTTCTTAACCGCCATGGCGCCGAACGCACTCGCTCTTTCCTTAATGGCGCCGATTCTCGGTTTCAAAATTGACTGGTTACATTGGTTCTTAGCCGCGTCCGTGCCTGGTTTACTGTGCTTGTTCGTGATTCCGTTAATCTGCTACTGGGTTTCCTCGCCGGAAATGAAAGAGGTGGATAACAAAGCCATCTCGAAAAAAGGCTTGGAAGAACTCGGCCCAATGTCATTCCGCGAAAAAGCGTTAATCGTGTTATTCGTCATTGCCCTCTTCGGCTGGATTTTCTCCTCTGCGTTAAACGTCAACGCGACCATCGTAGCATTAATTGTTATGGTGTGTTGTATCGTGCTGAACATCGTGTCTTGGGATGACATTCTAAAAAGCAAAGGCGGCTGGAACACCTTAATTTGGTATGGCGGTATTATCGGGATGTCCGGCTTGCTTGAAAAAGCCCAATTCTTCGGCTGGTTAGCCGAATCCTTAAAATCCGTTCTACAATTTGAAGGACAAGGCACTTTAGCCCTTATTGTGATCTTAACCCTCAGCGTTGCCGTGCGTTATCTGTTCGCCTCCGGCGGTGCCTATGTCGCCGCCATGGTACCGGTATTCGCTACCGTCGGTCACGTTGCCGGTGCACCTACAGAATTATTGGCATTAGGCTTGTTATTTGCCAATTCCTACGGTGGTTCCGTCACGCACTACGGCGGCGGTCCGGGTCCGATTGCATTTGGAGCCGGCTATAACGACATCAAATCC","","","47206","MALSKNAKLAILVAIPLVTFILPAPEGLSLIAWRLLGVYIATIVGLVLKPYGEPVILLAAVAVSGAIIGNTSGAAEFLKAGDILNGYKSGTTWLIFTAFTLSSAFVITGLGKRIAYHMIGAMGSTTLRLGYVTMFLDLLLSPATPSNTARSGGIIFPIINSVAVALGSDPEKSPKKAGRYLMMNVYMVVKTTSYIFLTAMAPNALALSLMAPILGFKIDWLHWFLAASVPGLLCLFVIPLICYWVSSPEMKEVDNKAISKKGLEELGPMSFREKALIVLFVIALFGWIFSSALNVNATIVALIVMVCCIVLNIVSWDDILKSKGGWNTLIWYGGIIGMSGLLEKAQFFGWLAESLKSVLQFEGQGTLALIVILTLSVAVRYLFASGGAYVAAMVPVFATVGHVAGAPTELLALGLLFANSYGGSVTHYGGGPGPIAFGAGYNDIKS","508138","","possible 2-oxoglutarate/malate transporter","Inner membrane, Cytoplasm","","
InterPro
IPR001898
Family
Sodium/sulphate symporter
PF00939\"[3-446]TNa_sulph_symp
TIGR00785\"[23-446]Tdass: transporter, divalent anion:Na+ sympo
noIPR
unintegrated
unintegrated
PTHR10283\"[24-446]TCATION TRANSPORTER RELATED
PTHR10283:SF13\"[24-446]TSODIUM/CARBOXYLATE COTRANSPORTER RELATED
signalp\"[1-23]?signal-peptide
tmhmm\"[5-24]?\"[30-48]?\"[55-75]?\"[89-109]?\"[124-142]?\"[148-168]?\"[183-205]?\"[224-246]?\"[274-289]?\"[295-315]?\"[330-350]?\"[364-384]?transmembrane_regions


","BeTs to 13 clades of COG0471COG name: Di- and tricarboxylate transportersFunctional Class: PThe phylogenetic pattern of COG0471 is -om-k-yq-d-lbcefghsnu--i--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.6e-18) to 4/8 blocks of the IPB001898 family, which is described as \"Sodium:sulfate symporter family\". Interpro entry for IP:IPR001898. IPB001898B 93-119 0.0053 IPB001898E 218-242 6.7 IPB001898F 266-292 1.2e-08 IPB001898G 323-352 0.15","Residues 35 to 156 match (1e-12) PD:PD006001 which is described as PROTEOME COMPLETE TRANSMEMBRANE TRANSPORTER COTRANSPORTER MEMBRANE DICARBOXYLATE ARSENICAL PUMP SODIUM ","","","","","","","","","","","","Fri Jan 24 12:37:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00741 is paralogously related to AA02254 (4e-72), AA00941 (3e-20), AA01784 (3e-14), AA00136 (4e-10) and AA00143 (9e-04).","","","","","","Residues 3 to 446 (E-value = 2e-219) place AA00741 in the Na_sulph_symp family which is described as Sodium:sulfate symporter transmembrane region (PF00939)","","","","","Weber,A., Menzlaff,E., Arbinger,B., Gutensohn,M., Eckerskorn,C. and Flugge,U.I. The 2-oxoglutarate/malate translocator of chloroplast envelopemembranes: molecular cloning of a transporter containing a 12-helix motif and expression of the functional protein in yeast cells. Biochemistry 34(8): 2621-2627, 1995. PubMed: 7873543.","","Tue Dec 17 11:40:12 2002","1","","","" "AA00742","508325","508489","165","ATGGAAATGTTACAGCTTTTTTTATATTTGATTGCGGCTTATTTAATTTTTTCTAAGCCCAAAGGAGAAAAAATAGCCTATAGGATTACATGCGTAGTCGTATTAAGTGCATTTTTTCTATTCTTTATGGCGACGAAAACAATGATTCTTCCGGGTGTTACCTAT","","","6330","MEMLQLFLYLIAAYLIFSKPKGEKIAYRITCVVVLSAFFLFFMATKTMILPGVTY","508489","","hypothetical protein","Inner membrane, Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide
tmhmm\"[25-45]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 10:43:36 2004","Mon Feb 23 10:43:36 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00742 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 10:43:36 2004","","","","","","","","","","","","","1","","","" "AA00743","508511","510007","1497","ATGAATGAAAAAATATTCAATGGAATACTAAGCTTATCTGCGCTTTCTATTGCAACGGTCTTGGGTGTTGCCTCTTTTTATCTGGGCTTTATTGATAAAGAGTCCCCCTGTATTCTTTGCTGGGCTCACCGTATGCTAATGTTCGCTGAAGTAATGTTTACTTTCCTAATAATACGATATGGACCAAAACCTAAATATATCGGCTGGGTAATATTTATCGCGGTATTTGGTATATTTGCCGGCTTTAGACATTCCTCCGGCAGCTTTGCATGGGATATTCATCAAGGTTGGTGGGCTGAAATTTTAGGTGCTCATACTTATAGCTGGCCAATGGTAATCCATGCTGTAGTTCTCATTTTTGTCGCCTTAATTTTTTGTTTTACTAAAGATATTTACAACTTTGTTAGTCAATCTCATAAACAATTGAACATATTAAGTAAAACATGTATGGCTATATTCATGATTGTCATCTGTGGCAATATGGTTCAGGCATTCATAAGTACAGGACTTCCTCCGAATATGGGAGTTAGTAATCCTGCAAGATTATCGTTTAATTCCGATTATTGGTACTGGACTACTGAAAGCTGGAAACGTCTTAGCAGACCGACATCATTACGCAATACTTGGCATGTAGAAGCACCGGATTTGCCAAGTCAACCAACAACCGCTATGCAATTTACGACTGATGCAAGACAAGCTCCATTGTCTTCTACCGGAAAATTAGTGATTCAAAAACAAGAAGCCATAACCATACCACTAAACGCCCCTGCAACAGATATTGCTTATAACGGAAAGGATAAATACTTTATTTCCACCGAAAAATGGGGATTATACTTACTTAATGATACATTAAGTGAAATTCAACGCTTTTCCGTGTTAGATCATTTAAACGGAGCTAATGGACGTATTCCGGTAGGCAGTGCATTCTTCAATGAAAATGAGTTTGGCGTACTAGGGTGGAACAAAATTTTTGTATTCTTTAAAGAAGATGCAAATCGTACTGCAAAAGAAAACTACCCGAGTTTTATAGAAGGCCTAAATAATTATGTTGTAACTGCCCGTGGTGCTTATAACACTGTACGCTCGCGCCTATTTCACGTTCTATCAATGGCTTACTTACCGGAAAACAATAGCATCTATACAGCTACTGTACCGAATTCCAAAAATCAGAAGCTCATAATTTCCCGCTTCGATAAAAGTGACAATATTCTTTCTGAGGAATTCACCCCGAAAGTAAAAAAGGGAATAGCGCTAACAGAAGGAAAAAGTATAGGTGATTATTACATCACAGGATTAACTGCCTATAATGGAAATCTATACGCAGTAAGCAAGCAATTTTCTCAAGTGTTAGAAATAAATCCAATCACAAGAGAAATCACTCATGTTTATGAATTTAATGGTATTGAAAACCCTCAGGGGATTACTTTCAAGCATGGTGTAATGCAAATTCTTAGCTATGAAAAAGGCAAAAATTTACTTTATTCTCTAACTGAAGAA","","","57141","MNEKIFNGILSLSALSIATVLGVASFYLGFIDKESPCILCWAHRMLMFAEVMFTFLIIRYGPKPKYIGWVIFIAVFGIFAGFRHSSGSFAWDIHQGWWAEILGAHTYSWPMVIHAVVLIFVALIFCFTKDIYNFVSQSHKQLNILSKTCMAIFMIVICGNMVQAFISTGLPPNMGVSNPARLSFNSDYWYWTTESWKRLSRPTSLRNTWHVEAPDLPSQPTTAMQFTTDARQAPLSSTGKLVIQKQEAITIPLNAPATDIAYNGKDKYFISTEKWGLYLLNDTLSEIQRFSVLDHLNGANGRIPVGSAFFNENEFGVLGWNKIFVFFKEDANRTAKENYPSFIEGLNNYVVTARGAYNTVRSRLFHVLSMAYLPENNSIYTATVPNSKNQKLIISRFDKSDNILSEEFTPKVKKGIALTEGKSIGDYYITGLTAYNGNLYAVSKQFSQVLEINPITREITHVYEFNGIENPQGITFKHGVMQILSYEKGKNLLYSLTEE","510009","","conserved hypothetical protein (possible membrane protein)","Inner membrane, Cytoplasm","","
InterPro
IPR003752
Family
Disulphide bond formation protein DsbB
PF02600\"[2-164]TDsbB
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide
tmhmm\"[10-30]?\"[40-58]?\"[67-87]?\"[106-128]?\"[149-169]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 4.3e-07) to 1/1 blocks of the IPB003752 family, which is described as \"Disulfide bond formation protein DsbB\". Interpro entry for IP:IPR003752. IPB003752 25-57 4.3e-07","Residues 6 to 169 match (6e-20) PD:PD143143 which is described as PROTEOME COMPLETE MEMBRANE B HP0595 DISULFIDE ATP FORMATION INNER CJAE ","","","","","","","","","","","","Tue Dec 17 11:45:20 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00743 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 164 (E-value = 4.6e-06) place AA00743 in the DsbB family which is described as Disulfide bond formation protein DsbB (PF02600)","","","","","","","","1","","","" "AA00744","511306","510278","1029","ATGCTAGAACAACGTGCACAAAGCACTGCACCGGACGGCTTGCCGTTTAACCTGTTTATCTTGCAAAACGCACAAGGTATGCGCGTGCAATTTACCGACTGGGGTGCGACTTGGATCTCTTGTTGTCTGCCGGTCAACGGCGAATTGCGTGAAGTGCTGTTGGGCTGCAAATTGGAAGATTATCCCGTTCAACAAGCCTACTTAGGCGTGAGCGTAGGACGCTATGCCAATCGTATCGCCAACGCGCAATTTCCGTTGAATGGCAAAGTTGTGCGCTTAACCGCCAACCAAGGCAAACACCAACTGCACGGCGGAAACGGTTTCGATAAACGCCGTTGGACGTTGGAAAAGTGCGGTGAAAATTTTGTGTGTTTTTCATTGTATTCCGCCGACGGCGATCAAGGTTTCCCCGGCAATGTGAAGGCGACGGTAACTTACACCTTGACGGAAGATAATGCGGTTAAAATCGAATATGCCGCCCAAAGCGATCAGGATACCGCACTGAATTTAACCAATCACGCCTATTTCAATTTAGAAAATGCGATGCAGGGCGCAGATGTGCGCAACCATAGCTTGCGCCTCAACGCCGATTTTTATTTACCGGTGGATAGCGAAGGCATTCCTAACTCGCCGCTCAAACATGTTGTCGGCACCGGCTTTGATTTCCGCATAGCCAAGCCAATTAAACAGGATTTTTTGCAAGGAGAACAGCTTGCTGCCAAAGGCTACGACCATTCTTTTATTGTGAATAAAGCCTGGCAAAAACCTTGTGTTCTGCTCACCTCTCCAAACGGCGATTTAAGCCTGGAAGTGCTGACTTCACAAGCCGCCTTACAGGTTTACACCGGCAACTTCCTCGCCGGCACGCCGACCCGTGAGGGTGCTCAATATGCCGACTACCACGGCATCGCCCTGGAAACCCAATGCCTTCCCGATACCCCAAATCACCCCGAATGGCAAAATTACGGCGGCATTGTAAAAGCAGGCGAAGAATATTACCAATGGACGGAATATCGATTTAAGGGAAAT","","","39318","MLEQRAQSTAPDGLPFNLFILQNAQGMRVQFTDWGATWISCCLPVNGELREVLLGCKLEDYPVQQAYLGVSVGRYANRIANAQFPLNGKVVRLTANQGKHQLHGGNGFDKRRWTLEKCGENFVCFSLYSADGDQGFPGNVKATVTYTLTEDNAVKIEYAAQSDQDTALNLTNHAYFNLENAMQGADVRNHSLRLNADFYLPVDSEGIPNSPLKHVVGTGFDFRIAKPIKQDFLQGEQLAAKGYDHSFIVNKAWQKPCVLLTSPNGDLSLEVLTSQAALQVYTGNFLAGTPTREGAQYADYHGIALETQCLPDTPNHPEWQNYGGIVKAGEEYYQWTEYRFKGN","510280","","aldose 1-epimerase (mutarotase)","Periplasm","","
InterPro
IPR008183
Family
Aldose 1-epimerase
PF01263\"[17-339]TAldose_epim
PS00545\"[169-178]TALDOSE_1_EPIMERASE
InterPro
IPR013458
Family
Galactose mutarotase
TIGR02636\"[13-341]TgalM_Leloir: galactose mutarotase
InterPro
IPR014718
Domain
Glycoside hydrolase-type carbohydrate-binding, subgroup
G3DSA:2.70.98.10\"[9-340]Tno description
InterPro
IPR015443
Family
Aldose_1_epimerase
PTHR10091\"[64-342]TALDOSE-1-EPIMERASE


","No hits to the COGs database.","Significant hit ( 1.2e-37) to 4/4 blocks of the IPB001823 family, which is described as \"Aldose 1-epimerase\". Interpro entry for IP:IPR001823. IPB001823A 69-84 3e-08 IPB001823B 136-148 1.9e-06 IPB001823C 166-178 4.3e-07 IPB001823D 302-319 4.4e-11","Residues 135 to 321 match (1e-07) PD:PD459414 which is described as 1-EPIMERASE ALDOSE PROTEOME COMPLETE ISOMERASE MUTAROTASE ","","","","","","","","","","","","Tue Dec 17 11:49:44 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00744 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 18 to 339 (E-value = 1.4e-122) place AA00744 in the Aldose_epim family which is described as Aldose 1-epimerase (PF01263)","","","","","9: Bouffard GG, Rudd KE, Adhya SL.Dependence of lactose metabolism upon mutarotase encoded in the gal operon in Escherichia coli.J Mol Biol. 1994 Dec 2;244(3):269-78.PMID: 7966338 ","","Tue Dec 17 11:49:44 2002","1","","","" "AA00745","512454","511303","1152","ATGCTCCCAATTGAAAAATCTCAATACATTTTCACCCAAAAACACCATAAGCAGTCTGAACTCACCGTTTATGCGCCCGGGCGTGTCAATATCATCGGTGAACATACCGACTACAACGACGGTTTCGTGATGCCTTGCGCCATTAACTACGGCACGGCGATTGCCGGGGCGAAACGCAGCGACCATATTTGGAACGTCTATGCCGCGGATTTGGATTTATCCGATGAATTTTCCCTTGATGGCCAGCTCCCTCAAAGTGAACAAAAATGGGCGAATTATGTGCGTGGAGTAGTGAAATTTATTCAGGAGCGTTGCCCGAATTTCAAACAGGGCGCGGATTTGGTGATTTCCGGCAACGTGCCGTATTCTTCGGGCTTGAGCTCATCGGCAGCGCTTGAGGTGGCAACAGGAAAGTTCTGTCAGCAACTGGGCGATTTGCCTTTAAGCCATACGGAGCTTGCGCTCATCGGCCAACAAGCGGAAAACAAATTTGTCGGTGCCAACTGCGGCAATATGGATCAGCTGATTTCCGCCCTCGGGCAACAGGATCATCTGTTGATGATTGACTGCCGTAGTCTGGAAACCCTGCCGACACCCGTGCCGCACGATGTGGCAGTGATTATCGTGAACTCCAATGTGCCGCACGATTTGGTGACGGGCGAATACAATACTCGTCGTCAGCAATGTGAATGCGCGGCGGCGTTTTTCGGCGTGAAAGCCCTGCGTGATGTTTCCGTCGCTCAATTTAAGGAAAGAGAGGCAGAATTGACCGCACTTTATCCGCTGGCAGCCAAACGCGCCAGACACGTTGTGACGGAAAATCAGCGGGTGCTGGATGCGGTGGAAGCCTTGAAGCGTAATGATTTAACCCGTCTCGGCGAGTTAATGGGGCAGTCACATGATTCCATGCGCGACGATTTCGAAATCACCGTGCCGCAAATTGATTATCTGGTGGAATTGGCACAATTGGTCATCGGCAAAAATGGCGGCGCACGCATGACCGGCGGCGGTTTCGGCGGTTGTATTGTCGCCCTTGCGCCCCATGACAAAGTGGACGCGGTGCGCAAAATCATTGCGGAGAATTATGAAAAACAAACGGGCTTGAAAGAAGATTTCTACGTTTGCACCGCTTCACAAGGAGTATGCGTATGC","","","42105","MLPIEKSQYIFTQKHHKQSELTVYAPGRVNIIGEHTDYNDGFVMPCAINYGTAIAGAKRSDHIWNVYAADLDLSDEFSLDGQLPQSEQKWANYVRGVVKFIQERCPNFKQGADLVISGNVPYSSGLSSSAALEVATGKFCQQLGDLPLSHTELALIGQQAENKFVGANCGNMDQLISALGQQDHLLMIDCRSLETLPTPVPHDVAVIIVNSNVPHDLVTGEYNTRRQQCECAAAFFGVKALRDVSVAQFKEREAELTALYPLAAKRARHVVTENQRVLDAVEALKRNDLTRLGELMGQSHDSMRDDFEITVPQIDYLVELAQLVIGKNGGARMTGGGFGGCIVALAPHDKVDAVRKIIAENYEKQTGLKEDFYVCTASQGVCVC","511305","","galactokinase","Cytoplasm","","
InterPro
IPR000705
Family
Galactokinase
PR00473\"[27-45]T\"[90-101]T\"[111-129]T\"[265-279]TGALCTOKINASE
PIRSF000530\"[3-384]TGalactokinase
TIGR00131\"[4-384]Tgal_kin: galactokinase
PS00106\"[27-38]TGALACTOKINASE
InterPro
IPR006203
Domain
GHMP kinase, ATP-binding region
PS00627\"[120-131]TGHMP_KINASES_ATP
InterPro
IPR006204
Domain
GHMP kinase
PF00288\"[113-181]TGHMP_kinases_N
InterPro
IPR006206
Family
Mevalonate and galactokinase
PR00959\"[25-49]T\"[118-140]T\"[161-180]T\"[330-347]TMEVGALKINASE
InterPro
IPR013750
Domain
GHMP kinase, C-terminal
PF08544\"[280-364]TGHMP_kinases_C
InterPro
IPR014721
Domain
Ribosomal protein S5 domain 2-type fold
G3DSA:3.30.230.10\"[2-212]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.890\"[244-371]Tno description
PTHR10457\"[82-365]TMEVALONATE KINASE/GALACTOKINASE
PTHR10457:SF6\"[82-365]TGALACTOKINASE 1


","BeTs to 9 clades of COG0153COG name: GalactokinaseFunctional Class: GThe phylogenetic pattern of COG0153 is ----k-y-v-rlb-e-gh------t-Number of proteins in this genome belonging to this COG is","Significant hit (9.9e-113) to 8/8 blocks of the IPB000705 family, which is described as \"Galactokinase\". Interpro entry for IP:IPR000705. IPB000705A 25-48 2.1e-21 IPB000705B 88-98 0.00081 IPB000705C 111-132 1.4e-10 IPB000705D 161-189 1.7e-17 IPB000705E 206-236 2.5e-16 IPB000705F 265-277 5.6e-09 IPB000705G 292-318 6.3e-15 IPB000705H 330-341 2.4e-09Significant hit ( 6.4e-57) to 4/4 blocks of the PR00959 family, which is described as \"Mevalonate kinase signature\". Prints database entry for PR:PR00959. PR00959A 25-49 2.1e-19 PR00959B 118-140 2.8e-11 PR00959C 161-180 5.8e-10 PR00959D 330-347 5.3e-12Significant hit ( 2e-25) to 4/4 blocks of the IPB001745 family, which is described as \"GHMP kinases putative ATP-binding domain\". Interpro entry for IP:IPR001745. IPB001745A 26-35 0.0001 IPB001745B 120-131 0.00022 IPB001745C 161-170 0.039 IPB001745D 330-341 5.4e-09Significant hit ( 9.7e-05) to 3/5 blocks of the PR00960 family, which is described as \"LmbP protein signature\". Prints database entry for PR:PR00960. PR00960A 25-40 7.2 PR00960B 119-140 2.1 PR00960C 161-180 3","Residues 156 to 321 match (9e-08) PD:PD306534 which is described as KINASE GALACTOSE PROTEOME COMPLETE GALACTOKINASE ATP-BINDING TRANSFERASE METABOLISM ","","","","","","","","","","","","Tue Dec 17 12:00:32 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00745 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 111 to 348 (E-value = 3.7e-53) place AA00745 in the GHMP_kinases family which is described as GHMP kinases putative ATP-binding protein (PF00288)","","","","","Debouck,C., Riccio,A., Schumperli,D., McKenney,K., Jeffers,J.,Hughes,C., Rosenberg,M., Heusterspreute,M., Brunel,F. and Davison,J.Structure of the galactokinase gene of Escherichia coli, the last(?) gene of the gal operonNucleic Acids Res. 13 (6), 1841-1853 (1985)PubMed: 3158881Bouffard,G.G., Rudd,K.E. and Adhya,S.L.Dependence of lactose metabolism upon mutarotase encoded in the gal operon in Escherichia coliJ. Mol. Biol. 244 (3), 269-278 (1994)PubMed: 7966338Schlesinger,D.H., Schell,M.A. and Wilson,D.B.The NH2-terminal sequences of galactokinase from Escherichia coliand Saccharomyces cerevisiaeFEBS Lett. 83 (1), 45-47 (1977)PubMed: 200486","","Tue Dec 17 12:00:32 2002","1","","","" "AA00747","513564","512524","1041","ATGTCAACCGTTTTTGACCCGACAGAACACCCCCATCGCCGATATAACCCGTTGATTGACCAATGGGTTTTGGTTTCCCCCCACCGTGCCAAACGCCCTTGGCAAGGACAACGGGAAAAAGTGAGTGAAGAACAAAAGCCGAGTCATGACCCGAGCTGCTATCTTTGCCCGTGTAATAAACGCATCACCGGCGAACCGAATCCGGATTATCACAAGCCTTATGTATTCAAAAACGATTTTTCCGCACTGTTGGAAGATACGCCGGCACCGCAGCAGAACGACAATCCACTGTTCCAAAGTTCGCAAGCCCGTGGAGAAAGTCGTGTTATTTGCTTCTCGCCCGACCACAGCAAAACGTTGCCATTATTGACCGCACTTGAGATCGAGGAAGTCATTAAAGTGTGGCAGGAACAACTCCGTGAACTGGGGCAAAAATACCAATGGGTACAGATTTTTGAAAACAAAGGTGCCGCAATGGGCTGCTCCAACCCACACCCGCATGGTCAAATCTGGGCGAACAGCTTCCTGCCGAACGAGGTGACTAGGGAAGATAAAGCACAATGTCAATATTATGAAAAACATGGTGCCGTGCTGTTGGTGGACTATGTTCAACAGGAATTGGAAAGAAAAGAGCGCATCGTGGTAGAAACCGCGCACTGGCTTGCCGTCGTGCCTTATTGGGCGGTCTGGCCTTTTGAAATCCTATTGCTACCGAAAGCCCACGTTAAACGCTTAACGGAATTAAGCGATGCGCAGGCGAAAGATTTGGCGGTGATTCTTAAAAAGCTCACCACTAAATATGACAACCTGTTTGAAACCTCTTTCCCGTATTCCATGGGCTTCCACGCCGCCCCGTTTAATGGCGAAGAAAACGCACATTGGCAACTGCACGCCCACTTTTACCCGCCGCTTTTACGTTCCGCCACCGTACGCAAGTTTATGGTGGGCTACGAAATGCTCGGCGAAAGCCAACGCGATTTAACGGCGGAACAGGCGGCAGAAAGATTGCGTGCGTTGAGTGAAGTACATTATAAAGTGCGG","","","40314","MSTVFDPTEHPHRRYNPLIDQWVLVSPHRAKRPWQGQREKVSEEQKPSHDPSCYLCPCNKRITGEPNPDYHKPYVFKNDFSALLEDTPAPQQNDNPLFQSSQARGESRVICFSPDHSKTLPLLTALEIEEVIKVWQEQLRELGQKYQWVQIFENKGAAMGCSNPHPHGQIWANSFLPNEVTREDKAQCQYYEKHGAVLLVDYVQQELERKERIVVETAHWLAVVPYWAVWPFEILLLPKAHVKRLTELSDAQAKDLAVILKKLTTKYDNLFETSFPYSMGFHAAPFNGEENAHWQLHAHFYPPLLRSATVRKFMVGYEMLGESQRDLTAEQAAERLRALSEVHYKVR","512526","","UTP--hexose-1-phosphate uridylyltransferase / UDPglucose-hexose-1-phosphate uridylyltransferas","Cytoplasm","","
InterPro
IPR001937
Family
Galactose-1-phosphate uridyl transferase, class I
PIRSF000808\"[1-346]TGalactose-1-phosphate uridylyltransferase
PTHR11943\"[1-347]TGALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE
TIGR00209\"[1-347]TgalT_1: galactose-1-phosphate uridylyltrans
PS00117\"[152-169]TGAL_P_UDP_TRANSF_I
InterPro
IPR005849
Domain
Galactose-1-phosphate uridyl transferase, N-terminal
PF01087\"[3-177]TGalP_UDP_transf
InterPro
IPR005850
Domain
Galactose-1-phosphate uridyl transferase, C-terminal
PF02744\"[179-345]TGalP_UDP_tr_C
InterPro
IPR011573
Family
Galactose-1-phosphate uridyl transferase
PD005051\"[7-178]T\"[187-328]TGAL7_HAEIN_P31764;
noIPR
unintegrated
unintegrated
G3DSA:3.30.428.10\"[45-176]T\"[177-345]Tno description


","No hits to the COGs database.","Significant hit (9.7e-217) to 7/7 blocks of the IPB001937 family, which is described as \"Galactose-1-phosphate uridyl transferase, class I\". Interpro entry for IP:IPR001937. IPB001937A 10-37 1.6e-31 IPB001937B 47-82 6.3e-24 IPB001937C 95-137 1.4e-26 IPB001937D 148-177 5.8e-33 IPB001937E 198-238 1.2e-30 IPB001937F 252-285 1.1e-25 IPB001937G 297-337 5.6e-39 IPB001937E 197-237 0.037","Residues 210 to 285 match (6e-08) PD:PD584008 which is described as TRANSFERASE GALACTOSE-1-PHOSPHATE COMPLETE PROTEOME NUCLEOTIDYLTRANSFERASE URIDYLYLTRANSFERASE URIDYLTRANSFERASE 327AA MICROTUBULES URIDYLYLTRANSFERASE ","","","","","","","","","","","","Tue Dec 17 12:16:49 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00747 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 179 to 347 (E-value = 1.5e-96) place AA00747 in the GalP_UDP_tr_C family which is described as Galactose-1-phosphate uridyl transferase, C-terminal domain (PF02744)","","","","","Lemaire,H.G. and Muller-Hill,B.Nucleotide sequences of the gal E gene and the gal T gene of E.coliNucleic Acids Res. 14 (19), 7705-7711 (1986)PubMed: 3022232Wedekind,J.E., Frey,P.A. and Rayment,I.Three-dimensional structure of galactose-1-phosphateuridylyltransferase from Escherichia coli at 1.8 A resolutionBiochemistry 34 (35), 11049-11061 (1995)PubMed: 7669762","","Tue Dec 17 12:10:40 2002","1","","","" "AA00748","513886","513758","129","TTGTTTAATACTCTGGAAACCGTTGCGACAGATACGCCGGCTTGGTTGGCGACATCTCGAATTGTGACCATGGAATACCTTTATTATGTCGTTAAAATTAGGCAAATCATAATCCTAAATTTTTCTTTT","","","5038","LFNTLETVATDTPAWLATSRIVTMEYLYYVVKIRQIIILNFSF","513758","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 10:45:11 2004","Mon Feb 23 10:45:11 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00748 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 10:45:11 2004","","","","","","","","","","","","","1","","","" "AA00749","513921","514826","906","GTGTTAAATGCCATTGAGCAATTAGGCTATCGCCCTAACGCCAACGCGCAGGCATTGGCTTCGCAAAGTTCTGATACTCTTGGCGTGGTGGTCACCGATGTCACGGATTCGTTTTTCGCCATTTTGGTTAAAGCGGTAGATCATGTGGCAATGGAGCACGGCAAAAATATTTTGATCGGCATGGGATACCATCAGGCGGAAAAAGAACGTGATGCAATCGATACCCTGTTACGAAAACGTTGCAATTGTTTGGTGGTGCATTCTAAAGCTTTGGATGATCAAACCCTGGCGGAATACTTGGATTCAGTTCCCGGCATGGTGATTATCAATCGCTGCATTAAAGGTTATGAATCCCGCTGCGTCAGCCTGGACAATCGAAAAGGCACTTTTATCGCCACCAACACCCTGATTCAAGCCGGTCATCGACATATCGGTTACATCGGCTCCAATCATAAAATTAACGATGAAACAGAACGTAAACAAGGTTATTTGAATGCGCTGACCGAACACCATATTCCTATAGTAGAAAACGCCATTGTGCATAATTCACCGGATTTTGAAGGCGGGGAAGAAGCCATGATTAACCTCTTGAGTTATAACGACAATCTCACGGCAGTGGTGGCGTATAACGATTCCATGGCGGCGGGCGCGTTATCCGTCTTAAATGAAAACAATATCAAAGTGCCGAAGCAATTTTCCATTATCGGCTTTGACGATATGCCTATCGCCCGCTATTTGGTACCGAAATTAACTACTATTCGCTATCCCATTGATCTCATGGCGAATTATGCAGCAAAACTGGCACTAGGTCTGGTGGATATGGACATTTGCCTGCCCATTAACCCCCAATTCAATCCGACCTTGGTTCAACGTTTTTCCGTCGAAAATATACATCACACGGGAGAA","","","37141","VLNAIEQLGYRPNANAQALASQSSDTLGVVVTDVTDSFFAILVKAVDHVAMEHGKNILIGMGYHQAEKERDAIDTLLRKRCNCLVVHSKALDDQTLAEYLDSVPGMVIINRCIKGYESRCVSLDNRKGTFIATNTLIQAGHRHIGYIGSNHKINDETERKQGYLNALTEHHIPIVENAIVHNSPDFEGGEEAMINLLSYNDNLTAVVAYNDSMAAGALSVLNENNIKVPKQFSIIGFDDMPIARYLVPKLTTIRYPIDLMANYAAKLALGLVDMDICLPINPQFNPTLVQRFSVENIHHTGE","514828","","galactose operon repressor (gal repressor)","Cytoplasm","","
InterPro
IPR000843
Domain
Bacterial regulatory protein, LacI
PS50932\"[1-21]THTH_LACI_2
InterPro
IPR001761
Domain
Periplasmic binding protein/LacI transcriptional regulator
PF00532\"[24-238]TPeripla_BP_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2300\"[125-267]Tno description


","BeTs to 9 clades of COG1609COG name: Transcriptional regulatorsFunctional Class: KThe phylogenetic pattern of COG1609 is --------vdrlb-efghs--j----Number of proteins in this genome belonging to this COG is","","Residues 201 to 258 match (5e-07) PD:PD588460 which is described as PROTEOME COMPLETE REGULATOR LACI FAMILY TRANSCRIPTIONAL TRANSCRITIONAL REGULATION DNA-BINDING PLASMID ","","","","","","","","","","","","Tue Dec 17 12:28:24 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00749 is paralogously related to AA02003 (8e-30), AA02673 (4e-23), AA00209 (1e-11), AA02006 (8e-11), AA00932 (9e-07) and AA01455 (4e-04).","","","","","","Residues 24 to 300 (E-value = 4.2e-07) place AA00749 in the Peripla_BP_1 family which is described as Periplasmic binding proteins and sugar binding domain of the LacI family (PF00532)","","","","","Geanacopoulos M, Adhya S.Genetic analysis of GalR tetramerization in DNA looping during repressosome assembly.J Biol Chem. 2002 Sep 6;277(36):33148-52.PMID: 12065579 ","","Tue Dec 17 12:28:24 2002","1","","","" "AA00750","515044","516033","990","ATGAAAAAAACAGTATTAAGTGCGGTGGTTTTCTCGATAGTTTTTGGTATCGGCATCAGTACAACACAAGCAGAAACCCGTATCGGTGTAACCATTTACAAATATGATGACAATTTCATGTCTTTAATGCGTAAAGAAATTCAAAAAAATGCAGAACAATTACAAAACGTAAAACTGCTGATGAATGATTCTCAAAACGCACAATCTATCCAAAACGACCAGGTGGACGTATTACTTTCCAAAGGTGTGAAAGCGCTTGCCATTAACTTGGTTGACCCTTCCGCCGCACCGACAATTATCGGCAAAGCCAAACTGGATAATATCCCGGTGGTGTTCTTCAACAAAGATCCGGGTGCAAAAGTCATTGGCAGCTATGAAAACGCTTATTATGTAGGTACGGATCCGAAAGAATCCGGTTTAATCCAAGGGGATTTAATCGCTAAACAATGGAAAGCCATGCCGGCATTAGACTTAAATAAAGACGGCAAAATCCAATATGTGTTATTAAAAGGCGAACCGGGCCACCCTGATGCGGAAGCACGTACCAAGTATGTGATTGAGCAACTAAACGCGCAAGGCATTCCAACGGAACAACTCTTTATCGACACCGGGATGTGGGATGCGGCACTGGCAAAAGACAAAATGGATGCGTGGTTATCCAGCTCTAAAGCCAATGACATTGAAGTCATTATTTCCAACAACGACGGCATGGCGATGGGCGCATTGGAAGCAACCAAAGCACACGGCAAAAAATTACCGATTTTCGGGGTAGATGCGTTGCCTGAAGTATTACAACTCATCAAGAAAGGCGACATTGCAGGTACCGTATTGAATGACGGCGCGACTCAAGGTAAAGCGATTGTGGATTTATCCAACAACCTGGCAAACGGCAAACCGGCTACCGAAGGCACCAAATGGGAGCTTAAAGATCGCGTTGTGCGCATTCCTTATGTTGGCGTAGATAAAGACAACTTGTCTCAATTCTTAAAA","","","35817","MKKTVLSAVVFSIVFGIGISTTQAETRIGVTIYKYDDNFMSLMRKEIQKNAEQLQNVKLLMNDSQNAQSIQNDQVDVLLSKGVKALAINLVDPSAAPTIIGKAKLDNIPVVFFNKDPGAKVIGSYENAYYVGTDPKESGLIQGDLIAKQWKAMPALDLNKDGKIQYVLLKGEPGHPDAEARTKYVIEQLNAQGIPTEQLFIDTGMWDAALAKDKMDAWLSSSKANDIEVIISNNDGMAMGALEATKAHGKKLPIFGVDALPEVLQLIKKGDIAGTVLNDGATQGKAIVDLSNNLANGKPATEGTKWELKDRVVRIPYVGVDKDNLSQFLK","516035","","periplasmic D-galactose-binding ABC transport protein","Periplasm","","
InterPro
IPR001761
Domain
Periplasmic binding protein/LacI transcriptional regulator
PF00532\"[25-323]TPeripla_BP_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2300\"[134-293]Tno description
signalp\"[1-24]?signal-peptide
tmhmm\"[5-23]?transmembrane_regions


","No hits to the COGs database.","","Residues 299 to 330 match (1e-09) PD:PD545697 which is described as PERIPLASMIC PROTEOME COMPLETE D-GALACTOSE-BINDING SIGNAL GBP GGBP PRECURSOR D-GALACTOSE/ D-GLUCOSE ","","","","","Tue Feb 18 14:17:45 2003","","","","","","","Tue Dec 17 12:35:03 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00750 is paralogously related to AA02788 (5e-20), AA00209 (1e-17), AA02787 (4e-16), AA01455 (8e-10) and AA00932 (4e-07).","","","","","","","","","",""," Salins LL, Ware RA, Ensor CM, Daunert S.A novel reagentless sensing system for measuring glucose based on the galactose/glucose-binding protein.Anal Biochem. 2001 Jul 1;294(1):19-26.PMID: 11412001 Lepine G, Ellen RP.MglA and mglB of Treponema denticola; similarity to ABC transport and spa genes.DNA Seq. 2000;11(5):419-31.PMID: 11328650 Zhang P, Cheng X, Duhamel GE.Cloning and DNA sequence analysis of an immunogenic glucose-galactose MglB lipoprotein homologue from Brachyspira pilosicoli, the agent of colonic spirochetosis.Infect Immun. 2000 Aug;68(8):4559-65.PMID: 1089985","","Tue Feb 18 14:17:45 2003","1","","","" "AA00751","516111","517646","1536","ATGACAGAACAAAATCAAAGTCCAAGCGGAAACCAAAGTCAAAGCGGTGAAGTGCTGCTTACGATGAAGGATGTCAGTAAATCCTTTCCGGGCGTAAAAGCCTTAGATCAGGCGAATCTGACCGTCCGTTCACATTCTGTACACGCATTGATGGGGGAAAACGGTGCGGGTAAATCCACACTGCTAAAATGTTTATTTGGTATTTATGCTAAAGATGAAGGCGATATTTTATTTTTAGGCAAGCCCGTTAACTTTAAAACCTCAAAAGAAGCCCTGGAAAACGGCATTTCCATGGTGCACCAGGAATTGAATCTGGTGCGTCAGACCAGCGTAATGGATAACCTGTGGCTCGGACGTTATCCGCTGAAAGGACCGTTTGTGGATCACGCCAAAATCTATCGTGATACCAAAGCCATTTTTGACGAGTTGGATATTGATATTGATCCGAAAGAAAAAGTGGCGAAACTTTCCGTTTCTCAAATGCAGATGATCGAAATTGCGAAAGCGTTTTCTTATAACGCCAAAATCGTGATTATGGATGAACCGGCATCCTCCCTTTCCGAAAAAGAAGTGGAACATCTGTTTAAAATCATTCAAAAACTCAAAGATCGCGGTTGCGGCATTATTTATATTTCCCACAAAATGGATGAAATCTTCAAAATTTGCGACGAAATCACCATTTTACGCGATGGCAAATGGATTAACACCGTGCCGGTGAAAGGTTCCACCATGGAACAAATTGTTTCCATGATGGTGGGTCGTGAGCTGACCCAACGCTTCCCGGAAAAAACCAATACGCCGAAAGAAGTGATTTTAACGGTAGAAAATCTGACCGCACTTAATCAACCGTCCATTCAGGACGTGTCATTCGATTTGCGCAAAGGTGAAATTTTAGGTATCGCCGGCTTGGTCGGAGCAAAACGTACGGATGTGGTGGAAGCCATTTTCGGCGTGCGTGAACTGAAAAGCGGCACCATTACCTTGCACGGAAAAACAGTGAAAAATCACACCGCACTTGAAGCCATCAATAACGGCTTTGCGCTGGTGACCGAAGAACGCCGCTCCACCGGGATTTATTCCAATTTAAGCATTGAATTCAATTCTTTGATTTCCAATATGAAATCCTATCTCACCTCCTGGAAATTACTGAGCAACAAAAAAATGCGCAGCGACACCCAATGGGTGATTGATTCCATGAACGTGAAAACACCGTCCCACAAAACCACGATCGGTTCCCTTTCCGGCGGTAACCAACAAAAAGTGATTATCGGACGCTGGTTACTTACCCAACCGGAAATTCTCATGCTGGACGAACCGACCCGTGGTATCGACATCGGTGCGAAATTTGAAATTTACCAACTCATTCAGGAACTCGCCAAAAAAGACAAAGGCATCATTATGATTTCTTCCGAAATGCCTGAATTGCTTGGGGTCACCGACCGAATTTTGGTGATGAGTAACGGTAAAGTCGCCGGTATTGTGGAAACCGCGAACACCTCACAAGAAGAAATTTTGCAACTTGCGGCAAAATATTTA","","","57395","MTEQNQSPSGNQSQSGEVLLTMKDVSKSFPGVKALDQANLTVRSHSVHALMGENGAGKSTLLKCLFGIYAKDEGDILFLGKPVNFKTSKEALENGISMVHQELNLVRQTSVMDNLWLGRYPLKGPFVDHAKIYRDTKAIFDELDIDIDPKEKVAKLSVSQMQMIEIAKAFSYNAKIVIMDEPASSLSEKEVEHLFKIIQKLKDRGCGIIYISHKMDEIFKICDEITILRDGKWINTVPVKGSTMEQIVSMMVGRELTQRFPEKTNTPKEVILTVENLTALNQPSIQDVSFDLRKGEILGIAGLVGAKRTDVVEAIFGVRELKSGTITLHGKTVKNHTALEAINNGFALVTEERRSTGIYSNLSIEFNSLISNMKSYLTSWKLLSNKKMRSDTQWVIDSMNVKTPSHKTTIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDIGAKFEIYQLIQELAKKDKGIIMISSEMPELLGVTDRILVMSNGKVAGIVETANTSQEEILQLAAKYL","517648","","galactoside ABC transporter, ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[156-198]T\"[413-455]TMGLA_HAEIN_P44884;
PF00005\"[45-231]T\"[406-488]TABC_tran
PS50893\"[20-255]T\"[265-512]TABC_TRANSPORTER_2
PS00211\"[413-427]?ABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[44-231]T\"[294-489]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[13-246]T\"[265-503]Tno description
PTHR19222\"[20-317]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF12\"[20-317]TSUGAR ABC TRANSPORTER


","BeTs to 7 clades of COG1129COG name: ABC-type sugar (aldose) transport system, ATPase componentFunctional Class: GThe phylogenetic pattern of COG1129 is -----z--v--lb-efgh---j--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.9e-24) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 34-80 2.5e-14 IPB001140B 410-448 1.4e-05 IPB001140C 465-494 0.26","Residues 156 to 268 match (3e-07) PD:PD535848 which is described as ABC PROTEOME BINDING/ATPASE NUCLEOTIDE COMPLETE TRANSPORTER ","","","","","","","","","","","","Tue Dec 17 12:47:56 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00751 is paralogously related to AA02786 (1e-120), AA00207 (1e-114), AA01456 (1e-107), AA02225 (7e-58), AA00933 (1e-53), AA02140 (4e-26), AA00934 (2e-23), AA02320 (3e-22), AA01645 (2e-19), AA00415 (2e-18), AA00700 (7e-18), AA02718 (3e-17), AA01568 (4e-17), AA02573 (1e-16), AA01524 (1e-16), AA02606 (3e-16), AA01779 (5e-16), AA01051 (1e-15), AA00799 (2e-15), AA02440 (3e-15), AA02353 (1e-14), AA01422 (1e-14), AA00858 (4e-14), AA02484 (5e-14), AA02899 (1e-13), AA01867 (1e-13), AA01656 (1e-13), AA01510 (1e-13), AA01616 (6e-13), AA02550 (7e-13), AA02152 (7e-13), AA01509 (7e-13), AA01393 (1e-12), AA01961 (2e-12), AA02898 (3e-12), AA01824 (5e-12), AA02609 (1e-11), AA02080 (1e-11), AA01820 (2e-11), AA02324 (3e-10), AA02226 (2e-09), AA02331 (2e-09), AA02805 (3e-09), AA01947 (2e-08), AA01684 (7e-08), AA02146 (1e-06), AA01569 (3e-06), AA02642 (4e-06), AA01757 (5e-06), A02145 (1e-05), AA00061 (1e-05), AA00591 (9e-05) and AA01291 (4e-04).","","","","","","Residues 295 to 488 (E-value = 6.4e-17) place AA00751 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Lepine G, Ellen RP.MglA and mglB of Treponema denticola; similarity to ABC transport and spa genes.DNA Seq. 2000;11(5):419-31.PMID: 1132865Baron GS, Nano FE.MglA and MglB are required for the intramacrophage growth of Francisella novicida.Mol Microbiol. 1998 Jul;29(1):247-59.PMID: 9701818","","Wed Feb 5 14:25:36 2003","1","","","" "AA00753","517668","518675","1008","ATGAGTGCTTTAGAAAAAAATAAATCCTTTGATTTTCTGAAACAGAATGCGATTTATTTTGTGTTATTGATTTTACTTGGCATCATCATCGCACAGGATCCGTCATTTCTTAACTTAATGAACTTCAGTAACATTCTTACCCAATCTTCCGTGCGTTTAATCATCGCCCTTGGGGTTGCCGGCTTACTGGTGACACAAGGCACCGACTTATCCGCTGGTCGTCAGGTTGGTTTGGCGGCGGTGATTTCCGCCACTATGTTGCAATCCATGGAAAACATAAACCGCGTGTTCCCGGATTTGGGCGAAATTCCGATTCCGGTAGTCATTCTTGCGGTCTGTGCCGTGGGTGCGGTTATCGGTTTGGTCAACGGCTTAGTTATCGCTTATCTGAACGTGACACCATTTATCGCCACCATGGGCACCATGATCATCGTGTACGGTTTCAACTCCCTCTATTACGATACCGTGGGCGGTTCCCCGATTGCCGGTTTCAGCGAAAACTTCTCCACCTTCGCTCAAGGTTTCTTCCGCATCGGCTCATTTAAACTTTCCTACATCACCATTTACGCCGCCATTTGTGCCTTCCTGGTGTGGGTCATGTGGAATAAAACCCGCTTCGGAAAAAACATCTTCGCCATTGGTGTCAACCCGGAAGCGGCAAAAGTGTCCGGTGTTAATGTAGCGCGTAACCTCGTGGTAATCTACATCATCGCCGGGATGTTCTACGCCTTCGGCGGTATGTTGGAGGCCGGTCGTATCGGCAGTGCGACCAATAACCTCGGCTTCATGTACGAATTAGACGCCATCGCAGCCTGCGTAGTGGGCGGCGTCTCCTTCGCCGGCGGTGTGGGTACGGTTATCGGCGTTATCACCGGGGTGATTATCTTCACCGTCATCAACTACGGCTTAACCTACATCGGCGTCAACCCTTACTGGCAATACATCATCAAAGGTAGCATCATCATCCTTGCCGTTGCCATCGACTCCTTGAAATACGCGAAGAAAAAA","","","35856","MSALEKNKSFDFLKQNAIYFVLLILLGIIIAQDPSFLNLMNFSNILTQSSVRLIIALGVAGLLVTQGTDLSAGRQVGLAAVISATMLQSMENINRVFPDLGEIPIPVVILAVCAVGAVIGLVNGLVIAYLNVTPFIATMGTMIIVYGFNSLYYDTVGGSPIAGFSENFSTFAQGFFRIGSFKLSYITIYAAICAFLVWVMWNKTRFGKNIFAIGVNPEAAKVSGVNVARNLVVIYIIAGMFYAFGGMLEAGRIGSATNNLGFMYELDAIAACVVGGVSFAGGVGTVIGVITGVIIFTVINYGLTYIGVNPYWQYIIKGSIIILAVAIDSLKYAKKK","518677","","galactoside ABC transporter, permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR001851
Family
Bacterial inner-membrane translocator
PF02653\"[41-325]TBPD_transp_2
noIPR
unintegrated
unintegrated
signalp\"[1-31]?signal-peptide
tmhmm\"[15-35]?\"[107-127]?\"[132-152]?\"[183-201]?\"[225-245]?\"[264-284]?\"[289-309]?\"[315-333]?transmembrane_regions


","BeTs to 7 clades of COG1172COG name: Ribose/xylose/arabinose/galactoside ABC-type transport systems, permease componentsFunctional Class: GThe phylogenetic pattern of COG1172 is --------v-rlb-efgh---j--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.8e-12) to 2/2 blocks of the IPB001851 family, which is described as \"Binding-system dependent bacterial transporters (araH, livH/limM families)\". Interpro entry for IP:IPR001851. IPB001851A 206-220 6e-06 IPB001851B 265-276 9.6e-05","Residues 300 to 335 match (3e-10) PD:PD409969 which is described as COMPLETE PROTEOME PERMEASE ABC SUGAR TRANSPORTER TRANSPORTER MEMBRANE SYSTEM PLASMID ","","","","","","","","","","","","Tue Dec 17 13:03:59 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00753 is paralogously related to AA02785 (1e-51), AA01457 (1e-44), AA00208 (8e-44), AA02224 (4e-28), AA02220 (4e-27), AA00936 (1e-26) and AA00935 (3e-12).","","","","","","Residues 41 to 325 (E-value = 1.8e-59) place AA00753 in the BPD_transp_2 family which is described as Branched-chain amino acid transport system / permease component (PF02653)","","","","","Richarme G, Kohiyama M.Purification of the MglC/E membrane proteins of the binding protein-dependent galactose transport system of Salmonella typhimurium.FEBS Lett. 1992 Jun 15;304(2-3):167-9.PMID: 1618318 Richarme G, el Yaagoubi A, Kohiyama M.Reconstitution of the binding protein-dependent galactose transport of Salmonella typhimurium in proteoliposomes.Biochim Biophys Acta. 1992 Feb 17;1104(1):201-6.PMID: 1550848 Rotman B, Guzman R.Identification of the mglA gene product in the beta-methylgalactoside transport systemof Escherichia coli using plasmid DNA deletions generated in vitro.J Biol Chem. 1982 Aug 10;257(15):9030-4.PMID: 6807987","","Tue Dec 17 13:03:59 2002","1","","","" "AA00757","520599","518755","1845","ATGAAAAATCTTAAAGACTTTGTTCGACGCTATGTGGATTGGGTGATCCGTCTCGGGCGCATTCGCTTTTCTTTGCTTGGCGTAATGGTGCTGGCGGTGCTGGCACTTTGTACGCAAATTCTGCTTAGTTTGTTGGTAATGGGGAAAATTCTTTGGGCAGATGTGGCACGCTCCATTGTGTTCGGTTTGATTTCTGCGCCTTTTGTGATTTATTTTTTCACGGTATTGGTGGAAAAACTGGAACACTCCCGTCAGGCGCTTTCGTGTTCCGTAGAAGAGCTGTGCAGAGAAGTTCAAGAGCGGGTATCGGCGGAGAAGAAATTGTCGGAAGCTTTGGATAACCTGGAAAAAATCAACCGCGATAAAACCACCTTGATGACCACCATCAGTCACGAGTTACGCACGCCGTTAAACGGCATTATCGGCTTGAGCCGTATTTTGTTGGAAGAAAATCCCTCCGAACGACAACAAAATTATCTTAAAACTATCAACAGCAGTACCCTTTCTCTCGCCCATATTTTTAGTGACATCATTGATTTAGAAAAAATTGATGCGAAACGTATTGAACTCAATCGTAAAGCCACGGATTTATACGCGTTGCTCAATGACATTGCCAATTTCGCGTTATTAATGACGGAAGAAAAGCATTTGCAATTTCAATTGGTTTGCCCGCCGACGCTACCTAATTGGCTGATGTTGGACGGCGTGCGGTTAAACCAAGTGCTGTGGAATTTAATCAATAACGCGGTGAAATTCACTCAACAGGGCAGCGTTACCTTATCTGTGGAGCAGACAGCAGAGGAAGAATTTGCGTTGCGCGTAACAGATACCGGTATCGGTATTGTCGAGCAGGATTTGCAGAAGATTTTTGAACTATATTATCAAGCGGGTTCTGATGCTAATAAATCCTTAGGCAGCGGCATCGGGTTGTCCGTGTCAAAAACCATTGCACAACTGATGGGTGGCGATTTAACCGTCAGTAGCGAAGTGGGCAAGGGTTCGACCTTCTTATTTACGTTCAAAGCCCGACAAGCTATCAAGCCGGTAGAAGAAGATGAACATTTGCCGCTAAAACTAAACATTCTTTTGGTAGAAGATATTGAAGTGAATGTGGTGGTGGCGAAATCTATGTTGGAGAAATTGGGTTATCAAATTGATATCGCCATGACCGGCGCCGAAGCCATTCGCAAATTTGAACAAAATTACTACGATCTGGTGTTTCTGGATATTCAGCTGCCCGATATGTCAGGCTTTGATATTGCCGCCCACTTCCGCCAAAACTACGAAAACGGCGTTTATGATTTTCTCCCGCCGCTTATTGCGCTGACGGCAAATGTGGTGCAGAAAAAACAGGAATATCTGGCGCAAGGCATGGACGATGTGATTCATAAGCCGCTCTCTTTAGAGGAACTGAGACATTGCCTGCATGATTATTTCGGCGAAGAACTGACTCAATTCAACCTGCCGAGCAATAAACCGCAAGCGGAATCTGTGGAGTTGGATACGAAAATGCTCACGGAGTTGGTGGAAATGCTGGGGGCGGATTTCGTGAAAAACAATCTCATTTTATTCGAGCAAACCATGCAGGATTATGTCGCCGAGCTACAACAGGCTTATCAGGCGTATTTGAACGATCCGCACACTCAACCGGAGGTGCTATCCATCGTGCATAAAATCAAAGGCGCACTGGCTTCCGTGGGGTTAAAACGCTTACAATGGATTGCCGCGCAGGCACAGAATGCCGACACGGCAGACTGGCAGGGCAATATCGCTCATTGGGTGAATTTGCTGGCAAAAGAATGGCAAACCGATGTAGCGAAATTACGGGAGTGGTTGGCAGGTTAT","","","70125","MKNLKDFVRRYVDWVIRLGRIRFSLLGVMVLAVLALCTQILLSLLVMGKILWADVARSIVFGLISAPFVIYFFTVLVEKLEHSRQALSCSVEELCREVQERVSAEKKLSEALDNLEKINRDKTTLMTTISHELRTPLNGIIGLSRILLEENPSERQQNYLKTINSSTLSLAHIFSDIIDLEKIDAKRIELNRKATDLYALLNDIANFALLMTEEKHLQFQLVCPPTLPNWLMLDGVRLNQVLWNLINNAVKFTQQGSVTLSVEQTAEEEFALRVTDTGIGIVEQDLQKIFELYYQAGSDANKSLGSGIGLSVSKTIAQLMGGDLTVSSEVGKGSTFLFTFKARQAIKPVEEDEHLPLKLNILLVEDIEVNVVVAKSMLEKLGYQIDIAMTGAEAIRKFEQNYYDLVFLDIQLPDMSGFDIAAHFRQNYENGVYDFLPPLIALTANVVQKKQEYLAQGMDDVIHKPLSLEELRHCLHDYFGEELTQFNLPSNKPQAESVELDTKMLTELVEMLGADFVKNNLILFEQTMQDYVAELQQAYQAYLNDPHTQPEVLSIVHKIKGALASVGLKRLQWIAAQAQNADTADWQGNIAHWVNLLAKEWQTDVAKLREWLAGY","518757","","aerobic respiration sensor-response protein","Inner membrane, Cytoplasm","","
InterPro
IPR001789
Domain
Response regulator receiver
PD000039\"[360-471]TQ9CNW0_PASMU_Q9CNW0;
PF00072\"[359-476]TResponse_reg
SM00448\"[359-475]TREC
PS50110\"[360-479]TRESPONSE_REGULATORY
InterPro
IPR003594
Domain
ATP-binding region, ATPase-like
G3DSA:3.30.565.10\"[182-341]Tno description
PF02518\"[233-343]THATPase_c
SM00387\"[233-344]THATPase_c
InterPro
IPR003661
Domain
Histidine kinase A, N-terminal
PF00512\"[121-186]THisKA
SM00388\"[121-186]THisKA
InterPro
IPR004358
Domain
Histidine kinase related protein, C-terminal
PR00344\"[270-284]T\"[288-298]T\"[304-322]T\"[328-341]TBCTRLSENSOR
InterPro
IPR005467
Domain
Histidine kinase
PS50109\"[128-344]THIS_KIN
InterPro
IPR008207
Domain
Hpt
PF01627\"[519-611]THpt
SM00073\"[509-612]THPT
PS50894\"[513-611]THPT
noIPR
unintegrated
unintegrated
G3DSA:1.20.120.160\"[489-612]Tno description
G3DSA:3.40.50.2300\"[358-488]Tno description
PTHR23283\"[95-484]TSENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF49\"[95-484]TTWO-COMPONENT SENSOR PROTEIN HISTIDINE PROTEIN KINASE (DHKK, DHKJ)
signalp\"[1-35]?signal-peptide
tmhmm\"[21-41]?transmembrane_regions


","BeTs to 17 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: TThe phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 2.8e-13) to 4/4 blocks of the PR00344 family, which is described as \"Bacterial sensor protein C-terminal signature\". Prints database entry for PR:PR00344. PR00344A 270-284 0.07 PR00344B 288-298 38 PR00344C 304-322 7.8e-05 PR00344D 328-341 0.12Significant hit ( 2e-12) to 3/3 blocks of the IPB003661 family, which is described as \"His Kinase A domain\". Interpro entry for IP:IPR003661. IPB003661A 129-138 6.1e-05 IPB003661B 244-253 0.0037 IPB003661C 274-282 1.3Significant hit ( 2.3e-09) to 2/4 blocks of the IPB001867 family, which is described as \"Transcriptional regulatory protein, C terminal\". Interpro entry for IP:IPR001867. IPB001867A 404-417 2.4e-05 IPB001867B 437-481 0.034Significant hit ( 6.4e-09) to 2/3 blocks of the IPB001789 family, which is described as \"Response regulator receiver domain\". Interpro entry for IP:IPR001789. IPB001789B 404-417 2e-06 IPB001789C 457-466 1.2Significant hit ( 3.5e-07) to 2/12 blocks of the IPB001294 family, which is described as \"Phytochrome\". Interpro entry for IP:IPR001294. IPB001294K 107-158 0.13 IPB001294L 306-337 0.0011","Residues 272 to 341 match (3e-07) PD:PD033548 which is described as RECEPTOR ETHYLENE TRANSDUCTION SENSORY PHOSPHORYLATION HOMOLOG KINASE COMPLETE 2.7.3.- ETR1 ","","","","","","","","","","","","Tue Feb 4 15:35:05 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00757 is paralogously related to AA00995 (3e-13), AA02284 (9e-13), AA01843 (1e-09), AA01837 (5e-08), AA00997 (5e-08) and AA02902 (2e-05).","","","","","","Residues 359 to 482 (E-value = 7.2e-24) place AA00757 in the Response_reg family which is described as Response regulator receiver domain (PF00072)","","","","","Kwon,O., Georgellis,D. and Lin,E.C. Phosphorelay as the sole physiological route of signal transmission by the arc two-component system of Escherichia coli J. Bacteriol. 182 (13), 3858-3862 (2000) PubMed: 10851007 Kato,M., Mizuno,T., Shimizu,T. and Hakoshima,T. Refined structure of the histidine-containing-phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB from Escherichia coli at 1.57-A resolution Acta Crystallogr. D 55, 1842-1849 (1999)Kato,M., Mizuno,T. and Hakoshima,T. Crystallization of a complex between a novel C-terminal transmitter, HPt domain, of the anaerobic sensor kinase ArcB and the chemotaxis response regulator CheY Acta Crystallogr. D 54, 140-142 (1998) Georgellis,D., Kwon,O., De Wulf,P. and Lin,E.C. Signal decay through a reverse phosphorelay in the Arc two-component signal transduction system J. Biol. Chem. 273 (49), 32864-32869 (1998) PubMed: 9830034 ","","Tue Dec 17 13:10:01 2002","1","","","" "AA00758","520625","520756","132","ATGAGTATTGTACCCTACAGAAAATACGCGGAGAAGTTTTGCCCAGACAAAAAAGTGCGGTCGAAAAACACAATGAATTTCGACCGCACTTTAAGAGAAAAATTACCCCGAGAGATTAACCGTTGTAACGTT","","","5359","MSIVPYRKYAEKFCPDKKVRSKNTMNFDRTLREKLPREINRCNV","520756","","hypothetical protein","Cytoplasm, Periplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 11:28:24 2004","Mon Feb 23 11:34:01 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00758 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 11:26:12 2004","","","","","","","","","","","","","1","","","" "AA00759","521960","520743","1218","ATGAAAAGAGTCGTAATTACCGGATTTGGTATCATTTCGAGTATTGGTAACAATAAAGAAGAAGTATTGGCTTCGTTAAAAGCCGGTAAATCCGGTATTGAAGTGGTTCCCGAATTTATCGAAATGAAAATGCGCAGCCATGTGGCGGGCACCGTTAAACTTAATCCGAGCGAATTAATTGATCGTAAAATTTATCGTTTCATGGGCGATGCTGCCGCCTATGCGTATCTTTCTATGAAAGAAGCCATCGAAGATGCCGGCTTAACGGAAGATCAAGTCTCCAACGAGCGCTCCGGTTTGGTGATCGGCGCAGGCACGGGTTCCGCCCATAACCAATTAATTGCTTGTGACGCCGTACGCGGTCCGCGCGGCGTGAAAGCTATCGGTCCTTATGCAGTAACCAAAACCATGGCGTCCAGCGTGTCCGCCTGTTTGGCAACCCCGTACAAAATCAAAGGTGTGAGTTACAGTATCAGCTCCGCGTGCGCCACTTCCGCACACTGTATCGGTAACGCTTACGAATTAATTCAATTAGGCAAGCAAGACATCGTTTTCGCCGGTGGAGCGGAGGAGCTGTCTTGGGAATGTGCCACTGAATTCGACGCCATGGGCGCTGTTTCCACCAAATACAACGACACCCCGACCAAAGCGTCCCGTGCCTACGATGCCAACCGTGACGGCTTCGTGATTGCCGGCGGCGGTGCAGTCGTGGTGGTGGAAGAATTGGAACACGCGTTAGCGCGCGGTGCGAAAATTTATGCGGAAATCGTGGGCTATGGCGCCACTTCCGATGGCTATGACATGGTGGCACCGAGCGGTGAAGGCGCAGAGCGCTGTATGAAACAAGCGATGGCAGGTTTGGATGCGCCTATTGATTACATCAACGTACATGGTACCTCCACCCCGGTGGGTGATGTGAAAGAATTGGGCGCGATTAAAAATGTGTTCGGCGATAAAATCCCGGCAATTTCTTCCACCAAATCCATGACCGGTCACTCTTTAGGCGCAGCTGGCGCGCATGAAGCCATTTATACTTTGTTAATGTTACACAATGATTTCATCGCCCCAAGCATTAACATTGAGACTCTGGACGAACAGGCGCAAGGTTGTAACATCGTCACTGAAACCGTTGAAAACGCCGGTTTGCAGACTGTGATGTCTAACAGCTTCGGCTTCGGTGGTACTAACGCCAGCCTCGTGTTCAAACGTTACAACGGT","","","42515","MKRVVITGFGIISSIGNNKEEVLASLKAGKSGIEVVPEFIEMKMRSHVAGTVKLNPSELIDRKIYRFMGDAAAYAYLSMKEAIEDAGLTEDQVSNERSGLVIGAGTGSAHNQLIACDAVRGPRGVKAIGPYAVTKTMASSVSACLATPYKIKGVSYSISSACATSAHCIGNAYELIQLGKQDIVFAGGAEELSWECATEFDAMGAVSTKYNDTPTKASRAYDANRDGFVIAGGGAVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVAPSGEGAERCMKQAMAGLDAPIDYINVHGTSTPVGDVKELGAIKNVFGDKIPAISSTKSMTGHSLGAAGAHEAIYTLLMLHNDFIAPSINIETLDEQAQGCNIVTETVENAGLQTVMSNSFGFGGTNASLVFKRYNG","520745","","3-oxoacyl-[acyl-carrier-protein] synthase I","Cytoplasm","","
InterPro
IPR000794
Domain
Beta-ketoacyl synthase
PTHR11712\"[2-406]TPOLYKETIDE SYNTHASE-RELATED
InterPro
IPR014030
Domain
Beta-ketoacyl synthase, N-terminal
PF00109\"[2-245]Tketoacyl-synt
PS00606\"[153-169]TB_KETOACYL_SYNTHASE
InterPro
IPR014031
Domain
Beta-ketoacyl synthase, C-terminal
PF02801\"[253-361]TKetoacyl-synt_C
noIPR
unintegrated
unintegrated
G3DSA:3.40.47.10\"[6-258]T\"[259-406]Tno description
PTHR11712:SF23\"[2-406]T3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE


","BeTs to 17 clades of COG0304COG name: 3-oxoacyl-(acyl-carrier-protein) synthaseFunctional Class: I,QThe phylogenetic pattern of COG0304 is ------yqvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-13) to 2/3 blocks of the IPB000794 family, which is described as \"Beta-ketoacyl synthase\". Interpro entry for IP:IPR000794. IPB000794B 217-229 3e-06 IPB000794C 327-336 1.1e-05","Residues 153 to 400 match (4e-07) PD:PD299528 which is described as NONJ NONK ","","","","","","","","","","","","Tue Dec 17 13:11:42 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00759 is paralogously related to AA01177 (4e-61) and AA01182 (2e-27).","","","","","","Residues 253 to 405 (E-value = 5.8e-62) place AA00759 in the Ketoacyl-synt_C family which is described as Beta-ketoacyl synthase, C-terminal domain (PF02801)","","","","","Olsen,J.G., Kadziola,A., von Wettstein-Knowles,P., Siggaard-Andersen,M., Lindquist,Y. and Larsen,S. The X-ray crystal structure of beta-ketoacyl [acyl carrier protein]synthase I FEBS Lett. 460 (1), 46-52 (1999) PubMed: 10571059 Jackowski S, Zhang YM, Price AC, White SW, Rock CO. A missense mutation in the fabB (beta-ketoacyl-acyl carrier proteinsynthase I) gene confers tiolactomycin resistance to Escherichia coli. Antimicrob Agents Chemother. 2002 May;46(5):1246-52. PMID: 11959552 ","","Tue Dec 17 13:11:42 2002","1","","","" "AA00760","522130","523875","1746","ATGCGCGTTATTACTCACGCCGACATCACATTCAACCAAGAAAACACGCCCGTTTCCAATCAATTTGATGACGTCTATTTTTCCAATCAGGACGGTTTAGAAGAAAGTCGCCATGTTTTTCAACAGGGCAACCAATTATGGCAGCGCTGGCAAAGTCATGAGCCGGCGCATTTCGTCATTGCGGAAACCGGCTTCGGCACAGGGCTGAATTTCTTTGCCGTCACAATGCTTTTCCGGGAATTTCGTCAGCAATTTCCGCAAGCAAAATTACGACGCTTATTTTTCCTTTCCTTTGAAAAATACCCGCTGACCTCGGAAGCCCTGAAACGCGCCCATCAGCATTACCCACAATTTTTCGCCCTCGCCGAACAATTACAGGCGTATTGGTTGGAACCCATTGAAGGCTGCTATCGTTTTCATTTTGAAGAAACTACCCTTGATTTATGGTTCGGTGATATTCACACCAATTTGCCGCAACTCGGCGATTATATGCGGGAGAAAATCGACGCTTGGTTTTTAGACGGTTTCGCGCCGAGCAAAAATCCCGAAATGTGGAACGACGGACTGTACGCGCAAATGTATCGCTACACCAAATCGCACGGCACCTTCGCCACCTTCACCGCAGCAAGCGCGGTGCGCAAAGGCCTGGAAAATGCGGGATTCAGCGTGCAAAAACGCAAAGGCTTCGGCAAAAAACGGGAATGTTTGGCGGGTGAAAAAACGTTTATAAAACCCACCGCACTTTTCACCCCCTGGTATCTTCCGCAAGCGGCACAATTTCAAGAAAAAGCCGATGTCGCCATTATCGGCGGAGGCGTGGCGTCGGTGTTTACCGCTCTTTCCCTCATTCAACGAGGCACCAAGGTCACCTTGTATTGCGAAGATCCGCAACCGGCGATGAACGCTTCCGGCAACAAACAAGGCGCTTTTTATCCGCAACTCAGCGACGATGACGAACGCAACATTCGCTTTTACATTCACGCCTTTGCTTACGGCTTACAACTGTTACACGAAGCGGAAAAACACATCGACTTTGAACATGAATTTTGCGGCGTGGCATTGTGCGGCTATAACGAAAAAAGTGCGGTCAAATTACATCACATTTCGCAATATCACTTGCCCACCGATCTTTATCAAGCCTTAACGCAGGCGGAATTAAGCGAAAAAGTCGGTTTGCCGTTGCCTTGTGGCGGCGGATTTATCCCCCAAGGGGCATGGCTTGCGCCACAGCAACTGGTGCAAAATCTTTTTGCGCACTTACAACAACAGGGCTTGATCTTAAAAACGCAGGAAAAAATGACCGCACTTTCATGGCTGGGCGACCACTGGCAGCTCACCAATGAACAAGGCGAACGCTTTCAACATCAAATTGTGGTGCTGGCGAACGGACATCAGCTCCCTCAGTTCCCGCAAACGCAGCATTTGCCGCTCTATGCCGTGCGCGGTCAGGTCAGCAAAATTCCTACCTCAGAAAATTTGTTGAAACTGAAATCCGTGCTCTGCTACGACGGCTATCTCACGCCTGCGGATCAAGCAAAAACCAGCCATTGCATCGGTGCCAGCCATGTGCGCGATTGCGCCGATCGTCGCTTTAGCGAACGGGAACAACAGGAAAATCAGGCAAAAAATCCAAAGAAACTTAGCCGAAATGCCTTGGGTAAACGATGTGGACACTTCCGCCAATCTGGCGCGAATCGGCGTGCGCTGTGCCGTACGGGATCGTATTCCGATGATGGGAAATGTGCC","","","66373","MRVITHADITFNQENTPVSNQFDDVYFSNQDGLEESRHVFQQGNQLWQRWQSHEPAHFVIAETGFGTGLNFFAVTMLFREFRQQFPQAKLRRLFFLSFEKYPLTSEALKRAHQHYPQFFALAEQLQAYWLEPIEGCYRFHFEETTLDLWFGDIHTNLPQLGDYMREKIDAWFLDGFAPSKNPEMWNDGLYAQMYRYTKSHGTFATFTAASAVRKGLENAGFSVQKRKGFGKKRECLAGEKTFIKPTALFTPWYLPQAAQFQEKADVAIIGGGVASVFTALSLIQRGTKVTLYCEDPQPAMNASGNKQGAFYPQLSDDDERNIRFYIHAFAYGLQLLHEAEKHIDFEHEFCGVALCGYNEKSAVKLHHISQYHLPTDLYQALTQAELSEKVGLPLPCGGGFIPQGAWLAPQQLVQNLFAHLQQQGLILKTQEKMTALSWLGDHWQLTNEQGERFQHQIVVLANGHQLPQFPQTQHLPLYAVRGQVSKIPTSENLLKLKSVLCYDGYLTPADQAKTSHCIGASHVRDCADRRFSEREQQENQAKNPKKLSRNALGKRCGHFRQSGANRRALCRTGSYSDDGKCA","523877","","conserved hypothetical protein (possible peptidase)","Cytoplasm","","
InterPro
IPR006076
Family
FAD dependent oxidoreductase
PF01266\"[265-522]TDAO
InterPro
IPR008471
Family
Protein of unknown function DUF752
PF05430\"[8-241]TDUF752
noIPR
unintegrated
unintegrated
G3DSA:3.50.50.60\"[260-477]Tno description


","No hits to the COGs database.","","Residues 251 to 300 match (1e-10) PD:PD565375 which is described as COMPLETE PROTEOME PEPTIDASE TRANSMEMBRANE YPO2756 YFCK HI1535 STY2610 VC2110 ","","","","","","","","","","","","Wed Feb 19 15:16:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00760 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 241 (E-value = 1.2e-134) place AA00760 in the DUF752 family which is described as Protein of unknown function (DUF752) (PF05430)","","","","","","","","1","","","" "AA00761","523694","524146","453","ATGTGCGCGATTGCGCCGATCGTCGCTTTAGCGAACGGGAACAACAGGAAAATCAGGCAAAAAATCCAAAGAAACTTAGCCGAAATGCCTTGGGTAAACGATGTGGACACTTCCGCCAATCTGGCGCGAATCGGCGTGCGCTGTGCCGTACGGGATCGTATTCCGATGATGGGAAATGTGCCTGACTTTGATCGCCAATGTGCGGATTACAAAAATCTGTTTAACCTCCGCCGCCGCAAACAATCCATTCCGCCTGCCGCCCACTATCCGAATCTCTATTTAATCGGCGCCCTCGGCTCACGTGGCTTAACCTCCGCTCCGATATTGGGCGAAACCTTAGCGTCATTGATTCACAACGAACCACTCCTGCTGAGTGAAGACTTAATTCACCACCTATCAGCAAGTCGCAGCTGGATACGTAAGCTGCTGAAGGGAACGTCCATTGAAAATCTA","","","17098","MCAIAPIVALANGNNRKIRQKIQRNLAEMPWVNDVDTSANLARIGVRCAVRDRIPMMGNVPDFDRQCADYKNLFNLRRRKQSIPPAAHYPNLYLIGALGSRGLTSAPILGETLASLIHNEPLLLSEDLIHHLSASRSWIRKLLKGTSIENL","524148","","conserved hypothetical protein (possible peptidase)","Periplasm, Inner membrane","","
InterPro
IPR006076
Family
FAD dependent oxidoreductase
PF01266\"[42-116]TDAO


","BeTs to 7 clades of COG0665COG name: Glycine/D-amino acid oxidases (deaminating)Functional Class: EThe phylogenetic pattern of COG0665 is ao-pkzyq--rlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is","","Residues 35 to 149 match (6e-41) PD:PD030924 which is described as COMPLETE PROTEOME PEPTIDASE FLAVOPROTEIN FAD OXIDOREDUCTASE PM0338 YFCK HI1536 STY2610 ","","","","","","","","","","","","Tue Dec 17 13:22:51 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00761 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00762","524339","525073","735","ATGAGCAAATTAAAATTAGGCTACCTCTCCTCTCATATTATTTTCCTTGCTTTAAGCGTTTCCACTGCCTACGCCGAAAACGACACACAGGAAAAATTAAATGAAATTGTGGTTTCAGGCAGCAGTGAAGGCAATGGAAATTCTGATGATAGAACCCCGCCCAAAATCGGTGAAACGGTTAAAAGTGCGAAAAAATTAGAGAAGCAACAAGCTCAAGATGTAAAAGATTTAGTTCGTTATGACACCGGTGTAACGGTAGTCGAAGCGGGGCGTTTCGGTAATAGCGGCTTTGCTGTGCGTGGTGTGGAGGAAAATCGGGTTGCGATTCAAATTGACGGACTGGCACAAGCAGAAACCATCTCATCACAAGGTTTTAAAGAATTATTTGAAGGTTACGGTAATTTTAATAATACACGTAATAGTGCAGAAATTGAGACACTAAAACAAGTTACGATCCGAAAAGGTGCTGATTCTTTAAAATCAGGTAGTGGCGCATTAGGTGGTTCGGTCAGTTTTGAAACCAAGGATGCACGCGACTATTTGACCGATAAAAACTATTATGCTTCCTACAAGCGGGGCTACAACACAGCAGATAACCAAAATCTCAATACACTAACGCTTGCCGGTCGCTATAAATATTTTGACGCAATTGCTGTTCTTACATCACGCAAAGGACATGAATTAGAGAATTTTGGTTACAAAAACTACAACGAGAGAGTTCAGGGAAAAACCAGA","","","26933","MSKLKLGYLSSHIIFLALSVSTAYAENDTQEKLNEIVVSGSSEGNGNSDDRTPPKIGETVKSAKKLEKQQAQDVKDLVRYDTGVTVVEAGRFGNSGFAVRGVEENRVAIQIDGLAQAETISSQGFKELFEGYGNFNNTRNSAEIETLKQVTIRKGADSLKSGSGALGGSVSFETKDARDYLTDKNYYASYKRGYNTADNQNLNTLTLAGRYKYFDAIAVLTSRKGHELENFGYKNYNERVQGKTR","525075","","hemoglobin binding protein A","Outer membrane, Extracellular","","
InterPro
IPR012910
Domain
TonB-dependent receptor, plug
PF07715\"[50-169]TPlug
noIPR
unintegrated
unintegrated
G3DSA:2.170.130.10\"[59-180]Tno description
signalp\"[1-25]?signal-peptide


","BeTs to 6 clades of COG1629COG name: Outer membrane receptor proteins, mostly Fe transportFunctional Class: PThe phylogenetic pattern of COG1629 is -------q-----cefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 7.9e-12) to 2/3 blocks of the IPB000531 family, which is described as \"TonB-dependent receptor protein\". Interpro entry for IP:IPR000531. IPB000531A 100-113 0.0036 IPB000531B 162-179 7.1e-07","Residues 27 to 91 match (5e-20) PD:PD003117 which is described as BINDING A RECEPTOR SIGNAL PRECURSOR MEMBRANE OUTER BOX TONB HEMOGLOBIN ","","","","","","","","","","","","Tue Dec 17 13:26:35 2002","","Thu Mar 18 09:20:38 2004","Thu Mar 18 09:20:38 2004","Thu Mar 18 09:20:38 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00762 is paralogously related to AA02202 (3e-21), AA02782 (3e-06), AA02157 (3e-06), AA02865 (8e-06) and AA02151 (2e-05).","Thu Mar 18 09:20:38 2004","","","","","","","",""," Haraszthy VI, Jordan SF, Zambon JJ.,Identification of Fur-regulated genes in Actinobacillus actinomycetemcomitans.Microbiology. 2006 Mar;152(Pt 3):787-96.PMID: 16514158Hayashida,H., Poulsen,K. and Kilian,M.Differences in iron acquisition from human haemoglobin amongstrains of Actinobacillus actinomycetemcomitansMicrobiology 148 (Pt 12), 3993-4001 (2002)PUBMED: 12480903","Ren Z, Jin H, Whitby PW, Morton DJ, Stull TL.Role of CCAA nucleotide repeats in regulation of hemoglobin and hemoglobin-haptoglobin binding protein genes of Haemophilusinfluenzae.J Bacteriol. 1999 Sep;181(18):5865-70.PMID: 10482534 Morton DJ, Stull TL.Distribution of a family of Haemophilus influenzae genes containing CCAA nucleotide repeating units.FEMS Microbiol Lett. 1999 May 15;174(2):303-9.PMID: 10339823 Morton DJ, Whitby PW, Jin H, Ren Z, Stull TL.Effect of multiple mutations in the hemoglobin- and hemoglobin-haptoglobin-binding proteins, HgpA, HgpB, and HgpC, ofHaemophilus influenzae type b.Infect Immun. 1999 Jun;67(6):2729-39.PMID: 10338475 Jin,H., Ren,Z., Whitby,P.W., Morton,D.J. and Stull,T.L.Characterization of hgpA, a gene encoding ahaemoglobin/haemoglobin-haptoglobin-binding protein of HaemophilusinfluenzaeMicrobiology 145 (Pt 4), 905-914 (1999)PubMed: 10220170","Tue Dec 17 13:26:35 2002","Mon Feb 17 13:35:30 2003","1","","","" "AA00763","525116","526897","1782","TTGAAATTTGCATTTCAACCAACAGATAACCACCGCTTCTCCGTTATGGCAGATTTATATAAGCAAACCTCTAAAGGACATGATTTTTCTTACACATTAAAGCCAAATACTCAATTTAGAACCTATGACGAGGAAGAGTTACGTCACACCAATGATAAAGTAGAACATAAAAATTTCGCCTTTACCTATGAAAACTTCACAACAACACCGCTTTGGGATACATTGAAAATCACCTATTCCCAACAAAAAATTACAACCCGAGCAAGAACAGATGATTATTGTGATGGAAATGATAAGTGCCCTACCTCACAAAATAAGTTAGGTATGAAATATAATGAGGATAATAAACTTGTCGGTAATGATAATAAATTAGCCAAATATACAAATACTCCGGCACAAACAAAAACAATAAAAGAGCAAGTCCCTTTAGATCCAAGTAGCACTGCAAAATACCGGTGGCAAAAAGCACAATGGCATGTGCTGGAACAAAAATATCCGGGGGTAAAATATTCTAAATACTGTGAAGAAGATGAAACAGATCCGAGTAATTTCTGTACTGTTGAACTAAAAATCCCCGGAGCCCCGGCTAAAAAATCCTTTGAAATAAATGGAAAAGAATACGATTTAAAATCGGAAGAGGTTATTGGTGATGAACAAACTCTGACAACAAATACTTCACATATATTAAGCTGTGATGCTATAAACTGTAATAAAAAAACGATTGGGGGTTTTCAACGTGATGGAACACCGGTTGATATTCCATTCGAAGTTTTTGAACGTGATGGTAAAAAATATGCCAAAACTAAAGTAATGAGTAAGGATCAATTAAGCGGTCCGGTATTTTTCATGCCAAATAAATCCGGCTATCAAGAAAACTTATGGACTCAGCGTGATCTTACAACCAAAACAAAGCAGATCAATATTGATTTAACAAAGCATATTGAAATCTCCGGTACAGAACATGATCTGTCCTATGGTGGGCTATGGGCAGAATCTAAAAAAGAAATGATAAATATTTCAGGCATCAGTGCTAGAAATATAAAGTGGTGGGCTCAGTATCCTAAAGATTGTTCACCTTCAATAAATAATCCGGATCGCTACAACGCACTTTGCAATAGAAAGAATGTTTATTCTTTCCTAATTCCTGTGAAAACTAAAACAGGCGCACTGTACTTTATTGACGATTTCAAATTAAATGATTACTTCAGTTTCGGTATCGGTTACCGTTATGACCGTGTGAAATATAATCCGGAATATATCCCCGGCGTCACCCCCAAAATTCCTGATGATCTGGTAACTAATCTGTATATAACAGATCCAAAGTTTGATCCATCCGATTTAATATCTCCTGAAAATCAGGCAAGACGGGAAGCTAACGCAAACGCGAATATTAAAAAAATTGCGCAGCCGAAAAAGTTCTCTGCCAGCTCATATTCATTGAATACGACGGTAGATCCACTAGATTGGTTACGTTTGCAGGCGAAATATAGCAAAGCATTCCGGGCACCAACCGGTGATGAGATTTATTTTACCTTTAAACACCCTGATTTCTCTGTATTACCCAATAAGGATCTTGAGCAAGAAACAGCAAAAACGAAAGAATTGTCTGTAACCTTACATAATGATATGGGTTATATTTCTACGTCTGTATTTGAGACCCGGTATAATAACTTCATTGATTTGGTATACAAAGGCAACAAACAACTACAAGGGCATTCCAAGTTACGCCCGTTTAATGTATATCAAAATATAAACAGACCCAATGCAAAAGTAACGGGTTTT","","","68591","LKFAFQPTDNHRFSVMADLYKQTSKGHDFSYTLKPNTQFRTYDEEELRHTNDKVEHKNFAFTYENFTTTPLWDTLKITYSQQKITTRARTDDYCDGNDKCPTSQNKLGMKYNEDNKLVGNDNKLAKYTNTPAQTKTIKEQVPLDPSSTAKYRWQKAQWHVLEQKYPGVKYSKYCEEDETDPSNFCTVELKIPGAPAKKSFEINGKEYDLKSEEVIGDEQTLTTNTSHILSCDAINCNKKTIGGFQRDGTPVDIPFEVFERDGKKYAKTKVMSKDQLSGPVFFMPNKSGYQENLWTQRDLTTKTKQINIDLTKHIEISGTEHDLSYGGLWAESKKEMINISGISARNIKWWAQYPKDCSPSINNPDRYNALCNRKNVYSFLIPVKTKTGALYFIDDFKLNDYFSFGIGYRYDRVKYNPEYIPGVTPKIPDDLVTNLYITDPKFDPSDLISPENQARREANANANIKKIAQPKKFSASSYSLNTTVDPLDWLRLQAKYSKAFRAPTGDEIYFTFKHPDFSVLPNKDLEQETAKTKELSVTLHNDMGYISTSVFETRYNNFIDLVYKGNKQLQGHSKLRPFNVYQNINRPNAKVTGF","526899","","hemoglobin binding protein A","Outer membrane, Periplasm","","
InterPro
IPR000531
Domain
TonB-dependent receptor
PF00593\"[477-565]TTonB_dep_Rec
noIPR
unintegrated
unintegrated
G3DSA:2.40.170.20\"[265-594]Tno description


","BeTs to 7 clades of COG1629COG name: Outer membrane receptor proteins, mostly Fe transportFunctional Class: PThe phylogenetic pattern of COG1629 is -------q-----cefghsnuj----Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Tue Dec 17 14:26:37 2002","","Thu Aug 4 11:28:50 2005","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00763 is paralogously related to AA02201 (0.001).","Thu Mar 18 09:23:08 2004","","","","","","","",""," Haraszthy VI, Jordan SF, Zambon JJ.,Identification of Fur-regulated genes in Actinobacillus actinomycetemcomitans.Microbiology. 2006 Mar;152(Pt 3):787-96.PMID: 16514158Hayashida,H., Poulsen,K. and Kilian,M.Differences in iron acquisition from human haemoglobin amongstrains of Actinobacillus actinomycetemcomitansMicrobiology 148 (Pt 12), 3993-4001 (2002)PMID: 12480903Bahrami F, Niven DF.Iron acquisition by Actinobacillus suis: Identification and characterization of a single-component haemoglobin receptor and encoding gene.Microb Pathog. 39(1-2):45-51.PMID: 15899574","Ren Z, Jin H, Whitby PW, Morton DJ, Stull TL. Role of CCAA nucleotide repeats in regulation of hemoglobin and hemoglobin-haptoglobin binding protein genesof Haemophilus influenzae. J Bacteriol. 1999 Sep;181(18):5865-70. PMID: 10482534 Morton DJ, Stull TL. Distribution of a family of Haemophilus influenzae genes containing CCAA nucleotide repeating units. FEMS Microbiol Lett. 1999 May 15;174(2):303-9. PMID: 10339823 Morton DJ, Whitby PW, Jin H, Ren Z, Stull TL. Effect of multiple mutations in the hemoglobin- and hemoglobin-haptoglobin-binding proteins, HgpA, HgpB, andHgpC, of Haemophilus influenzae type b. Infect Immun. 1999 Jun;67(6):2729-39. PMID: 10338475 Jin,H., Ren,Z., Whitby,P.W., Morton,D.J. and Stull,T.L. Characterization of hgpA, a gene encoding a haemoglobin/haemoglobin-haptoglobin-binding protein of Haemophilus influenzae Microbiology 145 (Pt 4), 905-914 (1999) PubMed: 10220170","Thu Aug 4 11:28:50 2005","Mon Feb 17 13:38:17 2003","1","","","" "AA00764","526988","527407","420","ATGGATGGCGATATTCCGATGAACGCAATTCAGCCCAGAACTGCTGTTTATGGTATAGGTTATGTTCATTCTGATGATAAATTCGGTTTAGATCTGTATATAACTCATGCCGGTGCAAAACAAGCTAAAGATACTTACAATATGTACCACAAAGAGGAAGGAAAAAAAGACAGCTCCATCAAATGGCGTAGTAATTCTTATACAACGATTGATTTACTTGGTTACATTAAGCCAATCAAAAATTTAACTTTAAGAGCCGGAGTATATAATCTCACAAACAGAAAATATATTACTTGGGATTCTGCGAGATCAATCCGCCCATTTGGTACAAGTAATCTGATTGACCAAAAGAGTGGATTGGGTATCAACCGCTTCAACGCACCGGGTCGTAATTATAGACTTTCAATGCAACTTGAATTC","","","15958","MDGDIPMNAIQPRTAVYGIGYVHSDDKFGLDLYITHAGAKQAKDTYNMYHKEEGKKDSSIKWRSNSYTTIDLLGYIKPIKNLTLRAGVYNLTNRKYITWDSARSIRPFGTSNLIDQKSGLGINRFNAPGRNYRLSMQLEF","527409","","hemoglobin binding protein A","Outer membrane, Extracellular","","
InterPro
IPR000531
Domain
TonB-dependent receptor
PF00593\"[8-140]TTonB_dep_Rec
InterPro
IPR010917
Domain
TonB-dependent receptor, C-terminal
PS01156\"[123-140]TTONB_DEPENDENT_REC_2
noIPR
unintegrated
unintegrated
G3DSA:2.40.170.20\"[2-140]Tno description


","BeTs to 7 clades of COG1629COG name: Outer membrane receptor proteins, mostly Fe transportFunctional Class: PThe phylogenetic pattern of COG1629 is -------q-----cefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 3.4e-05) to 1/3 blocks of the IPB000531 family, which is described as \"TonB-dependent receptor protein\". Interpro entry for IP:IPR000531. IPB000531C 87-98 3.7e-05","Residues 106 to 140 match (2e-07) PD:PD535850 which is described as HEMOGLOBIN BINDING OUTER BOX MEMBRANE FAMILY MULTIGENE SIGNAL PRECURSOR RECEPTOR ","","","","","","","","","","","","Tue Dec 17 14:30:58 2002","","Thu Mar 18 09:23:43 2004","Thu Mar 18 09:23:43 2004","Thu Mar 18 09:23:43 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00764 is paralogously related to AA02201 (1e-19) and AA02782 (1e-04).","Thu Mar 18 09:23:43 2004","","","","","","","",""," Haraszthy VI, Jordan SF, Zambon JJ.,Identification of Fur-regulated genes in Actinobacillus actinomycetemcomitans.Microbiology. 2006 Mar;152(Pt 3):787-96.PMID: 16514158Hayashida,H., Poulsen,K. and Kilian,M.Differences in iron acquisition from human haemoglobin amongstrains of Actinobacillus actinomycetemcomitansMicrobiology 148 (Pt 12), 3993-4001 (2002)PUBMED: 12480903","Ren Z, Jin H, Whitby PW, Morton DJ, Stull TL. Role of CCAA nucleotide repeats in regulation of hemoglobin and hemoglobin-haptoglobin binding protein genesof Haemophilus influenzae. J Bacteriol. 1999 Sep;181(18):5865-70. PMID: 10482534 Morton DJ, Stull TL. Distribution of a family of Haemophilus influenzae genes containing CCAA nucleotide repeating units. FEMS Microbiol Lett. 1999 May 15;174(2):303-9. PMID: 10339823 Morton DJ, Whitby PW, Jin H, Ren Z, Stull TL. Effect of multiple mutations in the hemoglobin- and hemoglobin-haptoglobin-binding proteins, HgpA, HgpB, andHgpC, of Haemophilus influenzae type b. Infect Immun. 1999 Jun;67(6):2729-39. PMID: 10338475 Jin,H., Ren,Z., Whitby,P.W., Morton,D.J. and Stull,T.L. Characterization of hgpA, a gene encoding a haemoglobin/haemoglobin-haptoglobin-binding protein of Haemophilus influenzae Microbiology 145 (Pt 4), 905-914 (1999) PubMed: 10220170","Tue Dec 17 14:30:58 2002","Mon Feb 17 13:39:14 2003","1","","","" "AA00765","528046","528192","147","TTGAATCTCTTGTTCCAATTCGTGCTGATTATCTGCGCTTTGGTGGTTTGTCATTCTTATTTCTCCTTGAGTCAAATTTGGGCGATTATAGCAAAAAATCTTAAACTTACCATGTGCGCCGACTGGCAAGCAAAAGGCGTTCTGTTG","","","5536","LNLLFQFVLIICALVVCHSYFSLSQIWAIIAKNLKLTMCADWQAKGVLL","528192","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-19]?signal-peptide
tmhmm\"[10-30]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 11:16:11 2004","Mon Feb 23 11:25:09 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00765 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 11:16:11 2004","","","","","","","","","","","","","1","","","" "AA00766","528099","527524","576","ATGACAAACCACCAAAGCGCAGATAATCAGCACGAATTGGAACAAGAGATTCAACCGGAAGACGTTGTTGATGAACTAAAAGAACAGGGTGAAGACCCGTTGGAAGAAGCCATTGCGCGTGTTCAGGAGTTAGAAGCTCAACTTGCCGAAACCTCAAAAAAAGAACAGGATTTATTGCTACGTACCCGCGCCGAAATCGATAATATTCGTCGTCGCACCGAACAAGATATTGAAAAAGCGCATAAATTTGCTTTGGAAAAATTTGCCAAAGACATTTTAAATACGATCGATAATTTAGAGCGCGCACTGGCCACCCCGGCAAATACCGAAGATGAAAGCGTAAAAGCGCTGTTTGATGGCGTTGAACTGACTTTAAAAGAATTATTGGCAACGGTTGCCCGCTTCGGTATTGAACCTGTCGGCGCGGTCGGTGAAGTTTTCGACCCGGAATTACACCAAGCCATTTCCATGCAGCCGGCGGAAGGTTTTCAAAGCAACCAAATCACCGCCGTATTACAAAAAGGCTACCTGTTAAACGGACGCGTCATCCGCCCGGCAATGGTGATGGTGGCGGCG","","","25510","MTNHQSADNQHELEQEIQPEDVVDELKEQGEDPLEEAIARVQELEAQLAETSKKEQDLLLRTRAEIDNIRRRTEQDIEKAHKFALEKFAKDILNTIDNLERALATPANTEDESVKALFDGVELTLKELLATVARFGIEPVGAVGEVFDPELHQAISMQPAEGFQSNQITAVLQKGYLLNGRVIRPAMVMVAA","527526","","heat shock protein B25.3 (HSP-70 cofactor)","Cytoplasm","","
InterPro
IPR000740
Family
GrpE nucleotide exchange factor
PR00773\"[60-76]T\"[88-103]T\"[144-159]T\"[171-190]TGRPEPROTEIN
PTHR21237\"[28-192]TGRPE PROTEIN
PF01025\"[21-192]TGrpE
PS01071\"[147-190]TGRPE
InterPro
IPR009012
Domain
GrpE nucleotide exchange factor, head
G3DSA:2.30.22.10\"[136-191]Tno description
InterPro
IPR013805
Domain
GrpE nucleotide exchange factor, coiled-coil
G3DSA:3.90.20.20\"[31-135]Tno description


","BeTs to 22 clades of COG0576COG name: Molecular chaperone GrpE (heat shock protein)Functional Class: OThe phylogenetic pattern of COG0576 is -omp--yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.7e-30) to 3/3 blocks of the IPB000740 family, which is described as \"GrpE protein\". Interpro entry for IP:IPR000740. IPB000740A 61-72 0.00085 IPB000740B 136-155 9.7e-08 IPB000740C 166-190 8.3e-16","Residues 87 to 191 match (1e-08) PD:PD532478 which is described as PROTEOME COMPLETE HEAT COFACTOR CHAPERONE HSP-70 GRPE SHOCK ","","","","","","","","","","","","Thu Jan 23 07:58:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00766 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 21 to 192 (E-value = 8.3e-71) place AA00766 in the GrpE family which is described as GrpE (PF01025)","","","","","Lipinska,B., King,J., Ang,D. and Georgopoulos,C. Sequence analysis and transcriptional regulation of theEscherichia coli grpE gene, encoding a heat shock protein Nucleic Acids Res. 16 (15), 7545-7562 (1988) PubMed: 3045760 Zavilgelsky GB, Kotova VY, Mazhul' MM, Manukhov IV. Role of Hsp70 (DnaK-DnaJ-GrpE) and Hsp100 (ClpA and ClpB)Chaperones in Refolding and Increased Thermal Stability of Bacterial Luciferases in Escherichia coli Cells. Biochemistry (Mosc). 2002 Sep;67(9):986-92. PMID: 12387711 Gelinas A, Langsetmo K, Toth J, Bethoney K, Stafford W,Harrison C. A Structure-based Interpretation of E.coli GrpE ThermodynamicProperties. J Mol Biol. 2002 Oct 11;323(1):131. PMID: 12368105 Wu,B., Wawrzynow,A., Zylicz,M. and Georgopoulos,C. Structure-function analysis of the Escherichia coli GrpE heatshock protein EMBO J. 15 (18), 4806-4816 (1996) PubMed: 8890154 ","","Wed Jan 29 14:40:54 2003","1","","","" "AA00768","528240","529154","915","ATGGATACCTTAAATGCGGTGAAACCGCACAGCTTACACACGTCATTTCAGACCATTGGTTTGGTGGGGAAACCGAGAAATGACTTAAACCTGCAAATGCATAAAAACCTGTTTTTTTGGCTGTTGGAGCACGGTTATCATGTTCTGGTTGAACGGGAAATCGGGGAAAAAATCGAACTTCCGCCGAAACATTTGGCGTCCGTTGATGAAATCGGCAGCGAAGCGCAGCTTGCTATCGTTATCGGCGGTGACGGCAATATGCTGGGGCGTGCGCGAATCCTTGCCAAATACGACATTCCGCTCATAGGCATTAACCGCGGAAACTTAGGTTTTTTAACGGACATTGACCCGAAAAACGCCTATGCACAGTTGCAAGCCTGTTTGGAACACGGCGAGTTTTTTGTGGAAGAGCGCTTTTTATTAAAAGCCTCTATTGAGCGGGATAATGAAATTGTCGCAAGCGGTATCGCCGTTAATGAAGTGGTGATTCACCCGGCAAAAATCGCCCACATGATTGATTTTCATGTACACATTAACGATCAATTTGCCTTTTCCCAACGTTCTGACGGTTTAATTATTTCCACGCCCACCGGTTCCACCGCTTATTCGCTGTCCGCCGGCGGTCCGATTTTAACGCCGAAACTGGATGCCATCGCTTTGGTGCCGATGTTTCCACACACCCTGACTTCACGCCCTTTGGTGATTGACGGCAACAGCAAAATTTCAATGCGTTTCGCCGAATACAATACTTCACAACTGGAAGTGGGCTGCGACAGCCAAATCACCATGCCGTTCTCCCCTTATGATGTGGTGCACATCCAAAAAAGCGAACATAAGCTACGTTTGCTGCACCTAAAAAACTACAATTATTACAAAGTATTAAGTTCTAAATTAGGTTGGTTACGCAATAAATCC","","","34028","MDTLNAVKPHSLHTSFQTIGLVGKPRNDLNLQMHKNLFFWLLEHGYHVLVEREIGEKIELPPKHLASVDEIGSEAQLAIVIGGDGNMLGRARILAKYDIPLIGINRGNLGFLTDIDPKNAYAQLQACLEHGEFFVEERFLLKASIERDNEIVASGIAVNEVVIHPAKIAHMIDFHVHINDQFAFSQRSDGLIISTPTGSTAYSLSAGGPILTPKLDAIALVPMFPHTLTSRPLVIDGNSKISMRFAEYNTSQLEVGCDSQITMPFSPYDVVHIQKSEHKLRLLHLKNYNYYKVLSSKLGWLRNKS","529156","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR002504
Family
ATP-NAD/AcoX kinase
PF01513\"[18-285]TNAD_kinase
noIPR
unintegrated
unintegrated
G3DSA:2.60.200.30\"[146-275]Tno description
PTHR20275\"[14-304]TPOLY(P)/ATP NAD KINASE


","No hits to the COGs database.","Significant hit ( 2.3e-49) to 4/4 blocks of the IPB002504 family, which is described as \"Domain of unknown function DUF15\". Interpro entry for IP:IPR002504. IPB002504A 76-88 0.00099 IPB002504B 99-116 6.8e-09 IPB002504C 157-163 1.4 IPB002504D 176-225 1.1e-31","Residues 80 to 235 match (2e-07) PD:PD560824 which is described as PROTEOME COMPLETE PAE0624 ","","","","","","","","","","","","Tue Dec 17 14:41:07 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00768 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 18 to 286 (E-value = 4.5e-97) place AA00768 in the NAD_kinase family which is described as ATP-NAD kinase (PF01513)","","","","","","","","1","","","" "AA00769","529231","530904","1674","ATGTTAACCCAACTCACTATCAATAATTTTGCTATCGTACGCCACTTAAACATTGAATTAATGCAAGGCATGTCCGTGATTACGGGCGAAACCGGCGCAGGAAAATCCATTGCCATTGATGCTTTAGGCGTTTGTTTGGGGCAACGTATAGAAGCTTCCATGCTACGCGAAGGGCAGGAACGCGCCGACATTTGCGCTACCTTTCAAATCAGCCGAAACAATCCCGCCTACCAATTTCTGTTGGAGCACGACTTACAGGATCAAGACAATCCCGAAGAGTGTATTTTACGCCGCATGATTAATCATGATGGACGCTCCAAAAGTTTTATTAACGGCATTCCCGTCGCCGCCGTGCAGCTCAAAGAAATCGGGCAACACCTGATTCAAATCAGCGGACAACACGCTTCACAACTGTTATTAAAAAACGAATATCAGCTACAACTGGTGGACAGTTTTTGTCATCACCCCGCCCTTTTACAACAAATGCAAACAGATTACCAACGCTGGCGCGATCTGCAACAGCAAATGAAAACCTTTCAGCAAAAATGTGCGGGAAATGAAGCCCGAAAGCAACTCTTGCAATATCAAGTCAGCGAACTGGATGAATTCAATTTGAAAGCCAATGAATATGCAGAATTGGAGGCGGATCATAACCGTTTGTCCAATAGCGAAGAATTGACCCAGCTTTCCCAATCCGTATTACAACTGTTAAGCGAAAATGAAACAGTGAGCGTAGACTCCCTGCTCTATCGTGCCACAAAACATTTAGACGAGCTTTGCAAACTGGATAGCCGTTACGCAGAAGTACAAAATTTACTCAATGAGGCGATGATTCAGGTGCAGGAAGCCACAGGTGAAATACAATCATTAAGCAGCAATATTGAGCAAGATCCCTCACTGTTGGCGAATATTGAACAACGCATCGGACAGGCGGTTCAACTGGCACGCAAACATAATGTAAAACCACAGGAATTGGTGGAATTGCACCACCAATTAAAAGCGGAATTGAATGCGTTAGAAGCATTTTCCGACAGCGAAGAAGAGCTCATTAAGCAAGCGGAGGCAGCGCATGAAAAAATGCTCGCCAGCGCCACCGCACTTCATCAAAGTCGCCAAAGCGGAGCACAAAAATTGGCGCAACAAGTAACCAAATCCATTAAACAGCTCGCCATGGAACACGCGGAATTTTTCATTACACTGGACACAGATTACGACAAAATCGGGGCAAACGGCGCAGATTTCGCCACATTCACGCTGCAAAGCAACCTGGGACAAACCGCCCAGCCGCTCGCAAAAATTGCTTCCGGCGGTGAACTTTCCCGCATTGCACTGGCGATTCAGGTGCAAGCTTCTAACCAAACGGCGATCCCAACCTTAATTTTCGATGAAATTGATGTGGGAATAAGCGGCGCCACTGCTAATGTAGTCGGAAAACTATTACGAAAACTCAGTGAAAAATGCCAGGTCATTTGCGTCACCCATTTGCCGCAGGTCGCCTGCCACGGCACACATCATTTTTCTGTAGAAAAATCCGCCGTTGATCAAAAAACGGAGACAAGAATGACCGCACTTTCCGCTCAACAACGGGTGAAAGCGCTGGCGAAGTTATTGGGCGGAAGCAAAATCACCGATGCCGTTTTAGCCAACGCACAGGAAATGTTAGATACTTCGATA","","","62148","MLTQLTINNFAIVRHLNIELMQGMSVITGETGAGKSIAIDALGVCLGQRIEASMLREGQERADICATFQISRNNPAYQFLLEHDLQDQDNPEECILRRMINHDGRSKSFINGIPVAAVQLKEIGQHLIQISGQHASQLLLKNEYQLQLVDSFCHHPALLQQMQTDYQRWRDLQQQMKTFQQKCAGNEARKQLLQYQVSELDEFNLKANEYAELEADHNRLSNSEELTQLSQSVLQLLSENETVSVDSLLYRATKHLDELCKLDSRYAEVQNLLNEAMIQVQEATGEIQSLSSNIEQDPSLLANIEQRIGQAVQLARKHNVKPQELVELHHQLKAELNALEAFSDSEEELIKQAEAAHEKMLASATALHQSRQSGAQKLAQQVTKSIKQLAMEHAEFFITLDTDYDKIGANGADFATFTLQSNLGQTAQPLAKIASGGELSRIALAIQVQASNQTAIPTLIFDEIDVGISGATANVVGKLLRKLSEKCQVICVTHLPQVACHGTHHFSVEKSAVDQKTETRMTALSAQQRVKALAKLLGGSKITDAVLANAQEMLDTSI","530906","","DNA repair protein","Cytoplasm","","
InterPro
IPR003395
Domain
SMC protein, N-terminal
PF02463\"[1-519]TSMC_N
InterPro
IPR004604
Family
DNA repair protein RecN
TIGR00634\"[1-556]TrecN: DNA repair protein RecN
InterPro
IPR013253
Family
Kinetochore Spc7
SM00787\"[100-387]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[1-176]T\"[435-540]Tno description
PTHR18937\"[20-407]TSTRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER


","BeTs to 15 clades of COG0497COG name: ATPases involved in DNA repairFunctional Class: LThe phylogenetic pattern of COG0497 is -------q-drlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","","Residues 104 to 222 match (4e-09) PD:PD008454 which is described as REPAIR DNA PROTEOME COMPLETE RECN RECOMBINATION ATP-BINDING N GENETIC AFG3-SEB2 ","","","","","","","","","","","","Tue Dec 17 14:42:27 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00769 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Rostas,K., Morton,S.J., Picksley,S.M. and Lloyd,R.G. Nucleotide sequence and LexA regulation of the Escherichia coli recN gene Nucleic Acids Res. 15 (13), 5041-5049 (1987) PubMed: 3037486 ","","Tue Dec 17 14:42:27 2002","1","","","" "AA00770","531572","530928","645","ATGCAAAAGCACAAAATTATCTTAGGTTTGGCGTCTGTTTTAGCAATGGGAGCGGTAAATGCCCATGAAGCAGGCAGCTTTATTGTTCGCGGTGGTGGTATTTTTGTTTCTGCCAATTCCAGCTCAGCCACTAAAACCCCGATTAATGTGAATTTAGATGTTGGAGATAACGCACAGTTAGGTTTAACCGGCACTTATATGTTCACTGACAATTTTGGAATTGAGTTATTGGGTGCAACGCCTTTTTCCCATAAAATTAGTGCGACTGTACCGGCGCTTAAGTTAGGCTTAGGTGATGTGGTTAAACTTAAACAATTGCCGCCCAGCCTGTATGCTCAATATTATTTCTTAGATCAAGATTCCGGTTCCCGCCCTTATGTCGGGGCAGGTATTAACTATACCCGCTTCTTTAGTGCAAAACCGATGGTAAATGCTGTTACTGATCTTGATGTGAAAAAACACTCTTTTAGCCCTATATTAAATGCCGGTATCGATATTAAATTAACCGATAACGTGTATTTAAATACCGCGATGTGGTACACAAAAATTAAAACAACCGCTAAATTTAAAGCGTTAGGAGCGGCTCATGAAGTAAAAATTAAATTGGATCCTCTTGTGTTCTTCACCGGTTTAGCATACCGCTTC","","","23183","MQKHKIILGLASVLAMGAVNAHEAGSFIVRGGGIFVSANSSSATKTPINVNLDVGDNAQLGLTGTYMFTDNFGIELLGATPFSHKISATVPALKLGLGDVVKLKQLPPSLYAQYYFLDQDSGSRPYVGAGINYTRFFSAKPMVNAVTDLDVKKHSFSPILNAGIDIKLTDNVYLNTAMWYTKIKTTAKFKALGAAHEVKIKLDPLVFFTGLAYRF","530930","","outer membrane protein precursor","Outer membrane, Extracellular","","
InterPro
IPR005618
Family
OmpW
PF03922\"[23-215]TOmpW
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide


","No hits to the COGs database.","","Residues 1 to 180 match (7e-42) PD:PD397076 which is described as OUTER MEMBRANE COMPLETE PROTEOME SIGNAL PRECURSOR PLASMID W OMPW PEPTIDE ","","","","","","","","","","","","Tue Dec 17 14:45:46 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00770 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 23 to 215 (E-value = 4.8e-65) place AA00770 in the OmpW family which is described as OmpW family (PF03922)","","","","","","","","1","","","" "AA00771","531680","531585","96","TTGATTGAGATCACATATTGCATTACTCATAAAGTGGTATATTTCACCGCGCTTAATAAACACATTTTTATTAGGGATAAACGTTATAATAATTTT","","","3957","LIEITYCITHKVVYFTALNKHIFIRDKRYNNF","531585","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 11:37:26 2004","Mon Feb 23 11:37:26 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00771 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 11:37:26 2004","","","","","","","","","","","","","1","","","" "AA00772","531658","531807","150","ATGCAATATGTGATCTCAATCAAATTTTTGGAAATTAGAGAAAATAATTTAGAGAATCTACATCATTTTTACATCATCCTGCGTGAGGAAAACATTGTGTTAAATCAAAATGGAGTTTTTTATGTTTTTATCCCAAAAGGACAGTATAAT","","","6097","MQYVISIKFLEIRENNLENLHHFYIILREENIVLNQNGVFYVFIPKGQYN","531807","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 11:40:12 2004","Mon Feb 23 11:41:18 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00772 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 11:40:12 2004","","","","","","","","","","","","","1","","","" "AA00773","531844","532599","756","ATGCCAATTAACTTTACCCAAATCATTAAAGATAGCTTCCATTTCATACAAAATGAAAAACAAAGTGTCATTATATTGTCGGCACTCTATTTCTTTGCCAACATCGCCATAGCATTGTTGCAATCGTCAATGTTGCCAAATGAAGTCATTATTTCCTTAACCGAAAAACAAATCTCTCCTGCGATGTCAGAGGGACAAGCTATAGATTTAGTAATCTTCTTTTTTCTGAAACAATTTATCTATATTTTTATCAGTGCATGGTGCTTGGTGAGTATTCACCAAATCAGTCTGCGTCACTTTAATACCTTCCAACACAGCTTCTCCATAACCTTAAAACGTATTTGGGGAGCAATTTTAATTAGCTTTGTGATATGTATTCCAATCTTCATCGGACTGGCCGAAGCGATAATTGCAATTCAACAGAAAATACAACCATCAATCATCTCACTACTTGCTATCATTATCGGTATTGGATTATACATTCGCCTCTGTTTAGCGCCGGTGCATTACTTGCTGACAGATGACACCGTGAGCACTTGCGGAAAAACGATATGGCACGCTGCTATCGGGCGCGTTTCTATGTTAGTTATTTTCTGTTTACTCATCTATTTTCTTATACCGATAGCAGAAAATTTTCTTGTCAGTTTTTCAACTAATTCAATCATGGCGTTGATTACAGGTATCATGGTGGCATTCTTGAATATCTTTGCATTAATTGTGACCTACCGTTTTTACACACGCTTTCTTCCAAAGGTA","","","28491","MPINFTQIIKDSFHFIQNEKQSVIILSALYFFANIAIALLQSSMLPNEVIISLTEKQISPAMSEGQAIDLVIFFFLKQFIYIFISAWCLVSIHQISLRHFNTFQHSFSITLKRIWGAILISFVICIPIFIGLAEAIIAIQQKIQPSIISLLAIIIGIGLYIRLCLAPVHYLLTDDTVSTCGKTIWHAAIGRVSMLVIFCLLIYFLIPIAENFLVSFSTNSIMALITGIMVAFLNIFALIVTYRFYTRFLPKV","532601","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-38]?signal-peptide
tmhmm\"[21-41]?\"[79-97]?\"[118-140]?\"[146-166]?\"[187-207]?\"[221-241]?transmembrane_regions


","No hits to the COGs database.","","Residues 1 to 249 match (5e-23) PD:PD119156 which is described as PROTEOME COMPLETE TRANSMEMBRANE PM0330 HI0825 ","","","","","","","","","","","","Tue Dec 17 14:49:04 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00773 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00774","532608","533156","549","ATGAAACAACTCCTTGAATTTATTCCGCTTATTTTATTCTTCGCCGTGTACAAACTAATGGGTATTCGCGCAGCGGCAGTCACCTTGGTGATTGCCACCATCGTGCAATTTATCATTTTGCAAGTGAAATACGGCAAAATTGAAGCTCAGCAAAAATTCGTTGCCGGCGCGGTGATTTTCTTCGGTACACTTACCGCTTATTTCAACGATCTTGAATTTTTAAAATGGAAAGTCACGATTATCTATGCTCTTTTCGCGTTGGTGTTATTAATCGCTCAATTCGGTTTCAAAAAACTGCTCATCAAACAATTGCTCGGTAAAGAAATCGAATTGCCCGAAGCCGTGTGGAAAAATGTAAATCTCGGCTGGAGCGGGTTCTTCATTTTGTGTATGCTGGTGAACATTTATATCAGCCAATATCTCTCCAACGATATTTGGGTGGACTTTAAATCCTTCGGTATTATCGGCATGACGTTTGTTGCCACTCTCATTACCGGTCTTTATATTTACCGTTATTTACCTAAAAACGAACAGGAACAAACAAAGGAA","","","21046","MKQLLEFIPLILFFAVYKLMGIRAAAVTLVIATIVQFIILQVKYGKIEAQQKFVAGAVIFFGTLTAYFNDLEFLKWKVTIIYALFALVLLIAQFGFKKLLIKQLLGKEIELPEAVWKNVNLGWSGFFILCMLVNIYISQYLSNDIWVDFKSFGIIGMTFVATLITGLYIYRYLPKNEQEQTKE","533158","","intracellular septation protein","Inner membrane, Cytoplasm","","
InterPro
IPR006008
Family
Intracellular septation protein A
PF04279\"[1-176]TIspA
TIGR00997\"[1-178]TispZ: intracellular septation protein A
noIPR
unintegrated
unintegrated
signalp\"[1-32]?signal-peptide
tmhmm\"[10-39]?\"[53-68]?\"[78-96]?\"[119-137]?\"[152-172]?transmembrane_regions


","BeTs to 6 clades of COG2917COG name: Intracellular septation protein AFunctional Class: DThe phylogenetic pattern of COG2917 is --------------efgh-n-jx---Number of proteins in this genome belonging to this COG is","","Residues 132 to 176 match (6e-11) PD:PD301727 which is described as SEPTATION DIVISION TRANSMEMBRANE CELL INTRACELLULAR COMPLETE PROBABLE PROTEOME PA3201 VIRULENCE ","","","","","","","","","","","","Tue Dec 17 14:55:15 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00774 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 176 (E-value = 1.4e-92) place AA00774 in the IspA family which is described as Intracellular septation protein A (PF04279)","","","","","Mac Siomoin,R.A., Nakata,N., Murai,T., Yoshikawa,M., Tsuji,H. andSasakawa,C.Identification and characterization of ispA, a Shigella flexnerichromosomal gene essential for normal in vivo cell division andintracellular spreadingMol. Microbiol. 19 (3), 599-609 (1996)PubMed: 8830250","","Tue Dec 17 14:55:15 2002","1","","","" "AA00775","533163","533630","468","ATGGTACATCAACCAGTTGATCCAAGAAACGCCCAACCGCACGGCACGTTATTGTTAAGAACTTTGGCGATGCCTTCCGACACCAACGCCAACGGCGATATTTTCGGCGGCTGGATTATGTCGCAAATGGATATGGGCGGCGCCATTCTCGCCAAAGAAATTGCCCACGGGCGTGTGGTGACCGTGGCGGTAGAAAGTATGAACTTCATCCGTCCGGTGACGGTCGGAGATGTGGTCTGCTGTTACGGACGCTGTTTATATGTAGGTCGCAGTTCGCTCAAAATCAAAGTGGAAGTGTGGGTGAAAAAAGTGGCAAGTGAACCCATCGGTGAACGTTATTGCGTCACCGAAGCGGTATTTACCTTCGTCGCCGTAAACAACGAGGGCAAATCCAGAGCGATTCCCCGTGAAAACAACCATGAATTGGATAACGCCTTAGCACAAATTCAAGCCCATCAAACGGAGAAA","","","17117","MVHQPVDPRNAQPHGTLLLRTLAMPSDTNANGDIFGGWIMSQMDMGGAILAKEIAHGRVVTVAVESMNFIRPVTVGDVVCCYGRCLYVGRSSLKIKVEVWVKKVASEPIGERYCVTEAVFTFVAVNNEGKSRAIPRENNHELDNALAQIQAHQTEK","533632","","conserved hypothetical protein (possible acyl CoA thioester hydrolase)","Cytoplasm","","
InterPro
IPR006683
Domain
Thioesterase superfamily
PF03061\"[31-108]T4HBT
noIPR
unintegrated
unintegrated
G3DSA:3.10.129.10\"[14-103]Tno description
PTHR11049\"[24-136]TCYTOSOLIC ACYL COENZYME A THIOESTER HYDROLASE


","BeTs to 13 clades of COG1607COG name: Acyl-CoA hydrolaseFunctional Class: IThe phylogenetic pattern of COG1607 is -o-p-z---d--b-efgh-nuj-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-54) to 3/3 blocks of the IPB002590 family, which is described as \"Cytosolic long-chain acyl-CoA thioester hydrolase\". Interpro entry for IP:IPR002590. IPB002590A 25-55 2.9e-17 IPB002590B 57-104 7.2e-30 IPB002590C 115-131 7.4e-05","Residues 100 to 137 match (3e-13) PD:PD470781 which is described as HYDROLASE PROTEOME COMPLETE ACYL-COA THIOESTER 3.1.2.- YCIA P14 HI0827 BU274 ","","","","","","","","","","","","Thu Feb 13 16:22:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00775 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 31 to 109 (E-value = 8.9e-22) place AA00775 in the 4HBT family which is described as Thioesterase superfamily (PF03061)","","","","","Zhuang Z, Song F, Martin BM, Dunaway-Mariano D.The YbgC protein encoded by the ybgC gene of the tol-pal gene cluster of Haemophilus influenzae catalyzes acyl-coenzyme A thioester hydrolysis.FEBS Lett. 2002 Apr 10;516(1-3):161-3.PMID: 11959124 ","","Thu Feb 13 16:20:40 2003","1","","","" "AA00776","533636","533929","294","ATGTACTACGTTATTTTTGCGCAAGACAAACCGAATACCTTGGCACAACGTTTGAGCGTGCGTGAGCAACATCTCGCGCGCTTAACCCAATTACAGGCAGAAAATCGTTTACTCACCGCCGGTCCGAATCCGGCAATTGATGATGAAAACCCGGGCGACGCGGGTTTTTCAGGCTCCACCGTCATCGCACAATTTGATAGCCTGCAAGCCGCAAAAGACTGGGCAGCACAGGATCCTTATGTAGAAGCCGGCGTATATGGCGAAGTGATTGTTAAACCGTTTAAGAAAGTGTTT","","","10795","MYYVIFAQDKPNTLAQRLSVREQHLARLTQLQAENRLLTAGPNPAIDDENPGDAGFSGSTVIAQFDSLQAAKDWAAQDPYVEAGVYGEVIVKPFKKVF","533931","","conserved hypothetical protein","Periplasm","","
InterPro
IPR005545
Domain
YCII-related
PF03795\"[9-98]TYCII
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.1060\"[1-98]Tno description


","BeTs to 6 clades of COG2350COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG2350 is ---------d--bcefgh-n-j----Number of proteins in this genome belonging to this COG is","","Residues 1 to 97 match (7e-42) PD:PD029750 which is described as PROTEOME COMPLETE ATU2526 CYTOPLASMIC YCII ATU2649 S-ADENOSYL NMB0343 R03076 PA3202 ","","","","","","","","","","","","Tue Dec 17 15:06:56 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00776 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 9 to 98 (E-value = 2.3e-47) place AA00776 in the YCII family which is described as YCII-related domain (PF03795)","","","","","","","","1","","","" "AA00777","534459","536672","2214","ATGCGATATTTGAAACAAACAACAATTTCACTGTTAATTTTGACCGCACTTTCCTCCTCCTTTGCCAATCAGCACAAGGCGACAACGCATAAAGCGAATGTTGCCCATACGCACGCCAAACCGGAGCAACACCACGCAGAATTAGAACGGCTAAAACAGCGTGCAACTTTTCTGCAGTTAGAAAGCCTGCTGAAAAGTGCGGTCAAAAATAACGGCGTTTTTATCAACCAAACTGTATTCCTGAAACTGATTGAGGATTTGAAAGGCTATCCGTTGCAAACAGATGCCATAGCGGCTTATTTCGACGCCTGCATTAAAAGCGTAAATCACGACACATCGAAGGGAGAAGTTAAGGCGCTAAAACAGGACATTGAGCAATTTATCGAAAAGCATCCGACTCATTTTCTACGGGAAAAATTGGAACAAAGACTTTTTACCTTATTTATCAACACGGAAGATCTTGAAGGCTTAGTTGGTTACGCGCAACGGGTTAAACCGAAAGGGTTGGAAGCCCAACTTGCAGTGTTGAATGCCGAATATCAACTGGGGCGCAAACGTGCCGAATCTGATAAAAATCCGAATGCGAATGTGTCGAAAATCATCGCCCGTTATGAGCAACTTTGGTTAAACAATAGTGAACTGCCAAACGATGCGCAGCTACGGGCAAAATGGTATTCCGACGGCGGCAGAATGGCAGAAAAAGTGTATCAAAAAGCTGAGAATCTCTTTATCAAAAACAATGTAAAAGGCTTGGAATTGTTAGCAACAGAGTTAAAGAAGGCGGGTAATGTCAAAGAAAACGAAATAGTTGCCTCACGTTTACAACGTTTGCAGAAATTATTAAAAACACCGGCAAGTTTACCGGAATTAGCCAAATTACCGCCGGTCGAAGCCAATAATAAAATCATGCTGAAATTTGCCGTGCTGCAAAGTTTCACCCGTTATTTGCGTACGCTGCCGGAAAATATGAAAGAACCTAACTTTGCCGCTTATGCACAATGGGCGAAAGATTGGCAACTGAGCGAAGCCGAAATTCGTGAGTGGAAAATCGCCTTTCTCGGGCGTTTCTTTGATAACGAAAGCCCAAGCTTTCAATTATGGCGTGATGTGGAAGTCGCCAAGCTCAATGCCGACAATCTCACCGAGCGCCGCTTGCGCATGGCAATTAGGCAAAAAACCGATTTAACCCCATGGCTCAACGCCCTATCGGCAGAAGGCAAACAGAAACAGGAATGGCGTTATTGGCAGGCAAAAAATATGGCGAAAACCAACAGCAAAAAAACGCAGGAAATATTGACCGCACTTTCGCACGAACGGGGCTTTTATCCGATGCTGGCGGCGGCAAAACTGGATCCGAAAACTCGTGGCAGCGGTTATGATTTCGGTCAGCCAAAACTGCTCATAGCACCGAGTATCACCGATGCTACCTGGGCGGATACCTGCAAAGCCGTTAACCCGACATTAGACGAAATCGCCGAATTACGTCAATTAGATCGCCTCGGCGCGGCAAAACAGCGTTGGCGTTTCCTGCTGGAAAATCTTTCCGATGAAAATAAAAAAGAAAAACAAATCGCGCTCAGTCAATACGCCAATCAGCAAAATTGGTTTGATTTAGGTGTGGACGGTTCCATTATGGCAAAAGCCTTTAATTACATTCAGTTACGCTTGCCAAATGCCTACAGCGATTATTTTGATATTGCGCTCAGCCCGAAATTTATCAACAACAATAAACCGCAGGCAGTGGTGAATAATAATGTGACGAAAACCTTCGCCATGGCAATCGCCCGCCAGGAAAGCGCATGGAACCCGCAGGCGCAATCTTCCGCCAATGCACGGGGTTTAATGCAACTGCTGCCAAGCACCGCAAAAGCCACGGCAAACAACGCAAAATTGCCTTATACGGGCGAAGGGGATTTATTCAAGCCGCTCAATAATATTTTGCTCGGCACGGCACATCTGGCGGAACTGAATGCCAAATATCCGAACAACCGCATTTTGATCGCTTCCGCTTATAACGCAGGCGCCCATCGCGTAGAAAAATGGCTGGCGCGCGCCAACGGCAAGCTGGCAATGGATGAATTTGTGGCATCCATTCCGTTTTATGAAACCCGAGGCTATGTGCAAAATGTGTTAACTTACGATTTTTACTATCAAATTCTGCAGAAAAAAGAAGATCCACAAACCTTTAGCAATGAGGAATACGATCGGCTATAC","","","84223","MRYLKQTTISLLILTALSSSFANQHKATTHKANVAHTHAKPEQHHAELERLKQRATFLQLESLLKSAVKNNGVFINQTVFLKLIEDLKGYPLQTDAIAAYFDACIKSVNHDTSKGEVKALKQDIEQFIEKHPTHFLREKLEQRLFTLFINTEDLEGLVGYAQRVKPKGLEAQLAVLNAEYQLGRKRAESDKNPNANVSKIIARYEQLWLNNSELPNDAQLRAKWYSDGGRMAEKVYQKAENLFIKNNVKGLELLATELKKAGNVKENEIVASRLQRLQKLLKTPASLPELAKLPPVEANNKIMLKFAVLQSFTRYLRTLPENMKEPNFAAYAQWAKDWQLSEAEIREWKIAFLGRFFDNESPSFQLWRDVEVAKLNADNLTERRLRMAIRQKTDLTPWLNALSAEGKQKQEWRYWQAKNMAKTNSKKTQEILTALSHERGFYPMLAAAKLDPKTRGSGYDFGQPKLLIAPSITDATWADTCKAVNPTLDEIAELRQLDRLGAAKQRWRFLLENLSDENKKEKQIALSQYANQQNWFDLGVDGSIMAKAFNYIQLRLPNAYSDYFDIALSPKFINNNKPQAVVNNNVTKTFAMAIARQESAWNPQAQSSANARGLMQLLPSTAKATANNAKLPYTGEGDLFKPLNNILLGTAHLAELNAKYPNNRILIASAYNAGAHRVEKWLARANGKLAMDEFVASIPFYETRGYVQNVLTYDFYYQILQKKEDPQTFSNEEYDRLY","536674","","soluble lytic murein transglycosylase","Periplasm","","
InterPro
IPR000189
Active_site
Prokaryotic transglycosylase, active site
PS00922\"[594-622]TTRANSGLYCOSYLASE
InterPro
IPR008258
Domain
Lytic transglycosylase, catalytic
PF01464\"[575-694]TSLT
InterPro
IPR008939
Domain
Lytic transglycosylase, superhelical U-shaped
G3DSA:1.25.20.10\"[52-450]Tno description
InterPro
IPR012289
Domain
Lytic transglycosylase, superhelical linker
G3DSA:1.10.1240.20\"[479-552]Tno description
noIPR
unintegrated
unintegrated
G3DSA:1.10.530.10\"[553-737]Tno description
PTHR21666\"[583-679]TPEPTIDASE-RELATED
PTHR21666:SF10\"[583-679]TLYTIC TRANSGLYCOSYLASE
signalp\"[1-22]?signal-peptide


","No hits to the COGs database.","Significant hit ( 5.4e-15) to 2/2 blocks of the IPB000189 family, which is described as \"SLT domain\". Interpro entry for IP:IPR000189. IPB000189A 598-622 5.2e-11 IPB000189B 639-653 0.026","Residues 21 to 122 match (8e-07) PD:PD140434 which is described as SOLUBLE PROTEOME GLYCOSIDASE TRANSGLYCOSYLASE MUREIN COMPLETE LYTIC PERIPLASMIC 3.2.1.- SIGNAL ","","","","","","","","","","","","Tue Dec 17 15:08:13 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00777 is paralogously related to AA00077 (3e-08) and AA01042 (4e-07).","","","","","","Residues 575 to 694 (E-value = 5.5e-32) place AA00777 in the SLT family which is described as Transglycosylase SLT domain (PF01464)","","","","Yoshida,Y., Nakano,Y., Yamashita,Y. and Koga,T.Identification of a genetic locus essential for serotype b-specific antigen synthesis in Actinobacillus actinomycetemcomitansInfect. Immun. 66 (1), 107-114 (1998)PubMed: 98084462Yoshida,Y., Nakano,Y., Nezu,T., Yamashita,Y. and Koga,T.A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidine diphosphate-D-fucoseJ. Biol. Chem. 274 (24), 16933-16939 (1999)PubMed: 99287888","Engel,H., Kazemier,B. and Keck,W. Murein-metabolizing enzymes from Escherichia coli: sequence analysis and controlled overexpression of the slt gene, which encodes the soluble lytic transglycosylase J. Bacteriol. 173 (21), 6773-6782 (1991) PubMed: 1938883 Betzner,A.S. and Keck,W. Molecular cloning, overexpression and mapping of the slt gene encoding the soluble lytic transglycosylase of Escherichiacoli Mol. Gen. Genet. 219 (3), 489-491 (1989) PubMed: 2695826 ","Tue Feb 11 14:34:36 2003","Tue Dec 17 15:08:13 2002","1","","","" "AA00778","536708","537013","306","ATGTACATTAGTCGCAACTTAGAACAATGGAACGCCTTTCTTAATATACTGCAAACCGCATTTGAACAAGGCAAAGCACAGGATGTATTAACCTTATTACTAACGCCGGATGAGCGCGACGCGCTGGGGCTTCGGCTCCAAATTGTCGCCCGGTTACTCAATAAAAATTTGCCGCAACGGGAAATTCAGCAAAATCTGAACACCAGCGCGGCAACCATCACACGGGGATCCAATATGCTAAAAACCATGGATCCCGCTTTCGTTGACTGGATAAAAACACAACTCAATGAGCAAGAAAAAAATCAC","","","11748","MYISRNLEQWNAFLNILQTAFEQGKAQDVLTLLLTPDERDALGLRLQIVARLLNKNLPQREIQQNLNTSAATITRGSNMLKTMDPAFVDWIKTQLNEQEKNH","537015","","trp operon repressor","Cytoplasm","","
InterPro
IPR000831
Family
Trp repressor
PF01371\"[8-95]TTrp_repressor
InterPro
IPR013318
Domain
Trp repressor-like fold
G3DSA:1.10.1270.10\"[1-99]Tno description
InterPro
IPR013335
Family
Trp repressor, bacterial
PD012582\"[8-92]TTRPR_HAEIN_P44889;
TIGR01321\"[1-95]TTrpR: trp operon repressor


","No hits to the COGs database.","Significant hit ( 2.3e-54) to 2/2 blocks of the IPB000831 family, which is described as \"Trp repressor\". Interpro entry for IP:IPR000831. IPB000831A 7-60 3e-32 IPB000831B 61-95 5.2e-21","","","","","","","","","","","","","Tue Dec 17 15:19:38 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00778 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 95 (E-value = 1.3e-39) place AA00778 in the Trp_repressor family which is described as Trp repressor protein (PF01371)","","","","","Jeeves M, Evans PD, Parslow RA, Jaseja M, Hyde EI.Studies of the Escherichia coli Trp repressor binding to its five operators and to variant operator sequences.Eur J Biochem. 1999 Nov;265(3):919-28.PMID: 10518785Arvidson,D.N., Arvidson,C.G., Lawson,C.L., Miner,J., Adams,C. andYouderian,P.The tryptophan repressor sequence is highly conserved among theEnterobacteriaceaeNucleic Acids Res. 22 (10), 1821-1829 (1994)PubMed: 8208606","","Tue Dec 17 15:19:38 2002","1","","","" "AA00780","536994","537764","771","ATGAGCAAGAAAAAAATCACTAAATCCCCTTTGGAATGGCTAAATCTACGTAACCTGAAGTTGCGCAGATTTACTTTTTTCAAGAAGTTCTCCACCAAAAGTGCGGTGTGTTTTTTATGTCGTTTTTTGCTGGCGATGACGGTGATTACCTTCGCCTTTCGCTTCATTCCCATCCCCTATTCCACCTATATGCTGCAACAGAAAGCGGCGCATTTATTCTCCGGCGATTTTGGCTATGAAACGCGCTACGATTGGGTCAGCTTAGATGAAATCTCCTGGCAAATGCAGCTTGCCGTCATTGCTGCCGAGGATCAGAATTTTCCCGAACATTACGGCTTTGATTTCAGCGCCATAAAAAGCGCATTTTCACATAATCAAAAAAGCACACGAATTCGCGGAGCCTCCACCATTTCCCAACAAACCGCCAAAAACCTTTATTTATGGCACGGGCAAAGCTGGTTACGTAAAGCCATTGAAGTGCCGACGACCTTGATGCTGGAAACCTTGTGGTCAAAAAAACGCATTTTAGAAGTGTATTTAAATATTGCCGAATTCGGGAATGGCATTTATGGTGTGGAAGCAGCAAGCCGTTTTTATTTCAAAAAGTCGGCAAAAAATTTATCGCAAAATGAAGCCGCACTTTTAGCCGCCGCGTTACCCAATCCGATTATTTACAAAGTCAATGCCCCCGGGCTCTACACCAAACGCAGACAGATTTGGATTCAACGCCAAATGAATCAACTGGGAAAATCCTATTTAGAAAATATCAAT","","","29875","MSKKKITKSPLEWLNLRNLKLRRFTFFKKFSTKSAVCFLCRFLLAMTVITFAFRFIPIPYSTYMLQQKAAHLFSGDFGYETRYDWVSLDEISWQMQLAVIAAEDQNFPEHYGFDFSAIKSAFSHNQKSTRIRGASTISQQTAKNLYLWHGQSWLRKAIEVPTTLMLETLWSKKRILEVYLNIAEFGNGIYGVEAASRFYFKKSAKNLSQNEAALLAAALPNPIIYKVNAPGLYTKRRQIWIQRQMNQLGKSYLENIN","537766","From Genbank:[gi:1176851] This protein plays a role in cell-wall formation.","monofunctional biosynthetic peptidoglycan transglycosylase","Inner membrane, Cytoplasm","","
InterPro
IPR001264
Domain
Glycosyl transferase, family 51
PD001895\"[153-199]TMTGA_HAEIN_P44890;
PF00912\"[64-230]TTransgly
InterPro
IPR011812
Family
Monofunctional biosynthetic peptidoglycan transglycosylase
TIGR02070\"[33-251]Tmono_pep_trsgly: monofunctional biosyntheti
noIPR
unintegrated
unintegrated
signalp\"[1-45]?signal-peptide
tmhmm\"[35-55]?transmembrane_regions


","BeTs to 16 clades of COG0744COG name: Membrane carboxypeptidase (penicillin-binding protein)Functional Class: MThe phylogenetic pattern of COG0744 is -------qvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.8e-59) to 3/3 blocks of the IPB001264 family, which is described as \"Glycosyltransferase family 51\". Interpro entry for IP:IPR001264. IPB001264A 86-125 9.5e-16 IPB001264B 133-185 7.4e-27 IPB001264C 190-216 2.6e-14","Residues 84 to 147 match (4e-18) PD:PD082053 which is described as PENICILLIN-BINDING PROTEOME COMPLETE PEPTIDOGLYCAN 1A TRANSGLYCOSYLASE 2.4.2.- TGASE SYNTHESIS CELL ","","","","","","","","","","","Wed Jan 15 07:57:36 2003","Tue Dec 17 15:23:44 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00780 is paralogously related to AA01304 (2e-18), AA02432 (2e-17) and AA01690 (2e-16).","","","","","","Residues 66 to 230 (E-value = 1.6e-70) place AA00780 in the Transgly family which is described as Transglycosylase (PF00912)","","","","","Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.Monofunctional biosynthetic peptidoglycan transglycosylasesMol. Microbiol. 19 (3), 639-640 (1996)PubMed: 8830253","","Tue Dec 17 15:25:51 2002","1","","","" "AA00781","538278","538027","252","ATGAAAAAATTATCTGTTTCCCTTCTTATTGCCGGTTCTTTGCTTGCTTTGGCTGGTTGTGAAGAAAAGAATATGACAATTTATGATTATCTTCAGAACGAAGAACTGTTAAATAAAACATTAAATGAATGTATTAGTGGAGCTTTAAATGATGAACACAAATGTCAGACGGTAAAGGGTGCTTATGCTAATATAGATAGTTTTAAAAATGGCTCATTAAGTGAAGAACATCTAAAAATGCTTGGTAAAAAA","","","9247","MKKLSVSLLIAGSLLALAGCEEKNMTIYDYLQNEELLNKTLNECISGALNDEHKCQTVKGAYANIDSFKNGSLSEEHLKMLGKK","538029","","hypothetical protein","Cytoplasm, Inner membrane","","
noIPR
unintegrated
unintegrated
PS51257\"[1-20]TPROKAR_LIPOPROTEIN
signalp\"[1-20]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Tue Dec 17 15:33:03 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00781 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00782","539180","538863","318","GTGGAATATAGCCAAATAACGCGCCAATTTAAGCTAATTCATGACAGTAACCGCAAATGCTTAGAGGTTTACCCCGACGACTTCCACCATAAGCTGAAAATGAGGGAAGAATGTGCTAACTTAGTAAACCGGTTAAACGGTGGTGGAAAGTTATTTAATGAATTAGCCAAGGGCACCAATTTAACCCAAGAACAGACCGCACTTTTGAAGGCGTTTAATCAGGTGAACGGCTATAAGTTTTCAGAAGTGGCAGAGCAAATAGACCAGCTCAATATTGAGCGCGTTGAAGAGCAAAAAACGACGGATAGCAAAATGAAT","","","12528","VEYSQITRQFKLIHDSNRKCLEVYPDDFHHKLKMREECANLVNRLNGGGKLFNELAKGTNLTQEQTALLKAFNQVNGYKFSEVAEQIDQLNIERVEEQKTTDSKMN","538865","","conserved hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","Residues 2 to 90 match (4e-25) PD:PD414570 which is described as PROTEOME COMPLETE PM1781 ","","","","","","","","","","","","Tue Dec 17 15:35:03 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00782 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00784","539371","539165","207","ATGAAACCAACTAACCCAATGGCACAACTTGAACAATGGAAAGCAAACAACGCGCCCAAAATTGGGCTGGTTAACCAATCCAAAACCGGATCAGTTAAAAATTCCGATGCCCTCAAATTTGAGGAGAGCCTAAAAACGCAACAGGAAGCGCAAGGAGCGACGAAAGAGAGACTACCATTTACCCTTTGGTGGTGGAATATAGCCAAA","","","7841","MKPTNPMAQLEQWKANNAPKIGLVNQSKTGSVKNSDALKFEESLKTQQEAQGATKERLPFTLWWWNIAK","539167","","hypothetical protein","Periplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Tue Dec 17 15:36:12 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00784 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00785","539732","539361","372","TTGGCACGTTTAACCAAACCGCTTACAAATACCGAAGTTAACAATGCTAAACCAAAGGCGAAGGAGTACACCCTATCAGACGGGAACGGTCTTTATTTGTTGGTGAAACCAAACGGCTCAAAGTTATGGCGGTTTACCCATTGCGCAATCCCGTTAACGGAGACGGGTAAAATTCATAGTTCTATTCGCAAAGCAAAAGCAATTTTGACATTAATTAGGAACGATGGGGCGGACATGGATTTGGAGGGCTTTTATACAAGTGAAGAAATTATCAGAACTGCATTATTTGTGATTGATGATTATTTAGAGAAAGCGGAGCAATCCTCAAAAGTCGATTTTTATTTCACGAAAGGGGGCGAAGATGAAACCAAC","","","13899","LARLTKPLTNTEVNNAKPKAKEYTLSDGNGLYLLVKPNGSKLWRFTHCAIPLTETGKIHSSIRKAKAILTLIRNDGADMDLEGFYTSEEIIRTALFVIDDYLEKAEQSSKVDFYFTKGGEDETN","539363","","conserved hypothetical protein (possible integrase)","Cytoplasm","","No hits reported.","BeTs to 3 clades of COG0582COG name: IntegraseFunctional Class: LThe phylogenetic pattern of COG0582 is aompkz-qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 7 to 53 match (1e-10) PD:PD007941 which is described as INTEGRASE COMPLETE PROTEOME DNA PROPHAGE RECOMBINATION INTEGRATION PHAGE INT CP4-LIKE ","","","","","","","","","","","","Wed Jan 22 16:54:47 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00785 is paralogously related to AA01449 (2e-07).","","","","","","","","","","","","","","1","","","" "AA00786","540462","540115","348","ATGTACTCAGCTTTGTTAATCATTTATTTGGTCGTTTCCATTGCCCTTATCGCGTTTATCCTGTTACAACAAGGTAAAGGCGCAGATGCAGGCGCATCTTTCGGTGGTGGCGCGTCCGGTACGGTTTTCGGTTCCGCCGGTGCAGGTAACTTCCTGTCCCGAACCACAGCGATTTTAGCAACTCTCTTCTTTATTATCAGTATCGTTATCGGCAACATCAATTCGCACAGAAACAACGTAAAACAAGGCGCATTTGACGATTTATCCGGCACAGCGGAACAAATTCAGCAGCAACAGCAACAACAAGCACCAGCTGTATTAGACACAAAAAACAACGATATTCCTCAA","","","12067","MYSALLIIYLVVSIALIAFILLQQGKGADAGASFGGGASGTVFGSAGAGNFLSRTTAILATLFFIISIVIGNINSHRNNVKQGAFDDLSGTAEQIQQQQQQQAPAVLDTKNNDIPQ","540117","","possible protein-export membrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR004692
Family
Preprotein translocase SecG subunit
PR01651\"[3-23]T\"[23-37]T\"[38-54]T\"[54-76]TSECGEXPORT
PF03840\"[2-75]TSecG
TIGR00810\"[2-74]TsecG: preprotein translocase, SecG subunit
noIPR
unintegrated
unintegrated
signalp\"[1-27]?signal-peptide
tmhmm\"[5-25]?\"[51-71]?transmembrane_regions


","BeTs to 9 clades of COG1314COG name: Preprotein translocase subunitFunctional Class: NThe phylogenetic pattern of COG1314 is -------q-drlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 1 to 88 match (2e-12) PD:PD015286 which is described as MEMBRANE COMPLETE PROTEOME SECG PROTEIN-EXPORT TRANSMEMBRANE TRANSLOCATION INNER PREPROTEIN TRANSLOCASE ","","","","","","","","","","","","Tue Dec 17 15:39:16 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00786 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 75 (E-value = 4.3e-36) place AA00786 in the SecG family which is described as Preprotein translocase SecG subunit (PF03840)","","","","","Nishiyama,K., Mizushima,S. and Tokuda,H. A novel membrane protein involved in protein translocationacross the cytoplasmic membrane of Escherichia coli. EMBO J. 12(9):3409-3415, 1993 PubMed: 8253068. Nishiyama,K., Hanada,M. and Tokuda,H. Disruption of the gene encoding p12 (SecG) reveals the directinvolvement and important function of SecG in the proteintranslocation of Escherichia coli at low temperature. EMBO J. 13(14):3272-3277, 1994. PubMed: 8045257. Bost,S. and Belin,D. A new genetic selection identifies essential residues in SecG,a component of the Escherichia coli protein export machinery. EMBO J. 14(18):4412-4421, 1995. PubMed: 7556084.","","Tue Dec 17 15:39:16 2002","1","","","" "AA00788","540491","540691","201","ATGAAAAATAACGGCGCAGATACTAACGGATATCTTGTCGTTTCGCAAGTCATTTTGTGCATTTTTAGGCGGTTTAGCGCAAATTCGATCAGAAAAAACACCGCTAAAAACCACCGCACTTTTCCGTTCCCGTTAACTTTTCGTGATTCTCGATGTTTTCTTTTTAATGCCCTGCTTTTTGACACCCGAATTATGCCGACT","","","7771","MKNNGADTNGYLVVSQVILCIFRRFSANSIRKNTAKNHRTFPFPLTFRDSRCFLFNALLFDTRIMPT","540691","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 11:43:10 2004","Mon Feb 23 11:43:10 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00788 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 11:43:10 2004","","","","","","","","","","","","","1","","","" "AA00789","542605","540626","1980","GTGAAATCGGCTAACTCCTCTTTTCGTGTCCTCCCGTTTCTTGTTATGCGACTTTTTATAGCGGAAAAACCCAGCCTCGGACGCGCCATCGCCGATGTGTTGCCGAAACCGCACCAGCGCGGTGACGGTTTTATTAAATGCGGCGAGAACGACTGCGTCACTTGGTGCGTGGGGCATTTGCTGGAACAGGCGGAGCCTGATGCGTACGACGCGCGTTTCAAACAATGGCGGCTGGAAGATTTGCCCATCGTGCCGCAAAAATGGCAACTCATTCCGAAAAAAGAAACCCACAAACAGCTGAAAACCGTTGAAAAATTAGTGCAGCAAGCGGATGTCTTGGTCAACGCCGGCGACCCCGATCGCGAAGGACAGTTGTTGGTGGACGAAGTGTTCAGTTATCTCAACCTGCCGGCGGAAAAACGCAATGCCATTCAACGCTGTTTAATCAGCGATTTGAACCCAAGTGCGGTAGAAAAAGCCATCAAAAAATTGCAGCCGAATCGTGATTTTGTCCCGCTTGCTACTTCTGCCTTAGCCCGCGCCCGTGCCGATTGGTTATACGGCATTAACATGACCCGCGCCTATACTATTCACGGTCGGCAGGCGGGCTACGACGGCGTGCTTTCCGTCGGGCGCGTACAAACACCGGTGCTTGGTTTAATCGTGCGCCGTGATTTGGAAATCGAACATTTTCAGCCGAAAGATTTTTTTGAAGTGCTGGCTTGGGTGCGGGATCCGAAAGGTGAAAAAACACCTGAAAAACCGACCGCACTTTTTTCCGCGTTATGGCAACCGAGCAAAGCCTGCGAAGATTATCAGGACGATGACGGACGCGTGTTATCCCGCGCGCTGGCGGAAAATGTGGTAAAACGCATTGCCGACCAACCGGCGGAAGTCACCGATTACACGGACAAACGAGAGAAAGAAACGGCGCCTTTGCCTTATTCGTTATCCGCCCTGCAAATTGATGCCGCCAAGCGTTTTGGGATGTCGGCGCAGGAGGTGCTCGACACGTGTCAGCGCTTGTATGAAACCTACAAATTGATTACTTATCCCCGTTCCGATTGTCGCTATTTACCACAAGAGCATTTTGCCGACCGAATGGCGGTGATGAATGCGATTTCCAGTCATTTATCCCAATTTCAGCCGTTGCCGGAAATCATCGATCCCGAGCAGAAAAATCGTTGCTGGAACGATAAAAAAGTGGAGGCGCACCACGCCATTATTCCCACGGCAAAAAATCGCCCGGTAGGTTTGACTTCGGCAGAACAAAATGTGTATTTTCTGATTGCCCGCCAATACCTCATGCAATTTTGTCCTGATGCGGAATACCGCAAATGTAAAATCACCTTAAATATCGCCGGCGGAACCTTTGTGGCACAGGCGCGCAATTTGCAAATTGCCGGCTGGAAGCAACTTTGGGGCAAAGAAGACAATGACGATGAACAGCAGGACGCGCTGCTGCCCGTGGTAAAAAAAGGGCAAATACTGCATTGCGAAAAGGGCGAGATTGTCAGTAAAAAAACGCAGCCGCCGAAACACTTCACCGACGCGACTTTGCTTTCCGCCATGACAGGCATTGCCCGCTTCGTGCAGGATAAAGAATTGAAAAAAATCTTGCGTGAAACCGATGGGCTTGGTACCGAAGCCACCCGTGCGGGCATCATCGAGTTGTTGTTTAAACGCGGTTTTCTGTATAAAAAAGGGCGCAATATTCACAGCACTGAAGCAGGGAGGATTCTGATTAACGCCTTGCCTGATGTGGCAACTCAGCCCGATATGACCGCACATTGGGAATCCCAGTTGGACGGTATTAGCCGCAAACAGGCGAGTTATCAGCTATTTATGGAAAACCTGACGCAACTTTTGCCGGAATTGTTACATTACATTAATTTTTCCGCCTTGCGTGAGTTAAGTCGGCATAATTCGGGTGTCAAAAAGCAGGGCATTAAAAAGAAAACATCGAGAATCACGAAAAGT","","","74895","VKSANSSFRVLPFLVMRLFIAEKPSLGRAIADVLPKPHQRGDGFIKCGENDCVTWCVGHLLEQAEPDAYDARFKQWRLEDLPIVPQKWQLIPKKETHKQLKTVEKLVQQADVLVNAGDPDREGQLLVDEVFSYLNLPAEKRNAIQRCLISDLNPSAVEKAIKKLQPNRDFVPLATSALARARADWLYGINMTRAYTIHGRQAGYDGVLSVGRVQTPVLGLIVRRDLEIEHFQPKDFFEVLAWVRDPKGEKTPEKPTALFSALWQPSKACEDYQDDDGRVLSRALAENVVKRIADQPAEVTDYTDKREKETAPLPYSLSALQIDAAKRFGMSAQEVLDTCQRLYETYKLITYPRSDCRYLPQEHFADRMAVMNAISSHLSQFQPLPEIIDPEQKNRCWNDKKVEAHHAIIPTAKNRPVGLTSAEQNVYFLIARQYLMQFCPDAEYRKCKITLNIAGGTFVAQARNLQIAGWKQLWGKEDNDDEQQDALLPVVKKGQILHCEKGEIVSKKTQPPKHFTDATLLSAMTGIARFVQDKELKKILRETDGLGTEATRAGIIELLFKRGFLYKKGRNIHSTEAGRILINALPDVATQPDMTAHWESQLDGISRKQASYQLFMENLTQLLPELLHYINFSALRELSRHNSGVKKQGIKKKTSRITKS","540628","","DNA topoisomerase III","Cytoplasm","","
InterPro
IPR000380
Family
DNA topoisomerase, type IA
PR00417\"[113-126]T\"[208-226]T\"[346-355]T\"[426-442]T\"[545-559]TPRTPISMRASEI
PTHR11390\"[38-249]T\"[268-525]T\"[543-630]TPROKARYOTIC DNA TOPOISOMERASE
PS00396\"[340-355]?TOPOISOMERASE_I_PROK
InterPro
IPR003601
Domain
DNA topoisomerase, type IA, domain 2
SM00436\"[143-238]TTOP1Bc
InterPro
IPR003602
Domain
DNA topoisomerase, type IA, DNA-binding
SM00437\"[303-582]TTOP1Ac
InterPro
IPR005738
Family
DNA topoisomerase III, bacterial-type
TIGR01056\"[14-657]TtopB: DNA topoisomerase III
InterPro
IPR006154
Domain
Toprim subdomain
SM00493\"[16-139]TTOPRIM
InterPro
IPR006171
Domain
TOPRIM
PF01751\"[16-150]TToprim
InterPro
IPR013497
Domain
DNA topoisomerase, type IA, central
PF01131\"[166-588]TTopoisom_bac
InterPro
IPR013825
Domain
DNA topoisomerase, type IA, central region, subdomain 2
G3DSA:2.70.20.10\"[233-512]Tno description
InterPro
IPR014396
Family
DNA topoisomerase IA
PIRSF001508\"[16-657]TDNA topoisomerase type IA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.140\"[16-171]Tno description
signalp\"[1-31]?signal-peptide


","BeTs to 26 clades of COG0550COG name: Topoisomerase IAFunctional Class: LThe phylogenetic pattern of COG0550 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 5.3e-97) to 12/12 blocks of the IPB000380 family, which is described as \"Prokaryotic DNA topoisomerase I\". Interpro entry for IP:IPR000380. IPB000380A 18-30 0.047 IPB000380B 46-63 0.00077 IPB000380C 113-130 4.5e-06 IPB000380D 146-157 0.51 IPB000380E 174-197 2.6e-06 IPB000380F 208-239 5.5e-15 IPB000380G 314-344 6e-13 IPB000380H 347-363 2.9e-05 IPB000380I 397-411 0.00012 IPB000380J 425-442 0.00084 IPB000380K 526-565 2.2e-14 IPB000380L 586-604 0.00048","Residues 488 to 612 match (4e-08) PD:PD579779 which is described as TOPOISOMERASE DNA ISOMERASE ENZYME COMPLETE PROTEOME DNA-BINDING I UNTWISTING RELAXING ","","","","","","","","","","","","Tue Dec 17 15:41:23 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00789 is paralogously related to AA02128 (4e-28).","","","","","","Residues 166 to 588 (E-value = 5.4e-182) place AA00789 in the Topoisom_bac family which is described as DNA topoisomerase (PF01131)","","","","","Wang JC. Cellular roles of DNA topoisomerases: a molecularperspective. Nat Rev Mol Cell Biol. 2002 Jun;3(6):430-40. Review. PMID: 12042765 DiGate,R.J. and Marians,K.J. Molecular cloning and DNA sequence analysis of Escherichiacoli topB, the gene encoding topoisomerase III. J. Biol. Chem. 264(30):17924-17930. PubMed: 2553698.","","Tue Dec 17 15:41:23 2002","1","","","" "AA00790","543194","542595","600","ATGCAAACCAGCCCCTTGTTAGAAAATCTGATCGAAAGTTTACGCGTATTGCCGGGCGTCGGTCCGAAATCCGCGCAACGTATGGCGTATCATTTATTGCAACGCAATCGCAGCGGCGGAATGCGCTTGGCGCAAGGGCTGACGGAAGCGATGTCGAAAATCGGGCATTGCGAACATTGCCGCACTTTTACGGAAGAAGACGTGTGCAACATTTGCAGTAATCCACGCCGCCAAAATTCGGGCTTGCTTTGCGTGGTGGAAACGCCGGCGGATATTCTTGCTATCGAGCAAACAGGGCAGTTTTCCGGGCGTTATTTCGTGCTGATGGGGCATTTGTCGCCGCTGGACGGTATCGGCCCGTGCGAAATTGGCTTGGATTTGTTGCAAAAACGCCTGCAAACGGAATCTTTCAATGAAGTGATTTTAGCCACTAACCCGACGGTAGAAGGCGACGCCACAGCAAACTACATTGCGGAGCTTTGCCTGCAACAAAACGTCAAAGTCAGCCGTATTGCCCACGGCATTCCGGTGGGGGGCGAATTGGAAATGGTGGACGGCACCACGCTGACCCATTCCTTCTTAGGTCGCCGTGAAATCGGC","","","21829","MQTSPLLENLIESLRVLPGVGPKSAQRMAYHLLQRNRSGGMRLAQGLTEAMSKIGHCEHCRTFTEEDVCNICSNPRRQNSGLLCVVETPADILAIEQTGQFSGRYFVLMGHLSPLDGIGPCEIGLDLLQKRLQTESFNEVILATNPTVEGDATANYIAELCLQQNVKVSRIAHGIPVGGELEMVDGTTLTHSFLGRREIG","542597","","recombination DNA repair protein","Cytoplasm","","
InterPro
IPR000093
Family
RecR protein
PF02132\"[38-79]TRecR
TIGR00615\"[1-197]TrecR: recombination protein RecR
PS01300\"[57-78]TRECR
InterPro
IPR003583
Domain
Helix-hairpin-helix DNA-binding, class 1
SM00278\"[12-31]THhH1
InterPro
IPR006154
Domain
Toprim subdomain
SM00493\"[81-166]TTOPRIM
InterPro
IPR006171
Domain
TOPRIM
PF01751\"[81-174]TToprim


","BeTs to 17 clades of COG0353COG name: Recombinational DNA repair protein (RecF pathway)Functional Class: LThe phylogenetic pattern of COG0353 is -------q-drlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit (2.9e-107) to 4/4 blocks of the IPB000093 family, which is described as \"RecR putative zinc finger\". Interpro entry for IP:IPR000093. IPB000093A 18-68 1.2e-36 IPB000093B 78-118 1.1e-26 IPB000093C 128-157 2.2e-19 IPB000093D 166-196 3.9e-21","Residues 7 to 91 match (5e-08) PD:PD177752 which is described as RECOMBINATION DNA PROTEOME COMPLETE RECR ZINC-FINGER REPAIR ","","","","","","","","","","","","Tue Dec 17 15:43:21 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00790 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 81 to 174 (E-value = 4.2e-21) place AA00790 in the Toprim family which is described as Toprim domain (PF01751)","","","","","Yeung,T., Mullin,D.A., Chen,K.S., Craig,E.A., Bardwell,J.C.and Walker,J.R. Sequence and expression of the Escherichia coli recR locus J. Bacteriol. 172 (10), 6042-6047 (1990) PubMed: 1698765 Mahdi,A.A. and Lloyd,R.G. The recR locus of Escherichia coli K-12: molecular cloning,DNA sequencing and identification of the gene product Nucleic Acids Res. 17 (17), 6781-6794 (1989) Kantake N, Madiraju MV, Sugiyama T, Kowalczykowski SC. Escherichia coli RecO protein anneals ssDNA complexed with itscognate ssDNA-binding protein: A common step in geneticrecombination. Proc Natl Acad Sci U S A. 2002 Nov 18 PMID: 12438681 Shiraishi K, Hanada K, Iwakura Y, Ikeda H. Roles of RecJ, RecO, and RecR in RecET-mediated illegitimaterecombination in Escherichia coli. J Bacteriol. 2002 Sep;184(17):4715-21. PMID: 12169595 ","","Tue Dec 17 15:43:21 2002","1","","","" "AA00792","543722","543282","441","ATGAATGGTGGCATGAGGCAATGTAACGGTAAAATTGATCGTTTCCAAGCGGCAAATTTTTCGCTAAAATGCATGCACTTTTTTACTCAACTTTTTAATAACGGAAGAAAATTTATGTTCGGAAAAGGCGGATTGGGCAATTTAATGAAACAAGCCCAACAAATGCAAGATCGTATGCAAAAAATGCAGGAAGAAATTGCGCAACTGGAAGTGACCGGCGAATCAGGCGCGGGCTTAGTGAAAATCACCATCAACGGCGCCCACAACTGCCGTCGTGTAGAAATCGATCCTTCTTTAATGGAAGACGATAAAGAGATGTTGGAAGACTTAATCGCCGCGGCATTTAACGATGCAGTGCGTCGTGCCGAAGAGTTACAAAAAGAAAAAATGGCGTCAGTCACCGCCGGTATGTCTTTACCGCCGGGCTTCAAAATGCCGTTT","","","18176","MNGGMRQCNGKIDRFQAANFSLKCMHFFTQLFNNGRKFMFGKGGLGNLMKQAQQMQDRMQKMQEEIAQLEVTGESGAGLVKITINGAHNCRRVEIDPSLMEDDKEMLEDLIAAAFNDAVRRAEELQKEKMASVTAGMSLPPGFKMPF","543284","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR004401
Family
Conserved hypothetical protein 103
PF02575\"[49-140]TDUF149
TIGR00103\"[38-143]TTIGR00103: conserved hypothetical protein T
noIPR
unintegrated
unintegrated
G3DSA:3.30.1310.10\"[36-147]Tno description


","BeTs to 16 clades of COG0718COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG0718 is --------vdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 9.4e-30) to 1/1 blocks of the IPB003727 family, which is described as \"DUF149\". Interpro entry for IP:IPR003727. IPB003727 57-104 8.3e-30","Residues 70 to 137 match (1e-24) PD:PD062413 which is described as PROTEOME COMPLETE YPO3121 AT2G24020/T29E15.22 TM0687 AT2G24020 CJ1642 JHP0031 HP0035 ORF102 ","","","","","","","","","","","","Tue Dec 17 15:44:55 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00792 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 49 to 140 (E-value = 3.5e-53) place AA00792 in the DUF149 family which is described as Uncharacterised BCR, YbaB family COG0718 (PF02575)","","","","","","","","1","","","" "AA00794","543793","544860","1068","ATGGAAACCCGATATTACATCACCATGCTAGCCGCTATGCTGGCACTGCAATTTATGCTATTTGGTTTTAGCCGAACACTTAACTGGATATTTAACCTTAACGGCAAAACACGCCGCACACTGACTATTGTGCTATTTCTTGGACTAAATGCACTCGTATTAAGTGCGCCATTACGTCTTTACACGGAAAGTTTTCGTGTCAGCGCCTTGATTTTAACCCTTTTGCTCTTTTCAACGTTCAGCAGTTTGATCGTCGGTTTTCTCTATTTATTGCGCAAAAAATGGCGTCATTCCTTAAAATGGCTTTATCCAATCCTTTTTTTGAGTTTTATTACTGTCGGTTTATATAATGCTTACGCGCCGGTGGTGCGCCACTATCAGGTGCATTTGGACAAGCCGATGAAGCCGTTGCGGATCGGCATGGCAAGCGACACCCATTTAGGCAAGTTTTTTGGTGGAAAACAACTGGATAAACTTGCAGACATTATGCAACGGGAAAAAGTGGATATTATTTTGCTGCCGGGCGACATTATAGACGATAACGTCAATGCTTATTTAGCGGAGAAAATGCAACCGCACTTAGCCAAACTGAAAGCCCCGCTCGGCGTCTATGCCACCCTTGGCAATCATGATTTTTTCGGCGATCAGGCGCGCATTGAGCGGGAAATTCGGAATGCCGGTATTATTCCGCTGATGGATGAAAGCCTGGTGGTGGATAATCGCTTTGTGTTAATCGGGCGCAACGATGATTTAGTGACCAACCGCCCCTCTACGGAACAATTATTGAAAGGCGTAGATACTAATCTGCCGATTATCCTGTTGGATCATCGCCCGTCGGAAATTGAACAGCACGCCAAGCTGCCTATTGATATTCAACTCTCCGGGCACGCCCATAACGGACAAATTTTCCCGGCGAATCTGATCGTGAAATTCATTTACCGTTTAAGTTACGGTTACGAACAAATTAACGGCGTACACTTCTTCGTCACCTCCGGTTATGGCTTTTGGGGCGTTCCGATGCGTTTAGGCTCACAATCGGAAGTGATGATTATCGACGTGGTTGGAAGT","","","40485","METRYYITMLAAMLALQFMLFGFSRTLNWIFNLNGKTRRTLTIVLFLGLNALVLSAPLRLYTESFRVSALILTLLLFSTFSSLIVGFLYLLRKKWRHSLKWLYPILFLSFITVGLYNAYAPVVRHYQVHLDKPMKPLRIGMASDTHLGKFFGGKQLDKLADIMQREKVDIILLPGDIIDDNVNAYLAEKMQPHLAKLKAPLGVYATLGNHDFFGDQARIEREIRNAGIIPLMDESLVVDNRFVLIGRNDDLVTNRPSTEQLLKGVDTNLPIILLDHRPSEIEQHAKLPIDIQLSGHAHNGQIFPANLIVKFIYRLSYGYEQINGVHFFVTSGYGFWGVPMRLGSQSEVMIIDVVGS","544862","","phosphohydrolase","Inner membrane, Cytoplasm","","
InterPro
IPR004843
Domain
Metallophosphoesterase
PF00149\"[137-300]TMetallophos
InterPro
IPR011156
Family
Membrane-bound phosphoesterase HP1044
PIRSF000888\"[12-356]TPredicted membrane-bound phosphoesterase, HP1044 type
noIPR
unintegrated
unintegrated
G3DSA:3.60.21.10\"[137-304]Tno description
signalp\"[1-26]?signal-peptide
tmhmm\"[4-24]?\"[39-59]?\"[65-87]?\"[102-120]?transmembrane_regions


","BeTs to 8 clades of COG1408COG name: Predicted phosphohydrolasesFunctional Class: RThe phylogenetic pattern of COG1408 is --m----q-drlb-e-----uj-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-09) to 4/4 blocks of the IPB003701 family, which is described as \"DNA repair exonuclease\". Interpro entry for IP:IPR003701. IPB003701A 138-148 0.4 IPB003701B 168-183 0.013 IPB003701C 206-211 22 IPB003701D 289-299 1.9Significant hit ( 3.8e-05) to 3/4 blocks of the IPB000979 family, which is described as \"Uncharacterized protein family UPF0025\". Interpro entry for IP:IPR000979. IPB000979A 137-146 0.25 IPB000979B 166-176 28 IPB000979C 201-211 2.4","Residues 272 to 349 match (1e-15) PD:PD007404 which is described as PROTEOME COMPLETE HYDROLASE SIGNAL PRECURSOR ALL0250 PHOSPHOHYDROLASE AQ_1054 PREDICTED F40B5.2 ","","","","","","","","","","","","Thu Feb 20 08:40:57 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00794 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 137 to 300 (E-value = 9.6e-13) place AA00794 in the Metallophos family which is described as Calcineurin-like phosphoesterase (PF00149)","","","","","","","","1","","","" "AA00795","544933","545823","891","ATGAAAAACTTTTTAAAAGCGACTTTCGCTTCACTTCTCTTTATTGGTTCAACTCACGCCGGCGCAGTAACGGTTACCGATGCAAAAGGCGAATTTACTATTGATCAAACACCAACCCGTATTGTGGCGTTGGAATATTCCTTTGTGGATGCATTGGCGCAAGTAGGCGTTAGTCCTGTCGGGGTTGCCGATGACAACAATAAAGAACGGATTTTGAAAGAAGTACGCGACAAAATTGAATCTTGGCAATCCGTCGGTACCCGCTCGCAACCGAGCCTTGAAGCCATCGCGGCATTAAAACCCGATTTAATCATCGCCGATCCTTCCCGTCATACCGCCGTGTATGAAGAATTGAAAAAAATCGCACCGACCATGATGTTTGATTCCCGCCATGAAAGCTATCAGGAAAACCTGGAAACCGCGCAGAAAATCGGTGATGTCGTGGGTAAAGGCGGCGAAATGAAACTGCAAATCAACAAACATAACGAATACATCGAAAACATTGCCAAATCCATTAATGTGAAAGGACAAAAAGGCGTATTCGGCACATCCCGCGAAGATAAATTCAACCTACAAAACGACAACGGCTATGTCGCCAGCTTCTTAGGCGTACTCGGTTTTGAAACGCCGAAATTACCAAACAGCACTCAAGCCTTCGTGGAAATCAACCTGGAACAATTGGTCATGGAAAAACCGGATTATTTGTTCATTGCACACTATCGTCAGGAAAGTATCGCCCGCAAATGGGAAAACGAGCCTTTGTGGCAGGCGATTCCGGCGGTAAAAGCCAAACAGGTGTTCAGCGTTGATGCCGATATGTGGGCGCGCGGACGCGGTATGGCGGCCAGTGAAATTATGGCGAAGCAAGTTGAGCAATTTGTGCAGCAAAAA","","","33142","MKNFLKATFASLLFIGSTHAGAVTVTDAKGEFTIDQTPTRIVALEYSFVDALAQVGVSPVGVADDNNKERILKEVRDKIESWQSVGTRSQPSLEAIAALKPDLIIADPSRHTAVYEELKKIAPTMMFDSRHESYQENLETAQKIGDVVGKGGEMKLQINKHNEYIENIAKSINVKGQKGVFGTSREDKFNLQNDNGYVASFLGVLGFETPKLPNSTQAFVEINLEQLVMEKPDYLFIAHYRQESIARKWENEPLWQAIPAVKAKQVFSVDADMWARGRGMAASEIMAKQVEQFVQQK","545825","","iron(III) dicitrate-binding periplasmic protein precursor","Periplasm, Cytoplasm","","
InterPro
IPR002491
Family
Periplasmic binding protein
PF01497\"[38-273]TPeripla_BP_2
PS50983\"[40-297]TFE_B12_PBP
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1980\"[34-127]Tno description
signalp\"[1-20]?signal-peptide


","BeTs to 16 clades of COG0614COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, periplasmic componentsFunctional Class: PThe phylogenetic pattern of COG0614 is aompkz--vdrlbcefgh-nuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 9.9e-06) to 2/2 blocks of the IPB002491 family, which is described as \"Periplasmic binding protein\". Interpro entry for IP:IPR002491. IPB002491A 38-43 17 IPB002491B 92-102 0.00031","Residues 13 to 82 match (8e-21) PD:PD579274 which is described as COMPLETE PROTEOME FECB PERIPLASMIC IRONIII SAV2177 YFMC SIGNAL SAV1038 PRECURSOR ","","","","","","","","","","","","Tue Dec 17 16:15:09 2002","","Mon Mar 15 16:51:55 2004","Mon Mar 15 16:52:59 2004","Mon Mar 15 16:51:55 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00795 is paralogously related to AA01827 (2e-12) and AA02154 (0.001).","Mon Mar 15 16:51:55 2004","","","","","Residues 38 to 273 (E-value = 3.3e-54) place AA00795 in the Peripla_BP_2 family which is described as Periplasmic binding protein (PF01497)","Mon Mar 15 16:51:55 2004","","","","Staudenmaier,H., Van Hove,B., Yaraghi,Z. and Braun,V.Nucleotide sequences of the fecBCDE genes and locations of theproteins suggest a periplasmic-binding-protein-dependent transportmechanism for iron(III) dicitrate in Escherichia coliJ. Bacteriol. 171 (5), 2626-2633 (1989)PubMed: Velayudhan J, Hughes NJ, McColm AA, Bagshaw J, Clayton CL, Andrews SC, Kelly DJ.Iron acquisition and virulence in Helicobacter pylori: a major role for FeoB, a high-affinity ferrous iron transporter.Mol Microbiol. 2000 Jul;37(2):274-86.PMID: 10931324Angerer A, Braun V.Iron regulates transcription of the Escherichia coli ferric citrate transport genes directly and through the transcription initiation proteins.Arch Microbiol. 1998 Jun;169(6):483-90.PMID: 9575233","","Mon Feb 17 14:07:32 2003","1","","","" "AA00796","545826","546812","987","ATGTTAAGCACCACCGTTCGTTGGGGCTTGCCCATTATCTTACTGGCTTTCCTGTTATGGGGAAGCCTGTTTTTGTATTACCCCATCGCCATTGCCCCGTTAGATGCCTTAAACGCCTTTTTACCCGACGGGGATGATCTGGCGAAAATTACCGTGGTGGGTTTACGCTTTCCGCGTGCTTTGGTGGCAATCGCCCTTGGCGCAAATTTAGCGGTCGCCGGTGCCTTATTGCAAACCGTCACCCGCAACCCATTAGCCTCCCCTTCCCTGTTAAGCGTCAACTCAGGCGCTGGATTGGCAATGGTCATCACCAGCGTCCTCAGCCCTTCACTGTTATCCGGTTACAGCATTGCTTTAATCGCAAGCATCGGGGGCGGCATCAGCTGGCTTACCGTGATGCTTATCAGCAATGCCTGGCACGACAATAGCGGCGATCGCAGTCGCGTCATTCTTGCCGGTATCGCCGTTTCCTTACTCTGCGCCGCCGCCACGAAATTACTCTTAATCGTCGCCGATGATAACGCCTTCGGCGTCATGAGTTGGCTTGCCGGCGGAATTTCTCACGCACGCTGGAAAGAATGGCATATCATTTGGCCTTTCTTACTATCAAGTGCGTTATTTTGTCTCTTCTTCGCCAGCAAGTTAAACCTGCTCAATCTCAGCGATGAATCCGCCCGTTCTTTGGGAATCAACCTTTTCCGCTTACGTTGGTATGCCAATATTATGGCATTACTCATCGTCGGTTCCGCCGTCAGCGTTGCCGGTCAGGTGGCGTTTATCGGACTGCTGATTCCCCATTTGGCGCGTTATTGGATCGGTTACGATTTACGCAAATCCCTCCCCATGTCCATGTTGCTTGGCGCCATGTTAATGCTCATCGCAGACACCATGGCAAGAGCGGTCAATTTTCCAAACGAAGTGCCTGCCGGCGCGGTATTGGCACTCATCGGCGCACCGGTATTCGTGTTATTTGCCAGAGGAAGACGC","","","35066","MLSTTVRWGLPIILLAFLLWGSLFLYYPIAIAPLDALNAFLPDGDDLAKITVVGLRFPRALVAIALGANLAVAGALLQTVTRNPLASPSLLSVNSGAGLAMVITSVLSPSLLSGYSIALIASIGGGISWLTVMLISNAWHDNSGDRSRVILAGIAVSLLCAAATKLLLIVADDNAFGVMSWLAGGISHARWKEWHIIWPFLLSSALFCLFFASKLNLLNLSDESARSLGINLFRLRWYANIMALLIVGSAVSVAGQVAFIGLLIPHLARYWIGYDLRKSLPMSMLLGAMLMLIADTMARAVNFPNEVPAGAVLALIGAPVFVLFARGRR","546814","","iron(III) dicitrate transport system permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR000522
Family
Bacterial transport system permease protein
PF01032\"[15-327]TFecCD
noIPR
unintegrated
unintegrated
signalp\"[1-24]?signal-peptide
tmhmm\"[10-30]?\"[57-77]?\"[89-109]?\"[115-135]?\"[150-170]?\"[200-220]?\"[241-263]?\"[307-325]?transmembrane_regions


","BeTs to 18 clades of COG0609COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, permease componentsFunctional Class: P,HThe phylogenetic pattern of COG0609 is aompkz--vd-lbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is","Significant hit ( 8.4e-38) to 3/3 blocks of the IPB000522 family, which is described as \"FecCD transport family\". Interpro entry for IP:IPR000522. IPB000522A 56-97 2.1e-21 IPB000522B 255-269 1.9e-06 IPB000522C 304-327 5.5e-07","Residues 150 to 218 match (2e-11) PD:PD247701 which is described as PROTEOME COMPLETE PERMEASE ABC MEMBRANE IRON SYSTEM TRANSPORTER FERRICHROME TRANSMEMBRANE ","","","","","","","","","","","","Tue Dec 17 16:25:49 2002","","Mon Mar 15 16:54:03 2004","Mon Mar 15 16:54:03 2004","Mon Mar 15 16:54:03 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00796 is paralogously related to AA00798 (3e-45), AA02144 (3e-37), AA02153 (2e-36), AA01826 (2e-30), AA01825 (3e-12) and AA01818 (6e-05).","Mon Mar 15 16:54:03 2004","","","","","Residues 28 to 326 (E-value = 2.3e-94) place AA00796 in the FecCD family which is described as FecCD transport family (PF01032)","Mon Mar 15 16:54:03 2004","","","","Staudenmaier,H., Van Hove,B., Yaraghi,Z. and Braun,V.Nucleotide sequences of the fecBCDE genes and locations of theproteins suggest a periplasmic-binding-protein-dependent transportmechanism for iron(III) dicitrate in Escherichia coliJ. Bacteriol. 171 (5), 2626-2633 (1989)PubMed: 2651410","","Tue Dec 17 16:24:47 2002","1","","","" "AA00798","546815","547795","981","ATGAAAAATGCCTATCATAAATTGCTTTCTCTCGGTTTTTACCCGTTTGCCGTGGTCGCCGTTATTGCCTTATTTATTTTAAGTCTTCGCTTAGGCACTTATACCCTCTCCTTTTCGGAAATTGTCGCGGCGTTTAATTCCGACGATAAAAACCATTTCACGCTGATTGAATACCGCCTGCCCCGTGCGTTGCTGGCAATTTTTATCGGCGGTACATTAGCCATTTCCGGGGTGTTGGTGCAAAGTGTGGTGCGTAATCCGTTAGCGTCACCGGATATTCTGGGCATTAATAACGCGGCGGGGCTGGTTGCCATCGCCATATTAATCTTTTTGCCGAACCTCGCCTTTTACTGGATTCCATTCTTTGCGTTTATCGGCGGCATATTGTCTTTCATCTTGTTATGGGTGATTTGCGGCTTTAATTTCCGTCCGATCAGGATGGCGATCATCGGAGTGGCGATTTCCGCCTTGTGGGCGGCGATCAACCATTATGTGATGCTCACCAATCCTGTAGAAATCAACACGGCAATGCTCTGGCTGACAGGCAGTTTATGGGGAAGAAGCTGGACCTACGCGAATGTGGTGTTGCCTTGGCTATTCCTTCTGCTGCCCCTACCGTTCATTTTTTGCCGCGATCTCGACACCTTGGGCTTGGGCGAAAATAAAGCCGCCACCTTGGGCGTTCACGTCAACAAAACTCAGATTTTCGTCTTAGTGCTGGCAGTAGCGCTCTCCACCACCGCTGTCGCCATTTGCGGCCCTATCGCCTTTTTAGGTTTGGTCGCACCGCATTTGGCACGCAAATTGGTGGGCGGACGACACCGCACTTTACTGCCTGCGGCATTGTTAATCGGAGCGTTATTGCTACAAATTTCCGATATTTTAGCGCGCGTCATCGATCCGCCGACCGAGTTGCCGGCAGGCATTCTGACCGCCATTATCGGCGCCCCTTACTTCTTCTATTTATTGATGAGAACCAAA","","","46651","MKNAYHKLLSLGFYPFAVVAVIALFILSLRLGTYTLSFSEIVAAFNSDDKNHFTLIEYRLPRALLAIFIGGTLAISGVLVQSVVRNPLASPDILGINNAAGLVAIAILIFLPNLAFYWIPFFAFIGGILSFILLWVICGFNFRPIRMAIIGVAISALWAAINHYVMLTNPVEINTAMLWLTGSLWGRSWTYANVVLPWLFLLLPLPFIFCRDLDTLGLGENKAATLGVHVNKTQIFVLVLAVALSTTAVAICGPIAFLGLVAPHLARKLVGGRHRTLLPAALLIGALLLQISDILARVIDPPTELPAGILTAIIGAPYFFYLLMRTK","547797","","iron(III) dicitrate transport system permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR000522
Family
Bacterial transport system permease protein
PF01032\"[20-325]TFecCD
noIPR
unintegrated
unintegrated
signalp\"[1-32]?signal-peptide
tmhmm\"[9-29]?\"[64-84]?\"[94-112]?\"[118-138]?\"[147-167]?\"[189-209]?\"[235-257]?\"[276-296]?\"[305-323]?transmembrane_regions


","BeTs to 18 clades of COG0609COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, permease componentsFunctional Class: P,HThe phylogenetic pattern of COG0609 is aompkz--vd-lbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-47) to 3/3 blocks of the IPB000522 family, which is described as \"FecCD transport family\". Interpro entry for IP:IPR000522. IPB000522A 59-100 1.5e-20 IPB000522B 253-267 3.4e-09 IPB000522C 302-325 4.7e-15","Residues 19 to 134 match (4e-09) PD:PD100245 which is described as PROTEOME COMPLETE YFME ","","","","","","","","","","","","Fri Sep 5 16:18:24 2003","","Mon Mar 15 16:54:30 2004","Mon Mar 15 16:54:30 2004","Mon Mar 15 16:54:30 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00798 is paralogously related to AA00796 (3e-45), AA02153 (1e-43), AA02144 (5e-38), AA01826 (6e-29) and AA01825 (8e-15).","Mon Mar 15 16:54:30 2004","","","","","Residues 32 to 325 (E-value = 6e-110) place AA00798 in the FecCD family which is described as FecCD transport family (PF01032)","Mon Mar 15 16:54:30 2004","","","","Staudenmaier,H., Van Hove,B., Yaraghi,Z. and Braun,V.Nucleotide sequences of the fecBCDE genes and locations of theproteins suggest a periplasmic-binding-protein-dependent transportmechanism for iron(III) dicitrate in Escherichia coliJ. Bacteriol. 171 (5), 2626-2633 (1989)PubMed: 2651410","","Tue Dec 17 16:28:16 2002","1","","","" "AA00799","547798","548562","765","ATGAGTATTGTTATCAACAACTTACAATTGGGTTATCAAAATAAAATCATCGTGCAGGATTTGTCGTTGGACTTTCCGCATAACCAAGTGATTGCCTTAATCGGACCGAACGGTTGCGGCAAATCCACCACCCTGAAAGCCATTGCCCGCCTGCTCAAACCGCGTACCGGCAAGATTACACATCATGGCAAAGATATTTGGCAAAGCACCCCGAAAGAATACGCCAAAGCCCTGTCTTTCCTGCCGCAACAACATTTAGTGCCGGAGGGCATTAAAGTGCGCGAGCTGATCGCCTACGGTCGTTCGCCTTATTTAAATTTATGGGGCAAATTGAACGATAAAGATGAAGCGTTGGTAACCTGGTCAATGGAACAAACCCACACCACAGAGTTGGCGAACAGATTAGTCTCCGATTTATCCGGCGGTCAGCAACAACGGGTATTCTTAGCCATGACATTGGCGCAGGATGCGGAATTGGTTTTGTTAGATGAACCCACCACTTATCTCGATTTAAACCGCCAAGCGGAACTCATGGGCATGATGCGCCAAATGCAACAAAACGGCAAAACCGTGATCACCGTACTGCATGATTTAAACCAAGCCTGTCGTTACTGCGATTATTTGGTCGTGCTAAAAGACGGCAACCTGATGGCGAAAGGCACGCCGGATGAAGTGATGTCGGAAGAACTTTTGAAAACCGTGTTTGACCTGGATGTGGAGATTCATCGCGATCCGGTCAGCCAAACACCGATGTTTATTTTGAAA","","","28769","MSIVINNLQLGYQNKIIVQDLSLDFPHNQVIALIGPNGCGKSTTLKAIARLLKPRTGKITHHGKDIWQSTPKEYAKALSFLPQQHLVPEGIKVRELIAYGRSPYLNLWGKLNDKDEALVTWSMEQTHTTELANRLVSDLSGGQQQRVFLAMTLAQDAELVLLDEPTTYLDLNRQAELMGMMRQMQQNGKTVITVLHDLNQACRYCDYLVVLKDGNLMAKGTPDEVMSEELLKTVFDLDVEIHRDPVSQTPMFILK","548564","","iron(III) dicitrate transport ATP-binding protein","Cytoplasm, Inner membrane","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[139-181]TQ9CPC0_PASMU_Q9CPC0;
PF00005\"[28-214]TABC_tran
PS50893\"[3-238]TABC_TRANSPORTER_2
PS00211\"[139-153]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[27-214]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[3-236]Tno description
PTHR19222\"[3-251]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF31\"[3-251]TMETAL ABC TRANSPORTER


","BeTs to 17 clades of COG1120COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, ATPase componentsFunctional Class: P,HThe phylogenetic pattern of COG1120 is aompk---vdrlbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.6e-26) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 17-63 1.6e-16 IPB001140B 136-174 2.3e-08 IPB001140C 191-220 2.9e+02Significant hit ( 7.8e-05) to 1/5 blocks of the IPB000897 family, which is described as \"GTP-binding signal recognition particle (SRP54) domain\". Interpro entry for IP:IPR000897. IPB000897A 30-49 8e-05","Residues 71 to 135 match (4e-07) PD:PD506944 which is described as ATP-BINDING ABC COMPLETE PROTEOME FERRICHROME TRANSPORTER ","","","","","","","","","","","","Wed Mar 10 15:21:55 2004","","Wed Mar 10 15:21:55 2004","Mon Mar 15 16:55:11 2004","Wed Mar 10 15:21:55 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00799 is paralogously related to AA01824 (2e-40), AA01051 (4e-28), AA02550 (2e-27), AA02152 (1e-26), AA00700 (6e-25), AA01645 (4e-24), AA02320 (2e-23), AA02324 (3e-22), AA01656 (1e-21), AA02718 (2e-21), AA00858 (4e-21), AA02899 (8e-20), AA02353 (1e-19), AA00415 (3e-19), AA02140 (8e-19), AA00933 (2e-18), AA01820 (2e-18), AA00207 (3e-18), AA01867 (9e-18), AA01509 (2e-17), AA02805 (4e-17), AA01524 (5e-17), AA02080 (2e-16), AA01393 (2e-16), AA00751 (9e-16), AA02786 (7e-15), AA01422 (7e-15), AA02606 (1e-14), AA01616 (1e-14), AA01510 (1e-14), AA02898 (2e-14), AA01779 (2e-14), AA02609 (2e-14), AA02331 (2e-14), AA01961 (2e-14), AA02642 (8e-14), AA02440 (2e-13), AA01456 (5e-13), AA01684 (1e-12), AA02146 (2e-12), AA00934 (4e-12), AA00061 (6e-12), AA02484 (2e-11), A02145 (4e-11), AA02573 (6e-11), AA01947 (8e-11), AA01568 (9e-10), AA01569 (2e-09), AA01555 (2e-09), AA01291 (1e-08), AA02225 (3e-08), AA01757 (3e-08) and AA00591 (9e-08).","Wed Mar 10 15:21:55 2004","","","","","Residues 28 to 214 (E-value = 4.3e-56) place AA00799 in the ABC_tran family which is described as ABC transporter (PF00005)","Wed Mar 10 15:21:55 2004","","","","Staudenmaier,H., Van Hove,B., Yaraghi,Z. and Braun,V.Nucleotide sequences of the fecBCDE genes and locations of theproteins suggest a periplasmic-binding-protein-dependent transportmechanism for iron(III) dicitrate in Escherichia coliJ. Bacteriol. 171 (5), 2626-2633 (1989)PubMed: 2651410","","Tue Dec 17 16:32:07 2002","1","","","" "AA00801","549599","548634","966","TTGGAACAGGAACAATGGCAGCCCACGGCATCCATTAAAAATTTACTTGCCCGCGCCAAATTCATGGCGGAAATTCGTCGATTTTTCACCGATCGTGGTTTATTGGAAGTGGAAACACCGGTGTTAAGCGAATTTGGTGTGACAGATGTTCACCTTGCTACCTTTAGCACGGAATTCATTTCCCCTTTCGGCGAGCAATCTAAAAAATTGTGGCTTTCCACCAGCCCGGAATATCACATGAAACGTTTGTTGGCGGCGGGCAGCGGTCCGATTTTTCAAATCGGCAAAGTGTTTCGTAACGAAGAAGCAGGCAATCGTCACAATCCGGAATTTACCATGCTGGAATGGTATCGCCCGCATTTCGATATGTACCGTTTAATCAATGAAGTGGATGATTTGTTGCAGCAGATTCTGGAATGCCCACCGGCGGAGAGCATGAGTTATCAGTTCGCTTTTCAGCAATATGTGGGCTTGGATCCTTTATCGGCGGAACATGAAGAATTGGTGGAAAAAGCCAAAAAATATCAACTGATGAACGCCGAAGAAGAAAATCGCGACACTTTGTTACAATTCCTTTTCAGCGCCGTGGTGGAAGCGCAAATCGGGCAGGAAAGCCCCGTGGTGGTGTATCATTTCCCGGCAAGTCAGGCGGCGTTGGCACAAATCAGTTCGGAAGATTTACGGGTGGCGGAACGTTTCGAGTTTTACTATAAAGGCTTGGAGCTTGCCAATGGTTTTCATGAACTGTCCGACGCGCGCGAACAATTAAGACGTTTTGAACAGGATAATCACCAGCGGGAAAAAATGGGCTTGCCGCCACAAACGATTGATACCCGTTTGTTATCCGCTTTGCAAGCGGGCATTCCGAACTGTTCCGGTGTGGCGCTTGGCGTGGATCGTCTGTTGATAATTGCCATGGGTGCGGAAAGCATTAAAGAAGTGATTTCTTTCGCCATTGATAATGCC","","","36859","LEQEQWQPTASIKNLLARAKFMAEIRRFFTDRGLLEVETPVLSEFGVTDVHLATFSTEFISPFGEQSKKLWLSTSPEYHMKRLLAAGSGPIFQIGKVFRNEEAGNRHNPEFTMLEWYRPHFDMYRLINEVDDLLQQILECPPAESMSYQFAFQQYVGLDPLSAEHEELVEKAKKYQLMNAEEENRDTLLQFLFSAVVEAQIGQESPVVVYHFPASQAALAQISSEDLRVAERFEFYYKGLELANGFHELSDAREQLRRFEQDNHQREKMGLPPQTIDTRLLSALQAGIPNCSGVALGVDRLLIIAMGAESIKEVISFAIDNA","548636","","lysine--tRNA ligase","Cytoplasm","","
InterPro
IPR002313
Family
Lysyl-tRNA synthetase, class-2
PR00982\"[30-40]T\"[98-115]TTRNASYNTHLYS
InterPro
IPR004364
Domain
tRNA synthetase, class II (D, K and N)
PF00152\"[13-322]TtRNA-synt_2
InterPro
IPR004525
Family
Lysyl-tRNA synthetase-related protein
TIGR00462\"[2-322]TgenX: lysyl-tRNA synthetase homolog GenX
InterPro
IPR006195
Domain
Aminoacyl-transfer RNA synthetase, class II
PS50862\"[18-322]TAA_TRNA_LIGASE_II
noIPR
unintegrated
unintegrated
G3DSA:3.30.930.10\"[8-318]Tno description
PTHR22594\"[11-319]TASPARTYL/LYSYL-TRNA SYNTHETASE
PTHR22594:SF7\"[11-319]TLYSYL-TRNA SYNTHETASE


","BeTs to 6 clades of COG2269COG name: Truncated, possibly inactive Class II lysyl-tRNA synthetaseFunctional Class: JThe phylogenetic pattern of COG2269 is -------q------e-ghs--j--t-Number of proteins in this genome belonging to this COG is","","Residues 8 to 95 match (3e-29) PD:PD012582 which is described as REPRESSOR TRP TRANSCRIPTION OPERON REGULATION DNA-BINDING COMPLETE PROTEOME HOMOLOG 3D-STRUCTURE ","","","","","","","","","","","","Tue Dec 17 17:05:43 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00801 is paralogously related to AA01743 (3e-33), AA02856 (5e-08) and AA02233 (3e-07).","","","","","","Residues 1 to 322 (E-value = 6.6e-124) place AA00801 in the tRNA-synt_2 family which is described as tRNA synthetases class II (D, K and N) (PF00152)","","","","","Kong,L., Fromant,M., Blanquet,S. and Plateau,P. Evidence for a new Escherichia coli protein resembling alysyl-tRNA synthetase. Gene 108 (1), 163-164 (1991) PubMed: 1761227. Cole,S.T. Nucleotide sequence coding for the flavoprotein subunit of thefumarate reductase of Escherichia coli. Eur. J. Biochem. 122 (3), 479-484 (1982) PubMed: 7037404. Gampel,A. and Tzagoloff,A. Homology of aspartyl- and lysyl-tRNA synthetases. Proc. Natl. Acad. Sci. U.S.A. 86 (16), 6023-6027 (1989) PubMed: 2668951 ","","Tue Dec 17 17:05:43 2002","1","","","" "AA00803","549666","549851","186","ATGCAAAAACACCTTGAGAATCGACCGCACTTTTTACTCTCACCGTGTATTTTTGCACAATATTTAAGAATAAAAAACGAACAACTCACTCTTCTTTCTAACTTTTTTGAGTTAGATCACGAAAGTATAACAAAAGTGAGAAAAAAGATTTTAATCCCCCCAAATAGTGGCAAAATGACGCTACCC","","","7301","MQKHLENRPHFLLSPCIFAQYLRIKNEQLTLLSNFFELDHESITKVRKKILIPPNSGKMTLP","549853","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Tue Dec 17 17:10:25 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00803 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00804","549910","551715","1806","GTGCAAACTGTTAACGTCGATATCGCCATTGTTGGCGCAGGTGGTGGTGGTTTACGTGCGGCGATTGCTGCAGCTCAAGCTAATCCAAATCTTAAAATTGCTTTAATATCAAAAGTTTATCCAATGCGCAGTCATACTGTTGCGGCTGAAGGTGGTGCTGCGGCAGTCATTAAAGAAGAAGATTCCTACGACAAACACTTCCATGATACCGTTGCCGGTGGTGACTGGTTATGTGAACAAGATGTGGTGGAATATTTCGTTGAACATTCCCCGGTGGAAATGACTCAGCTTGAACGTTGGGGCTGCCCTTGGAGTCGTAAAACCGATGGTGATGTGAACGTGCGTCGTTTCGGTGGAATGAAAATCGAACGTACTTGGTTCGCCGCCGATAAAACCGGTTTCCATTTGCTTCACACCTTATTCCAAACCTCCATTCAATTCCCGCAAATCATCCGTTTCGATGAACACTTCGTGTTGGATATTTTAGTAGATGACGTTCATGCCCGCGGTATGGTTGCCATGAACATGATGGAAGGCACCTTGGTACAAATCAATGCCAATGCGGTGGTTATCGCAACCGGCGGTGGTTGCCGTGCATTCCGTTTCAATACCAACGGCGGTATCGTGACCGGTGACGGCTTATCCATGGCATATCGTCACGGCGTTCCTCTGCGCGACATGGAATTCGTCCAATATCACCCGACCGGCTTACCGAACACCGGCATCTTAATGACCGAAGGTTGTCGTGGTGAAGGCGGTATTTTGGTCAATAAAGACGGCTACCGCTACTTACAAGATTACGGTTTGGGACCGGAAACCCCAATCGGCAAACCGGAAAACAAATACATGGAATTAGGTCCGCGCGATAAAGTTTCCCAAGCTTTCTGGCAAGAATGGCGTAAAGGCAACACGTTAAAAACCGCGAAAGGCGTTGATGTGGTGCATTTGGATTTACGCCATCTCGGTGAAAAATACTTACACGAGCGTTTACCGTTCATTTGCGAATTGGCGAAAGCTTATGAAGGTGTGGATCCGGCACAAGCGCCGATTCCGGTACGTCCTGTTGTACACTACACTATGGGCGGTATCGAAGTTGACTTCAACAGCGAAACCCGCATTAAAGGCTTATTTGCTGTGGGCGAATGTGCCTCTTCCGGCTTACACGGTGCCAACCGTTTAGGCTCCAACTCCTTGGCTGAATTAGTGGTATTAGGTCGCGTCGCCGGTAAATACGCCGCACAACGCGCCGTTGAAGCTACTCCTGCCAACCAAGCGGCAGTAGATGCGCAAGCACAAGACATTGTTAATCGTTTGAACGCATTATACGATCAAGAAGGTACCGAATCCTGGTCCGATATTCGTGATGAAATGGGTCAAGCCATGGAAGAAGGTTGCGGTATTTATCGTACCCAAGAAAGTATGCAACAAGCGGTGGATAAAATCGCCGAACTCAAAGAACGTTACAAACATATTCGTATTACCGATCGTTCCAGCGTGTTCAACACAAACGTGCTCTACACCGTGGAATTAGGTTATATCCTGGATGTGGCACAATCTATCGCCAATTCCGCTATTGAACGTAAAGAATCCCGTGGCGCGCACCAACGCTTGGATTACACCGAACGTGATGATGTGAACTACTTAAAACATACCTTAGCGTTTTATAACGAAAACGGCGCACCGCGTATCGAATACAGCCCGGTGAAAATCACCAAATCACAACCGGCAAAACGTGTTTACGGCGCGGAAGCAGAAGCTGCAGAAGCGGCAGCGAAGGCGAAAGAACAAGCTCAAGCGGGTAAGGAG","","","66329","VQTVNVDIAIVGAGGGGLRAAIAAAQANPNLKIALISKVYPMRSHTVAAEGGAAAVIKEEDSYDKHFHDTVAGGDWLCEQDVVEYFVEHSPVEMTQLERWGCPWSRKTDGDVNVRRFGGMKIERTWFAADKTGFHLLHTLFQTSIQFPQIIRFDEHFVLDILVDDVHARGMVAMNMMEGTLVQINANAVVIATGGGCRAFRFNTNGGIVTGDGLSMAYRHGVPLRDMEFVQYHPTGLPNTGILMTEGCRGEGGILVNKDGYRYLQDYGLGPETPIGKPENKYMELGPRDKVSQAFWQEWRKGNTLKTAKGVDVVHLDLRHLGEKYLHERLPFICELAKAYEGVDPAQAPIPVRPVVHYTMGGIEVDFNSETRIKGLFAVGECASSGLHGANRLGSNSLAELVVLGRVAGKYAAQRAVEATPANQAAVDAQAQDIVNRLNALYDQEGTESWSDIRDEMGQAMEEGCGIYRTQESMQQAVDKIAELKERYKHIRITDRSSVFNTNVLYTVELGYILDVAQSIANSAIERKESRGAHQRLDYTERDDVNYLKHTLAFYNENGAPRIEYSPVKITKSQPAKRVYGAEAEAAEAAAKAKEQAQAGKE","551717","","fumarate reductase flavoprotein subunit A","Cytoplasm, Periplasm","","
InterPro
IPR001100
Family
Pyridine nucleotide-disulphide oxidoreductase, class I
PR00411\"[7-29]T\"[376-383]TPNDRDTASEI
InterPro
IPR003952
Binding_site
Fumarate reductase/succinate dehydrogenase, FAD-binding site
PS00504\"[43-52]TFRD_SDH_FAD_BINDING
InterPro
IPR003953
Domain
Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal
PF00890\"[7-398]TFAD_binding_2
InterPro
IPR004112
Domain
Fumarate reductase/succinate dehydrogenase flavoprotein, C-terminal
PF02910\"[454-580]TSucc_DH_flav_C
InterPro
IPR005884
Family
Fumarate reductase, flavoprotein subunit
TIGR01176\"[3-581]Tfum_red_Fp: fumarate reductase, flavoprotei
InterPro
IPR013027
Domain
FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PR00368\"[7-29]T\"[376-383]TFADPNR
InterPro
IPR014006
Family
Succinate dehydrogenase or fumarate reductase, flavoprotein subunit
TIGR01812\"[7-580]TsdhA_frdA_Gneg: succinate dehydrogenase or
noIPR
unintegrated
unintegrated
G3DSA:1.20.58.100\"[424-543]Tno description
G3DSA:3.50.50.60\"[1-424]Tno description
PTHR11632\"[7-580]TSUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT
PTHR11632:SF5\"[7-580]TSUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT


","BeTs to 23 clades of COG1053COG name: Succinate dehydrogenase/fumarate reductase, flavoprotein subunitsFunctional Class: CThe phylogenetic pattern of COG1053 is aomp-zyqvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit (4.3e-221) to 10/10 blocks of the IPB003952 family, which is described as \"Fumarate reductase / succinate dehydrogenase FAD-binding site\". Interpro entry for IP:IPR003952. IPB003952A 7-21 1e-07 IPB003952B 30-59 2e-18 IPB003952C 61-76 2.5e-09 IPB003952D 91-119 1.6e-16 IPB003952E 124-141 7.9e-12 IPB003952F 210-260 2e-41 IPB003952G 315-366 3.1e-34 IPB003952H 375-406 2.5e-20 IPB003952I 437-489 1.1e-26 IPB003952J 504-544 1e-23Significant hit ( 3.8e-10) to 3/5 blocks of the PR00368 family, which is described as \"FAD-dependent pyridine nucleotide reductase signature\". Prints database entry for PR:PR00368. PR00368A 7-29 5.3e-08 PR00368B 189-198 8.6 PR00368E 376-383 1.6e+02Significant hit ( 4.1e-06) to 1/5 blocks of the IPB000103 family, which is described as \"Pyridine nucleotide-disulphide oxidoreductase class-II\". Interpro entry for IP:IPR000103. IPB000103A 7-27 4.2e-06","Residues 516 to 553 match (3e-08) PD:PD582076 which is described as FLAVOPROTEIN FUMARATE SUBUNIT COMPLETE FAD OXIDOREDUCTASE PROTEOME REDUCTASE REDUCTASE ELECTRON ","","","","","","","","","","","","Tue Dec 17 17:11:38 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00804 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 454 to 580 (E-value = 2.5e-72) place AA00804 in the Succ_DH_flav_C family which is described as Fumarate reductase/succinate dehydrogenase flavoprotein C-terminal domain (PF02910)","","","","","ole,S.T. Nucleotide sequence coding for the flavoprotein subunit thefumarate reductase of Escherichia coli. Eur. J. Biochem. 122 (3), 479-484 (1982) PubMed: 7037404. Blaut,M., Whittaker,K., Valdovinos,A., Ackrell,B.A.,Gunsalus,R.P. and Cecchini,G. Fumarate reductase mutants of Escherichia coli that lackcovalently bound flavin. J. Biol. Chem. 264 (23), 13599-13604 (1989) PubMed: 2668268. Schroder,I., Gunsalus,R.P., Ackrell,B.A., Cochran,B. andCecchini,G. Identification of active site residues of Escherichia colifumarate reductase by site-directed mutagenesis. J. Biol. Chem. 266 (21), 13572-13579 (1991) PubMed: 1856194. Iverson,T.M., Luna-Chavez,C., Cecchini,G. and Rees,D.C. Structure of the Escherichia coli fumarate reductaserespiratory complex. Science 284 (5422), 1961-1966 (1999) PubMed: 10373108 ","","Tue Dec 17 17:11:38 2002","1","","","" "AA00805","551723","552490","768","ATGGCCGAACAACCAATCATGAACGTTGAGATTCTACGTTACAATTCTGAAGTCGATAAAGAGCCGCACTTAAAAACTTACCAAGTACCTTTCGACAGCCAAACCTCGTTGCTTGATGCCTTAGGTTACATTAAAGATAAATTGGAACCAGAACTTTCCTATCGCTGGTCTTGCCGTATGGCGATTTGCGGTTCTTGCGGGATGATGGTCAACAACATTCCGAAACTGGCGTGTAAAACCTTCCTGCGCGACTACAGCGGTCATATGCGTATCGAGCCGCTCGCCAACTTCCCGATTGAACGTGACTTAGTGGTTGACCTAAGCCATTTCATCGAAAGTCTGGAAGCCATCAAGCCTTACATTATCGGCAACAAAATGCCGGAATTAGACGGCAAACCGCATCCGTCAAAAGAATTGGCAAAAAGCCGTACCAAACAAACACCGGCACAATTGGAAAAATACCGTCAATTCTCCATGTGTATCAACTGTGGCTTATGCTATGCCGCTTGCCCGCAATTCGGTTTAAATCCTGAATTCGTCGGTCCTGCCGCGTTAACCTTGGCACACCGTTATAACTTAGATAACCGTGACCACGGTCAAGCGGAACGGATGAAAATCATGAACGGCGAAAACGGCGTTTGGTCCTGTACCTTCGTCGGTGCCTGTTCCGAAGTTTGTCCGAAACACGTAGGCCCGGCAACCGCCATTAACCAAGGTAAATTAGAAAGTGCGAAAGACTATCTGATTTCCATGCTTAAACCGAAAGCA","","","32184","MAEQPIMNVEILRYNSEVDKEPHLKTYQVPFDSQTSLLDALGYIKDKLEPELSYRWSCRMAICGSCGMMVNNIPKLACKTFLRDYSGHMRIEPLANFPIERDLVVDLSHFIESLEAIKPYIIGNKMPELDGKPHPSKELAKSRTKQTPAQLEKYRQFSMCINCGLCYAACPQFGLNPEFVGPAALTLAHRYNLDNRDHGQAERMKIMNGENGVWSCTFVGACSEVCPKHVGPATAINQGKLESAKDYLISMLKPKA","552492","","fumarate reductase iron-sulfur protein","Periplasm","","
InterPro
IPR001041
Domain
Ferredoxin
PF00111\"[20-84]TFer2
PS51085\"[7-97]T2FE2S_FER_2
InterPro
IPR001450
Domain
4Fe-4S ferredoxin, iron-sulfur binding
PF00037\"[153-176]TFer4
PS00198\"[160-171]T4FE4S_FERREDOXIN
InterPro
IPR004489
Family
Succinate dehydrogenase/fumarate reductase iron-sulfur protein
PIRSF000176\"[7-251]TFumarate reductase/succinate dehydrogenase (ubiquinone), iron-sulphur protein
TIGR00384\"[11-240]TdhsB: succinate dehydrogenase and fumarate
InterPro
IPR006058
Binding_site
2Fe-2S ferredoxin, iron-sulfur binding site
PS00197\"[58-66]T2FE2S_FER_1
InterPro
IPR012285
Domain
Fumarate reductase, C-terminal
G3DSA:1.10.1060.10\"[107-255]Tno description
InterPro
IPR012675
Domain
Beta-grasp fold, ferredoxin-type
G3DSA:3.10.20.30\"[3-106]Tno description
noIPR
unintegrated
unintegrated
PTHR11921\"[21-127]T\"[145-238]TSUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN


","BeTs to 22 clades of COG0479COG name: Succinate dehydrogenase/fumarate reductase Fe-S proteinFunctional Class: CThe phylogenetic pattern of COG0479 is aomp-zyq-dr-bcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 2.6e-07) to 2/2 blocks of the IPB000564 family, which is described as \"2Fe-2S Ferredoxin\". Interpro entry for IP:IPR000564. IPB000564A 55-73 7.5e-07 IPB000564B 76-85 1.6e+02","Residues 19 to 230 match (4e-11) PD:PD315160 which is described as IRON-SULFUR REDUCTASE ","","","","","","","","","","","","Tue Dec 17 17:13:31 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00805 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Cole,S.T. Nucleotide sequence coding for the flavoprotein subunit thefumarate reductase of Escherichia coli. Eur. J. Biochem. 122 (3), 479-484 (1982) PubMed: 7037404. Blaut,M., Whittaker,K., Valdovinos,A., Ackrell,B.A.,Gunsalus,R.P. and Cecchini,G. Fumarate reductase mutants of Escherichia coli that lackcovalently bound flavin. J. Biol. Chem. 264 (23), 13599-13604 (1989) PubMed: 2668268. Schroder,I., Gunsalus,R.P., Ackrell,B.A., Cochran,B. andCecchini,G. Identification of active site residues of Escherichia colifumarate reductase by site-directed mutagenesis. J. Biol. Chem. 266 (21), 13572-13579 (1991) PubMed: 1856194. Iverson,T.M., Luna-Chavez,C., Cecchini,G. and Rees,D.C. Structure of the Escherichia coli fumarate reductaserespiratory complex. Science 284 (5422), 1961-1966 (1999) PubMed: 10373108. Cole,S.T., Grundstrom,T., Jaurin,B., Robinson,J.J. andWeiner,J.H. Location and nucleotide sequence of frdB, thegene coding for the iron-sulphur protein subunit of thefumarate reductase of Escherichia coli. Eur. J. Biochem. 126 (1), 211-216 (1982) PubMed: 6751816. Werth,M.T., Cecchini,G., Manodori,A., Ackrell,B.A.,Schroder,I., Gunsalus,R.P. and Johnson,M.K. Site-directed mutagenesis of conserved cysteine residues inEscherichia coli fumarate reductase: modification of thespectroscopic and electrochemical properties of the [2Fe-2S]cluster. Proc. Natl. Acad. Sci. U.S.A. 87 (22), 8965-8969 (1990) PubMed: 2174169 ","","Tue Dec 17 17:13:31 2002","1","","","" "AA00806","552505","552894","390","ATGACAACAACCGTAACTAAACGTAAAAAATACGTCCGTGAAATCACCCCGACTTGGTGGAAAAGTTGGGATTTCTACAAATTCTATATGGTGCGTGAAGCCACCGCACTACCGACCGTCTGGTTCAGCCTGGTGTTGCTTTACGGTGTGATTTGTTTGGGTAAAGCGGACGGTTTTATCGCAAGCTTCATTCCATTCCTGCAAAATCCGATTGTAGTGATTCTCAACATTATTTCACTTGCTGCATTATTGTTGCACGCCGTGACATTATTTGACATGACCGGTGAAGTGATGTCCGGCAGCACCGGATTACCGCCGACATTAATCAAAAACGCGTTACGCGGATTATTCGTCGCCGTCACCGTATTGGCTTTAGTACTTGTATTTATC","","","14512","MTTTVTKRKKYVREITPTWWKSWDFYKFYMVREATALPTVWFSLVLLYGVICLGKADGFIASFIPFLQNPIVVILNIISLAALLLHAVTLFDMTGEVMSGSTGLPPTLIKNALRGLFVAVTVLALVLVFI","552896","","fumarate reductase 15 kD hydrophobic protein","Inner membrane, Cytoplasm","","
InterPro
IPR003510
Family
Fumarate reductase, subunit C
PD015900\"[14-99]TFRDC_PASMU_Q9CP58;
PIRSF000180\"[5-130]TFumarate reductase, subunit C (membrane anchor)
PF02300\"[5-130]TFumarate_red_C
noIPR
unintegrated
unintegrated
tmhmm\"[34-52]?\"[71-91]?\"[111-129]?transmembrane_regions


","BeTs to 4 clades of COG3029COG name: Fumarate reductase subunit CFunctional Class: CThe phylogenetic pattern of COG3029 is ----------r---e-gh--------Number of proteins in this genome belonging to this COG is","Significant hit ( 1.7e-49) to 2/2 blocks of the IPB003510 family, which is described as \"Fumarate reductase subunit C\". Interpro entry for IP:IPR003510. IPB003510A 8-57 1.3e-34 IPB003510B 63-106 9.1e-14","Residues 14 to 99 match (3e-14) PD:PD015900 which is described as FUMARATE COMPLETE PROTEOME REDUCTASE HYDROPHOBIC MEMBRANE TRANSMEMBRANE INNER ANCHOR POLYPEPTIDE ","","","","","","","","","","","","Tue Dec 17 17:14:49 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00806 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 130 (E-value = 4.2e-56) place AA00806 in the Fumarate_red_C family which is described as Fumarate reductase subunit C (PF02300)","","","","","Cole,S.T. Nucleotide sequence coding for the flavoprotein subunit thefumarate reductase of Escherichia coli. Eur. J. Biochem. 122 (3), 479-484 (1982) PubMed: 7037404. Blaut,M., Whittaker,K., Valdovinos,A., Ackrell,B.A.,Gunsalus,R.P. and Cecchini,G. Fumarate reductase mutants of Escherichia coli that lackcovalently bound flavin. J. Biol. Chem. 264 (23), 13599-13604 (1989) PubMed: 2668268. Schroder,I., Gunsalus,R.P., Ackrell,B.A., Cochran,B. andCecchini,G. Identification of active site residues of Escherichia colifumarate reductase by site-directed mutagenesis. J. Biol. Chem. 266 (21), 13572-13579 (1991) PubMed: 1856194. Iverson,T.M., Luna-Chavez,C., Cecchini,G. and Rees,D.C. Structure of the Escherichia coli fumarate reductaserespiratory complex. Science 284 (5422), 1961-1966 (1999) PubMed: 10373108 ","","Tue Dec 17 17:14:49 2002","1","","","" "AA00807","552907","553248","342","ATGGTTAATCAAAATCCAAAACGTTCAAACGAACCGCCTGTATGGTTAATGTTCAGTGCGGGTGGCATGGTTAGCGGTCTAGCTTTCCCGGTACTCATTCTGATCATCGGTTTATTATTGCCTTTCGGCTTAGTCAGCCCGGATAACATCATTGCCTTCGCGCACCATTGGTTCGGCAAATTAGTTATCCTCGTGCTCACCATCTTCCCGATGTGGGCTGGCTTACACCGCGTCCACCACGGAATGCACGACATTAAAGTTCACGTCCCAGCCGGCGGATTCATCTTCTACGGTTTGGCAACACTTTATAGCATTATCGTGTTATTCGCTGTGTGCAATATC","","","12541","MVNQNPKRSNEPPVWLMFSAGGMVSGLAFPVLILIIGLLLPFGLVSPDNIIAFAHHWFGKLVILVLTIFPMWAGLHRVHHGMHDIKVHVPAGGFIFYGLATLYSIIVLFAVCNI","553250","","fumarate reductase 13 kD hydrophobic protein","Inner membrane, Cytoplasm","","
InterPro
IPR003418
Family
Fumarate reductase, D subunit
PD015693\"[1-114]TFRDD_HAEIN_P44891;
PIRSF000179\"[1-114]TFumarate reductase, subunit D (membrane anchor)
PF02313\"[2-113]TFumarate_red_D
noIPR
unintegrated
unintegrated
signalp\"[1-47]?signal-peptide
tmhmm\"[25-47]?\"[53-73]?\"[94-112]?transmembrane_regions


","BeTs to 4 clades of COG3080COG name: Fumarate reductase subunit DFunctional Class: CThe phylogenetic pattern of COG3080 is ----------r---e-gh--------Number of proteins in this genome belonging to this COG is","Significant hit ( 9.3e-51) to 2/2 blocks of the IPB003418 family, which is described as \"Fumarate reductase subunit D\". Interpro entry for IP:IPR003418. IPB003418A 6-43 1.4e-25 IPB003418B 70-98 5.4e-24","Residues 6 to 114 match (2e-28) PD:PD015693 which is described as FUMARATE COMPLETE PROTEOME REDUCTASE HYDROPHOBIC MEMBRANE TRANSMEMBRANE INNER ANCHOR POLYPEPTIDE ","","","","","","","","","","","","Tue Dec 17 17:16:51 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00807 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 113 (E-value = 1.5e-64) place AA00807 in the Fumarate_red_D family which is described as Fumarate reductase subunit D (PF02313)","","","","","Cole,S.T. Nucleotide sequence coding for the flavoprotein subunit thefumarate reductase of Escherichia coli. Eur. J. Biochem. 122 (3), 479-484 (1982) PubMed: 7037404. Blaut,M., Whittaker,K., Valdovinos,A., Ackrell,B.A.,Gunsalus,R.P. and Cecchini,G. Fumarate reductase mutants of Escherichia coli that lackcovalently bound flavin. J. Biol. Chem. 264 (23), 13599-13604 (1989) PubMed: 2668268. Schroder,I., Gunsalus,R.P., Ackrell,B.A., Cochran,B. andCecchini,G. Identification of active site residues of Escherichia colifumarate reductase by site-directed mutagenesis. J. Biol. Chem. 266 (21), 13572-13579 (1991) PubMed: 1856194. Iverson,T.M., Luna-Chavez,C., Cecchini,G. and Rees,D.C. Structure of the Escherichia coli fumarate reductaserespiratory complex. Science 284 (5422), 1961-1966 (1999) PubMed: 10373108 ","","Tue Dec 17 17:16:51 2002","1","","","" "AA00809","555495","553351","2145","ATGAAACAACTTTTTGCCACCACAGCCCGTGGATTTGAAGAACTTTTGAAATCTGAATTAACCGACCTAGGCGCGCGCGATGCGAAAGTGACGCAGGGCGGCGTGCATTATTGGGCGGATGATGAAACCCTGTATCGCACCTTGCTTTGGAGCCGTTTGAGTTCGCGCATTTTATTGCCTATCGTGCAAGCCAAAGTGTTCAGTGATTTGGATTTATATTCTGCGGTGGTGGGCGTGAACTGGCTGGATTATTTCGATGAAAAAGTCCATTTTTTCGTGGATTTTAACGGCACGAACCAAGAAATTCGCCACACCCAATTCGGCGCTATGCGTGTGAAAGACGGCATTGTGGATTATTTTGAACGTCATGGACGTGCGCGCCCGAACGTCGATAAAGAACAGCCAGACATTCGTATTCATGCTTATCTGAACCGTGATGAGGTGGTGCTTTCTCTGGATTTAAGCGGCGATGCACTACATATGCGCGGTTATCGTGAGGACACCGGCAAAGCGCCGTTGCGTGAAACTTTGGCGGCGGCGATTGTGATGCGTTCCGGCTGGCAGCAAGGCACGCCGTTGGTGGACCCCATGTGCGGTTCCGGCACCTTGCTGATTGAAGCGGCGCAAATGGAAGCGAAAATTGCACCGCAGTTATATCGCTTACATTGGGGCTTTGATTTCTGGCGGGGGCATAATCAGGCGGTGTGGGAAAAGGTGAAAGAAGAGGCTTTAGCCTTGGTGGACGCGGAAAAACAACGGGAAAATCCACTGCACTTTTATGGCTTCGATTTGGATCATCGAGTGCTGCAAAAAGCCAAACAAAATGCCAAAAGTGCCGGTGTGGCACATTTAATGCAATGGCAACAGGGCGATGTGGCGGCGCTTAAAAATCCAAGCCCAAACACCACGGGCACAGTGATTTGTAACCCGCCGTACGGCGAACGATTGGGCACAACGCCTGCATTGATTGCCTTGTATTCCGTGTTCGGGCAACGATTAAAACAACAATTCGCCGGTTGGAACGCGTCCGTTTTCAGTGGCGAACCGAGCCTGTTGGATTGTTTACGTTTGCGTTCCCATCGTCAGTTCAAAGCGAAAAACGGACCTTTGGATTGTGTGCAGAAAAACTACCAACTCGCTGAACGGGCAGCGCAAAGTGCGGTGGAAAACGCTGCCGAATTTGACCGCACTTCTGCCGCTTCTGCTCATGTCGCACCGGGTTTTGCCAATCGACTGCAGAAAAATATCAAGAAAATCGAAAAATGGGCGAAACAGCAGGGGTTGGATGCCTATCGTTTATATGACGCGGATTTGCCGGAATATAATTTGGCGGTGGATCGTTATGCCGATCATATTGTGGTGCAGGAATATGCCGCACCGAAAAATATTGATGAAAACAAAGCCCGCCAGCGTTTGTTGGATGCCGTGAATGCCACGTTAAACGTCACGGGCGTGGAGACCAATAAATTGATTTTGAAAGTGCGCCAGAAACAAAAAGGCACCAATCAATATGAAAAATTGGCGAATAAAGGCGAGTATTTTTATGTGAATGAATATGGCGCAAAATTGTGGGTGAACCTGACGGATTATTTGGATACGGGCTTGTTTTTGGATCACCGCCTGACCCGAAAAATGTTGGGTGAAATGGCGCAGGGCAAGGATTTTCTGAATCTGTTTGCTTACACCGGTTCCGCCACCGTTCACGCAGCACTTGGCGGGGCGAAATCCACCACTACGGTAGATATGTCAAATACCTATCTTAACTGGGCGGAACAAAATTTATTGCTCAATGACATTGAAGGCAAGCAGCACAAACTCATTCAAGCGGATTGTCTGCAATGGCTGGAAAAATGCGATCGTCAATTTGATTTGATTTTTGTTGATCCACCGACATTTTCTAATTCCAAACGTATGGAAGACAGCTGGGATGTGCAACGGGATCACATTAAGTTAATGACGAATTTAAAACGCATTCTGCGCCCGAACGGCACCATCGTGTTTTCCAACAATAAACGCGGGTTCAAAATGGATTTTGTCGGTTTGGAAGCGTTGGGATTAAGTGCGGTGGAAATTTCCCGCAAAACATTGCCGTTGGATTTTGAGCGCAATAAGCAGATTCATAATTGTTGGGTGGTGCAGGCGAAA","","","81230","MKQLFATTARGFEELLKSELTDLGARDAKVTQGGVHYWADDETLYRTLLWSRLSSRILLPIVQAKVFSDLDLYSAVVGVNWLDYFDEKVHFFVDFNGTNQEIRHTQFGAMRVKDGIVDYFERHGRARPNVDKEQPDIRIHAYLNRDEVVLSLDLSGDALHMRGYREDTGKAPLRETLAAAIVMRSGWQQGTPLVDPMCGSGTLLIEAAQMEAKIAPQLYRLHWGFDFWRGHNQAVWEKVKEEALALVDAEKQRENPLHFYGFDLDHRVLQKAKQNAKSAGVAHLMQWQQGDVAALKNPSPNTTGTVICNPPYGERLGTTPALIALYSVFGQRLKQQFAGWNASVFSGEPSLLDCLRLRSHRQFKAKNGPLDCVQKNYQLAERAAQSAVENAAEFDRTSAASAHVAPGFANRLQKNIKKIEKWAKQQGLDAYRLYDADLPEYNLAVDRYADHIVVQEYAAPKNIDENKARQRLLDAVNATLNVTGVETNKLILKVRQKQKGTNQYEKLANKGEYFYVNEYGAKLWVNLTDYLDTGLFLDHRLTRKMLGEMAQGKDFLNLFAYTGSATVHAALGGAKSTTTVDMSNTYLNWAEQNLLLNDIEGKQHKLIQADCLQWLEKCDRQFDLIFVDPPTFSNSKRMEDSWDVQRDHIKLMTNLKRILRPNGTIVFSNNKRGFKMDFVGLEALGLSAVEISRKTLPLDFERNKQIHNCWVVQAK","553353","","possible oxidoreductase","Cytoplasm","","
InterPro
IPR000241
Domain
Putative RNA methylase
PF01170\"[162-376]TUPF0020
PS01261\"[195-206]TUPF0020
InterPro
IPR002052
Domain
N-6 Adenine-specific DNA methylase
PS00092\"[306-312]?N6_MTASE
InterPro
IPR004114
Domain
THUMP
PF02926\"[56-154]TTHUMP
PS51165\"[43-154]TTHUMP
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[524-670]Tno description


","BeTs to 6 clades of COG0116COG name: Predicted N6-adenine-specific DNA methylasesFunctional Class: LThe phylogenetic pattern of COG0116 is a-m-kz---d-lbcefghsn------Number of proteins in this genome belonging to this COG is","Significant hit ( 5.2e-12) to 1/1 blocks of the IPB000241 family, which is described as \"Uncharacterized protein family UPF0020\". Interpro entry for IP:IPR000241. IPB000241 193-210 5.2e-12","Residues 349 to 380 match (8e-11) PD:PD468618 which is described as PROTEOME COMPLETE YCBY PM0304 VC1488 OXIDOREDUCTASE ","","","","","","","","","","","","Tue Dec 17 17:19:39 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00809 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 162 to 376 (E-value = 5e-98) place AA00809 in the UPF0020 family which is described as Putative RNA methylase family UPF0020 (PF01170)","","","","","","","","1","","","" "AA00810","555766","556791","1026","ATGATTCCCAAAACTTATTTAGCTATGCAAACCACGCCACAAGGAGATTTAGTACTAACCGAAAAGCAAACCGTATTGCCCACCGCTCATCAAGTATTGATTCAAGTAGAAGCCTGTGGCGTGTGCGGGGCAGATTTGGGCGATATCAAACATAACTTACAAACCCCACGCGTTATCGGGCATGAAGTGATCGGGTGGCTCCTGGCTAAAGGTGAAGCTGTTTCAAAGCGCTGGCAGGTAGGACAACGGGTTGGTGTAGGTCGGCTTGGCGGACATTGTCATGAGTGCGATGCATGCCGTGCGGGACAATTTGTGCATTGTGCGCACCAAAGCTACATAGGCGCAAGCCGTGATGGCGGTTATGCCGAGCTGATGATCGTGAACCAAACAGGTTTGGTTGCCATACCCGAAAGCCTGAATAGCACTGACGCGGCTCCATTACTTTGTGCCGGCTTAGCAACTTTTAATGCACTACGTAACAGCGATACCAAAGCCGGCGACACAGTGGCAGTGCTTGGCACAGGAGGCTTAGGCCATTTGGCGGTCCAATACGCGCAAAAAATGGGCTTTGAAGTGGTATCTATCGGGCGGCAAGACTTATCCGAAAAAATGACCTCGCTTGGTGCACATCATTACGTTAATTTAGCAAAACAAAGTGCGGTGGATTTTTTACGTGAATTGGGCGGTGCAGATTTAATCCTTAGCACTATAACCGACGCCGAAACCATCGGCGATGTGGCAAAAAGCTTAAAAGCAAGAGGAAAATTGTTGCTGTTGGGCGCAAGCGGTGAACCTTTAGCACTGCCGCTCAACCGTATAGTAGGCAAAGAACAAAGGATCCAAGGTTCGTTAACAGGTACGCCATTTGACGCAGAATGCACGCTCAAATTTAGTGTACTTTCAGGCGTAAAACCGCAGGTAGAAATCTTTCCGCTCACAAAAGCAAATGAAGCTATTGCGCGATTGAAATCAGGCAAAGCACGGTTTCGAATTGTGTTAAACGTCAATCAAAATAAGACTACACCA","","","36277","MIPKTYLAMQTTPQGDLVLTEKQTVLPTAHQVLIQVEACGVCGADLGDIKHNLQTPRVIGHEVIGWLLAKGEAVSKRWQVGQRVGVGRLGGHCHECDACRAGQFVHCAHQSYIGASRDGGYAELMIVNQTGLVAIPESLNSTDAAPLLCAGLATFNALRNSDTKAGDTVAVLGTGGLGHLAVQYAQKMGFEVVSIGRQDLSEKMTSLGAHHYVNLAKQSAVDFLRELGGADLILSTITDAETIGDVAKSLKARGKLLLLGASGEPLALPLNRIVGKEQRIQGSLTGTPFDAECTLKFSVLSGVKPQVEIFPLTKANEAIARLKSGKARFRIVLNVNQNKTTP","556793","","alcohol dehydrogenase","Cytoplasm","","
InterPro
IPR002085
Family
Alcohol dehydrogenase superfamily, zinc-containing
PTHR11695\"[16-88]T\"[117-335]TALCOHOL DEHYDROGENASE RELATED
InterPro
IPR002328
Domain
Alcohol dehydrogenase, zinc-containing
PS00059\"[60-74]?ADH_ZINC
InterPro
IPR013149
Domain
Alcohol dehydrogenase, zinc-binding
PF00107\"[165-300]TADH_zinc_N
InterPro
IPR013154
Domain
Alcohol dehydrogenase GroES-like
PF08240\"[29-135]TADH_N
noIPR
unintegrated
unintegrated
G3DSA:3.90.180.10\"[4-185]Tno description
PTHR11695:SF38\"[16-88]T\"[117-335]TZINC-TYPE ALCOHOL DEHYDROGENASE-RELATED


","No hits to the COGs database.","Significant hit ( 1.4e-31) to 4/4 blocks of the IPB002328 family, which is described as \"Zinc-containing alcohol dehydrogenase\". Interpro entry for IP:IPR002328. IPB002328A 16-47 1.6e-08 IPB002328B 56-81 0.00018 IPB002328C 93-107 0.00049 IPB002328D 132-179 1.2e-09","Residues 109 to 150 match (8e-07) PD:PD497171 which is described as OXIDOREDUCTASE PROBABLE PROTEOME DEHYDROGENASE ADH-HT ALCOHOL PLASMID COMPLETE ","","","","","Thu Feb 13 16:27:33 2003","","","","","","","Tue Dec 17 17:24:31 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00810 is paralogously related to AA02047 (3e-16) and AA01114 (4e-09).","","","","","","Residues 12 to 335 (E-value = 8.9e-71) place AA00810 in the ADH_zinc_N family which is described as Zinc-binding dehydrogenase (PF00107)","","","","","","","Thu Feb 13 16:27:33 2003","1","","","" "AA00811","558087","556876","1212","ATGTACCTTTCCCGCCAAATCCAACCTTTAGTAAGTCGTCTACTTAAGCAATTTCCGGCAGTTCTTGTCACCGGTGCGAGACAGGTCGGTAAATCGACGTTGTTAAAGCATATCGCAAAAGATTACGCTTATTTGACCTTCGACGATCCTCTGCTGCTGGAACAAGCCAAACAAGAACCGCGTTTATTCTTTTTAAATCACGCAGGTAATGTGATTTTAGACGAAGTGCAGTATGCACAAGAATTGTTTTCTTTATTAAAGCTTGAAATCGATAAACAGCAAAAAAATGGGATGTTTTTGCTTTCCGGTTCACAGGCCTTTGAGCTTATGCAAAATGTCAGTGAAACACTGGCGGGCAGAATCGCTATTCTCAAACTACAAGGATTATCGCTACGTGAAATATTAAACGTTGAGTTTTACCTGCCTTTTATTCCCAGTAGGGATTATTTAGCGAGCAGAGAGAAAATGCTGAAATCGCCTGAAAATATCTGGCAAATTATTCATAAAGGCGATATGCCGCGTTTATATCAGCAGGAAACAGATTGGGAAATTTACTATTCTTCCTACGTTTCCACTTACATTGAAAGGGATGTGCGCCAGCTCACCAATATTACCAATACAACGGATTTTACCCGCTTTATGGTGGCGTTGGCGTCCCGCAGTGGAGAGTTATTGAACTACAGTAATGTGGCACAGGAAGTTGGCGTCTCTAACGAAACGATTAAACGCTGGACGGCGATTTTACAGACCTCAGGCATTATTTATTTGTTACAGCCTTATAGTAATAATCATCTGAAACGCACCATTAAAACCCCGAAGATTTATTTTCTGAACACCGGTCTCATGGCATATTTAACCAAATGGCTTACACCGGAGACCATTTCTAAAGGTGCAAAGAGCGGTCAATTTTTTGAGAGTTTTGTGGTGAGTGAAATTATAAAATCTTTCACGAATAACGGCATTGAACCACCACTTTATTTTTATCGTAATACCAATCAGAAGGAAATTGATTTGATTATTGAATACGATCGCACGATTTATCCCATTGAAATCAAAACGACTGCTAACCCGAATAAAAAAATGGCAAAAAGTTTTGCGTTGTTAAATTCGCTTGGGAAAGAATCTACTATCGGGCTGGGGGTGATTATTAATCAGTATCCGAATAAGCATTATTTGGCAGAGAATCTGGTGGCGTTACCTGTTAGGTATTTA","","","46990","MYLSRQIQPLVSRLLKQFPAVLVTGARQVGKSTLLKHIAKDYAYLTFDDPLLLEQAKQEPRLFFLNHAGNVILDEVQYAQELFSLLKLEIDKQQKNGMFLLSGSQAFELMQNVSETLAGRIAILKLQGLSLREILNVEFYLPFIPSRDYLASREKMLKSPENIWQIIHKGDMPRLYQQETDWEIYYSSYVSTYIERDVRQLTNITNTTDFTRFMVALASRSGELLNYSNVAQEVGVSNETIKRWTAILQTSGIIYLLQPYSNNHLKRTIKTPKIYFLNTGLMAYLTKWLTPETISKGAKSGQFFESFVVSEIIKSFTNNGIEPPLYFYRNTNQKEIDLIIEYDRTIYPIEIKTTANPNKKMAKSFALLNSLGKESTIGLGVIINQYPNKHYLAENLVALPVRYL","556878","","conserved hypothetical protein","Cytoplasm, Outer membrane","","No hits reported.","No hits to the COGs database.","","Residues 162 to 353 match (2e-07) PD:PD234727 which is described as PLASMID ","","","","","","","","","","","","Tue Dec 17 17:28:48 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00811 is paralogously related to AA00504 (7e-05).","","","","","","","","","","","","","","1","","","" "AA00812","558910","558215","696","ATGTCAAATCAGCCTAACAAAGCCCTCGTGATTTTTTCCGGTGGGCAAGATTCCACCACCTGCCTGTTTCTCGCCATGCAAGAATTCGGCGCAGAAAATGTCGAAGTCATCACATTCCAATACGGTCAACGTCATGCCATTGAACTGGAAAAAGCCCGATGGATTGCACAGGATTTAAAGGTAAAGCAAACGGTGCTCGATACCAGCGTCATTAAAGCCATTACCCACAACGCCTTAATGGATCCGAACGCGCCAATCAGTCAAAAAGACAATGAATTGCCGAATACTTTCGTTGACGGACGCAACGCCTTATTTTTACTTTACGCCGCCATTTACGCCAAAAGCCAAGGCATTCGCGTTATTTATACCGGCGTGTGCGAAACGGATTTTAGCGGCTATCCCGATTGCCGCGATGTTTTCGTCAAATCTATGAATGTTACCTTAAACCTTGCCATGGCTTACCCTTTTGAAATCCGCACACCGTTAATGTGGCTGGATAAAAAAGAAACCTGGGCGCTGGCGGATCAACTTGGCGCGTTTGATTATATCCGCCGGCACACCCACACTTGCTACAACGGTGTCGAAGGCGGTTGCGGCGAATGCCCGAGTTGCGTTTTGCGCGAACGTGGATTGAAGGCGTATTTGCCGGAACGTGAGGAAAAAATGCCTGAGAAAACAACCGCACTTTCGAGGGAG","","","26146","MSNQPNKALVIFSGGQDSTTCLFLAMQEFGAENVEVITFQYGQRHAIELEKARWIAQDLKVKQTVLDTSVIKAITHNALMDPNAPISQKDNELPNTFVDGRNALFLLYAAIYAKSQGIRVIYTGVCETDFSGYPDCRDVFVKSMNVTLNLAMAYPFEIRTPLMWLDKKETWALADQLGAFDYIRRHTHTCYNGVEGGCGECPSCVLRERGLKAYLPEREEKMPEKTTALSRE","558217","","ATPase (PP-loop superfamily), confers aluminum resistance","Cytoplasm","","
InterPro
IPR004479
Family
ExsB
PIRSF006293\"[6-224]TUncharacterised conserved protein, ExsB type
PF06508\"[7-178]TExsB
TIGR00364\"[8-207]TTIGR00364: exsB protein


","BeTs to 19 clades of COG0603COG name: Predicted ATPase (PP-loop superfamily), confers aluminum resistanceFunctional Class: RThe phylogenetic pattern of COG0603 is aompkz-q----bcefghsnujx---Number of proteins in this genome belonging to this COG is","","Residues 142 to 175 match (5e-08) PD:PD283345 which is described as PROTEOME COMPLETE SUPERFAMILY ALUMINUM RESISTANCE SAV0712 YKVJ PP-LOOP EXSB MLL5936 ","","","","","Sat Feb 15 07:33:58 2003","","","","","","","Wed Dec 18 08:34:59 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00812 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 74 to 144 (E-value = 6.2e-37) place AA00812 in the ExsB family which is described as ExsB (PF06508)","","","","","","","","1","","","" "AA00813","559081","558947","135","TTGATCAGTTCATTCACGGTAAAATATCGGGCATTAAAGTGCGGTTGGTTTCAACGGCGTTTTTTTAAAGGGGATTTTCCATCCCTTTATTTCTTTGCTAAAATTCACCGCACTTTTCTTTGTGTTCGCTGTGGT","","","5425","LISSFTVKYRALKCGWFQRRFFKGDFPSLYFFAKIHRTFLCVRCG","558947","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 14:36:33 2004","Mon Feb 23 14:38:46 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00813 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 14:36:33 2004","","","","","","","","","","","","","1","","","" "AA00814","559265","559726","462","ATGCTGTATATCCCTCAAACAAACCCTGGGCGCTATGTAAGTAGCATCGTGGCATTAAACGTACATAGCCCAAACGGTACTGGCGATTGGCATAGTGCAGCGGCATTGAATGACGATGCTTATCCGCAAGATTTTTACATTTATGGTGAAAGCCAAAAAAGGAACACCAATCATCTATTGGGTAATCTAGGCGTAATTGATGGCACCCAACGATTAAATGAAATGGGATATTACCCTGAAAATTATCCTGTTTGGCTTGCCGACCACCCTCGTGCTTGCGTTGATTACCTCTACACCGCCGTACTTCAAACTGGTTCACTTGGAGAAGTTATGCTTGATGAATGGTTTCCTAGCGATGAAGATAAACAATCGGTTTACGATTTATTGAACCAGCTCGAACCCAATTTAACCGAACAAGAAAGGGAAAACTTACAATTATGGAAACGCAAAAACCCGATAATC","","","17648","MLYIPQTNPGRYVSSIVALNVHSPNGTGDWHSAAALNDDAYPQDFYIYGESQKRNTNHLLGNLGVIDGTQRLNEMGYYPENYPVWLADHPRACVDYLYTAVLQTGSLGEVMLDEWFPSDEDKQSVYDLLNQLEPNLTEQERENLQLWKRKNPII","559728","","conserved hypothetical protein","Periplasm, Extracellular","","No hits reported.","No hits to the COGs database.","","Residues 5 to 154 match (6e-68) PD:PD204443 which is described as PROTEOME COMPLETE NMB1760 ","","","","","","","","","","","","Wed Dec 18 08:37:44 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00814 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00815","559702","560523","822","ATGGAAACGCAAAAACCCGATAATCTAATCACCGAACGCGATAAACATCACGAAAAATTGATGGTGAGTATCCTGAAAAATCTTACCGATACGCCTTTAGTACTGAAAGGTGGCACAGCACTTTATCTCGGCTACGGCTTAAACCGCTTTTCCGAAGATTTGGATTTTGACTCGTCCAAAAAACTGAATTTACTCAACAAAATCAAAGCGTCCGCCCCACACGGTATTGTGATTGATGATATTAATGTGAAAAAAGATACAGACACAGTGAGTCGTTATATTGTGAATTATCATATCCGTGATACAGGTGTTAAAGATGCACTAAAAATGGAAATTTCTTATCGAACGCCAGCATCAGATGATCAAATTACGGTTAAAGATGGCATTCGTTTTTCATCAGTGGAACGCATTATTGATAACAAACTGCACGCAGCTTATGATAGCGATAACACGCGAACTAAAGGACGTGATTTATTTGACCTACATTTTCTCGCCAAACAATACCCCGAAGCCTTTACGCCTGAACTTGCCGAACGATTAAAAGGTTTCGCTCAAGATCCTGATAAATTAGTCAGCCTATATAGTCAAAATATCCAAGCGGATCCGCTACTTAATAAGATTATGGACGTTGAACAAATTGCACTTGAGCTAAATAAGATGGCAGAAACTATCTATTTCACTCAACAAATGCAAAATCACCCTGCAATGCAAGCATCAATGCCTAATGCTAAAAAACAATTTAAGGCGTTGTTAGATGAAGCTAAAAATAAGAAAGAAGAAACAACACAAAATGTTGTGCCGTCCTCTCTTAAAATGAAATTA","","","31174","METQKPDNLITERDKHHEKLMVSILKNLTDTPLVLKGGTALYLGYGLNRFSEDLDFDSSKKLNLLNKIKASAPHGIVIDDINVKKDTDTVSRYIVNYHIRDTGVKDALKMEISYRTPASDDQITVKDGIRFSSVERIIDNKLHAAYDSDNTRTKGRDLFDLHFLAKQYPEAFTPELAERLKGFAQDPDKLVSLYSQNIQADPLLNKIMDVEQIALELNKMAETIYFTQQMQNHPAMQASMPNAKKQFKALLDEAKNKKEETTQNVVPSSLKMKL","560525","","conserved hypothetical protein","Periplasm, Cytoplasm","","
InterPro
IPR014942
Family
Domain of unknown function DUF1814
PF08843\"[13-224]TDUF1814


","No hits to the COGs database.","","Residues 1 to 233 match (3e-62) PD:PD213001 which is described as PROTEOME COMPLETE ","","","","","","","","","","","","Wed Dec 18 08:38:53 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00815 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00816","561825","561040","786","GTGTTTCGTGTCATTCAAATCACGGATCCCCATTTATTTAAAGACGCAACCGGCGAGTTATTGGGGGTCAATACTCAAGAAAGCTTTTCACAGGTGTTAAGTGAAATTCGGCAACAACCCTATGATTATGATCTGGTGTTAGCCACCGGCGATTTGGTTCAAGACAGCAGCGAAGAAGGCTATCTGCGTTTTTGCGAAAGCGTTAAGCCCCTTGAGAAAACCGTATTTTGGATCCCCGGCAACCACGATTTCCAACCGAAAATGTTTGATATTCTCAAACGTGACAATATTTGCGATAAAAAGCACATTCTGTTGGGTGAAAATTGGCAAATTCTGTTACTGGACAGCCAAATCGCCGGCGTACCCCACGGTCAGCTCGGGCAATATCAGCTGGATTGGCTGATGGCGAAGCTGAAAGAACATCCGCAGCGTTATTCATTAGTGGTGTTGCATCATCATATTTTATCCACCCATTCCGCCTGGCTGGATCAACATAATCTGCGTAACGCACACGAATTGGCTTACACGCTGGCGCCGTTTAATAACGTGAAAGGCATTTTATACGGACATATTCATCAGCAAGTGGACGGCGAATGGAACGGTTACAAAATTATGGCAACGCCTTCGACGGGCATTCAATTCAAACCGGATAGCAATACCTTCGCTCTAGACACCGCTCAACCGGGCTGGCGTGAAATTGAATTGTACGCCGACGGACGCATCGAAACCCGCGTTAAACGCATTCAACACAAAACTTTCCTGCCGAATTTACAGGAAGAAGGGTAT","","","31781","VFRVIQITDPHLFKDATGELLGVNTQESFSQVLSEIRQQPYDYDLVLATGDLVQDSSEEGYLRFCESVKPLEKTVFWIPGNHDFQPKMFDILKRDNICDKKHILLGENWQILLLDSQIAGVPHGQLGQYQLDWLMAKLKEHPQRYSLVVLHHHILSTHSAWLDQHNLRNAHELAYTLAPFNNVKGILYGHIHQQVDGEWNGYKIMATPSTGIQFKPDSNTFALDTAQPGWREIELYADGRIETRVKRIQHKTFLPNLQEEGY","561042","","lacZ expression regulator","Cytoplasm","","
InterPro
IPR004843
Domain
Metallophosphoesterase
PF00149\"[2-194]TMetallophos
InterPro
IPR013622
Domain
Calcineurin-like phosphoesterase C-terminal
PF08413\"[196-262]TMetallophos_C
noIPR
unintegrated
unintegrated
G3DSA:3.60.21.10\"[2-192]Tno description


","BeTs to 11 clades of COG1409COG name: Predicted phosphohydrolasesFunctional Class: RThe phylogenetic pattern of COG1409 is a-m-kzyq--r--cefgh---j-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 3.3e-10) to 4/4 blocks of the IPB003701 family, which is described as \"DNA repair exonuclease\". Interpro entry for IP:IPR003701. IPB003701A 3-13 1.6 IPB003701B 43-58 0.33 IPB003701C 78-83 0.063 IPB003701D 183-193 1.7Significant hit ( 8.2e-05) to 3/4 blocks of the IPB000979 family, which is described as \"Uncharacterized protein family UPF0025\". Interpro entry for IP:IPR000979. IPB000979B 41-51 21 IPB000979C 73-83 1.5 IPB000979D 174-214 1.2","Residues 3 to 88 match (3e-31) PD:PD370008 which is described as COMPLETE PROTEOME PLASMID ORF ICC HOMOLOG 3'5'-CYCLIC-NUCLEOTIDE & PHOSPHODIESTERASE CPDA ","","","","","","","","","","","","Wed Dec 18 08:48:04 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00816 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 194 (E-value = 3.3e-17) place AA00816 in the Metallophos family which is described as Calcineurin-like phosphoesterase (PF00149)","","","","","","","","1","","","" "AA00817","562535","561915","621","ATGTATCAGTTTCAGCAATTTACTCAAAATGATATTGAAATTGTAAAGGATGAAACAGTTTATCAAGGTTTTTTTAAGCTGAATAAGGTTCAGTTTCGACATAAACTTTTTAACGGCGGCTGGAGCGGGATCGTCACCCGCGAGCTGTTGCTTAAAGGCGCCGCGTCGGCGGTAGTGGCTTATGACCCCGTGTTAGACAAGGTGGTTTTGGTGGAGCAGGTGCGTATCGGCGCTTATGATCCGAAACTGCAACAATCGCCGTGGTTGCTGGAACTCATCGCCGGCATGGTAGAAGAAGGCGAAACCCCGGAAAATGTAGCGCTGCGGGAAAGTGAAGAAGAAGCGGGCGCGCAAATTAGCCATTTGCAACATTGCTTGAGCGTATGGGACAGCCCGGGCGGCGCGCTGGAGCGGATCCATTTGTTCGTAGGCAACGTTGACAGCACAAACATTGGTGGCATTCACGGTTTAGCGGAAGAAAACGAAGATATTCGAGTTCATGTCGTCAGTAGGAAAACCGCGTATCAATGGGTTTGTGAGGGTAAAATTGATAACGGCATTGCAGTAATGGGATTACAGTGGCTGGAGTTAAATTACCGAAAATTGCAGGCGCAGTGGCTG","","","23348","MYQFQQFTQNDIEIVKDETVYQGFFKLNKVQFRHKLFNGGWSGIVTRELLLKGAASAVVAYDPVLDKVVLVEQVRIGAYDPKLQQSPWLLELIAGMVEEGETPENVALRESEEEAGAQISHLQHCLSVWDSPGGALERIHLFVGNVDSTNIGGIHGLAEENEDIRVHVVSRKTAYQWVCEGKIDNGIAVMGLQWLELNYRKLQAQWL","561917","","MutT-family protein","Cytoplasm","","
InterPro
IPR000086
Domain
NUDIX hydrolase
PR00502\"[90-104]T\"[104-119]TNUDIXFAMILY
G3DSA:3.90.79.10\"[2-207]Tno description
PF00293\"[52-195]TNUDIX
PS00893\"[95-116]TNUDIX
InterPro
IPR004385
Family
Nucleoside diphosphate pyrophosphatase
TIGR00052\"[10-197]TTIGR00052: conserved hypothetical protein T
noIPR
unintegrated
unintegrated
PTHR11839\"[1-197]TUDP/ADP-SUGAR PYROPHOSPHATASE
PTHR11839:SF1\"[1-197]TADP-RIBOSE PYROPHOSPHATASE


","BeTs to 19 clades of COG0494COG name: NTP pyrophosphohydrolases including oxidative damage repair enzymesFunctional Class: L,RThe phylogenetic pattern of COG0494 is aomp-zyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-08) to 1/1 blocks of the IPB000086 family, which is described as \"NUDIX hydrolase\". Interpro entry for IP:IPR000086. IPB000086 90-116 1.4e-08","","","","","","","","","","","","","Wed Dec 18 08:59:51 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00817 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 52 to 195 (E-value = 8.7e-17) place AA00817 in the NUDIX family which is described as NUDIX domain (PF00293)","","","","","Moreno-Bruna,B., Baroja-Fernandez,E., Munoz,F.J.,Bastarrica-Berasategui,A., Zandueta-Criado,A., Rodriguez-Lopez,M.,Lasa,I., Akazawa,T. and Pozueta-Romero,J.Adenosine diphosphate sugar pyrophosphatase prevents glycogenbiosynthesis in Escherichia coliProc. Natl. Acad. Sci. U.S.A. 98 (14), 8128-8132 (2001)PubMed: 11416161Dunn,C.A., O'Handley,S.F., Frick,D.N. and Bessman,M.J.Studies on the ADP-ribose pyrophosphatase subfamily of the nudixhydrolases and tentative identification of trgB, a gene associatedwith tellurite resistanceJ. Biol. Chem. 274 (45), 32318-32324 (1999)PubMed: 10542272","","Mon Feb 17 15:38:20 2003","1","","","" "AA00819","563461","562784","678","ATGAGCTTAACCCCTGAAATGCTTTGTGGCAAATCGCGTGAACATTTAGTAAACCTGCCGATACCCCATTCACCCAATCATTTCTTACAGGCGCAGGCAGCGAAAGCCTTTCAAGGCTTACAAAAAAGTGCGGTAAAAAATGGCTTTAATTTACAGCCGGCGAGCAGTTTTCGTGATTTTGCACGTCAGCAGCTGATTTGGAATGGCAAATTTAACGCTGAACGTAAAGTGCATGATGACGCAGGTAAGGCGTTAGATTTAACCAAATTGAACGACTGGCAAAAATGTCAGGTGATTTTGCGTTGGTCGGCGTTGCCGGGGGCGAGCCGCCATCATTGGGGCACGGAAATTGATATTTTTGATCCTGATTTATTACCGCCGGGTCAGGCATTACAGCTTGAACCTTGGGAATATGAACAAGGCGGTTATTTCTTTGGATTGAGCGAATTTCTCGCGGAAAATCTACCGCACTTTGATTTCGTCCTGCCGTTTATGAAAATGCCGGAAGGGAAAAAAATCGGGCGTGAGCCTTGGCATATTAGCTATGTTCCCCTGGCGGAAAAGGCGAAACAGCAATTTTCAGCGGCGGTGTTATTGCAGGCATGGGAAAATGAGGACATTGCCGGCAAGGCAGTTTTACAGCAGCACCTGCCACAGATTTTCGAGCAATATTTCGTG","","","25804","MSLTPEMLCGKSREHLVNLPIPHSPNHFLQAQAAKAFQGLQKSAVKNGFNLQPASSFRDFARQQLIWNGKFNAERKVHDDAGKALDLTKLNDWQKCQVILRWSALPGASRHHWGTEIDIFDPDLLPPGQALQLEPWEYEQGGYFFGLSEFLAENLPHFDFVLPFMKMPEGKKIGREPWHISYVPLAEKAKQQFSAAVLLQAWENEDIAGKAVLQQHLPQIFEQYFV","562786","","D-alanyl-D-alanine carboxypeptidase","Periplasm, Cytoplasm","","
InterPro
IPR003709
Domain
Peptidase M15B and M15C, D,D-carboxypeptidase VanY/endolysins
PF02557\"[26-185]TVanY


","No hits to the COGs database.","","Residues 3 to 104 match (2e-41) PD:PD354427 which is described as COMPLETE PROTEOME CARBOXYPEPTIDASE HI0101 PM1021 DD-CARBOXYPEPTIDASE-RELATED ","","","","","","","","","","","","Wed Dec 18 09:16:10 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00819 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 26 to 201 (E-value = 5.8e-11) place AA00819 in the VanY family which is described as D-alanyl-D-alanine carboxypeptidase (PF02557)","","","","","","","","1","","","" "AA00820","564596","563466","1131","ATGAAAGAAAAAGTTGTCTCTTTGGCGCAAGCATTAATCCGTCGTCCTTCCATCAGCCCGAATGACGAAGGCTGCCAGCAGCTGATTGCAGAACGGTTAGAAAAACTCGGTTTTCAAATTGAATGGCTGCCTTTTAACGACACGCTAAATTTATGGGCGAAACATGGCAGTGGCGATCCTGTCATTGCCTTTGCCGGGCATACGGATGTGGTGCCGACGGGCGATGAAAGCCAATGGACTTATCCGCCTTTCGACGCAAAAATTGTGGACGATATGCTTTATGGACGCGGTGCGGCGGATATGAAAGGATCACTGGCAGCAATGGTAGTGGCAACGGAAGAATATGTAAAAGCCCATCCGAATCATCAAGGCACCATCGCGTTGTTAATTACTTCCGATGAAGAAGCTGCTGCGAAAGACGGCACGGTGCGTGTGGTGGAAACCTTAATGGCGTGCGGCGAAAAGATCACTTATTGCATGGTGGGCGAGCCTTCCAGTACGCAAACCTTGGGCGATGTAGTGAAAAACGGTCGCCGTGGTTCCATCACAGGCAATCTGTATATTCAGGGCATTCAAGGGCACGTTGCCTATCCCCATCTGGCGGAGAATCCTATTCACAAAGCCGCGCCGTTCTTGCAGGAGCTCACCACATACCAATGGGACAACGGCAATGACTTTTTTCCTCCAACCAGTCTGCAAATCGCTAATATTCATGCCGGCACCGGCAGCAATAATGTGATTCCGGGCGAGCTTTATGTGCAATTTAATTTGCGTTATTGCACGGAAGTGACGGACGGGATGATTAAGCAGAAAGTCGCCGAGATGCTGGAAAAACACGGGCTGAAGTATCGTATTGAATGGAATCTTTCCGGCAAGCCGTTTTTAACCAAACCGGGAAAACTGGTGAGTGCGTTGGTGGACAGCCTGCAACAAATCGCAGGCATTACGCCGAAATTGGAAACCGGTGGTGGCACCTCAGACGGACGTTTTATTGCCCTCATGGGCGCGGAAGTGGTGGAATTCGGACCGCTTAACGCCACCATTCATAAAGTAAACGAGTGCGTGAGCGTGGAAGATCTTGGCAAATGCGGTCAGATTTACCATCAAATGTTAGTGAATTTATTGGAACAT","","","41133","MKEKVVSLAQALIRRPSISPNDEGCQQLIAERLEKLGFQIEWLPFNDTLNLWAKHGSGDPVIAFAGHTDVVPTGDESQWTYPPFDAKIVDDMLYGRGAADMKGSLAAMVVATEEYVKAHPNHQGTIALLITSDEEAAAKDGTVRVVETLMACGEKITYCMVGEPSSTQTLGDVVKNGRRGSITGNLYIQGIQGHVAYPHLAENPIHKAAPFLQELTTYQWDNGNDFFPPTSLQIANIHAGTGSNNVIPGELYVQFNLRYCTEVTDGMIKQKVAEMLEKHGLKYRIEWNLSGKPFLTKPGKLVSALVDSLQQIAGITPKLETGGGTSDGRFIALMGAEVVEFGPLNATIHKVNECVSVEDLGKCGQIYHQMLVNLLEH","563468","","succinyl-diaminopimelate desuccinylase","Cytoplasm","","
InterPro
IPR001261
Family
ArgE/dapE/ACY1/CPG2/yscS
PS00758\"[62-71]TARGE_DAPE_CPG2_1
InterPro
IPR002933
Family
Peptidase M20
PF01546\"[63-373]TPeptidase_M20
InterPro
IPR005941
Family
Succinyl-diaminopimelate desuccinylase, proteobacteria
TIGR01246\"[5-374]TdapE_proteo: succinyl-diaminopimelate desuc
InterPro
IPR011650
Domain
Peptidase M20, dimerisation
PF07687\"[176-284]TM20_dimer
noIPR
unintegrated
unintegrated
G3DSA:3.40.630.10\"[2-374]Tno description
PTHR11014\"[1-376]TPEPTIDASE M20 FAMILY MEMBER
PTHR11014:SF5\"[1-376]TACETYLORNITHINE DEACETYLASE


","BeTs to 21 clades of COG0624COG name: Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase and related deacylasesFunctional Class: EThe phylogenetic pattern of COG0624 is a-mpkzyqvdrlb-efghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 2.2e-11) to 3/3 blocks of the IPB001261 family, which is described as \"ArgE/dapE/ACY1/CPG2/yscS family\". Interpro entry for IP:IPR001261. IPB001261A 99-111 0.00038 IPB001261B 126-135 0.67 IPB001261C 180-196 0.015Significant hit ( 1.3e-08) to 3/3 blocks of the IPB002933 family, which is described as \"Peptidase family M20/M25/M40\". Interpro entry for IP:IPR002933. IPB002933A 96-100 64 IPB002933B 180-196 0.044 IPB002933C 245-258 0.0012","Residues 66 to 147 match (7e-10) PD:PD327509 which is described as PROTEOME COMPLETE AMINOPEPTIDASE HYDROLASE CARBOXYPEPTIDASE PRECURSOR SIGNAL G2 METALLOPROTEASE TRANSMEMBRANE ","","","","","","","","","","","","Wed Dec 18 09:17:44 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00820 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 9 to 376 (E-value = 1.3e-103) place AA00820 in the Peptidase_M20 family which is described as Peptidase family M20/M25/M40 (PF01546)","","","","","Bouvier,J., Richaud,C., Higgins,W., Bogler,O. and Stragier,P.Cloning, characterization, and expression of the dapE gene of Escherichia coli J. Bacteriol. 174 (16), 5265-5271 (1992) PubMed: 1644752 Wu,B., Georgopoulos,C. and Ang,D. The essential Escherichia coli msgB gene, a multicopysuppressor of a temperature-sensitive allele of the heatshock gene grpE, is identical to dapE J. Bacteriol. 174 (16), 5258-5264 (1992) PubMed: 1644751 ","","Wed Dec 18 09:17:44 2002","1","","","" "AA00822","565077","564736","342","ATGATTATTGTTTACGGCATTAAAAACTGCGACACGGTGAAGAAAGCATTGAAATGGCTTGCGGATCATCAGATTGAACACAAACTGCATGATTACCGCGTGGATGGGTTGGATAAGGCTTCTTTACAACAGGCGGAAGCACAATTTGGTTGGGAAAACTTGGTGAATAAACGCAGCACCACCTGGCGTAATCTTGACGAGCAAATCAAAAAAACACTTTCAAAATCCACCGCACTTTCTGTGCTTGCCGATAATCCAACCTTAATCAAACGCCCGATTATTTTGCAAGAGGGAAAGGCGTTGATTGGGTTTAGCGAAAAAGAATATCAGGCAGCGTTTAAT","","","14036","MIIVYGIKNCDTVKKALKWLADHQIEHKLHDYRVDGLDKASLQQAEAQFGWENLVNKRSTTWRNLDEQIKKTLSKSTALSVLADNPTLIKRPIILQEGKALIGFSEKEYQAAFN","564738","","conserved hypothetical protein (possible arsenate reductase)","Cytoplasm, Extracellular","","
InterPro
IPR006504
Family
Conserved hypothetical protein, ArsC related
TIGR01617\"[2-114]TarsC_related: conserved hypothetical protei
InterPro
IPR006660
Family
Arsenate reductase and related
PF03960\"[5-114]TArsC
InterPro
IPR012335
Domain
Thioredoxin fold
G3DSA:3.40.30.10\"[1-114]Tno description


","BeTs to 9 clades of COG1393COG name: Arsenate reductase and related proteins, glutaredoxin familyFunctional Class: PThe phylogenetic pattern of COG1393 is ---------drlb-efghsnuj---wNumber of proteins in this genome belonging to this COG is","","Residues 2 to 104 match (8e-08) PD:PD294860 which is described as PROTEOME COMPLETE SIMILAR ARSENATE REDUCTASE DR0136 ","","","","","","","","","","","","Wed Dec 18 09:21:43 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00822 is paralogously related to AA00391 (3e-05).","","","","","","Residues 5 to 114 (E-value = 5.6e-49) place AA00822 in the ArsC family which is described as ArsC family (PF03960)","","","","","","","","1","","","" "AA00823","567023","565146","1878","ATGAGTACAAATCAAGAAACCCGCGGCTTCCAGTCGGAAGTCAAACAACTGTTACAATTAATGATCCATTCTTTATATTCCAATAAAGAAATTTTCTTGCGCGAGCTGATTTCCAACGCCTCCGATGCGGCGGATAAATTGCGTTTTAAAGCTCTTTCCAATCCGGATTTATATGCAGGCGACGGCGAATTGCGCGTGTGTATCAGCTTTGACAGCGAGAAAGGCACCTTAACCGTAAGCGATAATGGTATCGGTATGACCCGCGAGCAGGTTATCGATCATTTGGGTACGATCGCCAAATCCGGCACGAAAGAATTTTTAGCGGCTCTCGGCAGCGACCAGGCGAAAGATAGCCAGCTTATCGGTCAATTCGGTGTGGGATTTTATTCCGCCTTTATCGTCGCTGATAAAGTCACCGTGAAAACCCGTGCGGCTGGCGAGCCGGCAGACAAAGGCGTGCTTTGGGAATCGGCAGGCGAAGGCGATTATACGGTAGCGGACATTGAGAAAAAATCTCGTGGCACCGATGTGATTTTGCACTTACGCGACGATGAAAAAGAATTCTTAAATGAATGGCGTTTACGCGGCATTATCGGTAAATATTCCGATCATATCGGTCTGCCGGTGGAAATGCTGACCAAAGAATATGAGGACGAAGGCAAAGAAATCGGCGAAAAATGGGAAAAAATCAACAAATCCGATGCTCTTTGGACGCGTAGTAAAAATGAGATTTCCGATGAAGAATACAAAGAATTCTACAAGCATTTAAGCCATGATTTCGCCGACCCGCTATTGTGGGCGCATAACAAAGTAGAAGGCAATCAGGAATATACCAGCCTGCTTTATGTGCCGTCCAAAGCGCCTTGGGATTTGTTTAATCGTGAGCATAAGCACGGTTTGAAGCTCTATGTGCAACGCGTGTTTATCATGGATGACGCGGAACAATTCATGCCGAATTATCTGCGTTTTATGCGCGGCTTAATTGATAGTAACGATTTGCCGTTAAACGTGTCCCGTGAAATCTTGCAAGACAACAAAGTCACGGCGGCGTTACGCAAAGCCTTAACCAAACGTTCCTTACAAATGCTGGAAAAATTGGCGAAAGACGATGCGGAAAAATACCAACAGTCCTGGAAAGAATTCGGCTTGGTGTTAAAAGAAGGGCCAGCGGAAGATTTTGCCAACAAAGAAGCCATCGCCAAATTGTTACGTTTTGCCTCCACCCACAATGACAGCAGCGAGCAAAATGTGTCTTTGGAAGACTATGTTTCCCGCATGAAAGAAGGGCAAAAAGCCATTTATTACATCACGGCGGACAGCTACGTGGCGGCGAGAAACAGCCCGCACTTGGAGTTGTTCAATAAAAAAGGCATTGAAGTGTTGCTGTTATCCGATCGCATTGACGAATGGATGCTGAGTTACTTAACGGAATTCGACGGCAAACCGTTACAAAGCATCACCAAAGCAGATCTGGATTTGGGCGATTTGGCGGACAAAGAGGCGGAAGAACAAAAAGCACAAGACGAATCTTTCGGCAGTTTTGTTGAGCGCGTCAAAACCTTGTTGGGCGGGCGTGTGAAAGAAGTGCGTTTAACCCACCGTTTAACCGACACCCCGGCAGTGGTTTCCACCGATAACGATCAAATGACCACGCAAATGGCAAAACTTTTTGCCGCCGCAGGTCAACCGGTGCCGGAAGTAAAATACACCTTCGAGCTAAATCCGGAACATCACTTGGTGAAAAAAGTCGCTGAAATTGCCGATGAAGCACAATTCGCCGATTGGGTGGAATTGTTACTGGAACAAGCCATGCTTGCCGAACGCGGTTCCTTAGAAAACCCGGCAGCGTTTATTAAACGCATCAATAAGTTATTAGGC","","","70925","MSTNQETRGFQSEVKQLLQLMIHSLYSNKEIFLRELISNASDAADKLRFKALSNPDLYAGDGELRVCISFDSEKGTLTVSDNGIGMTREQVIDHLGTIAKSGTKEFLAALGSDQAKDSQLIGQFGVGFYSAFIVADKVTVKTRAAGEPADKGVLWESAGEGDYTVADIEKKSRGTDVILHLRDDEKEFLNEWRLRGIIGKYSDHIGLPVEMLTKEYEDEGKEIGEKWEKINKSDALWTRSKNEISDEEYKEFYKHLSHDFADPLLWAHNKVEGNQEYTSLLYVPSKAPWDLFNREHKHGLKLYVQRVFIMDDAEQFMPNYLRFMRGLIDSNDLPLNVSREILQDNKVTAALRKALTKRSLQMLEKLAKDDAEKYQQSWKEFGLVLKEGPAEDFANKEAIAKLLRFASTHNDSSEQNVSLEDYVSRMKEGQKAIYYITADSYVAARNSPHLELFNKKGIEVLLLSDRIDEWMLSYLTEFDGKPLQSITKADLDLGDLADKEAEEQKAQDESFGSFVERVKTLLGGRVKEVRLTHRLTDTPAVVSTDNDQMTTQMAKLFAAAGQPVPEVKYTFELNPEHHLVKKVAEIADEAQFADWVELLLEQAMLAERGSLENPAAFIKRINKLLG","565148","","heat shock protein","Cytoplasm","","
InterPro
IPR001404
Family
Heat shock protein Hsp90
PR00775\"[6-26]T\"[27-49]T\"[76-93]T\"[94-111]T\"[121-143]T\"[173-190]T\"[191-209]THEATSHOCK90
PTHR11528\"[6-625]THEAT SHOCK PROTEIN 90
PF00183\"[221-544]THSP90
PS00298\"[26-35]THSP90
InterPro
IPR003594
Domain
ATP-binding region, ATPase-like
G3DSA:3.30.565.10\"[5-227]Tno description
PF02518\"[28-184]THATPase_c
SM00387\"[28-185]THATPase_c


","BeTs to 13 clades of COG0326COG name: Molecular chaperone, HSP90 familyFunctional Class: OThe phylogenetic pattern of COG0326 is ------y---r-bcefghs-ujx-t-Number of proteins in this genome belonging to this COG is","Significant hit (1.5e-225) to 8/8 blocks of the IPB001404 family, which is described as \"Heat shock hsp90 proteins family\". Interpro entry for IP:IPR001404. IPB001404A 10-54 3.8e-37 IPB001404B 76-110 5.4e-26 IPB001404C 117-157 4.1e-25 IPB001404D 179-209 1.3e-17 IPB001404E 252-293 1.4e-28 IPB001404F 295-344 6.4e-39 IPB001404G 404-451 3.8e-28 IPB001404H 547-593 3.2e-16","Residues 381 to 438 match (2e-24) PD:PD558941 which is described as HEAT SHOCK CHAPERONE ATP-BINDING HTPG HIGH TEMPERATURE G PROTEOME COMPLETE ","","","","","","","","","","","","Wed Dec 18 09:27:26 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00823 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 187 to 625 (E-value = 5.1e-88) place AA00823 in the HSP90 family which is described as Hsp90 protein (PF00183)","","","","Winston,J.L., Toth,S.I., Roe,B.A. and Dyer,D.W.Cloning and characterization of the Actinobacillusactinomycetemcomitans gene encoding a heat-shock protein 90homologueGene 179 (2), 199-204 (1996)PubMed: 8972900","Bardwell,J.C. and Craig,E.A.Eukaryotic Mr 83,000 heat shock protein has a homologue inEscherichia coliProc. Natl. Acad. Sci. U.S.A. 84 (15), 5177-5181 (1987)PubMed: 3299380Spence,J. and Georgopoulos,C.Purification and properties of the Escherichia coli heat shockprotein, HtpGJ. Biol. Chem. 264 (8), 4398-4403 (1989)PubMed: 2647735Nadeau,K., Das,A. and Walsh,C.T.Hsp90 chaperonins possess ATPase activity and bind heat shocktranscription factors and peptidyl prolyl isomerasesJ. Biol. Chem. 268 (2), 1479-1487 (1993)PubMed: 8419347Nemoto,T.K., Ono,T., Kobayakawa,T., Tanaka,E., Baba,T.T., Tanaka,K., Takagi,T. and Gotoh,T.Domain-domain interactions of HtpG, an Escherichia coli homologueof eukaryotic HSP90 molecular chaperoneEur. J. Biochem. 268 (20), 5258-5269 (2001)PubMed: 11606187","Wed Dec 18 09:30:34 2002","Wed Dec 18 09:30:34 2002","1","","","" "AA00824","567185","567060","126","TTGTCAAACCGACAGTGCTCCCCGAATAACTTCCAACATCAAAGTGCGGTTGAAAAAATACTTAAATTTTCAACCGCACTTTTTTTACTACAGCTCTTGAAATTTTGCCTTCCGCACTTATATCCA","","","4871","LSNRQCSPNNFQHQSAVEKILKFSTALFLLQLLKFCLPHLYP","567060","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-38]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 14:41:14 2004","Mon Feb 23 14:41:14 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00824 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 14:41:14 2004","","","","","","","","","","","","","1","","","" "AA00825","568317","567160","1158","ATGTCATTGGATTTAAGTGAAATTCGTCGGCAAATTACGCAAATTGACCGTAGTTTATTGAAACTGCTGTCCGAGCGCCATCGTTTGGCGTTTGATGTGGTGCGGAGCAAAGAAGTGACGCAAAAGCCGTTGCGTGATGCCGCCCGTGAAGAACAGTTATTGCAGGAACTGATACAGTTCGCGGAAAACGAAAACTATCAGCTTGAACCGCAATATATCACTTCGATTTTTCAGAAAATCATTGAAGATTCGGTGCTAACGCAGCAGGTCTATTTGCAGAAGAAACTTAATGAACAGCGTGAACAGGATATTCATATTGCGTTTCTCGGCAAACGCGGTTCGTATTCTCATCTGGCGGCGCGTAATTATGCCACCCGTTATCAGGAGCAACTGGTTGAAATCAGTTGTGCGAGTTTTGAACAGGTGTTTGAGAAAGTGCGTAATGGCGAAGCGGATTACGGCGTTCTGCCGTTGGAGAACACCACTTCCGGCGCCATTAACGAAGTGTATGATTTGTTACAGCACACCGATTTATTTTTGGTGGGCGAACTTGCCTATCCGATTCAACATTGCGTGTTAGTGAATGAACAGGATGATTTGAGCAAAATTGATACCTTGTACAGCCACCCACAAGTGATTCAACAATGCAGTCAATTTATCCAAGGTTTACGGGTGCATATTGAATATTGTGAAAGTAGCTCCCATGCCATGCAGTTGGTTGCCGGTTTAAATAAGCCGAATATTGCGGCATTAGGTAATGAGGACGGCGGCAAGTTGTATGGCTTGAAAGTGTTGCGACGCAATATCGCCAACCAAGAAAACAATATTACCCGTTTTATCGTGATCGCGAAGAAAGCACACAGCGTCTCCCCGCAAATTCACACCAAAACGCTATTGTTAATGAGCACAGGGCAACAAGCGGGATCTTTGGTTGACGCCTTATTGGTGTTTAAAAAGCACCATATTAATATGACAAAGCTGGAGTCCCGCCCGATTTACGGTAAGTCTTGGGAGGAAATGTTTTATTTGGAAATTGAAGCCAACATTCACCACCCTGATACGCAAGCTGCGTTGGAAGAATTAAAAAAATTCAGTAATTATCTGAAAATTCTGGGGTGTTATCCAAGCGAAATTGTCAAACCGACAGTGCTCCCCGAA","","","48999","MSLDLSEIRRQITQIDRSLLKLLSERHRLAFDVVRSKEVTQKPLRDAAREEQLLQELIQFAENENYQLEPQYITSIFQKIIEDSVLTQQVYLQKKLNEQREQDIHIAFLGKRGSYSHLAARNYATRYQEQLVEISCASFEQVFEKVRNGEADYGVLPLENTTSGAINEVYDLLQHTDLFLVGELAYPIQHCVLVNEQDDLSKIDTLYSHPQVIQQCSQFIQGLRVHIEYCESSSHAMQLVAGLNKPNIAALGNEDGGKLYGLKVLRRNIANQENNITRFIVIAKKAHSVSPQIHTKTLLLMSTGQQAGSLVDALLVFKKHHINMTKLESRPIYGKSWEEMFYLEIEANIHHPDTQAALEELKKFSNYLKILGCYPSEIVKPTVLPE","567162","","P-protein (chorismate mutase/prephenate dehydratase)","Cytoplasm","","
InterPro
IPR001086
Domain
Prephenate dehydratase
PF00800\"[106-287]TPDT
PS51171\"[105-284]TPREPHENATE_DEHYDR_3
PS00857\"[260-282]TPREPHENATE_DEHYDR_1
PS00858\"[324-331]TPREPHENATE_DEHYDR_2
InterPro
IPR002701
Domain
Chorismate mutase
PF01817\"[9-91]TCM_2
PS51168\"[1-92]TCHORISMATE_MUT_2
InterPro
IPR008242
Family
Bifunctional chorismate mutase/prephenate dehydratase P-protein
PIRSF001500\"[2-379]TBifunctional chorismate mutase/prephenate dehydratase (P-protein)
InterPro
IPR010952
Domain
Chorismate mutase, gammaproteobacteria
TIGR01797\"[5-89]TCM_P_1: chorismate mutase
noIPR
unintegrated
unintegrated
G3DSA:1.20.59.10\"[4-109]Tno description
PTHR21022\"[62-384]TPREPHENATE DEHYDRATASE (P PROTEIN)


","BeTs to 19 clades of COG0077COG name: Prephenate dehydrataseFunctional Class: EThe phylogenetic pattern of COG0077 is aomp--yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 5.8e-79) to 6/6 blocks of the IPB001086 family, which is described as \"Prephenate dehydratase (PDT)\". Interpro entry for IP:IPR001086. IPB001086A 106-118 7.1e-05 IPB001086B 152-173 2.4e-12 IPB001086C 182-193 0.0051 IPB001086D 203-220 2.9e-09 IPB001086E 249-282 8.3e-17 IPB001086F 296-348 1.8e-25Significant hit ( 7.1e-11) to 1/1 blocks of the IPB002701 family, which is described as \"Chorismate mutase\". Interpro entry for IP:IPR002701. IPB002701 5-37 7e-11","Residues 106 to 238 match (1e-06) PD:PD560121 which is described as PROTEOME COMPLETE P-PROTEIN DEHYDRATASE CHORISMATE MUTASE/PREPHENATE ","","","","","","","","","","","","Tue Jan 14 14:22:46 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00825 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 106 to 287 (E-value = 2.4e-95) place AA00825 in the PDT family which is described as Prephenate dehydratase (PF00800)","","","","","Zhang S, Pohnert G, Kongsaeree P, Wilson DB, Clardy J, Ganem B.1998. Chorismate mutase-prephenate dehydratase from Escherichia coli.Study of catalytic and regulatory domains using genetically engineered proteins. J Biol Chem. 273(11):6248-53. PubMed: . Fischer RS, Zhao G, Jensen RA. 1991. Cloning, sequencing, and expression of the P-protein gene (pheA) of Pseudomonas stutzeri in Escherichia coli: implications for evolutionary relationships in phenylalanine biosynthesis. J Gen Microbiol. 137 (Pt 6):1293-301. PubMed: .","","Wed Dec 18 09:34:44 2002","1","","","" "AA00826","569432","568518","915","ATGATTAAACAAAGAACATTAAAACAAAGTATAAAAGTTACCGGTGTGGGATTACACAGTGGTGATAAGGTTACTTTGGTTTTACGTCCTGCAATGCCGAATACCGGTGTTGTTTATTGCCGCACCGATTTGAATCCGCCGGTTACCTTTCCGGCGAATGCTAATGCAGTGCACGATACTATGCTTTGTACTTGTTTAGTGAATGAGCAGGGTGTGCGAATTTCAACGGTTGAACATCTAAATGCGGCTTTAGCAGGACTTGGTATCGATAACATTATTGTTGAAGTGGATGCGCCTGAAATTCCAATTATGGATGGTAGTGCAAGCCCGTTTATTTATTTATTATTAGATGCAGGTATTGAAGAACAAAATGCACCGAAAAAATTCATTCGTGTCAAACAAAAAGTTCGCGTGGAAGATGGTGATAAATGGGCGGAATTTTCTCCTTATAATGGTTTCCGTTTGAATTTCACTATTGATTTTAATCATCCGGTAATTAGCGAAGATGTACGTAATTATGTGATGGATTTCTCCGCGCAAGCATTTGTTCAGCAAATCAGCCGCGCGAGAACTTTTGGTTTTATGAAAGATATTGAGTATCTTCAATCTCAAGGTTTAGCGTTAGGCGGCAGTTTAGATAATGCTATCGTACTGGATGATTATCGCATTCTGAATGAGGACGGTTTGCGTTTCAAAGATGAACTGGTCCGTCACAAAATGCTGGATGCTATTGGTGATTTATATATGTGTGGTTATAACATTATCGGTGATTTCAAAGCCTATAAATCAGGTCATGGTTTAAACAATAAATTATTAAGAGCGGTATTGGATAATCAAGAAGCGTGGGAACTCGTAACCTTCGAAGACAAAGAACAAGTCCCACAAGGTTATATTTCTCCCGCACAAATATTGATT","","","34055","MIKQRTLKQSIKVTGVGLHSGDKVTLVLRPAMPNTGVVYCRTDLNPPVTFPANANAVHDTMLCTCLVNEQGVRISTVEHLNAALAGLGIDNIIVEVDAPEIPIMDGSASPFIYLLLDAGIEEQNAPKKFIRVKQKVRVEDGDKWAEFSPYNGFRLNFTIDFNHPVISEDVRNYVMDFSAQAFVQQISRARTFGFMKDIEYLQSQGLALGGSLDNAIVLDDYRILNEDGLRFKDELVRHKMLDAIGDLYMCGYNIIGDFKAYKSGHGLNNKLLRAVLDNQEAWELVTFEDKEQVPQGYISPAQILI","568520","","UDP-3-O-acyl-GlcNAc deacetylase","Cytoplasm","","
InterPro
IPR004463
Family
UDP-3-0-acyl N-acetylglucosamine deacetylase
PD011499\"[2-133]TLPXC_PASMU_Q9CPA5;
PF03331\"[2-280]TLpxC
TIGR00325\"[1-305]TlpxC: UDP-3-0-acyl N-acetylglucosamine deac
noIPR
unintegrated
unintegrated
G3DSA:3.30.1700.10\"[129-283]Tno description
G3DSA:3.30.230.20\"[2-127]Tno description


","BeTs to 12 clades of COG0774COG name: UDP-3-O-acyl-N-acetylglucosamine deacetylaseFunctional Class: MThe phylogenetic pattern of COG0774 is -------q-----cefghsnujxi--Number of proteins in this genome belonging to this COG is","","Residues 28 to 287 match (6e-136) PD:PD011499 which is described as DEACETYLASE LIPID N-ACETYLGLUCOSAMINE COMPLETE UDP-3-O-3-HYDROXYMYRISTOYL PROTEOME HYDROLASE 3.5.1.- BIOSYNTHESIS A ","","","","","","","","","","","","Wed Dec 18 09:37:20 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00826 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 280 (E-value = 3.3e-185) place AA00826 in the LpxC family which is described as UDP-3-O-acyl N-acetylglycosamine deacetylase (PF03331)","","","","","Beall,B. and Lutkenhaus,J. Sequence analysis, transcriptional organization, andinsertional mutagenesis of the envA gene of Escherichia coli J. Bacteriol. 169 (12), 5408-5415 (1987) M:88058745 Hyland,S.A., Eveland,S.S. and Anderson,M.S. Cloning, expression, and purification of UDP-3-O-acyl-GlcNAc deacetylase from Pseudomonas aeruginosa: a metalloamidase ofthe lipid A biosynthesis pathway J. Bacteriol. 179 (6), 2029-2037 (1997) PubMed: 9068651 Young,K., Silver,L.L., Bramhill,D., Caceres,C.A.,Stachula,S.A., Shelly,S.E., Raetz,C.R.H. and Anderson,M.S. The second step of lipid A biosynthesis, UDP-3-O-acyl-GlcNAc deacetylase is encoded by the pleotropic permeability/celldivision gene envA of E.coli FASEB J. 7, 1268-1268 (1993) Kloser,A.W., Laird,M.W. and Misra,R. asmB, a suppressor locus for assembly-defective OmpF mutants of Escherichia coli, is allelic to envA (lpxC) J. Bacteriol. 178 (17), 5138-5143 (1996) PubMed: 8752330 ","","Wed Dec 18 09:37:20 2002","1","","","" "AA00827","570753","569473","1281","ATGTTTGAGCCAGTAGATTATGATCTCGGTGAAATGAATGGAGCACTGATTAAAGTGGTCGGTGTCGGTGGCGGTGGCGGTAATGCCGTTAACCACATGGTTGCCACGATGGTTAAAGATGATATTGGCGGTGCCCTTGTTGATGAAACAATGTTGAACACTGATGAACATGGAAAAATCATGTTCTATGCCATTAATACCGATGCACAGGCATTGCGTAAAAGCCAAGTGCAGCAAACGGTTCAAATTGGTGCGAATACCACCAAGGGTTTGGGCGCGGGTGCCAACCCGAATGTCGGACGTAAAGCCGCAGAAGACGATCAGGATGCCATTCGTCAAATGTTAGAAGGCGCTGATATGGTGTTTATCGCTGCCGGCATGGGTGGTGGTACAGGCACAGGTGCTGCACCGATAGTCGCTCAAATCGCAAAAGAATTGGGTATTCTTACCGTTGCTGTGGTTACCAAGCCATTTGCTTTTGAAGGTAAGAAACGAATGATGTTCGCCGAAATGGGGATTAAAGAATTATCCAAACATGTAGATTCCCTAATCATCATCCCAAATGAACAATTAGCCAAGGTTATGCCGAAAAATGCAACATTAATGCAAGCTTTCTCCGCCGCTAATGATGTGTTGCGTAATTCTGTTACCGGTATTTCGGATATGATTACCTCTCCGGGTTTAATTAACGTGGACTTTGCCGATGTTCGTACCGTAATGTCGGAGATGGGGCAGGCAATGATTGGTTTTGGTTCTGCATTGGGTTCACCGGGTGAAGGTCGTGCGGAAGATGCAGCTAAAATTGCAGTGAAAAGTGACTTGTTAGAGCGTGTGGATTTATCCGGTGCCAGAGGGGTATTGGTTAATATTACGGCCGGTATGGACTTAGGCTTAACCGAGTTCCAGGCAGTAGGCGATACAATTAAAGCATTTGCTTCTGATGAGGCTACGGTTGTAGTCGGTACAACATTGGTGCCTGATATGGTGGATGAAATCCGCGTAACCATTGTTGCAACAGGTATTGGTGAACCCGAAGCGCCGGAGATTCAAATTTCTCCACGTCCACAAGCAGCCCCGAATAATCAACCGATAAATACTCAGTTCGGCGCGCCGAGAACAAATGCGCCAACTTATGGACATAGTGCACAGGATGCGAATAATTTGTCCAATAACCAGCAAAACGTACAACGTAGTAGAGACGATTTAGATACGCCGATTACCGAACGCTTGAAAGATACTAATTTGTTCAATGTTCAAGGTTTTATGCGTAATGGCGATAAA","","","44906","MFEPVDYDLGEMNGALIKVVGVGGGGGNAVNHMVATMVKDDIGGALVDETMLNTDEHGKIMFYAINTDAQALRKSQVQQTVQIGANTTKGLGAGANPNVGRKAAEDDQDAIRQMLEGADMVFIAAGMGGGTGTGAAPIVAQIAKELGILTVAVVTKPFAFEGKKRMMFAEMGIKELSKHVDSLIIIPNEQLAKVMPKNATLMQAFSAANDVLRNSVTGISDMITSPGLINVDFADVRTVMSEMGQAMIGFGSALGSPGEGRAEDAAKIAVKSDLLERVDLSGARGVLVNITAGMDLGLTEFQAVGDTIKAFASDEATVVVGTTLVPDMVDEIRVTIVATGIGEPEAPEIQISPRPQAAPNNQPINTQFGAPRTNAPTYGHSAQDANNLSNNQQNVQRSRDDLDTPITERLKDTNLFNVQGFMRNGDK","569475","From GenBank (gi:1169767):This protein is essential to the cell-division process. It seems to assemble into a dynamic ring on the inner surface of the cytoplasmic membrane at the place where division will occur, and the formation of the ring is the signal for septation to begin. Binds to and hydrolyzes GTP. It assembles at the inner surface of the cytoplasmic membrane ","cell division tubulin-like protein Z","Inner membrane, Periplasm, Cytoplasm","","
InterPro
IPR000158
Family
Cell division protein FtsZ
PR00423\"[82-100]T\"[120-140]T\"[148-169]T\"[211-233]T\"[234-255]T\"[282-300]TCELLDVISFTSZ
TIGR00065\"[2-373]TftsZ: cell division protein FtsZ
PS01134\"[66-100]TFTSZ_1
PS01135\"[119-140]TFTSZ_2
InterPro
IPR001412
Family
Aminoacyl-tRNA synthetase, class I
PS00178\"[371-381]?AA_TRNA_LIGASE_I
InterPro
IPR003008
Domain
Tubulin/FtsZ, GTPase
PF00091\"[15-227]TTubulin
InterPro
IPR008280
Domain
Tubulin/FtsZ, C-terminal
PF03953\"[229-360]TTubulin_C
noIPR
unintegrated
unintegrated
G3DSA:3.30.1330.20\"[243-341]Tno description
G3DSA:3.40.50.1440\"[4-242]Tno description


","BeTs to 23 clades of COG0206COG name: Cell division GTPaseFunctional Class: DThe phylogenetic pattern of COG0206 is aompk--qvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is","Significant hit (8.3e-108) to 4/4 blocks of the IPB000158 family, which is described as \"Cell division protein FtsZ\". Interpro entry for IP:IPR000158. IPB000158A 48-99 1.3e-20 IPB000158B 117-162 4.1e-41 IPB000158C 208-259 6.9e-30 IPB000158D 272-300 9.6e-13","Residues 64 to 277 match (2e-09) PD:PD040715 which is described as DIVISION CELL COMPLETE GTP-BINDING PROTEOME MULTIGENE FTSZ HOMOLOG FAMILY SEPTATION ","","","","","","","","","","","Tue Jan 14 14:30:26 2003","Wed Dec 18 09:39:47 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00827 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 229 to 358 (E-value = 8e-37) place AA00827 in the Tubulin_C family which is described as Tubulin/FtsZ family, C-terminal domain (PF03953)","","","","","Yi,Q.M. and Lutkenhaus,J. The nucleotide sequence of the essential cell-division geneftsZ of Escherichia coli Gene 36 (3), 241-247 (1985) M:86083166 Yi,Q.M., Rockenbach,S., Ward,J.E. Jr. and Lutkenhaus,J. Structure and expression of the cell division genes ftsQ,ftsA and ftsZ J. Mol. Biol. 184 (3), 399-412 (1985) M:86011551 RayChaudhuri,D. and Park,J.T. Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein Nature 359 (6392), 251-254 (1992) M:92408783 Baumann,L. and Baumann,P. Characterization of ftsZ, the cell division gene of Buchnera aphidicola (endosymbiont of aphids) and detection of theproduct Curr. Microbiol. 36 (2), 85-89 (1998) M:98087557 ","","Wed Dec 18 09:39:47 2002","1","","","" "AA00830","572117","570840","1278","ATGTCTAAAATTGTGGAATCAAAGACGATTGTTGGTTTGGAAGTGGGTACTTCTAAAGTCGTTGCCGTAGTCGGTGAAGTTTTACCGGACGGTGTCGTAAATGTGCTTGGCGTGGGCAGTTGTCCGTCTAAAGGGATCGATAAAGGAAGCATTACTGACCTCAATGCGGTGGTTATATCTATTCAACGGGCTATTGAAGCGGCCGAATCCGTTGCCGATTGCCGGATTATGAGCGTGACTTTGGCGATTACCGGTGAGCATATTCAAAGCCTGAATGAGAATGGCTTTGTACCTATTGCCGAAGGCGAGGTGACCCAAGATGAAATTGATTCTGCTATTCACACGGCAAGCTCGGTTAAAATGCCGGAAGGATTGTCGTTACTTCACATTATTCCGCAAGAATTTGCTGTCGATAAGCAAATGAACATTAAAAATCCGTTGGGCTTACAAGGTGTTCGTTTAAAAGCGCAGACTCACTTAATCGCTTGTCATCAGGACTGGTTAAATAACCTGAAGAAGGCGGTAGAACGTTGTAAATTAAAAGTCGATAAGATTGTGTTCTCAGGCTTGGCTTCCAGCTATTCCGTTTTAACCGAAGATGAAAAAGATTTAGGGGTTTGTTTGATTGATTTCGGTGCCGGTACCATGGACATTATGGTGTATATCAACGGTGCATTGCGTTTCAGTAAAGTGATTCCTTATGCCGGTAATCGTGTCACCGATGATATTGCGTATGCTTGTGCCACTTCTAGAATGGAGGCGGAAAGCATCAAAGTGAATCATGGTAGTGCATTAACGCCGCCGAAATATCATGCCGACAAGAAAATTGAAGTTTCCAGTATCGGCGGGCGAGGCCCTCGCACATTAACAAAAGAACAGCTTTCTTTAGTAACTTCGGCCCGTTATAAAGAACTATTGAGTTTGGTGAAAAATGAATTAATTTATTTGAAAACGGATTTGGAAGCTAAACATATTAAGTTTGATCTCATTGCCGGCGTTGTGATTACCGGTGGTGGTGCACAAATTGAAGACTTGAAAGATAGTGCGGCGGAAGTGTTTGGGCAAAATGCGCAGGTGAGAATTGGTAGCCCGCTAAATATTACCGGTTTGACCGATTATGTGAACAAACCGCAATACGCGACTGTCATTGGTTTGTTGCAATATGAACATAGCAATGAGGATGAAGGGCCGCTTAATGATGAGAATTCGGATAGCGGATTTTTTAGCGCATGCGGTAAGGTAGTGAAAAAAATTTTTAATAAAGTGCGGTCGGAATTT","","","45875","MSKIVESKTIVGLEVGTSKVVAVVGEVLPDGVVNVLGVGSCPSKGIDKGSITDLNAVVISIQRAIEAAESVADCRIMSVTLAITGEHIQSLNENGFVPIAEGEVTQDEIDSAIHTASSVKMPEGLSLLHIIPQEFAVDKQMNIKNPLGLQGVRLKAQTHLIACHQDWLNNLKKAVERCKLKVDKIVFSGLASSYSVLTEDEKDLGVCLIDFGAGTMDIMVYINGALRFSKVIPYAGNRVTDDIAYACATSRMEAESIKVNHGSALTPPKYHADKKIEVSSIGGRGPRTLTKEQLSLVTSARYKELLSLVKNELIYLKTDLEAKHIKFDLIAGVVITGGGAQIEDLKDSAAEVFGQNAQVRIGSPLNITGLTDYVNKPQYATVIGLLQYEHSNEDEGPLNDENSDSGFFSACGKVVKKIFNKVRSEF","570842","From GenBank (gi:1169751):This protein may be involved in anomalous filament growth, may be a component of the septum, and may interact with FtsZ. It belongs to the FtsA/MreB family.","cell division protein A","Cytoplasm","","
InterPro
IPR003494
Family
Cell division protein FtsA
PF02491\"[10-196]T\"[206-385]TFtsA
TIGR01174\"[9-388]TftsA: cell division protein FtsA


","BeTs to 14 clades of COG0849COG name: Predicted ATPases of the HSP70 class involved in cell divisionFunctional Class: DThe phylogenetic pattern of COG0849 is -------qvd-lbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 2.4e-17) to 2/2 blocks of the IPB003494 family, which is described as \"Cell division protein FtsA\". Interpro entry for IP:IPR003494. IPB003494A 196-215 3.1e-12 IPB003494B 331-340 0.0018","Residues 366 to 426 match (1e-13) PD:PD130901 which is described as CELL DIVISION FTSA COMPLETE PROTEOME SHAPE WITH ATP-BINDING INNER FTSZ ","","","","","","","","","","","Tue Jan 14 14:34:15 2003","Tue Jan 14 14:34:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00830 is paralogously related to AA01371 (0.001).","","","","","","Residues 199 to 386 (E-value = 6e-53) place AA00830 in the FtsA family which is described as Cell division protein FtsA (PF02491)","","","","","Robinson,A.C., Kenan,D.J., Hatfull,G.F., Sullivan,N.F., Spiegelberg,R. and Donachie,W.D. DNA sequence and transcriptional organization of essentialcell division genes ftsQ and ftsA of Escherichia coli: evidencefor overlapping transcriptional units J. Bacteriol. 160 (2), 546-555 (1984) M:85054557 Yi,Q.M., Rockenbach,S., Ward,J.E. Jr. and Lutkenhaus,J. Structure and expression of the cell division genes ftsQ,ftsA and ftsZ J. Mol. Biol. 184 (3), 399-412 (1985) M:86011551 Pichoff S, Lutkenhaus J. Unique and overlapping roles for ZipA and FtsA in septal ringassembly in Escherichia coli. EMBO J. 2002 Feb 15;21(4):685-93. PMID: 11847116 ","","Wed Dec 18 09:41:07 2002","1","","","" "AA00831","572909","572145","765","ATGAATTTACTAAAACGCAAAACCCCACAAAATATAAGATATGGTGAACCTAAATCAAAAGTTTTTGTGCAAATTAAATTATTACTTGTGCTATTATGCGTTGGCATTTTGTTCTATTCTTGTTCAAATTGGCAAAATTTTTTAGAAAAATTAGATAGTAAGCCAATCAGCGCATTTGCTTTGGTCGGCACGCCGAATTTTACCGATGATGCGGATGTGCGCGAAGCCCTGCTGAAAATGGGAGAACTTAAAGGGTTTTTCGGTCAGGATGCCGATTTAATTCGTGAACAAATTGAGACAATGCCTTGGATTAAAGGCGCGGTTGTTCGCAAAATGTGGCCGAACAGGTTAAGCATTTGGGTTACGGAGTATCAACCGGTCGCTATTTGGAACGAAACCGAATTCCTCTCAAAAGACGGCGTGGTTTTTCAGCTGCCGATGAATAAATTGAAAGAGCAGCATCTGCCTCGTTTGTCCGGACCCGATTTCCAAAGTGAAAAAGTGCTGGATGCCTGGAATAGAATTTATGCCGATTTAAAACAAAAAGGGTTAACCCTTAAAGCGGTTGCTATTGACGCACGCGGCGCTTGGCAGGTGGTATTGGATAATGATGTGGTGCTGAAACTTGGGCGTGGTGAGTGGAAAACAAAACTGGATCGTTTTGTGACCATTTATCCGCAAATTGAGGTGCCTGAAAATAAAAAACTCTCCTATGTGGATTTGCGTTACGCTTCCGGTGCTTCGGTGGGTATGGTTGATTTAAAT","","","29178","MNLLKRKTPQNIRYGEPKSKVFVQIKLLLVLLCVGILFYSCSNWQNFLEKLDSKPISAFALVGTPNFTDDADVREALLKMGELKGFFGQDADLIREQIETMPWIKGAVVRKMWPNRLSIWVTEYQPVAIWNETEFLSKDGVVFQLPMNKLKEQHLPRLSGPDFQSEKVLDAWNRIYADLKQKGLTLKAVAIDARGAWQVVLDNDVVLKLGRGEWKTKLDRFVTIYPQIEVPENKKLSYVDLRYASGASVGMVDLN","572147","From GenBank (gi:1169759):This protein may be involved in septum formation and is a type II inner membrane protein .","cell division protein Q","Inner membrane, Cytoplasm","","
InterPro
IPR005548
Family
Cell division protein FtsQ
PF03799\"[127-242]TFtsQ
InterPro
IPR013685
Domain
Polypeptide-transport-associated, FtsQ-type
PF08478\"[54-124]TPOTRA_1
noIPR
unintegrated
unintegrated
signalp\"[1-35]?signal-peptide
tmhmm\"[21-41]?transmembrane_regions


","BeTs to 9 clades of COG1589COG name: Cell division septal proteinFunctional Class: MThe phylogenetic pattern of COG1589 is ---------drlbcefghsn-jx-t-Number of proteins in this genome belonging to this COG is","","Residues 1 to 89 match (8e-19) PD:PD039125 which is described as PROTEOME COMPLETE DIVISION FTSQ CELL TRANSMEMBRANE MEMBRANE HOMOLOG SEPTATION INNER ","","","","","","","","","","","Tue Jan 14 14:37:47 2003","Wed Dec 18 09:43:20 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00831 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 25 to 242 (E-value = 3.1e-61) place AA00831 in the FtsQ family which is described as Cell division protein FtsQ (PF03799)","","","","","Yi,Q.M., Rockenbach,S., Ward,J.E. Jr. and Lutkenhaus,J. Structure and expression of the cell division genes ftsQ,ftsA and ftsZ J. Mol. Biol. 184 (3), 399-412 (1985) M:86011551 Robinson,A.C., Kenan,D.J., Hatfull,G.F., Sullivan,N.F., Spiegelberg,R. and Donachie,W.D. DNA sequence and transcriptional organization of essentialcell division genes ftsQ and ftsA of Escherichia coli: evidencefor overlapping transcriptional units J. Bacteriol. 160 (2), 546-555 (1984) M:85054557 Robinson,A.C., Kenan,D.J., Sweeney,J. and Donachie,W.D. Further evidence for overlapping transcriptional units in an Escherichia coli cell envelope-cell division gene cluster:DNA sequence and transcriptional organization of the ddl ftsQregion J. Bacteriol. 167 (3), 809-817 (1986) M:86304170 ","","Wed Dec 18 09:43:20 2002","1","","","" "AA00832","573835","572909","927","ATGAGTAAAACATTAAAACAGGAAAAAATCGCCGTTTTATTAGGCGGAACCTCCGCAGAACGCGAGGTGTCTTTAAATTCGGGCGAAGCAGTATTAAATGCGTTGCGTAAACAAGGGTATGACGCCCATCCGATTGATCCGAAAACCTTTCCGGTAGCGACCTTAAAAGAACAGGGATTTGATCGCGTGTTTAATATTTTGCACGGTCGCGGCGGCGAAGACGGCACGATGCAGGGCTTATTAGAGCAAATCGGCATTCCTTATACCGGTTGCGGCGTGATGACTTCTGCGTTAACTATGGATAAAATGCGTACTAAAATGTTGTGGAAGGCATTTGGTTTGCCGGTCGCCGAGATGGAAATCGTGACGACGGAAAATAGAGTAAACTTAAACCTGGAGTCTGTGGTCAAAAAGCTAGGATTACCGCTGATGGTTAAGCCTTCTCTGGAAGGTTCCAGCGTGGGGTTAACCAAAGTCAAAGCTGTGGATGAACTGGAAAGTGCGGTGGATTTCGCGCTTAAATTCGATAACACGGTGTTAATTGAAGAATGGCTTGCCGGCGATGAATTTACCGTGCCGGTGCTGGATAATGAAGTTTTGCCTTCCATTAAAATTGTGCCGGAAGGTGAGTTTTATGATTACGACGCGAAATACATCTCTGACAATACGCAATATTTTTGCCCGGCGGGATTAAGCGAGGAGCGTGAACAGGAGCTCCGCCGTTTGGTAAAACAGGCCTATGATGTGGTGGGCTGTCGTGGTTGGAGCCGTATTGATGTGATGGCGGATGCGGAAGGAAAGTTCCGTTTGGTGGAAGTTAATACCAACCCTGGCATGACCAGCCACAGTTTATTCCCGAAATCGGCGGCAACGGTCGGCTATTCTTTTGCGCAGTTGGTTGAGAAAATTTTAGAGTTGAGCGCGGAA","","","34492","MSKTLKQEKIAVLLGGTSAEREVSLNSGEAVLNALRKQGYDAHPIDPKTFPVATLKEQGFDRVFNILHGRGGEDGTMQGLLEQIGIPYTGCGVMTSALTMDKMRTKMLWKAFGLPVAEMEIVTTENRVNLNLESVVKKLGLPLMVKPSLEGSSVGLTKVKAVDELESAVDFALKFDNTVLIEEWLAGDEFTVPVLDNEVLPSIKIVPEGEFYDYDAKYISDNTQYFCPAGLSEEREQELRRLVKQAYDVVGCRGWSRIDVMADAEGKFRLVEVNTNPGMTSHSLFPKSAATVGYSFAQLVEKILELSAE","572911","From GenBank (gi:1169257):This protein is involve in cell wall formation. Along with alanine racemase, it makes up the D-alanine branch of the peptidoglycan biosynthetic route.","D-alanine-D-alanine ligase B","Cytoplasm","","
InterPro
IPR000291
Family
D-alanine--D-alanine ligase/VANA/B/C
PS00843\"[68-79]TDALA_DALA_LIGASE_1
PS00844\"[250-278]TDALA_DALA_LIGASE_2
InterPro
IPR005905
Family
D-alanine--D-alanine ligase
TIGR01205\"[9-308]TD_ala_D_alaTIGR: D-alanine--D-alanine ligas
InterPro
IPR011095
Domain
D-alanine--D-alanine ligase, C-terminal
PF07478\"[101-305]TDala_Dala_lig_C
InterPro
IPR011127
Domain
D-alanine--D-alanine ligase, N-terminal
PF01820\"[8-100]TDala_Dala_lig_N
InterPro
IPR011761
Domain
ATP-grasp fold
PS50975\"[106-305]TATP_GRASP
InterPro
IPR013816
Domain
ATP-grasp fold, subdomain 2
G3DSA:3.30.470.20\"[160-308]Tno description
InterPro
IPR013817
Domain
Pre-ATP-grasp fold
G3DSA:3.40.50.20\"[6-89]Tno description
noIPR
unintegrated
unintegrated
PTHR23132\"[50-309]TD-ALANINE--D-ALANINE LIGASE


","BeTs to 17 clades of COG1181COG name: D-alanine-D-alanine ligase and related ATP-grasp enzymesFunctional Class: MThe phylogenetic pattern of COG1181 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 7.5e-91) to 6/6 blocks of the IPB000291 family, which is described as \"D-alanine--D-alanine ligase\". Interpro entry for IP:IPR000291. IPB000291A 12-35 1.1e-12 IPB000291B 61-98 1.5e-28 IPB000291C 141-178 2.2e-16 IPB000291D 211-220 9.4e-05 IPB000291E 227-262 8.7e-17 IPB000291F 270-280 8.6e-05","Residues 211 to 307 match (6e-40) PD:PD522734 which is described as LIGASE PROTEOME COMPLETE D-ALANINE--D-ALANINE CELL SYNTHETASE D-ALA-D-ALA WALL D-ALANYLALANINE PEPTIDOGLYCAN ","","","","","","","","","","","Tue Jan 14 14:40:45 2003","Wed Dec 18 10:16:37 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00832 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 305 (E-value = 3.2e-162) place AA00832 in the Dala_Dala_ligas family which is described as D-ala D-ala ligase (PF01820)","","","","","Fan,C., Park,I.S., Walsh,C.T. and Knox,J.R. D-alanine:D-alanine ligase: phosphonate and phosphinate intermediates with wild type and the Y216F mutant Biochemistry 36 (9), 2531-2538 (1997) PubMed: 9054558 Fan,C., Moews,P.C., Walsh,C.T. and Knox,J.R. Vancomycin resistance: structure of D-alanine:D-alanineligase at 2.3 A resolution Science 266 (5184), 439-443 (1994) PubMed: 7939684 al-Bar,O.A., O\"Connor,C.D., Giles,I.G. and Akhtar,M. D-alanine: D-alanine ligase of Escherichia coli. Expression, purification and inhibitory studies on the cloned enzyme Biochem. J. 282 (Pt 3), 747-752 (1992) PubMed: 1554356 Robinson,A.C., Kenan,D.J., Sweeney,J. and Donachie,W.D. Further evidence for overlapping transcriptional units in an Escherichia coli cell envelope-cell division gene cluster:DNA sequence and transcriptional organization of the ddl ftsQregion J. Bacteriol. 167 (3), 809-817 (1986) PubMed: 3528126 ","","Tue Jan 14 14:41:31 2003","1","","","" "AA00833","575278","573851","1428","ATGGAAAATTATCATCAACAGATTAGAAACATCATTCCGGAAATGCGCCGAGTAAAACAAATTCATTTTATCGGCATCGGCGGCGCGGGGATGTGTGGTATTGCGGAAATTTTATTGAACGAAGGCTATTCGATCTCCGGTTCGGATATTGCCGAAAGTGCAGTTACTCAGTGCTTAACCAAAGCCGGGGCGAAAGTGTTTATCGGACATCAAGCGGAGAATATTGTAGGCGCCAGCGTGGTGGTGATTTCCTCTGCCATTCATGGCGATAACCCGGAAGTGATGGCGGCGAAAGAAGCCCGTATTCCGGTGATTCAACGTGCACAAATGCTGGCGGAGTTAATGCGTTTCCGCCACGGTATTGCCGTTGCCGGTACGCACGGTAAAACCACCACTACCGCGATGGTTTCCATGATTTACGCCGAAGCGGGATTGGACCCGACGTTCGTTAACGGTGGCTTGGTGAAATCCGCAGGCACCAATGCTCATTTAGGCTGTAGCCGTTATTTGATCGCCGAAGCCGACGAAAGTGACGCGTCTTTTCTGCATTTGCAACCGATGATTTCCATCGTGACGAATATTGAACCGGATCACATGGATACCTATCACGGCGATTTTGATGAAATGAAACAAACCTATGTGAATTTTCTGCATAATTTGCCGTTTTATGGTTTGGCGGTGTTATGTGCCGATGATGAGGTGCTGATGGAGTTGGTTCCGCTGGTCGGGCGTCAGGTGATCACTTACGGCTTTAGTGAAAATGCCGATTATCGCATTGAAGATTATCAACAAACCGGTTTTCAAGGGCATTACACGGTGATTTGCCCGAACGGTGAGCGTATTGATGTGTTGCTGAATGTGCCGGGACGCCATAATGCACTGAATGCTACCGCCGCCTTGGTGGTCGCCAAAGAAGAAGGCATTAAAAATGACGCTATTTTAGCCGCGTTGGCGGATTTCCAAGGCGCAGGACGTCGTTTCGATCAATTGGGACAATTTATCCGCCCGAACGGTAAAGTGATGTTGGTGGACGATTACGGTCATCATCCGACGGAAGTGGGCGTTACCATTCAAGCGGCGCGTCAAGGCTGGGAAAATAAACGTATTGTGATGATTTTCCAGCCGCACCGTTATTCCCGCACCCGCGATTTATTTGATGATTTCGTGCAGGTGTTATCTCAAGTGGATGCGTTGATTATGTTGGATGTGTATCCGGCAGGCGAAGCGCCGATAGTAGGCGCGGATAGTAAGGCATTGTGCCGTTCTATTCGTAATCTGGGAAAAGTGGATCCGATTTTGGTTTCCGATACGGAACAGTTGGGTGAGGTGCTCGATCAGATTATTCAGGATGGCGATTTAATTTTGGCGCAGGGCGCCGGTAGCGTGAGTAAACTTTCACGTCAGTTGGTGGAATGTTGGACGAAAGAA","","","54486","MENYHQQIRNIIPEMRRVKQIHFIGIGGAGMCGIAEILLNEGYSISGSDIAESAVTQCLTKAGAKVFIGHQAENIVGASVVVISSAIHGDNPEVMAAKEARIPVIQRAQMLAELMRFRHGIAVAGTHGKTTTTAMVSMIYAEAGLDPTFVNGGLVKSAGTNAHLGCSRYLIAEADESDASFLHLQPMISIVTNIEPDHMDTYHGDFDEMKQTYVNFLHNLPFYGLAVLCADDEVLMELVPLVGRQVITYGFSENADYRIEDYQQTGFQGHYTVICPNGERIDVLLNVPGRHNALNATAALVVAKEEGIKNDAILAALADFQGAGRRFDQLGQFIRPNGKVMLVDDYGHHPTEVGVTIQAARQGWENKRIVMIFQPHRYSRTRDLFDDFVQVLSQVDALIMLDVYPAGEAPIVGADSKALCRSIRNLGKVDPILVSDTEQLGEVLDQIIQDGDLILAQGAGSVSKLSRQLVECWTKE","573853","From GenBank (gi:1171071):This protein is involved in cell wall formation.","UDP-N-acetylmuramate-alanine ligase","Cytoplasm","","
InterPro
IPR000713
Domain
Cytoplasmic peptidoglycan synthetase, N-terminal
PF01225\"[20-119]TMur_ligase
InterPro
IPR004101
Domain
Cytoplasmic peptidoglycan synthetases, C-terminal
PF02875\"[323-414]TMur_ligase_C
InterPro
IPR005758
Family
UDP-N-acetylmuramate--alanine ligase
TIGR01082\"[20-470]TmurC: UDP-N-acetylmuramate--alanine ligase
InterPro
IPR012237
Family
UDP-N-acetylmuramate-alanine ligase
PIRSF001562\"[19-470]TUDP-N-acetylmuramate-alanine ligase
InterPro
IPR013221
Domain
Mur ligase, middle region
PF08245\"[121-303]TMur_ligase_M
noIPR
unintegrated
unintegrated
G3DSA:3.40.1190.10\"[107-322]Tno description
G3DSA:3.40.50.720\"[7-106]Tno description
G3DSA:3.90.190.20\"[324-475]Tno description
PTHR23135\"[123-471]TMUR LIGASE FAMILY MEMBER
PTHR23135:SF5\"[123-471]TUDP-N-ACETYLMURAMATE--L-ALANINE LIGASE
tmhmm\"[21-39]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 2.2e-05) to 2/5 blocks of the IPB001645 family, which is described as \"Folylpolyglutamate synthetase\". Interpro entry for IP:IPR001645. IPB001645A 120-144 0.00011 IPB001645D 427-460 97","Residues 429 to 473 match (1e-12) PD:PD386547 which is described as LIGASE CELL COMPLETE UDP-N-ACETYLMURAMATE--ALANINE PROTEOME ACETYLMURAMOYL-L-ALANINE DIVISION SYNTHETASE PEPTIDOGLYCAN ATP-BINDING ","","","","","","","","","","","Tue Jan 14 14:52:21 2003","Wed Dec 18 10:29:03 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00833 is paralogously related to AA02931 (2e-37), AA00838 (3e-12) and AA00840 (1e-07).","","","","","","Residues 323 to 416 (E-value = 8.2e-28) place AA00833 in the Mur_ligase_C family which is described as Mur ligase family, glutamate ligase domain (PF02875)","","","","","El Zoeiby,A., Sanschagrin,F., Lamoureux,J., Darveau,A. and Levesque,R.C. Cloning, over-expression and purification of Pseudomonasaeruginosa murC encoding uridine diphosphateN-acetylmuramate: L-alanine ligase FEMS Microbiol. Lett. 183, 281-288 (2000)PubMed: NOT_FOUND Eveland,S.S., Pompliano,D.L. and Anderson,M.S. Conditionally lethal Escherichia coli murein mutants containpoint defects that map to regions conserved among murein and folyl poly-gamma-glutamate ligases: identification of a ligase superfamily Biochemistry 36 (20), 6223-6229 (1997) PubMed: 9166795 Liger,D., Masson,A., Blanot,D., van Heijenoort,J. andParquet,C. Over-production, purification and properties of the uridine-diphosphate-N-acetylmuramate:L-alanine ligase from Escherichia coli Eur. J. Biochem. 230 (1), 80-87 (1995) PubMed: 7601127 Ikeda,M., Wachi,M., Jung,H.K., Ishino,F. and Matsuhashi,M. Nucleotide sequence involving murG and murC in the mra genecluster region of Escherichia coli Nucleic Acids Res. 18 (13), 4014 (1990) PubMed: 2197603 ","","Wed Jan 15 12:30:42 2003","1","","","" "AA00835","576413","575352","1062","ATGGGTAAAAAATTATTAGTGATGGCAGGCGGAACGGGCGGACATGTTTTTCCTGCCATTGCCGTTGCACAAGAATTACAACAGCAAGGCTGGGAAATCCGCTGGCTGGGCACCAAAGACAGAATGGAAGCTCAATTGGTTCCAAAACACGGCATTCCCATCGAATTTATCCAAATTTCAGGTTTACGCGGCAAAGGCATCAAGAGTTTATTATTGGCGCCTTTTGCCATTTTGCGCGCAGTATGTCAGGCGCGTAATATCATCAAGCAATATCAGCCTAACGCCGTATTAGGCATGGGCGGTTATGTGTCCGGTCCGGGCGGGCTTGCGGCGAAACTCTGCGGCGTGCCGGTGGTGTTGCATGAACAAAATGCCATTGCCGGGTTGACCAACAGTTGGTTGTCAAAAATTGCCACCCGCGTGTTGCAAGCGTTCCCGAATGCGTTTCCTGAGGCGGAAGTAGTGGGCAATCCCGTGCGTCGCGATTTATTCCAAACGGAAGTGCCGCAACAGCGTTTTGCTGCGCGTGATAAAACGTTGCGCATTTTAGTGGTCGGCGGTAGCCAAGGGGCACGCGTGCTGAATCAAACCGTGCCGCAGGTGGCGGCGAAACTTACCGCGCAGGGATTGGATATTTATGTGCGCCATCAGGTCGGCAAAGGCAATTTGGCGGGCATTGAAGACGTTTATCAGGCAAATCACAACGGTGTTGCCACCGAATTTATTGACGACATGGCGGAAGCCTACGCGTGGGCGGACATTGTCATTTGCCGCTCCGGCGCGTTGACCGTATGCGAATTGGCGGCGGTGGGTACACCGGCGATTTTCGTGCCGTTTCAGCATAAAGATCGTCAGCAGTTTTTGAATGCGAAATATTTAGCGGATGCAGGCGCGGCAGTCATTATTGAGCAGCCGGAATTTACCGAAGAACGCTTATTGCACGAATTAACTCCATTATTGGCAGACCGTGAAAAATTATTAGCCATGGCGTTAAATGCAAAAAAAATGGCGACACCAAGAGCGGCAAAACGGGTTGCCGAGGTGATTGAAGACGTCGTGAGC","","","38247","MGKKLLVMAGGTGGHVFPAIAVAQELQQQGWEIRWLGTKDRMEAQLVPKHGIPIEFIQISGLRGKGIKSLLLAPFAILRAVCQARNIIKQYQPNAVLGMGGYVSGPGGLAAKLCGVPVVLHEQNAIAGLTNSWLSKIATRVLQAFPNAFPEAEVVGNPVRRDLFQTEVPQQRFAARDKTLRILVVGGSQGARVLNQTVPQVAAKLTAQGLDIYVRHQVGKGNLAGIEDVYQANHNGVATEFIDDMAEAYAWADIVICRSGALTVCELAAVGTPAIFVPFQHKDRQQFLNAKYLADAGAAVIIEQPEFTEERLLHELTPLLADREKLLAMALNAKKMATPRAAKRVAEVIEDVVS","575354","From GenBank (gi:1171076):This protein is involved in cell wall formation. It catalyzes the transfer of a GLNAC subunit on undecaprenyl-pyrophosphoryl-murnac-pentapeptide (lipid intermediate I) to form undecaprenyl-phophosphoryl-murnac-(pentapetide) GLNAC (lipid intermediate II).","UDP-N-acetylglucosamine-N-acetylmuramyl-(pentapeptide)","Inner membrane, Cytoplasm","","
InterPro
IPR004276
Domain
Glycosyl transferase, family 28
PF03033\"[5-143]TGlyco_transf_28
InterPro
IPR006009
Family
N-acetylglucosaminyltransferase, MurG
TIGR01133\"[1-349]TmurG: undecaprenyldiphospho-muramoylpentape
InterPro
IPR007235
Domain
Glycosyltransferase 28, C-terminal
PF04101\"[181-345]TGlyco_tran_28_C
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2000\"[3-184]T\"[252-335]Tno description
PTHR21015\"[1-293]TGLYCOSYLTRANSFERASE


","No hits to the COGs database.","","Residues 3 to 349 match (3e-129) PD:PD005948 which is described as TRANSFERASE N-ACETYLGLUCOSAMINE PYROPHOSPHORYL-UNDECAPRENOL UNDECAPRENYL-PP-MURNAC-PENTAPEPTIDE-UDPGLCNAC 2.4.1.- UDP-N-ACETYLGLUCOSAMINE--N-ACETYLMURAMYL-PENTAPEPTIDE GLCNAC COMPLETE PROTEOME GLYCOSYLTRANSFERA ","","","","","","","","","","","Tue Jan 14 14:56:40 2003","Wed Dec 18 10:30:27 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00835 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 181 to 345 (E-value = 4.2e-54) place AA00835 in the Glyco_tran_28_C family which is described as Glycosyltransferase family 28 C-terminal domain (PF04101)","","","","","Mengin-Lecreulx D, Ayala J, Bouhss A, van Heijenoort J, Parquet C, Hara H.Contribution of the Pmra promoter to expression of genes in the Escherichia coli mra cluster of cell envelope biosynthesis and cell division genes.J Bacteriol. 1998 Sep;180(17):4406-12.PubMed: NOT_FOUNDGomez,M.J., Fluoret,B., van Heijenoort,J. and Ayala,J.A.Nucleotide sequence of the regulatory region of the gene pbpB ofEscherichia coliNucleic Acids Res. 18 (9), 2813 (1990)PubMed: 2187182Bupp,K. and van Heijenoort,J. The final step of peptidoglycan subunit assembly inEscherichia coli occurs in the cytoplasm J. Bacteriol. 175 (6), 1841-1843 (1993) PubMed: 8449890 Mengin-Lecreulx,D., Texier,L., Rousseau,M. and vanHeijenoort,J. The murG gene of Escherichia coli codes for the UDP-N-acetylglucosamine: N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase involved in the membrane steps of peptidoglycan synthesis J. Bacteriol. 173 (15), 4625-4636 (1991) PubMed: 1649817 Ikeda,M., Wachi,M., Jung,H.K., Ishino,F. and Matsuhashi,M. Nucleotide sequence involving murG and murC in the mra genecluster region of Escherichia coli Nucleic Acids Res. 18 (13), 4014 (1990) PubMed: 2197603 Mengin-Lecreulx,D., Texier,L. and van Heijenoort,J. Nucleotide sequence of the cell-envelope murG gene ofEscherichia coli Nucleic Acids Res. 18 (9), 2810 (1990) PubMed: 2187180 ","","Wed Jan 15 12:27:17 2003","1","","","" "AA00837","577644","576457","1188","ATGGGATTTTGGGATAGGTTCAAAGAAAGCAGTCAAAACGCCACCACAGTGGCGCCGACCAGTTTGCTATACGACCGCGCGTTATTGTGGTTGTATTTGGTGTTGTTGCTCATCGGTTTATTAGCGGTGTCCTCCGCTTCCATTCCGGTGGGGACCCGCTTGTATAATGATGCTTTTTATTTTGTCAAACGCGATATTATTTACATCATTTTGTCCTGTTTCACCTGTTACATCACCTTACAAATTTCCATGGAAAAATGGCAAAAATGGCATGCCAGATTATTTTGGGTTGCGATTATTCTGCTTGTTCTTGTGATGATTCCGGGCATCGGGCGTGAAGTTAACGGCGCACGCCGTTGGATTCCTATGGGGTTATTTAATTTCCAGCCGGCGGAATTCGCCAAATTAGCCTTAACCTGTTTCCTCGCCAGTTATTTCACCCGCCGTTATGACGAAGTGCGTAGTCGCAAACTGAGCGCGTTTAAGCCCTTTGTGGTGATGGGTGTCATGGGTTGTTTTCTGATTGTACAACCTGATTTGGGAAGTACTGTCGTATTATTTATTATCACTTTCGGCTTATTATTTATCGTCGGTGCCAACTTCTGGCAGTTCATCGGTTTAATCAGTATGGGCGTGTTCATGTTCGTGTGGTTGGTGCTTTCTTCCGCTTATCGACTGAAACGTATCATAGGTTTTATGGATCCTTTCAAAGACCCTTATGATACCGGTTTCCAATTATCCAACTCCTTAATGGCGTTCGGGCGCGGCGGCTTTTTCGGCGAGGGGTTAGGCAATTCCATCTTAAAACTGGAATATTTGCCCGAAGCGCATACGGACTTTGTGATGGCGATTGTGGGTGAAGAATTTGGTTTCTTCGGCATTTTCGTTATTATTATTTTGCTTGGGTTGTTGGTTTTTCGTGCCATGAAAATCGGGCGCGAATCCTTAATATTAGAACAGCGCTTTAAAGGTTTTTTAGCGTTTGGTATCAGTTTCTGGATTTTCTTCCAGGGCTTCGTCAACCTCGGTATGGCGCTTGGTATGTTGCCGACCAAAGGCTTAACGTTCCCGCTCATCAGCTATGGCGGTTCCAGTATCATCATTATGTCCGTCACCATCGGTATGTTATTGCGTATTGACCATGAAAATCGCTTAATGCGTGGCGGTCAGGCGCGATTACGGGATGAC","","","44920","MGFWDRFKESSQNATTVAPTSLLYDRALLWLYLVLLLIGLLAVSSASIPVGTRLYNDAFYFVKRDIIYIILSCFTCYITLQISMEKWQKWHARLFWVAIILLVLVMIPGIGREVNGARRWIPMGLFNFQPAEFAKLALTCFLASYFTRRYDEVRSRKLSAFKPFVVMGVMGCFLIVQPDLGSTVVLFIITFGLLFIVGANFWQFIGLISMGVFMFVWLVLSSAYRLKRIIGFMDPFKDPYDTGFQLSNSLMAFGRGGFFGEGLGNSILKLEYLPEAHTDFVMAIVGEEFGFFGIFVIIILLGLLVFRAMKIGRESLILEQRFKGFLAFGISFWIFFQGFVNLGMALGMLPTKGLTFPLISYGGSSIIIMSVTIGMLLRIDHENRLMRGGQARLRDD","576459","","cell division protein W","Inner membrane, Cytoplasm","","
InterPro
IPR001182
Family
Cell cycle protein
PF01098\"[26-385]TFTSW_RODA_SPOVE
PS00428\"[341-365]TFTSW_RODA_SPOVE
InterPro
IPR013437
Family
Cell division protein FtsW
TIGR02614\"[25-383]TftsW: cell division protein FtsW
noIPR
unintegrated
unintegrated
signalp\"[1-46]?signal-peptide
tmhmm\"[27-47]?\"[66-84]?\"[94-112]?\"[126-146]?\"[167-195]?\"[201-221]?\"[242-260]?\"[289-309]?\"[324-344]?\"[358-377]?transmembrane_regions


","BeTs to 17 clades of COG0772COG name: Bacterial cell division membrane proteinFunctional Class: DThe phylogenetic pattern of COG0772 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-56) to 4/4 blocks of the IPB001182 family, which is described as \"Cell cycle proteins\". Interpro entry for IP:IPR001182. IPB001182A 116-133 5e-10 IPB001182B 243-264 2.7e-10 IPB001182C 272-293 7.5e-15 IPB001182D 340-365 4e-17","Residues 81 to 167 match (9e-07) PD:PD487473 which is described as CELL DIVISION PROTEOME COMPLETE FTSW PEPTIDOGLYCAN TRANSMEMBRANE SYNTHESIS WALL SHAPE ","","","","","","","","","","","","Wed Dec 18 10:31:49 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00837 is paralogously related to AA00257 (6e-47).","","","","","","Residues 26 to 385 (E-value = 3.5e-169) place AA00837 in the FTSW_RODA_SPOVE family which is described as Cell cycle protein (PF01098)","","","","","Mercer KL, Weiss DS. The Escherichia coli cell division protein FtsW is required torecruit its cognate transpeptidase, FtsI (PBP3), to thedivision site. J Bacteriol. 2002 Feb;184(4):904-12. PubMed: NOT_FOUND Mengin-Lecreulx D, Ayala J, Bouhss A, van Heijenoort J, Parquet C, Hara H.Contribution of the Pmra promoter to expression of genes in the Escherichia coli mra cluster of cell envelope biosynthesis and cell division genes.J Bacteriol. 1998 Sep;180(17):4406-12.PubMed: NOT_FOUNDHara H, Yasuda S, Horiuchi K, Park JT. A promoter for the first nine genes of the Escherichia coli mracluster of cell division and cell envelope biosynthesis genes,including ftsI and ftsW. J Bacteriol. 1997 Sep;179(18):5802-11. PubMed: NOT_FOUND Boyle DS, Khattar MM, Addinall SG, Lutkenhaus J, Donachie WD. ftsW is an essential cell-division gene in Escherichia coli. Mol Microbiol 1997 Jun;24(6):1263-73. PubMed: 9218774Khattar MM, Addinall SG, Stedul KH, Boyle DS, Lutkenhaus J,Donachie WD. Two polypeptide products of the Escherichia coli cell divisiongene ftsW and a possible role for FtsW in FtsZ function. J Bacteriol. 1997 Feb;179(3):784-93. PubMed: NOT_FOUNDGomez,M.J., Fluoret,B., van Heijenoort,J. and Ayala,J.A.Nucleotide sequence of the regulatory region of the gene pbpB ofEscherichia coliNucleic Acids Res. 18 (9), 2813 (1990)PubMed: 2187182","","Wed Jan 15 12:22:15 2003","1","","","" "AA00838","578963","577662","1302","ATGCAATATCAAGATAAAAAAGTCACGGTAATCGGGTTAGGCAAAACAGGCTTATCCTGTGTGGATTTTCTGCGTGCCAAACAGGCGGATGTGCGTGTCATAGATACGCGTCAACATCCTGCGGGCGCTGAGCAGCTTGATAAAGCGATTCCTCTGCATACGGGCGGTTTAAACCAGCAATGGCTGCTGGAAAGCGATCTGATTGTTATCAGCCCGGGGCTGGCGGTAAAAACACCTGAAATTCAGACCGCACTTCAAGCAGGTGTCGAGGTGGTGGGCGACATCGAATTATTCTGTCGCGAGGCGGATAAACCGATTGTGGCAATTACCGGTTCCAACGGTAAAAGCACTGTCACCACATTGGTGGCGGAAATGGCGAAGGCCGCCGGTTTAAGAGTGGGTATGGGCGGCAATATTGGTATTCCGGCACTTTCCCTGTTAAATCAACAACATGATTTGTATGTGTTGGAACTGTCCAGCTTCCAATTGGAAACCACCTATTCCCTCAAGGCTGTGGCGGCAACAGTATTAAACGTGACCGAAGATCACATGAATCGCTATGTGGATCTGCAGGATTATCGCCACGCGAAATTAAACATTTACAATCATTGCCAAACGGCGGTGATTAATGCGGAAGATGCATTGACGTTGCCAACGACCCAGCGACCGCAAAAGCAGGTTTCTTTTGGTGAAAACCACGCGGATTATTGGTTAAAAACCGAAAATAACAAAACCTATTTAATGGCGTACGATGAAGCGGTGTTAGCCTGTGATGAAATGAAATTGACCGGTCGCCATAATTACATGAATGCCTTGGCTGCCATTGCGTTGGCACAGGCGGCAGGCATAAATTTAACCGGAATTCGAACCGCACTTTGTGCGTTCGGTGGTTTGGAGCACCGCTTCCAAGTGGCGCATATCGCTGACGGCGTGCGCTGGATTAACGATTCCAAAGCCACTAATGTGGGTAGCACCGTTGCCGCCTTAACCGGTTTGCAGGTAGCGGGCAAGCTCCATTTATTGCTCGGCGGTGACGGCAAAGGCGCGGATTTCTCCGAATTGGCACGCTTAATTAATCAACCGCACATTTACTGCTATTGTTTCGGTCGCGACGGCAAACAGTTAGCCGCACTCTCTTCCCAAAGCCAATTATTTGACACCATAGAACACGCCATTGCGGCGATTCGTCCGCAGCTACAGGCAGGCGACATGGTGCTGTTATCACCGGCTTGCGCCAGTTTGGATCAATTCAGCTGTTTTGAAGCTCGCGGTGATGAATTTACGCGTTTGTCACGCTTAAGT","","","47009","MQYQDKKVTVIGLGKTGLSCVDFLRAKQADVRVIDTRQHPAGAEQLDKAIPLHTGGLNQQWLLESDLIVISPGLAVKTPEIQTALQAGVEVVGDIELFCREADKPIVAITGSNGKSTVTTLVAEMAKAAGLRVGMGGNIGIPALSLLNQQHDLYVLELSSFQLETTYSLKAVAATVLNVTEDHMNRYVDLQDYRHAKLNIYNHCQTAVINAEDALTLPTTQRPQKQVSFGENHADYWLKTENNKTYLMAYDEAVLACDEMKLTGRHNYMNALAAIALAQAAGINLTGIRTALCAFGGLEHRFQVAHIADGVRWINDSKATNVGSTVAALTGLQVAGKLHLLLGGDGKGADFSELARLINQPHIYCYCFGRDGKQLAALSSQSQLFDTIEHAIAAIRPQLQAGDMVLLSPACASLDQFSCFEARGDEFTRLSRLS","577664","From GenBank (gi:1171072):This protein is involved in cell wall formation and catalyzes the addition of D-glutamate to the nucleotide precursor UDP-N-acetylmuamoyl-L-alanine (UMA). It belongs to the MURCDEF family.","UDP-N-acetylmuramoylalanine--D-glutamate ligase","Cytoplasm","","
InterPro
IPR004101
Domain
Cytoplasmic peptidoglycan synthetases, C-terminal
PF02875\"[298-378]TMur_ligase_C
InterPro
IPR005762
Family
UDP-N-acetylmuramoylalanine-D-glutamate ligase
TIGR01087\"[7-433]TmurD: UDP-N-acetylmuramoylalanine--D-glutam
InterPro
IPR006162
PTM
Phosphopantetheine attachment site
PS00012\"[111-126]?PHOSPHOPANTETHEINE
InterPro
IPR012237
Family
UDP-N-acetylmuramate-alanine ligase
PIRSF001562\"[6-434]TUDP-N-acetylmuramate-alanine ligase
InterPro
IPR013221
Domain
Mur ligase, middle region
PF08245\"[107-278]TMur_ligase_M
InterPro
IPR013222
Domain
Glycosyl hydrolase family 98, putative carbohydrate-binding module
SM00776\"[232-365]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.40.1190.10\"[93-297]Tno description
G3DSA:3.40.50.720\"[1-92]Tno description
G3DSA:3.90.190.20\"[298-432]Tno description
PTHR23135\"[109-434]TMUR LIGASE FAMILY MEMBER
PTHR23135:SF2\"[109-434]TUDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE


","No hits to the COGs database.","","Residues 97 to 200 match (7e-07) PD:PD551443 which is described as UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE PROTEOME COMPLETE ","","","","","","","","","","","Tue Jan 14 15:20:35 2003","Wed Dec 18 10:33:29 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00838 is paralogously related to AA00833 (3e-12), AA00840 (3e-11), AA02931 (1e-07) and AA00841 (2e-04).","","","","","","Residues 298 to 380 (E-value = 1.6e-13) place AA00838 in the Mur_ligase_C family which is described as Mur ligase family, glutamate ligase domain (PF02875)","","","","","Mengin-Lecreulx D, Ayala J, Bouhss A, van Heijenoort J, Parquet C, Hara H.Contribution of the Pmra promoter to expression of genes in the Escherichia coli mra cluster of cell envelope biosynthesis and cell division genes.J Bacteriol. 1998 Sep;180(17):4406-12.PubMed: NOT_FOUNDBertrand JA, Auger G, Fanchon E, Martin L, Blanot D, vanHeijenoort J, Dideberg O. Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli. EMBO J 1997 Jun;16(12):3416-25. PubMed: 9218784. Gomez,M.J., Fluoret,B., van Heijenoort,J. and Ayala,J.A.Nucleotide sequence of the regulatory region of the gene pbpB ofEscherichia coliNucleic Acids Res. 18 (9), 2813 (1990)PubMed: 2187182","","Wed Jan 15 11:04:03 2003","1","","","" "AA00839","579844","578993","852","ATGATTTTATTTGCCATCGGCGTGAGTACCTTACTTTGGGCGGATTTGCGTAATCCGTACGTTTGGTTCAGTTTATTCGTGTTATTCGGTTATGGCACGGTCGGTTTTGTGGACGATTACCGCAAAATTACCCGCAAAAGTACCGATGGCTTAATTGCCCGCTGGAAATATTTTTGGCTGTCCGTGGTCGCTCTAGTGGCAATTTTCGGTATGTACGCCATGGGTAAAGATACCGATGCTACCCGTTTGGTGGTGCCGTTTTTTAAAGAATTTATGCCACAACTCGGTGTCTTTTATATCGTGCTGTCTTATTTCGTTATCGTCGGCTCCAGTAACGCGGTGAATTTCACCGACGGCTTGGACGGCTTGGCAATTATGCCGACGGTGCTTGTTGCCGGTGCATTTGCCTTGGTGGCATGGGCGACGGGGAACATTAATTTCGCCGAATATTTACACATTCCGTATATTAAATTCAGTGCGGAATTAGTGGTGTTCTGTACCGCCATTGTGGGTGCCGGTTTGGGTTTTCTTTGGTTCAATACTTATCCTGCGCAGGTGTTTATGGGCGATGTAGGCTCATTAGCATTAGGCGGTGCGCTGGGCGTGATTGCCGTGTTAGTGCGTCAGGAATTTTTATTATTAATTATGGGCGGCGTGTTTGTCATGGAAACCCTGTCCGTCATTTTACAAGTGGGCTCCTACAAACTGCGTAATAAACAACGTATTTTCCTGATGGCGCCGATTCATCACCATTTCGAGAAAAAAGGCTGGCCGGAGCCGCGCGTGATTGTGCGTTTCTGGATCATTTCCCTGATGCTCGTGTTAATCGGTTTGGTGACGTTAAAACTGCGT","","","40387","MILFAIGVSTLLWADLRNPYVWFSLFVLFGYGTVGFVDDYRKITRKSTDGLIARWKYFWLSVVALVAIFGMYAMGKDTDATRLVVPFFKEFMPQLGVFYIVLSYFVIVGSSNAVNFTDGLDGLAIMPTVLVAGAFALVAWATGNINFAEYLHIPYIKFSAELVVFCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGVIAVLVRQEFLLLIMGGVFVMETLSVILQVGSYKLRNKQRIFLMAPIHHHFEKKGWPEPRVIVRFWIISLMLVLIGLVTLKLR","578995","From GenBank (gi:1171016):This protein is involved in the first step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan. It is an integral membrane protein and belongs to the glycosyltransferase family 4, MRAY subfamily.","UDP-MurNAc-pentapeptide phosphotransferase","Inner membrane, Cytoplasm","","
InterPro
IPR000715
Family
Glycosyl transferase, family 4
PTHR22926\"[1-284]TPHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE
PF00953\"[21-213]TGlycos_transf_4
InterPro
IPR003524
Family
Phospho-N-acetylmuramoyl-pentapeptide transferase
PTHR22926:SF3\"[1-284]TPHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE
TIGR00445\"[1-284]TmraY: phospho-N-acetylmuramoyl-pentapeptide
PS01348\"[112-123]TMRAY_2
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[136-282]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-32]?signal-peptide
tmhmm\"[20-38]?\"[57-75]?\"[96-116]?\"[122-142]?\"[162-182]?\"[186-206]?\"[211-231]?\"[263-281]?transmembrane_regions


","No hits to the COGs database.","Significant hit (1.2e-133) to 6/7 blocks of the IPB003524 family, which is described as \"Phospho-N-acetylmuramoyl-pentapeptide-transferase\". Interpro entry for IP:IPR003524. IPB003524B -12-19 94 IPB003524C 26-64 5.6e-28 IPB003524D 107-124 3.7e-12 IPB003524E 168-201 2.1e-33 IPB003524F 202-236 9.6e-27 IPB003524G 238-270 1.7e-28","Residues 67 to 205 match (3e-14) PD:PD294997 which is described as RESISTANCE TELLURITE ","","","","","","","","","","","Wed Jan 15 09:16:14 2003","Wed Jan 15 09:17:38 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00839 is paralogously related to AA02423 (1e-04).","","","","","","Residues 21 to 213 (E-value = 3e-70) place AA00839 in the Glycos_transf_4 family which is described as Glycosyl transferase (PF00953)","","","","","Dini C, Didier-Laurent S, Drochon N, Feteanu S, Guillot JC,Monti F, Uridat E, Zhang J, Aszodi J. Synthesis of sub-micromolar inhibitors of MraY by exploringthe region originally occupied by the diazepanone ring in theliposidomycin structure. Bioorg Med Chem Lett. 2002 Apr 22;12(8):1209-13. PMID: 11934590 Azzolina BA, Yuan X, Anderson MS, El-Sherbeini M. The cell wall and cell division gene cluster in the Mraoperon of Pseudomonas aeruginosa: cloning, production, andpurification of active enzymes. Protein Expr Purif. 2001 Apr;21(3):393-400. PMID: 11281713 Branstrom AA, Midha S, Longley CB, Han K, Baizman ER, AxelrodHR Assay for identification of inhibitors for bacterial MraYtranslocase or MurG transferase. Anal Biochem. 2000 May 1;280(2):315-9. PMID: 10790316 Mengin-Lecreulx D, Ayala J, Bouhss A, van Heijenoort J, Parquet C, Hara H.Contribution of the Pmra promoter to expression of genes in the Escherichia coli mra cluster of cell envelope biosynthesis and cell division genes.J Bacteriol. 1998 Sep;180(17):4406-12.PubMed: NOT_FOUNDGomez,M.J., Fluoret,B., van Heijenoort,J. and Ayala,J.A.Nucleotide sequence of the regulatory region of the gene pbpB ofEscherichia coliNucleic Acids Res. 18 (9), 2813 (1990)PubMed: 2187182","","Wed Jan 15 11:02:34 2003","1","","","" "AA00840","581448","580072","1377","ATGATTACATTATCTCTTTCACAAATTGCCGCCATTTTAGGAGCAGAACTCATAGGCGATGGTACGGTTATCGTCGAAAACGTGAGTACGGATAGCCGTCAGGCGGTCAATAAAGGGTTATTTTTTGCCCTTAAAGGCGAAAATTTTGATGCGCACCATTATGTTGCCAAAGCTGCCGAACAAGGTTGTGTGGCGGCGGTGGTTGAACATCCGACAGAAGGCAATATCGCCCGGCTTATCGTTAAAGACAGTCGTCTTGCTTTGGGGCGGCTTGCCAAATGGCTGCGTGAAAAAATTAACCCGAAAGTGGTGGCGATGACGGGATCTTCCGGTAAAACCACGGTAAAAGAGATGGTTGCCTCCATTTTGCAACAAAGTGCGGTGGATTCTGACGACGTTTTATTTACTCAAGGCAATTTTAACAACGACATCGGCGTGCCGCTCACTTTGTTACGTTTAACAGAACAGCATAAATTCGCGGTGATCGAACTCGGCGCCAATCATATCGGCGAAATCGCGTACACGACTTCCTTGGCGCAACCTGATGTGGCGCTGGTCAATAATGTCATGGCGGCGCATTTGGAAGGTTTTGGTTCCCTTGACGGCGTGGCGACGGCAAAAGGCGAAATCTTTCGCGGCTTGACGGAAAACGGCGTTGCCATTATCAATTTGGCACATAATTATCAGCAAAAATGGCAGGCGGACATCGGTCGGCACGCCGTGCAGTATTTTGCTTACGATAACCCGCGGGCGGATTTTTACGCCGAACAAATTCATTTCTCCGAACAAGGCGCCTATTTCTTACTCCACACGCCGCAAGGCCGCGTGCAAATCAATTCACCGTATTTGGGTGAGCATAATATCTCTAATGCGTTGGCGGCAACTGCCTTGGCGATGAACGTGGGTGCCACCACGGCGCAGGTGAAAAAAGGGTTGGAAACGCCCTCTTTGGTGAAAGGGCGTTTGTTCCCGATTCAGCCTTGTGAAAATCTGTTATTGCTGGACGATACTTACAACGCCAATGTGGGATCTATGAAATCGGCGATTTCCGTGTTACAAAAATATCCTGCTTTTCGCGTCTTTGTTGTTGGTGATATGGGCGAATTAGGCGATAATGCGCAACTTTGCCATCAAGAGGTGGGGGAGTTCGCTCATGCCGCCAAGTTAGACTTAGTGCTTTCTTTCGGGTGTTCCAGTGGCGTTATAAGTGCGGTTAATTCGGGACGCCATTTTACCGATAAAACGGAACTTGTAACTTATTTAACACCGATTATTCAACAACAATTAGCACAACAAAAAGTCGTTGTTTTGGTGAAAGGATCACGCAGCATGAAAATGGAAGAAGTGATCGATTTATTAAAAGGTAATTTTTTATGT","","","49607","MITLSLSQIAAILGAELIGDGTVIVENVSTDSRQAVNKGLFFALKGENFDAHHYVAKAAEQGCVAAVVEHPTEGNIARLIVKDSRLALGRLAKWLREKINPKVVAMTGSSGKTTVKEMVASILQQSAVDSDDVLFTQGNFNNDIGVPLTLLRLTEQHKFAVIELGANHIGEIAYTTSLAQPDVALVNNVMAAHLEGFGSLDGVATAKGEIFRGLTENGVAIINLAHNYQQKWQADIGRHAVQYFAYDNPRADFYAEQIHFSEQGAYFLLHTPQGRVQINSPYLGEHNISNALAATALAMNVGATTAQVKKGLETPSLVKGRLFPIQPCENLLLLDDTYNANVGSMKSAISVLQKYPAFRVFVVGDMGELGDNAQLCHQEVGEFAHAAKLDLVLSFGCSSGVISAVNSGRHFTDKTELVTYLTPIIQQQLAQQKVVVLVKGSRSMKMEEVIDLLKGNFLC","580074","From GenBank (gi:1171074):This protein is involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein. It is a cytoplasmic monomer and belongs to the MURCDEF family.","UDP-MurNAc-pentapeptide synthetase","Cytoplasm","","
InterPro
IPR000713
Domain
Cytoplasmic peptidoglycan synthetase, N-terminal
PF01225\"[24-96]TMur_ligase
InterPro
IPR004101
Domain
Cytoplasmic peptidoglycan synthetases, C-terminal
PF02875\"[318-401]TMur_ligase_C
InterPro
IPR005863
Family
UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanyl ligase
PTHR23135:SF3\"[106-459]TUDP-N-ACETYLMURAMOYLALANYL-D-GLUTAMYL-2,6-DIAMINOPIMELATE--D-ALANYL-D- ALANYL LIGASE
TIGR01143\"[30-453]TmurF: UDP-N-acetylmuramoyl-tripeptide--D-al
InterPro
IPR012237
Family
UDP-N-acetylmuramate-alanine ligase
PIRSF001562\"[8-458]TUDP-N-acetylmuramate-alanine ligase
InterPro
IPR013221
Domain
Mur ligase, middle region
PF08245\"[104-298]TMur_ligase_M
noIPR
unintegrated
unintegrated
G3DSA:3.40.1190.10\"[82-316]Tno description
G3DSA:3.40.1390.10\"[1-81]Tno description
G3DSA:3.90.190.20\"[317-459]Tno description
PTHR23135\"[106-459]TMUR LIGASE FAMILY MEMBER
signalp\"[1-15]?signal-peptide


","BeTs to 17 clades of COG0770COG name: UDP-N-acetylmuramyl pentapeptide synthaseFunctional Class: MThe phylogenetic pattern of COG0770 is --m----qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","","Residues 8 to 82 match (1e-14) PD:PD006359 which is described as LIGASE SYNTHETASE PROTEOME COMPLETE ENZYME CELL PEPTIDOGLYCAN SYNTHESIS UDP-N-ACETYLMURAMYL-TRIPEPTIDE DIAMINOPIMELATE-ADDING ","","","","","","","","","","","Wed Jan 15 09:21:45 2003","Wed Dec 18 10:36:59 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00840 is paralogously related to AA00841 (4e-14), AA00838 (4e-11), AA00833 (1e-07) and AA02931 (2e-07).","","","","","","Residues 318 to 404 (E-value = 8.3e-16) place AA00840 in the Mur_ligase_C family which is described as Mur ligase family, glutamate ligase domain (PF02875)","","","","","Dementin S, Bouhss A, Auger G, Parquet C, Mengin-Lecreulx D,Dideberg O, van Heijenoort J, Blanot D. Evidence of a functional requirement for a carbamoylatedlysine residue in MurD, MurE and MurF synthetases asestablished by chemical rescue experiments. Eur J Biochem. 2001 Nov;268(22):5800-7. PMID: 11722566 Mengin-Lecreulx D, Ayala J, Bouhss A, van Heijenoort J, Parquet C, Hara H.Contribution of the Pmra promoter to expression of genes in the Escherichia coli mra cluster of cell envelope biosynthesis and cell division genes.J Bacteriol. 1998 Sep;180(17):4406-12.PubMed: NOT_FOUNDGomez,M.J., Fluoret,B., van Heijenoort,J. and Ayala,J.A.Nucleotide sequence of the regulatory region of the gene pbpB ofEscherichia coliNucleic Acids Res. 18 (9), 2813 (1990)PubMed: 2187182Parquet C, Flouret B, Mengin-Lecreulx D, van Heijenoort J. Nucleotide sequence of the murF gene encoding theUDP-MurNAc-pentapeptide synthetase of Escherichia coli. Nucleic Acids Res 1989 Jul 11;17(13):5379. PubMed: 2668880. ","","Wed Jan 15 11:01:54 2003","1","","","" "AA00841","582921","581458","1464","ATGCACCGATTAACCGCACTTTTAGGGATTGATATTGCCGGAGACATCAACCTTACCGAAATGACATTAGACAGCCGTACTGCAAAGGCCGGCTGTCTTTTTATTGCCATTAAAGGGCACCAAACCGACGGTCGCCAATACATTCCGCAAGCCTTACGCAACGGCGCAAGTGCGGTCATTTTTGAAGCCGATTCTGCACAGCAACATCTTCAGGTTCATTACGAACAGGGGATTCCTCTCATTGCCTTTTATCGGCTAAGCGAAAATTTATCCCGTCTCGCCGATGTGTTTTATCAATATCCCTCCAAACACTTAACTTTGGTGGGCGTGACAGGTACCAACGGCAAAACTACAACTGCCCAATTATTGGCACAATGGACGCAACTGTTAGGACACACCGGTGCTGTGATGGGCACCATCGGTAACGGTTTATTCGGTCAGGTAAAAGAAGCCGCTAATACCACCGGTTCCGCCGTCGAGATTCAATCTTCGCTGGCGGATTTCGTCGCAAAAGGGGCAGACTTTGCGGCGATTGAAGTGTCTTCCCATGGTTTGGTACAGCATCGGGTAGAATCCGTGCATTTCAGCGCGGCGGTGTTTACCAATTTAAGCCGCGATCATTTGGATTACCATCACACCATGGAAAATTACGCAGCGGCAAAAAAACGCCTGTTTACCGAGCTGGATAGTCGTTATCAGATTATTGACGCGGATGATCCCGTCGGTGCGGTGTGGTTGGCGGAAATGCCTCATGCTGTGGCGGTCAGCGCTAAGGCGGATTTTCTCCCGCAACAAGCCAACTGGCTGAAAGCTGTCGATGTGCGTTTTAATCACAAAGGTGCAACGATTCAGTTTGAATCCTCCTGGGGCAACGGCGAATTACAAAGCCCGCTTATCGGTGCGTTTAACGTGAGCAATTTATTGTTGGTGACCGCAACCTTGCTAACGCTTGATTATCCCTTATCCGGCCTCATTAACAGCGTACATAAATTAACCGGCGTATGCGGTCGTATGGAAATGCTACACACACCACAGAAACCGACGGTGATTGTGGATTATGCACATACACCCGACGCATTGGAAAAAGCCTTACAGGCGGCACGACTACATTGCCGTGGTAAACTTTGGTGCATTTTTGGCTGTGGCGGCGATCGTGACAGCGGTAAACGCCCACTAATGGCAAAAATTGCCGAGCAGTTGGCGGATCATGTTATTGCCACCGACGACAATCCACGCACGGAAGAACCGAAGAAAATCATGGCGGATATTTTAAACGGTTTTGTTCATCCGCAAAGCGTGCAAGTTATTCATCAGCGTGCACAAGCCATTGCTACCGCGATTAAAAGTGCGGTGGAAAATGACGTTATTTTAATTGCCGGTAAAGGGCACGAAGACTATCAAATTATCGGCAAAACCAAATATCATTTTTCCGATCAGGAAGTGGTTCGTAACTATTTATCTCAA","","","53318","MHRLTALLGIDIAGDINLTEMTLDSRTAKAGCLFIAIKGHQTDGRQYIPQALRNGASAVIFEADSAQQHLQVHYEQGIPLIAFYRLSENLSRLADVFYQYPSKHLTLVGVTGTNGKTTTAQLLAQWTQLLGHTGAVMGTIGNGLFGQVKEAANTTGSAVEIQSSLADFVAKGADFAAIEVSSHGLVQHRVESVHFSAAVFTNLSRDHLDYHHTMENYAAAKKRLFTELDSRYQIIDADDPVGAVWLAEMPHAVAVSAKADFLPQQANWLKAVDVRFNHKGATIQFESSWGNGELQSPLIGAFNVSNLLLVTATLLTLDYPLSGLINSVHKLTGVCGRMEMLHTPQKPTVIVDYAHTPDALEKALQAARLHCRGKLWCIFGCGGDRDSGKRPLMAKIAEQLADHVIATDDNPRTEEPKKIMADILNGFVHPQSVQVIHQRAQAIATAIKSAVENDVILIAGKGHEDYQIIGKTKYHFSDQEVVRNYLSQ","581460","","UDP-MurNAc-tripeptide synthetase","Cytoplasm","","
InterPro
IPR000713
Domain
Cytoplasmic peptidoglycan synthetase, N-terminal
PF01225\"[17-98]TMur_ligase
InterPro
IPR000719
Domain
Protein kinase
PS00107\"[140-171]?PROTEIN_KINASE_ATP
InterPro
IPR004101
Domain
Cytoplasmic peptidoglycan synthetases, C-terminal
PF02875\"[334-420]TMur_ligase_C
InterPro
IPR005761
Family
UDP-N-acetylmuramyl-tripeptide synthetase
TIGR01085\"[15-487]TmurE: UDP-N-acetylmuramyl-tripeptide synthe
InterPro
IPR012237
Family
UDP-N-acetylmuramate-alanine ligase
PIRSF001562\"[1-488]TUDP-N-acetylmuramate-alanine ligase
InterPro
IPR013221
Domain
Mur ligase, middle region
PF08245\"[108-314]TMur_ligase_M
noIPR
unintegrated
unintegrated
G3DSA:3.40.1190.10\"[101-337]Tno description
G3DSA:3.40.1390.10\"[1-100]Tno description
G3DSA:3.90.190.20\"[339-486]Tno description
PTHR23135\"[110-128]T\"[149-486]TMUR LIGASE FAMILY MEMBER
PTHR23135:SF4\"[110-128]T\"[149-486]TUDP-N-ACETYLMURAMOYLALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE


","No hits to the COGs database.","","Residues 336 to 460 match (2e-19) PD:PD122331 which is described as COMPLETE PROTEOME SYNTHASE SYNTHETASE FOLYLPOLYGLUTAMATE LIGASE DIHYDROFOLATE ONE-CARBON FOLYLPOLY-GAMMA-GLUTAMATE METABOLISM ","","","","","","","","","","","","Wed Jan 15 13:06:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00841 is paralogously related to AA00840 (5e-14), AA00838 (2e-04) and AA02056 (0.001).","","","","","","Residues 334 to 422 (E-value = 2.3e-37) place AA00841 in the Mur_ligase_C family which is described as Mur ligase family, glutamate ligase domain (PF02875)","","","","","Dementin S, Bouhss A, Auger G, Parquet C, Mengin-Lecreulx D,Dideberg O, van Heijenoort J, Blanot D. Evidence of a functional requirement for a carbamoylatedlysine residue in MurD, MurE and MurF synthetases asestablished by chemical rescue experiments. Eur J Biochem. 2001 Nov;268(22):5800-7. PMID: 11722566 Wijayarathna CD, Wachi M, Nagai K. Isolation of ftsI and murE genes involved in peptidoglycansynthesis from Corynebacterium glutamicum. Appl Microbiol Biotechnol. 2001 May;55(4):466-70. PMID: 11398928 Mengin-Lecreulx D, Ayala J, Bouhss A, van Heijenoort J, Parquet C, Hara H.Contribution of the Pmra promoter to expression of genes in the Escherichia coli mra cluster of cell envelope biosynthesis and cell division genes.J Bacteriol. 1998 Sep;180(17):4406-12.PubMed: NOT_FOUNDGomez,M.J., Fluoret,B., van Heijenoort,J. and Ayala,J.A.Nucleotide sequence of the regulatory region of the gene pbpB ofEscherichia coliNucleic Acids Res. 18 (9), 2813 (1990)PubMed: 2187182Tao JS, Ishiguro EE. Nucleotide sequence of the murE gene of Escherichia coli. Can J Microbiol 1989 Nov;35(11):1051-4. PubMed: 2692800. ","","Wed Jan 15 11:00:48 2003","1","","","" "AA00844","584603","582942","1662","GTGGGGTTAACCGCACTTATCGCTCAAGCGGCTTACATTCAAATTGTGAATGCCGATCCGTTGGTTAACGAGGCGGATAAGCGCTCCTTGCGCAAACAGGAAGTACAGTTCGTACGCGGTTCGATTTTAGATCGTAATGGTCAGTTGCTTTCCGTTAGCGTGCCGATGTATTCCGTGGTTGCCGATCCAAAATTCATTTTTGATGAAAACTCGCTGAAGGATAAAGAACGTTGGCAAAAACTGGCGGAAGCCTTGGGTATTTCATACAGCAATTTACTTAAACGGGTGGAAAAAGATCCGAAATCCCGCTTCGTGTATTTATCCCGTCAGATTTCCCCGACACTGGCAAGCTATGTTAAAGATTTAAAAATTACCGGCATTGTGTTGAAATCAGAGTCTCGCCGTTTTTATCCTCGTGTGGAAGAAACCGCACATTTAATTGGTTATACCAACATTGATGGGGCGGGTATTGAAGGTATCGAGAAAAGTTTTGATTCCATGTTGATCGGCAAGTCCGGTTTGCGTACTTATCGTAAAGATAAACTTGGCAACATCGTGGAAAATATTGCGGATGTGAAGAAATATGATGCGCAAGACGTGACCTTAAGTATCGACGAAAAATTACAATCCATGGTGTACCGTGAAATTAAGAAAGCGGTGGCGGAAAATAAAGCGGAATCAGGCACCGCCGTGTTGGTGGATGTACGGACCGGTGAGGTGCTGGCGATGGCGAATGCGCCGTCTTATAACCCGAATAACCGTACCGGTCTGAAATCCGAATTGACGCGAAATCGTGCGATTACCGATACCTTTGAACCGGGTTCCACTGTAAAACCGTTCGTTGTTTTGACCGCACTTCAACGTGGTGCAGTGCGTCGTGACGAAGTGATTAATACCGGTCCGTTAGTCTTAAACGGTCATGCAGTCAAAGACGTGGCACCTCGTGATAAATTAACTTTAGACGGTATTTTGGAAAACTCCAGTAACCGTGGTGTGAGCCGTTTGGCGTTGCGTATGCCGCCGAATGCGTTGATGGAAACCTATCAAAATGCGGGATTAGGTAAAGCAACGGATTTAGGTTTAATCGGTGAGCAATCCGGTTTATTGAATGCACATCGTGCCCGTTGGTCGGATATTGAGCGCGCCAATGTGGCTTATGGTTACGGAATCAATGCTACGCCTTTACAAATTGCACGTGCTTATATGACGTTAGGCAGTTTTGGGATTTATCGCCCGTTATCCATTACTAAAGTAGATCCGCCGGTAGTGGGGAATCGTGTGTTCTCTGAAAAAATCACCCGTGAAGTGGTTAACATGATGGAAAAAGTGGCGATTAAAAACGGTCGTGCCATGGTGGATGGTTATCGTGTCGGTGTGAAAACCGGTACGGCGAAAAAATTGGAAAACGGTCGTTATGTAGATAAATATGTGGCGTACACCGCAGGTATCGCACCGATTTCCGACCCACGTTATGCTTTGGTGGTTCTGATTAACGATCCGAAAGCAGGTCAATACTACGGTGGTGCAGTATCTGCACCGTTGTTCTCCAGCATTATGGGTTACGCATTACGCGCCAACAATATTGCGCCGGATGGTTTGGGGCAGGAAAAAACGGTAAAACGCACTGTGCGTTTGAGTGATAAAAAAGCGAGTGGCGTAAAC","","","67076","VGLTALIAQAAYIQIVNADPLVNEADKRSLRKQEVQFVRGSILDRNGQLLSVSVPMYSVVADPKFIFDENSLKDKERWQKLAEALGISYSNLLKRVEKDPKSRFVYLSRQISPTLASYVKDLKITGIVLKSESRRFYPRVEETAHLIGYTNIDGAGIEGIEKSFDSMLIGKSGLRTYRKDKLGNIVENIADVKKYDAQDVTLSIDEKLQSMVYREIKKAVAENKAESGTAVLVDVRTGEVLAMANAPSYNPNNRTGLKSELTRNRAITDTFEPGSTVKPFVVLTALQRGAVRRDEVINTGPLVLNGHAVKDVAPRDKLTLDGILENSSNRGVSRLALRMPPNALMETYQNAGLGKATDLGLIGEQSGLLNAHRARWSDIERANVAYGYGINATPLQIARAYMTLGSFGIYRPLSITKVDPPVVGNRVFSEKITREVVNMMEKVAIKNGRAMVDGYRVGVKTGTAKKLENGRYVDKYVAYTAGIAPISDPRYALVVLINDPKAGQYYGGAVSAPLFSSIMGYALRANNIAPDGLGQEKTVKRTVRLSDKKASGVN","582944","From GenBank (gi:129668):This protein is involved in cell wall formation. It is essential for the formation of a septum of the murein sacculus, and it synthesizes cross-linked peptidoglycan from the lipid intermediates. It is part of the final stages in the peptidoglycan sythesis pathway. Its subcelluar location is the inner membrane. The bulk of the moledcule, except for the N-termianl membrane anchor region, protrudes into the periplasmic space, where it acts on murein. It has an N-terminal penicillin insensitive transglycosylase domain (formation of linear glycan strands) and a corboxy-terminal penicillin-sensitive transpeptidase domain (cross-linking of the peptide subunits). ","cell division protein I; penicillin binding protein 2X","Inner membrane, Outer membrane, Periplasm, Cytoplasm","","
InterPro
IPR001460
Domain
Penicillin-binding protein, transpeptidase
PF00905\"[228-520]TTranspeptidase
InterPro
IPR005311
Domain
Penicillin-binding protein, dimerisation domain
PF03717\"[34-190]TPBP_dimer
noIPR
unintegrated
unintegrated
G3DSA:3.40.710.10\"[207-519]Tno description
signalp\"[1-18]?signal-peptide


","No hits to the COGs database.","Significant hit ( 2.2e-10) to 3/3 blocks of the IPB001460 family, which is described as \"Penicillin binding protein transpeptidase domain\". Interpro entry for IP:IPR001460. IPB001460A 39-47 0.0063 IPB001460B 202-210 19 IPB001460C 393-408 0.00037","Residues 6 to 201 match (4e-07) PD:PD281682 which is described as PROTEOME COMPLETE BINDING PENICILLIN ","","","","","","","","","","","Wed Jan 15 10:40:04 2003","Tue Jan 28 14:20:04 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00844 is paralogously related to AA00258 (2e-20) and AA02432 (0.001).","","","","","","Residues 228 to 520 (E-value = 1.4e-105) place AA00844 in the Transpeptidase family which is described as Penicillin binding protein transpeptidase domain (PF00905)","","","","","Laible G, Hakenbeck R, Sicard MA, Joris B, Ghuysen JM. Nucleotide sequences of the pbpX genes encoding thepenicillin-binding proteins 2x from Streptococcus pneumoniae R6and a cefotaxime-resistant mutant, C506. Mol Microbiol 1989 Oct;3(10):1337-48. PubMed: 2615650 Chen JC, Beckwith J. FtsQ, FtsL and FtsI require FtsK, but not FtsN, forco-localization with FtsZ during Escherichia coli cell division.Mol Microbiol. 2001 Oct;42(2):395-413. PubMed: NOT_FOUND Wijayarathna CD, Wachi M, Nagai K. Isolation of ftsI and murE genes involved in peptidoglycansynthesis from Corynebacterium glutamicum. Appl Microbiol Biotechnol. 2001 May;55(4):466-70. PubMed: NOT_FOUND Ubukata K, Shibasaki Y, Yamamoto K, Chiba N, Hasegawa K,Takeuchi Y, Sunakawa K, Inoue M, Konno M. Association of amino acid substitutions in penicillin-bindingprotein 3 with beta-lactam resistance in beta-lactamase-negativeampicillin-resistant Haemophilus influenzae. Antimicrob Agents Chemother. 2001 Jun;45(6):1693-9. PubMed: NOT_FOUNDMengin-Lecreulx D, Ayala J, Bouhss A, van Heijenoort J, Parquet C, Hara H.Contribution of the Pmra promoter to expression of genes in the Escherichia coli mra cluster of cell envelope biosynthesis and cell division genes.J Bacteriol. 1998 Sep;180(17):4406-12.PubMed: NOT_FOUNDGomez,M.J., Fluoret,B., van Heijenoort,J. and Ayala,J.A.Nucleotide sequence of the regulatory region of the gene pbpB ofEscherichia coliNucleic Acids Res. 18 (9), 2813 (1990)PubMed: 2187182","","Wed Jan 15 10:59:34 2003","1","","","" "AA00845","584671","584790","120","TTGTTCGGTTTTACCGCAGAACCGCTTTTAGAAGAAGTTTTTGTCGTTTTCTTTGGTTTTAAAGGTTTTACCGATTTATTAAATTTCACCATTTTCATCACCTTCAGCTTTACTCAAGAA","","","4642","LFGFTAEPLLEEVFVVFFGFKGFTDLLNFTIFITFSFTQE","584790","","hypothetical protein","Cytoplasm, Periplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 14:46:21 2004","Mon Feb 23 14:46:21 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00845 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 14:46:21 2004","","","","","","","","","","","","","1","","","" "AA00846","585097","584783","315","ATGTTGGAAAATAACGATAGATACCCGTTACAAGACATTATTATGGAAGACTTATTTACGTCAAATAAGTTTGTCTTTATCTTGTTATTTTTGATTGTCATTACTGCGCTCGGCACAGTGTGGATTACCCATAAAACGCGGAGTCTGGTGGCGGAAAAAGGCGATTTGGTTCTTCAGCACCAAGCATTAGAAAACGAATTTTTAAATTTAAAATTGGAAGAGGCGACACAAAGCGATAACACTCGAATTGAAGCAATTGCCAAACAATTAGGCATGCAGCGTGCAACCCCCGAACAAGAAGTTGTTATTCTTGAG","","","12053","MLENNDRYPLQDIIMEDLFTSNKFVFILLFLIVITALGTVWITHKTRSLVAEKGDLVLQHQALENEFLNLKLEEATQSDNTRIEAIAKQLGMQRATPEQEVVILE","584785","From GenBank (gi:1169758):This protein is involved in cell division and cell growth. It may play some role in coupling cell division and peptidoglycan physiology. It is a type II membrane protein, and its subcellular location is the inner membrane. It belongs to the FTSL family.","cell division protein L","Inner membrane, Cytoplasm","","
InterPro
IPR007082
Family
Cell division protein FtsL
PF04999\"[10-105]TFtsL
InterPro
IPR011922
Family
Cell division protein, FtsL -like
TIGR02209\"[21-104]TftsL_broad: cell division protein FtsL
noIPR
unintegrated
unintegrated
signalp\"[1-38]?signal-peptide
tmhmm\"[24-44]?transmembrane_regions


","BeTs to 4 clades of COG3116COG name: Cell division proteinFunctional Class: DThe phylogenetic pattern of COG3116 is --------------efghs-------Number of proteins in this genome belonging to this COG is","","Residues 28 to 103 match (2e-18) PD:PD405666 which is described as DIVISION CELL PROTEOME COMPLETE FTSL TRANSMEMBRANE MEMBRANE INNER PROTEIN AT ","","","","","","","","","","","Wed Jan 15 10:43:41 2003","Wed Dec 18 10:41:08 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00846 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 10 to 105 (E-value = 6.2e-51) place AA00846 in the FtsL family which is described as Cell division protein FtsL (PF04999)","","","","","Ghigo JM, Beckwith J. Cell division in Escherichia coli: role of FtsL domains inseptal localization, function, and oligmerzation. J Bacteriol 2000 Jan;182(1):116-29. PubMed: 10613870. Hale CA, de Boer PA. ZipA is required for recruitment of FtsK, FtsQ, FtsL, and FtsNto the septal ring in Escherichia coli. J Bacteriol. 2002 May;184(9):2552-6. PubMed: NOT_FOUND Sievers J, Errington J. Analysis of the essential cell division gene ftsL of Bacillussubtilis by mutagenesis and heterologous complementation. J Bacteriol. 2000 Oct;182(19):5572-9. PubMed: NOT_FOUND Mengin-Lecreulx D, Ayala J, Bouhss A, van Heijenoort J, Parquet C, Hara H.Contribution of the Pmra promoter to expression of genes in the Escherichia coli mra cluster of cell envelope biosynthesis and cell division genes.J Bacteriol. 1998 Sep;180(17):4406-12.PubMed: NOT_FOUNDGomez,M.J., Fluoret,B., van Heijenoort,J. and Ayala,J.A.Nucleotide sequence of the regulatory region of the gene pbpB ofEscherichia coliNucleic Acids Res. 18 (9), 2813 (1990)PubMed: 2187182","","Wed Jan 15 10:57:37 2003","1","","","" "AA00847","586065","585100","966","ATGACGCATTTAAATACCTTTTCTTCAACTGAGCATTTGACGGTTTTATTACATGAAACTGTGGACGGCTTGGCGTTGAAAGAAAACGGCATTTATATTGATGGTACGTTTGGGCGTGGTGGACACTCCCGTTTAATCCTTTCCCAATTATCGGTGAACGGCAAGTTGATTGCCATCGATCGCGATCCGCAGGCGGTAGCTGAAGCACAAAAAATTCAAGATCCGCGTTTTCATATTGAACACAATACTTTCTCGGAAATCCTGCCGATTTGTGAAAAATTCGGTTTAGTCGGCAAGGTTGATGGCATTTTGCTTGATCTTGGCGTGTCTTCGCCGCAATTGGACGATGCAGAACGCGGTTTCAGTTTTATGAAAGATGGTCCGTTAGATATGCGGATGGACAGTTCAAAAGGCATATCTGCTGCCGAATGGCTTGCACAGGTTTCCGAGCAGGATTTGGCATGGGTGTTAAAAACCTTCGGTGAGGAACGTTTTGCCAAGCGCATCGCCAAAGTCATCGTCGACTACAACAAAAGTGCGGTGCAAAATGGCGGTGAATTTTTAGCGCGCACTTTGCAACTCGCAGAACTCATTACACAGGCAGTGCCGTTTAAAGATAAATACAAACATCCGGCAACCCGCAGCTTTCAGGCAATTCGGATTTATATTAATGCCGAGTTGGATGAATTGGAAAATGTATTGCAGTCCGCATTAAGCGTGTTAGCCCCTAAGGGGCGTTTATCCGTGATCAGTTTCCATTCGCTGGAAGATCGTATGGTCAAGCAATTTATGCGCAAACAAAGCCAAGGCGAAGTCATTCCGAAAGGGCTTCCGTTACGCGAAGATCAAATTCAGCGCAATCGGAGGTTAAAAGTGATCGGTAAAGCGATTATGCCGAGTGAAGCCGAGATTGTACAAAACCCAAGAGCCAGAAGTGCCGTGTTGCGCATTGCGGAGAGAATAAAC","","","36009","MTHLNTFSSTEHLTVLLHETVDGLALKENGIYIDGTFGRGGHSRLILSQLSVNGKLIAIDRDPQAVAEAQKIQDPRFHIEHNTFSEILPICEKFGLVGKVDGILLDLGVSSPQLDDAERGFSFMKDGPLDMRMDSSKGISAAEWLAQVSEQDLAWVLKTFGEERFAKRIAKVIVDYNKSAVQNGGEFLARTLQLAELITQAVPFKDKYKHPATRSFQAIRIYINAELDELENVLQSALSVLAPKGRLSVISFHSLEDRMVKQFMRKQSQGEVIPKGLPLREDQIQRNRRLKVIGKAIMPSEAEIVQNPRARSAVLRIAERIN","585102","","S-adenosyl-dependent methyltransferase","Cytoplasm","","
InterPro
IPR002903
Family
Bacterial methyltransferase
PD004685\"[249-320]TMRAW_LEPIC_P62472;
PTHR11265\"[27-321]TS-ADENOSYL-METHYLTRANSFERASE MRAW
PF01795\"[9-321]TMethyltransf_5
TIGR00006\"[6-321]TTIGR00006: S-adenosyl-methyltransferase Mra
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[3-320]Tno description
PIRSF004486\"[11-322]TS-adenosyl-methyltransferase, MraW type


","BeTs to 18 clades of COG0275COG name: Predicted S-adenosylmethionine-dependent methyltransferase involved in cell envelope biogenesisFunctional Class: MThe phylogenetic pattern of COG0275 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit (5.3e-101) to 6/6 blocks of the IPB002903 family, which is described as \"Methyltransferase family\". Interpro entry for IP:IPR002903. IPB002903A 32-47 1.9e-10 IPB002903B 99-133 1.4e-32 IPB002903C 156-170 2e-07 IPB002903D 210-227 4.6e-13 IPB002903E 245-261 5.8e-13 IPB002903F 291-320 8.7e-18","Residues 12 to 119 match (2e-08) PD:PD074425 which is described as COMPLETE PROTEOME TRANSFERASE METHYLTRANSFERASE PHOSPHOPANTETHEINE PLASMID SMTA SYNTHASE BIOSYNTHETIC YJHP ","","","","","Wed Feb 19 08:34:45 2003","","","","","","","Wed Dec 18 10:44:35 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00847 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 9 to 321 (E-value = 3.5e-176) place AA00847 in the Methyltransf_5 family which is described as MraW methylase family (PF01795)","","","","","Carrion M, Gomez MJ, Merchante-Schubert R, Dongarra S, Ayala JA.mraW, an essential gene at the dcw cluster of Escherichia coli codes for a cytoplasmic protein with methyltransferase activity.Biochimie. 1999 Aug-Sep;81(8-9):879-88.PMID: 10572301 Mengin-Lecreulx D, Ayala J, Bouhss A, van Heijenoort J, Parquet C, Hara H.Contribution of the Pmra promoter to expression of genes in the Escherichia coli mra cluster of cell envelope biosynthesis and cell division genes.J Bacteriol. 1998 Sep;180(17):4406-12.PMID: 9721276Gomez,M.J., Fluoret,B., van Heijenoort,J. and Ayala,J.A.Nucleotide sequence of the regulatory region of the gene pbpB ofEscherichia coliNucleic Acids Res. 18 (9), 2813 (1990)PubMed: 2187182 Martin JL, McMillan FM.SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold.Curr Opin Struct Biol. 2002 Dec;12(6):783-93.PMID: 12504684 ","","Wed Feb 19 08:34:45 2003","1","","","" "AA00849","586846","586178","669","ATGAAAATTGGCAGGGTGTTTTTTTATATCTGTGATTTCGGCTTAAAAAGATCCTGGCTTAAAAAACTTTACGTAGAAGATCCTGAAACAGCTTGCAACTTGAGCAAACAAATAATAAACTTAGCGAAAAGTGGTGGAAAGTGGTTTTTTGTGGAGAATTTTGGAAATAAATCCCAAATTCTGACCATACAAATGGAAAAAAGGAATAAATTCATGTTTCGTGGAGCTTCGGCGGTTAATTTAGATGCGAAGGGTAGAATTTCTATCCCGACCCGCCATCGCGCCGAACTTTTGGAACAAAATCAAGGGCAAATGGTTTGCACCGTGGATATTCGTCAACCTTGTTTATTGCTTTATCCGTTGCAGGAATGGGAAGTTATTGAACAAAAGCTACTCGAACTTTCCAACTTTGATCCTGTACAACGCAGTTTGCAACGGGTGATGTTGGGTTATGCCACCGAGTGTGAGTTGGATAGTGCAGGGCGGATTTTAATTAGCGGTCCACTGCGCCAACACGCCAAATTAGAAAAATCCATTATGCTGGTCGGGCAATTAAATAAATTTGAAATCTGGAGTGATGCGGAATGGAAAGCCCAGGTGGAACAAGACATGGCATTAGGTGCAACGGATACTTTTGCATTATCGGAAAAATTAAAAACGCTGTCATTA","","","25579","MKIGRVFFYICDFGLKRSWLKKLYVEDPETACNLSKQIINLAKSGGKWFFVENFGNKSQILTIQMEKRNKFMFRGASAVNLDAKGRISIPTRHRAELLEQNQGQMVCTVDIRQPCLLLYPLQEWEVIEQKLLELSNFDPVQRSLQRVMLGYATECELDSAGRILISGPLRQHAKLEKSIMLVGQLNKFEIWSDAEWKAQVEQDMALGATDTFALSEKLKTLSL","586180","","MraZ cell division protein","Cytoplasm","","
InterPro
IPR003444
Family
MraZ
PD006745\"[87-205]TMRAZ_PASMU_Q9CPB5;
PF02381\"[72-147]T\"[148-219]TMraZ
TIGR00242\"[72-223]TTIGR00242: mraZ protein


","BeTs to 11 clades of COG2001COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG2001 is ---------dr-b-ef-hsn-jx-twNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-57) to 3/3 blocks of the IPB003444 family, which is described as \"Domain of unknown function UPF0040\". Interpro entry for IP:IPR003444. IPB003444A 72-94 4.4e-11 IPB003444B 113-130 8.1e-07 IPB003444C 142-196 4.6e-37 IPB003444A 148-170 0.56","Residues 72 to 206 match (7e-63) PD:PD006745 which is described as MRAZ PROTEOME COMPLETE ","","","","","","","","","","","","Mon Feb 17 15:27:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00849 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 148 to 219 (E-value = 1.5e-21) place AA00849 in the UPF0040 family which is described as Domain of unknown function UPF0040 family (PF02381)","","","","","Ishii A, Nakasone K, Sato T, Wachi M, solation and characterization of the dcw sluster from the piezophilic deep-sea bacterium Shewanella violacea.J Biochem (Tokyo). 2002 Aug;132(2):183-8.PubMed: NOT_FOUND Francis F, Ramirez-Arcos S, Salimnia H, Victor C, Dillon JR.Organization and transcription of the division cell wall (dcw) cluster in Neisseria gonorrhoeae.Gene. 2000 Jun 27;251(2):141-51.PubMed: NOT_FOUNDCarrion M, Gomez MJ, Merchante-Schubert R, Dongarra S, Ayala JA.mraW, an essential gene at the dcw cluster of Escherichia coli codes for a cytoplasmic protein with methyltransferase activity.Biochimie. 1999 Aug-Sep;81(8-9):879-88.PubMed: NOT_FOUND Mengin-Lecreulx D, Ayala J, Bouhss A, van Heijenoort J, Parquet C, Hara H.Contribution of the Pmra promoter to expression of genes in the Escherichia coli mra cluster of cell envelope biosynthesis and cell division genes.J Bacteriol. 1998 Sep;180(17):4406-12.PubMed: NOT_FOUNDGomez,M.J., Fluoret,B., van Heijenoort,J. and Ayala,J.A.Nucleotide sequence of the regulatory region of the gene pbpB ofEscherichia coliNucleic Acids Res. 18 (9), 2813 (1990)PubMed: 2187182","","Wed Jan 15 12:35:42 2003","1","","","" "AA00851","588495","586900","1596","ATGTTGTGGTTTTTCTTCTGTGTTTTAATGTTGATTTTAGGGTATTTTATTTATGGCAAAGTCGTCGAAAAGATTTTTGCTATTAATCCCAAACGTCAAACGCCTGCTTACGAACTCACTGATGGCGTGGATTACATGCCAATGTCCAAAACCAAAATTTGGTTAATCCAATTACTAAATATTGCCGGTACCGGTCCGATTTTTGGTCCGATTCTGGGAGCGTTATACGGACCGGTGGCAATGTTGTGGATTGTGCTCGGTTGTATTTTTGCCGGCGCGGTGCACGATTATTTCTGCGGTATGTTAAGTATTCGTCACGGTGGCGCAACCATGCCTTATTTGGCAGGCAAATTTTTAGGTCGTCCCGTTAAAGTTTTCATTAATCTTTTAGCGCTGATTCTTCTTTTATTAGTCGGGGTGGTATTTGTGGCAAGCCCTGCACAGTTAATGGGTACCATCACGATGGATATTTTCGGCGTATCACAAGGTGCTTTGCAACTAGGTGATGCTGAAGCGCTACATCATTCCGTTGAAGCCGGTGGTATTCAAGTATGGGGCATGGATAAAGCAACAGTAGTTTCTGTTTGGACACTCGCTATTTTTGCTTACTATATCCTTGCTACCTTATTGCCAATTGATAAAATTATCGGTCGAATTTATCCGCTCTTTGGTGCGTTATTACTCTTCATGTCTGTGGGTATGGTGTATGGTTTAGTCTCTGCACATTTCAGTGCTGCGGATCCAATTGAATTTTTCCGCACGGTGGATGCAGACGGTCAAGGTTTAACTTGGGATAAATTTACACAAAACTTCCAAGTAAAAGGTGATGTTCCGATTTGGCCGCTCCTGTTCTTAACCATTTCCTGTGGTGCACTGTCCGGCTTCCATGCCACTCAAACTCCATTAATGGCACGTTGTGCAGAAAATGAAAAAGAGGGTCGCTTTATTTTCTATGGTGCAATGATTACGGAAGGTATTATTGCTTTAGTCTGGTGTACGGTCGGTCTTGCATTCTATGAGAATCCACAAGCGTTACAAGACGCGATCACTGCGGGTTCACCGTCTAAGGTTGTATATGACAGTTCATTACATTTCCTAGGTTTTGTAGGGGGGATTTTTGCCGTGCTAGGTGTAGTGGTATTACCAATTACATCCGGCGATACAGCCTTCCGTGCAGCACGTTTACAATTGGCGGAAATCTTCCATATTGATCAACGTGTACTTTCCAAACGTTTATTGATTGCACTTCCATTGTTTGCGCTAGGTTATTTTGTCTCTACCATTGACTTCAGCGTGTTATGGCGCTATTTCACTTGGGCAAACCAAATGACCGCTATGGTGATGTTATGGACAGCGGCAGCTTATTTGTATCGCTACCATAAATTCCACTGGGTAGCTTCAATCCCGGCATGGTTTATCACCACCGTTTGTGCGACCTACCTGTACTACAACAAGATCGGTTTTAGCTTAGATTATCAGTTGTCTGTTTATTTAGGTTTCGCAACCACCATCGTATGCGTTGTATTGTTCTTCATATTGGTTAAACGTTCGGGTGAACCGGATCCTGATGCGTTAGAGGATAACTTCGCAAAACAA","","","58847","MLWFFFCVLMLILGYFIYGKVVEKIFAINPKRQTPAYELTDGVDYMPMSKTKIWLIQLLNIAGTGPIFGPILGALYGPVAMLWIVLGCIFAGAVHDYFCGMLSIRHGGATMPYLAGKFLGRPVKVFINLLALILLLLVGVVFVASPAQLMGTITMDIFGVSQGALQLGDAEALHHSVEAGGIQVWGMDKATVVSVWTLAIFAYYILATLLPIDKIIGRIYPLFGALLLFMSVGMVYGLVSAHFSAADPIEFFRTVDADGQGLTWDKFTQNFQVKGDVPIWPLLFLTISCGALSGFHATQTPLMARCAENEKEGRFIFYGAMITEGIIALVWCTVGLAFYENPQALQDAITAGSPSKVVYDSSLHFLGFVGGIFAVLGVVVLPITSGDTAFRAARLQLAEIFHIDQRVLSKRLLIALPLFALGYFVSTIDFSVLWRYFTWANQMTAMVMLWTAAAYLYRYHKFHWVASIPAWFITTVCATYLYYNKIGFSLDYQLSVYLGFATTIVCVVLFFILVKRSGEPDPDALEDNFAKQ","586902","","carbon starvation protein","Inner membrane, Cytoplasm","","
InterPro
IPR003706
Family
Carbon starvation protein CstA
PF02554\"[1-370]TCstA
noIPR
unintegrated
unintegrated
PD052353\"[472-528]TQ9CPB6_PASMU_Q9CPB6;
signalp\"[1-19]?signal-peptide
tmhmm\"[4-22]?\"[54-76]?\"[82-104]?\"[125-145]?\"[190-210]?\"[219-239]?\"[277-295]?\"[316-338]?\"[363-383]?\"[413-435]?\"[441-459]?\"[464-484]?\"[494-514]?transmembrane_regions


","BeTs to 12 clades of COG1966COG name: Carbon starvation protein, predicted membrane proteinFunctional Class: TThe phylogenetic pattern of COG1966 is ----kz-q--rlb-efgh-nu-----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.5e-84) to 4/4 blocks of the IPB003706 family, which is described as \"Carbon starvation protein CstA\". Interpro entry for IP:IPR003706. IPB003706A 9-47 1.6e-17 IPB003706B 52-93 2.7e-26 IPB003706C 200-240 8.2e-18 IPB003706D 279-306 3.8e-19","Residues 472 to 528 match (4e-12) PD:PD052353 which is described as PROTEOME COMPLETE HI1128 PM0132 TRANSMEMBRANE ","","","","","","","","","","","","Wed Dec 18 11:16:15 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00851 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 370 (E-value = 1.8e-181) place AA00851 in the CstA family which is described as Carbon starvation protein CstA (PF02554)","","","","","Schultz,J.E. and Matin,A. Molecular and functional characterization of a carbon starvation gene of Escherichia coli J. Mol. Biol. 218 (1), 129-140 (1991) PubMed: 1848300 ","","Wed Dec 18 11:15:59 2002","1","","","" "AA00852","588678","588797","120","ATGCTGAACGAAAAGTGCGGTATAAATTTCTTATGTTTTAAACAAAAAATCGCCGGGTTATACGCTTTATCAAAACTGATTCCGTCACAGAAATCATGTTATATCACTACCCTGAAAACA","","","4494","MLNEKCGINFLCFKQKIAGLYALSKLIPSQKSCYITTLKT","588797","","hypothetical protein","Cytoplasm, Extracellular","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 14:50:57 2004","Mon Feb 23 14:50:57 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00852 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 14:50:57 2004","","","","","","","","","","","","","1","","","" "AA00853","588919","588818","102","ATGGGTAGTGAAGTAGGTATCGAAAAGTGGGCGGAATGTCGCCCCTTGTTATTTACTATTGGTCATCCGGCAGGCCACAATCAGCACCAATTAAAATTGTCC","","","3767","MGSEVGIEKWAECRPLLFTIGHPAGHNQHQLKLS","588818","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 14:48:05 2004","Mon Feb 23 14:48:05 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00853 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 14:48:05 2004","","","","","","","","","","","","","1","","","" "AA00854","589718","589038","681","ATGTTTCAAGAGTATTTAAGCGTTATTGCACAAGGCATTCCCACCAGTTTGTTATTAACCGTTATTTCATTGGCGATTGCGTTTTTCTTGGCGCTGGTGCTGACCGTTTTGCTTGCTATGGGCAATAAAGCGGTTAAAAGTGCGGTCAATTTATACCTTACTTTATTTACCGGCACGCCGTTATTGGTGCAATTTTTCCTTATTTATGCCGGTCCTGGACAATTTCAATGGATCGTCAACAGCCCCTTGTGGTCAGTGTTATCTAATGCGTGGTTTTGCGCGGCGTTGACATTGGCGTTAAACAGTGCGGCGTACTCCACCCAATTATTCCACGGCGCGGTAAAAGCCATTCCGAAAGGACAGTGGGAAAGTTGCGAAGCGCTTGGGTTAAGCCGTTTGCAAACCTTGAAAATCCTGATTCCGTATGCGTTAAAACGTGCATTGCCTTCTTATTCCAACGAAATTATTTTGGTGTTTAAAGGCACAGCGTTGGCGTCCACTATTACCATCATGGACATTATGGGCTACGCCCGCCAACTTTATGGCACGGAATACGATGCGCTTACGATTTATGGTATTGCCGGTGGTATTTATCTGATTATCACCGGTATCGCAACACTCTTGTTGCGCAGACTGGAAAACAAAGTACTTGCCTTTGAGCGCTTGGCTATGAAAAGCGTC","","","24926","MFQEYLSVIAQGIPTSLLLTVISLAIAFFLALVLTVLLAMGNKAVKSAVNLYLTLFTGTPLLVQFFLIYAGPGQFQWIVNSPLWSVLSNAWFCAALTLALNSAAYSTQLFHGAVKAIPKGQWESCEALGLSRLQTLKILIPYALKRALPSYSNEIILVFKGTALASTITIMDIMGYARQLYGTEYDALTIYGIAGGIYLIITGIATLLLRRLENKVLAFERLAMKSV","589040","","arginine transport system permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR000515
Family
Binding-protein-dependent transport systems inner membrane component
PF00528\"[13-214]TBPD_transp_1
PS50928\"[13-209]TABC_TM1
InterPro
IPR010065
Domain
Amino acid ABC transporter, permease protein, 3-TM region, His/Glu/Gln/Arg/opine
TIGR01726\"[5-112]THEQRo_perm_3TM: amino acid ABC transporter,
noIPR
unintegrated
unintegrated
signalp\"[1-39]?signal-peptide
tmhmm\"[19-39]?\"[49-69]?\"[83-103]?\"[155-175]?\"[189-209]?transmembrane_regions


","BeTs to 15 clades of COG0765COG name: ABC-type amino acid transport system, permease componentFunctional Class: EThe phylogenetic pattern of COG0765 is a----z--vd-lbcefgh-nujxi--Number of proteins in this genome belonging to this COG is","","Residues 96 to 174 match (1e-07) PD:PD545085 which is described as PROTEOME COMPLETE PERMEASE SYSTEM TRANSMEMBRANE HISTIDINE HISQ TRANSPORTER INNER ABC ","","","","","","","","","","","","Wed Dec 18 11:19:49 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00854 is paralogously related to AA00855 (2e-29), AA01525 (1e-21) and AA00416 (5e-04).","","","","","","Residues 13 to 214 (E-value = 1.2e-15) place AA00854 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component (PF00528)","","","","","Wissenbach U, Six S, Bongaerts J, Ternes D, Steinwachs S, Unden G. A third periplasmic transport system for L-arginine in Escherichia coli: molecular characterization of the artPIQMJ genes, arginine binding andtransport. Mol Microbiol. 1995 Aug;17(4):675-86. PMID: 8801422 Wissenbach,U., Keck,B. and Unden,G. Physical map location of the new artPIQMJ genes of Escherichia coli, encoding a periplasmic arginine transport system J. Bacteriol. 175 (11), 3687-3688 (1993) PubMed: 8501075 ","","Wed Dec 18 11:19:49 2002","1","","","" "AA00855","590383","589724","660","ATGTTTTCCGATTATTTTTCTTTAATGTTTACCGCAGCCCTAATGACCTTGGGGCTTGCGGTTTGTTCGTTGGTGTTTGGGCTGATTTTGGGCATGCTGTTCGCCGTGCTGGAAGCAAACCGCTTTGTGGGCAAACCGATGGCGGTGTTTGTCGCCTTATTGCGTGGCTTGCCTGAAATTCTGGTGGTGTTATTGGTGTATTTCGGTTCCAGCGAAGTGGTGGAAATGATCACCGGCGATTACATTGAATTCGGTGCGTTCGGTTGCGGTGTGTTCGCCCTTTCCCTTATTTTTGCGGCTTATGCTTCACAAACGTTGCGCGGTGCCATTCAGGCGATTGCTAAAGGACAATGGGAATCCGGCGCGGCATTAGGCTTGAGTAAAGGCTATACTTTCATTCATATCGTGATGCCGCAAGTATGGCGCCACGCGCTGCCGGGCTTGAGCAATCAATGGTTGGTGTTGTTGAAAGATACTGCACTCATTTCTTTAATCGGGGTGGATGATTTAATGCGTCAGGCACAGCTGATTAACACCAATACCCATCAGCCTTTCACGTGGTATGGCATTGCTGCCTTGATTTACTTACTGGTTACTTTAGTGAGCCAGGTGGGTATCCGTAAATTAGAACTGCGTTTTACCCGCTTTGAAAGAGGAGTG","","","24165","MFSDYFSLMFTAALMTLGLAVCSLVFGLILGMLFAVLEANRFVGKPMAVFVALLRGLPEILVVLLVYFGSSEVVEMITGDYIEFGAFGCGVFALSLIFAAYASQTLRGAIQAIAKGQWESGAALGLSKGYTFIHIVMPQVWRHALPGLSNQWLVLLKDTALISLIGVDDLMRQAQLINTNTHQPFTWYGIAALIYLLVTLVSQVGIRKLELRFTRFERGV","589726","","arginine ABC transporter, permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR000515
Family
Binding-protein-dependent transport systems inner membrane component
PF00528\"[9-215]TBPD_transp_1
PS50928\"[13-206]TABC_TM1
InterPro
IPR010065
Domain
Amino acid ABC transporter, permease protein, 3-TM region, His/Glu/Gln/Arg/opine
TIGR01726\"[5-108]THEQRo_perm_3TM: amino acid ABC transporter,
noIPR
unintegrated
unintegrated
signalp\"[1-39]?signal-peptide
tmhmm\"[19-37]?\"[47-67]?\"[81-101]?\"[122-142]?\"[186-206]?transmembrane_regions


","BeTs to 15 clades of COG0765COG name: ABC-type amino acid transport system, permease componentFunctional Class: EThe phylogenetic pattern of COG0765 is a----z--vd-lbcefgh-nujxi--Number of proteins in this genome belonging to this COG is","","Residues 12 to 71 match (5e-13) PD:PD001196 which is described as PROTEOME COMPLETE PERMEASE ABC TRANSMEMBRANE TRANSPORTER ACID AMINO TRANSPORTER SYSTEM ","","","","","","","","","","","","Wed Dec 18 11:21:10 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00855 is paralogously related to AA00854 (2e-29), AA01525 (8e-28) and AA01050 (8e-04).","","","","","","Residues 9 to 215 (E-value = 8.6e-17) place AA00855 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component (PF00528)","","","","","Nishijyo,T., Park,S.M., Lu,C.D., Itoh,Y. and Abdelal,A.T. Molecular characterization and regulation of an operon encoding a system for transport of arginine and ornithine and the ArgR regulatory protein in Pseudomonas aeruginosa J. Bacteriol. 180 (21), 5559-5566 (1998) PubMed: 9791103 Wissenbach U, Six S, Bongaerts J, Ternes D, Steinwachs S, Unden G.A third periplasmic transport system for L-arginine in Escherichia coli: molecular characterization of the artPIQMJ genes, arginine binding and transport.Mol Microbiol. 1995 Aug;17(4):675-86.PMID: 8801422Wissenbach,U., Keck,B. and Unden,G. Physical map location of the new artPIQMJ genes of Escherichia coli, encoding a periplasmic arginine transport system J. Bacteriol. 175 (11), 3687-3688 (1993) PubMed: 8501075 ","","Wed Dec 18 11:28:32 2002","1","","","" "AA00856","591107","590391","717","ATGAAAAAATTACTGCTAAGCGCCATTTTATTGGGTTCCGCCGTTGTGGCTAACGCACAGGATTTAACTTTCGCCATGGAACCGAGCTATCCGCCGTTTGAATTCACTAACGAAAAGGGCGAAATTATCGGTTTTGATGTGGACATTGCGAATGCCATTTGTAAAGAAATTCAAGCTACCTGCCATTTTAAAGGTGAAGCCTTTGATTCGTTAATTACCAATTTAAGATCAAAGCGTTTTGATGCGGCAATTTCCGCCATGGATATTACCGAGGCGCGCGCGAAACAAGTGTTATTCTCCGATCCTTATTATGACAGCACCGCAAGCTATGTGGCGCTGAAAGGCAAAGCCACATTGGACAGCGCGAAAAATGTCGGCGTGCAAAACGGCACCACCTTCCAGCAATATACCGTTGCCGAAACCAAACAATATGCATCGAAATCTTACGCCAGCCTGCAAGATGCGATTCTGGACTTAAAAAACGGGCGTATCGATATTATTTTCGGTGATACCGCCGTGCTTGCGGACATGATTTCCAAAGAACCGGAAATTCAATTTGTCGGTGACAAAGTGACCAATAAAAAATATTTCGGTAACGGTTTAGGCATCGCCATGAACAAATCCAACAAAGCCTTGGCGGAAAGCCTGAATAAAGGTTTGGCGGCGATCAAAGCCAACGGTGAGTATCAAAAAATCTATGATAAATGGATGACCAAA","","","26875","MKKLLLSAILLGSAVVANAQDLTFAMEPSYPPFEFTNEKGEIIGFDVDIANAICKEIQATCHFKGEAFDSLITNLRSKRFDAAISAMDITEARAKQVLFSDPYYDSTASYVALKGKATLDSAKNVGVQNGTTFQQYTVAETKQYASKSYASLQDAILDLKNGRIDIIFGDTAVLADMISKEPEIQFVGDKVTNKKYFGNGLGIAMNKSNKALAESLNKGLAAIKANGEYQKIYDKWMTK","590393","","arginine ABC transporter, periplasmic-binding protein","Periplasm","","
InterPro
IPR001638
Family
Bacterial extracellular solute-binding protein, family 3
PF00497\"[22-239]TSBP_bac_3
SM00062\"[21-239]TPBPb
PS01039\"[44-57]TSBP_BACTERIAL_3
InterPro
IPR005768
Family
Lysine-arginine-ornithine-binding periplasmic protein
TIGR01096\"[2-237]T3A0103s03R: lysine-arginine-ornithine-bindi
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[19-136]Tno description
signalp\"[1-19]?signal-peptide


","BeTs to 17 clades of COG0834COG name: ABC-type amino acid transport system, periplasmic componentFunctional Class: EThe phylogenetic pattern of COG0834 is a----z--vdrlbcefgh-nujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 3.3e-19) to 2/2 blocks of the IPB001638 family, which is described as \"Bacterial extracellular solute-binding proteins, family 3\". Interpro entry for IP:IPR001638. IPB001638A 40-49 0.0089 IPB001638B 72-103 8e-15","Residues 86 to 129 match (6e-12) PD:PD503017 which is described as PERIPLASMIC PROTEOME COMPLETE ARGININE-BINDING ARGININE PRECURSOR AMINO-ACID SYSTEM SIGNAL 3RD ","","","","","","","","","","","","Wed Dec 18 11:22:12 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00856 is paralogously related to AA01526 (2e-18).","","","","","","Residues 22 to 239 (E-value = 4.7e-83) place AA00856 in the SBP_bac_3 family which is described as Bacterial extracellular solute-binding proteins, family 3 (PF00497)","","","","","Wissenbach U, Six S, Bongaerts J, Ternes D, Steinwachs S, Unden G.A third periplasmic transport system for L-arginine in Escherichia coli: molecular characterization of the artPIQMJ genes, arginine binding and transport.Mol Microbiol. 1995 Aug;17(4):675-86.PMID: 8801422Highlander,S.K., Wickersham,E.A., Garza,O. and Weinstock,G.M. Expression of the Pasteurella haemolytica leukotoxin is inhibited by a locus that encodes an ATP-binding cassette homolog Infect. Immun. 61 (9), 3942-3951 (1993) PubMed: 8359916 Wissenbach,U., Keck,B. and Unden,G. Physical map location of the new artPIQMJ genes of Escherichia coli, encoding a periplasmic arginine transport system J. Bacteriol. 175 (11), 3687-3688 (1993) PubMed: 8501075 ","","Wed Dec 18 11:27:40 2002","1","","","" "AA00858","591862","591131","732","ATGACAATTAGTGTTGAGAATTTGAATTTTTTTTATGGCGCGAACCAAGCCTTGTTTGATATTAACTTAACCGCCGATGATGGCGATGTACTAGTGTTGCTGGGACCAAGTGGGGCGGGGAAAAGCACCTTAATCCGTACCCTGAACCTGTTGGAAGTGCCGCAATCCGGTAAATTGAGCATTGCCAATAATCAGTTTAATTTATCTTCCGGTAACGACCCGAAACAGCTTCGCCAATTGCGTCGCGATGTCGGCATGGTGTTCCAGCAATATAATTTGTGGCCGCACATGACGGTGATACAAAATTTAATTGAAGCACCGATGAACATTCTGGGCGTTAGCGAAACGGAAGCCAAGCAACAAGCGCTTGAATTATTACAGCGTTTGCGTTTGGATGAATTCGCCGATCGTTTCCCGTTGCATTTGTCCGGCGGTCAGCAACAGCGTGTGGCGATTGCCCGTGCGTTAATGATGAAACCGCAAGTGTTGTTGTTCGATGAACCGACGGCGGCACTGGATCCGGAAATTACCGCGCAGATCGTCTCCATTATTGAAGAATTGCAACAAACCGGTATTACGCAGGTTATCGTCACCCACGAAGTGAATGTGGCGAAAAAAGTGGCGACCAAAGTAGTATATATGGAGCAGGGGCATATTATTGAAATCGGCGATAAGACCTGCTTTGAACAGTCGCATACGGGACAATTCAAACAATATTTATCACATAATATT","","","27208","MTISVENLNFFYGANQALFDINLTADDGDVLVLLGPSGAGKSTLIRTLNLLEVPQSGKLSIANNQFNLSSGNDPKQLRQLRRDVGMVFQQYNLWPHMTVIQNLIEAPMNILGVSETEAKQQALELLQRLRLDEFADRFPLHLSGGQQQRVAIARALMMKPQVLLFDEPTAALDPEITAQIVSIIEELQQTGITQVIVTHEVNVAKKVATKVVYMEQGHIIEIGDKTCFEQSHTGQFKQYLSHNI","591133","","arginine ABC transporter, ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[142-184]TQ8D037_YERPE_Q8D037;
PF00005\"[28-217]TABC_tran
PS50893\"[3-241]TABC_TRANSPORTER_2
PS00211\"[142-156]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[27-218]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[3-243]Tno description
PTHR19222\"[3-223]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF33\"[3-223]TGLUTAMATE / GLUTAMINE ABC TRANSPORTER


","BeTs to 15 clades of COG1126COG name: ABC-type polar amino acid transport system, ATPase componentFunctional Class: EThe phylogenetic pattern of COG1126 is a----z--vd-lbcefgh-nujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.6e-30) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 17-63 4.8e-11 IPB001140B 139-177 5.8e-17 IPB001140C 194-223 18Significant hit ( 6.9e-06) to 1/3 blocks of the IPB000619 family, which is described as \"Guanylate kinase\". Interpro entry for IP:IPR000619. IPB000619A 31-48 7.1e-06","","","","","","","","","","","","","Wed Dec 18 11:23:12 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00858 is paralogously related to AA01524 (4e-48), AA02718 (5e-38), AA00415 (7e-37), AA00700 (3e-36), AA01051 (4e-36), AA01645 (5e-34), AA01656 (7e-34), AA02353 (1e-33), AA01422 (6e-33), AA02080 (1e-31), AA02440 (5e-29), AA01867 (5e-29), AA01616 (7e-28), AA02899 (2e-25), AA02324 (2e-24), AA02320 (5e-24), AA02898 (1e-23), AA02805 (2e-22), AA02140 (3e-22), AA01684 (3e-22), AA01779 (5e-22), AA00933 (2e-21), AA00799 (4e-21), AA01824 (9e-21), AA01947 (2e-20), AA01961 (3e-19), AA01568 (4e-19), AA02152 (2e-18), AA01510 (2e-18), AA01820 (2e-18), AA02550 (5e-18), AA02606 (2e-17), AA01456 (2e-17), AA01393 (4e-17), AA02786 (2e-16), AA00207 (2e-15), AA01509 (3e-15), AA02609 (5e-15), AA01757 (5e-15), AA00751 (2e-14), AA02642 (5e-14), AA01569 (1e-13), AA02331 (1e-13), AA02573 (9e-13), AA02225 (7e-12), AA02484 (1e-11), AA02146 (3e-11), AA01555 (1e-10), AA00591 (3e-10), AA00061 (3e-10), AA00934 (6e-09), AA01291 (2e-05), A02145 (2e-04) and AA02226 (4e-04).","","","","","","Residues 28 to 217 (E-value = 7.9e-70) place AA00858 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Wissenbach U, Six S, Bongaerts J, Ternes D, Steinwachs S, Unden G.A third periplasmic transport system for L-arginine in Escherichia coli: molecular characterization of the artPIQMJ genes, arginine binding and transport.Mol Microbiol. 1995 Aug;17(4):675-86.PMID: 8801422Wissenbach,U., Keck,B. and Unden,G. Physical map location of the new artPIQMJ genes of Escherichia coli, encoding a periplasmic arginine transport system J. Bacteriol. 175 (11), 3687-3688 (1993) PubMed: 8501075 ","","Wed Dec 18 11:25:03 2002","1","","","" "AA00860","592587","592006","582","ATGTATTTCGATCAAATCAAAGCCGAGCTTACCGAAGCGGCGGACGTATTAAACAAATTTTTATCTGATGACAACAAAATTAAATTGATTCAACAGGCGGCATTATTAATCTCTGATAGTTTTAAACAAGGCGGTAAAGTGCTGTCTTGCGGGAACGGCGGTTCACATTGTGACGCCATGCACTTTGCGGAAGAATTAACCGGCCGCTACCGTGAAAACCGTCCCGGTTATCCGGCAATCGCCATTTCCGATGTCAGCCATTTGAGCTGCGTAAGTAACGATTTCGGCTACGATTATGTGTTTTCCCGTTATGTAGAAGCCGTGGGGCAAAAAGGCGACGTGCTGTTCGGTTTATCCACCTCCGGCAATTCTAAAAACGTGCTTAACGCTATTGAAGCGGCAAAAGCCAAAGGTATGAAGGTGATTGCGATGACCGGCAAAGACGGTGGCAAAATGGCGGGGCTTGCTGATGTGGAAATTCGCGTGCCGCATTTCCGTTACGCAGATCGTATTCAGGAAATCCACATTAAAGTGATTCACATTTTGATGATGTTAATTGAATTCGAAATGGCGAAAGCAGAA","","","21298","MYFDQIKAELTEAADVLNKFLSDDNKIKLIQQAALLISDSFKQGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAISDVSHLSCVSNDFGYDYVFSRYVEAVGQKGDVLFGLSTSGNSKNVLNAIEAAKAKGMKVIAMTGKDGGKMAGLADVEIRVPHFRYADRIQEIHIKVIHILMMLIEFEMAKAE","592008","","phosphoheptose isomerase","Cytoplasm","","
InterPro
IPR001347
Domain
Sugar isomerase (SIS)
PF01380\"[111-164]TSIS
InterPro
IPR004515
Family
Phosphoheptose isomerase
TIGR00441\"[6-187]TgmhA: phosphoheptose isomerase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.10490\"[3-190]Tno description


","BeTs to 12 clades of COG0279COG name: Phosphoheptose isomeraseFunctional Class: GThe phylogenetic pattern of COG0279 is --mp---q--r--cefgh-nuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 6.5e-14) to 1/3 blocks of the IPB000281 family, which is described as \"Helix-turn-helix domain, RpiR family\". Interpro entry for IP:IPR000281. IPB000281B 98-145 5.9e-14Significant hit ( 9.7e-13) to 2/2 blocks of the IPB001347 family, which is described as \"SIS domain\". Interpro entry for IP:IPR001347. IPB001347A 54-62 0.45 IPB001347B 113-138 6.6e-10","Residues 95 to 163 match (1e-14) PD:PD308434 which is described as ISOMERASE COMPLETE PROTEOME PHOSPHOHEPTOSE PROBABLE 5.-.-.- LIPOPOLYSACCHARIDE BIOSYNTHESIS PHOSPHOSUGAR ISOMERASE ","","","","","","","","","","","","Wed Dec 18 11:33:15 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00860 is paralogously related to AA02015 (1e-17).","","","","","","Residues 38 to 192 (E-value = 3e-48) place AA00860 in the SIS family which is described as SIS domain (PF01380)","","","","","Bauer,B.A., Stevens,M.K. and Hansen,E.J. Involvement of the Haemophilus ducreyi gmhA gene product inlipooligosaccharide expression and virulence. Infect. Immun. 66(9): 4290-4298, 1998. PubMed: 9712780.Preston,A., Maskell,D., Johnson,A. and Moxon,E.R. Altered lipopolysaccharide characteristic of the I69 phenotype inHaemophilus influenzae results from mutations in a novel gene, isn. J. Bacteriol. 178(2): 396-402, 1996. PubMed: 8550458. Brooke,J.S. and Valvano,M.A. Biosynthesis of inner core lipopolysaccharide in enteric bacteriaidentification and characterization of a conserved phosphoheptoseisomerase. J. Biol. Chem. 271(7): 3608-3614, 1996. PubMed: 8631969. Brooke JS, Valvano MA. Molecular cloning of the Haemophilus influenzae gmhA (lpcA) gene encodinga phosphoheptose isomerase required for lipooligosaccharide biosynthesis. J Bacteriol. 1996 ","","Wed Dec 18 11:33:15 2002","1","","","" "AA00861","596210","592692","3519","TTGGAAATCCCCCTCGTTTGCGCTAAACTAACGGCAATTTTTTTCTTACTCTTTTGTCGTTTTATGCAAACTCAATTTTTTCATCTCGAAATTCCTACCCAAGCGAATGATCATAAAATTTTAGCCAATATCCTGCCCGGTGCGGATAGCCTCGCCATTAGCGAAATTGCCGCGCAGTTTGACGGTCTAACCGTGGTGGTGACCAATGACACCCGAAGTGCGGTGCGTTTGGCGAAAGAATTAACGCAACTGACGCCTTCCGAATTATTGCAAAACGTGACTTTTTTCCCCGATTGGGAAACCCTGCCTTATGATAGTTTTTCGCCTCATCAAGATATTATTTCCGCGCGCTTGAGCGCTTTGTTTCATTTGCAACAGCGCAAACAAGGCATTTTCATTTTACCTGTCGCCACCTTAATGCAACGGGTTTGCCCGCCGTCTTATTTGCAGCATAACGTATTGTTGATTAATAAAGGCGATCGTTTTGTCATCGAATCTCTTCGCCTACAATTGGAAAAAGCGGGTTATCGTGCGGTGGAGCAGGTATTGGAACATGGCGAATATGCGGTGCGCGGTGCGTTGTTGGATTTGTTCCCGATGGGAAGTGCGGTGCCTTTTCGCTTAGATTTTTTTGATGATGAAATTGATTCCATTCGCACTTTTGATGTGGACACCCAGCGTACGTTGCAGGAAATCGACCAAATTAATTTATTGCCGGCACATGAATTTCCGACGGATAGCACGGGTATTGAATTTTTCCGTAGCCAATTTCGGGCGGAATTCGGGGAAATTCGACGGGATCCGGAACACATTTATCAACAGGTCAGCAAAGGCACGCTGGCTGCGGGCATTGAATATTGGCAGCCGCTGTTTTTTGAGCAAATGGCAACCTTGTTCAATTATTTTCCGGTAAATACGCTGTTTACTACCGCCGAGCAAAATCAAGACCAAGGCGAGCGTTTTTACACCGATGCACAACAGCGTTTTGAAAGTCGTCGCGTGGATCCTATGCGCCCGTTGTTACCGCCCGATAAACTTTGGTTGCGCATTGATGAAGTGAATCGTCACTTGAAACAGTATCCCGCTATTGTGCTAAAAGCGGAAAAAGTGCGGTCGTCTGCGCGGCAGAAAAATTTAGTGATTGCGTCGCTGCCACCGTTGACCATTCAATCTCAACAAAAAGAACCTTTGCATCAACTGCGTCAATTTATTGAGCAATTTAAAGGCAATATTTTATTTATCGTGGAAACGGAAGGCCGTCGTGAAACCTTGCTGAGTCTGCTTGCGCCGTTAAAACTTAAACCGAAACAAATTCATACCTTAGCACGGGCGGAAGAACAAAAATTTTCGTTAATGGTCAGCCCATTGGAGCATGGCTTTATCATTGAACAAGGTACGCCGCTTGCGATTATTTGTGAAACTGAATTGTTGGGCGAACGCGTGCAACAACGGCAACGGGACAAATCCCGCACGGTGAATCCCGACACCTTAATTCGTAACCTGGCGGAACTGCAAATCGGTCAGCCTGTGGTGCATTTGGATCATGGCGTAGGGCGCTATGGCGGTTTGGTAACGCTGGAAAACGGCGGCGTGAAAGCGGAATATTTGCTGCTTAACTATGCTAACGATTCCAAATTGTATGTGCCGGTGGCATCTTTACATTTGATCAGCCGCTATGTGGGCGGTTCCGATGAAACGGCGCCGTTGCACAAATTAGGTTCTGAAGCTTGGGGCAAAGCACGTAGCAAAGCCGCCGAGAAAATCCGCGATGTGGCGGCGGAATTATTAGACGTGTATGCCCAGCGTGAAGCGCAAAAAGGCTTTGCGTTTCAATATGATCGTGAAGAATTTCAACAATTCACCGCGACGTTTCCTTTTGAAGAAACTCATGATCAGCTGATGGCTATTAACGCGGTGATTTCCGACATGACCCAACCGAAAGCCATGGACCGCTTGGTGTGCGGCGATGTGGGATTCGGCAAAACGGAAGTGGCAATGCGCGCGGCGTTTTTGGCGGTGATGAATCACAAACAGGTCGCCGTTTTGGTGCCGACCACGTTGTTGGCGCAACAACATTTTGATAATTTCAAAGACCGTTTCGCCAACCTGCCGGTAAACGTGGAAATGCTGTCCCGCTTTAAAACCGCCAAAGAACAAAAACAGGTGATTCAGGATTTAGCCGACGGCAAAGTGGATATTCTGATCGGCACTCATAAAATCATTCAGGGTGATGTGCAATTTCACGATCTGGGCTTATTGATTATTGACGAAGAACATCGCTTCGGTGTGCGTCAGAAAGAAAAAATGAAACAATTGCGTGCCAACATTGATATTCTCACCCTCACCGCAACGCCGATTCCGCGCACCTTAAATATGGCGATGAACGGCATTCGCGATCTTTCCATTATTTCTACACCGCCGGCGCGTCGTTTAACCATTAAAACGTTCGTGCGTCAAACGGACGATTTGGTCATTCGCGAGGCGATTTTGCGTGAAATTCTGCGTGGCGGGCAGGTGTATTATTTGCATAACGATGTGGCGAGCATTGAAAATACGGCGGAAAAACTGACCGCACTTGTGCCGGAAGCGCGCGTCACCGTGGGGCACGGGCAAATGCGCGAGCGGGAGCTGGAGCGCGTGATGTCGGATTTTTATCATCAACGTTATAACGTGTTGGTGTGTTCTACCATTATTGAAACGGGCATCGATGTGCCGACCGCTAATACCATTATTATTGAACGCGCCGATAATTTCGGCTTGGCGCAGTTACACCAGCTTCGTGGGCGAGTAGGGCGTTCCCATCATCAAGCCTATGCCTATTTGCTCACTCCGCCGCCAAAACTGATGACCAAAGACGCGCAAAAACGTTTAGAAGCCTTGGAAAGTCTGGATAACCTCGGGGCGGGCTTCATCTTGGCAACCCACGATTTGGAAATCCGTGGTGCCGGCGAATTGCTGGGCAACGAACAAAGCGGGCAAATTGAAAGCATCGGTTTTTCTCTTTATATGGAATTGCTGGAACGCGCCGTGAAGGCCCTAAAAGAAGGGCGTGAACCGTCGTTGGACGAACTGACCCAGCAACAAACGGAAATCGATTTGCGCGTGCCGTCCCTGTTGCGGGAAGATTATTTGGGCGATGTGAATATGCGCCTGTCTTTCTATAAACGCATTGCCGGCGCAGAAAATACGGAAGCCTTGGACGAGTTAAAAGTGGAGCTTATTGACCGCTTCGGTGCGCTTCCACAAGCCACTCGCAATTTATTGCAAATCGCCCAATTGCGTCTGGATTTAAAACCGCTCAACGTTATTCGATTGGATGCCAATGCGCAGGGCGGCTTTATTGAGTTTGCGCCGAACGCCGATTTGGACCCGACGATCTTTTTGCAGCTGATCCAACGCAATCCCTCCGTCTATCGCTTCGACGGCCCGCACAAATTCCGCTTTAGCAAAGATTTAACGGACAATAAAGTGCGGTTAGAATTTGTGGTGGATTTAGTGCGGGAATTGATTATCCCCCGA","","","133402","LEIPLVCAKLTAIFFLLFCRFMQTQFFHLEIPTQANDHKILANILPGADSLAISEIAAQFDGLTVVVTNDTRSAVRLAKELTQLTPSELLQNVTFFPDWETLPYDSFSPHQDIISARLSALFHLQQRKQGIFILPVATLMQRVCPPSYLQHNVLLINKGDRFVIESLRLQLEKAGYRAVEQVLEHGEYAVRGALLDLFPMGSAVPFRLDFFDDEIDSIRTFDVDTQRTLQEIDQINLLPAHEFPTDSTGIEFFRSQFRAEFGEIRRDPEHIYQQVSKGTLAAGIEYWQPLFFEQMATLFNYFPVNTLFTTAEQNQDQGERFYTDAQQRFESRRVDPMRPLLPPDKLWLRIDEVNRHLKQYPAIVLKAEKVRSSARQKNLVIASLPPLTIQSQQKEPLHQLRQFIEQFKGNILFIVETEGRRETLLSLLAPLKLKPKQIHTLARAEEQKFSLMVSPLEHGFIIEQGTPLAIICETELLGERVQQRQRDKSRTVNPDTLIRNLAELQIGQPVVHLDHGVGRYGGLVTLENGGVKAEYLLLNYANDSKLYVPVASLHLISRYVGGSDETAPLHKLGSEAWGKARSKAAEKIRDVAAELLDVYAQREAQKGFAFQYDREEFQQFTATFPFEETHDQLMAINAVISDMTQPKAMDRLVCGDVGFGKTEVAMRAAFLAVMNHKQVAVLVPTTLLAQQHFDNFKDRFANLPVNVEMLSRFKTAKEQKQVIQDLADGKVDILIGTHKIIQGDVQFHDLGLLIIDEEHRFGVRQKEKMKQLRANIDILTLTATPIPRTLNMAMNGIRDLSIISTPPARRLTIKTFVRQTDDLVIREAILREILRGGQVYYLHNDVASIENTAEKLTALVPEARVTVGHGQMRERELERVMSDFYHQRYNVLVCSTIIETGIDVPTANTIIIERADNFGLAQLHQLRGRVGRSHHQAYAYLLTPPPKLMTKDAQKRLEALESLDNLGAGFILATHDLEIRGAGELLGNEQSGQIESIGFSLYMELLERAVKALKEGREPSLDELTQQQTEIDLRVPSLLREDYLGDVNMRLSFYKRIAGAENTEALDELKVELIDRFGALPQATRNLLQIAQLRLDLKPLNVIRLDANAQGGFIEFAPNADLDPTIFLQLIQRNPSVYRFDGPHKFRFSKDLTDNKVRLEFVVDLVRELIIPR","592694","","transcription repair coupling factor","Cytoplasm, Periplasm","","
InterPro
IPR001650
Domain
Helicase, C-terminal
PF00271\"[857-934]THelicase_C
SM00490\"[850-934]THELICc
PS51194\"[824-978]THELICASE_CTER
InterPro
IPR003711
Domain
Transcription factor CarD
PF02559\"[503-600]TCarD_TRCF
InterPro
IPR004576
Family
Transcription-repair coupling factor
TIGR00580\"[171-1106]Tmfd: transcription-repair coupling factor
InterPro
IPR005118
Domain
TRCF
PF03461\"[1032-1140]TTRCF
InterPro
IPR011545
Domain
DEAD/DEAH box helicase, N-terminal
PF00270\"[629-793]TDEAD
InterPro
IPR014001
Domain
DEAD-like helicases, N-terminal
SM00487\"[624-814]TDEXDc
InterPro
IPR014021
Domain
Helicase superfamily 1 and 2 ATP-binding
PS51192\"[642-803]THELICASE_ATP_BIND_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[152-240]T\"[605-807]T\"[816-945]Tno description
PTHR14950\"[869-929]THELICASE-RELATED
PTHR14950:SF2\"[869-929]TRNA HELICASE/RNASEIII CAF
signalp\"[1-24]?signal-peptide


","BeTs to 16 clades of COG1197COG name: Transcription-repair coupling factor - superfamily II helicaseFunctional Class: L,KThe phylogenetic pattern of COG1197 is --------vdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","","Residues 997 to 1046 match (6e-08) PD:PD467336 which is described as PROTEOME COUPLING COMPLETE FACTOR TRANSCRIPTION-REPAIR HELICASE ATP-BINDING MFD TRCF REPAIR ","","","","","","","","","","","","Wed Dec 18 11:34:50 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00861 is paralogously related to AA02303 (8e-69), AA02480 (1e-10), AA01335 (1e-10) and AA00927 (1e-04).","","","","","","Residues 1032 to 1140 (E-value = 2.4e-46) place AA00861 in the TRCF family which is described as TRCF domain (PF03461)","","","","","Park JS, Marr MT, Roberts JW.E. coli Transcription repair coupling factor (Mfd protein) rescues arrested complexes by promoting forward translocation.Cell. 2002 Jun 14;109(6):757-67.PMID: 12086674 Svejstrup JQ.Transcription repair coupling factor: a very pushy enzyme.Mol Cell. 2002 Jun;9(6):1151-2.PMID: 12086609Tu Y, Bates S, Pfeifer GP. The transcription-repair coupling factor CSA is required for efficient repair only during the elongation stages of RNA polymerase II transcription. Mutat Res. 1998 May 25;400(1-2):143-51. PMID: 9685618 Tantin D, Kansal A, Carey M.Recruitment of the putativetranscription-repair coupling factor CSB/ERCC6 to RNA polymerase II elongation complexes. Mol Cell Biol. 1997 Dec;17(12):6803-14. PMID: 9372911","","Wed Feb 5 13:37:25 2003","1","","","" "AA00862","596775","596605","171","ATGGCTGAAGAAGCCAAAAAAGGTTGGTTAAAACGCGCTTGGGATGCGTATTCCGATTTCTGCAAAGAAGCAGGCGTGGATCAAGGCACTTGCCGAGGCTGCGTACCGGTGGTGAAGTTTGATGAAGATCCCGAACCGAAGGAAAAAACGGTGGAGGAGAAAGAAACGCAC","","","6486","MAEEAKKGWLKRAWDAYSDFCKEAGVDQGTCRGCVPVVKFDEDPEPKEKTVEEKETH","596605","","conserved hypothetical protein","Cytoplasm, Periplasm","This sequence is weakly similar to gi|23466552, a hypothetical from H. influenzae.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 14:56:03 2004","Mon Feb 23 14:56:03 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00862 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 14:56:03 2004","","","","","","","","","","","","","1","","","" "AA00863","598738","596819","1920","ATGGCGCGGCAGCTAATTCTCCTTGTTGGCGACGATGCCACGTTAGCGCGCCAATGGGAATACTTTCCTGCCCTGAAAAGTGCGGTGTGGATTGGCGGTGTTTTGCCGCACTTTTCCGCTCAACTTCATTTCCCTTTTAGCAAAAGTAAAAATCTGCTCGGCAGCGAATTCCCCGCGCTCATTTATGATGGGCGCCAAGGCATTCATTTAGATGCCCTCGCTATTGCCGCCGGTGCGTTGTCGGAAGGCGGCACATTGTTGCTGTTATTCAATGAGTGGCAGGATTTGGCGGCACAACCCGACGGCGACAGCCTGCGTTGGAGCAGTGAAAAACACCCGATAAACACACCGCACTTTATTGCCTTTCTGCAAGAAAAAATCCGGAAATACAGCTTCCCCATTTATCAACATTTGCCGTCTGCGCTCGTTTTCCCTAAGATTGAAAAGTCGCTTTCAGAACAACACCAACCGACCTTGGAACAAGCCCATTTATTGCGGCAAATGGCGACATCTGACGCGGAGATGTTAATCGTTACGGCAAAGCGCGGGCGGGGAAAATCCGCTTTGGCGGGCTTGTTCGCCAAACAGCAATTAGCGGCAAATAAGCCCGTTCTATTGACGGCGCCGAACAAAAGTGCGGTCAAGATTTTCAATGAATTTTCCGGTGTCGAAATCCCCTTTATGCCACCTGATGAACTGCGCCAAAAGGTTGGTGAAAATCCACAGCAATTTGCGGATTCGTGGTTATTTGTGGACGAAGCGGCGATGATTCCGTTGGATACGCTGTTTGATTTAACGACTGCCTTTAAACGTATTGTGCTGACGACCACCATTCACAGCTACGAAGGCACGGGCAGGGGCTTCTTGTTAAAATTCATGACGAAAACCGACCGCACTTTGCGGCATTTTGAATTGTTCAGCCCGTTACGTTGGCAGGCGGATGACAAACTGGAGCGCTTTATTGATGAATTGTTGTTGTGTGATTGCGAAGATCGTCTGACGCAACCGCGTTACGATGCCAACCTTGCCAAACAGATTCAGATTTCTTACGAAGAACAGATTCCGCCTTATCAAATCGAATCGGTTTATGGCTTGCTGACCTTGGCGCATTACCGAACCTCGCCGTTGGATTTACGTCGATTATTGGATGCGCCGCGACAACAATTTTATCTTGCGCAGACGCAGGAGGCCTTGTTGGGTTGTGTGTGGGCTGTGCCTGAGGGCGAATTTGGTGACGACGCATTAATTCGTAAAATTCGGCGCGGACAACGTCGTCCACGTGGTAATTTGGTGGCGCAAATGTTGTGTTTTCAGGCGGGATTGGAACAGGCGTGTAAATTGCGTTCACTGCGCATTTCCCGTATCGCCGTGCAACCCAACTGGCAGCAGCGGGGACTGGGGCAACGTTTAATCGAACGAGTTAAACAACAACGTGCGGTGGATTTCCTTTCCGTCAGTTTCGGTTACACCCCCGAGCTGCTGGCGTTTTGGCAAAAGTGCGGTTTTATTTTGGTGCATTTCAGCGAAGGCAAAGATGCAGGCAGCGGCTGTTATTCCGTAGTGGCATTGTGCCCGCTGACGGAGCGCGGACGGGCGTTGGTGCAACAGGCGGAGCAACAATTTAAACGTAATCTGCCCCTTTCGTTGCACCCGCTGGCGACGCAATTTGTCGGAACCGAAACGGATTGGTCGCTCAATGAAACCGATTGGCAATGCTTGGCGGATTTTGCCGATTTCTTCCTGCCGTTGGCGTTTGCCTTGCCCGCTATTCGGCGCTTGATGAAATTAAGCGGGGAGCGGGATTTTCCTTTATTGACAGCCTATTGCAAACGCCCTGATGACATTCAACATAAAAAAACGTGGCTGAAAAATTGTCGGTTGGAAGTGAAGAAAGGGTTGCAAAAAAATTTCGCCTTCTTA","","","72813","MARQLILLVGDDATLARQWEYFPALKSAVWIGGVLPHFSAQLHFPFSKSKNLLGSEFPALIYDGRQGIHLDALAIAAGALSEGGTLLLLFNEWQDLAAQPDGDSLRWSSEKHPINTPHFIAFLQEKIRKYSFPIYQHLPSALVFPKIEKSLSEQHQPTLEQAHLLRQMATSDAEMLIVTAKRGRGKSALAGLFAKQQLAANKPVLLTAPNKSAVKIFNEFSGVEIPFMPPDELRQKVGENPQQFADSWLFVDEAAMIPLDTLFDLTTAFKRIVLTTTIHSYEGTGRGFLLKFMTKTDRTLRHFELFSPLRWQADDKLERFIDELLLCDCEDRLTQPRYDANLAKQIQISYEEQIPPYQIESVYGLLTLAHYRTSPLDLRRLLDAPRQQFYLAQTQEALLGCVWAVPEGEFGDDALIRKIRRGQRRPRGNLVAQMLCFQAGLEQACKLRSLRISRIAVQPNWQQRGLGQRLIERVKQQRAVDFLSVSFGYTPELLAFWQKCGFILVHFSEGKDAGSGCYSVVALCPLTERGRALVQQAEQQFKRNLPLSLHPLATQFVGTETDWSLNETDWQCLADFADFFLPLAFALPAIRRLMKLSGERDFPLLTAYCKRPDDIQHKKTWLKNCRLEVKKGLQKNFAFL","596821","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR000182
Domain
GCN5-related N-acetyltransferase
PF00583\"[390-503]TAcetyltransf_1
PS51186\"[348-527]TGNAT
InterPro
IPR007807
Domain
Protein of unknown function DUF699, ATPase putative
PF05127\"[176-328]TDUF699
noIPR
unintegrated
unintegrated
PTHR10925\"[63-597]TN-ACETYLTRANSFERASE-RELATED
PTHR10925:SF1\"[63-597]Tgb def: Hypothetical protein ypfI


","BeTs to 8 clades of COG1444COG name: Predicted P-loop ATPase fused to an acetyltransferaseFunctional Class: RThe phylogenetic pattern of COG1444 is ao--kzy-------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 350 to 408 match (3e-07) PD:PD332488 which is described as PROTEOME COMPLETE ACETYLTRANSFERASE HEAT TRANSFERASE SHOCK SMALL STY2723 PM1043 YPFI ","","","","","","","","","","","","Wed Dec 18 11:35:57 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00863 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 176 to 328 (E-value = 2.1e-48) place AA00863 in the DUF699 family which is described as Putative ATPase (DUF699) (PF05127)","","","","","","","","1","","","" "AA00864","599443","598745","699","ATGTTAAAAAAATACTTACTTGTTTTACCGATTTCTATTTTAACCGCCTGCGCGGGTTATTATCCTTATCCGCAATTTGAACCCAGTTATCCGTCCTTTTCCGTGCAGCATAATGACGATGAAGAACATGCCGTTTTCAGCATCCGCCGCACGCATGAACCGAAATATCAGGATCCAAGATACAAAATTTCCACGGAAGACATGGAAAAATTCATTTTAGCCAAAAATAACCTGGAATATTGTTTGTTACCGGAATTGGGCAAGCAATCGGATAAACGTGTTACCGCCCTTGAAAAACGGCTATTAAAAGATATGATCAATGACGAGTTGTCGAAGATTGTGGGCAAAGCGTCGGCGCGTACGATTTTTGACGATCAGTCTTCTTACGATTATTTTCAATTTAAGTATCAACAACTCAATCACGGTGTGAATAACATTCGTGAATTTGAATGCCGCGATTTGAAACGGCACTTTCGCGATCGTCTCAACGAACGCAAACGCCGGCAAGGCTTGGCGGGCGACAGTCGTTCTGTTGAAAACCAAGTGCAAAAGCAACGACAAACGATAGACGACGCGTTTCGCCGTTTTCACACGCAACGAGAATCTATTGAACGCCAAATTCGCGGCGAAAGCGAACCGCTCTATAAAAGCAATAAAAATATCAATGTAGACTGGATGGATCCGTATTCGCGGGGTTGG","","","27857","MLKKYLLVLPISILTACAGYYPYPQFEPSYPSFSVQHNDDEEHAVFSIRRTHEPKYQDPRYKISTEDMEKFILAKNNLEYCLLPELGKQSDKRVTALEKRLLKDMINDELSKIVGKASARTIFDDQSSYDYFQFKYQQLNHGVNNIREFECRDLKRHFRDRLNERKRRQGLAGDSRSVENQVQKQRQTIDDAFRRFHTQRESIERQIRGESEPLYKSNKNINVDWMDPYSRGW","598747","","conserved hypothetical protein","Cytoplasm, Outer membrane","","
noIPR
unintegrated
unintegrated
PS51257\"[1-17]TPROKAR_LIPOPROTEIN
signalp\"[1-18]?signal-peptide
tmhmm\"[5-23]?transmembrane_regions


","No hits to the COGs database.","","Residues 1 to 231 match (2e-111) PD:PD313759 which is described as COMPLETE PROTEOME GENES FLP CDS PM1044 ORFA ORFB ORFC ORFD ","","","","","","","","","","","","Wed Dec 18 11:39:22 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00864 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","Inoue,T., Tanimoto,I., Ohta,H., Kato,K., Murayama,Y. and Fukui,K.Molecular characterization of low-molecular-weight componentprotein, Flp, in Actinobacillus actinomycetemcomitans fimbriaeMicrobiol. Immunol. 42 (4), 253-258 (1998)PubMed: 9623911","","Wed Dec 18 11:39:22 2002","","1","","","" "AA00865","600074","599613","462","ATGGGTAAAATGATTATTGATTTACAAATTGCCAGCGCAGATGAAAGTGGCTTGCCGACGGCGGCGCAAATTGAACAATGGGCAACAGCGGCAGTGCAACCGCAAAGCGGGGAAATTGAGATGACCGTACGCATTGTGGACGAGACGGAAAGCCACGCATTAAATCTTAATTATCGTGGCAAAGATCGCCCCACTAATGTGCTGTCTTTCCCTTTTGAATGCCCTGATGAAGTGGAGCTGTCGCTATTGGGCGATTTGGTGATTTGCCGTCAAGTGGTGGAGCGCGAAGCCCAAGAGCAAGACAAACCGCTCATGGCGTATTGGGCACACATGGTGGTGCATGGCGGTTTGCATTTACTCGGTTATGATCATATTGAAGATGACGAAGCGGAGGAAATGGAAAGCTTGGAGACGCAAATTATGATAGGGCTTGGCTTTGTCGATCCGTATCTGAGCGAGAAG","","","17227","MGKMIIDLQIASADESGLPTAAQIEQWATAAVQPQSGEIEMTVRIVDETESHALNLNYRGKDRPTNVLSFPFECPDEVELSLLGDLVICRQVVEREAQEQDKPLMAYWAHMVVHGGLHLLGYDHIEDDEAEEMESLETQIMIGLGFVDPYLSEK","599615","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR002036
Family
Protein of unknown function UPF0054
PD005688\"[54-122]TY004_HAEIN_P71335;
PF02130\"[46-137]TUPF0054
TIGR00043\"[39-145]TTIGR00043: conserved hypothetical protein T
PS01306\"[114-124]TUPF0054
noIPR
unintegrated
unintegrated
G3DSA:3.40.390.30\"[8-153]Tno description


","No hits to the COGs database.","Significant hit ( 7.9e-47) to 2/2 blocks of the IPB002036 family, which is described as \"Uncharacterized protein family UPF0054\". Interpro entry for IP:IPR002036. IPB002036A 40-66 4.3e-16 IPB002036B 83-129 1.6e-29","Residues 38 to 150 match (2e-08) PD:PD085040 which is described as PROTEOME COMPLETE RP741 RC1142 ","","","","","","","","","","","","Wed Dec 18 11:40:57 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00865 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 46 to 137 (E-value = 6.2e-54) place AA00865 in the UPF0054 family which is described as Uncharacterized protein family UPF0054 (PF02130)","","","","Inoue,T., Tanimoto,I., Ohta,H., Kato,K., Murayama,Y. and Fukui,K.Molecular characterization of low-molecular-weight componentprotein, Flp, in Actinobacillus actinomycetemcomitans fimbriaeMicrobiol. Immunol. 42 (4), 253-258 (1998)PubMed: 9623911","","Wed Dec 18 11:40:57 2002","","1","","","" "AA00866","600310","600065","246","TTGAACAAGCAATTTAGCCAAACTTTCACTCTTGAACCGCTAGATAACAAGCGTTTACGTTCTTTATGCGGGGCGGGGGATAAACACCTTTCTTTAATTAAAAAACATTTTGATCTTTCTGTTGCCCGCTGTGGGTTTACCTTTACCGTGCAACTGCGGGGTGAAAATCATCCTATATATTGCTGGAACGTCGTGCAAAGTGCGGTTGGAAATGGCAATGAATTTATGGGAGCAACATGGGTAAAA","","","9253","LNKQFSQTFTLEPLDNKRLRSLCGAGDKHLSLIKKHFDLSVARCGFTFTVQLRGENHPIYCWNVVQSAVGNGNEFMGATWVK","600067","","conserved hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","Residues 11 to 69 match (5e-08) PD:PD131633 which is described as PROTEOME COMPLETE ATP-BINDING PHOH-LIKE PHOH PHOSPHATE NMA1056 PROBABLE PROTEIN YPO2619 ","","","","","","","","","","","","Thu Jan 23 12:12:31 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00866 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00867","600782","601051","270","TTGAATTTTATTTTCTATAAACAACAAAGGAGCATTAAGACAATGTTAAATACTTTAACTACTAAAGCATACATCAAAGCAGCTGAAGCAATCCGTTCTTTCAGAGAAAATCAAGCAGGTGTGACTGCAATTGAATATGGTTTGATCGCTATTGCTGTTGCCGTGTTAATCGTTGCAGTATTCTACAGCAACAATGGTTTTATCGCTAACTTACAAAATAAGTTTAATAGTTTAGCTAGTACCGTCGGAAGTGCAGATGTCGGTAAGAAA","","","9804","LNFIFYKQQRSIKTMLNTLTTKAYIKAAEAIRSFRENQAGVTAIEYGLIAIAVAVLIVAVFYSNNGFIANLQNKFNSLASTVGSADVGKK","601053","","fimbrial protein Flp precursor","Cytoplasm, Extracellular","","
InterPro
IPR007047
Family
Flp/Fap pilin component
PF04964\"[34-83]TFlp_Fap
noIPR
unintegrated
unintegrated
tmhmm\"[43-63]?transmembrane_regions


","No hits to the COGs database.","","Residues 15 to 89 match (9e-22) PD:PD027924 which is described as FIMBRIAL FLP PRECURSOR SIGNAL ASSOCIATED FIMBRIAE COMPLETE FLP-1 PROTEOME PM0855 ","","","","","","","","","","","","Wed Dec 18 11:48:49 2002","","Thu Aug 4 11:46:34 2005","","Thu Aug 4 11:46:34 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA00867 is paralogously related to AA00868 (2e-11).","Thu Aug 4 11:46:34 2005","","","","","Residues 34 to 83 (E-value = 1.4e-22) place AA00867 in the Flp_Fap family which is described as Flp/Fap pilin component (PF04964)","Thu Aug 4 11:46:34 2005","",""," Tomich M, Fine DH, Figurski DH.,The TadV protein of Actinobacillus actinomycetemcomitans is a novel aspartic acid prepilin peptidase required for maturation of the Flp1 pilin and TadE and TadF pseudopilins.J Bacteriol. 2006 Oct;188(19):6899-914.PMID: 16980493Wang Y, Chen C.Mutation analysis of the flp operon in Actinobacillus actinomycetemcomitans.Gene. 2005 May;351:61-71.PMID: 15837433Kachlany,S.C., Planet,P.J., DeSalle,R., Fine,D.H. and Figurski,D.H.Genes for tight adherence of Actinobacillus actinomycetemcomitans:from plaque to plague to pond scumTrends Microbiol. 9 (9), 429-437 (2001)PubMed: 11553455Inoue,T., Tanimoto,I., Ohta,H., Kato,K., Murayama,Y. and Fukui,K.Molecular characterization of low-molecular-weight componentprotein, Flp, in Actinobacillus actinomycetemcomitans fimbriaeMicrobiol. Immunol. 42 (4), 253-258 (1998)PubMed: 9623911","","Thu Aug 4 11:54:52 2005","","1","","3","" "AA00868","601137","601376","240","TTGAAATTAATTATGATGGATTTACTGGATTACTTTTATCATCAAGTAGTCTTTTCTTCGTATAGGTTTTACAGAAATCGACAAGGGATTACTTCTGTTGAGTATGGGTTAATTGCTGTGGCTATTGCTGTTTTTGTAGTCGCCGTTTTAGTCGGGGATAACAGCTTTATTAAGGCAGTGTCAGGTAAGTTCTCGGATTTAACGACCACTGTCACTGACGCCATAGTTAGCAAAAGTAGC","","","10145","LKLIMMDLLDYFYHQVVFSSYRFYRNRQGITSVEYGLIAVAIAVFVVAVLVGDNSFIKAVSGKFSDLTTTVTDAIVSKSS","","","possible fimbril subunit","Cytoplasm, Inner membrane","","
InterPro
IPR007047
Family
Flp/Fap pilin component
PF04964\"[23-72]TFlp_Fap
noIPR
unintegrated
unintegrated
tmhmm\"[35-57]?transmembrane_regions


","No hits to the COGs database.","","Residues 5 to 80 match (1e-17) PD:PD027281 which is described as FLP-2 GENES FLP COMPLETE CDS ORF-2 ORFA ORFB ORFC ORFD ","Wed Nov 20 11:18:34 2002","","","Wed Nov 20 11:18:34 2002","Wed Nov 20 11:18:43 2002","","","Wed Nov 20 11:18:43 2002","Wed Nov 20 11:18:43 2002","Wed Nov 20 11:18:34 2002","Wed Nov 20 11:18:34 2002","Fri Feb 7 15:26:00 2003","","Thu Aug 4 11:55:19 2005","","Thu Aug 4 11:55:19 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA00868 is paralogously related to AA00867 (2e-11).","Thu Aug 4 11:55:19 2005","","","","","Residues 23 to 72 (E-value = 9.8e-21) place AA00868 in the Flp_Fap family which is described as Flp/Fap pilin component (PF04964)","Thu Aug 4 11:55:19 2005","",""," Perez BA, Planet PJ, Kachlany SC, Tomich M, Fine DH, Figurski DH.,Genetic analysis of the requirement for flp-2, tadV, and rcpB in Actinobacillus actinomycetemcomitans biofilm formation.J Bacteriol. 2006 Sep;188(17):6361-75.PMID: 16923904 Kachlany,S.C., Planet,P.J., Desalle,R., Fine,D.H., Figurski,D.H.and Kaplan,J.Bflp-1, the first representative of a new pilin gene subfamily, isrequired for non-specific adherence of Actinobacillus actinomycetemcomitansMol. Microbiol. 40 (3), 542-554 (2001)PubMed: 11359562Kachlany,S.C., Planet,P.J., DeSalle,R., Fine,D.H. and Figurski,D.H.Genes for tight adherence of Actinobacillus actinomycetemcomitans: from plaque to plague to pond scumTrends Microbiol. 9 (9), 429-437 (2001)PubMed: 11553455Inoue,T., Tanimoto,I., Ohta,H., Kato,K., Murayama,Y. and Fukui,K.Molecular characterization of low-molecular-weight componentprotein, Flp, in Actinobacillus actinomycetemcomitans fimbriaeMicrobiol. Immunol. 42 (4), 253-258 (1998)PubMed: 9623911Wang Y, Chen C.Mutation analysis of the flp operon in Actinobacillus actinomycetemcomitans.Gene. 2005 May;351:61-71.PMID: 15837433","","Thu Aug 4 11:55:19 2005","","1","","3","" "AA00869","601395","601820","426","ATGAACTGGCTTATTAACGCTTTAGTAATCATAACGCTCTCGCTGCTGGTTACTTTATCTATAACTGACATTCGTTTTCGGCTTATTAGTAACCGAATTGTTTTGTTTCTGTTATTCGTCATTATTCCGTTCAGTTTATTAAAATATCAGGCTATCTTTGTTATTCCCGCCTTATGTACACTTATTATCGGGTTTTTACTGTTTTCTCTGCACTTCATAGGTGCAGGAGATATTAAGCTTGCTTCGGTGCTAATGTTAGCCGTTCCAAGTGAGGAAATTTTTTCTTTTTTCTTCTTTACAACATTTGCCGGATTGGGACTAATTATTATCGGTTGGTTATTTTTCCGTAAATCAATTAAAGAAAACGGATTGCCTTATGGCGTAGCAATAAGCCTTGGCTTTATGATAAACATGGCTCTATCAAAT","","","15866","MNWLINALVIITLSLLVTLSITDIRFRLISNRIVLFLLFVIIPFSLLKYQAIFVIPALCTLIIGFLLFSLHFIGAGDIKLASVLMLAVPSEEIFSFFFFTTFAGLGLIIIGWLFFRKSIKENGLPYGVAISLGFMINMALSN","601822","","tight adherence protein V; prepilin peptidase","Inner membrane, Cytoplasm","","
InterPro
IPR000045
Domain
Peptidase A24A, prepilin type IV
PF01478\"[10-109]TPeptidase_A24
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide
tmhmm\"[5-25]?\"[29-47]?\"[52-74]?\"[93-113]?\"[123-141]?transmembrane_regions


","No hits to the COGs database.","","Residues 23 to 140 match (3e-34) PD:PD074575 which is described as COMPLETE PROTEOME TRANSMEMBRANE PREPILIN PEPTIDASE ASSEMBLY TYPE PILUS CPAA PROBABLE ","","","","","","","","","","","","Fri Feb 7 15:19:26 2003","","Thu Aug 4 12:02:06 2005","","Thu Aug 4 12:02:06 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA00869 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Aug 4 12:02:06 2005","","","","","Residues 10 to 109 (E-value = 1.3e-15) place AA00869 in the Peptidase_A24 family which is described as Type IV leader peptidase family (PF01478)","Thu Aug 4 12:02:06 2005","",""," Perez BA, Planet PJ, Kachlany SC, Tomich M, Fine DH, Figurski DH.,Genetic analysis of the requirement for flp-2, tadV, and rcpB in Actinobacillus actinomycetemcomitans biofilm formation.J Bacteriol. 2006 Sep;188(17):6361-75.PMID: 16923904 Tomich M, Fine DH, Figurski DH.,The TadV protein of Actinobacillus actinomycetemcomitans is a novel aspartic acid prepilin peptidase required for maturation of the Flp1 pilin and TadE and TadF pseudopilins.J Bacteriol. 2006 Oct;188(19):6899-914.PMID: 16980493Wang Y, Chen C.Mutation analysis of the flp operon in Actinobacillus actinomycetemcomitans.Gene. 2005 May;351:61-71.PMID: 15837433Kachlany,S.C., Planet,P.J., DeSalle,R., Fine,D.H. and Figurski,D.H.Genes for tight adherence of Actinobacillus actinomycetemcomitans:from plaque to plague to pond scumTrends Microbiol. 9 (9), 429-437 (2001)PubMed: 11553455Inoue,T., Tanimoto,I., Ohta,H., Kato,K., Murayama,Y. and Fukui,K.Molecular characterization of low-molecular-weight componentprotein, Flp, in Actinobacillus actinomycetemcomitans fimbriaeMicrobiol. Immunol. 42 (4), 253-258 (1998)PubMed: 9623911","","Thu Aug 4 12:02:06 2005","","1","","3","" "AA00870","601875","602696","822","ATGAATTACAGAACGCTCTTGATCATTTCAGTGCTTACGCTAGCGGTTGGCATTGGTGGCATTATGTTTATGCCAGCATTTGACAATACTGAAAATCAACAAACAATAATAATAAATAATCAGTCGGTTCCGGAAACTGAGAAAAAGCCGGAAAAGCTAATTTTAACTGCCGAATTAAAGAATGACGTGAGCAAAGGTCATTTATTACAGGCAGATGATTACATTTTAAATGAGATTTCTGTCCCTGAAGACAGTGCACTGGTCGACAATGACCTAAGAGAGGCTACGACTAAAAATGGTATTCAGGGATTACAAGGCTATTTAATGGCAGAAAATGTCAGAGCTGGTTCTTTTCTATCCAACAAATCTATTATCTCTCCGAATGATCCTAGATTCTTTACTTCCAGCTTGAATCCAAGTCAAGAAGTCGCATATCGCATCTATGTTAGATCTGGCGATGATTACATTCTAAATACTATTTTAAGCGGAGACTATGTATCTGTTTATAGCCAGCAAACCGCTTCAGATTCCCGCAATACTTATGATCGTAAAGATTTAGTTAAAGTTTTAGGTAAGGCAGTGGTTCTACAAGCACGGAATTTTGCTCAAGTAGCAGAACAAGGCACTGAAACTGAGAAAGCGTTAGGTCTGGCTCCAAATAGTGAAGTATATGCCGGTTATGTAGCATTAAAAATAACTGCTGAACAAGCTAAAAAATTCTATTCACTGGATAGAGAATCGAAGTTAGTCATATTACCTGTCGAAAATAATACTCAAGAAGTTGATTCACGCGGTGTATTCATCAGAAAATTAAGAGGTCAA","","","30379","MNYRTLLIISVLTLAVGIGGIMFMPAFDNTENQQTIIINNQSVPETEKKPEKLILTAELKNDVSKGHLLQADDYILNEISVPEDSALVDNDLREATTKNGIQGLQGYLMAENVRAGSFLSNKSIISPNDPRFFTSSLNPSQEVAYRIYVRSGDDYILNTILSGDYVSVYSQQTASDSRNTYDRKDLVKVLGKAVVLQARNFAQVAEQGTETEKALGLAPNSEVYAGYVALKITAEQAKKFYSLDRESKLVILPVENNTQEVDSRGVFIRKLRGQ","602698","","rough colony protein C","Outer membrane, Periplasm","","
InterPro
IPR002048
Domain
Calcium-binding EF-hand
PS00018\"[62-74]?EF_HAND_1
noIPR
unintegrated
unintegrated
signalp\"[1-20]?signal-peptide
tmhmm\"[5-27]?transmembrane_regions


","No hits to the COGs database.","","Residues 1 to 273 match (5e-125) PD:PD317096 which is described as PROTEOME COMPLETE PM0853 MEMBRANE RCPC ORFC ","","","","","","","","","","","","Wed Dec 18 11:54:21 2002","","Thu Aug 4 12:02:28 2005","","Thu Aug 4 12:02:28 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA00870 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Aug 4 12:02:28 2005","","","","","","","","","Haase,E.M., Zmuda,J.L. and Scannapieco,F.A.Identification and molecular analysis of rough-colony-specificouter membrane proteins of Actinobacillus actinomycetemcomitansInfect. Immun. 67 (6), 2901-2908 (1999)PubMed: 99270950Kachlany,S.C., Planet,P.J., DeSalle,R., Fine,D.H. and Figurski,D.H.Genes for tight adherence of Actinobacillus actinomycetemcomitans:from plaque to plague to pond scumTrends Microbiol. 9 (9), 429-437 (2001)PubMed: 11553455Wang Y, Chen C.Mutation analysis of the flp operon in Actinobacillus actinomycetemcomitans.Gene. 2005 May;351:61-71.PMID: 15837433","Nika,J.R., Latimer,J.L., Ward,C.K., Blick,R.J., Wagner,N.J., Cope,L.D., Mahairas,G.G., Munson,R.S. Jr. and Hansen,E.J. Haemophilus ducreyi requires the flp gene cluster for microcolony formation in vitro Infect. Immun. 70 (6), 2965-2975 (2002) PubMed: 12010986 ","Thu Aug 4 12:02:28 2005","Fri Jan 24 12:52:30 2003","1","","3","" "AA00871","602701","604080","1380","ATGCAAAATTGGAATCATACTTTTGGCAAAAAACAATTGATATGCTGTGCAGTTCTCGGAGCAATGTTCTCATTAAATGCGTACGCACAAAATTTCTCTCTGGATAAAGGTGCAACCCAGTTGGTTCAAACAAAAGAAAAGATCGACACTATTTTCGTCTCTTCACCAAATATTGCCGACTATGAAATTTTAGACGACAACACCTTTATTATCTACGCAAAGGAGGAAGGTAGAACAGAAGTTACTGCTTTCGGAGCAGATGGTCGGCCTTTGACGTCTGATACCGTTAATGTTGATTCTGTTGTCACCAGCATTGCAGATACGAATAAACAACTGAAGAGCCATTTTCCAAATACTAATCTATCTGTGAAGAAAGTAGGTAAGGCCTATGTAATTGAAGGTAAAGCTCGTTCACAAGAAGAAAGCGATGAAGTTCGTAGAATTGTAGGAGAAGCTTTAGGAAACGGTCGAAAGGTTACTGAAACAAAGTTAGGGGAAGATGCTTTACCGTTCTTAGACAAATACCATTACGATGGTGTTGTTGATAACGCAAATATTGCAGACACAACCCAAATTAATGTGAAGCTTTCTGTTGTAGAGGTAAATAAGAAACTTTCTGAGGCGATGGGTATTAACTGGAGTCACGTTGCCGGTAGTGGTCCATTAGTCGGAGGTAACTTCGGTTTCGGAGGTGGATTCAATGGAAATCAAGGTGTATTACGTTTAGACGCAAAAGGTATTTCTGCGTTTATTAATGCCTTAGATAACCAAAGTAATGGTAAGGTTCTGGCCGAACCGAACATTTCTATGTTATCAGGTGAAACTGCCGATATCTTAGTGGGAGGTGAAATCCCATTTGCACAACGAGATAAAGATGGTTCGCCAACAATTATATATAAGGAGTTTGGGATAAAGCTCGCTGTTGCTGCCAAATTGCAAAAAAATAATCGTATTCGTTTAGCCTTAGATCAATCAGTAAGCACCATAGCTGGTAACTATAACTTTGAGGGAGTCGGGAATATTCCGTTCTTTAATACCCGTAAAGCAAAGTCTTTATTTGAAGTAGCTAACGGAGAAAGTTTTATTATCGGTGGCTTATTCAGCTCAAATGACCTTGAAGGTATAAACAAAGTTCCTCTTTTAGGAGACATCCCAATTTTAGGTTCTTTCTTCCGTAATGCAACAACTGAGCGCGATAAAAAAGAGTTAGTTATCGTAGCAACAGTAAATGTAGTAAAACCGGTAAATGAAAAAGATGTTGTTTACCCTGATTTTGAAAAAACCGGAACAATGGAAAGATTCTTCCATACGACTCCGTTAAAGAATGTTTATTACAAGACATTAATATCTAACTTCTTAAAGAATAGTGGGTTCATACAA","","","50123","MQNWNHTFGKKQLICCAVLGAMFSLNAYAQNFSLDKGATQLVQTKEKIDTIFVSSPNIADYEILDDNTFIIYAKEEGRTEVTAFGADGRPLTSDTVNVDSVVTSIADTNKQLKSHFPNTNLSVKKVGKAYVIEGKARSQEESDEVRRIVGEALGNGRKVTETKLGEDALPFLDKYHYDGVVDNANIADTTQINVKLSVVEVNKKLSEAMGINWSHVAGSGPLVGGNFGFGGGFNGNQGVLRLDAKGISAFINALDNQSNGKVLAEPNISMLSGETADILVGGEIPFAQRDKDGSPTIIYKEFGIKLAVAAKLQKNNRIRLALDQSVSTIAGNYNFEGVGNIPFFNTRKAKSLFEVANGESFIIGGLFSSNDLEGINKVPLLGDIPILGSFFRNATTERDKKELVIVATVNVVKPVNEKDVVYPDFEKTGTMERFFHTTPLKNVYYKTLISNFLKNSGFIQ","604082","","rough colony protein A","Outer membrane, Cytoplasm","","
InterPro
IPR001775
Domain
Bacterial general secretion pathway protein D
PR00811\"[191-201]T\"[249-273]T\"[377-395]T\"[400-414]TBCTERIALGSPD
InterPro
IPR004846
Domain
Bacterial type II and III secretion system protein
PF00263\"[193-413]TSecretin
noIPR
unintegrated
unintegrated
signalp\"[1-29]?signal-peptide
tmhmm\"[12-32]?transmembrane_regions


","BeTs to 12 clades of COG1450COG name: General secretory pathway protein DFunctional Class: NThe phylogenetic pattern of COG1450 is -------qvd---cefghsnuj-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.7e-39) to 3/3 blocks of the IPB000016 family, which is described as \"General (type II) secretion pathway (GSP) D protein\". Interpro entry for IP:IPR000016. IPB000016A 182-213 0.00028 IPB000016B 251-286 6.5e-14 IPB000016C 351-392 2.1e-18","Residues 345 to 412 match (6e-09) PD:PD001316 which is described as SECRETION PROTEOME COMPLETE D GENERAL PATHWAY SIGNAL PRECURSOR MEMBRANE OUTER ","","","","","","","","","","","","Wed Dec 18 11:55:55 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00871 is paralogously related to AA01297 (2e-18).","","","","","","Residues 193 to 413 (E-value = 1.3e-65) place AA00871 in the Secretin_C family which is described as Bacterial type II and III secretion system protein (PF00263)","","","","Haase,E.M., Zmuda,J.L. and Scannapieco,F.A. Identification and Molecular Analysis of Rough-Colony-Specific Outer Membrane Proteins of Actinobacillus actinomycetemcomitans Infect. Immun. 67 (6), 2901-2908 (1999) PMID: 10338497Kachlany,S.C., Planet,P.J., DeSalle,R., Fine,D.H. and Figurski,D.H.Genes for tight adherence of Actinobacillus actinomycetemcomitans:from plaque to plague to pond scumTrends Microbiol. 9 (9), 429-437 (2001)PubMed: 21438116","Nika,J.R., Latimer,J.L., Ward,C.K., Blick,R.J., Wagner,N.J., Cope,L.D., Mahairas,G.G., Munson,R.S. Jr. and Hansen,E.J. Haemophilus ducreyi requires the flp gene cluster for microcolony formation in vitro Infect. Immun. 70 (6), 2965-2975 (2002) PubMed: 12010986 ","Fri Feb 7 15:08:53 2003","Fri Jan 24 12:51:57 2003","1","","3","" "AA00872","604080","604580","501","ATGAGAAAATTAGTTATTACGGCCTCCATTGCATTGGCCTCAATTATCGTTCCGGCAAAAACATTTGCAATCAATGAATTTGTTGACGATACGACTGTTGCACAACCGGTACAAAATAGTGAATTTAATCGTACACAGTTAGTCAATCGTTATGTATTACCGGATTATTCTAATGTCAGTTATAGTAATTTATTCAATTCTGTCATTCGTGATATAGGTAGTAACAACCAAAAACAAATCAATATCATTTGGCGTGATGCTACGGCAAAGAAAGCCGCAATGGAAATTCGTACAAAATTGATTAAAAATGGTATCGCCTCTAAATCCATTTACTTAGAGAAAAAAGCACATAAAGCAAAAATATATCCAATCTATATTGAAGTAGCTCAAATTGCGCAGAGACCGGCGCCTTGTGCATATCGTACCGGAGAAGTAGTTTTTTGGAATTCTAATGAGACTTCTTGTGCACTTAAAAGTAATCAGCGTGTTCAATTGAAGTAT","","","18871","MRKLVITASIALASIIVPAKTFAINEFVDDTTVAQPVQNSEFNRTQLVNRYVLPDYSNVSYSNLFNSVIRDIGSNNQKQINIIWRDATAKKAAMEIRTKLIKNGIASKSIYLEKKAHKAKIYPIYIEVAQIAQRPAPCAYRTGEVVFWNSNETSCALKSNQRVQLKY","604582","","rough colony protein B","Periplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-23]?signal-peptide


","No hits to the COGs database.","","Residues 1 to 167 match (2e-75) PD:PD304766 which is described as B ROUGH PROTEOME COLONY COMPLETE RCPB ","","","","","","","","","","","","Wed Dec 18 11:58:51 2002","","Thu Aug 4 12:02:49 2005","","Thu Aug 4 12:02:49 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA00872 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Aug 4 12:02:49 2005","","","","","","","",""," Perez BA, Planet PJ, Kachlany SC, Tomich M, Fine DH, Figurski DH.,Genetic analysis of the requirement for flp-2, tadV, and rcpB in Actinobacillus actinomycetemcomitans biofilm formation.J Bacteriol. 2006 Sep;188(17):6361-75.PMID: 16923904Wang Y, Chen C.Mutation analysis of the flp operon in Actinobacillus actinomycetemcomitans.Gene. 2005 May;351:61-71.PMID: 15837433Kachlany,S.C., Planet,P.J., DeSalle,R., Fine,D.H. and Figurski,D.H.Genes for tight adherence of Actinobacillus actinomycetemcomitans:from plaque to plague to pond scumTrends Microbiol. 9 (9), 429-437 (2001)PubMed: 21438116Haase,E.M., Zmuda,J.L. and Scannapieco,F.A.Identification and molecular analysis of rough-colony-specificouter membrane proteins of Actinobacillus actinomycetemcomitansInfect. Immun. 67 (6), 2901-2908 (1999)PubMed: 10338497Inoue,T., Tanimoto,I., Ohta,H., Kato,K., Murayama,Y. and Fukui,K.Molecular characterization of low-molecular-weight component protein,Flp, in Actinobacillus actinomycetemcomitans fimbriae. Microbiol.Immunol. 42(4): 253-258.1998.PubMed: 9623911","ika,J.R., Latimer,J.L., Ward,C.K., Blick,R.J., Wagner,N.J., Cope,L.D., Mahairas,G.G., Munson,R.S. Jr. and Hansen,E.J. Haemophilus ducreyi requires the flp gene cluster for microcolony formation in vitro Infect. Immun. 70 (6), 2965-2975 (2002) PubMed: 12010986 ","Thu Aug 4 12:02:49 2005","Wed Dec 18 11:58:51 2002","1","","3","" "AA00873","604599","605720","1122","ATGTTATTACTAGATCAAGAAACAATCACGGCAGACAGTGCACGTACTATTACTGTAGTATCAAGCCGTGATGATATTCAAGGTGAAGTTGCACAAACTCTACGTACTCGCGGTCTTGAAAATATTGAGATTGTTAAAAAGGATTTTTTTACCTCGTCTGATGAGATTTCATTTTCAGCAGAAGATACTGTAGGGATTATTATTGATATCACACATGAAACTAATATAAAGACTATTGTCGAACGAGTTTTTAGTGTAGTACCACAAAATGTATGGTGTTGTGTTATCGGTGATAGTGACTCAATCTCTTTATCACAAAAACTACTAGATGAGGGTATCCTTTACTTTAATTCGCATACCCAATTAAGTCAGATGGTTGAGAAAATCATTTTAGGTGTTGATATACCTCGTTTAAGAGATACTGTTAAAATTGCTGTATTAAGTTGTAAGGGCGGTATTGGCGCAAGTTTAATTAGTTCACATATTGCTAATGAGATTGTATCAAGTAAAAAAATTCCGGTGCTATTAGCCCAAGGTCCTAATGGTTCCCAGGATTTAGATTTATTATTTGATAAAAAGCTATCAGGTAATGTTATTGAATATGCTCCTAATTTAGATATATTTAACGGGAGCTTATTTGAGCTAACACCCGCAGCGACTGAAAAATACAATTTTATTATCTACGATCAACCTATCTATAACGTCAAAAAGGATAATTTCATTAGTTTTTTAGAAAACTATAATAATTTCGTATTAGTTGTAGAAAGAAAAATCGGTTCTCTACGTTTAGCTAAACAGTTTCTAGATGAATGTGAGCGTATTCGCAGTACTTCGAGAAAACCAATTCGCACTTTTGTATGTATTTCTGATAATCGGTTAGAAGCAGCTAAGTTAATGGCTAAGAATGATATCGAAACCTTAATCGGTTCTTCAATAGATGCCATAATTCCTTTTGTTAAAAATACTAATACAAAAACTGTATTGGGCATTAACTTAGGTCGTGATGGGAAAAAGGAAATTAATTCACTAATGTTAAAGGTTATTGGTGCAATATCTCGCAGTAGTAAGCCAAAAGAAAAACAAAGTTTATTTTCCTCATTTTTTACAAAACTCATTAAACAA","","","41605","MLLLDQETITADSARTITVVSSRDDIQGEVAQTLRTRGLENIEIVKKDFFTSSDEISFSAEDTVGIIIDITHETNIKTIVERVFSVVPQNVWCCVIGDSDSISLSQKLLDEGILYFNSHTQLSQMVEKIILGVDIPRLRDTVKIAVLSCKGGIGASLISSHIANEIVSSKKIPVLLAQGPNGSQDLDLLFDKKLSGNVIEYAPNLDIFNGSLFELTPAATEKYNFIIYDQPIYNVKKDNFISFLENYNNFVLVVERKIGSLRLAKQFLDECERIRSTSRKPIRTFVCISDNRLEAAKLMAKNDIETLIGSSIDAIIPFVKNTNTKTVLGINLGRDGKKEINSLMLKVIGAISRSSKPKEKQSLFSSFFTKLIKQ","605722","","Tadz protein","Outer membrane, Cytoplasm","","No hits reported.","BeTs to 4 clades of COG0455COG name: ATPases involved in chromosome partitioningFunctional Class: DThe phylogenetic pattern of COG0455 is aom-k--qv-r-b--fg---u---t-Number of proteins in this genome belonging to this COG is","","Residues 320 to 366 match (1e-09) PD:PD401805 which is described as PM0850 PROTEOME COMPLETE ","","","","","","","","","","","","Fri Feb 7 14:00:12 2003","","Thu Aug 4 12:03:20 2005","","Thu Aug 4 12:03:20 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA00873 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Aug 4 12:03:20 2005","","","","","","","","","Kachlany SC, Planet PJ, DeSalle R, Fine DH, Figurski DH.Genes for tight adherence of Actinobacillus actinomycetemcomitans: from plaque to plague to pond scum.Trends Microbiol. 2001 Sep;9(9):429-37.PMID: 11553455Wang Y, Chen C.Mutation analysis of the flp operon in Actinobacillus actinomycetemcomitans.Gene. 2005 May;351:61-71.PMID: 15837433","","Thu Aug 4 12:03:20 2005","","1","","3","" "AA00874","605737","607014","1278","ATGCTGACCAAACAACAAAAAATCTTACTTAGAAGTGAAGTATTGAGCAATCTTGATGTTGAAAAGATTGATGAACTTCAAAGTGAAAGAAACTCATTAGTAAACGAACTGGTTCAGATTGTTAATCGTATTGCCAATAAAAGTAACACTTATTTGACGTCATCCGATGCACTGGTTATGGCTGAAATTGTTGCTGATGAGATTGAGGGTTATGGTCCGTTACGGGATCTCGTGGCTGACGATACTATAAATGATATCTTAGTTAATGGCCCTAATGATATCTGGGTTGAACGTGCCGGTATTCTGGAAAAAACTGATAAAGAATTCGTTAGTAATGAACAATTAACTGATATTGCAAAAAGGTTAGTTGCTCGGGTTGGTCGTCGTATTGATGATGGTAGTCCACTAGTGGACTCCCGACTACCCGATGGTAGCCGTTTAAATGTTGTAATTGCACCGATTGCGTTAGATGGTACATCCATTTCCATTCGTAAGTTCAGTAAGAGTAAAAAAAGCTTGCAAGAGCTTGTAAATTTCGGTTCTATGACCCGCGATATGGCAAATTTTTTAATTATCGCTGCCAGATCTCGAGTAAATATAATTGTGTCAGGTGGTACAGGATCCGGTAAAACAACTCTCCTTAATGCGCTATCTAATTATATTTCCCATACCGAACGTGTCATCACATTAGAAGATACTGCTGAATTGCGTTTGGAACAACCTCATGTTGTACGCCTTGAAACACGTTTAGCCGGCGTTGAGCATACAGGCGAGGTTACTATGCAGGATTTAGTAATAAATGCACTACGTATGCGTCCTGAGCGTATTATCGTAGGTGAATGCCGTGGTGGAGAAGCATTCCAGATGTTACAAGCGATGAACACTGGTCACGATGGTTCTATGTCAACGTTGCACGCAAATACCCCTCGGGATGCAACATCTCGATTGGAGAGTATGGTTATGATGTCGAATGCGTCCCTACCGTTGGAAGCAATTCGCCGTAATATTGCATCTGCAGTAAATATCATCGTACAAGCCTCCCGTTTAAATGATGGAACAAGAAAAATCATGAATATTACTGAAATAATGGGTATGGAAAATGGGCAAATTGTTTTACAAGATATTTTTTCTTATAAGGCAAGTAAGTACCGTGATAAAGATGGCAAAATTATTGGTGAATTTGTTAACCATGGTTTATTAACTCGCTCTGCTGTTTTCCAAAATGCTCAAGTATTTAATCTGAGTACTGAGTTACAAAGTATTTTCGGAGAAGCTGAG","","","47080","MLTKQQKILLRSEVLSNLDVEKIDELQSERNSLVNELVQIVNRIANKSNTYLTSSDALVMAEIVADEIEGYGPLRDLVADDTINDILVNGPNDIWVERAGILEKTDKEFVSNEQLTDIAKRLVARVGRRIDDGSPLVDSRLPDGSRLNVVIAPIALDGTSISIRKFSKSKKSLQELVNFGSMTRDMANFLIIAARSRVNIIVSGGTGSGKTTLLNALSNYISHTERVITLEDTAELRLEQPHVVRLETRLAGVEHTGEVTMQDLVINALRMRPERIIVGECRGGEAFQMLQAMNTGHDGSMSTLHANTPRDATSRLESMVMMSNASLPLEAIRRNIASAVNIIVQASRLNDGTRKIMNITEIMGMENGQIVLQDIFSYKASKYRDKDGKIIGEFVNHGLLTRSAVFQNAQVFNLSTELQSIFGEAE","607016","","tight adherence protein A","Cytoplasm","","
InterPro
IPR000217
Family
Tubulin
PS00227\"[203-209]?TUBULIN
InterPro
IPR001482
Domain
Bacterial type II secretion system protein E
PD000739\"[175-274]TQ7X0L8_ACTAC_Q7X0L8;
PF00437\"[60-350]TGSPII_E
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[162-360]Tno description


","No hits to the COGs database.","Significant hit ( 1e-40) to 5/5 blocks of the IPB001482 family, which is described as \"Bacterial type II secretion system protein E\". Interpro entry for IP:IPR001482. IPB001482A 104-126 10 IPB001482B 196-218 1.6e-10 IPB001482C 226-236 0.048 IPB001482D 265-309 4.8e-23 IPB001482E 398-407 66","Residues 80 to 158 match (6e-17) PD:PD274147 which is described as PLASMID TRBB COMPLETE TRANSFER CONJUGAL PROTEOME ATP-BINDING PROBABLE CONJUGATION PROTEIN ","","","","","","","","","","","","Wed Dec 18 12:04:47 2002","","Thu Aug 4 12:05:27 2005","Thu Aug 4 12:05:27 2005","Thu Aug 4 12:05:27 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA00874 is paralogously related to AA00161 (2e-10).","Thu Aug 4 12:05:27 2005","","","","","Residues 60 to 350 (E-value = 2.5e-97) place AA00874 in the GSPII_E family which is described as Type II/IV secretion system protein (PF00437)","Thu Aug 4 12:05:27 2005","","","Bhattacharjee MK, Kachlany SC, Fine DH, Figurski DH. Nonspecific adherence and fibril biogenesis by Actinobacillusactinomycetemcomitans: TadA protein is an ATPase. J Bacteriol. 2001 Oct;183(20):5927-36. PMID: 11566992 Kachlany SC, Planet PJ, DeSalle R, Fine DH, Figurski DH. Genes for tight adherence of Actinobacillus actinomycetemcomitans: from plaque to plague to pond scum. Trends Microbiol. 2001 Sep;9(9):429-37. Review. PMID: 11553455Kachlany,S.C., Planet,P.J., Bhattacharjee,M.K., Kollia,E., DeSalle,R., Fine,D.H. and Figurski,D.H.Nonspecific adherence by Actinobacillus actinomycetemcomitans requires genes widespread in bacteria and archaeaJ. Bacteriol. 182 (21), 6169-6176 (2000)PubMed: 11029439Planet PJ, Kachlany SC, DeSalle R, Figurski DH.Phylogeny of genes for secretion NTPases: identification of the widespread tadA subfamily and development of a diagnostic key for gene classification.Proc Natl Acad Sci U S A. 2001 Feb;98(5):2503-8.PMID: 11226268Wang Y, Chen C.Mutation analysis of the flp operon in Actinobacillus actinomycetemcomitans.Gene. 2005 May;351:61-71.PMID: 15837433","Nika,J.R., Latimer,J.L., Ward,C.K., Blick,R.J., Wagner,N.J., Cope,L.D., Mahairas,G.G., Munson,R.S. Jr. and Hansen,E.J. Haemophilus ducreyi requires the flp gene cluster for microcolony formation in vitro Infect. Immun. 70 (6), 2965-2975 (2002) PubMed: 12010986 ","Thu Aug 4 12:05:27 2005","Wed Dec 18 12:04:47 2002","1","","3","" "AA00875","607017","607901","885","ATGAGCCATTATTTATATTATGCCGTCCTTACAATAGGTGGACTATTATTTATATATACCTTAAGTAGTTGGTTTTCTACTAAAAGAAAAATTAATGAGTATGATACCTCTATAAGTAGGACAACAAGTTTTTTTAAGAACCTCAAATCAAAAGTTAGTTTATGGTATTATCACTTTACTAAAGGTGATAAAAAAAACTTAGTTCGTAATATTGTTATAAGTTGTTTTATTTTCTTTGCTTTTTTTGTAATTAATGTTGCTTATATTCATATTGACCGATTAGTGTTTTGCTTAATTTTTCTTGTTGGATTTGTTTTGTTTATTTGGAAACTTGGTCAGTACCGTAATAAAAAAACATTCAACGCAATGTTTCCAGAGGTAATTCAGATTCTCAATGCTGCAGCAACTTCTAGCGTAGGCTTATTACAGGCATTGGAACGTTGCGGTAAGGATCTAACAGGTCAATTAGGCGAGGAGTTCAAAAGTATTCATAGACGCCTCTCTATAGGGGAGGACCCCGCTACAGTTTTTGACGATAGCTATGATCGTTACCCATATAAGGAGTTTTACTTTTTCATAACTATTGTACGCACTAATTTAAACAAAGGTGGACAGATACGGGAGGTTATTTCTCGTTTAGGTCGCGTAATTGCGGATAGCAATAAAATGGAAAAGAAAAAGAAAGCAATGACATCAGAGGCCAGAATGTCAGCTATAATCGTAGCATGTTTTCCGGTCGGTTTCTTTTTCTTTATGCAGTTTGCTATGCCGGAAAACTTTGATTTCTTAATTAATGACCCTACCGGTAGATACGTGCTTTATTATGTTTTTGGTAGTGAGCTTTTCGGTATGGGAATTATTTGGTGGTTGATGAGGAAGTCAACA","","","34498","MSHYLYYAVLTIGGLLFIYTLSSWFSTKRKINEYDTSISRTTSFFKNLKSKVSLWYYHFTKGDKKNLVRNIVISCFIFFAFFVINVAYIHIDRLVFCLIFLVGFVLFIWKLGQYRNKKTFNAMFPEVIQILNAAATSSVGLLQALERCGKDLTGQLGEEFKSIHRRLSIGEDPATVFDDSYDRYPYKEFYFFITIVRTNLNKGGQIREVISRLGRVIADSNKMEKKKKAMTSEARMSAIIVACFPVGFFFFMQFAMPENFDFLINDPTGRYVLYYVFGSELFGMGIIWWLMRKST","607903","","tight adherence protein B","Inner membrane, Cytoplasm","","
InterPro
IPR001992
Family
Bacterial type II secretion system protein
PF00482\"[127-254]TGSPII_F
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide
tmhmm\"[4-24]?\"[65-85]?\"[91-109]?\"[237-257]?\"[271-291]?transmembrane_regions


","BeTs to 5 clades of COG2064COG name: Predicted membrane proteinFunctional Class: SThe phylogenetic pattern of COG2064 is aompkz---------f-h---j----Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Wed Dec 18 12:06:55 2002","","Thu Aug 4 12:07:28 2005","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00875 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Aug 4 12:07:28 2005","","","","","Residues 125 to 254 (E-value = 4.7e-22) place AA00875 in the GSPII_F family which is described as Bacterial type II secretion system protein F domain (PF00482)","Thu Aug 4 12:07:28 2005","","","Kachlany SC, Planet PJ, DeSalle R, Fine DH, Figurski DH. Genes for tight adherence of Actinobacillus actinomycetemcomitans: from plaque to plague to pond scum. Trends Microbiol. 2001 Sep;9(9):429-37. Review. PMID: 11553455Kachlany,S.C., Planet,P.J., Bhattacharjee,M.K., Kollia,E.,DeSalle,R., Fine,D.H. and Figurski,D.H.Nonspecific adherence by Actinobacillus actinomycetemcomitansrequires genes widespread in bacteria and archaeaJ. Bacteriol. 182 (21), 6169-6176 (2000)PubMed: 11029439Wang Y, Chen C.Mutation analysis of the flp operon in Actinobacillus actinomycetemcomitans.Gene. 2005 May;351:61-71.PMID: 15837433","Nika,J.R., Latimer,J.L., Ward,C.K., Blick,R.J., Wagner,N.J., Cope,L.D., Mahairas,G.G., Munson,R.S. Jr. and Hansen,E.J. Haemophilus ducreyi requires the flp gene cluster for microcolony formation in vitro Infect. Immun. 70 (6), 2965-2975 (2002) PubMed: 12010986 ","Thu Aug 4 12:07:28 2005","Wed Dec 18 12:06:55 2002","1","","3","" "AA00876","607901","608764","864","ATGATAATTAAGCTATTACTGTCTTATGCATTATTAACCATTTTTGGTGTGTTTGTATTATTTTTGGCACTTTCAGCTAGAAGAAAATTCCAGCATAGGAAAGAAATTATTACTGGAGAAAGACCTAAGGATCAAAGTAATGATGAAATAGCCAAAGGTAAAAGCAAGCAGCAAATTGAACTTGAGCTGTTACTGATTAACAATAATCCCGTTTTAAAAATGCTTGGAATTATTGATAAAAATATAAAAGTAAAATTACTGATTATGGTTTTACTTTGCGGGGTTTATTATCTTTATTCACTTATTGATAAAACTACTGACAGCTCATCTCTGTTACTTGGCTTTCTAACTATATTAATAGTAACTATTGTTATTCCAGGAATTTTAATTGGTTCTATTTTAAAATCCAAAATTAAAAAAATCATGAATGATTTAGCAGGTTTCATTGATTTAGTAGCTGTTAATTTACAAACGGGAATGGGTATTGAAGCTGCGCTAAAGCACGTTGCAACTGACTTTAAAATATTAAACCCTGATCTGACTTATGTTATGTTACGTATTATTCGTAAATCCGAGATTACCGGTATGTCGCAGGCATTGCAGGATCTCTCTGTGTCTTTACCAACAGCAGAAATCCGAATGTTTTGTACTGTAATGCAACAAAGCCTTAATTTTGGTTCCTCTATTTATCATCAACTAGTTCAGCTATCGACTGATATTAGAGAAATTCAATTATTGGCTATAGAAGAAAAACTTGGTACACTGTCGGCAAAAATGAGTGTCCCTTTGATTCTATTTATTATGTTTCCAATTATTATTTTAATTCTGGCTCCAGGTGTAATGAGGGTATTTCCACATGTATTC","","","33083","MIIKLLLSYALLTIFGVFVLFLALSARRKFQHRKEIITGERPKDQSNDEIAKGKSKQQIELELLLINNNPVLKMLGIIDKNIKVKLLIMVLLCGVYYLYSLIDKTTDSSSLLLGFLTILIVTIVIPGILIGSILKSKIKKIMNDLAGFIDLVAVNLQTGMGIEAALKHVATDFKILNPDLTYVMLRIIRKSEITGMSQALQDLSVSLPTAEIRMFCTVMQQSLNFGSSIYHQLVQLSTDIREIQLLAIEEKLGTLSAKMSVPLILFIMFPIIILILAPGVMRVFPHVF","608766","","tight adherence protein C","Inner membrane, Cytoplasm","","
InterPro
IPR001992
Family
Bacterial type II secretion system protein
PF00482\"[148-277]TGSPII_F
noIPR
unintegrated
unintegrated
signalp\"[1-26]?signal-peptide
tmhmm\"[4-24]?\"[84-102]?\"[112-134]?\"[261-281]?transmembrane_regions


","No hits to the COGs database.","","Residues 1 to 58 match (1e-17) PD:PD490979 which is described as TADC PROTEOME COMPLETE ","","","","","","","","","","","","Wed Dec 18 12:09:04 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00876 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 146 to 277 (E-value = 1.4e-19) place AA00876 in the GSPII_F family which is described as Bacterial type II secretion system protein F domain (PF00482)","","","","Kachlany SC, Planet PJ, DeSalle R, Fine DH, Figurski DH. Genes for tight adherence of Actinobacillus actinomycetemcomitans: fromplaque to plague to pond scum. Trends Microbiol. 2001 Sep;9(9):429-37. Review. PMID: 11553455Kachlany,S.C., Planet,P.J., Bhattacharjee,M.K., Kollia,E.,DeSalle,R., Fine,D.H. and Figurski,D.H.Nonspecific adherence by Actinobacillus actinomycetemcomitansrequires genes widespread in bacteria and archaeaJ. Bacteriol.PubMed: 11029439","Nika,J.R., Latimer,J.L., Ward,C.K., Blick,R.J., Wagner,N.J., Cope,L.D., Mahairas,G.G., Munson,R.S. Jr. and Hansen,E.J. Haemophilus ducreyi requires the flp gene cluster for microcolony formation in vitro Infect. Immun. 70 (6), 2965-2975 (2002) PubMed: 12010986 ","Wed Dec 18 12:09:04 2002","Wed Dec 18 12:09:04 2002","1","","3","" "AA00877","608757","609515","759","ATGTATTCTAAATCTCTTAAAAATGTTCTATTATGCGGCATGATCTTATCTGTTACTGCATGTTCTGCTGTACTAAATAAAAAACCATTAAGTGCTGATAAATTAGCTGCTAAAGAAGCACTTTATCAGAGCACTAACAACAACGATGCGTTAATCACTATGTATCGTGATGGACTTAAAAATAAAGAAGATCCTCTCACGCGTTATAAATTATCTGAAATTTATTACAAGAAAGGGGACAGTAGTTCATCTCTACTCTACTTACAGCCGTTGCTAACAAACAGCGGGCAGTTAAGTGAAAGGGCCAAAATTCTACAAGCACGAAATTTAAATCAACTTAAGCGTTATCAAGAAGCGTTGGAAGTCGAAAACAGCTTATTAACAACATCTCCTAAAAACGGTGAAGTCTATAATCTTCGTGGTGTAACCTATGCTTTAATGGGCAATCCAAATAAAGCGAACGAAGATATTAACAAAGCACGAGAATATTTCTTAAATGATGCAGTGGCAGTAAATAATATGGCTATGCTAAGTATCATTAATGGAGATTATCGTAATGCTGTTTCATTATTATTGCCTCAGTATTTAAATGGAGTTAGGGAACAGCGTTTGATACACAATCTAGTCTTTGCTTTAGTCAAGAATAACGAAATTGATTACGCAAAAGATATTATTGTGAAGGAAAACATTAACACATCCCCTGATGATTTAGTTAATGCCCTCAAGAAAACTGAACGCGTGTCTAGTAATATCACCAGA","","","28415","MYSKSLKNVLLCGMILSVTACSAVLNKKPLSADKLAAKEALYQSTNNNDALITMYRDGLKNKEDPLTRYKLSEIYYKKGDSSSSLLYLQPLLTNSGQLSERAKILQARNLNQLKRYQEALEVENSLLTTSPKNGEVYNLRGVTYALMGNPNKANEDINKAREYFLNDAVAVNNMAMLSIINGDYRNAVSLLLPQYLNGVREQRLIHNLVFALVKNNEIDYAKDIIVKENINTSPDDLVNALKKTERVSSNITR","609517","","tight adherence protein D","Outer membrane, Periplasm","","
InterPro
IPR011990
Domain
Tetratricopeptide-like helical
G3DSA:1.25.40.10\"[17-191]Tno description
InterPro
IPR013026
Domain
Tetratricopeptide region
PS50293\"[65-191]TTPR_REGION
noIPR
unintegrated
unintegrated
PTHR23083\"[20-225]TTETRATRICOPEPTIDE REPEAT PROTEIN, TPR
PS51257\"[1-21]TPROKAR_LIPOPROTEIN
signalp\"[1-20]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","BeTs to 12 clades of COG0457COG name: TPR-repeat-containing proteinsFunctional Class: RThe phylogenetic pattern of COG0457 is aompk-yqvd-lbcefghsnujxit-Number of proteins in this genome belonging to this COG is","","Residues 110 to 175 match (1e-11) PD:PD596730 which is described as D PROTEOME TADD COMPLETE NONSPECIFIC TIGHT ADHERENCE ","","","","","","","","","","","","Wed Dec 18 12:10:50 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00877 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","Kachlany SC, Planet PJ, DeSalle R, Fine DH, Figurski DH. Genes for tight adherence of Actinobacillus actinomycetemcomitans: fromplaque to plague to pond scum. Trends Microbiol. 2001 Sep;9(9):429-37. Review. PMID: 11553455Kachlany,S.C., Planet,P.J., Bhattacharjee,M.K., Kollia,E.,DeSalle,R., Fine,D.H. and Figurski,D.H.Nonspecific adherence by Actinobacillus actinomycetemcomitansrequires genes widespread in bacteria and archaeaJ. Bacteriol. 182 (21), 6169-6176 (2000)PubMed: 11029439","Nika,J.R., Latimer,J.L., Ward,C.K., Blick,R.J., Wagner,N.J., Cope,L.D., Mahairas,G.G., Munson,R.S. Jr. and Hansen,E.J. Haemophilus ducreyi requires the flp gene cluster for microcolony formation in vitro Infect. Immun. 70 (6), 2965-2975 (2002) PubMed: 12010986 ","Wed Dec 18 12:10:50 2002","Wed Dec 18 12:10:50 2002","1","","3","" "AA00878","609532","610104","573","ATGGAAAAATTCCTATCAAATAAAAAGGGAGCGTCAGCCGTTGAGTTTGCCTTGACGGTTGTATTCTATTTCTTTATCGTATTCTTAATTCTAGAATTCTGCCGTATATCTATTACCACTGCATATTGGGATTTAGCCATAACTGAAAGTGCAAGGATCGCTAAAAACAGAACGGCGGAAGGTAACGATTATGCTGCAGAATTTGAAAAAGCTCTAAAACAACAACTTATTTATCAAGAAACCTCAACTATAGGCTATCTTGCCCGTTTGGATAAAAATGGCGGTTATGAAATTGATGTTAAATATGTTGATTGTGGTAGTGAGAGCTCTTGTATTAAATCTTTATTAGATGGTAAGTTTAGGCAGCCTACAAAAGACAGAAACGGTAATATTATACCCCCCAATGGTAGGTTAGCAACATTGGCTGTGTATTCATTAACCTACAAGTATGAATTTTTGGTTTCGCTGCCATTTTTACCTAGGGATAACGCTAGCAGTTTGTTGTCACGTAAGTTTGTAGCCGTACAAGAATTTAATAGATCTAAATTTCAGCATCCAGGTAGGTCAAACAAA","","","21673","MEKFLSNKKGASAVEFALTVVFYFFIVFLILEFCRISITTAYWDLAITESARIAKNRTAEGNDYAAEFEKALKQQLIYQETSTIGYLARLDKNGGYEIDVKYVDCGSESSCIKSLLDGKFRQPTKDRNGNIIPPNGRLATLAVYSLTYKYEFLVSLPFLPRDNASSLLSRKFVAVQEFNRSKFQHPGRSNK","","","tight adherence protein E","Outer membrane, Cytoplasm","","
InterPro
IPR012495
Family
TadE-like
PF07811\"[10-52]TTadE
noIPR
unintegrated
unintegrated
signalp\"[1-41]?signal-peptide
tmhmm\"[10-30]?transmembrane_regions


","No hits to the COGs database.","","Residues 1 to 188 match (2e-84) PD:PD308761 which is described as TADE PROTEOME COMPLETE ","Wed Nov 20 11:19:58 2002","","","Wed Nov 20 11:19:58 2002","Wed Nov 20 11:20:13 2002","","","Wed Nov 20 11:20:13 2002","Wed Nov 20 11:20:13 2002","Wed Nov 20 11:19:58 2002","Wed Nov 20 11:19:58 2002","Wed Jan 15 13:38:43 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00878 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","",""," Tomich M, Fine DH, Figurski DH.,Abstract The TadV protein of Actinobacillus actinomycetemcomitans is a novel aspartic acid prepilin peptidase required for maturation of the Flp1 pilin and TadE and TadF pseudopilins.J Bacteriol. 2006 Oct;188(19):6899-914.PMID: 16980493Kachlany,S.C., Planet,P.J., Bhattacharjee,M.K., Kollia,E.,DeSalle,R., Fine,D.H. and Figurski,D.H.Nonspecific adherence by Actinobacillus actinomycetemcomitans requires genes widespread in bacteria and archaeaJ. Bacteriol. 182 (21), 6169-6176 (2000)PubMed: 11029439","Nika,J.R., Latimer,J.L., Ward,C.K., Blick,R.J., Wagner,N.J.,Cope,L.D., Mahairas,G.G., Munson,R.S. Jr. and Hansen,E.J. Haemophilus ducreyi requires the flp gene cluster formicrocolony formation in vitro Infect. Immun. 70 (6), 2965-2975 (2002) PubMed: 12010986","Wed Jan 15 13:38:43 2003","Wed Jan 15 13:38:43 2003","1","","3","" "AA00879","610173","610748","576","ATGAAAAAAAATATCATCACTAGTATTAAAAAATTTTTTCGTAATAAAAAGGGCGCAGTTACGCTTGAGCTTCTTTTTATGCTTATTCTTTTAGTATTTATTTTCGCCTTTTTAACAGACCTAGTTATTGTTCGTACTACCCAGGGAAAACTGGACAATGCCTCGTATTCACTGGTCAATATTCTTCGCGAGCGTAATCAGTTATACAATGATAATGGGACCGAAAAACTAAAAAGTACTGACTTAACTGAATATGAAAAAATGGCAAAACTTATTTTGTTTGGAGATAAAGACAGTCCAAATAAAGTCGGTGTCACTATTGAGCACTGGGAAGAGAAAAAAAATCCTGAAATGTTAACGAATCTAGGCACATGTCGGCCTTATCGTAAGTTGGATGATAATCTCTCTTATTTGTCGCCACGCTCAGAATCAGCTAACCCTGACAACCAAAGAAAAATCCCACTGTATCAGGTGACCCTTTGCGTTGAAGCCGGTAGCTTTTTCAAAAATTTAATAACACGTAAAGAAAACCAGTCATTTGGTATGTTAAGTTCCTCTTCACTAGCAGTTGCTCGA","","","23265","MKKNIITSIKKFFRNKKGAVTLELLFMLILLVFIFAFLTDLVIVRTTQGKLDNASYSLVNILRERNQLYNDNGTEKLKSTDLTEYEKMAKLILFGDKDSPNKVGVTIEHWEEKKNPEMLTNLGTCRPYRKLDDNLSYLSPRSESANPDNQRKIPLYQVTLCVEAGSFFKNLITRKENQSFGMLSSSSLAVAR","610750","","tight adherence protein F","Outer membrane, Periplasm, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-36]?signal-peptide
tmhmm\"[24-44]?transmembrane_regions


","No hits to the COGs database.","","Residues 40 to 192 match (4e-33) PD:PD486154 which is described as PROTEOME COMPLETE YPO0685 TADF ","","","","","","","","","","","","Wed Dec 18 12:27:47 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00879 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","",""," Tomich M, Fine DH, Figurski DH.,Abstract The TadV protein of Actinobacillus actinomycetemcomitans is a novel aspartic acid prepilin peptidase required for maturation of the Flp1 pilin and TadE and TadF pseudopilins.J Bacteriol. 2006 Oct;188(19):6899-914.PMID: 16980493Kachlany SC, Planet PJ, DeSalle R, Fine DH, Figurski DH.Genes for tight adherence of Actinobacillus actinomycetemcomitans: fromplaque to plague to pond scum.Trends Microbiol. 2001 Sep;9(9):429-37. Review.PMID: 11553455Kachlany,S.C., Planet,P.J., Bhattacharjee,M.K., Kollia,E.,DeSalle,R., Fine,D.H. and Figurski,D.H.Nonspecific adherence by Actinobacillus actinomycetemcomitansrequires genes widespread in bacteria and archaeaJ. Bacteriol. 182 (21), 6169-6176 (2000)PubMed: 11029439","Nika,J.R., Latimer,J.L., Ward,C.K., Blick,R.J., Wagner,N.J., Cope,L.D., Mahairas,G.G., Munson,R.S. Jr. and Hansen,E.J. Haemophilus ducreyi requires the flp gene cluster for microcolony formation in vitro Infect. Immun. 70 (6), 2965-2975 (2002) PubMed: 12010986","Wed Dec 18 12:27:47 2002","Wed Dec 18 12:27:47 2002","1","","3","" "AA00880","610768","612336","1569","ATGAGCAAAAATTTTAACCTAACTGCTAAATTGTTTAATTCCATTAAGCAATTTTTCCAAAATGAGCATGGTGTATACGCTATAATAACAGCCCTGCTCGCCTTCCCGTTGTTACTGTTAGTTGCTTTTACTGTCGATGGTACGGGGATATTATTAGATAAAGCCCGCTTAGCACAAGCAACGGATCAGGCAGCATTATTATTAATTGCTGAAGATAACAAATATCGGAAAAATAAAGATCATTCTGATGTAAGCAGACAACACGTCTCTCAACAAGATATTAACCGGGAAGGTAATTCAAAAGTGCAAGCTCAGTGGAAGAAACGTAATCAAGAGCTAGTGCAAGGGTTAGTTAAACTTTATTTACGTTCCGACGACAAGAATGGTCAAAAAAATAGTTCTCCGGCAATAATTAAAGATCCCTTCCTTGCCGAGTGTTTGGAAGAAAAAACACAGCCTAAGAATAAAAATGGCACAGCAAAATCTATTGCTTGTGTAGTACAAGGTTCCGTGCAACGAAAATTCTGGTTACCTTGGGGTCAAACTTTAGTAAGTAGCAGTCGGTTACATGACGGAAGAGTAGGCATTAACTCAGGTAAAACCTACGCTGTTAAAGATAAACAAATCACAATTCCAATTGATTTAATGATGGTTACTGATTTATCTGGTTCAATGACATCACCTATAGTGGAAGGTACAATAGGTAGAAGAATTGATGCACTAAGAGAGGTAGTCAAGGATATTGAAGGTATATTATTACCTAAAGATGCTAGAGATGATGCCAGCCCCTATAATAGAATGGGGTTTGTAGCATTCGCTGGAGGGGCCCGCCAGAAAGGTGAAAAAAATGACTGTGTACTTCCATACTATACAAACCCGTCTGTAACAGCAGAGATATCTAGTTTACTTGCAATGAATAGATTAGACGACGCTTCTAACCTACTGGATCAGAATATGGATATACAAAAAACTATAAATCAGATTGATAAATTTAATGGCAGTAATATACGTTATGACTTTATAAATAGGACAAAAAAATGTTTAGGGAAAAGCGAAGGGAAAGAGACAACTCAAGCATGGTTTGACAAGAAAAAACCGGGTGTGTCAAATGCTTTAAACGAAATTACTCCAGACGGAGGGACAGCTGTTACTTCAGGTATGTTTATAGGGACTAACCTTATGATGGATACTAATAAAGATCCGGAAGCTACACCAAGCAAACTTAATACAAATACAAGACGCATACTTCTGGTGTTATCTGATGGAGAAGATAATCGCCCGACTAAAGGTACATTAGTTAAATTAATGAATGCCGGATTATGCAACAAAATTAAAGGAAAGATTGACTCATTACAAGATACTAAGTACCCTAAAGTGGAAGCACGCGTTGCTTTTGTTGCACTTGGTTATAATCCACCCCAAGATCAAGTAAACGTATGGAAACAGTGCGTCGGTAAACAATATTATCCTGTATTCAGTAAGCAGGGATTATTAGATGCTTTCAGACAAATCATTAGTTTTGAAGAAGAAGTAGGTCGTTCATCTTCACAAAAGCCAAAATTATTCCAA","","","59179","MSKNFNLTAKLFNSIKQFFQNEHGVYAIITALLAFPLLLLVAFTVDGTGILLDKARLAQATDQAALLLIAEDNKYRKNKDHSDVSRQHVSQQDINREGNSKVQAQWKKRNQELVQGLVKLYLRSDDKNGQKNSSPAIIKDPFLAECLEEKTQPKNKNGTAKSIACVVQGSVQRKFWLPWGQTLVSSSRLHDGRVGINSGKTYAVKDKQITIPIDLMMVTDLSGSMTSPIVEGTIGRRIDALREVVKDIEGILLPKDARDDASPYNRMGFVAFAGGARQKGEKNDCVLPYYTNPSVTAEISSLLAMNRLDDASNLLDQNMDIQKTINQIDKFNGSNIRYDFINRTKKCLGKSEGKETTQAWFDKKKPGVSNALNEITPDGGTAVTSGMFIGTNLMMDTNKDPEATPSKLNTNTRRILLVLSDGEDNRPTKGTLVKLMNAGLCNKIKGKIDSLQDTKYPKVEARVAFVALGYNPPQDQVNVWKQCVGKQYYPVFSKQGLLDAFRQIISFEEEVGRSSSQKPKLFQ","612338","","tight adherence protein G","Periplasm, Inner membrane","","
InterPro
IPR002035
Domain
von Willebrand factor, type A
SM00327\"[212-509]TVWA
noIPR
unintegrated
unintegrated
signalp\"[1-47]?signal-peptide
tmhmm\"[23-43]?transmembrane_regions


","No hits to the COGs database.","","Residues 208 to 277 match (4e-19) PD:PD576108 which is described as TADG ","","","","","","","","","","","","Wed Dec 18 12:29:40 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00880 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","Kachlany SC, Planet PJ, DeSalle R, Fine DH, Figurski DH. Genes for tight adherence of Actinobacillus actinomycetemcomitans: fromplaque to plague to pond scum. Trends Microbiol. 2001 Sep;9(9):429-37. Review. PMID: 11553455Kachlany,S.C., Planet,P.J., Bhattacharjee,M.K., Kollia,E.,DeSalle,R., Fine,D.H. and Figurski,D.H.Nonspecific adherence by Actinobacillus actinomycetemcomitansrequires genes widespread in bacteria and archaeaJ. Bacteriol. 182 (21), 6169-6176 (2000)PubMed: 11029439","Nika,J.R., Latimer,J.L., Ward,C.K., Blick,R.J., Wagner,N.J., Cope,L.D., Mahairas,G.G., Munson,R.S. Jr. and Hansen,E.J. Haemophilus ducreyi requires the flp gene cluster for microcolony formation in vitro Infect. Immun. 70 (6), 2965-2975 (2002) PubMed: 12010986 ","Wed Dec 18 12:29:40 2002","Wed Dec 18 12:29:40 2002","1","","3","" "AA00881","613545","613312","234","TTGAATATCCTTGCCGACGTCACCTTCTTTGGTCGGGATTTCGGTGTGCTTGTGCTGTTAGATTCGTTGTCGGGAAAAGTGATTTATCACCAAATCGTGAAAACCGAAAAAGACATTTATTATAAAATGGCATTTAATCGGCTAAGAGAAAAAGGTTATGTTATTCAATTGATTACCTGCGACGGTAGACGGGGAGTATTAAAGGATTTGTTCAACACACCGATACAAATGTGC","","","8998","LNILADVTFFGRDFGVLVLLDSLSGKVIYHQIVKTEKDIYYKMAFNRLREKGYVIQLITCDGRRGVLKDLFNTPIQMC","613314","","hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-25]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Dec 18 12:30:27 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00881 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00882","613705","613592","114","GTGTTTTCTTTCAAAAGTAAACTTAATCCAATCCAAATTTGGGAAGATTATGAGAAGGGAAAACAAACCTACAAAAAATTAGCCGAAAAATATCACTGCCATCCAACGTTATCT","","","4568","VFSFKSKLNPIQIWEDYEKGKQTYKKLAEKYHCHPTLS","613592","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 14:58:09 2004","Mon Feb 23 14:58:09 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00882 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 14:58:09 2004","","","","","","","","","","","","","1","","","" "AA00883","614527","614438","90","ATGTCAACCAACGCAATTATCATGATGGCTGTTGCACTTATCATCATTTGGGGCGGGTTATTAGTGTCTGTTATCAGATTACCGAAAGAA","","","3236","MSTNAIIMMAVALIIIWGGLLVSVIRLPKE","614438","","hypothetical protein","Cytoplasm, Inner membrane","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 14:59:28 2004","Mon Feb 23 14:59:28 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00883 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 14:59:28 2004","","","","","","","","","","","","","1","","","" "AA00884","616031","614532","1500","ATGACACACACAACACAAAAACGCGAAACCTTCTCCGGACGACGGGCATTTATTTTTGCCGCTATCGGTTCGGCAGTCGGTCTGGGCAATATCTGGCGTTTTCCCTATGTAACCTACGAAAACGGCGGCGGTGCCTTTATCATTCCTTACATCGTGGCATTATTAACCGCAGGGATCCCGTTATTGTTTTTAGATTATGCCATCGGGCATAAATTCCGTGCCTCTCCACCATTGGCATACCGCAAACTCAAAACCGGTTTTGAAACATTCGGTTGGTGGCAAGTGATGATTAACGTGATCATCGGGCTTTATTACGCCGTCATCCTCGGCTGGGCGGCAAGTTATACCTATTATTCCGTTACTTCCGCCTGGGGCAGCAACCCTGTCGATTTCTTCCTGCACGAACACATTAAAATGGCAGATGAAGTGGCGTTAAATCTGGATTTCGTCGGCACGGTTGTTGGTCCGTTACTTGCCGTTTGGCTAATTACTTTATTGATTTTATCCCTCGGTGTACAAAAAGGTGTTGCGCGCACTTCTGTGATTTTTATGCCAATTTTAGTCATCATGTTTGTCACTTTAATGGTTTATTCCTTATTTTTACCGGGCGCAGAAAAAGGGTTGGATGCCCTGTTCTCGCCGGATTGGGATAAATTAAAAGACCCGAGCGTCTGGATTGCCGCTTACGGACAAATATTCTTCTCCCTTTCCATTTGTTTCGGTATTATGGTGACCTATGCTTCCTATTTGAAAAAACAATCGGACTTAACCGGCGCCGGTTTGGTGGTAGGCTTTGCCAACAGCAGTTTTGAAGTGTTGGCCGGTATCGGCGTATTCTCCGCCTTAGGTTTCATTGCCGCTGCCAACGGACACGATGTGAGCGAAGTAGCAAAAGGCGGTATAGGTCTCGCCTTCTTTGCCTTCCCAACCATCATTAACCAAGCGCCATTAGGGCAATTATTAGGCGTGCTATTCTTCGGTTCTTTGGTTTTCGCAGGCTTAACCTCCTTTATTTCCGTATTGGAAGTGATTATTTCCGCCGTCCAGGACAAATTACGTCTACGCCGCGTCCATGCCACGTTTTTAGTGGGTTTACCAATGATGGTGGCTTCTACGCTCTTATTTGGCACCACCGCCGGTTTACCGATGCTCGATACCATGGATAACTTTGTGAACATGTTTGGTATCGTCGCTGTAGCATTCTTCTCCTTATTTTCCATTATCATGAGCGGCAGATTAAAAGAATTGGGCGAACACTTAAACGAAACCGGCTCTTTCAAAGTGGGCATGATTTGGAAAGCTTTTATCGTCATCACCACCGGTGTACTGGCTTTCATGCTATACAAAGAAGCAGGCAAAGTGCTCACCAAAGGCTACGAAGGCTATCCGGACCGGTTCGTCAACACCTTCGGCTGGGGCATGGCAATCGCTTTGGTGATCATCGCATTCCTGCTTTCCCGCCTGCCGTGGAAACACTTAACGCAAACACAAGGAGAAAAA","","","54604","MTHTTQKRETFSGRRAFIFAAIGSAVGLGNIWRFPYVTYENGGGAFIIPYIVALLTAGIPLLFLDYAIGHKFRASPPLAYRKLKTGFETFGWWQVMINVIIGLYYAVILGWAASYTYYSVTSAWGSNPVDFFLHEHIKMADEVALNLDFVGTVVGPLLAVWLITLLILSLGVQKGVARTSVIFMPILVIMFVTLMVYSLFLPGAEKGLDALFSPDWDKLKDPSVWIAAYGQIFFSLSICFGIMVTYASYLKKQSDLTGAGLVVGFANSSFEVLAGIGVFSALGFIAAANGHDVSEVAKGGIGLAFFAFPTIINQAPLGQLLGVLFFGSLVFAGLTSFISVLEVIISAVQDKLRLRRVHATFLVGLPMMVASTLLFGTTAGLPMLDTMDNFVNMFGIVAVAFFSLFSIIMSGRLKELGEHLNETGSFKVGMIWKAFIVITTGVLAFMLYKEAGKVLTKGYEGYPDRFVNTFGWGMAIALVIIAFLLSRLPWKHLTQTQGEK","614534","","sodium-dependent transporter","Inner membrane, Cytoplasm","","
InterPro
IPR000175
Family
Sodium:neurotransmitter symporter
PD000448\"[6-35]TY736_HAEIN_P44849;
PR00176\"[16-37]T\"[45-64]T\"[89-115]T\"[315-334]TNANEUSMPORT
PTHR11616\"[8-463]TSODIUM/CHLORIDE DEPENDENT TRANSPORTER
PF00209\"[8-500]TSNF
PS50267\"[7-500]TNA_NEUROTRAN_SYMP_3
PS00610\"[32-46]TNA_NEUROTRAN_SYMP_1
noIPR
unintegrated
unintegrated
PTHR11616:SF14\"[8-463]TSODIUM/CHLORIDE-DEPENDENT NORADRENALINE TRANSPORTER
tmhmm\"[15-33]?\"[47-69]?\"[90-108]?\"[149-171]?\"[181-201]?\"[225-247]?\"[262-282]?\"[321-341]?\"[362-382]?\"[388-408]?\"[429-447]?\"[466-486]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.8e-56) to 5/7 blocks of the IPB000175 family, which is described as \"Sodium:neurotransmitter symporter family\". Interpro entry for IP:IPR000175. IPB000175A 16-65 1.2e-27 IPB000175B 104-138 8.4 IPB000175C 151-202 29 IPB000175D 218-270 1.1e-15 IPB000175E 311-350 3.7e-08","Residues 123 to 192 match (2e-08) PD:PD582514 which is described as COMPLETE PROTEOME TRANSPORTER SODIUM-DEPENDENT SYMPORT TRANSMEMBRANE MJ1319 MEMBRANE CHLORIDE-DEPENDENT INNER ","","","","","Wed Feb 19 08:24:42 2003","","","","","","","Wed Dec 18 12:37:01 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00884 is paralogously related to AA01815 (1e-49).","","","","","","Residues 8 to 500 (E-value = 2.3e-147) place AA00884 in the SNF family which is described as Sodium:neurotransmitter symporter family (PF00209)","","","","","","","","1","","","" "AA00885","616447","616719","273","GTGCGGTTGATTTCCGAACCGGATTTTTTATGGCAACGCATTTCGCCTATTCGCGAACGCAAACATATTCCCACCGCGTGGCTGGAAGTGAAGATTGATGAAGGGCGCAATCGGCAGGTGCGCAGAATGACGGCGCATATCGGGTTTCCGACGTTACGTCTGATTCGTTATCAATTAACGGGATTCAACCTGCAAAATTTGATGCCGAAAACCTACCGCACTTTAACTCAAAACGAACTAAGAGAACTGTATCAATTACTTAAATTAACGATT","","","11027","VRLISEPDFLWQRISPIRERKHIPTAWLEVKIDEGRNRQVRRMTAHIGFPTLRLIRYQLTGFNLQNLMPKTYRTLTQNELRELYQLLKLTI","616721","","ribosomal large subunit pseudouridine synthase c","Cytoplasm","","
InterPro
IPR000748
Domain
Pseudouridine synthase, Rsu
TIGR00093\"[1-77]TTIGR00093: conserved hypothetical protein
InterPro
IPR006145
Domain
Pseudouridine synthase
PF00849\"[11-46]TPseudoU_synth_2
noIPR
unintegrated
unintegrated
PTHR21600\"[12-89]TRIBOSOMAL LARGE SUBUNIT PSEUDOURIDINE SYNTHASE B
PTHR21600:SF2\"[12-89]TRIBOSOMAL LARGE SUBUNIT PSEUDOURIDINE SYNTHASE B


","BeTs to 17 clades of COG1187COG name: 16S rRNA uridine-516 pseudouridylate synthase and related pseudouridylate synthasesFunctional Class: JThe phylogenetic pattern of COG1187 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 7.2e-12) to 1/4 blocks of the IPB000748 family, which is described as \"Pseudouridine synthase, Rsu family\". Interpro entry for IP:IPR000748. IPB000748D 30-64 6.7e-12","Residues 1 to 79 match (3e-23) PD:PD003862 which is described as PROTEOME COMPLETE SYNTHASE PSEUDOURIDINE RIBOSOMAL SUBUNIT PSEUDOURIDYLATE LARGE SMALL B ","","","","","","","","","","","","Wed Dec 18 12:53:33 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00885 is paralogously related to AA01998 (5e-05).","","","","","","","","","","","","","","1","","","" "AA00886","616724","616915","192","ATGAATAATTTATTAAATTTTATTGAAGCGTCGGCGCGCGACAGCCACTTTTTTATTTTCGCCAAAATGGCGTTTGCGATGATTCTGGGCGGCGGCAGGTATCGGCATTGCTTCCGGCGCGGGGTTTTATTTCGACGCCATGGTCGCCACCATCATGATTTTAATCGCCATTCGTTTAAGCCCGTATGTGCA","","","7587","MNNLLNFIEASARDSHFFIFAKMAFAMILGGGRYRHCFRRGVLFRRHGRHHHDFNRHSFKPVCA","616917","","hypothetical protein","Cytoplasm, Extracellular","","
noIPR
unintegrated
unintegrated
tmhmm\"[10-30]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Dec 18 12:54:38 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00886 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00887","617016","616879","138","TTGTTATGCAACAACTGCACGAATTGCGCAATGGCATTGGGTGAAAGCAATGTGGCGTTGATTCGTGTTTTTTCTTTTTATCGCGATGGCGCACCCAATTATGCACATACGGGCTTAAACGAATGGCGATTAAAATCA","","","5117","LLCNNCTNCAMALGESNVALIRVFSFYRDGAPNYAHTGLNEWRLKS","616879","","hypothetical protein","Cytoplasm, Extracellular","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:00:48 2004","Mon Feb 23 15:00:48 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00887 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:00:48 2004","","","","","","","","","","","","","1","","","" "AA00889","616997","617170","174","GTGCAGTTGTTGCATAACAACAATCATTCCATCGAAAACATCAACGTGAAAGATCAGCCCAACGGCGAAACCAAACTGACCATTCGCTGTTCTATCAACGATAAAGCCACCATTCAGGAGTTGTATTTATTGCTGAAAAACGACCCGAACGTGGTGAGTTTGGAACTGGAAAAT","","","7649","VQLLHNNNHSIENINVKDQPNGETKLTIRCSINDKATIQELYLLLKNDPNVVSLELEN","617172","","conserved hypothetical protein","Cytoplasm","","No hits reported.","BeTs to 3 clades of COG1285COG name: Uncharacterized membrane proteinFunctional Class: SThe phylogenetic pattern of COG1285 is -------q-drlbcef-h------t-Number of proteins in this genome belonging to this COG is","","Residues 2 to 58 match (2e-07) PD:PD078903 which is described as PROTEOME COMPLETE HI0647 TRANSMEMBRANE PM1753 ","","","","","","","","","","","","Wed Dec 18 13:14:08 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00889 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00890","618114","617215","900","ATGAAAAAATTACTCATTGCCACGCTCATCGCCGGTAGCCTGATGCTGACCGCCTGCGACGATAAAGAAAAAACTGCGCTCAGCGAGCAAATGCAAAAACAGGCACAAACCATTGAACAACTCAATGAGCAGGTGAAGACATTAGAGAAACAAGTGCTGGATTTAGCCGAAAATCAAACGATTCGGGTGGAGCCGGAAGTGCTGTTTGAAAAATCGGAAACCATCAAATTTGATAAAAAATCCGCCGACAGTTATACGCCGGAAAGCGGCGAAGTGAAAGTCAACGTAAAAACTTTAAAAACCGGCGAAGATTGGTTAACGGATTTATTATTAAATGAATTAATCCGACAATTCACCGCAAGCGGTCAAGTCAAAATCGAGAATAAACAACAACTTGTGGAATGGCTACAAGCGCTTTACACGGACAGCGTTAAAGAAGTTAAAGATAACGAAATGATTGGCAGCAGCACCGAATTCAGTGTGAAATATCTCGGACAACGGGAAAACATCGCCACCTTCACCATCAGTTATTCCGGCTATTCCGGCGGTGCGCACGGTATGTATTCCACCCAATTCCTTAACATTGATTTGGCGAAAAAAGCCTTGCTGGATATTGATGATGTCATCAATCCGGAACAGCATCAAAAACTAAAAGACCTCTTATGGGATGCTTACCGCGACAGTAATAATGAAGCGGAACCTTTTACCCAGAAAGACGGGGGATTTTACGTGCCAAAAGATTTTTACTTCTCCCGCAATGGCGTTACTTTCGTTTACCCGCCTTATGCCATCGGCAGTTTTTCGGAAGGGGAAAAAGAGCTGACGATTTATTGGTGGCAGTTGAAAGAAAACGACTTGATCAACCCGCAATTTAGCGCTTTAGCAAAATCGGTTATCGAA","","","34165","MKKLLIATLIAGSLMLTACDDKEKTALSEQMQKQAQTIEQLNEQVKTLEKQVLDLAENQTIRVEPEVLFEKSETIKFDKKSADSYTPESGEVKVNVKTLKTGEDWLTDLLLNELIRQFTASGQVKIENKQQLVEWLQALYTDSVKEVKDNEMIGSSTEFSVKYLGQRENIATFTISYSGYSGGAHGMYSTQFLNIDLAKKALLDIDDVINPEQHQKLKDLLWDAYRDSNNEAEPFTQKDGGFYVPKDFYFSRNGVTFVYPPYAIGSFSEGEKELTIYWWQLKENDLINPQFSALAKSVIE","617217","","conserved hypothetical protein","Outer membrane, Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
PS51257\"[1-19]TPROKAR_LIPOPROTEIN
signalp\"[1-19]?signal-peptide


","BeTs to 3 clades of COG1579COG name: Zn-ribbon protein, possibly nucleic acid-bindingFunctional Class: RThe phylogenetic pattern of COG1579 is -------q-dr---------u--it-Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Wed Dec 18 13:14:45 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00890 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00892","620019","618163","1857","ATGATTATCGTTACCTCCGGACACGTTGACCACGGCAAAACCGCCCTTTTGCAAGCCCTCACCGGCACCCATACGGCGCACTTGCCGGAAGAAAAGAAACGCGGCATGACCATTGATTTGGGCTACGCGTATTTGCCGTTCAACGATCAGATTCTCGGCTTTATTGATGTACCGGGACACGAGCATTTCCTCGCCAATATGCTGGCGGGGCTGGGCGGCATTCACTACGCCATGCTTATCGTTGCCGCCGACGAAGGCGTGCAGGCGCAAACCATCGAGCATTTAAGCATTTTAAGCCTGTTACAGTTACAGGAAATCATGGTGGTAATCACCAAAGCCGACCGCGCCGACGCGGTACAAATCGACGCGTTGGAAAATCAACTGCGCCAACAATATGCCGTATTGGCGAACAGCAAATTCTTCGTTACCTCTGCCATCACCGGTCAGGGCATTGACGCCTTGCGCGATTATTTGGCGCAGTTGGCGGAATTGTCAGAAGTGGATAAACCTTTCCGTTACGCCATCGACCGTATTTTCACCATTAAAGGCGCCGGCACGGTCGTCACCGGCACGGCATTCGCGGGCAAAGTCAGCCTGGATGACGAACTGTATTTGAGCAACGGGCAAAAAGTGCGAGTGAAAAATATCCACGCACAAAACGAACAAAACTGCGTAGGCTTGGCAGGACAACGCTTGGCGTTAAATATTAACCTGGATTTCGACCGCACTTCCATTGAACGCGGCGATTGGCTGTTCTCCCAAACACCCGGCGAACCGACGGATCGCATCACCGTTTGGCTGGAAAGCCAAATGGCATTAAACGAAAGCCAGCCGGTGCATATTTATCACGCCGCATCGCACACCACGGGCAAACTCACCTTGTTACAACAACAAAAGCTCGCCCCGCAACAGTTGGCATTGGCGGAACTGATTTTGGAACAACCGCTGTTTTTGGCGTACGGCGACAAAATCATTCTGCGCAACAGCAATTCCACCGCCGTGCTTGGCGGTGCCAAAGTGATTGAAATCGATTCGCCGAAACGGCACAAACGCACGGAAGCGCGTTTCGATTATTTACGCCGCTTGATTCAGGCGGAAACGGCGCAAAAACGCACCGCACTTTATTTGCAAAATCACGCGGTGGAAGTGCAAAAGCTCATGTGGATTGAGCAGCTGACGGGCGTGCAACTGGACGCCATTCTGCAACAAAACGGCGATATTCGCTTCCAAAGCTGGTGTTTTAACGCCGATTATCGCGCCCAACAAACGGCAAAATTATTGACCGCACTTGCCCAATATCATGAACAACATCCTGATCAACTCGGCTTGGGCAAAGCCCGTTTGTATCGCATTGCAGCGCTGAATCAGCCGGAAAAATTGATTTACCATTTTATCGACGAATTATTGGCAGAAAATCAATTACAACACACCCGTGGCTGGCTACACACCGCCGATCATAAAATCCAATTTAGCGAACAAGAACGTGCATTATGGCAACAAGTTCTCGCCCAATTCGAGCAACATAACGGACAAGCCCTGTGGGTGCGCGATCTTGCCAATGCGTTAGGACAGGAAGAAAGAGCCATGCGCAATTTTCTCTATAAAGCCGGCAAACTGGGCTATTTAACCGCCGTGGTGAAAGACCGTTTCTTCCTCACGGAGAACATTTACACCTTCGCCCGTTTAATTAAACAACTGACCGCCGGAAAAGAAGGCTTTTCGGTGAACGAACTGCGCGACGCCTTACAATTCGGACGCAAAATGACTGTGCAACTGGTGGAATATTTCGACCGTTGTGGCTTCCTGCGCCGTAAAGTCAACATTCACGTTTTACGCGATGTGGACGTGTTTGATTTA","","","70002","MIIVTSGHVDHGKTALLQALTGTHTAHLPEEKKRGMTIDLGYAYLPFNDQILGFIDVPGHEHFLANMLAGLGGIHYAMLIVAADEGVQAQTIEHLSILSLLQLQEIMVVITKADRADAVQIDALENQLRQQYAVLANSKFFVTSAITGQGIDALRDYLAQLAELSEVDKPFRYAIDRIFTIKGAGTVVTGTAFAGKVSLDDELYLSNGQKVRVKNIHAQNEQNCVGLAGQRLALNINLDFDRTSIERGDWLFSQTPGEPTDRITVWLESQMALNESQPVHIYHAASHTTGKLTLLQQQKLAPQQLALAELILEQPLFLAYGDKIILRNSNSTAVLGGAKVIEIDSPKRHKRTEARFDYLRRLIQAETAQKRTALYLQNHAVEVQKLMWIEQLTGVQLDAILQQNGDIRFQSWCFNADYRAQQTAKLLTALAQYHEQHPDQLGLGKARLYRIAALNQPEKLIYHFIDELLAENQLQHTRGWLHTADHKIQFSEQERALWQQVLAQFEQHNGQALWVRDLANALGQEERAMRNFLYKAGKLGYLTAVVKDRFFLTENIYTFARLIKQLTAGKEGFSVNELRDALQFGRKMTVQLVEYFDRCGFLRRKVNIHVLRDVDVFDL","618165","","selenocysteine-specific elongation factor (SelB translation factor)","Cytoplasm","","
InterPro
IPR000591
Domain
Pleckstrin/ G-protein, interacting region
PF00610\"[484-559]TDEP
InterPro
IPR000795
Domain
Protein synthesis factor, GTP-binding
PF00009\"[1-157]TGTP_EFTU
InterPro
IPR004161
Domain
Translation elongation factor EFTu/EF1A, domain 2
PF03144\"[185-252]TGTP_EFTU_D2
InterPro
IPR004535
Family
Translation elongation factor, selenocysteine-specific
TIGR00475\"[1-613]TselB: selenocysteine-specific translation e
InterPro
IPR005225
Domain
Small GTP-binding protein domain
TIGR00231\"[1-160]Tsmall_GTP: small GTP-binding protein domain
InterPro
IPR015190
Domain
Elongation factor SelB, winged helix 2
PF09106\"[426-483]TSelB-wing_2
InterPro
IPR015191
Domain
Elongation factor SelB, winged helix 3
PF09107\"[563-612]TSelB-wing_3
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[1-167]Tno description
PTHR23115\"[3-260]TTRANSLATION FACTOR
PTHR23115:SF39\"[3-260]TELONGATION FACTOR SELB


","BeTs to 5 clades of COG3276COG name: Selenocysteine-specific translation elongation factorFunctional Class: JThe phylogenetic pattern of COG3276 is -------q------ef-h--u-----Number of proteins in this genome belonging to this COG is","Significant hit ( 2.1e-23) to 3/3 blocks of the IPB000795 family, which is described as \"GTP-binding elongation factor\". Interpro entry for IP:IPR000795. IPB000795A 2-17 1.3e-05 IPB000795B 55-86 1.4e-10 IPB000795C 90-114 0.00066Significant hit ( 3.5e-09) to 3/8 blocks of the IPB000178 family, which is described as \"Initiation factor 2\". Interpro entry for IP:IPR000178. IPB000178A -1-37 0.12 IPB000178B 52-84 3.7e-05 IPB000178C 85-124 1.6e+02Significant hit ( 3.2e-08) to 3/6 blocks of the IPB000640 family, which is described as \"Elongation factor G, C-terminus\". Interpro entry for IP:IPR000640. IPB000640A 0-25 0.3 IPB000640B 25-47 0.27 IPB000640C 52-79 0.098","Residues 66 to 114 match (1e-08) PD:PD000134 which is described as FACTOR ELONGATION GTP-BINDING BIOSYNTHESIS INITIATION PROTEOME COMPLETE TRANSLATION TU EF-TU ","","","","","","","","","","","","Wed Dec 18 13:15:52 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00892 is paralogously related to AA00931 (5e-22), AA00563 (5e-22), AA01922 (1e-14), AA03003 (2e-08), AA01852 (7e-08) and AA02344 (1e-05).","","","","","","Residues 484 to 559 (E-value = 8.4e-06) place AA00892 in the DEP family which is described as Domain found in Dishevelled, Egl-10, and Pleckstrin (PF00610)","","","","","Forchhammer,K., Rucknagel,K.P. and Bock,A. Purification and biochemical characterization of SELB, a translation factor involved in selenoprotein synthesis J. Biol. Chem. 265 (16), 9346-9350 (1990) PubMed: 2140572 Forchhammer,K., Leinfelder,W. and Bock,A. Identification of a novel translation factor necessary for the incorporation of selenocysteine into protein Nature 342 (6248), 453-456 (1989) PubMed: 2531290 ","","Wed Dec 18 13:15:52 2002","1","","","" "AA00894","621410","620019","1392","ATGTCAGCCCTTTACCAGGCCCTTCCCGCCGTCGATAAATTACTCAAAACCCCGCAGGGTGAGCAGCTGGTGGCAGAATTCGGTCACAGCGCCACCGTTAATATGTGCCGAGACCTGTTACAGCAGGCACGCGAACACATAAAACGCCACGAAAACCTACCGCACTTTTTGCAGAATACCGACGCCACTTTTCAGCACCTCAAGGAACAACTTCTGTTACAACAACAGGTGAACATCAAAACCGTCCACAATTTAACCGGCACGGTGCTGCACACCAATCTCGGACGCGCTTTGTGGTCGCCGGCGGCGCAACAGGCGGCGCTGGACGCCATGCAGGGCAATGTGGCGTTGGAATATGATTTAAGCGCGGGCGAGCGCAGCCATCGGGATAATTACATCAGTGCTTTAATGCAGCAACTGACGGGCGCGGAAGCCGCCTGCGTGGTGAATAACAATGCGGCAGCGGTCTTGCTGATGCTGGCGACCTTCGCCCAGGGCAAAGAAGTGATTATTTCCCGTGGCGAGCTGATTGAAATCGGCGGCGCGTTCCGCATTCCCGACATCATGGCGCAGGCGGGCTGCAAGCTGGTGGAAGTGGGCACGACCAACCGCACCCATTTAAAAGATTATCGTAACGCAATTAACGAAAATACTGCCTTTTTAATGAAAGTTCACAGCAGTAACTATCAAATTTGCGGTTTTACCCACAGCGTTGACGAGCAGGAATTGGCGGATTTGGGCAAAGAATTCGGCATTCCGGTCATCACCGATTTAGGCAGCGGCGCGCTCATGGATTTAAAACAATTCGGCTTGCCGGAAGAGCCCACCGTGCAGGAAAAATTGCAGCACGGCGTGGATTTGATTTCCTTCTCCGGCGACAAATTGCTGGGCGGCCCGCAAGCGGGCATTATTGTGGGCAAAAAAGCACTCATTCAACAGCTGCAGGCCCACCCGCTCAAACGCGTGCTGCGTTGCGATAAAGTCACTCTTGCCGGGCTGGAAGCTACCTTTCGCCTCTATTTACAGCCGGAAAAAATCACCGAAAAACTGACCGCACTTTTGTTGCTTACGCAACCCATGGAACGCTTACAGGCGCAGGCGGAGCAACTCAAAGTGCGGTTGGAAAATCGCTTAAATACCAATTATGTGATTGCCATTGAACCGAGCGAGGCACAAATCGGCAGCGGTTCGCAACCGTTGGCGCGAATTCCGTCGGTGGCGGTGACTATTGCGCCGGCAAGCGAAAAAACGCCGGCAAAAACCACCGCACTTTTCGCCCGTTTATTAGCCTTGCCGCAGCCGGTTATCGGGCGCATTGAGCGGGATAAAATTTGGTTGGATTTACACAGTTTGGCGAGCCTTGATCGCCTTCTAAACAGCTTGGAGACATTA","","","50885","MSALYQALPAVDKLLKTPQGEQLVAEFGHSATVNMCRDLLQQAREHIKRHENLPHFLQNTDATFQHLKEQLLLQQQVNIKTVHNLTGTVLHTNLGRALWSPAAQQAALDAMQGNVALEYDLSAGERSHRDNYISALMQQLTGAEAACVVNNNAAAVLLMLATFAQGKEVIISRGELIEIGGAFRIPDIMAQAGCKLVEVGTTNRTHLKDYRNAINENTAFLMKVHSSNYQICGFTHSVDEQELADLGKEFGIPVITDLGSGALMDLKQFGLPEEPTVQEKLQHGVDLISFSGDKLLGGPQAGIIVGKKALIQQLQAHPLKRVLRCDKVTLAGLEATFRLYLQPEKITEKLTALLLLTQPMERLQAQAEQLKVRLENRLNTNYVIAIEPSEAQIGSGSQPLARIPSVAVTIAPASEKTPAKTTALFARLLALPQPVIGRIERDKIWLDLHSLASLDRLLNSLETL","620021","","selenium transferase (Cysteinyl-tRNA(Sec) selenium transferase)","Cytoplasm","","
InterPro
IPR004534
Family
L-seryl-tRNA selenium transferase
PF03841\"[82-452]TSelA
TIGR00474\"[23-463]TselA: L-seryl-tRNA selenium transferase


","BeTs to 9 clades of COG1921COG name: Selenocysteine synthase seryl-tRNASer selenium transferaseFunctional Class: EThe phylogenetic pattern of COG1921 is --mp---q------ef-h--uj----Number of proteins in this genome belonging to this COG is","","Residues 367 to 464 match (2e-22) PD:PD579642 which is described as TRANSFERASE SELENIUM SYNTHASE PROTEOME COMPLETE SELENOCYSTEINE PYRIDOXAL PHOSPHATE L-SERYL-TRNASEC TRNASEC ","","","","","","","","","","","","Wed Dec 18 13:17:11 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00894 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 82 to 452 (E-value = 2.6e-226) place AA00894 in the SelA family which is described as L-seryl-tRNA selenium transferase (PF03841)","","","","","Thanbichler M, Bock A. Selenoprotein biosynthesis: purification and assay of componentsinvolved in selenocysteine biosynthesis and insertion in Escherichiacoli. Methods Enzymol. 2002;347:3-16. PMID: 11898420 Engelhardt H, Forchhammer K, Muller S, Goldie KN, Bock A. Structure of selenocysteine synthase from Escherichia coli and locationof tRNA in the seryl-tRNA(sec)-enzyme complex. Mol Microbiol. 1992 Dec;6(23):3461-7. PMID: 1474891","","Wed Dec 18 13:17:11 2002","1","","","" "AA00895","621529","621425","105","ATGAGAAAAAAATTGGCGATAGTGTATCTAATGCGTAAGCAAAAGCAAGCAGGAAATCAGGTTTCGCGCCTTTTCGCCGCGATTTCATCCGCCAATTTCAGCGCA","","","3910","MRKKLAIVYLMRKQKQAGNQVSRLFAAISSANFSA","621425","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database. ","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:28:52 2004","Mon Feb 23 15:28:52 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00895 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:28:52 2004","","","","","","","","","","","","","1","","","" "AA00896","621554","623266","1713","ATGCGTACAAGTAAATATTTATTATCCACCTTAAAAGAAACCCCGGCAGAAGCGGCGGTGGTGAGCCACCAATTAATGTTGCGTGCGGGCATGATTCGTCCTCTCGCGTCCGGTTTATATAATTGGTTGCCGACCGGGCTTCGCGTATTAAAGAAAGTTGAAAATATTATTCGTGACGAAATGAATAAAAGCGGCGCCATTGAAGTGGAAATGCCGGTGGTGCAACCGGCGGAGTTGTGGCAGGAATCCGGTCGCTGGGAGCAATACGGTCCGGAATTGCTGCGTTTTGAGGATCGTGGCAACCGTAATTTTGTGTTAGGTCCGACTCACGAAGAAGTGATCACCGATTTAGTGCGTCGTGAAGTGAGTTCTTATCGTCAACTTCCCCTCAATTTGTATCAAATTCAAACCAAATTCCGCGATGAAGTGCGTCCGCGTTTCGGCGTGATGCGCGGGCGTGAATTTTTAATGAAAGATGCCTATTCCTTCCACACGTCAAAAGAAAGTTTGCAGGAAACCTACGATGTGATGTACCAAACCTACAGCAACATTTTCACCCGCTTAGGCTTGGATTTTCGCGCCGTGCAGGCGGACACCGGTTCCATCGGCGGCAGTGCGTCCCATGAGTTCCAAGTGCTTGCCAACAGCGGCGAAGATGATGTGATTTTCTCCACCGAATCCGATTACGCGGCAAATATTGAACTTGCCGAAGCCGTTGCCGTCGGCGAACGTGCGCAACCGACCAAAGCCATGGAATTAGTGGATACGCCGAAGGCAAAAACCATTGCGGAATTGGTGGAACAGTTCAATCTGCCGATTGAAAAAACCGTGAAAACTTTGATTGTGAAAGGCGCAAACGAAGAACAGCCGTTGGTGGCGTTAATCCTTCGTGGCGACCATGAATTAAATGAAGTGAAAGCGGAAAAACTGGCGGAAGTGGCTTCTCCCCTTGAATTTGCCGATGAAGCCGCCATTAAAGCGAAAATCGGCGCCGGCGTGGGTTCACTCGGTCCGGTCAACTTAAACATTCCGGTGATTATTGACCGCAGCGTGGCGTTAATGAGTGATTTCGGCGCCGGCGCCAATATTGACGGCAAGCATTATTTCAACATTAACTGGGAACGTGATGTGGCGTTGCCGAAAATCGCCGACATTCGTAATGTGGTGGAAGGCGATCCGAGCCCGGACGGCAAGGGCACGCTGTTGATTAAACGCGGCATTGAAGTGGGCCATATTTTCCAATTAGGCGACAAATATTCCCAAGCCATGAACGCTACCGTGCAAGGCGAAGACGGTCGCCCAATGGTGGTTACCATGGGCTGTTACGGTATCGGTGTGACCCGCGTGGTTGCCGCTGCCATCGAACAACATCACGATGAACGTGGCATTATTTGGCCGTCCGACGCCATTGCGCCGTTCAGCGTGGCGATTGTGCCGATGAATATGTACAAATCGGAAAGCGTGCAACAATTTGCCGAAGATTTATACCGCACTTTACAGGCGCAGGGCGTGGAAGTGATTTTCGATGACCGCAAAGAACGCCCGGGCGTGATGTTCGCCGACATGGAACTGATCGGCGTGCCGCATATGGTCGTCATCGGCGAGAAGAATCTGGCAAACGGTGAAATCGAATATAAAAATCGTCGCACCGGAGAGAAGCAGATGATCGCCAAAGCGCAGTTGTTGGATTTCCTGAAAAGCCAAATTAACGTA","","","63516","MRTSKYLLSTLKETPAEAAVVSHQLMLRAGMIRPLASGLYNWLPTGLRVLKKVENIIRDEMNKSGAIEVEMPVVQPAELWQESGRWEQYGPELLRFEDRGNRNFVLGPTHEEVITDLVRREVSSYRQLPLNLYQIQTKFRDEVRPRFGVMRGREFLMKDAYSFHTSKESLQETYDVMYQTYSNIFTRLGLDFRAVQADTGSIGGSASHEFQVLANSGEDDVIFSTESDYAANIELAEAVAVGERAQPTKAMELVDTPKAKTIAELVEQFNLPIEKTVKTLIVKGANEEQPLVALILRGDHELNEVKAEKLAEVASPLEFADEAAIKAKIGAGVGSLGPVNLNIPVIIDRSVALMSDFGAGANIDGKHYFNINWERDVALPKIADIRNVVEGDPSPDGKGTLLIKRGIEVGHIFQLGDKYSQAMNATVQGEDGRPMVVTMGCYGIGVTRVVAAAIEQHHDERGIIWPSDAIAPFSVAIVPMNMYKSESVQQFAEDLYRTLQAQGVEVIFDDRKERPGVMFADMELIGVPHMVVIGEKNLANGEIEYKNRRTGEKQMIAKAQLLDFLKSQINV","623268","","prolyl-tRNA synthetase (proline-tRNA ligase)","Cytoplasm","","
InterPro
IPR002314
Domain
tRNA synthetase, class II (G, H, P and S)
PF00587\"[49-219]TtRNA-synt_2b
InterPro
IPR002316
Family
Prolyl-tRNA synthetase, class IIa
PR01046\"[68-86]T\"[104-115]T\"[134-142]T\"[144-155]TTRNASYNTHPRO
InterPro
IPR004154
Domain
Anticodon-binding
G3DSA:3.40.50.800\"[468-570]Tno description
PF03129\"[474-568]THGTP_anticodon
InterPro
IPR004500
Family
Prolyl-tRNA synthetase, bacterial
TIGR00409\"[1-568]TproS_fam_II: prolyl-tRNA synthetase
InterPro
IPR006195
Domain
Aminoacyl-transfer RNA synthetase, class II
PS50862\"[38-466]TAA_TRNA_LIGASE_II
InterPro
IPR007214
Domain
YbaK/prolyl-tRNA synthetase associated region
PF04073\"[251-385]TYbaK
noIPR
unintegrated
unintegrated
G3DSA:3.30.930.10\"[5-466]Tno description
PTHR11451\"[38-252]T\"[329-570]TTRNA SYNTHETASE-RELATED
PTHR11451:SF3\"[38-252]T\"[329-570]TPROLYL-TRNA SYNTHETASE


","BeTs to 25 clades of COG0442COG name: Prolyl-tRNA synthetaseFunctional Class: JThe phylogenetic pattern of COG0442 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 401 to 447 match (5e-09) PD:PD549222 which is described as LIGASE SYNTHETASE AMINOACYL-TRNA PRORS ATP-BINDING PROLINE--TRNA PROLYL-TRNA BIOSYNTHESIS ","","","","","","","","","","","","Wed Dec 18 13:19:08 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00896 is paralogously related to AA02030 (4e-11) and AA02724 (0.001).","","","","","","Residues 474 to 568 (E-value = 4.2e-30) place AA00896 in the HGTP_anticodon family which is described as Anticodon binding domain (PF03129)","","","","","Beuning PJ, Musier-Forsyth K. Species-specific differences in amino acid editing by class II prolyl-tRNAsynthetase. J Biol Chem. 2001 Aug 17;276(33):30779-85. PMID: 11408489 Stathopoulos C, Li T, Longman R, Vothknecht UC, Becker HD, Ibba M, Soll D.One polypeptide with two aminoacyl-tRNA synthetase activities. Science. 2000 Jan 21;287(5452):479-82. PMID: 10642548","","Wed Dec 18 13:19:08 2002","1","","","" "AA00899","623354","623539","186","TTGGCGATTTCCATTTGTTTGGAAATTGTCGCGACCAACCTGCTGAAAGTGAGCGATGGTTTCACCAAATTGGTACCGACCCTTGGTGCGCTGGCTTTTTATGGTTGTTCATTTTATTTTGTTTCCATTATTTTTCGTACGCTGTCGGTGGGCCTGGTGATTAATTTATTTTCGCAAACCTCGCAC","","","6696","LAISICLEIVATNLLKVSDGFTKLVPTLGALAFYGCSFYFVSIIFRTLSVGLVINLFSQTSH","623541","","possible quaternary ammonium compound resistance protein","Cytoplasm, Inner membrane","","
InterPro
IPR000390
Family
Small multidrug resistance protein
PF00893\"[1-42]TMulti_Drug_Res
noIPR
unintegrated
unintegrated
signalp\"[1-12]?signal-peptide
tmhmm\"[38-58]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Jan 22 17:03:32 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00899 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Sidhu MS, Langsrud S, Holck A.Disinfectant and antibiotic resistance of lactic acid bacteria isolated from the food industry.Microb Drug Resist. 2001 Spring;7(1):73-83.PMID: 11310806 Heir E, Sundheim G, Holck AL.Identification and characterization of quaternary ammonium compound resistant staphylococci from the food industry.Int J Food Microbiol. 1999 Jun 1;48(3):211-9. PMID: 10443540 Heir E, Sundheim G, Holck AL.The Staphylococcus qacH gene product: a new member of the SMR family encoding multidrug resistance.FEMS Microbiol Lett. 1998 Jun 1;163(1):49-56.PMID: 9631545","","Wed Dec 18 13:23:51 2002","1","","","" "AA00900","623582","623833","252","ATGAAAGATTATGATCCGTTTCGCATTGAGTGGGATTGCCGACGCGGTATGTTGGAGTTGGATAAAGTGATTATGCCTTTTTATCAGCAACATTTTGCCCAATTAAGCGAACACCAAAAGGCTGTTTTTGTGCGCTTGCTGGCGTGTTCCGACTTGCAATTGTTTTCGTGGTTTTTTAATAACGGCACGATCGACGACCCGGAATTGTGCAAAATGGTGGCGGAAATTCAACAAAAATTAAATTTAACAAAT","","","10802","MKDYDPFRIEWDCRRGMLELDKVIMPFYQQHFAQLSEHQKAVFVRLLACSDLQLFSWFFNNGTIDDPELCKMVAEIQQKLNLTN","623835","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR005631
Family
Protein of unknown function DUF339
PF03937\"[1-79]TDUF339
noIPR
unintegrated
unintegrated
G3DSA:1.10.150.250\"[4-77]Tno description


","BeTs to 7 clades of COG2938COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG2938 is ------y-------efghsn-jx---Number of proteins in this genome belonging to this COG is","","Residues 8 to 76 match (4e-11) PD:PD479021 which is described as PROTEOME COMPLETE VC2471 BMEII0687 NMA1147 CYTOSOLIC ","","","","","","","","","","","","Wed Dec 18 14:03:48 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00900 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 79 (E-value = 2.8e-25) place AA00900 in the TPR_div1 family which is described as TPR repeat region (PF03937)","","","","","","","","1","","","" "AA00902","623969","624541","573","ATGGCTGAACAGCTAACAGATCAAGCTTTGGTAGAGAGGGTGCAGCAGGGCGATAAGAAAGCTTTCAACTTATTGGTATCGCGTTATCAAAATAAAGTGGCTGGATTACTGACTCGGTATATTTCACCGAATGATATTCCTGATGTTGTACAAGAATCATTTATAAAAGCGTATCGTTCCATTGATTCTTTTCGTGGTGATAGCGCCTTCTACACTTGGCTATATAGAATTGCAGTAAATACGGCAAAAAATTACTTAACTGCCCAGGGTCGTCGTCCGCCAAATGAAGATATTTTGGCTGAAGATGCGGAATCCTACGATGTGGGGACAAATTTACGGGATGTGGATACGCCCGAAAATGAGATGTTATCCAATGAATTGAAAAAGATTGTGTTTGATACGATCAAAAGCTTGCAGGAAGATTTACGCACGGCAATTACTTTACGCGAAATCGAAGGATTGAGTTATGAAGAAATTGCGGAAATCATGGATTGCCCTGTGGGAACCGTCAGATCGCGGATTTTCAGAGCGCGTGAAATCATTGAAAGCAAGGTCAAACCGCTTTTACAACGT","","","21895","MAEQLTDQALVERVQQGDKKAFNLLVSRYQNKVAGLLTRYISPNDIPDVVQESFIKAYRSIDSFRGDSAFYTWLYRIAVNTAKNYLTAQGRRPPNEDILAEDAESYDVGTNLRDVDTPENEMLSNELKKIVFDTIKSLQEDLRTAITLREIEGLSYEEIAEIMDCPVGTVRSRIFRAREIIESKVKPLLQR","624543","","RNA polymerase sigma-E factor sigma-24","Cytoplasm","","
InterPro
IPR000838
Domain
RNA polymerase sigma factor 70, ECF
PS01063\"[46-77]TSIGMA70_ECF
InterPro
IPR007627
Domain
RNA polymerase sigma-70 region 2
PF04542\"[25-92]TSigma70_r2
InterPro
IPR013249
Domain
RNA polymerase sigma factor 70, region 4 type 2
PF08281\"[128-181]TSigma70_r4_2
InterPro
IPR014284
Domain
RNA polymerase sigma-70
TIGR02937\"[20-185]Tsigma70-ECF: RNA polymerase sigma factor, s
InterPro
IPR014286
Family
RNA polymerase sigma-70 RpoE type
TIGR02939\"[1-189]TRpoE_Sigma70: RNA polymerase sigma factor R
noIPR
unintegrated
unintegrated
G3DSA:1.10.1740.10\"[9-94]Tno description


","BeTs to 12 clades of COG1595COG name: DNA-directed RNA polymerase specialized sigma subunits, sigma24 homologsFunctional Class: KThe phylogenetic pattern of COG1595 is --------vdrlbcefghsn-j--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 2.7e-44) to 2/2 blocks of the IPB000838 family, which is described as \"Sigma factor, ECF subfamily\". Interpro entry for IP:IPR000838. IPB000838A 48-84 3.2e-19 IPB000838B 135-181 7.4e-24","Residues 87 to 130 match (4e-14) PD:PD572714 which is described as FACTOR RNA POLYMERASE SIGMA TRANSCRIPTION PROTEOME REGULATION DNA-BINDING DNA-DIRECTED COMPLETE ","","","","","","","","","","","","Wed Dec 18 14:06:32 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00902 is paralogously related to AA00948 (2e-07).","","","","","","Residues 134 to 183 (E-value = 4.4e-13) place AA00902 in the Sigma70_r4 family which is described as Sigma-70, region 4 (PF04545)","","","","","Yu,H., Schurr,M.J. and Deretic,V. Functional equivalence of Escherichia coli sigma E and Pseudomonas aeruginosa AlgU: E. coli rpoE restores mucoidy and reduces sensitivity to reactive oxygen intermediates in algU mutants of P. aeruginosa J. Bacteriol. 177 (11), 3259-3268 (1995) M:95286510 Rouviere,P.E., De Las Penas,A., Mecsas,J., Lu,C.Z., Rudd,K.E. and Gross,C.A. rpoE, the gene encoding the second heat-shock sigma factor, sigma E, in Escherichia coli EMBO J. 14 (5), 1032-1042 (1995) M:95196747 Lonetto,M.A., Brown,K.L., Rudd,K.E. and Buttner,M.J. Analysis of the Streptomyces coelicolor sigE gene reveals the existence of a subfamily of eubacterial RNA polymerase sigma factors involved in the regulation of extracytoplasmic functions Proc. Natl. Acad. Sci. U.S.A. 91 (16), 7573-7577 (1994) M:94329558 Raina,S., Missiakas,D. and Georgopoulos,C. The rpoE gene encoding the sigma E (sigma 24) heat shock sigma factor of Escherichia coli EMBO J. 14 (5), 1043-1055 (1995) M:95196748 ","","Tue Feb 4 14:29:05 2003","1","","","" "AA00904","624583","625164","582","ATGCAAAAAGAATTACTTTCAGCATACATTGACGGTGAGCAAGTCAGCAGTGAACTCACCGAACAATTATGCCAAGATGCGGAATTGCAAGAAAGCTGGGCGAATTTTCATACAATTCGCGCGGTGATGCGTCAGGAGACAAATGTTTTCTTAAGTGCTGATTTCACTGCGAAAATGGAAAGTCTGATTGCGGAAGAAGAAATTGTTGTCGCACAACCGACCGTTTCTCAACCGTTACCGCAAGAAGTCGAATCTTCTCCGTTCATGCAAAAACTCAAATCATGGTTTGTGCCGATGACACAGGTTGCGGTGGCGGCGGGCGTCTGCTTAGTGGCTGTGTTAGGCGTGCAATCTTTGAACAGCAAGTCTGCGGTGCAAAATGCGCCGGATACCCCGGTGTTGCAAACATTACCGTTTAATAACGGGGTGCAGGAAGTGAGTTATAATGCGCCAAGTAAAGATGTGATTACCACCGAGCAGTTGGAACAAAAAAATAAACGTATCGGTGCGATGTTACAAAGTTACGAGTTACAACGTCGGGTTTACGGCGATTCCTTGAGTTTGGAACAAACCAGCGCCAAG","","","21469","MQKELLSAYIDGEQVSSELTEQLCQDAELQESWANFHTIRAVMRQETNVFLSADFTAKMESLIAEEEIVVAQPTVSQPLPQEVESSPFMQKLKSWFVPMTQVAVAAGVCLVAVLGVQSLNSKSAVQNAPDTPVLQTLPFNNGVQEVSYNAPSKDVITTEQLEQKNKRIGAMLQSYELQRRVYGDSLSLEQTSAK","625166","","sigma-E factor negative regulatory factor","Outer membrane, Periplasm","","
InterPro
IPR005572
Family
Anti sigma-E protein RseA, N-terminal
PF03872\"[1-87]TRseA_N
InterPro
IPR005573
Domain
Anti sigma-E protein RseA, C-terminal
PF03873\"[129-194]TRseA_C
noIPR
unintegrated
unintegrated
tmhmm\"[95-115]?transmembrane_regions


","BeTs to 4 clades of COG3073COG name: Negative regulator of sigma E activityFunctional Class: TThe phylogenetic pattern of COG3073 is --------------efghs-------Number of proteins in this genome belonging to this COG is","","Residues 1 to 186 match (4e-58) PD:PD022787 which is described as PROTEOME COMPLETE REGULATORY NEGATIVE SIGMA-E FACTOR SIGMA E RSEA FACTOR ","","","","","","","","","","","","Wed Dec 18 14:10:23 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00904 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 129 to 194 (E-value = 1.3e-24) place AA00904 in the RseA_C family which is described as Anti sigma-E protein RseA, C-terminal domain (PF03873)","","","","","Alba BM, Leeds JA, Onufryk C, Lu CZ, Gross CA. DegS and YaeL participate sequentially in the cleavage of RseA toactivate the sigma(E)-dependent extracytoplasmic stress response. Genes Dev. 2002 Aug 15;16(16):2156-68. PMID: 12183369 Kanehara K, Ito K, Akiyama Y. YaeL (EcfE) activates the sigma(E) pathway of stress response through asite-2 cleavage of anti-sigma(E), RseA. Genes Dev. 2002 Aug 15;16(16):2147-55. PMID: 12183368 Tam C, Collinet B, Lau G, Raina S, Missiakas D. Interaction of the conserved region 4.2 of sigma(E) with the RseAanti-sigma factor. J Biol Chem. 2002 Jul 26;277(30):27282-7. PMID: 12016219 Collinet B, Yuzawa H, Chen T, Herrera C, Missiakas D. RseB binding to the periplasmic domain of RseA modulates the RseA:sigmaEinteraction in the cytoplasm and the availability of sigmaE.RNApolymerase. J Biol Chem. 2000 Oct 27;275(43):33898-904. PMID: 11777003 ","","Wed Dec 18 14:10:23 2002","1","","","" "AA00906","625250","626203","954","ATGTTAAAAACGCTTCTGAAAACCACCGCACTTTTCTTATTGTTGAGCTGTTCGCTTTCCTCCGTGGCGCAAGAGAATCTTTCGCCGAAGCAACTTTTAGGCGAAATGAAAAAAGCCGCGCAGCAGTTAAATTACGAATTTTCTTTCGTGCAAACCACACCGTCAAATATGGATTCTCTGCGCTATCGCCATTTTGTCGCCGACGGCAAAACTTATGCTCAGCTGGTTACGCTAGACGGTCCGCAACAAGAAATTGTGCAACGGGAGAATTTAATCAGTTATTTCCAGCCGAACTATCAGGCGTTTACCATTAACGGCTCCGGCATTATTGATAATTTACCGCCGTTGTCGCGTGCTAATTTTGATGCTTTGGAAAAATATTATGATTTCGTGAATATCGGGCGCAACCGTGTGGCGGATCATGTGGTGCAAACCATCCGAATTCTGCCGAAAGACGATTTCCGCTATCAGTATCTGGCGTTTATTGACGAAGAAAATCACCTGTTATTACGCACCGATATGCTTGATCGCGAAGGCAATTTATTAGATCAGTTCCGTGTGGTGAATTTATATATCGGCAATGAATTATCCGGCTTGCCGGCGTATTTGAACCGCGTCGTTTTCCCGCCGTTGTTAATGGATCAAAAAGCCAATAATCCCCCCGCGTTTAAATGGCAGCCCGGCTGGCTTCCACAAGGGTTTAAATTAGTGAATCATAGCATTGAATTGGACGGTGAAGAGAAAATTGAATCGCAACTTTACAGCGACGGTTTATTTTCTTTCACATTATATGTTTCCGATAAAATCGCCGAATCCACGCAGCAGGATAACACGTGGCGGCAGGGCGCTTACACGATTTATACCGAAAGCATGGAAAACAAAGAGATGACCATTATCGGGCAACTGCCGATTTCCACGGCAAAACGCATTGTGCAAGACATTGAATTCAGAAAA","","","37900","MLKTLLKTTALFLLLSCSLSSVAQENLSPKQLLGEMKKAAQQLNYEFSFVQTTPSNMDSLRYRHFVADGKTYAQLVTLDGPQQEIVQRENLISYFQPNYQAFTINGSGIIDNLPPLSRANFDALEKYYDFVNIGRNRVADHVVQTIRILPKDDFRYQYLAFIDEENHLLLRTDMLDREGNLLDQFRVVNLYIGNELSGLPAYLNRVVFPPLLMDQKANNPPAFKWQPGWLPQGFKLVNHSIELDGEEKIESQLYSDGLFSFTLYVSDKIAESTQQDNTWRQGAYTIYTESMENKEMTIIGQLPISTAKRIVQDIEFRK","626205","","sigma-E factor regulatory protein","Periplasm, Outer membrane, Cytoplasm","","
InterPro
IPR005588
Family
MucB/RseB
PF03888\"[6-317]TMucB_RseB
noIPR
unintegrated
unintegrated
signalp\"[1-23]?signal-peptide


","BeTs to 4 clades of COG3026COG name: Negative regulator of sigma E activityFunctional Class: TThe phylogenetic pattern of COG3026 is --------------efgh--------Number of proteins in this genome belonging to this COG is","","Residues 25 to 317 match (2e-113) PD:PD017730 which is described as PROTEOME COMPLETE REGULATORY FACTOR SIGMA-E RSEB SIGMA REGULATOR PERIPLASMIC SIGNAL ","","","","","","","","","","","","Wed Dec 18 14:18:03 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00906 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 6 to 317 (E-value = 1e-162) place AA00906 in the MucB_RseB family which is described as MucB/RseB family (PF03888)","","","","","Craig JE, Nobbs A, High NJ.The extracytoplasmic sigma factor, final sigma(E), is required for intracellular survival of nontypeable Haemophilus influenzae in J774 macrophages.Infect Immun. 2002 Feb;70(2):708-15.PMID: 11796603 Collinet B, Yuzawa H, Chen T, Herrera C, Missiakas D.RseB binding to the periplasmic domain of RseA modulates the RseA:sigmaE interaction in the cytoplasm and the availability of sigmaE.RNA polymerase.J Biol Chem. 2000 Oct 27;275(43):33898-904.PMID: 1177700De Las Penas A, Connolly L, Gross CA.The sigmaE-mediated response to extracytoplasmic stress in Escherichia coli is transduced by RseA and RseB, two negative regulators of sigmaE.Mol Microbiol. 1997 Apr;24(2):373-85.PMID: 9159523Missiakas D, Mayer MP, Lemaire M, Georgopoulos C, Raina S.Modulation of the Escherichia coli sigmaE (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins.Mol Microbiol. 1997 Apr;24(2):355-71.PMID: 9159522","","Tue Feb 4 14:31:17 2003","1","","","" "AA00908","626216","626650","435","ATGTTAACGGAAAGTGCGGTCGTTATTGAGTACGAATCCGGCAGAGCCAAAGTGAAATGCCAATCACAAAGCGCATGCGGCGCTTGCGCGGCAAAACCGGCGTGCGGTAATTCTGCCTTGTCGGAATTAGCCAGCAGCGGCGCGCGCGGCGAACATATTTTCACCATCGAGACCATTACGCCACTGAAAATCGGGCAACGGGTGGAAATCGGTTTGTCCGAACGTTCCTTAATCAAATCCGCCTTGCTCATGTATTGCGTGCCGCTATTTACTTTATTATTCAGCACGTTATTATTTGATTCGCTGTTTGCCCATGAGCTCGTCAGCGTCTTTTTTATCTTCATTTCCACTGCACTTTCTTTCCTTGGTGTGCGTTGGTATGCGCAAAAACTCAATCGCCAATCCGCCTACCAACCGGTGTTATTGCGCGTGTTA","","","15839","MLTESAVVIEYESGRAKVKCQSQSACGACAAKPACGNSALSELASSGARGEHIFTIETITPLKIGQRVEIGLSERSLIKSALLMYCVPLFTLLFSTLLFDSLFAHELVSVFFIFISTALSFLGVRWYAQKLNRQSAYQPVLLRVL","626652","","probable sigma-E factor regulatory protein","Cytoplasm, Inner membrane","","
InterPro
IPR000985
Domain
Legume lectin, alpha
PS00308\"[64-73]?LECTIN_LEGUME_ALPHA
InterPro
IPR007359
Family
Positive regulator of sigma(E), RseC/MucC
PF04246\"[7-145]TRseC_MucC
noIPR
unintegrated
unintegrated
PD010876\"[10-145]TQ9CK48_PASMU_Q9CK48;
tmhmm\"[81-101]?\"[107-127]?transmembrane_regions


","BeTs to 4 clades of COG3086COG name: Positive regulator of sigma E activityFunctional Class: TThe phylogenetic pattern of COG3086 is --------v-----efgh--------Number of proteins in this genome belonging to this COG is","","Residues 10 to 145 match (1e-27) PD:PD010876 which is described as PROTEOME COMPLETE REGULATORY FACTOR SIGMA-E RSEC MEMBRANE TRANSMEMBRANE INNER SIGMA ","","","","","","","","","","","","Wed Dec 18 14:23:36 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00908 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 145 (E-value = 2e-67) place AA00908 in the RseC_MucC family which is described as Positive regulator of sigma(E), RseC/MucC (PF04246)","","","","","Beck BJ, Connolly LE, De Las Penas A, Downs DM. Evidence that rseC, a gene in the rpoE cluster, has a role in thiaminesynthesis in Salmonella typhimurium. J Bacteriol. 1997 Oct;179(20):6504-8. PMID: 9335303 Beck BJ, Connolly LE, De Las Penas A, Downs DM.Evidence that rseC, a gene in the rpoE cluster, has a role in thiamine synthesis in Salmonella typhimurium.J Bacteriol. 1997 Oct;179(20):6504-8.PMID: 9335303Missiakas D, Mayer MP, Lemaire M, Georgopoulos C, Raina S.Modulation of the Escherichia coli sigmaE (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins.Mol Microbiol. 1997 Apr;24(2):355-71.PMID: 9159522","","Wed Dec 18 14:23:36 2002","1","","","" "AA00909","626734","627243","510","ATGCTCCCTATGCTCGGCATTACCGGTTACAGCGGCAGCGGCAAAACCACGTTATTGGAAAAATTGCTTCCGCAATTAAAACAGTGCGGTTTACGTCCCGCCGTGATTAAACACAGCCATCACGATGTACAAATTGACAAGCCGGGCAAAGACAGCTGGCGCATGAAAGATGCCGGTGCCAGTCAAGTAATTATGGCGTGTGACCAACGCTGGGCGCTGATGACCGAAACCCCGCAACAACATATTTCCCTGCCGTATTTGTGCACGCAATTTGACGAGGCGTTAGCGGATTTAATTTTAGTAGAGGGCTTCAAACAAGAACCCATCGAAAAGATACTGTTACATCGCAAAGACATGACCAGACCGCTTCCGGAAATCGATGAATATGTTCTGGCTGTCGCCACGGATTACCCCTTAACCGCCCACAAGCCTCACTTGGATATTAACGATATTAAACAAATCGCCCAGTTTATTGTGATGTGGTACGAACAAAAGTGCGGCGGAAAAAAA","","","24578","MLPMLGITGYSGSGKTTLLEKLLPQLKQCGLRPAVIKHSHHDVQIDKPGKDSWRMKDAGASQVIMACDQRWALMTETPQQHISLPYLCTQFDEALADLILVEGFKQEPIEKILLHRKDMTRPLPEIDEYVLAVATDYPLTAHKPHLDINDIKQIAQFIVMWYEQKCGGKK","627245","","molybdopterin-guanine dinucleotide biosynthesis protein B","Cytoplasm","","
InterPro
IPR003495
Domain
Cobalamin (vitamin B12) biosynthesis CobW-like
PF02492\"[3-36]TcobW
InterPro
IPR004435
Domain
Molybdopterin-guanine dinucleotide biosynthesis MobB region
PF03205\"[3-135]TMobB
TIGR00176\"[4-161]TmobB: molybdopterin-guanine dinucleotide bi
InterPro
IPR012249
Family
Molybdopterin-guanine dinucleotide biosynthesis MobB
PIRSF036622\"[2-167]TMolybdenum cofactor guanine dinucleotide biosynthesis adapter protein MobB
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[2-166]Tno description


","BeTs to 13 clades of COG1763COG name: Molybdopterin-guanine dinucleotide biosynthesis proteinFunctional Class: HThe phylogenetic pattern of COG1763 is aompkz-q----b-e-gh--uj----Number of proteins in this genome belonging to this COG is","Significant hit ( 2.1e-05) to 1/4 blocks of the PR00364 family, which is described as \"Disease resistance protein signature\". Prints database entry for PR:PR00364. PR00364A 4-19 2.2e-05Significant hit ( 6.1e-05) to 1/4 blocks of the IPB002891 family, which is described as \"Adenylylsulfate kinase\". Interpro entry for IP:IPR002891. IPB002891A 5-22 6.4e-05","Residues 5 to 50 match (6e-09) PD:PD008267 which is described as BIOSYNTHESIS PROTEOME COMPLETE DINUCLEOTIDE MOLYBDOPTERIN-GUANINE B GTP-BINDING MOLYBDENUM MOBB COFACTOR ","","","","","","","","","","","","Wed Dec 18 14:32:05 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00909 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 135 (E-value = 6e-56) place AA00909 in the MobB family which is described as Molybdopterin guanine dinucleotide synthesis protein B (PF03205)","","","","","Iobbi-Nivol,C., Palmer,T., Whitty,P.W., McNairn,E. and Boxer,D.H. The mob locus of Escherichia coli K12 required for molybdenum cofactor biosynthesis is expressed at very low levels Microbiology 141 (Pt 7), 1663-1671 (1995) PubMed: 7551035 Eaves,D.J., Palmer,T. and Boxer,D.H. The product of the molybdenum cofactor gene mobB of Escherichia coli is a GTP-binding protein Eur. J. Biochem. 246 (3), 690-697 (1997) PubMed: 9219527 ","","Wed Dec 18 14:26:13 2002","1","","","" "AA00909.1","626610","626110","501","TTGAGTTTTTGCGCATACCAACGCACACCAAGGAAAGAAAGTGCAGTGGAAATGAAGATAAAAAAGACGCTGACGAGCTCATGGGCAAACAGCGAATCAAATAATAACGTGCTGAATAATAAAGTAAATAGCGGCACGCAATACATGAGCAAGGCGGATTTGATTAAGGAACGTTCGGACAAACCGATTTCCACCCGTTGCCCGATTTTCAGTGGCGTAATGGTCTCGATGGTGAAAATATGTTCGCCGCGCGCGCCGCTGCTGGCTAATTCCGACAAGGCAGAATTACCGCACGCCGGTTTTGCCGCGCAAGCGCCGCATGCGCTTTGTGATTGGCATTTCACTTTGGCTCTGCCGGATTCGTACTCAATAACGACCGCACTTTCCGTTAACATAATCGCCTGCTATTTTCTGAATTCAATGTCTTGCACAATGCGTTTTGCCGTGGAAATCGGCAGTTGCCCGATAATGGTCATCTCTTTGTTTTCCATGCTTTCGGTA","8.50","5.37","18308","LSFCAYQRTPRKESAVEMKIKKTLTSSWANSESNNNVLNNKVNSGTQYMSKADLIKERSDKPISTRCPIFSGVMVSMVKICSPRAPLLANSDKAELPHAGFAAQAPHALCDWHFTLALPDSYSITTALSVNIIACYFLNSMSCTMRFAVEIGSCPIMVISLFSMLSV","","","hypothetical protein","Periplasm, Cytoplasm","No matches in gapped BLAST.AA00909.1 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus ducreyi gene.AA00909.1 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus influenzae Rd gene.","
noIPR
unintegrated
unintegrated
tmhmm\"[147-165]?transmembrane_regions


","No hits to the COGs database.","","","Fri Feb 27 09:23:09 2004","Sat Feb 28 16:48:47 2004","Sat Feb 28 16:48:47 2004","Sat Feb 28 16:48:47 2004","Fri Feb 27 09:23:09 2004","Fri Feb 27 09:23:09 2004","Fri Feb 27 09:23:09 2004","Fri Feb 27 09:23:09 2004","Fri Feb 27 09:23:09 2004","Fri Feb 27 09:23:09 2004","Fri Feb 27 09:23:09 2004","Fri Feb 27 09:23:09 2004","Fri Feb 27 09:23:09 2004","Fri Feb 27 09:23:09 2004","Fri Feb 27 09:23:09 2004","Fri Feb 27 09:23:09 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00909.1 has no significant similarity (blastp p-value < 1e-03) to any other gene in this genome.AA00909.1 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Fri Feb 27 09:23:09 2004","Fri Feb 27 09:23:09 2004","No hits to the PDB database.","","","No significant hits to the Pfam 7.7 database.","Fri Feb 27 09:23:09 2004","","","","","","","1","Fri Feb 27 09:23:09 2004","","" "AA00910","627228","627320","93","GTGCGGCGGAAAAAAATAATGTTTTTTCTTACCGCACTTCAAGTGCTTGCTCTTGCTAACGTGCGGTTATTTTTGGAGTTTATAAACTTGGAA","","","3690","VRRKKIMFFLTALQVLALANVRLFLEFINLE","627320","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-19]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 08:27:13 2004","Wed Feb 25 08:27:13 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00910 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 08:27:13 2004","","","","","","","","","","","","","1","","","" "AA00912","627340","628092","753","ATGAGAAACATCATTATCACCGGTGCCGGTGGGGATTTGGCGCAGGCAATCGTAAAACAACTGCCTGATGCCCGTTTGATTTTAATTGGCAGAGAAGCGGCGTTGTTGGAAAACCTGTATGCGTTTCATCCGCATAAAGCCTGTTTTCAGCTGGATATTTGCGATGAGCACGCTGTCGCTGCCTGCTTGCATGAGGTTGAGCAGCGTTATGGCGCGATAGATGTGTTGATCAATAACGCAGGCTATGCGGTGTATGATGATTTTGATTGCCTGACGACGGAAGAGGCGCGTAAGATGTTTGAAGTGAACGTGTTTGCCGGCATGGCCTTTTGCCAACTTGTCGGACACAACATGAAAGCGCTTGGGCGTGGGCATATCGTCAATATCGTTTCTATGTCGGGATTTTTGGCATCTGCCAAATCCAGTCTGTACTCCGCCAGTAAATTTGCCATGATCGGCTACTCCGACGCCATCCGTTTGGAACTGGCGGATAAAGGTGTATTCGTCACCACCGTCAACCCCGGTCCGATCGCCACTAAGTTCTTCAAACAGGCGGATCCCGAGGGGACTTATCTAAAATCTATCAAGCCCTTTTTAATTCCAGTGGATTTGGTAGCACAAAAAATCGTCATGGCGTTGGGAAAAAATGTACGTGAAATCAATTTACCCCGCACCCTTGCCTTTGCCCGTAAATTTTATGTGTTATTCCCCAAAACCGCCGATTTCCTGGCAAGAACGCTGTTTAATTATAAA","","","27688","MRNIIITGAGGDLAQAIVKQLPDARLILIGREAALLENLYAFHPHKACFQLDICDEHAVAACLHEVEQRYGAIDVLINNAGYAVYDDFDCLTTEEARKMFEVNVFAGMAFCQLVGHNMKALGRGHIVNIVSMSGFLASAKSSLYSASKFAMIGYSDAIRLELADKGVFVTTVNPGPIATKFFKQADPEGTYLKSIKPFLIPVDLVAQKIVMALGKNVREINLPRTLAFARKFYVLFPKTADFLARTLFNYK","628094","","short-chain dehydrogenase","Cytoplasm","","
InterPro
IPR002198
Family
Short-chain dehydrogenase/reductase SDR
PR00080\"[71-82]T\"[124-132]T\"[144-163]TSDRFAMILY
PTHR19410\"[2-221]TSHORT-CHAIN DEHYDROGENASES/REDUCTASE FAMILY MEMBER
PF00106\"[2-163]Tadh_short
PS00061\"[131-159]TADH_SHORT
InterPro
IPR002347
Family
Glucose/ribitol dehydrogenase
PR00081\"[3-20]T\"[71-82]T\"[118-134]T\"[144-163]T\"[165-182]TGDHRDH
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[2-251]Tno description
PTHR19410:SF44\"[2-221]TDEHYDROGENASE, SHORT CHAIN PROTEIN 30-RELATED


","BeTs to 6 clades of COG0300COG name: Short-chain dehydrogenases of various substrate specificitiesFunctional Class: RThe phylogenetic pattern of COG0300 is -o----y---rlb-ef-hsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 6e-11) to 1/1 blocks of the IPB002198 family, which is described as \"Short-chain dehydrogenase/reductase (SDR) superfamily\". Interpro entry for IP:IPR002198. IPB002198 124-159 5.8e-11","Residues 69 to 119 match (5e-07) PD:PD126102 which is described as OXIDOREDUCTASE COMPLETE PROTEOME DEHYDROGENASE SHORT-CHAIN REDUCTASE PROBABLE DEHYDROGENASE/REDUCTASE CHAIN SHORT ","","","","","Wed Feb 19 08:26:07 2003","","","","","","","Wed Dec 18 14:38:26 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00912 is paralogously related to AA00269 (9e-15), AA02205 (2e-14), AA01109 (4e-12), AA01179 (1e-09) and AA02383 (1e-08).","","","","","","Residues 4 to 240 (E-value = 1.5e-27) place AA00912 in the adh_short family which is described as short chain dehydrogenase (PF00106)","","","","","","","","1","","","" "AA00914","629635","628178","1458","ATGTCAGAAATACAAAAATTAACCCCGAATTTACTCTGGAAATGGTTCGATCAAATTTGTGCCATTCCCCATCCGTCTTATCAAGAAAATGCCCTGGCGGAATTCATCGTTAATTGGGCAAAAGGCAAAGCTTTTTACGCCGAACGCGATGAAGCGGGCAACGTGTTAATTCGCAAACCGGCAACAAAAGGCATGGAAAATCGCCGAAAAGTCGCCCTTCAGGCGCATTTGGATATGGTGCCGCAAGCCAACGAAGGCAGCTTGCATAATTTTGCCACCGATCCGATTCAACCTTATATCGACGGCGAATGGGTGCGTGCCACCAACACCACATTAGGCGCCGATAACGGCATCGGTATGGCGGCGACCTTAGCGGTGCTGGACAGCGACGACTTACCGCATCCTGATCTCGAAGTGTTACTCACTATGACAGAAGAACGCGGCATGGAAGGCGCCATTGGGTTACGCCCAAACTGGTTGCAAAGCGACATCATGATCAACACCGACACGGAAGAAAACGCGGAAATTTATGTGGGCTGTGCCGGCGGTGAAAACGCCAACATTTCGTTGCCCGTTGAATATGAAAACAACCGTTTCGCGCATAGTACGCAAATCGTGTTAAAAGGCTTACGCGGCGGGCATTCCGGCTGTGATATCCACACCGGACGCGCCAATGCCATCAAATTGCTGGTTCGCTTCCTGGCAAAACTCGCTCAAAATCAACCGCACTTTGATTTCGCGTTAAGCGATATTCGCGGTGGTTCCATCCGCAACGCCATTCCGCGCGAAGCCTTTGCCACCTTAAACTTCAACGGTGATGTTGACAGGCTGAAAAGTGCGGTGGAAAATTTCGGCGTTTTATTGAAGACCGAATTGGCATTAATTGAACCGAATCTTTCTTTCGAATTGCAACCGATTGATAAACCGACAAAGATTTTCACACCATTAACCACAGAACACATTATCCATTTATTAAATGTATTGCCGAATGGCGTAATTCGCAACAGCGATGTGTTGGAAAATATTGTGGAAACTTCGCTTAGCGTCGGCGTGTTAGAAACCGAAGAAAATTGGATTAAAGCCACCATTTTAGTGCGCTCGCTGATTGACAGCGGCAAAGAATATGTTGCCGAAATGTTGAAATCCTTGGCACAATTGAGCGATGCAAAAGCCGAATTCTCCGGCTCTTATCCTGGCTGGGAACCGCAAGCGCATTCACCGATTGTGGACTTAACCTACAAAATTTATGCGCAAGTGCTGGGCTACGAACCGGCTATTAAAGTGATTCACGCCGGCTTGGAATGTGGTTTGCTGAAGAAAATTTACCCAAATATGGACATGGTTTCCATCGGCCCGACCATCAAAAATGCCCACTCCCCGGACGAAAAAGTCCACATCCCGGCAGTGCAAATTTTCTGGTCGTTAATCACCAAATTATTAGCCGAAATTCCGGTTAAA","","","53695","MSEIQKLTPNLLWKWFDQICAIPHPSYQENALAEFIVNWAKGKAFYAERDEAGNVLIRKPATKGMENRRKVALQAHLDMVPQANEGSLHNFATDPIQPYIDGEWVRATNTTLGADNGIGMAATLAVLDSDDLPHPDLEVLLTMTEERGMEGAIGLRPNWLQSDIMINTDTEENAEIYVGCAGGENANISLPVEYENNRFAHSTQIVLKGLRGGHSGCDIHTGRANAIKLLVRFLAKLAQNQPHFDFALSDIRGGSIRNAIPREAFATLNFNGDVDRLKSAVENFGVLLKTELALIEPNLSFELQPIDKPTKIFTPLTTEHIIHLLNVLPNGVIRNSDVLENIVETSLSVGVLETEENWIKATILVRSLIDSGKEYVAEMLKSLAQLSDAKAEFSGSYPGWEPQAHSPIVDLTYKIYAQVLGYEPAIKVIHAGLECGLLKKIYPNMDMVSIGPTIKNAHSPDEKVHIPAVQIFWSLITKLLAEIPVK","628180","","aminoacyl-histidine dipeptidase; Beta-alanyl-histidine dipeptidase","Cytoplasm, Extracellular","","
InterPro
IPR001160
Family
Peptidase M20C, Xaa-His dipeptidase
PR00934\"[80-99]T\"[101-119]T\"[135-152]T\"[159-177]T\"[205-222]T\"[253-272]T\"[364-382]T\"[429-445]T\"[451-473]TXHISDIPTASE
PIRSF016599\"[1-486]TAminoacyl-histidine dipeptidase
TIGR01893\"[7-484]Taa-his-dipept: aminoacyl-histidine dipeptid
InterPro
IPR002933
Family
Peptidase M20
PF01546\"[72-482]TPeptidase_M20
InterPro
IPR011650
Domain
Peptidase M20, dimerisation
PF07687\"[205-296]TM20_dimer
noIPR
unintegrated
unintegrated
G3DSA:3.40.630.10\"[9-480]Tno description
PTHR11014\"[7-304]T\"[396-486]TPEPTIDASE M20 FAMILY MEMBER
PTHR11014:SF2\"[7-304]T\"[396-486]TAMINOACYL-HISTIDINE PEPTIDASE


","BeTs to 6 clades of COG2195COG name: Di- and tripeptidasesFunctional Class: EThe phylogenetic pattern of COG2195 is ---------d-lb-e-gh--uj--t-Number of proteins in this genome belonging to this COG is","Significant hit (1.6e-115) to 9/9 blocks of the PR00934 family, which is described as \"X-His dipeptidase (M25) signature\". Prints database entry for PR:PR00934. PR00934A 80-99 4.4e-14 PR00934B 101-119 3e-11 PR00934C 135-152 6.9e-11 PR00934D 159-177 2.5e-09 PR00934E 205-222 1.4e-11 PR00934F 253-272 1.8e-12 PR00934G 364-382 1.7e-11 PR00934H 429-445 5.2e-11 PR00934I 451-473 6.5e-12","Residues 18 to 156 match (3e-53) PD:PD591037 which is described as DIPEPTIDASE PROTEOME COMPLETE D XAA-HIS X-HIS MANGANESE AMINOACYL-HISTIDINE M20/M25/M40 PEPTIDASE ","","","","","","","","","","","","Fri Jan 24 13:24:48 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00914 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 16 to 485 (E-value = 4e-38) place AA00914 in the Peptidase_M20 family which is described as Peptidase family M20/M25/M40 (PF01546)","","","","","Henrich B, Monnerjahn U, Plapp R. Peptidase D gene (pepD) of Escherichia coli K-12: nucleotide sequence, transcript mapping, and comparison with other peptidase genes. J Bacteriol 1990 Aug;172(8):4641-51. PubMed: 1695895 ","","Wed Dec 18 14:46:09 2002","1","","","" "AA00915","629750","630211","462","ATGAGTGAAAAATATGTTGTGACGTGGGATATGTTCCATATGCACGCACGCAAATTATCCGAACGTTTGCTTCCGGCTTCACAGTGGAAAGGCATTGTTGCCGTGAGCCGTGGCGGTTTATTTCCGGCGGCGGTACTTGCCCGCGAATTAAGCATTCGTCATGTGGAAACTATTTGTATCGCCAGTTATAACCACGACACACAAGGCGAATTGCAGGTGTTACACGCCGCACAACTGGCGAACGGTGGTGAAGGATTTATCATCATTGACGATTTGGTGGATACCGGCAACACCGCGCGCGCTATTCGTGAAATGTACCCGAACGCCCGCCTTGTGACGGTTTTCGCGAAACCGGCCGGCGCGGAATTGGTAGATAATTATGTGGTAGATATTCCGCAAAATACCTGGATTGAACAACCTTGGGATATGGGCATTTGTTTCGTTCCTCCGCTTGCCAGAAAA","","","20105","MSEKYVVTWDMFHMHARKLSERLLPASQWKGIVAVSRGGLFPAAVLARELSIRHVETICIASYNHDTQGELQVLHAAQLANGGEGFIIIDDLVDTGNTARAIREMYPNARLVTVFAKPAGAELVDNYVVDIPQNTWIEQPWDMGICFVPPLARK","630213","","xanthine-guanine phosphoribosyltransferase","Cytoplasm","","
InterPro
IPR000836
Domain
Phosphoribosyltransferase
PF00156\"[1-132]TPribosyltran
InterPro
IPR002375
Family
Purine/pyrimidine phosphoribosyl transferase
PS00103\"[86-98]TPUR_PYR_PR_TRANSFER
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2020\"[1-154]Tno description


","BeTs to 5 clades of COG0503COG name: Adenine/guanine phosphoribosyltransferases and related PRPP-binding proteinsFunctional Class: FThe phylogenetic pattern of COG0503 is -om-kzy-vdrlbcefgh-nuj--twNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.6e-05) to 1/2 blocks of the IPB002375 family, which is described as \"Purine/pyrimidine phosphoribosyl transferase\". Interpro entry for IP:IPR002375. IPB002375B 83-98 1.6e-05","Residues 1 to 154 match (3e-76) PD:PD000249 which is described as TRANSFERASE GLYCOSYLTRANSFERASE PHOSPHORIBOSYLTRANSFERASE COMPLETE PROTEOME HYPOXANTHINE-GUANINE PURINE HYPOXANTHINE SALVAGE XANTHINE-GUANINE ","","","","","","","","","","","","Wed Dec 18 14:47:46 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00915 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 132 (E-value = 2.6e-14) place AA00915 in the Pribosyltran family which is described as Phosphoribosyl transferase domain (PF00156)","","","","","Gershanovitch VN, Yourovitskaya NV, Komissarova LV, Bolshakova TN,Erlagaeva RS, Bourd GI. Catabolite repression in Escherichia coli K12 mutants defective inglucose transport. Mol Gen Genet. 1975 Sep 15;140(1):81-90. PMID: 1102954 Jardim A, Bergeson SE, Shih S, Carter N, Lucas RW, Merlin G, Myler PJ, Stuart K, Ullman B. Xanthine phosphoribosyltransferase from Leishmania donovani. Molecularcloning, biochemical characterization, and genetic analysis. J Biol Chem. 1999 Nov 26;274(48):34403-10. PMID: 10567419 ","","Wed Dec 18 14:47:46 2002","1","","","" "AA00918","630184","630315","132","TTGTTTCGTTCCTCCGCTTGCCAGAAAATAAAAAACAATCAGAAAATCTACCGCACTTTTTTTGCACCTAATAAAAACCATGAGCAGAATAACTCACGGTTTTTTTTTATTTTTTCCCTTTCTAGTAAAGAC","","","5285","LFRSSACQKIKNNQKIYRTFFAPNKNHEQNNSRFFFIFSLSSKD","630315","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 08:29:02 2004","Wed Feb 25 08:29:02 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00918 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 08:29:02 2004","","","","","","","","","","","","","1","","","" "AA00919","632737","630308","2430","GTGCGCGTACAAAACGCCACATTAAACAATGCGATCCCCTACGTTTTACAGTATAATCCCATTAAATTTGGCTCAAATAATGGTTGTCCGATGAAGAAAAATTATTACACGTTAATTTCACTGTCAATTTTGACCGCACTTTATACTGCCGACAGCGCAGCAGACTTGAATCAGCAATGTTTATTAGGCGTACCGCATTTTACCGGAGAAGTGGTGACCGGCGATCCGAATGATCAGCCGGTGTACATTGAAGCGGATAAAGTAGAAATCAATCAGCCGAGCAGCGCCCTTTATCAAGGCAATGTGGACATCAAACAAGGTAACCGCCATTTGAAATCCGCGGCGGTGGAAATGCAACAATCGGGCGAAGGCGGCAATGTGCAGCGTTATGCCTTTGCGCGCGGCGGATTTGATTATCGCGACAACCAAATCAACTTACTCGGCAGCGATGCCAAAATCCATCTCAACAGCAAAGATACCGACATTCAACACGCCGATTATCAATTTGTTGATCGCCAAGGGCGCGGTTCGGCGAAAAGCGTGGAATTGCGCGAAGATTACCGCTTAATGAAAAACGCCACTTTTACCTCCTGTTTGCCGAATGATAATGCCTGGTCTATTTACGCCAGCGAAATGCGCCAACATGTGAAAGAAGAATATGCGGAAATGTGGCACGCCCGTTTTCGCGTGCATGGTGTACCGGTGTTCTACACACCGTATTTCCAACTGCCTATCGGCGATCGTCGTCGTTCCGGTTTGTTGGTACCTACCGCCGGACATTCCAGCCGCGGCGGTTATTTCTATGCACAACCGGTGTATTGGAACATCGCGCCGAATTACGACGCTACCATTGCGCCGAAATATATGTCAAAACGGGGTTGGCAGTTCAACGGCGAATTTCGTTATTTAACACCACTCGGTGAAGGGAAAATTGCCGGTGAATATTTAGGCAATGATCGATTAACGGATTACACGGCAGAAAATCGCAAACGCCATTTATTGCACTGGTTACACAGTTCCAGCTTTTTGGAAAATTGGCGCTTGAATGTGGATTATACACGGGTCAGCGACAAGCGTTATTTCACCGATTTTGATTCCGAATACGGCAGCAGTACGGATGGTTATGCCGATCAAAAAGCGCGTATTGCCTACTATCAACCGAATTACAACCTTGCCATTTCGGCAAAACAATTCCAGATTTTCGATGAAGTGGCCATTGGTCCATATCGTACTTTGCCGCAAATTGATTTCAATTATTACAAAAATAATTTATGGAATAACCTGGATTTCAAACTTTTTTCGCAAGCGGCACGCTTTGATAACGACAGCATTCAGATGCCAAAAGCCTGGCGTTTCCATTTGGAACCCGGCTTAAACAAAACCTTATCCAATCGTTATGGCAGCATTAACTTTGAAACCAAACTTTACGCAACCCATTATCAGCAAAAGAACGGAAGGATTGTTTCTGAAGATGAAAAGGTGGAACGCAGCGTAACCCGTGTATTACCGCAGTTTAAAGTAGAATTGCAAACGGTATTGGCATCCAATAAAACCTTGTTCAACGGTTATACCCAAACCCTCGAACCGCGCGTTCAATATTTATATCGCCCTTATAAGAATCAAGGCAATATCGGACCTAAAAATCCGCAATATCTTGGTTTCGGTTACGATTCTACTTTATTGCAACAGGATTATTTCTCCTTATTCCGTGACCGTCGTTACAGCGGTTTGGACCGAATAGCCTCTGCCAATCAGGTAACATTGGGAGGGACTACACGTTTCTTTGATGTGGAAAAAGAAGAACGCTTCAATTTTTCCATCGGGCAAACCTTTTATTTAAAGCCGTCCCGCATTGATGATAACCCGAATAATAAAACCTCCGGCGCATCTTCGTCATGGGCATTGGAATCCAACTGGAAAATAAGCGACCAATGGCGTTGGCGCGCAAGTTATCAATATGATCCGCAGTTAAAACAGGTTTCATTGGCAAATACCGGATTAGAATGGAATCCGCAAAAAGAGAATTTAATTCAGTTAACTTACCGTTATGCAAGCCAAAGATATATCGATCAAAACCTGGATGTCGGCGCTAATCGTTATAATCAGGATATTAAACAATTGGGCGTGCAGGCAGCGTGGGAAATCACCGACAATTGGGCGGTGGTCGGGCGTTATTATCAGGATTTGGCGCTGAAGAAACCGGTGGAACAATACCTTGGCGTACAATACAACTCCTGCTGTTGGAGCATCGGTGTAGGCGCCAGACGTTATGTCACCAGCCGCCAAAATCAAAAATATGATGAAATTTTCTATGATAACAGTATTGGCGTCACCTTCCAGTTGCGGGGATTTGGTAACGATCACAAAAATGGTATCGAAGAGTTATTAAAACGCGGAAAATTGCCGTATTTACAAGCCTTCAGTCTTTAC","","","93713","VRVQNATLNNAIPYVLQYNPIKFGSNNGCPMKKNYYTLISLSILTALYTADSAADLNQQCLLGVPHFTGEVVTGDPNDQPVYIEADKVEINQPSSALYQGNVDIKQGNRHLKSAAVEMQQSGEGGNVQRYAFARGGFDYRDNQINLLGSDAKIHLNSKDTDIQHADYQFVDRQGRGSAKSVELREDYRLMKNATFTSCLPNDNAWSIYASEMRQHVKEEYAEMWHARFRVHGVPVFYTPYFQLPIGDRRRSGLLVPTAGHSSRGGYFYAQPVYWNIAPNYDATIAPKYMSKRGWQFNGEFRYLTPLGEGKIAGEYLGNDRLTDYTAENRKRHLLHWLHSSSFLENWRLNVDYTRVSDKRYFTDFDSEYGSSTDGYADQKARIAYYQPNYNLAISAKQFQIFDEVAIGPYRTLPQIDFNYYKNNLWNNLDFKLFSQAARFDNDSIQMPKAWRFHLEPGLNKTLSNRYGSINFETKLYATHYQQKNGRIVSEDEKVERSVTRVLPQFKVELQTVLASNKTLFNGYTQTLEPRVQYLYRPYKNQGNIGPKNPQYLGFGYDSTLLQQDYFSLFRDRRYSGLDRIASANQVTLGGTTRFFDVEKEERFNFSIGQTFYLKPSRIDDNPNNKTSGASSSWALESNWKISDQWRWRASYQYDPQLKQVSLANTGLEWNPQKENLIQLTYRYASQRYIDQNLDVGANRYNQDIKQLGVQAAWEITDNWAVVGRYYQDLALKKPVEQYLGVQYNSCCWSIGVGARRYVTSRQNQKYDEIFYDNSIGVTFQLRGFGNDHKNGIEELLKRGKLPYLQAFSLY","630310","","organic solvent tolerance protein","Outer membrane, Extracellular","","
InterPro
IPR005653
Family
OstA-like protein
PF03968\"[36-220]TOstA
InterPro
IPR007543
Family
Organic solvent tolerance protein
PF04453\"[329-719]TOstA_C


","No hits to the COGs database.","","Residues 74 to 213 match (5e-07) PD:PD305692 which is described as SOLVENT OSTA PROTEOME COMPLETE ORGANIC PRECURSOR TOLERANCE ","","","","","","","","","","","","Wed Dec 18 14:56:34 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00919 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 317 to 719 (E-value = 2.3e-149) place AA00919 in the OstA_C family which is described as Organic solvent tolerance protein (PF04453)","","","","","Braun M, Silhavy TJ. Imp/OstA is required for cell envelope biogenesis in Escherichia coli. Mol Microbiol. 2002 Sep;45(5):1289-302. PMID: 12207697","","Wed Dec 18 14:59:05 2002","1","","","" "AA00920","633273","632716","558","ATGAAAAAACGTTGCACATGGGCGGAAAACTCACAAATTTATCAGGATTACCACGACAACGAATGGGGTAAACCACAATTTGATGATCGCAAATTATTTGAAAAACTGTGTCTGGAAGGGCAGCAAGCGGGCCTGTCGTGGATTACGGTATTAAAAAAACGGGAAGCTTATCGGCAGGCGTTTTTCCATTTTGATCCGCACAAAGTCGCAGCAATGACTGATGCCGATATCGATCACTGTATGCAAAATACAGGCTTAATTCGCCATCGCGCTAAATTACAGGCAATCGTCACCAATGCGCGGGCGTTTCTTGCCATGCAAAAGTGCGGTGAAAATTTCAGTCATTTTATTTGGTCTTTCGTGAATCATCAGCCGCAAATTCATGACGTGCCCGAGTTAAGCCATGTGCCGGCGCAAACGGCAACCTCAATCGCGTTATCCAAAGCCCTGAAAAAACGCGGCTTCGTGTTTGTCGGTCCGACAACTTGTTATGCGTTTATGCAATCCATGGGGTTGGTGGATGATCACTGGAATGCGTGCGCGTACAAAACGCCACAT","","","21458","MKKRCTWAENSQIYQDYHDNEWGKPQFDDRKLFEKLCLEGQQAGLSWITVLKKREAYRQAFFHFDPHKVAAMTDADIDHCMQNTGLIRHRAKLQAIVTNARAFLAMQKCGENFSHFIWSFVNHQPQIHDVPELSHVPAQTATSIALSKALKKRGFVFVGPTTCYAFMQSMGLVDDHWNACAYKTPH","632718","","DNA-3-methyladenine glycosylase I","Periplasm, Cytoplasm","","
InterPro
IPR004597
Family
DNA-3-methyladenine glycosylase I
TIGR00624\"[3-183]Ttag: DNA-3-methyladenine glycosylase I
InterPro
IPR005019
Family
Methyladenine glycosylase
PF03352\"[7-185]TAdenine_glyco
noIPR
unintegrated
unintegrated
G3DSA:1.10.340.30\"[2-183]Tno description


","No hits to the COGs database.","","Residues 5 to 155 match (4e-50) PD:PD013429 which is described as COMPLETE PROTEOME DNA-3-METHYLADENINE GLYCOSIDASE I GLYCOSYLASE HYDROLASE DNA CONSTITUTIVE I ","","","","","","","","","","","","Wed Dec 18 15:07:11 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00920 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 185 (E-value = 6.8e-117) place AA00920 in the Adenine_glyco family which is described as Methyladenine glycosylase (PF03352)","","","","","Drohat AC, Kwon K, Krosky DJ, Stivers JT.3-Methyladenine DNA glycosylase I is an unexpected helix-hairpin-helix superfamily member.Nat Struct Biol. 2002 Sep;9(9):659-64.PMID: 12161745Costa de Oliveira R, Laval J, Boiteux S.Induction of SOS and adaptive responses by alkylating agents in Escherichia coli mutants deficient in 3-methyladenine-DNA glycosylase activities.Mutat Res. 1987 Jan;183(1):11-20.PMID: 3099190","","Wed Dec 18 15:07:11 2002","1","","","" "AA00921","633472","634074","603","ATGTCTGGATTATTTGTTCAAACTGATCCGTCCCGTCGTCGTTATGGTGTCGCGGCGTTCGTGGCGATTATCGCCGGTGTGGTTTCTTCATTCGTAAAATGGGGCGCCGAGCACCCATTCCCACCACGTAGTCCGTTGGATTTATTCACCGCTGCCTGTAAAGATCCCAGCCAAGCCCTTGAGGTTTGTTCCCGTGCATTTTTAAACCCGCCGCATGTTTTCTTACGTGATTATATCGGTATTAATCCGACGGAAGCGGTGTTTACTTTCGCCGATTACGGATTTAACTGGATTGGCGTGACCCACATTACTTTCTCGGTTGTATTCGCACTGTTCTATTGTATCGTCGCAGAACGTTTCCCGAAAATTAAATTATGGCAAGGTATTCTGTTCAGTATTATTTGTAATATTGGTGTTCACTATATCGCTTTTCCATTACTTAATTTAACACCACAAATATCTGAGTTACCTTGGTATGAACATGTTTCCGAATTTGTCGGCCATGTTTTTTGGTTCTGGAGCATTGAGTTAATTCGTCGTGATTTACGTAACCGCATTACGCACGAGCCGGATCCGGAAGTGCCGTTAAATCAGCCATATCGT","","","23074","MSGLFVQTDPSRRRYGVAAFVAIIAGVVSSFVKWGAEHPFPPRSPLDLFTAACKDPSQALEVCSRAFLNPPHVFLRDYIGINPTEAVFTFADYGFNWIGVTHITFSVVFALFYCIVAERFPKIKLWQGILFSIICNIGVHYIAFPLLNLTPQISELPWYEHVSEFVGHVFWFWSIELIRRDLRNRITHEPDPEVPLNQPYR","634076","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR009898
Family
Protein of unknown function DUF1440
PF07274\"[22-178]TDUF1440
noIPR
unintegrated
unintegrated
PD109226\"[64-178]TQ6DA14_BBBBB_Q6DA14;
signalp\"[1-30]?signal-peptide
tmhmm\"[15-35]?\"[95-115]?\"[125-143]?\"[157-175]?transmembrane_regions


","No hits to the COGs database.","","Residues 12 to 180 match (6e-49) PD:PD109226 which is described as COMPLETE PROTEOME MEMBRANE SAV0181 TRANSMEMBRANE INTEGRAL YAGU ","","","","","","","","","","","","Wed Dec 18 15:59:38 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00921 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 22 to 178 (E-value = 2.1e-66) place AA00921 in the DUF1440 family which is described as Protein of unknown function (DUF1440) (PF07274)","","","","","","","","1","","","" "AA00923","635380","634133","1248","ATGGACTTTTTCCAATATCAATATGATCGACTTATGGTGGAAAATCTGCCGGTCAAACAACTTGCCGAGGAGTTCGGCACGCCCTTATATGTTTATTCCAAAGCCGCTCTTGAGCACCACTGGTATGCTTTTGAGAACGCCTTTGGAAACCATCCGCACTTAGTGTGTTTCGCCGTGAAATCCAATCCGAATATTGCTATTTTGAACATCATGGCAAGACTGGGTTCCGGCTTTGACATTGTGTCCCAAGGAGAATTGGAACGGGTGCTTGCCGCCGGCGGTGAGGCGCATAAAGTGGTGTTTTCCGGCGTGGCGAAATCCCGCCGGGAAATCGCCCGCGCGCTGGAAGTGGGCATTCGTTGCTTTAACATAGAATCGGAAGCAGAATTGTTACGCATTAATCAAGTCGCTGGCGACATAGGCAAAATCGCACCCATATCTTTACGCGTCAATCCTGATGTGGACGCCCACACCCACCCTTACATTTCCACCGGTTTAAAAGAAAATAAGTTCGGTGTGAGTGTGGAACAGGCACGTGAGGTGTATAAATTAGCCACAACGCTGCCGAATATTGAAATTGTCGGTATGGATTGTCACATCGGTTCGCAACTCACGGAATTACAACCATTTTTAGATGCCGCCGATCGGTTAATCATGCTCATGGAACAGTTAAAACAGGACAGCATTCAGTTGAAACATTTGGATTTGGGCGGCGGTTTAGGCGTCACTTACACCGACGAAACGCCACCACACCCGACGGAATACGCCAAAGCCCTGTGGGAAAAATTAAGTGCGTTCAACGAGTTGGAAATTATCGTTGAGCCCGGTCGCGCCATCACCGCCAATGCGGGGATTTTGGTGACCAAAGTGGAATATTTAAAATCCAACGAAAGCCGTAATTTCGCCATTGTAGATGCGGGCATGAACGACATGATTCGCCCGGCGTTATATCAGGCTTATATGAACATTCTGGAAATCGACCGCACTTTAGCGCGCGAAGAGAAAATTTATGACGTGGTGGGGCCGATTTGCGAAACCTCGGATTTCCTCGGCAAACAACGTAAACTTGCCATTGCGGAAGGGGATTATTTAGCCCAACGCTCTGCGGGAGCTTATGGCGCCAGTATGTCTTCCAACTACAATTCCCGCCCGAGAACGGCGGAGGTTATGGTGGACGGCGACAACGCCTATTTAATCCGCCGCCGTGAAGCGTTAAATGAATTGTGGCGACTGGAAAGTTTGTTGCCA","","","50361","MDFFQYQYDRLMVENLPVKQLAEEFGTPLYVYSKAALEHHWYAFENAFGNHPHLVCFAVKSNPNIAILNIMARLGSGFDIVSQGELERVLAAGGEAHKVVFSGVAKSRREIARALEVGIRCFNIESEAELLRINQVAGDIGKIAPISLRVNPDVDAHTHPYISTGLKENKFGVSVEQAREVYKLATTLPNIEIVGMDCHIGSQLTELQPFLDAADRLIMLMEQLKQDSIQLKHLDLGGGLGVTYTDETPPHPTEYAKALWEKLSAFNELEIIVEPGRAITANAGILVTKVEYLKSNESRNFAIVDAGMNDMIRPALYQAYMNILEIDRTLAREEKIYDVVGPICETSDFLGKQRKLAIAEGDYLAQRSAGAYGASMSSNYNSRPRTAEVMVDGDNAYLIRRREALNELWRLESLLP","634135","","diaminopimelate decarboxylase","Cytoplasm","","
InterPro
IPR000183
Domain
Orn/DAP/Arg decarboxylase 2
PR01179\"[57-75]T\"[77-89]T\"[190-203]T\"[271-290]T\"[370-383]TODADCRBXLASE
PF00278\"[285-391]TOrn_DAP_Arg_deC
PF02784\"[33-282]TOrn_Arg_deC_N
PS00878\"[57-75]?ODR_DC_2_1
PS00879\"[228-241]?ODR_DC_2_2
InterPro
IPR002986
Domain
Diaminopimelate decarboxylase
PR01181\"[75-92]T\"[164-173]T\"[299-317]T\"[380-402]TDAPDCRBXLASE
TIGR01048\"[4-413]TlysA: diaminopimelate decarboxylase
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.10\"[34-281]Tno description
PTHR11482\"[10-416]TARGININE/DIAMINOPIMELATE/ORNITHINE DECARBOXYLASE
PTHR11482:SF5\"[10-416]TDIAMINOPIMELATE DECARBOXYLASE


","No hits to the COGs database.","Significant hit ( 6.9e-71) to 7/7 blocks of the IPB000183 family, which is described as \"Orn/DAP/Arg decarboxylases family 2\". Interpro entry for IP:IPR000183. IPB000183A 57-101 1e-21 IPB000183B 158-172 7.2e-06 IPB000183C 193-204 0.00023 IPB000183D 226-245 3.9e-06 IPB000183E 271-294 6.1e-12 IPB000183F 339-348 0.054 IPB000183G 361-381 1.2e-09","Residues 21 to 202 match (6e-07) PD:PD552258 which is described as PROTEOME DECARBOXYLASE COMPLETE DIAMINOPIMELATE LYASE ","","","","","","","","","","","","Wed Dec 18 16:01:11 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00923 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 285 to 392 (E-value = 5.6e-47) place AA00923 in the Orn_DAP_Arg_deC family which is described as Pyridoxal-dependent decarboxylase, C-terminal sheet domain (PF00278)","","","","","Stragier,P., Danos,O. and Patte,J.C. Regulation of diaminopimelate decarboxylase synthesis inEscherichia coli. II. Nucleotide sequence of the lysA gene andits regulatory region. J. Mol. Biol. 168 (2), 321-331 (1983) PubMed: 6350601.","","Wed Dec 18 16:01:11 2002","1","","","" "AA00924","635517","635401","117","ATGAAAAAACTCATTTCCTTATTTTTACTCGTCACCTTATGTGTCTTAAGCAGTGGCTGTGGCGTGAAAGGTCCGTTGTATTTTCCTGCACAAGATTCAGCCGATCAGGCGACCAAA","","","4126","MKKLISLFLLVTLCVLSSGCGVKGPLYFPAQDSADQATK","635401","","hypothetical protein","Outer membrane, Periplasm, Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
PS51257\"[1-20]TPROKAR_LIPOPROTEIN
signalp\"[1-21]?signal-peptide
tmhmm\"[5-27]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 08:31:05 2004","Wed Feb 25 08:31:05 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00924 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 08:31:05 2004","","","","","","","","","","","","","1","","","" "AA00925","635504","635623","120","ATGAGTTTTTTCATCGGTTGCTCCTTGTTCTCAAATTTGACTGCTCTTTTTACCATTAAATCGGGCTTTGTGCTATCACAACGCGCAGAAAATCTTTATAATTCCCTCTTTGCCAACATT","","","4448","MSFFIGCSLFSNLTALFTIKSGFVLSQRAENLYNSLFANI","635623","","hypothetical protein","Cytoplasm, Extracellular","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-29]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 08:32:51 2004","Wed Feb 25 08:32:51 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00925 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 08:32:51 2004","","","","","","","","","","","","","1","","","" "AA00926","635640","635951","312","ATGAATATCATCGAGTTTCATCAGAAAATCGAGCAAGTTTGGGATGAAATTGAAGAACAACTGGAAGCGCAGGATTGCGATGTGGATTGCGAACGTCAGGGTTCCGTGTTCACCATCACCCTTGGCGATCGCAGCCAAATCGTGATCAACAAACAGGAATCGTTATTGGAATTATGGCTGGCGAGCCACAACGGCGGCTTTCATTTTGCCTATAAAGAAGACGGACGTTGGGTCAGTAACGACGGTTTGGATTTCTGGCAGGCGCTCACCGAAGCCCTTGCTAAACACGGCGAACAGGTTCAATTTAATCAA","","","14726","MNIIEFHQKIEQVWDEIEEQLEAQDCDVDCERQGSVFTITLGDRSQIVINKQESLLELWLASHNGGFHFAYKEDGRWVSNDGLDFWQALTEALAKHGEQVQFNQ","635953","","CyaY protein","Cytoplasm","","
InterPro
IPR002908
Family
Frataxin-like
PD238818\"[11-92]TCYAY_PASMU_P57943;
PF01491\"[1-103]TFrataxin_Cyay
PS50810\"[1-100]TFRATAXIN_2
PS01344\"[48-62]TFRATAXIN_1
noIPR
unintegrated
unintegrated
G3DSA:3.30.920.10\"[1-103]Tno description


","BeTs to 7 clades of COG1965COG name: Protein implicated in iron transport, frataxin homologFunctional Class: PThe phylogenetic pattern of COG1965 is ------y-------efgh-n--x---Number of proteins in this genome belonging to this COG is","Significant hit ( 3.3e-21) to 2/2 blocks of the IPB002908 family, which is described as \"Frataxin-like domain\". Interpro entry for IP:IPR002908. IPB002908A 17-28 0.047 IPB002908B 34-68 1.4e-17","Residues 2 to 103 match (2e-31) PD:PD238818 which is described as CYAY PROTEOME COMPLETE MITOCHONDRION PRECURSOR MITOCHONDRIAL FRATAXIN TRANSIT PEPTIDE HOMOLOG ","","","","","","","","","","","","Wed Dec 18 16:06:24 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00926 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 103 (E-value = 2e-47) place AA00926 in the Frataxin_Cyay family which is described as Frataxin-like domain (PF01491)","","","","","Adinolfi S, Trifuoggi M, Politou AS, Martin S, Pastore A.A structural approach to understanding the iron-binding properties of phylogeneticallydifferent frataxins.Hum Mol Genet. 2002 Aug 1;11(16):1865-77.PMID: 12140189 Huynen MA, Snel B, Bork P, Gibson TJ.The phylogenetic distribution of frataxin indicates a role in iron-sulfur cluster proteinassembly.Hum Mol Genet. 2001 Oct 1;10(21):2463-8.PMID: 11689493 Lee MG, Cho SJ, Yang JK, Song HK, Suh SW.Crystallization and preliminary X-ray crystallographic analysis of Escherichia coli CyaY, a structural homologue of human frataxin.Acta Crystallogr D Biol Crystallogr. 2000 Jul;56 ( Pt 7):920-1.PMID: 10930845Li DS, Ohshima K, Jiralerspong S, Bojanowski MW, Pandolfo M.Knock-out of the cyaY gene in Escherichia coli does not affect cellular iron content andsensitivity to oxidants.FEBS Lett. 1999 Jul 30;456(1):13-6.PMID: 10452520","","Wed Dec 18 16:06:24 2002","1","","","" "AA00927","635951","637837","1887","ATGAGCGACCTTAACCCGTCCAAACCAACAAAAAGTGCGGTAGATTTTGCCGATGAATCGTCGGTAAATTCCACCGCACTTCATGCTTCCGCATTGCACGTTTTGCATTCGGTTTTCGGCTATCAATCCTTCCGCAAAGGGCAGCAGGAAATCATCAATGCGGTACTTAACGGGCAGGATTGTTTGGTGATTATGGCGACGGGCACGGGCAAATCGTTGTGTTATCAAATTCCCGCCCTTTGTTTTGACGGCACGACGCTGGTGGTTTCACCGTTGATTTCCCTGATGAAAGACCAAGTGGATCAGCTGCGCGCCAACGGCGTGGAAGCGGATTATTTAAATTCCACACAAACCTTCGAAGAACAGCAACAGGTGCAGAATCGGGCAATTTCCGGGCAATTAAAATTATTGTATTTATCGCCGGAAAAAGTCATGACCAGCAGCTTTTTCCAATTTATTTCTTTATGCCAAGTGAGTTTTATCGCCATTGATGAAGCGCACTGCATTTCCCAATGGGGACACGATTTCCGTCCCGAATATACCCAACTCGGCGGCTTAAAAGGCAGCTTTCCGAACGTGCCGATCATGGCGCTCACTGCTACAGCGGATCAGACTACACAACAAGACATCCTGCAAAATCTCCGGCTAAATCGACCGCACTTTTATGTGGGCAGCTTCGATCGCCCGAACATTCGTTACACCTTGGTGGAAAAATTCAAACCCATGGAACAGCTTTGCCGTTTCGTGCTGGCGCAAAAGGGCAAGAGCGGCATTGTGTATTGCAACAGCCGCAATAAAGTGGAACGTATCGCGGAAACCCTGTACAACAAAGGCGTGCGGGCGGCGGCGTATCATGCCGGCATGGAAAACGGCTTGCGCGAAAAAGTACAACGGGATTTTCAGCGTGACAACATTCAAGTGGTGGTGGCGACCATTGCGTTCGGCATGGGCATTAATAAATCCAACGTGCGCTTTGTGGCACATTTTGACCTGCCGCGCAGCATCGAATCCTACTATCAGGAAACCGGTCGTGCGGGGCGCGATGATTTGCCGGCGGAAGCGGTATTGTTTTACGACCCGGCAGATTATGTGTGGCTCAACAAAATGCTGATGGAAAAGCCGGAAACGCCGCAACGGCAGATTGAACAGCACAAATTGCAAGCCATCGGTGAATTTGCCGAAAGCCAAACCTGCCGTCGTTTGGTTTTATTGAATTATTTCGGCGAACATCGCCAAACGCCCTGTCAAAATTGCGATATTTGTCTCGATCCGCCGAAAAAATATAACGGCTTGTTGGATGCGCAAAAAATCATGTCGGCGATTTATCGCACCGGTCAATGTTATGGCGCGCATTATGTCATCGCCGTATTGCGTGGCATGAACAATCAGAAAATTCGTGACCAACACCATGATCAATTAAGCGTGTACGGCATTGGCAAAGAACATGGCACGGAATATTGGCAGTCGGTATTGCGCCAGTTGGTTCACTTGGGGTTGGTACGCCAAATCATCGGCGAATACGGCAACACCTTACAATTAACGGAAAACGCCAAACCGATTCTACGCGGAGAAGAACCGCTGGAATTGGCAACTCCTCGCCTGTCTTCCATTGTCACTACCGCCATGACGCCCAAAAGTGCGGTGGGTTCTTACGACAAAGATCTGTTTGCCCGCTTGCGCTTTCTGCGTAAACAAATTGCCGATAAGGAAAATATTCCGCCGTATATTGTGTTTAACGACGCAACGCTACAAGAAATGGCGCAATATCAACCTGTCAGTAACATTGAAATGCTGCAAATCAACGGCGTTGGCGCCATTAAACTGGAGCGTTTCGGGCAGGCATTTCTCACCTTGATCCGCGAACATAAAAGTGCCCGCGCCGGCGAA","","","70977","MSDLNPSKPTKSAVDFADESSVNSTALHASALHVLHSVFGYQSFRKGQQEIINAVLNGQDCLVIMATGTGKSLCYQIPALCFDGTTLVVSPLISLMKDQVDQLRANGVEADYLNSTQTFEEQQQVQNRAISGQLKLLYLSPEKVMTSSFFQFISLCQVSFIAIDEAHCISQWGHDFRPEYTQLGGLKGSFPNVPIMALTATADQTTQQDILQNLRLNRPHFYVGSFDRPNIRYTLVEKFKPMEQLCRFVLAQKGKSGIVYCNSRNKVERIAETLYNKGVRAAAYHAGMENGLREKVQRDFQRDNIQVVVATIAFGMGINKSNVRFVAHFDLPRSIESYYQETGRAGRDDLPAEAVLFYDPADYVWLNKMLMEKPETPQRQIEQHKLQAIGEFAESQTCRRLVLLNYFGEHRQTPCQNCDICLDPPKKYNGLLDAQKIMSAIYRTGQCYGAHYVIAVLRGMNNQKIRDQHHDQLSVYGIGKEHGTEYWQSVLRQLVHLGLVRQIIGEYGNTLQLTENAKPILRGEEPLELATPRLSSIVTTAMTPKSAVGSYDKDLFARLRFLRKQIADKENIPPYIVFNDATLQEMAQYQPVSNIEMLQINGVGAIKLERFGQAFLTLIREHKSARAGE","637839","","ATP-dependent DNA helicase","Cytoplasm","","
InterPro
IPR001650
Domain
Helicase, C-terminal
PF00271\"[273-349]THelicase_C
SM00490\"[268-349]THELICc
PS51194\"[241-389]THELICASE_CTER
InterPro
IPR002121
Domain
HRDC
PF00570\"[549-629]THRDC
SM00341\"[549-629]THRDC
PS50967\"[549-629]THRDC
InterPro
IPR004589
Family
ATP-dependent DNA helicase RecQ
PTHR13710\"[20-622]TDNA HELICASE RECQ FAMILY MEMBER
TIGR00614\"[33-482]TrecQ_fam: ATP-dependent DNA helicase, RecQ
InterPro
IPR006293
Family
ATP-requiring DNA helicase RecQ
TIGR01389\"[31-622]TrecQ: ATP-dependent DNA helicase RecQ
InterPro
IPR011545
Domain
DEAD/DEAH box helicase, N-terminal
PF00270\"[45-210]TDEAD
InterPro
IPR014001
Domain
DEAD-like helicases, N-terminal
SM00487\"[40-236]TDEXDc
InterPro
IPR014021
Domain
Helicase superfamily 1 and 2 ATP-binding
PS51192\"[52-220]THELICASE_ATP_BIND_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[7-223]T\"[224-395]Tno description
PTHR13710:SF11\"[20-622]TDNA HELICASE RECQ


","No hits to the COGs database.","Significant hit ( 8.4e-13) to 2/5 blocks of the IPB000629 family, which is described as \"ATP-dependent helicase, DEAD-box\". Interpro entry for IP:IPR000629. IPB000629A 40-83 9.8e-08 IPB000629E 311-352 0.0023","Residues 482 to 551 match (3e-09) PD:PD532351 which is described as HELICASE ATP-DEPENDENT PROTEOME COMPLETE ATP-BINDING DNA RECQ ","","","","","","","","","","","","Wed Dec 18 16:09:11 2002","","Wed Jun 1 10:02:46 2005","Wed Jun 1 10:02:46 2005","Wed Jun 1 10:02:46 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA00927 is paralogously related to AA00148 (4e-19), AA00506 (4e-15), AA00263 (2e-06), AA00861 (7e-05) and AA02480 (8e-04).","Wed Jun 1 10:02:46 2005","","","","","Residues 549 to 629 (E-value = 4.4e-27) place AA00927 in the HRDC family which is described as HRDC domain (PF00570)","Wed Jun 1 10:02:46 2005","","","","Irino,N., Nakayama,K. and Nakayama,H. The recQ gene of Escherichia coli K12: primary structure and evidence for SOS regulation Mol. Gen. Genet. 205 (2), 298-304 (1986) PubMed: 3027506 Umezu,K., Nakayama,K. and Nakayama,H. Escherichia coli RecQ protein is a DNA helicase Proc. Natl. Acad. Sci. U.S.A. 87 (14), 5363-5367 (1990) PubMed: 2164680 Nakayama H.RecQ family helicases: roles as tumor suppressor proteins.Oncogene. 2002 Dec 16;21(58):9008-21.PMID: 12483516 Wu L, Hickson ID.RecQ helicases and cellular responses to DNA damage.Mutat Res. 2002 Nov 30;509(1-2):35-47.PMID: 12427530 ","","Wed Dec 18 16:11:57 2002","1","","","" "AA00929","637937","640354","2418","ATGTCAACAAATACTCCTGAAACTTATGGTGCAAACAGTATTAAAGTGCTGAAAGGGCTTGATGCGGTGCGTAAACGTCCCGGAATGTATATCGGTGACACAGACGATGGAACGGGTTTACACCATATGGTTTTTGAAGTGGTGGATAACGCCATTGACGAAGCCTTGGCAGGGTATTGCGACGACATCGTAGTCACTATTCATTCCGACAATTCCGTTTCCGTGCAAGACGATGGGCGCGGTATTCCGGTGGATATTCACCCGGAAGAAGGCGTTTCCGCTGCCGAAGTGATCATGACCGTGTTACACGCCGGCGGTAAATTTGACGATAACTCCTATAAAGTATCCGGCGGTTTGCACGGCGTGGGGGTATCCGTGGTAAACGCGCTGTCCGACAAGTTACAGCTCACCATTCGCCGTCAAGGCAAGGTGCACGAGCAATTTTACAGCCTCGGCGATCCGCAAGCGCCGTTAGCCGTCATCGGCGAAACCACGCAAACCGGTACCACCGTGCGTTTCTGGCCAAGCCCGACTATCTTCACTAATATTGAATTTGAATACGATATTTTAGCCAAGCGTTTAAGAGAGTTGTCTTTCTTAAACTCTGGCGTGTCCATTCGTTTAATTGACGAACGTACCGACAAACAAGACCACTTCCATTACAAAGGTGGCATTCAGGCGTTCGTTGAATATATTAACCGCGGTAAAACCCCGATTCATCCGAAACCTTTCTATTTTTCCGCTGAAAAAGATGGCATTGGTGTAGAAATTGCGTTGCAATGGAACGACGGTTACGCGGAAAACATTTATTGTTTCACCAACAACATTCCGCAACGGGACGGCGGTACGCACTTAGCCGGTTTCCGTGGCGCAATGACCCGCACCTTGAACAACTACATGGAAAACGAAGGCTACACCAAGAAATCCAAAGTGGCGACTTCCGGTGATGATGCCCGTGAAGGCTTGGTGGCGGTGATTTCCGTGAAAGTACCGGATCCGAAATTCTCTTCTCAAACAAAAGACAAACTGGTTTCCTCCGAAGTGAAAAGTGCGGTGGAATCCCTGATGAACGAATATTTACAAACCTATTTGTTGGAAAACCCGAACGATGTAAAAATCATCGTGACCAAAATTATTGATGCCGCGCGTGCCCGTGAAGCCGCCCGCAAAGCCCGCGAAATGACCCGTCGTAAAGGCGCGTTGGATTTAGGCGGCTTGCCGGGCAAATTGGCGGATTGTCAGGAACGCGATCCGGCGTTATCCGAGCTTTACATCGTGGAGGGGGACTCTGCGGGCGGTTCCGCAAAACAAGGGCGTAACCGTAAAAACCAAGCGATTTTGCCGTTAAAAGGGAAAATCCTGAACGTGGAAAAAGCCCGTTTCGACAAAATGTTGTCTTCTGCGGAAGTGGGCACATTAATTACCGCATTGGGCTGCGGTATCGGCCGTGACGAATATAATCCCGACAAATTGCGCTATCACAGCATCATCATCATGACCGATGCGGACGTGGACGGTTCCCACATTCGTACTTTATTGTTAACGTTCTTCTATCGCCAAATGCCGGAACTGATTGAGCGCGGTTACGTTTATATTGCCCAGCCGCCGCTCTATAAAGTGAAAAAAGGTAAGCAGGAACAATACATTAAAGATGACGAAGCGATGGCGGAATTTGAACTGGCGATTGCGTTGGAAAATGCCGCGCTTTATGTGAATGAAAGTGCACCGGGTATGCAAGGCGTGGCGTTGCAAAACTTGGCGTCCGAATATCTTGCCGTACAAAAAATGATTGCCCGCTTAACCCGCTATTATCCGGAAAGCGTGTTAAAAGAATTGATTTATCAACCGGCGTTGACCACTGCACTGATGCAGCAGGAAAGTGCGGTCAATTCCTGGGCCGATTCTCTGGTTGCCACCTTAAATATGAAAGAAACCGACGGCAGACATTATAGCTATCGTCTGCAATTTAACGCCGAACGGAATTTGTACGAAGTGGTATTAACGGTGAGAACACACGGTATTGATACGGATTATTTCCTCAATTTCCAATTCGCCACCGGTAGCGAATATACCCGCCTAATCGCCCTCGGCGAAAAATTAGTTGACTTGTTGGAAGGCAGCGCCTATGTGATGCGTGGTGAGCGCAAAGTGGCGGTGGGCTCTTTTGAACAGGCAATTGAGTGGCTGATGAGAGAATCCCGTCGCGGCTTAATGATCCAACGTTATAAAGGCTTGGGCGAGATGAATCCTGAGCAACTTTGGGAAACCACCATGGATCCGAATATCCGCCGTATGTTGAAAGTATCGATTAAAGATGCCGTGGCGGCAGATCAACTTTTCACCACCTTAATGGGTGACGAAGTGGAGCCGCGTCGCGATTTCATCGAAAGCAATGCGTTAAGAGCAAATCTGGATATT","","","89940","MSTNTPETYGANSIKVLKGLDAVRKRPGMYIGDTDDGTGLHHMVFEVVDNAIDEALAGYCDDIVVTIHSDNSVSVQDDGRGIPVDIHPEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSDKLQLTIRRQGKVHEQFYSLGDPQAPLAVIGETTQTGTTVRFWPSPTIFTNIEFEYDILAKRLRELSFLNSGVSIRLIDERTDKQDHFHYKGGIQAFVEYINRGKTPIHPKPFYFSAEKDGIGVEIALQWNDGYAENIYCFTNNIPQRDGGTHLAGFRGAMTRTLNNYMENEGYTKKSKVATSGDDAREGLVAVISVKVPDPKFSSQTKDKLVSSEVKSAVESLMNEYLQTYLLENPNDVKIIVTKIIDAARAREAARKAREMTRRKGALDLGGLPGKLADCQERDPALSELYIVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMLSSAEVGTLITALGCGIGRDEYNPDKLRYHSIIIMTDADVDGSHIRTLLLTFFYRQMPELIERGYVYIAQPPLYKVKKGKQEQYIKDDEAMAEFELAIALENAALYVNESAPGMQGVALQNLASEYLAVQKMIARLTRYYPESVLKELIYQPALTTALMQQESAVNSWADSLVATLNMKETDGRHYSYRLQFNAERNLYEVVLTVRTHGIDTDYFLNFQFATGSEYTRLIALGEKLVDLLEGSAYVMRGERKVAVGSFEQAIEWLMRESRRGLMIQRYKGLGEMNPEQLWETTMDPNIRRMLKVSIKDAVAADQLFTTLMGDEVEPRRDFIESNALRANLDI","640356","","DNA gyrase subunit B","Cytoplasm","","
InterPro
IPR000565
Family
DNA topoisomerase, type IIA, subunit B
PR01159\"[9-19]T\"[184-199]T\"[199-212]T\"[223-245]T\"[315-331]T\"[363-377]T\"[377-397]T\"[473-482]T\"[760-772]T\"[776-792]TDNAGYRASEB
InterPro
IPR001241
Domain
DNA topoisomerase, type IIA, subunit B or N-terminal
PR00418\"[39-54]T\"[74-87]T\"[117-131]T\"[271-284]T\"[423-437]T\"[490-506]T\"[508-525]T\"[528-540]T\"[739-755]TTPI2FAMILY
SM00433\"[39-800]TTOP2c
PS00177\"[425-433]TTOPOISOMERASE_II
InterPro
IPR002288
Domain
DNA topoisomerase, type IIA, subunit B, C-terminal
PF00986\"[731-796]TDNA_gyraseB_C
InterPro
IPR003594
Domain
ATP-binding region, ATPase-like
G3DSA:3.30.565.10\"[6-223]Tno description
PF02518\"[35-178]THATPase_c
SM00387\"[35-179]THATPase_c
InterPro
IPR006171
Domain
TOPRIM
PF01751\"[421-533]TToprim
InterPro
IPR011557
Family
DNA gyrase, subunit B
TIGR01059\"[9-806]TgyrB: DNA gyrase, B subunit
InterPro
IPR011558
Domain
DNA topoisomerase, type IIA, subunit B, conserved region
PD149633\"[428-551]TQ9CKX5_PASMU_Q9CKX5;
InterPro
IPR013506
Domain
DNA topoisomerase, type IIA, subunit B, region 2
PF00204\"[224-394]TDNA_gyraseB
InterPro
IPR013759
Domain
DNA topoisomerase, type IIA, subunit B or N-terminal, alpha-beta
G3DSA:3.40.50.670\"[387-779]Tno description
noIPR
unintegrated
unintegrated
PTHR10169\"[28-572]T\"[737-801]TDNA TOPOISOMERASE/GYRASE


","BeTs to 22 clades of COG0187COG name: DNA gyrase (topoisomerase II) B subunitFunctional Class: LThe phylogenetic pattern of COG0187 is ao-p--yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit (2.1e-148) to 8/8 blocks of the IPB001241 family, which is described as \"DNA topoisomerase II family\". Interpro entry for IP:IPR001241. IPB001241A 14-35 3.9e-16 IPB001241B 113-131 6.3e-15 IPB001241C 168-180 7.4e-07 IPB001241D 271-284 1.3e-07 IPB001241E 317-343 5.2e-15 IPB001241F 422-470 6.6e-37 IPB001241G 491-517 5.4e-25 IPB001241H 740-763 6.4e-17","","","","","","","","","","","","","Thu Jan 16 09:42:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00929 is paralogously related to AA02486 (1e-108).","","","","","","Residues 731 to 796 (E-value = 4.4e-43) place AA00929 in the DNA_gyraseB_C family which is described as DNA gyrase B subunit, carboxyl terminus (PF00986)","","","","","Yamagishi,J., Yoshida,H., Yamayoshi,M. and Nakamura,S. Nalidixic acid-resistant mutations of the gyrB gene of Escherichia coli Mol. Gen. Genet. 204 (3), 367-373 (1986) PubMed: 3020376 Adachi,T., Mizuuchi,M., Robinson,E.A., Appella,E., O'Dea,M.H., Gellert,M. and Mizuuchi,K. DNA sequence of the E. coli gyrB gene: application of a new sequencing strategy Nucleic Acids Res. 15 (2), 771-784 (1987) PubMed: 3029692 Funatsuki,K., Tanaka,R., Inagaki,S., Konno,H., Katoh,K. and Nakamura,H. acrB mutation located at carboxyl-terminal region of gyrase B subunit reduces DNA binding of DNA gyrase J. Biol. Chem. 272 (20), 13302-13308 (1997) PubMed: 9148951 Adachi,T., Mizuuchi,K., Menzel,R. and Gellert,M. DNA sequence and transcription of the region upstream of the E. coli gyrB gene Nucleic Acids Res. 12 (16), 6389-6395 (1984) PubMed: 6089112 ","","Fri Nov 21 14:37:49 2003","1","","","" "AA00930","641326","640415","912","ATGCCGTTTTTGTCGTTTAATCGACAACGTTGGGCGGAATTGCGCAAATCCGTACCGTTAAAATTAACCGAGCAAGATCTCAAACCGTTGCTTGGTATTAACGAAGCACTTTCCCTTGATGAAGTCCGTACTATCTATTTACCGTTAACCCGTTTGATTAACTACTATATAGATGAAAACATTCGTCGTCAGGACGTGTTGCACCGTTTTCTTGGCGGTCAAAGCCCGAAAGTGCCTTACATTATTAGTATTGCAGGTAGCGTGGCGGTAGGAAAAAGTACTTCGGCGCGGATTTTGCAATCCTTATTAAGCCATTGGCCGCAGGAGCGAAAAGTTGATTTGATCACGACCGATGGTTTCCTGCATCCTTTATCCTATTTGCAACAACATAATTTGCTGCATAAAAAAGGTTTTCCGATTTCTTATAACACGCCGAAACTGATTCATTTTTTAGCCGACATAAAATCCGGCAAACCCAATGTCAGCGCGCCTATTTATTCACATTTAACCTATGACATTGTTCCCGATCAATTTAATGTTATCGATCAGCCCGACATTCTGATTCTGGAAGGATTGAATGTGTTACAACCGAACAAAAATCAGGCCAATGAGCTGTTCGTTTCGGATTTTGTGGATTTTTCCATTTATGTGGATGCGGAAGAAACATTACTGAAAGAATGGTATATCCGTCGTTTCCTGAAATTCCGCCAAAGTGCGTTTTCCAATCCGAGTTCTTATTTCAAACATTATGCCAACCTGTCCGAACAGGAAGCCACCGAAACGGCAGGAAAAATCTGGGATGAAATTAACGGATTGAATCTGAAAGAAAATATTTTACCGACTCGTGAGCGTGCGAACCTTATTTTGAAAAAAGGGGCGAACCATGAAGTGGAATTGGTGAAGCTAAGAAAA","","","36504","MPFLSFNRQRWAELRKSVPLKLTEQDLKPLLGINEALSLDEVRTIYLPLTRLINYYIDENIRRQDVLHRFLGGQSPKVPYIISIAGSVAVGKSTSARILQSLLSHWPQERKVDLITTDGFLHPLSYLQQHNLLHKKGFPISYNTPKLIHFLADIKSGKPNVSAPIYSHLTYDIVPDQFNVIDQPDILILEGLNVLQPNKNQANELFVSDFVDFSIYVDAEETLLKEWYIRRFLKFRQSAFSNPSSYFKHYANLSEQEATETAGKIWDEINGLNLKENILPTRERANLILKKGANHEVELVKLRK","640417","","pantothenate kinase","Cytoplasm","","
InterPro
IPR004566
Family
Bacterial pantothenate kinase
PIRSF000545\"[1-304]TPantothenate kinase, bacterial type
TIGR00554\"[1-304]TpanK_bact: pantothenate kinase
InterPro
IPR006083
Family
Phosphoribulokinase/uridine kinase
PF00485\"[81-264]TPRK
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[1-304]Tno description
PTHR10285\"[87-295]TURIDINE KINASE RELATED
PTHR10285:SF7\"[87-295]TPANTOTHENATE KINASE


","BeTs to 5 clades of COG1072COG name: Panthothenate kinaseFunctional Class: HThe phylogenetic pattern of COG1072 is ----------rlb-e-gh---j----Number of proteins in this genome belonging to this COG is","Significant hit ( 3.5e-05) to 2/5 blocks of the IPB001324 family, which is described as \"Phosphoribulokinase family\". Interpro entry for IP:IPR001324. IPB001324A 78-99 0.079 IPB001324C 182-193 0.23","Residues 2 to 304 match (2e-139) PD:PD015803 which is described as KINASE COMPLETE PROTEOME TRANSFERASE PANTOTHENATE ATP-BINDING PHOSPHORIBULOKINASE PANTOTHENIC COENZYME ACID ","","","","","","","","","","","","Fri Sep 5 16:23:08 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00930 is paralogously related to AA00695 (1e-05).","","","","","","Residues 81 to 264 (E-value = 4.2e-06) place AA00930 in the PRK family which is described as Phosphoribulokinase / Uridine kinase family (PF00485)","","","","","Song WJ, Jackowski S. Cloning, sequencing, and expression of the pantothenate kinase (coaA) geneof Escherichia coli. J Bacteriol. 1992 Oct;174(20):6411-7. PMID: 1328157 Vallari DS, Rock CO. Isolation and characterization of temperature-sensitive pantothenate kinase(coaA) mutants of Escherichia coli. J Bacteriol. 1987 Dec;169(12):5795-800. PMID: 2824448 Dunn SD, Snell EE. Isolation of temperature-sensitive pantothenate kinase mutants of Salmonellatyphimurium and mapping of the coaA gene. J Bacteriol. 1979 Dec;140(3):805-8. PMID: 230178 ","","Fri Sep 5 16:24:34 2003","1","","","" "AA00931","642060","643241","1182","ATGTCTAAAGAAAAATTTGAACGTACAAAACCGCACGTTAACGTGGGTACAATCGGCCACGTTGACCATGGTAAAACCACTTTAACAGCAGCTATCACTACCGTATTGGCAAAACACTACGGCGGTGCAGCACGTGCATTTGACCAAATCGATAATGCACCTGAAGAAAAAGCGCGTGGTATCACCATCAACACTTCACACGTTGAATATGACACCCCAACCCGTCACTATGCACACGTTGACTGCCCGGGACACGCCGACTATGTGAAAAACATGATTACCGGTGCGGCGCAAATGGACGGTGCTATCTTAGTAGTAGCAGCAACCGACGGTCCTATGCCACAAACTCGTGAGCACATCTTATTAGGTCGCCAAGTAGGTGTTCCTTACATCATCGTATTCTTAAACAAATGCGACATGGTAGATGACGAAGAGTTATTAGAATTAGTTGAAATGGAAGTTCGTGAACTTCTTTCTCAATATGACTTCCCGGGCGATGACACCCCAATCGTACGCGGTTCTGCATTAAAAGCGCTTGAAGGCGATGCCGCATGGGAAGAAAAAATCCTTGAATTAGCAAACCATTTAGATACTTACATCCCGGAACCTGAGCGTGCTATCGACCAACCGTTCCTTCTTCCAATTGAAGATGTGTTCTCTATCTCCGGTCGTGGTACCGTAGTAACGGGTCGTGTTGAGCGCGGTATCATCCGTACCGGTGATGAAGTTGAAATCGTGGGTATCAAACCGACTGCAAAAACCACCGTAACCGGTGTTGAAATGTTCCGTAAATTACTTGACGAAGGTCGTGCGGGTGAAAACATCGGTGCATTATTGCGTGGTACTAAACGTGAAGAAATCGAACGTGGTCAGGTATTGGCGAAACCGGGTTCAATCACCCCGCACACTGACTTCGAATCTGAAGTGTACGTATTGTCCAAAGAAGAAGGTGGTCGTCATACTCCATTCTTCAAAGGTTACCGTCCACAATTCTATTTCCGTACAACTGACGTAACCGGTACTATCGAGTTACCTGAAGGCGTGGAAATGGTTATGCCCGGTGATAACATCAAAATGACCGTATCCTTAATTCACCCAATTGCGATGGACCAAGGTTTACGTTTCGCTATCCGTGAAGGTGGCCGTACAGTGGGTGCCGGCGTGGTAGCTAAAATTATCAAA","","","43312","MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKHYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAAWEEKILELANHLDTYIPEPERAIDQPFLLPIEDVFSISGRGTVVTGRVERGIIRTGDEVEIVGIKPTAKTTVTGVEMFRKLLDEGRAGENIGALLRGTKREEIERGQVLAKPGSITPHTDFESEVYVLSKEEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMTVSLIHPIAMDQGLRFAIREGGRTVGAGVVAKIIK","643243","","elongation factor Tu (tufA)","Cytoplasm","","
InterPro
IPR000795
Domain
Protein synthesis factor, GTP-binding
PR00315\"[14-27]T\"[58-66]T\"[78-88]T\"[94-105]T\"[131-140]TELONGATNFCT
PF00009\"[10-204]TGTP_EFTU
PS00301\"[51-66]TEFACTOR_GTP
InterPro
IPR004160
Domain
Translation elongation factor EFTu/EF1A, C-terminal
PF03143\"[299-393]TGTP_EFTU_D3
InterPro
IPR004161
Domain
Translation elongation factor EFTu/EF1A, domain 2
PF03144\"[225-294]TGTP_EFTU_D2
InterPro
IPR004541
Family
Translation elongation factor EFTu/EF1A, bacterial and organelle
PTHR23115:SF31\"[1-328]TELONGATION FACTOR TU (EF-TU)
TIGR00485\"[1-394]TEF-Tu: translation elongation factor Tu
InterPro
IPR005225
Domain
Small GTP-binding protein domain
TIGR00231\"[10-185]Tsmall_GTP: small GTP-binding protein domain
noIPR
unintegrated
unintegrated
G3DSA:2.40.30.10\"[206-335]T\"[339-394]Tno description
G3DSA:3.40.50.300\"[3-205]Tno description
PTHR23115\"[1-328]TTRANSLATION FACTOR


","No hits to the COGs database.","Significant hit ( 1.3e-56) to 3/3 blocks of the IPB000795 family, which is described as \"GTP-binding elongation factor\". Interpro entry for IP:IPR000795. IPB000795A 14-29 8.8e-14 IPB000795B 80-111 8.2e-26 IPB000795C 115-139 2.4e-14Significant hit ( 2e-13) to 3/6 blocks of the IPB000640 family, which is described as \"Elongation factor G, C-terminus\". Interpro entry for IP:IPR000640. IPB000640A 12-37 1.7e-05 IPB000640B 50-72 0.13 IPB000640C 77-104 0.012Significant hit ( 1.1e-10) to 4/8 blocks of the IPB000178 family, which is described as \"Initiation factor 2\". Interpro entry for IP:IPR000178. IPB000178A 11-49 8.2 IPB000178B 77-109 0.0018 IPB000178C 110-149 0.18 IPB000178E 225-277 4.9","Residues 56 to 89 match (2e-13) PD:PD173400 which is described as FACTOR ELONGATION GTP-BINDING BIOSYNTHESIS PROTEOME COMPLETE TU EF-TU 1-ALPHA EF-1-ALPHA ","","","","","","","","","","","","Wed Dec 18 16:17:17 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00931 is paralogously related to AA00563 (0.0), AA00892 (3e-22), AA02344 (3e-17), AA01922 (6e-14), AA03003 (8e-14), AA00564 (4e-10) and AA01852 (1e-07).","","","","","","Residues 299 to 393 (E-value = 6.2e-62) place AA00931 in the GTP_EFTU_D3 family which is described as Elongation factor Tu C-terminal domain (PF03143)","","","","","Miyajima,A., Shibuya,M., Kuchino,Y. and Kaziro,Y. Transcription of the E. coli tufB gene: cotranscription with four tRNA genes and inhibition by guanosine-5\"-diphosphate-3\"-diphosphate Molecular & general genetics : MGG. 183 (1), 13-19 (1981) PubMed: 7035813 Laursen,R.A., L\"Italien,J.J., Nagarkatti,S. and Miller,D.L. The amino acid sequence of elongation factor Tu of Escherichia coli. The complete sequence J. Biol. Chem. 256 (15), 8102-8109 (1981) PubMed: 7021545 Jones,M.D., Petersen,T.E., Nielsen,K.M., Magnusson,S., Sottrup-Jensen,L., Gausing,K. and Clark,B.F. The complete amino-acid sequence of elongation factor Tu from Escherichia coli Eur. J. Biochem. 108 (2), 507-526 (1980) PubMed: 6997043 An,G. and Friesen,J.D. The nucleotide sequence of tufB and four nearby tRNA structural genes of Escherichia coli Gene 12 (1-2), 33-39 (1980) PubMed: 7011904 ","","Fri Nov 21 14:40:02 2003","1","","","" "AA00932","644255","643317","939","ATGAAATTAAAGTTATTAAAAAATATATTTAAAATAAGTGCATTGCTTGCTGCGTTACCAACGCTTGCGGTGGCAGCGGATAAACCGCAGATTGCATTATTAATGAAAACACTAAGCAATGAATATTTTATTTCAATGCAACAGGGAGCAGAGGAAGCCGCCAAACAAAAAAATGTTGATTTAATTATTCAGGTGGCCGAGAAAGAAGATTCTACGGAACAATTAGTGGGCTTGGTTGAAAATATGATAGCCAAAAAAGTCGACGCCATTATTGTGACGCCGAATGATTCTATCGCTTTCATTCCGGCTTTCCAAAAAGCGCAAAAAGCAGGGATTCCTATTATTGATCTTGATGTTCGTCTTGACGCAAAAGCTGCTGAAGCCGCGGGACTGAAATTTAATTACGTGGGCGTAGATAATTTTAATGGTGGTTATCTGGAAGCGAAAAATCTTGCCGAAGCGTTGGGTGGGAAAGGTAATGTCGCGGTTTTGGAGGGCATCCCGGGCGTTGATAATGGCGAACAACGCAAAGGTGGTGCATTAAAAGCCTTTGCCGAATATCCGGACATAAAAATCGTGGCATCACAATCAGCAAACTGGGAAACCGAACAAGCACTTAATGTAACTACTAATATTTTAACCGCTAATCCAAATGTTAATGGTATTTTTGCCGCTAACGATAATATGGCAATCGGTGCGGTTACGGCTGTGGAAAACGCCGGTCTGGCAGGCAAAGTATTGGTTACCGGCTATGATGGTATTCCGCTTGCCATTGAATATGTAAAACAAGGCAAAATGCAAAATACTATTGATCAGCTGCCGAAAAAACAAGTGGCTATTGCTATTGAGCATGCGTTAAAACAAATCAATAAACAGGAAATTCCGGCTGTTTATTATGTAGATCCGGTCGTCGTGGATAAAGAACAATCTAAAAATTAC","","","33883","MKLKLLKNIFKISALLAALPTLAVAADKPQIALLMKTLSNEYFISMQQGAEEAAKQKNVDLIIQVAEKEDSTEQLVGLVENMIAKKVDAIIVTPNDSIAFIPAFQKAQKAGIPIIDLDVRLDAKAAEAAGLKFNYVGVDNFNGGYLEAKNLAEALGGKGNVAVLEGIPGVDNGEQRKGGALKAFAEYPDIKIVASQSANWETEQALNVTTNILTANPNVNGIFAANDNMAIGAVTAVENAGLAGKVLVTGYDGIPLAIEYVKQGKMQNTIDQLPKKQVAIAIEHALKQINKQEIPAVYYVDPVVVDKEQSKNY","643319","","ribose ABC transporter, periplasmic protein","Periplasm","","
InterPro
IPR001761
Domain
Periplasmic binding protein/LacI transcriptional regulator
PF00532\"[28-309]TPeripla_BP_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2300\"[137-284]Tno description
signalp\"[1-25]?signal-peptide


","No hits to the COGs database.","","Residues 187 to 294 match (7e-08) PD:PD445834 which is described as ABC PROTEOME COMPLETE BINDING TRANSPORTER ","","","","","","","","","","","","Wed Dec 18 17:48:52 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00932 is paralogously related to AA00209 (2e-34), AA02788 (2e-29), AA02787 (7e-29), AA01455 (3e-23), AA02219 (2e-14), AA02003 (1e-10), AA00750 (3e-07), AA00749 (1e-06) and AA02673 (5e-06).","","","","","","","","","","","Park Y, Cho YJ, Ahn T, Park C. Molecular interactions in ribose transport: the binding proteinmodule symmetrically associates with the homodimeric membranetransporter. EMBO J. 1999 Aug 2;18(15):4149-56. PMID: 10428954 Zaitseva J, Zhang H, Binnie RA, Hermodson The proteins encoded by the rbs operon of Escherichia coli: II. Use of chimeric protein constructs to isolate and characterize RbsC. Protein Sci. 1996 Jun;5(6):1100-7. PMID: 8762141 Barroga CF, Zhang H, Wajih N, Bouyer JH, Hermodson MA. The proteins encoded by the rbs operon of Escherichia coli: I.Overproduction, purification, characterization, and functionalanalysis of RbsA. Protein Sci. 1996 Jun;5(6):1093-9. PMID: 8762140 ","","Wed Dec 18 17:51:37 2002","1","","","" "AA00933","644418","645257","840","ATGAGTGAAAATATCATTTTAGAATTAAAAAATATATCCAAGCGTTTTTTCGGTGTGACCGTACTAGACGACATTCACTTGGATATTCGTCAAGGGGAGGTACTTTGCCTGATAGGTGAAAACGGTGCCGGAAAATCGACTTTGTGTAAGATTATTGCCGGTATTTATCATTGTGATGAGGGCGAAATGTTTTATTCCGACCGAAAATATTCTCCGGACACCGTTAAACAGGCGCAGGAGGCAGGAATCGGGTTTATTCATCAGGAATTGATGCTAGTCCCCAAATTAACTGTACTGGAAAATATCTTTCTGGGTTCAGAGAAAACCTCCTCTTTAGGGTGCATGAACTGGACGGTCATGCGGGAAAAAACGCAACATATCATTAACGAACTGGAACTGGATATAAAGCCGGACGATTTAATTTCCGACTTATCCATCGCTCAGCAACAAATAGTAGAAATCGCTAAAGCGGTATTCAGCGAATATAAGATCATTATTTTTGACGAACCGACATCGTCCATTTCTCGCAAAAATACCGAGGTATTGTTTAACATTATTCATCAACTAAAGGCGAAAGGCGTGGCAATGATTTATATTTCGCATCGTCTGGAGGAATTCAAATATATTGCCGATCGCGTTACCGTTTTAAGAGACGGACGAATTACGGGAACGATGCGCTATCAGGATACATCGCCGGAAGAAATCGTACGTTTGATGGTCGGACGTAAAATTGATTTCACTAGATACCTGCGTACAGGTTCCTTTAACCAGGAAAAATTACGGGTGGAAAATTTACACAACAAATATATTAAACCGATTTCTTTCAGTGTAAACAAAGGA","","","32039","MSENIILELKNISKRFFGVTVLDDIHLDIRQGEVLCLIGENGAGKSTLCKIIAGIYHCDEGEMFYSDRKYSPDTVKQAQEAGIGFIHQELMLVPKLTVLENIFLGSEKTSSLGCMNWTVMREKTQHIINELELDIKPDDLISDLSIAQQQIVEIAKAVFSEYKIIIFDEPTSSISRKNTEVLFNIIHQLKAKGVAMIYISHRLEEFKYIADRVTVLRDGRITGTMRYQDTSPEEIVRLMVGRKIDFTRYLRTGSFNQEKLRVENLHNKYIKPISFSVNKG","645259","May not be correct functional class.","ribose ABC transporter, ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[144-186]TQ9CLB3_PASMU_Q9CLB3;
PF00005\"[32-219]TABC_tran
PS50893\"[7-243]TABC_TRANSPORTER_2
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[31-220]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[6-234]Tno description
PTHR19222\"[7-280]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF12\"[7-280]TSUGAR ABC TRANSPORTER


","BeTs to 7 clades of COG1129COG name: ABC-type sugar (aldose) transport system, ATPase componentFunctional Class: GThe phylogenetic pattern of COG1129 is -----z--v--lb-efgh---j--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.6e-20) to 2/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 21-67 2.2e-14 IPB001140B 141-179 0.00013","Residues 4 to 160 match (6e-07) PD:PD007586 which is described as PROTEOME COMPLETE PLASMID YPDP MEMBRANE GTG ORF TRANSMEMBRANE TM0792 VNG2264C ","","","","","","","","","","","Wed Dec 18 17:00:16 2002","Thu May 13 09:01:38 2004","","Thu May 13 09:01:03 2004","Thu May 13 09:01:38 2004","Thu May 13 09:01:03 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00933 is paralogously related to AA01456 (1e-56), AA00751 (7e-54), AA00207 (2e-52), AA02786 (2e-48), AA01645 (4e-25), AA02440 (2e-24), AA02320 (6e-24), AA02225 (4e-23), AA02718 (1e-22), AA01051 (1e-22), AA01656 (7e-22), AA00858 (2e-21), AA01524 (3e-21), AA00700 (3e-21), AA01616 (2e-20), AA02080 (4e-20), AA00799 (2e-18), AA00415 (2e-18), AA02353 (5e-18), AA01867 (8e-18), AA01510 (2e-17), AA01779 (2e-17), AA01568 (2e-16), AA02805 (3e-16), AA01422 (1e-15), AA02573 (2e-15), AA01820 (2e-15), AA02899 (4e-15), AA02152 (4e-15), AA02140 (8e-15), AA01824 (2e-13), AA02550 (3e-12), AA01684 (3e-12), AA01961 (7e-12), AA01509 (1e-11), AA02609 (3e-11), AA01947 (3e-11), AA02324 (4e-11), AA02642 (2e-10), AA02226 (2e-10), AA01393 (5e-10), AA02331 (8e-10), AA02484 (2e-09), AA02606 (7e-09), AA00061 (1e-08), AA01757 (3e-08), AA00591 (6e-08), AA01569 (8e-08), A02145 (1e-07), AA00934 (1e-07), AA02898 (2e-06), AA02146 (1e-04), AA01555 (2e-04) and AA01291 (0.001).","Thu May 13 09:01:03 2004","","","","","Residues 32 to 219 (E-value = 1.1e-49) place AA00933 in the ABC_tran family which is described as ABC transporter (PF00005)","Thu May 13 09:01:03 2004","","","","","","","1","","","" "AA00934","645441","645902","462","TTGGTACTTGGTATGAGTATTCGGGAAAATATCACACTACCGATTTTAAAACGCTTTTGGCGTAAATTTTATCTGGATAAAAAACAAGAACGGAGAGTCGCTGAAAAAAACAGAACCAAACTACATATCGTTTCTCACGATCAGGAACAGCAAACCAAAACCTTATCGGGCGGAAATCAGCAGAAAGTGATTTTGGCTCGCTGGTTAGAAAGCGGGGTGGATATTTTGTTTTTTGATGAACCGACTCGCGGCATTGATATCGGGGCAAAGTCGGAAATTTATGATTTAATGCGCCAATTTACCGAAAGCGGCGGCACTATCGTGATGGTATCGTCGGATTTACCGGAATTAATCACCATTTCTGATCGCATCGTAGTAATGCGTAACGGTGAAAAGATAAAAGAAATCACCGATCGCACCGAAATTACGGAAGAAAATTTAATGCACCTGATGATAGGTGTT","","","17814","LVLGMSIRENITLPILKRFWRKFYLDKKQERRVAEKNRTKLHIVSHDQEQQTKTLSGGNQQKVILARWLESGVDILFFDEPTRGIDIGAKSEIYDLMRQFTESGGTIVMVSSDLPELITISDRIVVMRNGEKIKEITDRTEITEENLMHLMIGV","645904","","ribose ABC transporter, ATP binding protein","Cytoplasm, Inner membrane","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[54-97]TQ9CLB3_PASMU_Q9CLB3;
PF00005\"[5-130]TABC_tran
PS00211\"[55-69]?ABC_TRANSPORTER_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[1-153]Tno description
PTHR19222\"[1-139]TATP BINDING CASSETE (ABC) TRANSPORTER


","No hits to the COGs database.","Significant hit ( 3.2e-08) to 2/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140B 52-90 8.3e-05 IPB001140C 107-136 0.13","Residues 1 to 43 match (8e-10) PD:PD003603 which is described as ATP-BINDING PROTEOME COMPLETE ABC SUGAR TRANSPORTER RIBOSE TRANSPORTER PLASMID RBSA ","","","","","","","","","","","","Wed Dec 18 17:37:23 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00934 is paralogously related to AA02786 (6e-33), AA00207 (1e-30), AA01456 (8e-25), AA00751 (4e-24), AA02225 (1e-22), AA02080 (4e-13), AA00799 (2e-12), AA02440 (2e-11), AA00700 (3e-11), AA01645 (4e-11), AA01820 (2e-10), AA01524 (6e-10), AA02718 (2e-09), AA00858 (3e-09), AA02550 (4e-09), AA01947 (4e-09), AA01051 (4e-09), AA01824 (8e-09), AA01656 (1e-08), AA02353 (2e-08), AA01779 (3e-08), AA01509 (3e-08), AA00933 (5e-08), AA00415 (4e-07), AA02899 (6e-07), AA02805 (6e-07), AA02898 (8e-07), AA02573 (1e-06), AA02320 (1e-06), AA01422 (1e-06), AA02609 (2e-06), AA02146 (2e-06), AA01616 (2e-06), AA01291 (2e-06), AA02324 (3e-06), AA02140 (3e-06), AA01867 (3e-06), AA02152 (4e-06), AA01555 (5e-06), AA01393 (9e-06), AA02606 (1e-05), AA01684 (2e-05), AA02484 (3e-05), AA01569 (3e-05), AA01757 (2e-04), AA01961 (4e-04) and AA00591 (6e-04).","","","","","","Residues 1 to 130 (E-value = 7.2e-09) place AA00934 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Park Y, Cho YJ, Ahn T, Park C.Molecular interactions in ribose transport: the binding protein module symmetrically associates with the homodimeric membrane transporter.EMBO J. 1999 Aug 2;18(15):4149-56.PMID: 10428954Zaitseva J, Zhang H, Binnie RA, Hermodson The proteins encoded by the rbs operon of Escherichia coli: II. Use of chimeric proteinconstructs to isolate and characterize RbsC.Protein Sci. 1996 Jun;5(6):1100-7.PMID: 8762141Barroga CF, Zhang H, Wajih N, Bouyer JH, Hermodson MA.The proteins encoded by the rbs operon of Escherichia coli: I. Overproduction, purification, characterization, and functional analysis of RbsA.Protein Sci. 1996 Jun;5(6):1093-9.PMID: 8762140 ","","Wed Dec 18 17:49:36 2002","1","","","" "AA00935","645921","646388","468","ATGTTTTCATTGAAAAAAATAATCTCCAAATTAGGCATCGGGTTAGTTTTATTTTTCATGATTTTAGGAATGTCTTTCACATCAGAAGCCTTTTTATCGACTAACAATATTTTTAATATCCTATTACAAGTATCCGTCATTTGCGTGATCTCCGTCGGCATGACTTACGTCATTCTAACCGGAGGTATTAACTTATCGGTCGGCTCTATCGTCGCATTGAGCGCTGTTTGTTTGGGGTTATTCACCCATAGGGGAGTGGCTATTCTAGGTAAAAATCCGACGGAACCGATGCTTTCGATCGTTGTGATGGTATCCGTGCTTGGTTCCATCGGAGTTGGAGCTTTATGCGGGTATGTCAACGGTGTGATTATCGTTTACGGCAAGGTTACTTCGTTTATTACTACCTTAGGCATGATGGGGATTGCGCGAGGGCTGGCACTCACGCTGTCTAACGGTAAAAACTATCTA","","","16269","MFSLKKIISKLGIGLVLFFMILGMSFTSEAFLSTNNIFNILLQVSVICVISVGMTYVILTGGINLSVGSIVALSAVCLGLFTHRGVAILGKNPTEPMLSIVVMVSVLGSIGVGALCGYVNGVIIVYGKVTSFITTLGMMGIARGLALTLSNGKNYL","646390","","ribose ABC transporter, permease protein, N-terminal","Inner membrane, Extracellular","","
InterPro
IPR001851
Family
Bacterial inner-membrane translocator
PF02653\"[36-152]TBPD_transp_2
noIPR
unintegrated
unintegrated
signalp\"[1-30]?signal-peptide
tmhmm\"[10-32]?\"[38-58]?\"[63-83]?\"[97-119]?\"[129-149]?transmembrane_regions


","BeTs to 7 clades of COG1172COG name: Ribose/xylose/arabinose/galactoside ABC-type transport systems, permease componentsFunctional Class: GThe phylogenetic pattern of COG1172 is --------v-rlb-efgh---j--t-Number of proteins in this genome belonging to this COG is","","Residues 25 to 75 match (7e-08) PD:PD579478 which is described as PROTEOME COMPLETE PERMEASE ABC SUGAR TRANSPORTER RIBOSE SYSTEM TRANSPORTER MEMBRANE ","","","","","","","","","","","","Thu May 13 08:57:41 2004","","Thu May 13 08:57:41 2004","","Thu May 13 08:57:41 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00935 is paralogously related to AA02785 (6e-23), AA00208 (1e-18), AA01457 (7e-14), AA02224 (3e-13), AA00753 (1e-12) and AA02220 (2e-11).","Thu May 13 08:57:41 2004","","","","","","","","","","Park Y, Cho YJ, Ahn T, Park C. Molecular interactions in ribose transport: the bindingprotein module symmetrically associates with the homodimericmembrane transporter. EMBO J. 1999 Aug 2;18(15):4149-56. PMID: 10428954 Zaitseva J, Zhang H, Binnie RA, Hermodson The proteins encoded by the rbs operon of Escherichia coli:II. Use of chimeric protein constructs to isolate andcharacterize RbsC. Protein Sci. 1996 Jun;5(6):1100-7. PMID: 8762141 Barroga CF, Zhang H, Wajih N, Bouyer JH, Hermodson MA. The proteins encoded by the rbs operon of Escherichia coli:I. Overproduction, purification, characterization, andfunctional analysis of RbsA. Protein Sci. 1996 Jun;5(6):1093-9. PMID: 8762140 ","","Wed Dec 18 18:01:44 2002","1","","","" "AA00936","646429","646947","519","TTGAATATAACGGATGGCTTTGGTATTCCGATACCGGTAATCATTGCTTTAATCGTCGTATTAATCAGCTTTTACATCTTAACCCAAACCGTTTTTGGACGGCAGGTTTACGCGCTTGGCGGTAATCGTGAGGCGGTGAGATTATCCGGCATTAATGTAAATAAACTGGAAATTAAAACCTATGTGATTAACGGTGCGCTGGCGGCGATCGGAGCGGTGATTCTGGTAGGACGGTTAAACGCTGCACAACCTATTGCCGGAACAGGCTATGAACTGGATGCCATTGCCGCAACGGTGATCGGCGGAACCAGTTTGATCGGCGGCGTCGGTTCGGTGATCAGCACCTCCATTGGCGCGCTGATTATGGGCGTGCTGCAAAACGGACTAACGCTTCTGAACGTCACCTCGTATCTGCAACGTTTGATTATCGGCTTGGTTATTATTCTTGCCGTATTTCTTGATCAATTGCGTCGCGGAGAAGTTTCCACCGGTCGTTTAAGACGTATTTTCTTCAGAGAG","","","21681","LNITDGFGIPIPVIIALIVVLISFYILTQTVFGRQVYALGGNREAVRLSGINVNKLEIKTYVINGALAAIGAVILVGRLNAAQPIAGTGYELDAIAATVIGGTSLIGGVGSVISTSIGALIMGVLQNGLTLLNVTSYLQRLIIGLVIILAVFLDQLRRGEVSTGRLRRIFFRE","646949","","ribose ABC transporter, permease protein, C-terminal","Inner membrane, Cytoplasm","","
InterPro
IPR001851
Family
Bacterial inner-membrane translocator
PF02653\"[7-151]TBPD_transp_2
noIPR
unintegrated
unintegrated
signalp\"[1-33]?signal-peptide
tmhmm\"[9-27]?\"[60-80]?\"[95-117]?\"[136-156]?transmembrane_regions


","BeTs to 7 clades of COG1172COG name: Ribose/xylose/arabinose/galactoside ABC-type transport systems, permease componentsFunctional Class: GThe phylogenetic pattern of COG1172 is --------v-rlb-efgh---j--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 5.6e-11) to 2/2 blocks of the IPB001851 family, which is described as \"Binding-system dependent bacterial transporters (araH, livH/limM families)\". Interpro entry for IP:IPR001851. IPB001851A 32-46 0.00017 IPB001851B 91-102 0.00012","Residues 119 to 158 match (9e-09) PD:PD409969 which is described as COMPLETE PROTEOME PERMEASE ABC SUGAR TRANSPORTER TRANSPORTER MEMBRANE SYSTEM PLASMID ","","","","","","","","","","","","Thu May 13 08:58:55 2004","","Thu May 13 08:58:55 2004","Thu May 13 08:58:55 2004","Thu May 13 08:58:55 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00936 is paralogously related to AA01457 (2e-39), AA00208 (2e-36), AA02785 (3e-34), AA00753 (5e-27), AA02224 (7e-21) and AA02220 (1e-20).","Thu May 13 08:58:55 2004","","","","","","","","","","Park Y, Cho YJ, Ahn T, Park C. Molecular interactions in ribose transport: the binding protein module symmetrically associates with the homodimericmembrane transporter. EMBO J. 1999 Aug 2;18(15):4149-56. PMID: 10428954 Zaitseva J, Zhang H, Binnie RA, Hermodson The proteins encoded by the rbs operon of Escherichia coli: II. Use of chimeric protein constructs to isolate and characterize RbsC. Protein Sci. 1996 Jun;5(6):1100-7. PMID: 8762141 Barroga CF, Zhang H, Wajih N, Bouyer JH, Hermodson MA. The proteins encoded by the rbs operon of Escherichia coli: I. Overproduction, purification, characterization, and functional analysis of RbsA. Protein Sci. 1996 Jun;5(6):1093-9. PMID: 8762140 ","","Thu Dec 19 08:35:12 2002","1","","","" "AA00937","646956","647585","630","ATGCATTATTATTTAGGTATTGACTGCGGAGGTACTTTTATCAAAGCCGCGCTTTTTGATAAAACGGGAAAAATCCACGCCTGCGAAAGAGAAAGTCTCAGTGTAATAAGCGAGCAAGCGAGCTATGCCGAACGGGATATGGACGAGCTTTGGCGGGCATGTGCCAATGTTATTCGCACTACCATAAAACACAGTAAAATTGAACCGCACTTTATTAAAAGTGTCGGCATTTCCGCCCAAGGTAAAGGCGCTTTTTTGCTGGACAAAGAAAATAAACCGTTAGGGCGGGCAATTCTGTCTTCCGATCAACGCTCGCAACCCATTGTTAAACGCTGGCAGCAAGAGGGGCTGGAAAAGAAAGTTTATCCGCTTTCCTATCAAGGGTTATGGACCGGTCATCCTGTTTCTATTTTACGCTGGTTGAAAGAAAACCAACCGCAACGTTATTATGCGATCAATAAGTTACTCATGGCGCACGATTACCTGCGCTTTTGTTTAACCGGAGAGTTGTATTGTGAAGAGAGTAATATTTCGGAAAGTAATTTATACAATATGGCAATAGGAAATTATGAACCCGAATTGGCTCGATTGCTAGGCATTGAAGAAATCATAGGTAAACTGCCCCCATTG","","","23963","MHYYLGIDCGGTFIKAALFDKTGKIHACERESLSVISEQASYAERDMDELWRACANVIRTTIKHSKIEPHFIKSVGISAQGKGAFLLDKENKPLGRAILSSDQRSQPIVKRWQQEGLEKKVYPLSYQGLWTGHPVSILRWLKENQPQRYYAINKLLMAHDYLRFCLTGELYCEESNISESNLYNMAIGNYEPELARLLGIEEIIGKLPPL","647587","","L-xylulokinase","Cytoplasm","","
InterPro
IPR000577
Family
Carbohydrate kinase, FGGY
PTHR10196\"[51-210]TXYLULOSE KINASE
PF00370\"[3-210]TFGGY_N
noIPR
unintegrated
unintegrated
PTHR10196:SF10\"[51-210]TXYLULOSE KINASE


","BeTs to 7 clades of COG1070COG name: Sugar (pentulose and hexulose) kinasesFunctional Class: GThe phylogenetic pattern of COG1070 is a----zy-v-rlbcef-h---j--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.3e-06) to 5/9 blocks of the IPB000577 family, which is described as \"Carbohydrate kinase, FGGY family\". Interpro entry for IP:IPR000577. IPB000577A 38-51 13 IPB000577B 74-89 1 IPB000577C 91-100 1.7e+02 IPB000577D 125-144 61 IPB000577E 170-208 3.7","Residues 5 to 210 match (4e-07) PD:PD557892 which is described as PROTEOME KINASE ERYTHRITOL COMPLETE TRANSFERASE ","","","","","","","","","","","","Thu Dec 19 08:43:33 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00937 is paralogously related to AA01451 (2e-21) and AA02230 (4e-15).","","","","","","Residues 3 to 210 (E-value = 2.1e-71) place AA00937 in the FGGY_N family which is described as FGGY family of carbohydrate kinases, N-terminal domain (PF00370)","","","","","Jin YS, Jones S, Shi NQ, Jeffries TW.Molecular cloning of XYL3 (D-xylulokinase) from Pichia stipitis and characterization of its physiological function.Appl Environ Microbiol. 2002 Mar;68(3):1232-9.PMID: 11872473vanKuyk PA, de Groot MJ, Ruijter GJ, de Vries RP, Visser J.The Aspergillus niger D-xylulose kinase gene is co-expressed with genes encoding arabinan degrading enzymes, and is essential for growth on D-xylose and L-arabinose.Eur J Biochem. 2001 Oct;268(20):5414-23.PMID: 1160626Johansson B, Christensson C, Hobley T, Hahn-Hagerdal B.Xylulokinase overexpression in two strains of Saccharomyces cerevisiae also expressing xylose reductase and xylitol dehydrogenase and its effect on fermentation of xylose andlignocellulosic hydrolysate.Appl Environ Microbiol. 2001 Sep;67(9):4249-55.PMID: 11526030 Sanchez,J.C., Gimenez,R., Schneider,A., Fessner,W.D., Baldoma,L.,Aguilar,J. and Badia,J.Activation of a cryptic gene encoding a kinase for L-xylulose opens a new pathway for the utilization of L-lyxose by Escherichia coliJ. Biol. Chem. 269 (47), 29665-29669 (1994)PubMed: 7961955","","Thu Dec 19 08:49:13 2002","1","","","" "AA00938","647696","648418","723","TTGTGTTTGACCGATGATAATGACGAAACCAAATTAAATGTGCTGTTAGGCACCTGGTCAATTGTGACAGGAATTTCCCATACGATTGATGAAAACCAAACTCTACCATTCGCCCACGGACGTTATGTCGAACAAAATACCTTCTTGATTCAGGAAGCAAGTCCGACTTCTGCCGGCAATTTAGAATGGTTCATCAAGCAATGGAATTTAACTTATCATCAGACAAATCAAATGGTAGAAGCATTACCGCCGGCACAAAGTGCGGTCATTTTCATCCCATTTTTATACGGAACTAACGCCAAATTAGGCATGACTGCCGGATTCTATGGCATGCAAGCCCACCACACTTTGGCACATTTACTGCAAGCGGTCTATGAAGGTGTATTATTCAGCCTCATGATACACTTAGAGCGGATGTATCAACGTTTTCCTCACGTACAACGTTTGCGTGTAACAGGCGGCCCGGTAAAATCACAAGTTTGGTTGCAAATGCTGGCAGATTTTAGTGGAAAAACCTTGGAAGTTCTGCAAACTGAAGAAGTCGGCTGCCTCGGCGCGGCTTTAATGGCCGCGGAAGGAGCCAATCACGAAGCAGCCACTTTAAAACGTAATCAGAAATTAAAAATTATTCATCCTAATTCCTTTCATTTCGACGCATATCAACAGAAATATCAGAAATATCAGAAATATCGTAAGCTAGTTAATCTACTGAGCGAAATGGCA","","","29017","LCLTDDNDETKLNVLLGTWSIVTGISHTIDENQTLPFAHGRYVEQNTFLIQEASPTSAGNLEWFIKQWNLTYHQTNQMVEALPPAQSAVIFIPFLYGTNAKLGMTAGFYGMQAHHTLAHLLQAVYEGVLFSLMIHLERMYQRFPHVQRLRVTGGPVKSQVWLQMLADFSGKTLEVLQTEEVGCLGAALMAAEGANHEAATLKRNQKLKIIHPNSFHFDAYQQKYQKYQKYRKLVNLLSEMA","648420","","L-xylulokinase","Cytoplasm","","
InterPro
IPR000577
Family
Carbohydrate kinase, FGGY
PTHR10196\"[8-241]TXYLULOSE KINASE
PF02782\"[8-191]TFGGY_C
PS00445\"[106-126]?FGGY_KINASES_2
noIPR
unintegrated
unintegrated
PTHR10196:SF10\"[8-241]TXYLULOSE KINASE


","BeTs to 8 clades of COG1070COG name: Sugar (pentulose and hexulose) kinasesFunctional Class: GThe phylogenetic pattern of COG1070 is a----zy-v-rlbcef-h---j--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 3.6e-06) to 2/9 blocks of the IPB000577 family, which is described as \"Carbohydrate kinase, FGGY family\". Interpro entry for IP:IPR000577. IPB000577H 85-126 3.2e+02 IPB000577I 149-185 4.6e-06","Residues 17 to 56 match (1e-10) PD:PD471733 which is described as KINASE L-XYLULOSE COMPLETE TRANSFERASE PROTEOME CRYPTIC L-XYLULOKINASE PROBABLE KINASE 5-KINASE ","","","","","","","","","","","","Thu Dec 19 09:05:32 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00938 is paralogously related to AA01451 (5e-11) and AA02230 (4e-05).","","","","","","Residues 8 to 221 (E-value = 2.9e-60) place AA00938 in the FGGY_C family which is described as FGGY family of carbohydrate kinases, C-terminal domain (PF02782)","","","","","Jin YS, Jones S, Shi NQ, Jeffries TW. Molecular cloning of XYL3 (D-xylulokinase) from Pichiastipitis and characterization of its physiological function. Appl Environ Microbiol. 2002 Mar;68(3):1232-9. PMID: 11872473 vanKuyk PA, de Groot MJ, Ruijter GJ, de Vries RP, Visser J. The Aspergillus niger D-xylulose kinase gene is co-expressedwith genes encoding arabinan degrading enzymes, and isessential for growth on D-xylose and L-arabinose. Eur J Biochem. 2001 Oct;268(20):5414-23. PMID: 1160626 Johansson B, Christensson C, Hobley T, Hahn-Hagerdal B. Xylulokinase overexpression in two strains of Saccharomycescerevisiae also expressing xylose reductase and xylitoldehydrogenase and its effect on fermentation of xylose and lignocellulosic hydrolysate. Appl Environ Microbiol. 2001 Sep;67(9):4249-55. PMID: 11526030 Sanchez,J.C., Gimenez,R., Schneider,A., Fessner,W.D.,Baldoma,L., Aguilar,J. and Badia,J. Activation of a cryptic gene encoding a kinase for L-xyluloseopens a new pathway for the utilization of L-lyxose byEscherichia coli J. Biol. Chem. 269 (47), 29665-29669 (1994) PubMed: 7961955 ","","Thu Dec 19 09:05:32 2002","1","","","" "AA00939","650784","648472","2313","ATGTTAAACCAACAAATCAGCCAACTTATCGCGCAGGAATTGAATGTGTGTGATAACCAAATTCTCGCCGCCATTCAACTGTTAGACGATGGCAACACCATTCCCTTTATCGCCCGTTATCGTAAAGAAGCCACCGGCGGGCTGGACGACACCCAATTACGCCATTTTGAGACCCGTTTAATTTATTTGCGTGAACTGGAAGAACGTCGTCAAACCATTCTGAAATCCATTGAAGAGCAAGGCAAATTAACGGATGAATTGCGTGGCAAAATCCAAGCTACGCAGAGCAAAACTGAATTGGAAGATTTATATTTACCGTTCAAACCGAAACGCCGCACCAAAGGACAAATTGCCATTGAAGCCGGGCTTGAGCCGTTGGCGGATTTACTTTGGAACGAACCGAAAACCGATCCGGAAACGGCGGCAAATGAATTCATTAATGTGGAAAAAGGCGTTGCCGATAGCAAAGCGGTACTGGACGGCGCCCGTTATATTTTAATGGAACGTTTCGCCGAGGACGCTGGCTTACTGGCGAAAGTGCGCGATTATTTAAGCAAAAATGCCTTATTGGTTTCCAAAGTGCTTGAGGGCAAAGAAACGGAAGGTGCAAAATTCCAAGATTATTTTGACCATCAGGAGTTATTCAAAAATGTACCTTCGCACCGTGCGTTGGCAATGTTTCGTGGGCGTAACGAAGGCATTTTGCAGCTAAGTTTAAATGCCGATCCCGACGCGGAAGAAGGAAGCCGCCAAAGTTATTGCGAAGAGATTATCCGCGACTATTTGGGCGTTCGTTTCACCGGACAACCTGCGGATAAATGGCGTGAGCAGGTTATCGCCTGGACATGGAAAATCAAGGTGGCGCTGCATTTAGAAACGGAATTGATGGCAACGTTGCGTGAGAAAGCGGAAGAAGAAGCCATTGATGTTTTTGCTCGAAATCTGACCGCACTTTTAATGGCGGCACCGGCAGGCGCGAAAAATACCATGGGTCTAGACCCGGGTTTGCGTACCGGCGTGAAAGTGGCGGTAGTGGATAGCACCGGTAAATTATTGGCAACGGACACCATTTATCCACATACGGGACAAATGGATCGCGCCATGTTGTCCATTTTCCAATTAATTAAGCAACATAATGTGGAATTAATCGCCATCGGTAACGGCACCGCTTCCCGTGAGACGGAGCGTTTTGCCAAAGATGTGATTAAAGAAATCAAAGAGAATAAACCGCAAACGGTAGTGGTGAGTGAGGCAGGCGCTTCCGTGTATTCCGCTTCCGAATTGGCGGCGCAGGAATTCCCTGAATTGGACGTGTCGTTGCGCGGTGCGGTATCTATCGCTCGTCGTTTGCAGGATCCGTTGGCGGAGTTGGTAAAAATCGAACCGAAAGCCATTGGTGTAGGGCAATATCAACATGATGTGAATCAAAGCCAGCTGGCGCGCAAACTGGACGCCGTAGTGGAAGACTGCGTGAACGCCGTGGGCGTGGATTTGAATACCGCTTCCGTACCGTTATTGGCACGCGTGGCGGGAATGACCAAAACCATTGCGCAGAATATTGTGGCATATCGTGATGAAAATGGGCGTTTCGACAGCCGTGAGCAACTGAAAAAAGTGCCGCGTTTGGGACCGAAATCCTTTGAACAATGTGCCGGTTTTATGCGTATTGCGGCGGGCAACAATCCATTAGACGCTTCCGGCGTACACCCGGAGGCTTATCCTGTTGTGGAAAAAATCCTGCAGGCAACGGAACAGTCCATTCAGGATTTAATGGGCAATGCCGGTTTGGTGCGTCAGCTTGATGCAAAACAGTTTACTGATGAACAATTCGGCTTGCCGACGGTGCAGGATATTTTCAAAGAATTGGAAAAACCGGGACGCGACCCGCGCGGCGAATTTAAAACCGCGACCTTCGCGGATGGTGTGGAGGAGATTACCGACTTAAAAGCGGGCATGATTTTAGAAGGAACGGTAACTAACGTCACTAATTTTGGCGCCTTTGTGGACATCGGCGTTCACCAAGACGGTTTGGTGCATATTTCTTCTTTAAGCGATAAATTCGTGGAAGATCCGCATCAAGTAGTGAAAACCGGTGATATAGTCAAAGTGAAAGTACTGGAAGTGGATGTCGCGCGTCGCCGTATTGCGCTGACGATGCGTTTAGATGAAAGTGCGGTGAAAAACGATGGCAAATCCGACCGCACTTTATCGGCAAAACCACGCACCAATGCTTCTCGTCAAGAACGTAATGCGCCAAGAACCAATAACGCTATGGGCAACGCATTTGCCGACGCGTTGAAGAATTGGAAGAGG","","","85513","MLNQQISQLIAQELNVCDNQILAAIQLLDDGNTIPFIARYRKEATGGLDDTQLRHFETRLIYLRELEERRQTILKSIEEQGKLTDELRGKIQATQSKTELEDLYLPFKPKRRTKGQIAIEAGLEPLADLLWNEPKTDPETAANEFINVEKGVADSKAVLDGARYILMERFAEDAGLLAKVRDYLSKNALLVSKVLEGKETEGAKFQDYFDHQELFKNVPSHRALAMFRGRNEGILQLSLNADPDAEEGSRQSYCEEIIRDYLGVRFTGQPADKWREQVIAWTWKIKVALHLETELMATLREKAEEEAIDVFARNLTALLMAAPAGAKNTMGLDPGLRTGVKVAVVDSTGKLLATDTIYPHTGQMDRAMLSIFQLIKQHNVELIAIGNGTASRETERFAKDVIKEIKENKPQTVVVSEAGASVYSASELAAQEFPELDVSLRGAVSIARRLQDPLAELVKIEPKAIGVGQYQHDVNQSQLARKLDAVVEDCVNAVGVDLNTASVPLLARVAGMTKTIAQNIVAYRDENGRFDSREQLKKVPRLGPKSFEQCAGFMRIAAGNNPLDASGVHPEAYPVVEKILQATEQSIQDLMGNAGLVRQLDAKQFTDEQFGLPTVQDIFKELEKPGRDPRGEFKTATFADGVEEITDLKAGMILEGTVTNVTNFGAFVDIGVHQDGLVHISSLSDKFVEDPHQVVKTGDIVKVKVLEVDVARRRIALTMRLDESAVKNDGKSDRTLSAKPRTNASRQERNAPRTNNAMGNAFADALKNWKR","648474","Fuchs et al., 1996, report similarity of this protein to mannitol repressor protein MtlR and the presumptive RNA-binding domains of Pnp.","transcription accessory protein (toxin expression)","Cytoplasm","","
InterPro
IPR003029
Domain
RNA binding S1
PF00575\"[647-720]TS1
SM00316\"[649-720]TS1
PS50126\"[651-720]TS1
InterPro
IPR003583
Domain
Helix-hairpin-helix DNA-binding, class 1
SM00278\"[504-523]T\"[534-553]THhH1
InterPro
IPR006641
Domain
Resolvase, RNase H-like fold
SM00732\"[327-424]TYqgFc
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[651-746]Tno description
noIPR
unintegrated
unintegrated
PTHR10724\"[1-771]TTEX PROTEIN-RELATEDTRANSCRIPTION ACCESSORY PROTEIN (S1 RNA BINDING DOMAIN)


","BeTs to 9 clades of COG2183COG name: Predicted RNA binding protein, contains S1 domainFunctional Class: RThe phylogenetic pattern of COG2183 is -----------lb-efghsn-j--twNumber of proteins in this genome belonging to this COG is","Significant hit ( 6.7e-13) to 2/2 blocks of the IPB003029 family, which is described as \"S1 RNA binding domain\". Interpro entry for IP:IPR003029. IPB003029A 656-667 2.7e-05 IPB003029B 698-709 7.3e-06Significant hit ( 1.2e-08) to 2/9 blocks of the PR00681 family, which is described as \"Ribosomal protein S1 signature\". Prints database entry for PR:PR00681. PR00681H 664-683 0.00077 PR00681I 703-721 0.0058 PR00681A 651-669 0.5 PR00681G 672-693 0.35","Residues 720 to 771 match (2e-08) PD:PD381869 which is described as PM1448 PROTEOME COMPLETE ","","","","","","","","","","","Wed Feb 5 13:57:06 2003","Wed Feb 5 13:57:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00939 is paralogously related to AA02528 (1e-12), AA01372 (3e-09), AA00151 (3e-09), AA00943 (3e-08) and AA01213 (1e-05).","","","","","","Residues 647 to 720 (E-value = 1.2e-30) place AA00939 in the S1 family which is described as S1 RNA binding domain (PF00575)","","","","","Fuchs TM, Deppisch H, Scarlato V, Gross R.A new gene locus of Bordetella pertussis defines a novel family of prokaryotic transcriptional accessory proteins.J Bacteriol. 1996 Aug;178(15):4445-52.PMID: 8755871","","Wed Feb 5 13:57:06 2003","1","","","" "AA00940","651888","651004","885","ATGAATATAAACCAATTAAAGACATTTATTGTGCTTGCCGATTGTTTGAGTGTGACTGAAACATCGAAGCGTTTGTTTTGTACACAGCCTGCGGTGAGTATAAAAATCCGCAAATTGGAAGAGACCTTAAATACTGTACTTTTTGAGCGAATCAACAACCGCTTGTATTTAACAGAACAAGGTAAAATTTTTTATAGTTATGCGGAACAGATAATTAGTACCTTAGAAATGTCAGTGGAGCACCTACATCAATATGATGATCCTAATTATGGCAAGATTATTATCGGCGCAAGCCATTTTGTCGGTGTTTATTTGTTACCGCAGGTTATTGCAGAGTATCGAAAATTATCACCGAATGTAGAACTTCGTCTTGAGATTCTTTCTTCCCAACAGCTGATTCAGGGGCTGGAGAATCATTCCATTGACTTTATTATTATGTCTGACCAAATTTATTTTGATCCGCAAAAATATGATGTTAATCGTTTTTTGTCTGATGAACTGATTTTGATTGTTCCTCCTGATCATGTGTTAGCCACATATGAATCTTGTCATTTTGAGCAACTTTGTGACGAATTATTTATCATTAAACCGAAGAATTCTCAAACCCGAAAATTTCTTTTACAGCAATTTTCAAAAGATCAGATTTCTCTGCTTAAGTTTATGGAAATCAATAGTTTAGAAGGTATTAAACGTTGTGTAATGAATGGATTAGGGGTTTCCATTATTTCTCGATTTTCCGTTGAAAACGAACTGAAAATGGGTATGTTGAAGGCTGTAGAATTAGACAGTTTTCAATTTAAACGTGGGATAAATTATATTTACCATAAAGAAAAATGCCTTTCATCAGCAATTGGGCGATTTATTGGGCTGTTGAACATACTTAAA","","","34149","MNINQLKTFIVLADCLSVTETSKRLFCTQPAVSIKIRKLEETLNTVLFERINNRLYLTEQGKIFYSYAEQIISTLEMSVEHLHQYDDPNYGKIIIGASHFVGVYLLPQVIAEYRKLSPNVELRLEILSSQQLIQGLENHSIDFIIMSDQIYFDPQKYDVNRFLSDELILIVPPDHVLATYESCHFEQLCDELFIIKPKNSQTRKFLLQQFSKDQISLLKFMEINSLEGIKRCVMNGLGVSIISRFSVENELKMGMLKAVELDSFQFKRGINYIYHKEKCLSSAIGRFIGLLNILK","651006","","probable transcriptional regulator (LysR family)","Cytoplasm","","
InterPro
IPR000847
Domain
Bacterial regulatory protein, LysR
PR00039\"[18-29]T\"[29-39]T\"[39-50]THTHLYSR
PF00126\"[3-62]THTH_1
PS50931\"[1-58]THTH_LYSR
InterPro
IPR005119
Domain
LysR, substrate-binding
PF03466\"[86-295]TLysR_substrate
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[1-87]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[87-203]Tno description
signalp\"[1-21]?signal-peptide


","BeTs to 14 clades of COG0583COG name: Transcriptional regulatorFunctional Class: KThe phylogenetic pattern of COG0583 is a-m----q-drlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-10) to 1/1 blocks of the IPB000847 family, which is described as \"Bacterial regulatory protein, LysR family\". Interpro entry for IP:IPR000847. IPB000847 17-50 1.3e-10Significant hit ( 1.4e-06) to 1/2 blocks of the IPB001583 family, which is described as \"NodD transcription activator carboxyl terminal region\". Interpro entry for IP:IPR001583. IPB001583A 5-55 1.3e-06","Residues 186 to 288 match (8e-07) PD:PD016091 which is described as TRANSCRIPTIONAL PROTEOME COMPLETE REGULATION TRANSCRIPTION DNA-BINDING REGULATOR LYSR FAMILY ACTIVATOR ","","","","","","","","","","","","Thu Dec 19 09:17:08 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00940 is paralogously related to AA01513 (1e-16), AA01794 (3e-14), AA01999 (4e-12), AA02539 (2e-11), AA00371 (3e-11) and AA00985 (6e-11).","","","","","","Residues 86 to 295 (E-value = 1.2e-37) place AA00940 in the LysR_substrate family which is described as LysR substrate binding domain (PF03466)","","","","","Viale AM, Kobayashi H, Akazawa T, Henikoff S.rbcR [correction of rcbR], a gene coding for a member of the LysR family of transcriptional regulators, is located upstream of the expressed set of ribulose 1,5-bisphosphate carboxylase/oxygenase genes in the photosynthetic bacterium Chromatium vinosum.J Bacteriol. 1991 Aug;173(16):5224-9.PMID: 1907267","","Thu Dec 19 09:22:30 2002","1","","","" "AA00941","651998","653464","1467","ATGAACAAAGCTATTCAGACTACCCCAATAGAGAATAAAGAAAGGAATAAACTTCTCAAACAATTAGGTATTCCTCTGGCGCTTGTCATCTTACTACTTTTAATGTGGATGCCTACCCCGGAGGGGCTAACCATTCAGGGACAAAAATCCATTGCAATTTTTGTTGGCGCCTTGATTTTGTGGGTGTGTGGTTCTATTCCTATTTATTTGACATCAATGATTGTCATCATCTTATTATCACTCACCCAGACTGTGGAAAAAGATAAACTTGTTTTTGCCACATTAGGGTATGATGTGATTTGGTTAATGGTATCGGCATTTGTTCTCACCTCGGCTATGATCAAATCGAATATCGCCCGCCGTTTTGCGCTTTGGATGATTACTCATTTTGGACAAACACCGAAGAAAGCCTTATTTGTGCTTGTATTAATTAATTTTATACTTGTTTTCTTTGTTCCTTCAACAACAGCACGAGCCTCATTAATGGTTCCTATTTGCTTAATTCTTTTAGAAATTTATAAAGCCATGCCAGGTGAAAGCAATTTTGGACGATTGATGATGTTACAAGGTGTACAGGCCGATGCGATTGCCACATCGGGTGTGATGACAGGTACTGCTGCCAACATTATTTCCGTTGGTTTTATCAATAGCCAAGCAAACGGCGATATCGGTTATATTGACTGGGTAATAGCCTCCTTCCCTATTGCCTTTATATCCATGATGATTTCTTTTATGGTGGGCTTTAAATTATTTTCTATTAAAAAAGAAACACAATTTATTGAGGCATTGGGGCTCTTACAGGCGGAATTCAAAAAACTTGGTAAATTTACCTTAGATGAGAAGAAAGCCATGGTAATCTTCTTGCTCACCGTGGTGTTATGGGCAACAGAAGATTATCAAAAAATCTTATTTGGTTTCAAAATCAGTGTATATATGACTGCCGTTATTGCAGCCGTACTGTGCTTAATGCCTAAAATTGGATTACTAACCTGGAATGAAGCAAAAATCAAATGGGATTTAATGCTATTTGCTGCCGGTGCTTACGCCGCAGGAAATACGCTTGAGTCAACCAAAGGTGCTCAATGGATTATGGATAAAATTGTTCATGGATTGGGTTTAGAGAGCATGAATCATACCTTCGTCTATATCGCCGTCATTTTTATTTGCATGTATAGTCACCTGATCTTCACCAGTAAAACCGTACGAACTACGATTCTAATTCCATCTATTATCGCATTAGCCCAATCTTTAGGGATAAATCCGGTGACACTCGCACTCTCAGCATCATTTACTCTTACCTACACTATAACCTTACCGCCACATTCTAAGGTAAATACCATTTATTTTGCGACCGGCTATTTCAGTGTATTAGATCAGATGAAGTATGGATTAATCACCTGTTTCATTAGTGCCTGCATGATCTGCCTTGCAACCTTTACATGGTTCCAATTACTCGGATACGGTTTA","","","54126","MNKAIQTTPIENKERNKLLKQLGIPLALVILLLLMWMPTPEGLTIQGQKSIAIFVGALILWVCGSIPIYLTSMIVIILLSLTQTVEKDKLVFATLGYDVIWLMVSAFVLTSAMIKSNIARRFALWMITHFGQTPKKALFVLVLINFILVFFVPSTTARASLMVPICLILLEIYKAMPGESNFGRLMMLQGVQADAIATSGVMTGTAANIISVGFINSQANGDIGYIDWVIASFPIAFISMMISFMVGFKLFSIKKETQFIEALGLLQAEFKKLGKFTLDEKKAMVIFLLTVVLWATEDYQKILFGFKISVYMTAVIAAVLCLMPKIGLLTWNEAKIKWDLMLFAAGAYAAGNTLESTKGAQWIMDKIVHGLGLESMNHTFVYIAVIFICMYSHLIFTSKTVRTTILIPSIIALAQSLGINPVTLALSASFTLTYTITLPPHSKVNTIYFATGYFSVLDQMKYGLITCFISACMICLATFTWFQLLGYGL","653466","","symporter transmembrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR001898
Family
Sodium/sulphate symporter
PF00939\"[18-488]TNa_sulph_symp
TIGR00785\"[38-482]Tdass: transporter, divalent anion:Na+ sympo
noIPR
unintegrated
unintegrated
PTHR10283\"[39-487]TCATION TRANSPORTER RELATED
PTHR10283:SF13\"[39-487]TSODIUM/CARBOXYLATE COTRANSPORTER RELATED
signalp\"[1-42]?signal-peptide
tmhmm\"[20-38]?\"[44-62]?\"[67-85]?\"[99-119]?\"[134-154]?\"[160-178]?\"[193-215]?\"[225-245]?\"[302-322]?\"[379-397]?\"[418-438]?\"[462-482]?transmembrane_regions


","BeTs to 16 clades of COG0471COG name: Di- and tricarboxylate transportersFunctional Class: PThe phylogenetic pattern of COG0471 is -om-k-yq-d-lbcefghsnu--i--Number of proteins in this genome belonging to this COG is","Significant hit ( 2.9e-34) to 8/8 blocks of the IPB001898 family, which is described as \"Sodium:sulfate symporter family\". Interpro entry for IP:IPR001898. IPB001898A 61-84 0.098 IPB001898B 101-127 6.5e-05 IPB001898C 146-165 30 IPB001898D 186-210 3.3 IPB001898E 223-247 0.011 IPB001898F 273-299 9.7e-07 IPB001898G 335-364 0.0051 IPB001898H 420-468 0.0059","Residues 50 to 239 match (2e-08) PD:PD377184 which is described as INTEGRAL MEMBRANE TRANSPORTER ","","","","","","","","","","","","Thu Feb 20 08:33:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00941 is paralogously related to AA02254 (6e-31), AA01784 (1e-22), AA00136 (4e-21), AA00741 (3e-20) and AA00615 (2e-05).","","","","","","Residues 18 to 488 (E-value = 3.7e-30) place AA00941 in the Na_sulph_symp family which is described as Sodium:sulfate symporter transmembrane region (PF00939)","","","","","Weber,A., Menzlaff,E., Arbinger,B., Gutensohn,M.,Eckerskorn,C. and Flugge,U.I. The 2-oxoglutarate/malate translocator of chloroplast envelopemembranes: molecular cloning of a transporter containing a12-helix motif and expression of the functional protein inyeast cells. Biochemistry 34(8): 2621-2627, 1995. PubMed: 7873543.","","Thu Dec 19 09:39:05 2002","1","","","" "AA00942","653479","654075","597","ATGCGTTTAATTTTATTAAGACATGGTGAAACTTTATGGAATAAAGAACACCGTCTACAAGGACACCTAAATTCTCCACTTTCGGAAAAAGGTATTGCTCAAGCAAAAGCGATTAAACCTTTAATCGAAAAATTTTCCTTAAAAAAAGTTATTTGCTCCGATTTGGAACGCGCCAAGCAAACCGCTGAACTTATCGGTTTTCCCAATGCCACACCGGATAGCCATTTGCGCGAACTTGCCATGGGGGAATGGGAAGGGCGAAAAAAAGACGAGATTATGCAAGAAAACCCCATTCTTTACCAAGACTGGAGAAACGGTAACTACACACCTAGAGGTGGTGAGAGTTGGCAAGATTTTTGTCATCGAATTTCAACCGCACTTTTTCAGTGGACAAATAAATCTGATGGAGACATCTTAGCCATCGTACATAGTGGTGTAGTTCGCGCTGCCTGTGAAAGATTAATTTCTTTATCAACCAAGCATCTATTACCGGTAACCCAGGGAACACTTACTATTTTTGACATAACGCCAAATCATCCCATCAAGTTAGAAGCCTATAATCTAGGAAGTTTTGTGCCGGAAATCAATGTGGCAGAT","","","24285","MRLILLRHGETLWNKEHRLQGHLNSPLSEKGIAQAKAIKPLIEKFSLKKVICSDLERAKQTAELIGFPNATPDSHLRELAMGEWEGRKKDEIMQENPILYQDWRNGNYTPRGGESWQDFCHRISTALFQWTNKSDGDILAIVHSGVVRAACERLISLSTKHLLPVTQGTLTIFDITPNHPIKLEAYNLGSFVPEINVAD","654077","","related to phosphoglycerate mutase","Cytoplasm","","
InterPro
IPR001345
Active_site
Phosphoglycerate/bisphosphoglycerate mutase
PS00175\"[5-14]TPG_MUTASE
InterPro
IPR013078
Domain
Phosphoglycerate mutase
PF00300\"[2-150]TPGAM
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1240\"[2-198]Tno description
PIRSF001490\"[1-194]TCofactor-dependent phosphoglycerate mutase
PTHR23029\"[1-175]TPHOSPHOGLYCERATE MUTASE


","No hits to the COGs database.","Significant hit ( 7.1e-27) to 4/4 blocks of the IPB001345 family, which is described as \"Phosphoglycerate mutase family\". Interpro entry for IP:IPR001345. IPB001345A 3-32 1.9e-12 IPB001345B 50-62 0.00061 IPB001345C 68-99 0.00012 IPB001345D 111-129 0.97","Residues 3 to 149 match (3e-30) PD:PD002638 which is described as PROTEOME COMPLETE PHOSPHOGLYCERATE MUTASE PGAM ISOMERASE KINASE GLYCOLYSIS BPG-DEPENDENT PHOSPHOGLYCEROMUTASE ","","","","","","","","","","","","Wed Feb 19 15:14:38 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00942 is paralogously related to AA02057 (1e-11) and AA00453 (3e-04).","","","","","","Residues 1 to 184 (E-value = 2.9e-27) place AA00942 in the PGAM family which is described as Phosphoglycerate mutase family (PF00300)","","","","","Rigden DJ.Unexpected catalytic site variation in phosphoprotein phosphatase homologues of cofactor-dependent phosphoglycerate mutase.FEBS Lett. 2003 Feb 11;536(1-3):77-84.PMID: 12586342 Rigden,D.J., Bagyan,I., Lamani,E., Setlow,P. and Jedrzejas,M.J.A cofactor-dependent phosphoglycerate mutase homolog from Bacillusstearothermophilus is actually a broad specificity phosphataseJOURNAL Protein Sci. 10 (9), 1835-1846 (2001)PubMed: 11514674Rigden,D.J., Mello,L.V., Setlow,P. and Jedrzejas,M.J.Structure and mechanism of action of a cofactor-dependentphosphoglycerate mutase homolog from Bacillus stearothermophiluswith broad specificity phosphatase activityJ. Mol. Biol. 315 (5), 1129-1143 (2002)PubMed: 11827481","","Wed Feb 19 15:13:11 2003","1","","","" "AA00943","654602","654471","132","GTGGAAGAGATTGCCGACTTAAGAGCGGTAACTAACGCTACCAATTTAGGCGCCGTTGTGGACATCGGTGTTCGCCAAGACGGTTTGGTGCATATTCCTTGCTTAAGTGATAGGAAGATCCGCGCCAAGTGG","","","4796","VEEIADLRAVTNATNLGAVVDIGVRQDGLVHIPCLSDRKIRAKW","654471","","conserved hypothetical protein","Cytoplasm","This sequence is similar to gi|23467376, a predicted transcriptional accessory protein from H.somnus. See also gi|16272511 from H.influenzae.","
noIPR
unintegrated
unintegrated
PTHR10724\"[10-41]TTEX PROTEIN-RELATEDTRANSCRIPTION ACCESSORY PROTEIN (S1 RNA BINDING DOMAIN)


","BeTs to 9 clades of COG2183COG name: Predicted RNA binding protein, contains S1 domainFunctional Class: RThe phylogenetic pattern of COG2183 is -----------lb-efghsn-j--twNumber of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Wed Feb 25 08:37:59 2004","Wed Feb 25 08:37:59 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00943 is paralogously related to AA00939 (1e-09).","Wed Feb 25 08:37:59 2004","","","","","","","","","","","","","1","","","" "AA00944","654813","655292","480","ATGGCAAAGTCAAATTACATCACCCGACAAGGCTGGAATATGCTGGATCGGGAATTGAAATTTTTATGGAAAGAAGAGCGTCCGCAGGTGACGCAAGCCGTCTCCGACGCGGCGGCATTAGGCGATCGCAGCGAAAATGCGGAATATATTTACGGTAAACGACGCTTACGGGAAATCGATCGCCGTGTACGCTTTCTGACCAAGCGTCTGGAAGTATTGCAAATTGTGGATTATTCCCCCAAACAGGAAAGCAAAGTGTTTTTCGGCGCATGGGTGGAACTGGAAAATGAAGACGGCGAAGTGAAACAATATCGCATTGTCGGCTGTGATGAATTTGATCCGGCAAATAACTGGATTTCCATTGATTCACCGGTGGCACGCGCACTAATCGGCAAGCAGGAAGATGACGAAATTACGGTGGACACGCCTGCCGGTAAAATTTGGCTATGTGTGAATCGAATTTGGTATGAAAAAAACGCA","","","20498","MAKSNYITRQGWNMLDRELKFLWKEERPQVTQAVSDAAALGDRSENAEYIYGKRRLREIDRRVRFLTKRLEVLQIVDYSPKQESKVFFGAWVELENEDGEVKQYRIVGCDEFDPANNWISIDSPVARALIGKQEDDEITVDTPAGKIWLCVNRIWYEKNA","655294","","transcription elongation factor","Cytoplasm","","
InterPro
IPR001437
Domain
Transcription elongation factor, GreA/GreB region, prokaryotic
PD004918\"[90-156]TGREB_HAEIN_P43882;
G3DSA:1.10.287.180\"[2-76]Tno description
G3DSA:3.10.50.30\"[76-157]Tno description
PF01272\"[81-156]TGreA_GreB
PF03449\"[2-75]TGreA_GreB_N
PS00829\"[18-49]TGREAB_1
PS00830\"[120-136]TGREAB_2
InterPro
IPR006358
Family
Transcription elongation factor GreB, prokaryotic
TIGR01461\"[3-158]TgreB: transcription elongation factor GreB
InterPro
IPR012243
Family
Prokaryotic transcription elongation factor GreA, GreB
PIRSF006092\"[2-157]TTranscription elongation factor GreA/GreB


","BeTs to 16 clades of COG0782COG name: Transcription elongation factorFunctional Class: KThe phylogenetic pattern of COG0782 is --------vdrlb-efghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.6e-51) to 2/2 blocks of the IPB001437 family, which is described as \"Prokaryotic transcription elongation factor GreA/GreB\". Interpro entry for IP:IPR001437. IPB001437A 18-67 1e-27 IPB001437B 104-136 1.2e-22","Residues 111 to 145 match (2e-09) PD:PD344060 which is described as FACTOR ELONGATION TRANSCRIPTION COMPLETE PROTEOME GREB TRANSCRIPT CLEAVAGE COIL DNA-BINDING ","","","","","","","","","","","","Thu Dec 19 09:49:57 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00944 is paralogously related to AA01668 (8e-23).","","","","","","Residues 81 to 156 (E-value = 4.3e-38) place AA00944 in the GreA_GreB family which is described as Prokaryotic transcription elongation factor, GreA/GreB, C-terminal domain (PF01272)","","","","","Borukhov S, Laptenko O, Lee J. Escherichia coli transcript cleavage factors GreA and GreB:functions and mechanisms of action. Methods Enzymol. 2001;342:64-76. PMID: 11586920 Nowicka-Sans B, Wolska KI. The role of GreA and GreB factors in bacterial transcriptionelongation Postepy Biochem. 2001;47(1):30-7. PMID: 11503438 Borukhov,S., Sagitov,V. and Goldfarb,A. Transcript cleavage factors from E. coli Cell 72 (3), 459-466 (1993) PubMed: 8431948 ","","Thu Dec 19 09:49:57 2002","1","","","" "AA00946","655318","655542","225","ATGAAAAGTGCGATCGAAAAAACATATAAATTTCTCACCGCACTTTTAGGATACTTAATATTACCGAGCCTTCTCATTATCCGGTTGTTCAGCGAATTCGTGCATCATATCGTGCATTTTTGCGCAATTTCGAGCAAAAGCACGACAGTACGGACAAATAGCCAAATGCATATAAACCTGACTGTGTTGCAGCAAGGAAAGCGGTTTTTCCTGACCATCGGAAAT","","","8564","MKSAIEKTYKFLTALLGYLILPSLLIIRLFSEFVHHIVHFCAISSKSTTVRTNSQMHINLTVLQQGKRFFLTIGN","655544","","hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-31]?signal-peptide
tmhmm\"[12-30]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Dec 19 09:50:46 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00946 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00947","655569","655381","189","ATGAAGTGTAAACAGGTTACCAAGTTAATTTCCGATGGTCAGGAAAAACCGCTTTCCTTGCTGCAACACAGTCAGGTTTATATGCATTTGGCTATTTGTCCGTACTGTCGTGCTTTTGCTCGAAATTGCGCAAAAATGCACGATATGATGCACGAATTCGCTGAACAACCGGATAATGAGAAGGCTCGG","8.20","2.75","7335","MKCKQVTKLISDGQEKPLSLLQHSQVYMHLAICPYCRAFARNCAKMHDMMHEFAEQPDNEKAR","","","hypothetical protein","Periplasm, Cytoplasm","No significant matches in gapped BLAST.AA00947 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus ducreyi gene.AA00947 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus influenzae Rd gene.","No hits reported.","No hits to the COGs database.","","","Fri Feb 27 09:35:29 2004","Sat Feb 28 16:50:06 2004","Sat Feb 28 16:50:06 2004","Sat Feb 28 16:50:06 2004","Fri Feb 27 09:35:29 2004","Fri Feb 27 09:35:29 2004","Fri Feb 27 09:35:29 2004","Fri Feb 27 09:35:29 2004","Fri Feb 27 09:35:29 2004","Fri Feb 27 09:35:29 2004","Fri Feb 27 09:35:29 2004","Fri Feb 27 09:35:29 2004","Fri Feb 27 09:35:29 2004","Fri Feb 27 09:35:29 2004","Fri Feb 27 09:35:29 2004","Fri Feb 27 09:35:29 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA00947 has no significant similarity (blastp p-value < 1e-03) to any other gene in this genome.AA00947 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Fri Feb 27 09:35:29 2004","Fri Feb 27 09:35:29 2004","No hits to the PDB database.","","","No significant hits to the Pfam 7.7 database.","Fri Feb 27 09:35:29 2004","","","","","","","1","Fri Feb 27 09:35:29 2004","","" "AA00948","656183","655587","597","ATGGACTCAACAATGCAATTTTCTTTTCAACACATTTCATCTCAAGAAATTGAGGATATTCGCCGGCAGATGCTGAAATTTGCCACTTTACAGTTAAGGGACGAAGATTTAGCGGAAGATGTCGTGCAGGAAACCTTAGTGAAAGCGTATCAACATGCGACCTCATTTAAAGGGGCTTCTGCGCTGAAAACCTGGTTTTTTGCCATTTTGAAGAATCAAATCATTGATTTGATTAATTATCGTAAACGTACGGTGAATGTGTCAGAAATTTATGATGACGAGGATGAGGCAGATGAGCCCAATGCCTTTTTTGATCAGAGCGGTCACTGGGATCGCAGCCATTTTTCCCCACAAACCTGGCACGAACCTGATAATCAGGTACATAAACGGGAATTTTGGGTTGTTTTTGAAGCTTGTTTGGAGCATTTGCCGGCACAACAAGCCCGCGTATTTATGATGCGCGAGTATTTTGAAATGAAAAGTGAACAGATTTGTGAGGAATGTGATTTATCCGTCTCCAATCTGCATGTTTTACTTTATCGCGCACGCTTACAGTTGCAAGCCTGCCTGTCTAATAATTGGTTTGATGAAAAGAAA","","","23707","MDSTMQFSFQHISSQEIEDIRRQMLKFATLQLRDEDLAEDVVQETLVKAYQHATSFKGASALKTWFFAILKNQIIDLINYRKRTVNVSEIYDDEDEADEPNAFFDQSGHWDRSHFSPQTWHEPDNQVHKREFWVVFEACLEHLPAQQARVFMMREYFEMKSEQICEECDLSVSNLHVLLYRARLQLQACLSNNWFDEKK","655589","","probable ECF-family RNA polymerase sigma factor","Cytoplasm","","
InterPro
IPR000838
Domain
RNA polymerase sigma factor 70, ECF
PS01063\"[38-69]?SIGMA70_ECF
InterPro
IPR007627
Domain
RNA polymerase sigma-70 region 2
PF04542\"[16-84]TSigma70_r2
InterPro
IPR013249
Domain
RNA polymerase sigma factor 70, region 4 type 2
PF08281\"[133-186]TSigma70_r4_2
InterPro
IPR014284
Domain
RNA polymerase sigma-70
TIGR02937\"[11-190]Tsigma70-ECF: RNA polymerase sigma factor, s
InterPro
IPR014289
Family
RNA polymerase sigma-24 related
TIGR02943\"[10-199]TSig70_famx1: RNA polymerase sigma-70 factor
noIPR
unintegrated
unintegrated
G3DSA:1.10.1740.10\"[14-83]Tno description


","BeTs to 11 clades of COG1595COG name: DNA-directed RNA polymerase specialized sigma subunits, sigma24 homologsFunctional Class: KThe phylogenetic pattern of COG1595 is --------vdrlbcefghsn-j--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-27) to 2/2 blocks of the IPB000838 family, which is described as \"Sigma factor, ECF subfamily\". Interpro entry for IP:IPR000838. IPB000838A 40-76 1.4e-13 IPB000838B 140-186 1.1e-12","Residues 17 to 83 match (2e-14) PD:PD350580 which is described as FACTOR RNA POLYMERASE SIGMA TRANSCRIPTION DNA-BINDING DNA-DIRECTED REGULATION PROTEOME COMPLETE ","","","","","","","","","","","","Fri Sep 5 16:25:18 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00948 is paralogously related to AA00902 (2e-07).","","","","","","Residues 16 to 84 (E-value = 5.8e-13) place AA00948 in the Sigma70_r2 family which is described as Sigma-70 region 2 (PF04542)","","","","","","","","1","","","" "AA00949","656638","656360","279","ATGAAAAAAACAGCATTATTCGCTACATTAGCAGGTGTATTCACTATGGCAATGGCGACTCAAGCTTCAGCTGAAATGAAAGCAATGGACCATAAAATGGAACAAGGTATGGAACATAAAATGGAGCATACCATGAAAGATGATAAAGCCATGATGGACCATAAAATGGATAAAACCATGAAGGATGGCAAAATGATGGATCATAAAAAAGACAAAATGATGAAAGACGGTAAGTCCATGGACCATAAAATGGACAAGGAAATGAAAGATCACAAAATG","","","10833","MKKTALFATLAGVFTMAMATQASAEMKAMDHKMEQGMEHKMEHTMKDDKAMMDHKMDKTMKDGKMMDHKKDKMMKDGKSMDHKMDKEMKDHKM","656362","","hypothetical protein","Periplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-19]?signal-peptide
tmhmm\"[5-23]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Dec 19 09:57:12 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00949 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00950","657062","657634","573","ATGTTTCACAGCACGTGGGGCACACTGACCTTCCCGTTTATTTTCCTGGCGACAGATTTAACCGTTCGCGTGTTCGGTGCCAAAGAAGCGCGCTGGATTATTTTCGTGGTAATGATTCCGGCGTTAATCATCAGTTATGCGGTGTCCACCCTGTTTTCAGACAGCCAATATAAGGGTTTGCAGGCATTAGCGACATTCAATCTATTTGTATTCCGTATTGCGGTGGCAAGTTTCTGCGCCTATGTATTCGGACAATTATTAGACGTATTGGTGTTTAATCGCTTACGCCAACTAAAAACCTGGTGGATTGCACCGACCAGTTCTATGGTGTTCGGTTCCATGGCGGATACTTATTTATTCTTCGCTATCGCGTTTTACGCCAGCAACGATCCGTTTATGGCGGAACATTGGATGGAAATCGGTTTCGTGGATTATTTGTTTAAATTGTTCATCGGATTATTATTGTTCGTGCCCGCTTACGGCGTCGTGTTAAATATGATTTTACGCAAAATTCAAACCTTAACGGCGACCATGCAACGGGACTTTGATGGCAAAATCGAAGAAGCGAACGGA","","","28150","MFHSTWGTLTFPFIFLATDLTVRVFGAKEARWIIFVVMIPALIISYAVSTLFSDSQYKGLQALATFNLFVFRIAVASFCAYVFGQLLDVLVFNRLRQLKTWWIAPTSSMVFGSMADTYLFFAIAFYASNDPFMAEHWMEIGFVDYLFKLFIGLLLFVPAYGVVLNMILRKIQTLTATMQRDFDGKIEEANG","657636","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR003744
Family
Protein of unknown function DUF165
PF02592\"[2-149]TDUF165
TIGR00697\"[1-169]TTIGR00697: conserved hypothetical integral
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide
tmhmm\"[33-53]?\"[72-92]?\"[107-127]?\"[146-168]?transmembrane_regions


","BeTs to 12 clades of COG1738COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG1738 is ao---z--vd--b-efgh-n-j-it-Number of proteins in this genome belonging to this COG is","Significant hit ( 7.5e-70) to 3/4 blocks of the IPB003744 family, which is described as \"DUF165\". Interpro entry for IP:IPR003744. IPB003744B 5-47 9.2e-25 IPB003744C 62-97 2.1e-21 IPB003744D 132-162 3e-21","","","","","","","","","","","","","Thu Dec 19 09:58:04 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00950 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 149 (E-value = 2.1e-65) place AA00950 in the DUF165 family which is described as Uncharacterized ACR, YhhQ family COG1738 (PF02592)","","","","","","","","1","","","" "AA00952","658955","657681","1275","ATGGTCAGAGTGCTATTTTTAATGTTGTTGCTGCTGGCAGGCTTAATTGCCGGCCCATATTTGTCGGGCAAACAGGGTTATGTGCGCATTGAAACCGCAAGCAACATCATCGAAATGTCCATTACCACATTGGTGATTTTCTTTGTGATTGCGCTGGCGTTGGTGTACAGCATTGAAGTGGCGATTAGTCGCTTTTTCCGTTTGAGCAATAACACTTACAGCTGGTTTTCCCGCCGTAAACGGGCAAAAGCGCAAAAACAAACGCTGGAAGGCTTAATGCGCATGGATGAAGGCGATTATTCCAAGGCGGAAAAACTTATCGGCAAAAATGCCAAACATTCCGATGAGCCGGTGTTGAATTTCATTAAAGCGGCGGAAGCGGCACAGCAACGGGGCGATGAATTCAGCGCGAATCGTTATTTAATCGAAGCCACGGAAATTGCTGGTTCCGACAGTTTGATTCTGGAAATTGCGCGCACCCGCATTTTGTTACAACAGCATAAATTACCGGCGGCACGCAGTTCTGTGGACAGTTTGTTGTTGATGGAAGGTCGCAATAAAGAAGTGTTAAAGCTGGCGGTGGATATTTATTCTAAATCCAAAGCCTATCAGGCGTTAGATAATATTTTGGAACAAGTGGAAAAATCCGGTTTGTACTCGGCAGAAGGCTTTGTTCAGTTACAGCATCAGGTAGAAGACGGTTTGCTGGATGAAAAAATGAACGAAGAAGGCGTGGACGGTTTGTTGGATTGGTGGGATGAACAACCACGTAAACGTCGTAACGATGCCTATGTCAAACTGGCGCTTATCAGCCGTTTAATTGATGCCAACGACCATGAATCTGCTTATGAACTCATGTTGGAATTGGTGAAGAAACTGGACGATGAAAACAGCCCGCTAAATCAGGAACTCTTCAAGCAAATTAGCCGTTTGCAGCCGGAAGATAATACGAAATTGATTAAATTTATCAGCAAGTGGTTAAAAGGCGCTAATCCGTCGGTGCAATGCGGCGCCAACCGCGCTTTAGGTTATCTGTATATGCGCAACAATGATTTTGCCAAAGCCAATGAGGTGTTTAAGGCGTTAATCGCGAATAAAGATAAATTGGAGCCGGCTGACATCACCATGGCGTCTTATGTGTTTGAACAGGTGGGCGACACGGCTGCTGCTGCACAATTACGCAAAGATGGTCTGCAATCCATGATGGCAATCCGAAAACCGCAGGCGGCAGAAAAAACACCTGAAAAAGAGACCGCACTTATTGCCCAAAAAGAC","","","47922","MVRVLFLMLLLLAGLIAGPYLSGKQGYVRIETASNIIEMSITTLVIFFVIALALVYSIEVAISRFFRLSNNTYSWFSRRKRAKAQKQTLEGLMRMDEGDYSKAEKLIGKNAKHSDEPVLNFIKAAEAAQQRGDEFSANRYLIEATEIAGSDSLILEIARTRILLQQHKLPAARSSVDSLLLMEGRNKEVLKLAVDIYSKSKAYQALDNILEQVEKSGLYSAEGFVQLQHQVEDGLLDEKMNEEGVDGLLDWWDEQPRKRRNDAYVKLALISRLIDANDHESAYELMLELVKKLDDENSPLNQELFKQISRLQPEDNTKLIKFISKWLKGANPSVQCGANRALGYLYMRNNDFAKANEVFKALIANKDKLEPADITMASYVFEQVGDTAAAAQLRKDGLQSMMAIRKPQAAEKTPEKETALIAQKD","657683","","hemY protein homolog","Cytoplasm, Inner membrane","","
InterPro
IPR005254
Family
Protoheme IX biosynthesis protein
TIGR00540\"[1-410]ThemY_coli: hemY protein
InterPro
IPR010817
Domain
HemY, N-terminal
PF07219\"[1-133]THemY_N
InterPro
IPR013212
Domain
Mad3/BUB1 homology region 1
SM00777\"[262-363]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-17]?signal-peptide
tmhmm\"[5-23]?\"[42-62]?transmembrane_regions


","BeTs to 3 clades of COG3071COG name: Uncharacterized enzyme of heme biosynthesisFunctional Class: HThe phylogenetic pattern of COG3071 is --------------efgh-n------Number of proteins in this genome belonging to this COG is","","Residues 16 to 67 match (7e-17) PD:PD579573 which is described as COMPLETE PROTEOME HEMY PORPHYRIN A DOMAIN 96% LATE BIOSYNTHETIC SP:P09128 ","","","","","Sat Jan 25 14:31:42 2003","","","","","","","Thu Dec 19 10:00:22 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00952 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 133 (E-value = 2.9e-58) place AA00952 in the HemY_N family which is described as HemY protein N-terminus (PF07219)","","","","","Hansson M, Gustafsson MC, Kannangara CG, Hederstedt L. Isolated Bacillus subtilis HemY has coproporphyrinogen III tocoproporphyrin III oxidase activity. Biochim Biophys Acta. 1997 Jun 20;1340(1):97-104. PMID: 9217019 Hansson M, Hederstedt L. Bacillus subtilis HemY is a peripheral membrane proteinessential for protoheme IX synthesis which can oxidizecoproporphyrinogen III and protoporphyrinogen IX. J Bacteriol. 1994 Oct;176(19):5962-70. PMID: 7928957 ","","Thu Dec 19 10:00:22 2002","1","","","" "AA00953","660353","658971","1383","ATGGCTAACAAGAAATCCAATCATCCGAAAAACAATGCGGAAATTGAACATAAAATTGATGTCAGCGATGATCTTGATTTAGCGACACAAGATACCACGCCTAATGAACACGTTGAAACAAATGCAGAGGATAAGACAGAAACGATGCAACAAAATGAAGAAAAAATCACGCCGTCAGAGCAAAAACCGATCGTGCATGAAACCGTTGTGGTGAAGAAAACCGGTTCCGCGTTAGGTTTGCTGGCACTTTTAATTGCGTTGGGTTTAGGCGGCGCGGGCTATTATTTCGGTCAGCTACAGGTTGACGAAATACAGCAAAAACTGACCGCACTTGAAAACCAATTGCAACAAAAAGGCACTTCCGCCGATGTTGCCGGCATGCCGGATTTTAGTGCAGAGAAAAATCAGCTGGCGAAATTAACGGAATTTTCCCAAGTGGCAAGTGATCAAATCAGCGCCTTGAATCAGAATTTGTCCGCCAAAGAACAAAGCCTGTCGGCATTGCAACAACAGGTGCAACGTTTGTCCAATCAAGCCAAAGCGGAGCAGCCGAATGACTGGTTACTGACCGAAGCGGATTTTCTGTTAAATAACGCTTTGCGCAAACTGGTGTTGGATAACGACGTGGATACCAGTGTGTCCTTGTTGAAAGTTGCCGATGAAACCCTTTCCAAAGTCGCCATGCCACAAGTGGCGCAGGTGCGTAGCGCCATTAACGCCGATTTAAAACAGTTGTTGTCCCTGAACAATGTGGACCAAAATGCCATCATGCAGAATTTATCCCAGCTGGCGAATAACGTAGATGAATTGACGGTGCTGGATGTGAATTTTGATGAAGATCCGAGTAGCGACAAGTTGACGGATTCCTTAGACGATTGGAAGGAAAACGCAGAGAAAAGTGCGGTCAGTTTTTTAAATCATTTTATTCGTGTCACGCCGAAGAAAGCGGACAGCAAAGCGTTGTTAGCGCCGAATCAGGATATTTATTTACGTGAAAACATTCGCTTACGTTTGCAAATTGCCATTCTCGCCGTACCGCGTCAGCAGGACGATTTGTATAAACAATCCCTGGAAACCGTGGCATCCTGGATCAGAAGCTATTTTGATACCAACACCGAAGTGGCGCAAATTTTCCTGAAAACCCTTGATGAACTGGCGGAACAGTCCATTTATGTGGATGTCCCGACTCAGTTAAATAGTTTGAATGCGTTGGATAAATTGTTGGATAAACAACCGCAGGAAGTCCAAAAAATCACCCTTTCCGTGGACAAAGATTTAACCGATGCCGTGGATAAACCGGTAACCGACAAGCCAGTAAATGAAAATGAAGCGGGTTCTGTGCTGGCAAATGAAGCAAACCAAGATACCAATCAAGGGCAACAA","","","51038","MANKKSNHPKNNAEIEHKIDVSDDLDLATQDTTPNEHVETNAEDKTETMQQNEEKITPSEQKPIVHETVVVKKTGSALGLLALLIALGLGGAGYYFGQLQVDEIQQKLTALENQLQQKGTSADVAGMPDFSAEKNQLAKLTEFSQVASDQISALNQNLSAKEQSLSALQQQVQRLSNQAKAEQPNDWLLTEADFLLNNALRKLVLDNDVDTSVSLLKVADETLSKVAMPQVAQVRSAINADLKQLLSLNNVDQNAIMQNLSQLANNVDELTVLDVNFDEDPSSDKLTDSLDDWKENAEKSAVSFLNHFIRVTPKKADSKALLAPNQDIYLRENIRLRLQIAILAVPRQQDDLYKQSLETVASWIRSYFDTNTEVAQIFLKTLDELAEQSIYVDVPTQLNSLNALDKLLDKQPQEVQKITLSVDKDLTDAVDKPVTDKPVNENEAGSVLANEANQDTNQGQQ","658973","","uroporphyrinogen III methylase","Outer membrane, Cytoplasm, Extracellular","","
InterPro
IPR007470
Domain
HemX
PF04375\"[47-429]THemX
noIPR
unintegrated
unintegrated
tmhmm\"[77-97]?transmembrane_regions


","BeTs to 5 clades of COG2959COG name: Uncharacterized enzyme of heme biosynthesisFunctional Class: SThe phylogenetic pattern of COG2959 is --------------efgh-n------Number of proteins in this genome belonging to this COG is","","Residues 94 to 270 match (2e-40) PD:PD038178 which is described as PROTEOME COMPLETE METHYLTRANSFERASE III METHYLASE TRANSFERASE UROPORPHYRINOGEN UROPORPHYRIN-III C-METHYLTRANSFERASE ORF ","","","","","Sat Jan 25 14:32:24 2003","","","","","","","Thu Dec 19 10:01:28 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00953 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 47 to 429 (E-value = 1.7e-130) place AA00953 in the HemX family which is described as HemX (PF04375)","","","","","Schroder I, Johansson P, Rutberg L, Hederstedt L. The hemX gene of the Bacillus subtilis hemAXCDBL operonencodes a membrane protein, negatively affecting thesteady-state cellular concentration of HemA (glutamyl-tRNAreductase). Microbiology. 1994 Apr;140 ( Pt 4):731-40. PMID: 8012594 Sasarman A, Echelard Y, Letowski J, Tardif D, Drolet M. Nucleotide sequence of the hemX gene, the third member ofthe Uro operon of Escherichia coli K12. Nucleic Acids Res. 1988 Dec 23;16(24):11835. PMID: 30625","","Sat Jan 25 14:32:24 2003","1","","","" "AA00954","661130","660387","744","ATGGCAGTTTTGGTCACCCGCCCCGATGAACGCGGTCAGCAGTTGGTGGATATGTTGGCGAAAGCCGGCGTTGTCGCCATTCATTTGCCGTTATTTCGTATTGAAAGCGGCGCGGAACTGAACGAATTGCCGAATAAATTTGCAAAGCTGAAAAACGGCGATTATGTTTTTGCTGTGTCAAAAAGTGCGGTGGATTTTGCCTTCAAAACCTTAACGGCAACAGGGTTTGTGTGGCGTCATGATTTGCATTATTTCACCGTCGGACAAGGCACGGCACAGTATTTTACCGCCACGACGGAAATGCCGGTGCATTATCCCACCGCGCAGGAAAACAGCGAAGGGTTGTTACAATTAAACGCCATGCAGGATCTGTCCGATAAAACCGTGTTAATTTTGCGTGGCAACGGCGGACGTGAATTATTTGCCGAACAGGCGCAACAGCGTGGGGCGAATGTGGAAATTGTCGAATGTTATCGACGTGAGCCCATTGTTTATAATAACGCCGAGCAAACCAGCATTTGTAAGCGTGCCGGCATTCAAACCATTGTGGTGACCAGTGCCGAAATTCTCACCCAATTAGTGGATTTTGTGCCGCAAAATGAACATAATTGGTTAAAAAGTTGTCAACTTATTACAGTAAGCGAACGAATCGCCCATTTGGCGGAAGCGTTAGGCTGGCAAAATGTGGTGATTTCTCCGCGTGCGGACAATCAAACTTTATTACAAACCTTATTACAATGTCGT","","","27672","MAVLVTRPDERGQQLVDMLAKAGVVAIHLPLFRIESGAELNELPNKFAKLKNGDYVFAVSKSAVDFAFKTLTATGFVWRHDLHYFTVGQGTAQYFTATTEMPVHYPTAQENSEGLLQLNAMQDLSDKTVLILRGNGGRELFAEQAQQRGANVEIVECYRREPIVYNNAEQTSICKRAGIQTIVVTSAEILTQLVDFVPQNEHNWLKSCQLITVSERIAHLAEALGWQNVVISPRADNQTLLQTLLQCR","660389","","uroporphyrinogen III synthase","Cytoplasm","","
InterPro
IPR003754
Domain
Tetrapyrrole biosynthesis, uroporphyrinogen III synthase
PF02602\"[10-243]THEM4
noIPR
unintegrated
unintegrated
PIRSF036524\"[1-248]TUroporphyrinogen-III synthase
PIRSF500147\"[1-248]TUroporphyrinogen-III synthase, classical type
PTHR20845\"[3-232]TFAMILY NOT NAMED


","BeTs to 11 clades of COG1587COG name: Uroporphyrinogen-III synthaseFunctional Class: HThe phylogenetic pattern of COG1587 is aomp--yq-dr-bcefghsnu-xi--Number of proteins in this genome belonging to this COG is","","Residues 67 to 229 match (3e-07) PD:PD275823 which is described as PROTEOME UROPORPHYRINOGEN-III COMPLETE SYNTHASE ","","","","Mon Feb 10 15:59:19 2003","Mon Feb 10 15:59:19 2003","","","","","","","Thu Dec 19 10:03:44 2002","","Fri Jul 20 14:10:38 2007","","Fri Jul 20 14:10:38 2007","yes","Fri Feb 20 15:41:32 MST 1998","AA00954 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Fri Jul 20 14:10:38 2007","","","","","Residues 10 to 243 (E-value = 6.4e-19) place AA00954 in the HEM4 family which is described as Uroporphyrinogen-III synthase HemD (PF02602)","Fri Jul 20 14:10:38 2007","","","","Johansson P, Hederstedt L. Organization of genes for tetrapyrrole biosynthesis ingram--positive bacteria. Microbiology. 1999 Mar;145 ( Pt 3):529-38. PMID: 10217486 Schroder I, Johansson P, Rutberg L, Hederstedt L. The hemX gene of the Bacillus subtilis hemAXCDBL operonencodes a membrane protein, negatively affecting thesteady-state cellular concentration of HemA (glutamyl-tRNA reductase). Microbiology. 1994 Apr;140 ( Pt 4):731-40. PMID: 8012594","","Sat Jan 25 14:06:22 2003","1","","","" "AA00957","662003","661146","858","GTGAAAGACCTCTTGCAGCAGTTATATCCTGATCTGAATGTGGAACTCGTCCCAATGGTCACCAAAGGCGATGTGATTTTGGATTCGCCGTTGGCGAAAATCGGCGGCAAAGGTTTGTTTGTCAAAGAACTGGAAAATGCGCTGCTGAATAAAGAGGCGGATATTGCCGTGCATTCCATGAAAGATGTGCCCATGCAATTTCCCGAAGGGCTTGGGTTGGCGGTGATTTGCAAACGTGAAGATCCGCGTGATGCATTCGTCTCAAATTCTTACCGCACTTTAGCGGAATTACCGCAAGGTGCCGTGGTCGGCACTTCCAGTTTACGCCGTCAATGTCAGTTAAAAACATTACGTCCCGATTTGGAAATTCGTTCTTTGCGCGGCAATGTGGGTACGCGTTTGAGTAAATTAGATAACGGTGATTATGATGCCATTATTTTGGCTTCCGCCGGTTTGATTCGGTTAGGTTTAGCAGAGCGTATCGCTTCTTTTATTGATGTGGAGCAATCCTTGCCTGCTGCCGGACAAGGCGCGGTGGGCATCGAATGTCGGACAGACGATGTTGCGGTTCAACAATTACTGGCGCCACTGGCGGATGCGGAAACTACCTCTTGCGTGCTGGCGGAACGCGCCATGAACAATCGCTTACAAGGCGGCTGCCAAGTGCCTATCGGCGGTTATGCGGTGTTGCGCGATGGCGAATTGTATTTACGCGCCTTAGTGGGCAGCGTGGACGGTTCGACGATTATTCGCGCGGAAGGCAAAAGCGCGGTGGAAAACGCCGACGTTTTAGGCGTGCAAATTGCCGAACAGCTATTGGCGCAGGGGGCGGATAAAATTTTGCAGGATATTTACGCG","","","35365","VKDLLQQLYPDLNVELVPMVTKGDVILDSPLAKIGGKGLFVKELENALLNKEADIAVHSMKDVPMQFPEGLGLAVICKREDPRDAFVSNSYRTLAELPQGAVVGTSSLRRQCQLKTLRPDLEIRSLRGNVGTRLSKLDNGDYDAIILASAGLIRLGLAERIASFIDVEQSLPAAGQGAVGIECRTDDVAVQQLLAPLADAETTSCVLAERAMNNRLQGGCQVPIGGYAVLRDGELYLRALVGSVDGSTIIRAEGKSAVENADVLGVQIAEQLLAQGADKILQDIYA","661148","","porphobilinogen deaminase (hydroxymethylbilane synthase)","Cytoplasm","","
InterPro
IPR000860
Family
Tetrapyrrole biosynthesis, hydroxymethylbilane synthase
PD002745\"[71-184]THEM3_PASMU_Q9CK24;
PR00151\"[23-43]T\"[54-73]T\"[102-119]T\"[121-138]T\"[208-225]TPORPHBDMNASE
G3DSA:3.30.160.40\"[199-285]Tno description
PTHR11557\"[56-286]TPORPHOBILINOGEN DEAMINASE
PF01379\"[1-195]TPorphobil_deam
PF03900\"[203-276]TPorphobil_deamC
TIGR00212\"[1-276]ThemC: porphobilinogen deaminase
PS00533\"[209-225]TPORPHOBILINOGEN_DEAM
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[78-177]Tno description


","BeTs to 21 clades of COG0181COG name: Porphobilinogen deaminaseFunctional Class: HThe phylogenetic pattern of COG0181 is aomp-zyq-dr-bcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 3.2e-89) to 4/5 blocks of the IPB000860 family, which is described as \"Porphobilinogen deaminase\". Interpro entry for IP:IPR000860. IPB000860B 31-64 1.3e-29 IPB000860C 105-155 4.2e-39 IPB000860D 172-182 3.3e-05 IPB000860E 208-225 1.4e-11","Residues 141 to 283 match (3e-08) PD:PD252146 which is described as PROTEOME DEAMINASE COMPLETE PORPHOBILINOGEN ","","","","","Tue Feb 18 15:40:00 2003","","","","","","","Thu Dec 19 10:09:19 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00957 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 203 to 276 (E-value = 7.4e-29) place AA00957 in the Porphobil_deamC family which is described as Porphobilinogen deaminase, C-terminal domain (PF03900)","","","","","Kafala B, Sasarman A.Isolation of the Staphylococcus aureus hemCDBL gene cluster coding for early steps inheme biosynthesis.Gene. 1997 Oct 15;199(1-2):231-9.PMID: 9358061Majumdar D, Wyche JH.Molecular cloning and nucleotide sequence of the porphobilinogen deaminase gene, hemC,from Chlorobium vibrioforme.Curr Microbiol. 1997 Apr;34(4):258-63.PMID: 9058548 McNicholas PM, Javor G, Darie S, Gunsalus RP.Expression of the heme biosynthetic pathway genes hemCD, hemH, hemM, and hemA ofEscherichia coli.FEMS Microbiol Lett. 1997 Jan 1;146(1):143-8.PMID: 8997718","","Tue Feb 18 15:40:00 2003","1","","","" "AA00958","662258","664723","2466","GTGGATTATTTAGATAAACTTCGCATTCAGCGCGCTCTATCCGATACGCCTGAATCCTTTCAACAAGTATTCCGCCTGATTCCGCTGTTGCTCCATTTTAACCACCCCGATTTGCCCGGCTACATTGCTGATGCGCCGTGCGGTATTGTGCATTTCGTCGCTAATAAATTTCAGCAGAATTATCTCAAACACAATTATGCCCCTGACAGCGTAAAAAACATTTTAAAATCCCACCGCACTTTTCACGAACGGGCGATTCTCGGCGTGTATGTGATGGGCAGTATCGCCTCCATTGCGCAAACGCCTTCTTCTGATTTGGACATTTGGCTTTGTCATCGGGAAGATTTAAGTGCGCAATCCCGCCAATTATTACAACAAAAAATCGAATTGATTCAACAATGGGCAAAACGGTTTCATGTGGAAATCAATTTCTATCTAATGGATCAAAAACGCTTCCGTTGCTTTCATGACACCGAACCCGTCGGCATTGAAAACTGTGGTTCAGCGCAATATATGTTGTTGCTTGATGAATTTTATCGCTCCGCCATTCGCCTCGCGGGTAAACCCTTGTTATGGCTACATTTAGCCGTTGAAAACGAAGCGGATTACGAAGCGGAAATCGAGCGTCTGGCACAAAATGGCGAGCTGGATTTAAATGATTGGGTGGATTTCGGCGGATTGGGCACCTTGTCGGCAAACGAATATTTCGGTGCCAGCCTCTGGCAGCTATATAAAGGGATTGATTATCCGTATAAATCCCTGCTCAAAATTTTATTGTTGGAGGCTTATTCGCATGATTATCCGAACACCTTTTTAATTTCCCGCGAATTTAAACAGGCATTGTTAAACAATCAGCGCAAAGTTGAACATAAATTTGACGCTTATCTTGCCATGTTGCAACGGGTAACCGCCTATTTAACCCAGCAAAAAGAATTCAAACGGTTGGATTTCGTGCGCTGTTGTTTTTACATTAAAGTCCACGAAAACGAAGTGGAGCCGGAACAAAGCAACTGGCGTCTGGATGAATTACTCAAACTCACCCAGCAATGGGGTTGGAAGTGCGGTCAGTTGGAGCACTTAAATCACCGTGCCCAGTGGAAAATCAAGCAAACCACCAAAGTACACAACGATTTGATTAAATTCCTGATGTTAAGTTATCGCAATTTGGTGAACTTTGCCCGCAAACATCAGGTCAATGCCAGCATTATCCCACAAGATATGAGCATATTAACCCGCAAACTTTATACCGCATTTGAAGAATTGCCGGGCAAAGTGACCTTGCTCAATCCGCAACTCGCGGTGGATTTATCGGAAAAATACCTGACCTTCATTGAAGTGAAAAACAATCGTCGCTTTAAAGACGGCTGGTATCTCATCAACCAAACGCCGACGGTGCAAGGTTTTAGCCGACCACGTTATACGGAATATAATGAAAGCCTGAATAAATTGGTGGCATGGGCGTATTTCAACCGATTGCTAACCGCCAACACCGAATTGTTCATTACCAGCGAAAACGTGGATCTGAAAACCTTACGCCAATATGTCACCGATTTACGTTTAGCCTTCCCGCTGGAAAGCCGATTCGCCAATAATTCCGAGCTGAGCCATCCTTGCGAAATTCGCAATCTGGCGGTCATCGTGAATTTAACGCAGGATCCGACCCGTCATTTAACGGAAGTCAAATCCAGCATTCAATCCAGTGATTTATTCAGTTTCGGACCGAATGAAGAAAGTTTGGTAGGCAGCATTGATCTCACTTATCGCAACGTGTGGAATGAAATCCGCACGTTACACTTTGAAGGGGCAAATGCGATTTTGTTGGCGTTAAAAGTGCTTTCCAACAAAATCTATCGTGGCGCGCCGCTGCCGCAACAGGTTCAGGTGTTCTGTTACAGCCGTTATTATCACCACGCTTTGCGTCGCATCGTGACCACCCTGATTAACAAGTGTATCAGCATCCAAGTGGGTACCGCCGAACCACCGAAAAATAACCTGTTACGCGTTGCCGGCAAAAACTGGCAATTCTTCTTTGAAGAACGCGGTATCAGTCTGCAGGAAATTCATCATGCGGACATCGGCAAAACGCACCAATTAGACACCGCACTTAATGCCAAAGTCAAAGCGACAGAGCCGAAAATCGTCAAACTGCAGAAATACCCGCACGAGATTGACATGTTCGCCAGCGAGGGCTTCCTGCAATTTTTCTTTGAAGATAACGCGAACGGCAGCTTTAACGTGTATATTCTCGACGAACTGAATCGAATTGAAATTTATCGCAACTGCGACGGCACGAAAGAGAAAAAAATTCATGAGATAAATCGAATTTATCAGTTATCCGGCTTGGATGAAAATGACAATCCGTATAAAATCGTGCAACGTGATTTTAACTACCCGCAATTTTATCAATTCGTCACGACCAAAGAAGGCACGACCATCGTTCCGTTCCATAGTCGCTTGGCTTTATCC","","","97401","VDYLDKLRIQRALSDTPESFQQVFRLIPLLLHFNHPDLPGYIADAPCGIVHFVANKFQQNYLKHNYAPDSVKNILKSHRTFHERAILGVYVMGSIASIAQTPSSDLDIWLCHREDLSAQSRQLLQQKIELIQQWAKRFHVEINFYLMDQKRFRCFHDTEPVGIENCGSAQYMLLLDEFYRSAIRLAGKPLLWLHLAVENEADYEAEIERLAQNGELDLNDWVDFGGLGTLSANEYFGASLWQLYKGIDYPYKSLLKILLLEAYSHDYPNTFLISREFKQALLNNQRKVEHKFDAYLAMLQRVTAYLTQQKEFKRLDFVRCCFYIKVHENEVEPEQSNWRLDELLKLTQQWGWKCGQLEHLNHRAQWKIKQTTKVHNDLIKFLMLSYRNLVNFARKHQVNASIIPQDMSILTRKLYTAFEELPGKVTLLNPQLAVDLSEKYLTFIEVKNNRRFKDGWYLINQTPTVQGFSRPRYTEYNESLNKLVAWAYFNRLLTANTELFITSENVDLKTLRQYVTDLRLAFPLESRFANNSELSHPCEIRNLAVIVNLTQDPTRHLTEVKSSIQSSDLFSFGPNEESLVGSIDLTYRNVWNEIRTLHFEGANAILLALKVLSNKIYRGAPLPQQVQVFCYSRYYHHALRRIVTTLINKCISIQVGTAEPPKNNLLRVAGKNWQFFFEERGISLQEIHHADIGKTHQLDTALNAKVKATEPKIVKLQKYPHEIDMFASEGFLQFFFEDNANGSFNVYILDELNRIEIYRNCDGTKEKKIHEINRIYQLSGLDENDNPYKIVQRDFNYPQFYQFVTTKEGTTIVPFHSRLALS","664725","","adenylate cyclase","Cytoplasm","","
InterPro
IPR000274
Family
Adenylate cyclase, class-I
PIRSF001444\"[1-822]TAdenylate cyclase
PF01295\"[1-822]TAdenylate_cycl
PS01092\"[234-245]TADENYLATE_CYCLASE_1_1
PS01093\"[587-601]TADENYLATE_CYCLASE_1_2


","BeTs to 4 clades of COG3072COG name: Adenylate cyclaseFunctional Class: FThe phylogenetic pattern of COG3072 is --------------efgh--------Number of proteins in this genome belonging to this COG is","","Residues 1 to 818 match (0) PD:PD007853 which is described as CYCLASE ADENYLATE CAMP ATP PYROPHOSPHATE-LYASE LYASE ADENYLYL SYNTHESIS PROTEOME COMPLETE ","","","","","","","","","","","","Tue Jan 21 13:58:10 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00958 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Kimura Y, Mishima Y, Nakano H, Takegawa K. An adenylyl cyclase, CyaA, of Myxococcus xanthus functions insignal transduction during osmotic stress. J Bacteriol. 2002 Jul;184(13):3578-85. PMID: 12057952 Lawrence AJ, Coote JG, Kazi YF, Lawrence PD, MacDonald-FyallJ, Orr BM, Parton R, Riehle M, Sinclair J, Young J, Price NC. A direct pyrophosphatase-coupled assay provides new insightsinto the activation of the secreted adenylate cyclase fromBordetella pertussis by calmodulin. J Biol Chem. 2002 Jun 21;277(25):22289-96. PMID: 11934879Dorocicz,I.R., Williams,P.M. and Redfield,R.J.The Haemophilus influenzae adenylate cyclase gene: cloning, sequence, and essential role in competenceJ. Bacteriol. 175 (22), 7142-7149 (1993)PubMed: 8226661Mock,M., Crasnier,M., Duflot,E., Dumay,V. and Danchin,A.Structural and functional relationships between Pasteurella multocida and enterobacterial adenylate cyclasesJ. Bacteriol. 173 (19), 6265-6269 (1991)PubMed: 1917858","","Tue Jan 21 13:59:27 2003","1","","","" "AA00959","664736","665362","627","ATGACTGATAAATTAAAAGTATTAATTATTGATGACCATCCGTTAATGCGTCGCGGAATCAAACAACTCGTTGAGCTGGAAGAGGGTTTTGAAGTTGTCGGCGGTGCAGGGAACGGTACTGAAGGCATTAATCTGGCATTACAAACCTCGCCCGATTTGATTATTTTAGATCTGAACATGAAAGGGCTTTCCGGGTTGGATACACTTAAAGCATTGAGAGCAGAAGGCGTGGATGCGCGCATCGTGATTTTAACCGTTTCCGATGCCAAAAATGACATTTTCACGTTGATTGATGCCGGCGCGGACGGTTATTTATTGAAAGACACCGAGCCCGATACTTTGCTTTCTCAGCTAAAACGAATCGCCCGGGGGGAAGTGATTTTAAGCGATTCCATCAAAAATTTATTGCTGGAACGTCAATCTGCTCAAGAACCCATTTATTCCCTCACCGATCGCGAAATGGGCGTACTACGTTTAATCGCCACCGGTCTTTCCAACAAGCAAATTGCAGGACAATTATTCATTTCGGAAGAAACGGTAAAAGTGCATATTCGCAATTTGTTACGCAAATTGAACGTCCATTCCCGTGTTGCGGCAACCGTATTATATTTTGAACATAAAAACGGT","","","22949","MTDKLKVLIIDDHPLMRRGIKQLVELEEGFEVVGGAGNGTEGINLALQTSPDLIILDLNMKGLSGLDTLKALRAEGVDARIVILTVSDAKNDIFTLIDAGADGYLLKDTEPDTLLSQLKRIARGEVILSDSIKNLLLERQSAQEPIYSLTDREMGVLRLIATGLSNKQIAGQLFISEETVKVHIRNLLRKLNVHSRVAATVLYFEHKNG","665364","","nitrate/nitrite response regulator","Cytoplasm","","
InterPro
IPR000792
Domain
Bacterial regulatory protein, LuxR
PD000307\"[148-206]TQ9CK25_PASMU_Q9CK25;
PR00038\"[149-163]T\"[163-179]T\"[179-191]THTHLUXR
PF00196\"[146-203]TGerE
SM00421\"[146-203]THTH_LUXR
PS50043\"[142-207]THTH_LUXR_2
PS00622\"[163-190]THTH_LUXR_1
InterPro
IPR001789
Domain
Response regulator receiver
PD000039\"[6-123]TNARP_HAEIN_P44845;
PF00072\"[5-119]TResponse_reg
SM00448\"[5-118]TREC
PS50110\"[6-122]TRESPONSE_REGULATORY
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[138-207]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2300\"[4-126]Tno description
PTHR23283\"[6-123]TSENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF47\"[6-123]TSENSORY TRANSDUCTION HISTIDINE KINASE (DHKB)


","BeTs to 10 clades of COG2197COG name: Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domainFunctional Class: T,KThe phylogenetic pattern of COG2197 is ---------drlbcefghsn-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.9e-27) to 1/1 blocks of the IPB000792 family, which is described as \"Bacterial regulatory protein, LuxR family\". Interpro entry for IP:IPR000792. IPB000792 149-195 1.8e-27Significant hit ( 1.5e-13) to 2/6 blocks of the IPB000673 family, which is described as \"CheB methylesterase\". Interpro entry for IP:IPR000673. IPB000673A 7-17 0.013 IPB000673B 24-77 3e-09Significant hit ( 5.1e-11) to 3/3 blocks of the IPB001789 family, which is described as \"Response regulator receiver domain\". Interpro entry for IP:IPR001789. IPB001789A 7-13 0.46 IPB001789B 52-65 0.0002 IPB001789C 100-109 0.12Significant hit ( 6e-11) to 2/4 blocks of the IPB001867 family, which is described as \"Transcriptional regulatory protein, C terminal\". Interpro entry for IP:IPR001867. IPB001867A 52-65 0.0066 IPB001867B 80-124 2.8e-06","Residues 148 to 206 match (1e-22) PD:PD000307 which is described as TRANSCRIPTION DNA-BINDING REGULATION REGULATOR COMPLETE PROTEOME TRANSDUCTION SENSORY PHOSPHORYLATION RESPONSE ","","","","","","","","","","","","Thu Dec 19 10:15:30 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00959 is paralogously related to AA01837 (4e-12), AA00997 (2e-11), AA02902 (5e-09), AA01983 (9e-08) and AA02511 (0.001).","","","","","","Residues 146 to 203 (E-value = 9.9e-29) place AA00959 in the GerE family which is described as Bacterial regulatory proteins, luxR family (PF00196)","","","","","Darwin AJ, Stewart V. Expression of the narX, narL, narP, and narQ genes ofEscherichia coli K-12: regulation of the regulators. J Bacteriol. 1995 Jul;177(13):3865-9. PMID: 7601854 Browning DF, Beatty CM, Wolfe AJ, Cole JA, Busby SJ. Independent regulation of the divergent Escherichia coli nrfAand acsP1 promoters by a nucleoprotein assembly at a sharedregulatory region. Mol Microbiol. 2002 Feb;43(3):687-701. PMID: 11929525","","Thu Dec 19 10:15:30 2002","1","","","" "AA00960","665405","667288","1884","TTGTCGGCTATTTTTTATGGAAAACCCTTGACCGACCTCAGAAAATATTTTGAAAATCCACCGCACTTTGCATTGCAGGGCTTTAGCCTAACGGGTACACTACTGGCATTTGATTTTGAGGTAAATATGAAGCAATCGGGCAATCGGATAACACATTGGGCAGCCAAAACAATTTTCGTTTTTTGTTTTCTTTGGCATCCGTCAGTATGGGCGGAACATCTCGTTGATTTGCAGGTCAGCGGCATCAAAAACGAAAAATTAAATGAAAACGTGCAGATTTATACCAATGCCATAGAAAAAGAAGACATGGACGGTTCCGATCGTTATCAGGAATCCGTTCGTCAGGCGGTGGATAAAGGCTTGCGTGCTTTCGGTTATTATGAAAGTGCGGTCAGTTTTGAACTCAAAAATCGCGCCAAGCCCAATAAACCCTTATTAATCGCTCACGTCACCGTCGGCAATCCGGTGAAAATCGCCGCCACTGACGTGGTTATCAGCGGACAGGCGGATGAAGATCCCGAATTTGCCAAGCTGGAAAGAAAAGTGCCGAAACCAGGCACAGTGCTGAATCACGAAACCTACGACGATTACAAAAGTTCGTTGCAACAACTCGCCTTAACACGCGGCTATTTCGATGCGGGGTTTGAAACCTCACGATTGGAAGTCATGCCTTCCACTTATCAGGCCTGGTGGAAACTTCACTTTAATTCAAAAGCACGTTACCACTACGGCAAAATCAATTTCCAACACGCGCAAATTCGCGAAGATTATTTACGCAATATGCTGAATATTCAGCCCGGTGAAGACTACTTACTCAGCGATCTTTCCACTCTGACCAATAATTATTCTTCCACCAACTGGTTTAACTCGGTGCTGTTACAGCCGCATTTGGACGATGAAAATAAATTGGTCGATCTGGACGTATTGCTTTATCCGCGCAAGAAAAACATCATGAGCGTGGGTGTCGGTTATTCCACCGATGTAGGTCCGCGCCTGCAATGGAGCTGGACCAAGCCCTGGATTAACGCTCGTGGGCATAGCGTAAGAAGCAATATGTATATTTCTTCGCCAAAACAGACATTGGAGCTCACGTACAAACACCCTTTATTGAAAAATCCGCTGAATTATTACTACGAATATTCCGCCGGTTTCGAAAACGAAAATACAAACGACACCAAAACCACCGCCTCTACCCTTGCCGCCCTGCGCTACTGGAATCATCCGACGGGCTGGCAATACTCGCTGGGGTTACGGGTGCGCCATGATTCTTTTACCCAAGCGGAAATCAGCGATAAAACCTTACTCATCTACCCGACAACCTCCCTCACCCGCAGCCGGTTACGAGGCGGCGCATTTCCCGATTGGGGCGATTCACAACGTATCACCTTTGATTTCGGGCGCAAGTTTTGGCTATCCGACGTAGATTTCTGGAAAATTCAGGCATCCACCGCATGGATTCGAACCTACGCGCAAAATCACCGCTTCCTCACGCGATTAGAAGCCGGCGTGTTAAATACCGCCAGCATTCACCGCATTCCGCCTTCTTTACGTTTCTTCGCCGGTGGTGATCGTAGCGTACGTGGCTATGGCTATAAAAAAATCTCACCGAAAGATCGTAACGGCAAACTCATCGGCGGTTCGCGCTTACTTACCGGTTCCATCGAATATCAATATCAGGTTTATCCGGATTGGTGGCTTGCCACCTTCGTGGACAGCGGGCTGGCGGCAAATTCCTTTGATATGAGCGAATTGCGTTACGGCACCGGCGTAGGTGTGCGTTGGGCATCGCCAGTAGGCGCGATTAAATTTGATATTGCCACACCGGTGCGCGATAAAGACAACAGCAAAAATATTCAATTTTATATCGGGTTGGGTTCCGAGCTA","","","71932","LSAIFYGKPLTDLRKYFENPPHFALQGFSLTGTLLAFDFEVNMKQSGNRITHWAAKTIFVFCFLWHPSVWAEHLVDLQVSGIKNEKLNENVQIYTNAIEKEDMDGSDRYQESVRQAVDKGLRAFGYYESAVSFELKNRAKPNKPLLIAHVTVGNPVKIAATDVVISGQADEDPEFAKLERKVPKPGTVLNHETYDDYKSSLQQLALTRGYFDAGFETSRLEVMPSTYQAWWKLHFNSKARYHYGKINFQHAQIREDYLRNMLNIQPGEDYLLSDLSTLTNNYSSTNWFNSVLLQPHLDDENKLVDLDVLLYPRKKNIMSVGVGYSTDVGPRLQWSWTKPWINARGHSVRSNMYISSPKQTLELTYKHPLLKNPLNYYYEYSAGFENENTNDTKTTASTLAALRYWNHPTGWQYSLGLRVRHDSFTQAEISDKTLLIYPTTSLTRSRLRGGAFPDWGDSQRITFDFGRKFWLSDVDFWKIQASTAWIRTYAQNHRFLTRLEAGVLNTASIHRIPPSLRFFAGGDRSVRGYGYKKISPKDRNGKLIGGSRLLTGSIEYQYQVYPDWWLATFVDSGLAANSFDMSELRYGTGVGVRWASPVGAIKFDIATPVRDKDNSKNIQFYIGLGSEL","667290","","possible outer membrane protein","Outer membrane, Cytoplasm","","
InterPro
IPR000184
Family
Bacterial surface antigen (D15)
PTHR12815\"[328-628]TSORTING AND ASSEMBLY MACHINERY (SAM50) PROTEIN
PF01103\"[340-628]TBac_surface_Ag
InterPro
IPR000209
Domain
Peptidase S8 and S53, subtilisin, kexin, sedolisin
PS00136\"[567-577]?SUBTILASE_ASP
InterPro
IPR010827
Repeat
Surface antigen variable number
PF07244\"[241-313]TSurf_Ag_VNR
noIPR
unintegrated
unintegrated
signalp\"[1-71]?signal-peptide


","No hits to the COGs database.","","Residues 418 to 452 match (8e-08) PD:PD042296 which is described as COMPLETE PROTEOME HI0698 PM1809 SIGNAL PRECURSOR ","","","","","","","","","","","","Thu Dec 19 10:16:13 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00960 is paralogously related to AA00608 (4e-07).","","","","","","Residues 330 to 628 (E-value = 3.5e-73) place AA00960 in the Bac_surface_Ag family which is described as Surface antigen (PF01103)","","","","","","","","1","","","" "AA00961","667319","671194","3876","ATGACAGAACACACGGAACAAGCACCGCAAACCCCTGCACCAAAAACGAAAAAAAGCAAATGGCGTCGCCGTCTCTGCGCCGTAAGTGCGGTCGTTTTTTTTGCTGTTTTTGCCCTGTTGGGTATGCTTGCCACAGAAAACGGGCAGCATAAACTGATTCAGTGGGCGGATGATTTCACAGATGCCCTTTCCATTAAACGGATAGAAGGCAATTTAAGTGAAGGTTTGGTGCTAACCGATGTGCGTTTCCAAACGCAAGGCATCGGCGTCCAGGTAAACCAAGCCCGCCTGCAAATGCAATTAAGCTGCTTATGGAAATTAAAGGTTTGCGTTAACGACATCAGCCTGCAACAACCCGGTATTCAAATTGATACCGCCCTATTGCCGCCGTCGGGGCAAAAGCCCAAAGAAAGCGCACCGATGAAGCGTATTTCCCTACCGATCTCCGTGCAGGTCAATCAGCTTGCCGTGAAAGATTTGAGCTTGCTGATTGACAAAAACCAAATGCACTTGGCGACATTTCACACCGCCGCCGGTTTAAATAATGAAACGGGGATCACCTTATCGCCAACTCAAATCGACGATTTTCGTTTTGTTCAACAGCTGACTGAAAAAACACCGTGGGAAACCGAGGTTAAATCGGCAGAGACCACCCCCACGCCGATTAACTGGGAACAGATGGAACAGGATCTTAGCCGTCCGTTACTTGCCGATTTACCAAAAATAGACTTGCCCTTTGATATACACGTTCAAGGCATTAGCGGGAAAAACTGGCAATATCAACTGATTAACGATAAACAGGAAACCCTGCAAGACATTCTGGTTTCTTCTGTCGAACTGCAAGCCGACGCAACGGATTATACGGTGCAGTTACAAAAATTTGACGTAAAAAGCTCTCTCGGTGGTTTAACGGCAAGCGGGCAAATGCAGCTCAGCGAAGATTTCCCATTGCAATTTAAATTATTAGGCGATTTCAACACCTTCAAACACAATAATAACGTGTTGCTTCCTGCAAGCAAAATCGATCTAACGCTTTCAGGATCGCTGAAAAAACAGACCGCACTTTCCCTGCAAACCCAGGGTGCCTTAGAAACGACACTGGAAGCGCAGGCACAACCTGCTGCGCCGAAATTGCCATTAACGCTACATTTCACCGCCGATAAGGCACAATACCCGTTTAACAATAAAGATCCGCTGCAAATTAACGATCTGGTGTTGGATATTGAAGGAGATTTACTGACGGCACAAGTGAACTTAAAAAGTGCGGTCAGTGGCATGGGAATTCCAACCAACACTCTTAAATTACAGGCAGTTAGCCATTTATCCAATGTGGAAATTCAGCGTCTCTTGCTTAACGCGTTAAGTGGTTCGGCAGAATTACAAGGCAATTTGAACTGGCGTGACGGCATTGCCTGGGACAGCCATTTGCAGTTGGCAAAAATCAATGTGGGCAAATACTTATCCGTCTTCCCGGCCCAGTTATCAGGCAAATTAAGCTCACAAGGCAAAGCCAATCAAAGCGGTTGGCAGGTTGCCGTGCCGGAATTGGATATTCAAGGCACACTGTCCCAACGCCCGCTGAACCTGAAAGGCAATTTCACTGCGGGCAATCAGCAGTTGCTCAATATCCCGCAGTTATTGCTCACTTATGGCGACAATAAAATTGAGGTGCAGGGCCATCTCGGTGATACATCGGATTTTAACCTGGACATTAATGCGCCGAATTTACAGGGCTTGTGGGCGGATTTATCGGCGGGTTTGAAAGGCAACGTAAAATTAAACGGCAGCATCGCCCGACCAAGCATTCATGCGGATTTAACCGCAAGCCGCTTTGCATTCCAACACATGCGCCTGAACCAAGCCCTGATTAAAGGCGAAATCAACAGCGCGGAACAAATTAGCGGTCAGCTTGAAGTGAATTTAAACGGCTTTAATTACGATGAAATCAAAGTAAATCAGCTCAAATTGACGGCAAACGGCGACGAACAAAAACACAGTTTGCAGCTACAATCGGACGGCACCCCTGTGGCGACCAACTTAAATTTCACCGGAAATTTCAACCGCACTTTACAGCAATGGAAAGGCACGTTGAGCCAAATGATGATTAAATCGGAATTCGGTAACCTGCAAACCAACAAAAATGTTGCCATAACTTACAACAATAAAACCACCGAAGCCACTATTTCCGCGCACTGCTGGATACACAGCCACGCGGATTTATGTTTCCCGCAAAGCTTTAACGTGGGCGCAAACGGTGAAGTGCCGTTTGATATTAAGCGCTTTAATCTGGCTTTCATCAATAAACTGCTGGAACAGGAACTACTCAGCGGTCAGCTAAACAGTCAGGGCAAAGTGGCTTGGTTTACCGATAAACCGTTACAGGCTGAGTTACAACTTAACGGCAATCATGTGTCGCTAACGCAAAAGGTGGATCGTAAAACCTTCCGCCTGGTAATTCCGCAAATTGGTTTAAATGCCAATTTAGCCAACAATAACCTGGCGCTGAAATCCGATATTCATCTTCAGGATCAAGGGCGAATCGGCTCCGATCTGAAACTATCGGATATTGCCAATGCCCGTAAGTTGGGCGGTACATTCAGCATTCAAAACCTGAATTTGAATCTGGCGAATCAACTGCTTAACCGTGATGAACAGGTTAATGGCGCGCTGAGAGCCAATCTCACCCTCGGCGGCAGTTTAACCGCGCCGACCCTCAACGGCGATGTTAATCTAAACAAACTTACTGCCAAAATACGCGCATTGCCTTTTGGCATTACCGAAAGTGAGCTGACGCTGCGTTTTACCGGCACCAACTCCACCCTGCAAGGGTATGTACAAACTGCCGACAGCCGTTTACACCTGAGCGGTGAGGCAAATTGGAAAAATGTGAATGACTGGCGCACCCGTTTACACGCCGAGGCGGATAAATTTAAAGTGGATATTCCGTCTATGGCAAGACTGAGAATCAGCCCGAATATCGACATCAGTGCGACACCGAAGCTGTTGGAACTTTCCGGCAATATTGATATTCCCTGGGCGCGCATTGCCATTGAAAACCTGCCGGACAGTGCAGTGGCGGTCAGCTCCGATGAAGTGATTTTAAATGGCAATAAGAAGAGTACTCTGCCGAAAACATTGCCGAGCGAAACCCAAAGCGGCATGGCAATTCGTTCTGATTTAAGAATCAATATCGGCGATGATGTCAGTTTAAATGCCTATGGCTTGAAAACCCATCTCCACGGGTTGCTCTCGGTGAAACAGGAAAAGGGCAATTTGGGGCTTTACGGCGAGGTCAACCTGAAGAACGGTCGTTACGCCTCTTTCGGGCAGGATTTAATTATTCGTAAAGGGCTCATCAGTTTTGTCGGTCAACCGTCGCAACCGATGCTGAATATTGAAGCAATTCGTAATCCGGAAGCCATGGAAGACGCAGGCGTTACTGCCGGTGTGAAAGTGAATGGTATAGCGACCGCACCCAGTGTAACCATTTTCTCCGAACCGGGAATGCCGCAGGATCAGGCACTATCTTATATTTTAACCGGCCGCTCCTTAGAAAACAGCGGCGATACCGCTTCCAGCGGTTCTGTGGGCGCCGCTTTGCTCGGCATGGGGCTCGCTAAAAGCGGTAATGTGGTCGGGGGAATCGGAAAAGCCTTTGGTATCAAAGATCTGAACCTGAGTACCGCCGGGGTGGGCGACAGATCTAAAGTAGTGGTCAGCGGCACCATTACACCGCGCTTACAGGTAAAATACGGCGTTGGGTTATTTGACGGTTTAGCCGAAGTGACTCTGCGTTACCGATTATTGCCACAACTGTATGTTCAATCCGTTTCGGGTGTTAATCAAGCCTTTGATCTACTCTATCAATTTGAATTT","","","140869","MTEHTEQAPQTPAPKTKKSKWRRRLCAVSAVVFFAVFALLGMLATENGQHKLIQWADDFTDALSIKRIEGNLSEGLVLTDVRFQTQGIGVQVNQARLQMQLSCLWKLKVCVNDISLQQPGIQIDTALLPPSGQKPKESAPMKRISLPISVQVNQLAVKDLSLLIDKNQMHLATFHTAAGLNNETGITLSPTQIDDFRFVQQLTEKTPWETEVKSAETTPTPINWEQMEQDLSRPLLADLPKIDLPFDIHVQGISGKNWQYQLINDKQETLQDILVSSVELQADATDYTVQLQKFDVKSSLGGLTASGQMQLSEDFPLQFKLLGDFNTFKHNNNVLLPASKIDLTLSGSLKKQTALSLQTQGALETTLEAQAQPAAPKLPLTLHFTADKAQYPFNNKDPLQINDLVLDIEGDLLTAQVNLKSAVSGMGIPTNTLKLQAVSHLSNVEIQRLLLNALSGSAELQGNLNWRDGIAWDSHLQLAKINVGKYLSVFPAQLSGKLSSQGKANQSGWQVAVPELDIQGTLSQRPLNLKGNFTAGNQQLLNIPQLLLTYGDNKIEVQGHLGDTSDFNLDINAPNLQGLWADLSAGLKGNVKLNGSIARPSIHADLTASRFAFQHMRLNQALIKGEINSAEQISGQLEVNLNGFNYDEIKVNQLKLTANGDEQKHSLQLQSDGTPVATNLNFTGNFNRTLQQWKGTLSQMMIKSEFGNLQTNKNVAITYNNKTTEATISAHCWIHSHADLCFPQSFNVGANGEVPFDIKRFNLAFINKLLEQELLSGQLNSQGKVAWFTDKPLQAELQLNGNHVSLTQKVDRKTFRLVIPQIGLNANLANNNLALKSDIHLQDQGRIGSDLKLSDIANARKLGGTFSIQNLNLNLANQLLNRDEQVNGALRANLTLGGSLTAPTLNGDVNLNKLTAKIRALPFGITESELTLRFTGTNSTLQGYVQTADSRLHLSGEANWKNVNDWRTRLHAEADKFKVDIPSMARLRISPNIDISATPKLLELSGNIDIPWARIAIENLPDSAVAVSSDEVILNGNKKSTLPKTLPSETQSGMAIRSDLRINIGDDVSLNAYGLKTHLHGLLSVKQEKGNLGLYGEVNLKNGRYASFGQDLIIRKGLISFVGQPSQPMLNIEAIRNPEAMEDAGVTAGVKVNGIATAPSVTIFSEPGMPQDQALSYILTGRSLENSGDTASSGSVGAALLGMGLAKSGNVVGGIGKAFGIKDLNLSTAGVGDRSKVVVSGTITPRLQVKYGVGLFDGLAEVTLRYRLLPQLYVQSVSGVNQAFDLLYQFEF","671196","","conserved hypothetical protein","Outer membrane, Periplasm","","
InterPro
IPR000887
Family
KDPG and KHG aldolase
PS00159\"[924-933]?ALDOLASE_KDPG_KHG_1
InterPro
IPR007452
Family
Protein of unknown function DUF490
PF04357\"[937-1292]TDUF490
noIPR
unintegrated
unintegrated
signalp\"[1-45]?signal-peptide
tmhmm\"[25-45]?transmembrane_regions


","BeTs to 6 clades of COG2911COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG2911 is --------------efghsn-j----Number of proteins in this genome belonging to this COG is","","Residues 516 to 914 match (5e-09) PD:PD402471 which is described as FROM CHROMOSOME PRP8 ORF1061 SPLICING FACTOR S4 RIBOSOMAL U5 SNRNP-SPECIFIC ","","","","","","","","","","","","Thu Dec 19 10:17:00 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00961 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 937 to 1292 (E-value = 1.5e-153) place AA00961 in the DUF490 family which is described as Family of unknown function (DUF490) (PF04357)","","","","","","","","1","","","" "AA00962","671200","672744","1545","ATGAATAACGAAAATTTACTAAAGAAAGCTAACGAACTCTACGCCCGACGTGGCGAGGTGCGTGAAATCGCCGCGATCGACTTAGGTTCCAACAGCTTTCACATGATCATCGCCCGCATCGTCAACGGCACGTTACAGGTATTATCGCGGTTGAAGCAGAAAGTCCAGCTTGCGGAAGGCTTGGATGAAAACCAAGTGTTAAGCCAGGCAGCAATTGAACGCGGGGTAAATTGTCTGGCGTTATTTGCCGAACGCTTGCAGGGATTTTCTGCCGAAAACGTGAGCGTCGTCGGCACTTACACCTTACGACGCGCGGTAAATAACGACGTGTTTTTACGCCAAGCCGCCAACGTATTTCCTTATCAAATTAATATTATTAGCGGCAAAACCGAAGCCAAAACCATCTACGCGGGCGTTTGCCACACCCAACCGGAAACCGGACGTAAATTCGTTATTGATATTGGCGGCGGTTCAACAGAGATGATTATCGGCGATAATTTCACGCCGTTAATTTACGAAAGCCGTCATGTGGGCTGCGTCAGTTTTGCGAAAAAATTCTTTCCGAACGGCGAAATCAGCGCGGAAAATTTCCGGCAAGCAAAACAAAGTGCATTGAATAAAATTGAAGATCTCGCCTGGGAATACCGTAACCTGGGTTGGCAATCGGTGCTGGGTTCATCAGGAACAATCAAAACCGTGCATCAAGTAATTTACGAAAATATCGATCCCAACGGCACCATCACGGCGCCCCGCTTAGACCAATTGATTGAACAAACTTTACAACATTCCCATTTTAACCAACTGAAATTCAACGGTTTAAACCCTGACCGTGCCGATGTTTTTGTGCCGGGATTAGCGATTTTAAGCGCGGTTTTTGAAAATTTTCACATTGAAAAAATGCGCTATTCCGACGGCGCATTGCGCGAAGGCGTAATGTACAGTCTGGAGCAAAATTTTCAGGTCAACAATATTCGGGAGCGCACCGCACTAGGTTTGGCGGAGCAATTTAATATCGATCAGGCACAGGCAGAGCGGGTGTATCAAAGCGCGGTTTTATTGTTTAATCAATATAATGCCTGGCAAAACACCGAGCTAATTCCGGAAATGCAGGATGTGCTTTTTTGGGCAGCGCGTTTGCATGAAGTGGGCATTGTGATTAACCATAAAGCTATGCAGAAACATTCCGCATACATTTTATACAACACGGAACTGCCCGGTTTTGACAACGAACAGCATCGTCTGCTTTCTACGCTGGTGCGCTATCATATCGGCAACTTTAAACTGCCGGATATGTTCAAGTTTTCCCGCTATAACGAAAAAGACGTTTTAGCCCTCATCCGTATTTTACGTTTGGCGGCGATTATTAACCGCTCCCGTCAAGCCACCGAGAAAACCGAAAAAATCATCTTGAAAAACGACCGCACTTTTAGCGACTGGCAGTTGGAATTTGAAACAGATTATTTAACCCATAACCCGTTACTGAAAAATGATTTGGCATTGGAAAATCGTTTTTTACAAACCTTGGAATTAAGCCTGTCGGCACGT","","","58705","MNNENLLKKANELYARRGEVREIAAIDLGSNSFHMIIARIVNGTLQVLSRLKQKVQLAEGLDENQVLSQAAIERGVNCLALFAERLQGFSAENVSVVGTYTLRRAVNNDVFLRQAANVFPYQINIISGKTEAKTIYAGVCHTQPETGRKFVIDIGGGSTEMIIGDNFTPLIYESRHVGCVSFAKKFFPNGEISAENFRQAKQSALNKIEDLAWEYRNLGWQSVLGSSGTIKTVHQVIYENIDPNGTITAPRLDQLIEQTLQHSHFNQLKFNGLNPDRADVFVPGLAILSAVFENFHIEKMRYSDGALREGVMYSLEQNFQVNNIRERTALGLAEQFNIDQAQAERVYQSAVLLFNQYNAWQNTELIPEMQDVLFWAARLHEVGIVINHKAMQKHSAYILYNTELPGFDNEQHRLLSTLVRYHIGNFKLPDMFKFSRYNEKDVLALIRILRLAAIINRSRQATEKTEKIILKNDRTFSDWQLEFETDYLTHNPLLKNDLALENRFLQTLELSLSAR","672746","","exopolyphosphatase (metaphosphatase)","Cytoplasm","","
InterPro
IPR003695
Family
Ppx/GppA phosphatase
PF02541\"[36-319]TPpx-GppA
noIPR
unintegrated
unintegrated
G3DSA:3.30.420.150\"[144-315]Tno description
G3DSA:3.30.420.40\"[10-143]Tno description


","BeTs to 15 clades of COG0248COG name: ExopolyphosphataseFunctional Class: F,PThe phylogenetic pattern of COG0248 is ------yqvdr-bcefghsnujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 5e-67) to 5/5 blocks of the IPB003695 family, which is described as \"Ppx/GppA phosphatase\". Interpro entry for IP:IPR003695. IPB003695A 24-35 9.3e-09 IPB003695B 78-131 6.6e-24 IPB003695C 147-187 1e-20 IPB003695D 216-230 0.00011 IPB003695E 277-287 0.0031","Residues 118 to 166 match (4e-13) PD:PD566479 which is described as PROTEOME METAPHOSPHATASE COMPLETE MEMBRANE MAGNESIUM EXOPOLYPASE EXOPOLYPHOSPHATASE HYDROLASE ","","","","","","","","","","","","Thu Dec 19 10:18:42 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00962 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 36 to 319 (E-value = 1.9e-124) place AA00962 in the Ppx-GppA family which is described as Ppx/GppA phosphatase family (PF02541)","","","","","Akiyama,M., Crooke,E. and Kornberg,A. An exopolyphosphatase of Escherichia coli. The enzyme and itsppx gene in a polyphosphate operon. J. Biol. Chem. 268(1):633-639, 1993. PubMed: 8380170. Reizer,J., Reizer,A., Saier,M.H. Jr., Bork,P. and Sander,C.Exopolyphosphate phosphatase and guanosine pentaphosphatephosphatase belong to the sugar kinase/actin/hsp 70superfamily. Trends Biochem. Sci. 18(7):247-248, 1993. PubMed: 8212131.","","Thu Dec 19 10:18:09 2002","1","","","" "AA00964","674428","672815","1614","ATGACAGATGTAAACGACGTAGTTAAAGAACTTGAGGCAATTGGTATTCATAATGTAAAAGAAGTGGTTTATAACCCAAGTTATGAACAACTTTTTGAAGAAGAAACCAAACCGGGCTTGGAAGGTTTCGAAAAAGGCACCGTCACCACCACCGGCGCGGTCGCTGTGGATACCGGCATTTTTACCGGACGTTCTCCTAAGGATAAATATATTGTTTTAGATGACACCACCAAAGACACCGTATGGTGGACTTCCGACGCGGCGAAAAACGACAATAAACCGATGACCCAAGAAACCTGGGCAAGCTTAAAAGACATCGTCACCAAAGAGCTTTCCGGCAAACGCTTATTCGTGATTGACGGTTTCTGCGGCGCCAGCGAAAAAGACCGTATTGCGGTGCGTATCGTGACTGAAGTGGCATGGCAGGCGCATTTCGTGAAAAATATGTTTATTCGTCCGACCGACGCCGAATTAAAAGATTTCAAACCAAGTTTCGTGGTGATGAACGGTTCTAAATGCACTAACCCGAACTGGAAAGAACAAGGCTTGAATTCCGAAAACTTCGTAGCGTTTAACTTAACCGAACGCATTCAATTAATCGGCGGCACCTGGTACGGCGGCGAAATGAAGAAAGGTATGTTCTCTATGATGAACTACTTCCTGCCGCTAAAAGGCGTGGGCGCAATGCACTGTTCCGCTAACGTAGGCAAAGACGGTGATGTTGCTGTGTTCTTCGGCTTGTCCGGCACCGGTAAAACCACCCTTTCTACCGATCCGAAACGTGAGCTAATTGGTGATGATGAACACGGTTGGGATGATGTGGGTATCTTCAACTTTGAAGGTGGTTGTTACGCGAAAACCATTCACCTTTCCGAAGAAAACGAACCGGATATTTATCGCGCAATCCGTCGTGATGCCTTATTAGAAAACGTAGTGGTGCGTGCAGACGGTTCAGTGGATTTCGATGACGGTTCCAAAACCGAAAACACCCGCGTTTCCTATCCGATTTATCACATCGATAACATCGTTAAACCGGTTTCCCGCGCAGGTCACGCTACTAAAGTGATTTTCTTAACCGCTGACGCTTTCGGCGTGTTGCCGCCGGTATCTAAATTGACACCGGAACAAACCAAATACTACTTCTTATCCGGTTTCACTGCGAAATTAGCCGGTACCGAACGTGGTATTACCGAACCGACCCCAACATTCTCCGCTTGTTTCGGTGCGGCATTCTTAACCTTACACCCAACCCAATATGCGGAAGTGTTGGTAAAACGTATGCAAGCGGCAGGTGCGGAAGCCTATTTGGTGAACACCGGTTGGAACGGCACGGGCAAACGTATCTCCATTAAAGATACGCGCGGTATTATCGACGCCATCTTAGACGGTTCTATCGAAAAAGCGCAAATGAGCGAATTACCAATCTTCAATTTGGCAATTCCTAAGGCATTACCCGGCGTTGATCCGGCTATTTTAGATCCGCGTGATACTTATGCCGATAAAGCGCAATGGGAAGCCAAAGCGAAAGATCTTGCTGGTCGTTTTGTGAAGAATTTCGAAAAATACGCTACCAATGCAGAAGGTAAAGCCTTAATTTCTGCCGGGCCCAAAGCG","","","59487","MTDVNDVVKELEAIGIHNVKEVVYNPSYEQLFEEETKPGLEGFEKGTVTTTGAVAVDTGIFTGRSPKDKYIVLDDTTKDTVWWTSDAAKNDNKPMTQETWASLKDIVTKELSGKRLFVIDGFCGASEKDRIAVRIVTEVAWQAHFVKNMFIRPTDAELKDFKPSFVVMNGSKCTNPNWKEQGLNSENFVAFNLTERIQLIGGTWYGGEMKKGMFSMMNYFLPLKGVGAMHCSANVGKDGDVAVFFGLSGTGKTTLSTDPKRELIGDDEHGWDDVGIFNFEGGCYAKTIHLSEENEPDIYRAIRRDALLENVVVRADGSVDFDDGSKTENTRVSYPIYHIDNIVKPVSRAGHATKVIFLTADAFGVLPPVSKLTPEQTKYYFLSGFTAKLAGTERGITEPTPTFSACFGAAFLTLHPTQYAEVLVKRMQAAGAEAYLVNTGWNGTGKRISIKDTRGIIDAILDGSIEKAQMSELPIFNLAIPKALPGVDPAILDPRDTYADKAQWEAKAKDLAGRFVKNFEKYATNAEGKALISAGPKA","672817","","phosphoenolpyruvate carboxykinase/carboxylase","Cytoplasm","","
InterPro
IPR001272
Family
Phosphoenolpyruvate carboxykinase (ATP)
PIRSF006294\"[8-538]TPhosphoenolpyruvate carboxykinase [ATP]
PF01293\"[18-491]TPEPCK_ATP
TIGR00224\"[2-538]TpckA: phosphoenolpyruvate carboxykinase (AT
PS00532\"[263-278]TPEPCK_ATP
InterPro
IPR008210
Domain
Phosphoenolpyruvate carboxykinase, N-terminal
PD004738\"[10-225]TPPCK_HAEIN_P43923;
noIPR
unintegrated
unintegrated
G3DSA:3.40.449.10\"[25-225]Tno description
G3DSA:3.90.228.20\"[226-538]Tno description


","BeTs to 9 clades of COG1866COG name: Phosphoenolpyruvate carboxykinase (ATP)Functional Class: CThe phylogenetic pattern of COG1866 is -----zy--d--b-efgh--uj----Number of proteins in this genome belonging to this COG is","Significant hit (4.3e-232) to 8/8 blocks of the IPB001272 family, which is described as \"Phosphoenolpyruvate carboxykinase (ATP)\". Interpro entry for IP:IPR001272. IPB001272A 48-82 1.7e-27 IPB001272B 124-168 3.4e-29 IPB001272C 199-222 1.4e-23 IPB001272D 239-280 3.9e-39 IPB001272E 319-342 9.6e-19 IPB001272F 370-423 6.9e-49 IPB001272G 428-444 5.3e-10 IPB001272H 457-500 2.6e-27","Residues 10 to 225 match (4e-103) PD:PD004738 which is described as PHOSPHOENOLPYRUVATE CARBOXYKINASE LYASE DECARBOXYLASE GLUCONEOGENESIS CARBOXYLASE PEPCK PEP COMPLETE ATP ","","","","","","","","","","","","Thu Dec 19 10:20:00 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00964 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Medina,V., Pontarollo,R., Glaeske,D., Tabel,H. and Goldie,H.Sequence of the pckA gene of Escherichia coli K-12: relevanceto genetic and allosteric regulation and homology of E. coliphosphoenolpyruvate carboxykinase with the enzymes fromTrypanosoma brucei and Saccharomyces cerevisiae. J. Bacteriol. 172(12): 7151-7156, 1990. PubMed: 1701430. Laivenieks,M., Vieille,C. and Zeikus,J.G. Cloning, sequencing, and overexpression of theAnaerobiospirillum succiniciproducens phosphoenolpyruvatecarboxykinase (pckA) gene. Appl. Environ. Microbiol. 63(6):2273-2280, 1997. PubMed: 9172347. Velayudhan J, Kelly DJ. Analysis of gluconeogenic and anaplerotic enzymes inCampylobacter jejuni: an essential role forphosphoenolpyruvate carboxykinase. Microbiology. 2002 Mar;148(Pt 3):685-94. PMID: 11882702 Prost JF, Cozzone AJ. Detection of an extended-10 element in the promoter region ofthe pckA gene encoding phosphoenolpyruvate carboxykinase in Escherichia coli. Biochimie. 1999 Mar;81(3):197-200. PMID: 10385000 ","","Thu Dec 19 10:20:00 2002","1","","","" "AA00965","674660","674538","123","TTGTGTTACTTAGAACGGGCGCTAAATCATAAGTTCCCATTGAAAGTGCGGTGGTTTTTTGCGTTACTTTTAATAGAGCGAAAATGCTTCTCAAATCGGCGGGTAAATTTACCTAAAATGCAA","","","5075","LCYLERALNHKFPLKVRWFFALLLIERKCFSNRRVNLPKMQ","674538","","hypothetical protein","Cytoplasm","No sequence similarities found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-31]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 08:39:50 2004","Wed Feb 25 08:39:50 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences to this sequence.AA00965 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 08:39:50 2004","","","","","","","","","","","","","1","","","" "AA00967","674686","675327","642","ATGAAATTACGCAAAACCTTTTTACTTGTCGCTTTACTTTACTTTCCCGCCGCGTGGGCTGCAGACCTTGCCGGTTTAAACATCAAATACAGTTCCAATTATTTAATGCCGGCTTATGTACATTTCAAATCGGACGGCTTTGAATATACAATTAAAGCTAACATTAACGTGCCTTTATACAACATTCAGTTCACCTCCAAAGGTACGCAAAGTAGTAATTTTTTCAATATGTTAAGTTATCAAGACACGCGTAATAACAAACCTTATGCAAAAGCCAAAATCGCCAATCATAAAATCGAATACGGCAAAGTAAAAAACGGCTTAAAAACCGAAGAGTTAACCCTGCCGACCTATGATTTATTCACTGTGGCATTCCAGCTCAGTTATTATGATAAACTGCCGAACAGCTTCCAAATCACCAACGGCAAAAAACTCTACCCAATGGAAAATGTAGTGCTGAACACCAGCAAGAAACAGGTTAAATATAACAAACAAGAGGTGACCGAAATCACCTACAAATTCAAAACCGGCGATAAAGACATTATGGTGAAAAAACACGAGGGAGAAAAATTCCCTCGCTTTATTTCCTACAATCGCGACGGCGATAAGTACAAACTCACCTTCAGCGAGTTTGTGAAAGAC","","","24936","MKLRKTFLLVALLYFPAAWAADLAGLNIKYSSNYLMPAYVHFKSDGFEYTIKANINVPLYNIQFTSKGTQSSNFFNMLSYQDTRNNKPYAKAKIANHKIEYGKVKNGLKTEELTLPTYDLFTVAFQLSYYDKLPNSFQITNGKKLYPMENVVLNTSKKQVKYNKQEVTEITYKFKTGDKDIMVKKHEGEKFPRFISYNRDGDKYKLTFSEFVKD","675329","","conserved hypothetical protein","Periplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-20]?signal-peptide
tmhmm\"[7-27]?transmembrane_regions


","No hits to the COGs database.","","Residues 28 to 206 match (1e-62) PD:PD312868 which is described as PROTEOME COMPLETE NMA1754 PM1623 ","","","","","","","","","","","","Thu Dec 19 10:20:54 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00967 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00969","675469","676266","798","ATGAACGCTATTCAGCCTGAAGATAAGAGCTTTTGGCTTTTCACTCAGAGATCAAAAATACATTTAATTGACGGCAAGCTTCCTTTCGGCAATGCCACCGAACTGGGTTTCGTCGGGCTTCATGCTATGCGCATCGGCGAATGGCTGGAGCAACCGTTATATTTGGTGGAAACCCAACCGAACGACAACCGCACCTATTTTTCTTTACGCGATCAACTGCCGCTGCCGCAAGCGCAATTTAATCTGTTGAGCTGCGGCGTGGAGTTAAATCATTTCTATCAGACCCATCAATTCTGCGGAAAGTGCGGTGGAAAAACCGAGCAAATGCAGGAGGAATGGGCGGTAAAATGCCGTGCCTGCGGTTTTCATACCTATCCCGTCATTTGCCCTTCCATTATCGTTGCAGTACGACACGATTCACAAATCCTGCTGGCAAATCATATGCGCCACAAAGGCGGCATTTACACCACGTTGGCGGGTTTTGTGGAAGTAGGCGAAACCTTTGAGGATGCGGTACATCGCGAAATTTGGGAGGAAACCCAAATCAAAGTAAAAAATTTGCGTTATTTCGACAGCCAGCCTTGGGCGTTTCCTAATTCGCAAATGGTGGGTTTTTTAGCCGATTATGAAGGAGGCGAGATTACTATTCAGCGTGAAGAACTTTATGACGCACAATGGTTTGATTGCGACCAACCGTTGCCCGAACTGCCACCGCACGGCACCATCGCACGCAAATTAATTGAAACCACACTTGAATTGTGTAAACAGCATAAAATAAACCATAATAAGGAACGGGCA","","","34098","MNAIQPEDKSFWLFTQRSKIHLIDGKLPFGNATELGFVGLHAMRIGEWLEQPLYLVETQPNDNRTYFSLRDQLPLPQAQFNLLSCGVELNHFYQTHQFCGKCGGKTEQMQEEWAVKCRACGFHTYPVICPSIIVAVRHDSQILLANHMRHKGGIYTTLAGFVEVGETFEDAVHREIWEETQIKVKNLRYFDSQPWAFPNSQMVGFLADYEGGEITIQREELYDAQWFDCDQPLPELPPHGTIARKLIETTLELCKQHKINHNKERA","676268","","conserved hypothetical protein (possible NADH pyrophosphatase)","Cytoplasm","","
InterPro
IPR000086
Domain
NUDIX hydrolase
PR00502\"[155-169]T\"[169-184]TNUDIXFAMILY
G3DSA:3.90.79.10\"[116-241]Tno description
PF00293\"[128-253]TNUDIX
InterPro
IPR015375
Domain
NADH pyrophosphatase-like, N-terminal
PF09296\"[9-92]TNUDIX-like
InterPro
IPR015376
Domain
Zinc ribbon, NADH pyrophosphatase
PF09297\"[94-125]Tzf-NADH-PPase
noIPR
unintegrated
unintegrated
PTHR22769\"[132-231]TMUTT/NUDIX HYDROLASE


","No hits to the COGs database.","Significant hit ( 2e-06) to 1/1 blocks of the IPB000086 family, which is described as \"NUDIX hydrolase\". Interpro entry for IP:IPR000086. IPB000086 155-181 2e-06","Residues 77 to 191 match (2e-07) PD:PD376364 which is described as NADH MANGANESE MAGNESIUM 3.6.1.- PYROPHOSPHATASE NAD HYDROLASE ","","","","","Tue Feb 18 10:01:32 2003","","","","","","","Tue Feb 18 10:01:32 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00969 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 128 to 253 (E-value = 3.8e-23) place AA00969 in the NUDIX family which is described as NUDIX domain (PF00293)","","","","","","","Tue Feb 18 10:01:32 2003","1","","","" "AA00970","676266","677327","1062","ATGACTACATTGAAAAATGATCGTTATTTGAGAGCGTTGCTACGCCAACCGGTGGATATGACGCCGATTTGGATGATGCGTCAGGCGGGACGCTATTTGCCGGAATATAAGGCGACCCGTGCACAGGCAGGCGATTTTATGTCCCTGTGCCGCAATGCGGAATTGGCGTGTGAGGTGACGTTACAGCCATTGCGTCGCTATGATTTGGACGCGGCGATTTTATTTTCCGATATTTTAACGATTCCTGACGCCATGGGGCTGGGATTAAGCTTTGGTGCAGGGGAAGGACCGAAATTTGAACGGGTTATCGACAGCAAAAGTGCGGTGGAAAATTTACCCGTTCCTGACCCGGAACAGGAGCTGCAATATGTAATGAACGCTGTGCGCACTATTCGCCGTGAACTGAAAGGTGAGGTACCACTCATCGGTTTCTCCGGCAGCCCGTGGACCTTGGCGACCTATATGGTGGAGGGCAGTTCTTCCAAAGCCTTCACAAAAATAAAAAAAATGTTGTATGCCGAACCGCACTTATTGCACGCGTTGTTGGATAAACTCGCCGACAGCGTTATTTTGTATTTGAATGCACAAATTAAAGCGGGTGCGCAAGCGGTGATGGTGTTTGACACCTGGGGCGGCGTGTTGGCGCACCGCGATTATCCGGCATTTTCGCTGCACTATATGCACAAAATCGTGGACGGCTTAATTCGCGAACATGAAGAGCGTCGCGTGCCGGTCACGTTATTTACCAAAGGCGGCGGACTCTGGCTGGAAGCCATTGCCGACACCGGCTGTGATGCGGTGGGGCTGGACTGGACGGTGGACATCGCCGAAGCCCGTCGTCGTGTGGGGCATAAAATAGCGCTGCAAGGCAATTTGGATCCGAGCGTGTTGTACGCACCGGCAAACCGAATTGAAGATGAAGTGCGGTCAATTTTGGCGGCGTTTGGTGCGGGCAACGGCCATGTGTTTAACCTCGGTCACGGCATTCATCAGGATGTGCCGGTAGAAAGTCCGAAACGGTTGGTAGACGCAGTACATCAGCTGTCTCAGCCTTATCATCTC","","","39327","MTTLKNDRYLRALLRQPVDMTPIWMMRQAGRYLPEYKATRAQAGDFMSLCRNAELACEVTLQPLRRYDLDAAILFSDILTIPDAMGLGLSFGAGEGPKFERVIDSKSAVENLPVPDPEQELQYVMNAVRTIRRELKGEVPLIGFSGSPWTLATYMVEGSSSKAFTKIKKMLYAEPHLLHALLDKLADSVILYLNAQIKAGAQAVMVFDTWGGVLAHRDYPAFSLHYMHKIVDGLIREHEERRVPVTLFTKGGGLWLEAIADTGCDAVGLDWTVDIAEARRRVGHKIALQGNLDPSVLYAPANRIEDEVRSILAAFGAGNGHVFNLGHGIHQDVPVESPKRLVDAVHQLSQPYHL","677329","","uroporphyrinogen decarboxylase (uroporphyrinogen III decarboxylase)","Cytoplasm","","
InterPro
IPR000257
Family
Uroporphyrinogen decarboxylase (URO-D)
PD003225\"[10-346]TDCUP_PASMU_P57964;
PF01208\"[4-348]TURO-D
PS00906\"[22-31]TUROD_1
PS00907\"[142-158]TUROD_2
InterPro
IPR006361
Family
Uroporphyrinogen decarboxylase HemE
PIRSF001349\"[6-351]TUroporphyrinogen-III decarboxylase/methylcobamide:CoM methyltransferase
PTHR21091:SF2\"[19-350]TUROPORPHYRINOGEN DECARBOXYLASE
TIGR01464\"[8-347]ThemE: uroporphyrinogen decarboxylase
InterPro
IPR014670
Family
Uroporphyrinogen-III decarboxylase
PIRSF500079\"[6-351]TUroporphyrinogen-III decarboxylase
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.210\"[4-353]Tno description
PTHR21091\"[19-350]TMETHYLTETRAHYDROFOLATE:HOMOCYSTEINE METHYLTRANSFERASE RELATED


","BeTs to 16 clades of COG0407COG name: Uroporphyrinogen-III decarboxylaseFunctional Class: HThe phylogenetic pattern of COG0407 is ---p--yq-dr-bcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit (1.6e-146) to 7/7 blocks of the IPB000257 family, which is described as \"Uroporphyrinogen decarboxylase (URO-D)\". Interpro entry for IP:IPR000257. IPB000257A 22-36 9.2e-14 IPB000257B 53-97 3e-34 IPB000257C 140-162 8.6e-18 IPB000257D 168-222 4.5e-35 IPB000257E 243-257 2e-06 IPB000257F 263-294 8.6e-25 IPB000257G 321-331 6.2e-07","","","","","","Sat Jan 25 14:33:43 2003","","","","","","Thu Dec 19 10:39:46 2002","Thu Dec 19 10:36:13 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00970 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 348 (E-value = 3.3e-193) place AA00970 in the URO-D family which is described as Uroporphyrinogen decarboxylase (URO-D) (PF01208)","","","","","Phillips JD, Parker TL, Schubert HL, WhitbyFG, Hill CP, Kushner JP.Functional consequences of naturally occurring mutations in humanuroporphyrinogen decarboxylase.Blood. 2001 Dec 1;98(12):3179-85.PMID: 1171935","","Thu Dec 19 10:36:13 2002","1","","","" "AA00971","677348","677935","588","ATGCGAAATCCTATTCATAAACGTTTAGAAAATTTAGCCACCTGGCAACACCTGACTTTCATAGCGTGCCTGTGCGAGCGGATGTACCCTAATTATCAGCTGTTTTGCCAAATTACCGAACAACCGCAACATGCCAAGGTGTATCACAATATTCTGAATTTGGCGTGGGAATATTTAACCGTTAAAGACGCGAAGATTAATTTTGAAAATCAGCTGGAAAAACTGGAAAACATCATTCCCGATGTGAATGACTATGATTTTTACGGTGTGGTGCCTGCGTTGGATGCCTGTGAAGCATTATCGGAAATGTTACATACCATCATTGCCGGCGATTCCCTAACCCAAGCGGTGAAATTAAGCCAATTATCTTTACAAACCGTGGCGGATTTGCTGGCGGAACAAAATGAACGCGAATTATCCGAGACAGAATTAAAGGAAAGCGAGGAAATTCAGCAAGAATTGGACGTGCAATGGCAAATTTATCGCGTACTGAAAGACGCGAAAAAGCACAATGTTGAGCTGATTCTGGGTTTAAAAAATGAGTTACGCGAGGTAGGAATTTCGAATATTTGTGTAAAAATTGACCAA","","","22897","MRNPIHKRLENLATWQHLTFIACLCERMYPNYQLFCQITEQPQHAKVYHNILNLAWEYLTVKDAKINFENQLEKLENIIPDVNDYDFYGVVPALDACEALSEMLHTIIAGDSLTQAVKLSQLSLQTVADLLAEQNERELSETELKESEEIQQELDVQWQIYRVLKDAKKHNVELILGLKNELREVGISNICVKIDQ","677937","","conserved hypothetical protein","Cytoplasm, Inner membrane","","
InterPro
IPR007338
Family
Protein of unknown function DUF416
PF04222\"[1-194]TDUF416
InterPro
IPR013194
Domain
Histone deacetylase interacting
SM00761\"[24-121]Tno description
noIPR
unintegrated
unintegrated
PS51257\"[1-23]TPROKAR_LIPOPROTEIN


","BeTs to 3 clades of COG3068COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3068 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 1 to 196 match (2e-63) PD:PD036534 which is described as COMPLETE PROTEOME YJAG PM1733 VC0268 YPO3732 HI0431 ORF ","","","","","","","","","","","","Thu Dec 19 10:51:55 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00971 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 194 (E-value = 1.8e-136) place AA00971 in the DUF416 family which is described as Protein of unknown function, DUF (PF04222)","","","","","","","","1","","","" "AA00972","678105","678374","270","ATGAACAAAACAGATTTAATTGATGCTATCGCAAGCTCAGCTGAATTGAACAAAAAACAAGCTAAAGCAGCTTTAGAAGCAACTTTAGACGCTATCACCGGCAGCTTGAAAAAAGGTGAGGCGGTGCAATTAATCGGTTTCGGTACATTTAAAGTGAACGCACGCAAAGCGCGTACCGGTCGTAATCCGCAAACCGGCGCAGAAATCAAAATTGCCGCATCTAAAGTTCCGGCATTCGTTTCCGGTAAAGCATTAAAAGATGCTGTTAAA","","","9337","MNKTDLIDAIASSAELNKKQAKAALEATLDAITGSLKKGEAVQLIGFGTFKVNARKARTGRNPQTGAEIKIAASKVPAFVSGKALKDAVK","678376","","DNA-binding protein HU-ALPHA","Cytoplasm, Periplasm","","
InterPro
IPR000119
Family
Histone-like bacterial DNA-binding protein
PD000945\"[8-90]TDBH_PASMU_Q9CK94;
PR01727\"[40-55]T\"[58-71]T\"[74-88]TDNABINDINGHU
G3DSA:4.10.520.10\"[1-89]Tno description
PF00216\"[1-90]TBac_DNA_binding
SM00411\"[1-90]TBHL
PS00045\"[46-65]THISTONE_LIKE


","BeTs to 19 clades of COG0776COG name: Bacterial nucleoid DNA-binding proteinFunctional Class: LThe phylogenetic pattern of COG0776 is ---p---qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.7e-20) to 1/1 blocks of the IPB000119 family, which is described as \"Bacterial histone-like DNA-binding protein\". Interpro entry for IP:IPR000119. IPB000119 36-66 2.6e-20","Residues 1 to 90 match (5e-07) PD:PD516788 which is described as TRANSCRIPTION REGULATION DNA-BINDING REPRESSOR 3D-STRUCTURE FACTOR ","","","","","","","","","","","","Thu Dec 19 10:53:19 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00972 is paralogously related to AA02527 (8e-14) and AA02163 (1e-12).","","","","","","Residues 1 to 90 (E-value = 1.3e-51) place AA00972 in the Bac_DNA_binding family which is described as Bacterial DNA-binding protein (PF00216)","","","","","Kano,Y., Osato,K., Wada,M. and Imamoto,F. Cloning and sequencing of the HU-2 gene of Escherichia coli Molecular & general genetics : MGG. 209 (2), 408-410 (1987) PubMed: 3312963 Kohno,K., Wada,M., Kano,Y. and Imamoto,F. Promoters and autogenous control of the Escherichia colihupA and hupB genes Journal of molecular biology. 213 (1), 27-36 (1990) PubMed: 2187099 ","","Thu Dec 19 10:53:19 2002","1","","","" "AA00973","678503","679297","795","TTGAACTATTTTGACCCAAAAATGACTAAGCGAAACATTCAGACCCGTAATACGCAACAGCGTCGCCACGGCATCATGCAATTATTGCAGGAACGGGGCGAAATCAGCGTCGAGCAATTGGTGCAATTATTCGATACCTCGGAAGTGACTATTCGTAAAGATTTATCGGTGCTGCAAAGTAATGGTTTTCTGCTGCGTCGTTACGGCGGTGCGATTTTAATGCCGCAGGAATTGCTGGAAGATGCGCAAGAAGATTTTCTTTCGGAACGAAAGTTGGCAATTGCGAAAGTCGCGGCGGAACGCATTCGTGATCATAATCGTATTATTATCGACAGTGGTACCACCACGGCAGCATTGATTAAACAGCTAAATCACAAGCAAGGTCTGGTGGTAATGACCAATTCCATGTATGTAGCGAATGAGTTGCGTTCTTTAGAAAATGAACCGACCCTGTTAATGACCGGCGGCACTTGGGATAACCGCTCCGAATCCTTTCAAGGCAATGTGGCGGAACAGGTGTTGCGTTCTTATAACTTTGATCAGTTATTTATCGGCGCGGATGGCATTGATTTTGAACGCGGCACGACCACCTTTAACGAATTGGTTGGTTTAAGCCGTGTTATGGCGGAAGTGGCACGTGAAGTGATTGTGATGGTGGAATCACAAAAAATCGGGCGCAAAATGCCCAATGTAGAATTAACCTGGCAGCAAATTGATGTATTAATTACCGATAGTTTGTTGTCGGAAGAAAGCAAAAACCGTATTGCAGCCCATGGCGTAGAGGTGATCTGTGCT","","","30040","LNYFDPKMTKRNIQTRNTQQRRHGIMQLLQERGEISVEQLVQLFDTSEVTIRKDLSVLQSNGFLLRRYGGAILMPQELLEDAQEDFLSERKLAIAKVAAERIRDHNRIIIDSGTTTAALIKQLNHKQGLVVMTNSMYVANELRSLENEPTLLMTGGTWDNRSESFQGNVAEQVLRSYNFDQLFIGADGIDFERGTTTFNELVGLSRVMAEVAREVIVMVESQKIGRKMPNVELTWQQIDVLITDSLLSEESKNRIAAHGVEVICA","679299","","transcriptional regulator, DeoR family","Cytoplasm","","
InterPro
IPR001034
Domain
Bacterial regulatory protein, DeoR N-terminal
PR00037\"[39-53]T\"[53-71]THTHLACR
PF08220\"[21-77]THTH_DeoR
SM00420\"[21-73]THTH_DEOR
PS51000\"[18-73]THTH_DEOR_2
PS00894\"[21-55]?HTH_DEOR_1
InterPro
IPR014036
Domain
Bacterial regulatory protein, DeoR
PF00455\"[88-244]TDeoR


","BeTs to 8 clades of COG1349COG name: Transcriptional regulators of sugar metabolismFunctional Class: K,GThe phylogenetic pattern of COG1349 is -------qvd-lb-efgh-n-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.5e-37) to 5/5 blocks of the IPB001034 family, which is described as \"Bacterial regulatory protein, DeoR family\". Interpro entry for IP:IPR001034. IPB001034A 35-70 1.7e-15 IPB001034B 91-115 1.4e-10 IPB001034C 132-142 0.01 IPB001034D 155-167 0.87 IPB001034E 216-226 0.26","Residues 23 to 104 match (7e-17) PD:PD469489 which is described as COMPLETE PROTEOME TRANSCRIPTION REPRESSOR DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR LACTOSE PHOSPHOTRANSFERASE ","","","","","","","","","","","","Thu Dec 19 10:57:06 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00973 is paralogously related to AA02048 (2e-35), AA00308 (2e-16), AA01698 (4e-14), AA01546 (1e-12) and AA00585 (3e-11).","","","","","","Residues 21 to 244 (E-value = 4.1e-65) place AA00973 in the DeoR family which is described as Bacterial regulatory proteins, deoR family (PF00455)","","","","","","","","1","","","" "AA00974","679355","681187","1833","ATGTGTGGAATCGTCGGTGCAGTGGCACAACGTGATATCGCGGAAATTTTAATTAACGGATTACATCGTCTTGAGTATCGTGGTTACGACTCGGCAGGTTTGGCGGTGGTCAATTCGCAACATGAATTGCAACGTGTGCGCTGCTTAGGCAAAGTGAAAGCGTTAGATGATGCAGTGGAAAAAACGCCATTAATCGGCGGCACCGGGATTGCGCATACCCGTTGGGCAACCCATGGTGAACCTTCCGAAGAAAATGCCCATCCGCACGTTTCCGACAATTTCGCTGTAGTGCATAACGGTATTATTGAAAACTACGAAGAATTGCGCACCTTGTTAAAAGAACGCGGCTATGTCTTTACCTCCCAAACCGACACGGAAGTGATTGCGCACTTAGTGGAATGGGAAATGCGCACGGCGGGTAGCTTATTGGAAGCGGTGCAAAAAGTGGTGAAACAATTAACCGGTGCTTACGGCATGGTGGTGATGGATCGTATGCAACCGGAACATTTGGTTGCCGCCCGTTCCGGTAGCCCGTTGGTGATCGGTTTAGGGATTGGTGAAAACTTCCTTGCTTCCGACCAGCTTGCGTTGTTAAGCGTGACACGTCGCTTTATTTTCCTGGAAGAAGGCGACATTGCCGAAATTACCCGTCGTTCCGTGGATATTTACGATCATCGCGACGGCAACAAAGTCGAACGTGAAGCGCACGATTCCAATTTAGAAAACGATGCGGCGGAAAAAGGCAAATATCGCCACTTCATGCAAAAAGAAATTTACGAACAGCCGACCGCACTGATTAACACCATGGAAGGTCGTGTGACCCACAATAACGTGATAGTTGAAGCTATCGGTAACAGTGCCAAAGAAATTCTGGAAAAAGTCGAACATGTTCAAATCGTTGCCTGCGGTACTTCGTACAACTCCGGTATGGTGGCGCGTTATTGGTTTGAAAGCATAGCAGGCGTCAGCTGCGATATTGAAATCGCTTCCGAATTCCGTTACCGCAAATTTGTGGTGCGCCCGAACAGCCTGTTGATTACTCTTTCCCAATCCGGTGAAACGGCGGACACTTTAGCCGCCTTGCGTTTGGCGAAAGAAAAAGGCTACATGGCGGCAATGACCATTTGTAACGTGGCGGGTTCCTCTCTGGTGCGTGAATCCGATTTAGCCTTCATGACCCGCGCCGGCGTGGAAATCGGCGTGGCTTCGACCAAAGCTTTCACTACACAATTAGCGTCATTGTTAATGTTGGTGGTGGCGATCGGTAAGGCGAAACACACGCTTTCCGCCGAAAAAGAACAGGAAATGGTCAAAGCATTACAAGCCTTGCCGGCAGAAATTGAGAAAGCCTTGGCGTTCGATAAACAAATTGAAACGCTGGCGGAAGATTTCGCCGAAAAACACCATGCCTTATTCTTAGGTCGCGGCGAATATTATCCGATTGCCATGGAAGCGTCCTTGAAGCTGAAAGAAATTTCTTACATTCACGCCGAAGCCTATGCCGCCGGTGAATTGAAACACGGCCCGTTGGCGTTAATTGACGCGGATATGCCGGTTATTGTGGTGGCGCCGAACAATGAACTATTGGAAAAAATCAAATCCAATATCGAAGAGGTGCGCGCTCGCGGCGGTCAGTTATATGTTTTCGCCGACAAAGAAGCAGGCTTCACCGAAGCGGAAGGGATGAAAATCATCACCATGCCGACGGTCAACGAAATCACCGCGCCGATTTATTATACCGTGCCAATGCAGTTGTTGGCGTATCACATCGCGCTGATTAAAGGTACCGACGTGGATCAGCCGCGTAATCTGGCGAAAGCGGTCACCGTAGAG","","","69045","MCGIVGAVAQRDIAEILINGLHRLEYRGYDSAGLAVVNSQHELQRVRCLGKVKALDDAVEKTPLIGGTGIAHTRWATHGEPSEENAHPHVSDNFAVVHNGIIENYEELRTLLKERGYVFTSQTDTEVIAHLVEWEMRTAGSLLEAVQKVVKQLTGAYGMVVMDRMQPEHLVAARSGSPLVIGLGIGENFLASDQLALLSVTRRFIFLEEGDIAEITRRSVDIYDHRDGNKVEREAHDSNLENDAAEKGKYRHFMQKEIYEQPTALINTMEGRVTHNNVIVEAIGNSAKEILEKVEHVQIVACGTSYNSGMVARYWFESIAGVSCDIEIASEFRYRKFVVRPNSLLITLSQSGETADTLAALRLAKEKGYMAAMTICNVAGSSLVRESDLAFMTRAGVEIGVASTKAFTTQLASLLMLVVAIGKAKHTLSAEKEQEMVKALQALPAEIEKALAFDKQIETLAEDFAEKHHALFLGRGEYYPIAMEASLKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKIKSNIEEVRARGGQLYVFADKEAGFTEAEGMKIITMPTVNEITAPIYYTVPMQLLAYHIALIKGTDVDQPRNLAKAVTVE","681189","","glucosamine-fructose-6-phosphate","Cytoplasm","","
InterPro
IPR000583
Domain
Glutamine amidotransferase, class-II
PF00310\"[2-194]TGATase_2
PS00443\"[1-6]?GATASE_TYPE_II
InterPro
IPR001347
Domain
Sugar isomerase (SIS)
PF01380\"[290-423]T\"[463-597]TSIS
InterPro
IPR005855
Family
Glucosamine-fructose-6-phosphate aminotransferase, isomerising
TIGR01135\"[2-611]TglmS: glucosamine--fructose-6-phosphate ami
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.10490\"[243-463]Tno description
G3DSA:3.60.20.10\"[2-225]Tno description
PTHR10937\"[2-611]TGLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE


","BeTs to 22 clades of COG0449COG name: Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domainsFunctional Class: MThe phylogenetic pattern of COG0449 is -ompkzyqvdrlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is","Significant hit ( 5.8e-35) to 4/4 blocks of the IPB000583 family, which is described as \"Glutamine amidotransferase class-II\". Interpro entry for IP:IPR000583. IPB000583A 24-34 0.0012 IPB000583B 70-79 9e-06 IPB000583C 98-126 2.2e-16 IPB000583D 595-610 0.00025Significant hit ( 4.7e-17) to 2/2 blocks of the IPB001347 family, which is described as \"SIS domain\". Interpro entry for IP:IPR001347. IPB001347A 71-79 0.0065 IPB001347B 343-368 1.7e-12","Residues 63 to 91 match (2e-09) PD:PD530988 which is described as AMINOTRANSFERASE AMIDOTRANSFERASE GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE ISOMERIZING GFAT TRANSFERASE HEXOSEPHOSPHATE D-FRUCTOSE-6- PHOSPHATE PROTEOME ","","","","","","","","","","","","Thu Dec 19 10:58:48 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00974 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 461 to 597 (E-value = 7.3e-39) place AA00974 in the SIS family which is described as SIS domain (PF01380)","","","","","Walker,J.E., Gay,N.J., Saraste,M. and Eberle,A.N. DNA sequence around the Escherichia coli unc operon.Completion of the sequence of a 17 kilobase segment containingasnA, oriC, unc, glmS and phoS. Biochem. J. 224(3): 799-815, 1984. PubMed: 6395859. Gay,N.J., Tybulewicz,V.L. and Walker,J.E. Insertion of transposon Tn7 into the Escherichia coli glmStranscriptional terminator. Biochem. J. 234(1): 111-117, 1986. PubMed: 3010949. Dutka-Malen,S., Mazodier,P. and Badet,B. Molecular cloning and overexpression of the glucosaminesynthetase gene from Escherichia coli. Biochimie 70(2): 287-290, 1988. PubMed: 3134953. ","","Thu Dec 19 10:58:48 2002","1","","","" "AA00976","682338","681346","993","ATGGCAGCAGATTACAAACAAAATCCGTTCACCTTGGCTTATGACGGGGCAATCACCGAAAACGTGAAAGGCAAAGTGAATATTCACCCGGTGACTTACGTTAATAACGACGGCATTAAAATTTCCGCCAACGTTTACACACCAGCCAACTTTGACCCAAACAAAAAATACCCGGCAATTACCGTAGCGCACCCGAACGGCGGCGTGAAAGAGCAAGTGGCAGGCTTATACGCCCAAAAATTAGCCGAACAAGGCTATATCACCATCGCGGCTGATGCGGCATACCAAGGTGCAAGCGGTGGCGAACCACGTCAAACCGACAAACCGGCAAACCGTATCAACGATGTTCACGCAATGGTGGACTTCCTTGAAAAATATCAAGGCGTAGATACCAACCGTATCGGGGCATTAGGAATTTGTGGCGGTGGCGGTTACACCTTCGCGGCAGCACAAAGCGACAAACGCTTGCACGCCGTGGCAACCGTGAGCTTGTTCAACACAGGTGATGTGCGTCGTAACGGCTTAGGCGGAAGCCAAGTTTCTACTATTCAAGAACGCCTTGCACAAGCGGCGGCAGCGCGTACCGAAGAAGCCAAAGGCAACGTGGAATACGCAGCGAATGCGGATATGAGCAAAATCACCGAAGCGGACGTGGCGAAAATGCCTGCTGGCTTATACAAAGACGGTTTTGAATACTACGGCATCACCCACCGCCACCCAAACAGCACGCCACGTTACACCATGGGTAGCTTGTTAGACTTAATGACATGGGACGCCACCGACCACGCGGAACTCATCAACACGCCATTATTGATCGTGGCAGGCGACAAAGCCGACACCCTTTATATGAGCGACAAAGCCTTTGAAAAAGCAGGTTCGCAAGACAAAGAATTGGTGAAAATCCCAGGAGCGAGCCATATCGAAACCTACTGGAAGCCTGAATATGTGAAACAAATCAGCGAGAAATTGACGGATTTCTTTGGGAAGAAATTG","","","39349","MAADYKQNPFTLAYDGAITENVKGKVNIHPVTYVNNDGIKISANVYTPANFDPNKKYPAITVAHPNGGVKEQVAGLYAQKLAEQGYITIAADAAYQGASGGEPRQTDKPANRINDVHAMVDFLEKYQGVDTNRIGALGICGGGGYTFAAAQSDKRLHAVATVSLFNTGDVRRNGLGGSQVSTIQERLAQAAAARTEEAKGNVEYAANADMSKITEADVAKMPAGLYKDGFEYYGITHRHPNSTPRYTMGSLLDLMTWDATDHAELINTPLLIVAGDKADTLYMSDKAFEKAGSQDKELVKIPGASHIETYWKPEYVKQISEKLTDFFGKKL","681348","","conserved hypothetical protein","Periplasm","","
InterPro
IPR000383
Domain
Peptidase S15
PF02129\"[37-308]TPeptidase_S15
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1820\"[38-309]Tno description
PTHR17630\"[56-161]TDIENELACTONE HYDROLASE
PTHR17630:SF20\"[56-161]TCARBOXYMETHYLENEBUTENOLIDASE


","BeTs to 4 clades of COG1073COG name: Hydrolases of the alpha/beta superfamilyFunctional Class: RThe phylogenetic pattern of COG1073 is ao--kzy-vdrlb-efg-s--j-i--Number of proteins in this genome belonging to this COG is","","Residues 1 to 36 match (2e-10) PD:PD526369 which is described as PROTEOME YPO2002 COMPLETE ","","","","","","","","","","","","Tue Jan 21 14:07:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00976 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00977","682507","683394","888","ATGCTTAACAATCTTCCCAACCTCAACGAGCTTTATTATTTTATCCAAGTGGTTCAGGCAGGCTCTTTTGCCAAAGCGGCGAACAAGCTGGGCGTAACGTCATCGGCACTCAGCCAGAATGTGAAAAGCTTAGAAAAATCGCTGGACTTACGGCTGCTCAACCGCACCACACGCAGCATTTCCCCCACCAACGCAGGGGAAAAATTACTCGCCCAAATCACACCGCACTTTCACGCCATCGTAGGCGGACTCAATCAGTTAGACGACTGGCGAAATTCCCCCCTTGGCACCATCCGCATCAACACCAGCGAAGTGGCGGCGAATTTGTTGCTTTACCCGAAATTAAAAACGCTCATGCAACGCTACCCCGAACTGAAAATCGAAATGGTGGTGGAAAACCGTTGGGTGGACATTGTGGAACAGGGCTTTGATATGGGCGTGCGGCTGGGATATGCCTTGTATAAGGATATGATTGCAGTAAAAATTTCTGACCCCGTCCGAATGGCGGTGGTGGCAAGCCCCGATTATTTGCGTGGCAAACCGTCCGTGCAAGCCATCGCTGACTTGCCCGCCCATCTCCTGATTGGTCTGCGACTTTCCAACCAACACGGCGAAGCCCACTGGGAATTTCAACACAAGGGCGAACGCATCACCTTCCAACCCGAACCACATTTTTCCGTGAATAACGGCTTACGCCACCAAGCCGCCCTAGACGGCTTAGGCATTGCGTGGCTGCCAAAAATCGTGGTGGAAAAGGATTTGGAAGCGGGGCGGTTAGTGGAATTGCTCGACGAATACGCAATGGAATACGAACCGCTGTATCTCTACTACCCAAACCGACAAGGGCATTCACGAGCGTTTGAGTTGGTGGTGGAGGCGTTGCGGGTG","","","33350","MLNNLPNLNELYYFIQVVQAGSFAKAANKLGVTSSALSQNVKSLEKSLDLRLLNRTTRSISPTNAGEKLLAQITPHFHAIVGGLNQLDDWRNSPLGTIRINTSEVAANLLLYPKLKTLMQRYPELKIEMVVENRWVDIVEQGFDMGVRLGYALYKDMIAVKISDPVRMAVVASPDYLRGKPSVQAIADLPAHLLIGLRLSNQHGEAHWEFQHKGERITFQPEPHFSVNNGLRHQAALDGLGIAWLPKIVVEKDLEAGRLVELLDEYAMEYEPLYLYYPNRQGHSRAFELVVEALRV","683396","","transcriptional regulator (LysR family)","Cytoplasm","","
InterPro
IPR000847
Domain
Bacterial regulatory protein, LysR
PF00126\"[8-67]THTH_1
PS50931\"[6-63]THTH_LYSR
InterPro
IPR005119
Domain
LysR, substrate-binding
PF03466\"[91-295]TLysR_substrate
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[6-92]Tno description


","No hits to the COGs database.","Significant hit ( 2e-09) to 1/1 blocks of the IPB000847 family, which is described as \"Bacterial regulatory protein, LysR family\". Interpro entry for IP:IPR000847. IPB000847 22-55 2e-09","Residues 84 to 135 match (5e-08) PD:PD411333 which is described as TRANSCRIPTION YCAN PROTEOME REGULATION DNA-BINDING COMPLETE ","","","","","","","","","","","","Thu Dec 19 12:04:44 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00977 is paralogously related to AA00985 (1e-58), AA01794 (8e-16), AA02539 (9e-07) and AA01999 (5e-05).","","","","","","Residues 91 to 295 (E-value = 1.3e-34) place AA00977 in the LysR_substrate family which is described as LysR substrate binding domain (PF03466)","","","","","Sperandio V, Li CC, Kaper JB.Quorum-sensing Escherichia coli regulator A: a regulator of the LysR family involved in the regulation of the locus of enterocyte effacement pathogenicity island inenterohemorrhagic E. coli.Infect Immun. 2002 Jun;70(6):3085-93.PMID: 12011002 Colmer JA, Hamood AN.Molecular analysis of the Pseudomonas aeruginosa regulatory genes ptxR and ptxS.Can J Microbiol. 2001 Sep;47(9):820-8.PMID: 11683464 Colmer JA, Hamood AN.Expression of ptxR and its effect on toxA and regA expression during the growth cycle ofPseudomonas aeruginosa strain PAO1.Can J Microbiol. 1999 Dec;45(12):1008-16.PMID: 10696480","","Thu Dec 19 11:07:34 2002","1","","","" "AA00978","684645","683539","1107","ATGAAAAAATTCGCAAAAATTTCTACACTTTTAACCGCTTGTGCCTTAGCCGTACAAGCCTACGCTGCCCCACTTTCCATTGAGAAGCAAGGCTCCTTTGCCGTGGGCGGCACGGTGAAAACCTCGGAAGGCACTTATACGCCAATCCCTGATGCGATTAAAAACCGCCAAAGCTCGGCATTTTTTGATGTGTACGGCGAGGCGGTGAAAGCAGGAGGAATGACGCTACACGGTGATCATGCCAGCGTGTTTTACCAAATTCCAACCAATGCGAAACAAAATTCGTTGGTGTTCTTGCAAGGCTACGGGCAATCTGCACGCGGTTGGATGACCACACCAGACGGACACGAAGGCTTTAACGAGCTTTTCTTGCAACGCAACTACCCAGTTTATTTGGTGGATCAACCTCGTCGCGGACAAGCAGGACGCAGTACTGTTGATGCCAATGTGCCAGCCACACCTGACGACCAATTTTGGTATGCCCAATTCCGTATCGGTGTTTATCCGAAGATGAACGAAGGCGTGGCATTCCCGAAAGATGCGGAAAGCCAAGCACAATTCTTCCGAATGATGACGCCAGACACGGGGGCATTTGATGTGCCGGTTATCACCGATAGTATGGTGAAACTCTTTGATAAAACAAGCGGTGGCGTATTTGTGACCCACTCCGCAGGCGGGGTTATCGGTTGGACAACAGCGATGGCAAGCGATAAAGTCAAAGGCGTGGTTGCTTATGAACCCGGTGCGTTTTTCTTCCCCGAAGGCGAAACGCCTGCGAAATTAGAGAGCAAATTTGGTGATGTTGCTCCGCTGACTGTGCCGAAAGCGCAATTTGAAAAACTCACTAAAATGCCAATTGTCATCTACTTTGGCGACTTCATTCCCGACCATTTAGACGGCACGCAAGGCGGCGAGCAATGGTTTATCCGAATGAAAATGGCACAACAATTTGTGGATACCATCAACAAACACGGCGGCAAAGCGGAGCTAATTCATCTGCCGAAAATCGGCATCAAAGGCAACACGCACTTTATGTTTAGCGATTTGAACAATGATAAAGTGGCGGAAGAAATGGCGCGCTGGTTGAAGGCAAAGGGGTTGGATAAG","","","40460","MKKFAKISTLLTACALAVQAYAAPLSIEKQGSFAVGGTVKTSEGTYTPIPDAIKNRQSSAFFDVYGEAVKAGGMTLHGDHASVFYQIPTNAKQNSLVFLQGYGQSARGWMTTPDGHEGFNELFLQRNYPVYLVDQPRRGQAGRSTVDANVPATPDDQFWYAQFRIGVYPKMNEGVAFPKDAESQAQFFRMMTPDTGAFDVPVITDSMVKLFDKTSGGVFVTHSAGGVIGWTTAMASDKVKGVVAYEPGAFFFPEGETPAKLESKFGDVAPLTVPKAQFEKLTKMPIVIYFGDFIPDHLDGTQGGEQWFIRMKMAQQFVDTINKHGGKAELIHLPKIGIKGNTHFMFSDLNNDKVAEEMARWLKAKGLDK","683541","","conserved hypothetical protein","Periplasm","","
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1820\"[13-365]Tno description
signalp\"[1-22]?signal-peptide


","No hits to the COGs database.","","Residues 24 to 358 match (1e-85) PD:PD494256 which is described as PROTEOME EXPORTED COMPLETE ","","","","","","","","","","","","Tue Jan 21 14:15:41 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00978 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00979","685114","684785","330","GTGTATAACTATTTGTTTACCTGGGATACGCCTGTGTTTAATGGCACGCCAATGAGCTACCACACCGCAGAAATTGCCTTTGTGTTCAACAATATTCAACGTATGGCACAAGCCACAGGCGGTGGTGATGAAGCTCAAGCGTTGGCGGATAAAATGGCCCGTGCGTGGACGAACTTCGCTAAAGCAGGCAACCCGAACGGTGAAGGCTTACCGCAATGGGACGCTTACACCCGCGAAAACGGCAATGTGATGATTTTTGATAACCAAGTGGAAGTGAAACAACATCACGATGCGAAGTTGCAGCGTTTGTTGGCGCCGAGTATGAAGTTT","","","12383","VYNYLFTWDTPVFNGTPMSYHTAEIAFVFNNIQRMAQATGGGDEAQALADKMARAWTNFAKAGNPNGEGLPQWDAYTRENGNVMIFDNQVEVKQHHDAKLQRLLAPSMKF","684787","","type B carboxylesterase; p-nitrobenzyl esterase","Periplasm, Extracellular","","
InterPro
IPR002018
Family
Carboxylesterase, type B
PTHR11559\"[1-94]TCARBOXYLESTERASE
PF00135\"[43-103]TCOesterase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1820\"[1-105]Tno description
PTHR11559:SF14\"[1-94]TCARBOXYLESTERASE-RELATED, BACTERIA


","BeTs to 4 clades of COG2272COG name: Carboxylesterase type BFunctional Class: IThe phylogenetic pattern of COG2272 is ---------dr-b--------j----Number of proteins in this genome belonging to this COG is","","Residues 2 to 77 match (1e-08) PD:PD000605 which is described as HYDROLASE ESTERASE PRECURSOR SIGNAL SERINE CARBOXYLESTERASE GLYCOPROTEIN ACETYLCHOLINESTERASE FAMILY MEMBRANE ","","","","","","","","","","","","Tue Feb 18 15:55:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00979 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Zock J, Cantwell C, Swartling J, Hodges R, Pohl T, Sutton K, Rosteck P Jr, McGilvray D, Queener S.The Bacillus subtilis pnbA gene encoding p-nitrobenzyl esterase: cloning, sequence and high-level expression in Escherichia coli.Gene. 1994 Dec 30;151(1-2):37-43.PMID: 7828905","","Thu Dec 19 11:29:00 2002","1","","","" "AA00980","685469","685110","360","GTGGGCACCAACAATGGACGGCGATTATATCCCGCAGGAGCCTGTGGGCAAAAATACCCAGAAATCGCGAAAGATATTCCACTTCTGATTGGTTCAAACTTAACGGAATGGGAAAGTTTTGGGGCACAGCTTGATCTTGTCAACACTCAAAAAGACAACCGTTTCATTTGGACGGAAGCACAAGTTCAAGAAAAATTAAAAGCGAAATATGGCGAGAAAACCGATGAAATCGTGGCTGCATTCCGTGAAGCGTACCCAGATCGTATGCTTGCCGATGCGTTATATGTAGATAGCTTCTTGCGTGCCCCTGCGTTAAAAACCGCGGGCTTGAAATCAAGATCAAAAAGGTGCACCTGTGTA","","","13399","VGTNNGRRLYPAGACGQKYPEIAKDIPLLIGSNLTEWESFGAQLDLVNTQKDNRFIWTEAQVQEKLKAKYGEKTDEIVAAFREAYPDRMLADALYVDSFLRAPALKTAGLKSRSKRCTCV","685112","","hypothetical protein","Periplasm, Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Dec 19 11:21:49 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00980 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA00981","686437","685385","1053","ATGAAACTTTTCCCTTCCAAATTGACGTTAGCTCTTGCTATTGCAAGTGGCTTAAGTGTAACAAATTTAAGCTATGCCACTAACGATACTATTCAAGCGGGCAACGGCATTGCCGTGGTACAAACCCAATCGGGTGAAATCCAAGGTTATATTCATAACGATATTTTGACCTATAAAGGCATTCCGTATGCCACAGCAGAACGTTTTATGCCACCAAAACCGGTGGAGAATTGGCAAGGGACAAAAATGGCGTTGACTTATGGCGATGTCTGCCCGCAAGTGCCGATGGGCGGTCGTAGTTTCTTCTTTACCGGACCTGAAATGACGGAAAGTGAGCAATGTTTAAATTTAAACGTTTGGGCGCCGAAAAATGACGGTAAAAAACGGGCGGTGATGGTGTGGATTCACGGCGGCGGTTTTCAATCGGGCGCATCAAATGATTTAGACAGTTACGATGGCGAAAACTTAGCCCGCAAAGGTGATGTAGTCGTTGTGTCGGTTAATCACCGTTTAAATGCCATGGGATATTTAGATCTTTCTGCTTACGGAAAACAGTATAAAAATTCAGCAAATGCGGGTATTCAAGATTTAGTGGCTGCATTGGAATGGGTGAAAGCGAATGCTGAACAATTTGGCGGTGATCCGAATAATGTGACCATCTTCGGTGAAAGTGGCGGTGGTGCGAAAGTGTTAACCTTAATGGCGACACCAGCAGCAAAAGGCTTGTTCAACAAAGCGATTGTGCAAAGTGGTGCGGTAGAAAAAATGGGTATGACGCTTACGTCACCGAAAACAGGGCAACGAGTGGCGGAGCTGACCCTTGCAAATTTAGGCGTAAAACCGACCGCACTTAATCGACTTAATAGCTTTACACCGGATCAAATTAATGCTGCCGCCAATAAAGCCTTAAAACAAACCGCAGAAGAACAAAAAATCACACCATTACGCGGAACGGGCTATGGCTTAGCGTGGGCACCAACAATGGACGGCGATTATATCCCGCAGGAGCCTGTGGGCAAAAATACCCAGAAATCGCGAAAGATATTCCACTTC","","","37614","MKLFPSKLTLALAIASGLSVTNLSYATNDTIQAGNGIAVVQTQSGEIQGYIHNDILTYKGIPYATAERFMPPKPVENWQGTKMALTYGDVCPQVPMGGRSFFFTGPEMTESEQCLNLNVWAPKNDGKKRAVMVWIHGGGFQSGASNDLDSYDGENLARKGDVVVVSVNHRLNAMGYLDLSAYGKQYKNSANAGIQDLVAALEWVKANAEQFGGDPNNVTIFGESGGGAKVLTLMATPAAKGLFNKAIVQSGAVEKMGMTLTSPKTGQRVAELTLANLGVKPTALNRLNSFTPDQINAAANKALKQTAEEQKITPLRGTGYGLAWAPTMDGDYIPQEPVGKNTQKSRKIFHF","685387","","carboxylesterase","Periplasm, Extracellular","","
InterPro
IPR002018
Family
Carboxylesterase, type B
PTHR11559\"[39-337]TCARBOXYLESTERASE
PF00135\"[8-349]TCOesterase
PS00122\"[211-226]?CARBOXYLESTERASE_B_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1820\"[39-338]Tno description
PTHR11559:SF14\"[39-337]TCARBOXYLESTERASE-RELATED, BACTERIA
signalp\"[1-26]?signal-peptide


","BeTs to 4 clades of COG2272COG name: Carboxylesterase type BFunctional Class: IThe phylogenetic pattern of COG2272 is ---------dr-b--------j----Number of proteins in this genome belonging to this COG is","Significant hit ( 3.1e-21) to 1/1 blocks of the IPB002018 family, which is described as \"Carboxylesterases type-B\". Interpro entry for IP:IPR002018. IPB002018 190-230 2.9e-21","Residues 131 to 238 match (8e-25) PD:PD000713 which is described as HYDROLASE ESTERASE PROTEOME COMPLETE PRECURSOR SIGNAL CARBOXYLESTERASE SERINE GLYCOPROTEIN LIPASE ","","","","","Sun Feb 16 16:10:40 2003","","","","","","","Thu Dec 19 11:25:39 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00981 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 349 (E-value = 9.3e-14) place AA00981 in the COesterase family which is described as Carboxylesterase (PF00135)","","","","","Zock J, Cantwell C, Swartling J, Hodges R, Pohl T, Sutton K, Rosteck P Jr, McGilvray D, Queener S.The Bacillus subtilis pnbA gene encoding p-nitrobenzyl esterase: cloning, sequence and high-level expression in Escherichia coli.Gene. 1994 Dec 30;151(1-2):37-43.PMID: 7828905","","Thu Dec 19 11:29:05 2002","1","","","" "AA00982","687643","686666","978","ATGCAAACTCGACAACTTGGCTCACAAGGTTTAACGGTTTCTGAGCTTGGTTTGGGCTGCATGGGCATAACTTTCGGCTATAGCACGGAAATTCCTCAAGCAGAGGGGGTAAAACTCATTCGGCAAGCCTTTGATTTAGGCGTCACGTTTTTTGATACCGCCGAAGCCTATGGTGAAGCGAATGAAGTGTTAGTGGGGAAAGCTGTTGCGCCATTTCGTGATCAGGTAGTGGTTGCGACCAAGTTCGGTTTCAAAAATGGTAATGTGGCGGAGGGGCTGGACAGCCGTCCTGAACGCATTCGCCAAGTGGTGGAGCAATCACTCAAACGCATGAACACCGATTATATTGATTTGTTGTATCAGCACCGCGTCGATCCGAATGTGCCGATTGAAGAGGTGGTGGGCGCGGTGAAAGACTTGATTGCAGAGGGCAAAGTGAAGTATTTCGGCTTGTCTGAAGTGGGTGCGGAGATTATCCGTCGCGCTCACGCCGTTCAACCTGTGTCGGCATTGCAAAGCGAATATTCGTTGATGTGGCGTGAACCTGAAGCGGAAATTTTCCCACTGCTAGAAGAATTAAACATTGGCTTCGTGCCATTTAGTCCATTGGCAAAATCCTTGCTTACCGGAACGATCACCGCCGATACCCAATTTGCCGCCAACGATTTCCGCAACAGCGTTCCCCGTTTGCAAGGCGATGCGCTGAAAAGCAACCTTGGGCTAGCCGAATTGGTGAAAAACATCGCCGCTCAAAAAGGCGTAACTCTAGCACAAGTTGCCTTGGCTTGGGTGTTGGCGCAAAAACCATGGATTGCCCCGATTTTCGGCACCACGAAACCTCATCGTTTAGTGGAAAATTTAGGTGGTGCGGACGTGCATTTAAGCGCAGAAGATTTAACTCGAATTCAAACCGCACTTTCGCAAATTCAGATTGTGGGCGAGCGTTATAGTGCGGCAGGGCAGGCATTGATTAATCGT","","","35503","MQTRQLGSQGLTVSELGLGCMGITFGYSTEIPQAEGVKLIRQAFDLGVTFFDTAEAYGEANEVLVGKAVAPFRDQVVVATKFGFKNGNVAEGLDSRPERIRQVVEQSLKRMNTDYIDLLYQHRVDPNVPIEEVVGAVKDLIAEGKVKYFGLSEVGAEIIRRAHAVQPVSALQSEYSLMWREPEAEIFPLLEELNIGFVPFSPLAKSLLTGTITADTQFAANDFRNSVPRLQGDALKSNLGLAELVKNIAAQKGVTLAQVALAWVLAQKPWIAPIFGTTKPHRLVENLGGADVHLSAEDLTRIQTALSQIQIVGERYSAAGQALINR","686668","","aldo-keto reductase","Cytoplasm","","
InterPro
IPR001395
Family
Aldo/keto reductase
PD000288\"[6-318]TQ89IT7_BRAJA_Q89IT7;
PR00069\"[43-67]T\"[106-124]T\"[239-263]TALDKETRDTASE
G3DSA:3.20.20.100\"[1-318]Tno description
PTHR11732\"[1-213]T\"[235-278]TALDO/KETO REDUCTASE
PF00248\"[7-307]TAldo_ket_red
noIPR
unintegrated
unintegrated
PTHR11732:SF12\"[1-213]T\"[235-278]TALDO/KETO REDUCTASE


","No hits to the COGs database.","Significant hit ( 1.3e-19) to 6/6 blocks of the IPB001395 family, which is described as \"Aldo/keto reductase family\". Interpro entry for IP:IPR001395. IPB001395A 7-18 1.2e+02 IPB001395B 43-62 2.2e-05 IPB001395C 71-83 37 IPB001395D 113-124 0.057 IPB001395E 167-204 2.7 IPB001395F 254-299 0.00016","Residues 81 to 156 match (7e-10) PD:PD596523 which is described as F8A5.26 T16B5.5 ","","","","","","","","","","","","Thu Dec 19 11:33:19 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00982 is paralogously related to AA00983 (1e-08).","","","","","","Residues 7 to 307 (E-value = 2.5e-59) place AA00982 in the Aldo_ket_red family which is described as Aldo/keto reductase family (PF00248)","","","","","","","","1","","","" "AA00983","688552","687710","843","ATGGAAAAAGTATTCAAATTAAACAACGGTGTAGAAATGCCAATGGTAGGTTTCGGCGTATATCAAGTGAGCGATGAAGAAACCGAAAAAGCGGTATTGGAAGCACTCAAAGCAGGCTACCGTTTATTAGACACCGCCGCAGTGTACGCCAACGAAGCGGGCGTAGGGCGTGCCATTAAAACCAGTGGCATTCCGCGTGAAGACATTTTCGTCACTACCAAACTGTGGATTCAACGTAAAAACGGTTATGAAAACACCAAAAAAGCCTTGGAAGATTCCCTTGAACGTTTAGGGTTGGATTATGTGGATTTATATTTAATGCACCAACCGTTGGGCGATGTACACGAAGAATGGCGTGCGATGGAAGAGTTATACAAGGCCGGCAAAGCTCGTGCCATCGGCGTGAGTAACTTCCACACTGACCGTTTAATGGATTTAATCACCTGCCACGACATCGTGCCGGCGGTGAATCAAATTGAAACCCACCCGTTCTATCAACGTGATGAAGAAATTGCGTTCCACAAAGAACACGGCATTTTGCAACAATCTTGGGGCCCGTTGGCAGAAGGGAAATTTGACATTTTTACCAACCCTGTATTAACCAAAATTGCCGAAAAACACGGTAAATCGGTGGCGCAAGTGGTGTTGCGCTGGTTAAACCAACGTGGCGTGGCGATTATCCCGAAATCGGTGAAAGTGGAACGTATGCTTGAAAACCGCGATATTTTCGGCTTCACCTTAGATGAACAAGATTTAGCCGACATCGCAATCCTCAACCGCAATGAAATCATCTTCAATCACCGCGATCCCAAAATGATTGTGTGGTTGGCGCAGGCAAGAGGG","","","32060","MEKVFKLNNGVEMPMVGFGVYQVSDEETEKAVLEALKAGYRLLDTAAVYANEAGVGRAIKTSGIPREDIFVTTKLWIQRKNGYENTKKALEDSLERLGLDYVDLYLMHQPLGDVHEEWRAMEELYKAGKARAIGVSNFHTDRLMDLITCHDIVPAVNQIETHPFYQRDEEIAFHKEHGILQQSWGPLAEGKFDIFTNPVLTKIAEKHGKSVAQVVLRWLNQRGVAIIPKSVKVERMLENRDIFGFTLDEQDLADIAILNRNEIIFNHRDPKMIVWLAQARG","687712","","aldo-keto reductase","Cytoplasm","","
InterPro
IPR001395
Family
Aldo/keto reductase
PD000288\"[7-259]TQ9X0A2_THEMA_Q9X0A2;
PR00069\"[35-59]T\"[92-110]T\"[121-138]T\"[155-184]T\"[194-218]TALDKETRDTASE
G3DSA:3.20.20.100\"[1-261]Tno description
PTHR11732\"[1-231]TALDO/KETO REDUCTASE
PF00248\"[7-260]TAldo_ket_red
PS00062\"[121-138]TALDOKETO_REDUCTASE_2
PS00063\"[227-242]TALDOKETO_REDUCTASE_3
PS00798\"[39-56]TALDOKETO_REDUCTASE_1
noIPR
unintegrated
unintegrated
PTHR11732:SF34\"[1-231]TALDO-KETO REDUCTASE


","BeTs to 12 clades of COG0656COG name: Aldo/keto reductases, related to diketogulonate reductaseFunctional Class: RThe phylogenetic pattern of COG0656 is -o-pkzy-v-rlbcefg----j----Number of proteins in this genome belonging to this COG is","Significant hit ( 5.2e-76) to 6/6 blocks of the IPB001395 family, which is described as \"Aldo/keto reductase family\". Interpro entry for IP:IPR001395. IPB001395A 7-18 0.0011 IPB001395B 35-54 2.6e-09 IPB001395C 64-76 7.7e-09 IPB001395D 99-110 1.2e-06 IPB001395E 151-188 9.9e-16 IPB001395F 207-252 1.5e-24","Residues 7 to 259 match (1e-86) PD:PD000288 which is described as REDUCTASE PROTEOME COMPLETE OXIDOREDUCTASE CHANNEL DEHYDROGENASE NADP POTASSIUM ALDO/KETO FAMILY ","","","","","Thu Feb 13 16:43:18 2003","","","","","","","Thu Dec 19 11:35:06 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00983 is paralogously related to AA00982 (9e-09).","","","","","","Residues 7 to 260 (E-value = 6.8e-120) place AA00983 in the Aldo_ket_red family which is described as Aldo/keto reductase family (PF00248)","","","","","","","","1","","","" "AA00985","688911","689801","891","ATGATCGACAACATCAACGAACTTCGCACCTTTATCACCGCGGCGCAAGAAGGCAGTTTCACCAAAGCCGCCGCAAAATTAAACGTTTCCACCTCCGCATTAAGCCATTCCATTCGCAAGCTGGAAGAACAGCTCAACATCAAACTGTTCAACCGCACCACACGCAGCATTGCCACCACGGAGGCGGGCGAGCAGTTGTTTCAAAATCTCTTGCCGTTGTTTGAAAGTATTGAAGATAATCTCAACGCATTAAGCACCTTTCGCAACACGTTGAAAGGGAAATTATGCATTAACGGTAACGATCATGTTTTTTTATCCATTTTGTGGGATAAATTGATGGCGTTCGCGGAACAATACCCCGAAATGGAATTGGAATTGACCAGTGACACCAAATTTGTGGATATCGTGGCGGGGCGGTTTGATGCGGGTATTCGCTTAGGATCGGACGTGGCACAAGATATGATCGCCGTGAGATTAAGCGACAAAATGCAAATGGCGGTGGTCGGCACGCCAGAGTATTTCGCCAAAAAAGCCACACCGAAGAAAGTAGAAGACTTGGGCGAACACGAGTGCTTGCTGGTGCGTTTGCCAACTTCAGACAGCATTATGACGTGGGAATTTCAGCCTGCAAAAAAATCCGCGCCTGTGGTGAAATTCCACCCGAAAGGACAACTTTGTTTTAACAACAGCCATTTAATCAGCCGTGCCGTGTTGGTGGGCAAAGGCTTGGCATGGTTGCCCATCGACACCATGCAGCCTTATTTAGACAGCGGCGAATTAGTAGAAGTGTTGAGCAATGTCGCTATCAGCTACGACGGCTATCATCTCTACTACCCAAATCGCCGCCAAAATTCACCGCTCTTTAAAGCCTTGGTGGCGGCATTGAAAATC","","","33202","MIDNINELRTFITAAQEGSFTKAAAKLNVSTSALSHSIRKLEEQLNIKLFNRTTRSIATTEAGEQLFQNLLPLFESIEDNLNALSTFRNTLKGKLCINGNDHVFLSILWDKLMAFAEQYPEMELELTSDTKFVDIVAGRFDAGIRLGSDVAQDMIAVRLSDKMQMAVVGTPEYFAKKATPKKVEDLGEHECLLVRLPTSDSIMTWEFQPAKKSAPVVKFHPKGQLCFNNSHLISRAVLVGKGLAWLPIDTMQPYLDSGELVEVLSNVAISYDGYHLYYPNRRQNSPLFKALVAALKI","689803","","transcriptional regulator (LysR family)","Cytoplasm","","
InterPro
IPR000847
Domain
Bacterial regulatory protein, LysR
PR00039\"[20-31]T\"[31-41]T\"[41-52]THTHLYSR
PF00126\"[5-64]THTH_1
PS50931\"[3-60]THTH_LYSR
InterPro
IPR005119
Domain
LysR, substrate-binding
PF03466\"[88-296]TLysR_substrate
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[3-89]Tno description


","BeTs to 11 clades of COG0583COG name: Transcriptional regulatorFunctional Class: KThe phylogenetic pattern of COG0583 is a-m----q-drlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 2.5e-15) to 1/1 blocks of the IPB000847 family, which is described as \"Bacterial regulatory protein, LysR family\". Interpro entry for IP:IPR000847. IPB000847 19-52 2.4e-15Significant hit ( 1.3e-08) to 1/2 blocks of the IPB001583 family, which is described as \"NodD transcription activator carboxyl terminal region\". Interpro entry for IP:IPR001583. IPB001583A 7-57 1.2e-08","Residues 254 to 296 match (1e-07) PD:PD242324 which is described as PROTEOME COMPLETE TRANSCRIPTIONAL REGULATOR TRANSCRIPTION DNA-BINDING REGULATION PROBABLE LYSR FAMILY ","","","","","","","","","","","","Thu Dec 19 12:04:45 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00985 is paralogously related to AA00977 (1e-58), AA01794 (2e-12), AA02539 (1e-11), AA00940 (6e-11) and AA01513 (7e-09).","","","","","","Residues 88 to 296 (E-value = 2.1e-27) place AA00985 in the LysR_substrate family which is described as LysR substrate binding domain (PF03466)","","","","","Sperandio V, Li CC, Kaper JB. Quorum-sensing Escherichia coli regulator A: a regulator ofthe LysR family involved in the regulation of the locus ofenterocyte effacement pathogenicity island in enterohemorrhagic E. coli. Infect Immun. 2002 Jun;70(6):3085-93. PMID: 12011002 Colmer JA, Hamood AN. Molecular analysis of the Pseudomonas aeruginosa regulatorygenes ptxR and ptxS. Can J Microbiol. 2001 Sep;47(9):820-8. PMID: 11683464 Colmer JA, Hamood AN. Expression of ptxR and its effect on toxA and regAexpression during the growth cycle of Pseudomonas aeruginosa strain PAO1. Can J Microbiol. 1999 Dec;45(12):1008-16. PMID: 10696480","","Thu Dec 19 12:04:18 2002","1","","","" "AA00987","690646","689885","762","ATGCGCTATCACGAGTCCCTCAAACCCGATCCGATTATTCACGACGCATCGGCGCTACGCCTGGTGCCGCAAATTGATTATGATTTCAGTAAGTTTGACACTGCTATCCGCAGTTCAGTAGGGTCGGCTATTCGCGCTACCTATTTGGATAGCCTCACCAAAGCCTTTATTCAACAGCACCAACAACCGATTATCGTGATGATCGGTTGCGGGCTGGATGCGCGTCATGAGCGTGTGGGTGACATCGGCAAAAATGTGCCGTTCTATGAGCTGGATTTGCCCGATGTGATCGCATTGCGCAAGCAACTGATGCCGCCGGCGGAAAATGAAATTTTGCTTGCCGCGTCGGCGTTTGACACGGATTGGATGGACGAATTACGCTCCACCTATCCGCAGGCACAGTTTTTATTTGTTATTGAAGGCGTATTGATGTATTTCAATGAAGCGCAGGTGAAAAAGCTGTTTGAAGATCTTGCCGTCCGTTTTAGTGGTGGCGAAATCGCCTTTGACATCGGCAGCACTTGGATGAGTCGCAATTCGCAAAAACACCATGACGTGATGAAACATATGCGGGCACAGTTTGATTACGGCTGCGATGATGATCATGAAATGGAACGTTGGGCGGATAATCTCCACCTGATTTCGGCGAAGTATATGTTTGATTTTCCCGCCTGGAAACGTATCGGCTTGTTGCAAGCCGCCATCATGTGGATTGTGCCCTTCGTGCGCAAATCTTATCGTTTCCTGTATTATCGGATAAGT","","","29496","MRYHESLKPDPIIHDASALRLVPQIDYDFSKFDTAIRSSVGSAIRATYLDSLTKAFIQQHQQPIIVMIGCGLDARHERVGDIGKNVPFYELDLPDVIALRKQLMPPAENEILLAASAFDTDWMDELRSTYPQAQFLFVIEGVLMYFNEAQVKKLFEDLAVRFSGGEIAFDIGSTWMSRNSQKHHDVMKHMRAQFDYGCDDDHEMERWADNLHLISAKYMFDFPAWKRIGLLQAAIMWIVPFVRKSYRFLYYRIS","689887","","tetracenomycin polyketide synthesis O-methyltransferase","Cytoplasm","","
InterPro
IPR003455
Domain
O-methyltransferase, N-terminal
PF02409\"[5-78]TOmt_N


","BeTs to 4 clades of COG3315COG name: O-Methyltransferase involved in polyketide biosynthesisFunctional Class: QThe phylogenetic pattern of COG3315 is ----------r-b--fgh---j----Number of proteins in this genome belonging to this COG is","","Residues 8 to 205 match (4e-29) PD:PD039622 which is described as PROTEOME COMPLETE TRANSFERASE METHYLTRANSFERASE TETRACENOMYCIN TCMP POLYKETIDE SYNTHESIS SAV0804 PLASMID ","","","","","","","","","","","","Thu Dec 19 12:12:35 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00987 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 78 (E-value = 9.3e-06) place AA00987 in the Omt_N family which is described as O-methyltransferase N-terminus (PF02409)","","","","","Decker H, Motamedi H, Hutchinson CR.Nucleotide sequences and heterologous expression of tcmG and tcmP, biosynthetic genes for tetracenomycin C in Streptomyces glaucescens.J Bacteriol. 1993 Jun;175(12):3876-86.PMID: 8509339","","Thu Dec 19 12:12:35 2002","1","","","" "AA00988","692324","691038","1287","ATGCAAGGCAAAGTCGCCGAGCGTATCGAACAGTTCAATTTAGGCGGCGAAAGCTATTTAAGCGGCTATCCCGTGTCCTTTTGGGATGTCTTCGGCGAAACCGGCATTCCGCTGCGCACCACCATTTCCGAAATGGGGCCGTTGTTGCTCTCCCGTTTATTGAATTTGAACGCCACCCAAGAAGGCTTGCTCAATCTGGTGTTCCGCGTAGCCGACGACAAAGGCTTATTGCTTATCGACTTAAAAGATCTGCGCGCCATGTTGAAATATGTGGCGGAAAATGCCAAAACCTTCCAAGTGGAATACGGTAATGTATCCGCTGCCAGCGTGGGAGCCATCCAACGGGCATTATTAACTCTGGAAAATGAAGGCGCGGCAAATTTATTCGGCGAACCGGCGCTGAATCTGGAAGACTGGTTGCAAACCCGTGACGGTCGTGGTGTCATCAATGTGTTAAATTCGGAAAAACTGATCAATTCTCCGCGCATGTACAGCGCCTTCCTGCTTTGGTTAATGGCGGAATTATTTGAGCAATTGCCGGAAGTGGGCGACCCCGACAAACCGAAATTCGTCATGTTCTTTGACGAAGCTCACTTGCTGTTCGACGGCGCGCCAAGTGTATTGGTGGATAAAGTGGAACAGGTTGTGCGCCTGATTCGCTCCAAAGGCGTGGGCATTTATTTCGTGACCCAAAACCCGCTGGATTTGCCGGACACCGTGCTTGGGCAATTAGGTAACCGCGTACAACACGCCCTGCGTGCCTTTACGCCGCGTGATCAAAAAGCAGTGAAATCGGCGGCGGAAACTTTCCGCACCAACCTAAAAGTCAACGTGGTGGAAACTATCTCCACCCTTGGCGTGGGGCAAGCGCTGGTCTCTTTCCTGGATGAAAAAGGTATGCCGACACCGGTGGAAATCGCCTACATTTTCCCGCCGAAAAGCCAATTGGCACCGATTAGCGCCGAACAACGCGCCGCATGGGTGAAAGACGACGATTTGTACGCGTTCTATAAAGATTATGTGGATAACGAATCGGCATTTGAAGTGTTAAATGCGCAGGCAGATCTCGCCGCCGTAGCGCAAAAACAGGCGGAACAAGCCAAACAGGAAGAAGAAAACGGCATCATGGGCAGTCTCAGCCGCATGATTTTCGGCACCAAAAAACGCGGCGAACAACTCTCGGTTACCGAACAAGTCGTCAGCAGTGTGGCAAAATCCGTCGGTCGCAATATTCGCAACCAAGTGACAAAACAAATTATGCGCGGTATTCTGGGCGCGTTTAAGAAG","","","54777","MQGKVAERIEQFNLGGESYLSGYPVSFWDVFGETGIPLRTTISEMGPLLLSRLLNLNATQEGLLNLVFRVADDKGLLLIDLKDLRAMLKYVAENAKTFQVEYGNVSAASVGAIQRALLTLENEGAANLFGEPALNLEDWLQTRDGRGVINVLNSEKLINSPRMYSAFLLWLMAELFEQLPEVGDPDKPKFVMFFDEAHLLFDGAPSVLVDKVEQVVRLIRSKGVGIYFVTQNPLDLPDTVLGQLGNRVQHALRAFTPRDQKAVKSAAETFRTNLKVNVVETISTLGVGQALVSFLDEKGMPTPVEIAYIFPPKSQLAPISAEQRAAWVKDDDLYAFYKDYVDNESAFEVLNAQADLAAVAQKQAEQAKQEEENGIMGSLSRMIFGTKKRGEQLSVTEQVVSSVAKSVGRNIRNQVTKQIMRGILGAFKK","691040","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR008571
Family
Protein of unknown function DUF853, NPT hydrolase putative
PF05872\"[1-429]TDUF853


","BeTs to 11 clades of COG0433COG name: Predicted ATPaseFunctional Class: RThe phylogenetic pattern of COG0433 is aompkz-qvdrlbcef-h---j----Number of proteins in this genome belonging to this COG is","","Residues 307 to 429 match (2e-41) PD:PD098708 which is described as PM1435 PROTEOME COMPLETE ","","","","","","","","","","","","Thu Dec 19 12:14:56 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00988 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 429 (E-value = 6.5e-274) place AA00988 in the DUF853 family which is described as Bacterial protein of unknown function (DUF853) (PF05872)","","","","","","","","1","","","" "AA00989","692704","692459","246","TTGCACCTTGCCGATTTTAATGATCAAAATTTCTGCCGTTGCCATCACTTTCCCTGTTATTTTCTAAAATCTGCGGAATTATACCGTAAAAACAACTTATTTTTTGACCGCACTTCTATTTTTAAATATCATGCGGGAAATTTATCCGTCATCAATCAGGAACACTCAACATGCAATATTTACTCGCCCAAACCGAACAAAATCAACAATTCGGCATTTCCGCCAAAATGGCAAACCGCCACGGCT","","","9609","LHLADFNDQNFCRCHHFPCYFLKSAELYRKNNLFFDRTSIFKYHAGNLSVINQEHSTCNIYSPKPNKINNSAFPPKWQTATA","692459","","hypothetical protein","Cytoplasm, Extracellular","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 08:46:42 2004","Wed Feb 25 08:46:42 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA00989 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 08:46:42 2004","","","","","","","","","","","","","1","","","" "AA00990","692699","693325","627","GTGCAACAGCTTACCTTTGCCGACGGTTCGCTGTATGAAAGCGCCATTCGCAAAGTGCCGGTGGAGGCGGTGAAAATTCACTCACTTGGTGCGGAAGGCAATGATGTGGGATTGAAAGCCCATCATGGCGGTGTGGATAAAGCGTTATTTTTTATGTCGGCAGATGCCTTTCCTGCGTTAAATGCGTTATTAGACGAAAATTTTTCGTATCAGGACACAGCAGTTTACGGCGAGAATTTTGTGGTTTCCGCGCTGAATGAAGATTCCGTGTGTGTGGGCGATATTTATCAAATCGGCTCCTGCGTGGTGGAGGTGTCGCAGCCGCGTAAACCTTGTGAGCGCTTATCGAAAAATACCAATAATCCGAACACGCAACAAACCGTGTATCGCTCCGGCTGGTCGGGCTGGTATGTGCGGGTGGTACGCGAGGGGGAAATTCAGCGGGGCGACAAATTAATTTTGCAGGCGCGTCCGCATCCCGACTTTACCATTCGCCATTTGAACCGCTTGCTTTCGGCGCCCGACACGATTAACGAATTGGAACAGGCGTTGGCACTTGAGGTGTTGGCGCCGGCGTTTAAACGCTCGTTGCATTCTCAGCTTACCAAGTTACAACAAAAACAAAGT","","","24646","VQQLTFADGSLYESAIRKVPVEAVKIHSLGAEGNDVGLKAHHGGVDKALFFMSADAFPALNALLDENFSYQDTAVYGENFVVSALNEDSVCVGDIYQIGSCVVEVSQPRKPCERLSKNTNNPNTQQTVYRSGWSGWYVRVVREGEIQRGDKLILQARPHPDFTIRHLNRLLSAPDTINELEQALALEVLAPAFKRSLHSQLTKLQQKQS","693327","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR005163
Domain
Conserved hypothetical porotein YiiM, 3-alpha
PF03475\"[161-206]T3-alpha
InterPro
IPR005302
Domain
Molybdenum cofactor sulphurase, C-terminal
PF03473\"[29-154]TMOSC
InterPro
IPR015808
Domain
Molybdenum cofactor sulphurase, C-terminal-like
G3DSA:2.40.33.20\"[12-202]Tno description


","BeTs to 7 clades of COG2258COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG2258 is ---------dr-b-ef-h--u-----Number of proteins in this genome belonging to this COG is","","Residues 76 to 152 match (2e-09) PD:PD518818 which is described as PROTEOME LIN2166 COMPLETE ","","","","","","","","","","","","Thu Dec 19 12:17:33 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00990 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 161 to 206 (E-value = 8.2e-10) place AA00990 in the 3-alpha family which is described as 3-alpha domain (PF03475)","","","","","","","","1","","","" "AA00991","693331","693801","471","ATGACCGCACTTTTAGATTCCTATTGCCCTTGTCACTCCCATAACACCTATGGGGAATGCTGCGGGCGTTTTCATGCTTACGTGCAGTTTCCCGAAACTACCGAGCAGCTCATGCGCTCGCGCTATGCCGCGTATGTGTTAAAAAATGTGCCTTATATTGTGGAAACCACCGTGCCGAACCAACAAAAGCTGCTGAACGTGCAGGCAATTCAAACCTGGGCGGAAAATACGCAATGGCTTGGCTTACAGATTCTGAATACGGAAACCCTGACGAAGGTGCAAAGTGCGGTGGAATTTAACGCCATTTTTCAGGGCGAAGAAGGTGAGCAGGCGCATCATGAACGTTCGATTTTTGTGAAAATTGACAGGCGTTGGTATTTTGTGGATCCGACGGTGCCGCTACCGACCATGAAACAGCCTTGCATATGCGATTCCGGCAAAAAATTTAAGCATTGTTGCGGAGGATTTTTA","","","18052","MTALLDSYCPCHSHNTYGECCGRFHAYVQFPETTEQLMRSRYAAYVLKNVPYIVETTVPNQQKLLNVQAIQTWAENTQWLGLQILNTETLTKVQSAVEFNAIFQGEEGEQAHHERSIFVKIDRRWYFVDPTVPLPTMKQPCICDSGKKFKHCCGGFL","693803","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR004027
Domain
SEC-C motif
PF02810\"[137-157]TSEC-C


","BeTs to 6 clades of COG3012COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3012 is ---------d----efgh-n------Number of proteins in this genome belonging to this COG is","","Residues 130 to 157 match (1e-08) PD:PD469909 which is described as PROTEOME COMPLETE PM1617 NMB1923 HI0277 ","","","","","","","","","","","","Thu Dec 19 12:19:12 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00991 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 137 to 157 (E-value = 1.8e-07) place AA00991 in the SEC-C family which is described as SEC-C motif (PF02810)","","","","","","","","1","","","" "AA00992","693801","694628","828","ATGATTGATCTAAAAACCTTTTGTGCGTTGTTTTGGCAACGTTTTAATCAAAATAAACTCACGCAAGCCGCCGGTTATCTGACGTACAGCACCATGCTCGCCATTGTGCCGCTGATTATGGTGGTGTTTTCCATCTTCTCCGCTTTTCCGGTTTTTAACGAAGTTACCGGTGCGTTGAAAGAGTTTATTTTTACTAATTTCGCTCCCTCCGCCGGTGACGTGGTGGGGCAATATATTGATGAATTTGTGAATAATTCCAAACAGATGAGTGCGGTGGGTATCATCAGTTTAATTGTGGTGGCATTGATGTTGATTAATTCCATCGACCGCACCCTGAACGGCATTTGGCATGACACCAGTACCCGCCCGATTTTTACCTCTTTTGCGATTTATTGGCTGATTTTGACGTTAGGTCCGCTGTTAGTAGGCACCAGTATTGCCGCCAGTTCTTATGTGAAAACCATGTTTGAGTATTCTGCAGCTTCTTCTTTCGGTTTGAAATTACTCAGTTTTGTGCCGTTTCTTTCCACCTGGTTTATTTTCACCGTGATTTATATGGTGGTGCCGAATAAAAAAGTCAGTATTAAACATTCTGCTGCCGGTGCGCTGATTGCCGCGGTGTTTTTTACGCTGGGTAAGCAGGCATTTGCTTGGTACATTGTGACTTTTCCCTCTTATCAATTAATTTACGGCGCCATGGCGACCTTGCCGATTATGCTGCTATGGATTCAGTTAAGCTGGACTTTCGTGTTGCTCGGCGCACAACTGGCGGCGGTGCTGGCGGAAGTGCGGTCGAAAAAACAAGTAAATCATCAGGAGGTAAAACAG","","","31518","MIDLKTFCALFWQRFNQNKLTQAAGYLTYSTMLAIVPLIMVVFSIFSAFPVFNEVTGALKEFIFTNFAPSAGDVVGQYIDEFVNNSKQMSAVGIISLIVVALMLINSIDRTLNGIWHDTSTRPIFTSFAIYWLILTLGPLLVGTSIAASSYVKTMFEYSAASSFGLKLLSFVPFLSTWFIFTVIYMVVPNKKVSIKHSAAGALIAAVFFTLGKQAFAWYIVTFPSYQLIYGAMATLPIMLLWIQLSWTFVLLGAQLAAVLAEVRSKKQVNHQEVKQ","694630","","ribonuclease BN","Inner membrane, Cytoplasm","","
InterPro
IPR004664
Domain
Ribonuclease BN
PF03631\"[16-264]TRibonuclease_BN
TIGR00765\"[6-263]TyihY_not_rbn: YihY family protein
noIPR
unintegrated
unintegrated
tmhmm\"[33-53]?\"[90-108]?\"[129-149]?\"[168-188]?\"[203-221]?\"[240-260]?transmembrane_regions


","BeTs to 15 clades of COG1295COG name: Predicted multitransmembrane proteinFunctional Class: RThe phylogenetic pattern of COG1295 is -------q-drlbcefghsnujxi--Number of proteins in this genome belonging to this COG is","","Residues 4 to 247 match (1e-89) PD:PD007690 which is described as COMPLETE PROTEOME RIBONUCLEASE BN MEMBRANE HYDROLASE 3.1.-.- BRKB PLASMID INTEGRAL ","","","","","","","","","","","","Thu Dec 19 12:20:58 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00992 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 16 to 264 (E-value = 4e-85) place AA00992 in the Ribonuclease_BN family which is described as Ribonuclease BN-like family (PF03631)","","","","","allahan,C. and Deutscher,M.P. 1996. Identification and characterization of the Escherichia colirbn gene encoding the tRNA processing enzyme RNase BN. J. Bacteriol. 178(24):7329-7332. PubMed: 8955422.","","Thu Dec 19 12:20:58 2002","1","","","" "AA00993","694628","695059","432","GTGATTGCGTTAATTCAACGGGTAACACAGGCGAAAGTGGAAGTCGGTGGCGAAGTGGTCGGGCAAATCGGCAAGGGATTGTTGGTGCTGCTGGGCGTGGAAAAGGATGATGACCGACAAAAAGCGGATAAACTGGCGGAGAAGGTGTTGAATTATCGCGTGTTTAGCGACGCAGATGACAAAATGAATCTGAATGTACAGCAAATCGGCGGCGAATTATTGGTGGTGTCGCAATTTACCTTGGCGGCAGATACGGAAAAAGGGCTACGCCCGAGTTTCTCTAAAGGGGCACCACCGCCGTTGGCAAATGAGCTTTATACGTATTTCGTGCGAAAGTGCGGTGACAAATTAAAGGTAGAATGTGGACGTTTTGCGGCGGATATGCAGGTGAGTTTGGTTAACGACGGTCCCGTCACATTTTGGTTAAGTTGT","","","15700","VIALIQRVTQAKVEVGGEVVGQIGKGLLVLLGVEKDDDRQKADKLAEKVLNYRVFSDADDKMNLNVQQIGGELLVVSQFTLAADTEKGLRPSFSKGAPPPLANELYTYFVRKCGDKLKVECGRFAADMQVSLVNDGPVTFWLSC","695061","","possible D-tyrosyl-tRNA(Tyr) deacylase","Cytoplasm","","
InterPro
IPR003732
Family
D-tyrosyl-tRNA(Tyr) deacylase
PD005653\"[37-142]TDTD_NEIMA_Q9JST7;
G3DSA:3.50.80.10\"[1-144]Tno description
PTHR10472\"[3-144]TD-TYROSYL-TRNA(TYR) DEACYLASE
PF02580\"[2-144]TTyr_Deacylase
TIGR00256\"[1-144]TTIGR00256: D-tyrosyl-tRNA(Tyr) deacylase
noIPR
unintegrated
unintegrated
PTHR10472:SF4\"[3-144]TD-TYROSYL-TRNA(TYR) DEACYLASE


","BeTs to 11 clades of COG1490COG name: D-Tyr-tRNAtyr deacylaseFunctional Class: JThe phylogenetic pattern of COG1490 is ------yqvdrlb-efgh-n------Number of proteins in this genome belonging to this COG is","Significant hit ( 5.6e-80) to 4/4 blocks of the IPB003732 family, which is described as \"DUF154\". Interpro entry for IP:IPR003732. IPB003732A 1-29 2.6e-15 IPB003732B 35-66 5.4e-18 IPB003732C 70-115 1.4e-26 IPB003732D 122-141 2.7e-16","Residues 1 to 143 match (4e-49) PD:PD005653 which is described as D-TYROSYL-TRNATYR 3.1.-.- HYDROLASE DEACYLASE COMPLETE PROTEOME 0610006H08RIK SYNTHETASE I AMINOACYL-TRNA ","","","","","","","","","","","","Thu Dec 19 12:34:12 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00993 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 28 to 144 (E-value = 4.8e-74) place AA00993 in the Tyr_Deacylase family which is described as D-Tyr-tRNA(Tyr) deacylase (PF02580)","","","","","Soutourina J, Blanquet S, Plateau P.D-tyrosyl-tRNA(Tyr) metabolism in Saccharomyces cerevisiae.J Biol Chem. 2000 Apr 21;275(16):11626-30.PMID: 10766779Soutourina,J., Plateau,P., Delort,F., Peirotes,A. and Blanquet,S.Functional characterization of the D-Tyr-tRNATyr deacylase from Escherichia coliJ. Biol. Chem. 274 (27), 19109-19114 (1999)PubMed: 10383414","","Thu Dec 19 12:38:10 2002","1","","","" "AA00994","695228","696433","1206","ATGACTTTCAATACTTTTGAAACCCTCGCATTAGCGGGCTTTGTGCTGTTGCTTGGGTATTTTCTGGTAAAACGTATTTCCTTATTGAAAAGCTATAATATTCCTGAGCCGGTTGTGGGTGGTTTCTTAGTCGCGATTATTCTCACCGTTTTATATCAAGGCTGGGGATTGTCTTTTATGTTTGATACGAATTTGCAGTTCACCATGATGTTGGTATTTTTTTCTTCCATCGGTTTAAGTGCTAACTTTGCGCGCTTGGTAAAAGGTGGTAAACCGTTAATTATTTTTGTGATTGCAGCGACATTATTGATTACTGTACAAAATATCGTGGGTGTAACAGGTTCGGTCTTACTCGGCATCGACCCTGCTTACGGTCTAATTGCCGGTTCGGTCACCTTAACCGGCGGACATGGTACCGGTGCGGCGTGGGCCGGTAAATTAACAGAGTTATTCCACCTTGAAGGCGCCTTGGAATTAGCCATGGCTTGTGCCACCTTTGGTTTGGTCTCCGGTGGTATTATCGGCGGTCCGGTGGCACGCCATTTATTAGGGAAAATGAAACATGGCGAGAATCCGGAAAGCGATGATGTCGATGATGTACAAGAAGCTTTTGAGCACCCTACTTACCAACGTAAAATTACAACCCGCTCACTGATTGAAACGATTACCATGATGACGTGCTGTTTACTTATCGGTCAGTTCTTGGATGCACACACAAAAGGTAGCGTCATTGAATTGCCAACATTCGTATGGTGTCTGTTTACCGGGGTAATCATTCGTAATTCTTTGACCCATATTTTCAAATTTAATGTTGCTGATTCTGCCGTAGATGTTTTGGGTAACGTGGGTCTGTCCTTATTCTTAGCTATTGCATTAATGTCCTTAAAACTATGGCAATTGGCAGGGTTGGCGTTACCGGTCATGGTCATTTTGGCAATTCAGGTTGTTCTTATGGCAGTCTTTGCGGTTTATGTGACTTACCGTATAATGGGTAAAGATTACGACGCAGTAGTATTAAGTGCCGGTCACTGTGGTTTCGGCCTTGGTGCAACACCGACGGCAGTAGCGAACATGCAGGCGGTGACAAGCCGTTTTGGACCGTCACACAAAGCTTTCTTAATTGTACCGATGGTTGGCGCGTTCTTCATTGACTTGGTAAATGCTTCCGTGCTCAAAGTCTTTTTATTTGTGGTATCCGCATTGCAC","","","42992","MTFNTFETLALAGFVLLLGYFLVKRISLLKSYNIPEPVVGGFLVAIILTVLYQGWGLSFMFDTNLQFTMMLVFFSSIGLSANFARLVKGGKPLIIFVIAATLLITVQNIVGVTGSVLLGIDPAYGLIAGSVTLTGGHGTGAAWAGKLTELFHLEGALELAMACATFGLVSGGIIGGPVARHLLGKMKHGENPESDDVDDVQEAFEHPTYQRKITTRSLIETITMMTCCLLIGQFLDAHTKGSVIELPTFVWCLFTGVIIRNSLTHIFKFNVADSAVDVLGNVGLSLFLAIALMSLKLWQLAGLALPVMVILAIQVVLMAVFAVYVTYRIMGKDYDAVVLSAGHCGFGLGATPTAVANMQAVTSRFGPSHKAFLIVPMVGAFFIDLVNASVLKVFLFVVSALH","696435","","sodium/glutamate symport carrier protein (glutamate permease)","Inner membrane, Cytoplasm","","
InterPro
IPR001254
Domain
Peptidase S1 and S6, chymotrypsin/Hap
PS00134\"[339-344]?TRYPSIN_HIS
InterPro
IPR004445
Family
Sodium/glutamate symporter
PD017853\"[364-392]TGLTS_HAEIN_P45240;
PF03616\"[1-367]TGlt_symporter
TIGR00210\"[1-399]TgltS: sodium/glutamate symporter
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[181-331]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-29]?signal-peptide
tmhmm\"[4-22]?\"[37-59]?\"[65-83]?\"[98-118]?\"[124-144]?\"[159-179]?\"[243-263]?\"[278-298]?\"[304-324]?\"[371-391]?transmembrane_regions


","BeTs to 7 clades of COG0786COG name: Na+/glutamate symporterFunctional Class: EThe phylogenetic pattern of COG0786 is -------------cefgh-nu-----Number of proteins in this genome belonging to this COG is","","Residues 2 to 393 match (1e-139) PD:PD017853 which is described as COMPLETE PROTEOME GLUTAMATE SODIUM/GLUTAMATE SYMPORT PERMEASE CARRIER SYMPORTER GLTS SODIUM ","","","","","","","","","","","","Thu Dec 19 12:40:42 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00994 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 367 (E-value = 2.5e-230) place AA00994 in the Glt_symporter family which is described as Sodium/glutamate symporter (PF03616)","","","","","Deguchi,Y., Yamato,I. and Anraku,Y. Nucleotide sequence of gltS, the Na+/glutamate symport carriergene of Escherichia coli B J. Biol. Chem. 265 (35), 21704-21708 (1990) PubMed: 2254324 Kalman,M., Gentry,D.R. and Cashel,M. Characterization of the Escherichia coli K12 gltS glutamate permease gene Mol. Gen. Genet. 225 (3), 379-386 (1991) PubMed: 2017136 ","","Thu Dec 19 12:40:42 2002","1","","","" "AA00995","697736","696495","1242","ATGATAAAGTATCAAAAAGAAATTACAACTTCGATGCGTAACAACCAAATTTCCCGTATTTTAGCAGGAATTCCAAGTTTCCCTAATGATCGATTTACCCCCCATCCTGTACTAATCTCGCCGAGTGGACAAATTCTCGGCGCACTCACTGAAGAAGAAAAATCAGTACGTCAATTTATTTTTAACAACGCTTCATTGGATCAACCGTTAAAAAAAATCTATTCCAATATTCAAATTGTCGGTCCGTTTTCTCTGTACCTAAATCCTGAGCATAATCAATCTTATAGCTTATATTTTGTCAATCAGATCAATGCACAGAAAGAGATCCTAAACTACATTTTTGATCGTCCGTTTTTCCTGATCATCTTGGTCATTTTAATTTCCACACCGTTATTGTGGTGGCTATCACGCAGTATAGGTCAGCCTATTCGTAACCTACAACTTGCAGCAAATGCCGTTGCCATAGGAAATTTAAAAATTAATAAAAATCTTGAAACCAAAGGGTTGATCGAGTTACGTCAAGTAGGACAAAGTTTTAACCGCATGATGCTTTCTCTTGAAGAGGTATTGTCAAATCAGCAATCGTTATTATCTTCTATTTCTCACGAATTAAGAACCCCTCTGACCCGTCTACAACTGGCAACGGCGTTATTGCGTCGTCGCTTAGGCGATAGTAACGAAATTCAGCGTATTGATACGGAAGCACAACGTTTAGATAAAATGGTCAGTGACTTGCTACAGCTTTCCCGTCAACAGCTGAATAGTCATCTGGAAAAAGACATCTTCCCGATACCTTTACTTTGGAAAGAAATTTTAGAAGATGCAAAATTTGAAGCAGCTCAACGAAATATTCGTTTTCACGTGGAGCAAGGCATCGCCCATCCTGAACAGTATTACCTCAATGGTAACCACGGACTTCTTGCAAGTGCGGTGGAAAATATTGTCAGAAATGCGTTGAAATATACAAAATCAGCAATTTCCGTTCACATCTATACTCATGAAAATGACTTATTTATTCGCATTGAAGATAACGGTGCAGGCTTACCGGAAGATGAATATGAAAAAATCTTTAAGCCGTTTTATCGCGTTGATGAAACGCGTACCCGCGAAACCGGTGGCACCGGCTTAGGCTTATCCATTGTTGCCAATACAGCGAAGGACCATCACGGCGCAGTCTGGGCAGGGAAAGCTGATCTGGGTGGCTTAGCCGTTATCTTACGCTTACCACTTTGGGTGGCAAAA","","","53074","MIKYQKEITTSMRNNQISRILAGIPSFPNDRFTPHPVLISPSGQILGALTEEEKSVRQFIFNNASLDQPLKKIYSNIQIVGPFSLYLNPEHNQSYSLYFVNQINAQKEILNYIFDRPFFLIILVILISTPLLWWLSRSIGQPIRNLQLAANAVAIGNLKINKNLETKGLIELRQVGQSFNRMMLSLEEVLSNQQSLLSSISHELRTPLTRLQLATALLRRRLGDSNEIQRIDTEAQRLDKMVSDLLQLSRQQLNSHLEKDIFPIPLLWKEILEDAKFEAAQRNIRFHVEQGIAHPEQYYLNGNHGLLASAVENIVRNALKYTKSAISVHIYTHENDLFIRIEDNGAGLPEDEYEKIFKPFYRVDETRTRETGGTGLGLSIVANTAKDHHGAVWAGKADLGGLAVILRLPLWVAK","696497","","sensory transduction protein for cpxR/basR","Inner membrane, Cytoplasm","","
InterPro
IPR000215
Family
Proteinase inhibitor I4, serpin
PS00284\"[112-122]?SERPIN
InterPro
IPR003594
Domain
ATP-binding region, ATPase-like
G3DSA:3.30.565.10\"[259-410]Tno description
PF02518\"[302-411]THATPase_c
SM00387\"[302-412]THATPase_c
InterPro
IPR003660
Domain
Histidine kinase, HAMP region
PF00672\"[117-188]THAMP
SM00304\"[137-191]THAMP
PS50885\"[137-191]THAMP
InterPro
IPR003661
Domain
Histidine kinase A, N-terminal
PF00512\"[192-254]THisKA
SM00388\"[192-254]THisKA
InterPro
IPR004358
Domain
Histidine kinase related protein, C-terminal
PR00344\"[337-351]T\"[355-365]T\"[372-390]TBCTRLSENSOR
InterPro
IPR005467
Domain
Histidine kinase
PS50109\"[199-412]THIS_KIN
noIPR
unintegrated
unintegrated
G3DSA:1.10.287.240\"[182-250]Tno description
PTHR23283\"[45-50]T\"[111-410]TSENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF23\"[45-50]T\"[111-410]TSENSORY TRANSDUCTION HISTIDINE KINASE (BACTERIAL SENSOR PROTEIN)
tmhmm\"[118-136]?transmembrane_regions


","BeTs to 18 clades of COG0642COG name: Signal transduction histidine kinaseFunctional Class: TThe phylogenetic pattern of COG0642 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 4.2e-15) to 3/4 blocks of the PR00344 family, which is described as \"Bacterial sensor protein C-terminal signature\". Prints database entry for PR:PR00344. PR00344A 337-351 0.018 PR00344B 355-365 0.017 PR00344C 372-390 1.6e-06Significant hit ( 7.2e-13) to 3/3 blocks of the IPB003661 family, which is described as \"His Kinase A domain\". Interpro entry for IP:IPR003661. IPB003661A 200-209 1.3e-05 IPB003661B 313-322 0.042 IPB003661C 341-349 0.21Significant hit ( 1e-08) to 3/3 blocks of the IPB003660 family, which is described as \"HAMP domain\". Interpro entry for IP:IPR003660. IPB003660A 135-153 1.3e+02 IPB003660B 307-318 0.48 IPB003660C 367-382 4e-05","Residues 224 to 264 match (6e-08) PD:PD253602 which is described as PROTEOME KINASE PHOSPHORYLATION CPXA COMPLETE SENSORY TRANSFERASE TRANSDUCTION ","","","","","","","","","","","","Tue Feb 4 14:00:43 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00995 is paralogously related to AA01843 (6e-17), AA00757 (2e-13) and AA02284 (1e-04).","","","","","","Residues 302 to 411 (E-value = 5.6e-33) place AA00995 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase (PF02518)","","","","","Shimohata N, Chiba S, Saikawa N, Ito K, Akiyama Y. The Cpx stress response system of Escherichia coli sensesplasma membrane proteins and controls HtpX, a membraneprotease with a cytosolic active site. Genes Cells. 2002 Jul;7(7):653-62. PMID: 12081643 De Wulf P, McGuire AM, Liu X, Lin EC. Genome-wide profiling of promoter recognition by thetwo-component response regulator CpxR-P in Escherichia coli. J Biol Chem. 2002 Jul 19;277(29):26652-61. PMID: 11953442","","Thu Dec 19 14:05:09 2002","1","","","" "AA00997","698620","697928","693","ATGGCTAAAATTTTACTTGTTGATGATGATGCGGAGCTCACCGAACTGTTAGCACAATTACTCGATTTAGAAGGCTTTCAGGTGAATGTCGCAAACAATGGTAAAGAAGCATTGGAATTGCTTGACCATAGTTATGATCTCATCTTATTAGATATTATGATGCCGGTCTTAAACGGTATCGAAACATTAAAACAAATCAGAAAAAACTATTCCACGCCGGTCATGATGCTGACTGCCCGCGGTGATGATATTGATCGTATTTTAGGTCTTGAATTAGGTGCGGACGACTACCTACCGAAGCCGTTTAATGATCGTGAATTGGTTGCGCGAATTAAAGCGATTTTAAGACGTACAGCACAGGCAAATAACGCGAAAGATCCGACAGATGTGGATAAAATCGAGTTCGGCGGCATCGTATTTTATCCGGGACGCCAACAGGCAATGCTGGGTTCAAAAGATCTTGAACTCACCGGCACCGAGTTTGCTTTATTACTAAAACTTATTACTCATCCCGGGTTAATTCTGACTCGTGAAGAGTTAAGTCTTGAAGTTTTGGGCAAGCCACTTACGCCTTTCGATCGTGCCATTGATATGCATATGTCGAATTTACGAAAAAAATTACCGGCTCGCTCCGATGATCTACCATGGTTTAAAACACTTCGTGGTCGCGGTTATTTATTAATAGCGGAAAAA","","","25966","MAKILLVDDDAELTELLAQLLDLEGFQVNVANNGKEALELLDHSYDLILLDIMMPVLNGIETLKQIRKNYSTPVMMLTARGDDIDRILGLELGADDYLPKPFNDRELVARIKAILRRTAQANNAKDPTDVDKIEFGGIVFYPGRQQAMLGSKDLELTGTEFALLLKLITHPGLILTREELSLEVLGKPLTPFDRAIDMHMSNLRKKLPARSDDLPWFKTLRGRGYLLIAEK","697930","","response regulatory protein","Cytoplasm","","
InterPro
IPR001789
Domain
Response regulator receiver
PD000039\"[25-116]TQ9CJV4_PASMU_Q9CJV4;
PF00072\"[2-112]TResponse_reg
SM00448\"[2-111]TREC
PS50110\"[3-115]TRESPONSE_REGULATORY
InterPro
IPR001867
Domain
Transcriptional regulatory protein, C-terminal
PD000329\"[135-228]TQ9CJV4_PASMU_Q9CJV4;
PF00486\"[151-227]TTrans_reg_C
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2300\"[3-137]Tno description
PTHR23283\"[3-117]TSENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF21\"[3-117]TTWO-COMPONENT SYSTEM SENSOR HISTIDINE KINASE/RESPONSE REGULATOR (INTESTINAL BACTERIA - BACTEROIDES THETAIOTAOMICRON)


","BeTs to 15 clades of COG0745COG name: Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domainFunctional Class: T,KThe phylogenetic pattern of COG0745 is -------qvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.7e-54) to 4/4 blocks of the IPB001867 family, which is described as \"Transcriptional regulatory protein, C terminal\". Interpro entry for IP:IPR001867. IPB001867A 46-59 2.1e-05 IPB001867B 73-117 6.4e-33 IPB001867C 154-185 8.9e-10 IPB001867D 213-227 0.046Significant hit ( 4.6e-16) to 3/3 blocks of the IPB001789 family, which is described as \"Response regulator receiver domain\". Interpro entry for IP:IPR001789. IPB001789A 4-10 1.3 IPB001789B 46-59 4e-06 IPB001789C 93-102 1.1e-05Significant hit ( 3.4e-05) to 2/6 blocks of the IPB000673 family, which is described as \"CheB methylesterase\". Interpro entry for IP:IPR000673. IPB000673B 18-71 0.015 IPB000673C 71-101 1","Residues 138 to 228 match (6e-33) PD:PD000329 which is described as DNA-BINDING COMPLETE PROTEOME TRANSCRIPTION REGULATOR SENSORY TRANSDUCTION REGULATION PHOSPHORYLATION RESPONSE ","","","","","","","","","","","","Tue Feb 4 14:01:47 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00997 is paralogously related to AA02902 (1e-33), AA01837 (1e-17), AA00959 (2e-11), AA00757 (2e-08) and AA02283 (2e-04).","","","","","","Residues 151 to 227 (E-value = 4.1e-16) place AA00997 in the Trans_reg_C family which is described as Transcriptional regulatory protein, C terminal (PF00486)","","","","","Raffa RG, Raivio TL. A third envelope stress signal transduction pathway inEscherichia coli. Mol Microbiol. 2002 Sep;45(6):1599-611. PMID: 12354228 Shimohata N, Chiba S, Saikawa N, Ito K, Akiyama Y. The Cpx stress response system of Escherichia coli sensesplasma membrane proteins and controls HtpX, a membraneprotease with a cytosolic active site. Genes Cells. 2002 Jul;7(7):653-62. PMID: 12081643 De Wulf P, McGuire AM, Liu X, Lin EC. Genome-wide profiling of promoter recognition by thetwo-component response regulator CpxR-P in Escherichia coli.J Biol Chem. 2002 Jul 19;277(29):26652-61. PMID: 11953442 Otto K, Silhavy TJ. Surface sensing and adhesion of Escherichia coli controlledby the Cpx-signaling pathway. Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):2287-92. PMID: 11830644 ","","Thu Dec 19 14:06:49 2002","1","","","" "AA00998","699075","698665","411","ATGCAATTCAGATCTGTCGTAACCGCACTTATTTTCACGCTCAGTGTTACCGCCTGTTCCACCGTCAATAAAGTCGTTTATCGTATTGATGTGCCACAAGGTAACTATTTGGAAGCCTCAAAAGTTACACAATTAAAAACCGGCATGACAGCCCAACAGGTTCAGTATTTACTCGGTACGCCGGTTCTCATCGATCCTTACAGTAACCACACCTGGTATTATGTTTACTTACAACAAAAAGCCTATGAAACGCCGGAACAGCACACTCTGGTCGTAAATTTTGACCAAAATGGTACCGTAAGCAACTTTGACTTGGACAAACCGTTACCGAATGACGATAAAGTCGAAGTGAATAATACCATTATCACAGCACCTGACGCTCAAGCTAAGCGTTGGTGGCAATTCTGGAAA","","","15735","MQFRSVVTALIFTLSVTACSTVNKVVYRIDVPQGNYLEASKVTQLKTGMTAQQVQYLLGTPVLIDPYSNHTWYYVYLQQKAYETPEQHTLVVNFDQNGTVSNFDLDKPLPNDDKVEVNNTIITAPDAQAKRWWQFWK","698667","From GenBank (gi:8039800):This protein is attached to the outer membrane by a lipid anchor (By similarity).","small protein A homolog","Outer membrane, Periplasm","","
InterPro
IPR007450
Domain
SmpA/OmlA
PF04355\"[19-104]TSmpA_OmlA
noIPR
unintegrated
unintegrated
PS51257\"[1-19]TPROKAR_LIPOPROTEIN
signalp\"[1-21]?signal-peptide


","BeTs to 7 clades of COG2913COG name: Small protein A (tmRNA-binding)Functional Class: JThe phylogenetic pattern of COG2913 is --------------efghsn-jx---Number of proteins in this genome belonging to this COG is","","Residues 1 to 62 match (4e-19) PD:PD012701 which is described as LIPOPROTEIN PROTEOME COMPLETE MEMBRANE OUTER SMALL A SIGNAL PRECURSOR OMLA ","","","","","","","","","","","Fri Jan 24 13:17:00 2003","Fri Jan 24 13:15:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA00998 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 19 to 104 (E-value = 3e-37) place AA00998 in the SmpA_OmlA family which is described as SmpA / OmlA family (PF04355)","","","","","Miczak,A., Chauhan,A.K. and Apirion,D. Two new genes located between 2758 and 2761 kilobase pairs onthe Escherichia coli genome J. Bacteriol. 173 (11), 3271-3272 (1991) PubMed: 2045357 ","","Thu Dec 19 14:33:11 2002","1","","","" "AA01001","700034","699144","891","ATGATGTTGCAGCTACACCAAGGCTATCAAAACAAAGCGAAAGGTTATGGTATTTTCCTGGACTCCTCGGTGTTTGCCCAAAGTCTGAATCGCTTGTTGGAAAATGAACTGGAATTCCTGCCGTTCAGCTATGAAGCAACGAATTTATTGATTAACGAACTGAGTAAATATAATTTTGCCGATAGCGGCACTTTGGTTTTATGCCAATATAATTTTCTCGCCACCGATTACCTGTTTATCGCGTTATTGGACAGTCGTGTCAGTATGTTGGTGGATGACAAATTGGAAATTCAGCGTACCGAATATTTAGACATCACCCAATTTGATGTGGCAGCACGTATTAATTTAACCGACCTGCAACTTAATGCCAATTCCAATCGTTACTTAACCTTCATCAAAGGGCGCGTCGGGCGCAAAATCGCGGACTTCTTTATGGATTTTCTGGGTGCGGAAGAAGGGCTTAACCCGCAAGTACAAAATCAATGTTTATTACAGGCGGTGAGTGATTACTGCGCACAAGGCGAGTTAAATCGTGAACAAACCCAAGCGGTAAAAAAACAGGTGTTTGAATACTGCAAAGGACAGATAAATAACGGCGAAGACATTGAACTTACGGAACTTTCCGGCGAGCTGCCGACTCTAAACCAACAACCTTTTGCCGAGTTTACTCAAGCGCAAAATTACGGCTTGGAAGAAAATATACCGCCGGTTCGCACCGCACTTAAGTCGCTCACGAAATTCTCCGGTTCCGGCAAAGGAGTGACCATCAGTTTTGATGCGGAGTTAATTAATCAACGTATCATTTGGGATGAAGCCGCAGATACGCTTACAATCAAAGGGCTTCCGCCAAATTTACGCGATCAGTTGCAGCGCCAGTTAAAAGAACAGAAT","","","38724","MMLQLHQGYQNKAKGYGIFLDSSVFAQSLNRLLENELEFLPFSYEATNLLINELSKYNFADSGTLVLCQYNFLATDYLFIALLDSRVSMLVDDKLEIQRTEYLDITQFDVAARINLTDLQLNANSNRYLTFIKGRVGRKIADFFMDFLGAEEGLNPQVQNQCLLQAVSDYCAQGELNREQTQAVKKQVFEYCKGQINNGEDIELTELSGELPTLNQQPFAEFTQAQNYGLEENIPPVRTALKSLTKFSGSGKGVTISFDAELINQRIIWDEAADTLTIKGLPPNLRDQLQRQLKEQN","699146","","conserved hypothetical protein","Cytoplasm, Outer membrane","","
InterPro
IPR007358
Family
37kDa nucleoid-associated bacterial protein
PF04245\"[1-294]TNA37


","BeTs to 4 clades of COG3081COG name: Nucleoid-associated proteinFunctional Class: RThe phylogenetic pattern of COG3081 is --------------efgh--------Number of proteins in this genome belonging to this COG is","","Residues 147 to 287 match (7e-37) PD:PD583862 which is described as PROTEOME COMPLETE NUCLEOID-ASSOCIATED STY1607 NUCLEOID-ASOCIATED NUCLEOIDS NUCLEOTIDE SPERMIDINE PROTEIN ASSOCIATED ","","","","","","","","","","","","Thu Dec 19 14:33:51 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01001 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 294 (E-value = 2e-192) place AA01001 in the NA37 family which is described as 37-kD nucleoid-associated bacterial protein (PF04245)","","","","","","","","1","","","" "AA01003","700260","700514","255","ATGCGGCATTTTAAATCGGCAGACCAACCAAACATGGCAATTCAATCAAAATATCAAGATAAACAAATAGATGAAATTCTCAACGACATGATTGCAGTGCTGGAAAAACACCAAGCGCCGCTGGATTTATCCTTAATCGTGTTAGGCAATATGACCACCAATTTACTGCTCGGCAGTGTCGGAAAACAGCAACGACAAGTGCTGGCAAAAGCCTTCTCCGACGCTTTGCTGAACTCTCTTAATACGACGAACCAA","","","9463","MRHFKSADQPNMAIQSKYQDKQIDEILNDMIAVLEKHQAPLDLSLIVLGNMTTNLLLGSVGKQQRQVLAKAFSDALLNSLNTTNQ","700516","","conserved hypothetical protein","Cytoplasm, Extracellular","","
InterPro
IPR009857
Family
Protein of unknown function DUF1414
PIRSF006188\"[12-85]TUncharacterised conserved protein
PF07208\"[12-80]TDUF1414
noIPR
unintegrated
unintegrated
PD027794\"[33-81]TQ9CJV7_PASMU_Q9CJV7;


","BeTs to 3 clades of COG3082COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3082 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 12 to 80 match (2e-18) PD:PD027794 which is described as PROTEOME COMPLETE CYTOPLASMIC YPO1261 STY2465 YEJL HI0840 VC2040 PM1884 ","","","","","","","","","","","","Thu Dec 19 14:35:00 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01003 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 12 to 80 (E-value = 4.4e-42) place AA01003 in the DUF1414 family which is described as Protein of unknown function (DUF1414) (PF07208)","","","","","","","","1","","","" "AA01005","700522","702258","1737","ATGTGGAAATTTAACAGCAAACAATATCGAGAAGAAACCTCGCAAAAAATTTCGTGGGGGCACTGGTTTGCTTTTTTTAATATTCTGTGGGCGATTTTTATCGGCGCCCGTTATGCTTTTATTATCGACTGGCCCGACACCTTATTCGGTAAAGTGTATTTTTTCATCAGTTTATTAGGGCATTTCAGTTTTATTGTTTTCGCCTTTTATCTGCTGGTGATTTTCCCCCTCAGTTTTATCGTCAAAAACCACCGCACTTTTCGCGGTCTGACCGTTATTCTTGCGACCATTAGCAACACCTTATTATTAGTGGATACGGAAGTTTTTGTTCGCTTTAATCTTCACCTTTCCTCCTTAGTCTGGAATTTACTGGTGAATCCGGAAAACGGTGAACTCTCCCGCAACTGGCAACTTTTTTTCGTACCTATGCCGTTGATTTTATTAATACAAATGCTATTTTCACGTTGGTCTTGGCAAAAATTACGCAGTTTAGAACGGCAAAAATGGCTGAAAGGCATAGGCATCTTTTTTGTTTGCACATTTAGTGCCACCCACCTGATTTATGCGTGGGCGGATGCTTATTTGTATCGTCCGATTACGATGCAGCGTTCCAATTTTCCGTTGTCCTATCCGATGACTGCCCGCTCATTATTAGAAAAGCGTGGTTTTATCAACAAGCGGGAATACGCCGAACGGTTGGCACAGGAAGGCCGCTTGGATGCGTTGGCGATTGAATATCCTAAAAAGCCACTGACGTTTGATGAGCCGATGGAGAAGCAAAATATCATTCTGATTACCATTTCCGGGCTGCGTTATGATGCCATTAATGAAAAGAGCATGCCGAATTTAGCACGGTTCACCACCGATTCCACGCAATTTACCAATCATTACAGTAGCGGAAATAACAATAACGCCGGGTTAACAGGCCTATTTTATGGTTTGAATGCAAATTATACCGACAGCTTATTGAGCAGCAAAATCCCTTCCGCACTGGTTGAACACATAACGCAACAGAAATACGTGCAAGGGCTGTTTTCCGGCAGGAAGTTTAATTCCAGCATTTTACGGCGTGCGATTTATCAGCAAACCAAACTGATCGGTGACACTTCCAATCAAGGGGCAGTAAATGCTTTTCAACATTGGCTGGAGACGGCAAAAACGCAGGAAAAACCGTTCTGGGGCTATTTGAGCTTGGATATTAAACCGAATTTATCACCGGAAAATTATGCGCAGGAACGTACCAAAATTGATGAATTATTAGGGCAGATTTTGCCGCAATTGGATTTACCTAATACCCTGGTGATTATTACTGCTGAGCATGGCTATACCTTCCGGCAGCTCACGGAGAAAGAGGAAAATCGCTATTTCGCCCAAGATAAAGTGCGGGTGCCGATGATCGTACATTGGCAAGGTTTGGCGAAAGGTAAAGTGACAAAATTAACCTCTCATGTGGATGTGCTGCCGGCGTTAATGAAACACGTTTTCAAGGTGAGAAATCCGATTGGCGATTACGCGCAGGGACGTGATTTGTTTGACTTGAATCAGACCCCGGATTGGGTTTTGGTGTCTAATTATCGCTGGAATGTGATTATTCAGCCGGATGGCACGCAATATCATATTGATACGCGCGGAAACTATCAAAAATATGACCGCACTTATCAGAAAATTTCCTCTAAAAGACCGCCATTAGGGCTGTTTTTGGAAGTGTTTAATCAAGAGCGTTCATTTTTAGAAAAA","","","67627","MWKFNSKQYREETSQKISWGHWFAFFNILWAIFIGARYAFIIDWPDTLFGKVYFFISLLGHFSFIVFAFYLLVIFPLSFIVKNHRTFRGLTVILATISNTLLLVDTEVFVRFNLHLSSLVWNLLVNPENGELSRNWQLFFVPMPLILLIQMLFSRWSWQKLRSLERQKWLKGIGIFFVCTFSATHLIYAWADAYLYRPITMQRSNFPLSYPMTARSLLEKRGFINKREYAERLAQEGRLDALAIEYPKKPLTFDEPMEKQNIILITISGLRYDAINEKSMPNLARFTTDSTQFTNHYSSGNNNNAGLTGLFYGLNANYTDSLLSSKIPSALVEHITQQKYVQGLFSGRKFNSSILRRAIYQQTKLIGDTSNQGAVNAFQHWLETAKTQEKPFWGYLSLDIKPNLSPENYAQERTKIDELLGQILPQLDLPNTLVIITAEHGYTFRQLTEKEENRYFAQDKVRVPMIVHWQGLAKGKVTKLTSHVDVLPALMKHVFKVRNPIGDYAQGRDLFDLNQTPDWVLVSNYRWNVIIQPDGTQYHIDTRGNYQKYDRTYQKISSKRPPLGLFLEVFNQERSFLEK","702260","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR000917
Domain
Sulfatase
PF00884\"[407-515]TSulfatase
InterPro
IPR001952
Family
Alkaline phosphatase
G3DSA:3.40.720.10\"[258-555]Tno description
InterPro
IPR012159
Family
Membrane sulphatase, HI0842-related
PIRSF004950\"[8-579]TPredicted membrane sulfatase, HI0842 type
noIPR
unintegrated
unintegrated
PTHR10342\"[409-488]TSULFATASE
signalp\"[1-39]?signal-peptide
tmhmm\"[21-41]?\"[55-75]?\"[90-112]?\"[138-158]?\"[173-191]?transmembrane_regions


","BeTs to 4 clades of COG3083COG name: Predicted hydrolase of alkaline phosphatase superfamilyFunctional Class: RThe phylogenetic pattern of COG3083 is --------------efgh--------Number of proteins in this genome belonging to this COG is","","Residues 420 to 467 match (9e-08) PD:PD492914 which is described as PROTEOME COMPLETE HI0842 PM1883 ","","","","","","","","","","","","Thu Dec 19 14:35:46 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01005 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 258 to 553 (E-value = 2.8e-06) place AA01005 in the Sulfatase family which is described as Sulfatase (PF00884)","","","","","","","","1","","","" "AA01006","702520","703506","987","ATGACGAAGAATCATGTTCGGAGTTTCAAAACCTATATTCGAGATGAAATTATTAAAAAAGGTGGCTGGGTTAATGCACATGCGCATGCCGATCGCGCTTTTACCATGACCCCGGAAAAAATCGGGATTTATCACAGCAGTAATTTGCAGCAAAAATGGGACTTGGTGGACGAGGTAAAACGCACCTCCTCCGTGGATGATTATTACGCCCGTTTTTGTCAATCTATCGAATTGATGATTTCCCAAGGGGTTACGGCGTTCGGTACCTTTGTGGATATTGACCCGGTGTGTGAAGATCGCGCCATTATTGCCGCCCACAAAGCGCGCGAAGTGTATAAAAATGACATTATCCTGAAATTCGCCAACCAAACGTTGAAAGGCGTGATTGAACCGACGGCACGCAAATGGTTCGACATCGGTTCGGAAATGGTGGATATGATCGGTGGCTTGCCTTATCGTGATGAATTAGATTACGGACGCGGTTTGGACGCCATGGATATTTTGTTGGATAAAGCCAAGTCTCTCGGCATTATGTGCCATGTGCATGTGGATCAGTTCAATTCGCCGCAGGAAAAAGAAACGGAGCAGTTATGCGATAAAGCCATTGAACATGGTATGCAAGGTCGGGTGGTGGCGATTCACGGTATTTCTATCGGTTCGCATTCCAAAGAATATCGCTATCGTTTATATGAAAAAATGCGTCAGGCGCAAATGATGATGATTGCCTGTCCGATGGCATGGATTGATAGTAACCGAAAAGAGGAACTGATGCCGTTCCATAATGCACTCACGCCGGCGGATGAAATGATTCCGGAAGGCATTACGGTAGCGATTGGTACAGATAATATTTGCGATTACATGGTGCCTTTATGTGAAGGCGATATGTGGCAGGAGCTGAGCTTGCTGGCGGCAGGTTGCCGCTTCCCGGATTTGGATGCCATGGTGAATATTGCCAGCATCAACGGGCGTAAAGTGTTGGGCATTGAT","","","41768","MTKNHVRSFKTYIRDEIIKKGGWVNAHAHADRAFTMTPEKIGIYHSSNLQQKWDLVDEVKRTSSVDDYYARFCQSIELMISQGVTAFGTFVDIDPVCEDRAIIAAHKAREVYKNDIILKFANQTLKGVIEPTARKWFDIGSEMVDMIGGLPYRDELDYGRGLDAMDILLDKAKSLGIMCHVHVDQFNSPQEKETEQLCDKAIEHGMQGRVVAIHGISIGSHSKEYRYRLYEKMRQAQMMMIACPMAWIDSNRKEELMPFHNALTPADEMIPEGITVAIGTDNICDYMVPLCEGDMWQELSLLAAGCRFPDLDAMVNIASINGRKVLGID","703508","","conserved hypothetical protein (possible cytosine deaminas)","Cytoplasm","","
noIPR
unintegrated
unintegrated
PD049525\"[287-329]TY843_HAEIN_P44059;
G3DSA:3.20.20.140\"[22-327]Tno description


","BeTs to 7 clades of COG0402COG name: Cytosine deaminase and related metal-dependent hydrolasesFunctional Class: F,RThe phylogenetic pattern of COG0402 is aompkzyqvd--bcef-hs-uj----Number of proteins in this genome belonging to this COG is","Significant hit ( 7.6e-07) to 3/6 blocks of the IPB002604 family, which is described as \"Chlorohydrolase\". Interpro entry for IP:IPR002604. IPB002604A 21-30 2.8 IPB002604C 172-185 29 IPB002604E 268-281 0.0032","Residues 287 to 329 match (9e-17) PD:PD049525 which is described as PROTEOME COMPLETE HI0843 ","","","","","","","","","","","","Thu Dec 19 14:42:08 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01006 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01008","704473","703610","864","ATGAAAAAAATGATCCCAAATGCCTTTTGTGTTAGGATCCGAAACCCTTTTTTAACTAATTTTGAACATAAAATGACCTATTCTATTCATGATTTTACCCAACTCATTGCCCAACTGCGTGATCCCGAACACGGTTGTCCGTGGGATATTAAACAGACCTACCAATCCATGATTCCATGCCTGAAAGAAGAAGCCTACGAAATTATTGAAGCCATTGAACAAAACAATGTGGAAAATCTTAAGGAAGAATTGGGCGATTTACTTTTACAAGTGGTCTTTCTCAGTCAATTAGCAGCGGAGGAGAAAAAGTTTACCTTTGATCAAGTCGTACAAGACGTTGCGGAAAAAATCGTGCGTCGCCATCCCCACGTGTTCGGTGACAAGCATGCCAATAATGAACAGGAAGCCTTACAGAATTGGAATGCCATGAAAGCGCAGGAGCATCAAAATCAAGGTTACACCTCCATTTTAGATAACATTCCGCATGCCTTTCCCGCCTTAATGCGAGCAGAAAAATTGCAAAAACGCTGTGCCAAAGTCGGCTTTGACTGGAAAGACATTGCACCGGTTTTTGCCAAAGTGGAAGAGGAATTACAGGAAGTGAAACAGGAAATGGAACGCTCTCCGCAAGATCAACAGAAAATCGAAGAAGAAATGGGCGATTTGTTATTTGCTACCGTCAATTTAAGCCGTCATTTGAAATGTCAGGCGGAAGAAAGCCTAAGCAAAGCGAACCAAAAATTTGAACAACGCTTTCGTCGCGTAGAAGAAAAATTAAAGCAACAACATCGTTCTTTGGAAGACGCGTCTCTGGTCGAAATGGATCTGTTATGGGATGAAGTGAAGCAGGAAGAAAAACACCGC","","","33958","MKKMIPNAFCVRIRNPFLTNFEHKMTYSIHDFTQLIAQLRDPEHGCPWDIKQTYQSMIPCLKEEAYEIIEAIEQNNVENLKEELGDLLLQVVFLSQLAAEEKKFTFDQVVQDVAEKIVRRHPHVFGDKHANNEQEALQNWNAMKAQEHQNQGYTSILDNIPHAFPALMRAEKLQKRCAKVGFDWKDIAPVFAKVEEELQEVKQEMERSPQDQQKIEEEMGDLLFATVNLSRHLKCQAEESLSKANQKFEQRFRRVEEKLKQQHRSLEDASLVEMDLLWDEVKQEEKHR","703612","","mazG beta-lactamase regulatory protein homolog","Cytoplasm","","
InterPro
IPR004518
Domain
NTP pyrophosphohydrolase MazG, putative catalytic core
PF03819\"[52-125]T\"[185-252]TMazG
InterPro
IPR011551
Domain
NTP pyrophosphohydrolase MazG, bacterial
TIGR00444\"[35-282]TmazG: MazG family protein
InterPro
IPR012199
Family
NTP pyrophosphohydrolase MazG
PIRSF002844\"[31-286]TNucleoside triphosphate pyrophosphohydrolase MazG
InterPro
IPR012231
Family
NTP pyrophosphohydrolase MazG duplicated
PIRSF500056\"[1-288]TNucleoside triphosphate pyrophosphohydrolase MazG, duplicated domain type


","BeTs to 14 clades of COG1694COG name: Predicted pyrophosphataseFunctional Class: RThe phylogenetic pattern of COG1694 is a---kz-qvdrlbcefghs--j-it-Number of proteins in this genome belonging to this COG is","","Residues 244 to 286 match (1e-07) PD:PD013792 which is described as PROTEOME COMPLETE MAZG YABN ORTHOLOG UROPORPHYRINOGEN-III MLL0404 STY3083 YPO3378 PROTEIN ","","","","","","","","","","","","Thu Dec 19 14:46:13 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01008 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 185 to 252 (E-value = 6.9e-05) place AA01008 in the MazG family which is described as MazG nucleotide pyrophosphohydrolase domain (PF03819)","","","","","","","","1","","","" "AA01009","704583","705005","423","ATGTACAAACATGTGTTAGTTGCGGTTGATCTTTCAGAAGAAAGTGCGTTCTTGTTGAAAAAAGCGGTCGGCGTGGCAAAGCGTTATGATGCGAAGTTATCCATTATTCATGTGGATGTTAACTTCTCGGATCTTTACACAGGGCTTATTGACGTAAATATGGTATCAATGCAGGATCGCATTTCCAGCGAAACCCAACAGGCGTTGATCAAACTCGCCGAACAAGCGGGTTACCCGATCACCGAAAAACTCAGTGGTAGTGGGGATTTAGGGCAAGTGTTAGCCGATGCCATCGACAAATATGATGTGGACTTACTTGTCACCGGCCACCACCAAGACTTTTGGAGTAAATTGATGTCATCCACCCGTCAGGTGATGAATTCAATTACTGTTGATATGCTTGTTGTTCCTCTTCGTGACGAA","","","15869","MYKHVLVAVDLSEESAFLLKKAVGVAKRYDAKLSIIHVDVNFSDLYTGLIDVNMVSMQDRISSETQQALIKLAEQAGYPITEKLSGSGDLGQVLADAIDKYDVDLLVTGHHQDFWSKLMSSTRQVMNSITVDMLVVPLRDE","705007","","universal stress protein A","Cytoplasm","","
InterPro
IPR006016
Domain
UspA
PF00582\"[1-137]TUsp
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620\"[1-141]Tno description


","BeTs to 9 clades of COG0589COG name: Universal stress protein UspA and related nucleotide-binding proteinsFunctional Class: TThe phylogenetic pattern of COG0589 is aompkzyq-drlbcefgh-n-jx---Number of proteins in this genome belonging to this COG is","Significant hit ( 7e-07) to 3/3 blocks of the PR01438 family, which is described as \"Universal stress protein signature\". Prints database entry for PR:PR01438. PR01438A 2-20 0.0029 PR01438B 100-112 8.2 PR01438C 115-137 10","Residues 2 to 138 match (8e-13) PD:PD016172 which is described as PROTEOME YECG COMPLETE ","","","","","","","","","","","","Fri Jan 24 13:17:59 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01009 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 137 (E-value = 7.3e-16) place AA01009 in the Usp family which is described as Universal stress protein family (PF00582)","","","","","ystrom,T. and Neidhardt,F.C. Cloning, mapping and nucleotide sequencing of a gene encodinga universal stress protein in Escherichia coli Mol. Microbiol. 6 (21), 3187-3198 (1992) PubMed: 1453957 Freestone,P., Nystrom,T., Trinei,M. and Norris,V. The universal stress protein, UspA, of Escherichia coli is phosphorylated in response to stasis J. Mol. Biol. 274 (3), 318-324 (1997) PubMed: 9405142 ","","Thu Dec 19 14:50:56 2002","1","","","" "AA01010","705313","705179","135","ATGTCGGGTCATTTTCCGGAACCAAAGAACTACTTGCTACAACTTGATGCCCCTTGCTATGGAAAAAATCAAGATATGATTGTCGGATTTGTGCTGTTGTCTTCATTTACAAGCCTTGCTTTCTTAAAATATCTT","","","5080","MSGHFPEPKNYLLQLDAPCYGKNQDMIVGFVLLSSFTSLAFLKYL","705179","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
tmhmm\"[26-44]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 09:09:59 2004","Wed Feb 25 09:09:59 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01010 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 09:09:59 2004","","","","","","","","","","","","","1","","","" "AA01011","705289","707829","2541","TTGGTTCCGGAAAATGACCCGACATTACTGTTTACCAATGCGGGAATGAACCAATTTAAAAATGTTTTTTTAGGTTTGGAAAAACGCCCTTATAGCCGTGCCACTACCGCTCAACGCTGTGTGCGTGCCGGAGGAAAACATAATGATTTAGAAAATGTGGGTTACACAGCCAGACATCATACATTCTTTGAAATGCTCGGAAACTTCAGTTTTGGGGATTATTTTAAACAGGACGCGATCCACTTCGGTTGGGAATTTTTAACTTCCCCGCAATGGTTGGGATTACCGAAAGAAAGATTATGGGTCACCGTGTACGAAACCGATGAAGAAGCCTATAAAATTTGGCATGATGAAATCGGCATTGTGGCAGAACGCATTATTCGTATTGGCGATAACAAAGGCGCGCCTTATGCTTCCGATAATTTCTGGCAAATGGGCGATACCGGTCCTTGCGGTCCTTGTACCGAAATTTTCTACGATCATGGCGATCACATTTGGGGCGGACCGCCGGGATCGCCGGAAGAAGATGGCGATCGTTACATTGAAATCTGGAATATCGTGTTCATGCAATTTAATCGCCATGCCGATGGCACCATGGAAAAATTGCCGAAGCCTTCTGTGGATACCGGTATGGGCTTGGAGCGAATCAGTGCGGTGTTGCAACATGTGAATTCCAACTACGATATTGATATTTTCCAAAAATTAATTGCTAAAACGGCGGAATTAACCGGTGAAAAAGATTTAACCAATAAGTCTTTACGTGTGATTGCCGACCACATTCGTTCTTGCGCCTATTTAATCGTAGACGGTGTGGTACCTTCCAACGAAGGACGTGGCTATGTGCTGCGCCGTATTATTCGCCGCGCTGTGCGTCACGGGCATTTATTGGGTGCCGCCGAAGCGTTTTTCTATAAGCTCGTGCCAACCTTAATTGAAGTGATGGCGCAGGCGGGCGAAGAAGTGAAAAAACACCAAGCCACTGTGGAGAAATTGCTGCGTTTGGAAGAAGAACAATTTGCGCGTACGCTGGAACGTGGTTTAACCTTATTAGATGAGGCTTTAGCTGAGGTGAAAGGCAAGGTATTATCCGGCGAAGTGGCGTTCAAGTTATATGATACTTACGGTTTCCCGCTGGATTTAACTGCCGATGTTTGTCGTGAACGCGGCATTACCATCGATGAGGCGGGATTTGAACGCGAGATGGAAAATCAACGTTTGCGCGCGCAGTCCGCCAGCCAATTCGGTATGGATTATAACAATGTTATTCGTGTTGATGGCATAACCCGTTTTGAAGGCTATACTGAATCGGAAACGCTGGCAAAAGTGACCGCACTTTTCCATGACGGCAAACCGGTAGATACCATCAGTTCCGGTCAAAGTGCGGTGGTGATTTTAGATAATACGCCATTCTATGCGGAATCCGGTGGTCAAATCGGAGACATCGGGCGCTTAGAAGGCAACGGTTTTAATTTTGACGTAAAAGACACCCAAAAATATGGTCAGGTATTCGGTCATATCGGTGAACTTACCCAAGGTAGTTTATCCGTCGGGCAGTCCGTGAATGCAGTGGTTGACGAGGTTCGCCGTCAACGTATTTCATTAAATCACTCTGCAACCCATTTGTTGCACGCCGCGTTACGTCAGGTCTTAGGCGAACACGTCGCTCAGAAAGGATCGCTTGTTTCTGATGCATTATTGCGTTTTGACTTTGCTCAACATGAACCTATCAGTAAAGCGCAATTAGCCGAAGTAGAACGCATAGTTAATCAGCAAGTTAGAGCGAATAACCCGATTAAAACGGATATTATGGAGCTGGAAGCCGCCAAAGCGAAAGGTGCGATGGCGTTGTTCGGCGAGAAATATTCCGATCAAGTACGCGTACTAACTATGGGAGATTTTTCCATTGAATTATGTGGTGGGATCCATGCGAAACGTACCGGCGACATCGGGCTGTTTAAAATAGTAACGGAAACGGCAGTGGCGGCAGGCATTCGTCGTATTGAGGCGATTACCGGTGAAACTGCAATCGAATGGTTACAAAACCAACAATCTTTATTAAATCAAAGCGCCGAGTTACTGAAATCGGATGTTAATTCCATTACGGATAAGATTTCTCTGTTGCAAGATAAATTTAAGAAAGTTGAAAAAGAGCTACAAACATTAAAAGAAAAAGCTGCGCTGCAAGCCGGTAATGACCTGGCACAAAGTGCGGTGAAAATTAATGGTGTTTCTGTCATTGCGCAACAACTTGATGGTATTGAAGCGAAGTCTTTACGTTCAATGGTCGATAGCCTGAAAAATCAATTAGGTTCGGCAGTGATTGTATTTGCTTCCGTAGTAGATGAAAAAGTTAATCTTATTGTAGGGGTAACTCAGGATCTGACAGGGAAAGTAAAAGCCGGCGAATTAGTGAATTTGATGGCTCAACAAGTTGGCGGTAAAGGCGGTGGTCGTCCTGATATGGCCATGGCCGGCGGTACTCAGCCGGAAAATGTAAACAAAGCGTTATCGGTTTGCTCCGATTGGTTGAAAGCGAATTTA","","","96518","LVPENDPTLLFTNAGMNQFKNVFLGLEKRPYSRATTAQRCVRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKQDAIHFGWEFLTSPQWLGLPKERLWVTVYETDEEAYKIWHDEIGIVAERIIRIGDNKGAPYASDNFWQMGDTGPCGPCTEIFYDHGDHIWGGPPGSPEEDGDRYIEIWNIVFMQFNRHADGTMEKLPKPSVDTGMGLERISAVLQHVNSNYDIDIFQKLIAKTAELTGEKDLTNKSLRVIADHIRSCAYLIVDGVVPSNEGRGYVLRRIIRRAVRHGHLLGAAEAFFYKLVPTLIEVMAQAGEEVKKHQATVEKLLRLEEEQFARTLERGLTLLDEALAEVKGKVLSGEVAFKLYDTYGFPLDLTADVCRERGITIDEAGFEREMENQRLRAQSASQFGMDYNNVIRVDGITRFEGYTESETLAKVTALFHDGKPVDTISSGQSAVVILDNTPFYAESGGQIGDIGRLEGNGFNFDVKDTQKYGQVFGHIGELTQGSLSVGQSVNAVVDEVRRQRISLNHSATHLLHAALRQVLGEHVAQKGSLVSDALLRFDFAQHEPISKAQLAEVERIVNQQVRANNPIKTDIMELEAAKAKGAMALFGEKYSDQVRVLTMGDFSIELCGGIHAKRTGDIGLFKIVTETAVAAGIRRIEAITGETAIEWLQNQQSLLNQSAELLKSDVNSITDKISLLQDKFKKVEKELQTLKEKAALQAGNDLAQSAVKINGVSVIAQQLDGIEAKSLRSMVDSLKNQLGSAVIVFASVVDEKVNLIVGVTQDLTGKVKAGELVNLMAQQVGGKGGGRPDMAMAGGTQPENVNKALSVCSDWLKANL","707831","","alanyl-tRNA synthetase (alanine--tRNA ligase)","Cytoplasm","","
InterPro
IPR002318
Family
Alanyl-tRNA synthetase, class IIc
PR00980\"[48-59]T\"[181-192]T\"[208-221]T\"[254-270]T\"[278-291]TTRNASYNTHALA
PF01411\"[1-528]TtRNA-synt_2c
TIGR00344\"[1-826]TalaS: alanyl-tRNA synthetase
PS50860\"[1-681]TAA_TRNA_LIGASE_II_ALA
InterPro
IPR003156
Domain
Phosphoesterase, DHHA1
PF02272\"[771-841]TDHHA1
InterPro
IPR012947
Domain
Threonyl/alanyl tRNA synthetase, SAD
PF07973\"[625-668]TtRNA_SAD
noIPR
unintegrated
unintegrated
PTHR11777\"[8-847]TALANYL-TRNA SYNTHETASE


","No hits to the COGs database.","Significant hit (5.5e-191) to 11/12 blocks of the IPB003156 family, which is described as \"DHHA1 domain\". Interpro entry for IP:IPR003156. IPB003156B 46-76 5.9e-34 IPB003156C 141-156 2.2e-13 IPB003156D 178-193 6.7e-14 IPB003156E 202-215 1.9e-09 IPB003156F 255-292 2.1e-34 IPB003156G 335-346 1.2e-06 IPB003156H 370-381 2.5e-08 IPB003156I 470-480 1.7e-07 IPB003156J 536-589 6.1e-34 IPB003156K 617-627 7e-05 IPB003156L 633-650 1.7e-11 IPB003156C 144-159 0.025","Residues 536 to 844 match (3e-09) PD:PD568391 which is described as LIGASE PROTEOME COMPLETE TRUNCATED ALANINE-TRNA ","","","","","","","","","","","","Thu Dec 19 14:52:56 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01011 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 771 to 841 (E-value = 3.8e-20) place AA01011 in the DHHA1 family which is described as DHHA1 domain (PF02272)","","","","","Putney,S.D., Royal,N.J., Neuman de Vegvar,H., Herlihy,W.C., Biemann,K. and Schimmel,P. Primary structure of a large aminoacyl-tRNA synthetase Science 213 (4515), 1497-1501 (1981) PubMed: 7025207 ","","Thu Dec 19 14:52:22 2002","1","","","" "AA01012","707955","708134","180","ATGCTGATCTTAACCCGGAAAGTTGGTGAAAGCTTGCTCATCGGCGATGATGTTTCTATCACGATTCTGAATATACGAGGTAACCAAGTCAAAATCGGTGTGCAGGCGCCGAAGGATGTTTCTATTCATAGAGAAGAAATTTACCAACGTATTCATCAAGCAAGGGATGAACAGAAAGCG","","","6790","MLILTRKVGESLLIGDDVSITILNIRGNQVKIGVQAPKDVSIHREEIYQRIHQARDEQKA","708136","","probable carbon storage regulator homolog","Cytoplasm","","
InterPro
IPR003751
Family
Carbon storage regulator
PD009007\"[1-51]TCSRA_PASMU_P57934;
PF02599\"[1-60]TCsrA
TIGR00202\"[1-60]TcsrA: carbon storage regulator


","BeTs to 10 clades of COG1551COG name: Carbon storage regulator (could also regulate swarming and quorum sensing)Functional Class: TThe phylogenetic pattern of COG1551 is --------v---b-efghs-u---t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1e-33) to 1/1 blocks of the IPB003751 family, which is described as \"Carbon storage regulator\". Interpro entry for IP:IPR003751. IPB003751 2-55 7.8e-34","Residues 1 to 51 match (2e-16) PD:PD009007 which is described as REGULATOR STORAGE CARBON PROTEOME COMPLETE HOMOLOG RNA-BINDING SECONDARY GLOBAL RSMAPM ","","","","","","","","","","","","Thu Dec 19 14:59:14 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01012 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 60 (E-value = 1e-32) place AA01012 in the CsrA family which is described as Global regulator protein family (PF02599)","","","","","Suzuki K, Wang X, Weilbacher T, Pernestig AK, Melefors O, Georgellis D, Babitzke P, Romeo T.Regulatory circuitry of the CsrA/CsrB and BarA/UvrY systems of Escherichia coli.J Bacteriol. 2002 Sep;184(18):5130-40.PMID: 12193630Baker CS, Morozov I, Suzuki K, Romeo T, Babitzke P. CsrA regulates glycogen biosynthesis by preventing translation of glgC in Escherichia coli.Mol Microbiol. 2002 Jun;44(6):1599-610.PMID: 1206738 Gudapaty S, Suzuki K, Wang X, Babitzke P, Romeo T.Regulatory interactions of Csr components: the RNA binding protein CsrA activates csrB transcription in Escherichia coli.J Bacteriol. 2001 Oct;183(20):6017-27.PMID: 1156700210 Tatarko M, Romeo T.Disruption of a global regulatory gene to enhance central carbon flux into phenylalaninebiosynthesis in Escherichia coli.Curr Microbiol. 2001 Jul;43(1):26-32.PMID: 11375660","","Thu Dec 19 14:59:14 2002","1","","","" "AA01013","708169","709530","1362","ATGACTAAACTGACTTGCTTTAAAGCTTATGATATCCGTGGTCGCTTGGGTGATGAATTAAACACAGATATTGTTTATCGCATAGGTCATGCATTCGGGCAGTTTTTAACGCCCAAAACGATTGTCGTTGGTGGCGATGTTCGCTTAACGAGTAAAGAGTTAAAAAGTGCGGTAACAAATGGATTATTGGATTCAGGTGTTAATGTAATTGATTTAGGTGAAACGGGGACAGAGGAAGTCTATTTTGCTACATCATTTTTGAAAACTGACGGTGGTATTGAAGTGACCGCAAGCCACAACCCGATGGACTACAACGGCTTAAAATTAGTGCGTGAAGGGTCCCGTCCGATTAGCGCGGATACCGGGTTGGCGGATATTCAACGTCTGGCGGAGGAAAATAATTTCCCGCCGGTGACCAAACGCGGCGAGTATAAACAACTTTCCGTACTTGATGATTATGTTGAGCACCTCTTATCTTATATTAATCTCGATTCGCTAAAACCGTTGAAGTTAGTGATTAACTCAGGTAATGGCGCCGCAGGGCACGTGATTGATGCGATTGAAGCGCAATTTAAAACAAAACACATACCTGTCGAGTTCATCAAAGTACATAATAATCCGGACGGCACCTTCCCGCACGGTATTCCTAATCCGTTGTTGCATGAAAACCGCCAGGATACCATTGATGCGGTGCTAAAACACAAGGCGGATATGGGCATTGCGTTTGATGGCGATTTCGACCGTTGCTTCCTGTTTGATGAGCACGCAAATTTCATTGAAGGTTATTACATTGTTGGCTTGTTAGGTCAGGCATTCCTGCAAAAAAACCAAGGTGCGAAAATTATTTATGACCCGCGCTTAATCTGGAATACGGTGAAATTAGTGGAAGAAAACGGTGGTGAAGCCGTGATGTCGAAATCCGGACATTCTTTCATTAAAGAAAAAATGCGCGCTGTCGATGCCATTTATGGCGGTGAAATGAGTGCACACCATTATTTCCGTGACTTCTTCTATTGCGACAGCGGCATGATTCCATGGTTGTTGGTGATGGAATTGGTTTCCGTTACCGGTAAATCCCTGAGTGAACTGGTGAATAATAGCGTGAATACATTCCCGCCTCCCGGGGAAATTAATAGCAAATTAGTCGATGCAAAAAGCGCCATTGCCCGCGTGCTCGCCGCTTATGAAAAAGACGCTATTCGCGTAGATGAAATTGACGGCATTAGCATTGAATATCCGAACTGGCGTTTCAACCTGCGTTCATCAAATACCGAGCCGGTCGTTCGTTTGAACCTGGAAACCCGTGGCGATAAGCAATTAATGGCGGAAAAAACAGAAGAAATTCTGGCGTTATTACGTCAA","","","50515","MTKLTCFKAYDIRGRLGDELNTDIVYRIGHAFGQFLTPKTIVVGGDVRLTSKELKSAVTNGLLDSGVNVIDLGETGTEEVYFATSFLKTDGGIEVTASHNPMDYNGLKLVREGSRPISADTGLADIQRLAEENNFPPVTKRGEYKQLSVLDDYVEHLLSYINLDSLKPLKLVINSGNGAAGHVIDAIEAQFKTKHIPVEFIKVHNNPDGTFPHGIPNPLLHENRQDTIDAVLKHKADMGIAFDGDFDRCFLFDEHANFIEGYYIVGLLGQAFLQKNQGAKIIYDPRLIWNTVKLVEENGGEAVMSKSGHSFIKEKMRAVDAIYGGEMSAHHYFRDFFYCDSGMIPWLLVMELVSVTGKSLSELVNNSVNTFPPPGEINSKLVDAKSAIARVLAAYEKDAIRVDEIDGISIEYPNWRFNLRSSNTEPVVRLNLETRGDKQLMAEKTEEILALLRQ","709532","","phosphomannomutase","Cytoplasm","","
InterPro
IPR001969
Active_site
Peptidase aspartic, active site
PS00141\"[61-72]?ASP_PROTEASE
InterPro
IPR005841
Family
Phosphoglucomutase/phosphomannomutase
PR00509\"[91-105]T\"[168-187]T\"[207-220]T\"[236-251]TPGMPMM
PS00710\"[92-101]TPGM_PMM
InterPro
IPR005843
Domain
Phosphoglucomutase/phosphomannomutase C-terminal
PF00408\"[376-454]TPGM_PMM_IV
InterPro
IPR005844
Domain
Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain I
PF02878\"[4-137]TPGM_PMM_I
InterPro
IPR005845
Domain
Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain II
PF02879\"[151-258]TPGM_PMM_II
InterPro
IPR005846
Domain
Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain III
PF02880\"[260-371]TPGM_PMM_III
noIPR
unintegrated
unintegrated
G3DSA:3.40.120.10\"[3-145]T\"[170-252]T\"[253-370]Tno description
PTHR22573\"[250-445]TPHOSPHOHEXOMUTASE FAMILY MEMBER
PTHR22573:SF6\"[250-445]TPHOSPHOMANNOMUTASE


","BeTs to 26 clades of COG1109COG name: PhosphomannomutaseFunctional Class: GThe phylogenetic pattern of COG1109 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 273 to 338 match (1e-07) PD:PD551910 which is described as PHOSPHOMANNOMUTASE PROTEOME COMPLETE ","","","","","Tue Feb 18 15:25:23 2003","","","","","","","Thu Dec 19 15:06:32 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01013 is paralogously related to AA00636 (5e-24) and AA00452 (2e-07).","","","","","","Residues 376 to 454 (E-value = 2.4e-26) place AA01013 in the PGM_PMM_IV family which is described as Phosphoglucomutase/phosphomannomutase, C-terminal domain (PF00408)","","","","","Jensen,S.O. and Reeves,P.R.Molecular evolution of the GDP-mannose pathway genes (manB andmanC) in Salmonella entericaMicrobiology 147 (Pt 3), 599-610 (2001)PubMed: 11238967Aoyama,K., Haase,A.M. and Reeves,P.R.Evidence for effect of random genetic drift on G+C content afterlateral transfer of fucose pathway genes to Escherichia coli K-12Mol. Biol. Evol. 11 (6), 829-838 (1994)PubMed: 7815923Stevenson,G., Andrianopoulos,K., Hobbs,M. and Reeves,P.R.Organization of the Escherichia coli K-12 gene cluster responsiblefor production of the extracellular polysaccharide colanic acidJ. Bacteriol. 178 (16), 4885-4893 (1996)PubMed: 8759852","","Tue Feb 18 15:25:23 2003","1","","","" "AA01014","709609","710493","885","ATGAAAGCGATTATTCCTGTTGCAGGCTTAGGTACACGTATGTTACCTGCTACTAAAGCCATTCCGAAAGAAATGTTAACTTTAGTGGATAAACCGCTAATCCAATATGTGGTAAATGAATGTGTCGCCGCCGGTATTAAAGAAATCGTCCTGGTGACTCATTCCTCAAAAAATGCCATAGAAAACCATTTTGATACTTCCTTCGAATTGGAAACGATGCTGGAAAAACGCGTAAAACGCCAATTATTGGAAGAAGTGCGTTCCATCGTGCCCAAAAATGTCACAATCATGCACGTTCGCCAAGGTAATGCGAAAGGGTTGGGGCATGCCGTATTGTGCGGTCGTCCGCTGGTGGGTAACGAGCCTTTTGCCGTGGTGTTGCCGGATGTGTTGCTGGCCGAGTTTTCCGCTAATCAGAAAAAAGAAAATCTGGCGTTAATGTTAAAACGCTTTAAACAAACCCAAGCCAGCCAAATCATGGTGAACCCGGTTAAACCTGAAGAAGTCAGCAGTTACGGTATCGCCGACTGTGGTGGTGTGGAAATTCCTCCGGGTGAAAGTGCCAAAATTGATAGTATCGTAGAGAAACCAAGTGTGGATGAAGCACCGTCTAATTTGGCTGTTGTAGGGCGTTATGTGTTCTCGGCAACCATTTGGGATTTATTGGAAAAGACCCCGGTGGGCGTGGGCGATGAAATCCAGTTAACCGATGCCATTGATATGCTGATTGATAAGGAAACCGTCGAAGCCTTCCACATGACAGGCATTTCTTACGACTGCGGCGATAAAATCGGTTATATGAAAGCCTTTGTGGAGTACGGGCTGCACCACAATAAACTTGCCAGTGAATTTAAAGCTTACCTCAAAGATTTGGTGAAAACATTT","","","32406","MKAIIPVAGLGTRMLPATKAIPKEMLTLVDKPLIQYVVNECVAAGIKEIVLVTHSSKNAIENHFDTSFELETMLEKRVKRQLLEEVRSIVPKNVTIMHVRQGNAKGLGHAVLCGRPLVGNEPFAVVLPDVLLAEFSANQKKENLALMLKRFKQTQASQIMVNPVKPEEVSSYGIADCGGVEIPPGESAKIDSIVEKPSVDEAPSNLAVVGRYVFSATIWDLLEKTPVGVGDEIQLTDAIDMLIDKETVEAFHMTGISYDCGDKIGYMKAFVEYGLHHNKLASEFKAYLKDLVKTF","710495","","UTP-glucose-1-phosphate uridylyltransferase","Cytoplasm, Periplasm","","
InterPro
IPR005771
Family
UTP--glucose-1-phosphate uridylyltransferase, bacterial and archaeal type
TIGR01099\"[1-269]TgalU: UTP-glucose-1-phosphate uridylyltrans
InterPro
IPR005835
Domain
Nucleotidyl transferase
PF00483\"[2-280]TNTP_transferase
noIPR
unintegrated
unintegrated
G3DSA:3.90.550.10\"[2-281]Tno description
PTHR22572\"[9-73]T\"[96-290]TSUGAR-1-PHOSPHATE GUANYL TRANSFERASE
PTHR22572:SF14\"[9-73]T\"[96-290]TGLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE


","No hits to the COGs database.","","Residues 2 to 76 match (2e-19) PD:PD408709 which is described as COMPLETE PROTEOME URIDYLYLTRANSFERASE UTP-GLUCOSE-1-PHOSPHATE NUCLEOTIDYLTRANSFERASE TRANSFERASE UTP--GLUCOSE-1-PHOSPHATE GALU ","","","","","","","","","","","","Thu Dec 19 15:40:42 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01014 is paralogously related to AA02646 (4e-12).","","","","","","Residues 2 to 280 (E-value = 5.3e-12) place AA01014 in the NTP_transferase family which is described as Nucleotidyl transferase (PF00483)","","","","","Boels IC, Ramos A, Kleerebezem M, de Vos WM. Functional analysis of the Lactococcus lactis galU and galEgenes and their impact on sugar nucleotide andexopolysaccharide biosynthesis. Appl Environ Microbiol. 2001 Jul;67(7):3033-40. PMID: 11425718 Mollerach M, Garcia E. The galU gene of Streptococcus pneumoniae that codes for aUDP-glucose pyrophosphorylase is highly polymorphic andsuitable for molecular typing and phylogenetic studies. Gene. 2000 Dec 30;260(1-2):77-86. PMID: 11137293 Nesper J, Lauriano CM, Klose KE, Kapfhammer D, Kraiss A, ReidlJ. Characterization of Vibrio cholerae O1 El tor galU and galEmutants: influence on lipopolysaccharide structure,colonization, and biofilm formation. Infect Immun. 2001 Jan;69(1):435-45. PMID: 11119535 Dean CR, Goldberg JB. Pseudomonas aeruginosa galU is required for a completelipopolysaccharide core and repairs a secondary mutation in aPA103 (serogroup O11) wbpM mutant. FEMS Microbiol Lett. 2002 May 7;210(2):277-83. PMID: 12044687 ","","Thu Jan 23 07:55:45 2003","1","","","" "AA01015","710651","710965","315","ATGGCGGATTGGAACGGACAATATATTAGTCCTTATGCGGAACACGGAAAAAAAAGCGAACAAGTTAAAAAAATCACGGTATCCATTCCGATTAAAGTGCTTGAAATTCTGACCAACGAGCGTACCCGCCGTCAAATTCGTAATTTACGCCATGCCACCAACAGCGAACTGCTGTGTGAAGCCTTCTTGCACGCCTTTACCGGTCAACCTTTGCCAACGGATGAGGATCTGTTAAAAGAACGCAGTGACGAAATCCCGGAAGAAGCAAAAGTTATTATGCGCACACTGGGAATTGACCCGGATAATTGGGAATAT","","","14825","MADWNGQYISPYAEHGKKSEQVKKITVSIPIKVLEILTNERTRRQIRNLRHATNSELLCEAFLHAFTGQPLPTDEDLLKERSDEIPEEAKVIMRTLGIDPDNWEY","710967","","met repressor","Cytoplasm","","
InterPro
IPR002084
Family
Methionine repressor MetJ
PD020365\"[2-105]TMETJ_PASMU_Q9CLE7;
G3DSA:1.10.140.10\"[2-105]Tno description
PIRSF003191\"[1-105]TMet repressor
PF01340\"[2-105]TMetJ


","BeTs to 3 clades of COG3060COG name: Transcriptional regulator of met regulonFunctional Class: E,KThe phylogenetic pattern of COG3060 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","Significant hit ( 7.2e-92) to 4/4 blocks of the IPB002084 family, which is described as \"Methionine repressor (MetJ)\". Interpro entry for IP:IPR002084. IPB002084A 2-30 4e-29 IPB002084B 31-52 5.8e-20 IPB002084C 58-82 4.3e-24 IPB002084D 83-105 5.8e-15","Residues 2 to 105 match (2e-47) PD:PD020365 which is described as REPRESSOR MET PROTEOME COMPLETE METJ METHIONINE REGULON DNA-BINDING REGULATION TRANSCRIPTION ","","","","","","","","","","","","Thu Dec 19 15:42:55 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01015 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 105 (E-value = 5.2e-82) place AA01015 in the MetJ family which is described as Met Apo-repressor, MetJ (PF01340)","","","","","Merlin C, Gardiner G, Durand S, Masters M. The Escherichia coli metD locus encodes an ABC transporterwhich includes Abc (MetN), YaeE (MetI), and YaeC (MetQ). J Bacteriol. 2002 Oct;184(19):5513-7. PMID: 12218041 He YY, Garvie CW, Elworthy S, Manfield IW, McNally T,Lawrenson ID, Phillips SE, Stockley PG. Structural and functional studies of an intermediate on thepathway to operator binding by Escherichia coli MetJ. J Mol Biol. 2002 Jun 28;320(1):39-53. PMID: 12079333 Liu R, Blackwell TW, States DJ. Conformational model for binding site recognition by theE.coli MetJ transcription factor. Bioinformatics. 2001 Jul;17(7):622-33. PMID: 11448880 ","","Thu Dec 19 15:42:55 2002","1","","","" "AA01017","711055","711786","732","ATGCGAGTGCCTCGAATTTACCATCCAATCCCGCTTAATCAGCACACAACCTGCGCGCTTTCAGAAGACGGCGCCAATCATGTCGGTCGTGTCTTGCGTATGCGGGCAGGCGATCAACTTGAACTTTTCGATGGTAGCAACCATATATATCAAGCCGTCATTACCGCCGTCGCGAAAAAATCCGTTGAAGTGGATATTTTAAGTCGCCAATTTGACGATCGCGAAAGCCCGTTAGCCATCCATTTAGGACAAGTCATTTCCCGTGGCGAACGCATGGAATTTACCATTCAGAAGTCCGTTGAATTAGGGGTGAATGTGATTACGCCATTATGGTCGGAACGTTGCGGTGTGAAATTAGACGGCGAGCGGATGGATAAAAAAATTCAGCAATGGCAGAAAATCGCCATTGCCGCCTGTGAACAATGCGGGCGCAATAAAATCCCGGAAATTCGTCCGTTAATGAAATTACAACAATGGTGTGCGGAGCCTAATGACGCGCTCAAATTGAATTTACATCCGAGAGCACGCTATTCCATTCGCACCTTGCCTGAAATCCCGGCAGCGGGTGTGCGTTTATTAATTGGTTCGGAAGGCGGTTTATCACCACAGGAAATCGCACAAACCGAGCAACAGGGATTTGTGGACGTGTTATTGGGAAAACGAGTATTACGCACCGAAACCGCCGCTATGGCGGCAATTACCGCCTTGCAGGTGTGTTTCGGTGATTTAGGA","","","27150","MRVPRIYHPIPLNQHTTCALSEDGANHVGRVLRMRAGDQLELFDGSNHIYQAVITAVAKKSVEVDILSRQFDDRESPLAIHLGQVISRGERMEFTIQKSVELGVNVITPLWSERCGVKLDGERMDKKIQQWQKIAIAACEQCGRNKIPEIRPLMKLQQWCAEPNDALKLNLHPRARYSIRTLPEIPAAGVRLLIGSEGGLSPQEIAQTEQQGFVDVLLGKRVLRTETAAMAAITALQVCFGDLG","711788","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR006700
Family
Protein of unknown function DUF558, methyltransferase predicted
PF04452\"[18-238]TDUF558
TIGR00046\"[1-244]TTIGR00046: conserved hypothetical protein T
noIPR
unintegrated
unintegrated
G3DSA:2.40.240.20\"[1-73]Tno description
G3DSA:3.40.1280.10\"[74-242]Tno description
PIRSF015601\"[5-243]TPredicted methyltransferase, slr0722 type


","BeTs to 17 clades of COG1385COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG1385 is -------qvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is","","Residues 31 to 132 match (3e-42) PD:PD081730 which is described as PROTEOME COMPLETE YQEU VC0469 MYPU_5420 SP1781 CYTOPLASMIC PA0419 OPERON MLL6903 ","","","","","","","","","","","","Thu Dec 19 15:43:57 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01017 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 132 to 237 (E-value = 7.9e-45) place AA01017 in the DUF558 family which is described as Protein of unknown function (DUF558) (PF04452)","","","","","","","","1","","","" "AA01018","711803","712360","558","ATGATGGATTTACAAGATCACTTGCTGATTGCCATGCCCAATTTAGATGACAGCTATTTTTATCGCACGGTCATTTATATTTGCGAGCATAATGAAAAAGGTTCCATGGGGTTGGTGTTAAACCAGCCGACGGATTTAAGCATTGCGGAGCTGGGCGCCAAAATGAATTTCATGATGGTTACCCACCGCACTTATAACGATAAACTGGTGCTTGCCGGTGGACCGGTGAATATCGATCGCGGCTTTATTTTGCATACCAACACCAAAGTGCCTTTTGATCACAGTTATCGGGTCAGCGACAACCTCATGCTCACCACCTCCGCAGATGTGGTGGACACCTTTGGGACGATGTTAGAACCGGAAAAATACCTGGTGACGCTAGGCTGTGCCAGTTGGGAAGCCAATCAGCTTGAACAGGAAATCATGAATAATTCCTGGTTAGTTGTGCCGGCAACGGAACAAATCCTATTTGATTTGCCTTATGAACAACGTTGGTGGGCGGCGAATCAATTATTAGGCATTGATTCCCATAATTTCGCCGGTCAGGTGGGGCACAGT","","","21086","MMDLQDHLLIAMPNLDDSYFYRTVIYICEHNEKGSMGLVLNQPTDLSIAELGAKMNFMMVTHRTYNDKLVLAGGPVNIDRGFILHTNTKVPFDHSYRVSDNLMLTTSADVVDTFGTMLEPEKYLVTLGCASWEANQLEQEIMNNSWLVVPATEQILFDLPYEQRWWAANQLLGIDSHNFAGQVGHS","712362","","conserved hypothetical protein (possible transcriptional regulator)","Cytoplasm","","
InterPro
IPR003774
Family
Protein of unknown function DUF179
PF02622\"[2-186]TDUF179


","BeTs to 10 clades of COG1678COG name: Putative transcriptional regulatorFunctional Class: KThe phylogenetic pattern of COG1678 is ---------dr---efghsn-jxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 4e-37) to 4/4 blocks of the IPB003774 family, which is described as \"DUF179\". Interpro entry for IP:IPR003774. IPB003774A 20-39 9.2e-14 IPB003774B 73-84 3.3e-05 IPB003774C 105-124 0.0013 IPB003774D 125-147 9.8e-10","Residues 8 to 151 match (6e-08) PD:PD036073 which is described as PROTEOME COMPLETE L7913.02 ML0028 FUNCTION PREDICTED F14M2.10 CAB72194.1 RV0038 ","","","","","","","","","","","","Thu Dec 19 15:46:55 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01018 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 186 (E-value = 1.7e-86) place AA01018 in the DUF179 family which is described as Uncharacterized ACR, COG1678 (PF02622)","","","","","","","","1","","","" "AA01019","712363","712779","417","ATGGGTATCACGGTGCTTGCTTTCGACTTCGGGACGAAAAGTATCGGCTGTGCCGTCGGGCAAAGCATCACCGGCACGGCACAATCCTTGCCGGCGTTTAAAGCGCAGGACGGTATTCCCAATTGGGATGCCATTGAGAAATGTATTCAGGAATGGCAACCGGCGCGTATTGTGGTCGGTTTGCCACTGAATATGGATGGTACGGAACAGCCCTTAACGTTGCGTGCCAAAAAGTTTGCTAAGCGTTTGCACGGACGTTTTAACGTGCCGGTGGATTTACAGGACGAACGTCTTACCACCACCGAAGCGCGTAGCGAAATTTTCAGTCGTGGTGGTTATCGCGCCTTAAATAAAAGCAAAGTGGACGGCATTTCCGCCTGTTTGATTTTGGAAAGTTGGTTTGAGAATTACGCAGGT","","","15245","MGITVLAFDFGTKSIGCAVGQSITGTAQSLPAFKAQDGIPNWDAIEKCIQEWQPARIVVGLPLNMDGTEQPLTLRAKKFAKRLHGRFNVPVDLQDERLTTTEARSEIFSRGGYRALNKSKVDGISACLILESWFENYAG","712781","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR005227
Family
Resolvase, holliday junction-type, YqgF-like
PF03652\"[3-136]TUPF0081
TIGR00250\"[6-135]TTIGR00250: conserved hypothetical protein T
InterPro
IPR006641
Domain
Resolvase, RNase H-like fold
SM00732\"[3-103]TYqgFc
noIPR
unintegrated
unintegrated
G3DSA:3.30.420.140\"[1-135]Tno description


","No hits to the COGs database.","","Residues 1 to 25 match (9e-07) PD:PD408399 which is described as PROTEOME COMPLETE PM1870 HI0305 ","","","","","","","","","","","","Thu Dec 19 15:47:48 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01019 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 136 (E-value = 4e-67) place AA01019 in the UPF0081 family which is described as Uncharacterised protein family (UPF0081) (PF03652)","","","","","","","","1","","","" "AA01020","714188","712881","1308","ATGGCAAAAATCGTTAAAGTCATTGGTCGTGAAATTATCGACTCTCGTGGTAATCCAACTGTTGAAGCAGAAGTGCATTTAGAAGGCGGTTTCGTCGGTCTTGCGGCAGCGCCATCAGGTGCTTCCACCGGTTCACGTGAAGCATTGGAATTACGCGATGGCGACAAATCCCGTTTCTTAGGTAAAGGTGTATTAAAAGCAGTTGCGGCAGTAAACGGCCCGATTGCAGACGCGATCATCGGCAAAGATGGTTTAAACCAAGCTGAAATCGATCAAATCATGATCGATTTAGACGGCACAGATAACAAATCCAAATTCGGCGCAAACGCCATTCTTGCCGTTTCTCTTGCTAACGCCAAAGCGGCTGCGGCATCTAAAGGTCTTCCACTTTACGCTTACATCGCAGAACTCAACGGCACACCAGGCGTGTACTCTATGCCATTACCAATGATGAACATCATCAACGGCGGTGAACACGCAGACAACAACGTGGATATTCAAGAATTTATGATTCAACCGGTGGGCGCGAAAACCTTGCGTGAAGCCCTTCGTATCGGTGCGGAAGTGTTCCATAATTTAGCGAAAGTATTAAAAGCCAAAGGCTTAAATACTGCAGTAGGTGACGAAGGCGGTTTCGCACCAAACCTTGCTTCTAACGCGGAAGCATTGGCTTGCATTAAAGAAGCTGTTGAAAAAGCGGGTTATGTATTAGGCAAAGACGTGACATTAGCCATGGACTGCGCTTCTTCCGAATTCTACAACAAAGAAACCGGCAAATATGAAATGAAAGGCGAAGGTCGTTCATTCACTTCTCAAGAATTCACACACTATCTTGAAGAATTAACCAAACAATACCCAATCGTGTCTATCGAAGACGGTCAAGACGAATCCGACTGGGAAGGCTTTGCATATCAAACTAAAGTATTAGGCGACCGCGTTCAATTAGTGGGCGACGACTTATTCGTCACCAACACCAAAATCCTGAAAGAAGGTATTGAGAAAGGTATCGCAAACTCTATCTTAATCAAGTTCAACCAAATCGGTTCTTTAACAGAAACCTTAGCTGCGATCAAAATGGCGAAAGATGCCGGCTACACTGCGGTTATCTCTCACCGTTCCGGTGAAACCGAAGATGCCACCATCGCCGATTTGGCAGTAGGTACCGCAGCAGGTCAAATCAAAACCGGTTCTATGAGTCGTTCCGACCGTATCGCGAAATACAACCAATTAATCCGTATTGAAGAAGCTTTAGAACGTGCAGGTACACCGGCGCCGTTCCCAGGTTTAAAAGCGGTTAAAGGTCAGGCT","","","46115","MAKIVKVIGREIIDSRGNPTVEAEVHLEGGFVGLAAAPSGASTGSREALELRDGDKSRFLGKGVLKAVAAVNGPIADAIIGKDGLNQAEIDQIMIDLDGTDNKSKFGANAILAVSLANAKAAAASKGLPLYAYIAELNGTPGVYSMPLPMMNIINGGEHADNNVDIQEFMIQPVGAKTLREALRIGAEVFHNLAKVLKAKGLNTAVGDEGGFAPNLASNAEALACIKEAVEKAGYVLGKDVTLAMDCASSEFYNKETGKYEMKGEGRSFTSQEFTHYLEELTKQYPIVSIEDGQDESDWEGFAYQTKVLGDRVQLVGDDLFVTNTKILKEGIEKGIANSILIKFNQIGSLTETLAAIKMAKDAGYTAVISHRSGETEDATIADLAVGTAAGQIKTGSMSRSDRIAKYNQLIRIEEALERAGTPAPFPGLKAVKGQA","712883","","enonolase; 2-phosphoglycerate dehydratase","Cytoplasm","","
InterPro
IPR000941
Family
Enolase
PD000902\"[149-435]TENO_HAEIN_P43806;
PR00148\"[37-51]T\"[107-123]T\"[165-178]T\"[317-328]T\"[340-354]T\"[369-386]TENOLASE
PTHR11902\"[1-214]TENOLASE
PF00113\"[143-435]TEnolase_C
PF03952\"[3-134]TEnolase_N
TIGR01060\"[4-435]Teno: phosphopyruvate hydratase
PS00164\"[340-353]TENOLASE
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.120\"[128-434]Tno description
G3DSA:3.30.390.10\"[3-127]Tno description
PIRSF001400\"[2-434]TEnolase


","BeTs to 25 clades of COG0148COG name: EnolaseFunctional Class: GThe phylogenetic pattern of COG0148 is aompkzyqvdrlbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 5e-183) to 8/8 blocks of the IPB000941 family, which is described as \"Enolase\". Interpro entry for IP:IPR000941. IPB000941A 9-22 6.1e-09 IPB000941B 34-55 2.9e-15 IPB000941C 90-135 8.2e-37 IPB000941D 146-182 1.8e-28 IPB000941E 204-235 2.7e-20 IPB000941F 285-302 1.3e-10 IPB000941G 313-348 1.5e-25 IPB000941H 381-418 1.2e-28","Residues 1 to 109 match (2e-35) PD:PD235537 which is described as ENOLASE LYASE MAGNESIUM GLYCOLYSIS HYDRO-LYASE DEHYDRATASE 2-PHOSPHOGLYCERATE GLYCERATE 2-PHOSPHO-D- PROTEOME ","","","","","","","","","","","","Thu Jan 23 08:48:18 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01020 is paralogously related to AA00974 (0.001).","","","","","","Residues 143 to 435 (E-value = 2.1e-179) place AA01020 in the Enolase_C family which is described as Enolase, C-terminal TIM barrel domain (PF00113)","","",""," Haraszthy VI, Jordan SF, Zambon JJ.,Identification of Fur-regulated genes in Actinobacillus actinomycetemcomitans.Microbiology. 2006 Mar;152(Pt 3):787-96.PMID: 16514158","Leroy A, Vanzo NF, Sousa S, Dreyfus M, Carpousis AJ. Function in Escherichia coli of the non-catalytic part ofRNase E: role in the degradation of ribosome-free mRNA. Mol Microbiol. 2002 Sep;45(5):1231-43. PMID: 12207692 Liou GG, Chang HY, Lin CS, Lin-Chao S. DEAD box RhlB RNA helicase physically associates withexoribonuclease PNPase to degrade double-stranded RNAindependent of the degradosome-assembling region of RNase E. J Biol Chem. 2002 Oct 25;277(43):41157-62. PMID: 12181321 Garcia-Alles LF, Erni B. Synthesis of phosphoenol pyruvate (PEP) analogues andevaluation as inhibitors of PEP-utilizing enzymes. Eur J Biochem. 2002 Jul;269(13):3226-36. PMID: 12084063","","Wed Jan 29 13:14:24 2003","1","","","" "AA01021","714336","714211","126","ATGTTGACCGCACTTTCGTTCCGGAAATTGGATCCAAATCAAGTTCGGCGCATTTTTTACAAGACAAAATGGCAAAATAGCTTTATCATACCGAGCATTTTAGGGCTTGCTCTAACTGGTTTTAAT","","","4882","MLTALSFRKLDPNQVRRIFYKTKWQNSFIIPSILGLALTGFN","714211","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 09:11:55 2004","Wed Feb 25 09:11:55 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01021 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 09:11:55 2004","","","","","","","","","","","","","1","","","" "AA01022","715977","714829","1149","ATGAAATCACAAACTTACGAAAATCATTTCCCGAAACTCACGGCGCAACAACTTGCCGAAAATGCGACGAAAAAAATCATTTGCGGGATGTCCGGCGGGGTGGATTCTTCCGTGTCTGCGTTTATTCTGCAACAGCAAGGCTACCAAGTGGAAGGCTTGTTCATGAAAAATTGGGAGGAGGATGATGACACCGATTACTGCACGGCGGCGGCAGATTTGGCGGATGCGCAGGCAGTGTGTGACAAGCTCGGTATTAAACTACATAAAATCAATTTTGCGGCGGAATATTGGGACAATGTGTTTGAACATTTCCTTAGCGAATACAAAGCAGGGCGCACGCCGAATCCGGATATTCTGTGTAATAAAGAAATTAAGTTCAAAGCTTTTTTGGAATACGCGGCGGAAGATTTAGGCGCCAATTATATTGCCACCGGGCATTATGTGCGTCGTCGCGGTGCTGATGACAACGCGCAGTTATTACGTGGCTTGGACAACAATAAAGACCAAAGCTATTTCTTATACACCCTAAGCAAAACCCAAGTGGGACAGAGTCTGTTTCCGGTGGGCAATATTGAAAAGCCTATCGTGCGTGCAATTGCGGAAGAGTTAGGTTTGGTGACGGCGAAGAAAAAAGACTCCACCGGCATTTGTTTTATCGGGGAGCGGAAATTTAAGGATTTCTTGGCGCGTTATTTGCCGGCGCAACCGGGCAATATTCGCACGGTGGACGGCGAAATTATCGGTCGCCATGACGGTTTGATGTATCACACGTTAGGACAACGTAAAGGCTTAGGCATCGGTGGCGTGAAAGGCGCCGGTGAAGACGCTTGGTATGTAGTGGAAAAAGATCTCATTAATAATGAGCTGATTGTGGCGCAGGGGCATGACCATTCCGCTTTACTTTCCACCGGTTTAATCGCACAGCAATTACATTGGGTTGATTGCCTGCCGATTCGCGCGCCATTGCGTTGCACGGTGAAAACCCGTTATCGTCAAACGGATGTACCTTGCATTATTGAACCTATAGATGATGAAACCATTAAAGTTATATTTGACGAACCACAAATTGCGGTCACTCCGGGACAATCGGCGGTGTTTTATTTAGACGAAATTTGCCTTGGCGGCGGCATCATTGAAAAGCAATTAAAA","","","42601","MKSQTYENHFPKLTAQQLAENATKKIICGMSGGVDSSVSAFILQQQGYQVEGLFMKNWEEDDDTDYCTAAADLADAQAVCDKLGIKLHKINFAAEYWDNVFEHFLSEYKAGRTPNPDILCNKEIKFKAFLEYAAEDLGANYIATGHYVRRRGADDNAQLLRGLDNNKDQSYFLYTLSKTQVGQSLFPVGNIEKPIVRAIAEELGLVTAKKKDSTGICFIGERKFKDFLARYLPAQPGNIRTVDGEIIGRHDGLMYHTLGQRKGLGIGGVKGAGEDAWYVVEKDLINNELIVAQGHDHSALLSTGLIAQQLHWVDCLPIRAPLRCTVKTRYRQTDVPCIIEPIDDETIKVIFDEPQIAVTPGQSAVFYLDEICLGGGIIEKQLK","714831","","tRNA (5-methylaminomethyl-2-thiouridylate) methyltransferase","Cytoplasm","","
InterPro
IPR004506
Family
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase
PTHR11933\"[39-382]TTRNA (5-METHYLAMINOMETHYL-2-THIOURIDYLATE)-METHYLTRANSFERASE
PF03054\"[24-378]TtRNA_Me_trans
TIGR00420\"[24-378]TtrmU: tRNA (5-methylaminomethyl-2-thiouridy
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620\"[3-205]Tno description


","No hits to the COGs database.","Significant hit ( 4.6e-05) to 2/6 blocks of the IPB000541 family, which is described as \"Uncharacterized protein family UPF0021\". Interpro entry for IP:IPR000541. IPB000541B 24-42 0.0074 IPB000541D 126-164 3","Residues 158 to 187 match (1e-08) PD:PD548442 which is described as TRNA PROTEOME COMPLETE TRANSFERASE METHYLTRANSFERASE 5-METHYLAMINOMETHYL-2-THIOURIDYLATE-METHYLTRANSFERASE PROCESSING PROBABLE ORF ","","","","","","","","","","","","Thu Dec 19 15:51:32 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01022 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 24 to 378 (E-value = 7.8e-220) place AA01022 in the tRNA_Me_trans family which is described as tRNA methyl transferase (PF03054)","","","","","Hagervall TG, Pomerantz SC, McCloskey JA. Reduced misreading of asparagine codons by Escherichia colitRNALys with hypomodified derivatives of 5-methylaminomethyl-2-thiouridine in the wobble position. J Mol Biol. 1998 Nov 20;284(1):33-42. PMID: 9811540 ","","Thu Dec 19 15:51:32 2002","1","","","" "AA01023","716495","716241","255","ATGAAACTATTTTTGCTCACCTTAGGCATTTTCCTGCTTATTATTCTTGCCATGGCATTGGGTTACATCGTGAAACGCCAAGCTCTCAAAGGTAGCTGCGGCGGCTTATCTTCCTTAGGTATTGCTAAAGCCTGCGACTGCGACAAACCGTGCGACACGCTGCAATCTAAATTAGACGCGGGAGATGAGCAAGCCAAAGTAGAATATGAACAAAAATTCACCAATAACGTGCAAACGCAGTTTTATGAAGTGAAA","","","9333","MKLFLLTLGIFLLIILAMALGYIVKRQALKGSCGGLSSLGIAKACDCDKPCDTLQSKLDAGDEQAKVEYEQKFTNNVQTQFYEVK","716243","","conserved hypothetical protein","Periplasm, Inner membrane, Cytoplasm","","
InterPro
IPR007495
Family
Protein of unknown function DUF539
PF04400\"[22-66]TDUF539
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide
tmhmm\"[4-24]?transmembrane_regions


","BeTs to 4 clades of COG2991COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG2991 is ---------------fgh-n------Number of proteins in this genome belonging to this COG is","","Residues 18 to 66 match (2e-07) PD:PD330881 which is described as COMPLETE PROTEOME TRANSMEMBRANE VC1322 EXPORTED PERIPLASMIC HI0173 VC2288 PM1335 ","","","","","","","","","","","","Thu Dec 19 15:53:07 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01023 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 22 to 66 (E-value = 3.1e-27) place AA01023 in the DUF539 family which is described as Protein of unknown function (DUF539) (PF04400)","","","","","","","","1","","","" "AA01024","717662","716577","1086","ATGAACATAAAACAACCTCTCGTTCGCGGATTCGCACTTGCTGCCATGGCATTGGCACTGATGGCCTGCGATAAACCGAATCCGTCACAACAAGCGGACACACAACAAGCCATGGCAGCAAAAAATGAAATTGTTTCCCTCACCGGTAAAACCATGGGGACAACCTACCACATCAAATATTCAAACAACGGCGAAGTCTCAACGGCGTCGCAACAGGCACATGAACAAATCGAACTAATTTTGAAGGATGTGAATGCGAAAATGTCCACTTACATCAAAGATTCCGAGCTCAGCCGTTTTAATCAAAATACGCAAATTAACACGCCCATTGAAATCTCGGCGGATCTTGCCAAAGTGGTTAAAGAAGCCATTCGGTTAAATCAGGTGACGCAGGGTGCCTTGGATATTACAGTCGGGCCGGTAGTGAATCTTTGGGGGTTCGGTCCGGAAAAGCGGGTGGATAAACGGCCGACATCAGCACAAATTGCCGAACGTCAGGCATGGGTGGGCATTGATAAGTTGTCACTCACTGAAGAGGGCGGTAAGTTTTTCCTGGCAAAAGCCGTACCGCAACTTTATGTGGATCTTTCTTCTATCGCCAAAGGTTTTGGGGTGGATCAAGTGGCGGATTATCTGGAAAGCATTCGCGTACAAAATTACATGGTGGAAATCGGCGGTGAAATTCGCGCCAAAGGGAAGAATGCCGAAGGAAAAGCGTGGCAAATTGCTATCGAACGTCCAACCCTGGATGGCAAGCAGGTGGCACAACAAGTCATCGGTTTGAATAATATGGCGATGGCGACATCAGGCGATTATCGTAATTATTTTGAACAAGACGGCGTGCGTTTTTCCCATGAAATCGATCCGCACACCGGTTACCCGATTCAGCATGCATTGGCATCGATCACGGTGTTAGCGCCGACTTCCATGACTGCTGACGGGCTTTCCACCGGGTTATTTGTGTTAGGGGAACAGAAAGCGTTGGACGTGGCGGAACAGGAAAAATTACCGATTTTTATGATTATTAAAGACAGCAAGGGCTACCGCACAGAAATGTCTACCACATTCAAACAATTTTTAGCACAG","","","39692","MNIKQPLVRGFALAAMALALMACDKPNPSQQADTQQAMAAKNEIVSLTGKTMGTTYHIKYSNNGEVSTASQQAHEQIELILKDVNAKMSTYIKDSELSRFNQNTQINTPIEISADLAKVVKEAIRLNQVTQGALDITVGPVVNLWGFGPEKRVDKRPTSAQIAERQAWVGIDKLSLTEEGGKFFLAKAVPQLYVDLSSIAKGFGVDQVADYLESIRVQNYMVEIGGEIRAKGKNAEGKAWQIAIERPTLDGKQVAQQVIGLNNMAMATSGDYRNYFEQDGVRFSHEIDPHTGYPIQHALASITVLAPTSMTADGLSTGLFVLGEQKALDVAEQEKLPIFMIIKDSKGYRTEMSTTFKQFLAQ","716579","From GenBank (gi:1176633):This protein is involved in the conversion of aminoimidazole ribotide (AIR), a purine intermediate, to the 4-amino-5-hydroxymethyl-2-methyl pyrimidine moiety of thiamine. ApbE is attached to the membrane by a lipid anchor","thiamine biosynthesis lipoprotein precursor","Periplasm, Inner membrane, Cytoplasm","","
InterPro
IPR003374
Family
ApbE-like lipoprotein
PF02424\"[16-346]TApbE
noIPR
unintegrated
unintegrated
PS51257\"[1-23]TPROKAR_LIPOPROTEIN
signalp\"[1-22]?signal-peptide


","BeTs to 11 clades of COG1477COG name: Membrane-associated lipoprotein involved in thiamine biosynthesisFunctional Class: HThe phylogenetic pattern of COG1477 is -------qvd-l--efghsn-j-it-Number of proteins in this genome belonging to this COG is","Significant hit ( 6.4e-64) to 3/3 blocks of the IPB003374 family, which is described as \"ApbE family\". Interpro entry for IP:IPR003374. IPB003374A 130-148 1.6e-10 IPB003374B 183-226 9.7e-18 IPB003374C 259-313 3.9e-33","Residues 303 to 359 match (5e-08) PD:PD584305 which is described as COMPLETE LIPOPROTEIN PROTEOME BIOSYNTHESIS THIAMINE PRECURSOR APBE PA2993 ","","","","","","","","","","","Fri Jan 24 13:12:00 2003","Thu Dec 19 15:55:35 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01024 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 16 to 346 (E-value = 7.4e-127) place AA01024 in the ApbE family which is described as ApbE family (PF02424)","","","","","Beck BJ, Downs DM. A periplasmic location is essential for the role of the ApbElipoprotein in thiamine synthesis in Salmonella typhimurium.J Bacteriol. 1999 Dec;181(23):7285-90. PMID: 10572132 Beck BJ, Downs DM. The apbE gene encodes a lipoprotein involved in thiaminesynthesis in Salmonella typhimurium. J Bacteriol. 1998 Feb;180(4):885-91. PMID: 9473043 ","","Thu Dec 19 15:55:35 2002","1","","","" "AA01025","717829","717662","168","ATGATTTCGGCGGCTAACGCCTTGCAGTTTAAAAACACCGTAAAAAATGACCGCACTTTGCATGAAGTGCGGTCGAAATTTACAGCGTTTTTCATATTGATTCATCACACGCAAACCAATTTAAACCGTTGGTTTGCGTGTGATCCATCTAATATCAGGAAAGTATTA","","","6541","MISAANALQFKNTVKNDRTLHEVRSKFTAFFILIHHTQTNLNRWFACDPSNIRKVL","717662","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 09:14:49 2004","Wed Feb 25 09:14:49 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01025 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 09:14:49 2004","","","","","","","","","","","","","1","","","" "AA01027","719048","717816","1233","ATGAGCGAAACTACAATTCTTTTACTTGGTGTTGCAGCCTTTACAGCCATTGTTTTAGTGCTTGTTGCAATCATCTTGTTTGCGAAATCCAAATTGGTGGACTCCGGCGACATTACCATTAAGATTAATGATGACCCGAGCAAAGCCATCACTTTGCCGGCCGGCGGTAAGTTACTCAGCGCACTTGCCGGCAAGGGCATCTTCGTATCTTCCGCTTGTGGCGGCGGTGGTTCCTGCGGTCAATGTGTAGTACGGGTAAAAAGCGGTGGCGGCGAAATTTTACCGACCGAGCTTTCCCACATCACCAAACGTGAAGCCAAAGAAGGCTATCGTCTTTCTTGCCAAGTGAACGTGAAAGGTAATATGGATATTGAATTGCCGGAAGAGATCTTTGGTGTGAAAAAATGGGAGTGCACCGTCATTTCCAATGATAACAAAGCGACTTTCATTAAAGAGCTTAAATTGGCGATTCCGGAAGGAGAAGAAGTGCCGTTCCGTGCCGGTGGTTATATCCAAATTGAAGCAGAACCACACACGGTTTACTATAAAGACTTCGATATTCCGCAAGAGTATCACGAAGACTGGAATAAATATGATCTGTGGCGCTATGTATCAAAAGTGGATAAGCATATTATCCGCGCTTATTCCATGGCATCCTATCCGGAAGAAAAAGGCATTATCATGCTGAATGTGCGTATTGCAACGCCTCCTCCACGTCAACCTGATGCGCCTCCGGGACAAATGTCTTCTTATATTTGGTCTTTAAAACCGGGTGATAAAGTGATTATTTCCGGTCCGTTCGGTGAATTCTTCGCGAAAGAAACCGATGCTGAAATGGTCTTTATCGGTGGTGGTGCAGGTATGGCACCAATGCGTTCACACATCTTCGACCAATTAAAACGTTTACACTCTAAACGTAAAATGTCCTTCTGGTACGGTGCCCGTTCTAAACGTGAAATGTTCTATGTAGAAGATTTTGATACATTGCAAGCGGAAAATCCGAATTTCCAATGGCATGTGGCATTATCCGATCCATTGCCGGAAGACAACTGGACAGGCTACACCGGCTTTATTCACAATGTACTTTATGAAAACTATCTGAAAAATCACGAAGCGCCGGAAGATTGTGAATACTACATGTGCGGACCTCCGGTGATGAACGCTGCGGTAATCAAAATGTTGAAAGACCTTGGTGTTGAAGATGAAAATATCTTGTTAGATGATTTCGGCGGC","","","45788","MSETTILLLGVAAFTAIVLVLVAIILFAKSKLVDSGDITIKINDDPSKAITLPAGGKLLSALAGKGIFVSSACGGGGSCGQCVVRVKSGGGEILPTELSHITKREAKEGYRLSCQVNVKGNMDIELPEEIFGVKKWECTVISNDNKATFIKELKLAIPEGEEVPFRAGGYIQIEAEPHTVYYKDFDIPQEYHEDWNKYDLWRYVSKVDKHIIRAYSMASYPEEKGIIMLNVRIATPPPRQPDAPPGQMSSYIWSLKPGDKVIISGPFGEFFAKETDAEMVFIGGGAGMAPMRSHIFDQLKRLHSKRKMSFWYGARSKREMFYVEDFDTLQAENPNFQWHVALSDPLPEDNWTGYTGFIHNVLYENYLKNHEAPEDCEYYMCGPPVMNAAVIKMLKDLGVEDENILLDDFGG","717818","From GenBank (gi:15214142):The NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinal by two successive reactions, coupled with the transport of NA(+) ions from the cytoplasm to the periplasm. The first step is catalyzed by NQRF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one electron transfer pathway. The NQR complex located in the inner membrane (potential) and is composed of six subunits NqrA, NqrB, NqrC, NqrD, NqrE, and NqrF.","Na(+)-translocating NADH-quinone reductase subunit F","Cytoplasm, Inner membrane","","
InterPro
IPR001041
Domain
Ferredoxin
PF00111\"[42-120]TFer2
PS51085\"[36-130]T2FE2S_FER_2
InterPro
IPR001433
Domain
Oxidoreductase FAD/NAD(P)-binding
PF00175\"[280-392]TNAD_binding_1
InterPro
IPR001709
Domain
Flavoprotein pyridine nucleotide cytochrome reductase
PR00371\"[213-220]T\"[280-299]T\"[306-315]T\"[377-385]TFPNCR
InterPro
IPR008333
Domain
Oxidoreductase FAD-binding region
PF00970\"[208-271]TFAD_binding_6
InterPro
IPR010205
Family
NADH:ubiquinone oxidoreductase, Na(+)-translocating, F subunit
TIGR01941\"[7-411]TnqrF: NADH:ubiquinone oxidoreductase, Na(+)
InterPro
IPR012254
Family
Methane/phenol monooxygenase/ferrodoxin-NAD+ reductase [2Fe-2S]-component
PIRSF000044\"[39-411]TMethane monooxygenase, reductase component
InterPro
IPR012675
Domain
Beta-grasp fold, ferredoxin-type
G3DSA:3.10.20.30\"[32-130]Tno description
noIPR
unintegrated
unintegrated
G3DSA:2.40.30.10\"[208-266]Tno description
G3DSA:3.40.50.80\"[272-410]Tno description
PTHR19370\"[277-402]TNADH-CYTOCHROME B5 REDUCTASE
PTHR19370:SF3\"[277-402]TNADH-CYTOCHROME B5 REDUCTASE
signalp\"[1-30]?signal-peptide
tmhmm\"[5-27]?transmembrane_regions


","BeTs to 6 clades of COG2871COG name: Na+-transporting NADH:ubiquinone oxidoreductase beta subunitFunctional Class: CThe phylogenetic pattern of COG2871 is ---------------fgh-n---i--Number of proteins in this genome belonging to this COG is","Significant hit ( 4.6e-11) to 4/6 blocks of the PR00410 family, which is described as \"Phenol hydroxylase reductase family signature\". Prints database entry for PR:PR00410. PR00410B 213-220 3.4 PR00410C 265-274 1.4 PR00410D 280-299 0.0048 PR00410F 377-385 0.27Significant hit ( 6.9e-06) to 2/2 blocks of the IPB001433 family, which is described as \"Oxidoreductase FAD and NAD(P)-binding domain\". Interpro entry for IP:IPR001433. IPB001433A 281-290 0.42 IPB001433B 377-388 0.0082Significant hit ( 9.7e-05) to 3/8 blocks of the PR00371 family, which is described as \"Flavoprotein pyridine nucleotide cytochrome reductase signature\". Prints database entry for PR:PR00371. PR00371B 213-220 14 PR00371D 280-299 0.11 PR00371H 377-385 29","","","","","","","","","","","","Thu Jan 16 10:22:11 2003","Thu Dec 19 15:56:49 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01027 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 276 to 393 (E-value = 7e-23) place AA01027 in the NAD_binding_1 family which is described as Oxidoreductase NAD-binding domain (PF00175)","","","","","Barquera B, Hellwig P, Zhou W, Morgan JE, Hase CC, Gosink KK, Nilges M, Bruesehoff PJ, Roth A, Lancaster CR, Gennis RB.Purification and characterization of the recombinant Na(+)-translocating NADH:quinone oxidoreductase from Vibrio cholerae.Biochemistry. 2002 Mar 19;41(11):3781-9.PMID: 11888296 Steuber J.Na(+) translocation by bacterial NADH:quinone oxidoreductases: an extension to the complex-I family of primary redox pumps.Biochim Biophys Acta. 2001 May 1;1505(1):45-56. Review.PMID: 11248188 Hayashi M, Nakayama Y, Unemoto T.Recent progress in the Na(+)-translocating NADH-quinone reductase from the marine Vibrio alginolyticus.Biochim Biophys Acta. 2001 May 1;1505(1):37-44. Review.PMID: 11248187","","Thu Dec 19 15:58:34 2002","1","","","" "AA01028","719656","719063","594","GTGGAACATTATATTAGCCTATTTGTGAAGGCGATCTTCATTGAAAACATGGCACTTTCCTTCTTTTTGGGAATGTGCACTTTCCTTGCTGTATCTAAGAAGGTGTCAACAGCGTTTGGCTTGGGCATTGCTGTCGTTGTTGTGCTTGGCATTGCGGTTCCTGCAAACCAATTCGTATACGAGCATGTCCTAAAAGAAAGTGCTTTAGTTGAAGGGGTGGATTTATCCTTCTTAAACTTCATCACGTTTATCGGGATTATCGCCGGTCTGGTTCAATTACTTGAAATGACTTTAGATAAATTCTTTCCGGCATTATATAACGCACTGGGGATCTTCTTACCGCTTATCGCCGTAAACTGTGCGATCTTCGGTGGCGTATCCTTTGCCATCCAGCGTGAATATACTTTCGCCGAATCTGCCGTATATGGTATCGGTGCAGGATTAGGTTGGATGTTGGCGATTGTTGCATTAGCGGGCTTAACTGAGAAAATGAAATATTCTGATGTACCGGCAGGTTTACGCGGTTTAGGGATTACATTCATCTCCGCAGGCTTAATGGCGCTCGGCTTTATGTCATTCTCCGGTATTCAGCTA","","","21113","VEHYISLFVKAIFIENMALSFFLGMCTFLAVSKKVSTAFGLGIAVVVVLGIAVPANQFVYEHVLKESALVEGVDLSFLNFITFIGIIAGLVQLLEMTLDKFFPALYNALGIFLPLIAVNCAIFGGVSFAIQREYTFAESAVYGIGAGLGWMLAIVALAGLTEKMKYSDVPAGLRGLGITFISAGLMALGFMSFSGIQL","719065","From GenBank (gi:15214142): The NQR complex catalyzes the reduction of ubiquinone-1 toubiquinal by two successive reactions, coupled with the transportof NA(+) ions from the cytoplasm to the periplasm. The first stepis catalyzed by NQRF, which accepts electrons from NADH andreduces ubiquinone-1 to ubisemiquinone by a one electron transferpathway. The NQR complex located in the inner membrane(potential) and is composed of six subunits NqrA, NqrB, NqrC,NqrD, NqrE, and NqrF.From GenBank (gi:6093529):NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.","Na(+)-translocating NADH-quinone reductase subunit E","Inner membrane, Cytoplasm","","
InterPro
IPR003667
Family
RnfA-Nqr electron transport subunit
PF02508\"[1-198]TRnf-Nqr
InterPro
IPR009229
Family
Staphylococcal AgrD
SM00794\"[67-95]Tno description
InterPro
IPR010967
Family
NADH:ubiquinone oxidoreductase, Na(+)-translocating, E subunit
TIGR01940\"[2-197]TnqrE: NADH:ubiquinone oxidoreductase, Na(+)
noIPR
unintegrated
unintegrated
signalp\"[1-32]?signal-peptide
tmhmm\"[4-24]?\"[39-59]?\"[73-93]?\"[108-130]?\"[140-160]?\"[175-195]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.8e-83) to 4/4 blocks of the IPB003667 family, which is described as \"RnfA-Nqr electron transport subunit\". Interpro entry for IP:IPR003667. IPB003667A 12-44 2.1e-24 IPB003667B 78-130 2.5e-34 IPB003667C 139-169 2.6e-19 IPB003667D 179-187 0.12","Residues 4 to 196 match (3e-65) PD:PD006282 which is described as SUBUNIT E D NA-TRANSLOCATING NQR COMPLEX ELECTRON NADH-QUINONE REDUCTASE 1.6.5.- ","","","","","","","","","","","Thu Jan 16 10:26:40 2003","Fri Dec 20 08:28:28 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01028 is paralogously related to AA01805 (9e-39), AA01813 (2e-18) and AA01029 (4e-11).","","","","","","Residues 1 to 198 (E-value = 3.2e-111) place AA01028 in the Rnf-Nqr family which is described as Rnf-Nqr subunit, membrane protein (PF02508)","","","","","Barquera B, Hellwig P, Zhou W, Morgan JE, Hase CC, Gosink KK, Nilges M, Bruesehoff PJ, Roth A, Lancaster CR, Gennis RB.Purification and characterization of the recombinant Na(+)-translocating NADH:quinone oxidoreductase from Vibrio cholerae.Biochemistry. 2002 Mar 19;41(11):3781-9.PMID: 11888296 ","","Thu Jan 16 11:08:30 2003","1","","","" "AA01029","720289","719663","627","ATGGCTGATGCAAAAAGCAATTTAAGAGCACTTTTGCTTGATCCAATCGCGAAAAACAACCCGATTGCACTACAAATCTTAGGAATTTGTTCCGCATTAGCGGTGACCACCCAATTACAAACGGCGTTAGTCATGGCAATTGCGGTATGTTTGGTAACCGGTTTTTCCAGCATGTTCATTGCAATGATTCGTAACTATATTCCGAATAGTATTCGTATCATTGTGCAATTGGCGATTATCGCGTCGTTGGTAATTTTGGTTGACCAAGTGTTAAAAGCCTTTGCTTACGGTTTATCCAAACAATTATCGGTATTCGTCGGTTTGATTATCACCAACTGTATCGTCATGGGGCGTGCAGAAGCTTTCGCTATGAAATCCCGTCCATTAGAGAGTTTTGTTGACGGTATCGGTAACGGTTTAGGTTACGGCGCTATTCTCTTAATTGTGGCGACTTTGCGTGAGTTAATCGGCTCAGGTCGTTTGTTCGGTTTCCCGATATTACAAACGATTCAGGATGGTGGTTGGTATCAACCGAACGGTTTATTCCTTCTTGCACCGAGTGCGTTCTTTATCATTGGCTTCGTGATCTGGGGCGTAAGAACGTGGAAACCTGAGCAACAGGAGAAA","","","22586","MADAKSNLRALLLDPIAKNNPIALQILGICSALAVTTQLQTALVMAIAVCLVTGFSSMFIAMIRNYIPNSIRIIVQLAIIASLVILVDQVLKAFAYGLSKQLSVFVGLIITNCIVMGRAEAFAMKSRPLESFVDGIGNGLGYGAILLIVATLRELIGSGRLFGFPILQTIQDGGWYQPNGLFLLAPSAFFIIGFVIWGVRTWKPEQQEK","719665","From GenBank (gi:15214142): The NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinal by two successive reactions, coupled with the transport of NA(+) ions from the cytoplasm to the periplasm. The first step is catalyzed by NQRF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one electron transfer pathway. The NQR complex located in the inner membrane (potential) and is composed of six subunits NqrA, NqrB, NqrC, NqrD, NqrE, and NqrF.From GenBank (gi:6093529): NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.","Na(+)-translocating NADH-quinone reductase subunit D","Inner membrane, Cytoplasm","","
InterPro
IPR003667
Family
RnfA-Nqr electron transport subunit
PF02508\"[5-197]TRnf-Nqr
InterPro
IPR011292
Family
NADH:ubiquinone oxidoreductase, Na(+)-translocating, D subunit
TIGR01939\"[3-208]TnqrD: NADH:ubiquinone oxidoreductase, Na(+)
noIPR
unintegrated
unintegrated
signalp\"[1-54]?signal-peptide
tmhmm\"[21-39]?\"[43-63]?\"[73-95]?\"[101-119]?\"[140-162]?\"[181-199]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.4e-72) to 4/4 blocks of the IPB003667 family, which is described as \"RnfA-Nqr electron transport subunit\". Interpro entry for IP:IPR003667. IPB003667A 16-48 3.9e-17 IPB003667B 71-123 1.9e-36 IPB003667C 131-161 5.2e-14 IPB003667D 193-201 0.49","Residues 157 to 208 match (3e-19) PD:PD036369 which is described as SUBUNIT D NQR NA-TRANSLOCATING NAD NA-NQR UBIQUINONE SODIUM 1.6.5.- NQR-1 ","","","","","","","","","","","Thu Jan 16 10:31:15 2003","Fri Dec 20 08:38:17 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01029 is paralogously related to AA01813 (3e-29), AA01805 (2e-13), AA01028 (4e-11) and AA01889 (0.001).","","","","","","Residues 5 to 197 (E-value = 4.1e-95) place AA01029 in the Rnf-Nqr family which is described as Rnf-Nqr subunit, membrane protein (PF02508)","","","","","Barquera B, Hellwig P, Zhou W, Morgan JE, Hase CC, Gosink KK, Nilges M, Bruesehoff PJ, Roth A, Lancaster CR, Gennis RB.Purification and characterization of the recombinant Na(+)-translocating NADH:quinone oxidoreductase from Vibrio cholerae.Biochemistry. 2002 Mar 19;41(11):3781-9.PMID: 11888296 Barquera B, Hase CC, Gennis RB.Expression and mutagenesis of the NqrC subunit of the NQR respiratory Na(+) pump from Vibrio cholerae with covalently attached FMN.FEBS Lett. 2001 Mar 9;492(1-2):45-9.PMID: 11248234 ","","Thu Jan 16 10:42:09 2003","1","","","" "AA01031","721137","720292","846","TTGCACCGATTTTCGATTACATCGTGGTTCAGGCAAATATCAAACGTCGGAGAGCAAGAACAAATGGCTAAATTTAATAAAGATAGCGTAAGTGGCACCGTAACCGTTGTTGTGTTATTGAGTCTGGTTTGTTCTATTGTGGTTTCAGGTGCCGCCGTTGCCCTTAAATCAAAACAGGATGAACAAAAAGCCCTTGACGTTCAACGCAATATTTTAACTGTTGCCGGTTTAATGAAAGAAGATAACGCTTCCGTTATCAAAGAGACTTACAACAAATTTATCGAGCCTCGTTTGGTGGATTTACAAAGCGGTGATTTCGTTCAGGCAACAAAAGAAGAAGCCGAAAAGTTTGATCCGAAAGCGGCGATAAAAGACACCGCACTTAGTCAGCCGATTCCTGCTGACCAGGATAAGGCGGGCTTAAAAGTGCGGGCGAAACAGGCCGTGGTTTATTTGGTAAAAGATGAGCAAGGTACGGTAAACCAAGTAGTATTGCCGATGTATGGTCGCGGCTTATGGTCCACTATGTATGGTTTTGTTTCCGTCGCGCCGGATGCCAATACCATTAAAGGTATTACCTATTATGACCAAGGTGAAACCGCCGGTCTTGGCGGTGAAATTGCCAATCCGCGCTGGCAGGCATTTTTCGTTGATAAAAAACTGTTTGATGATAACCAAAATGTGGCGATTCGTATTGCCAAAAACGCCTCTTCCGACAAAGAACACGGCATTGACGCGTTATCCGGTGCAACCTTGACTTCAAACGGCGTACAAGGCTCATTTGATTATTGGTTTAGTCAAAACGGTTTTGGTCCATTCTTAGCAAAATTTAAAGCGGGGGCAAGA","","","31290","LHRFSITSWFRQISNVGEQEQMAKFNKDSVSGTVTVVVLLSLVCSIVVSGAAVALKSKQDEQKALDVQRNILTVAGLMKEDNASVIKETYNKFIEPRLVDLQSGDFVQATKEEAEKFDPKAAIKDTALSQPIPADQDKAGLKVRAKQAVVYLVKDEQGTVNQVVLPMYGRGLWSTMYGFVSVAPDANTIKGITYYDQGETAGLGGEIANPRWQAFFVDKKLFDDNQNVAIRIAKNASSDKEHGIDALSGATLTSNGVQGSFDYWFSQNGFGPFLAKFKAGAR","720294","From GenBank (gi:15214142): The NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinal by two successive reactions, coupled with the transport of NA(+) ions from the cytoplasm to the periplasm. The first step is catalyzed by NQRF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one electron transfer pathway. The NQR complex located in the inner membrane (potential) and is composed of six subunits NqrA, NqrB, NqrC, NqrD, NqrE, and NqrF.From GenBank (gi:6093529): NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.","Na(+)-translocating NADH-quinone reductase subunit C","Periplasm, Inner membrane","","
InterPro
IPR007329
Domain
FMN-binding
PF04205\"[171-268]TFMN_bind
InterPro
IPR010204
Family
NADH:ubiquinone oxidoreductase, Na(+)-translocating, C subunit
PIRSF009437\"[22-282]TNa+-translocating NADH-quinone reductase, subunit C
TIGR01938\"[27-276]TnqrC: NADH:ubiquinone oxidoreductase, Na(+)
noIPR
unintegrated
unintegrated
tmhmm\"[34-54]?transmembrane_regions


","BeTs to 6 clades of COG2869COG name: Na+-transporting NADH:ubiquinone oxidoreductase gamma subunitFunctional Class: CThe phylogenetic pattern of COG2869 is --------v-----efgh-n---i--Number of proteins in this genome belonging to this COG is","","Residues 51 to 280 match (2e-67) PD:PD038728 which is described as SUBUNIT C NA-TRANSLOCATING NQR REDUCTASE NADH-QUINONE NQR-1 COMPLEX NA-NQR OXIDOREDUCTASE ","","","","","","","","","","","Thu Jan 16 10:34:33 2003","Thu Jan 16 10:34:33 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01031 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 165 to 268 (E-value = 4.2e-36) place AA01031 in the FMN_bind family which is described as FMN-binding domain (PF04205)","","","","","Barquera B, Hellwig P, Zhou W, Morgan JE, Hase CC, Gosink KK, Nilges M, Bruesehoff PJ, Roth A, Lancaster CR, Gennis RB.Purification and characterization of the recombinant Na(+)-translocating NADH:quinone oxidoreductase from Vibrio cholerae.Biochemistry. 2002 Mar 19;41(11):3781-9.PMID: 11888296 Barquera B, Hase CC, Gennis RB.Expression and mutagenesis of the NqrC subunit of the NQR respiratory Na(+) pump from Vibrio cholerae with covalently attached FMN.FEBS Lett. 2001 Mar 9;492(1-2):45-9.PMID: 11248234 ","","Thu Jan 16 10:50:05 2003","1","","","" "AA01032","722302","721070","1233","ATGGGTTTGAAAAATCTTTTAGAAAAAATGGAACCCGCGTTTTTACCGGGCGGTAAATACAGCAAGCTTTATCCGATCTTTGAATCGATTTATACCTTGCTTTATACACCGGGTACGGTAACCCACAAAAACACGCATGTTCGTGATGCGTTAGACTCAAAACGTATGATGATCATTGTTTTCCTTGCATTGTTCCCTGCAATTTTTTATGGCATGTACAATGTGGGTAACCAAGCAATTCCTGCGTTAAATCAATTAGGTAATTTAGAGCAGCTGATTTCAAGCAATTGGCATTATGCGTTGGCAAATGGTTTAGGGTTAGATTTAACTTTAAATGCAGGCTGGGGTAGTAAAATGGCACTTGGTGCAATTTTTTTCCTACCAATTTATTTAGTCGTCTTCACTGTTTGTACGATTTGGGAATTATTATTCTCTGTGGTGCGCGGTCATGAAGTGAATGAAGGGATGTTTGTTTCAACCATTCTGTTTGCCTTAATTGTTCCGCCAACATTGCCATTATGGCAGGCTGCACTTGGTATCAGCTTTGGTATCGTGGTGGCAAAAGAAATTTTTGGTGGTGTCGGTCGTAACTTTATGAATCCGGCATTGGCAGGTCGTGCTTTTTTATTCTTTGCTTATCCGGCACAAATTTCCGGTGACTTAGTATGGGCTGCGGCAGATGGTTTCTCCGGTGCGACTGCACTTTCACAATGGTCACAAGGCGGTCAAGACGCATTGCAGCATACTGTAACCGGTCAATCAATTTCTTGGATGGATGCCTTCATTGGTAATATTCCGGGTTCAATGGGGGAAGTGTCAACCTTAGCAATTTTAATTGGTGGTGCGATTATTGTGTTCACCCGTATTGCGGCATGGCGCATTATCGCGGGTGTGATGATCGGTATGATTGCAACTTCAACATTGTTTAATTTAATCGGTTCAGAAACTAACCATATGTTTTCAATGCCTTGGTATTGGCACCTTGTATTAGGTGGTTTTGCATTAGGTATGGTGTTTATGGCGACGGACCCTGTTTCAGCCTCATTCACTAACACCGGTAAATGGTGGTATGGTGCATTGATCGGTGTCATGGCGGTGTTAATTCGTACCATCAACCCGGCTTATCCTGAAGGGATGATGTTAGCGATTTTATTTGCAAACTTATTTGCACCGATTTTCGATTACATCGTGGTTCAGGCAAATATCAAACGTCGGAGAGCAAGAACAAATGGC","","","44812","MGLKNLLEKMEPAFLPGGKYSKLYPIFESIYTLLYTPGTVTHKNTHVRDALDSKRMMIIVFLALFPAIFYGMYNVGNQAIPALNQLGNLEQLISSNWHYALANGLGLDLTLNAGWGSKMALGAIFFLPIYLVVFTVCTIWELLFSVVRGHEVNEGMFVSTILFALIVPPTLPLWQAALGISFGIVVAKEIFGGVGRNFMNPALAGRAFLFFAYPAQISGDLVWAAADGFSGATALSQWSQGGQDALQHTVTGQSISWMDAFIGNIPGSMGEVSTLAILIGGAIIVFTRIAAWRIIAGVMIGMIATSTLFNLIGSETNHMFSMPWYWHLVLGGFALGMVFMATDPVSASFTNTGKWWYGALIGVMAVLIRTINPAYPEGMMLAILFANLFAPIFDYIVVQANIKRRRARTNG","721072","From GenBank (gi:15214142): The NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinal by two successive reactions, coupled with the transport of NA(+) ions from the cytoplasm to the periplasm. The first step is catalyzed by NQRF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one electron transfer pathway. The NQR complex located in the inner membrane (potential) and is composed of six subunits NqrA, NqrB, NqrC, NqrD, NqrE, and NqrF.From GenBank (gi:6093529): NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.","Na(+)-translocating NADH-quinone reductase subunit B","Inner membrane, Cytoplasm","","
InterPro
IPR004338
Family
NQR2 and RnfD
PF03116\"[38-405]TNQR2_RnfD_RnfE
InterPro
IPR010966
Family
NADH:ubiquinone oxidoreductase, Na(+)-translocating, B subunit
TIGR01937\"[3-405]TnqrB: NADH:ubiquinone oxidoreductase, Na(+)
noIPR
unintegrated
unintegrated
tmhmm\"[58-76]?\"[95-115]?\"[125-147]?\"[166-186]?\"[207-227]?\"[266-286]?\"[291-313]?\"[323-341]?\"[356-376]?\"[382-402]?transmembrane_regions


","BeTs to 7 clades of COG1805COG name: Na+-transporting NADH:ubiquinone oxidoreductase subunit 2Functional Class: CThe phylogenetic pattern of COG1805 is --------v----cefgh-n-j-it-Number of proteins in this genome belonging to this COG is","","Residues 3 to 79 match (7e-21) PD:PD336900 which is described as SUBUNIT B NQR NA-TRANSLOCATING NADH-QUINONE NAD NA-NQR UBIQUINONE SODIUM 1.6.5.- ","","","","","","","","","","","Thu Jan 16 10:58:26 2003","Thu Jan 16 11:00:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01032 is paralogously related to AA01810 (4e-22).","","","","","","Residues 38 to 405 (E-value = 9.7e-219) place AA01032 in the NQR2_RnfD_RnfE family which is described as NQR2, RnfD, RnfE family (PF03116)","","","","","Hayashi M, Shibata N, Nakayama Y, Yoshikawa K, Unemoto T.Korormicin insensitivity in Vibrio alginolyticus is correlated with a single point mutation of Gly-140 in the NqrB subunit of the Na(+)-translocating NADH-quinone reductase.Arch Biochem Biophys. 2002 May 15;401(2):173-7.PMID: 12054467Barquera B, Hellwig P, Zhou W, Morgan JE, Hase CC, Gosink KK, Nilges M, Bruesehoff PJ, Roth A, Lancaster CR, Gennis RB.Purification and characterization of the recombinant Na(+)-translocating NADH:quinone oxidoreductase from Vibrio cholerae.Biochemistry. 2002 Mar 19;41(11):3781-9.PMID: 11888296 Barquera B, Hase CC, Gennis RB.Expression and mutagenesis of the NqrC subunit of the NQR respiratory Na(+) pump from Vibrio cholerae with covalently attached FMN.FEBS Lett. 2001 Mar 9;492(1-2):45-9.PMID: 11248234Hayashi M, Nakayama Y, Unemoto T.Recent progress in the Na(+)-translocating NADH-quinone reductase from the marine Vibrio alginolyticus.Biochim Biophys Acta. 2001 May 1;1505(1):37-44. Review.PMID: 11248187","","Thu Jan 16 10:58:26 2003","1","","","" "AA01033","723495","722308","1188","GTGAAAAAAGGTCAGGTGATTTTTGAAGACAAAAAGAATCCGGGCGTTGTTTTTACCGCACCTGCCGGCGGCATGATCACTGCGATTCACCGCGGCGAGAAGCGCGTGTTACAGTCTGTAGTGATTAAAATTGAAGGCGATGCTGCGCTTTCTTTCGATAAATACCCGGCGGCTGAGCTAAGCGCGTTAACCGCTGAGCAAGTACGTAAAAACTTACAGGAATCGGGTTTGTGGACAGCGTTTCGTACCCGTCCGTTCAGTAAAGTGCCTGCAGTAGATAGCATACCTTCATCTATTTTCGTCAATGCCATGGATACGAATCCGTTAGCGGCGGATCCTTCAGTGGTGATTGCCGAAGCGGAAAATGATTTTGTAAATGGTTTAACGGTGTTAAGCCGTTTACATGAAGGTAACATTCATTTATGTAAAGCGCCTGACAATAAAATTCCAGGATCACATGCAAGTAATGTGATTGTGAACGAATTTTCAGGCCCTCACCCTGCCGGTTTGAGCGGTACCCATATTCACTTTATCGATCCTGTCGGCATTCAGAAAACCGTTTGGTATATCAACTATCAAGATGTAATTGCTATCGGTAGATTATTCACCACCGGTGAACTTTACACTGAACGTGTGATTTCTCTTGCCGGCCCGCAAGTGAAAAAACCACGTTTGGTCCGTACCGTGATCGGTGCAAATCTTTCTCAATTAACCAAAGATGAGATAAGTGCGGGTGAAAATCGTGTGATTTCAGGCTCTGTACTTTGTGGTAATACCGCGAAAGGTGCACATGATTATTTAGGTCGTTATGCCTTGCAGGTGTCTGTAATTGCAGAAGGTAATGAAAAAGAGTTGTTTGGCTGGATTACACCTCAACCAAATAAATATTCCATTACCCGGACCGTATTGGGTCATTTTAGTAAAAAGTTATTTAACTTTACAACTGCCGAAAATGGTGGTGAACGCGCAATGGTGCCGATCGGTAGTTATGAGCGCGTGATGCCGCTGGATATTTTACCAACTTTATTGTTACGTGATTTGATTGCAGGCGACACTGATGGTGCACAAGCATTAGGTTGTTTGGAGTTGGATGAAGAAGATTTAGCGCTTTGTTCATTTGTTTGCCCGGGCAAATATGAATATGGTTCAATCTTGCGTCAAGCGTTAGATAAGATTGAGAAGGAAGGT","","","48306","VKKGQVIFEDKKNPGVVFTAPAGGMITAIHRGEKRVLQSVVIKIEGDAALSFDKYPAAELSALTAEQVRKNLQESGLWTAFRTRPFSKVPAVDSIPSSIFVNAMDTNPLAADPSVVIAEAENDFVNGLTVLSRLHEGNIHLCKAPDNKIPGSHASNVIVNEFSGPHPAGLSGTHIHFIDPVGIQKTVWYINYQDVIAIGRLFTTGELYTERVISLAGPQVKKPRLVRTVIGANLSQLTKDEISAGENRVISGSVLCGNTAKGAHDYLGRYALQVSVIAEGNEKELFGWITPQPNKYSITRTVLGHFSKKLFNFTTAENGGERAMVPIGSYERVMPLDILPTLLLRDLIAGDTDGAQALGCLELDEEDLALCSFVCPGKYEYGSILRQALDKIEKEG","722310","From GenBank (gi:15214142): The NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinal by two successive reactions, coupled with the transport of NA(+) ions from the cytoplasm to the periplasm. The first step is catalyzed by NQRF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one electron transfer pathway. The NQR complex located in the inner membrane (potential) and is composed of six subunits NqrA, NqrB, NqrC, NqrD, NqrE, and NqrF.From GenBank (gi:6093529): NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.","Na(+)-translocating NADH-quinone reductase subunit A","Cytoplasm, Inner membrane","","
InterPro
IPR008703
Family
Na-translocating NADH-quinone reductase subunit A
PF05896\"[1-396]TNQRA
TIGR01936\"[1-396]TnqrA: NADH:ubiquinone oxidoreductase, Na(+)
noIPR
unintegrated
unintegrated
PD025201\"[1-396]TNQRA_HAEIN_P43955;


","BeTs to 7 clades of COG1726COG name: Na+-transporting NADH:ubiquinone oxidoreductase alpha subunitFunctional Class: CThe phylogenetic pattern of COG1726 is --------v-----efgh-n---it-Number of proteins in this genome belonging to this COG is","","Residues 1 to 396 match (5e-170) PD:PD025201 which is described as SUBUNIT A NA-TRANSLOCATING NQR REDUCTASE NADH-QUINONE OXIDOREDUCTASE 1.6.5.- UBIQUINONE NQR-1 ","","","","","","","","","","","Thu Jan 16 11:04:11 2003","Thu Jan 16 11:04:11 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01033 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 396 (E-value = 1.7e-258) place AA01033 in the NQRA family which is described as Na(+)-translocating NADH-quinone reductase subunit A (NQRA) (PF05896)","","","","","Barquera B, Hellwig P, Zhou W, Morgan JE, Hase CC, Gosink KK, Nilges M, Bruesehoff PJ, Roth A, Lancaster CR, Gennis RB.Purification and characterization of the recombinant Na(+)-translocating NADH:quinone oxidoreductase from Vibrio cholerae.Biochemistry. 2002 Mar 19;41(11):3781-9.PMID: 11888296 ","","Thu Jan 16 11:04:11 2003","1","","","" "AA01035","723837","723673","165","ATGGGCGCGGAAGTCCGTAAAATCAATACAGAATTTGAGTTTTATTTTTATCGGTTGGAGAGTGGTTATTCGGGCGTAATGTGGTATTTCGTCGCTTTCTTCTTTAATCATTTCAACAACCATCACTCAAGACGAGGTAATAACCTTTCGGTTATTGCTGTATTT","","","6631","MGAEVRKINTEFEFYFYRLESGYSGVMWYFVAFFFNHFNNHHSRRGNNLSVIAVF","723673","","hypothetical protein","Cytoplasm, Extracellular","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
tmhmm\"[14-34]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 09:16:18 2004","Wed Feb 25 09:16:18 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01035 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 09:16:18 2004","","","","","","","","","","","","","1","","","" "AA01037","723972","723859","114","ATGCAAAAATTGATTTTGTGCAAGAAAAGTGCATATTTTCACGAAAAATGCGCAAACAGACGGCTTTCAAAGTGGCGTGGACGTTATTATTTAGTTAAAATAAAGCGTTTATTT","","","4759","MQKLILCKKSAYFHEKCANRRLSKWRGRYYLVKIKRLF","723859","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 09:18:02 2004","Wed Feb 25 09:18:02 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01037 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 09:18:02 2004","","","","","","","","","","","","","1","","","" "AA01039","724312","724004","309","ATGACAAAACAACAAGAATTGGAACAGCGCTTACGGCAGGAATTTCGACCGCACTTTATTGCGGTTGAAAACGAAAGTTATATGCACAGTTCCGGGCGGGGTGCCGATTCGCATTTCAAAGTGGTGTTAGTGAGCGATGTATTTGAGGGGATCGGTAAAGTCGCCCGTCATCGCAAAATTTACCAATTCTTAGTACAGGATTTGCAGCAAGGCATTCATGCCTTGGCGCTCCATCTTTATACGTTATCCGAGTGGAAGGCCTTAGGGCAACAATTCCCGAAATCACCAAATTGTACCGGCGTGGGGCAA","","","12050","MTKQQELEQRLRQEFRPHFIAVENESYMHSSGRGADSHFKVVLVSDVFEGIGKVARHRKIYQFLVQDLQQGIHALALHLYTLSEWKALGQQFPKSPNCTGVGQ","724006","","transcriptional regulator (possible murein gene regulator)","Cytoplasm","","
InterPro
IPR002634
Family
BolA-like protein
PTHR12735\"[19-100]TBOLA-LIKE PROTEIN-RELATED
PF01722\"[10-85]TBolA
noIPR
unintegrated
unintegrated
G3DSA:3.30.300.90\"[2-87]Tno description
PTHR12735:SF3\"[19-100]TBOLA-LIKE PROTEIN CGI-143


","BeTs to 10 clades of COG0271COG name: Stress-induced morphogen (activity unknown)Functional Class: TThe phylogenetic pattern of COG0271 is -o----y------cefghsn-jx---Number of proteins in this genome belonging to this COG is","Significant hit ( 8.2e-20) to 2/2 blocks of the IPB002634 family, which is described as \"BolA-like protein\". Interpro entry for IP:IPR002634. IPB002634A 34-68 1e-13 IPB002634B 72-85 0.00017","Residues 24 to 84 match (4e-19) PD:PD004789 which is described as COMPLETE PROTEOME BOLA FAMILY TRANSCRIPTION BOLA/YRBA ACTIVATOR HOMOLOG REGULATOR REGULATION ","","","","","","","","","","","","Fri Dec 20 08:47:38 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01039 is paralogously related to AA02329 (7e-09).","","","","","","Residues 10 to 85 (E-value = 2.7e-28) place AA01039 in the BolA family which is described as BolA-like protein (PF01722)","","","","","Santos JM, Freire P, Vicente M, Arraiano CM. The stationary-phase morphogene bolA from Escherichia coli isinduced by stress during early stages of growth. Mol Microbiol 1999 May;32(4):789-98. PubMed: 10361282. ","","Fri Dec 20 08:47:38 2002","1","","","" "AA01040","724416","725006","591","ATGAAATTTAAGATGAAGTCTCTTACCCTGGGTACGGTTTTACTTTCCGGCGTATTATTAACCGGCTGCCAAAGCGAACCGAACACACTCACCTTCACCCTGGCGCCACCGAAAGCCTCAATGAATGTCAACCAATCCGCCGTGGTTTATGTCACCACCCGCGATTTGCGTAACACCCCGGAAATCAGCAGTTATGTAAAAGACGGACAATTACTCAAATTATCCGCCTCACCGGAACTGACCCAATTGTTCCAACAAATTGAACAACAGGATTTGGTCAGCAAAGGCTTCCGTATCGGCATGGCGAACAATTCCAATGCTGCCGTCACCGTAGATATTCAGCAATTTTATGCCAAAGTGAATCAAGGCAATTTACGCTACGACATTGACAGCAAAATTCAGCTTGCCATTCATGTTCAAGGTCGCAGAGGTCAATTCACGAAAAATATAAATGCCGGGCGCACGCACTCCGGTGCATTTTTCGCGCGAAATTCGGAAATTCAAAAAGTGTTAGGCGAAACCTTTAATGAAGTGGTGGAATCAATTTATAAAGACCAGGAAGTTGCTAACGCCATTAATCAATACGCCAAC","","","21794","MKFKMKSLTLGTVLLSGVLLTGCQSEPNTLTFTLAPPKASMNVNQSAVVYVTTRDLRNTPEISSYVKDGQLLKLSASPELTQLFQQIEQQDLVSKGFRIGMANNSNAAVTVDIQQFYAKVNQGNLRYDIDSKIQLAIHVQGRRGQFTKNINAGRTHSGAFFARNSEIQKVLGETFNEVVESIYKDQEVANAINQYAN","725008","","possible lipoprotein","Outer membrane, Periplasm","","
InterPro
IPR001547
Family
Glycoside hydrolase, family 5
PS00659\"[170-179]?GLYCOSYL_HYDROL_F5
InterPro
IPR005619
Family
Uncharacterized lipoprotein
PD036382\"[23-190]TQ9CLB6_PASMU_Q9CLB6;
PF03923\"[1-197]TLipoprotein_16
noIPR
unintegrated
unintegrated
PS51257\"[1-23]TPROKAR_LIPOPROTEIN
signalp\"[1-25]?signal-peptide


","No hits to the COGs database.","","Residues 23 to 192 match (1e-57) PD:PD036382 which is described as LIPOPROTEIN COMPLETE PROTEOME PRECURSOR YAJG MEMBRANE SIGNAL POLYMERASE/PROTEINASE HI0162 LIPOPROTEIN ","","","","","","","","","","","","Fri Dec 20 08:49:23 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01040 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 197 (E-value = 2e-64) place AA01040 in the Lipoprotein_16 family which is described as Uncharacterized lipoprotein (PF03923)","","","","","","","","1","","","" "AA01041","725115","724993","123","TTGTTTTTTTCCGGTTTTACGCTTTTGTGTGGGGGCAAATTAAAAAACACCGGAAAAATCTACCGCACTTTTAAGCGTAAAGTGCGGTGGATTTTAGAAAAGTTTTTTAGTTGGCGTATTGAT","","","4984","LFFSGFTLLCGGKLKNTGKIYRTFKRKVRWILEKFFSWRID","724993","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 09:19:23 2004","","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01041 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 09:19:23 2004","","","","","","","","","","","","","1","","","" "AA01042","726589","725513","1077","ATGAAGAAATATTTGATTTTAGCCTTGATTCCTTTTTTGTATGCGTGTGGTGGCGGTATGTCATATAAAAAGGGATTGGATTATGATGAGGCCTTTGCGAAAGATACGCGCGGATTGGATATTTTAACCGGACAATTCGCCAATAATATCGACCGCATTTGGGGGGTTAATGAGTTATTGGTGGCGAGCCGCAAAGACTATGTGAAATATACGGATCGTTACTACACCCGTAGCCACGTCAGTTTCGACGAAGGGTTGATTACCATTGAAACGCAAGCGGATTTAAACCGTTTGCATAATGCCATTGTGCATACGTTGTTGATGGGTTCCGATGCCAACGGTATTGATTTATTTACTTCCGGCGATGTGCCGATTAGTTCCCGCCCGTTTTTAGTGGGGCAGGTGATTGATAATCAAGGCGAGTCAATTATAGATCAATTTACTGCAGGCAATTTCGCTACTTATTTAATTCGGAATAAATTGCAAACCCGCCGTTTGGCGAATGGCCATCAGGTACAGTTCGTGGTGATTCCGATGATTGCCAACCACGTTGAAGTGCGGGCGCAAAAATACCTGCCGATCGTGCGTAAAGTGGCGCGTCATTACGGGCTGGATGAAAGCCTGATTCTCGGTATTATGCAAACGGAATCCAGTTTCAACCCGTATGCCATCAGTTATGCGAACGCGATGGGACTGATGCAGGTAGTGCCGCATACCGCAGGGCGTGATGTGTTCCAAATGAAAGGCATGAGCGGTCAGCCAAGCAAGGCTTACTTGTTCGATCCGGAGAAAAATATTGATACTGGCGCCTCTTATTTATGGTTGCTGCAAAATAAATATTTGGACGGCATTACCAATCCGACCTCGAAACGCTTTGCGATGATCTCCGCCTATAACAGCGGTGCCGGTGCGGTGTTGCGTGTGTTCAATGATGATAAAGATGTGGCGATAATGCAAATCAACCGGCTTTATCCGGAACAGATATATCGAATTTTAACTACCAACCATCCGTCTGCACAGGCGAGAAATTACCTGGTTAAAGTGGATAAAGCACAGAAGAGTTATCGTGTGCGTCGT","","","40491","MKKYLILALIPFLYACGGGMSYKKGLDYDEAFAKDTRGLDILTGQFANNIDRIWGVNELLVASRKDYVKYTDRYYTRSHVSFDEGLITIETQADLNRLHNAIVHTLLMGSDANGIDLFTSGDVPISSRPFLVGQVIDNQGESIIDQFTAGNFATYLIRNKLQTRRLANGHQVQFVVIPMIANHVEVRAQKYLPIVRKVARHYGLDESLILGIMQTESSFNPYAISYANAMGLMQVVPHTAGRDVFQMKGMSGQPSKAYLFDPEKNIDTGASYLWLLQNKYLDGITNPTSKRFAMISAYNSGAGAVLRVFNDDKDVAIMQINRLYPEQIYRILTTNHPSAQARNYLVKVDKAQKSYRVRR","725515","","membrane-bound lytic murein transglycosylase C","Outer membrane, Periplasm, Inner membrane, Cytoplasm","","
InterPro
IPR000189
Active_site
Prokaryotic transglycosylase, active site
PS00922\"[212-240]TTRANSGLYCOSYLASE
InterPro
IPR008258
Domain
Lytic transglycosylase, catalytic
PF01464\"[193-321]TSLT
noIPR
unintegrated
unintegrated
G3DSA:1.10.530.10\"[190-359]Tno description
PTHR21666\"[184-306]TPEPTIDASE-RELATED
PTHR21666:SF10\"[184-306]TLYTIC TRANSGLYCOSYLASE
PS51257\"[1-16]TPROKAR_LIPOPROTEIN
signalp\"[1-21]?signal-peptide


","BeTs to 14 clades of COG0741COG name: Soluble lytic murein transglycosylase and related regulatory proteins (some contain LysM/invasin domains)Functional Class: MThe phylogenetic pattern of COG0741 is -------qv---bcefghsnujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 8.3e-24) to 2/2 blocks of the IPB000189 family, which is described as \"SLT domain\". Interpro entry for IP:IPR000189. IPB000189A 216-240 4.2e-16 IPB000189B 259-273 3.5e-06","Residues 187 to 235 match (1e-16) PD:PD102249 which is described as PROTEOME COMPLETE TRANSGLYCOSYLASE MUREIN LYTIC HYDROLASE MEMBRANE-BOUND C 3.2.1.- GLYCOSIDASE ","","","","","","","","","","","","Fri Dec 20 08:51:31 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01042 is paralogously related to AA00777 (2e-07) and AA00077 (2e-07).","","","","","","Residues 193 to 321 (E-value = 2.4e-40) place AA01042 in the SLT family which is described as Transglycosylase SLT domain (PF01464)","","","","","Dijkstra,A.J. and Keck,W. Identification of new members of the lytic transglycosylasefamily in Haemophilus influenzae and Escherichia coli Microb. Drug Resist. 2 (1), 141-145 (1996) PubMed: 9158737 ","","Fri Dec 20 08:51:31 2002","1","","","" "AA01043","726870","726595","276","ATGGCAAGAATGGTGTTTTGTGAGCGTTTAAAACAGGAAGCCGAAGGGCTGGATTTTCAATTGTATCCGGGCGAATTGGGCAAACGCATTTTTGATTCTATTAGTAAACAGGCGTGGGGCGAGTGGATGAAAAAACAAACCATGCTGGTGAATGAGAAAAAGTTAAATATGATGAATGCGGAGCACCGCAAACTGCTGGAGCAGGAAATGGTGAATTTTTTGTTTGAAGGCAAAGATGTGCATATTGAAGGTTATACACCGCCGGAAGCGAAAGAA","","","10879","MARMVFCERLKQEAEGLDFQLYPGELGKRIFDSISKQAWGEWMKKQTMLVNEKKLNMMNAEHRKLLEQEMVNFLFEGKDVHIEGYTPPEAKE","726597","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR007457
Family
Fe(II) trafficking protein YggX
PD029191\"[1-76]TY760_HAEIN_P44048;
PIRSF029827\"[1-90]TFe(II) trafficking protein YggX
PF04362\"[1-88]TIron_traffic


","BeTs to 6 clades of COG2924COG name: Fe-S cluster protector proteinFunctional Class: C,OThe phylogenetic pattern of COG2924 is --------------efghsn------Number of proteins in this genome belonging to this COG is","","Residues 1 to 76 match (2e-30) PD:PD029191 which is described as PROTEOME COMPLETE VC0451 CYTOPLASMIC NMA0419 RSC1235 BU553 XF1908 PA5148 HI0760 ","","","","","","","","","","","","Fri Dec 20 08:52:28 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01043 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 88 (E-value = 4.1e-69) place AA01043 in the DUF495 family which is described as Protein of unknown function (DUF495) (PF04362)","","","","","","","","1","","","" "AA01044","728038","726851","1188","GTGAAAAACACAGTTAAAAATAACCGCACTTTTATTGAATTATCAGGATTTATGCCGGCTCAATCATCTTCCAATGCGCCTTTTGCCCACGCCGTGCTGACGTGGTACGCCAAGTTCGGGCGGAAAAATTTGCCGTGGCAGCAAAATAAAACTTTATACGGCGTTTGGTTGTCCGAAGTAATGTTGCAGCAAACGCAAGTGACGACGGTGATACCTTATTTCGAGCGCTTTGTAAAAACGTTCCCGAATTTGACCGCACTTGCCAATGCGCCTTTGGACGAAGTGTTGCATTTGTGGACGGGCTTGGGCTATTACGCGCGGGCGCGCAATTTGCATAAAGCGGCGCAGATCATGCGTGATCAACACGGCGGCGAATTCCCGACGGAATTTGAACAGGTATGGGCGTTGCCCGGCGTGGGGCGCAGCACGGCGGGGGCGGTGTTGTCTTCTTGTTTAAATGCGCCTTATCCGATTTTGGACGGCAATGTGAAGCGGGTACTGTCCCGTTATTTTGCGGTGAGCGGCTGGCCGGGCGAAAAGAAAACGGAAGATCATTTGTGGCACTTAACGGCGCAGGTGACGCCGACAGAACAGGTGGCAGATTTTAATCAGGCGATGATGGACATCGGCGCCATGGTGTGTACCCGTTCCAAGCCGAAATGCGAACTTTGCCCGCTGAAAAGCGATTGCAAGGCGAACGCCGAACAAAACTGGCAGGCGTATCCCGGCAGAAAACCGAAGAAAGTCTTGCCGGAGCGGGAAAGTTATTTTTTGCTGTTGGAAAAAGATGGCAAAATTGCGTTGGAACAACGGGACAATGCCGGTTTATGGGGCGGGTTGTACTGTTTTCCGCAATTTTCCGAGAAGCAGGAATTGCTGGCGTATTTAGCGGCAAACGGAATTCGGCAATATCAGGAGTGGACGGCATTTCGCCATACCTTCAGCCATTTCCATCTGGATATTTATCCGATTTATGCGCAAGTGGACACGCCGAAAGCGTTGGCGGAAGAGAACCGTTCCCACCGGCAAAAAGTGGCTGAAACGGCGGGGGAATATCAATCAGACCTATTAAGTGCGGTTAAATATTGGTATGATCCACAAAATCCTGAACCTATCGGGTTAGCAGCGCCCGTGAAGAATTTATTAACTCAATATGTAAGGAATCATTATGGCAAGAATGGTGTTTTG","","","44982","VKNTVKNNRTFIELSGFMPAQSSSNAPFAHAVLTWYAKFGRKNLPWQQNKTLYGVWLSEVMLQQTQVTTVIPYFERFVKTFPNLTALANAPLDEVLHLWTGLGYYARARNLHKAAQIMRDQHGGEFPTEFEQVWALPGVGRSTAGAVLSSCLNAPYPILDGNVKRVLSRYFAVSGWPGEKKTEDHLWHLTAQVTPTEQVADFNQAMMDIGAMVCTRSKPKCELCPLKSDCKANAEQNWQAYPGRKPKKVLPERESYFLLLEKDGKIALEQRDNAGLWGGLYCFPQFSEKQELLAYLAANGIRQYQEWTAFRHTFSHFHLDIYPIYAQVDTPKALAEENRSHRQKVAETAGEYQSDLLSAVKYWYDPQNPEPIGLAAPVKNLLTQYVRNHYGKNGVL","726853","","A/G-specific adenine glycosylase","Periplasm","","
InterPro
IPR000086
Domain
NUDIX hydrolase
G3DSA:3.90.79.10\"[256-396]Tno description
InterPro
IPR003265
Domain
HhH-GPD
PF00730\"[57-192]THhH-GPD
SM00478\"[61-212]TENDO3c
InterPro
IPR003651
Domain
Iron-sulfur cluster loop
SM00525\"[213-233]TFES
InterPro
IPR004035
Domain
Endonuclease III, FCL
PS00764\"[214-230]TENDONUCLEASE_III_1
InterPro
IPR005760
Family
A/G-specific adenine glycosylase MutY, bacterial form
TIGR01084\"[27-300]TmutY: A/G-specific adenine glycosylase
noIPR
unintegrated
unintegrated
G3DSA:1.10.1670.10\"[126-250]Tno description
PTHR10359\"[45-291]TA/G-SPECIFIC ADENINE GLYCOSYLASE/ENDONUCLEASE III
PTHR10359:SF1\"[45-291]TA/G-SPECIFIC ADENINE GLYCOSYLASE MUTY


","No hits to the COGs database.","Significant hit ( 1.6e-18) to 3/5 blocks of the IPB001502 family, which is described as \"Endonuclease III\". Interpro entry for IP:IPR001502. IPB001502C 122-153 5.2e-06 IPB001502D 159-185 1.4 IPB001502E 203-230 1.8e-08","Residues 242 to 339 match (6e-08) PD:PD537730 which is described as PROBABLE GLYCOSYLASE PROTEOME A/G-SPECIFIC GLYCOSIDASE COMPLETE 3.2.2.- ADENINE HYDROLASE ","","","","","","","","","","","","Fri Dec 20 08:54:28 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01044 is paralogously related to AA01814 (7e-10).","","","","","","Residues 57 to 192 (E-value = 5.2e-22) place AA01044 in the HhH-GPD family which is described as HhH-GPD superfamily base excision DNA repair protein (PF00730)","","","","","Michaels,M.L., Pham,L., Nghiem,Y., Cruz,C. and Miller,J.H. MutY, an adenine glycosylase active on G-A mispairs, hashomology to endonuclease III Nucleic Acids Res. 18 (13), 3841-3845 (1990) PubMed: 2197596 Tsai-Wu,J.J., Radicella,J.P. and Lu,A.L. Nucleotide sequence of the Escherichia coli micA generequired for A/G-specific mismatch repair: identity of micA and mutY J. Bacteriol. 173 (6), 1902-1910 (1991) PubMed: 2001994 Guan,Y., Manuel,R.C., Arvai,A.S., Parikh,S.S., Mol,C.D., Miller,J.H., Lloyd,S. and Tainer,J.A. MutY catalytic core, mutant and bound adenine structuresdefine specificity for DNA repair enzyme superfamily Nat. Struct. Biol. 5 (12), 1058-1064 (1998) PubMed: 9846876 ","","Fri Dec 20 08:54:28 2002","1","","","" "AA01045","728204","728968","765","ATGTTAGAAACCCAATCATCAGATTCCATACAACCGACCTTTGCCGACCAAAAACGCAAAACCGTTGAATCCGCCGAATTTACCGCCGATGGGCGCTACAAGCGCAAAGTCCGCAGCTTCGTGTTACGCACCGGACGTTTAAGCGATTACCAAAAAAACGCCATGAACCAAAACTGGGCGACATTCGGCTTGGACTACCAACCACAACCTTTTGATTTCCAAGCGATTTATGGCAACGACAATCCCGTGATTTTAGAAATCGGCTTCGGCATGGGCAGTTCGCTGGTGGAAATGGCGGCGCAAAATCCCGATAAAAACTATTTGGGCATTGAAGTGCACACCCCGGGCGTGGGTGCTTGTATTGCATACGCCGTGGAAAAAGGCGTGACCAATTTGCGTGTGATTTGTCACGATGCCACCGAAATTCTGCGCGACAGCATTGGCAATCACAGCCTCGGCGGGTTACAACTGTTCTTCCCCGATCCGTGGCACAAAGCCAGACATCACAAACGCCGCATTGTGCAACCACATTTTATTGACGGTTTATTGAACAAATTACACGAAGGCGCCTTTATTCACATGGCGACCGACTGGCAAGACTATGCCGAACACATGCTGGAGGTGCTAAGCCAATACCCGCAGCTGCGCAATACCTCCGTCGCTAACGACTATATCCCGCGTCCCGATTTTCGCCCGCTGACTAAATTTGAACAACGCGGTCACCGTCTCGGGCATGGCGTGTGGGATTTGTATTTCGTCAAATCA","","","29149","MLETQSSDSIQPTFADQKRKTVESAEFTADGRYKRKVRSFVLRTGRLSDYQKNAMNQNWATFGLDYQPQPFDFQAIYGNDNPVILEIGFGMGSSLVEMAAQNPDKNYLGIEVHTPGVGACIAYAVEKGVTNLRVICHDATEILRDSIGNHSLGGLQLFFPDPWHKARHHKRRIVQPHFIDGLLNKLHEGAFIHMATDWQDYAEHMLEVLSQYPQLRNTSVANDYIPRPDFRPLTKFEQRGHRLGHGVWDLYFVKS","728970","","S-adenosylmethionine-dependent methyltransferase","Cytoplasm","","
InterPro
IPR003358
Family
Putative methyltransferase
PF02390\"[59-255]TMethyltransf_4
InterPro
IPR004395
Family
Conserved hypothetical protein 91
TIGR00091\"[65-255]TTIGR00091: tRNA (guanine-N(7)-)-methyltrans
noIPR
unintegrated
unintegrated
PTHR23417\"[46-253]T3-DEOXY-D-MANNO-OCTULOSONIC-ACID TRANSFERASE/TRNA (GUANINE-N(7)-)-METHYLTRANSFERASE
PTHR23417:SF1\"[46-253]TTRNA (GUANINE-N(7)-)-METHYLTRANSFERASE


","BeTs to 19 clades of COG0220COG name: Predicted S-adenosylmethionine-dependent methyltransferaseFunctional Class: RThe phylogenetic pattern of COG0220 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1e-53) to 3/3 blocks of the IPB003358 family, which is described as \"Putative methyltransferase\". Interpro entry for IP:IPR003358. IPB003358A 85-111 2.3e-17 IPB003358B 151-169 3.4e-12 IPB003358C 170-209 1.8e-21","","","","","","Wed Feb 19 08:29:30 2003","","","","","","","Fri Dec 20 09:03:37 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01045 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 59 to 255 (E-value = 6.1e-94) place AA01045 in the Methyltransf_4 family which is described as Putative methyltransferase (PF02390)","","","","","Martin JL, McMillan FM.SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold.Curr Opin Struct Biol. 2002 Dec;12(6):783-93.PMID: 12504684 ","","Wed Feb 19 08:29:30 2003","1","","","" "AA01046","729002","729340","339","ATGGCTATTAAACGTAATCAAAGACAACGCAAAAAAATGCACCTCGCCGAATTCCAGGAATTAGGCTTTTTAGTGCAATGGCAATTCGCCGAGGGCACTTCCGTAGAACAAATCGACAACACCGTCGACCGCTTCATCAGCGAAGTGATCCAACCAAACGGCTTGGCATACGAAGGCAGCGGTTACTTACATTGGGAAGGCTTGGTTTGCCTGGAGAAAATCGGCAAATGCGACGCGTCTCACCAAGAATTAGTGAAAAACTGGCTAACCCAAAACGGCTTACAACAAGTGGAAGTGAGCGAGTTGTTTGATATTTGGTGGGATTATCCTGCGAAAGAC","","","13183","MAIKRNQRQRKKMHLAEFQELGFLVQWQFAEGTSVEQIDNTVDRFISEVIQPNGLAYEGSGYLHWEGLVCLEKIGKCDASHQELVKNWLTQNGLQQVEVSELFDIWWDYPAKD","729342","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR007416
Family
Protein of unknown function DUF469
PF04320\"[1-107]TDUF469
noIPR
unintegrated
unintegrated
PD030453\"[6-106]TYGGL_HAEIN_P44649;


","BeTs to 4 clades of COG3171COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3171 is --------------ef-h-n------Number of proteins in this genome belonging to this COG is","","Residues 1 to 108 match (6e-46) PD:PD030453 which is described as COMPLETE PROTEOME CYTOPLASMIC PA3046 YPO0950 STY3263 YGGL HI0341 PM1316 ORF ","","","","","","","","","","","","Fri Dec 20 09:06:36 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01046 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 107 (E-value = 2.8e-76) place AA01046 in the DUF469 family which is described as Protein with unknown function (DUF469) (PF04320)","","","","","","","","1","","","" "AA01048","729562","730557","996","ATGAAGATTAATCAATTCAAACTTGCAGCTCTTGCTACTGCGTTAGCTTTCTCTACTGCCGCTTTCGCCGACATCACTGTATATAGCGGTCAGCATAAAGAAGGAGCAAAAGCTGTCGCCGATGCTTTTACCAAAGAAACCGGGATTAAAGTAACACTTAACAGTGCGAAAAGCGAGCAACTTGCCGGTCAGTTAAAAGAAGAAGGCGATAAAACCCCTGCCGATGTCTTCTATTCGGAGCAAACTGCACCATTTGCTGCGTTATCCGAAGCGGGATTGTTAGAACCGCTTTCTGCCGAAACCATTAAACAAACAGAGTACAAAGGCGTGCCTGTAGCGCCAAAAAAAGACTGGATTGCGTTAAGTGGTCGCTCTCGTGTAGTGGTTTATGATAAAAATAAACTCTCTGAGAAAGACATGGAAAAATCTGTATTGGATTACGCCACGCCGAAATGGAAAGATAAAATCGGTTATGTGCCGACTTCCGGGGCATTTTTGGAACAAGTTATTGCTATCACTAAATTAAAAGGTGAAAAAGCCGCGTTGGATTGGCTGAAGGGCTTAAAAGAAAATGGCAAACTTTATGCAAAAAACAGCGTAGCACTCCAAGCGGTAGAAAACGGCGAAGTTCCGGCAGCACTAATTAATAATTATTATTGGTATGCTTTAGCAAAAGAAAAAGGCGAAGATAAACTAAACTCCCGTTTATATTTCATTCGCCATCAAGACCCGGGTGCGTTGGTGACCTATTCCGGCGCTGCAGTGTTAAAAGGATCGAAAAATAAAGAAGAAGCGAAAAAATTTGTGGATTTCTTAGCCGGTAAAAAAGGTCAGGAAGCCTTTACTGCTGTGCGTGCAGAATACCCGCTACGTCCTGACGTACACTCTCCATTCAACATGGAACCTTACGCAAAATTAGAAGCTCCTGAGGTCAGCGCAACCACTGCAAAAGATAGGGAAAATGCCAATAAATTGATTGAACAGGCAGGATTGAAA","","","36278","MKINQFKLAALATALAFSTAAFADITVYSGQHKEGAKAVADAFTKETGIKVTLNSAKSEQLAGQLKEEGDKTPADVFYSEQTAPFAALSEAGLLEPLSAETIKQTEYKGVPVAPKKDWIALSGRSRVVVYDKNKLSEKDMEKSVLDYATPKWKDKIGYVPTSGAFLEQVIAITKLKGEKAALDWLKGLKENGKLYAKNSVALQAVENGEVPAALINNYYWYALAKEKGEDKLNSRLYFIRHQDPGALVTYSGAAVLKGSKNKEEAKKFVDFLAGKKGQEAFTAVRAEYPLRPDVHSPFNMEPYAKLEAPEVSATTAKDRENANKLIEQAGLK","730559","","iron binding protein afuA, periplasmic protein","Periplasm","","
InterPro
IPR006059
Family
Bacterial extracellular solute-binding protein, family 1
PF01547\"[6-279]TSBP_bac_1
InterPro
IPR006061
Domain
Bacterial extracellular solute-binding family 1
PS01037\"[120-137]TSBP_BACTERIAL_1
InterPro
IPR011587
Domain
Prokaryotic extracellular metal-binding protein
PD008688\"[201-282]TMBP_prokaryotic
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[23-96]T\"[125-332]TG3DSA:3.40.190.10
SSF53850\"[24-332]TSSF53850


","BeTs to 12 clades of COG1840COG name: ABC-type iron/thiamine transport systems, periplasmic componentFunctional Class: HThe phylogenetic pattern of COG1840 is -o--kz---d-lbcefghsnuj--t-Number of proteins in this genome belonging to this COG is","","Residues 38 to 279 match (2e-07) PD:PD566445 which is described as PROTEOME COMPLETE PERIPLASMIC THIAMINE-BINDING ","","","","","","","","","","","","Fri Dec 20 09:10:42 2002","","Tue Mar 16 08:19:17 2004","","Tue Mar 16 08:19:17 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01048 is paralogously related to AA01642 (3e-14), AA00696 (5e-14), AA00698 (8e-12) and AA01479 (6e-07).","Tue Mar 16 08:19:17 2004","","","","","Residues 6 to 279 (E-value = 1e-23) place AA01048 in the SBP_bac_1 family which is described as Bacterial extracellular solute-binding protein (PF01547)","Tue Mar 16 08:19:17 2004","","","Willemsen,P.T., Vulto,I., Boxem,M. and de Graaff,J.Characterization of a periplasmic protein involved in ironutilization of Actinobacillus actinomycetemcomitansJ. Bacteriol. 179 (15), 4949-4952 (1997)PubMed: 9244288Fong KP, Chung WO, Lamont RJ, Demuth DR.Intra- and interspecies regulation of gene expression by Actinobacillus actinomycetemcomitans LuxS.Infect Immun. 2001 Dec;69(12):7625-34.PMID: 11705942","Chin N, Frey J, Chang CF, Chang YF.Identification of a locus involved in the utilization of iron by Actinobacillus pleuropneumoniae.FEMS Microbiol Lett. 1996 Sep 15;143(1):1-6.PMID: 8807793","Mon Feb 17 13:56:11 2003","Mon Feb 17 13:56:11 2003","1","","","" "AA01050","730641","732158","1518","TTGAACCGTCGCCTCCCATTCTGGCTCACCATTTTGATTCTACTTATCAGCCTGCCGTTACTGTTGCCGTTTTTGTATGTTGTCGTACGGGCAATTGAGGTAGGTTGGGATCGTAGTATTGAACTGTTATGGCGTCCCCGCATGTGGGAATTATTAAGCAATACCCTGCTTCTGATGGTTTGCGTGACCTCCGGTGCCATTACCCTTGGCACTTTTTGTGCATTCTTGCTGGAGCGCTATCGTTTTTGGGGAAAATCCTTTTTTCAGGTGTCAATGACATTACCCTTGTGTATCCCTGCCTTTGTCAGTTGTTTTACTTGGATTAGTCTTACTTTCCGCGTTGAAGGCTTTTGGGGCACTATCGGAATTATGACCTTAAGCTCGTTTCCTCTTGCTTATTTACCTGTCGCTGCCACTTTAAAACGATTGGATCGTTCACTGGAAGAAGTCAGTTTTTCCCTTGGCAAGAACCTAAGCTACACCTTTTGGCACGCTATTTTCCCGCAGCTAAAACCGGCCATCGGCAGCAGTTTTTTACTCATTGCGTTACATATGCTGGTGGAATTCGGTGCGGTATCCATTCTCAATTACCAAACCTTCACTACGGCTATTTTTCAAGAATACGAAATGTCCTTTAACAACAGCACGGCGGCATTACTTTCAGCAGTATTGATGGTGATTTGTGCCTTTATTGTCTTTGGTGAAATTTTCTTTCGTGGACAACAAACCCTTTATAACAGTGGCAAAGGTGTCGTCCGTCCTTATCCTGTAAAAAACTTAAGTGGTGGCAAACAAGCACTGATTATCGTCTTTTTCATGACGATCCTTATCCTCAGTATAGGCATACCTTTTACCATGCTGATTTACTGGCTGATAGTGGGGCATTCTATTGAAAGTGCGGTCGATTTCCATGCTTTTTTTGAAGCCTTCAGTAACTCATTGGTCATTTCGGCTTTAGGTACAATACTGACCGTCGTCTGTGCCCTGCCTTTGGTGTGGAGTGCCGTGCGCTATCGTAGCCGTCTCACCATCTGGATTGATCGCCTGCCTTATTTATTGCATGCCGTACCGGGCTTGGTTATCGCATTGGCATTAGTATATTTCACTATCAACTACGCCTATTCCTTCTACCAAACCTTTCTCATGGTGGTCATCGCCTATTTAATGCTCTATCTGCCTATGGCACAAACCACCTTGCGTAGCTCTTTGGAACAAATCTCCGACAAGATGGAAAAAGTGGGACAAAGTCTCGGCAGAAGTCATTTTTATATTTTCCGTACACTCACCTTTCCCGCAATTTTACCTGGCATCGCCGCAGCGTTTGCATTGGTGTTTCTAAATCTGATGAAAGAACTTACTGCTACTTTATTGCTCACCCCAAATGACATCAAAACCCTCTCTATTGCTGTCTGGGAATACACCAGCGACGCCCAATATGCCGCCGCCACGCCTTATGCCGTAATGCTTGTACTCTTTTCCGGTATTCCGGTGTTTTTGTTGAAGAAATATGCGTTTAAA","","","57146","LNRRLPFWLTILILLISLPLLLPFLYVVVRAIEVGWDRSIELLWRPRMWELLSNTLLLMVCVTSGAITLGTFCAFLLERYRFWGKSFFQVSMTLPLCIPAFVSCFTWISLTFRVEGFWGTIGIMTLSSFPLAYLPVAATLKRLDRSLEEVSFSLGKNLSYTFWHAIFPQLKPAIGSSFLLIALHMLVEFGAVSILNYQTFTTAIFQEYEMSFNNSTAALLSAVLMVICAFIVFGEIFFRGQQTLYNSGKGVVRPYPVKNLSGGKQALIIVFFMTILILSIGIPFTMLIYWLIVGHSIESAVDFHAFFEAFSNSLVISALGTILTVVCALPLVWSAVRYRSRLTIWIDRLPYLLHAVPGLVIALALVYFTINYAYSFYQTFLMVVIAYLMLYLPMAQTTLRSSLEQISDKMEKVGQSLGRSHFYIFRTLTFPAILPGIAAAFALVFLNLMKELTATLLLTPNDIKTLSIAVWEYTSDAQYAAATPYAVMLVLFSGIPVFLLKKYAFK","732160","","iron(III) ABC transporter, permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR000515
Family
Binding-protein-dependent transport systems inner membrane component
PF00528\"[48-251]T\"[306-505]TBPD_transp_1
PS50928\"[52-233]T\"[310-500]TABC_TM1
noIPR
unintegrated
unintegrated
PTHR10117\"[259-291]TTRANSIENT RECEPTOR POTENTIAL CHANNEL
PTHR10117:SF9\"[259-291]TTRANSIENT RECEPTOR POTENTIAL CHANNEL 7
signalp\"[1-31]?signal-peptide
tmhmm\"[5-27]?\"[57-77]?\"[87-107]?\"[117-137]?\"[177-197]?\"[216-238]?\"[268-290]?\"[309-329]?\"[350-370]?\"[374-392]?\"[428-448]?\"[480-500]?transmembrane_regions


","BeTs to 13 clades of COG1178COG name: ABC-type iron/thiamine transport systems, permease componentsFunctional Class: HThe phylogenetic pattern of COG1178 is -o--kz---d--bcefgh-nuj--t-Number of proteins in this genome belonging to this COG is","","Residues 146 to 241 match (8e-09) PD:PD075490 which is described as FBPB ","","","","","","","","","","","","Fri Dec 20 09:26:04 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01050 is paralogously related to AA00699 (7e-27), AA01644 (1e-23), AA01866 (6e-17), AA01780 (1e-11), AA01950 (9e-11), AA02719 (2e-06), AA01948 (2e-06), AA01649 (2e-06) and AA02720 (3e-06).","","","","","","Residues 306 to 505 (E-value = 5.2e-11) place AA01050 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component (PF00528)","","","","Graber KR, Smoot LM, Actis LA.Expression of iron binding proteins and hemin binding activity in the dental pathogen Actinobacillus actinomycetemcomitans.FEMS Microbiol Lett. 1998 Jun 15;163(2):135-42.PMID: 9673015","Adhikari P, Kirby SD, Nowalk AJ, Veraldi KL, Schryvers AB, Mietzner TA.Biochemical characterization of a Haemophilus influenzae periplasmic iron transport operon.J Biol Chem. 1995 Oct 20;270(42):25142-9.PMID: 7559648Sanders,J.D., Cope,L.D. and Hansen,E.J.Identification of a locus involved in the utilization of iron byHaemophilus influenzaeInfect. Immun. 62 (10), 4515-4525 (1994)PubMed: 7927717","Fri Dec 20 09:44:07 2002","Fri Dec 20 09:44:07 2002","1","","","" "AA01051","732183","733232","1050","ATGAACTTACCATTGCTTCAAATCGACCATCTCAACAAATATTTCGGGCAAACACATGTTCTGCACGATATTTCGTTGCAACTTAACAGTGGAGAAATCTTGTTTTTATTAGGTCCCTCCGGCTGTGGCAAAACCACATTGTTACGTGCCATTGCCGGCTTTGAACAGCCTGATAGCGGCGAAATTCGCCTAAAAGAGCGGTTGATTTTCGGTGCAAATTGTAATGTGCCGACCCAACAGCGCCATTTAGGTTATGTCGTGCAAGAAGGCGTGCTATTTCCTCATTTGAACGTATATCGCAATATTGCTTATGGCTTGGGTAACGGCAAAGGTAACAGCCCGAAAGAACGCGCACGGGTTGAACAGGTAATGTTGCTTACCGGTATTGTTGAACTTGCCGAACGTTTTCCTCATCAGCTTTCCGGTGGACAGCAACAACGCGTAGCGCTCGCTCGGGCTATCGCCCCCAATCCTGAATTAATTTTGCTGGATGAACCCTTTAGTGCCCTGGATGAACACCTGCGCCAGAAAATTCGTCACGATATGCTGCAAGCCCTACGCCAAAGCGGCACCTCGGCGATTTTCGTCACCCATGATCGCGATGAGGCCCTACGTTATGCCGATAAAATCGCGGTGATCCAAGACGGGCGAATTTTACAAATCGCTGATCCGCACACCCTTTATCACGCTCCGCAACACCTCGCTGCCGCTACCTTTATCGGCGATGCCATCACATTACCCGCAACCTTAAATAACGCTTCAAATGCACATTGCCAACTCGGTGATATTCCCATTATCGACAAAAGCGGCGGACATGCTACCGGTACGCTGCTCCTGCGCCCGGAACAATTCAGTCTGCTAAAAACACCGAAAAAACCCACCGCACTTTTTAACGCGATTATTAAACAGGTAGAGTTTAGAGGCAAAACAACCATTGCTCAGATTAAGGTAAATGGAGTGGAAGTGAATTTAGAAGAGCGTTATAGCGAGGGATTACGTGTTGGTGAAGAAGTTGAGATTTATTTATATGGCGAAGGGTTATTTTATGAA","","","39025","MNLPLLQIDHLNKYFGQTHVLHDISLQLNSGEILFLLGPSGCGKTTLLRAIAGFEQPDSGEIRLKERLIFGANCNVPTQQRHLGYVVQEGVLFPHLNVYRNIAYGLGNGKGNSPKERARVEQVMLLTGIVELAERFPHQLSGGQQQRVALARAIAPNPELILLDEPFSALDEHLRQKIRHDMLQALRQSGTSAIFVTHDRDEALRYADKIAVIQDGRILQIADPHTLYHAPQHLAAATFIGDAITLPATLNNASNAHCQLGDIPIIDKSGGHATGTLLLRPEQFSLLKTPKKPTALFNAIIKQVEFRGKTTIAQIKVNGVEVNLEERYSEGLRVGEEVEIYLYGEGLFYE","733234","","iron (III) ABC transporter, ATP-binding protein","Cytoplasm, Inner membrane","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[139-182]TFBC2_HAEIN_P44513;
PF00005\"[31-216]TABC_tran
PS50893\"[6-240]TABC_TRANSPORTER_2
PS00211\"[140-154]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[30-217]TAAA
InterPro
IPR013611
Domain
Transport-associated OB
PF08402\"[277-342]TTOBE_2
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[4-249]Tno description
PTHR19222\"[6-251]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF43\"[6-251]TSPERMIDINE/PUTRESCINE ABC TRANSPORTER


","BeTs to 3 clades of COG3841COG name: ABC-type iron transport systems, ATPase componentsFunctional Class: PThe phylogenetic pattern of COG3841 is ------------b-efgh-n----t-Number of proteins in this genome belonging to this COG is","Significant hit ( 4.9e-40) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 20-66 1.1e-17 IPB001140B 137-175 9.7e-17 IPB001140C 193-222 0.0096","Residues 90 to 218 match (1e-08) PD:PD588333 which is described as ATP-BINDING PROTEOME COMPLETE COMPONENT POSSIBLE COBALT ABC SUBUNIT ABC- PROTEIN ","","","","","","","","","","","","Fri Dec 20 09:39:13 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01051 is paralogously related to AA02718 (4e-55), AA01645 (3e-48), AA01656 (6e-47), AA00700 (8e-47), AA02353 (3e-39), AA00858 (7e-36), AA01947 (2e-34), AA01779 (7e-33), AA01867 (1e-31), AA01524 (1e-31), AA01684 (2e-29), AA00415 (1e-28), AA02320 (4e-28), AA01616 (5e-28), AA00799 (7e-28), AA02080 (2e-27), AA02324 (3e-27), AA02440 (5e-26), AA02140 (1e-24), AA01568 (3e-24), AA02899 (8e-24), AA00933 (2e-22), AA01820 (3e-22), AA01422 (9e-22), AA01824 (8e-21), AA01456 (2e-20), AA02550 (3e-19), AA02152 (3e-19), AA01510 (6e-19), AA01757 (2e-18), AA02805 (4e-18), AA00207 (5e-18), AA02898 (5e-17), AA02786 (3e-16), AA00751 (8e-16), AA01509 (4e-15), AA00061 (2e-14), AA02484 (4e-14), AA02642 (9e-14), AA01961 (9e-14), AA01393 (9e-14), AA02573 (2e-13), AA02225 (4e-13), AA02609 (6e-13), AA01569 (1e-12), AA02606 (2e-12), AA02331 (2e-11), AA00591 (2e-09), AA01555 (5e-09), AA00934 (1e-08), AA02226 (1e-07), A02145 (2e-07), AA02146 (6e-07) and AA01291 (2e-04).","","","","","","Residues 31 to 216 (E-value = 7.2e-64) place AA01051 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","Graber KR, Smoot LM, Actis LA.Expression of iron binding proteins and hemin binding activity in the dental pathogen Actinobacillus actinomycetemcomitans.FEMS Microbiol Lett. 1998 Jun 15;163(2):135-42.PMID: 9673015","Adhikari P, Kirby SD, Nowalk AJ, Veraldi KL, Schryvers AB, Mietzner TA.Biochemical characterization of a Haemophilus influenzae periplasmic iron transport operon.J Biol Chem. 1995 Oct 20;270(42):25142-9.PMID: 7559648Sanders JD, Cope LD, Hansen EJ.Identification of a locus involved in the utilization of iron by Haemophilus influenzae.Infect Immun. 1994 Oct;62(10):4515-25.PMID: 792771","Fri Dec 20 09:43:20 2002","Fri Dec 20 09:43:20 2002","1","","","" "AA01053","733807","733259","549","GTGCGCTTAGGTTGGGATTCTACGGAATTCGCTTACGACATTGCCGACGCGGTACAACAAGGCGGCGCCACGGAAATCGCCATTCACGGACGCACCAAAACCGATGGCTACCGCGCCGATCGCATCAATTGGCAAAAAATCGGCGAAATCCGTCAAAAATTGAAGATTCCCGTTATCGCCAACGGCGAAATTTGGCGTTGGGCGGACGGGCAACAATGCCGCGACGTCACCGGCTGCGAGGATCTGATGGTGGGGCGTGGTGCGTTAAATATCCCGAATTTAAGTCGGGTGTTGAAACGTAATGCCGCGCCCTTAAGCTGGGCTGAAATCATGCCGATTCTGCGTAAATACGCCGCACTGGAAAACTGCCATGACAGCGGGTTTTATCATGTGGCGCGCATTAAGCAGTGGTTGCAGTATTTAAAATATGAATACGCAGAAGCCGCTGACCTGTTTGAGATGGTGAAGTGCTGTGATGATGGGCGTAAGTTAAAAGGGATTTTGGATTCCTATTATGTGGATAAAAACATCTCAATAACAATCCGGATT","","","21138","VRLGWDSTEFAYDIADAVQQGGATEIAIHGRTKTDGYRADRINWQKIGEIRQKLKIPVIANGEIWRWADGQQCRDVTGCEDLMVGRGALNIPNLSRVLKRNAAPLSWAEIMPILRKYAALENCHDSGFYHVARIKQWLQYLKYEYAEAADLFEMVKCCDDGRKLKGILDSYYVDKNISITIRI","733261","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR001269
Family
Dihydrouridine synthase, DuS
PF01207\"[1-176]TDus
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[1-100]Tno description
noIPR
unintegrated
unintegrated
PTHR11082\"[1-101]TTRNA-DIHYDROURIDINE SYNTHASE
PTHR11082:SF9\"[1-101]TTRNA-DIHYDROURIDINE SYNTHASE-RELATED


","No hits to the COGs database.","Significant hit ( 4.5e-19) to 3/6 blocks of the IPB001269 family, which is described as \"Uncharacterized protein family UPF0034\". Interpro entry for IP:IPR001269. IPB001269D 22-45 2.8e-06 IPB001269E 55-64 0.0045 IPB001269F 77-94 3.2e-06","Residues 17 to 102 match (1e-08) PD:PD107064 which is described as 5'REGION IBPB ","","","","","","","","","","","","Fri Dec 20 09:44:44 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01053 is paralogously related to AA00172 (7e-11).","","","","","","Residues 1 to 176 (E-value = 3.8e-05) place AA01053 in the Dus family which is described as Dihydrouridine synthase (Dus) (PF01207)","","","","","","","","1","","","" "AA01054","734000","733818","183","TTGGCGGAAAATGCCGAACTTGCCGTTCAATTAGGTTCCCACGGCGTGGATTTAAACTGCGGCTGCCCGTCGAAAACGGTGAACGGCAGTAACGGCGGCGCTTCCTTGTTAAAACAACCCGAACTCATTTACCAAGCCACCAAAGCCATTCGTCAGGCAGGCGGTCCCGCAACATCACACCGT","","","6183","LAENAELAVQLGSHGVDLNCGCPSKTVNGSNGGASLLKQPELIYQATKAIRQAGGPATSHR","733820","","conserved hypothetical protein","Periplasm, Extracellular","","
InterPro
IPR001269
Family
Dihydrouridine synthase, DuS
PF01207\"[1-53]TDus
PS01136\"[16-34]TUPF0034
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[1-53]Tno description
noIPR
unintegrated
unintegrated
PTHR11082\"[1-53]TTRNA-DIHYDROURIDINE SYNTHASE
PTHR11082:SF9\"[1-53]TTRNA-DIHYDROURIDINE SYNTHASE-RELATED


","BeTs to 17 clades of COG0042COG name: Predicted TIM-barrel enzymes, possibly dehydrogenases, nifR3 familyFunctional Class: RThe phylogenetic pattern of COG0042 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.9e-14) to 1/6 blocks of the IPB001269 family, which is described as \"Uncharacterized protein family UPF0034\". Interpro entry for IP:IPR001269. IPB001269B 5-37 1.8e-14","Residues 1 to 53 match (8e-21) PD:PD468831 which is described as COMPLETE PROTEOME FAMILY TRANSCRIPTIONAL REGULATOR NIFR3 NIFR3-LIKE REGULATION YHDG NITROGEN ","","","","","","","","","","","","Fri Dec 20 09:46:50 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01054 is paralogously related to AA00172 (2e-07) and AA00384 (4e-05).","","","","","","","","","","","","","","1","","","" "AA01056","734228","734007","222","TTGCGCGTTATTTTAGCCCCCATGCAGGGCGTGCTTGATCCGCTCGTGCGTCAATTATTAACGGAAGTGAACGATTACGATTTGTGCATTTCCGAATTCGTGCGCGTGGTGGATCAACGGCTTCCGCCGAAAGTGTTTTATCGCCTTTGCCCCGAGTTACACCAACGGGGCTTCACCCCAAGCGGCACGCCGGTGCGCGTGCAACTTCTTGGACAACATCCC","","","8462","LRVILAPMQGVLDPLVRQLLTEVNDYDLCISEFVRVVDQRLPPKVFYRLCPELHQRGFTPSGTPVRVQLLGQHP","734009","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR001269
Family
Dihydrouridine synthase, DuS
PF01207\"[4-74]TDus
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[2-74]Tno description


","BeTs to 5 clades of COG0042COG name: Predicted TIM-barrel enzymes, possibly dehydrogenases, nifR3 familyFunctional Class: RThe phylogenetic pattern of COG0042 is aom---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-05) to 1/6 blocks of the IPB001269 family, which is described as \"Uncharacterized protein family UPF0034\". Interpro entry for IP:IPR001269. IPB001269A 4-24 1.4e-05","Residues 1 to 74 match (7e-14) PD:PD107064 which is described as 5'REGION IBPB ","","","","","","","","","","","","Fri Dec 20 09:47:35 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01056 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01057","735107","734235","873","ATGAATTTTATCGGAAAATTTTTAGGTGCCTTGATCGGTTTTCGATTAGGCGGTTTTTTCGGCATGTTAACAGGGATTTTCCTCGGTCATCTCGCCGACAAAAAACTGTATGAACTGGGCACGGTAAATTCTTCTTTCTTCAAAAATAAAACCACCCGCCAATTGCTGTTTATGCAAACCACCTTTGCGGTGCTCGGACATATCAGCAAAGCCAAAGGACGCGTGACGGAAAACGACATTCAGCTTGCCAATCATTTGATGAATCAATTGCAGCTGGACGATGCCGGTCGCCGTCTGGCACAGGACGCGTTTAATCGTGGCAAACAGGCGGATTTCCCTATTCGTCAGGTGATTCGCGAATTTCGTATCGGCTGCGGACAGCGCGCCGATTTGTTGCGCATGTTCCTGCATGTGCAGGTTCAGGCGGCATTTGCCGATGATCATTTGCATGAAAATGAAAAAGAACTGTTGTTTGTGGTGGCGGAAGAACTGGGTCTATCCCGCTTTCAGTTTGAACAAATGCTGGCGATGGAAATGGCGGCGCGTCAATTCAGCCGCGGCGGTTATTACCAACAGGGCGGCTATCAGCAAGGCTCTTATCAACAAAGTGGTTATCAATACAACGATTACCAACAACATTCTTATGGTCAGTCTTCCGGTCCGACGTTAGACGATGCTTATAAAGTGCTGGGCGTCGGCGCCAATGATGATCAAAATACGGTGAAACGGGCGTATCGCCGTTTAATGAACGAACATCACCCGGACAAACTGGTGGCGAAAGGTTTGCCGCCGGAAATGATGGAAATGGCGAAAGAAAAAGCACAACAAATTCAAGCGGCATACGATTTGATCTGCAAAGCCAAAGGTTGGAAA","","","33070","MNFIGKFLGALIGFRLGGFFGMLTGIFLGHLADKKLYELGTVNSSFFKNKTTRQLLFMQTTFAVLGHISKAKGRVTENDIQLANHLMNQLQLDDAGRRLAQDAFNRGKQADFPIRQVIREFRIGCGQRADLLRMFLHVQVQAAFADDHLHENEKELLFVVAEELGLSRFQFEQMLAMEMAARQFSRGGYYQQGGYQQGSYQQSGYQYNDYQQHSYGQSSGPTLDDAYKVLGVGANDDQNTVKRAYRRLMNEHHPDKLVAKGLPPEMMEMAKEKAQQIQAAYDLICKAKGWK","734237","Tentative functional class from gi:1175487 comment field.","DnaJ-like protein djlA","Inner membrane, Periplasm, Cytoplasm","","
InterPro
IPR001623
Domain
Heat shock protein DnaJ, N-terminal
PF00226\"[225-282]TDnaJ
SM00271\"[224-289]TDnaJ
PS50076\"[225-291]TDNAJ_2
InterPro
IPR015609
Family
Molecular chaperone, heat shock protein, Hsp40, DnaJ
PTHR11821\"[100-109]T\"[224-284]TDNAJ/HSP40
noIPR
unintegrated
unintegrated
G3DSA:1.10.287.110\"[224-288]Tno description
PTHR11821:SF49\"[100-109]T\"[224-284]TDNAJ-RELATED
signalp\"[1-25]?signal-peptide
tmhmm\"[10-30]?transmembrane_regions


","BeTs to 5 clades of COG1076COG name: DnaJ-domain-containing proteins 1Functional Class: OThe phylogenetic pattern of COG1076 is ------y------cefgh-nujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 1.6e-09) to 1/6 blocks of the IPB001305 family, which is described as \"DnaJ central domain (CXXCXGXG)\". Interpro entry for IP:IPR001305. IPB001305A 225-257 1.6e-09Significant hit ( 1.4e-05) to 1/2 blocks of the IPB001623 family, which is described as \"DnaJ N-terminal domain\". Interpro entry for IP:IPR001623. IPB001623A 241-255 1.5e-05Significant hit ( 2.2e-05) to 1/8 blocks of the PR00625 family, which is described as \"DnaJ protein family signature\". Prints database entry for PR:PR00625. PR00625A 236-255 2.3e-05","Residues 227 to 284 match (4e-10) PD:PD416371 which is described as PROTEOME COMPLETE DJLA DNAJ-RELATED DNAJ-LIKE R02189 ","","","","","","","","","","","Fri Dec 20 10:03:48 2002","Fri Dec 20 09:54:47 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01057 is paralogously related to AA00688 (8e-05).","","","","","","Residues 225 to 289 (E-value = 5.1e-14) place AA01057 in the DnaJ family which is described as DnaJ domain (PF00226)","","","","","Genevaux P, Schwager F, Georgopoulos C, Kelley WL.The djlA gene acts synergistically with dnaJ in promoting Escherichia coli growth.J Bacteriol. 2001 Oct;183(19):5747-50.PMID: 11544239 Genevaux P, Wawrzynow A, Zylicz M, Georgopoulos C, Kelley WL.DjlA is a third DnaK co-chaperone of Escherichia coli, and DjlA-mediated induction ofcolanic acid capsule requires DjlA-DnaK interaction.J Biol Chem. 2001 Mar 16;276(11):7906-12.PMID: 1110664","","Fri Dec 20 09:54:47 2002","1","","","" "AA01059","735833","735192","642","ATGGAAAATTACAAACAACAGTTTATTGAATTCGCATTGGCGCGTCAGGTGTTAAAATTCGGCGAGTTCACCTTGAAATCAGGGCGCGTCAGCCCTTATTTCTTTAACGCCGGGTTGTTTAACCAAGGCGCGGATCTTGCCCGCTTGGGCGAATTTTATGCCGCCGCCTTGCAAGCCGGCGGTTTGCAATATGATGTGATTTTCGGCCCGGCATACAAAGGTATTCCCATCGCCACCACGGTGTCGATTGCCTTATTTAACTGTTTTAACGTCAATAAACCGGTGTGTTTTAACCGCAAAGAAGCCAAAGATCACGGCGAGGGCGGCAACTTAATCGGTAGTCCGCTACAAGGCAAAGTGTTGTTGGTGGACGACGTGATCACCGCCGGCACGGCAATTCGCGAATCCATGCAAATTATTCAGGCGAATGGCGCACAATTAAGCGCCGTGCTGATTGCGTTAAATCGTCAGGAACGCGGTAATGGCGAGCTTTCCGCCATTCAGGAAGTGGAGCGCGACTACCAATGCAACGTGCTATCCATCGTTGATTTTGCCGATTTAATGGCGTTTATTGAAACCCAACCGGAATATCAACAATATTTGCCGGCAATGCGCGCTTACCGCGCACAATACGGCATTAAA","","","23622","MENYKQQFIEFALARQVLKFGEFTLKSGRVSPYFFNAGLFNQGADLARLGEFYAAALQAGGLQYDVIFGPAYKGIPIATTVSIALFNCFNVNKPVCFNRKEAKDHGEGGNLIGSPLQGKVLLVDDVITAGTAIRESMQIIQANGAQLSAVLIALNRQERGNGELSAIQEVERDYQCNVLSIVDFADLMAFIETQPEYQQYLPAMRAYRAQYGIK","735194","","orotate phosphoribosyltransferase","Cytoplasm","","
InterPro
IPR000836
Domain
Phosphoribosyltransferase
PF00156\"[29-170]TPribosyltran
InterPro
IPR002375
Family
Purine/pyrimidine phosphoribosyl transferase
PS00103\"[120-132]TPUR_PYR_PR_TRANSFER
InterPro
IPR004467
Domain
Orotate phosphoribosyl transferase
TIGR00336\"[10-187]TpyrE: orotate phosphoribosyltransferase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2020\"[1-213]Tno description


","No hits to the COGs database.","Significant hit ( 1e-06) to 2/2 blocks of the IPB002375 family, which is described as \"Purine/pyrimidine phosphoribosyl transferase\". Interpro entry for IP:IPR002375. IPB002375A 99-103 10 IPB002375B 117-132 5e-05","Residues 1 to 53 match (3e-09) PD:PD580680 which is described as GLYCOSYLTRANSFERASE TRANSFERASE PYRIMIDINE OPRT OROTATE PHOSPHORIBOSYLTRANSFERASE BIOSYNTHESIS PYROPHOSPHORYLASE FAMILY MULTIGENE ","","","","","","","","","","","","Fri Dec 20 10:16:55 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01059 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 29 to 170 (E-value = 8.9e-33) place AA01059 in the Pribosyltran family which is described as Phosphoribosyl transferase domain (PF00156)","","","","","Lucas S, Toffin L, Zivanovic Y, Charlier D, Moussard H, Forterre P, Prieur D, Erauso G.Construction of a shuttle vector for, and spheroplast transformation of, the hyperthermophilic archaeon Pyrococcus abyssi.Appl Environ Microbiol. 2002 Nov;68(11):5528-36.PMID: 12406746Watrin L, Lucas S, Purcarea C, Legrain C, Prieur D.Isolation and characterization of pyrimidine auxotrophs, and molecular cloning of the pyrE gene from the hyperthermophilic archaeon Pyrococcus abyssi.Mol Gen Genet. 1999 Sep;262(2):378-81.PMID: 10517335 ","","Fri Dec 20 10:16:55 2002","1","","","" "AA01062","736559","735846","714","ATGCGCCCGAATCAACGTGCCAATCACCAACCCCGCCCGATTCAGATCACCCGTCATTACACCAAACACGCGGAAGGTTCCGTGTTGGTGGAATTCGGCGATACCAAAGTGTTGTGTACCGCCTCGGTCGAAGAGAGTGTGCCGCGCTTTCTAAAAGGGCAAGGACAAGGTTGGGTGACGGCGGAATACGGCATGTTGCCGCGTTCCACCCACAGCCGTATGCAACGTGAAGCGGCGAAAGGCAAACAAGGCGGACGCACCTTGGAAATTCAGCGTTTAATCGCCCGTTCCTTGCGTGCCATGGTGGATTTGGAAGCCCTCGGCGAGCGTTGTATTACCTTGGATTGCGATGTGATCCAAGCGGACGGCGGCACGCGCACGGCATCCATTACCGGTGCTTGCGTGGCGTTATGCGATGCGCTGAACAGCTTGGTGACAAACGGCACGCTGGCGAAAAACCCGCTGAAAGGTTTGGTTGCCGCCATTTCTGTGGGCATTGTGAACGGCGAAGCGGTGTGCGATTTGGAATATGTGGAAGATTCCGCCGCCGAAACGGACATGAACGTGGTGATGATGGAAGACGGTCGTATGATTGAAGTGCAGGGCACGGCGGAAGGCAAGCCTTTCAGCCACGAAGAACTCTTAACCTTGCTCGATCTTGCCAAACAAGGTTGCGACATGATTTTCCAAACCCAACGCGCCACGCTGGCGGAA","","","29010","MRPNQRANHQPRPIQITRHYTKHAEGSVLVEFGDTKVLCTASVEESVPRFLKGQGQGWVTAEYGMLPRSTHSRMQREAAKGKQGGRTLEIQRLIARSLRAMVDLEALGERCITLDCDVIQADGGTRTASITGACVALCDALNSLVTNGTLAKNPLKGLVAAISVGIVNGEAVCDLEYVEDSAAETDMNVVMMEDGRMIEVQGTAEGKPFSHEELLTLLDLAKQGCDMIFQTQRATLAE","735848","","ribonuclease PH (RNase PH)","Cytoplasm","","
InterPro
IPR001247
Domain
Exoribonuclease
PF01138\"[10-143]TRNase_PH
PF03725\"[157-224]TRNase_PH_C
InterPro
IPR002381
Family
Ribonuclease PH
TIGR01966\"[2-237]TRNasePH: ribonuclease PH
PS01277\"[116-128]TRIBONUCLEASE_PH
noIPR
unintegrated
unintegrated
PTHR11953\"[1-238]TRIBONUCLEASE PH RELATED


","No hits to the COGs database.","Significant hit (2.3e-134) to 4/4 blocks of the IPB002381 family, which is described as \"Ribonuclease PH\". Interpro entry for IP:IPR002381. IPB002381A 2-22 7.8e-11 IPB002381B 47-94 6.9e-50 IPB002381C 96-137 1.2e-39 IPB002381D 174-209 8.3e-31","Residues 188 to 236 match (1e-09) PD:PD491013 which is described as PH RIBONUCLEASE PROTEOME COMPLETE NUCLEOTIDYLTRANSFERASE TRANSFERASE TRNA PROCESSING RNASE PROBABLE ","","","","","","","","","","","","Fri Dec 20 10:20:36 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01062 is paralogously related to AA00151 (1e-04).","","","","","","Residues 157 to 224 (E-value = 3.7e-20) place AA01062 in the RNase_PH_C family which is described as 3' exoribonuclease family, domain 2 (PF03725)","","","","","","","","1","","","" "AA01063","736677","737537","861","ATGATTTATAGCATGACGGCATTTGCTGCGTTAGAGATAAAAAAAGACTGGGGCAACGCAGTTTGGGAAATTCGCTCGGTGAATCAACGTTATCTGGAAACCTTTTTCCGCCTGCCGGAACAGTTCCGCAGCTTAGAAAACACCTTGCGCGAAAGCCTGCGTCAAAAGCTCACCCGTGGCAAAATCGAATGCACATTGCGCATCGATAATAAAAAACAAACCGCCGCCGAATTGCACATTAACCAAGAACTCGCCGGTCAAGTGCTGCAATCCTTACAATGGCTGAAACAACAAGCGGGCGAAGGCGAATTCAATTTAACCGATGTATTGCGCTATCCGGGCGTGGTGGAAGTGCCGGAACAAGATGTGGATTTAATCAGTCAGGATTTATTGGCGGCATTTGAACAAGTGGTCGGCGAATTTATCGCCATGCGTCAGCGCGAAGGGGAAAAAATCCATACCTTACTGGAACAGCGCCTTGACGCCATCAACGTCGAACAGCAAAAAGTGCGGTCAAAAATGCCGGAGATTTTACAATGGCAGCGTGAGCGGATGCTGCAACGCTTCGAGGAAATTCAACTGCAACCCGATCCACAACGTTTAGAGCAGGAGCTGATTATGCTGGCGCAACGCATTGATGTGGCGGAAGAACTGGATCGGTTACAGTTACACGTGAAAGAAACCCAAAATATTCTGCGCAAAGGCGGCGCGGTGGGACGTAAGCTGGATTTTATGATGCAGGAACTAAACCGCGAATCCAACACGCTGGCGTCCAAATCTATTAATGTGGACGTCACCAATTCCGCCATTGAGCTTAAAGTGTTAATCGAGCAAATGCGTGAGCAAATTCAAAATCTTGAG","","","33610","MIYSMTAFAALEIKKDWGNAVWEIRSVNQRYLETFFRLPEQFRSLENTLRESLRQKLTRGKIECTLRIDNKKQTAAELHINQELAGQVLQSLQWLKQQAGEGEFNLTDVLRYPGVVEVPEQDVDLISQDLLAAFEQVVGEFIAMRQREGEKIHTLLEQRLDAINVEQQKVRSKMPEILQWQRERMLQRFEEIQLQPDPQRLEQELIMLAQRIDVAEELDRLQLHVKETQNILRKGGAVGRKLDFMMQELNRESNTLASKSINVDVTNSAIELKVLIEQMREQIQNLE","737539","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR005229
Family
Conserved hypothetical protein 255
TIGR00255\"[1-287]TTIGR00255: conserved hypothetical protein T
InterPro
IPR013527
Domain
YicC-like, N-terminal
PF03755\"[2-155]TYicC_N
InterPro
IPR013551
Domain
Domain of unknown function DUF1732
PF08340\"[200-287]TDUF1732


","No hits to the COGs database.","","Residues 105 to 175 match (9e-13) PD:PD538879 which is described as PROTEOME COMPLETE VC0209 ","","","","","","","","","","","","Fri Dec 20 10:21:25 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01063 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 155 (E-value = 1.5e-72) place AA01063 in the YicC_N family which is described as YicC-like family, N-terminal region (PF03755)","","","","","","","","1","","","" "AA01064","737568","738452","885","ATGGCATATGCACTTTTAACGGCACAACAGGACGACATCATCTGCCCGCTCAGCCATTACACCCTCATTGAAATGGCGGGTGTGGATGCGGAAAAATATTTGCAGGGGCAACTCACCTGCGATGTGACAAAACTGGCGGCAGGCGAATCCACCCTCACCGCCCATTGCGATCCGAAAGGCAAAATGAGCGCGCTATTCCGCCTGATTCGACAAGACGAACAGACCTTTTATATGTTGCTGAAAAGTGAATTATTGCCGTCGGCATTGGATCAACTGAAGAAATATGCGGTGTTTTCCAAAGTCACCTTCACCCCGTTAGATTGGCAAATTATCGGCGCGGCAGGTGCGAAAGGCATCGAAAAGTACGGTCAGATTTCCGCGCAAATTCGTGTTGCAGTTAACGATCGACAACCACGTGTCATTTTGTTAAATCCGACCCGCTTATCCATCGAACCGACTGCCGAAGCAAACGTGTGGGATTTGTTGGATATTCAGGACGGCGTGCCCGGTTTAGCGGTGGCAACCCAACTACAATTCATTCCGCAGGCGTTAAATCTGCAAAGCATCGAACAAGCGATTTCCTTCCACAAAGGCTGTTACATCGGGCAAGAAACGGTGGCGCGCGCCAAATATCGCGGCGCCAACAAACGCGCCTTGTTTATCTTTGCGGCACAAACGGAAAGCCTACCTGACATCGGTTCGCCGTTGGAAATGGCGCTCGGCGACAACTGGCGCTGCACCGGCACGATCATAAGTGCGGTCAATTTTCACGACGTTTTATGGTTGCAGGCGGTGCTTAATACGCCGTTGGAAGACGGGCAGGCATTCCGTTTACCAGACAGCCAAACGACGTTGACATTACAACCTTTACCTTACGAGTTAAGC","","","32512","MAYALLTAQQDDIICPLSHYTLIEMAGVDAEKYLQGQLTCDVTKLAAGESTLTAHCDPKGKMSALFRLIRQDEQTFYMLLKSELLPSALDQLKKYAVFSKVTFTPLDWQIIGAAGAKGIEKYGQISAQIRVAVNDRQPRVILLNPTRLSIEPTAEANVWDLLDIQDGVPGLAVATQLQFIPQALNLQSIEQAISFHKGCYIGQETVARAKYRGANKRALFIFAAQTESLPDIGSPLEMALGDNWRCTGTIISAVNFHDVLWLQAVLNTPLEDGQAFRLPDSQTTLTLQPLPYELS","738454","","conserved hypothetical protein (possible aminomethyltransferase)","Cytoplasm","","
InterPro
IPR006222
Family
Glycine cleavage T protein (aminomethyl transferase)
PF01571\"[14-78]TGCV_T
noIPR
unintegrated
unintegrated
PTHR13847\"[13-209]TFAD NAD BINDING OXIDOREDUCTASES
PTHR13847:SF3\"[13-209]TFAD OXIDOREDUCTASE


","No hits to the COGs database.","","Residues 158 to 278 match (3e-42) PD:PD008318 which is described as PROTEOME COMPLETE AMINOMETHYLTRANSFERASE TRANSFERASE METHYLTRANSFERASE RP464 SLR0635 RC0698 VC2472 2D-PAGE ","","","","","Tue Feb 18 15:48:10 2003","","","","","","","Tue Feb 18 15:48:10 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01064 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 14 to 295 (E-value = 1.3e-06) place AA01064 in the GCV_T family which is described as Glycine cleavage T-protein (aminomethyl transferase) (PF01571)","","","","","","","","1","","","" "AA01066","738520","738960","441","ATGTGTTCCCGGATGAGCGGATTCCTATCGACGATCGTCAGCGTCCGCCGGGCCTTGTTCGGCGTGAATTTGCCGTCGAAACAAAAAGGGCGCGTTGCGTTACAACAAAAATACCTGAACGACAAACGCTATATGGGCTTCCACAGCCTGTTCACCACGGGCAACATCGTCAACAAAGATTTCACTCTTTATCAACTGCCTTTTGAACTAGATATATTCGATCAGGACGAATTCGCCCGCGCCGGCATCGACTTTAGTTGCTTTAGGAGTGTTGATATTTATCATCGGCGGGGTACTTCGGACAAATCATTATCTATTTATCCTCGTCAAAAAATCCGCTGGAAACCGACCGCACTTTATGGTATAAAGCACGCCGTTATTTTGCTGTTTAAAAATAACGTTCAATTTTTAATCAAACTTACTAAAACACACACATATCAG","","","17539","MCSRMSGFLSTIVSVRRALFGVNLPSKQKGRVALQQKYLNDKRYMGFHSLFTTGNIVNKDFTLYQLPFELDIFDQDEFARAGIDFSCFRSVDIYHRRGTSDKSLSIYPRQKIRWKPTALYGIKHAVILLFKNNVQFLIKLTKTHTYQ","738962","","conserved hypothetical protein","Periplasm, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide


","No hits to the COGs database.","","Residues 19 to 85 match (5e-19) PD:PD004383 which is described as PROTEOME COMPLETE TRANSMEMBRANE NEUROPATHY TARGET ESTERASE CHROMOSOME PA3339 CPE1574 PHOSPHOESTERASE ","","","","","","","","","","","","Fri Dec 20 10:26:07 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01066 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01067","739038","739757","720","ATGGCACAAGTTTCTATGCGCGATATGCTTCAGGCAGGTGTTCACTTCGGTCACCAAACCCGTTACTGGAACCCAAAAATGAAACCGTTCATTTTCGGACCACGCAACGGCGTTCACATCATCAATCTTGAAAAAACCGTTCCAATGTTCAACGCGGCATTAGCCGAGTTAACCCGCATTGCAAGCAACAACGGCAAAGTGTTATTCGTTGGTACCAAACGCGCAGCGACCGATGCAGTTCAAGCAGCGGCATTAGAATGTCAACAATACTATGTAAATCACCGTTGGTTAGGCGGTATGTTGACCAACTGGAAAACAGTTCGTCAATCCATCAAACGCTTAAAAGATTTAGAAACCCAATCTCAAGACGGCACCTTCGACAAATTAACCAAAAAAGAAGCGTTAATGCGTAGCCGTGAGATGGAAAAACTTGAATTAAGCCTTGGCGGTATCAAAGATATGGGCGGTTTGCCGGATGCGTTATTCGTTATCGGTGCGGATCACGAACATATCGCGGTTAAAGAAGCAAACAACTTGGGCATTCCTGTATTTGCTATCGTTGATACCAACTCCGATCCGGACGGCGTAGATTTCGTTATTCCGGGTAACGACGACGCAGCGCGCGCCATTCAACTTTACTTGGCTTCGGCGGTTGCAGCGATCAAAGAAGGTCGTGGTAACGAAGAAGCGGTTGCTGAAGAATTAGCGCAAGCCGCAGAA","","","26348","MAQVSMRDMLQAGVHFGHQTRYWNPKMKPFIFGPRNGVHIINLEKTVPMFNAALAELTRIASNNGKVLFVGTKRAATDAVQAAALECQQYYVNHRWLGGMLTNWKTVRQSIKRLKDLETQSQDGTFDKLTKKEALMRSREMEKLELSLGGIKDMGGLPDALFVIGADHEHIAVKEANNLGIPVFAIVDTNSDPDGVDFVIPGNDDAARAIQLYLASAVAAIKEGRGNEEAVAEELAQAAE","739759","","30S ribosomal protein S2","Cytoplasm","","
InterPro
IPR001865
Family
Ribosomal protein S2
PR00395\"[6-24]T\"[37-46]T\"[87-104]T\"[158-175]T\"[175-186]T\"[196-210]TRIBOSOMALS2
PF00318\"[9-225]TRibosomal_S2
PS00962\"[6-17]TRIBOSOMAL_S2_1
PS00963\"[158-182]?RIBOSOMAL_S2_2
InterPro
IPR005706
Family
Ribosomal protein S2, bacterial and organelle form
PTHR12534\"[1-240]T30S RIBOSOMAL PROTEIN S2 (PROKARYOTIC AND ORGANELLAR)
TIGR01011\"[3-227]TrpsB_bact: ribosomal protein S2


","BeTs to 26 clades of COG0052COG name: Ribosomal protein S2Functional Class: JThe phylogenetic pattern of COG0052 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.7e-68) to 3/3 blocks of the IPB001865 family, which is described as \"Ribosomal protein S2\". Interpro entry for IP:IPR001865. IPB001865A 20-73 3.3e-30 IPB001865B 91-104 1.1e-10 IPB001865C 172-213 3.7e-25","Residues 60 to 187 match (2e-08) PD:PD548578 which is described as MITOCHONDRION S2 RIBOSOMAL ","","","","","","","","","","","","Fri Dec 20 10:27:13 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01067 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 9 to 225 (E-value = 1.6e-122) place AA01067 in the Ribosomal_S2 family which is described as Ribosomal protein S2 (PF00318)","","","","","An,G., Bendiak,D.S., Mamelak,L.A. and Friesen,J.D.Organization and nucleotide sequence of a new ribosomal operonin Escherichia coli containing the genes for ribosomal proteinS2 and elongation factor Ts. Nucleic Acids Res. 9(16): 4163-4172. 1981. PubMed: 6272196.","","Fri Dec 20 10:27:13 2002","1","","","" "AA01068","739809","739910","102","TTGGTTAGCAGGGGGCTGAAACAGCTCCCTGTATTTTTTGAGCTAAAAGTGCGGTTAAAAAACAAGTTATTTTTCAACCGCACTTTAACCGACAGAGGATTT","","","4064","LVSRGLKQLPVFFELKVRLKNKLFFNRTLTDRGF","739910","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 09:20:42 2004","","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01068 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 09:20:42 2004","","","","","","","","","","","","","1","","","" "AA01069","739915","740760","846","ATGGCTGAAATCACAGCATCATTAGTAAAAGAACTGCGTGAACGTACCGGCGCAGGCATGATGGAATGTAAAAAAGCATTAGTTGAAGCAAACGGCGACATCGAATTAGCCATCGACAACATGCGTAAATCCGGTCAAGCCAAAGCGGCGAAAAAAGCCGGTCGTGTTGCCGCTGAAGGTGTGATCATCGCGCGCGTACAAAACGGTTTCGGTGTGGTGGTTGAATTAAACTGCGAAACCGACTTCGTGGCAAAAGATGCCGGCTTCTTAGGTTTAGCCAATGAAGTGGCTGACTACGCAGTCGCACACAAAGGCACCTCCATCGAACAATTACAAGCGGAATTTGAAGAAAAACGTGCGGCATTGGTAGCCAAAATCGGTGAAAACATGACTATTCGTCGTGTAGCTTACATCGAAGGCGACGTGGTAGGTTCTTACTTACACGGCGCGAAAATCGGCGTATTGGTTGCAGGTAAAGGCGCAGACGACGAGTTATTAAAACACATCGCTATGCACATCGCGGCAAGCCGTCCTGACTACGTTAACCCAAGCGACGTGCCTGCCGACGTGGTTGAACACGAGCGCAACATCCAAGTGGATATCGCTATGCAATCCGGCAAACCACGCGAAATCGCAGAAAAAATGGTTGAAGGCCGCATGAAGAAATTCACCGGCGAAGTGTCCTTAACCGGCCAACCGTTCGTCATGGATCCATCTAAATCCGTTGGCGATTTATTAAAAGAAAAAGGTGCCGAAGTCTCTAACTTCATCCGTTTAGAAGTGGGCGAAGGTATCGAGAAAGTGGAAACCGACTTTGCCGCAGAAGTGGCTGCAATGTCTAAAGCT","","","30185","MAEITASLVKELRERTGAGMMECKKALVEANGDIELAIDNMRKSGQAKAAKKAGRVAAEGVIIARVQNGFGVVVELNCETDFVAKDAGFLGLANEVADYAVAHKGTSIEQLQAEFEEKRAALVAKIGENMTIRRVAYIEGDVVGSYLHGAKIGVLVAGKGADDELLKHIAMHIAASRPDYVNPSDVPADVVEHERNIQVDIAMQSGKPREIAEKMVEGRMKKFTGEVSLTGQPFVMDPSKSVGDLLKEKGAEVSNFIRLEVGEGIEKVETDFAAEVAAMSKA","740762","","translation elongation factor (EF-Ts)","Cytoplasm","","
InterPro
IPR000449
Domain
Ubiquitin-associated/Translation elongation factor EF1B, N-terminal
PF00627\"[4-44]TUBA
InterPro
IPR001816
Family
Translation elongation factor EFTs/EF1B
PTHR11741\"[7-278]TELONGATION FACTOR TS
TIGR00116\"[1-282]Ttsf: translation elongation factor Ts
PS01126\"[12-27]TEF_TS_1
PS01127\"[75-85]TEF_TS_2
InterPro
IPR014039
Domain
Translation elongation factor EFTs/EF1B, dimerisation
PF00889\"[57-263]TEF_TS
noIPR
unintegrated
unintegrated
G3DSA:1.10.8.30\"[2-55]Tno description
G3DSA:3.30.479.20\"[57-138]T\"[142-262]Tno description


","BeTs to 18 clades of COG0264COG name: Translation elongation factor TsFunctional Class: JThe phylogenetic pattern of COG0264 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-92) to 5/5 blocks of the IPB001816 family, which is described as \"Elongation factor Ts\". Interpro entry for IP:IPR001816. IPB001816A 9-55 2e-38 IPB001816B 73-89 3.1e-11 IPB001816C 123-136 8.7e-08 IPB001816D 167-192 1.4e-12 IPB001816E 206-235 1.9e-17","Residues 171 to 230 match (5e-10) PD:PD514746 which is described as ELONGATION FACTOR EF-TS PROTEOME TS COMPLETE BIOSYNTHESIS ","","","","","","","","","","","","Fri Dec 20 10:29:28 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01069 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 57 to 263 (E-value = 2e-104) place AA01069 in the EF_TS family which is described as Elongation factor TS (PF00889)","","","","","Fountoulakis M, Langen H, Gray C, Takacs B. 1998. Enrichmentand purification of proteins of Haemophilus influenzae bychromatofocusing. J Chromatogr A 806(2):279-91. PubMed: NOT_FOUNDZhang Y, Yu NJ, Spremulli LL. Mutational analysis of the roles of residues in Escherichiacoli elongation factor Ts in the interaction with elongationfactor Tu. J Biol Chem 273(8):4556-62 1998. PubMed: NOT_FOUND. Zhang Y, Tao J, Zhou M, Meng Q, Zhang L, Shen L, Klein R,Miller DL Elongation factor Ts of Chlamydia trachomatis: structure ofthe gene and properties of the protein. Arch Biochem Biophys 344(1):43-52.1997. PubMed: NOT_FOUND. An,G., Bendiak,D.S., Mamelak,L.A. and Friesen,J.D. Organization and nucleotide sequence of a new ribosomaloperon in Escherichia coli containing the genes forribosomal protein S2 and elongation factor Ts. Nucleic Acids Res. 9(16): 4163-4172.1981. MEDLINEe: 82059454.","","Fri Dec 20 10:30:56 2002","1","","","" "AA01070","741060","741743","684","GTGCTACATCGCAAATCTTACAGCGAAACCAGCTTACTGATCGATTTACTCACGGAAGACTTCGGGCGGATCAGCGTCTTGGCAAAAGGCGCACGGGCGAAGCGTTCCATGTTAAAAGGCGTGTTGCAGCCTTTCACGCCGTTGTTGTTACGCTGGAGCGGACGCGGTGAGCTGAAAATCCTGACCAAAGCGGAACCCGCCGCCATTGCGCTTCCGTTGCAAAATATCGCTTTATACAGCGGGTTTTATTTAAACGAACTCCTCTGCCGCGTGCTGGAACCGGAAACCGCCTATCCGCAACTGTTCCAACAATATTTGCAATGTTTAACCCAACTGGCGATGAATCAACAGCAAGTGGAACCCGCTCTGCGCACCTTTGAATTTCAGCTGTTGCGCACCCTTGGATACGGCATTGATTTCACCCATTGCGCCAGTTCGGGCAACACGGTAGAAGCGGACATGACCTATCGTTACCGCGAAGAAAAAGGCTTTATCGCCTCCTTAATTAAAGACAATTTAACTTTTTACGGGCGCGAATTGCTGGCATTTGAGCAAACCCGATTTGACGACCCGAGCATATTAGTGGCGGCAAAACGTTTTACACGCATCGCCTTAAAGCCTTATTTAGGTGACAAGCCATTGAAAAGCCGAGAATTATTTACACAACATAGCTTATATTCCAAA","","","26067","VLHRKSYSETSLLIDLLTEDFGRISVLAKGARAKRSMLKGVLQPFTPLLLRWSGRGELKILTKAEPAAIALPLQNIALYSGFYLNELLCRVLEPETAYPQLFQQYLQCLTQLAMNQQQVEPALRTFEFQLLRTLGYGIDFTHCASSGNTVEADMTYRYREEKGFIASLIKDNLTFYGRELLAFEQTRFDDPSILVAAKRFTRIALKPYLGDKPLKSRELFTQHSLYSK","741745","","DNA repair protein","Cytoplasm","","
InterPro
IPR003717
Family
Recombination protein O, RecO
PF02565\"[1-225]TRecO
TIGR00613\"[1-223]Treco: DNA repair protein RecO


","BeTs to 9 clades of COG1381COG name: Recombinational DNA repair protein (RecF pathway)Functional Class: LThe phylogenetic pattern of COG1381 is ---------drlbcefghsn-jxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 4.8e-36) to 4/4 blocks of the IPB003717 family, which is described as \"Recombination protein O (RecO)\". Interpro entry for IP:IPR003717. IPB003717A 0-18 3.5e-06 IPB003717B 54-105 1.7e-23 IPB003717C 123-127 68 IPB003717D 210-219 0.011","Residues 1 to 149 match (3e-07) PD:PD109899 which is described as DNA REPAIR RECOMBINATION O PROTEOME COMPLETE RECO HEMA-PSBN ORF206 CYANELLE ","","","","","","","","","","","","Fri Dec 20 10:46:53 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01070 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 225 (E-value = 2.9e-70) place AA01070 in the RecO family which is described as Recombination protein O (PF02565)","","",""," Haraszthy VI, Jordan SF, Zambon JJ.,Identification of Fur-regulated genes in Actinobacillus actinomycetemcomitans.Microbiology. 2006 Mar;152(Pt 3):787-96.PMID: 16514158","Anderson,P.E., Matsunaga,J., Simons,E.L. and Simons,R.W. 1996.Structure and regulation of the Salmonella typhimuriumrnc-era-recO operon. Biochimie 78(11-12): 1025-1034. PubMed: 9150881. Lam,H.M., Tancula,E., Dempsey,W.B. and Winkler,M.E. 1992.Suppression of insertions in the complex pdxJ operon ofEscherichia coli K-12 by lon and other mutations. J. Bacteriol. 174(5): 1554-1567. PubMed: 1537800. Morrison,P.T., Lovett,S.T., Gilson,L.E. and Kolodner,R. Molecular analysis of the Escherichia coli recO gene. J.Bacteriol. 171 (7), 3641-3649. PubMed: 2544549.","","Fri Dec 20 10:46:53 2002","1","","","" "AA01071","741847","743061","1215","ATGAACGGCAAAACCTGGTTTATCGAAAATGCGCTACCGCAGGAAAGCGTGGAAGTGCGTGTGCTGGAAGAAAAACGCCAATACGGACACGGCATAGCACAGCGCATTTTGCACCCAAGCCCGCAACGCCAAACGCCACCGTGTACCTATTTTACGCAATGCGGTGGCTGCCAAAATCAACATATTCCCATCGAATTACAACGTTCCGCCAAACAAAAGGCGCTGATTCAACGCCTCAGTCGTTTGCAACCCGAGCCGATTCAGTTTATGCCGTTATTACAGGGCGAACCTTGGCATTATCGCCGTCGGGTGAGATTAAGTGTGGGCTTTGATAGTAAAACGCGCAAGCTGAGTATCGGCTTACGGCGTAAAAATGCACAACAAATTATCCCGATTGAACATTGCCCTGTACTGGAACAACCGCTCAACGATTTACTGCCGAAACTGACCGCACTTTTCGCGCAGTGGTCCGCCCCGCAACAACTGGGTCACATTGAGCTAGTGGCGGCGGACAACGGTGTCGCCATGCTGTTGCGGCACATCAAAAACGTCGCCGAAAACGACCGCACTTTATTGCTGAAATTCGCCGAGCAGCACAACCTCATGTTATTCGTGCAAGAACTGGATGCCATTGAACATTGGCACGGCGAACAACCTTTTTATCGTTTGGATAACGACCTGACCTTGCAATTTGATATTCGTGATTTCATACAAATTAACGCCGAATTAAACCGCCAAATGATCAACACCGCGCTGGATTGGTTAGCGTTAAACGAACGGGAGCATGTGCTGGATTTATTCTGCGGTATGGGCAATTTCACCTTGCCGATCGCCCGTCGGGTAAAAAGTGCGGTGGGAATTGAAGGCGTTTCCGCGATGGTGGAAAAAGCCCGTAGAAATGCCGAACGAAACCGCTGTCACAATGTCCAATTCTATCAAGCAGATTTGGATAAATCGTTTGTCAATCAAGGCTGGGCGCAGCAACCTTTCAATAAGATTCTGCTCGACCCGCCACGCACAGGAGCGGCATTTGCGTTAAATGCGCTCTGTCAATTACAGGCTGAAAATATCCTGTATGTTTCTTGCAATCCTGCAACGCTCGTGCGAGATACGGAAATCTTGCGTAATGCAGGCTACCAACTGGATAAAGTCGCCATGATCGATATGTTCCCGCATACCGGTCATTTGGAATCGATAAGTTTATTTCGGAAAAAA","","","50147","MNGKTWFIENALPQESVEVRVLEEKRQYGHGIAQRILHPSPQRQTPPCTYFTQCGGCQNQHIPIELQRSAKQKALIQRLSRLQPEPIQFMPLLQGEPWHYRRRVRLSVGFDSKTRKLSIGLRRKNAQQIIPIEHCPVLEQPLNDLLPKLTALFAQWSAPQQLGHIELVAADNGVAMLLRHIKNVAENDRTLLLKFAEQHNLMLFVQELDAIEHWHGEQPFYRLDNDLTLQFDIRDFIQINAELNRQMINTALDWLALNEREHVLDLFCGMGNFTLPIARRVKSAVGIEGVSAMVEKARRNAERNRCHNVQFYQADLDKSFVNQGWAQQPFNKILLDPPRTGAAFALNALCQLQAENILYVSCNPATLVRDTEILRNAGYQLDKVAMIDMFPHTGHLESISLFRKK","743063","","RNA methyltransferase","Cytoplasm","","
InterPro
IPR001566
Family
23S rRNA methyltransferase/RumA
TIGR00479\"[1-397]TrumA: 23S rRNA (uracil-5-)-methyltransferas
InterPro
IPR002792
Domain
Deoxyribonuclease/rho motif-related TRAM
PF01938\"[1-35]TTRAM
InterPro
IPR010280
Family
(Uracil-5)-methyltransferase
PF05958\"[65-405]TtRNA_U5-meth_tr
PS01230\"[336-366]TTRMA_1
PS01231\"[387-397]TTRMA_2
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[239-318]Tno description
PTHR11061\"[2-404]TRNA M5U METHYLTRANSFERASE FAMILY
PTHR11061:SF2\"[2-404]TRNA M5U METHYLTRANSFERASE


","BeTs to 15 clades of COG2265COG name: SAM-dependent methyltransferases related to tRNA (uracil-5-)-methyltransferaseFunctional Class: JThe phylogenetic pattern of COG2265 is ----k-yqv-rlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-48) to 4/4 blocks of the IPB001566 family, which is described as \"RNA methyltransferase trmA family\". Interpro entry for IP:IPR001566. IPB001566A 263-304 8.5e-22 IPB001566B 333-343 0.0052 IPB001566C 357-366 1.2e-05 IPB001566D 379-402 8.7e-14Significant hit ( 4.5e-05) to 1/3 blocks of the IPB001737 family, which is described as \"Ribosomal RNA adenine dimethylase\". Interpro entry for IP:IPR001737. IPB001737A 248-293 4.4e-05","Residues 261 to 304 match (9e-08) PD:PD016907 which is described as COMPLETE PROTEOME METHYLTRANSFERASE TRANSFERASE TRNA 2.1.1.- HEMK PROCESSING RNA RRNA ","","","","","","","","","","","","Fri Dec 20 10:51:43 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01071 is paralogously related to AA00324 (6e-20), AA02992 (3e-16) and AA01342 (0.001).","","","","","","Residues 65 to 405 (E-value = 2.5e-10) place AA01071 in the tRNA_U5-meth_tr family which is described as tRNA (Uracil-5-)-methyltransferase (PF05958)","","","","","","","","1","","","" "AA01072","743074","745302","2229","ATGGTCGCTGTGAGAGGATCTCATTTATTAAATCCTAAAGATTTTGAGATTGAACAATGGTGCGCTAATTTAAATGTGGCAGACAATATCAAAACCGGTCTCACCGCCTGTTGGCACTATTCGCAGCAAAAAATCGCACTGCGTGCCGAGCATCATACGGAAGAGGCGCATTTGTTGTCCTTCGGTGTGGAAATGGTGGAAATTCTGCACAGTTTAAACATGGATTGCGACAGCCTGCTCACGGCGATGTTATTTCCAATTGTGAACGATCAGCTGGTGGATTTTGCACAAATTGAAGCAGATTTCGGCGCCAATATCAGCAAATTGGCAAAAGGCGTCATCGAGATGGACAACATTCGTCAGTTAAACGTCACCCACTCCGCCAGCGGCCTGCAAGTGGATAATGTGCGTCGTATGTTGCTTGCCATGGTGGACGACTTCCGCTGCGTCATTATCAAACTCGCCGAAAGAATCGCCTTCCTGCGCGACGCGGTGAATAACAATTACACCGAAGAACAACGGGTACTCGCCGCCAAGGAATGCGCCAATATTTACGCCCCACTCGCCAACCGCCTCGGTATCGGACAACTCAAATGGGAGCTGGAAGACTATTGCTTCCGCTATCTGCACCCGGAACAATACCGCGCCATCGCCAAACTGTTGCAAGAACGCCGCATTGACCGCGAACAATATATCGCCGATTTTATCACCGAACTCACCGGCTATTTGCAGGAAAACATCCAACAGGTGGAAGTGTACGGACGTCCGAAACACATTTACAGCATTTGGCGCAAAATGCAGAAAAAAAATCTGGAATTCAGCGAGTTATACGACGTTCGCGCGGTGCGTATTATCGTGCAAAAATTGCAGGATTGTTACACCGCACTTGGCATCGTACACACCCATTTCAAACATTTACCGAAAGAATTCGACGATTATGTCGCCAACCCAAAACCGAATGGCTATCAATCCATTCATACCGTGGTGCTAGGCAAAGGCGGCAAGCCCATTGAAGTGCAAATCCGCACCCAGCAAATGCACGATGATGCCGAGCTGGGTGTAGCGGCGCACTGGAAATATAAAGAAGGCGCCACCGCAGGGCGTTCCGGCTACGCAGAAAAAATCGCCTGGTTACGCAAACTGCTGGCATGGCAGGACGATATTACCGACTCCGGCGAAGTCATGGCAGAATTGCGTAGCCAAGTATTCGACGACCGCGTATATGTGTTTACGCCGAAAGGCGAAGTGGTGGATCTGCCCACCGGCTCCACCCCGCTGGATTTCGCTTATGCCATTCACAGCGAAATCGGGCACCGTTGTATCGGCGCCAAAGTGGGCGGACGCATTGTGCCCTTCACGTATCAGCTGCAAATGGGCGATCAGGTGGACATCATCACCCAGAAAAACCCGAACCCAAGCCGCGACTGGCTGAACCCGAATCTTGGCTTTACCCACACGGCGAAATCCCGCGCGAAAATTCACGCGTGGTTCAAAAAACAGGATCGCGATAAAAACATTCCGGCAGGCAAAGAATTGCTGGAAAGCGAGATTAACCGCTTAGGCATCAGTTTAAAACAGGTAGAACAGCAGGCGCTGCCCCGTTACAACCTGAAAAATCTGGACGATTTATATGCCGGCATCGGCGGCGGTGATATTCGCATCAGCCCGCTGATTAACTTCCTACAAAACAAATTTATCAAAACCTCCGCCCAGGAAGTGGACGAAGAAATTTTGCGCCATGTGAGCAACAAAAGTGCGGTCAATTCTCAGCAAAAATCCGAGCGCAAAGACTGTGTGATCGTGGAAGGCGTGGGCAACCTCATGCACCATATCGCCCGCTGCTGCCAACCTATTCCGGGCGACAGCATCGTGGGCTACATCACCATGGGACGCGGTATTTCCATTCACTGCTGCGACTGCGACCAATTCCTCGAATTGCAAGCCGCACACCCGGAACGCGTGGTGGAATCCCGCTGGGGCGACAATTATTCCAGCGGCTTCTATCTCAACATCCGCATCGTGGCGTCGGATCGCAACGGCTTATTGCGCGACATCACCACCGTGCTGGCAAATGAAAAAATCAGCGTACTCGGCGTTTCCACTCACACGGACAGCAAGCGCCAAGTGGCGAATATTGATATGCAAATTGAACTGAATAACGTGGAAATGTTAAGTAAAATTCTGTTCCGTTTGGAAAAACTGGATGATGTCATTGAAGCCAAACGCCTC","","","84481","MVAVRGSHLLNPKDFEIEQWCANLNVADNIKTGLTACWHYSQQKIALRAEHHTEEAHLLSFGVEMVEILHSLNMDCDSLLTAMLFPIVNDQLVDFAQIEADFGANISKLAKGVIEMDNIRQLNVTHSASGLQVDNVRRMLLAMVDDFRCVIIKLAERIAFLRDAVNNNYTEEQRVLAAKECANIYAPLANRLGIGQLKWELEDYCFRYLHPEQYRAIAKLLQERRIDREQYIADFITELTGYLQENIQQVEVYGRPKHIYSIWRKMQKKNLEFSELYDVRAVRIIVQKLQDCYTALGIVHTHFKHLPKEFDDYVANPKPNGYQSIHTVVLGKGGKPIEVQIRTQQMHDDAELGVAAHWKYKEGATAGRSGYAEKIAWLRKLLAWQDDITDSGEVMAELRSQVFDDRVYVFTPKGEVVDLPTGSTPLDFAYAIHSEIGHRCIGAKVGGRIVPFTYQLQMGDQVDIITQKNPNPSRDWLNPNLGFTHTAKSRAKIHAWFKKQDRDKNIPAGKELLESEINRLGISLKQVEQQALPRYNLKNLDDLYAGIGGGDIRISPLINFLQNKFIKTSAQEVDEEILRHVSNKSAVNSQQKSERKDCVIVEGVGNLMHHIARCCQPIPGDSIVGYITMGRGISIHCCDCDQFLELQAAHPERVVESRWGDNYSSGFYLNIRIVASDRNGLLRDITTVLANEKISVLGVSTHTDSKRQVANIDMQIELNNVEMLSKILFRLEKLDDVIEAKRL","745304","","GTP pyrophosphokinase (ppGpp synthetase I) / ATP:GTP3'-pyrophosphotransferase","Cytoplasm","","
InterPro
IPR002912
Domain
Amino acid-binding ACT
PF01842\"[669-736]TACT
InterPro
IPR004095
Domain
TGS
PF02824\"[407-466]TTGS
InterPro
IPR004811
Family
RelA/SpoT protein
TIGR00691\"[49-742]TspoT_relA: RelA/SpoT family protein
InterPro
IPR007685
Domain
RelA/SpoT
PF04607\"[254-364]TRelA_SpoT
InterPro
IPR012675
Domain
Beta-grasp fold, ferredoxin-type
G3DSA:3.10.20.30\"[406-469]Tno description
noIPR
unintegrated
unintegrated
PTHR21262\"[133-743]TGUANOSINE-3',5'-BIS(DIPHOSPHATE) 3'-PYROPHOSPHOHYDROLASE


","BeTs to 16 clades of COG0317COG name: Guanosine polyphosphate pyrophosphohydrolases/synthetasesFunctional Class: T,KThe phylogenetic pattern of COG0317 is -------qvdrlbcefghsnuj--twNumber of proteins in this genome belonging to this COG is","","Residues 373 to 414 match (2e-07) PD:PD402602 which is described as COMPLETE PROTEOME SYNTHETASE KINASE GTP PYROPHOSPHOKINASE PPPGPP TRANSFERASE HYDROLASE PPGPP ","","","","","","","","","","","","Fri Nov 21 14:53:18 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01072 is paralogously related to AA02305 (1e-103) and AA01534 (5e-07).","","","","","","Residues 669 to 743 (E-value = 2.6e-09) place AA01072 in the ACT family which is described as ACT domain (PF01842)","","","","","Metzger,S., Dror,I.B., Aizenman,E., Schreiber,G., Toone,M., Friesen,J.D., Cashel,M. and Glaser,G. The nucleotide sequence and characterization of the relA geneof Escherichia coli J. Biol. Chem. 263 (30), 15699-15704 (1988) PubMed: 2844820 Wendrich TM, Blaha G, Wilson DN, Marahiel MA, Nierhaus KH. Dissection of the Mechanism for the Stringent Factor RelA. Mol Cell. 2002 Oct;10(4):779-88. PMID: 12419222 Masucci JP, Gallant J, Lindsley D, Atkinson J. Influence of the relA gene on ribosome frameshifting. Mol Genet Genomics. 2002 Sep;268(1):81-6. PMID: 12242502 ","","Fri Dec 20 10:54:46 2002","1","","","" "AA01074","745330","745683","354","ATGGATAAAACCACGGGACTGACCCACTTAATTAAATCTACCCAATATTCGATGAAAGGCTTAAAAAGTGCGGTCAAATATGAAACCGCTTTTCGCCACGAGCTTTTTTGCTGCATTTTCATGATCCCGCTGGCGTTATGGCTCGGCGAAAATGCCATTGAACGCGCCCTGATGATTGGTTCCGTGTTGTTGGTGTTGGTGGTAGAACTGCTCAACAGCGCCATTGAAGCCGTGGTCGATCGCATCGGCACCGAACGCCACGAACTCTCCGGGCGTGCCAAAGATCAAGGCTCCGCTGCCGTGTTTGTCGCCTTAGTTATCGTAGTGGTCACTTGGGGATTAATGTTGTTTAAC","","","13007","MDKTTGLTHLIKSTQYSMKGLKSAVKYETAFRHELFCCIFMIPLALWLGENAIERALMIGSVLLVLVVELLNSAIEAVVDRIGTERHELSGRAKDQGSAAVFVALVIVVVTWGLMLFN","745685","","diacylglycerol kinase","Inner membrane, Cytoplasm","","
InterPro
IPR000829
Family
Prokaryotic diacylglycerol kinase
PD010722\"[55-118]TQ8XF39_SALTI_Q8XF39;
PF01219\"[7-117]TDAGK_prokar
PS01069\"[69-80]TDAGK_PROKAR
InterPro
IPR014380
Family
Diacylglycerol kinase, proteobacteria
PIRSF000717\"[1-118]TDiacylglycerol kinase, Proteobacteria type
noIPR
unintegrated
unintegrated
tmhmm\"[29-49]?\"[59-79]?\"[98-116]?transmembrane_regions


","BeTs to 11 clades of COG0818COG name: Diacylglycerol kinaseFunctional Class: MThe phylogenetic pattern of COG0818 is --------vd-lbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.5e-52) to 2/2 blocks of the IPB000829 family, which is described as \"Prokaryotic diacylglycerol kinase\". Interpro entry for IP:IPR000829. IPB000829A 9-53 1.4e-19 IPB000829B 54-100 7e-32","Residues 1 to 117 match (6e-30) PD:PD010722 which is described as KINASE DIACYLGLYCEROL PROTEOME COMPLETE TRANSFERASE TRANSMEMBRANE DGK DAGK PHOSPHOLIPID BIOSYNTHESIS ","","","","","","","","","","","","Fri Dec 20 10:57:08 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01074 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 117 (E-value = 2.1e-56) place AA01074 in the DAGK_prokar family which is described as Prokaryotic diacylglycerol kinase (PF01219)","","","","","Lightner,V.A., Bell,R.M. and Modrich,P. The DNA sequences encoding plsB and dgk loci of Escherichiacoli. J. Biol. Chem. 258(18): 10856-10861, 1983. PubMed: 6309817. Loomis,C.R., Walsh,J.P. and Bell,R.M. sn-1,2-Diacylglycerol kinase of Escherichia coli.Purification, reconstitution, and partial amino- andcarboxyl-terminal analysis. J. Biol. Chem. 260(7):4091-4097,1985. PubMed: 2984194. Smith,R.L., O\"Toole,J.F., Maguire,M.E. and Sanders,C.R. 2nd.Membrane topology of Escherichia coli diacylglycerol kinase. J. Bacteriol. 176(17): 5459-5465, 1994. PubMed: 8071224.","","Fri Dec 20 10:57:08 2002","1","","","" "AA01075","745745","746128","384","TTGAGGTGCAGATTATGTCTTACTCTTATCAATTTCGTTAAAAAACTATCAAACAGGTCACCGAGCAGGATTTTGGTATCCGTGAGGTGGCTAAATTTCATCAGATTTCTCGTTCTCAAGTCATTTATTGGAAAAGCCTTTCGTGAAAGAGGGCTTAATGGCGTAAAATCCCCTTATATAAACCCTCAACGCCCTAAAATAGTGAAGCCAAAGATGAAAAAGAAAGCGATTGAAATCCCGGAACAAACAGACTTTTCCCCAAAAGCGTTTAAAAAGCTGCAACGAGAGCTGGCATTAGCACGTGCACAGATTGCTTACCTAAAGGAGTTGGAGGCACTCGACCGTCAAAAACAGCGACAGAAAAAAGAAAAATCATTGAAAGAT","","","15047","LRCRLCLTLINFVKKLSNRSPSRILVSVRWLNFIRFLVLKSFIGKAFRERGLNGVKSPYINPQRPKIVKPKMKKKAIEIPEQTDFSPKAFKKLQRELALARAQIAYLKELEALDRQKQRQKKEKSLKD","746128","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 09:52:57 2004","Wed Feb 25 09:22:29 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA0348, a hypothetical.AA01075 is paralogously related to AA02115 (4e-69), AA01289 (4e-69), AA00008 (4e-69), AA02340 (2e-66), AA00535 (1e-22), AA01267 (4e-18), AA00631 (1e-13), AA00227 (2e-11), AA01404 (6e-11) and AA01549 (0.001).","Wed Feb 25 09:52:57 2004","","","","","","","","","","","","","1","","","" "AA01076","746305","746427","123","ATGGGTTTCCATTTGAATCATAAAACGGTGTTAAAACTGATGAATGCGTTAGGTATTCATTCTATTTTACGCAAGAAAAGACATGGAAAACGAGGAAAACATCGCATATTGCCCCGAATGTGC","","","4810","MGFHLNHKTVLKLMNALGIHSILRKKRHGKRGKHRILPRMC","746427","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 09:24:14 2004","Wed Feb 25 09:24:14 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paraloogus to AA0945 and AA0835.AA01076 is paralogously related to AA02341 (1e-20), AA02116 (1e-20), AA01288 (1e-20), AA00009 (1e-20), AA01444 (3e-12) and AA01268 (3e-12).","Wed Feb 25 09:24:14 2004","","","","","","","","","","","","","1","","","" "AA01077","746424","746930","507","GTGCTAAATCGTGATTTTACAGCGACGGCGCTCAATCAAAAATGGGTAACCGATGTCACTGAGTTTCGAGTTGGGGAAGAAAAGCTCTATTTTTCACCGTTGATGGATTTAGCGAACCGGGAAATTATTGCCTATAATTTTGCGAAACGCCCTAAGTTCTCATTGGTAAAAAGAATGCCGGAAGAAGGACTTGGCAAACTAAAACCGAGCGAATGCCCGATTATTCACAGCGACCAAGGGGTATTGTACGGCTCAGCAGAATGGGTAAAGATGTTGGAAGGCAAGGCGATACAAAGTATGAGTCGCCGAGGGAATTGCTATGATAATGCGGTGATTGAAAGCTTTTTTGCGATATTAAAATCTGAGTGTTTTTACTCACGCACTTATACTTCGATTGCCGAATTACAGGCGGAAATTGAAGAATATTTGGTGTATTACAACCAAGAACGAATTAAACTTGATTTAAAAGGATTAAGCCCGGTGCAATACCGAGCTCAATATTTAAGT","","","19548","VLNRDFTATALNQKWVTDVTEFRVGEEKLYFSPLMDLANREIIAYNFAKRPKFSLVKRMPEEGLGKLKPSECPIIHSDQGVLYGSAEWVKMLEGKAIQSMSRRGNCYDNAVIESFFAILKSECFYSRTYTSIAELQAEIEEYLVYYNQERIKLDLKGLSPVQYRAQYLS","746930","","transposase","Cytoplasm","This sequence is similar to gi|28872132, a predicted transposase fragment from Pseudomonas syringae.","
InterPro
IPR001584
Domain
Integrase, catalytic core
PF00665\"[7-165]Trve
PS50994\"[7-168]TINTEGRASE


","BeTs to 10 clades of COG2801COG name: Putative transposaseFunctional Class: LThe phylogenetic pattern of COG2801 is ---p-----drlbcefgh-n-j---wNumber of proteins in this genome belonging to this COG is","","Residues 55 to 114 match (3e-09) PD:PD001459 which is described as TRANSPOSASE COMPLETE PROTEOME PLASMID ORFB IS629 INSERTION ELEMENT SEQUENCE FOR ","","","","","","","","","","","","Wed Feb 25 09:32:17 2004","Wed Feb 25 09:32:17 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to several transposase sequences in AA: AA1522, AA0945, AA0845, AA0835, AA0709, AA0006, AA1371, AA1578.AA01077 is paralogously related to AA02342 (1e-95), AA01444 (1e-95), AA01287 (1e-95), AA01268 (1e-95), AA00010 (1e-95), AA02117 (2e-89), AA00145 (2e-23) and AA02420 (4e-17).","Wed Feb 25 09:32:17 2004","","","","","Residues 7 to 165 (E-value = 5.6e-31) place AA01077 in the rve family which is described as Integrase core domain (PF00665)","","","","","","","","1","","","" "AA01078","747513","747013","501","TTGTTCACCCTTTCGGGGCCGTCGGTAGAACCGACGTTCAAAAAGCATTGCTTTTTGTGCGGTCGTTTTCACGGACGTTTTTACGGAGATAACATGAAAATAGGGAAATTAGCCAAAGCCGTAGGATGCAGCGTGGAAGCCATCCGATTTTACGAACAAAAAGGCTTAATGCCATGCCCGCCCCGTTCCGCCGGCGGTTTTCGTTTATACACGGACGAGCACCTGCAACGCCTGTCGTTTATTTGTTATTGCCGCTCCTTGGATATGTCTCTTAAAGAAATCAAATTGCTGTTGAGCCTGGAAAGTGCTTCCGAACAACAAAAAGCGGAAATCAATCAATTGCTCGATCGACATATTCAAGACATTGCCAAACACATCCACCGCCTGCAACATTTACGCATGAATCTCATCCAACTGAAACAACAATGCGGAGAAGTGAATCAGCAACAAAACTTGCTGCGAATCCTGCAATACAGTCAGGTAAAGTTTAGACCGTTGAAG","","","19375","LFTLSGPSVEPTFKKHCFLCGRFHGRFYGDNMKIGKLAKAVGCSVEAIRFYEQKGLMPCPPRSAGGFRLYTDEHLQRLSFICYCRSLDMSLKEIKLLLSLESASEQQKAEINQLLDRHIQDIAKHIHRLQHLRMNLIQLKQQCGEVNQQQNLLRILQYSQVKFRPLK","747015","","transcriptional regulator (probable MerR family)","Cytoplasm","","
InterPro
IPR000551
Domain
Bacterial regulatory protein, MerR
PR00040\"[33-44]T\"[44-57]T\"[68-88]THTHMERR
PF00376\"[33-70]TMerR
SM00422\"[32-101]THTH_MERR
PS50937\"[31-100]THTH_MERR_2
PS00552\"[35-57]THTH_MERR_1
InterPro
IPR015358
Domain
Transcription regulator MerR, DNA binding
PF09278\"[75-139]TMerR-DNA-bind
noIPR
unintegrated
unintegrated
G3DSA:1.10.1660.10\"[32-145]Tno description


","BeTs to 13 clades of COG0789COG name: Predicted transcriptional regulatorsFunctional Class: KThe phylogenetic pattern of COG0789 is a------q-drlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-26) to 2/2 blocks of the IPB000551 family, which is described as \"Bacterial regulatory proteins, MerR family\". Interpro entry for IP:IPR000551. IPB000551A 34-55 1.9e-08 IPB000551B 57-98 1.1e-16","Residues 32 to 88 match (4e-08) PD:PD406858 which is described as COMPLETE PROTEOME TRANSCRIPTIONAL REGULATOR TRANSCRIPTION DNA-BINDING REGULATION FAMILY MERR MERCURIC ","","","","","","","","","","","","Fri Dec 20 11:19:52 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01078 is paralogously related to AA00131 (4e-13) and AA01113 (2e-07).","","","","","","Residues 33 to 70 (E-value = 3.8e-18) place AA01078 in the MerR family which is described as MerR family regulatory protein (PF00376)","","","","","","","","1","","","" "AA01079","747801","747544","258","TTGGCAAAAATCGTGCAAAAAGGCATTCGCTTAAATGAACTAAACCAACAGGTTAACGGATTTTTCCCGCCCGAGTTCAAGGATTTGTATCGCATTGCCAATATAGAACAAAACAGTTTGCGCATTGAAGTGGCGAATGCCATGGTGCGGCAAAGTTTTTTGTTTCGTCAGCGGGAATTATTACGTTTAATTCAGCAACATTTGCCGGAAATCACGCAATTAACCTTTTACATCAACCCCGAATTTCGCCGCGGTGCC","","","12238","LAKIVQKGIRLNELNQQVNGFFPPEFKDLYRIANIEQNSLRIEVANAMVRQSFLFRQRELLRLIQQHLPEITQLTFYINPEFRRGA","747546","","conserved hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","Residues 2 to 80 match (6e-15) PD:PD069360 which is described as PROTEOME COMPLETE YPO0562 HI0907 PM1221 VC2395 ","","","","","","","","","","","","Fri Dec 20 11:26:39 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01079 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01080","747819","747944","126","ATGTTTGAATATTTACCGGTTTTTGATAACGCATTGCCTTGTTTTCCGCCTTTTCGCCCTAATATTTATGACATTGTAGCGAATTTCCGCTACAATACCGACAATTTTTTGATATTGAGATCCTTA","","","5040","MFEYLPVFDNALPCFPPFRPNIYDIVANFRYNTDNFLILRSL","747944","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 09:43:15 2004","Wed Feb 25 09:43:15 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01080 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 09:43:15 2004","","","","","","","","","","","","","1","","","" "AA01081","747944","748249","306","ATGATAATTTCTCACAAAAGCAAACATCATTTTTGGTCGCAACTGCTGCTTGGCATGCTTGCGATTTTTGTTTTGCCTGTCGGTCAGGAACTGAATTATTCCTCTTCCGTCGGCAGAGAAAATTATCAAAACGCCCAGCAACAAAACGCGCCGCAGATTTTAACCACCGTTGCGTTGCTGCAACAAACCAGTCAGCAGCAACACCAACCGCAACATGCGCCGTTGGAAGCTGAAAATCTTCCGCAAAATGAACCGCACTTTGCGCGTTCGCCTTTCGTTCCCAATGCACCGATTCGTGCCGGACCT","","","11424","MIISHKSKHHFWSQLLLGMLAIFVLPVGQELNYSSSVGRENYQNAQQQNAPQILTTVALLQQTSQQQHQPQHAPLEAENLPQNEPHFARSPFVPNAPIRAGP","748251","","hypothetical protein","Periplasm, Cytoplasm","","
noIPR
unintegrated
unintegrated
PD067723\"[8-102]TQ9CLK6_PASMU_Q9CLK6;
signalp\"[1-29]?signal-peptide
tmhmm\"[10-28]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Fri Dec 20 11:38:52 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01081 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01083","748271","751030","2760","TTGTATATTCCGTCGTTTAATTCGTTAAACGATCTCATTTATCTATTTTTAAAAGAAAAAATTATGCTTAGAACTATTGCAACTAAAATCTTCGGCAGCCGTAACGATCGTATCTTACGCCGCCTCAATAAAATCGTCGTTAAAATTAATAAATTAGAACCGGAATTTGAAGCCTTAAGCGATGAACAGCTGAAAGCCAAAACCGCCGAATTCCGTGAGCGTTTAGGCAAAGGTGAAACCTTGGAAAGCCTGATGCCGGAAGCCTTTGCTACCGTGCGTGAAGCCAGTAAACGTGTGCTGGGCATGCGTCACTTCGACGTGCAACTTATCGGCGGCATGGTGCTTAACGATCGTTGTATCGCGGAAATGCGTACCGGTGAAGGGAAAACCTTAACCGCCACATTATCTTGCTACCTTAACGCCTTACCGGGCAAAGCGGTACACGTGGTGACCGTGAATGACTACTTGGCGCGCCGCGATGCGGAAACCAATCGTCCGTTATTTGAATTTTTGGGCATTACCGTAGGCGTAAACATTCCGGGCTTGTCACCGGAAGAAAAACGCGCAGCATACGCAGCGGACATTACCTACGCCACCAACAGTGAATTAGGTTTCGACTATTTACGTGACAACCTGGCGCACTCGCCGCAGGAACGCTTCCAAAAAGATTTATATTATGCGCTGGTGGATGAAGTGGACTCCATCTTAATTGATGAAGCACGGACCCCATTGATTATTTCCGGTCAGGCAGAAGACAGCTCCGAGCTTTACATCGCCATTGATAAATTGATCCCAAACCTGATTAAACAAGACAAAGAAGACACGGAAGAATATCAAGGCACCGGCGACTACACCTTAGATTTAAAAACCAAACAGGCACACTTAACCGAGCGCGGTCAGGAAAAATGTGAACAATGGTTGATTCAACAAGGCTTCATGAAAGACACCGAATCTCTTTATTCACCGTCAAAAATCACTTTACTCCATCATGTCATGGCGGCATTGCGCGCTCACACGCTGTTTGAGCGCGATGTTGATTACATCGTCAAAGACGGAGAGATCGTTATCGTGGACGAACACACCGGTCGTACCATGGCGGGTCGTCGCTGGTCCGATGGCTTACACCAAGCCATTGAGGCCAAAGAGGGCGTGCGCATTCAAAGCGAAAACCAAACCGTCGCCTCCATCACTTACCAAAACTATTTCCGTTTATATGAAAAATTGGCGGGTATGACCGGTACGGCGGATACGGAAGCCTTTGAATTCCAAAAAATTTATGGTTTAGAAACAGTGGTCATTCCAACCAACCGTCCGATGATTCGTGATGACCGTACCGACGTCATGTTTGAAACGGAAGAATATAAATTCAACGCCATTATTGACGACATCAAAGATTGCGTAGCGCGTCAACAACCGGTATTGGTGGGAACAATTTCCATCGAAAAATCCGAATTGCTTTCCAACGCATTGGATAAAGCGGGCATCAAACACAATGTACTGAACGCCAAATTCCACGCGCAGGAAGCAGAAATCGTAGCGAACGCCGGCTATCCGGGTGCTGTGACCATTGCCACCAATATGGCGGGGCGTGGTACCGACATCGTGTTAGGTGGTAACTGGAAAGCAGAAGTGGATAAACTGGAGAATCCGACAGCGGAACAAATCGAAGCCATTAAAGCAGCATGGCAGGAACGCCATGACATCGTGAAAAATGCCGGCGGGTTACACATTATCGGCACCGAACGCCACGAATCCCGTCGTATCGACAACCAGCTACGCGGTCGTTCCGGCCGTCAGGGCGACCCGGGTTCCTCCCGTTTCTACCTGTCCTTGGAAGATGCGTTAATGCGCATTTACCTCAATGAAGGCAAACTCAACATGATGCGTAAAGCCTTCAGTAATACAGCTGAAGCCATGGAATCCAAGCTGCTGGCGAAAGTAATTGCTTCCGCACAAGCGAAAGTGGAAGCGCATAACTTCGACGGACGTAAAAACCTGCTTGAATTTGACGATGTGGCAAACGATCAACGCCACGCCATTTACGAGCAGCGTAACGAATTACTGGAAAATGACGATATTTCAGAAACTATTGATGTGATTCGCCGGGATGTGTTCAACAGCGTGATCGATCAATATATCCCGCCGCAATCTTTGGAAGAGCAATGGGATATTCCTGCCTTGGAACAGCGCTTGAAACAAGATTTTGCCTTGGATTTGCCAATCAGAAAATGGCTGGATGAAGACAATCATCTGCACGAAGAAACCCTGCGTGAGCGCATTATTCAATCTGCCGTGGATGAATACAAACGCAAAGAAGAATTGGCGGGCGAACAAACTATGCGCAACTTTGAAAAAGGCGTGATGTTGCAAACCTTAGATGAGCTTTGGAAAGAACATTTATCCGCCATGGATCATTTGCGTCGCGGTATTCATTTACGCGGTTATGCGCAAAAAGATCCGAAACAGGAATACAAAAAAGAGTCCTTTCAAATGTTTACGGAAATGTTGGATGCCCTGAAATTAAGCGTGGTCACCACCTTAAGTCGCGTTCAGGTTCGGACCTCGGAAGAAATGGAAGAAGCGGAACGTTTGCGTCAGGAACTGGCACAACGTGAAGCCGCCGCCATGCAGTATAACAACGACGAATCGCAAGGGGCGCAACAGGGTACGGAAGAACACCATAAAATTGGTCGTAACGAGCCTTGCCCGTGCGGCTCCGGCAAGAAATACAAACATTGCCACGGCAGCCGGGCCAGACAT","","","104954","LYIPSFNSLNDLIYLFLKEKIMLRTIATKIFGSRNDRILRRLNKIVVKINKLEPEFEALSDEQLKAKTAEFRERLGKGETLESLMPEAFATVREASKRVLGMRHFDVQLIGGMVLNDRCIAEMRTGEGKTLTATLSCYLNALPGKAVHVVTVNDYLARRDAETNRPLFEFLGITVGVNIPGLSPEEKRAAYAADITYATNSELGFDYLRDNLAHSPQERFQKDLYYALVDEVDSILIDEARTPLIISGQAEDSSELYIAIDKLIPNLIKQDKEDTEEYQGTGDYTLDLKTKQAHLTERGQEKCEQWLIQQGFMKDTESLYSPSKITLLHHVMAALRAHTLFERDVDYIVKDGEIVIVDEHTGRTMAGRRWSDGLHQAIEAKEGVRIQSENQTVASITYQNYFRLYEKLAGMTGTADTEAFEFQKIYGLETVVIPTNRPMIRDDRTDVMFETEEYKFNAIIDDIKDCVARQQPVLVGTISIEKSELLSNALDKAGIKHNVLNAKFHAQEAEIVANAGYPGAVTIATNMAGRGTDIVLGGNWKAEVDKLENPTAEQIEAIKAAWQERHDIVKNAGGLHIIGTERHESRRIDNQLRGRSGRQGDPGSSRFYLSLEDALMRIYLNEGKLNMMRKAFSNTAEAMESKLLAKVIASAQAKVEAHNFDGRKNLLEFDDVANDQRHAIYEQRNELLENDDISETIDVIRRDVFNSVIDQYIPPQSLEEQWDIPALEQRLKQDFALDLPIRKWLDEDNHLHEETLRERIIQSAVDEYKRKEELAGEQTMRNFEKGVMLQTLDELWKEHLSAMDHLRRGIHLRGYAQKDPKQEYKKESFQMFTEMLDALKLSVVTTLSRVQVRTSEEMEEAERLRQELAQREAAAMQYNNDESQGAQQGTEEHHKIGRNEPCPCGSGKKYKHCHGSRARH","751032","","preprotein translocase SecA subunit","Cytoplasm, Inner membrane","","
InterPro
IPR000185
Family
SecA protein
PR00906\"[84-108]T\"[122-136]T\"[138-148]T\"[191-211]T\"[360-382]T\"[397-414]T\"[434-447]TSECA
TIGR00963\"[49-839]TsecA: preprotein translocase, SecA subunit
PS01312\"[521-536]TSECA
InterPro
IPR001650
Domain
Helicase, C-terminal
PS51194\"[462-643]THELICASE_CTER
InterPro
IPR004027
Domain
SEC-C motif
PF02810\"[898-918]TSEC-C
InterPro
IPR011115
Domain
SecA DEAD-like
PF07517\"[27-423]TSecA_DEAD
InterPro
IPR011116
Domain
SecA Wing and Scaffold
PF07516\"[638-852]TSecA_SW
InterPro
IPR011130
Domain
SecA preprotein cross-linking region
PF01043\"[249-379]TSecA_PP_bind
InterPro
IPR014018
Domain
SecA motor DEAD
PS51196\"[24-640]TSECA_MOTOR_DEAD
InterPro
IPR014021
Domain
Helicase superfamily 1 and 2 ATP-binding
PS51192\"[110-268]THELICASE_ATP_BIND_1
noIPR
unintegrated
unintegrated
G3DSA:1.10.3060.10\"[669-852]Tno description


","BeTs to 18 clades of COG0653COG name: Preprotein translocase subunit SecA (ATPase, RNA helicase)Functional Class: NThe phylogenetic pattern of COG0653 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 836 to 894 match (5e-08) PD:PD475177 which is described as COMPLETE PROTEOME SECA PREPROTEIN TRANSLOCASE SUBUNIT TRANSLOCASE MEMBRANE ATP-BINDING SECRETION ","","","","","","","","","","","","Fri Dec 20 11:40:42 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01083 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 898 to 918 (E-value = 2.6e-10) place AA01083 in the SEC-C family which is described as SEC-C motif (PF02810)","","","","","Lill R, Cunningham K, Brundage LA, Ito K, Oliver D, Wickner W.SecA protein hydrolyzes ATP and is an essential component ofthe protein translocation ATPase of Escherichia coli. EMBO J Mar;8(3):961-6 (1989). PubMed: 2542029 Benach J, Chou YT, Fak JJ, Itkin A, Nicolae DD, Smith PC,Wittrock G, Floyd DL, Golsaz CM, Gierasch LM, Hunt JF. Phospholipid-induced monomerization and signal-peptide-inducedoligomerization of SecA. J Biol Chem. 2002 Oct 27 [epub ahead of print] PMID: 12403785 Chou YT, Swain JF, Gierasch LM. Functionally significant mobile regions of Escherichia coliSecA ATPase identified by NMR. J Biol Chem. 2002 Oct 22 [epub ahead of print] PMID: 12397065 Hunt JF, Weinkauf S, Henry L, Fak JJ, McNicholas P, Oliver DB,Deisenhofer J. Nucleotide control of interdomain interactions in theconformational reaction cycle of SecA. Science. 2002 Sep 20;297(5589):2018-26. PMID: 12242434 ","","Fri Nov 21 14:55:21 2003","1","","","" "AA01085","751110","751511","402","ATGAGCAAACCGCTTGTACAGGTTGCAGCCGGGATTATTCGTAACGAATTCGGACAAATTTATTTAACTCAACGTCTGGAAGGACAGGATTTCGCGCAAGCCCTGGAATTCCCCGGCGGGAAAGTGGATAAAGGGGAAACGCCGGAACAAGCGCTTAAACGCGAGCTGGAAGAAGAAATCGGCATCGTGGTGCTAAATGCTCAATTGTTCGAACGCTTTGAATTTGAGTATCCCACTAAAGTCATTACATTCTTTTTTTATCTGGTGGAAGAATGGGTCGGTGAACCGTTCGGGCGGGAAGGACAAGACGGTTTCTGGTTAGCACAAAACGAACTGGATGCCGGACAATTTCCGCCGGCAAATGCCAAATTAATTCAACGACTGTTGGCGGAAAGTGGAGAT","","","15184","MSKPLVQVAAGIIRNEFGQIYLTQRLEGQDFAQALEFPGGKVDKGETPEQALKRELEEEIGIVVLNAQLFERFEFEYPTKVITFFFYLVEEWVGEPFGREGQDGFWLAQNELDAGQFPPANAKLIQRLLAESGD","751513","","mutator mutT protein (7,8-dihydro-8-oxoguanine-triphosphatase) (8-oxo-dGTPase) (dGTP pyrophosphohydrolase)","Cytoplasm","","
InterPro
IPR000086
Domain
NUDIX hydrolase
PR00502\"[35-49]T\"[49-64]TNUDIXFAMILY
G3DSA:3.90.79.10\"[3-131]Tno description
PF00293\"[5-131]TNUDIX
PS00893\"[40-61]TNUDIX
InterPro
IPR002667
Family
Isopentenyl-diphosphate delta-isomerase
PD004109\"[15-117]TQ8A0P9_BACTN_Q8A0P9;
InterPro
IPR003561
Family
Mutator MutT
PR01401\"[4-25]T\"[79-92]TMUTATORMUTT
TIGR00586\"[2-130]Tmutt: mutator mutT protein
noIPR
unintegrated
unintegrated
PTHR22769\"[10-131]TMUTT/NUDIX HYDROLASE


","BeTs to 22 clades of COG0494COG name: NTP pyrophosphohydrolases including oxidative damage repair enzymesFunctional Class: L,RThe phylogenetic pattern of COG0494 is aomp-zyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 3.8e-18) to 2/2 blocks of the PR01401 family, which is described as \"Mutator MutT protein signature\". Prints database entry for PR:PR01401. PR01401A 4-25 4.8e-10 PR01401B 79-92 1.9e-06Significant hit ( 5.5e-14) to 1/1 blocks of the IPB000086 family, which is described as \"NUDIX hydrolase\". Interpro entry for IP:IPR000086. IPB000086 35-61 5.4e-14","Residues 3 to 121 match (4e-07) PD:PD063287 which is described as COMPLETE PROTEOME MUTT FAMILY SAV2490 MUTT/NUDIX ","","","","","","","","","","","","Fri Dec 20 11:44:59 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01085 is paralogously related to AA02850 (6e-05), AA01160 (6e-05) and AA00204 (6e-05).","","","","","","Residues 5 to 131 (E-value = 5.3e-29) place AA01085 in the NUDIX family which is described as NUDIX domain (PF00293)","","","","","Legler PM, Massiah MA, Mildvan AS. Mutational, kinetic, and NMR studies of the mechanism of E.coli GDP-mannose mannosyl hydrolase, an unusual Nudixenzyme. Biochemistry. 2002 Sep 3;41(35):10834-48. PMID: 12196023 Lu AL, Li X, Gu Y, Wright PM, Chang DY. Repair of oxidative DNA damage: mechanisms and functions. Cell Biochem Biophys. 2001;35(2):141-70. Review. PMID: 11892789 Akiyama,M., Horiuchi,T. and Sekiguchi,M. Molecular cloning and nucleotide sequence of the mutTmutator of Escherichia coli that causes A:T to C:G transversion Mol. Gen. Genet. 206 (1), 9-16 (1987) PubMed: 3033442 Bhatnagar,S.K. and Bessman,M.J. Studies on the mutator gene, mutT of Escherichia coli.Molecular cloning of the gene, purification of the gene product, and identification of a novel nucleoside triphosphatase J. Biol. Chem. 263 (18), 8953-8957 (1988) PubMed: 3288626 ","","Fri Dec 20 11:44:59 2002","1","","","" "AA01086","751651","751532","120","ATGAGAGAGAGCGAAATTGATAATTTATCTTTAGTTTTTGGTAGTTCTCCAGTAAAAATAGTTGCGGCTGTTTCTAAACGGGAAATTCTCACTTTTTATTGTGGTTTGTCAGATTTGGCC","","","4342","MRESEIDNLSLVFGSSPVKIVAAVSKREILTFYCGLSDLA","751532","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 09:49:13 2004","Wed Feb 25 09:49:13 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01086 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 09:49:13 2004","","","","","","","","","","","","","1","","","" "AA01087","753040","752009","1032","ATGAATCGGCTATTTCCTGAACAGCTTGCTTCGTCACTGGAACGGCATTTAGCCCATGTGTATTTTCTGGTGGGCGAGGATCCGTTGTTGCTCAATGAAAGCGCCAATGGTATTTACCAAACGGCGCTTCAGCGGGGATTCGATGAAAAAGTTGAACTGGACATTAATGCCTCCACCGACTGGAATGATTTATTCGAGCGGGTGCAATCCATGGGCTTATTTTTCAATAAACAGCTCATTATTTTAGATTTACCTGAAAATGCGACCGCACTTTTACAGAAAAACTTATCCGAATTCATTTCGTTGCTTCAGCCCGATGTGCTACCGATTTTCCGTTTAGCCAAACTCACTAAAGCCGCTGAAAAGCAGGCGTGGTTTATGGCGGCGAATCAGTATGAACCGCAGGCGGTATTGGTAAACTGTCAAACCCCCAATGCCGAACAATTGCCCCGCTGGGTGGCGAATCGGGCGAAGATGTTGGGGTTAAGCATTGAACAAGAAGCGGTGCAGTTGTTGTGTTACAGCTACGAAAACAACCTGTTGGCACTCAAGCAAACACTGCAATTACTGGATTTGCTTTATCCTGATCGTAAACTCACTTTTGCCCGCGTGAATAGCGTGGTGGAACAGTCCTCGGTGTTTACGCCGTTCCAATGGGTTGATGCGATTTTAGGCGGAAAAGGGAATCGCGCCCGCCGAATTCTCACCGGTTTAAAAGATGAAGATGTTCAGCCGATTATTCTCCTGCGCACGTTGCAGCGCGATTTAATGACTTTACTGGAGATCAGTAAACCGGAACAACCCCAATCCCTTGACTCGCCTTTACCCACCGATCAACTGCGTGAACAGTTTGATCGCCTGAAAGTATGGCAAAACCGCCGTTCATTGTTTACTCAAGCGGTGCAACGTTTAACCTACCGTAAACTCTATCTTTTTTTTCAGCAACTCGCCGATGTGGAGCGCTGTGCGAAACAGGAATTTAGCGATGATATTTGGCAACAACTGGAAGATTTATCGGTAAGATTTGCCGGT","","","39762","MNRLFPEQLASSLERHLAHVYFLVGEDPLLLNESANGIYQTALQRGFDEKVELDINASTDWNDLFERVQSMGLFFNKQLIILDLPENATALLQKNLSEFISLLQPDVLPIFRLAKLTKAAEKQAWFMAANQYEPQAVLVNCQTPNAEQLPRWVANRAKMLGLSIEQEAVQLLCYSYENNLLALKQTLQLLDLLYPDRKLTFARVNSVVEQSSVFTPFQWVDAILGGKGNRARRILTGLKDEDVQPIILLRTLQRDLMTLLEISKPEQPQSLDSPLPTDQLREQFDRLKVWQNRRSLFTQAVQRLTYRKLYLFFQQLADVERCAKQEFSDDIWQQLEDLSVRFAG","752011","","DNA polymerase III, delta subunit","Cytoplasm","","
InterPro
IPR005790
Family
DNA polymerase III, delta subunit
TIGR01128\"[17-343]TholA: DNA polymerase III, delta subunit
InterPro
IPR010372
Family
DNA polymerase III, delta
PF06144\"[21-340]TDNA_pol3_delta
noIPR
unintegrated
unintegrated
G3DSA:1.10.8.60\"[145-215]Tno description
G3DSA:1.20.272.20\"[216-344]Tno description
G3DSA:3.40.50.300\"[1-142]Tno description


","BeTs to 6 clades of COG1466COG name: DNA polymerase III delta subunitFunctional Class: LThe phylogenetic pattern of COG1466 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 275 to 341 match (3e-16) PD:PD277480 which is described as DNA POLYMERASE COMPLETE PROTEOME DELTA SUBUNIT III TRANSFERASE REPLICATION DNA-DIRECTED ","","","","","","","","","","","","Fri Dec 20 11:47:45 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01087 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 344 (E-value = 1e-179) place AA01087 in the DNA_pol3_delta family which is described as DNA polymerase III, delta subunit (PF06144)","","","","","Dong,Z., Onrust,R., Skangalis,M. and O'Donnell,M. DNA polymerase III accessory proteins. I. holA and holBencoding delta and delta' J. Biol. Chem. 268 (16), 11758-11765 (1993) PubMed: 8505303 Carter,J.R., Franden,M.A., Aebersold,R. and McHenry,C.S. Molecular cloning, sequencing, and overexpression of thestructural gene encoding the delta subunit of Escherichia coliDNA polymerase III holoenzyme J. Bacteriol. 174 (21), 7013-7025 (1992) PubMed: 1400251 O'Donnell,M. Accessory protein function in the DNA polymerase IIIholoenzyme from E. coli Bioessays 14 (2), 105-111 (1992) PubMed: 1575709 ","","Fri Dec 20 11:47:45 2002","1","","","" "AA01088","753543","753043","501","ATGCTTAAACACGTCAAAACCTTATTTCTGACCGTTGCCGTTTTAGGGCTTTTCGCCTGCGGATTTCATTTCCAAAACGGCGAATTAATTCCGAAAGAATTACAAACCCTACGTCTAGAAAGCAGCGATCCTTACAGTGATATGGCACGCGTCATGCGCCGTCAGTTGCAGCTAAATAACGTGACGCTGGTAGAAGATCAGACAAACGTGCCGGTGTTGCGCTTAAACGGCATTTCCACTAAAGACCAAGTGGTGTCCATTTTCAAACAGGGTCGAGAAGCGGAAAAACAACTGATTCTGGAAGTAGACGCCAGTGTAAAACTGCCGAATCAGGACAGTTTCCCGATTTCCACCCGTGTGAATCGTACGTTCTTTGATAACTCCCGTGCGGCGTTGGCGAAATCGGCGGAAAAAGACGTGATTTGGCAGGATATGCGCGAGCAGGCGGCACGCCAGTTAATTAACAAAATGGTTGCCTTACAGCATCAAATTCAAGAGAAA","","","19062","MLKHVKTLFLTVAVLGLFACGFHFQNGELIPKELQTLRLESSDPYSDMARVMRRQLQLNNVTLVEDQTNVPVLRLNGISTKDQVVSIFKQGREAEKQLILEVDASVKLPNQDSFPISTRVNRTFFDNSRAALAKSAEKDVIWQDMREQAARQLINKMVALQHQIQEK","753045","","rare lipoprotein B precursor","Cytoplasm, Outer membrane","","
InterPro
IPR007485
Family
Rare lipoprotein B
PF04390\"[20-163]TRplB
noIPR
unintegrated
unintegrated
PD339286\"[17-165]TQ9CLL1_PASMU_Q9CLL1;
PS51257\"[1-20]TPROKAR_LIPOPROTEIN
signalp\"[1-21]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","BeTs to 5 clades of COG2980COG name: Rare lipoprotein BFunctional Class: MThe phylogenetic pattern of COG2980 is --------------efghsn------Number of proteins in this genome belonging to this COG is","","Residues 5 to 160 match (9e-57) PD:PD339286 which is described as LIPOPROTEIN PROTEOME COMPLETE B RARE PRECURSOR SIGNAL A MINOR MEMBRANE ","","","","","","","","","","","","Fri Dec 20 11:52:01 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01088 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 20 to 163 (E-value = 2e-78) place AA01088 in the RplB family which is described as Rare lipoprotein B family (PF04390)","","","","Dong Z, Onrust R, Skangalis M, O'Donnell M.DNA polymerase III accessory proteins. I. holA and holB encoding delta and delta'.J Biol Chem. 1993 Jun 5;268(16):11758-65.PMID: 85053033 Carter JR, Franden MA, Aebersold R, McHenry CS.Molecular cloning, sequencing, and overexpression of the structural gene encoding the delta subunit of Escherichia coli DNA polymerase III holoenzyme.J Bacteriol. 1992 Nov;174(21):7013-25.PMID: 1400251","","Fri Dec 20 11:52:01 2002","","1","","","" "AA01089","753532","753657","126","GTGTTTAAGCATAAAATCACCTTAAAGATTATTCATAAGCGCATTAGTTCGCTCATTCACCCCTTCGGGGCGGTTGATAGAACCGATGTTCAAAAAAACGTTGTTTTTGCCAACCGCACTTTGATG","","","4855","VFKHKITLKIIHKRISSLIHPFGAVDRTDVQKNVVFANRTLM","753657","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 09:50:51 2004","Wed Feb 25 09:50:51 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01089 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 09:50:51 2004","","","","","","","","","","","","","1","","","" "AA01090","756273","753688","2586","ATGCAAGAGCAATATCGTCCTGATTTGCTTGAACCGGAAGTGCAAAAATTCTGGCAGGACAATAAAACTTTCAAAGCAGTACAAGATAACAACAAAGAAAAATATTACTGTCTTTCCATGCTGCCGTATCCCTCCGGTCGTTTGCACATGGGGCATGTGCGGAACTATACCATCGGCGATGTGGTGTCCCGCTATCAACGTATGATTGGTAAAAACGTGTTACAGCCGATGGGCTGGGATGCCTTCGGTTTGCCGGCGGAAGGCGCGGCGGTGAAGAATAATACCGCCCCGGCGAAATGGACTTACGAAAATATTGCCTACATGAAAAACCAGTTGCAACTGTTGGGTTTCAGTTACGATTGGGATCGCGAAGTGACCACTTGCCGTCCGGAATATTACAAATGGGAGCAATGGTTCTTTACCGAGTTATACAAAAAAGGCTTAGTGTATAAAAAAACCTCTACCGTGAACTGGTGCCCGAACGATAAAACCGTGTTGGCGAACGAGCAGGTGCATGAAGGTTGTTGCTGGCGTTGTGATACACCGGTGGAGCAAAAAGAGATTCCACAATGGTTTATCAAAATCACCGATTACGCCGAGCAGTTGCTTAATTGCTTAGATGAGTTGCCACAATGGCCGGAAACGGTGAAAACCATGCAACGCAACTGGATCGGGCGTTCCGAAGGGGTGGAAATCACCTTTGATATTAAAGATACCAACGAGAAGCTCGCGGTTTATACCACCCGCCCTGACACTTTCTATGGCGTCAGCTATGTGGCGGTGGCAGCGGCCCATCCGTTAGCCACGTTGGCGGCGCAAAATAATCCGGCGTTGGCGCAATTCATTCAGGAAGCGAAAAATACCAAAGTTGCCGAGGCAGACATTGCCACTATGGAGAAAAAAGGCATGGCGACCGGTTTGTATGCAGTGCACCCGCTAACCGGTGAATTGTTGCCGGTGTGGGTGGCGAATTTTGTCTTAATGCACTATGGTACCGGCGCGGTCATGGCGGTGCCGGCGCACGATCAGCGCGACTATGAATTCGCACAAAAATACGGTTTACCGATTAAACAGGTTATTGAGCCGATTCATGGCGAAGAAATCGATTTAACCAAACAAGCCTTTACCGAACACGGCAAACTCATTTATTCTGCCGAATTTGACGGTTTGGAATTTGACGCGGCGTTCAGCGGCATTGCCGATAAATTGGAACAGTTAGGCATGGGTAAACGCCAAGTGAATTACCGCCTGCGTGACTGGGGCGTGTCCCGTCAGCGTTATTGGGGCGCACTGATTCCGATGTTGACCTTGGAAAATGGCGATGTGGTGCCGGCACCAATGGAAGATTTGCCGATTATCCTGCCGGAAGATGTGGTGATGAACGGCGTGAACAGCCCGATTAAAGCGGATCCCGAATGGGCGAAAACCACCTATCAGGGCAAGCCGGCGTTGAGAGAAACGGACACCTTTGACACTTTCATGGAATCTTCCTGGTATTACGCCCGTTACACCTGCCCTGAATACCAACAAGGTATGCTGAACAGCGAAGAAGCTAATTACTGGTTGCCGGTAGATCAATATATCGGCGGTATCGAACACGCCACCATGCACTTGTTGTATTTCCGTTTCTTCCATAAATTATTGCGCGATGCCGGCTTTGTCACCAGCGACGAACCGGCGAACAAGTTGTTGTGTCAAGGCATGGTGTTGGCGGACGCGTTCTATTACACCAGCCCGACCAATGAGCGTATTTGGGTTTCGCCGACCAAAGTTACATTAGAACGTGACGACAAAGGACGTATTGTCAAAGCGACGGATGACGAAGGACATGAACTGGTACACGCCGGTATGACCAAAATGTCGAAATCCAAAAACAACGGTATCGACCCGCAGGAAATGGTGGAAAAATACGGCGCGGACACCGTGCGTTTGTTCATGATGTTCGCTTCCCCGGCGGAAATGACCTTGGAATGGCAGGAATCCGGCGTGGAAGGCGCGAAACGCTTCTTGGCGCGCGTGTGGAATTTGGTGTTTGAATACAACAAAAATCCGGCAAAAACGCCGTTAAATCCGACCGCACTTTCCGCCGCCCAAAAAGCCTTGCGTCGTGACGTGCACAAAACCATCGCGAAAGTGAGCGATGATATCGGTCGCCGTCAAACCTTCAATACCGCCATTGCGGCGATTATGGAGTTGATGAACAAACTCACCCGCGCGCCGTTGGACGACCAACAAGATCGCGCCATGATGGCGGAGGCCTTGAGCGCGGTGGTTCGTATGCTTTACCCGATTACCCCGCACATTTGCTTCCGTTTATGGCAAGAACTCGGCAATCAGGACATCATTGATTTCGCCCCTTGGGTGGAAGCCGATGCCGAGGCGATGATTGAAGATGAAAAACTCATCGTAGTGCAAGTGAACGGTAAAGTGCGCGGCAAAGTAACCGTGGCGGCGGATGCCGATAAAGACACGGTGAAAGCGGTTGCCTTTGCCGATGAAAATGTCAAACGCTTTACCGACGGAATGCAAATTGTGAAAGTAATTTATGTTGCCGGTAAATTGCTCAACGTGGTGGTGAAACCACAA","","","98267","MQEQYRPDLLEPEVQKFWQDNKTFKAVQDNNKEKYYCLSMLPYPSGRLHMGHVRNYTIGDVVSRYQRMIGKNVLQPMGWDAFGLPAEGAAVKNNTAPAKWTYENIAYMKNQLQLLGFSYDWDREVTTCRPEYYKWEQWFFTELYKKGLVYKKTSTVNWCPNDKTVLANEQVHEGCCWRCDTPVEQKEIPQWFIKITDYAEQLLNCLDELPQWPETVKTMQRNWIGRSEGVEITFDIKDTNEKLAVYTTRPDTFYGVSYVAVAAAHPLATLAAQNNPALAQFIQEAKNTKVAEADIATMEKKGMATGLYAVHPLTGELLPVWVANFVLMHYGTGAVMAVPAHDQRDYEFAQKYGLPIKQVIEPIHGEEIDLTKQAFTEHGKLIYSAEFDGLEFDAAFSGIADKLEQLGMGKRQVNYRLRDWGVSRQRYWGALIPMLTLENGDVVPAPMEDLPIILPEDVVMNGVNSPIKADPEWAKTTYQGKPALRETDTFDTFMESSWYYARYTCPEYQQGMLNSEEANYWLPVDQYIGGIEHATMHLLYFRFFHKLLRDAGFVTSDEPANKLLCQGMVLADAFYYTSPTNERIWVSPTKVTLERDDKGRIVKATDDEGHELVHAGMTKMSKSKNNGIDPQEMVEKYGADTVRLFMMFASPAEMTLEWQESGVEGAKRFLARVWNLVFEYNKNPAKTPLNPTALSAAQKALRRDVHKTIAKVSDDIGRRQTFNTAIAAIMELMNKLTRAPLDDQQDRAMMAEALSAVVRMLYPITPHICFRLWQELGNQDIIDFAPWVEADAEAMIEDEKLIVVQVNGKVRGKVTVAADADKDTVKAVAFADENVKRFTDGMQIVKVIYVAGKLLNVVVKPQ","753690","","leucyl-tRNA synthetase, leucyl-tRNA ligase","Cytoplasm, Periplasm","","
InterPro
IPR001412
Family
Aminoacyl-tRNA synthetase, class I
PS00178\"[42-53]TAA_TRNA_LIGASE_I
InterPro
IPR002302
Family
Leucyl-tRNA synthetase bacterial/mitochondrial, class Ia
PR00985\"[127-144]T\"[153-169]T\"[185-198]T\"[215-234]T\"[485-503]T\"[524-546]T\"[557-567]TTRNASYNTHLEU
PTHR11946:SF7\"[5-205]T\"[234-567]T\"[617-859]TLEUCYL-TRNA SYNTHETASE
TIGR00396\"[5-860]TleuS_bact: leucyl-tRNA synthetase
InterPro
IPR013155
Domain
tRNA synthetase, valyl/leucyl, anticodon-binding
PF08264\"[698-828]TAnticodon_1
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620\"[31-628]Tno description
InterPro
IPR015413
Domain
tRNA synthetase class I (M)
PF09334\"[619-643]TtRNA-synt_1g
noIPR
unintegrated
unintegrated
G3DSA:1.10.730.10\"[637-795]Tno description
PTHR11946\"[5-205]T\"[234-567]T\"[617-859]TISOLEUCYL, LEUCYL, TYROSYL, VALYL AND METHIONYL-TRNA SYNTHETASES


","No hits to the COGs database.","Significant hit ( 7e-09) to 2/2 blocks of the IPB001412 family, which is described as \"Aminoacyl-transfer RNA synthetases class-I\". Interpro entry for IP:IPR001412. IPB001412A 42-52 8e-05 IPB001412B 616-626 0.033","Residues 619 to 698 match (4e-08) PD:PD487013 which is described as LIGASE BIOSYNTHESIS AMINOACYL-TRNA MITOCHONDRIAL MITOCHONDRION LEURS SYNTHETASE ATP-BINDING SYNTHETASE PEPTIDE ","","","","","","","","","","","","Fri Dec 20 11:53:36 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01090 is paralogously related to AA01724 (7e-19), AA02950 (3e-12) and AA00717 (1e-09).","","","","","","Residues 13 to 659 (E-value = 4.1e-281) place AA01090 in the tRNA-synt_1 family which is described as tRNA synthetases class I (I, L, M and V) (PF00133)","","","","","Tang Y, Tirrell DA. Attenuation of the editing activity of the Escherichia colileucyl-tRNA synthetase allows incorporation of novel amino acids into proteins in vivo. Biochemistry. 2002 Aug 27;41(34):10635-45. PMID: 12186549 Du X, Wang ED. Discrimination of tRNA(Leu) isoacceptors by the mutants ofEscherichia coli leucyl-tRNA synthetase in editing. Biochemistry. 2002 Aug 27;41(34):10623-8. PMID: 12186547Li T, Wang ED, Wang YL. The Overproduction of Leucyl-tRNA Synthetase in E. coli andIts Purification. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai).1997;29(6):591-596. PMID: 12215774 ","","Fri Dec 20 11:53:36 2002","1","","","" "AA01092","756421","756254","168","ATGAGGCTTGTCATCAGTTTAAGCCGTAAAAATATCCAAAATTCCCACCGCACTTTCTGTTATTTTTCCCCGTTTTACGCTATTCTATGCCGTATTTTCCAAGTTAAAACCCGCCGAAAAGTGCGGTCTATTTTTAAGGTGATTTTCTATGCAAGAGCAATATCGTCC","","","7942","MRLVISLSRKNIQNSHRTFCYFSPFYAILCRIFQVKTRRKVRSIFKVIFYARAISS","756256","","hypothetical protein","Cytoplasm, Extracellular","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Fri Dec 20 11:54:34 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01092 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01095","757021","756467","555","GTGAATCTAATTAACGCCAACGCCTGCGATCTTTTCAACATTCCCTTCTTCCAATTCGCCCAAATGAAAAAATTTTGTCCGGAAGAGATTCCGCGCATTAAGGCGGATTACAAAGCCCATTGGGACAACTGGAAAGCGACGATTTTGCAGGTTTCCGCGGCGCTTGGTTCGCACTTTGCCAAACCGCATATTGAAAGCTGGACGAACGGCTGGCAGGTGCGCGGGCATTTTTTCGCCTATTTTAAATATGAATATAACCTCAATTCCGCGGCGATTTTGTCGGTGTTGCTAAACAGATGTCGTTTATCGGTCAGTCTGGACTGGCATTGTTATTGCGCCGATCGTTCGCAAATTAATGTGCAGCAATATAATCAATGGCTGGAAAATTTTGATTTTGCCCGTTTTGCCGATTTCGATATTTGGCGTGGCGATGAAAGCGAATACGATGATGTTCGCCAAGTGAATCAATTCACGCAGCAGGATTTCACCTTGCGTTCCGACAAGGATTTTTGGTGTATCGGACGCAATGCGGAGCCGAGCTGGATAAATTGGACG","","","22403","VNLINANACDLFNIPFFQFAQMKKFCPEEIPRIKADYKAHWDNWKATILQVSAALGSHFAKPHIESWTNGWQVRGHFFAYFKYEYNLNSAAILSVLLNRCRLSVSLDWHCYCADRSQINVQQYNQWLENFDFARFADFDIWRGDESEYDDVRQVNQFTQQDFTLRSDKDFWCIGRNAEPSWINWT","756469","","conserved hypothetical protein","Periplasm, Extracellular","","
noIPR
unintegrated
unintegrated
PD110134\"[4-183]TY552_HAEIN_P44013;


","No hits to the COGs database.","","Residues 4 to 183 match (5e-70) PD:PD110134 which is described as PROTEOME COMPLETE NMA1731 HI0552 ","","","","","","","","","","","","Fri Dec 20 11:56:20 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01095 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01096","757342","757052","291","ATGCTCACCATCACTGAACAAGAACTGCAAATCGTTAAAGCGATTTTACAACAACATGTCCCGAATCATTCGGTTTGGGCGTTCGGTTCGCGCGTGAAAGGATACGCCAAAACGTATTCCGATTTGGATTTGGCAATTATTGGCGAATCGCCACTTTCGATGAAAACCTTGGCAAATTTAACGGAGGCTTTCTCCGAATCGGATTTGCCGTGGAAAGTGGATATTGTGGATTGGGCAGTGACGAATGATGCCTTTAAACAGATTATTTTGCAGTGTTTTGAGGTTATTCAG","","","17722","MLTITEQELQIVKAILQQHVPNHSVWAFGSRVKGYAKTYSDLDLAIIGESPLSMKTLANLTEAFSESDLPWKVDIVDWAVTNDAFKQIILQCFEVIQ","757054","","conserved hypothetical protei","Cytoplasm","","
InterPro
IPR002934
Domain
DNA polymerase, beta-like region
PF01909\"[9-96]TNTP_transf_2
noIPR
unintegrated
unintegrated
G3DSA:3.30.460.10\"[2-96]Tno description


","BeTs to 6 clades of COG1708COG name: Predicted nucleotidyltransferasesFunctional Class: RThe phylogenetic pattern of COG1708 is a-m-kz-qv--------h--------Number of proteins in this genome belonging to this COG is","","Residues 11 to 76 match (4e-19) PD:PD004242 which is described as PROTEOME COMPLETE PAREP11 NUCLEOTIDYLTRANSFERASE TRANSFERASE DR0248 SLR1241 AF2304 STS014 TM0614 ","","","","","","","","","","","","Fri Dec 20 11:57:36 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01096 is paralogously related to AA00187 (5e-05).","","","","","","Residues 5 to 96 (E-value = 6.7e-06) place AA01096 in the NTP_transf_2 family which is described as Nucleotidyltransferase domain (PF01909)","","","","","","","","1","","","" "AA01097","757745","757329","417","ATGACGGAACTGGACTTGACACCATTGACTAATGCGATTAACCGTTTAGCTGAAGGATTAGCGCGTTATCAATCGGATATTACAGATATACAAATTCGCGACGGTTTGATTCAACGTTTTGAATTTACCTATGAAATCAGTCATAAAATGCTTAAGCGCTTTCTGGAATACACCGAAGCGAATCCCGAGCAAATTGACGCTATGACGTTTCAAGATCTGATTCGTACGAGTAATGAAAGAGGTTTATTGCTGGGAAATTGGCAAAACTGGAAGCAATATCGTGAAATGCGTAGCCGTACCAGTCATACTTATGATGAAGAAACGGCAATTCTCGTGGTATCCGGCATTCCGGATTTTTTGTGGGAAGCACGATTTTTACAGCAATCTTTACAAGAACGCTTACATGCTCACCATCAC","","","16683","MTELDLTPLTNAINRLAEGLARYQSDITDIQIRDGLIQRFEFTYEISHKMLKRFLEYTEANPEQIDAMTFQDLIRTSNERGLLLGNWQNWKQYREMRSRTSHTYDEETAILVVSGIPDFLWEARFLQQSLQERLHAHHH","757331","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR010235
Family
Nucleotidyltransferase substrate binding protein, HI0074
PF08780\"[11-131]TNTase_sub_bind
TIGR01987\"[5-132]THI0074: nucleotidyltransferase substrate bi
noIPR
unintegrated
unintegrated
G3DSA:1.20.120.330\"[4-137]Tno description


","No hits to the COGs database.","","Residues 24 to 126 match (9e-16) PD:PD088951 which is described as PROTEOME COMPLETE RC0161 HI0074 ","","","","","","","","","","","","Fri Dec 20 11:59:38 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01097 is paralogously related to AA00188 (2e-08).","","","","","","","","","","","","","","1","","","" "AA01098","758663","757839","825","ATGGCGACATATTTAATCGGCGACCTGCACGGTTGCTATGATGAATTTCAAATGCTGTTGGAAAGGGTACGCTTTGATCCCGCGCAGGATACGCTGTATTTAACGGGCGATTTGCTAGCGCGCGGGGATAACTCTTTGGCGTGCCTGCGTCTGGTGAAATCCTTGGGAAATGCGGCGCGTACCGTGTTAGGCAACCACGATTTACATTTTATTTCCACCGCACTTGGGGTGAAAAAAATTAAACCGCGCGATCGCGTAGATGCCATTTTTGCTGCCGAAGATTTCTTTGAACTGGTGAACTGGCTGCGTTGCCAGCCTTTGTTGATTCACAACCCCGCGCAGAATTTCGTGCTTGTGCATGCAGGGATTTCGCCCGATTGGGATTTGACCGCCGCCAAAGTCTGCGCCAATGAAGTGGAAAATGTGTTACGCCACGGCAATTATCGCTATCTGGTGGAAAATATGTATGCCGAACAGCCCGATCGTTGGTCGCCGCATTTACAGGGGCTGGACCGCCTGCGTTACAGCATCAACGTGCTCACCCGTATGCGTTTTTGCTATCTCGATCATCGGTTGGATTTCGCCTGCAAGCTGTCAATTAAGGACGCGCCGAAAGCACTTGCACCTTGGTTTGCCTTGGATAATCCGCTGTATCAAACGGGAAATATTGTTTTTGGTCATTGGGCAAGTTTAGTGGATGAAACCACTCCGCCGAACATTTACGCCCTCGATACCGGCTGCGTCTGGGGCAACCGCTTAACCATGCTACGTTGGGAAGACAAGCAATATTTCACTCAAAGTGCGGTGAAAAAAAGCAATGCTTTT","","","31466","MATYLIGDLHGCYDEFQMLLERVRFDPAQDTLYLTGDLLARGDNSLACLRLVKSLGNAARTVLGNHDLHFISTALGVKKIKPRDRVDAIFAAEDFFELVNWLRCQPLLIHNPAQNFVLVHAGISPDWDLTAAKVCANEVENVLRHGNYRYLVENMYAEQPDRWSPHLQGLDRLRYSINVLTRMRFCYLDHRLDFACKLSIKDAPKALAPWFALDNPLYQTGNIVFGHWASLVDETTPPNIYALDTGCVWGNRLTMLRWEDKQYFTQSAVKKSNAF","757841","","bis(5'-nucleosyl)-tetraphosphatase","Cytoplasm","","
InterPro
IPR004617
Family
Bis(5'-nucleosyl)-tetraphosphatase (symmetrical)
PIRSF000903\"[1-275]TBis(5'-nucleosyl)-tetraphosphatase (symmetrical)
TIGR00668\"[1-275]TapaH: bis(5'-nucleosyl)-tetraphosphatase (s
InterPro
IPR004843
Domain
Metallophosphoesterase
PF00149\"[1-231]TMetallophos
noIPR
unintegrated
unintegrated
G3DSA:3.60.21.10\"[4-263]Tno description


","BeTs to 12 clades of COG0639COG name: Diadenosine tetraphosphatase and related serine/threonine protein phosphatasesFunctional Class: TThe phylogenetic pattern of COG0639 is aompkzy-vd-lbcefghsnuj----Number of proteins in this genome belonging to this COG is","","Residues 223 to 264 match (9e-09) PD:PD404763 which is described as COMPLETE PROTEOME PHOSPHATASE HYDROLASE SERINE/THREONINE IRON PLASMID DIADENOSINE MANGANESE P1P4-TETRAPHOSPHATE ","","","","","","","","","","","","Fri Dec 20 12:01:22 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01098 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 231 (E-value = 3.9e-15) place AA01098 in the Metallophos family which is described as Calcineurin-like phosphoesterase (PF00149)","","","","","Guranowski,A., Jakubowski,H. and Holler,E. Catabolism of diadenosine 5\",5\"\"-P1,P4-tetraphosphate inprocaryotes. Purification and properties of diadenosine5\",5\"\"-P1,P4-tetraphosphate (symmetrical) pyrophosphohydrolasefrom Escherichia coli K12. J. Biol. Chem. 258(24):14784-14789, 1983. PubMed: 6317672 Blanchin-Roland,S., Blanquet,S., Schmitter,J.M. and Fayat,G. The gene for Escherichia coli diadenosine tetraphosphatase islocated immediately clockwise to folA and forms an operon withksgA. Mol. Gen. Genet. 205(3):515-522, 1986. PubMed: 3031429 Azakami,H., Sugino,H. and Murooka,Y. Cloning and nucleotide sequence of a negative regulator genefor Klebsiella aerogenes arylsulfatase synthesis andidentification of the gene as folA. J. Bacteriol. 174(7):2344-2351, 1992. PubMed: 1551851 ","","Fri Dec 20 12:01:22 2002","1","","","" "AA01099","759542","758682","861","ATGAATTCAAAAAAGCATTTAGGCCATACGGCGCGTAAGCGGTTCGGGCAGAATTTCCTGCATGACAACAACGTTATTCAGAATATCGTGGCGGCAATTTATCCGCAGCCGAATCAGTTTTTAGTGGAAATCGGCCCCGGTTTGGGCGCCTTGACGGAGCCTGTGGCAGAACAGGTGGAACATCTGACCGTGCTAGAGCTTGACCGTGATTTGGCAGAACGTTTGCGTCATCACCCGTTTTTACATCAAAAACTTACGGTTATCGAAACCGACGCCATGCAGTTCGATTTTTCCTCTCTCTATGAACAAGAACGGCTGGCGGAGAAGGGACAAAAACTGCGCGTGTTCGGTAACCTGCCTTACAACATTTCCACGCCGTTAATGTTCCATTTGTTTCACTATCACCACATTATTCAGGATATGCATTTCATGTTGCAGAAAGAAGTGGTGAAACGCCTGTGTGCCGCGCCGAATAGCAAGGCTTACGGGCGACTGACTATTATGGCGCAATATTTCTGTCAGGTTATGCCAGTGCTGGAAGTGCCGCCGAGCGCGTTTAAACCGGCGCCGAAAGTGGATTCGGCAGTGGTGCGTTTGATTCCGCACGCCACATTGCCGCACCCGGTGAAAGACTTATATTGGCTCAATCGTGTGTGTTCACAAGCGTTCAATCAGCGCCGTAAAACCTTACGCAATGCTTTTTCGGGGTTATTTTCAGCGGGAAATCTGACCGCACTTGGGATCAATTTGAATGCCCGCGCAGAAAATCTCAGCATCGCCGATTATGCGCGGTTGGCGAACTGGTTGGCGGACAATCCGCCGGCGGATGTGAATAAAGATGATGTGACGGATTCGGACGAG","","","32595","MNSKKHLGHTARKRFGQNFLHDNNVIQNIVAAIYPQPNQFLVEIGPGLGALTEPVAEQVEHLTVLELDRDLAERLRHHPFLHQKLTVIETDAMQFDFSSLYEQERLAEKGQKLRVFGNLPYNISTPLMFHLFHYHHIIQDMHFMLQKEVVKRLCAAPNSKAYGRLTIMAQYFCQVMPVLEVPPSAFKPAPKVDSAVVRLIPHATLPHPVKDLYWLNRVCSQAFNQRRKTLRNAFSGLFSAGNLTALGINLNARAENLSIADYARLANWLADNPPADVNKDDVTDSDE","758684","","dimethyladenosine transferase","Cytoplasm","","
InterPro
IPR001737
Family
Ribosomal RNA adenine methylase transferase
PTHR11727\"[2-270]TDIMETHYLADENOSINE TRANSFERASE
PF00398\"[8-271]TRrnaAD
SM00650\"[25-203]TrADc
PS01131\"[41-68]TRRNA_A_DIMETH
InterPro
IPR011530
Family
RRNA 16S rRNA dimethylase
TIGR00755\"[9-269]TksgA: dimethyladenosine transferase
noIPR
unintegrated
unintegrated
G3DSA:1.10.8.100\"[206-273]Tno description
G3DSA:3.40.50.150\"[17-205]Tno description
PIRSF000392\"[1-284]TDimethyladenosine transferase (rRNA adenosine dimethyltransferase)


","BeTs to 26 clades of COG0030COG name: Dimethyladenosine transferase (rRNA methylation)Functional Class: JThe phylogenetic pattern of COG0030 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.4e-41) to 3/3 blocks of the IPB001737 family, which is described as \"Ribosomal RNA adenine dimethylase\". Interpro entry for IP:IPR001737. IPB001737A 26-71 2.7e-17 IPB001737B 115-128 9.7e-08 IPB001737C 181-202 2e-13","Residues 118 to 173 match (3e-08) PD:PD595334 which is described as TRANSFERASE DIMETHYLADENOSINE COMPLETE PROTEOME RRNA DIMETHYLTRANSFERASE S-ADENOSYLMETHIONINE-6-N' N'-ADENOSYLRRNA METHYLTRANSFERASE 2.1.1.- ","","","","","","","","","","","","Fri Dec 20 12:03:37 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01099 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 271 (E-value = 2.6e-110) place AA01099 in the RrnaAD family which is described as Ribosomal RNA adenine dimethylase (PF00398)","","","","","van Buul,C.P. and van Knippenberg,P.H. Nucleotide sequence of the ksgA gene of Escherichia coli: comparison of methyltransferases effecting dimethylation of adenosine in ribosomal RNA Gene 38 (1-3), 65-72 (1985) PubMed: 3905517 Blanchin-Roland,S., Blanquet,S., Schmitter,J.M. and Fayat,G. The gene for Escherichia coli diadenosine tetraphosphatase is located immediately clockwise to folA and forms an operon withksgA Mol. Gen. Genet. 205 (3), 515-522 (1986) PubMed: 3031429 Roa,B.B., Connolly,D.M. and Winkler,M.E. Overlap between pdxA and ksgA in the complexpdxA-ksgA-apaG-apaH operon of Escherichia coli K-12 J. Bacteriol. 171 (9), 4767-4777 (1989) PubMed: 2670894 van Gemen,B., Koets,H.J., Plooy,C.A., Bodlaender,J. and Van Knippenberg,P.H. Characterization of the ksgA gene of Escherichia colidetermining kasugamycin sensitivity Biochimie 69 (8), 841-848 (1987) PubMed: 3122846 ","","Fri Dec 20 12:03:37 2002","1","","","" "AA01101","760552","759623","930","ATGAAGATGAATTTAAAATCTGTTTTGTTTGCCGCAATCGGCTTTTTTGTGTTAGCTGCCCATGTTCACGCCGAGGAAAAAGTGGTCGCTACCGTTAATGGCATTCCCATATTGGAAAGTCAGGTGCAGAGTGCGATCAATAAGAAAACCAATGATCGTCAGGCGGCACTAAATAAAGTCATCGATGATATTCTGGTGGACCAGGCGGTGAAAGAATCCGACGTGAAAGTAAATAACGCGCAAATCGATCAAATTATTGAAGGCATTGCAGCGCAAAACGGCTTAACTTTCGGTCAATTATTGGATGCATTGGATTATCAGGGCATTAGCTATCGCGCCTATCGTCAGCAAATCGCACAGCAGGTGATGATGTCCGAAGTGCGTAACCACGCTATCAGCCAAAGTGTGGATGTGTCCCGCGAACAGGTTGAAGCGCTTGCCAAGAAAATGTTGGATGAAGCGAAAGCCAAGGGCAGCGTAGCTCAGATCTCCGACACGCAATATGAAGTACGTCATATCTTACTGAAACTGAACCCGTTATTAAATGATGCACAAGCCAAGGCGCAACTTGAACAAATCCGCGCGGACATCATTGCCGGTAAAACCACCTTTGCCGATGCCGCGTTGAAATATTCCAAAGATTATTTGTCCGGCGCCAACGGCGGTAGCTTGGGTTATGCCTTTCCGGAAATGTACGTCGGTCCGTTTAACCAAGCGGTACGCACCACCAAACCGGGCGTCATCAGCGCGCCGTTTAAAACCGAATTCGGCTGGCACATTCTGGAAGTGACCAACACCCGTCAAGCAGATCGTACGGAAGATGCCTACCGCCAAAAAGCCTACGAGCAAATCGTCAATCAGCAATTGCAGGATTCCGCACGCGACTGGGTACAGGCACTGCGTAAACGAGTGGATATTAAATACATAAAT","","","34470","MKMNLKSVLFAAIGFFVLAAHVHAEEKVVATVNGIPILESQVQSAINKKTNDRQAALNKVIDDILVDQAVKESDVKVNNAQIDQIIEGIAAQNGLTFGQLLDALDYQGISYRAYRQQIAQQVMMSEVRNHAISQSVDVSREQVEALAKKMLDEAKAKGSVAQISDTQYEVRHILLKLNPLLNDAQAKAQLEQIRADIIAGKTTFADAALKYSKDYLSGANGGSLGYAFPEMYVGPFNQAVRTTKPGVISAPFKTEFGWHILEVTNTRQADRTEDAYRQKAYEQIVNQQLQDSARDWVQALRKRVDIKYIN","759625","","stationary phase survival protein SurA","Periplasm, Cytoplasm","","
InterPro
IPR000297
Domain
Peptidyl-prolyl cis-trans isomerase, PpiC-type
PF00639\"[172-265]TRotamase
PS50198\"[165-265]TPPIC_PPIASE_2
PS01096\"[204-225]?PPIC_PPIASE_1
InterPro
IPR006162
PTM
Phosphopantetheine attachment site
PS00012\"[2-17]?PHOSPHOPANTETHEINE
InterPro
IPR015391
Domain
SurA N-terminal domain
PF09312\"[27-147]TSurA_N
noIPR
unintegrated
unintegrated
G3DSA:3.10.50.40\"[161-267]Tno description
PTHR10657\"[119-309]TROTAMASE
signalp\"[1-24]?signal-peptide


","BeTs to 14 clades of COG0760COG name: Parvulin-like peptidyl-prolyl isomeraseFunctional Class: OThe phylogenetic pattern of COG0760 is ------yqvd-lbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","","Residues 267 to 308 match (3e-07) PD:PD064420 which is described as COMPLETE SURA PROTEOME SURVIVAL ISOMERASE PERIPLASMIC HOMOLOG ROTAMASE SIGNAL PRECURSOR ","","","","","","","","","","","","Fri Dec 20 12:05:37 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01101 is paralogously related to AA00114 (0.001).","","","","","","Residues 172 to 265 (E-value = 8.2e-39) place AA01101 in the Rotamase family which is described as PPIC-type PPIASE domain (PF00639)","","","","","Tormo,A., Almiron,M. and Kolter,R. surA, an Escherichia coli gene essential for survival instationary phase J. Bacteriol. 172 (8), 4339-4347 (1990) PubMed: 2165476 Lazar,S.W. and Kolter,R. SurA assists the folding of Escherichia coli outer membrane proteins J. Bacteriol. 178 (6), 1770-1773 (1996) PubMed: 8626309 Missiakas,D., Betton,J.M. and Raina,S. New components of protein folding in extracytoplasmiccompartments of Escherichia coli SurA, FkpA and Skp/OmpH Mol. Microbiol. 21 (4), 871-884 (1996) PubMed: 8878048 ","","Fri Dec 20 12:05:37 2002","1","","","" "AA01102","761153","760620","534","ATGGAAAAAATCATTATTGACGAAAATCAGTTCCTTCGAACCATTTCCCGTATTTCTCATGAAATCATTGAAAAACACCAACGTTTAGATAATCTGGTTATTGTCGGGATTAAACGGCGGGGAGCGGAAATTGCGGAACTGATTAAGAATAAAATTAAATTGTTAACGCAAACCGACATTCCCGCTTTTGATTTGGATATTACCTTTTATCGCGATGATCTTGAACACGTACAGGAAGATCAAGTGCCGGTTTACAGTGGCGCGTCGGATTTTATTAATATTCAACACAAAGAAGTGATTTTAGTGGATGATGTACTGTTTACCGGTCGCACGATTCGCGCGGCATTGGATGCCTTGGTGGATTTCGGGCGGGCGGCGAAAGTGGAATTGGTGATCTTTGTGGACCGCGGACATCGTGAATTGCCGATTCGCGCCGACTATGTGGGAAAAAACGTGCCGACTAGTCGAAGCGAAAATATTCAGGTGCGCACCATGAAGTTTGACCAATGCTATGAAGTAGCGCTGCTGTCCAAA","","","20471","MEKIIIDENQFLRTISRISHEIIEKHQRLDNLVIVGIKRRGAEIAELIKNKIKLLTQTDIPAFDLDITFYRDDLEHVQEDQVPVYSGASDFINIQHKEVILVDDVLFTGRTIRAALDALVDFGRAAKVELVIFVDRGHRELPIRADYVGKNVPTSRSENIQVRTMKFDQCYEVALLSK","760622","","pyrimidine operon regulatory protein","Cytoplasm","","
InterPro
IPR000836
Domain
Phosphoribosyltransferase
PF00156\"[2-153]TPribosyltran
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2020\"[3-175]Tno description
PTHR22573\"[87-153]TPHOSPHOHEXOMUTASE FAMILY MEMBER
PTHR22573:SF8\"[87-153]THYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE


","No hits to the COGs database.","","Residues 25 to 162 match (8e-53) PD:PD405441 which is described as TRANSFERASE COMPLETE PROTEOME PYRIMIDINE REGULATORY PYRR OPERON GLYCOSYLTRANSFERASE PHOSPHORIBOSYLTRANSFERASE URACIL ","","","","","","","","","","","","Fri Dec 20 12:07:00 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01102 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 153 (E-value = 1.3e-13) place AA01102 in the Pribosyltran family which is described as Phosphoribosyl transferase domain (PF00156)","","","","","Elagoz,A., Abdi,A., Hubert,J.C. and Kammerer,B. Structure and organisation of the pyrimidine biosynthesispathway genes in Lactobacillus plantarum: a PCR strategy forsequencing without cloning Gene 182 (1-2), 37-43 (1996) PubMed: 8982065 Savacool HK, Switzer RL. Characterization of the interaction of Bacillus subtilisPyrR with pyr mRNA by site-directed mutagenesis of theprotein. J Bacteriol. 2002 May;184(9):2521-8. PMID: 11948166 ","","Fri Dec 20 12:07:00 2002","1","","","" "AA01104","761702","761295","408","ATGCAAGCTATTTTAAAAACGCTGTTAATTTTAACCGCACTTTTGCCCTTCTGTGTGAGCGCAAAAATCAGCGTAGAAAACGCCACTGTCTTCGCCACCCAAAGCCCTGATGAACCTTCGGCAATTTTCATGAATTTACACAATGACGGCAAGGAACCCGTTAATCTTGCTTTTGCACAAAGCCCCTGGGCGGCGCGCCTTGAATTGCACGGTACGCAACATGGCAAAATGCTCACCTTGTCCGGCATTGAAATCCCCGCCAACGGCAATGTTCAGTTAAAACGCGGCGGCTTGCATATTATGGTGTTTGAAGCCGCGAAAACGTTACAGGCGGGAGAAAAGTTTCCATTGGAACTGATGTTTGATAACGGCGAGCGGGTTGTGGTTGAGGCGAATGTGGTGGGACAC","","","15446","MQAILKTLLILTALLPFCVSAKISVENATVFATQSPDEPSAIFMNLHNDGKEPVNLAFAQSPWAARLELHGTQHGKMLTLSGIEIPANGNVQLKRGGLHIMVFEAAKTLQAGEKFPLELMFDNGERVVVEANVVGH","761297","","conserved hypothetical protein","Cytoplasm, Periplasm","","
InterPro
IPR007410
Family
Protein of unknown function DUF461
PF04314\"[25-136]TDUF461
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide


","BeTs to 8 clades of COG2847COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG2847 is -------q-d-----fgh-nujx---Number of proteins in this genome belonging to this COG is","","Residues 16 to 131 match (8e-27) PD:PD090927 which is described as PROTEOME COMPLETE NMA1745 NMB1557 PA3785 RP573 AQ_1253 DR1885 ATU1468 PERIPLASMIC ","","","","","","","","","","","","Fri Dec 20 12:08:21 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01104 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 25 to 136 (E-value = 5.9e-42) place AA01104 in the DUF461 family which is described as Protein of unknown function (DUF461) (PF04314)","","","","","","","","1","","","" "AA01106","761815","762423","609","ATGGCAAATTATTACGACATTACCCTCGCCCTTGCCGGCGTATGCCAGGCGGCAAAATTAGCTCAACAACTGGCGTTAAACGGCGAAGCCGATCAACAGGCGCTGGAAATTTCCCTGAACAGCTTATTGCAAACCGCACCGCAAACCACGTTAGATGTATTCGGTGGCGCTGAGAACCATCTGAAACCGGGCTTAACCACCCTGTGTGAGCAACTCAACGGCAGCGAACCGGAACTTGGGCGTTATTGGTTGAGTTTGTTGGCATTGGCAGGAAAATTGAATAAAACCCCGGAGGCCAAGCAGGAACTGGCGCGTCGCGTGCAATATTTACCGACACAACTGGAACACTATCATTTGCTGGATGAACAAATGTTATCCAACTTCGCCGGCATTTATGTGGATGTGATCAGCCCGCTGGGTCGTCGTATTCAAGTCACCGGCGTCACTCAATATTTGCAACAAGTGGGCACGCAAAATCGCATTCGTGCCGCCTTGTTAGCCGGTATTCGCGCGGCGATTTTATGGCAACAGGTGGGCGGCACCAAATGGCAGTTGTTGTTCTTTCGAGGCAAAATCGCCGCCACCGCACAACAAATTCTCTCTTCTCTT","","","22270","MANYYDITLALAGVCQAAKLAQQLALNGEADQQALEISLNSLLQTAPQTTLDVFGGAENHLKPGLTTLCEQLNGSEPELGRYWLSLLALAGKLNKTPEAKQELARRVQYLPTQLEHYHLLDEQMLSNFAGIYVDVISPLGRRIQVTGVTQYLQQVGTQNRIRAALLAGIRAAILWQQVGGTKWQLLFFRGKIAATAQQILSSL","762425","","conserved hypothetical protein","Periplasm, Inner membrane, Cytoplasm","","
InterPro
IPR007451
Family
Protein of unknown function DUF489
PF04356\"[1-201]TDUF489
noIPR
unintegrated
unintegrated
PD037115\"[1-203]TYI50_PASMU_Q9CJY8;
signalp\"[1-17]?signal-peptide


","No hits to the COGs database.","","Residues 1 to 203 match (1e-59) PD:PD037115 which is described as COMPLETE PROTEOME FUNCTION YCFC VC1127 HI0638 PA2627 MEMBRANE XF1439 STY1273 ","","","","","","","","","","","","Fri Dec 20 12:09:25 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01106 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 201 (E-value = 3.1e-111) place AA01106 in the DUF489 family which is described as Protein of unknown function (DUF489) (PF04356)","","","","","","","","1","","","" "AA01107","762450","763814","1365","ATGCAACTCAGCGCATTAACCGCACTCTCCCCCATTGACGGACGTTATCAGGATAAAACCGCCGAATTACGCAGCATTTTCAGTGAATTCGGTTTATTAAAATTCCGTGTAACGGTAGAAGTTCGTTGGCTGCAAAAACTGGCGGCGACCGCACAAATCACGGAAGTGCCTTCTTTGTCGCAGGAAGCAAACGATTACCTTGACGGTATTGTAGAAAATTTCAGCATAATTGATGCACAACGCATTAAAGACATCGAAAAAACCACCAATCACGACGTAAAAGCGGTGGAATATTTCCTCAAAGAAAAAAGCGCAGCGTTGCCGGAATTGGCGGCAATCAGTGAATTTATCCATTTTGCCTGCACATCCGAAGACATTAATAACCTGTCCCACGCCCTGATGTTAAGCACCGCGCGGGATAATGTGCTGTTACCGGCATGGTTAAATTTAATCGGAAAAATCACCGCACTTGCCGAGCAATATAAACGCATTCCACTGCTTTCCCGCACGCACGGACAACCTGCCTCACCGACCACTGTGGGCAAAGAAATGGCAAATGTGGTATATCGTTTAAGACGCCAATATAAACAATTACAAACGCTTGAAATTTTGGGCAAAATTAACGGCGCGGTAGGCAACTATAACGCCCATTTATCCGCCTATCCAAACATTGACTGGCATAAATTAAGCGAAGAATTCGTTACCTCTTTGGGGGTGACCTGGAACCCGTACACCACCCAAATCGAACCCCATGATTACATTGCCGAGCTGTTTGATTGCGTGGCACGCTTCAACACCATCATTATTGATTTCGACCGCGACCTGTGGGGCTACATCGCCTTAAATCACTTTAAACAACGCACCCTCGCGGGCGAAATCGGTTCCTCCACCATGCCGCACAAAGTCAACCCGATTGACTTTGAAAACTCCGAAGGCAACCTTGGCTTGGCAAATGCCGTGATGGCGCACTTAGGCAGCAAACTGCCGATTTCCCGCTGGCAGCGCGATCTTACAGATTCCACCGTGTTACGTAACCTCGGCGTGGGCTTGGGCTATTGCTTAATCGCCTATGCGGCGACACAGAAAGGCATCAGCAAACTGGAAGTGAATGAAGCCCATTTACGCGAAGAATTGGATCAAAACTGGGAAGTGCTTGCCGAACCGATTCAAACCGTGATGCGTCGTTATAGCATTGAAAAACCATACGAAAAACTGAAAGAATTGACTCGTGGCAAACGCGTGGATGCCCAAGCCATGTTTGATTTCATTGAGAAATTAGCCATCCCGGCGGAAGAAAAAGCCCGCCTGCAACAACTCACCCCTGCCGGCTACATCGGTGCCGCTGTGGAGCTGGTGGAAAAACTT","","","51830","MQLSALTALSPIDGRYQDKTAELRSIFSEFGLLKFRVTVEVRWLQKLAATAQITEVPSLSQEANDYLDGIVENFSIIDAQRIKDIEKTTNHDVKAVEYFLKEKSAALPELAAISEFIHFACTSEDINNLSHALMLSTARDNVLLPAWLNLIGKITALAEQYKRIPLLSRTHGQPASPTTVGKEMANVVYRLRRQYKQLQTLEILGKINGAVGNYNAHLSAYPNIDWHKLSEEFVTSLGVTWNPYTTQIEPHDYIAELFDCVARFNTIIIDFDRDLWGYIALNHFKQRTLAGEIGSSTMPHKVNPIDFENSEGNLGLANAVMAHLGSKLPISRWQRDLTDSTVLRNLGVGLGYCLIAYAATQKGISKLEVNEAHLREELDQNWEVLAEPIQTVMRRYSIEKPYEKLKELTRGKRVDAQAMFDFIEKLAIPAEEKARLQQLTPAGYIGAAVELVEKL","763816","","adenylosuccinate lyase","Cytoplasm","","
InterPro
IPR000362
Domain
Fumarate lyase
PR00149\"[163-179]T\"[294-310]TFUMRATELYASE
PF00206\"[14-321]TLyase_1
PS00163\"[294-303]TFUMARATE_LYASES
InterPro
IPR004769
Family
Adenylosuccinate lyase
TIGR00928\"[12-455]TpurB: adenylosuccinate lyase
InterPro
IPR013539
Domain
Adenylosuccinate lyase C-terminal
PF08328\"[331-445]TASL_C
noIPR
unintegrated
unintegrated
G3DSA:1.20.200.10\"[120-439]Tno description
PTHR11444\"[1-455]TASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE
PTHR11444:SF2\"[1-455]TADENYLOSUCCINATE LYASE


","No hits to the COGs database.","Significant hit ( 3e-14) to 2/2 blocks of the IPB000362 family, which is described as \"Fumarate lyase\". Interpro entry for IP:IPR000362. IPB000362A 168-181 1.3e-05 IPB000362B 294-304 6.4e-07","Residues 370 to 451 match (5e-10) PD:PD392745 which is described as LYASE PROTEOME ADENYLOSUCCINATE COMPLETE ","","","","","","","","","","","","Fri Dec 20 12:10:32 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01107 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 14 to 321 (E-value = 5.6e-86) place AA01107 in the Lyase_1 family which is described as Lyase (PF00206)","","","","","He B, Smith JM, Zalkin H. Escherichia coli purB gene: cloning, nucleotide sequence,and regulation by purR. J Bacteriol. 1992 Jan;174(1):130-6. PMID: 1729205 Helling RB, Janes BK, Kimball H, Tran T, Bundesmann M, CheckP, Phelan D, Miller C. Toxic waste disposal in Escherichia coli. J Bacteriol. 2002 Jul;184(13):3699-703. PMID: 12057966 Green SM, Malik T, Giles IG, Drabble WT. The purB gene of Escherichia coli K-12 is located in anoperon. Microbiology. 1996 Nov;142 ( Pt 11):3219-30. PMID: 8969519","","Fri Dec 20 12:10:32 2002","1","","","" "AA01108","763786","764043","258","GTGCCGCTGTGGAGCTGGTGGAAAAACTTTAAACAACAAAAAGGACGTATTCAATGCGCTCTTAAAAACACCGCAGAAAATAACCGCACTTTATGGCATGAAGAACGGATAATAGATGGTTTTAGAAGAAAAGTACGTGAAATTAAAATGAGTGCGGTTGTTTTTTCCGGCGTTTTTGCAATGATTTATCCATGTGATATGAGGTTATTTAATCCAAGCCACTTTGTGGCTTTTACAAGAGAGGAGAAACAATATGAA","","","10423","VPLWSWWKNFKQQKGRIQCALKNTAENNRTLWHEERIIDGFRRKVREIKMSAVVFSGVFAMIYPCDMRLFNPSHFVAFTREEKQYE","764045","","hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
tmhmm\"[50-70]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Fri Dec 20 12:15:15 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01108 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01109","764039","764785","747","ATGAATAATATCAAAGGTAAAGTCGTGATTATCACCGGCGCCTCTTCAGGCATTGGTGAAGCCACCGCATACAAATTAGCTGAAAACGGCGCGAAATTGGTGTTAGGCGCGCGTCGTGAAGCGAAGTTGCAAGCCATTGTGGACAACATCAAGACAAAAGGCAGCGAAGCGATTTATCGTGTCACCGACGTGGTGAAAGCGGAAGATAACGCCGCACTGGTTGAACTCGCAAAAGCAACCTTCGGCAAAGTGGACGCGATTTTCTTGAACGCGGGCTTAATGCCGAACTCACCGCTTTCTGCACTGGAAACCAACAATTGGAATGCCATGGTGGACGTAAACATCAAAGGCGTGTTAAACGGCATCGCGGCGGTATTACCAACCTTTGAAGCACAAAAATCAGGGCATATCTTGGCGGTGTCTTCCGTGGCCGGCTTGAAAGTGTACCCGGGCGCCACGGTTTACTGCGGCACCAAATGGGCGGTGAAAGCGATTATGGAAGGTTTGCGTATGGAATCGGCGCAAGCAGGCACCAACGTTCGCACGGCAACTATTTATCCTGCGGCAGTGCAATCCGAATTGGTGGATCACATCACCAACGAAGATACTTCAAAGGGTTACCGAGAGCTTTACGACACCTTTGAAATTCCTGCCGAACGCGTGGCAAATGTAGTGGCATTTGCACTTTCACAACCGGCAGATACCAATATTAGTGAATTTACCTTAGGGCCGACCACGCAGCCTTGG","","","27694","MNNIKGKVVIITGASSGIGEATAYKLAENGAKLVLGARREAKLQAIVDNIKTKGSEAIYRVTDVVKAEDNAALVELAKATFGKVDAIFLNAGLMPNSPLSALETNNWNAMVDVNIKGVLNGIAAVLPTFEAQKSGHILAVSSVAGLKVYPGATVYCGTKWAVKAIMEGLRMESAQAGTNVRTATIYPAAVQSELVDHITNEDTSKGYRELYDTFEIPAERVANVVAFALSQPADTNISEFTLGPTTQPW","764787","","oxidoreductase (possible short-chain alcohol dehydrogenase)","Cytoplasm","","
InterPro
IPR002198
Family
Short-chain dehydrogenase/reductase SDR
PTHR19410\"[1-246]TSHORT-CHAIN DEHYDROGENASES/REDUCTASE FAMILY MEMBER
PF00106\"[7-174]Tadh_short
PS00061\"[142-170]?ADH_SHORT
InterPro
IPR002347
Family
Glucose/ribitol dehydrogenase
PR00081\"[8-25]T\"[82-93]T\"[129-145]T\"[155-174]T\"[178-195]TGDHRDH
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[5-232]Tno description
PTHR19410:SF42\"[1-246]TSHORT-CHAIN DEHYDROGENASE-RELATED


","BeTs to 16 clades of COG1028COG name: Dehydrogenases with different specificities (related to short-chain alcohol dehydrogenases)Functional Class: Q,RThe phylogenetic pattern of COG1028 is ao-pkzyqvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.8e-11) to 1/1 blocks of the IPB002198 family, which is described as \"Short-chain dehydrogenase/reductase (SDR) superfamily\". Interpro entry for IP:IPR002198. IPB002198 135-170 1.7e-11","Residues 7 to 50 match (3e-07) PD:PD428945 which is described as OXIDOREDUCTASE PROTEOME COMPLETE DEHYDROGENASE SHORT-CHAIN REDUCTASE 1.-.-.- DEHYDROGENASE/REDUCTASE PROBABLE NADP ","","","","","Tue Feb 18 10:49:03 2003","","","","","","","Fri Dec 20 13:05:24 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01109 is paralogously related to AA02205 (2e-19), AA00269 (4e-19), AA01179 (4e-15) and AA00912 (4e-12).","","","","","","Residues 9 to 246 (E-value = 1.3e-56) place AA01109 in the adh_short family which is described as short chain dehydrogenase (PF00106)","","","","","","","","1","","","" "AA01111","765033","764905","129","GTGAAGCAACAAATTTCAGAATTGAAACGTTATTTGAGCTTATTGGAATATAAAGTTGCCTTTTACCAACAAGCAAAAGCCTTAGGTTCTGTACAGGCTGTGGCAGAAATGATGCCGGAGATTCCAAAA","","","4910","VKQQISELKRYLSLLEYKVAFYQQAKALGSVQAVAEMMPEIPK","764905","","conserved hypothetical protein","Cytoplasm, Periplasm","This sequence is similar to gi|15677169, a predicted transcriptional regulator from Enterococcus faecium. See also gi|42630488 from H.influenzae.","No hits reported.","No hits to the COGs database.","","Residues 1 to 43 match (7e-08) PD:PD585737 which is described as TRANSCRIPTIONAL PROTEOME COMPLETE REGULATOR TRANSCRIPTION MERR REGULATION DNA-BINDING FAMILY PLASMID ","","","","","","","","","","","","Wed Feb 25 10:36:54 2004","Wed Feb 25 10:36:54 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01111 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 10:36:54 2004","","","","","","","","","","","","","1","","","" "AA01113","765309","765040","270","ATGAGCTACACCACCGCACAAGCCGCCCAAAAAATGGGCATTTCCGCCCATACATTACGCTTTTACGATAAAGAAGGCTTACTGCCGAATGTGGGGCGTGATGAACACGGCAATCGCCGCTTCACCGACAAAGATTTACAATGGCTTAGCCTGCTGCAATGTTTAAAAAACACAGGTATGAGTTTAAAAGACATTAAACGCTTTGCCAAATGCACAACTATCGGCGATAGCACTATTGAAGAACGCCTTGCCCTTTTTGAAAATCAAACC","","","10252","MSYTTAQAAQKMGISAHTLRFYDKEGLLPNVGRDEHGNRRFTDKDLQWLSLLQCLKNTGMSLKDIKRFAKCTTIGDSTIEERLALFENQT","765042","","transcriptional regulator (merR family)","Cytoplasm","","
InterPro
IPR000551
Domain
Bacterial regulatory protein, MerR
PR00040\"[4-15]T\"[15-28]T\"[39-59]THTHMERR
PF00376\"[4-41]TMerR
SM00422\"[3-72]THTH_MERR
PS50937\"[1-71]THTH_MERR_2
noIPR
unintegrated
unintegrated
G3DSA:1.10.1660.10\"[3-89]Tno description


","BeTs to 13 clades of COG0789COG name: Predicted transcriptional regulatorsFunctional Class: KThe phylogenetic pattern of COG0789 is a------q-drlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 3.5e-22) to 2/2 blocks of the IPB000551 family, which is described as \"Bacterial regulatory proteins, MerR family\". Interpro entry for IP:IPR000551. IPB000551A 5-26 1.1e-07 IPB000551B 28-69 5.4e-13","Residues 64 to 90 match (7e-07) PD:PD585737 which is described as TRANSCRIPTIONAL PROTEOME COMPLETE REGULATOR TRANSCRIPTION MERR REGULATION DNA-BINDING FAMILY PLASMID ","","","","","","","","","","","","Fri Dec 20 13:16:08 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01113 is paralogously related to AA01078 (5e-08) and AA00131 (1e-05).","","","","","","Residues 4 to 41 (E-value = 3.5e-14) place AA01113 in the MerR family which is described as MerR family regulatory protein (PF00376)","","","","","","","","1","","","" "AA01114","765447","766568","1122","ATGGAAATTAAAAGCATTAAATCTCGCGCTGCGGTGGCATTTGCGCCGAATCAACCGTTACAAATTGTTGAAATTGACGTAGAAATGCCGCGCAAAGGCGAAGTGTTAATTCGCAATACCCACACGGGCGTTTGCCATACCGACGCGTTCACCCTTTCAGGGCAAGATCCTGAAGGCGTATTCCCTGTGGTGCTCGGTCACGAAGGTGCGGGCGTGGTGGTGGCTGTGGGCGAAGGCGTAACCAGCGTGAAAGAAGGCGATCACGTGATTCCACTTTACACCGCAGAATGTGGCGAATGCGAATTTTGCCGTTCAGGAAAAACTAATTTATGCGTGGCGGTTCGCGATACCCAAGGCAGAGGCTTCATGCCTGATGGTACCACGCGTTTTTCTTACCAAGGTCAGCCAATTTATCACTACATGGGCTGCTCAACTTTCAGTGAATATTCGGTGGTGGCCGAAGTGTCTTTAGCAAAAATCAATCCTGAAGCCAACCACGAACACGTTTGTTTGCTCGGCTGTGGCGTGACCACGGGGATCGGTGCAGTACACAACACCGCAAAAGTGCAGGAAGGCGATTCTGTAGCGGTGTTTGGTTTGGGCGCGATTGGTTTGGCGGTGGTGCAAGGCGCCCGTCAAGCGAAAGCGGGTCGTATTATTGCCATTGATACTAATCCCGCTAAATTTGAATTGGCAAAACAATTCGGCGCGACCGATTGTTTAAACCCGAACGATTACGATAAACCGATTAAAGATGTGTTGTTAGACATCAACAAATGGGGCATCGACCATACCTTTGAATGTATCGGCAACGTAAACGTGATGCGCCAAGCGCTTGAAAGCGCACACCGCGGTTGGGGGCAATCGATCATTATTGGTGTGGCCGGTGCGGGACAGGAAATTTCAACCCGTCCATTCCAATTAGTGACTGGGCGTGTATGGAAAGGTTCGGCATTTGGTGGCGTGAAAGGTCGCACCCAATTGCCAAAAATGGTGGATGATTCGATGAAAGGCGAAATTGATTTGAAACCGTTCGTGACTCACACCATGACATTAGATCAAATCAACAAAGCCTTTGATTTGATGCACGAAGGTAAATCCATTCGTACCGTGATTCACTAT","","","42439","MEIKSIKSRAAVAFAPNQPLQIVEIDVEMPRKGEVLIRNTHTGVCHTDAFTLSGQDPEGVFPVVLGHEGAGVVVAVGEGVTSVKEGDHVIPLYTAECGECEFCRSGKTNLCVAVRDTQGRGFMPDGTTRFSYQGQPIYHYMGCSTFSEYSVVAEVSLAKINPEANHEHVCLLGCGVTTGIGAVHNTAKVQEGDSVAVFGLGAIGLAVVQGARQAKAGRIIAIDTNPAKFELAKQFGATDCLNPNDYDKPIKDVLLDINKWGIDHTFECIGNVNVMRQALESAHRGWGQSIIIGVAGAGQEISTRPFQLVTGRVWKGSAFGGVKGRTQLPKMVDDSMKGEIDLKPFVTHTMTLDQINKAFDLMHEGKSIRTVIHY","766570","","alcohol dehydrogenase, class III; glutathione-dependent formaldehyde dehydrogenase","Cytoplasm","","
InterPro
IPR002085
Family
Alcohol dehydrogenase superfamily, zinc-containing
PTHR11695\"[6-225]TALCOHOL DEHYDROGENASE RELATED
InterPro
IPR002328
Domain
Alcohol dehydrogenase, zinc-containing
PS00059\"[66-80]TADH_ZINC
InterPro
IPR013149
Domain
Alcohol dehydrogenase, zinc-binding
PF00107\"[191-333]TADH_zinc_N
InterPro
IPR013154
Domain
Alcohol dehydrogenase GroES-like
PF08240\"[32-160]TADH_N
InterPro
IPR014183
Family
Alcohol dehydrogenase class III/S-(hydroxymethyl)glutathione dehydrogenase
TIGR02818\"[7-374]Tadh_III_F_hyde: S-(hydroxymethyl)glutathion
noIPR
unintegrated
unintegrated
G3DSA:3.90.180.10\"[6-374]Tno description
PTHR11695:SF4\"[6-225]TALCOHOL DEHYDROGENASE


","BeTs to 8 clades of COG1062COG name: Zn-dependent alcohol dehydrogenases, class IIIFunctional Class: CThe phylogenetic pattern of COG1062 is ------y---r-bcef-h-n-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 4.8e-64) to 4/4 blocks of the IPB002328 family, which is described as \"Zinc-containing alcohol dehydrogenase\". Interpro entry for IP:IPR002328. IPB002328A 19-50 1.2e-12 IPB002328B 62-87 1.8e-17 IPB002328C 97-111 2.9e-10 IPB002328D 157-204 1.5e-19Significant hit ( 1.2e-13) to 1/1 blocks of the IPB002364 family, which is described as \"Quinone oxidoreductase/zeta-crystallin\". Interpro entry for IP:IPR002364. IPB002364 62-89 1.2e-13","Residues 329 to 371 match (1e-14) PD:PD000463 which is described as DEHYDROGENASE ALCOHOL OXIDOREDUCTASE ZINC NAD FAMILY MULTIGENE CLASS FORMALDEHYDE III ","","","","","Thu Feb 13 16:31:08 2003","","","","","","","Thu Feb 13 16:31:08 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01114 is paralogously related to AA02047 (1e-21) and AA00810 (4e-09).","","","","","","Residues 15 to 374 (E-value = 5e-141) place AA01114 in the ADH_zinc_N family which is described as Zinc-binding dehydrogenase (PF00107)","","","","","Hildebrandt P, Musidlowska A, Bornscheuer UT, Altenbuchner J.Cloning, functional expression and biochemical characterization of a stereoselective alcohol dehydrogenase from Pseudomonas fluorescens DSM50106.Appl Microbiol Biotechnol. 2002 Aug;59(4-5):483-7.PMID: 12172614 [PubMed - indexed for MEDLINE]Nordling E, Persson B, Jornvall H.Differential multiplicity of MDR alcohol dehydrogenases: enzyme genes in the human genome versus those in organisms initially studied.Cell Mol Life Sci. 2002 Jun;59(6):1070-5. Review.PMID: 12169018 Castronuevo P, Martin PF. Galamba A, Soetaert K, Buyssens P, Monnaie D, Jacobs P, Content J.Molecular and biochemical characterisation of Mycobacterium smegmatis alcohol dehydrogenase C.FEMS Microbiol Lett. 2001 Mar 1;196(1):51-6.PMID: 1125754","","Thu Feb 13 16:31:08 2003","1","","","" "AA01115","766685","767413","729","TTGCCACCTAATCCGGAAAATCGACCGCTTGGTGTGATTTATTGGCTTTCTGGCTTAACCTGCACCGAGCAAAATTTCATCACCAAATCAGGTTTTCAGCGTTATGCCGCAGAACATCAAGTGATTGTGGTCGCGCCAGATACCAGCCCGCGTGGTGAAGAAGTGCCGAACGATGCAGCGTATGATTTAGGGCAAGGTGCTGGGTTCTATTTGAACGCAACCGAATCGCCTTGGAATACGCACTATCATATGTATGATTACGTTTTAAACGAACTGCCAAGCCTGATTGAGCAACATTTCCCAACCAATGGCAAACGTGCCATTATGGGGCATTCCATGGGGGGACATGGGGCATTGGTGTTGGCATTACGCAACCCTGAGCATTATCAAAGCGTATCGGCGTTTTCCCCGATTCTTGCGCCGAGCCTCGTGCCTTGGGGAGAAAAAGCGTTTTCGGCATATTTAGGCGAAGATCGTAAAAAATGGCAGCAATATGATGCCAACTCGCTCATCAAACAAGGTTCTAAACTCAAAAAGATGCGGATTGATCAGGGGCTAGACGACGAGTTTTTAGCGACACAATTACGCACCGAAGAGTTTATCGAAACCTGCCGTAAAGCCAATCAACCTGTGGACGTACGTTTCCACAAAGGCTACGACCATAGCTATTATTTCATCGCCAGTTTTATTGGGGAACATATTGCATATCACGCGCAGTGTTTAGCTAAT","","","31573","LPPNPENRPLGVIYWLSGLTCTEQNFITKSGFQRYAAEHQVIVVAPDTSPRGEEVPNDAAYDLGQGAGFYLNATESPWNTHYHMYDYVLNELPSLIEQHFPTNGKRAIMGHSMGGHGALVLALRNPEHYQSVSAFSPILAPSLVPWGEKAFSAYLGEDRKKWQQYDANSLIKQGSKLKKMRIDQGLDDEFLATQLRTEEFIETCRKANQPVDVRFHKGYDHSYYFIASFIGEHIAYHAQCLAN","767415","","carboxylesterase","Periplasm, Cytoplasm","","
InterPro
IPR000801
Family
Putative esterase
PF00756\"[1-236]TEsterase
InterPro
IPR014186
Family
S-formylglutathione hydrolase
TIGR02821\"[1-241]TfghA_ester_D: S-formylglutathione hydrolase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1820\"[1-236]Tno description
PTHR10061\"[1-243]TESTERASE-RELATED


","BeTs to 6 clades of COG0627COG name: Predicted esteraseFunctional Class: RThe phylogenetic pattern of COG0627 is ------y---rl-cef-h-n-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 5.3e-47) to 4/4 blocks of the IPB000801 family, which is described as \"Putative esterase\". Interpro entry for IP:IPR000801. IPB000801A 44-55 6.4e-05 IPB000801B 67-93 1.8e-15 IPB000801C 110-119 4.8e-07 IPB000801D 138-167 4.7e-15","Residues 13 to 139 match (2e-07) PD:PD017485 which is described as PROTEOME COMPLETE ESTERASE TRIBUTYRIN Z HYDROLASE SIGNAL PRECURSOR REPEAT XYLAN ","","","","","Sun Feb 16 16:14:54 2003","","","","","","","Fri Dec 20 13:40:24 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01115 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 236 (E-value = 4.9e-97) place AA01115 in the Esterase family which is described as Putative esterase (PF00756)","","","","","","","","1","","","" "AA01116","767769","767900","132","GTGAAAAACCCGATTGTTCGATTCACCAAATCCGCTAACCAAGCAGGCTTTAATATTGCTACCCCACGCATCGGGCAGATTTTCCAAATCAACGCCGAGCTGCGAAAAGAAGCTTGGTGGGAAAGCGTGAAA","","","5040","VKNPIVRFTKSANQAGFNIATPRIGQIFQINAELRKEAWWESVK","767900","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 10:39:03 2004","Wed Feb 25 10:39:03 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01116 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 10:39:03 2004","","","","","","","","","","","","","1","","","" "AA01117","769435","768059","1377","ATGTTTGAAAATTTATCCGATCGTCTTTCCAAAACCCTGCGCAACATCAGCGGACGCGGGCGTTTAACCGAAGATAACATTAAAGACACGCTGCGCGAAGTGCGCATGGCGTTACTGGAAGCCGATGTGGCGCTTCCGGTGGTACGTGATTTTATTAATAAAGTGAAAGAACGCGCCATCGGTGTCGAAGTGAACAAAAGCCTCACGCCGGGGCAGGAGTTCGTCAAAATCGTCCAAGCCGAACTGGAAACGGCGATGGGCGAAGCCAACGAAAGCCTGAATTTAGCCGCGCAACCGCCGGCAGTGATTTTAATGGCGGGCTTACAAGGGGCGGGGAAAACCACCAGCGTAGGGAAACTGGCAAAATTTTTGCGTGAACGCCACAAGAAAAAAGTGTTGGTCGTCTCTGCCGACGTGTATCGCCCTGCGGCGATCAAGCAATTGGAAACCCTTGCCCAAGCGGTAAATGCCGATTTCTTCCCGTCTGACGTGAAACAAAATCCGGTGGAGATTGCCAAAGCGGCATTGGCGGAAGCCAAACTGAAATTCTACGATGTGCTGATCGTGGATACGGCAGGTCGCTTGCACGTTGACGGCGAAATGATGGACGAAATCAAACAGGTTCACGCGGCGTTAAACCCTGTCGAAACCCTGTTCACCGTGGACGCCATGACCGGTCAGGACGCGGCGAATACGGCAAAAGCCTTTAATGAAGCCCTCCCGCTCACCGGTGTAATCCTTACCAAAGTGGACGGTGACGCCCGCGGCGGTGCGGCGTTATCCATTCGTCAAATTACCGGCAAACCGATTAAATTCCTTGGGGTGGGCGAAAAAACCGATGCGTTGGAGCCTTTCCATCCCGATCGCGTGGCATCACGCATTCTCGGCATGGGTGATGTGCTTTCCCTAATTGAAGATTTGGAACGTTCCGTTGACCGCGAAAAAGCGGAAAAAATGGCACAAAAATTTAAGAAAGGCGATGATTTCACTTTGGAAGATTTCCGCGAACAGTTACGCGAAATGAAAAAAATGGGCGGTATGATGTCCATGCTGGAAAAATTACCGGGCGCGAAAAACCTGCCGGATCATGTGAAAAATCAAGTGGATGACAAAATGTTCAACAAATTGGAAGCCATCATCAATTCCATGACCTTAAAAGAACGCGCCAATCCCGACATTATCAAAGGCTCCCGCCGCCGCCGTATTGCCCTCGGCTCCGGCACGCAGGTGCAAGATGTCAACAAATTGCTCAAACAATTCGACGAAATGCAACGCATGATGAAGAAAATGCGCAAAGGCGGCATGGCGAAAATGATGCGCGGCATGCAAGGCTTAATGGGCGGCGGACTTGGCGGGTTAGGCGGAATGTTCAGACGT","","","50550","MFENLSDRLSKTLRNISGRGRLTEDNIKDTLREVRMALLEADVALPVVRDFINKVKERAIGVEVNKSLTPGQEFVKIVQAELETAMGEANESLNLAAQPPAVILMAGLQGAGKTTSVGKLAKFLRERHKKKVLVVSADVYRPAAIKQLETLAQAVNADFFPSDVKQNPVEIAKAALAEAKLKFYDVLIVDTAGRLHVDGEMMDEIKQVHAALNPVETLFTVDAMTGQDAANTAKAFNEALPLTGVILTKVDGDARGGAALSIRQITGKPIKFLGVGEKTDALEPFHPDRVASRILGMGDVLSLIEDLERSVDREKAEKMAQKFKKGDDFTLEDFREQLREMKKMGGMMSMLEKLPGAKNLPDHVKNQVDDKMFNKLEAIINSMTLKERANPDIIKGSRRRRIALGSGTQVQDVNKLLKQFDEMQRMMKKMRKGGMAKMMRGMQGLMGGGLGGLGGMFRR","768061","","signal recognition particle protein 54 (GTP-binding export factor)","Cytoplasm, Inner membrane","","
InterPro
IPR000897
Domain
GTP-binding signal recognition particle SRP54, GTPase
PD000819\"[103-194]TSR54_HAEIN_P44518;
PF00448\"[99-296]TSRP54
PS00300\"[269-282]TSRP54
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[99-276]TAAA
InterPro
IPR004125
Domain
GTP-binding signal recognition particle SRP54, M-domain
G3DSA:1.10.260.30\"[328-432]Tno description
PF02978\"[328-427]TSRP_SPB
InterPro
IPR004780
Family
Signal recognition particle protein
PTHR11564:SF7\"[74-448]TSIGNAL RECOGNITION PARTICLE PROTEIN
TIGR00959\"[2-429]Tffh: signal recognition particle protein
InterPro
IPR013822
Domain
GTP-binding signal recognition particle SRP54, helical bundle
G3DSA:1.20.120.140\"[1-90]Tno description
PF02881\"[1-87]TSRP54_N
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[93-298]Tno description
PTHR11564\"[74-448]TGTPASE CONTAINING FAMILY OF SIGNAL RECOGNITION PARTICLE PROTEINS


","No hits to the COGs database.","Significant hit ( 3.5e-81) to 5/5 blocks of the IPB000897 family, which is described as \"GTP-binding signal recognition particle (SRP54) domain\". Interpro entry for IP:IPR000897. IPB000897A 102-121 6.2e-13 IPB000897B 134-148 6.5e-06 IPB000897C 185-205 4e-13 IPB000897D 214-256 4.9e-28 IPB000897E 269-296 1e-15","Residues 141 to 194 match (2e-13) PD:PD490262 which is described as SIGNAL RECOGNITION PARTICLE COMPLETE PROTEOME DIVISION CELL GTP-BINDING HOMOLOG FTSY ","","","","","","","","","","","","Fri Dec 20 15:33:55 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01117 is paralogously related to AA00474 (1e-37) and AA02265 (0.001).","","","","","","Residues 328 to 427 (E-value = 7.1e-54) place AA01117 in the SRP_SPB family which is described as Signal peptide binding domain (PF02978)","","","","","Herskovits AA, Shimoni E, Minsky A, Bibi E. Accumulation of endoplasmic membranes and novel membrane-boundribosome-signal recognition particle receptor complexes in Escherichia coli. J Cell Biol. 2002 Nov 4 [epub ahead of print] PMID: 12417577 Huang Q, Abdulrahman S, Yin J, Zwieb C. Systematic site-directed mutagenesis of human protein SRP54:interactions with signal recognition particle RNA and modes ofsignal peptide recognition. Biochemistry. 2002 Sep 24;41(38):11362-71. PMID: 12234178 Rinke-Appel J, Osswald M, von Knoblauch K, Mueller F, BrimacombeR, Sergiev P, Avdeeva O, Bogdanov A, Dontsova O. Crosslinking of 4.5S RNA to the Escherichia coli ribosome in thepresence or absence of the protein Ffh. RNA. 2002 May;8(5):612-25. PMID: 12022228 ","","Fri Dec 20 15:31:58 2002","1","","","" "AA01119","769568","769431","138","TTGGCGTTTTATTCTAGCGATATCGGGTTAAAATCGCCATCACTTTATTTCAAGGGTGAAAACGCGCCGAATTTCAGTATAATGAACGGCATTTTACCGATAACCTCTTTCCGATTTAACCACAGGCAATATTATGTT","","","5287","LAFYSSDIGLKSPSLYFKGENAPNFSIMNGILPITSFRFNHRQYYV","769431","","hypothetical protein","Cytoplasm, Extracellular","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 10:40:26 2004","Wed Feb 25 10:40:26 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01119 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 10:40:26 2004","","","","","","","","","","","","","1","","","" "AA01120","769589","770380","792","ATGTGGATTGCTGTTTTATCAATTATTTTTTATTTAATCAGCGTGTTATTTATCACGCCGATGTTATTAACGTCGCAGGTCAATGGCGGGCAAACCCAACCTAAAAAAACGCCATTTTTTCTGACCGCACTTTTCGCCATTATTTGCCATGTTTTCACCACGTTGCCGTTGCTCAATGATCTGGCAAACGGACAAGCCTTTACCCTGATGGAAGTGGCGTCATTGATGAGCGTGATTATCGCCTCATTAGCCACACTTGCCATGTTGCGGGTGAACAGCATGTGGTTTGTGTTGCCAATTGTGTATTGCTTTTCCATGGTTAATCTGGTTTGTGCCACTTTTATTCCAAGCCATATTATTCAGCTGTTGAATCAAAACGGTTCCATGTTATTTCATATCGGCTTGTCCATTTTTGCCTACGCGGTATGCTGCATCGCCACGCTATACGCCATTCAACTGGGCTGGATTGACCGTCGCTTAAAAGCTAAAAAAATGCACTTTTCGCCGATGGTGCCGCCATTGATGACGGTGGAACACCATTTTTTCCGTTTATTGGTAAGCGGTGAAATATTGCTGACGCTGACCTTGATTTCCGGCTCCTACCATTTGATGCACGCTATGACGCCCGACAATCTTCATAAAGGAGGATTTTCATTGCTCGGTTGGATTGTATTCGGCATTGCGATTCTGGGGCATAAGAAATACCGCTGGCGTGGAAAAAAGATGATTATTTATGCGATTTCGGGTATGATTTTGCTCACGATTGCTTACTTTGGTAGTCGATTGATTGTG","","","29576","MWIAVLSIIFYLISVLFITPMLLTSQVNGGQTQPKKTPFFLTALFAIICHVFTTLPLLNDLANGQAFTLMEVASLMSVIIASLATLAMLRVNSMWFVLPIVYCFSMVNLVCATFIPSHIIQLLNQNGSMLFHIGLSIFAYAVCCIATLYAIQLGWIDRRLKAKKMHFSPMVPPLMTVEHHFFRLLVSGEILLTLTLISGSYHLMHAMTPDNLHKGGFSLLGWIVFGIAILGHKKYRWRGKKMIIYAISGMILLTIAYFGSRLIV","770382","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR002541
Family
Cytochrome c assembly protein
PF01578\"[38-263]TCytochrom_C_asm
noIPR
unintegrated
unintegrated
signalp\"[1-29]?signal-peptide
tmhmm\"[4-24]?\"[39-57]?\"[67-87]?\"[97-117]?\"[136-156]?\"[181-201]?\"[215-233]?\"[243-263]?transmembrane_regions


","BeTs to 7 clades of COG0755COG name: ABC-type transport system involved in cytochrome c biogenesis, permease componentFunctional Class: OThe phylogenetic pattern of COG0755 is a----z-q-dr-bcefghsnujx---Number of proteins in this genome belonging to this COG is","","Residues 4 to 263 match (1e-61) PD:PD039671 which is described as PROTEOME COMPLETE MEMBRANE TRANSMEMBRANE C PA3747 C-TYPE 5'REGION PROBABLE VC0559 ","","","","","","","","","","","","Fri Dec 20 15:37:10 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01120 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 38 to 263 (E-value = 2.8e-40) place AA01120 in the Cytochrom_C_asm family which is described as Cytochrome C assembly protein (PF01578)","","","","","","","","1","","","" "AA01123","770458","771717","1260","TTGGACAGTATTCCCCTTAGTACGTTATTTATCATTTTAATTGTGTGTTTGGTGCTTTCCGCCTATTTTTCCGGTTCCGAAACCGGGCTACTTTCCTTAAATAAATACCGCCTGCGCTTCTTATCCGAGCAAGGGAATAAAGGCGCGCAAAAAGCGGAAAAACTGTTGGCCAAACCGGATAACCTATTAAGTTTTATCCTTATTTTCAATAATCTTGTTAATGTCAGTGCTTCCGCCATTGCTACCGTGATCGGAATGCGTTTATACGGCGATGCAGGTGTGGCGATTGCCACCGGGCTACTGACCTTCGTTATGCTGATTTTCTCCGAAATTTTTCCAAAAACTGTGGCGGCGATGCACCCGGAAAAAGTGGGCTTGACCACCAGCCATTTATTAATCCCGCTGATCAAAATCTTTTCTCCGTTAGCTTGGGTCATGAACCTGTTCACTAAAACCTTAATGCGTTTGGTAGGCTTAAAACCGGCGCTGAAAAAACAGGTTATCAGCCGTGAAGAATTACGCAGTATCGTCAGCGAAGCGGGCGAAGCCACGCCGGATGAGCAACATCCGCAAATGTTGTTGTCTATTTTAGATATGGATACCGTCACCGTGGACGACATTATGGTACCGCGCAATGAAATCGGCAGTATTGATATTGATGATGATTGGAAGGCGATTATGCGCCAGCTCAACCATGCGGCGCATAACCGCGTGGTGTTATACAAAGGCAGCATGGATGAAAATGTGCTCGGTATATTGCGGGTGCGCGAAGCCTTCCGTTTGTTATTGGAAAAAAATGAGTTCACCAAAGAAACGCTGATTCGTGCCGCCGACAAAGTGTATTTTATTCCGGAAGGGACGCCATTAAAAGCGCAGTTGGCGAATTTCCGCCAACGGAAAGAACGTATCGGTTTAGTGGTAGACGAATATGGTGATATTAAAGGTTTGGTGACACTGGAAGACATTTTGGAAGAAATCGTGGGCGAATTTACCACCTCCAACGCCCCGACTATTGATGAAGAAGTTACTCAACAATCGGACGGTTCCATTATTATTGATGGCTCTGCTAATTTACGCGACTTAAATAAAATGTTTCACTGGAATTTGGATACGGATGAGGCTCGTACATTTAACGGTTTGATTTTAGAGCATTTGGAAGAAATCCCACACGAAGGCACAGTCTGTGAACTTAATGGCTTGCAGGTTACCGTGTTGGAAGTGAGTGAGAATATGATTAAGCGGGCGAAGGTTATTAAATTA","","","46840","LDSIPLSTLFIILIVCLVLSAYFSGSETGLLSLNKYRLRFLSEQGNKGAQKAEKLLAKPDNLLSFILIFNNLVNVSASAIATVIGMRLYGDAGVAIATGLLTFVMLIFSEIFPKTVAAMHPEKVGLTTSHLLIPLIKIFSPLAWVMNLFTKTLMRLVGLKPALKKQVISREELRSIVSEAGEATPDEQHPQMLLSILDMDTVTVDDIMVPRNEIGSIDIDDDWKAIMRQLNHAAHNRVVLYKGSMDENVLGILRVREAFRLLLEKNEFTKETLIRAADKVYFIPEGTPLKAQLANFRQRKERIGLVVDEYGDIKGLVTLEDILEEIVGEFTTSNAPTIDEEVTQQSDGSIIIDGSANLRDLNKMFHWNLDTDEARTFNGLILEHLEEIPHEGTVCELNGLQVTVLEVSENMIKRAKVIKL","771719","","possible hemolysin; membrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR000644
Domain
Cystathionine-beta-synthase
PF00571\"[208-327]TCBS
SM00116\"[279-327]TCBS
InterPro
IPR002550
Domain
Protein of unknown function DUF21
PF01595\"[8-190]TDUF21
InterPro
IPR005170
Domain
Transporter-associated region
PF03471\"[343-420]TCorC_HlyC
noIPR
unintegrated
unintegrated
PTHR22777\"[43-420]THEMOLYSIN-RELATED
signalp\"[1-20]?signal-peptide
tmhmm\"[5-25]?\"[63-83]?\"[92-112]?\"[131-149]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 20 09:41:02 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01123 is paralogously related to AA00296 (8e-26) and AA00729 (1e-24).","","","","","","Residues 343 to 420 (E-value = 8.4e-18) place AA01123 in the CorC_HlyC family which is described as Transporter associated domain (PF03471)","","","","","","","","1","","","" "AA01124","771895","772362","468","ATGCCACAAATTTTTGAATTCTTACAAAATTATAGTGACTACATTATTATCGGTTTATTACTGTTTATGAGCGTATTAATGCTCACCATGGTCATCGAACGTTTCTTCTTTTTATCCCGTGTTAAAGTGAGTCAATATTCCACCATTTATGCACTTGAAATTGATTTAAACCGTAACCTCACCATAGTTTCTACTGTGGGAGCAAACGCGCCCTATGTGGGTCTCTTAGGCACGGTTATCGGGATTTTGTTGACCTTCTACCAAATCGGCCAATCCGGTGGTGAAGTAGATGCCGGTGAAATCATGCTGCACTTATCTTTGGCCCTAAAAGCCACCGCACTGGGTATTCTGGTGGCGATTCCTTCCATGATTTTCTATAACGCCTTGGGACGCAAAGTCGAAGTGAACCGTCTGAAGTGGAAAGTACTAAATTCTCAACAACATAAAAAAGAAGAACAGGATAAGGAA","","","17548","MPQIFEFLQNYSDYIIIGLLLFMSVLMLTMVIERFFFLSRVKVSQYSTIYALEIDLNRNLTIVSTVGANAPYVGLLGTVIGILLTFYQIGQSGGEVDAGEIMLHLSLALKATALGILVAIPSMIFYNALGRKVEVNRLKWKVLNSQQHKKEEQDKE","772364","","biopolymer transport protein","Inner membrane, Cytoplasm","","
InterPro
IPR002898
Family
MotA/TolQ/ExbB proton channel
PF01618\"[8-145]TMotA_ExbB
InterPro
IPR014172
Family
TonB-system energizer ExbB type-2
TIGR02805\"[6-144]TexbB2: tonB-system energizer ExbB
noIPR
unintegrated
unintegrated
signalp\"[1-29]?signal-peptide
tmhmm\"[14-32]?\"[68-88]?\"[107-129]?transmembrane_regions


","BeTs to 12 clades of COG0811COG name: Biopolymer transport proteinsFunctional Class: NThe phylogenetic pattern of COG0811 is --m----q-d---cefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-15) to 2/2 blocks of the IPB002898 family, which is described as \"MotA/TolQ/ExbB proton channel family\". Interpro entry for IP:IPR002898. IPB002898A 70-86 5.1e-09 IPB002898B 105-119 7.5e-05","Residues 6 to 135 match (1e-37) PD:PD003317 which is described as COMPLETE PROTEOME EXBB BIOPOLYMER TRANSMEMBRANE MEMBRANE INNER TOLQ FAMILY CHANNEL ","","","","","","","","","","","","Fri Dec 20 15:49:53 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01124 is paralogously related to AA02836 (3e-08).","","","","","","Residues 8 to 145 (E-value = 1.1e-52) place AA01124 in the MotA_ExbB family which is described as MotA/TolQ/ExbB proton channel family (PF01618)","","","","","Elkins,C., Totten,P.A., Olsen,B. and Thomas,C.E. Role of the Haemophilus ducreyi Ton system in internalization of heme from hemoglobin Infect. Immun. 66 (1), 151-160 (1998) PubMed: 9423852Jarosik,G.P. and Hansen,E.J. Cloning and sequencing of the Haemophilus influenzae exbB andexbD genes Gene 152 (1), 89-92 (1995) PubMed: 7828935 ","","Fri Dec 20 15:50:21 2002","1","","","" "AA01124.1","772369","772812","444","GTGAAAAAGTTTGATGAAATCAACATTATCCCGTTCATTGATATTATGTTGGTGCTACTTGCGATTGTGCTGATTACGGCATCTTTCATTTCCCAGGGGAAAATCCAAGTGAATGTACCGAAAGCCAGTTCTTCCGTCGCATTCAAATCCAATGAGTTGGCAAAATTGTTAACGGTAACGGCAAAAGGTGAATTATATTTCAACGATAAACCTACCAATCTTGAAAGCTTGGAGAGTGAAATCGCCGGTTGGGATAAAAAGCAAAAAGTGACGCTAAAAATTGATTCCGAGGCTTCTTTCCAAGATTTCGTTTCCGTCACCGATTTACTGGCAAAAAATGAAATTAAAGATGTAGCGATTGTGGCAACCAAAGACAACAGTGCGGACAAACCGAGACCTGCCGATGAAAAATCCGCCAAACCTGCAGAGCAGCCGGTCAGCAAC","5.10","-2.00","16161","VKKFDEINIIPFIDIMLVLLAIVLITASFISQGKIQVNVPKASSSVAFKSNELAKLLTVTAKGELYFNDKPTNLESLESEIAGWDKKQKVTLKIDSEASFQDFVSVTDLLAKNEIKDVAIVATKDNSADKPRPADEKSAKPAEQPVSN","","","biopolymer transport protein D","Periplasm, Inner membrane","AA01124.1 has significant similarity to the Haemophilus ducreyi gene HD0328, a biopolymer transport protein (5e-46).AA01124.1 has significant similarity to the Haemophilus influenzae Rd gene 16272210 (2e-53).","
InterPro
IPR003400
Family
Biopolymer transport protein ExbD/TolR
PF02472\"[1-125]TExbD
InterPro
IPR014171
Family
TonB system transport protein ExbD type-2
TIGR02804\"[4-124]TExbD_2: TonB system transport protein ExbD
noIPR
unintegrated
unintegrated
signalp\"[1-28]?signal-peptide
tmhmm\"[10-30]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.1e-13) to 1/1 blocks of the IPB003400 family, which is described as \"Biopolymer transport protein ExbD/TolR\". Interpro entry for IP:IPR003400. IPB003400 6-28 1.2e-13","Residues 1 to 125 match (3e-43) PD:PD007356 which is described as COMPLETE PROTEOME BIOPOLYMER EXBD TRANSMEMBRANE MEMBRANE INNER TOLR FAMILY EXBD/TOLR ","Fri Feb 27 09:52:30 2004","Sat Feb 28 16:51:26 2004","Sat Feb 28 16:51:26 2004","Sat Feb 28 16:51:26 2004","Fri Feb 27 09:52:30 2004","Fri Feb 27 09:52:30 2004","Fri Feb 27 09:52:30 2004","Fri Feb 27 09:52:30 2004","Fri Feb 27 09:52:30 2004","Fri Feb 27 09:52:30 2004","Fri Feb 27 09:52:30 2004","Fri Feb 27 09:52:55 2004","Fri Feb 27 09:52:30 2004","Fri Feb 27 09:52:30 2004","Fri Feb 27 09:52:30 2004","Fri Feb 27 09:52:30 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01124.1 is paralogously related to AA02834, a colicin transport protein (3e-07).AA01124.1 is paralogously related to AA02834 (3e-07).","Fri Feb 27 09:52:30 2004","Fri Feb 27 09:52:30 2004","No hits to the PDB database.","","","Residues 1 to 125 (E-value = 2.4e-55) place AA01124.1 in the ExbD family which is described as Biopolymer transport protein ExbD/TolR (PF02472)","Fri Feb 27 09:52:30 2004","","","","Elkins,C., Totten,P.A., Olsen,B. and Thomas,C.E.Role of the Haemophilus ducreyi Ton system in internalization of heme from hemoglobinInfect. Immun. 66 (1), 151-160 (1998)PubMed: 9423852Jarosik,G.P. and Hansen,E.J.Cloning and sequencing of the Haemophilus influenzae exbB and exbD genesGene 152 (1), 89-92 (1995)PubMed: 7828935 ","","Fri Feb 27 09:53:38 2004","1","Fri Feb 27 09:52:30 2004","","" "AA01125","772811","772332","480","TTGCTGACCGGCTGCTCTGCAGGTTTGGCGGATTTTTCATCGGCAGGTCTCGGTTTGTCCGCACTGTTGTCTTTGGTTGCCACAATCGCTACATCTTTAATTTCATTTTTTGCCAGTAAATCGGTGACGGAAACGAAATCTTGGAAAGAAGCCTCGGAATCAATTTTTAGCGTCACTTTTTGCTTTTTATCCCAACCGGCGATTTCACTCTCCAAGCTTTCAAGATTGGTAGGTTTATCGTTGAAATATAATTCACCTTTTGCCGTTACCGTTAACAATTTTGCCAACTCATTGGATTTGAATGCGACGGAAGAACTGGCTTTCGGTACATTCACTTGGATTTTCCCCTGGGAAATGAAAGATGCCGTAATCAGCACAATCGCAAGTAGCACCAACATAATATCAATGAACGGGATAATGTTGATTTCATCAAACTTTTTCACGGGTTATTCCTTATCCTGTTCTTCTTTTTTATGTTGT","","","16999","LLTGCSAGLADFSSAGLGLSALLSLVATIATSLISFFASKSVTETKSWKEASESIFSVTFCFLSQPAISLSKLSRLVGLSLKYNSPFAVTVNNFANSLDLNATEELAFGTFTWIFPWEMKDAVISTIASSTNIISMNGIMLISSNFFTGYSLSCSSFLCC","772334","","hypothetical protein","Outer membrane, Periplasm, Extracellular","","
noIPR
unintegrated
unintegrated
signalp\"[1-32]?signal-peptide
tmhmm\"[19-39]?\"[139-159]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Fri Dec 20 15:55:02 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01125 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01127","772825","773580","756","ATGCAAACAGCAAAGCGTTCACTCTTAAGTTTGCTTTTGTCTCTGCTGATTCATGCTGTGATTGTTTATTTGTTGTTTTGGAGTCACGTAAAGAAATCAGATTTCAGCGCCAATAGCGTTGTCGGGGAATTGTCCACCAGCATCTCTATGGAAATGCTGATGGCGCAAGTGGAAGCTGAACCGCCACCGGTAGAAGAAAAAGCGCCGGAACCTGAAAAGCAGGAAGCGGTGGATGATCCGACGGTAAAACCGGAACCGCCGAAAGTTGAAAAACCGAAAGAACCGGAAAAACCAAAAGAGAAGCCGAAAGAAAAGCCAAAGGAAAAACCGAAAGAGAAGCCGAAGCAAAAACCGAGAACTGATGTGCCTGTGGGTGACAAAACGGTAGATTCCAATGCTTCGGTGAATTCTAAAGCCACATCAACCGGTCCGGTGACAACCAATAATCCGAATTTGGCAGGCAGTGGCGCCAGCAGCGATGAAAGAAATGCCTATTTATCGGCAATTCGACGTGAAATTGAGAAACATAAACGCTACCCAACACGTGCCAAAATGATGCGTAAGCAAGGCATTGTGACCGTTTCTTTCTCCATCGGTGCAGATGGTTCCATTAGTGGGGCGAGCATCGTAAAAAGTTCAGGCGCGGAAGATTTGGATAATGCGGCGTTAAGTGCGGTCAATAGCGCCCGCTCTATTGGTCCGCGCCCGGCGGGGATTTCATCTTCAATCAGCGTGCCGATCAGTTTCAAAATTAAC","","","27091","MQTAKRSLLSLLLSLLIHAVIVYLLFWSHVKKSDFSANSVVGELSTSISMEMLMAQVEAEPPPVEEKAPEPEKQEAVDDPTVKPEPPKVEKPKEPEKPKEKPKEKPKEKPKEKPKQKPRTDVPVGDKTVDSNASVNSKATSTGPVTTNNPNLAGSGASSDERNAYLSAIRREIEKHKRYPTRAKMMRKQGIVTVSFSIGADGSISGASIVKSSGAEDLDNAALSAVNSARSIGPRPAGISSSISVPISFKIN","773582","TonB transduces energy to outer membrane receptors, especially those involved in iron uptake.","energy transducer protein","Periplasm, Inner membrane","","
InterPro
IPR003538
Family
Gram-negative bacterial tonB protein
PR01374\"[97-107]T\"[171-192]T\"[192-210]TTONBPROTEIN
PF03544\"[176-210]TTonB
InterPro
IPR006260
Domain
TonB, C-terminal
TIGR01352\"[177-252]TtonB_Cterm: TonB family C-terminal domain
noIPR
unintegrated
unintegrated
signalp\"[1-19]?signal-peptide
tmhmm\"[9-27]?transmembrane_regions


","BeTs to 6 clades of COG0810COG name: Periplasmic protein TonB, links inner and outer membranesFunctional Class: MThe phylogenetic pattern of COG0810 is -------q------efghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 2e-10) to 3/4 blocks of the PR01374 family, which is described as \"Gram-negative bacterial tonB protein signature\". Prints database entry for PR:PR01374. PR01374A 97-107 0.00063 PR01374B 171-192 5.3 PR01374C 192-210 0.012","Residues 2 to 85 match (5e-26) PD:PD062008 which is described as PROTEOME COMPLETE TP0072 PM1099 HI0926 ","","","","","","","","","","","Tue Jan 28 14:47:39 2003","Fri Dec 20 15:56:40 2002","","Thu Mar 18 09:24:22 2004","Thu Mar 18 09:24:22 2004","Thu Mar 18 09:24:22 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01127 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Mar 18 09:24:22 2004","","","","","Residues 176 to 210 (E-value = 4.4e-14) place AA01127 in the TonB family which is described as Gram-negative bacterial tonB protein (PF03544)","Thu Mar 18 09:24:22 2004","","","","Elkins,C., Totten,P.A., Olsen,B. and Thomas,C.E. Role of the Haemophilus ducreyi Ton system in internalization of heme from hemoglobin Infect. Immun. 66 (1), 151-160 (1998) PubMed: 9423852 Killmann H, Herrmann C, Torun A, Jung G, Braun V. TonB of Escherichia coli activates FhuA through interaction with the beta-barrel. Microbiology. 2002 Nov;148(Pt 11):3497-509. PMID: 12427941 Held KG, Postle K. ExbB and ExbD do not function independently in TonB-dependent energy transduction. J Bacteriol. 2002 Sep;184(18):5170-3. PMID: 12193634","","Tue Jan 28 14:47:39 2003","1","","","" "AA01128","774170","774262","93","ATGCTCTTTGGTGACTGTGATGTCTTGGTTATCGTGTTTAACAGTAAGCTCAGAGATTTCTCACAAGGTGAAAGTGCGGTAAGAGCATTGATG","","","3444","MLFGDCDVLVIVFNSKLRDFSQGESAVRALM","774262","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 10:42:12 2004","Wed Feb 25 10:42:12 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01128 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 10:42:12 2004","","","","","","","","","","","","","1","","","" "AA01129","774753","774848","96","TTGATTGATAAACTTTTAGAAGTTACTAATCTTAATAAAAAAGCAGCGTTATTTAATACTGTGGCAGAATTTATGTGTATTGATTTTAACTATCTT","","","3687","LIDKLLEVTNLNKKAALFNTVAEFMCIDFNYL","774848","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 10:52:05 2004","Wed Feb 25 10:52:05 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01129 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 10:52:05 2004","","","","","","","","","","","","","1","","","" "AA01130","774832","775083","252","TTGATTTTAACTATCTTTGATTATGTTGATTATCTTGATTTTGTTACAGGTTCAAATGTACAAAAATCAGGGCGTACTTATGCTATACAGAAAAATCGCACCTATGAATTTTTCTATGAACTTTACGAAGATTATCAGGTAAATTGGATCAATGTTCGTGTTAGAGGTGTGATTATTCTTGCCTTGTTGCATTATGCAAAATGTAAGTTAAATTTGAATTTGGACGAACTTTTAAAAGGACTAAATGATGAG","","","9970","LILTIFDYVDYLDFVTGSNVQKSGRTYAIQKNRTYEFFYELYEDYQVNWINVRVRGVIILALLHYAKCKLNLNLDELLKGLNDE","775085","","conserved hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","Residues 7 to 68 match (8e-13) PD:PD540374 which is described as PLASMID ","","","","","","","","","","","","Fri Dec 20 16:09:48 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01130 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01131","775415","775591","177","ATGATTACTAATGAAGAAAAATTAAGTAGACAAAAATCAGTTCAATTTGCTATTGATAACAATCGTCTTGAGGGATTGGATACTGATAGCGATATTTTAGAACTTTCTCAAGATTGGGTAAACGGTGAAATTAGTTATAAAGAATTTCAGGAGAGAGTTTATGAAATATACGGGATC","","","6954","MITNEEKLSRQKSVQFAIDNNRLEGLDTDSDILELSQDWVNGEISYKEFQERVYEIYGI","775591","","conserved hypothetical protein","Cytoplasm","This sequence is similar to gi|32030928, a hypothetical from H. somnus.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 10:56:20 2004","Wed Feb 25 10:56:20 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01131 is paralogously related to AA01134 (0.001).","Wed Feb 25 10:56:20 2004","","","","","","","","","","","","","1","","","" "AA01132","775575","775967","393","ATGAAATATACGGGATCTGATCCATATATTTATGAAAATGGAGTTTTAATAAATAAAAAAGGAATTAAAGATGAAGCTGAATTAAATAGGATAGAAAGAGCTTCTTCTTATATGAAAGCTCTTGATTTAAATCAAAATTCAATTAACGGTAAATTTGATTTAAAGCACCTTCAAGCTATCCATAAAAAATTATTCGAAGATATTTATCCCTTTGCTGGAAAAATAAGAGATGGATATTTACAAAAAGGTGAACAAGATTTCACTATGGGCTATCGTATTATTCCGCAATCTGAAAGACTGTTTAAAGAACTCAAAAATGAGCAATTTTTGAAGAAAACAGAGTCTGATAAAATTGCGGGTAGATTAGCTTACTATATGGGGGAAATTGACGAA","","","16824","MKYTGSDPYIYENGVLINKKGIKDEAELNRIERASSYMKALDLNQNSINGKFDLKHLQAIHKKLFEDIYPFAGKIRDGYLQKGEQDFTMGYRIIPQSERLFKELKNEQFLKKTESDKIAGRLAYYMGEIDE","775969","","possible cell filamentation protein","Cytoplasm","","No hits reported.","BeTs to 7 clades of COG2184COG name: Protein involved in cell divisionFunctional Class: DThe phylogenetic pattern of COG2184 is ----------r---ef-hsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.6e-08) to 1/2 blocks of the IPB003812 family, which is described as \"Fic (filamentation induced by cAMP) protein\". Interpro entry for IP:IPR003812. IPB003812A 60-91 1.5e-08","Residues 101 to 130 match (8e-07) PD:PD525146 which is described as PROTEOME COMPLETE CELL FILAMENTATION PLASMID FIC BY PHASE RECOGNIZED DIVISION ","","","","","","","","","","","","Thu Jan 23 08:15:11 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01132 is paralogously related to AA02921 (7e-08), AA01133 (1e-05) and AA00175 (2e-04).","","","","","","","","","","","","","","1","","","" "AA01133","777100","776663","438","ATGATGAAGGATTATTCTGAAGAAGAGATAAAGGATAAGTTGTCATTTATTCGTTTATCAGAATTGAGAGAAAATCCTGTAAAAGGGAAATTTGATTTAGAACATCTGAAAAGATTAAATGGTTATATTTTTCAGGATAGCCCTGATGTAGCTGGTAAATTTAGATCTGAAGTTGAAATAGGTAGTAATGAGTTGTGGCATAAGGTACGCCATTATCAGGGCTTTGGGAATATAACCGTTTTTTATAGCTCTATGGATAGTAGAAATATTAAAGAGGCTGAAGATACTTTAAATGTGATCAATATAAACCAATTAAAAACTTTTAATAAAGATGAATTTGCTAAAGAAGTTGTAGATATTTATAAAAAGCTAGATTACATTCACCCATTCCCTGATGGGAATAGTCGAACATTACGAGAATTTACTCGAATTCTTTCG","","","17240","MMKDYSEEEIKDKLSFIRLSELRENPVKGKFDLEHLKRLNGYIFQDSPDVAGKFRSEVEIGSNELWHKVRHYQGFGNITVFYSSMDSRNIKEAEDTLNVININQLKTFNKDEFAKEVVDIYKKLDYIHPFPDGNSRTLREFTRILS","776663","","conserved hypothetical protein","Cytoplasm","This sequence is similar to gi|23466462, a hypothetical from H.somnus. See also gi|16751963 from plasmid pIPO2T.","No hits reported.","BeTs to 3 clades of COG2184COG name: Protein involved in cell divisionFunctional Class: DThe phylogenetic pattern of COG2184 is ----------r---ef-hsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-05) to 2/2 blocks of the IPB003812 family, which is described as \"Fic (filamentation induced by cAMP) protein\". Interpro entry for IP:IPR003812. IPB003812A 39-70 42 IPB003812B 121-142 0.00014","Residues 8 to 60 match (2e-08) PD:PD009618 which is described as PROTEOME COMPLETE FILAMENTATION CELL PLASMID NMA0004 HI0977 MOBILIZATION FIC-RELATED CAMP-INDUCED ","","","","","","","","","","","","Wed Feb 25 11:08:15 2004","Wed Feb 25 11:08:15 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is weakly paralogous to AA0742, a possible cell filamentation protein.AA01133 is paralogously related to AA01132 (1e-05).","Wed Feb 25 11:08:15 2004","","","","","","","","","","","","","1","","","" "AA01134","777347","777105","243","ATGGTGTATAAAATACCTACTATTTATAATAGGTATATCCGTTTTTTAAAGATGCAAATTATGATTTCTGAAGCTGAAAAAGAAGTTAGACGTGAAGCAGTTGAATATGCAAAATCTAGCGTAGGATTAGAGGGGGTGACTTTATCTAAAGGATTGTTAGAAATTGCCGATAAATATATTCAAGGTTTATTAACAAGAGAAGAATTTACAAAAGAATATATTACAGCAGTAAGAGCAGGTGTG","","","9333","MVYKIPTIYNRYIRFLKMQIMISEAEKEVRREAVEYAKSSVGLEGVTLSKGLLEIADKYIQGLLTREEFTKEYITAVRAGV","777107","","conserved hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Fri Dec 20 16:19:23 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01134 is paralogously related to AA01131 (0.001).","","","","","","","","","","","","","","1","","","" "AA01135","777724","777521","204","TTGAGGGACTGGCAACGCATAAGGATATACAACCAAAAAGGCATAACTGTAGAAGCCTTGAAATCGGGAGTTATCCAGCCTAAACAGCTAGATAATGAATTAAAAGTCAATCGCCCTGAAGCAAGAACAATTAACGCCGCAGGTTCTAAAATTAAACCCAAATCTCAGGAACAACAAGCTCAAAAATCTAAAGGTTTTTCCCTA","","","7714","LRDWQRIRIYNQKGITVEALKSGVIQPKQLDNELKVNRPEARTINAAGSKIKPKSQEQQAQKSKGFSL","777523","","possible cell filamentation protein","Periplasm","","No hits reported.","No hits to the COGs database.","","Residues 12 to 67 match (3e-15) PD:PD484950 which is described as PLASMID RELAXASE-LIKE ","","","","","","","","","","","","Thu Jan 23 08:16:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01135 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01136","778425","778562","138","GTGAACAACGAAAAAATTTCAAATATCTCTCAACAAGTAATTACTATTTTAGATATTAAACTTCACGAAACTGAAAACGATCAATTCCTTTTACATTTTGAGGGAAAAGTAAGAGGCATTGTAGTTTATTTTAACTAT","","","5402","VNNEKISNISQQVITILDIKLHETENDQFLLHFEGKVRGIVVYFNY","778562","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 11:11:10 2004","Wed Feb 25 11:11:10 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01136 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 11:11:10 2004","","","","","","","","","","","","","1","","","" "AA01137","778700","781117","2418","ATGAATAATTTTAACCAACTTAGTCGCCGAGATTTTATTAAGTCATCATTGGCAGGTGCTGCCATTATAGCGGCGGATATTGTCCTGCCGTTTAATGTGATGGCGACGAACACATTAAAAAAAGAACAAGAAAGTGTGGAAAAGGTGGTATGGAGCGCCTGTACTGTCAATTGCGGAAGTCGTTGCCCGTTACGTATGCATGTTAAGGATAATCGCATTACCTATGTGGAAACCGATAATACAGGCACGGAAACTTATAATGTGGATCACCAGGTGCGCGCCTGTTTACGTGGGCGTTCTATGCGTCGTCGTGTTTATAATCCCGATCGTTTGAAATATCCGATGAAACGCGTAGGAAAACGTGGTGAAGGCAAGTTCAAACGCATCAGTTGGGATGAAGCTTTAACAGAAATTGCCGATGCCTTGAAACGTAATATTGCAAAATACGGCAATGAATCTATTTATTTGAACTACGGCACCGGTACACTGGGCGGCACCATGACCAAATCCTGGCCACCGGCTTCTACTATGGTGGCGCGTTTTATGAACTGTATCGGTGGGTATTTAAACCACTACGGCGATTACAGCACCGCGCAAATTGCTGTGGGGTTAGATTATACCTACGGAGGCGGATGGGCGCTCGGAAACGGGATGGCGGACATCGAAAACACCAAGCTTATCGTACTGTTTGGTAACAATCCCGCCGAGACACGCATGAGCGGCGGTGGCTTGACCTACTGTATCGAACAGGCAAAGCAACGCTCCAACGCCAAAATGATTTTAATTGACCCACGCTATACCGACACAGGCGTCGGGCGTGAAGACGAATGGATTCCGATTCGTCCCGGCACTGATGCGGCACTGGTTTCTGCGCTGGCGTATGTGATGATTACCGAAGATTTGGTGGATCAGCCCTTCCTTGATAAATACTGTGTCGGCTACGATGAAAAAACCTTACCGGAGGGCGCACCGCAAAACGGACATTACAAAGCCTATATTTTGGGGCAGGGCGATGATGGTATAGCCAAAACTCCGGAGTGGGCATCGAAAATCACCGGTATTCCGGTGGATCGTATTATTAAATTAGCCCGTGAAATCGGTAGCACCAAACCGGCATTTATTTCCCAAGGTTGGGGACCACAACGACGCAGTAACGGTGAACTCATTTCCCGCGCCATTGCCATGCTGCCGATTTTAACCGGTAATGTCGGCATTCATGGCGGCAACACCGGCGCACGGGAAAGTGCGTACAGCATTCCGTTTGTGCGAATGCCAACGTTAAAAAATCCGGTGAAAGCCAGTATTCCGATGTTCATGTGGACTGACGCCATTATTCGGGGACCGGAAATGACCGCACTTACCGACGGCATTCGCGGCGTAGATAAACTGTCCGCGCCGATTAAAGTAATCTGGAACTATTCAAGTAACTGCCTTATCAATCAGCACGCGCAAATTAACCGCACTCATGACATTTTGCAGGACGACAGCCAATGCAAAATGGTCATCACCATTGATAATCACATGACTTCCACCGCGAAATACAGCGATATTTTGTTGCCGGATTGCACCACTTCGGAACAAATGGATTTTGCACTGGACGCTTTCGTCTCCAATATGGCGTATGTGATTTTTGCCGACCAAGTGGTTAAACCGTCTTTTGAATGTCGCACGATTTACGATATGTTGAGCGACTTGGCGGACAAAATGGGGGTAAAAGACAAATTCACCGAAGGTCGCACACAGGAAGAATGGCTACGCTATATTTATGCACAATCCCGCGAAAAACTGCCTGAATTACCGACCTTTGAGGAATTCAGACAACAAGGGATTTTCAAAAAGGTGGATCCGAACGGTTTCAAAGTGGCATATAAAGATTTCCGCGACGACCCGGAAGCTCACCCGCTGAAAACACCATCCGGCAAAATTGAAATTTATTCCTCCCGTCTAGCGGAAATCGCCAAAACCTGGAAGCTGGCAGAAGATGAAGTGATTCATCCGTTACCGGTTCATGCGCAAAGCTTCGAGCATTATGGCGATCCGCTCATGGAAAAATACCCGCTACAACTCAGCGGTTTCCATTACAAAGCCCGCACGCACTCCACCTATGGTAATGTGGATGTGTTAAAAGCCGCCAATCCGCAGGAAGTGTGGATGAACCCCATTGATGCGCAACCGCGTGGTATTCAAAACGGCGATCTGATTCGTATTTTTAATGATCGTGGTGAAGTGCGTATTAACGTCAAGGTGACTCCGCGTATTATTCCGGGGGTCGTCGCATTAAGCGAAGGAGCGTGGTATGCACCGGATAAGGATCGCATCGACCATTCCGGTTGTATTAATGTGCTGACCACCCAACGCCCGTCACCACTGGCGAAAGGCAATCCGCAACATTCTAATTTGGTTCAAGTGGAACGCTTG","","","92880","MNNFNQLSRRDFIKSSLAGAAIIAADIVLPFNVMATNTLKKEQESVEKVVWSACTVNCGSRCPLRMHVKDNRITYVETDNTGTETYNVDHQVRACLRGRSMRRRVYNPDRLKYPMKRVGKRGEGKFKRISWDEALTEIADALKRNIAKYGNESIYLNYGTGTLGGTMTKSWPPASTMVARFMNCIGGYLNHYGDYSTAQIAVGLDYTYGGGWALGNGMADIENTKLIVLFGNNPAETRMSGGGLTYCIEQAKQRSNAKMILIDPRYTDTGVGREDEWIPIRPGTDAALVSALAYVMITEDLVDQPFLDKYCVGYDEKTLPEGAPQNGHYKAYILGQGDDGIAKTPEWASKITGIPVDRIIKLAREIGSTKPAFISQGWGPQRRSNGELISRAIAMLPILTGNVGIHGGNTGARESAYSIPFVRMPTLKNPVKASIPMFMWTDAIIRGPEMTALTDGIRGVDKLSAPIKVIWNYSSNCLINQHAQINRTHDILQDDSQCKMVITIDNHMTSTAKYSDILLPDCTTSEQMDFALDAFVSNMAYVIFADQVVKPSFECRTIYDMLSDLADKMGVKDKFTEGRTQEEWLRYIYAQSREKLPELPTFEEFRQQGIFKKVDPNGFKVAYKDFRDDPEAHPLKTPSGKIEIYSSRLAEIAKTWKLAEDEVIHPLPVHAQSFEHYGDPLMEKYPLQLSGFHYKARTHSTYGNVDVLKAANPQEVWMNPIDAQPRGIQNGDLIRIFNDRGEVRINVKVTPRIIPGVVALSEGAWYAPDKDRIDHSGCINVLTTQRPSPLAKGNPQHSNLVQVERL","781119","","anaerobic dimethyl sulfoxide reductase, chain A","Periplasm, Cytoplasm","","
InterPro
IPR006311
Domain
Twin-arginine translocation pathway signal
TIGR01409\"[7-35]TTAT_signal_seq: Tat (twin-arginine transloc
InterPro
IPR006655
Family
Prokaryotic molybdopterin oxidoreductase
PS00490\"[509-526]TMOLYBDOPTERIN_PROK_2
PS00551\"[52-71]TMOLYBDOPTERIN_PROK_1
PS00932\"[723-750]?MOLYBDOPTERIN_PROK_3
InterPro
IPR006656
Domain
Molybdopterin oxidoreductase
PF00384\"[110-568]TMolybdopterin
InterPro
IPR006657
Domain
Molydopterin dinucleotide-binding region
PF01568\"[687-800]TMolydop_binding
InterPro
IPR006963
Domain
Molybdopterin oxidoreductase Fe4S4 region
PF04879\"[47-107]TMolybdop_Fe4S4
InterPro
IPR011888
Family
Anaerobic dimethyl sulfoxide reductase, subunit A, DmsA/YnfE
TIGR02166\"[7-806]TdmsA_ynfE: anaerobic dimethyl sulfoxide red
noIPR
unintegrated
unintegrated
G3DSA:2.40.40.20\"[661-805]Tno description
G3DSA:3.40.228.10\"[196-418]Tno description
G3DSA:3.90.55.10\"[42-172]Tno description
PTHR11615\"[47-633]T\"[674-806]TNITRATE, FROMATE, IRON DEHYDROGENASE
PTHR11615:SF18\"[47-633]T\"[674-806]TDIMETHYL SULFOXIDE REDUCTASE
tmhmm\"[15-35]?transmembrane_regions


","BeTs to 17 clades of COG0243COG name: Anaerobic dehydrogenases, typically selenocysteine-containingFunctional Class: CThe phylogenetic pattern of COG0243 is aompkz-q-dr-bcefgh--uj----Number of proteins in this genome belonging to this COG is","Significant hit ( 8.6e-36) to 3/3 blocks of the IPB001467 family, which is described as \"Prokaryotic molybdopterin oxidoreductases\". Interpro entry for IP:IPR001467. IPB001467A 95-117 8.4e-11 IPB001467B 123-145 3.6e-11 IPB001467C 501-526 8.2e-11","Residues 94 to 140 match (2e-07) PD:PD134436 which is described as COMPLETE PROTEOME SUBUNIT MOLYBDOPTERIN A REDUCTASE TETRATHIONATE OXIDOREDUCTASE BINDING TTRA ","","","","","","","","","","","","Fri Dec 20 16:39:48 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01137 is paralogously related to AA02251 (6e-84), AA02699 (3e-19), AA00552 (1e-16), AA02676 (2e-12), AA02698 (7e-07) and AA02675 (2e-04).","","","","","","Residues 687 to 800 (E-value = 6.6e-44) place AA01137 in the Molydop_binding family which is described as Molydopterin dinucleotide binding domain (PF01568)","","","","","Loosmore,S.M., Shortreed,J.M., Coleman,D.C., England,D.M. andKlein,M.H.Sequences of the genes encoding the A, B and C subunits of theHaemophilus influenzae dimethylsulfoxide reductase complexGene 169 (1), 137-138 (1996)PubMed: 8635740Trieber,C.A., Rothery,R.A. and Weiner,J.H.Multiple pathways of electron transfer in dimethyl sulfoxide reductase of Escherichia coliJ. Biol. Chem. 269 (10), 7103-7109 (1994)PubMed: 8125918Bilous,P.T., Cole,S.T., Anderson,W.F. and Weiner,J.H.Nucleotide sequence of the dmsABC operon encoding the anaerobicdimethylsulphoxide reductase of Escherichia coliMol. Microbiol. 2 (6), 785-795 (1988)PubMed: 3062312","","Fri Dec 20 16:38:15 2002","1","","","" "AA01138","781131","781745","615","ATGGAACAATATGGTTTTTATTTTGATTCGGATCGCTGTACAGGCTGTAAAACTTGCGAATTAGCCTGTAAAGATTACAAAGATTTAGGCACGGAGGTAAATTTCCGTCGTATTTATGAATACACCGGTGGCAACTGGAGCCAACAGCCGGACGGTTGTTGGCTCCAAAACGTGTTTGCTTATTATATGTCCATTTCATGCAATCATTGCGCCGATCCGGCTTGTACCAAGGTTTGCCCGACAGGCGCCATGCAAAAAAATGCAGACGGTTTTGTGATTGTGAATGAAGAAATCTGCATTGGCTGTCGCTATTGCCACATGGCGTGTCCGTATGACGCGCCGCAATTCGACGCGGAAAAAGGTCACATGACCAAATGTGACGGTTGCTATTCGCGTATTAAAGCAGGGCAAAAACCGATTTGCGTGGATGCCTGTCCATTGCGCGCTCTTGATTTTGCACCCATTAAAGAATTGCGCGCTAGGTATGGTGAACAGGTCTCTATTGCACCCTTGCCTCCGGCAGAAGTGACCCATCCGAATTTGGTCGTGAAACCAAACAAAAACGCCCGTCTAAGCGGCGATACCAACGGGTTCTTAGGTAACCCGGGAGAGGTG","","","22744","MEQYGFYFDSDRCTGCKTCELACKDYKDLGTEVNFRRIYEYTGGNWSQQPDGCWLQNVFAYYMSISCNHCADPACTKVCPTGAMQKNADGFVIVNEEICIGCRYCHMACPYDAPQFDAEKGHMTKCDGCYSRIKAGQKPICVDACPLRALDFAPIKELRARYGEQVSIAPLPPAEVTHPNLVVKPNKNARLSGDTNGFLGNPGEV","781747","","anaerobic dimethyl sulfoxide reductase, chain B","Periplasm, Inner membrane","","
InterPro
IPR001450
Domain
4Fe-4S ferredoxin, iron-sulfur binding
PR00353\"[92-103]T\"[140-151]T4FE4SFRDOXIN
PF00037\"[6-29]T\"[92-115]TFer4
PS00198\"[99-110]T4FE4S_FERREDOXIN
InterPro
IPR014297
Family
Dimethylsulfoxide reductase, chain B
TIGR02951\"[3-163]TDMSO_dmsB: dimethylsulfoxide reductase, cha
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.20\"[56-128]Tno description
PTHR11938\"[7-161]TFAD NADPH DEHYDROGENASE/OXIDOREDUCTASE
PTHR11938:SF10\"[7-161]TMOLYBDOPTERIN OXIDOREDUCTASE


","No hits to the COGs database.","Significant hit ( 3.2e-07) to 2/2 blocks of the PR00353 family, which is described as \"4Fe-4S ferredoxin signature\". Prints database entry for PR:PR00353. PR00353A 6-17 0.069 PR00353B 74-85 0.0021 PR00353B 104-115 1","Residues 4 to 36 match (2e-08) PD:PD007945 which is described as COMPLETE PROTEOME IRON-SULFUR REDUCTASE SUBUNIT B CHAIN SULFOXIDE OXIDOREDUCTASE MOLYBDOPTERIN ","","","","","","","","","","","","Fri Dec 20 16:32:34 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01138 is paralogously related to AA02677 (8e-25), AA00044 (2e-22) and AA02683 (1e-12).","","","","","","Residues 92 to 115 (E-value = 7.7e-07) place AA01138 in the Fer4 family which is described as 4Fe-4S binding domain (PF00037)","","","","","Loosmore,S.M., Shortreed,J.M., Coleman,D.C., England,D.M. andKlein,M.H.Sequences of the genes encoding the A, B and C subunits of theHaemophilus influenzae dimethylsulfoxide reductase complexGene 169 (1), 137-138 (1996)PubMed: 8635740Trieber,C.A., Rothery,R.A. and Weiner,J.H.Multiple pathways of electron transfer in dimethyl sulfoxide reductase of Escherichia coliJ. Biol. Chem. 269 (10), 7103-7109 (1994)PubMed: 8125918Bilous,P.T., Cole,S.T., Anderson,W.F. and Weiner,J.H.Nucleotide sequence of the dmsABC operon encoding the anaerobicdimethylsulphoxide reductase of Escherichia coliMol. Microbiol. 2 (6), 785-795 (1988)PubMed: 3062312","","Fri Dec 20 16:38:13 2002","1","","","" "AA01140","781750","782586","837","ATGAACATAGTGATACATGAATTACCGTTGGTGGTATTCACCGTGTTGGCACAAAGTGCGGTCGGTTCCTGGCTTGTTTTTAGCTTCGTGCTTTGCACCAATTTAAATGCGCAGAGCCGTCGTTATGTGCATAAAGTCATGTTTGTGATTCTCGCTTTACTCGGCATCGGCTTTACTGCCTCCGTGTTGCACTTAGGTACACCGATCCGCGCGTTTAATTCGCTGAACCGCGTGGGCGAATCTATGATGAGTAATGAAATCGCGTCGGGGGCGTTGTTCTTTGCTATGGCGGGTATGTATTGGTTGCTTGCCATCATGCGCAAAATGCCTCTTGCACTCGACAAACTGTGGCTGGTGATAAGCTCCCTTATCGGTTTGGTTTTTATGGTGATCATGGATCAGGTTTACCACATTCCAAGCGTGCCGACCTGGAACACGCCGATGACCTCCTGCTTGTTCTTTGGCACGGTAGCATTGGGTGGCATCGCGTTAAGTTCCGCGTTGATTATGGCAAATCCGCAACGGACTTATCAACTTAGCGCCCTGCCTTGGTTATTTGCTCTGGCGGTGTTATTCGCCGCCATTGTCGCAGTTTACCAAGGTTTCTCCTTACCACAAATTCACAGCGCTATACAAAATGCCGCCGCCCTCGTGCCGGATTACGCCGCCTTCAGCGCACTACGCTTTTGTTGCTTAGCCCTCGCTGCACTCTTTATTTTCCGCAGTAAAAACATCGGTGTACTCGCATTGGCTGCCATTTTGACGCTGTTTGCCGAAATGTTGGGACGCAATTTGTTTTATGCTGCGCACATGACCCTTGGCATGGCGGTAGGTGGT","","","30247","MNIVIHELPLVVFTVLAQSAVGSWLVFSFVLCTNLNAQSRRYVHKVMFVILALLGIGFTASVLHLGTPIRAFNSLNRVGESMMSNEIASGALFFAMAGMYWLLAIMRKMPLALDKLWLVISSLIGLVFMVIMDQVYHIPSVPTWNTPMTSCLFFGTVALGGIALSSALIMANPQRTYQLSALPWLFALAVLFAAIVAVYQGFSLPQIHSAIQNAAALVPDYAAFSALRFCCLALAALFIFRSKNIGVLALAAILTLFAEMLGRNLFYAAHMTLGMAVGG","782588","","anaerobic dimethyl sulfoxide reductase, chain C","Inner membrane, Cytoplasm","","
InterPro
IPR007059
Family
DMSO reductase anchor subunit (DmsC)
PF04976\"[1-269]TDmsC
noIPR
unintegrated
unintegrated
signalp\"[1-37]?signal-peptide
tmhmm\"[10-32]?\"[47-67]?\"[86-106]?\"[116-136]?\"[150-170]?\"[182-202]?\"[221-240]?\"[245-267]?transmembrane_regions


","BeTs to 3 clades of COG3302COG name: DMSO reductase anchor subunitFunctional Class: RThe phylogenetic pattern of COG3302 is -------q------e--h---j----Number of proteins in this genome belonging to this COG is","","Residues 203 to 279 match (3e-08) PD:PD565311 which is described as REDUCTASE COMPLETE PROTEOME SUBUNIT DIMETHYL SULFOXIDE C ANAEROBIC DMSO CHAIN ","","","","","","","","","","","","Fri Dec 20 16:37:12 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01140 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 269 (E-value = 8.6e-114) place AA01140 in the DmsC family which is described as DMSO reductase anchor subunit (DmsC) (PF04976)","","","","","Loosmore,S.M., Shortreed,J.M., Coleman,D.C., England,D.M. andKlein,M.H.Sequences of the genes encoding the A, B and C subunits of theHaemophilus influenzae dimethylsulfoxide reductase complexGene 169 (1), 137-138 (1996)PubMed: 8635740Trieber,C.A., Rothery,R.A. and Weiner,J.H.Multiple pathways of electron transfer in dimethyl sulfoxide reductase of Escherichia coliJ. Biol. Chem. 269 (10), 7103-7109 (1994)PubMed: 8125918Bilous,P.T., Cole,S.T., Anderson,W.F. and Weiner,J.H.Nucleotide sequence of the dmsABC operon encoding the anaerobicdimethylsulphoxide reductase of Escherichia coliMol. Microbiol. 2 (6), 785-795 (1988) PubMed: 3062312 ","","Fri Dec 20 16:38:39 2002","1","","","" "AA01141","782637","783248","612","ATGGATAACGGATTAATGCAATGGATTTCCACCACAGGGCGGTTATTGGGCGCGGCGTTTTATTATGCGCCCGATGACGCGCGGGTTGCTTCTGTGTTGTGTTTTTTTGAACGGGAAAATTGGCAGCAGGAATGGGCGCCCTTTGTGGATGAAAAAACGTTGGAAAAAACCACCGCACTGTTTGCCGAAGGTTTACAGCAACCGCTTGCTGAACAATATCAGGCGTTGTTTATCGGCCCGAATGCGCTGCCTGCGCCGCCTTGGGGTTCCGTCTATTTGGATCCGGAGTCGGTGATTTTCGGCAGTTCGTTGTTAGAGCTGCGTGCCTTCCTGCAACGTCATCAAATTGCCTTTCAATCTCATCAAAATGAACCGGAAGATCATCTCGGCCTGATGTTAATGCTGGCGGCATATTTGGCGGAAAATCAACCGCACTTAATGAGGGAGTTTCTCAACCGCCATTTCCTCACTTGGGCGCCGCATTGCTTACAACTGCTTGCTGCTTTGGAGGATTTCCTGTTTTATCGAGGCTTGGCGTTATTGACGTTAGCCACGCTGAAACAATGGCAACAAGCCCTAAATTTAGAGGTACCAACCGTTCGTTTTTATCGT","","","23486","MDNGLMQWISTTGRLLGAAFYYAPDDARVASVLCFFERENWQQEWAPFVDEKTLEKTTALFAEGLQQPLAEQYQALFIGPNALPAPPWGSVYLDPESVIFGSSLLELRAFLQRHQIAFQSHQNEPEDHLGLMLMLAAYLAENQPHLMREFLNRHFLTWAPHCLQLLAALEDFLFYRGLALLTLATLKQWQQALNLEVPTVRFYR","783250","","conserved hypothetical protein (possible component of anaerobic dehydrogenase/oxidoreductase)","Cytoplasm","","
InterPro
IPR010395
Family
Cytoplasmic chaperone TorD
PF06192\"[32-166]TTorD


","BeTs to 4 clades of COG3381COG name: Uncharacterized component of anaerobic dehydrogenasesFunctional Class: RThe phylogenetic pattern of COG3381 is -o------------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 7 to 45 match (9e-07) PD:PD485601 which is described as PROTEOME COMPLETE PM1757 HI1044 ","","","","","Tue Feb 18 16:05:29 2003","","","","","","","Tue Feb 18 16:05:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01141 is paralogously related to AA02587 (7e-07).","","","","","","Residues 32 to 166 (E-value = 1.1e-54) place AA01141 in the TorD family which is described as Cytoplasmic chaperone TorD (PF06192)","","","","","","","","1","","","" "AA01143","783595","783251","345","GTGGAAAATGCGTGCCATTATACTGAAAACACAAGGCGGGATAAAGGAAAGGCGGAAAAAAGTGCGGTGGGGAAAACACTTGGATTTCCAACCGCACTTTATGTGAGCGCCAGCCGAATCACCTATACAGAACAGGCGATTTTGCATTCGTCGCAGCCGTTACATACGGTCAAAATAAATCTTCCCGCGCAGCAAACGGCGGGTGATTTGCCGCACGTTGGTTTTCCACGGGCGGATGTTCCACTGCACCGAAAATACCGCGGAATAAGCCCCGTCGGGAAATGGCGTTGTGGCTTAAATATGCCTGATAATAGGTTTCTTTTTTTGGCATATGGCGCTTTCCGT","","","12807","VENACHYTENTRRDKGKAEKSAVGKTLGFPTALYVSASRITYTEQAILHSSQPLHTVKINLPAQQTAGDLPHVGFPRADVPLHRKYRGISPVGKWRCGLNMPDNRFLFLAYGAFR","783253","","hypothetical protein","Periplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Fri Dec 20 16:53:31 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01143 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01145","783618","784520","903","ATGACAACATTTAATGTAAAAACTTTTCAAGGCATGATTCTTGCCTTACAGGAATACTGGGCGAACCAAGGTTGTACGGTGGTGCAGCCGTTTGATATGGAAGTGGGCGCGGGCACTTCGCACCCGATGACGGCACTTCGCGCGTTAGGGCCGGAACCGATGGCGTTTGCCTATGTGCAGCCTTCACGCCGTCCGACAGACGGTCGTTATGGCGAAAATCCGAACCGTTTGCAACATTATTATCAATTCCAGGTGGTGATCAAACCTTCACCGGACAACATTCAGGAACTGTATTTGGATTCCTTAAAAATGCTCGGTTTCGACCCGACCCAGAACGACATTCGTTTTGTGGAAGACAACTGGGAAAACCCGACGCTGGGTGCGTGGGGCTTGGGCTGGGAAGTGTGGCTGAACGGTATGGAAGTGACCCAATTCACCTATTTCCAACAGGTGGGCGGCTTGGAATGTAAACCGGTGACCGGCGAAATCACTTACGGCTTGGAACGTTTGGCGATGTACATTCAGGGCGTAGACAGCGTGTATGATTTGGTGTGGTCAGACGGTCCGCTCGGCAAAACCACTTACGGCGACGTGTTCCATCAAAACGAAGTGGAACAATCCACCTACAACTTTGAATATGCCGACACCGATTTCTTGTTCTACTGTTTCGATCAATACGAAAAAGAAGCGCAAAGCCTGTTAGCATTGGAAAAACCGCTGCCGTTGCCGGCGTATGAGCGCATTTTGAAAGCGGCGCACAGCTTTAACTTATTGGACGCACGCAAAGCCATTTCCGTAACCGAACGTCAACGTTACATTTTACGCATTCGTGCGCTCACCAAAGGCGTGGCGGAAGCCTATTACGCCAGCCGCGAAGCCTTGGGGTTCCCGGGGTGTAAGAAG","","","34386","MTTFNVKTFQGMILALQEYWANQGCTVVQPFDMEVGAGTSHPMTALRALGPEPMAFAYVQPSRRPTDGRYGENPNRLQHYYQFQVVIKPSPDNIQELYLDSLKMLGFDPTQNDIRFVEDNWENPTLGAWGLGWEVWLNGMEVTQFTYFQQVGGLECKPVTGEITYGLERLAMYIQGVDSVYDLVWSDGPLGKTTYGDVFHQNEVEQSTYNFEYADTDFLFYCFDQYEKEAQSLLALEKPLPLPAYERILKAAHSFNLLDARKAISVTERQRYILRIRALTKGVAEAYYASREALGFPGCKK","784522","","glycyl-tRNA synthetase alpha subunit","Cytoplasm","","
InterPro
IPR002310
Domain
Glycyl-tRNA synthetase, alpha subunit
PD006985\"[28-281]TSYGA_PASMU_P57904;
PR01044\"[61-76]T\"[82-102]T\"[113-137]T\"[139-159]T\"[162-177]T\"[253-269]TTRNASYNTHGA
PF02091\"[9-298]TtRNA-synt_2e
TIGR00388\"[7-301]TglyQ: glycyl-tRNA synthetase, alpha subunit
InterPro
IPR006194
Domain
Heterodimeric glycyl-transfer RNA synthetase
PS50861\"[8-288]TAA_TRNA_LIGASE_II_GLYAB
noIPR
unintegrated
unintegrated
G3DSA:1.20.58.180\"[215-298]Tno description
G3DSA:3.30.930.10\"[5-214]Tno description


","BeTs to 14 clades of COG0752COG name: Glycyl-tRNA synthetase, alpha subunitFunctional Class: JThe phylogenetic pattern of COG0752 is -------qv--lbcefghsnujxi--Number of proteins in this genome belonging to this COG is","","Residues 9 to 295 match (1e-156) PD:PD006985 which is described as SYNTHETASE ALPHA CHAIN LIGASE GLYCYL-TRNA COMPLETE PROTEOME AMINOACYL-TRNA GLYCINE--TRNA GLYRS ","","","","","","","","","","","","Wed Feb 12 10:24:46 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01145 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 9 to 298 (E-value = 2.9e-240) place AA01145 in the tRNA_synt_2e family which is described as Glycyl-tRNA synthetase alpha subunit (PF02091)","","","","","Arnez JG, Dock-Bregeon AC, Moras D. Glycyl-tRNA synthetase uses a negatively charged pit for specificrecognition and activation of glycine. J Mol Biol. 1999 Mar 12;286(5):1449-59. PMID: 10064708 Webster,T.A., Gibson,B.W., Keng,T., Biemann,K. and Schimmel,P. Primary structures of both subunits of Escherichia coliglycyl-tRNA synthetase. J. Biol. Chem. 258(17): 10637-10641 1983. PubMed: 6309809. Keng,T., Webster,T.A., Sauer,R.T. and Schimmel,P. Gene for Escherichia coli glycyl-tRNA synthetase has tandemsubunit coding regions in the same reading frame. J. Biol. Chem. 257(21): 12503-12508. 1982 PubMed: 6290471.","","Fri Dec 20 16:56:15 2002","1","","","" "AA01146","784573","784830","258","ATGAAACCGATTCTTTATTATGCCGAAAAATGCCCTGACACCGCGCCTTTTGTGGCAGAACTGAAACGCTTGAGCGTAGAATATGACGAAGTGGAAGTGATGTCTTCCATCCCGAATTTAAAACAGTGGCTGCGTTTGCGTGATAACAACGCCGCGTTTGATACCGTCAAAGCGAAAGGCAATGCGGGCTTTCCCGCGCTGTTATTGGAAGACGGGCGGGTCATTCTGACAGAAAGCGAACTGCGCGAAATTTTCGCT","","","14595","MKPILYYAEKCPDTAPFVAELKRLSVEYDEVEVMSSIPNLKQWLRLRDNNAAFDTVKAKGNAGFPALLLEDGRVILTESELREIFA","784832","","conserved hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
PD062008\"[3-82]TY926_HAEIN_P44076;


","No hits to the COGs database.","","","","","","","","","","","","","","Fri Dec 20 16:57:36 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01146 is paralogously related to AA01172 (3e-20).","","","","","","","","","","","","","","1","","","" "AA01147","785000","785287","288","ATGAAACCATCACAAAAACTGCGACTTAACCGAGAGAAAGTGAAAGCGCTTTCTGTTCGGTTTCATTTTTCAAATTCGAGAGTATTCGGTTCGGTATTAACGCAGCAAGACACGGAGCAAAGTGATTTAGATTTACTGGTTGAACCCTCCGTGAAAACCACCTTATTTGATTATTGCGGTTTAAAAGAAGAATTAGAAACCTTGCTTGGCGTCAAAGTGGATTTGTTAACACCACGCAGTTTACCTGAAAAATTTAGAGATCATATTTTGCAAACGGCACAATCGATA","","","10986","MKPSQKLRLNREKVKALSVRFHFSNSRVFGSVLTQQDTEQSDLDLLVEPSVKTTLFDYCGLKEELETLLGVKVDLLTPRSLPEKFRDHILQTAQSI","785289","","nucleotidyltransferase","Cytoplasm","","
InterPro
IPR002934
Domain
DNA polymerase, beta-like region
PF01909\"[7-96]TNTP_transf_2


","BeTs to 6 clades of COG1669COG name: Predicted nucleotidyltransferasesFunctional Class: RThe phylogenetic pattern of COG1669 is a-m-----vd---c-----n-j----Number of proteins in this genome belonging to this COG is","","Residues 4 to 78 match (4e-10) PD:PD004242 which is described as PROTEOME COMPLETE PAREP11 NUCLEOTIDYLTRANSFERASE TRANSFERASE DR0248 SLR1241 AF2304 STS014 TM0614 ","","","","","","","","","","","","Tue Feb 18 16:24:49 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01147 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01148","785381","786082","702","ATGCAGAATGATGATTTAGACGAAAATAATACAGATAAACTAATTTCACTTACAAATTCTATTTTAGGAGAATTTCCTGGTGGTTCTATTGTAAGTGGAATTATTAACAAGTTAGTATCAAATCAACGTCAAGACAGAATAACTAAATATATTAGAGAACTAGAAAAAAGAATATCTAATTTAGAATGTTTGATAGGTTCAGAAGCTGAAAAATTATCTAAATATATAGCATTGTTTGAAGATGGTTTATTCTACGCTTTTCGAGCTGCTAGTGAAAAGCGTCTTGAGCATATTGCCTCTATAGTGGCGAATGGATTAAATAAAGAACAAGTACAAATATCTCAATCTATCCATTTACTCAATTTACTATCAGACTTAAATGATGAAGAGATTATTTGGTTAAGATTTTATTTACACCCAACACTGGGTGGTGATGAGGAATTTAGAGATAAACATAAGAGTACCTTAACTCTAGCTAGAAATTATATTGGAGCTTCAGAAGAAGAGGCTAATAAATCTGCTATTCAAGAGAGCTATAAAGAGCATTTAGAAAGATTAGGTTTAATAAAAACTAAATTTAATATAGATAGAAATACGAATATGCCTATTTATGATAAATCATCAGGAAAACCTAAAGGTTCTAGATATATAACTCATTTAGGAAAAATGTTGCTTAAAGAGATTGGTTTTTCTGAAGTACCA","","","26616","MQNDDLDENNTDKLISLTNSILGEFPGGSIVSGIINKLVSNQRQDRITKYIRELEKRISNLECLIGSEAEKLSKYIALFEDGLFYAFRAASEKRLEHIASIVANGLNKEQVQISQSIHLLNLLSDLNDEEIIWLRFYLHPTLGGDEEFRDKHKSTLTLARNYIGASEEEANKSAIQESYKEHLERLGLIKTKFNIDRNTNMPIYDKSSGKPKGSRYITHLGKMLLKEIGFSEVP","786084","","hypothetical protein","Cytoplasm","","
InterPro
IPR005639
Domain
Delta endotoxin, N-terminal
PF03945\"[11-40]TEndotoxin_N


","No hits to the COGs database.","","","","","","","","","","","","","","Fri Dec 20 17:06:03 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01148 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01149","786167","788245","2079","ATGACAACCCAAAACTTCCTAGTAGAAATCGGTACGGAAGAGCTGCCGCCAAAAGCTCTGAAAACATTAGCCACGGCCTTTGCGGATAACGTACAGGCGGAATTGAACCAAGCGGGGCTGGCGTTCGACAAAATCGAATGGTTTGCGGCACCGCGTCGTTTGGCGGTGAAGGTGTTAGCGCTTGCCACACAGCAGCCGGGCAAAGAAATTGAAAAGCGTGGGCCTGCGGTGTCAGCGGCGTTTGATACGGAAGGCAATCCGACCAAAGCGGCAGAAGGCTGGGCGCGTGGTTGCGGGATTACCGTGGATCAAGCGGAACGCCTTGCCACCGACAAAGGCGAATGGCTGGTTCACCGTGCGAAAATCGAGGGTCAGCCGACCAAAAACTTGCTGGCGGATATCGTGGCGAACGCTTTGGCGAAATTGCCAATTCCGAAACCAATGCGTTGGGCGGACAAAACCGTGCAATTCATTCGTCCTGTTCACACGGTGACGATGTTGCTTGGCGATGAATTAATCGAAGGCGAAATTTTAGGCGTGGCAAGCGGTCGCACGATTCGTGGTCACCGTTTCTTAGGCGAGCGTGAATTTGAAATTCAACACGCGGATCAATACCCACAACTGTTGCGTGAAAAAGGATCTGTGGTAGCTGATTTCAACGAGCGTAAAGCGGAAATTTTGGCAAAATCTCAAGCAAAAGCGACCGCACTTGGCGGTGTGGCAGACATTGAAGAAAGCCTGTTGGAAGAAGTGACTTCATTGGTGGAATACCCGAATGTGTTGGCGGCGAAATTTGAAGAACGTTTCCTTGCCGTGCCTGCGGAAGCCTTGGTTTACACCATGAAAGGCGACCAAAAATACTTCCCGCTATACAAAAAAACAGAAGGCGACAAAGACGGCAAATTATTACCGCACTTTATCTTCGTATCGAACATCAACCCTGATGATCCAAGTGCGATTATCGAAGGCAACGAAAAAGTGGTTCGCCCTCGTTTAACCGACGCGGAATTCTTCTCCAAAACCGACTTAAAACAAAAATTAGTGGATCGCTTACCGCGCTTGGAAACTGTGTTGTTCCAACAACAACTTGGCACATTGCGTGATAAAACCGACCGCATCGAACAACTTGCGGGTGCAATCGCCAAACAAATCGGTGCCGACGAAGCGAAAGCAAAACGTGCGGGCTTGCTGTCAAAATGCGATTTGATGACCAATATGGTGTTTGAATTCACCGACACCCAAGGCGTAATGGGTATGCACTATGCCCGTCACGACGGCGAAGATGAAGAAGTGGCAGTGGCGTTGAATGAACAATATATGCCGCGTTTCGCAGGGGATGAATTGCCGAAATCGTTGGTGGCAAGTGCGGTGGCATTAGCCGATAAATTCGACACCCTCACAGGAATTTTGGGGATCGGACAAGCGCCGAAAGGCAGTGCCGACCCATTCGCTTTACGCCGTGCCGCATTGGGCGCGTTACGCATTATTGTTGAGAAAAACCTACCGCTTGATTTGGAAGATTTAGTGCAAAAATCAGCCGCACTTTTCGGCGATAAACTCACCAACAAAAATGTGGTTGCCGACGTGGTGGACTTTATGCTCGGTCGTTTCCGTGCGTGGTATCAAGACGAAGGCATTGCGGTGGACGTCATCCAAGCCGTGCTTGCCCGTCGCCCAACCCGCCCTGCGGATTTTGACGCCCGCGTGCGTGCCGTATCGCATTTCCGCACCTTAGATTCTGCAGAAGCCTTAGCCGCAGCAAACAAACGCGTGGCGAACATTCTTGCCAAAGCAGATGTTGCAATCGGTGAGATTAATTTGATCGCCTGCGTTGAGTCGGCAGAAAAAAACCTCGCCGAAGCCGTGCTTGTGTTACAAACGGAAGTGCAACCACTTATCGCGAAAGGCGAATACACCGCCGTGTTGGATAAACTCGCGAACTTACGTACTCCGGTGGATAACTTCTTCGACAACGTGATGGTGAACGCAGAAGATCCAACACTCCGCCAAAACCGCTTGGCGATTTTGAATACGCTACAAGGTTTATTCTTACAGGTGGCGGATATTTCGTTGTTGCAA","","","78986","MTTQNFLVEIGTEELPPKALKTLATAFADNVQAELNQAGLAFDKIEWFAAPRRLAVKVLALATQQPGKEIEKRGPAVSAAFDTEGNPTKAAEGWARGCGITVDQAERLATDKGEWLVHRAKIEGQPTKNLLADIVANALAKLPIPKPMRWADKTVQFIRPVHTVTMLLGDELIEGEILGVASGRTIRGHRFLGEREFEIQHADQYPQLLREKGSVVADFNERKAEILAKSQAKATALGGVADIEESLLEEVTSLVEYPNVLAAKFEERFLAVPAEALVYTMKGDQKYFPLYKKTEGDKDGKLLPHFIFVSNINPDDPSAIIEGNEKVVRPRLTDAEFFSKTDLKQKLVDRLPRLETVLFQQQLGTLRDKTDRIEQLAGAIAKQIGADEAKAKRAGLLSKCDLMTNMVFEFTDTQGVMGMHYARHDGEDEEVAVALNEQYMPRFAGDELPKSLVASAVALADKFDTLTGILGIGQAPKGSADPFALRRAALGALRIIVEKNLPLDLEDLVQKSAALFGDKLTNKNVVADVVDFMLGRFRAWYQDEGIAVDVIQAVLARRPTRPADFDARVRAVSHFRTLDSAEALAAANKRVANILAKADVAIGEINLIACVESAEKNLAEAVLVLQTEVQPLIAKGEYTAVLDKLANLRTPVDNFFDNVMVNAEDPTLRQNRLAILNTLQGLFLQVADISLLQ","788247","","glycyl-tRNA synthetase beta subunit","Cytoplasm","","
InterPro
IPR002311
Domain
Glycyl-tRNA synthetase, beta subunit
PR01045\"[7-20]T\"[50-62]T\"[246-261]T\"[323-339]T\"[399-418]TTRNASYNTHGB
PF02092\"[6-561]TtRNA_synt_2f
TIGR00211\"[1-693]TglyS: glycyl-tRNA synthetase, beta subunit
InterPro
IPR006194
Domain
Heterodimeric glycyl-transfer RNA synthetase
PS50861\"[368-657]TAA_TRNA_LIGASE_II_GLYAB
InterPro
IPR008909
Domain
DALR anticodon binding
PF05746\"[584-676]TDALR_1


","BeTs to 14 clades of COG0751COG name: Glycyl-tRNA synthetase, beta subunitFunctional Class: JThe phylogenetic pattern of COG0751 is -------qv--lbcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 8.5e-51) to 5/5 blocks of the PR01045 family, which is described as \"Glycyl-tRNA synthetase beta subunit signature\". Prints database entry for PR:PR01045. PR01045A 7-20 9e-08 PR01045B 50-62 0.00098 PR01045C 246-261 2e-07 PR01045D 323-339 1.5e-09 PR01045E 399-418 4e-16","Residues 524 to 692 match (2e-12) PD:PD351074 which is described as AMINOACYL-TRNA PROTEOME SUBUNIT BETA SYNTHETASE COMPLETE SYNTHETASE GLYCYL-TRNA ","","","","","","","","","","","","Fri Dec 20 17:08:12 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01149 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 584 to 679 (E-value = 2e-05) place AA01149 in the tRNA-synt_1d_C family which is described as DALR anticodon binding domain (PF05746)","","","","","Arnez JG, Dock-Bregeon AC, Moras D. Glycyl-tRNA synthetase uses a negatively charged pit forspecific recognition and activation of glycine. J Mol Biol. 1999 Mar 12;286(5):1449-59. PMID: 10064708 Webster,T.A., Gibson,B.W., Keng,T., Biemann,K. and Schimmel,P. Primary structures of both subunits of Escherichia coliglycyl-tRNA synthetase. J. Biol. Chem. 258(17): 10637-10641 1983. PubMed: 6309809. Keng,T., Webster,T.A., Sauer,R.T. and Schimmel,P. Gene for Escherichia coli glycyl-tRNA synthetase has tandemsubunit coding regions in the same reading frame. J. Biol. Chem. 257(21): 12503-12508. 1982 PubMed: 6290471.","","Fri Dec 20 17:08:12 2002","1","","","" "AA01151","789482","788463","1020","ATGACGCAACAAATTTTCACCGGTTTTCCCACCCGCCGTTTACGCCGCATGCGTAAACAGGACTTTAGTCGCCGCTTGATGGCGGAACACAAACTGACCGTTGACGATCTGATTTATCCCGTGTTTATTATTGAAGGCGAAAATCACCGCGAAGCCGTGCCTTCCATGCCGAATGTAGAACGTTTAACCCTTGATCAGTTGTTAATTGAAGCGGGATTATTGGTGAAATACGGTGTGCCGGTCATCGCCCTGTTCCCTGTGGTGGAGCAAACCAAAAAATCCCTCATGGCGGAAGAAGCCTATAATCCGAACGGCTTGGTGCAACGCGCGGTAAGAGCCTTAAAAGCCGCTTATCCCGAACTGGGCGTATTAACCGATGTGGCACTTGACCCTTACACCGTGCACGGGCAAGACGGCATTATCGACGAGGACAGCTATGTACTGAACGACATCACCACCGAAGTGTTAATCAAACAAGCCCTTTCCCACGCGGAAGCCGGCGCCGATGTGGTAGCGCCAAGCGACATGATGGACGGTCGAATCGGCAGAATCCGCCACGCGCTGGAAGAAAACGGCTTTATCAATACCCTCATCATGGCATACTCCGCCAAATATGCCTCCAACTATTACGGCCCGTTCCGCGACGCGGTGGGTTCTTCCGGTAATTTAAAAGGTGGCGATAAAAAAACCTATCAACTTGATCCCGCCAATAGCGACGAAGGCTTGCAGGAAGTGGCGTTAGACTTGGAAGAAGGCGCCGATATGGTGATGGTCAAACCGGGCATGCCGTATTTGGATTTGGTCTATCGCGTGAAACAACAATTCGGCGTGCCGACCTTCGCCTACCAAGTCTCCGGCGAATACGCCATGCACATGGCAGCCATTCAAAACGGTTGGCTGAAAGAAAAAGAGTGCATCATGGAATCGCTACTTTGCTTCAAACGCGCCGGCGCCGACGGCATTCTGACTTACTTCGCCAAACAAGTGGCGGAATGGTTGTACTTGGAAGGGAAAAATAAA","","","37986","MTQQIFTGFPTRRLRRMRKQDFSRRLMAEHKLTVDDLIYPVFIIEGENHREAVPSMPNVERLTLDQLLIEAGLLVKYGVPVIALFPVVEQTKKSLMAEEAYNPNGLVQRAVRALKAAYPELGVLTDVALDPYTVHGQDGIIDEDSYVLNDITTEVLIKQALSHAEAGADVVAPSDMMDGRIGRIRHALEENGFINTLIMAYSAKYASNYYGPFRDAVGSSGNLKGGDKKTYQLDPANSDEGLQEVALDLEEGADMVMVKPGMPYLDLVYRVKQQFGVPTFAYQVSGEYAMHMAAIQNGWLKEKECIMESLLCFKRAGADGILTYFAKQVAEWLYLEGKNK","788465","","porphobilinogen synthase (delta-aminolevulinic acid dehydratase)","Cytoplasm","","
InterPro
IPR001731
Family
Tetrapyrrole biosynthesis, porphobilinogen synthase
PD002304\"[9-333]THEM2_PSEAE_Q59643;
PR00144\"[129-143]T\"[160-179]T\"[198-217]T\"[252-268]T\"[277-292]T\"[307-326]TDALDHYDRTASE
PIRSF001415\"[12-336]TPorphobilinogen synthase
PTHR11458\"[13-337]TPORPHOBILINOGEN SYNTHASE
PF00490\"[9-333]TALAD
PS00169\"[252-264]TD_ALA_DEHYDRATASE
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[9-337]Tno description


","No hits to the COGs database.","Significant hit (3.5e-157) to 6/6 blocks of the IPB001731 family, which is described as \"Delta-aminolevulinic acid dehydratase\". Interpro entry for IP:IPR001731. IPB001731A 13-45 2.7e-16 IPB001731B 53-88 3.8e-14 IPB001731C 119-141 6.6e-14 IPB001731D 147-201 2.2e-39 IPB001731E 226-278 2.3e-38 IPB001731F 288-326 2.4e-29","Residues 10 to 333 match (8e-163) PD:PD002304 which is described as DELTA-AMINOLEVULINIC ACID BIOSYNTHESIS DEHYDRATASE SYNTHASE PORPHOBILINOGEN LYASE PORPHYRIN ALADH PROTEOME ","","","","","Tue Feb 18 15:46:50 2003","","","","","","","Fri Dec 20 17:11:01 2002","","Wed Sep 29 17:36:08 2004","Wed Sep 29 17:36:08 2004","Wed Sep 29 17:36:08 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01151 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Sep 29 17:36:08 2004","","","","","Residues 9 to 333 (E-value = 2.8e-194) place AA01151 in the ALAD family which is described as Delta-aminolevulinic acid dehydratase (PF00490)","Wed Sep 29 17:36:08 2004","","","","Vaudaux P, Francois P, Bisognano C, Kelley WL, Lew DP, Schrenzel J, Proctor RA, McNamara PJ, Peters G, Von Eiff C.Increased expression of clumping factor and fibronectin-binding proteins by hemB mutants of Staphylococcus aureus expressing small colony variant phenotypes.Infect Immun. 2002 Oct;70(10):5428-37.PMID: 1222826von Eiff C, Proctor RA, Peters G.Small colony variants of Staphylococci: a link to persistent infections.Berl Munch Tierarztl Wochenschr. 2000 Sep;113(9):321-5. Review.PMID: 11042943Koyama M, Katayama S, Kaji M, Taniguchi Y, Matsushita O, Minami J,Morita S, Okabe A.A Clostridium perfringens hem gene cluster contains a cysG(B) homologue that is involved in cobalamin biosynthesis.Microbiol Immunol. 1999;43(10):947-57.PMID: 10585141Gudmundsdottir K, Sigurdsson E, Thorbjarnardottir SI, Eggertsson G.Cloning and sequence analysis of the hemB gene of Rhodothermus marinus.Curr Microbiol. 1999 Aug;39(2):103-5.PMID: 10398836 Stumpfle P, Broll H, Beutin L.Absence of DNA sequence homology with genes of the Escherichia coli hemB locus in Shiga-toxin producing E. coli (STEC) O157 strains.FEMS Microbiol Lett. 1999 May 1;174(1):97-103.PMID: 10234826","","Tue Feb 18 15:46:50 2003","1","","","" "AA01152","790265","789504","762","ATGACCAGCGTTGACGATACTCAACCCCTCATCACTCACTTGGTAGAACTACGCACTCGCTTATTACGCAGCATTATTTTCGTCGCCGTGGTGTTTGTTGCACTAGTTTACTTTTCTAACGAAATTTATAATTTTGTGGCGGCACCGCTGACAGCGAACCTGCCGAACGGTTCCAGCATGATTGCCACCAACATCGCCACGCCGTTTTTTACCCCGATTAAACTCACCGGTGTGGTTGCCGTTTTTATTTCCGTGCCTTATTTGCTTTATCAAATCTGGGCGTTTGTAGCGCCGGCATTATATCAACATGAAAAACGCCTGATTTATCCGCTGCTCTTTTCCAGCACCGTGCTTTTTTATTTAGGCGTGGCATTTGCTTATTATGTGGTGTTCCCGCTGGTGTTCAGTTTCCTAACCAAGACCGCGCCGGAAGGCGTCGCTATTGCCACGGACATCAGCAGTTATCTGGATTTCGTGCTCACCCTGTTCCTCGCTTTCGGCGTTTGTTTTGAAGTGCCGGTGGCGATTATTTTACTGTGCTGGACGGGTGTGACTACACCGGAAGATTTAAGATCCAAACGTCCGTATATTATCGTAGCCGCTTTCTTTATCGGTATGCTTCTGACTCCGCCGGACGTATTTTCACAAACCTTACTCGCTGCCCCGATGTGCTTGTTATTTGAAGTGGGTGTGCTATGCGCCCGTTTCTACCGTCCACGCGAAGATGACGAGACGCAAAATGAAAGCGACAGCGCAAAGCAA","","","28333","MTSVDDTQPLITHLVELRTRLLRSIIFVAVVFVALVYFSNEIYNFVAAPLTANLPNGSSMIATNIATPFFTPIKLTGVVAVFISVPYLLYQIWAFVAPALYQHEKRLIYPLLFSSTVLFYLGVAFAYYVVFPLVFSFLTKTAPEGVAIATDISSYLDFVLTLFLAFGVCFEVPVAIILLCWTGVTTPEDLRSKRPYIIVAAFFIGMLLTPPDVFSQTLLAAPMCLLFEVGVLCARFYRPREDDETQNESDSAKQ","789506","","sec-independent protein translocase protein","Inner membrane, Cytoplasm","","
InterPro
IPR002033
Family
Sec-independent periplasmic protein translocase
PR01840\"[9-36]T\"[86-104]T\"[104-130]T\"[155-183]TTATCFAMILY
PF00902\"[19-222]TTatC
TIGR00945\"[10-227]TtatC: twin arginine-targeting protein trans
PS01218\"[155-174]TTATC
noIPR
unintegrated
unintegrated
signalp\"[1-35]?signal-peptide
tmhmm\"[21-39]?\"[70-90]?\"[111-131]?\"[161-181]?\"[196-214]?transmembrane_regions


","BeTs to 18 clades of COG0805COG name: Sec-independent protein secretion pathway component TatCFunctional Class: NThe phylogenetic pattern of COG0805 is ao-p-z-q-dr-bcefghsnujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-77) to 4/4 blocks of the IPB002033 family, which is described as \"Uncharacterized protein family UPF0032\". Interpro entry for IP:IPR002033. IPB002033A 10-22 0.00015 IPB002033B 86-132 4.6e-32 IPB002033C 155-186 5.1e-20 IPB002033D 202-231 3.6e-17","Residues 170 to 231 match (4e-19) PD:PD597269 which is described as COMPLETE PROTEOME TRANSMEMBRANE TATC SEC-INDEPENDENT TRANSLOCASE MEMBRANE INNER TRANSLOCATION MTTB ","","","","","","","","","","","","Mon Jan 6 08:38:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01152 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 19 to 222 (E-value = 1.8e-94) place AA01152 in the TatC family which is described as Sec-independent protein translocase protein (TatC) (PF00902)","","","","","Weiner,J.H., Bilous,P.T., Shaw,G.M., Lubitz,S.P., Frost,L., Thomas,G.H., Cole,J.A. and Turner,R.J. A novel and ubiquitous system for membrane targeting andsecretion of cofactor-containing proteins Cell. 93 (1), 93-101 (1998) PubMed: 9546395 Bogsch,E.G., Sargent,F., Stanley,N.R., Berks,B.C.,Robinson,C. and Palmer,T. An essential component of a novel bacterial protein exportsystem with homologues in plastids and mitochondria The Journal of biological chemistry. 273 (29), 18003-18006(1998) PubMed: 9660752 Berks,B.C., Sargent,F. and Palmer,T. The Tat protein export pathway Molecular microbiology. 35 (2), 260-274 (2000) PubMed: 10652088 ","","Mon Jan 6 08:38:24 2003","1","","","" "AA01153","790965","790306","660","ATGTTTGATATTGGCTTTTCCGAAATCGTATTGGTGTGCATTGTGGGCTTAGTGGTGCTAGGCCCACAACGTTTACCGGTGGCGATTCGCACCGTGATGAGCTGGGTGCGTACCATTCGTGGCTTGGCGGCGAACGTGCAAAACGAGCTGAAACAGGAACTCAAATTGCAGGAATTGCAAGAAAGTATCAAAAAAGCGGAAAGCCTGAACCTGAAAGCCTTGTCACCGGAATTGGGTAACACCGTTGAAGAACTGAAAGCCTCCGCCGATAAATTGCGTGCCGAGTTGGAGCAAAAAGACAACGACACCAACACCACTTTTCAGGATCAGGTGGTTCAACTGAAACAGGCGCAGGCAACGAAAAGTGCGGTGGAAAACGGCGGTGAAAATGACAACCTTCATCCTGGCACAGACCAATACAACCCAATGGCTAATTACGATATTCTTGATGTGGAAGATTATGCCGAGCCACAAACGGAAGCCCTCGCTGCCACAAAAACAACGGAAAAAACGACCGCACTTTCCCCGGCGGAGCTGGCGGAACAGGAAGAAATCGAACTGGACGAAAAACTCGCCCATTACATCAATCAATACGATCCGGACAATCCGCTGCCGGCTAATACGGCATCGGCACATTTGGCCAAAGTCTCAGAGAAAAGT","","","24228","MFDIGFSEIVLVCIVGLVVLGPQRLPVAIRTVMSWVRTIRGLAANVQNELKQELKLQELQESIKKAESLNLKALSPELGNTVEELKASADKLRAELEQKDNDTNTTFQDQVVQLKQAQATKSAVENGGENDNLHPGTDQYNPMANYDILDVEDYAEPQTEALAATKTTEKTTALSPAELAEQEEIELDEKLAHYINQYDPDNPLPANTASAHLAKVSEKS","790308","","sec-independent protein translocase","Inner membrane, Cytoplasm","","
InterPro
IPR003998
Family
Twin-arginine translocation protein TatB
PR01506\"[1-21]T\"[21-40]T\"[40-58]T\"[68-88]TTATBPROTEIN
TIGR01410\"[2-81]TtatB: twin arginine-targeting protein trans
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide


","BeTs to 4 clades of COG1826COG name: Sec-independent protein secretion pathway componentsFunctional Class: NThe phylogenetic pattern of COG1826 is ao-p-z-q-dr-bcefghsnujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 3.1e-49) to 4/4 blocks of the PR01506 family, which is described as \"Bacterial sec-independent translocation TatB protein signature\". Prints database entry for PR:PR01506. PR01506A 1-21 2.1e-14 PR01506B 21-40 8.5e-13 PR01506C 40-58 4.5e-11 PR01506D 68-88 1.7e-06","","","","","","","","","","","","","Mon Jan 6 08:43:52 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01153 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Porcelli I, de Leeuw E, Wallis R, van den Brink-van der Laan E, de Kruijff B, Wallace BA, Palmer T, Berks BC.Characterization and membrane assembly of the TatA component of the Escherichia coli twin-arginine protein transport system.Biochemistry. 2002 Nov 19;41(46):13690-7.PMID: 12427031 Lee PA, Buchanan G, Stanley NR, Berks BC, Palmer T.Truncation analysis of TatA and TatB defines the minimal functional units required for protein translocation.J Bacteriol. 2002 Nov;184(21):5871-9.PMID: 12374820 de Leeuw E, Granjon T, Porcelli I, Alami M, Carr SB, Muller M, Sargent F, Palmer T, Berks BC.Oligomeric properties and signal peptide binding by Escherichia coli Tat protein transport complexes.J Mol Biol. 2002 Oct 4;322(5):1135-46.PMID: 12367533","","Mon Jan 6 08:43:52 2003","1","","","" "AA01154","791193","790972","222","ATGGGCGGCATTAGCATTTGGCAATTAGCGATTTTGGTCTTAATTATCGTGTTGCTGTTCGGTACGAAAAAATTGCGCACCTTGGGCACGGACTTAGGTGAGTCTGTGAAAGGCTTCAAAAAAGCCATGAACGAAGAAAATAAACCGGAAGATGCGACGTTTAGTAAAGTAGAACAAAACGCACAACCGGAACAAGAAAAAAATAAAGAGAAAGAACAGGCT","","","8243","MGGISIWQLAILVLIIVLLFGTKKLRTLGTDLGESVKGFKKAMNEENKPEDATFSKVEQNAQPEQEKNKEKEQA","790974","","sec-independent protein translocase protein","Inner membrane, Cytoplasm","","
InterPro
IPR003369
Family
Bacterial sec-independent translocation protein mttA/Hcf106
PF02416\"[4-71]TMttA_Hcf106
InterPro
IPR006312
Family
Twin-arginine translocation protein TatA/E
TIGR01411\"[3-49]TtatAE: twin arginine-targeting protein tran
noIPR
unintegrated
unintegrated
signalp\"[1-29]?signal-peptide
tmhmm\"[4-22]?transmembrane_regions


","BeTs to 14 clades of COG1826COG name: Sec-independent protein secretion pathway componentsFunctional Class: NThe phylogenetic pattern of COG1826 is ao-p-z-q-dr-bcefghsnujx---Number of proteins in this genome belonging to this COG is","","Residues 3 to 51 match (1e-08) PD:PD005534 which is described as PROTEOME COMPLETE TRANSLOCASE SEC-INDEPENDENT TRANSMEMBRANE TRANSLOCATION TATA/E INNER MEMBRANE HOMOLOG ","","","","","","","","","","","","Mon Jan 6 08:59:02 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01154 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 71 (E-value = 1.9e-10) place AA01154 in the MttA_Hcf106 family which is described as mttA/Hcf106 family (PF02416)","","","","","Porcelli I, de Leeuw E, Wallis R, van den Brink-van der Laan E, de Kruijff B, Wallace BA, Palmer T, Berks BC. Characterization and membrane assembly of the TatA component of the Escherichia coli twin-arginine protein transport system.Biochemistry. 2002 Nov 19;41(46):13690-7.PMID: 12427031 Lee PA, Buchanan G, Stanley NR, Berks BC, Palmer T.Truncation analysis of TatA and TatB defines the minimal functional units required for protein translocation.J Bacteriol. 2002 Nov;184(21):5871-9.PMID: 12374820 de Leeuw E, Granjon T, Porcelli I, Alami M, Carr SB, Muller M, Sargent F, Palmer T, Berks BC.Oligomeric properties and signal peptide binding by Escherichia coli Tat protein transport complexes.J Mol Biol. 2002 Oct 4;322(5):1135-46.PMID: 12367533 Sargent,F., Bogsch,E.G., Stanley,N.R., Wexler,M.,Robinson,C., Berks,B.C. and Palmer,T. Overlapping functions of components of a bacterial Sec-independent protein export pathway EMBO J. 17 (13), 3640-3650 (1998) PubMed: 9649434 ","","Mon Jan 6 08:59:02 2003","1","","","" "AA01155","791471","791367","105","ATGGATGTGTTACAACAGCGTGTCATCGGTGCCGTAGCATCTTTTTCTATCTTGCGGCAGCCGGACTGGGTAAGTGCGGTGCTTTTTTCACTTGCTTTTGTGATT","","","3860","MDVLQQRVIGAVASFSILRQPDWVSAVLFSLAFVI","791367","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 11:14:32 2004","Wed Feb 25 11:14:32 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01155 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 11:14:32 2004","","","","","","","","","","","","","1","","","" "AA01156","792468","791599","870","ATGACAAATTATACTCAAGGCAATGACCAACTTTATCGCTACCTGTTCAAAGATCGCGCCGTGCGTGGCGAATGGGTGCGTTTAAATCAAACTTTCAACGATACCTTAAACACCCATCATTATCCCCAAGCGGTACGCAACTTACTGGGCGAAATGATGGTCGCCACCGCCTTACTCACCGCCATCTTAAAATTTAACGGCGACATCACCGTGCAAATTCAGGGCGACGGTCCGTTAAAATTGGCGCTTGTAAATGGCAATAACCAACAACAAATCCGCGCCCTTGCCCGCTTACAAGGCGACATTGACAACAGCATGAGCCTGCATCAAATGATCGGCAAAGGCGTATTGGTGATTACTATTGCACGAAAAGAAGGCGAACGTTATCAAGGCATTGTACCGTTGGACAAACCGACTATCAGCGAATGTTTGGAAGATTATTTCATGCGCTCCGAACAGCTACAAACCCAGCTCATCATTCGCACCGGCGAATATGACGGCAGACCGGTCAGCGCGGGCGTGTTGTTGCAAATCGTGCCGGACGGTTCCGGTTCACCGGAAGATTTCGAACATTTGGCAACGCTAACGGCAACCATTAAAGAAGAAGAAATTTTCGGTTTAACGGCGGAAGAATTGTTATACCGTTTATATCACGAAGAAAGCGTGGAACTCTTCCCGCCACAAGCGGTAAGTTTTCACTGCGGTTGCTCGCAAGAACGCTCCGGCGCCGCGCTGTTATTGATTTCCGAAGGAGAAATCGAACAAATTCTGGCAGAACACCAAGGCACCATCGATATGCAATGCGAATGCTGCGGCACTCATTATTTGTTCAATAAAGAGGCGATTGAGAAGTTGAAGCAATCGGCTTCT","","","33671","MTNYTQGNDQLYRYLFKDRAVRGEWVRLNQTFNDTLNTHHYPQAVRNLLGEMMVATALLTAILKFNGDITVQIQGDGPLKLALVNGNNQQQIRALARLQGDIDNSMSLHQMIGKGVLVITIARKEGERYQGIVPLDKPTISECLEDYFMRSEQLQTQLIIRTGEYDGRPVSAGVLLQIVPDGSGSPEDFEHLATLTATIKEEEIFGLTAEELLYRLYHEESVELFPPQAVSFHCGCSQERSGAALLLISEGEIEQILAEHQGTIDMQCECCGTHYLFNKEAIEKLKQSAS","791601","","chaperonin heat shock protein 33 homolog","Cytoplasm","","
InterPro
IPR000397
Family
Hsp33 protein
PF01430\"[8-279]THSP33
noIPR
unintegrated
unintegrated
G3DSA:3.55.30.10\"[8-233]Tno description
G3DSA:3.90.1280.10\"[234-287]Tno description


","BeTs to 11 clades of COG1281COG name: Disulfide bond chaperones of the HSP33 familyFunctional Class: OThe phylogenetic pattern of COG1281 is -------qvd-lbcefghsn-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 6.5e-82) to 5/5 blocks of the IPB000397 family, which is described as \"Hsp33 protein\". Interpro entry for IP:IPR000397. IPB000397A 21-63 4.5e-23 IPB000397B 69-88 1.6e-10 IPB000397C 117-162 7.1e-26 IPB000397D 230-260 1.9e-13 IPB000397E 268-275 0.0014","Residues 9 to 283 match (8e-07) PD:PD571480 which is described as MT4 ","","","","","","","","","","","","Mon Jan 6 09:09:25 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01156 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 279 (E-value = 2.9e-126) place AA01156 in the HSP33 family which is described as Hsp33 protein (PF01430)","","","","","Secondary Laboratory Evidence:Jakob,U., Muse,W., Eser,M. and Bardwell,J.C. Chaperone activity with a redox switch Cell 96 (3), 341-352 (1999) PubMed: 10025400 Barbirz,S., Jakob,U. and Glocker,M.O. Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone J. Biol. Chem. 275 (25), 18759-18766 (2000) PubMed: 10764757 Graumann J, Lilie H, Tang X, Tucker KA, Hoffmann JH,Vijayalakshmi J, Saper M, Bardwell JC, Jakob U. Activation of the redox-regulated molecular chaperoneHsp33--a two-step mechanism. Structure (Camb). 2001 May 9;9(5):377-87. PubMed: NOT_FOUND Vijayalakshmi J, Mukhergee MK, Graumann J, Jakob U, Saper MA.The 2.2 A crystal structure of Hsp33: a heat shock proteinwith redox-regulated chaperone activity. Structure (Camb). 2001 May 9;9(5):367-75. PubMed: NOT_FOUND ","","Mon Jan 6 09:11:15 2003","1","","","" "AA01158","792952","792539","414","ATGGCAAAACATCAGCAAACAACCGATGAAAAAGACGCAGTTCGCTTAGACAAATGGCTGTGGGCAGCGCGTTTTTATAAAACCCGTACCCTCGCCAAAGAGATGATTGACGGCGGCAAAGTGCATTACAACGGTCAACGCAGCAAACCGAATAAAATCGTGGAAGTGGGCGCAACCTTAAAATTACGTCAAGGCAGCGAAGAAAGAGAAATCACGGTGCTGGCGTTATCCACCCAACGACGCGGCGCAGCGGAAGCGCAGCTGCTCTATCGTGAAACAGAACAAAGTGTTGCCAACCGCGAAAAACTCGCTATGGCTCGCAAAATGAATGCCCTTTCCATGCCCCACCCCGATCGCCGTCCCGATAAAAAAGAACGCCGCGATCTGCTTAAATTCAAACACCGCAACCAAGAA","","","16110","MAKHQQTTDEKDAVRLDKWLWAARFYKTRTLAKEMIDGGKVHYNGQRSKPNKIVEVGATLKLRQGSEEREITVLALSTQRRGAAEAQLLYRETEQSVANREKLAMARKMNALSMPHPDRRPDKKERRDLLKFKHRNQE","792541","From GenBank: [gi:1176867].This protein is involved in the recycling of free 50s ribosomal subunits that still carry a nascent chain, binds RNA more specifically than DNA, binds with very high affinity to the free 50s ribosomal subunit, and does not bind it when it is part of the 70s ribosome.","ribosome associated heat shock protein 15 homolog","Cytoplasm","","
InterPro
IPR002942
Domain
RNA-binding S4
PF01479\"[14-60]TS4
SM00363\"[14-77]TS4
PS50889\"[14-76]TS4
noIPR
unintegrated
unintegrated
G3DSA:3.10.290.10\"[6-113]Tno description


","BeTs to 8 clades of COG1188COG name: Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog)Functional Class: JThe phylogenetic pattern of COG1188 is --------v--lb-efgh-nuj----Number of proteins in this genome belonging to this COG is","","Residues 14 to 115 match (1e-36) PD:PD021159 which is described as COMPLETE PROTEOME HEAT SHOCK RNA-BINDING DNA-BINDING HSP15 PROTEIN HOMOLOG YABO ","","","","","","","","","","","Mon Jan 6 09:50:23 2003","Mon Jan 6 09:46:10 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01158 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 14 to 60 (E-value = 5.3e-12) place AA01158 in the S4 family which is described as S4 domain (PF01479)","","","","","Korber,P., Zander,T., Herschlag,D. and Bardwell,J.C. A new heat shock protein that binds nucleic acids J. Biol. Chem. 274 (1), 249-256 (1999) M:99085016 Korber,P., Stahl,J.M., Nierhaus,K.H. and Bardwell,J.C. Hsp15: a ribosome-associated heat shock protein EMBO J. 19 (4), 741-748 (2000) M:20141199 Staker,B.L., Korber,P., Bardwell,J.C. and Saper,M.A. Structure of Hsp15 reveals a novel RNA-binding motif EMBO J. 19 (4), 749-757 (2000) M:20141200 ","","Mon Jan 6 09:46:10 2003","1","","","" "AA01159","793711","792968","744","TTGTCATCGCCTTCCCTTGTTTTACAAACAGCTGAAATAGCGATACCATACCCCACTATTTTCACAAAGAAAAGGGACTGCAACGGAATGAATAAACAAAAATTTAACTGGCAGGCAATTGAAACCGTAATTCTGGATTTGGACGGCACGCTGATTGATCTTTATTTCGATCACCGCTTCTGGAAAAATATCGTTCCGCAGGCGTATGCCGATAAATTTAAGGTTTCCGTGGAACAAAGCCGCGAGCTGATTCATCGCCGTTATCAACAGCTGAAATTCAGTATGCAATGGTATTGCATTGATTTTTGGGCGGAAAATCTGGATTTGCCGTTGCGCGAACTATTACAACAACAGCGCGACTACATCAAAGTGCGGTCGGATGTTTACCCGTTTTTACAAGCCGCCCACGAACGGCACAAAAAGCTGATTTTGCTCACCGACAGCCACCCGTTCAGTCTGCAGGAAAAGCTAAAACACTGCGATTTAGCACCGCACTTTGATCTGCTGCTGTCCAGCCATCAGTTTAATGCGCCGAAAGTGGAACAATCCCTGTGGCATCGCCTGCAACAGTTCACGCCTTTTGATCCCGGCAGAACCCTATTTATTGACGACACGGAGCCGGTATTAGACAGCGCCAAACAGTTCGGCATCGCTTATACCATCGGCGTGGAAAATCCCGACAGCACCCTGGCGGATAAATCCTTCGCGCGGCATTTCTCCATCAAAAACTACCGCACTTTACTG","","","31310","LSSPSLVLQTAEIAIPYPTIFTKKRDCNGMNKQKFNWQAIETVILDLDGTLIDLYFDHRFWKNIVPQAYADKFKVSVEQSRELIHRRYQQLKFSMQWYCIDFWAENLDLPLRELLQQQRDYIKVRSDVYPFLQAAHERHKKLILLTDSHPFSLQEKLKHCDLAPHFDLLLSSHQFNAPKVEQSLWHRLQQFTPFDPGRTLFIDDTEPVLDSAKQFGIAYTIGVENPDSTLADKSFARHFSIKNYRTLL","792970","","phosphatase","Cytoplasm","","
InterPro
IPR005834
Domain
Haloacid dehalogenase-like hydrolase
PF00702\"[40-225]THydrolase
InterPro
IPR006402
Domain
HAD-superfamily hydrolase, subfamily IA, variant 3
TIGR01509\"[42-222]THAD-SF-IA-v3: HAD-superfamily hydrolase, su
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1000\"[106-248]Tno description


","BeTs to 5 clades of COG1011COG name: Predicted hydrolases of the HAD superfamilyFunctional Class: RThe phylogenetic pattern of COG1011 is -ompk-yqvdrlb-efghsn-j--t-Number of proteins in this genome belonging to this COG is","","Residues 36 to 114 match (2e-24) PD:PD107562 which is described as COMPLETE PROTEOME HYDROLASE PROBABLE YRFG PM1545 YPO0141 PHOSPHATASE ","","","","","","","","","","","","Mon Jan 6 10:00:43 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01159 is paralogously related to AA02446 (8e-06).","","","","","","Residues 40 to 225 (E-value = 1.3e-19) place AA01159 in the Hydrolase family which is described as haloacid dehalogenase-like hydrolase (PF00702)","","","","","","","","1","","","" "AA01160","793705","794250","546","ATGACAACGTTACAAAAACCACAAATTCTAAATATAAAAACCGTAGCAAAATCAACAATTTTTGAAATTCAGTCGGTAGATTTGAAATTCGCCAACGGGGAGCACCGCACTTATGAACGTTTTCGTCCCGGAAAGTATGCGGCGGTGATGGTGGTGGCTATTGACGGCGAGGATTTATTGTTGGTGCGTGAATATGCCGTGGGGACGGAACGTTATGAGCTGGGGTTTGTGAAAGGCAGAATGGACGCGGGGGAAACGCCGGAACAAAGTGCCAATCGGGAATTGCAGGAAGAAATCGGCTTGGCGGCGAAATCCTGGGTGCATTTGCGCACCATTAATATGTCCGTGGGGTTCATGAATAACCCGATGCGCATTTTACTGGCGCAGGATTTTTATCCGAGCAAACTGGAAGGCGACGAGCCGGAACCGTTGGAAATGGTACGCATACCATTGGCTAAAATCGACGATTTGTTAGCGGATCCGGAATTTAATGAAGCGAAAAATCTGACCGCACTTTATCTGGTGAGGGATTATTTACAACGGAAA","","","22342","MTTLQKPQILNIKTVAKSTIFEIQSVDLKFANGEHRTYERFRPGKYAAVMVVAIDGEDLLLVREYAVGTERYELGFVKGRMDAGETPEQSANRELQEEIGLAAKSWVHLRTINMSVGFMNNPMRILLAQDFYPSKLEGDEPEPLEMVRIPLAKIDDLLADPEFNEAKNLTALYLVRDYLQRK","794252","","ADP compounds hydrolase","Cytoplasm","","
InterPro
IPR000086
Domain
NUDIX hydrolase
PR00502\"[74-88]T\"[88-103]TNUDIXFAMILY
G3DSA:3.90.79.10\"[5-179]Tno description
PF00293\"[45-172]TNUDIX
noIPR
unintegrated
unintegrated
PTHR11839\"[34-181]TUDP/ADP-SUGAR PYROPHOSPHATASE
PTHR11839:SF1\"[34-181]TADP-RIBOSE PYROPHOSPHATASE


","BeTs to 20 clades of COG0494COG name: NTP pyrophosphohydrolases including oxidative damage repair enzymesFunctional Class: L,RThe phylogenetic pattern of COG0494 is aomp-zyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 4e-08) to 1/1 blocks of the IPB000086 family, which is described as \"NUDIX hydrolase\". Interpro entry for IP:IPR000086. IPB000086 74-100 4e-08","Residues 5 to 57 match (5e-10) PD:PD403757 which is described as PROTEOME COMPLETE HYDROLASE NTP COMPOUNDS ADP PM1544 PA5176 MAGNESIUM XF0188 ","","","","","","","","","","","","Mon Jan 27 15:44:11 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01160 is paralogously related to AA01085 (1e-04) and AA00204 (2e-04).","","","","","","Residues 45 to 172 (E-value = 1.4e-13) place AA01160 in the NUDIX family which is described as NUDIX domain (PF00293)","","","","","O'Handley,S.F., Frick,D.N., Dunn,C.A. and Bessman,M.J. Orf186 represents a new member of the Nudix hydrolases, activeon adenosine(5')triphospho(5')adenosine, ADP-ribose, and NADH J. Biol. Chem. 273 (6), 3192-3197 (1998) PubMed: 9452430 ","","Mon Jan 27 15:44:11 2003","1","","","" "AA01161","795139","794261","879","ATGGACTACTTAGATCAGCTTATCCGATTATCGGGCATTGAAGGAGAAATCAATATCCTCTGCCGTTTCCGGGGAGACTGGCTGATTCATCACAAGCAGGAACCCAATTTAATCGGCAAATTTCACATTGTGTCACGCGGCGAATGTCAGATTCGGCTGAAAAATCAAACCTGCCATCTAAAACCGGGCGATGTGATCTTCCTGCCTTATGGTGAGGAACATAGCCTTTATCACGGCGCGGGAACAGAAAGCCCGATTACCGAAACCACGCAGGGCGCATTTACATTGCATCGTAACAGCACAAGCGAATCCGATGATTTTGAAATGTTCTGCGGTTATTTCCGTTATCTCAATCTTGCCCAAAACCTACTTTTTAACTTGCCCCATTGGTATCTTTCCAGCAATAACATCGCCATCATGGCGCTACTGGAATTACTGCGCAAAGAAACCGAGGAAAATTTAGGCAGCAAAGTGGTGGTCAACGCGCTATGCAATATTCTCTTTACTTACCTGATCAGAGATTATCTGCAACATCATCAAGTCAACCAAGGCATTCTCGGCGCTTTGCAGGATAAACGTTTAAAAAATGCGGTAAATGCTATGGTGGAAACGCCTAAAAAAAGCTGGAGCATGGAAGCCTTAGCGGAAAGTTGTGCTATGTCGCGTGCCAACTTCATCCGCGCATTCAAACAAAAAATCGGGATTCCGCCCGGTAAATTTCTGACCATCATAAGAATGAATATTGCCGGCGTATTACTGAAAAACACCCAAAAACCCATTTCCGTCATTGCTTCGGAAGTGGGTTATCAATCGGACACGCATTTTACGAAAGTCTTTAAATCCTATTACGGCATTTCCCCGGGGAAATATCGTGCAATG","","","33362","MDYLDQLIRLSGIEGEINILCRFRGDWLIHHKQEPNLIGKFHIVSRGECQIRLKNQTCHLKPGDVIFLPYGEEHSLYHGAGTESPITETTQGAFTLHRNSTSESDDFEMFCGYFRYLNLAQNLLFNLPHWYLSSNNIAIMALLELLRKETEENLGSKVVVNALCNILFTYLIRDYLQHHQVNQGILGALQDKRLKNAVNAMVETPKKSWSMEALAESCAMSRANFIRAFKQKIGIPPGKFLTIIRMNIAGVLLKNTQKPISVIASEVGYQSDTHFTKVFKSYYGISPGKYRAM","794263","","araC-like transcriptional regulator","Cytoplasm","","
InterPro
IPR000005
Domain
Helix-turn-helix, AraC type
PR00032\"[260-275]T\"[275-291]THTHARAC
PF00165\"[196-242]T\"[248-292]THTH_AraC
SM00342\"[208-291]THTH_ARAC
PS01124\"[195-293]THTH_ARAC_FAMILY_2
PS00041\"[193-237]?HTH_ARAC_FAMILY_1
InterPro
IPR003313
Domain
AraC protein, arabinose-binding/dimerisation
PF02311\"[16-178]TAraC_binding
InterPro
IPR012287
Domain
Homeodomain-related
G3DSA:1.10.10.60\"[246-293]Tno description


","BeTs to 11 clades of COG2207COG name: AraC-type DNA-binding domain-containing proteinsFunctional Class: KThe phylogenetic pattern of COG2207 is --------v-rlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 4e-13) to 1/1 blocks of the IPB000005 family, which is described as \"AraC type helix-turn-helix\". Interpro entry for IP:IPR000005. IPB000005 260-291 4e-13 IPB000005 210-241 0.00027Significant hit ( 6.3e-08) to 2/6 blocks of the IPB003313 family, which is described as \"Arac arabinose-binding and dimerisation domain\". Interpro entry for IP:IPR003313. IPB003313E 209-254 3.7 IPB003313F 255-293 5.9e-06","Residues 245 to 291 match (9e-08) PD:PD402035 which is described as COMPLETE PROTEOME TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR ACTIVATOR FAMILY REGULATORY ","","","","","Thu Feb 13 17:38:57 2003","","","","","","","Mon Jan 6 11:56:34 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01161 is paralogously related to AA01394 (8e-53).","","","","","","Residues 248 to 292 (E-value = 3.7e-12) place AA01161 in the HTH_AraC family which is described as Bacterial regulatory helix-turn-helix proteins, araC family (PF00165)","","","","","Rouquette C, Harmon JB, Shafer WM.Induction of the mtrCDE-encoded efflux pump system of Neisseria gonorrhoeae requires MtrA, an AraC-like protein.Mol Microbiol. 1999 Aug;33(3):651-8.PMID: 10417654 Gallegos MT, Michan C, Ramos JLThe XylS/AraC family of regulators.Nucleic Acids Res 1993 Feb 25;21(4):807-10PMID: 8451183Zahrt TC, Deretic V.An essential two-component signal transduction system in Mycobacterium tuberculosis.J Bacteriol. 2000 Jul;182(13):3832-8.PMID: 10851001 ","","Thu Feb 13 17:38:57 2003","1","","","" "AA01162","795836","795213","624","ATGAATGCATTCATTGAATTACTTGCTAAAATTGTTGCACCGATGCAACGCCAATTTATTAATTTTGTACGCATTGCCATTTGTATCGTAATGGTCTGGATTGGTGGCTTAAAAGTCTGTCAATATGAAGCTGACGGCATTGCGCATTTTGTATCTAATAGTCCGTTTTTAAGTTTCTTGTACAAAAACGGATCGAATTTAGTACAAAATGACAAAGGCGAGCTGGTGAAAGAATATACCCTTTATAAAAATCCGGAGGGTAAAATGGTGGTGAAAAATATTGAATGGCATAAAGCGAACGGCACTTACACCGCCTCTTATATTATCGGTGCAATGATTGTAACCATTGGTTTATTAACCTTAGCCGGCATCCGGTCGCCGACATTGGGCTTATTTGGCGGGTTGCTCACGTTCGGGATGTCCATCGTCACTTTGTCGTTCCTTATTTTCACACCGGAGACCTGGGTGCCTAATTTGGGCGGTGATTTACCAACGCCGAATTATGGTTTCCCTTATTTATCTGCGGCAGGGCGGCTGGTTATTAAAGATATCATCATGATGGCAGGAGGATTGGTTGCCGCCGCCGAATGTGCAAATCGGTGGTTAAAGGCGAAACAATCCGTC","","","23241","MNAFIELLAKIVAPMQRQFINFVRIAICIVMVWIGGLKVCQYEADGIAHFVSNSPFLSFLYKNGSNLVQNDKGELVKEYTLYKNPEGKMVVKNIEWHKANGTYTASYIIGAMIVTIGLLTLAGIRSPTLGLFGGLLTFGMSIVTLSFLIFTPETWVPNLGGDLPTPNYGFPYLSAAGRLVIKDIIMMAGGLVAAAECANRWLKAKQSV","795215","","conserved hypothetical protein (possible transmembrane protein)","Inner membrane, Cytoplasm","","
InterPro
IPR007339
Family
Protein of unknown function DUF417
PF04224\"[6-202]TDUF417
noIPR
unintegrated
unintegrated
signalp\"[1-37]?signal-peptide
tmhmm\"[19-37]?\"[103-125]?\"[131-151]?transmembrane_regions


","BeTs to 4 clades of COG3059COG name: Uncharacterized membrane proteinFunctional Class: SThe phylogenetic pattern of COG3059 is --------------e-gh--u-----Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Mon Jan 6 12:10:33 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01162 is paralogously related to AA02594 (9e-05).","","","","","","Residues 6 to 202 (E-value = 3.2e-123) place AA01162 in the DUF417 family which is described as Protein of unknown function, DUF417 (PF04224)","","","","","Chang,Y.F., Ma,D.P., Young,R. and Struck,D.K.Cloning, sequencing and expression of a Pasteurella haemolytica A1gene encoding a PurK-like proteinDNA Seq. 3 (6), 357-367 (1993)PubMed: 8219279","","Mon Jan 6 12:10:01 2003","1","","","" "AA01164","796130","798208","2079","ATGAATCTTGATTGTTTTATAATTTTTTGCCAAGGTATCGTCGTTTTTTATAAAAAATTAATGAATAGGTATGTTATGCAATCGACAAATTTAAAAGAACTGACCTTTCGGGGGATATTGCTTGGGGCGCTGATTACAGTGCTGTTCACTGCATCTAATGTTTATTTAGGTTTAAAAGTGGGAGTAACTTTTGCTTCCTCTATTCCGGCAGCCGTGATTTCCATGGCGGTACTGAAATTCTACAAGGATTCCAGTATTTTAGAAAATAATATGGTGCAAACCCAAGCCTCTTCTGCGGGGACACTTTCTTCCGTGATTTTCGTATTGCCGGGTTTGTTAATGATGGGCTATTGGCAGGATTTTCCGTTTTGGCAAACCATGTTGATTTGTGCGGCGGGCGGTACTTTGGGGGTATTATTTACTATTCCGTTACGTCGTGCCATGGTAGTAAACAGTGATTTGCCTTATCCTGAGGGTGTGGCAGCGGCAGAAATTTTAAAAGCCGGTAATCACACTGATGGTGACAGCGGTGTGAAAGACATTTTTTACGGCGGCGTGCTGGCGAGTATAGTGGCGTTTTTAACCAATGGTCTGCGCGTGATGGCAGATAGCGCCAGCGGCTGGTTCACCGGATTTGGTGGCAAAGCCGTCTTTCAGGTACCGATGGGATTTTCTTTAGCCTTATTGGGCGCGGGTTACTTAATCGGTATCGTGGGTGGGATTGCGATCTTACTGGGTACGTTGTTCGCTTGGGGTTTTGCCGTACCGTTCTTTACTATGTCCGGTGATATGCCGGCTGATGCCACTATTGCGGGCTACGCGATGGACGCATGGAAAACCAAAGTACGCTTTATCGGCGTAGGGACTATCGGTATTGCGGCTATCTGGACCTTATTGATTCTACTAAAACCGATGGTACAAGGTATGGCGCATTCTTTCCGTATGTTGAAGGGACATCAGGCAGAATACGAACATCGTATTGATATTGACCTATCGCCGAAAACCATGATTTATATTTTGATCGCGACTGTTATCTTGATTGTGATTTCTTTACATCACTTTATCGCTGCCGCACCGATTTCACCTGAGTTAACACTCTTATTGGTGGTGGTTTGTACATTCCTTGCAGTTTTTATCGGTTTTTTCATAGCGGCAGCGTCCGGTTACATGGCCGGGCTTGTAGGGGCCTCTTCCAGCCCGATTTCCGGTATCGGGATTATTTCCGTCATCGCGATTTCTTTGGTGTTGGTTTCTATCGGTAATGCATCCGGTTTATTTGAAACCACCGATGGACAGAAATTTTTGACCGCACTGACCTTGTTCACCGCTTCCATCGTGCTCACCACAGCAACCATTTCCAACGACAACCTGCAGGATTTGAAAACCGGCTTGTTGGTGGAAGCCACCCCTTGGCGTCAACAGGTGGCATTGATTATCGGTTGTTTCGTGGGTGCGTTAGTGATTGCACCGGTATTGGAAATTCTATACCACGCTTATGGCTTTACCGGTGCCTTACCGCGCCCGGATATGGATCCGTCACAAGCCTTATCCGCACCGCAAGCCACCCTGATGACCACCATTTCACAAGGGATTTTCTCCAACAAATTGGAATGGACTTACATCTTAACCGGTGTGGGCTTAGGTGCCGTGTTGATTATTATCGACAGTTTCCTGAAAAAAGTGAGTAACAAAACCTTCGCGTTGCCGGTGCTTGCTGTGGGGATTGGTATTTACTTACCGCCTTCTATTAATATGCCGGTGGTATGCGGTGCGGTGTTGGCGTGGTTGATCAACCGTCACATTAATCGCTATGCGGCCCGTACCGGCGATAAGGAGCCGGGCAAGCGGGCAGAACGTTTCGGCACCTTGTTCTCTGCCGGTTTAATCGTAGGCGAAAGCTTGATGGGCGTGGTATTAGCCTTCATTATTGCGGCATCCGTGACCTCCGGCGGTTCTGAAGCGCCATTGGCGTTGAATCTGGAAAATTGGGACACCATCGCCGAGGTGCTGGGTTTAATCGTCTTTGTTCTCGGCATCGTGATTTTCACCTCTCGCGTATTACGTGCAAAAAAATCTGCA","","","73616","MNLDCFIIFCQGIVVFYKKLMNRYVMQSTNLKELTFRGILLGALITVLFTASNVYLGLKVGVTFASSIPAAVISMAVLKFYKDSSILENNMVQTQASSAGTLSSVIFVLPGLLMMGYWQDFPFWQTMLICAAGGTLGVLFTIPLRRAMVVNSDLPYPEGVAAAEILKAGNHTDGDSGVKDIFYGGVLASIVAFLTNGLRVMADSASGWFTGFGGKAVFQVPMGFSLALLGAGYLIGIVGGIAILLGTLFAWGFAVPFFTMSGDMPADATIAGYAMDAWKTKVRFIGVGTIGIAAIWTLLILLKPMVQGMAHSFRMLKGHQAEYEHRIDIDLSPKTMIYILIATVILIVISLHHFIAAAPISPELTLLLVVVCTFLAVFIGFFIAAASGYMAGLVGASSSPISGIGIISVIAISLVLVSIGNASGLFETTDGQKFLTALTLFTASIVLTTATISNDNLQDLKTGLLVEATPWRQQVALIIGCFVGALVIAPVLEILYHAYGFTGALPRPDMDPSQALSAPQATLMTTISQGIFSNKLEWTYILTGVGLGAVLIIIDSFLKKVSNKTFALPVLAVGIGIYLPPSINMPVVCGAVLAWLINRHINRYAARTGDKEPGKRAERFGTLFSAGLIVGESLMGVVLAFIIAASVTSGGSEAPLALNLENWDTIAEVLGLIVFVLGIVIFTSRVLRAKKSA","798210","","conserved hypothetical protein (possible integral membrane protein)","Inner membrane, Cytoplasm","","
InterPro
IPR004813
Family
Oligopeptide transporter OPT superfamily
PF03169\"[33-643]TOPT
TIGR00728\"[20-647]TOPT_sfam: oligopeptide transporters, OPT su
InterPro
IPR004814
Family
Oligopeptide transporter OPT
TIGR00733\"[33-644]TTIGR00733: oligopeptide transporter, OPT fa
noIPR
unintegrated
unintegrated
signalp\"[1-17]?signal-peptide
tmhmm\"[34-52]?\"[58-78]?\"[99-117]?\"[123-143]?\"[181-201]?\"[220-254]?\"[282-302]?\"[335-355]?\"[365-385]?\"[399-419]?\"[434-454]?\"[476-496]?\"[538-558]?\"[577-597]?\"[623-643]?\"[662-682]?transmembrane_regions


","BeTs to 10 clades of COG1297COG name: Uncharacterized membrane proteinFunctional Class: SThe phylogenetic pattern of COG1297 is -o--k-y---r----f-hsnuj----Number of proteins in this genome belonging to this COG is","","Residues 39 to 195 match (9e-09) PD:PD126236 which is described as CLUSTER CPE1278 PROTEOME COMPLETE GENE ","","","","","","","","","","","","Thu Feb 20 08:58:32 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01164 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 33 to 644 (E-value = 4e-107) place AA01164 in the OPT family which is described as OPT oligopeptide transporter protein (PF03169)","","","","","Lubkowitz MA, Hauser L, Breslav M, Naider F, Becker JM.An oligopeptide transport gene from Candida albicans.Microbiology. 1997 Feb;143 ( Pt 2):387-96.PMID: 9043116","","Mon Jan 6 13:29:50 2003","1","","","" "AA01165","798273","798698","426","ATGTCGCCTAATTATCCTTATATTAAAACATTGGTTATATTTCCTCTGCTTGCTCAACTTATCGGCACCATCATCAGCATTTGTGTGGATGACAATACTGACAGTTTTCTCGGCACTGCCGACGTGATCCTTTTTAGTCTGTTATCGACTTTTATCGTGGCAACCGTGCCCGCTTTTTTGATTGCACTGTGGACAAAAATTTATCGCTATACGCGCTATAACATGATGGCGATTGTGTTAATCTCGCTGATTATCGCTTTTTGTTATGGCAACGTAGCTAGCTTTATCTACATGACGTTCTCTCAGCCAAACATGACGTTTGGTATTTGGCTGCGTAGCGGCGGCATTGATATGGCGTTTTTACTGAGTTTCGGCATGGCGTTGTATTCAGTTCTTGTCTTGCCTTTGTTGTTACCGCAAACCAGA","","","15887","MSPNYPYIKTLVIFPLLAQLIGTIISICVDDNTDSFLGTADVILFSLLSTFIVATVPAFLIALWTKIYRYTRYNMMAIVLISLIIAFCYGNVASFIYMTFSQPNMTFGIWLRSGGIDMAFLLSFGMALYSVLVLPLLLPQTR","798700","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[19-142]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-26]?signal-peptide
tmhmm\"[10-28]?\"[42-64]?\"[79-99]?\"[118-138]?transmembrane_regions


","No hits to the COGs database.","","Residues 7 to 118 match (2e-10) PD:PD173886 which is described as PROTEOME TRANSMEMBRANE HI0559.1 COMPLETE ","","","","","","","","","","","","Mon Jan 6 14:15:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01165 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01166","798739","799545","807","ATGCCAATCCTCACGACCCATTTATTGCAGGATGTAATAGAGATCGCCCAACAGGCGGGTGAGCATTTACGTTGCTTTTATCAACGTTCGGTGACAGTTCGAATGAAAGAAGACAACACACCGGTGACCGAAGCGGATTTATTCGTCAGCCAATTTTTAACGGAAAAACTGACCGCACTTACGCCGCAGATTCCGATTCTTTCTGAAGAAAATTGCCATATTCCGCTGACCGAGCGGCAAACCTGGCGTTCTTACTGGTTAATCGATCCCCTGGACGGCACGCAACAATTTATCAATCGCACCGGTCAATTCTCCGTGCTCGTCAGTTTGGTGAAAGATCATCAACCGGTGTTGGGCGTGATTCATGCGCCGATGTTGGGTTCCACCTATTACGCCATGCAGGGTTTCGGTGCGTATAAACACCATGACGGGCAGCACCTTAAATTAGCCTTCCATGATATTCAAGCGGACAATGCCTTGCGTATTGCTGTGGGTTCCGCCGCCGCAGCCGAAAAAGTGCGGTCGATTTTAAATAAGAATTTGGCTTACGAATTTCATATTTGCGGATCCAGCGGGTTAAAAAGCACACTGGTGGCAGACGGCGTATGCGATTGCTACATTCGCTTGGGTTGCACCGGTGAATGGGATACTGCCGCTTCCGAGATTTTACTGGCGGAAATGGGTGGCATTATTTTTGACTTGAATTATCAACCGCTGACTTATAATAAACGGGAATCTTTCGTCAATCCGAATTTTGTCATGGGAATCACGCAGGATTTTCCGTGGGATAAAATCTTTCACTCCAAT","","","32954","MPILTTHLLQDVIEIAQQAGEHLRCFYQRSVTVRMKEDNTPVTEADLFVSQFLTEKLTALTPQIPILSEENCHIPLTERQTWRSYWLIDPLDGTQQFINRTGQFSVLVSLVKDHQPVLGVIHAPMLGSTYYAMQGFGAYKHHDGQHLKLAFHDIQADNALRIAVGSAAAAEKVRSILNKNLAYEFHICGSSGLKSTLVADGVCDCYIRLGCTGEWDTAASEILLAEMGGIIFDLNYQPLTYNKRESFVNPNFVMGITQDFPWDKIFHSN","799547","From GenBank gi|2497351.This protein could help control the pool of 3'-phosphoadenoside 5'-phospohosulfate, or its use in sulfite synthesis.","sulphite synthesis pathway protein","Cytoplasm","","
InterPro
IPR000760
Family
Inositol monophosphatase
PD023420\"[41-98]TInositol_P
PR00378\"[58-74]T\"[81-100]T\"[193-208]T\"[211-229]TINOSPHPHTASE
PTHR20854\"[50-261]TInositol_P
PF00459\"[4-266]TInositol_P
PS00629\"[86-99]TIMP_1
PS00630\"[215-229]TIMP_2
InterPro
IPR006240
Family
3(2),5 -bisphosphate nucleotidase, bacterial
TIGR01331\"[8-256]Tbisphos_cysQ
noIPR
unintegrated
unintegrated
G3DSA:3.30.540.10\"[3-142]TG3DSA:3.30.540.10
G3DSA:3.40.190.80\"[150-254]TG3DSA:3.40.190.80
PTHR20854:SF5\"[50-261]TPTHR20854:SF5
SSF56655\"[5-266]TSSF56655


","BeTs to 10 clades of COG1218COG name: 3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphataseFunctional Class: PThe phylogenetic pattern of COG1218 is ------yq--r--cefghs-ujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.7e-27) to 3/3 blocks of the IPB000760 family, which is described as \"Inositol monophosphatase\". Interpro entry for IP:IPR000760. IPB000760A 40-70 1e-10 IPB000760B 86-97 1.8e-06 IPB000760C 215-233 4.5e-07","Residues 65 to 249 match (2e-08) PD:PD472437 which is described as IPP POLYPHOSPHATE 1-PHOSPHATASE INOSITOL IPPASE LITHIUM HYDROLASE Y6B3B.5 CG15743 MYO-INOSITOL ","","","","","","","","","","","Mon Jan 6 14:41:11 2003","Mon Jan 6 14:25:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01166 is paralogously related to AA00705 (2e-16) and AA02793 (2e-09).","","","","","","Residues 4 to 266 (E-value = 3.5e-78) place AA01166 in the Inositol_P family which is described as Inositol monophosphatase family (PF00459)","","","","Yoshida,Y., Nakano,Y., Yamashita,Y. and Koga,T. The gnd gene encoding a novel 6-phosphogluconate dehydrogenaseand its adjacent region of Actinobacillus actinomycetemcomitanschromosomal DNA Biochem. Biophys. Res. Commun. 230 (1), 220-225 (1997) PubMed: 9020051","Peng Z, Verma DP. A rice HAL2-like gene encodes a Ca(2+)-sensitive3'(2'),5'-diphosphonucleoside 3'(2')-phosphohydrolase andcomplements yeast met22 and Escherichia coli cysQ mutations. J Biol Chem. 1995 Dec 8;270(49):29105-10. PMID: 7493934 Neuwald AF, Krishnan BR, Brikun I, Kulakauskas S, Suziedelis K,Tomcsanyi T, Leyh TS, Berg DE. cysQ, a gene needed for cysteine synthesis in Escherichia coliK-12 only during aerobic growth. J Bacteriol. 1992 Jan;174(2):415-25. PMID: 1729235","Mon Jan 6 14:41:11 2003","Mon Jan 6 14:41:11 2003","1","","","" "AA01167","799571","801127","1557","ATGATTTTACCTATTATACGAAGCAGTTATTTAAACAATGACATCAACATGGTAACAAATCAACATGGTAACAAAATGAAAGCAGAAAACTGTTGTATTGTAATTTTCGGCGCCTCCGGCGATCTCACTTATCGTAAACTTATTCCGGCTTTATATAGCCTCTATAAAATTGATCGACTGGGTGAAGATTTCTCCGTTCTCGGCGTGGCACGTACCGAACTGAATGACAAATCATTCCGTGAGAAAATGCGCCAAACGCTGATCAAAAATGAAGGCGCGAAAGGCGAGTGCTTGGAGCAATTTTGCAGCCACCTGTATTATCAGGCGGTCAATACGGCGGACAAAGCGGATTACGCCAAACTGGTTCCGCGTCTTGACGAACTGCACGACACCTATCGCACCGAAGGCAACACCTTGTATTATCTTTCCACGCCGCCGAGCCTATATGGCGTGATTCCGGAATGTTTGGGCGAACATGGCTTAAATAAAGAAGATCGCGGCTGGAAGCGTCTTATTGTGGAAAAACCGTTCGGTTATGACCGTGAAACCGCCGAAGCGCTGGATATTCAAATTCACCGTTTCTTTGAAGAACATCAAATTTACCGTATCGACCATTATCTTGGTAAAGAAACCGTCCAAAACCTGCTTGTGTTGCGCTTTTCCAACGGTTGGTTTGAGCCGTTGTGGAACCGTAATTTCATTGATTACATTGAAATCACCGGCGCGGAATCTATCGGTGTAGAAGAGCGTGGCGGCTATTATGACGGTTCCGGCGCGATGCGCGATATGTTCCAAAACCATTTATTACAAGTGCTGGCAATGGTGGCGATGGAGCCGCCGGCGATTATCAACGCCAATTCCATGCGTGACGAAGTGGCGAAAGTGCTGCATTGTTTGCGCCCGTTGACCCAGGAAGACGTGGAGCATAATCTGGTGTTGGGACAATATGTCGCAGGCGAAGTGGACGGCGAATGGGTGAAAGGCTATTTAGAGGAAAAAGGCGTGCCGCCGTATTCCACCACCGAAACCTACATGGCGCTACGCTGTGAAATCGAAAACTGGCGTTGGGCGGGCGTGCCTTTCTACGTGCGCACCGGTAAACGTCTGCCGGCACGCGTCACGGAAATCGTGATTCACTTCAAAACCACCCCGCACCCGGTATTCAGCCAAAATGCGCCGGAAAATAAACTGATTATCCGTATTCAACCGGACGAAGGCATTTCTATGCGTTTTGGCTTGAAAAAACCGGGCGCCGGCTTTGAAGCCAAAGAAGTGTCGATGGATTTCCGCTATGCCGATCTTGCGGGTGCCACCGTCATGACCGCTTATGAGCGTTTATTGCTTGATGCCATGAAAGGCGACGCGACCCTATTTGCGCGTACCGATGCCGTACACGCCGCCTGGAAATTCGTTCAACCGATTTTGAACTATAAAGCCCAAGGCGGCAGACTTTATGATTACGAGGCCGGCACCTGGGGACCGACGGCAGCCGATAAACTCATCGCCAAAAGCGGTCGTGTATGGCGCCGCCCAAGCGGGTTGATGAAGAAAAAAGTG","","","59188","MILPIIRSSYLNNDINMVTNQHGNKMKAENCCIVIFGASGDLTYRKLIPALYSLYKIDRLGEDFSVLGVARTELNDKSFREKMRQTLIKNEGAKGECLEQFCSHLYYQAVNTADKADYAKLVPRLDELHDTYRTEGNTLYYLSTPPSLYGVIPECLGEHGLNKEDRGWKRLIVEKPFGYDRETAEALDIQIHRFFEEHQIYRIDHYLGKETVQNLLVLRFSNGWFEPLWNRNFIDYIEITGAESIGVEERGGYYDGSGAMRDMFQNHLLQVLAMVAMEPPAIINANSMRDEVAKVLHCLRPLTQEDVEHNLVLGQYVAGEVDGEWVKGYLEEKGVPPYSTTETYMALRCEIENWRWAGVPFYVRTGKRLPARVTEIVIHFKTTPHPVFSQNAPENKLIIRIQPDEGISMRFGLKKPGAGFEAKEVSMDFRYADLAGATVMTAYERLLLDAMKGDATLFARTDAVHAAWKFVQPILNYKAQGGRLYDYEAGTWGPTAADKLIAKSGRVWRRPSGLMKKKV","801129","","glucose-6-phosphate 1-dehydrogenase","Cytoplasm","","
InterPro
IPR001282
Family
Glucose-6-phosphate dehydrogenase
PD001129\"[326-406]TG6PD_ACTAC_P77809;
PR00079\"[170-183]T\"[194-222]T\"[246-263]T\"[264-280]T\"[355-381]TG6PDHDRGNASE
PIRSF000110\"[31-512]TGlucose-6-phosphate dehydrogenase
PTHR23429\"[76-509]TGLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE (G6PD)
PF00479\"[34-214]TG6PD_N
PF02781\"[216-511]TG6PD_C
TIGR00871\"[29-511]Tzwf: glucose-6-phosphate 1-dehydrogenase
PS00069\"[204-210]TG6P_DEHYDROGENASE
noIPR
unintegrated
unintegrated
G3DSA:3.30.360.10\"[203-512]Tno description
G3DSA:3.40.50.720\"[26-202]Tno description


","BeTs to 16 clades of COG0364COG name: Glucose-6-phosphate 1-dehydrogenaseFunctional Class: GThe phylogenetic pattern of COG0364 is ------yqvdrlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is","Significant hit (1.5e-164) to 8/8 blocks of the IPB001282 family, which is described as \"Glucose-6-phosphate dehydrogenase\". Interpro entry for IP:IPR001282. IPB001282A 33-50 1.7e-10 IPB001282B 137-149 1.4e-05 IPB001282C 203-230 7.9e-24 IPB001282D 234-280 2.5e-35 IPB001282E 328-381 2.3e-40 IPB001282F 395-417 1.8e-13 IPB001282G 440-475 2.7e-22 IPB001282H 487-497 0.00019","Residues 443 to 511 match (1e-08) PD:PD587279 which is described as PROTEOME COMPLETE GLUCOSE DEHYDROGENASE 6-PHOSPHATE PROBABLE GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE OXIDOREDUCTASE METABOLISM ","","","","","","","","","","","","Mon Jan 6 14:32:34 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01167 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 216 to 511 (E-value = 1.1e-190) place AA01167 in the G6PD_C family which is described as Glucose-6-phosphate dehydrogenase, C-terminal domain (PF02781)","","","","Yoshida,Y., Nakano,Y., Yamashita,Y. and Koga,T.The gnd gene encoding a novel 6-phosphogluconate dehydrogenase and its adjacent region of Actinobacillus actinomycetemcomitans chromosomal DNABiochem. Biophys. Res. Commun. 230 (1), 220-225 (1997)PubMed: 9020051","","Mon Jan 6 14:32:34 2003","","1","","","" "AA01168","801383","802078","696","ATGAACTACATCACCTTCCCCACCGCCCAACATGCGGTAGAAAAAATCGCGCAGGAATTTGTGATTTACAGCCAATTAAATCATCCTGCGCACATTTCCCTTTCCGGCGGTTCCACACCGAAACTGTTATTTAAAACCCTTGCACAATCTCCTTACGCCGAACAAATCAACTGGAGAAACCTGCATTTCTGGTGGGGCGATGATCGTATGGTTAGCCCAAGTGATCCGGAAAGCAATTACGGTGAAGTGCAAAAATTGTTGTTCGATCATATTCAAATTCCCGCTGAAAACATTCATCGAATCCGTGGCGAAAATGAACCGCACTTTGAACTCAAACGCTTCCAAGCAGAATTAAGTGCGGTCATTTCTGACGGCGTTTTTGATTGGATCATTCTCGGCATGGGCGCCGACGGTCACACCTCGTCCCTTTTCCCACATCAAACCAACTTTGATGATGAAAACCTTGCCGTCATCGCTAAGCACCCGGAAAGCGGACAAATTCGCATTTCCAAAACCGCTAAACTCATTGAGCAGGCAAAACGCATTACTTACCTCGTCACCGGCGAAGGCAAAGCCGAAATTTTAAAAGAAATCCAAAGCACGCCGGCTGAAAATCTACCTTACCCCGCCGCCAAAATCCACGCGAAGAATGGCGTAACGGAGTGGTATTTGGATAAAGATGCGGCGAAGTTGTTG","","","26183","MNYITFPTAQHAVEKIAQEFVIYSQLNHPAHISLSGGSTPKLLFKTLAQSPYAEQINWRNLHFWWGDDRMVSPSDPESNYGEVQKLLFDHIQIPAENIHRIRGENEPHFELKRFQAELSAVISDGVFDWIILGMGADGHTSSLFPHQTNFDDENLAVIAKHPESGQIRISKTAKLIEQAKRITYLVTGEGKAEILKEIQSTPAENLPYPAAKIHAKNGVTEWYLDKDAAKLL","802080","From GenBank gi:7404326.This protein hydrolyzes 6-phosphogluconolactone to 6-phosphogluconate.","6-phosphogluconolactonase","Cytoplasm","","
InterPro
IPR005900
Domain
6-phosphogluconolactonase
TIGR01198\"[5-232]Tpgl: 6-phosphogluconolactonase
InterPro
IPR006148
Domain
Glucosamine/galactosamine-6-phosphate isomerase
PF01182\"[8-230]TGlucosamine_iso
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1360\"[1-232]Tno description
PTHR11054\"[32-232]T6-PHOSPHOGLUCONOLACTONASE


","BeTs to 14 clades of COG0363COG name: 6-phosphogluconolactonase/Glucosamine-6-phosphate isomerase/deaminaseFunctional Class: GThe phylogenetic pattern of COG0363 is ------y-v-rlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is","Significant hit ( 2.8e-62) to 3/3 blocks of the IPB000457 family, which is described as \"Glucosamine/galactosamine-6-phosphate isomerase\". Interpro entry for IP:IPR000457. IPB000457A 31-73 2.3e-20 IPB000457B 117-169 1.1e-21 IPB000457C 172-226 8.7e-18","Residues 27 to 141 match (3e-07) PD:PD542210 which is described as POTENTIAL 6PGL 6-PHOSPHOGLUCONOLACTONASE HYDROLASE ","","","","","","","","","","","Mon Jan 6 14:40:11 2003","Mon Jan 6 14:40:11 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01168 is paralogously related to AA02465 (6e-08).","","","","","","","","","","Yoshida,Y., Nakano,Y., Yamashita,Y. and Koga,T. The gnd gene encoding a novel 6-phosphogluconate dehydrogenaseand its adjacent region of Actinobacillus actinomycetemcomitanschromosomal DNA Biochem. Biophys. Res. Commun. 230 (1), 220-225 (1997) PubMed: 9020051","Petruschka L, Adolf K, Burchhardt G, Dernedde J, Jurgensen J, Herrmann H.Analysis of the zwf-pgl-eda-operon in Pseudomonas putida strains H and KT2440.FEMS Microbiol Lett. 2002 Sep 24;215(1):89-95.PMID: 12393206Miclet E, Stoven V, Michels PA, Opperdoes FR, Lallemand JY, Duffieux F.NMR spectroscopic analysis of the first two steps of the pentose-phosphate pathway elucidates the role of6-phosphogluconolactonase.J Biol Chem. 2001 Sep 14;276(37):34840-6.PMID: 11457850","Mon Jan 6 14:41:49 2003","Wed Jan 29 14:27:51 2003","1","","","" "AA01169","802125","802289","165","GTGCTTGTAGATAAAGGCACGCGTTGGGAAACCATCGTAGGGAGAAACATGAAACAGATTATTTTTTGTATAGTTATGGCGATTACACTTGCCCTTCTGGGTATCGGCATTTGGTTTTTCCATATGATGCTTCAAGGTTTTTGTTCATCAGGTACGGGTTGTCAT","","","6128","VLVDKGTRWETIVGRNMKQIIFCIVMAITLALLGIGIWFFHMMLQGFCSSGTGCH","802289","","hypothetical protein","Cytoplasm, Inner membrane","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-38]?signal-peptide
tmhmm\"[20-40]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 11:44:58 2004","Wed Feb 25 11:44:58 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01169 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 11:44:58 2004","","","","","","","","","","","","","1","","","" "AA01170","802604","802699","96","ATGAATGTGTTAGCCATAACCTGTATGCTCTTCACCACCAAAACTGTAATTTTATTTTTGGTACATAAAGAACTCGAGGCGGAAGTTGCCAAGCAG","","","3618","MNVLAITCMLFTTKTVILFLVHKELEAEVAKQ","802699","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database. ","
noIPR
unintegrated
unintegrated
signalp\"[1-27]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 12:46:29 2004","Wed Feb 25 12:46:29 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01170 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 12:46:29 2004","","","","","","","","","","","","","1","","","" "AA01171","802951","803640","690","ATGAAAACATTAGGTATTTTAGGTGGGATGAGTCCCGAAAGCACGGTTTCCTATTATTTAATCATTAACCGTGCGGTGAATCAGGCGTTGGGTGGCAATGCAAGTGCGCCGTTATTGATGTCGAGCGTCAATTTTGAAGAGATTGTGCAATGCCAAAAATCAGGAAATTGGGCTAAAGCAGGTGAAATTTTGGCAGAGCAGGCGCGTTTGCTGGAAAGTATTGGGGCGGAAGGTATTTTAATTGGTGCCAATACCATGCACAAAGTCGCGGATGCCGTCCAAAATGTCATTTCTGTGCCGTTGTTACATATTTTAGATGTGGTGGCGGATAGCATTAAAGTACAAGGTTTATGCAAAGTAGCATTGCTTGGCACGCATTATGTGATGGCGGATAATTTTTATGTCGATGGCTTACGTGAGCGTGGTGTTGAGCCAATTGTGCCAAATGATAAAGATAAATTGGAAATTCATCGTATTATTTTTGAAGAGCTTTGCACGGGAAAAATAAAACCTGAGTCTAAAGCCTTTTATCTAAAAACGATCGAAAAATTGACCGCACTTGGTGCCGAAGGCGTCATTTTGGGCTGTACGGAAATCGGTTTATTGATTAATCAAATAGACAGCGATTTGCCGTTTTTCGACACCGCACTTTTACACAGCCAAATGGCGATTGATTTTATTTTGGAGAAA","","","24920","MKTLGILGGMSPESTVSYYLIINRAVNQALGGNASAPLLMSSVNFEEIVQCQKSGNWAKAGEILAEQARLLESIGAEGILIGANTMHKVADAVQNVISVPLLHILDVVADSIKVQGLCKVALLGTHYVMADNFYVDGLRERGVEPIVPNDKDKLEIHRIIFEELCTGKIKPESKAFYLKTIEKLTALGAEGVILGCTEIGLLINQIDSDLPFFDTALLHSQMAIDFILEK","803642","","LysA activator protein","Cytoplasm","","
InterPro
IPR001920
Family
Asp/Glu racemase
PF01177\"[3-228]TAsp_Glu_race
PS00924\"[192-202]?ASP_GLU_RACEMASE_2
InterPro
IPR004380
Family
Aspartate racemase
TIGR00035\"[1-230]Tasp_race: aspartate racemase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1860\"[106-230]Tno description


","BeTs to 5 clades of COG1794COG name: Aspartate racemaseFunctional Class: MThe phylogenetic pattern of COG1794 is a---k------lb-e--h--uj----Number of proteins in this genome belonging to this COG is","Significant hit ( 5.6e-22) to 4/4 blocks of the IPB001920 family, which is described as \"Aspartate and glutamate racemases\". Interpro entry for IP:IPR001920. IPB001920A 3-34 8.6e-05 IPB001920B 76-106 6e-07 IPB001920C 120-131 90 IPB001920D 190-206 3.7e-06","Residues 169 to 228 match (2e-16) PD:PD033224 which is described as COMPLETE PROTEOME RACEMASE ASPARTATE ISOMERASE LONG RESISTANCE PM1626 226AA STY3159 ","","","","","Wed Feb 19 07:31:23 2003","","","","","","","Mon Feb 17 14:52:11 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01171 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 228 (E-value = 3.7e-32) place AA01171 in the Asp_Glu_race family which is described as Asp/Glu/Hydantoin racemase (PF01177)","","","","Yoshida,Y., Nakano,Y., Yamashita,Y. and Koga,T.The gnd gene encoding a novel 6-phosphogluconate dehydrogenase andits adjacent region of Actinobacillus actinomycetemcomitans chromosomal DNABiochem. Biophys. Res. Commun. 230 (1), 220-225 (1997)PubMed: 9020051","Martin C, Cami B, Borne F, Jeenes DJ, Haas D, Patte JC.Heterologous expression and regulation of the lysA genes of Pseudomonas aeruginosa and Escherichia coli.Mol Gen Genet. 1986 Jun;203(3):430-4.PMID: 3018430 Stragier P, Richaud F, Borne F, Patte JC.Regulation of diaminopimelate decarboxylase synthesis in Escherichia coli. I. Identification of a lysR gene encoding an activator of the lysA gene.J Mol Biol. 1983 Aug 5;168(2):307-20.PMID: 6411928 Stragier P, Danos O, Patte JC.Regulation of diaminopimelate decarboxylase synthesis in Escherichia coli. II. Nucleotide sequence of the lysA gene and itsregulatory region.J Mol Biol. 1983 Aug 5;168(2):321-31.PMID: 635060","Mon Jan 6 14:58:43 2003","Wed Feb 19 07:31:23 2003","1","","","" "AA01172","803656","803907","252","ATGAAACCGATTTTGTACTTTGCCCTTTGGTGTCCGGATACCGAATCTTTTGTGGCGGAATTACAGCGACTAAATATCGCTTATGAAGCAAAAGATATTGCTGGCGACCGTTTAAATTTTAAAGCCTTCTTAAAATTACGCGACACCCATTCCGCCTTTGATGACGCCAAAGCCAACGGCTACATCGGCATTCCCGCGCTGGTGTTGGAAAATGGTGAAGTGATTTTAGATAAAGAGGCGTTAAAAAACGTT","","","9427","MKPILYFALWCPDTESFVAELQRLNIAYEAKDIAGDRLNFKAFLKLRDTHSAFDDAKANGYIGIPALVLENGEVILDKEALKNV","803909","","conserved hypothetical protein","Cytoplasm, Periplasm","","
noIPR
unintegrated
unintegrated
PD062008\"[3-82]TQ9CLV3_PASMU_Q9CLV3;
signalp\"[1-16]?signal-peptide


","BeTs to 3 clades of COG0695COG name: Glutaredoxin and related proteinsFunctional Class: OThe phylogenetic pattern of COG0695 is aom-k-y-vdrlbcefghsn-jx-t-Number of proteins in this genome belonging to this COG is","","Residues 2 to 84 match (5e-20) PD:PD062008 which is described as PROTEOME COMPLETE TP0072 PM1099 HI0926 ","","","","","Wed Feb 19 13:13:03 2003","","","","","","Wed Feb 19 12:14:34 2003","Wed Feb 19 13:15:34 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01172 is paralogously related to AA01146 (3e-20).","","","","","","","","","","","","","Wed Feb 19 13:17:47 2003","1","","","" "AA01173","803990","804445","456","ATGGATCGCACATTAATTGTTTTTGATATGGATACGCATTGCTTGGAGGAAAATTACCATAATCCTAGTTGGCGTAATGCTTATGCAGATATTCAGCGCATTTTAAAAAAACACGGCTTCACTAATATTCAAGGCACAGTTTATTTGAGCGATATTGGCATTAAACAAGCGCATGGCACATTGGCATTACAAGAGGTTGCGGCGCGATTTGAATGGTTTTATCACTGCGCATCCAATATTCAATTTTATGAATTAAAAGATGATTTTAATGCACAATTTATTGTAGAAGGCGTACAGCGTGCCCGTGAGGCCTTTAATCGCTCGCTTAATAGCTTACGCCAAGAATTATTACAAGCAGGTTTATCTGCTGATAAAGTGGAAGAAATTGTGAGAAAACGTCAATTTTCCTTACAGCAAATTCCGGAGAAGGAGTTATTACAAAATAATCAAGAAAAT","","","17804","MDRTLIVFDMDTHCLEENYHNPSWRNAYADIQRILKKHGFTNIQGTVYLSDIGIKQAHGTLALQEVAARFEWFYHCASNIQFYELKDDFNAQFIVEGVQRAREAFNRSLNSLRQELLQAGLSADKVEEIVRKRQFSLQQIPEKELLQNNQEN","804447","","VapD-homolog","Cytoplasm","","
InterPro
IPR007683
Family
Virulence-associated protein D (VapD) conserved region
PF04605\"[10-49]TVapD_N
noIPR
unintegrated
unintegrated
PD012479\"[15-89]TP70717_ACTAC_P70717;


","BeTs to 4 clades of COG3309COG name: Uncharacterized BCR (virulence-associated protein D)Functional Class: SThe phylogenetic pattern of COG3309 is -----------------hsnu-----Number of proteins in this genome belonging to this COG is","","Residues 90 to 138 match (5e-08) PD:PD086953 which is described as PROTEOME COMPLETE D VIRULENCE-ASSOCIATED VAPD-RELATED ","","","","","","","","","","","","Mon Jan 6 15:20:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01173 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 10 to 49 (E-value = 1.6e-24) place AA01173 in the VapD_N family which is described as Virulence-associated protein D (VapD) conserved region (PF04605)","","","","Yoshida Y, Nakano Y, Yamashita Y, Koga T. The gnd gene encoding a novel 6-phosphogluconatedehydrogenase and its adjacent region of Actinobacillusactinomycetemcomitans chromosomal DNA. Biochem Biophys Res Commun. 1997 Jan 3;230(1):220-5. PMID: 9020051","Benoit S, Benachour A, Taouji S, Auffray Y, Hartke A.Induction of vap genes encoded by the virulence plasmid of Rhodococcus equi during acidtolerance response.Res Microbiol. 2001 Jun;152(5):439-49.PMID: 11446512Cao P, Cover TL.High-level genetic diversity in the vapD chromosomal region of Helicobacter pylori.J Bacteriol. 1997 May;179(9):2852-6.PMID: 9139899Katz ME, Strugnell RA, Rood JI.Molecular characterization of a genomic region associated with virulence in Dichelobacternodosus.Infect Immun. 1992 Nov;60(11):4586-92.PMID: 1398971","Mon Jan 6 15:16:59 2003","Wed Feb 19 07:00:33 2003","1","","","" "AA01174","804983","804840","144","GTGCAACTTGTTGCACCGATTTTAAATATTTTGGTGCAACAAGTTGCACCCTACATAACGACGCGCCAAAAGTGCGGTCGTTTTTTCAATTGTTTTTTAATTCACTTGATTCATACCGCCGCGAGTCTGCCGACGTGTGCCTTA","","","5320","VQLVAPILNILVQQVAPYITTRQKCGRFFNCFLIHLIHTAASLPTCAL","804840","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-42]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 12:48:03 2004","Wed Feb 25 12:48:03 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to th8s sequence.AA01174 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 12:48:03 2004","","","","","","","","","","","","","1","","","" "AA01175","805004","806455","1452","ATGTCAGTAAAAGGCGACATCGGTGTTATCGGCTTAGCCGTGATGGGGCAGAACCTCATTTTAAATATGAATGACCACGGGTTTAAAGTGGTGGCGTATAACCGTACTACTTCAAAAGTGGACGAGTTTTTAGAAGGCGCGGCGAAAGGCACGAACATTATCGGCGCGTATTCTTTGGAAGATTTGGCGAACAAATTGGAAAAACCGCGTAAAGTGATGTTAATGGTGCGTGCGGGTGAAGTGGTGGATCACTTTATTGATGCATTGCTTCCGCATTTAGAAGCCGGCGACATCATTATCGACGGCGGTAACTCCAATTATCCAGACACCAACCGTCGCGTGGCGGCATTACGTGAAAAAGGCATTCGTTTCATCGGCACCGGCGTTTCCGGCGGTGAAGAAGGTGCGCGTCACGGACCTTCCATCATGCCGGGCGGTAACGAAGAAGCATGGCAATTTGTGAAACCGGTATTGCAAGCCATTTCCGCCAAAACCGAACAAGGCGAACCTTGTTGCGACTGGGTGGGTAAAGACGGCGCAGGTCATTTCGTGAAAATGGTGCATAACGGCATCGAATACGGCGATATGCAACTGATTTGTGAAGCGTACCAATTCCTAAAAGAAGGCGTGGGCTTGTCCGACGACGAATTGCAAGCCACCTTCAACGAATGGCGCAATACCGAATTAGACAGCTACTTAATTGACATCACCGCTGACATTTTGGGCTATAAAGACGCAGACGGCAGCCGTTTGGTGGATAAAGTCTTAGATACCGCAGGGCAAAAAGGAACCGGCAAATGGACAGGGATCAACGCATTGGATTTCGGCATTCCGTTGACCTTAATCACCGAATCCGTGTTCGCCCGTTGCGTGTCTGCCTTTAAAGATCAACGCGTCGCCGCAAGCAAATTGTTCCACAAAACCATCGGTAAAGTGGAAGGCGATAAAAAAGTGTGGATTGAAGCGGTGCGCAAAGCATTGTTGGCGTCTAAAATCATTTCTTACGCACAAGGCTTTATGTTGATTCGTGAAGCGTCCGAACACTTCAACTGGAACATCAACTACGGCAACACGGCATTGTTATGGCGTGAAGGTTGTATTATCCGTAGCCGTTTCTTGGGCAACATTCGTGATGCGTACGAAGCCAATCCGGATCTAATTTTCTTAGGCTCCGACAGCTACTTCAAAGGCATTTTAGAAAACGCCATGAGCGACTGGCGCAAAGTGGTGGCGAAATCCATCGAAGTGGGTATCCCAATGCCTTGTATGGCATCTGCGATTACCTTCTTAGATGGCTACACGTCAGCTCGTTTGCCTGCAAACTTATTGCAAGCACAACGCGACTACTTCGGCGCCCACACCTATGAGCGTACCGACAAACCACGCGGTGAATTCTTCCACACCAACTGGACGGGACGTGGCGGCAACACCGCTTCCACTACTTATGATGTG","","","55934","MSVKGDIGVIGLAVMGQNLILNMNDHGFKVVAYNRTTSKVDEFLEGAAKGTNIIGAYSLEDLANKLEKPRKVMLMVRAGEVVDHFIDALLPHLEAGDIIIDGGNSNYPDTNRRVAALREKGIRFIGTGVSGGEEGARHGPSIMPGGNEEAWQFVKPVLQAISAKTEQGEPCCDWVGKDGAGHFVKMVHNGIEYGDMQLICEAYQFLKEGVGLSDDELQATFNEWRNTELDSYLIDITADILGYKDADGSRLVDKVLDTAGQKGTGKWTGINALDFGIPLTLITESVFARCVSAFKDQRVAASKLFHKTIGKVEGDKKVWIEAVRKALLASKIISYAQGFMLIREASEHFNWNINYGNTALLWREGCIIRSRFLGNIRDAYEANPDLIFLGSDSYFKGILENAMSDWRKVVAKSIEVGIPMPCMASAITFLDGYTSARLPANLLQAQRDYFGAHTYERTDKPRGEFFHTNWTGRGGNTASTTYDV","806457","","6-phosphogluconate dehydrogenase","Cytoplasm","","
InterPro
IPR006113
Family
6-phosphogluconate dehydrogenase, decarboxylating
TIGR00873\"[6-472]Tgnd
InterPro
IPR006114
Domain
6-phosphogluconate dehydrogenase, C-terminal
PF00393\"[181-471]T6PGD
InterPro
IPR006115
Domain
6-phosphogluconate dehydrogenase, NAD-binding
PF03446\"[4-177]TNAD_binding_2
InterPro
IPR006183
Family
6-phosphogluconate dehydrogenase
PR00076\"[5-28]T\"[68-97]T\"[121-146]T\"[170-198]T\"[251-278]T\"[358-380]T6PGDHDRGNASE
InterPro
IPR006184
Binding_site
6-phosphogluconate-binding site
PS00461\"[255-267]T6PGD
InterPro
IPR008927
Domain
6-phosphogluconate dehydrogenase, C-terminal-like
SSF48179\"[179-474]T6DGDH_C_like
InterPro
IPR012284
Domain
Fibritin/6-phosphogluconate dehydrogenase, C-terminal extension
G3DSA:1.20.5.320\"[437-484]TFibritin/6PGD_C-extension
InterPro
IPR013328
Domain
Dehydrogenase, multihelical
G3DSA:1.10.1040.10\"[183-436]TOpine_DH
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[3-182]TG3DSA:3.40.50.720
PTHR11811\"[182-483]TPTHR11811
SSF51735\"[4-178]TSSF51735


","No hits to the COGs database.","Significant hit (4.1e-240) to 8/8 blocks of the IPB001744 family, which is described as \"6-phosphogluconate dehydrogenase\". Interpro entry for IP:IPR001744. IPB001744A 13-39 1.4e-19 IPB001744B 50-87 6e-22 IPB001744C 96-147 1.4e-43 IPB001744D 167-202 2.8e-35 IPB001744E 212-243 3.6e-19 IPB001744F 245-289 6e-33 IPB001744G 343-396 1.3e-35 IPB001744H 426-456 2.2e-24Significant hit ( 2.5e-05) to 3/5 blocks of the IPB002204 family, which is described as \"3-hydroxyisobutyrate dehydrogenase\". Interpro entry for IP:IPR002204. IPB002204A 7-20 0.63 IPB002204C 125-142 74 IPB002204D 176-211 0.21","Residues 102 to 162 match (3e-08) PD:PD516450 which is described as 6-PHOSPHOGLUCONATE DEHYDROGENASE PROTEOME COMPLETE GND DEHYDROGENASE DECARBOXYLATING NAD-LINKED GND2 ","","","","","","","","","","","","Mon Jan 6 15:24:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01175 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 179 to 471 (E-value = 1.4e-232) place AA01175 in the 6PGD family which is described as 6-phosphogluconate dehydrogenase, C-terminal domain (PF00393)","","","","Yoshida Y, Nakano Y, Yamashita Y, Koga T. The gnd gene encoding a novel 6-phosphogluconatedehydrogenase and its adjacent region of Actinobacillusactinomycetemcomitans chromosomal DNA. Biochem Biophys Res Commun. 1997 Jan 3;230(1):220-5. PMID: 9020051","Tarr PI, Schoening LM, Yea YL, Ward TR, Jelacic S, WhittamTS. Acquisition of the rfb-gnd cluster in evolution ofEscherichia coli O55 and O157. J Bacteriol. 2000 Nov;182(21):6183-91. PMID: 11029441 ","Mon Jan 6 15:24:00 2003","Mon Jan 6 15:24:00 2003","1","","","" "AA01176","806577","806449","129","GTGATATTTAATTTAATAATTTTTACTATAAAAGAGCTGCACCTTAATTGGTTGGTTGTAGTGTCCAACTTTTGGGGCGCAGATCAAAGTGCGGTCGATTTACAGGATGTTTTTACCCACTACACATCA","","","4977","VIFNLIIFTIKELHLNWLVVVSNFWGADQSAVDLQDVFTHYTS","806449","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-30]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 12:49:53 2004","Wed Feb 25 12:49:53 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01176 is paralogously related to AA02629 (2e-05).","Wed Feb 25 12:49:53 2004","","","","","","","","","","","","","1","","","" "AA01177","808113","806872","1242","ATGAAACGAGTTGTGATCACAGGCATCGGCGCGGTTACCGCCTTCGGTAAAACATGGCAGGAGATTAAAACGGCATTCCAACGCAAACAAAACGCCGTACAAGCCAAAGCGGATTGGGCGGAACGCTACCCTGAACTGGAAGCCCGTTTAGGCGCGGAAATTCATGGTTATCAGCCGCCGTCACATTGGAACCGCAAACAATTACGCAGCCTCGGGCGGGTGTCGCAATTCGCCGTCGAGGCTGCCGAGCGTGCGTTGGCGAATGCCGATTTACTAGACGAAAACGGCGACATTCTTGCGTACCTCAAAGACGGCAGAATGGGCGTGGCGTGCGGTTCTTCCACCGGTTCCACGAATGATATTAAAGATGCCGCCGAGCTTCTCATGACCGGTAAATCCGACGGCTTCAACGCCAACACCTATGTGCGCATGATGCCCCATACTACCACCGCCAATATCGGTATTTTCTTCGGCTTAACGGGGCGTATTATTCCCACCTCCAGTGCCTGTTCTTCCGGCAGTCAGGGCATTGGCTATGCCTATGAATCCATCAAATACGGTTTGATTCCCATGATGCTCGCCGGCGGCGCCGAGGAATTTTGCCCGTCGGAAGTTTATGTGTTTGATTCCCTCTATGCGGCAAGTCGCAATGTGAATAATCCAAGTAAAACACCGCGCCCTTATGATAACGATCGCGACGGCTTGGTGATCGGCGAAGGGGCGGGGATTTTCGTGCTGGAAGAACTGGAGCACGCCCTGGCACGCGGAGCGAATATTATTGCGGAAGTGGTGGGCTACGGCGCAAACAGCGACGGCGCACACGTCACCCGCCCGCAAAAAGACACCATGCAACGTTGCATGGAATTGGCATTAAAAGACGCCCATTTATCCGCGCAAAAAATCGGCTATGTCAACGGACACGGCACGGCGACGGAGCAAGGGGATATTGCCGAAACCTTGGCAACGGAAGCGGTGTTTGGCAAGGTACCGTTAAGCTCGCAAAAAAGCTATTTAGGGCATACCCTTGGTGCGTGCGGCGCGTTGGAATCCTGGTTTTCCATTGAAATGATGCGCGACGGCTGGTTTGCGCCGACCATTAATCTGGATAATATTGACGAACGCTGCGGCAAATTGGATTACATTCAAGGCGACGGGCGCCATATTGAAACGGATTATGTGATGAATAATAACTTTGCCTTTGGCGGCGTGAATACCTCATTGATTTTTAAACGTTGGCAGGCG","","","45312","MKRVVITGIGAVTAFGKTWQEIKTAFQRKQNAVQAKADWAERYPELEARLGAEIHGYQPPSHWNRKQLRSLGRVSQFAVEAAERALANADLLDENGDILAYLKDGRMGVACGSSTGSTNDIKDAAELLMTGKSDGFNANTYVRMMPHTTTANIGIFFGLTGRIIPTSSACSSGSQGIGYAYESIKYGLIPMMLAGGAEEFCPSEVYVFDSLYAASRNVNNPSKTPRPYDNDRDGLVIGEGAGIFVLEELEHALARGANIIAEVVGYGANSDGAHVTRPQKDTMQRCMELALKDAHLSAQKIGYVNGHGTATEQGDIAETLATEAVFGKVPLSSQKSYLGHTLGACGALESWFSIEMMRDGWFAPTINLDNIDERCGKLDYIQGDGRHIETDYVMNNNFAFGGVNTSLIFKRWQA","806874","","beta-ketoacyl-ACP synthase IV","Cytoplasm","","
InterPro
IPR000794
Domain
Beta-ketoacyl synthase
PTHR11712\"[2-413]TKetoacyl_synth
InterPro
IPR014030
Domain
Beta-ketoacyl synthase, N-terminal
PF00109\"[2-252]Tketoacyl-synt
PS00606\"[161-177]?B_KETOACYL_SYNTHASE
InterPro
IPR014031
Domain
Beta-ketoacyl synthase, C-terminal
PF02801\"[260-369]TKetoacyl-synt_C
noIPR
unintegrated
unintegrated
G3DSA:3.40.47.10\"[6-265]T\"[268-412]TG3DSA:3.40.47.10


","No hits to the COGs database.","Significant hit ( 1.6e-05) to 2/3 blocks of the IPB000794 family, which is described as \"Beta-ketoacyl synthase\". Interpro entry for IP:IPR000794. IPB000794B 224-236 0.041 IPB000794C 335-344 0.21","Residues 1 to 37 match (4e-13) PD:PD091330 which is described as BETA-KETOACYL-ACP IV SYNTHASE ","","","","","","","","","","","","Mon Jan 6 15:32:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01177 is paralogously related to AA00759 (4e-61) and AA01182 (3e-27).","","","","","","Residues 260 to 413 (E-value = 2.1e-55) place AA01177 in the Ketoacyl-synt_C family which is described as Beta-ketoacyl synthase, C-terminal domain (PF02801)","","","","Yoshida,Y., Nakano,Y., Yamashita,Y. and Koga,T.The gnd gene encoding a novel 6-phosphogluconate dehydrogenase andits adjacent region of Actinobacillus actinomycetemcomitanschromosomal DNABiochem. Biophys. Res. Commun. 230 (1), 220-225 (1997)PubMed: 9020051","Edwards P, Nelsen JS, Metz JG, Dehesh K.Cloning of the fabF gene in an expression vector and in vitro characterization of recombinant fabF and fabB encoded enzymes from Escherichia coli.FEBS Lett. 1997 Jan 27;402(1):62-6.PMID: 9013860 ","Mon Jan 6 15:32:00 2003","Mon Jan 6 15:39:11 2003","1","","","" "AA01179","808861","808136","726","ATGAGCGAAACAATTTTAATTACAGGTTCCAGCCGCGGCATCGGCAAAGCCATTGCTTTACGTTTGGCGCAGGCGGGATTTGATATTGTGGTGCATTGCCGTAGCCGCATAGAAGAAGCGGAAGCGGTGGCGCAGGCGGTGCGTGAACTGGGGCAAAATGCCCGCGTGTTGCAGTTTGATGTTAGCTGTCGCAGTGAAGCAGCAGACAAACTTACCGCCGATGTAGAAGCCCATGGTGCTTATTACGGCGTGGTGCTGAATGCCGGCTTAACCCGTGATAACGCCTTCCCGGCGTTAACCGATGAAGATTGGGACCGTGTTTTACGCACGAATCTGGACGGTTTCTATAATGTGTTACACCCGATTATGATGCCGATGATTCGCCGTCGCAAAGCAGGGCGCATTGTGTGTATTACCTCCGTATCGGGCTTAATCGGCAATCGTGGTCAGGTCAATTACAGCGCCTCCAAAGCCGGCATTATCGGCGCGGCGAAAGCGCTGGCGGTGGAATTGGCGAAACGTAAAATTACCGTGAATTGCGTGGCGCCGGGCTTAATTGATACGGATATTCTGGATGAAAATGTGCCAATTGACGAGATCCTGAAAATGATTCCCGCAGGACGTATGGGCGATCCTGAAGAAGTGGCACACGCCGTAAATTTCCTGATGGGCGAAAAAGCTGCGTATGTTACCCGCCAAGTGATCGCCGTAAATGGCGGTTTGTGC","","","25973","MSETILITGSSRGIGKAIALRLAQAGFDIVVHCRSRIEEAEAVAQAVRELGQNARVLQFDVSCRSEAADKLTADVEAHGAYYGVVLNAGLTRDNAFPALTDEDWDRVLRTNLDGFYNVLHPIMMPMIRRRKAGRIVCITSVSGLIGNRGQVNYSASKAGIIGAAKALAVELAKRKITVNCVAPGLIDTDILDENVPIDEILKMIPAGRMGDPEEVAHAVNFLMGEKAAYVTRQVIAVNGGLC","808138","","beta-ketoacyl-ACP reductase; short-chain alcohol dehydrogenase","Cytoplasm","","
InterPro
IPR002198
Family
Short-chain dehydrogenase/reductase SDR
PR00080\"[79-90]T\"[133-141]T\"[153-172]TSDRFAMILY
PTHR19410\"[2-239]TADH_short_C2
PF00106\"[3-172]Tadh_short
InterPro
IPR002347
Family
Glucose/ribitol dehydrogenase
PR00081\"[4-21]T\"[79-90]T\"[127-143]T\"[153-172]T\"[174-191]T\"[205-225]TGDHRDH
InterPro
IPR011285
Family
3-oxoacyl-(acyl-carrier-protein) reductase, putative
TIGR01831\"[5-242]TfabG_rel
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[3-241]TG3DSA:3.40.50.720
PTHR19410:SF92\"[2-239]TPTHR19410:SF92
SSF51735\"[1-241]TSSF51735


","BeTs to 22 clades of COG1028COG name: Dehydrogenases with different specificities (related to short-chain alcohol dehydrogenases)Functional Class: Q,RThe phylogenetic pattern of COG1028 is ao-pkzyqvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 7.4e-14) to 1/1 blocks of the IPB002198 family, which is described as \"Short-chain dehydrogenase/reductase (SDR) superfamily\". Interpro entry for IP:IPR002198. IPB002198 133-168 7.1e-14","Residues 4 to 37 match (2e-10) PD:PD058480 which is described as OXIDOREDUCTASE COMPLETE PROTEOME DEHYDROGENASE REDUCTASE SHORT-CHAIN DEHYDROGENASE/REDUCTASE PROBABLE FAMILY NADP ","","","","","","","","","","","","Mon Jan 6 15:49:19 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01179 is paralogously related to AA00269 (1e-40), AA01109 (4e-15), AA02205 (2e-10), AA00912 (1e-09) and AA02383 (1e-09).","","","","","","Residues 5 to 241 (E-value = 1.6e-66) place AA01179 in the adh_short family which is described as short chain dehydrogenase (PF00106)","","","","Yoshida,Y., Nakano,Y., Yamashita,Y. and Koga,T.The gnd gene encoding a novel 6-phosphogluconate dehydrogenase andits adjacent region of Actinobacillus actinomycetemcomitanschromosomal DNABiochem. Biophys. Res. Commun. 230 (1), 220-225 (1997)PubMed: 9020051","Rawlings,M. and Cronan,J.E. Jr. The gene encoding Escherichia coli acyl carrier protein lies within a clusterof fatty acid biosynthetic genes J. Biol. Chem. 267 (9), 5751-5754 (1992) PubMed: 1556094 Ren Q, Sierro N, Witholt B, Kessler B. FabG, an NADPH-dependent 3-ketoacyl reductase of Pseudomonas aeruginosa,provides precursors for medium-chain-length poly-3-hydroxyalkanoate biosynthesis in Escherichia coli. J Bacteriol. 2000 May;182(10):2978-81. PMID: 10781572 ","Mon Jan 6 15:46:45 2003","Mon Jan 6 15:46:45 2003","1","","","" "AA01181","809354","808914","441","ATGCTTGATTTAACTTGCCCTATTACCGACATCGCGCCTTTGGTGCCACATAGCGGTAAAATGATTTTATTGGATCGGGTCACTGATTTCGGCGATGACTTTTTGATCGCGGAAGCGGAAGTGCGCCCCGATAATCTGTTGGTGAAAGACAATAAACTGCCCGGTTTTCTTGGCGCGGAAATCATGGCGCAAGGAGTTGCCGCCTGGGCTGGGTGCAAATGCGTACGTGCCGGCAAACCCATCACCTTGGGCTATTGGATCGGCTCCCGCAAACTCTGCATTCACCAACCGGACATTGCCATCGGCAGCAAATTACGCATTCAAATTAAGCTTTCTATTGAAGATGCCACCGGCTTCGGCGTGTTTGATTGCCAATTAATTGATTCAGCAAACCAACGGGTGATTGTGGAAGGTGCGCTGAACGTATTCCGACCGCAGGTG","","","15957","MLDLTCPITDIAPLVPHSGKMILLDRVTDFGDDFLIAEAEVRPDNLLVKDNKLPGFLGAEIMAQGVAAWAGCKCVRAGKPITLGYWIGSRKLCIHQPDIAIGSKLRIQIKLSIEDATGFGVFDCQLIDSANQRVIVEGALNVFRPQV","808916","","conserved hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
G3DSA:3.10.129.10\"[7-142]Tno description


","BeTs to 3 clades of COG0764COG name: 3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratasesFunctional Class: IThe phylogenetic pattern of COG0764 is -------qvd-lbcefghsnujxi--Number of proteins in this genome belonging to this COG is","","Residues 11 to 126 match (2e-11) PD:PD398202 which is described as COMPLETE PROTEOME PLASMID RSP0360 TRANSFERASE PHOSPHOTRANSFERASE RSC0425 ","","","","","","","","","","","","Mon Jan 6 15:55:32 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01181 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01182","810570","809350","1221","ATGACCGCACTTTATCTAAGTAAACCAGCTATTTTGAGCAGCCTTGGCGATGGCATCGAAACACACATTGCGCGTTTGCTGGCTGCCGAGGATTCCCCTTTGGCATTTTCCGATTCGGCGTTTAAGTTGTATCACACCGAAGGAAAAGCGCGCGTGTTCGGTGAAGTAAACGTGCCGCTACGCCCGTTTGCCGAAAGTTTGCCTGCGATACATCAAAGTCGTAACAATCAGTTATTGTGGCATTGTCTGGCGCAAATTGAACCGCAAATCGAACAGGCAATTGCCCGTTTCGGACGCCAACGCATTGCCGTGATTATCGGCACTTCCACCACCGGTGTAGATGAAAACGTACCGGTATTTAAATATGCCGTTAGCCATAACGATTGGTCCGGTGCCGAGTTTAAACAACAGCAACAATATTTTTCCGCGCCTTCCGATTTCGTTGCTTATCAGTATGGCTTGCAGGGGTTGAGTTACGGCATTTCCACCGCCTGTACCTCCGGTGCCAAAGCGTTGATTAGCGCCGCGCGTTTGTTGAACGCCGGTTTATGCGATGCGGTGATTTGCGGCGGTGTGGATGAGCTTTCGCCTCTCACCATCAGCGGTTTCGGCTCTTTATCCGTTTTATCCGATAAGCGTTCCAATCCGCTTTCCGTGAATCGCGACGGGATTAATCTCGGCGAAGGCGCCGCGGTTTTCGTGATGAGCCAGGAAAAATTAGACGATACGGCGATTCAATTACTCGGCTACGGCGCCAGTAGCGACGCTTATCATATGTCTTCCCCGCACCCGGAAGGCGAGGGCGCGATCAGCGCGTTTCGAGCCGCGTTGGCGTCTTCCGAATTAAGCGCCGATGCGATTGGCTGGATCAATTTGCACGGTACGGGAACGGTACATAATGATCAAATGGAAAGTTTGGCGGTACACCGGGTTTTTGGCGACGACACGCCTTGCACCACTACTAAGCCTTACACCGGGCACACCCTCGGCGCCGCCGGTGCCGTGGAAGCCGCGATTTTATGGGGCATCATCGACCGCAAACTGAACCCGCAGGGCAAGTTGCCGGCACAATTGTGGGACAAACAGGCGGATCCCGCGTTGCCGAAAATTGCCATTACCGACGAACACAGCCACTGGCGCAGCGAACCCCGTATCGGCGCAAGCAGTTCTTTTGCTTTCGGCGGCAATAATACGGTGCTGATTTTAGGAGAACGGGATGCT","","","43348","MTALYLSKPAILSSLGDGIETHIARLLAAEDSPLAFSDSAFKLYHTEGKARVFGEVNVPLRPFAESLPAIHQSRNNQLLWHCLAQIEPQIEQAIARFGRQRIAVIIGTSTTGVDENVPVFKYAVSHNDWSGAEFKQQQQYFSAPSDFVAYQYGLQGLSYGISTACTSGAKALISAARLLNAGLCDAVICGGVDELSPLTISGFGSLSVLSDKRSNPLSVNRDGINLGEGAAVFVMSQEKLDDTAIQLLGYGASSDAYHMSSPHPEGEGAISAFRAALASSELSADAIGWINLHGTGTVHNDQMESLAVHRVFGDDTPCTTTKPYTGHTLGAAGAVEAAILWGIIDRKLNPQGKLPAQLWDKQADPALPKIAITDEHSHWRSEPRIGASSSFAFGGNNTVLILGERDA","809352","","3-oxoacyl-(acyl-carrier-protein) synthase","Cytoplasm, Periplasm","","
InterPro
IPR000794
Domain
Beta-ketoacyl synthase
PTHR11712\"[144-406]TPOLYKETIDE SYNTHASE-RELATED
InterPro
IPR000833
Family
Alpha-amylase inhibitor
SM00783\"[297-341]Tno description
InterPro
IPR014030
Domain
Beta-ketoacyl synthase, N-terminal
PF00109\"[148-240]Tketoacyl-synt
PS00606\"[156-172]?B_KETOACYL_SYNTHASE
InterPro
IPR014031
Domain
Beta-ketoacyl synthase, C-terminal
PF02801\"[247-338]TKetoacyl-synt_C
noIPR
unintegrated
unintegrated
G3DSA:3.40.47.10\"[4-235]T\"[250-404]Tno description
PTHR11712:SF23\"[144-406]T3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE


","BeTs to 17 clades of COG0304COG name: 3-oxoacyl-(acyl-carrier-protein) synthaseFunctional Class: I,QThe phylogenetic pattern of COG0304 is ------yqvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is","","Residues 202 to 266 match (1e-08) PD:PD000224 which is described as SYNTHASE PHOSPHOPANTETHEINE TRANSFERASE POLYKETIDE COMPLETE PROTEOME I ACYLTRANSFERASE II BIOSYNTHESIS ","","","","","","","","","","","","Mon Jan 6 16:17:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01182 is paralogously related to AA00759 (2e-27) and AA01177 (3e-27).","","","","","","Residues 244 to 406 (E-value = 5.5e-31) place AA01182 in the Ketoacyl-synt_C family which is described as Beta-ketoacyl synthase, C-terminal domain (PF02801)","","","","","","","","1","","","" "AA01183","810962","810582","381","GTGTTTAAAGTGGAACAGTTAAATGCGCAACATCAGTTACAACAAGCCAGCCTGCTGACATTGCAAACCGAACCACAACAATGGCGCTGGGTGCAAACGGATCCCCTGGGTGCGCCTCTGGCGCGCGTGATTTTAACGCCACAAGGCTGGCAAAATGACGGCTTTATCATGCCGAATCAACAAGCGCGCCGTTTGTTTTCCGCCTTGGCGACAGCATTGAATCCGCAGCACCCGTTATTTACCTTCAGCCGCATTGAACCCGTGGCGCAGGGTAATGATTATTTTATTCAGCATAACAAAGTCTGGCGCATTGCATTGCGTCCGCCACAGATTGAAATCCACCTGGCGGATGACAGCCGTTGGCGTATTGAAGAATTAAAT","","","21903","VFKVEQLNAQHQLQQASLLTLQTEPQQWRWVQTDPLGAPLARVILTPQGWQNDGFIMPNQQARRLFSALATALNPQHPLFTFSRIEPVAQGNDYFIQHNKVWRIALRPPQIEIHLADDSRWRIEELN","810584","","conserved hypothetical protein","Periplasm, Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Jan 6 16:24:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01183 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01184","810978","811193","216","TTGCGGCGGCAACCGTTCCACCTGCGGCAACGAGCTGCACGCGGTCAGCCAAAAGCAGAACAACAGAGCAAAGTATTTCATTATTTCGCCACAAACGGATTTTCCGTATTCCGCGTATCGCCCGCTACAATGGAACAACGATTGCCGGCAAAGGAAATCAACTATAGCCATAAATCACCACATCACATTGTGCCATTTGGGTTCTCCGAATTAACG","","","8488","LRRQPFHLRQRAARGQPKAEQQSKVFHYFATNGFSVFRVSPATMEQRLPAKEINYSHKSPHHIVPFGFSELT","811195","","hypothetical protein","Periplasm, Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Jan 6 16:28:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01184 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01185","813461","811191","2271","ATGAAAAAATCCACCGCACTTTCCGTTCTGTATGCCCTGTTCCTGACGGCGACATTGTTGCTCTTTGGTTATGCGGTGAAAAAAGGCGCTTGGTTAGAAACGGATTTGCGTGCCCTGCTGCCGCAAGAACAAGGCTGGACTACCGTGCAAGTACGGGCGGATGAACAACAGGAAGCGCGCCTCAACCAGCAACTTATTTCCCTTATCGGGCATTCATCGCCGCAAAAGGCATTTCAGCTGGCAGAACAGGTTGCGCAGCAATGGCAAAAGAGCGGGTTGTTTGCCCGGATGGATGCCAAAACGCAACCGGATCTTGAAGCATTGCGTGCCGAAATCGCCCGATTACGCCTCGCCACTTTGCCGCCCTCCGTTCGCCATCAGTTGCTTCATACGCCACAGGATTATTTCCAACATTACGCCGAGCAGATCATGAATCCTTTCGCGCAAACCAATTTGCTTCCGCTGGATCAGGATTGGCTCGGTTTCGGCAGGTTCGTTTTGCCGCAGGCGCAATTGCAGGGGCAGATTCAATGGTATGCCGAAAATGGCATGTTGTATGTCACGGACAAGGATAAAACCTGGGTGCTGTTGCGCGGGGTGTTGCAACAAGGGGACCTGATGGATCCGTCGTTAAATCTGACCGCACTTTTAACGCAGAACCGCCAAGCCGTTGAAGCGGCACAGGGCGATATGTTGGCGACCGGCGCCGCCTTGTTCGCCATTGACGCCAAAGTCAAAGCGGAGCGGGAAAGCACCTTAATGAGCGCGTTGGGCGTAAGCCTGACGTTGTTGTTGCTGTTGCTCGTGTTCAGAACGGCGCGCGTGTTGTGGCTGTTTTTGCCGATTCTAACGGGCATGCTATGCGGCGTCACCGCCACAATTTTCGTTTTCGGACACATTCATATTCTCACCATTGTCATCGGCACCAGTTTAATCGGCGTGTTGATTGATTTTCCGCTGCATTGGCTGGCATCTTCCTTATTTCATCAACCATGGCACGCCGCGCAGGCGATGCAAAAACTACGGTTTACTTTTCTGATTAGCCTGCTTGTGACGCTGTTGGGCTACGGCTTGCTCGGTTTTACTGCCCTTCCGGTGTTAAAACAGACCGCACTTTTCTCCGCTATCGCGTTAATCTCGGCAATGTTCGCCACCTTGCTTTTTTTGCCTGCATTATTTCGCCGTTATCAAAACAAACCGCGCACCCCGAACCCAAAAGTGCGGTGGATTTTGGATGCGTTTTTTACCCGTCGCATGGGCGTGGTTTCAATCCTGTTAGGGGGGATTTTTATCGTCGGCGGTTTGTATCGTTCCGAATGGCGTGATGATATTCGTCAATGGGTTTCTATGCCGCAGGTGATGTTAGACGAGGCGAAGCAAATCGCTGACTTGACCGGCGTGGATTTGGGCAACCGTTATTTCCTGGTGCTTGCCGACAACGACGATGCCTTACTGGAAAAAGAACGGGCGCTGACAACAAAACTGGATGAACAGCACATCCCTTATCGCGCCCTTTCCCAATGGATGATGTCGGAAGCGCAACAGCGGCAATTTATAGTGGAATTGCAGGCAAAACTCAAACCGCAGGATTATGCCGTATTGGATGAGATTGGCGTGCCGTCGGAAAGATTACAACAGGCACTGCGGGAATTGAACACGCAGCCGCCGTTATCCTTGCAGCAGGCGTTGCAATCTACCGTCGGGCAAGCATGGCTGCCGCTCTATTTAGGCAAATTAGCGGAAAATCAGGTGGCTGGCATCGTGCAGGTAAGCGGACACAGTGCCGTTTCCCTTGCGCATTTGGCAAATCAACAGGATATTTTCTGGCAGGATAAACGGGCGCACTTGAATCAAGCGTTTCAGCAAACCCGCGATCAGGCGGCGTGGCTGAAAATGCTTTCTTTTGTATTTGCCGGCGTGTTGTTGTGGCGTTTGTTCGGGGTTAAACGCACTTTCACCATGTTGCTTCCGCCCTTGTGCGCTATTGTGATCACCGTGGCAATTTTCGGCTGGGTCGGTTTGCCCATCAGTTTATTTACTATGTTCGGGCTATTGCTGGTATCGGCGATCGGCATTGATTACACCGCGTATATGCAAACTGCAAATGAGCCTTTATACGGCAAATACATTGCGGTATTATTGGCGGCAATGACAACCCTCATTTCCTTCGTCTTATTGGGGCTGAGCTCCACACCGGCGGTGGCTTCCTTCGGTTTAAGCGTGAGCCTCGGTGTGTTATTGAGCGTCATCCTGACTTTTAAACTATTACGT","","","84618","MKKSTALSVLYALFLTATLLLFGYAVKKGAWLETDLRALLPQEQGWTTVQVRADEQQEARLNQQLISLIGHSSPQKAFQLAEQVAQQWQKSGLFARMDAKTQPDLEALRAEIARLRLATLPPSVRHQLLHTPQDYFQHYAEQIMNPFAQTNLLPLDQDWLGFGRFVLPQAQLQGQIQWYAENGMLYVTDKDKTWVLLRGVLQQGDLMDPSLNLTALLTQNRQAVEAAQGDMLATGAALFAIDAKVKAERESTLMSALGVSLTLLLLLLVFRTARVLWLFLPILTGMLCGVTATIFVFGHIHILTIVIGTSLIGVLIDFPLHWLASSLFHQPWHAAQAMQKLRFTFLISLLVTLLGYGLLGFTALPVLKQTALFSAIALISAMFATLLFLPALFRRYQNKPRTPNPKVRWILDAFFTRRMGVVSILLGGIFIVGGLYRSEWRDDIRQWVSMPQVMLDEAKQIADLTGVDLGNRYFLVLADNDDALLEKERALTTKLDEQHIPYRALSQWMMSEAQQRQFIVELQAKLKPQDYAVLDEIGVPSERLQQALRELNTQPPLSLQQALQSTVGQAWLPLYLGKLAENQVAGIVQVSGHSAVSLAHLANQQDIFWQDKRAHLNQAFQQTRDQAAWLKMLSFVFAGVLLWRLFGVKRTFTMLLPPLCAIVITVAIFGWVGLPISLFTMFGLLLVSAIGIDYTAYMQTANEPLYGKYIAVLLAAMTTLISFVLLGLSSTPAVASFGLSVSLGVLLSVILTFKLLR","811193","","conserved hypothetical protein (possible membrane protein)","Inner membrane, Cytoplasm","","
InterPro
IPR000731
Domain
Sterol-sensing 5TM box
PS50156\"[303-395]TSSD
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[231-397]Tno description
InterPro
IPR013248
Family
Shr3 amino acid permease chaperone
SM00786\"[279-470]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-25]?signal-peptide
tmhmm\"[5-25]?\"[251-269]?\"[278-298]?\"[302-324]?\"[345-365]?\"[371-393]?\"[414-436]?\"[627-647]?\"[652-672]?\"[678-698]?\"[710-730]?\"[736-756]?transmembrane_regions


","BeTs to 4 clades of COG1033COG name: Predicted exporters of the RND superfamilyFunctional Class: RThe phylogenetic pattern of COG1033 is aom-k---v---b--f----u---t-Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Mon Jan 6 16:36:11 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01185 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01187","814052","813471","582","ATGAAGACATTTTTTGTCCTTTGCTGCCTGTTTTTCAGCCCGCTGACCTTTGCCTTTTCCGAAGCGGAACTCATTACATTGCTACAAACCCCGCAAAACGTGCAGGGCAATTTCACCCAGCAACGTTTTCTCAAATCCCTTGCTAAGCCCATTACCACACAAGGCAAGTTCACCTTGTTGGCGAAAAAAGGCTTGTTATGGCAAATGGAAAAACCCTTCACCAACCAACTGCGGGTGAAAACCGACGGCATTATGCAATGGGACGGCAAGCAATGGGTGGCAAACGGCAACATGGGGCAGGCGCAGCAAATTAGCCTGTTTTTGGGCTTATTGTCGGGCGATATTTCCGGTTTGAAAGCGCAGTTTGAGGTGGCGTTGTCGGGCGAGGCGAAAAACTGGCAATTGACTTTAACGCCAAGTTCCTTGCTGATGAAACAGATTTTTACCGATATTCAGATTCAAGGTGATGAGGTGGTGAAAGCCATTGTGTTAAACGAAAAACAGGGCGATAAAACCCACATTCAATTTGACCATATTCAACAAAATCAGCCTTTGGCGGCGTTCGCACAATCCGCGTTAGAA","","","23564","MKTFFVLCCLFFSPLTFAFSEAELITLLQTPQNVQGNFTQQRFLKSLAKPITTQGKFTLLAKKGLLWQMEKPFTNQLRVKTDGIMQWDGKQWVANGNMGQAQQISLFLGLLSGDISGLKAQFEVALSGEAKNWQLTLTPSSLLMKQIFTDIQIQGDEVVKAIVLNEKQGDKTHIQFDHIQQNQPLAAFAQSALE","813473","","conserved hypothetical protein","Periplasm, Cytoplasm","","
InterPro
IPR004564
Family
Outer membrane lipoprotein carrier protein LolA
PF03548\"[29-191]TLolA
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide


","No hits to the COGs database.","","Residues 34 to 176 match (2e-15) PD:PD589609 which is described as COMPLETE PROTEOME TRANSMEMBRANE PLASMID Z4860 RSP0363 PEPTIDE SIGNAL ","","","","","","","","","","","","Mon Jan 6 16:39:13 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01187 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01188","814495","814052","444","ATGAAAAAACACATTTACTGCCATCATGCCTCCGAATATGAAATTCAGTTTTTTGACGTGGATTCCATGAATATCATGTGGCACGGGCATTATGTGAAATATCTGGAAATGGCGCGCTGTGCCTTTCTGGAAGAAATTCACTACACTTATGATGTGATGAAAGAAAAAGGGTACGGCTGGCCGGTGGTAAAATTAAATTTGAAATATGTGCAACCGACCGTTTTTCGCCAGAAAATTCTGGTGGAACTGGCGTTGGTGGAATACGAAAGCTGCATTCGCATCGATTATGTCATTCGTGATGCGGTGACCAATCAAAAACTCACCAGCGGCAGTACCACGCAAGTGGCGGTGGAAATCAAAAGCGGCGAAATGCAGTTGCAAACCCCGCCGTGTTGGCGAAGTGCGGTGGAAAATCACCGCACTTTTCAGGCGGAGAACGCATCA","","","17400","MKKHIYCHHASEYEIQFFDVDSMNIMWHGHYVKYLEMARCAFLEEIHYTYDVMKEKGYGWPVVKLNLKYVQPTVFRQKILVELALVEYESCIRIDYVIRDAVTNQKLTSGSTTQVAVEIKSGEMQLQTPPCWRSAVENHRTFQAENAS","814054","","conserved hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
G3DSA:3.10.129.10\"[2-140]Tno description


","BeTs to 13 clades of COG0824COG name: Predicted thioesteraseFunctional Class: RThe phylogenetic pattern of COG0824 is -omp-z-q-dr-bcefghsnuj--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 6.2e-07) to 1/1 blocks of the IPB000365 family, which is described as \"4-hydroxybenzoyl-CoA thioesterase family active site\". Interpro entry for IP:IPR000365. IPB000365 14-43 6.1e-07","Residues 10 to 79 match (4e-14) PD:PD007339 which is described as COMPLETE PROTEOME HYDROLASE THIOESTERASE 4-HYDROXYBENZOYL-COA ESTERASE YBGC 3.1.-.- ALR4079 SIMILAR ","","","","","","","","","","","","Mon Jan 6 16:52:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01188 is paralogously related to AA02837 (3e-04).","","","","","","","","","","","","","","1","","","" "AA01189","815418","814495","924","ATGACTTCACAACATTGGGCGCAACAACATGAACGGGGCAGCAAGTTTTTCTTAAACTTAACCCGTTTGATCGTGCAATATTGCCCACTTTGGGTGATTCGAATCGTGACCTTTGTCGTAGTGAGTTATTTTTTCCTCACCTCCGCAAAAGCACGTCGCCACATTCGCCGTTATCATCAGCGTTTACAGCGCACGTTCCCGCAGTTGACCCTGCCCCGCTATGCCTTATTCCGTCATTTTTTAGCCTTCGGCGAAGCCATCGCCGATCGTTTTGCCGTGTGGCAGAAAAAAATCCGTTATCCCGATTTGATTTTGGACGATAGTGATAACGTGTATCGTGACATTCGTTCCGAAGGGCGCGGCCAGATTCTGATTTGCTCCCATTTCGCCAATATTGAAATTTGTCGTGCGCTGGTGGACAGCAGACATCACGGCAATTTCCGCCTGAATATTTTGGTGCATAATCGCCATGCGCAGGCATTTAACAAGGCCTTGGAAAAGGCGGGCGCCACCTCGTTGCCGTTAATTCAGGTGGAAGATTTGGATACGCAAAAAATGCTGGAATTGAATGAACGTATTGAACGGGGCGAGTGGATCTCTATTGCCGCCGATCGCATTCCGGTGCGTGGCAATAAAACCGAACAGGTGGATTTTCTGGGTTCACCGGCAACCTTCCCGCAGGGCCCGTGGTTGTTGGCGAGCTTGTTGAAAACGCCGATTAATACTGTGTTCTGCGTGAAAAAACGCGGCGAATACCATTTAAAATTGCGTCATTTTTCCCCGCCCATTGAAGGCAGAGGCAAACAGCGCAACGAGAATATCAAACGCGCCATGCAACAATATGCCGATATTCTTGCCAAAGAATGTGAAGAAAATCCGCTCTATTGGTTTAATTTTTACGATTTCTGGGACGATTATTCAAAA","","","37265","MTSQHWAQQHERGSKFFLNLTRLIVQYCPLWVIRIVTFVVVSYFFLTSAKARRHIRRYHQRLQRTFPQLTLPRYALFRHFLAFGEAIADRFAVWQKKIRYPDLILDDSDNVYRDIRSEGRGQILICSHFANIEICRALVDSRHHGNFRLNILVHNRHAQAFNKALEKAGATSLPLIQVEDLDTQKMLELNERIERGEWISIAADRIPVRGNKTEQVDFLGSPATFPQGPWLLASLLKTPINTVFCVKKRGEYHLKLRHFSPPIEGRGKQRNENIKRAMQQYADILAKECEENPLYWFNFYDFWDDYSK","814497","","conserved hypothetical protein (possible glycosyl transferase)","Cytoplasm","","
InterPro
IPR004960
Family
Bacterial lipid A biosynthesis acyltransferase
PF03279\"[10-305]TLip_A_acyltrans
noIPR
unintegrated
unintegrated
tmhmm\"[27-47]?transmembrane_regions


","BeTs to 4 clades of COG1560COG name: Lauroyl/myristoyl acyltransferase involved in lipid A biosynthesisFunctional Class: NThe phylogenetic pattern of COG1560 is ----------r---efghsnujxi--Number of proteins in this genome belonging to this COG is","","Residues 5 to 303 match (3e-40) PD:PD319838 which is described as COMPLETE PROTEOME TRANSFERASE TRANSMEMBRANE PLASMID XF0775 RSP0366 ACYL ENZYME RSC0431 ","","","","","","","","","","","","Mon Jan 6 16:56:02 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01189 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 10 to 305 (E-value = 8.2e-06) place AA01189 in the Lip_A_acyltrans family which is described as Bacterial lipid A biosynthesis acyltransferase (PF03279)","","","","","","","","1","","","" "AA01190","816137","815418","720","ATGCAAAAGGTCATTGTGATTATTCCTCATTACAACCATTCCGCCACTGTAGGCGAGGTGGTAAGGCAGTTGCGCGCCTTGGATTTACCCGTTTTGGTCGTGGATGACGGTTCCGCCGAAAATCACCTGAGCGTCCTTCGGACGTTACAACAACAGCCTGAGGTTTTTATACATTATTGCCCGACCAACGGCGGCAAAGGTGCGGCAATGAAAACGGGTTTTCGCCTTGCGGCGGATATGGGATTTAGTCACGCCGTGCAAGTGGATGCGGACGGGCAACATCACTTGCCCGATGTGTTAAAAATGATCGCAGAAATGCAGAAAAATCCCACCGCACTTATTTGCGGTCGCCCGCTTTATAGCGACGACGCACCGAAAGCGCGCCTGTACGGACGCAAAATCACCGATTTCTGGAACGCCATTCATACCCTTTCCCTGGACATTAAAGACGGTATGTGCGGTTTTCGGTTGTATCCTTTAGCTTCCATTTTATCGCTCATGCAACAGGAATCCCTTGGCAATCGCATGGATTTTGATATTGATATTTTGGTGAAAGCCCATTGGTACCAAATCCCGTTGGTGTGGGTGGATACGCCGGTGCGTTACGAACCGGGCGGCATTTCGCATTTTCGCGGGTTTGCCGATAACTGGGAGATCAGCAAACTGCACACCCGATTATTTTTTGGTATGCTGTGGCGCATTTGCACGGGGCGGAAAGTA","","","30670","MQKVIVIIPHYNHSATVGEVVRQLRALDLPVLVVDDGSAENHLSVLRTLQQQPEVFIHYCPTNGGKGAAMKTGFRLAADMGFSHAVQVDADGQHHLPDVLKMIAEMQKNPTALICGRPLYSDDAPKARLYGRKITDFWNAIHTLSLDIKDGMCGFRLYPLASILSLMQQESLGNRMDFDIDILVKAHWYQIPLVWVDTPVRYEPGGISHFRGFADNWEISKLHTRLFFGMLWRICTGRKV","815420","","glycosyl transferase (possible dolichol-phosphate mannosyltransferase)","Cytoplasm, Inner membrane","","
InterPro
IPR001173
Domain
Glycosyl transferase, family 2
PF00535\"[5-164]TGlycos_transf_2
noIPR
unintegrated
unintegrated
G3DSA:3.90.550.10\"[3-209]Tno description
PTHR10859\"[11-234]TGLYCOSYLTRANSFERASE RELATED


","BeTs to 17 clades of COG0463COG name: Glycosyltransferases involved in cell wall biogenesisFunctional Class: MThe phylogenetic pattern of COG0463 is aompkzyqvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is","","Residues 4 to 108 match (6e-09) PD:PD395383 which is described as TRANSFERASE COMPLETE PROTEOME SYNTHASE GLYCOSYLTRANSFERASE MANNOSYLTRANSFERASE DOLICHOL-PHOSPHATE MANNOSE GLYCOSYL DOLICHYL-PHOSPHATE ","","","","","","","","","","","","Wed Feb 19 15:36:03 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01190 is paralogously related to AA02636 (3e-08) and AA01593 (2e-06).","","","","","","Residues 5 to 164 (E-value = 1e-16) place AA01190 in the Glycos_transf_2 family which is described as Glycosyl transferase (PF00535)","","","","","Ernst B, Oehrlein R.Substrate and donor specificity of glycosyl transferases.Glycoconj J. 1999 Feb;16(2):161-70. Review.PMID: 10612415","","Wed Feb 19 15:36:03 2003","1","","","" "AA01191","817498","816140","1359","ATGATAAATAACCTACATTTTTTCAATATCCCCGATTTATGGCATGACCAAGGCGATGAGACCGCGCTGATTGCGCGCAATCCCGATTGGCAATGGGCGGATTTTCGTACACGCGCACGGCAAATTGCTGAGCAGTTGACACAGGATAACGTGAAATCCGTGGCGTTCTGGTTTGACGATGCCGCCTTGTTTGCCTGCGCCATGTTGGCGTGCTTTCATGCCGGTGTGCGGATTTTACTGCCACCCAATTTACTGGCGGAAAATCAGCAATGGATCAAAGAAAACGCCGATTTTTTGTTGGATGATGCGTTGTTCGCCGAGTATGGCATCACGCAACACGCCTCGCAAAAACACCCGGCAAAACGACCGCACTTTAATGTCTGTAACCAAACGGAAATCTGGCTGAAAACCTCCGGCAGCAGCGGTCAGCCGAAGATTCTGGTGAAGACCGCCGCACAGATGTGGCTGGAATCGGCGGCGATTCGTCAATCCTTGCCTTTCTCCACCAGCAATGACATTCATTTGGTCTCCAGCGTTTCCGCTCAACACCATTACGGCTTGTCCTATCGCATTATTCTACCCCTCACCATGGGCTGGAGCATTGCCCGAAAGCAGTTGCCTTATCCGGAATATTTAATTGAAGAAAGTCTGCTCGCGCCGAAAACGGTGTGGATTAGTAGCCCGGCATTGTTGACCCGTTTAAATTTAGCCGACACGAAATTAAAACAATGCGCTTTTGCAGGCGTCATTTCCTCCGGCGGCGTATTGCCTGCCGACGTGGGCAACGCCATCCGCGAGAGATTAGGCGTTAAGCTGATTGAATGCTACGGCAGTACGGAAACCGGCGCCATCGCTTTTCGTGCTGATGACGGCTTGTGGCAACCGACCCCGCTCACAACCGTTGGATTAAACGAAGAAGGCGCTCTATGGGTGGAATCTGAGTGGCTCAACCAACGTGAGCAAACCGCCGATGCCGCCGAATTGATTGACGGCAAATTCAATTTATTGGGACGCCTTGATCGCATTGTGAAATTCGGTGATAAACGTATTTCTCTGGTGAAAATCGAACAGGATTTATTGCGCCATCCCTGGGTGACGGATTGTTATGTGGCGCAACATCCGCAGCATTTACGTCCGGCAGCTTGGGTCGCTTTGAATGAGGCGGGCATTGCGGCGTACCGGCAACAAGGGCGTCATGAATTTGTCAATGAATTACGCGCGTTTTTAATGCAAACCCAAGAGCGCGCCGGCTTGCCACGTTTTTGGCGATTCACCACGGAGTTGCCGCGCAACAGCCAGTCAAAACTCAGCAAAGAGGCTTTTTATCAGGTATTTTTAACGGAAAAAGAGGAACATTTT","","","55674","MINNLHFFNIPDLWHDQGDETALIARNPDWQWADFRTRARQIAEQLTQDNVKSVAFWFDDAALFACAMLACFHAGVRILLPPNLLAENQQWIKENADFLLDDALFAEYGITQHASQKHPAKRPHFNVCNQTEIWLKTSGSSGQPKILVKTAAQMWLESAAIRQSLPFSTSNDIHLVSSVSAQHHYGLSYRIILPLTMGWSIARKQLPYPEYLIEESLLAPKTVWISSPALLTRLNLADTKLKQCAFAGVISSGGVLPADVGNAIRERLGVKLIECYGSTETGAIAFRADDGLWQPTPLTTVGLNEEGALWVESEWLNQREQTADAAELIDGKFNLLGRLDRIVKFGDKRISLVKIEQDLLRHPWVTDCYVAQHPQHLRPAAWVALNEAGIAAYRQQGRHEFVNELRAFLMQTQERAGLPRFWRFTTELPRNSQSKLSKEAFYQVFLTEKEEHF","816142","","AMP-binding enzyme","Cytoplasm","","
InterPro
IPR000873
Domain
AMP-dependent synthetase and ligase
PF00501\"[32-302]T\"[330-370]TAMP-binding
noIPR
unintegrated
unintegrated
G3DSA:3.30.300.30\"[340-445]Tno description
G3DSA:3.40.50.980\"[128-299]Tno description
PTHR11968\"[14-448]TATP-DEPENDENT AMP-BINDING ENZYME FAMILY MEMBER
tmhmm\"[61-81]?transmembrane_regions


","BeTs to 9 clades of COG0365COG name: Acyl-coenzyme A synthetases/AMP-(fatty) acid ligasesFunctional Class: IThe phylogenetic pattern of COG0365 is aomp-zyq-dr-bcefghs-uj----Number of proteins in this genome belonging to this COG is","","Residues 133 to 287 match (5e-08) PD:PD040658 which is described as LIGASE SYNTHASE 4-COUMARATE--COA METABOLISM 4-COUMAROYL-COA PHENYLPROPANOID 4CL PROTEOME RSP0367 COMPLETE ","","","","","","","","","","","","Tue Jan 7 10:33:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01191 is paralogously related to AA01193 (1e-119) and AA02108 (5e-08).","","","","","","Residues 31 to 370 (E-value = 1.5e-09) place AA01191 in the AMP-binding family which is described as AMP-binding enzyme (PF00501)","","","","","Eichler K, Bourgis F, Buchet A, Kleber HP, Mandrand-Berthelot MA.Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli.Mol Microbiol. 1994 Sep;13(5):775-86.PMID: 7815937","","Wed Jan 29 14:05:57 2003","1","","","" "AA01192","818037","817498","540","ATGAAAGTACTTATTAATGTGTTACTCAGCCTCACCGGCGTGGCTTATCCCATCATTTGGTTGTTTGCCGAAGATCAAACGCCGTTGTTTTATTTGCCTTGGATAATGGCATTGCTGTGGGCGGCGAAAGGCTTCTTTCAGCAGCAAGGGCAGCGCTATTTCGCTTGGGCGATGGCATTGATTCTGGCGGTGGTGGGCATCACCCGTTCCGTTGAAACCATGTTTTGGTATCCCATTATTATTAACGGCTTAATGTTGTCCCTGTTCGGTGGCAGCTTATGGAGCGAACAAACCGTGGTAGAGCGTCTCGCCCGTTTGCAGACACCCGATTTAAGCGAAGCCGGTGTGCGTTATACGCGTAAAGTAACCCAACTGTGGTGCGGTGTCTTCGTGATTAATATCGTCATTATCGCCTCGGCAATTTGGTTGAAATATTACGATTTCTGGGCGTTATACACCGGCGTGCTTTCTTATTGCTTCATCGGCATGGTGATGGCGGGGGAATGGCTGGTTCGACAAAAAGTCAAAAAACAACAAACA","","","20853","MKVLINVLLSLTGVAYPIIWLFAEDQTPLFYLPWIMALLWAAKGFFQQQGQRYFAWAMALILAVVGITRSVETMFWYPIIINGLMLSLFGGSLWSEQTVVERLARLQTPDLSEAGVRYTRKVTQLWCGVFVINIVIIASAIWLKYYDFWALYTGVLSYCFIGMVMAGEWLVRQKVKKQQT","817500","","conserved hypothetical protein (possible membrane protein)","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-15]?signal-peptide
tmhmm\"[2-22]?\"[28-46]?\"[53-71]?\"[75-95]?\"[125-145]?\"[151-171]?transmembrane_regions


","No hits to the COGs database.","","Residues 51 to 177 match (5e-26) PD:PD299574 which is described as PROTEOME COMPLETE TRANSMEMBRANE MEMBRANE Z4855 PLASMID INTEGRAL PROBABLE RSP0368 ","","","","","","","","","","","","Tue Jan 7 09:56:33 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01192 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01193","819732","818068","1665","ATGTTTGCCAAATATACCGACAATAGTCTTATTGCAAACCATCCCGAGTGGTGTTATGCGGATTTCACACAAAAAGCTCTGCAAATTTCCGCCGAATTACAACAGCGTCAAATTAAAGCCATTGCCGTTTGGCTGGAAGACGGTGCCAAACTGGCGTGCACCTTATTAGCTGCGTGGCACGCCAATGTGCGGGTGTTATTTCCACCGAATTTCACCCCGGAAAGCATTCAATGGGTGAATGAAAATGCCGATCTCTGGCTCACCGACAGCGACATAGACCAACCGACAGCGGAATGGTTTGATCGCTTTGGTGAATCCCGCCACATTGAAAAACACCCGCAAAATCCACCGCTCTTTGACTACACCAATCAGACCGAAATCTGGCTGAAAACCTCCGGCAGCACCGGAGAAGCGAAAACCATCGTGAAAACCGCCGAACAAATGTGGCTTGGTGCGGAAGCCCTTGCCACGGCATTGCCGTTTAACGCGGATAACACCGTTACCGCCTTGAGCACCGTCAGTATTCAGCATATTTACGGCTTAACCGTGCATATCATGATGTCTTTGGTGAATGGTTGGCAAATCGGGCGCAAACAACAGTTTTATCCGGAATGTATCATCAGCGAAGCGCAAAAAAGCACGCAAACCGTGGTAGTCAGCAGCCCCACTATGTTGTCACGAATTGACTGGCAGAATACCAAAATGCCGCAAACCATTGCGGGGGTGATTTCTTCCGGCGGCGCATTGGCGGAAGACATTTCCGAGCAAATGCGCCAGGTGTTGCAACAACCGGTGATTGAGATCTATGGCAGCACGGAAACCGGCCCGATCGCCATTCGTGACGACATTCATTTGTGGCAAACGTTACCGAACAGTCGATTAGGCAGTGATGAACAGGGTGCCCTGTGGATTGAAGGTTGCTGGTTGTCCGCCCGCGAACAAACCGCCGATATGGTGGAATTTTTAGCGGACGGCTTCCGCCTGCTCGGGCGTAGCGATCGCATTGTGAAAATCGGCGATAAACGCACCTCCCTTGCCGGCATTGAAGGCAAATTGCTGCAACATGACTGGGTGGACGATTGTTATATCGCACAACATCCCGAGGTCCCCCGCTTGGCGGCGTGGGTCGGTTTACATGCGCAGGGTGTGGAAATTTTGCGTGAAAAGGGGCGTCGTTATCTCATCGAACAGTTCAAAGATTATTTGGCGGAAACCCAGGACAAAACCGCCATTCCGCGTTTCTGGCGTTTTACCGATAAACTTCCGCGCAACAGTCAATCGAAAATAAATAAGCCGGAATTTAACCGCACTTGTGTGGAAGCACAGCGTGATCCGATTTGGTTTACGCAGGAAAAAGATGAGCGACATTATCAGGCGACGGGCAAAGTGCCTTTGGATTTGCTGTATTTGAAAGATCATTTCGCCAATTTTCCGCTTGTGCCGGGCGTCATTGAGCTGCAATGGATTAGCGAAAAAGTGAACGCGTTCTTGGGGCGTGAAGTGACATTTAGTCGCGTCGATAAACTCAAGTTCCAGAAATTCCTTCGTCCGAACGACACCTTCATATTGCAACTGAACGCCAACGAATCGCTGGACAAAATCACCTTTCAGTTAAAGGTGGACAATGAAATCTGTTGTAGCGGCGTGGCGATTTTGGCACGAACA","","","63214","MFAKYTDNSLIANHPEWCYADFTQKALQISAELQQRQIKAIAVWLEDGAKLACTLLAAWHANVRVLFPPNFTPESIQWVNENADLWLTDSDIDQPTAEWFDRFGESRHIEKHPQNPPLFDYTNQTEIWLKTSGSTGEAKTIVKTAEQMWLGAEALATALPFNADNTVTALSTVSIQHIYGLTVHIMMSLVNGWQIGRKQQFYPECIISEAQKSTQTVVVSSPTMLSRIDWQNTKMPQTIAGVISSGGALAEDISEQMRQVLQQPVIEIYGSTETGPIAIRDDIHLWQTLPNSRLGSDEQGALWIEGCWLSAREQTADMVEFLADGFRLLGRSDRIVKIGDKRTSLAGIEGKLLQHDWVDDCYIAQHPEVPRLAAWVGLHAQGVEILREKGRRYLIEQFKDYLAETQDKTAIPRFWRFTDKLPRNSQSKINKPEFNRTCVEAQRDPIWFTQEKDERHYQATGKVPLDLLYLKDHFANFPLVPGVIELQWISEKVNAFLGREVTFSRVDKLKFQKFLRPNDTFILQLNANESLDKITFQLKVDNEICCSGVAILART","818070","","AMP-binding enzyme","Cytoplasm, Extracellular","","
InterPro
IPR000873
Domain
AMP-dependent synthetase and ligase
PF00501\"[131-279]T\"[315-363]TAMP-binding
noIPR
unintegrated
unintegrated
G3DSA:3.10.129.10\"[453-553]Tno description
G3DSA:3.30.300.30\"[333-448]Tno description
G3DSA:3.40.50.980\"[122-292]Tno description
PTHR11968\"[16-453]TATP-DEPENDENT AMP-BINDING ENZYME FAMILY MEMBER


","BeTs to 5 clades of COG0365COG name: Acyl-coenzyme A synthetases/AMP-(fatty) acid ligasesFunctional Class: IThe phylogenetic pattern of COG0365 is aomp-zyq-dr-bcefghs-uj----Number of proteins in this genome belonging to this COG is","","Residues 127 to 291 match (2e-09) PD:PD040658 which is described as LIGASE SYNTHASE 4-COUMARATE--COA METABOLISM 4-COUMAROYL-COA PHENYLPROPANOID 4CL PROTEOME RSP0367 COMPLETE ","","","","","","","","","","","","Tue Jan 7 10:32:39 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01193 is paralogously related to AA01191 (1e-119), AA02108 (8e-08), AA02598 (9e-06), AA02512 (2e-05) and AA00611 (2e-04).","","","","","","Residues 18 to 363 (E-value = 2.9e-08) place AA01193 in the AMP-binding family which is described as AMP-binding enzyme (PF00501)","","","","","Eichler K, Bourgis F, Buchet A, Kleber HP, Mandrand-Berthelot MA.Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli.Mol Microbiol. 1994 Sep;13(5):775-86.PMID: 7815937","","Wed Jan 29 14:05:01 2003","1","","","" "AA01194","819983","819735","249","ATGACCGAACAGGAAATCCGCGACTTACTCAGTGAAGCGCTGGAATATTTATTTGAGATCGAACCGGAGAGAATCAAACCGGACACCAATCTGTACGAAGATTTGGAAATCGATAGCATTGATGCCATTGATTTAATCGACCACATTAAACGAAAAACCGGACATAAATTACAAGCGGAAGATTTTCGTAATGTCCGCACCGTGGATGATGTGGTTAAAGCCGTTCTGAAACTGAGCCAAAACGCACAA","","","9679","MTEQEIRDLLSEALEYLFEIEPERIKPDTNLYEDLEIDSIDAIDLIDHIKRKTGHKLQAEDFRNVRTVDDVVKAVLKLSQNAQ","819737","","acyl carrier protein","Cytoplasm","","
InterPro
IPR006163
Domain
Phosphopantetheine-binding
PF00550\"[8-75]TPP-binding
PS50075\"[2-76]TACP_DOMAIN
InterPro
IPR009081
Family
Acyl carrier protein-like
G3DSA:1.10.1200.10\"[1-75]Tno description
noIPR
unintegrated
unintegrated
PTHR20863\"[1-83]TACYL CARRIER PROTEIN/ZINC FINGER PROTEIN 593-RELATED


","BeTs to 18 clades of COG0236COG name: Acyl carrier proteinFunctional Class: I,QThe phylogenetic pattern of COG0236 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 1 to 82 match (2e-13) PD:PD508963 which is described as CARRIER PROTEOME COMPLETE ACYL ","","","","","","","","","","","","Tue Jan 7 10:12:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01194 is paralogously related to AA00268 (1e-04).","","","","","","Residues 8 to 75 (E-value = 4.6e-08) place AA01194 in the PP-binding family which is described as Phosphopantetheine attachment site (PF00550)","","","","","Hoang TT, Sullivan SA, Cusick JK, Schweizer HP.beta-Ketoacyl acyl carrier protein reductase (FabG) activity of the fatty acid biosynthetic pathway is a determining factor of 3-oxo-homoserine lactone acyl chain lengths.Microbiology. 2002 Dec;148(Pt 12):3849-56.PMID: 12480888Keating MM, Gong H, Byers DM.Identification of a key residue in the conformational stability of acyl carrier protein.Biochim Biophys Acta. 2002 Dec 16;1601(2):208-14.PMID: 12445484 Waters NC, Kopydlowski KM, Guszczynski T, Wei L, Sellers P, Ferlan JT, Lee PJ, Li Z, Woodard CL, Shallom S, Gardner MJ, Prigge ST.Functional characterization of the acyl carrier protein (PfACP) and beta-ketoacyl ACP synthase III (PfKASIII) from Plasmodium falciparum.Mol Biochem Parasitol. 2002 Aug 28;123(2):85-94.PMID: 12270624","","Tue Jan 7 10:12:07 2003","1","","","" "AA01195","820249","819989","261","ATGGAACTGGAACAACAGCTTAAACAACTTATTATTGATAGCCTCGCGTTAGAAGATATTGGTATTGAAGACATTGATAACGATACTGTCTTGTTCAGCGACAGCGGTTTGGGATTGGATTCCGTTGATGCCCTTGAACTTGGTCTGGCGGTGCAAAAAACCTTCGGTTTACAGTTGGATAGCGAACAAACCCAACTTAGTGATCATTTTGCAAGCGTCGCCACGCTGGCGCAATTCATCCGCAGCCAAAAAGGTGAGGTA","","","9462","MELEQQLKQLIIDSLALEDIGIEDIDNDTVLFSDSGLGLDSVDALELGLAVQKTFGLQLDSEQTQLSDHFASVATLAQFIRSQKGEV","819991","","acyl carrier protein","Cytoplasm","","
InterPro
IPR006163
Domain
Phosphopantetheine-binding
PS50075\"[3-78]TACP_DOMAIN


","No hits to the COGs database.","","Residues 2 to 84 match (2e-19) PD:PD331683 which is described as PROTEOME COMPLETE PHOSPHOPANTETHEINE CARRIER ACYL ACYL-CARRIER PLASMID PROTEIN ACYL-CARRIER-PROTEIN ACPC ","","","","","","","","","","","","Tue Jan 7 10:24:39 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01195 is paralogously related to AA00268 (1e-05).","","","","","","","","","","","Hoang TT, Sullivan SA, Cusick JK, Schweizer HP. beta-Ketoacyl acyl carrier protein reductase (FabG) activity ofthe fatty acid biosynthetic pathway is a determining factor of3-oxo-homoserine lactone acyl chain lengths. Microbiology. 2002 Dec;148(Pt 12):3849-56. PMID: 12480888 Keating MM, Gong H, Byers DM. Identification of a key residue in the conformational stability ofacyl carrier protein. Biochim Biophys Acta. 2002 Dec 16;1601(2):208-14. PMID: 12445484 Waters NC, Kopydlowski KM, Guszczynski T, Wei L, Sellers P, FerlanJT, Lee PJ, Li Z, Woodard CL, Shallom S, Gardner MJ, Prigge ST. Functional characterization of the acyl carrier protein (PfACP)and beta-ketoacyl ACP synthase III (PfKASIII) from Plasmodiumfalciparum. Mol Biochem Parasitol. 2002 Aug 28;123(2):85-94. PMID: 12270624McAllister KA, Peery RB, Meier TI, Fischl AS, Zhao G. Biochemical and molecular analyses of the Streptococcus pneumoniaeacyl carrier protein synthase, an enzyme essential for fatty acidbiosynthesis. J Biol Chem. 2000 Oct 6;275(40):30864-72. PMID: 11032795","","Thu Feb 13 16:05:27 2003","1","","","" "AA01196","821015","820230","786","ATGGCAGAAAAGCTAGACTGGCTACGCCGCTTTGTGTTCACCACCATCGGGTTTCTGTTTTGGGGCGTGGCAGGCACATTGTTACAACTAGTACTTTATCCTTATGCACGTAAACATAAACACGGCGATTTGCAAACCCAACTGAAAGTGCGCCGTTTTGTTGGGGGTAGCTGGTATTATTTCATCCGCTATTTATCCTGTGCCGGCGTGTTGGAGGTGAGTTATAAAGGCTTTGAAAAACTTGGGCGTACCGGGCAGCTAATTTTGCCGAATCACCCGTCCTTATTGGATGTGGTGCTCATTTTGGGGAAAACACCAACTCTGAATTGCATTGTGAAAAAGGAGCTGTTGGATAACCCCACCATGCGCAATCAAATTTTAGCCTGCGGTTTTTTGCCTAATACGGAATCCGTAGAACTGTTGGAACAAAGCCATGAAGTGTTGCAACAACAGGCGTTACTGCTGTTTGCCGAAGGCACGCGCACAGGCTGGAACGGCGAAGTGAAACTGAATCGCGGCGCGGTATCCATCGGGTTACGCAGCGCCAAAGTGATTACGCCGGTGGTGATTCGGATGAATCCGCTCAGCTTAAAAAAAGGGCATCCGTGGTATAAAATCCCGCGCAAACGTATTCATTATGAATTGATTGTTGGTGACGATATTGACCCGCAAGATTGGCTGAAAGAACAGTCAATTCCTATGGCATCACGCCGCTTAACCAAATATCTGGAAAATTATTTCAACACACATATAAAGGACAACGAAAATGGAACTGGAACAACAGCT","","","30150","MAEKLDWLRRFVFTTIGFLFWGVAGTLLQLVLYPYARKHKHGDLQTQLKVRRFVGGSWYYFIRYLSCAGVLEVSYKGFEKLGRTGQLILPNHPSLLDVVLILGKTPTLNCIVKKELLDNPTMRNQILACGFLPNTESVELLEQSHEVLQQQALLLFAEGTRTGWNGEVKLNRGAVSIGLRSAKVITPVVIRMNPLSLKKGHPWYKIPRKRIHYELIVGDDIDPQDWLKEQSIPMASRRLTKYLENYFNTHIKDNENGTGTTA","820232","From GenBank (gi:12230506): This protein converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position. ","1-acyl-sn-glycerol-3-phosphate acetyltransferase","Inner membrane, Cytoplasm","","
InterPro
IPR002123
Domain
Phospholipid/glycerol acyltransferase
PF01553\"[72-191]TAcyltransferase
SM00563\"[86-193]TPlsC
noIPR
unintegrated
unintegrated
PTHR10434\"[58-190]T1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE
signalp\"[1-25]?signal-peptide
tmhmm\"[15-35]?transmembrane_regions


","BeTs to 11 clades of COG0204COG name: 1-acyl-sn-glycerol-3-phosphate acyltransferaseFunctional Class: IThe phylogenetic pattern of COG0204 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","","","","","","","","","","","","Tue Jan 7 11:10:33 2003","Fri Mar 25 08:43:08 2005","","Fri Mar 25 08:43:08 2005","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01196 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Fri Mar 25 08:43:08 2005","","","","","Residues 72 to 191 (E-value = 1.5e-05) place AA01196 in the Acyltransferase family which is described as Acyltransferase (PF01553)","Fri Mar 25 08:43:08 2005","","","","Heath RJ, Goldfine H, Rock CO.A gene (plsD) from Clostridium butyricum that functionally substitutes for the sn-glycerol-3-phosphate acyltransferase gene (plsB) of Escherichia coli.J Bacteriol. 1997 Dec;179(23):7257-63.PMID: 9393688Coleman J.Characterization of the Escherichia coli gene for 1-acyl-sn-glycerol-3-phosphate acyltransferase (plsC).Mol Gen Genet. 1992 Mar;232(2):295-303.PMID: 1557036 ","","Tue Jan 7 10:48:12 2003","1","","","" "AA01197","821743","821003","741","ATGACGCAAACGATTTGTCAGTTTTCATTCAATATAGCCGATTGGAAAATCGTGTGTAATAAGCAATTAAGCACCGAGGATTGGAAATCGGGTTATGCCCATTGGCAGCAAAATCAGGCAAATTTCGCCGATTTTTCGCCTAAACTTGCTTTTCTTCCGCCGCTGAAACGTCGTCGTTTAAGCGATTCCGCCCGTTTGTTTTTTGAAGCCGCCTGGGATTTGGTAGAGGAACAATCCAATTTGCCTGTAGTGTACGCTTCCGCAAATAGTGAAATTAACCGGAATTTCACGTTATGGTATTCATTATTGACGGAAGGTGACGTGTCACCGACTTCCTTTAGTTTGTCGGTGCATAACGCCCTTATCGGCCAATGGTCGGAGTTCCGTCAGGTGAAAGCGGAAACCACCGCTTTAACGGCAAATAAAGACAACTTGGAAGTGGCATTATTGGAAGCCTATTTATTACTCAAAGAAGGCGCAAAAAAAGTGTTGGTGGTGATTGCCGAATCGCCGTTGGAGCTGCGTTATAACGTGCAGCCTGTGGTGCGCCGGCCGTTTATTTATGCTTTGGCATTGGTGGTTGAAGCGGGCGGGCAATATCAGTTAAGCCTGACTAATCAAGCACCGAAAGCGGACGATGTTCCTGATACGGCGTTGGAATGGGTGAAAAATCAACATCTGGATTGTACGCAATGGCGTACGCCGAGTAGCGCCGGGGGAGCTTGGTTATGGCAGAAAAGC","","","27957","MTQTICQFSFNIADWKIVCNKQLSTEDWKSGYAHWQQNQANFADFSPKLAFLPPLKRRRLSDSARLFFEAAWDLVEEQSNLPVVYASANSEINRNFTLWYSLLTEGDVSPTSFSLSVHNALIGQWSEFRQVKAETTALTANKDNLEVALLEAYLLLKEGAKKVLVVIAESPLELRYNVQPVVRRPFIYALALVVEAGGQYQLSLTNQAPKADDVPDTALEWVKNQHLDCTQWRTPSSAGGAWLWQKS","821005","","conserved hypothetical protein","Periplasm","","No hits reported.","No hits to the COGs database.","","Residues 7 to 201 match (1e-13) PD:PD560672 which is described as PROTEOME Z4851 COMPLETE ","","","","","","","","","","","","Tue Jan 7 10:49:41 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01197 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01198","822111","821776","336","TTGATAGTAAAAAAGATGAAAACCGTACGTAAGTATAGCATTTTTATTGATAACGAATACATGGTTCTTGCGGTGCGCCAATTGCTTTCGAACCGGAGCCTAGGTAAAATTGACCCGGTTTTTATCTTTACTATTTTAGCCGAACCGGTGAAAGAAAAAGGCAATTGTGATCGTATTTTATTTTTCACTGTCAAAGGAAATAGCCGTATTATCGCCGGAGCTAAACCGGATTTGCGCGACGTCGCCGTCAAGCAACTTAGGTTTTTTTATCTTATAAACGTCGTGGCGATGAAGACGATCGTGTTGATCAGGTCGGCTTACAAGGTTAAACAGACT","","","12864","LIVKKMKTVRKYSIFIDNEYMVLAVRQLLSNRSLGKIDPVFIFTILAEPVKEKGNCDRILFFTVKGNSRIIAGAKPDLRDVAVKQLRFFYLINVVAMKTIVLIRSAYKVKQT","821778","","hypothetical protein","Inner membrane, Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Tue Jan 7 10:50:27 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01198 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01199","822124","822546","423","ATGAAACTGATGACTAAATTAACCTTTGCCGTTGCGACTGTATTTATCGCCGCCTGTGCCCCGCGTGATACCACTCATCACTATGATATTCAAAGTGTATTGAATTCCCCTGAAGCACAGCGTTTCCTCAACCCGAATGTAAAACTTTACTTCGGTAAACCGGCACCGGGTAAAGTGGTGGTCGACAATGCTGTCACCAACAAGAAAACCAATGCTGCCAACAAATCTGACGAAAAAGCCTGCAAACGCGCTTTCTTGTCTGCCGTTAAGCAATTACAGGATAAAGCACAATCTTCCGGCGCCACCAAAGTGGGCAATATCGTCAGTTACTACAAGAAAAACGTTTATAAAAGTACCACTCAATATGAATGCCACGCCGGTCATCTTATCGCTGGTGTAGCCTTAAAAGGCGATATTGTGAAA","","","19138","MKLMTKLTFAVATVFIAACAPRDTTHHYDIQSVLNSPEAQRFLNPNVKLYFGKPAPGKVVVDNAVTNKKTNAANKSDEKACKRAFLSAVKQLQDKAQSSGATKVGNIVSYYKKNVYKSTTQYECHAGHLIAGVALKGDIVK","822548","","conserved hypothetical protein","Periplasm, Outer membrane","","
InterPro
IPR003006
Family
Immunoglobulin/major histocompatibility complex
PS00290\"[122-128]?IG_MHC
noIPR
unintegrated
unintegrated
PS51257\"[1-19]TPROKAR_LIPOPROTEIN
signalp\"[1-19]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Tue Jan 7 10:51:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01199 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01201","823363","822653","711","ATGAAATTCTACCGCACTTTAATGCCTTTTCAGGTGATTAGTTTTGATTTAGACGACACCCTTTACGACAATTCGCACGTCATCACCACGGCGGAACAGAAATTCGTCACCTTCGTGCAACAACATTGCCACATGGCGGATTTTAGTTTGGAAATGTGGGCGGCGTATAAAAGAGCCACCGCACAACATAATCCGCTGATGGCAGAAGATGTGACCTTATGGCGCTTGCGCAGTTTGCAGGTATTGCTGGCAGAACGGGGCAAAAGTGCGGTGGAAATTGCCGGTGTTTCGCAAACCGCGATGGATTACTTCTTACATTGGCGCCATCAAATTGACGTGCCGCCACAAAGTTTTGCCGTTCTGCAACAGCTAAAACCGCGATATAAATTGGTGGCAATTACCAACGGCAATGTGGATCCCGTGCGTATCGGTTTTGATCAGTTTGATTTGGTGTTACGCGGCGGTAAGCATGGGCGGGCAAAGCCCCATAAAGATTTATTTCTGCAAACTGCTCACTATTTTAATATTCTACCGGAACAGATTTTACATGTCGGCGATAATTTAGGTACGGATGTGCAGGGCGCCATACAGGCAGGTTGTCAGTCTGTATGGTTAAATTTGAGCGGAAAAGACATCACTGAATTTAGCGAAGTGCATATTTTGCCGACGGTGGAGATGAATGAGTTGACGGATTTGTTGCAATTATACGGA","","","33778","MKFYRTLMPFQVISFDLDDTLYDNSHVITTAEQKFVTFVQQHCHMADFSLEMWAAYKRATAQHNPLMAEDVTLWRLRSLQVLLAERGKSAVEIAGVSQTAMDYFLHWRHQIDVPPQSFAVLQQLKPRYKLVAITNGNVDPVRIGFDQFDLVLRGGKHGRAKPHKDLFLQTAHYFNILPEQILHVGDNLGTDVQGAIQAGCQSVWLNLSGKDITEFSEVHILPTVEMNELTDLLQLYG","822655","","phosphatase; hydrolase","Cytoplasm","","
InterPro
IPR000223
Family
Peptidase S26A, signal peptidase I
PS00761\"[181-194]?SPASE_I_3
InterPro
IPR005834
Domain
Haloacid dehalogenase-like hydrolase
PF00702\"[10-208]THydrolase
InterPro
IPR006439
Family
HAD-superfamily hydrolase, subfamily IA, variant 1
TIGR01549\"[68-199]THAD-SF-IA-v1: HAD-superfamily hydrolase, su
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1000\"[95-235]Tno description
PTHR12725\"[5-234]THALOACID DEHALOGENASE-LIKE HYDROLASE
PTHR12725:SF4\"[5-234]THALOACID DEHALOGENASE-LIKE HYDROLASE DOMAIN CONTAINING PROTEIN 4


","BeTs to 10 clades of COG1011COG name: Predicted hydrolases of the HAD superfamilyFunctional Class: RThe phylogenetic pattern of COG1011 is -ompk-yqvdrlb-efghsn-j--t-Number of proteins in this genome belonging to this COG is","","Residues 11 to 235 match (1e-08) PD:PD107557 which is described as DEHALOGENASE ACID HYDROLASE COMPLETE PROTEOME 2-HALOALKANOIC HALIDOHYDROLASE L-2-HALOACID HALOCARBOXYLIC HALOACID ","","","","","Tue Feb 18 14:21:46 2003","","","","","","","Tue Feb 18 14:21:46 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01201 is paralogously related to AA01421 (4e-07).","","","","","","Residues 10 to 208 (E-value = 2.2e-19) place AA01201 in the Hydrolase family which is described as haloacid dehalogenase-like hydrolase (PF00702)","","","","","","","","1","","","" "AA01202","824267","823380","888","ATGCAAAATGCCTTGCAACATTATTTCACCTATCTGCGCGTTGAACGTCAGGTCAGCCCGCATACTTTGAGCAATTATCAGCGCCAGCTTACGCGGGTCACAGCGATTCTACAGGGCGCGGGTATTACGCAATGGCAACAGGTGACGGCGAGCGTGGTGCGTTATGTGGTGGCGCAAAGCAGTAAGCAGGACGGTTTAAAAGAAAAAAGTCTGGCGTTGCGCCTTTCTGCGTTGCGCCGTTTTTTGACTTATTTGGTGCAACAGGGCGAACTGAAAGTGAATCCGGCGACGGGCATTTCCGCGCCGAAACAGGCGAAACATCTACCGAAAAATATTGACACCGATCAGGTGCAGCTGTTACTTGCCAATGACAGCAAAGAACCCATTGATATTCGTGATCGGGCGATCATCGAATTGTTATATAGTTCCGGTTTGCGCTTGTCCGAATTACAGGGCTTGAATCTCAATAGCATTCACCTCCGCTCGCGTGAAGTGCGGGTTATCGGGAAAGGTAACAAGGAACGGGTGGTGCCATTCGGGCGTTATGCCTCCCACGCCATTCAGCAATGGCTGAAAGTGCGGTTGTTATTTAACCCGAAAGACAATGCGTTATTTGTCAGCCAATTGGGTAACCGAATGTCACACCGCGCAATCCAAATGCGTTTGGAAACCTGGGGCATTCGGCAAGGTTTGAACAGCCATTTAAATCCGCATAAATTGCGCCATTCGTTTGCCACCCACATGCTGGAAGCCAGTTCCGATTTACGCGCGGTGCAAGAACTGCTCGGACACAGCAATTTATCCACCACACAAATTTATACCCACCTTAATTTCCAACATTTGGCGGCGGTGTATGATGCCGCGCACCCGCGCGCGAAACGTAAAAAA","","","33737","MQNALQHYFTYLRVERQVSPHTLSNYQRQLTRVTAILQGAGITQWQQVTASVVRYVVAQSSKQDGLKEKSLALRLSALRRFLTYLVQQGELKVNPATGISAPKQAKHLPKNIDTDQVQLLLANDSKEPIDIRDRAIIELLYSSGLRLSELQGLNLNSIHLRSREVRVIGKGNKERVVPFGRYASHAIQQWLKVRLLFNPKDNALFVSQLGNRMSHRAIQMRLETWGIRQGLNSHLNPHKLRHSFATHMLEASSDLRAVQELLGHSNLSTTQIYTHLNFQHLAAVYDAAHPRAKRKK","823382","From GenBank (gi:14917067): In E. coli, XerD participates in thesite-specific recombination at plasmid COLE1 Xer (or Cer) site atthe DIF loci in the chromosome which is involved in the normalpartition of the E. coli chromosome. It acts by catalyzing thecutting and rejoining of the recombinating DNA molecules. Actsjointly with XerC (see HD1940) and belongs to the \"PHAGE\" integrasefamily. ","integrase/recombinase","Cytoplasm, Outer membrane","","
InterPro
IPR002104
Domain
Integrase, catalytic core, phage
PF00589\"[120-283]TPhage_integrase
InterPro
IPR004107
Domain
Integrase, N-terminal SAM-like, phage
PF02899\"[5-89]TPhage_integr_N
InterPro
IPR011931
Family
Tyrosine recombinase XerC
TIGR02224\"[6-294]Trecomb_XerC: tyrosine recombinase XerC
InterPro
IPR013762
Domain
Integrase-like, catalytic core, phage
G3DSA:1.10.443.10\"[110-286]Tno description
noIPR
unintegrated
unintegrated
G3DSA:1.10.150.130\"[5-99]Tno description


","BeTs to 25 clades of COG0582COG name: IntegraseFunctional Class: LThe phylogenetic pattern of COG0582 is aompkz-qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 5.3e-12) to 2/2 blocks of the IPB002104 family, which is described as \"Phage integrase family\". Interpro entry for IP:IPR002104. IPB002104A 238-252 8.6e-06 IPB002104B 262-273 0.0002","Residues 132 to 263 match (5e-07) PD:PD569264 which is described as PROBABLE PROTEOME PLASMID COMPLETE INTEGRASE/RECOMBINASE ","","","","","","","","","","","Tue Jan 7 11:08:23 2003","Tue Jan 7 11:08:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01202 is paralogously related to AA02956 (1e-48).","","","","","","Residues 112 to 283 (E-value = 2.4e-61) place AA01202 in the Phage_integrase family which is described as Phage integrase family (PF00589)","","","","","Colloms,S.D., Sykora,P., Szatmari,G. and Sherratt,D.J.Recombination at ColE1 cer requires the Escherichia coli xerC geneproduct, a member of the lambda integrase family of site-specificrecombinases. J. Bacteriol. 172 (12), 6973-6980 (1990) PubMed: 2254268. Blakely,G., May,G., McCulloch,R., Arciszewska,L.K., Burke,M.,Lovett,S.T. and Sherratt,D.J. Two related recombinases are required for site-specificrecombination at dif and cer in E. coli K12. Cell 75 (2), 351-361 (1993) PubMed: 8402918 ","","Tue Jan 7 11:08:23 2003","1","","","" "AA01203","825101","824280","822","ATGCAATTTTCCAAAATGCACGGTTTGGGTAATGATTTTATGGTGGTGGATGCGGTGACACAGAACATTTACTTCCCGACGGAAACCATCAAACGCCTGGCGGATCGCCATCGCGGCGTTGGTTTTGATCAACTATTGGTGGTGGAGCCACCTTATGATCCCGAACTGGATTTTCATTATCGCATTTTTAACGCGGACGGCAGCGAAGTGGCGCAATGTGGCAACGGCGCACGCTGTTTTGCCCGTTTCGTGACGCTCAAAGGCTTAACCAATAAAAAAGACATCGCCGTAAGCACGCAAAACGGCAAAATGCTGCTGACCGTGAAAGAAGATGGTAACGTGCGGGTGAACATGGGCGAACCGATTTGGGAGCCGAATAAAATTCCGTTTACCGCCAATAAATTTGAGAAAAATTATATTCTGCGCACGGAAATCCAAACGGTGCTGTGCAGCGCGGTATCTATGGGCAATCCGCATTGCGTGGTGCAGGTGGAGGATATTCAAACCGCCAATGTGGAACAACTCGGTCCGCTATTGGAAAATCATGAACGTTTTCCGGAACGGGTGAATGCGGGCTTTATGCAGGTGGTGAATCGTCATCACATCAAACTACGCGTATACGAACGCGGTACCGGCGAAACCCAGGCTTGCGGTAGCGGCGCTTGTGCGGCGGTGGCGGTGGGTATTATGCAAGGCGTGTTGGATAACGAAGTGCAGGTGGATTTGCCCGGCGGCAGTTTGACCATCGAATGGCAGGGCGAAGGGCATCCGTTATACATGACCGGCAGCGCCACCCACGTGTATGACGGCGTGGTTTGTTTG","","","31173","MQFSKMHGLGNDFMVVDAVTQNIYFPTETIKRLADRHRGVGFDQLLVVEPPYDPELDFHYRIFNADGSEVAQCGNGARCFARFVTLKGLTNKKDIAVSTQNGKMLLTVKEDGNVRVNMGEPIWEPNKIPFTANKFEKNYILRTEIQTVLCSAVSMGNPHCVVQVEDIQTANVEQLGPLLENHERFPERVNAGFMQVVNRHHIKLRVYERGTGETQACGSGACAAVAVGIMQGVLDNEVQVDLPGGSLTIEWQGEGHPLYMTGSATHVYDGVVCL","824282","From GenBank (gi:8247918): This protein catalyzes the reaction:LL-2,6-DIAMINOHEPTANEDIOATE = MESO-DIAMINOHEPTANEDIOATE, involvedin the sixth step in the biosynthesis of lysine from aspartatesemialdehyde. ","diaminopimelate epimerase","Cytoplasm","","
InterPro
IPR001653
Family
Diaminopimelate epimerase
PF01678\"[3-124]T\"[151-267]TDAP_epimerase
TIGR00652\"[1-274]TDapF: diaminopimelate epimerase
PS01326\"[64-78]TDAP_EPIMERASE
noIPR
unintegrated
unintegrated
G3DSA:3.10.310.10\"[115-274]Tno description


","BeTs to 18 clades of COG0253COG name: Diaminopimelate epimeraseFunctional Class: EThe phylogenetic pattern of COG0253 is a-m----qv-r-bcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 2.1e-70) to 7/7 blocks of the IPB001653 family, which is described as \"Diaminopimelate epimerase\". Interpro entry for IP:IPR001653. IPB001653A 3-15 3.7e-10 IPB001653B 36-46 2.2e-05 IPB001653C 63-79 1e-13 IPB001653D 112-123 0.00021 IPB001653E 153-175 1.2e-13 IPB001653F 185-195 1.9e-05 IPB001653G 212-223 2.5e-08","Residues 156 to 214 match (5e-10) PD:PD485115 which is described as EPIMERASE DIAMINOPIMELATE PROTEOME COMPLETE ISOMERASE DAP LYSINE BIOSYNTHESIS ","","","","","","","","","","","Tue Jan 7 11:09:51 2003","Tue Jan 7 11:09:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01203 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 151 to 267 (E-value = 4.1e-53) place AA01203 in the DAP_epimerase family which is described as Diaminopimelate epimerase (PF01678)","","","","","Richaud,C. and Printz,C. Nucleotide sequence of the dapF gene and flanking regions fromEscherichia coli K12. Nucleic Acids Res. 16 (21), 10367 (1988) PubMed: 3057443","","Tue Jan 7 11:09:51 2003","1","","","" "AA01204","825155","825256","102","TTGAGTAAATCGATTGCTTCTATACTTAATATGAAGAAAAAGTGCGGTCGTTTTTCACCGCACTTTTTGCCTGTTGTAAGCCGAAAGCATCCGCGTTATTGC","","","3912","LSKSIASILNMKKKCGRFSPHFLPVVSRKHPRYC","825256","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:00:40 2004","Wed Feb 25 13:00:40 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01204 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 13:00:40 2004","","","","","","","","","","","","","1","","","" "AA01206","826387","825362","1026","GTGAGCAAACAATCCTTAAGTTACAAAGATGCCGGCGTGGACATTAGCGCCGGTAACGACTTAGTCGAACGTATTAAATCCGACGTCAAACGTACAACACGTCCGGAAGTAATGAGCGGTTTCAATGCATTGTGCGCTATTCCGGCAAAATATAAAGAGCCGATTTTAGTTTCCGGCACGGGCGGCGTGGGCACAAAGTTGCGTTTGGCGATCGATTTAAAGCGTCACGACACCATCGGGGTTGATTTGGTTGCTATGTGCGTAAACGATTTAGTGGTGCAAGGTGCGGAACCGTTGTTTTTCCTTGATTATTACGCCACCGGCAAATTAGAAGTGGATGTTGTCGCGAGCGTAATTAAAGGCATTGCTAACGGTTGTGAACAATCCGGTTGCGCATTGGTCGGCGGGGAAACGGCGGAGATGCCGGGAATGTACCATCAAGGGGATTACAATCTTGCCGGTTTCTGCGTCGGCGTGGTGGAAAAATCCGAAATTATCGACGGCTCCGAAGTGAAAGTGGGCGACGCATTAATCGCCTTGGGTTCCAGCGGGCCGCATTCCAACGGGTATTCTTTAATTCGTAAAGTTGTGGACCTGTCCGGCGTGAACCCTGCCGAAGCGCAGGTGGGCGATCGTCCGTTAGCCGATCATTTATTGGCACCGACGAAAATCTATGTGAAATCCATTTTACAGCTCATCAAACACGTTGATGTGCACGCCATCGCCCACTTAACCGGCGGCGGTTTTTGGGAAAATATCCCGCGCGTCTTGCCGCCGAGCGTGAAAGCCGTTATCAATGAAAACAGCTGGCAATGGACTGCGGTGTTTAGTTGGCTGCAACAACAAGGCAATATTACCGACCATGAAATGTACCGCACCTTTAACTGTGGCGTAGGCATGATTGTGGCGTTGCCGCAGGAAGATGTGGAAACCGCACTCGGTTTATTGCATCAGGCAGGGGAAAATGCCTGGGTGATTGGTGAAGTGCAACATTTAGGCAACGACGAAGCACAAGTGATTATTCGC","","","36639","VSKQSLSYKDAGVDISAGNDLVERIKSDVKRTTRPEVMSGFNALCAIPAKYKEPILVSGTGGVGTKLRLAIDLKRHDTIGVDLVAMCVNDLVVQGAEPLFFLDYYATGKLEVDVVASVIKGIANGCEQSGCALVGGETAEMPGMYHQGDYNLAGFCVGVVEKSEIIDGSEVKVGDALIALGSSGPHSNGYSLIRKVVDLSGVNPAEAQVGDRPLADHLLAPTKIYVKSILQLIKHVDVHAIAHLTGGGFWENIPRVLPPSVKAVINENSWQWTAVFSWLQQQGNITDHEMYRTFNCGVGMIVALPQEDVETALGLLHQAGENAWVIGEVQHLGNDEAQVIIR","825364","From HD0561: This enzyme catalyzes the fifth step, the ATP-dependent synthesis of 5\"-phosphoribosyl-5-aminoimidazole from 5\"-phosphoribosylformylglycinamide, in the de novo synthesis of purine nucleotides.(No GenBank reference provided)","phosphoribosylformylglycinamidine cyclo-ligase","Cytoplasm","","
InterPro
IPR000728
Domain
AIR synthase related protein
PF00586\"[4-161]TAIRS
InterPro
IPR004733
Domain
Phosphoribosylformylglycinamidine cyclo-ligase
TIGR00878\"[6-332]TpurM: phosphoribosylformylglycinamidine cyc
InterPro
IPR010918
Domain
AIR synthase related protein, C-terminal
PF02769\"[172-340]TAIRS_C
noIPR
unintegrated
unintegrated
G3DSA:3.30.1330.10\"[4-166]Tno description
G3DSA:3.90.650.10\"[167-341]Tno description
PTHR10520\"[6-340]TPHOSPHORIBOSYLAMINE-GLYCINE LIGASE-RELATED


","No hits to the COGs database.","","Residues 167 to 341 match (3e-77) PD:PD002449 which is described as SYNTHETASE LIGASE PROTEOME COMPLETE CYCLO-LIGASE PHOSPHORIBOSYLFORMYLGLYCINAMIDINE PURINE PHOSPHORIBOSYLAMINOIMIDAZOLE BIOSYNTHETIC RIBONUCLEOTIDE ","","","","","","","","","","","Tue Jan 7 11:13:40 2003","Tue Jan 7 11:13:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01206 is paralogously related to AA01628 (9e-06).","","","","","","Residues 172 to 340 (E-value = 3.4e-54) place AA01206 in the AIRS_C family which is described as AIR synthase related protein, C-terminal domain (PF02769)","","","","","Li,C., Kappock,T.J., Stubbe,J., Weaver,T.M. and Ealick,S.E. X-ray crystal structure of aminoimidazole ribonucleotide synthetase(PurM), from the Escherichia coli purine biosynthetic pathway at2.5-A resolution Structure 7, 1155-1166 (1999) Smith,J.M. and Daum,H.A. III. Nucleotide sequence of the purM gene encoding 5\"-phosphoribosyl-5-aminoimidazole synthetase of Escherichia coli K12 The Journal of biological chemistry. 261 (23), 10632-10636 (1986) PubMed: 3015935 Schrimsher,J.L., Schendel,F.J., Stubbe,J. and Smith,J.M. Purification and characterization of aminoimidazole ribonucleotide synthetase from Escherichia coli Biochemistry. 25 (15), 4366-4371 (1986) PubMed: 3530323","","Tue Jan 7 11:13:40 2003","1","","","" "AA01207","826428","826523","96","TTGTACCACGCTTACAAAATCGTTTGCGATATGGGCATGGGATTTTTCTGTTCGGTGGTGCTTTCAGTTAGCTATTCTACGGGAATTGTGCCAAAA","","","3498","LYHAYKIVCDMGMGFFCSVVLSVSYSTGIVPK","826523","","hypothetical protein","Cytoplasm, Extracellular","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
tmhmm\"[12-30]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:02:10 2004","Wed Feb 25 13:02:10 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01207 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 13:02:10 2004","","","","","","","","","","","","","1","","","" "AA01209","826570","827067","498","ATGAAAAAAACGATCGTAATTCTCACCGCACTTTTATTGGCTGCCTGTACAAATCCCCCTGCAACCCAAACCGCCTCCGCCAAAAATGCCGACATTCCGCCACAACAAGAGGTGCCGATTACCCCGCCGAAAGACACCAAAAACGGCTTTCTACAACTCATGCCGGGCATTTTTTATTATGTGGATATGGATTCCATTTGGGTGGATAACCAAGACAAACGCCTGATTCATTTTGATGCGGTGATTAATTTAGATAAAGGGCTGTATGTGTTTAAAGAATATCCGGCGCTTTTCGCCAAATCCATGCGCCAGTATAAAATCCTGAACTGCGAAAACTTCTATTTCACCCACGTACGCAGCGATTTCTATGCCGATTTCTGGGGCGACGGCATCCGCACCGCACCAAAACGCCAGTCCCAACACACCATCACGCTGCAACCGCAATCTTCCCTGTATATTCTGGGGCAAGTGATGTGCGCCAATATGTATCGACGGAAG","","","19794","MKKTIVILTALLLAACTNPPATQTASAKNADIPPQQEVPITPPKDTKNGFLQLMPGIFYYVDMDSIWVDNQDKRLIHFDAVINLDKGLYVFKEYPALFAKSMRQYKILNCENFYFTHVRSDFYADFWGDGIRTAPKRQSQHTITLQPQSSLYILGQVMCANMYRRK","827069","","conserved hypothetical protein","Periplasm, Outer membrane","","
noIPR
unintegrated
unintegrated
PS51257\"[1-16]TPROKAR_LIPOPROTEIN
signalp\"[1-16]?signal-peptide


","No hits to the COGs database.","","Residues 24 to 135 match (1e-30) PD:PD415250 which is described as COMPLETE PROTEOME HI0178 SIGNAL PRECURSOR PM0022 ","","","","","","","","","","","","Tue Jan 7 11:15:33 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01209 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01210","827043","827159","117","GTGCGCCAATATGTATCGACGGAAGTAGGACAAAAAAGTGCGGTGAATTTTCACCGCACTTTCAATACAGTCCCACAAAAAAGCCATTTAGCATTCACTAAATGGCTTTTTAATCAT","","","4586","VRQYVSTEVGQKSAVNFHRTFNTVPQKSHLAFTKWLFNH","827159","","hypothetical protein","Periplasm, Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:03:23 2004","","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01210 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 13:03:23 2004","","","","","","","","","","","","","1","","","" "AA01211","829742","827175","2568","ATGAATATTGAAAAATTTACCACAAAATTCCAACAAGCCTTGGCGGAAGCACAATCTTTGGCGGTCGGCAAGGATAATCAATTTATTGAACCGGTACATTTATTGAGCGCCTTGTTAAATCAACAAGACGGTTCCATAGCACCGATTCTCACCACCGGCGGCGTAAACGTCGCTTTATTGCGTAACGAAATCAACAACGAGCTTGCCAAGCTCCCGCAAGTGTCCGGCAACGGCGGCGATGTGCAAATTTCCCGTCAGTTGCTTAACATCTTGAATTTATGTGACAAATTGGCACAACAACGGCAGGATAAATTTATTTCGTCCGAAATCTTTTTGCTTGCCGCTTTAGAAGAAAAAGGCACCCTGAGCGAGATTTTGAAAAAGTGCGGTGCGAAAAAAGAACAGATTTTACAAGCCATCGAGCAGATTCGCGGAGGACAAAAAGTGAATGATCAAAATGCGGAAGAAAGCCGCCAAGCACTCGAAAAATATACTATCGACTTAACCGCCCGCGCAGAAAGCGGCAAATTGGATCCGGTGATTGGACGTGACGAGGAAATCCGCCGCACCATTCAAGTGTTGCAGCGCCGTACCAAAAACAATCCGGTGCTTATCGGTGAACCGGGTGTGGGTAAAACCGCCATTGTGGAAGGTTTGGCACAGCGTATCGTGAACGGCGAAGTGCCGGAAGGGTTGAAAAACAAACGTGTGCTGTCGCTTGATATGGGCGCGTTAATCGCCGGGGCGAAATATCGCGGCGAATTTGAAGAACGTTTGAAAGCGGTGTTAAACGAACTCGCCAAAGAAGAAGGCAGAGTGATTTTGTTCATCGATGAAATTCACACTATGGTGGGCGCGGGTAAAACCGACGGCGCCATGGACGCAGGCAACCTGCTCAAACCAAGTTTGGCGCGCGGTGAATTGCATTGCGTGGGCGCCACTACCTTGGATGAATATCGTCAATACATTGAAAAAGACGCGGCGCTTGAACGTCGTTTCCAAAAAGTGTTTGTGGGCGAACCGAGCGTGGAAGACACCATCGCCATTTTGCGCGGTTTGAAAGAGCGTTATGAAATCCACCACCATGTACAAATTACCGACCCGGCAATCGTGGCGGCGGCAACGCTTTCTCATCGTTATATTTCCGATCGTCAGTTGCCGGATAAAGCCATCGACTTAATCGACGAAGCGGCATCCAGCATTCGGATGGAAATCGACTCCAAACCGCAACCGTTAGATCGTTTGGATCGCCGTATTATCCAGCTCAAACTGGAACAACAGGCGTTGCAAAAAGAAGATGACGATGCCAGCCGTAAACGTTTGGAAATGCTGGAAAAAGAATTGGCGGAAAAAGAACGTGAATATGCCGAATTAGAAGAAGTGTGGAAATCGGAAAAAGCCGCGCTGTCCGGCACGCAACACATTAAAGCGGAATTGGAAAATGCCCGCACGCAAATGGAACAAGCACGCCGCGCTGGTGATTTAAGCAAAATGTCCGAATTGCAATACGGCAAAATTCCGGATTTGGAAAAACAATTAGCCCAAGCGGAAGGTGCCGAGGGCAAAGAAATGAGTCTGTTACGCTATCGCGTGACCGACGAAGAAATCGCCGAAGTGCTTTCCCGCGCTACCGGTATTCCGGTCGCTAAAATGATGGAAGGCGAAAAAGAAAAATTATTGCACATGGAAGAATTTCTGCACAAACGGGTTATCGGTCAAAACGAAGCGGTGGATGCCGTGGCGAACGCTATTCGTCGTAGCCGCGCCGGTCTTTCCGATCCGAACCGTCCGATTGGTTCCTTCTTATTCTTAGGTCCGACCGGTGTGGGTAAAACCGAGTTGTGCAAAGCCTTGGCGTCCTTCTTATTCGACAGCGAAGATGCCATGGTGCGTATCGATATGTCCGAGTTCATGGAAAAACACAGCGTGTCCCGTTTGGTGGGCGCACCTCCGGGCTATGTGGGCTATGAAGAAGGCGGTTACTTAACCGAAGCGGTGCGTCGCCGTCCGTATTCCGTGATTTTGCTCGACGAAGTGGAAAAAGCGCATCACGATGTGTTTAACATTCTGTTGCAAGTGTTGGACGACGGTCGTCTCACCGACGGACAGGGCAGAACCGTGGATTTCCGCAATACGGTGGTGATTATGACCTCCAACCTCGGTTCCGACTTGATTCAGGATCACGCACAGGAAGGGTACGACACCGTGAAAAGCATGGTGATGGAAGTGGTCGGTCGTTATTTCCGTCCGGAATTTATCAACCGTATCGACGAAACCGTCATGTTCCACCCGTTGAACAAAGAAAATATTCGTCAAATTGCCGATATTCAATTAAGACGCTTAACCCGTCGCATGGAAACTCATGGCTATGTGTTGAACTTTACCGATGCTACCCTTGATTTCATCAGCGACATCGGTTACGACCCGATTTTCGGTGCACGTCCGCTCAAACGGGCAATCCAGCAAGAAATCGAAAATCCGTTGGCACAACAAATTTTATCCGGCGCCTTGCTGCCTGATAAAGTGATTGATGTGGACTACGTGGACGGTCAAATCGTGGCAAAACAA","","","97866","MNIEKFTTKFQQALAEAQSLAVGKDNQFIEPVHLLSALLNQQDGSIAPILTTGGVNVALLRNEINNELAKLPQVSGNGGDVQISRQLLNILNLCDKLAQQRQDKFISSEIFLLAALEEKGTLSEILKKCGAKKEQILQAIEQIRGGQKVNDQNAEESRQALEKYTIDLTARAESGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGEVPEGLKNKRVLSLDMGALIAGAKYRGEFEERLKAVLNELAKEEGRVILFIDEIHTMVGAGKTDGAMDAGNLLKPSLARGELHCVGATTLDEYRQYIEKDAALERRFQKVFVGEPSVEDTIAILRGLKERYEIHHHVQITDPAIVAAATLSHRYISDRQLPDKAIDLIDEAASSIRMEIDSKPQPLDRLDRRIIQLKLEQQALQKEDDDASRKRLEMLEKELAEKEREYAELEEVWKSEKAALSGTQHIKAELENARTQMEQARRAGDLSKMSELQYGKIPDLEKQLAQAEGAEGKEMSLLRYRVTDEEIAEVLSRATGIPVAKMMEGEKEKLLHMEEFLHKRVIGQNEAVDAVANAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALASFLFDSEDAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHHDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNLGSDLIQDHAQEGYDTVKSMVMEVVGRYFRPEFINRIDETVMFHPLNKENIRQIADIQLRRLTRRMETHGYVLNFTDATLDFISDIGYDPIFGARPLKRAIQQEIENPLAQQILSGALLPDKVIDVDYVDGQIVAKQ","827177","","ATP-dependent Clp protease, ATPase subunit","Cytoplasm","","
InterPro
IPR001270
Family
Chaperonin clpA/B
PR00300\"[601-619]T\"[646-664]T\"[675-693]T\"[708-722]TCLPPROTEASEA
PS00870\"[294-306]TCLPAB_1
PS00871\"[631-649]TCLPAB_2
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[198-343]T\"[597-757]TAAA
InterPro
IPR003959
Domain
AAA ATPase, core
PF00004\"[201-286]TAAA
InterPro
IPR004176
Domain
Clp, N-terminal
PF02861\"[17-69]T\"[94-145]TClp_N
InterPro
IPR013093
Domain
ATPase AAA-2
PF07724\"[596-759]TAAA_2
noIPR
unintegrated
unintegrated
G3DSA:1.10.8.60\"[765-853]Tno description
G3DSA:3.40.50.300\"[157-351]T\"[549-764]Tno description
PTHR11638\"[1-402]T\"[459-698]TATP-DEPENDENT CLP PROTEASE
PTHR11638:SF18\"[1-402]T\"[459-698]TCHAPERONE CLPB


","No hits to the COGs database.","Significant hit (1.8e-272) to 8/8 blocks of the IPB001270 family, which is described as \"Chaperonins clpA/B\". Interpro entry for IP:IPR001270. IPB001270A 180-222 8.3e-42 IPB001270B 223-271 1.1e-37 IPB001270C 273-287 6.8e-11 IPB001270D 313-367 8.5e-53 IPB001270E 577-631 5e-51 IPB001270F 658-712 9.5e-54 IPB001270G 748-762 7.1e-08 IPB001270H 806-820 2.4e-09Significant hit ( 7.7e-05) to 1/5 blocks of the IPB001482 family, which is described as \"Bacterial type II secretion system protein E\". Interpro entry for IP:IPR001482. IPB001482B 597-619 7.7e-05","Residues 562 to 603 match (2e-07) PD:PD234600 which is described as ATP-DEPENDENT CLPB PROTEIN-LIKE ","","","","","","","","","","","","Tue Jan 7 11:23:08 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01211 is paralogously related to AA00460 (7e-06), AA02347 (1e-04), AA02501 (4e-04), AA02832 (5e-04) and AA02395 (0.001).","","","","","","Residues 201 to 395 (E-value = 3.3e-14) place AA01211 in the AAA family which is described as ATPase family associated with various cellular activities (AAA) (PF00004)","","","","","Kitagawa,M., Wada,C., Yoshioka,S. and Yura,T. Expression of ClpB, an analog of the ATP-dependent protease regulatory subunit in Escherichia coli, is controlled by a heat shock sigma factor (sigma 32) J. Bacteriol. 173 (14), 4247-4253 (1991) PubMed: 1906060 Pontis,E., Sun,X.Y., Jornvall,H., Krook,M. and Reichard,P. ClpB proteins copurify with the anaerobic Escherichia coli reductase Biochem. Biophys. Res. Commun. 180 (3), 1222-1226 (1991) PubMed: 1953774 Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M., Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T., Clark,W.P., Ross,B., Squires,C.L. and Maurizi,M.R. Conservation of the regulatory subunit for the Clp ATP-dependent protease in prokaryotes and eukaryotes Proc. Natl. Acad. Sci. U.S.A. 87 (9), 3513-3517 (1990) PubMed: 2185473 ","","Tue Jan 7 11:23:08 2003","1","","","" "AA01212","829754","829873","120","TTGAGTGTTCCAATGGATATTCTGTTGAACATTTATTCGCCAAAATTAAATAAGATCGTTTTAAAAGATTTCAAGGGAAAAATGCAAAAATTTTCATTTTGCCTATTGACTTTTCGGGCT","","","4644","LSVPMDILLNIYSPKLNKIVLKDFKGKMQKFSFCLLTFRA","829873","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:04:45 2004","","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01212 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 13:04:45 2004","","","","","","","","","","","","","1","","","" "AA01213","830007","830585","579","ATGAAATCATTAAAATCGCTGCTTGCTGTAGCCGTCGTGATGACCGTTTCCACCACCGTATTCGCCGAAGAAAGCGTGTTCACGGAAGTCAAAGACGGGGCGAAATCCGCCTGGCAAACCGTTAAATCCGATGCCAAAACCGTGGGCGGTAAAGTGAAAGAGGGCGCGGTGAAAGTCAAAGACGCGACCAAAGAGAAATTCGTTGAAGCGAAAGAGGCGACTAAAGAGACCTTTACCAAAGCCAAAGATGCTACCAAGGAAAAATTTGCCGAAGGGAAAAAGGCGGTAAAAGACACCTTTCAAAATGAAAAACCGGCGCCGGTAGAAGATAAATCCACCGCCAAAGAGAAAAGTACGGTGGAAAATAAAGCCAAAATCACACGCAGCAAAAAAGTGGATATTAACACTGCCGACGCAGCGACTTTAGAAAACCTATCCGGTATCGGTGAAGCAAAAGCTAAAGCAATTGTGGAATACCGTGAGAAAAACGGGAAATTTAAGAACCTGAATGACTTATCCAACGTGCCGGGTATCGGTGACGTGACCTTAGAAAAAGTCAAATCCCATGTGCGTTTTAAC","","","25117","MKSLKSLLAVAVVMTVSTTVFAEESVFTEVKDGAKSAWQTVKSDAKTVGGKVKEGAVKVKDATKEKFVEAKEATKETFTKAKDATKEKFAEGKKAVKDTFQNEKPAPVEDKSTAKEKSTVENKAKITRSKKVDINTADAATLENLSGIGEAKAKAIVEYREKNGKFKNLNDLSNVPGIGDVTLEKVKSHVRFN","830587","","competence related protein","Periplasm, Inner membrane","","
InterPro
IPR003583
Domain
Helix-hairpin-helix DNA-binding, class 1
SM00278\"[140-159]T\"[170-189]THhH1
InterPro
IPR004509
Domain
Competence protein ComEA helix-hairpin-helix region
TIGR00426\"[129-192]TTIGR00426: competence protein ComEA helix-h
noIPR
unintegrated
unintegrated
PTHR21180\"[131-192]TFAMILY NOT NAMED
PTHR21180:SF4\"[131-192]Tgb def: ComEA protein-related protein
signalp\"[1-22]?signal-peptide


","No hits to the COGs database.","","Residues 132 to 188 match (2e-08) PD:PD011817 which is described as COMPLETE PROTEOME RNA-BINDING ACCESSORY TRANSCRIPTION SPT6 EMB-5 FIS CDNA DOMAIN ","","","","","","","","","","","","Tue Jan 7 11:36:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01213 is paralogously related to AA02367 (2e-11), AA00939 (2e-06), AA02832 (4e-05) and AA00639 (5e-05).","","","","","","","","","","","Berge M, Moscoso M, Prudhomme M, Martin B, Claverys JP.Uptake of transforming DNA in Gram-positive bacteria: a view from Streptococcus pneumoniae.Mol Microbiol. 2002 Jul;45(2):411-21.PMID: 12123453 Chen I, Gotschlich EC.ComE, a competence protein from Neisseria gonorrhoeae with DNA-binding activity.J Bacteriol. 2001 May;183(10):3160-8.PMID: 11325945 Provvedi R, Dubnau D.ComEA is a DNA receptor for transformation of competent Bacillus subtilis.Mol Microbiol. 1999 Jan;31(1):271-80.PMID: 9987128 Inamine GS, Dubnau D.ComEA, a Bacillus subtilis integral membrane protein required for genetic transformation, is needed for both DNA binding and transport.J Bacteriol. 1995 Jun;177(11):3045-51.PMID: 7768800 ","","Tue Jan 7 11:28:25 2003","1","","","" "AA01215","831773","830664","1110","ATGAAAAACGTTGGTTTTATCGGTTGGCGCGGAATGGTGGGTTCCGTTTTAATGGATCGTATGCAGCAGGAAAATGATTTTACGAATATCAATCCGATCTTCTTTACCACTTCTCAAGCAGGACAAGCTGCACCGACATTCGGCGGTAAAGACGCCGGCACCTTGAAAAATGCGTTCGACATTGAAGAACTGAAAAAACTGGACATTATCGTCACCTGCCAAGGCGGCGATTACACCAACGAAGTTTATCCGAAATTAAAAGCCACCGGCTGGAGCGGTTACTGGGTGGATGCGGCGTCCGCATTGCGTATGGAAGAAGACGCGATTATCGTGTTGGACCCGGTGAATCAACACGTGATCAGCGAAGGCTTGAAAAACGGCGTGAAAACCTATGTAGGCGGTAACTGTACTGTCAGCTTGATGCTCATAGCGTTAGGCGGTTTATTTGAAAAAGATTTAGTGGAATGGATCTCCGTTGCCACTTACCAAGCCGCCAGTGGTGCCGGTGCGAAAAATATGCGCGAATTATTGGTGCAAATGGGTGAGTTAAACGGCGAAGTGAAAGGCTTACTTGCGGATCCGAATTCTTCCATTTTAGACATTGAACGTGCCGTGACCGCCAAAATGCGCGACAAAGACTTCCCGATTGATAACTTCGGCGCACCGTTGGCGGGCAGCCTGATTCCTTGGATCGACAAATTATTGGAAAGCGGTCAAACCAAAGAAGAATGGAAAGGTTACGCAGAAACCAACAAAATTCTGGGCTTGAGCGATAACCCGATTCCGGTGGATGGCTTATGCGTGCGTATCGGCGCGTTGCGTTGCCACAGCCAAGCCTTCACCATCAAATTGAAACGCGACATTCCGCTTGCCGAAATCGAACAAATTTTGGCTTCGCACAACGAGTGGGTGAAAGTGATCCCGAACGACAAAGAAACCACATTACGCGAATTAACACCGACCAAAGTCACCGGCACATTGAGCGTTCCGGTCGGGCGTTTACGCAAACTCAATCTTGGACCGGAATATTTGGCGGCGTTCACCGTGGGCGACCAATTATTGTGGGGCGCGGCAGAACCGATTCGCCGTATTTTGGTGCAATTGGTCAAA","","","40446","MKNVGFIGWRGMVGSVLMDRMQQENDFTNINPIFFTTSQAGQAAPTFGGKDAGTLKNAFDIEELKKLDIIVTCQGGDYTNEVYPKLKATGWSGYWVDAASALRMEEDAIIVLDPVNQHVISEGLKNGVKTYVGGNCTVSLMLIALGGLFEKDLVEWISVATYQAASGAGAKNMRELLVQMGELNGEVKGLLADPNSSILDIERAVTAKMRDKDFPIDNFGAPLAGSLIPWIDKLLESGQTKEEWKGYAETNKILGLSDNPIPVDGLCVRIGALRCHSQAFTIKLKRDIPLAEIEQILASHNEWVKVIPNDKETTLRELTPTKVTGTLSVPVGRLRKLNLGPEYLAAFTVGDQLLWGAAEPIRRILVQLVK","830666","","aspartate-semialdehyde dehydrogenase","Cytoplasm","","
InterPro
IPR000319
Domain
Aspartate-semialdehyde dehydrogenase, conserved region
PS01103\"[263-277]TASD
InterPro
IPR000534
Domain
Semialdehyde dehydrogenase, NAD - binding
PF01118\"[3-123]TSemialdhyde_dh
InterPro
IPR011534
Family
Aspartate-semialdehyde dehydrogenase, proteobacteria
TIGR01745\"[2-369]Tasd_gamma: aspartate-semialdehyde dehydroge
InterPro
IPR012080
Family
Aspartate-semialdehyde dehydrogenase
PIRSF000148\"[1-370]TAspartate-semialdehyde dehydrogenase
InterPro
IPR012280
Domain
Semialdehyde dehydrogenase, dimerisation region
PF02774\"[145-355]TSemialdhyde_dhC
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[1-148]Tno description
PTHR10174\"[1-175]T\"[221-370]TRETINALDEHYDE BINDING PROTEIN-RELATED
PTHR10174:SF2\"[1-175]T\"[221-370]TASPARTATE SEMIALDEHYDE DEHYDROGENASE
tmhmm\"[131-149]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.1e-55) to 8/9 blocks of the IPB000319 family, which is described as \"Aspartate-semialdehyde dehydrogenase\". Interpro entry for IP:IPR000319. IPB000319A 4-15 0.0058 IPB000319C 65-81 0.00056 IPB000319D 95-116 4e-10 IPB000319E 159-169 7.7e-06 IPB000319F 242-255 0.00091 IPB000319G 263-283 1.2e-07 IPB000319H 318-337 4.2e-05 IPB000319I 351-365 0.00015Significant hit ( 3e-07) to 2/2 blocks of the IPB000534 family, which is described as \"Semialdehyde dehydrogenase\". Interpro entry for IP:IPR000534. IPB000534A 68-85 0.0012 IPB000534B 266-278 0.11 IPB000534A 131-148 0.2 IPB000534B 351-363 0.3","Residues 337 to 368 match (5e-09) PD:PD240221 which is described as DEHYDROGENASE BIOSYNTHESIS OXIDOREDUCTASE ASPARTATE-SEMIALDEHYDE PROTEOME COMPLETE NADP LYSINE ASA DIAMINOPIMELATE ","","","","","","","","","","","","Fri May 20 13:34:33 2005","","Fri May 20 13:34:33 2005","Fri May 20 13:34:33 2005","Fri May 20 13:34:33 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA01215 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Fri May 20 13:34:33 2005","","","","","Residues 145 to 355 (E-value = 4.9e-79) place AA01215 in the Semialdhyde_dhC family which is described as Semialdehyde dehydrogenase, dimerisation domain (PF02774)","Fri May 20 13:34:33 2005","","","","James CL, Viola RE. Production and characterization of bifunctional enzymes. Substratechanneling in the aspartate pathway. Biochemistry. 2002 Mar 19;41(11):3726-31. PMID: 11888290 James CL, Viola RE. Production and characterization of bifunctional enzymes. Domainswapping to produce new bifunctional enzymes in the aspartate pathway. Biochemistry. 2002 Mar 19;41(11):3720-5. PMID: 11888289 Langford,P.R. and Kroll,J.S. Distribution, cloning, characterisation and mutagenesis of sodC, the gene encoding copper/zinc superoxide dismutase, a potential determinant of virulence, in Haemophilus ducreyi FEMS Immunol. Med. Microbiol. 17 (4), 235-242 (1997) PubMed: 9143881 Karsten,W.E. and Viola,R.E. Identification of an essential cysteine in the reaction catalyzed by aspartate-beta-semialdehyde dehydrogenase from Escherichia coli Biochim. Biophys. Acta 1121 (1-2), 234-238 (1992) M:92287957 ","","Fri May 20 13:34:33 2005","1","","","" "AA01216","832769","831960","810","ATGACGATCCCGAATTATCGTGACCAAATTAAAGTGATCTTTTTTGACATCGACGAAACCCTGTTTATGAAAGAACAGGATCATTTACCCGCAAGCGTGCCGTTGTTTATTCGCAAACTCAAACAAAACGGCATTATTCCCGCCATTGCCAGCGGGCGTTCGCGCACCATGTTCCCGTGGCAGGTGAAACAGCTGGTTGAGCAGGAAGGCATGGCGTTGTTCGTGACCATGAACGGACAATCCGTGACCCACAAAAATCAAGTGATTGCCAAGCATACCATTCCAACCGAGCAAATTCGTCGCTTAACCTATTTCTTCGACCAACATCATATTGCCTATGCGTTTATTACCGATGACGCGGTGAACGTGTCGGAGAAAAATGCACGGGTGACCAGCTCCTTTGATGTGATTACCACGGATTATGCCGTGGATAAAGCATTTTTTGAACGCCATGCGATTAGTCAGATTCTGCCTTTTTACCGTGAAGAACAAGACCAATTAGTGCAAAATTGCGGTTTATTGGATGGCTTGCGCATGGTGCGCTGGCATGAGGAATCCGTGGATTTGTTCGACGCGGAAGGTTCCAAAGCGCGCGGCATTGAAACGGCGGTGAAGCATTTAGGGCTATCAATGGAAAATGTGATGGCGTTCGGTGACGGTTTAAATGACCTGGAAATGTTAAGCCGCGTGGGTGTCGGCGTCGCCATGGGCAACGGGCATGAGAAATTAAAAGCCATCGCCGATCATGTGGCGGATCCTATCGACCAAGACGGTATTTATCGGTTTCTGGTGAAGGCAGGGTTGATTGAT","","","30556","MTIPNYRDQIKVIFFDIDETLFMKEQDHLPASVPLFIRKLKQNGIIPAIASGRSRTMFPWQVKQLVEQEGMALFVTMNGQSVTHKNQVIAKHTIPTEQIRRLTYFFDQHHIAYAFITDDAVNVSEKNARVTSSFDVITTDYAVDKAFFERHAISQILPFYREEQDQLVQNCGLLDGLRMVRWHEESVDLFDAEGSKARGIETAVKHLGLSMENVMAFGDGLNDLEMLSRVGVGVAMGNGHEKLKAIADHVADPIDQDGIYRFLVKAGLID","831962","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR000150
Family
Cof protein
TIGR00099\"[12-263]TCof-subfamily: Cof-like hydrolase
PS01229\"[217-239]TCOF_2
InterPro
IPR006379
Family
HAD-superfamily hydrolase, subfamily IIB
TIGR01484\"[12-236]THAD-SF-IIB: HAD-superfamily hydrolase, subf
InterPro
IPR013200
Domain
HAD superfamily hydrolase-like, type 3
PF08282\"[13-263]THydrolase_3
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1000\"[9-265]Tno description


","No hits to the COGs database.","Significant hit ( 4.2e-30) to 3/3 blocks of the IPB000150 family, which is described as \"Cof protein\". Interpro entry for IP:IPR000150. IPB000150A 9-23 0.00014 IPB000150B 44-53 0.69 IPB000150C 215-247 1.7e-21","Residues 195 to 250 match (1e-09) PD:PD186741 which is described as COMPLETE PROTEOME TRANSFERASE ACID FIXI NUCLEOTIDYLTRANSFERASE SYNTHETASE YRBI COF FAMILY ","","","","","","","","","","","","Mon Feb 17 13:45:33 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01216 is paralogously related to AA00482 (1e-12), AA00316 (1e-11) and AA01431 (2e-07).","","","","","","Residues 10 to 240 (E-value = 8.2e-09) place AA01216 in the Hydrolase family which is described as haloacid dehalogenase-like hydrolase (PF00702)","","","","","","","","1","","","" "AA01217","832796","832915","120","ATGTCGCCGGATTTTATCATTTTTGCGAGGCGGATCCTAAACTCGATGAAAAAACATCGGAAAAAACTACCGCACTTTTATGATGCGCCATTTCCATCCCTAAAAGTGCGGTCAATTTCA","","","4756","MSPDFIIFARRILNSMKKHRKKLPHFYDAPFPSLKVRSIS","832915","","hypothetical protein","Periplasm, Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:06:12 2004","","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01217 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 13:06:12 2004","","","","","","","","","","","","","1","","","" "AA01220","832915","833598","684","ATGAACGTTTTTCAATCCTGCTGCGTGCATTGCCACACGCCGCTTAAACTTGCCAAACATGGCTTATGCAGCCGTTGTAACCGCACCATTCGGCGTTTTGCCTATTGCGGTTGCTGCGGCGCGGAATTGGCGGAAAACGCATTACATTGCGGAAACTGTTTGCGGCAGGAACCGGCGTGGGATCGCATGGTGATTATCGGGCGTTATAACGAACCGCTTTCCACCTTAATTCATCGCTTTAAATTCCAAAATCAATTTTGGCTTGACCGCACCTTAGCCCGCCTGCTGTATCTGGCGATTCGCGATGCGCGTCGCACTCATCGGCTACCTTTGCCCGAGGTGATTCTTCCCGTGCCGTTACATCATTTTCGTCAATGGCGACGCGGTTATAATCAGGCGGATTTACTGGCGCAGCAATTAGCTAAATGGTTCAAAATTCCCGTTGATAACGGTTTGCTTCTCCGCACCAAACGAACACCGACACAGCGTGGCTTAACGGCAAAAGATCGGCGCCACAACCTGAAAAATGCTTTTCGAATTTCAACCAACGACAGACATTTTCCTTATCGTAGCGTGGCGTTAGTGGACGATGTGATCACCAGCGGCTCCACCTTAAACGAAATCGCCAAGCGGTTACGCCAAGCCAACGTGGTACATATTCAGGTGTGGGGGCTTGCCCGTACA","","","26568","MNVFQSCCVHCHTPLKLAKHGLCSRCNRTIRRFAYCGCCGAELAENALHCGNCLRQEPAWDRMVIIGRYNEPLSTLIHRFKFQNQFWLDRTLARLLYLAIRDARRTHRLPLPEVILPVPLHHFRQWRRGYNQADLLAQQLAKWFKIPVDNGLLLRTKRTPTQRGLTAKDRRHNLKNAFRISTNDRHFPYRSVALVDDVITSGSTLNEIAKRLRQANVVHIQVWGLART","833600","","competence protein F; amidophosphoribosyltransferase","Cytoplasm","","
InterPro
IPR000836
Domain
Phosphoribosyltransferase
PF00156\"[192-222]TPribosyltran


","BeTs to 15 clades of COG1040COG name: Predicted amidophosphoribosyltransferasesFunctional Class: RThe phylogenetic pattern of COG1040 is -------qvdrlbcefghsnuj--t-Number of proteins in this genome belonging to this COG is","","Residues 124 to 228 match (2e-08) PD:PD109635 which is described as COMPLETE PROTEOME COMPETENCE COMFC LATE OPERON COMF F REQUIRED GLYCOSYLTRANSFERASE ","","","","","","","","","","","","Tue Jan 7 12:02:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01220 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Busch S, Rosenplanter C, Averhoff B. Identification and characterization of ComE and ComF, two novelpilin-like competence factors involved in natural transformation of Acinetobacter sp. strain BD413. Appl Environ Microbiol. 1999 Oct;65(10):4568-74. PMID: 10508090 Londono-Vallejo JA, Dubnau D. comF, a Bacillus subtilis late competence locus, encodes a proteinsimilar to ATP-dependent RNA/DNA helicases. Mol Microbiol. 1993 Jul;9(1):119-31. PMID: 8412657 Yamaoka T, Yano M, Kondo M, Sasaki H, Hino S, Katashima R, Moritani M, Itakura M.Feedback inhibition of amidophosphoribosyltransferase regulates the rate of cell growth via purine nucleotide, DNA, and protein syntheses.J Biol Chem. 2001 Jun 15;276(24):21285-91.PMID: 11290738 Zalkin H.Structure, function, and regulation of amidophosphoribosyltransferase from prokaryotes.Adv Enzyme Regul. 1983;21:225-37.PMID: 6443594","","Tue Jan 7 12:14:38 2003","1","","","" "AA01221","833718","834299","582","ATGCAACAAATTACTATTTCAGAAGCGGCGCAAGCGCATTTTCGCCGTTTATTGGATCAACAGGAAGAAGGCACTCATATTCGTATTTTCGTAGCCAATCCCGGCACGCCGAATGCCGAATGTGGCGTTTCTTACTGCCCACCGAATTCCGTTGAAGCCGACGACATGGAAATCAAATACGACAGTTTCTCCGCCTTTGTAGACGAAATCAGCCTGCCGTTTCTGGAAGATGCGGAAATTGATTACGTCACCGAAGAACTGGGCGCGCAGCTCACCTTAAAAGCGCCGAATGCCAAAATGAGAAAAGTCGCGGACGATGCGCCGCTAATCGAACGGGTGGAATATGTCATTCAAACCCAGATCAACCCGCAATTGGCAAGCCACGGCGGCAAAATCACCTTATTGGAAATCACCGATGACGGCTATGCCATTTTGCAATTCGGTGGCGGTTGCAACGGCTGTTCCATGGTGGATGTTACCCTGAAAGACGGCGTGGAAAAACAATTGGTCAATATCTTTCCGGGCGAATTAAACGGCGCCAGGGACGTCACCGAACACCGACGCGGCGAACATTCCTATTAT","","","21435","MQQITISEAAQAHFRRLLDQQEEGTHIRIFVANPGTPNAECGVSYCPPNSVEADDMEIKYDSFSAFVDEISLPFLEDAEIDYVTEELGAQLTLKAPNAKMRKVADDAPLIERVEYVIQTQINPQLASHGGKITLLEITDDGYAILQFGGGCNGCSMVDVTLKDGVEKQLVNIFPGELNGARDVTEHRRGEHSYY","834301","","transformation locus protein orfG homolog","Cytoplasm","","
InterPro
IPR000361
Family
HesB/YadR/YfhF
PD002183\"[49-90]TQ9A6S4_CAUCR_Q9A6S4;
PTHR10072\"[1-99]THES-B
PF01521\"[4-96]TFe-S_biosyn
InterPro
IPR001075
Domain
Nitrogen-fixing NifU, C-terminal
PD002830\"[121-183]TYF57_PASMU_Q9CKP9;
PF01106\"[113-182]TNifU
noIPR
unintegrated
unintegrated
G3DSA:2.60.300.12\"[4-96]Tno description
PTHR10072:SF26\"[1-99]THES-B


","BeTs to 11 clades of COG0694COG name: Thioredoxin-like proteins and domainsFunctional Class: OThe phylogenetic pattern of COG0694 is ao----y-----bcefghs-ujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 5e-17) to 3/3 blocks of the IPB001075 family, which is described as \"Nitrogen-fixing protein NifU\". Interpro entry for IP:IPR001075. IPB001075A 37-44 1.9 IPB001075B 120-134 0.00043 IPB001075C 143-161 6.9e-09Significant hit ( 8.6e-17) to 2/2 blocks of the IPB000361 family, which is described as \"Hypothetical hesB/yadR/yfhF family\". Interpro entry for IP:IPR000361. IPB000361A 27-47 2.5e-06 IPB000361B 77-108 8.1e-09","Residues 27 to 193 match (4e-84) PD:PD351313 which is described as PROTEOME COMPLETE ORFG STY4285 BU544 PA1847 THIOREDOXIN-LIKE PROTEINS XF2603 VC2720 ","","","","","","","","","","","","Tue Jan 7 12:18:20 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01221 is paralogously related to AA02430 (7e-04) and AA00711 (7e-04).","","","","","","Residues 113 to 182 (E-value = 4.3e-07) place AA01221 in the NifU family which is described as NifU-like domain (PF01106)","","","","","","","","1","","","" "AA01222","834446","834351","96","GTGCAGATTTTGCATTATCGCCTCACGGTGTTATTGCAGAACGCGGATTTAAACTGGGCGGATATGATTGAGAAATTGAAAGAACGTCATACAAAA","","","3873","VQILHYRLTVLLQNADLNWADMIEKLKERHTK","834351","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database. A very weak similarity is seen to gi|15603071 of P.multocida.","
InterPro
IPR008179
Domain
Phosphoribosyl-ATP pyrophosphohydrolase
PD002611\"[4-30]THIS2_PASMU_Q9CLL8;
noIPR
unintegrated
unintegrated
signalp\"[1-20]?signal-peptide


","BeTs to 4 clades of COG0140COG name: Phosphoribosyl-ATP pyrophosphohydrolaseFunctional Class: EThe phylogenetic pattern of COG0140 is -om---yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Wed Feb 25 13:07:37 2004","Wed Feb 25 13:08:56 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01222 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 13:07:37 2004","","","","","","","","","","","","","1","","","" "AA01223","836214","834802","1413","GTGAATTATGGAAAAAGTGCGGTCATGACTCTCTGCGTTTTGTATGATTTTATTACGAATCGTAAGGCTTTTGTAGTAGAATATCGTGGCTTTTTATCACAAGAGAAATTTATTATGTTTTCACGTAAAGATATTGTTGTTTTAGGAATGATGATTTTCGCGCTGTTTTTAGGCGCAGGAAACATTATTTTTCCACCTATGGAAGGCTACACCGCAGGGCAGCATTGGGCGATCGCTGCTTTAGGATTCGTGCTCACCGGCGTATTAATGCCGTTTATTACACTGGTGGTTGTGTCGGTTTTAGGGCGCGGCGAAGAGCTCACCCGCGATTTACCGAAATGGGCAGAAGTACTGTTTTTAGCCACCTTATATTTGGTGATTGGTTCCACTTTCGCCATGCCACGCATTACCAATGTCGCCTATGAAATGGCGTTGGTACCGTTGGAGATTGTGGCGGACACCTCCGCGAACCACCTGATTTTCGCCGTGGCATTTAACATTATCGCCATGTTATTCATGTTAAAACCGAACACCATTATTTCCAGCGTAGGCAAATTTATGACGCCGGCGTTATTGGTGTTATTGGTGGTGGTTACCGCTGCCGTATTTATTTCCCCATTATCTGAGATCTCTGCGCCAAGCAAAGCCTATGCCGAGGGTTCTGTACTAACTACAGGCTTAATCAGTGGATATCAAACCATGGATGTGTTGGCAGCGATCGCCTTCGGCGGTATCGTTGCCCGAGCATTAAGCAGTAAAAATGTCACCGAGCCGCATAAAATCATGCGTTACACCATTTTCGCCGGCTGTATTTCAGTGGTATTACTCGCTGCACTGTATTTTTCCTTATTCTATCTTGGTGCCACCAGTGACGCAGTAGCGCAAGGGGCAAACAACGGCGGACAAATTTTCTCCCGCTATGTAGGCGTGTTGTTCGGCAAAGAAGGCTCCTTGATTATGTCAGGCATCATTTTCTTAGCGAGTTTAACTACTCTTGTAGGTGTTACCAGCGCCTGCGCTTACTACTTTGCCAAATTTTCTAACCGCTTGCCATATTCCTTCTGGGTAGTATTTTTTACCATCATGACTACAATCATTTCCGAAAACGGCTTAACCAAACTATTACAAGTGACCATTCCCGCCTTGTTATTAATTTACCCGGTGACAATTATGCTGGTGGTGTTACAAATGGTACGCACCAAACTACCATGGGTGAAATTGACCTATAACGCCACTATCATCATCACCGTTTGTTTTAGTTTGTGCGACAGCTTGAATAACGTGGAATTATTGCCTGCCGGCGTAAAACGGCTTCTTGAAAATTTCCCTTTATATGACAATGGTTTGGCGTGGTTAATTCCGGCATTAGGTATGATGGTGTTGACTATTTTGATAGGGAAAATGGCGAAAAAA","","","54651","VNYGKSAVMTLCVLYDFITNRKAFVVEYRGFLSQEKFIMFSRKDIVVLGMMIFALFLGAGNIIFPPMEGYTAGQHWAIAALGFVLTGVLMPFITLVVVSVLGRGEELTRDLPKWAEVLFLATLYLVIGSTFAMPRITNVAYEMALVPLEIVADTSANHLIFAVAFNIIAMLFMLKPNTIISSVGKFMTPALLVLLVVVTAAVFISPLSEISAPSKAYAEGSVLTTGLISGYQTMDVLAAIAFGGIVARALSSKNVTEPHKIMRYTIFAGCISVVLLAALYFSLFYLGATSDAVAQGANNGGQIFSRYVGVLFGKEGSLIMSGIIFLASLTTLVGVTSACAYYFAKFSNRLPYSFWVVFFTIMTTIISENGLTKLLQVTIPALLLIYPVTIMLVVLQMVRTKLPWVKLTYNATIIITVCFSLCDSLNNVELLPAGVKRLLENFPLYDNGLAWLIPALGMMVLTILIGKMAKK","834804","","branched-chain amino acid carrier protein","Inner membrane, Cytoplasm","","
InterPro
IPR004685
Family
Branched-chain amino acid transport system II carrier protein
PF05525\"[41-469]TBranch_AA_trans
TIGR00796\"[49-454]Tlivcs: branched-chain amino acid transport
noIPR
unintegrated
unintegrated
tmhmm\"[45-63]?\"[82-102]?\"[117-137]?\"[156-174]?\"[189-207]?\"[231-251]?\"[266-286]?\"[322-344]?\"[349-369]?\"[375-395]?\"[407-425]?\"[448-466]?transmembrane_regions


","BeTs to 7 clades of COG1114COG name: Branched-chain amino acid permeasesFunctional Class: EThe phylogenetic pattern of COG1114 is -----------lb-efgh-----it-Number of proteins in this genome belonging to this COG is","","Residues 393 to 471 match (2e-18) PD:PD170018 which is described as CARRIER AMINO ACID PROTEOME TRANSMEMBRANE CHAIN COMPLETE AMINO-ACID MEMBRANE BRANCHED-CHAIN ","","","","","","","","","","","","Tue Jan 7 12:21:53 2003","","","","Thu Mar 18 09:48:55 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01223 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Mar 18 09:48:55 2004","","","","","Residues 41 to 469 (E-value = 3.9e-185) place AA01223 in the Branch_AA_trans family which is described as Branched-chain amino acid transport protein (PF05525)","Thu Mar 18 09:48:55 2004","","","","Hoshino,T., Kose,K. and Uratani,Y. Cloning and nucleotide sequence of the gene braB coding for the sodium-coupled branched-chain amino acid carrier in Pseudomonas aeruginosa PAO Mol. Gen. Genet. 220 (3), 461-467 (1990) PubMed: 2111004 ","","Tue Jan 7 12:21:53 2003","1","","","" "AA01224","836361","837959","1599","GTGGTTTCTTCGCTTGGTAAAGGCATCGCGGCGGCATCGCTTGCGGCAATCTTAGAAGCGCGTGGTTTGAACGTCACGATCATGAAACTCGACCCTTATATCAACGTTGATCCGGGTACCATGAGCCCGACTCAGCACGGTGAAGTGTTCGTTACCCAAGACGGCGCAGAAACGGACTTAGACTTAGGTCACTACGAGCGTTTTATTCGCACCAAAATGACCAAACGCAATAACTTCACCACCGGCAAAATCTATTCCGAAGTATTACGCAAAGAACGTCGCGGTGACTATTTGGGCGCCACCATTCAAGTGATTCCACACATTACCAACGAAATCAAAGCACGTGTTATTGACGGCGCGGCAGGGCATGACGTGGTAATTGTAGAAGTGGGTGGTACCGTAGGCGACATCGAATCGCTTCCGTTCCTTGAAGCCTTGCGTCAGCTTGCGGTGCAGGTTGGTCGCGAACGCACTATTTTCATGCATTTAACCTTAGTGCCGTACATTCCGACTGCCGGCGAACTAAAAACCAAACCGACCCAACATTCTGCGAAAGAATTATTGTCCATCGGCATTCAGCCGGACGTACTCATTTGCCGGTCTGACCGCATGATCCCGCCAAACGAACGCGCCAAAATCGCTTTATTCTGTAATGTGCCGGAACGCGCGGTGATTTCTCTGAAAGATGTGTCATCCATTTATCAAATTCCAGCATTGCTGAAATCTCAAGGGCTGGACGATTTCATTTGCGATCGTTTCCATTTAACCTGCCCGGAAGCGGATTTGTCCGAATGGGAGCAAGTGTTGTATCAACAAGCTAACCCGACGGGCGAAGTGATCATCGGCATGGTGGGAAAATACACCGAATTACCGGACGCTTACAAATCCGTGAACGAAGCCCTAAAACACGCAGGTTTAAAAAATCGCTTAACCGTAAACATTAAATATATCGACTCGCAGGACGTGGAAACCAAAGGCGTTGAAATCTTAAAAGGCTTGGACGGCATTTTAGTACCGGGCGGTTTCGGCTATCGTGGCGTGGAAGGCAAAATCCTCACCGCCAAATATGCACGCGAAAACAGCATTCCATATTTAGGCATTTGTTTGGGAATGCAAGTAGCGTTAATCGAATTCGCCCGCAACGTTGCCGGCATGAGCCACGCAAACTCCTCAGAATTCGACCGCACTTGTGAACAGCCAGTGGTAGGTTTAATCACCGAATGGCAAGACGCCGACGGCAACACCGAAGTGCGCAGCGACGAATCCGACTTAGGCGGCACTATGCGTCTTGGCGCACAAAAATGCCACTTGGCGGAAGGCAGCCTGGCACGCAAATTATATGGCACCGAAACCATCGAAGAACGCCACCGCCACCGTTACGAAGTAAACAACGTCCTGCTTCCGCAAATTGAAAAAGCGGGTTTGAAAGTCACCGGATTATCCGCCGATAAAAAATTGGTAGAAATCATTGAAGTGCCGAACCACCCTTGGTTTGTCGCCTGCCAATTCCATCCGGAGTTTACCTCCACCCCGCGCGACGGCCACCCGTTATTTGAAGGCTTTGTAAAAGCGGCAAAAGACAATCAGAAAAGATCCGAC","","","59954","VVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPTQHGEVFVTQDGAETDLDLGHYERFIRTKMTKRNNFTTGKIYSEVLRKERRGDYLGATIQVIPHITNEIKARVIDGAAGHDVVIVEVGGTVGDIESLPFLEALRQLAVQVGRERTIFMHLTLVPYIPTAGELKTKPTQHSAKELLSIGIQPDVLICRSDRMIPPNERAKIALFCNVPERAVISLKDVSSIYQIPALLKSQGLDDFICDRFHLTCPEADLSEWEQVLYQQANPTGEVIIGMVGKYTELPDAYKSVNEALKHAGLKNRLTVNIKYIDSQDVETKGVEILKGLDGILVPGGFGYRGVEGKILTAKYARENSIPYLGICLGMQVALIEFARNVAGMSHANSSEFDRTCEQPVVGLITEWQDADGNTEVRSDESDLGGTMRLGAQKCHLAEGSLARKLYGTETIEERHRHRYEVNNVLLPQIEKAGLKVTGLSADKKLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFEGFVKAAKDNQKRSD","837961","","CTP synthase","Cytoplasm","","
InterPro
IPR000991
Domain
Glutamine amidotransferase class-I
PF00117\"[289-524]TGATase
InterPro
IPR004468
Family
CTP synthase
PTHR11550\"[107-525]TCTP SYNTHASE
PF06418\"[1-265]TCTP_synth_N
TIGR00337\"[1-524]TPyrG: CTP synthase
InterPro
IPR012998
Active_site
Glutamine amidotransferase, class I, active site
PS00442\"[363-374]TGATASE_TYPE_I
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[1-274]Tno description
G3DSA:3.40.50.880\"[275-531]Tno description
signalp\"[1-22]?signal-peptide


","BeTs to 26 clades of COG0504COG name: CTP synthase (UTP-ammonia lyase)Functional Class: FThe phylogenetic pattern of COG0504 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.3e-09) to 2/2 blocks of the IPB000991 family, which is described as \"Glutamine amidotransferase class-I\". Interpro entry for IP:IPR000991. IPB000991A 363-372 9.2e-05 IPB000991B 498-508 0.0053Significant hit ( 5.5e-05) to 2/10 blocks of the IPB001674 family, which is described as \"GMP synthase C terminal domain\". Interpro entry for IP:IPR001674. IPB001674B 363-372 0.0041 IPB001674D 499-520 7.1","Residues 299 to 416 match (2e-54) PD:PD137961 which is described as CTP LIGASE PROTEOME COMPLETE SYNTHASE SYNTHETASE UTP--AMMONIA GLUTAMINE PYRIMIDINE AMIDOTRANSFERASE ","","","","","","","","","","","","Tue Jan 7 12:27:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01224 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 289 to 524 (E-value = 4e-77) place AA01224 in the GATase family which is described as Glutamine amidotransferase class-I (PF00117)","","","","","Meng Q, Switzer RL. Regulation of transcription of the Bacillus subtilis pyrG gene,encoding cytidine triphosphate synthetase. J Bacteriol. 2001 Oct;183(19):5513-22. PMID: 11544212 Wadskov-Hansen SL, Willemoes M, Martinussen J, Hammer K, NeuhardJ, Larsen S. Cloning and verification of the Lactococcus lactis pyrG gene andcharacterization of the gene product, CTP synthase. J Biol Chem. 2001 Oct 12;276(41):38002-9. PMID: 11500486","","Tue Jan 7 12:27:28 2003","1","","","" "AA01226","838206","838571","366","ATGGTAAGTAAAGCCAATGACGATTCAAGTCTATCACATACCAAATGGAACTGTAAGTATCACATCGTCTTCACCCCGAAATATAGAAGAAAAGCCATTTACGGAAGGCTTAGAACGGATATAGGTAGCATATTAAGGCAGTTATGCGACTATAAAAATGTGGAAATAATAGAAGCGCACGCAATGAAAGAGCATATTCATATGCTTCTAAAAATTCCGCCGAAATTATCGGTATCAAGTTTTATGGGGTATTTAAAGGGAAAATCATTTGAAAGGCACGCAAACCTAAAATACAACTATGGTAACCGACATTTTTGGTCGAAAGGCTATTATGTAAGCACGGTAGGGCTAAATACAAAGGTAGTG","","","14253","MVSKANDDSSLSHTKWNCKYHIVFTPKYRRKAIYGRLRTDIGSILRQLCDYKNVEIIEAHAMKEHIHMLLKIPPKLSVSSFMGYLKGKSFERHANLKYNYGNRHFWSKGYYVSTVGLNTKVV","838573","","IS200-like transposase ISAa1","Cytoplasm, Extracellular","","
InterPro
IPR002686
Family
Transposase IS200-like
PD003831\"[16-69]TTransposase_17
PF01797\"[23-122]TTransposase_17


","BeTs to 9 clades of COG1943COG name: Predicted transposaseFunctional Class: LThe phylogenetic pattern of COG1943 is -o-p----vd--b-efgh-nuj----Number of proteins in this genome belonging to this COG is","","Residues 16 to 69 match (1e-07) PD:PD590305 which is described as TRANSPOSASE PROTEOME COMPLETE ORFA PLASMID TRANSPOSASE PROBABLE VNG6182H IS605 A ","","","","","","","","","","","","Mon Feb 17 14:11:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01226 is paralogously related to AA00357 (1e-69), AA01244 (2e-32) and AA02040 (2e-24).","","","","","","Residues 23 to 122 (E-value = 3.2e-59) place AA01226 in the Transposase_17 family which is described as Transposase IS200 like (PF01797)","","","","Hayashida,H., Hotokezaka,H., Ohara,N., Kimura,M., Takagi,O. andYamada,T.Molecular analysis of a new insertion sequence from Actinobacillus(Haemophilus) actinomycetemcomitans FDC Y4Microbiology 142 (Pt 9), 2449-2452 (1996)PubMed: 8828211","","Tue Jan 7 12:36:08 2003","","1","","","" "AA01227","838759","838905","147","GTGCGGATTGTTATTTTTCTTGATTCACAGCTAAAAAACATCTGGAAATTCGACCGCACTTTTTGTTGTTTACGTCTCAAATTCATTCTTTTCATGAAAGCGTATAAGTTATTTAAAAGCTTATTGCTTTCGTTATGTTTTTTGTGC","","","5963","VRIVIFLDSQLKNIWKFDRTFCCLRLKFILFMKAYKLFKSLLLSLCFLC","838905","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-34]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:10:40 2004","Wed Feb 25 13:10:40 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01227 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 13:10:40 2004","","","","","","","","","","","","","1","","","" "AA01228","839037","839348","312","ATGTGTATCAAGGTTCTAGGTGGATCGCACCGTCGTTATGCTGCTATTGGTGACATTATCAAAATTACTGTGAAAGAAGCAATTCCACGCGGTAAAGTAAAAAAAGGTGATGTGTTAAAAGCAGTTGTTGTGCGCACCAAGAAGGGTGTTCGTCGCCCAGATGGGTCAGTTATTCGTTTCGATGGTAATGCCTGTGTGATTTTAAATAATAACACCGAGCAACCAATCGGTACTCGTATTTTTGGACCGGTGACTCGTGAACTTCGTTCTGAGAAATTCATGAAGATCATTTCCTTAGCTCCAGAAGTACTG","","","13485","MCIKVLGGSHRRYAAIGDIIKITVKEAIPRGKVKKGDVLKAVVVRTKKGVRRPDGSVIRFDGNACVILNNNTEQPIGTRIFGPVTRELRSEKFMKIISLAPEVL","839350","From GenBank (gi:1172957):This protein binds directly to 23s ribosomal RNA.","50S ribosomal protein L14","Cytoplasm","","
InterPro
IPR000218
Family
Ribosomal protein L14b/L23e
PD001093\"[1-103]TRL14_HAEIN_P44352;
G3DSA:2.40.150.20\"[1-104]Tno description
PTHR11761\"[1-104]T50S/60S RIBOSOMAL PROTEIN L14/L23
PF00238\"[1-104]TRibosomal_L14
PS00049\"[41-67]TRIBOSOMAL_L14
InterPro
IPR005745
Family
Ribosomal protein L14, bacterial and organelle form
PTHR11761:SF3\"[1-104]T50S RIBOSOMAL PROTEIN L14
TIGR01067\"[1-104]TrplN_bact: ribosomal protein L14


","BeTs to 26 clades of COG0093COG name: Ribosomal protein L14Functional Class: JThe phylogenetic pattern of COG0093 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-47) to 3/4 blocks of the IPB000218 family, which is described as \"Ribosomal protein L14b/L23e family\". Interpro entry for IP:IPR000218. IPB000218B 13-48 1.7e-22 IPB000218C 55-90 1.5e-18 IPB000218D 95-104 0.00083","Residues 2 to 104 match (5e-10) PD:PD529458 which is described as RIBOSOMAL MITOCHONDRIAL MITOCHONDRION 60S L14 ","","","","","","","","","","","Thu Jan 16 11:46:25 2003","Tue Jan 7 12:39:18 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01228 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 104 (E-value = 1.3e-55) place AA01228 in the Ribosomal_L14 family which is described as Ribosomal protein L14p/L23e (PF00238)","","","","","Cerretti,D.P., Dean,D., Davis,G.R., Bedwell,D.M. and Nomura,M. The spc ribosomal protein operon of Escherichia coli: sequenceand cotranscription of the ribosomal protein genes and a proteinexport gene. Nucleic Acids Res. 11(9): 2599-2616.1983 PubMed: 6222285.Morinaga,T., Funatsu,G. and Funatsu,M.Primary structure of protein L14 isolated from Escherichia coliribosomesFEBS Lett. 91 (1), 74-77 (1978)PubMed: 352727","","Tue Jan 7 12:42:03 2003","1","","","" "AA01229","839362","839670","309","ATGGCTGCAAAAATCCGTCAAAATGATGAAGTAATTGTGCTTACCGGCAAAAGCAAAGGTAAGCGCGGTAAGGTAACCAAAGTGTTATCTAACGGTAAAGTGATTGTTGAAGGCGTAAACATTATTACTAAACATGAGAAATCGGTACCTGCATTAGGTAAAGAGGGTGGTTTAGTGAAGAAAGAAGCTGCGATTGATGTATCAAATGTTGCTATTTTCAATCCAACAACAAATAAAGCTGACCGAGTAGGCTTTAGATTTGAAGACGGCAAAAAAGTACGTTTCTTCAAATCTAATAATGAAATTATT","","","11205","MAAKIRQNDEVIVLTGKSKGKRGKVTKVLSNGKVIVEGVNIITKHEKSVPALGKEGGLVKKEAAIDVSNVAIFNPTTNKADRVGFRFEDGKKVRFFKSNNEII","839672","From GenBank (gi:1172999): This protein is found in the ribonucleoprotein core and is involved in the early assembly of the 50s subunit. It is not involved in the functions of the mature subunit.","50S ribosomal protein L24","Cytoplasm","","
InterPro
IPR003256
Family
Ribosomal protein L24
PD001677\"[8-40]TRL24_HAEIN_P44362;
PTHR12903\"[2-103]TMITOCHONDRIAL RIBOSOMAL PROTEIN L24
TIGR01079\"[2-103]TrplX_bact: ribosomal protein L24
InterPro
IPR005824
Domain
KOW
PF00467\"[5-37]TKOW
InterPro
IPR005825
Family
Ribosomal protein L24/L26
PS01108\"[8-25]TRIBOSOMAL_L24
InterPro
IPR006646
Domain
KOW (Kyrpides, Ouzounis, Woese) motif
SM00739\"[4-31]TKOW


","BeTs to 23 clades of COG0198COG name: Ribosomal protein L24Functional Class: JThe phylogenetic pattern of COG0198 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.7e-17) to 2/2 blocks of the IPB000302 family, which is described as \"Ribosomal protein L24/bacterial NUSG\". Interpro entry for IP:IPR000302. IPB000302A 5-39 4.2e-13 IPB000302B 62-72 0.015","Residues 71 to 103 match (2e-09) PD:PD019472 which is described as RIBOSOMAL L24 PROTEOME COMPLETE 50S SUBUNIT ","","","","","","","","","","","Tue Jan 7 12:48:18 2003","Tue Jan 7 12:43:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01229 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 37 (E-value = 5.4e-07) place AA01229 in the KOW family which is described as KOW motif (PF00467)","","","","","Cerretti,D.P., Dean,D., Davis,G.R., Bedwell,D.M. and Nomura,M.The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene. Nucleic Acids Res. 11(9): 2599-2616. 1983 PubMed: 6222285. ","","Tue Jan 7 12:43:29 2003","1","","","" "AA01230","839691","840227","537","ATGGCGAAACTGCATGATTACTACAGAGATCAAGTAGTAAATGAATTGAAAACGAAATTCAACTACTCATCTGTCATGCAAGTCCCACGAATCGAAAAGATAACCCTAAATATGGGTGTGGGTGAAGCATTGACCGATAAAAAATTGCTAGATAATGCGGTGGCAGATCTGGCAGCAATTAGCGGTCAAAAACCTTTGATTACTAAAGCCCGTAAATCTGTTGCAGGCTTTAAAATCCGTCAGGGATATCCAATCGGTTGTAAAGTAACACTACGTGGTGAACGTATGTGGGAGTTCTTAGAACGTTTAATTACAATTGCTGTTCCACGTATTCGTGACTTCCGCGGTTTAAGCGCGAAATCATTTGATGGTCGTGGAAATTACAGTATGGGTGTGCGTGAGCAAATCATCTTCCCTGAAATCGACTACGATAAAGTAGATCGTGTACGTGGTTTAGATATTACTATTACCACCACAGCTAAGAATGATGAAGAAGGTCGAGCACTATTGGCTGCCTTTAATTTCCCATTCCGTAAG","","","20333","MAKLHDYYRDQVVNELKTKFNYSSVMQVPRIEKITLNMGVGEALTDKKLLDNAVADLAAISGQKPLITKARKSVAGFKIRQGYPIGCKVTLRGERMWEFLERLITIAVPRIRDFRGLSAKSFDGRGNYSMGVREQIIFPEIDYDKVDRVRGLDITITTTAKNDEEGRALLAAFNFPFRK","840229","From GenBank (gi:1173053): This is one of the 3 proteins that mediate the attachment of the 5s RNA into the large ribosomal subunit.","50S ribosomal protein L5","Cytoplasm","","
InterPro
IPR002132
Family
Ribosomal protein L5
PTHR11994\"[1-179]T60S RIBOSOMAL PROTEIN L11-RELATED
PF00281\"[24-80]TRibosomal_L5
PF00673\"[84-178]TRibosomal_L5_C
PS00358\"[57-73]TRIBOSOMAL_L5
InterPro
IPR003236
Family
Mitochondrial ribosomal protein L5
PD013434\"[8-179]TRL5_BACHD_Q9Z9K2;
noIPR
unintegrated
unintegrated
G3DSA:3.30.1440.10\"[1-179]Tno description
PTHR11994:SF4\"[1-179]T50S RIBOSOMAL PROTEIN L5


","BeTs to 26 clades of COG0094COG name: Ribosomal protein L5Functional Class: JThe phylogenetic pattern of COG0094 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.7e-62) to 3/3 blocks of the IPB002132 family, which is described as \"Ribosomal protein L5\". Interpro entry for IP:IPR002132. IPB002132A 26-43 2.6e-12 IPB002132B 60-102 1.9e-36 IPB002132C 122-139 5.8e-11","Residues 1 to 179 match (5e-93) PD:PD013434 which is described as RIBOSOMAL L5 50S PROTEOME COMPLETE RRNA-BINDING 60S L11 CHLOROPLAST L5P ","","","","","","","","","","","Tue Jan 7 12:51:04 2003","Tue Jan 7 12:49:54 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01230 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 84 to 178 (E-value = 5.1e-60) place AA01230 in the Ribosomal_L5_C family which is described as ribosomal L5P family C-terminus (PF00673)","","","","","Cerretti,D.P., Dean,D., Davis,G.R., Bedwell,D.M. and Nomura,M. The spc ribosomal protein operon of Escherichia coli: sequenceand cotranscription of the ribosomal protein genes and aprotein export gene. Nucleic Acids Res. 11(9): 2599-2616.1983. PubMed: 6222285.","","Tue Jan 7 12:49:54 2003","1","","","" "AA01231","840243","840545","303","ATGGCTAAACAATCAATGAAAGCACGCGACGTAAAACGCGTGAAATTGGCTGAAAAATTCTATGCTAAACGTGTAGAGTTGAAAAAAATTATTTCTGACATTAATGCCTCTGACGAAGATCGTTGGAATGCCGTGTTGAAGTTACAAACTTTACCTCGTGATTCTAGCCCTAGTCGTCAACGTAACCGTTGTCGTCAAACCGGACGTCCACATGGCGTTCTTCGTAAGTTTGGTTTAAGCCGTATTAAGGTTCGTGAAGCTGCTATGCGGGGAGAGATCCCAGGTCTTAAGAAAGCTAGTTGG","","","11672","MAKQSMKARDVKRVKLAEKFYAKRVELKKIISDINASDEDRWNAVLKLQTLPRDSSPSRQRNRCRQTGRPHGVLRKFGLSRIKVREAAMRGEIPGLKKASW","840547","From GenBank(gi:1173203): This protein is required for the assembly of 30s particles and may also be responsible for determining the conformation of the 16s rRNA at the A site.","30S ribosomal protein S14","Periplasm, Cytoplasm","","
InterPro
IPR001209
Family
Ribosomal protein S14
PTHR19836\"[1-101]T30S RIBOSOMAL PROTEIN S14
PF00253\"[46-100]TRibosomal_S14
PS00527\"[63-85]TRIBOSOMAL_S14
noIPR
unintegrated
unintegrated
G3DSA:4.10.830.10\"[41-101]Tno description
PTHR19836:SF1\"[1-101]TCHLOROPLAST 30S RIBOSOMAL PROTEIN S14


","BeTs to 20 clades of COG0199COG name: Ribosomal protein S14Functional Class: JThe phylogenetic pattern of COG0199 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.1e-23) to 1/1 blocks of the IPB001209 family, which is described as \"Ribosomal protein S14\". Interpro entry for IP:IPR001209. IPB001209 63-101 1.9e-23","Residues 1 to 41 match (7e-09) PD:PD187684 which is described as RIBOSOMAL 30S S14 COMPLETE PROTEOME CHLOROPLAST CYANELLE S14-2 ","","","","","","","","","","","Thu Jan 16 11:58:16 2003","Tue Jan 7 12:53:37 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01231 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 101 (E-value = 2.5e-57) place AA01231 in the Ribosomal_S14 family which is described as Ribosomal protein S14p/S29e (PF00253)","","","","","Cerretti,D.P., Dean,D., Davis,G.R., Bedwell,D.M. andNomura,M. The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene. Nucleic Acids Res. 11(9): 2599-2616. PubMed: 6222285.","","Tue Jan 7 12:53:37 2003","1","","","" "AA01232","840585","840974","390","ATGAGTATGCAAGATCCTATCGCAGATATGTTGACCCGCATTCGTAACGGTCAAGCTGCGAATAAAGTTGCGATCAGTATGCCTTCATCCAGGCTAAAAGTTGCAATTGCCAATGTATTAGCTAGCGAAGGTTATATCGAAAGCGTTAAAGTAGTTGAAGGTGTAAAACCTGAATTGGAAATTACGTTAAAATATTTCCAAGGTAAACCGGTTGTAGAAAGTATCCAGCGTGTAAGTCGCCCAGGTCTTCGTATTTATAAACGTAAAGACGAATTACCAAAAGTAATGGGTGGCTTAGGTATCGCTGTGGTATCTACATCTAAAGGTGTAATGACTGACCGTGCAGCTCGTCAAGCTGGTTTAGGCGGTGAGATCATTTGTTATGTAGCT","","","14001","MSMQDPIADMLTRIRNGQAANKVAISMPSSRLKVAIANVLASEGYIESVKVVEGVKPELEITLKYFQGKPVVESIQRVSRPGLRIYKRKDELPKVMGGLGIAVVSTSKGVMTDRAARQAGLGGEIICYVA","840976","From GenBank (gi:1173281): This protein is one of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.","30S ribosomal protein S8","Cytoplasm","","
InterPro
IPR000630
Family
Ribosomal protein S8
PD001098\"[10-129]TRS8_PASMU_Q9CL44;
PTHR11758\"[2-130]T30S RIBOSOMAL PROTEIN S8
PF00410\"[5-130]TRibosomal_S8
PS00053\"[100-117]TRIBOSOMAL_S8
noIPR
unintegrated
unintegrated
G3DSA:3.30.1370.30\"[2-72]Tno description
G3DSA:3.30.1490.10\"[73-130]Tno description


","BeTs to 26 clades of COG0096COG name: Ribosomal protein S8Functional Class: JThe phylogenetic pattern of COG0096 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.2e-40) to 3/3 blocks of the IPB000630 family, which is described as \"Ribosomal protein S8\". Interpro entry for IP:IPR000630. IPB000630A 5-17 4.6e-08 IPB000630B 28-50 8.3e-08 IPB000630C 98-130 1.5e-21 IPB000630C 73-105 0.5","Residues 2 to 129 match (3e-58) PD:PD001098 which is described as RIBOSOMAL S8 30S PROTEOME COMPLETE RRNA-BINDING CHLOROPLAST S15A 40S S8P ","","","","","","","","","","","Thu Jan 16 11:59:20 2003","Tue Jan 7 12:56:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01232 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 130 (E-value = 1.6e-68) place AA01232 in the Ribosomal_S8 family which is described as Ribosomal protein S8 (PF00410)","","","","","Cerretti,D.P., Dean,D., Davis,G.R., Bedwell,D.M. andNomura,M. The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes Frand a protein export gene. Nucleic Acids Res. 11(9): 2599-2616.1983. PubMed: 6222285.","","Tue Jan 7 12:56:24 2003","1","","","" "AA01233","840993","841523","531","ATGTCTCGTGTTGCAAAAGCACCTGTTAGTATTCCTGCCGGCGTTGAGGTAAAACTTAACGGACAGTTACTAACAATTAAAGGTAAAAATGGTGAGTTGTCACGCTCTATTCATCATTCAGTAGAAGTTAAGCATGAAAATAATGAATTAACATTCTCGCCACGTGAAGGTGTTGAAGGTGGTAACGCTCAATCCGGTACTGCCAGAGCATTAGTTAATTCCATGGTTATTGGTGTTACTGAAGGATTTACAAGAAAACTACAATTAGTAGGTGTAGGTTATAGAGCTCAAATTAAAGGAAATGCTGTTGCTTTAAGTCTTGGATTTTCTCACCCTGTTGAGCATGTTTTACCTGCGGGGATTACTGCTGAATGTCCTTCTCAAACTGAAATTGTTTTGAAAGGTTCAGATAAACAGTTAATCGGTCAAGTTGCCGCAGATATTCGTGCTTATCGTCGTCCTGAACCGTATAAAGGTAAAGGGGTACGTTACGCTGATGAAGTGGTGCGTATTAAAGAAGCTAAGAAGAAA","","","18973","MSRVAKAPVSIPAGVEVKLNGQLLTIKGKNGELSRSIHHSVEVKHENNELTFSPREGVEGGNAQSGTARALVNSMVIGVTEGFTRKLQLVGVGYRAQIKGNAVALSLGFSHPVEHVLPAGITAECPSQTEIVLKGSDKQLIGQVAADIRAYRRPEPYKGKGVRYADEVVRIKEAKKK","841525","From GenBank (gi:1173060): This protein binds directly to 23s ribosomal RNA and is located at the aminoacyl-tRNA binding site of the peptidyltransferase center.","50S ribosomal protein L6","Cytoplasm","","
InterPro
IPR000702
Family
Ribosomal protein L6
PD002236\"[87-177]TQ9CL45_PASMU_Q9CL45;
PR00059\"[71-96]T\"[99-115]T\"[141-162]TRIBOSOMALL6
G3DSA:3.90.930.12\"[2-82]T\"[83-175]Tno description
PTHR11655\"[2-176]T60S/50S RIBOSOMAL PROTEIN L6/L9
PF00347\"[11-82]T\"[90-165]TRibosomal_L6
InterPro
IPR002358
Family
Ribosomal protein L6, signature 1
PS00525\"[154-162]TRIBOSOMAL_L6_1
noIPR
unintegrated
unintegrated
PTHR11655:SF6\"[2-176]T50S RIBOSOMAL PROTEIN L6


","No hits to the COGs database.","Significant hit ( 6e-83) to 3/3 blocks of the IPB002358 family, which is described as \"Ribosomal protein L6, signature 1\". Interpro entry for IP:IPR002358. IPB002358A 1-31 2.8e-15 IPB002358B 65-113 9.3e-34 IPB002358C 133-175 1.2e-31Significant hit ( 6.7e-44) to 3/3 blocks of the PR00059 family, which is described as \"Ribosomal protein L6 signature\". Prints database entry for PR:PR00059. PR00059A 71-96 1.2e-17 PR00059B 99-115 2.3e-07 PR00059C 141-162 5.2e-16Significant hit ( 4.1e-15) to 3/3 blocks of the IPB002359 family, which is described as \"Ribosomal protein L6, signature 2\". Interpro entry for IP:IPR002359. IPB002359A 9-39 6.6e-07 IPB002359B 59-98 0.00033 IPB002359C 128-171 1.7","","","","","","","","","","","","Thu Jan 16 12:00:38 2003","Tue Jan 7 12:59:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01233 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 90 to 165 (E-value = 3.1e-31) place AA01233 in the Ribosomal_L6 family which is described as Ribosomal protein L6 (PF00347)","","","","","Cerretti,D.P., Dean,D., Davis,G.R., Bedwell,D.M. andNomura,M. . The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene. Nucleic Acids Res. 11(9): 2599-2616.1983 PubMed: 6222285.","","Tue Jan 7 12:59:24 2003","1","","","" "AA01234","841540","841890","351","ATGGATAAGAAATCAGCTCGTATCCGTCGTGCGGCTCGTGCGCGTCATATGATGAGAGAGCAAGGTGTAACGCGTTTAGTTGTTCACCGTACTCCGCGTCATATTTACGCTCAAGTTATCGCACCAAACGGTTCAGAAGTGCTTGCCGCTGCTTCTACTGTTGAGAAGGCAATTATTGAGCAAGTAAAATATACCGGAAATAAAGATGCAGCAGCAGTTGTAGGCAAAATTGTTGCAGAAAGAGCATTAGCAAAAGGGGTCAAAGATATTGCTTTTGACCGTTCTGGTTTTAAATATCATGGCCGTATCCAATCTTTAGCGGATGCTGCTCGTGAAGCTGGTCTACAGTTC","","","12822","MDKKSARIRRAARARHMMREQGVTRLVVHRTPRHIYAQVIAPNGSEVLAAASTVEKAIIEQVKYTGNKDAAAVVGKIVAERALAKGVKDIAFDRSGFKYHGRIQSLADAAREAGLQF","841892","From GenBank (gi:1172979): This is one of the 3 proteins that mediate the attachment of the 5s RNA into the large ribosomal subunit.","50S ribosomal protein L18","Cytoplasm","","
InterPro
IPR004389
Family
Ribosomal protein L18
TIGR00060\"[3-117]TL18_bact: ribosomal protein L18
InterPro
IPR005484
Family
Ribosomal protein L18P/L5E
PD001394\"[28-117]TQ9CL46_PASMU_Q9CL46;
PF00861\"[1-117]TRibosomal_L18p
noIPR
unintegrated
unintegrated
G3DSA:3.30.420.100\"[23-117]Tno description


","BeTs to 23 clades of COG0256COG name: Ribosomal protein L18Functional Class: JThe phylogenetic pattern of COG0256 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 25 to 117 match (5e-33) PD:PD001394 which is described as RIBOSOMAL L18 50S PROTEOME COMPLETE RRNA-BINDING CHLOROPLAST SUBUNIT PROBABLE CYANELLE ","","","","","","","","","","","Thu Jan 16 12:02:39 2003","Tue Jan 7 13:01:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01234 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 117 (E-value = 2.7e-50) place AA01234 in the Ribosomal_L18p family which is described as Ribosomal L18p/L5e family (PF00861)","","","","","Cerretti,D.P., Dean,D., Davis,G.R., Bedwell,D.M. andNomura,M. The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene. Nucleic Acids Res. 11(9): 2599-2616.1983 PubMed: 6222285.","","Tue Jan 7 13:01:23 2003","1","","","" "AA01235","841909","842406","498","ATGTCAAACATCGAAAAACAAGCTGGTGAACTGCAAGAGAAGCTAATTGCGGTAAACCGCGTATCTAAAACTGTAAAAGGTGGTCGTATCATGAGCTTTACTGCGTTAACCGTAGTAGGTGATGGTAATGGTCGCGTTGGTTTTGGATATGGCAAAGCGCGCGAAGTTCCTGCAGCTATTCAAAAAGCAATGGAGAAAGCGCGTCGTAATATGATCAATGTTGCTTTAAGTGAAGGTACATTGCAGCATCCTATTAAAGGTACCCACACCGGTTCTCGTGTATTTATGCAACCGGCAAGTGAGGGTACCGGTATCATTGCAGGTGGTGCGATGCGTGCTGTATTGGAAGTAGCTGGCGTACGTAACGTATTGTCAAAAGCTTATGGTTCAACTAATCCAATCAATGTTGTTCGTGCAACTATTGATGCTTTAGCAAATATGAAATCACCAGAAATGGTTGCTGCTAAACGTGGTAAATCAGTTGATGAAATTTTGGGG","","","17432","MSNIEKQAGELQEKLIAVNRVSKTVKGGRIMSFTALTVVGDGNGRVGFGYGKAREVPAAIQKAMEKARRNMINVALSEGTLQHPIKGTHTGSRVFMQPASEGTGIIAGGAMRAVLEVAGVRNVLSKAYGSTNPINVVRATIDALANMKSPEMVAAKRGKSVDEILG","842408","From GenBank (gi:1173266): This protein with s4 and s12 plays an important role in translational accuracy.","30S ribosomal protein S5","Cytoplasm","","
InterPro
IPR000851
Family
Ribosomal protein S5
PTHR13718\"[10-165]TRIBOSOMAL S SUBUNIT
InterPro
IPR002197
Domain
Helix-turn-helix, Fis-type
PR01590\"[58-75]T\"[162-166]THTHFIS
InterPro
IPR005324
Domain
Ribosomal protein S5, C-terminal
PF03719\"[85-158]TRibosomal_S5_C
InterPro
IPR005712
Family
Ribosomal protein S5, bacterial and chloroplast
TIGR01021\"[8-163]TrpsE_bact: ribosomal protein S5
InterPro
IPR013810
Domain
Ribosomal protein S5, N-terminal
PF00333\"[10-76]TRibosomal_S5
PS50881\"[11-74]TS5_DSRBD
PS00585\"[28-60]TRIBOSOMAL_S5
InterPro
IPR014720
Domain
Double-stranded RNA-binding-like
G3DSA:3.30.160.20\"[1-73]Tno description
InterPro
IPR014721
Domain
Ribosomal protein S5 domain 2-type fold
G3DSA:3.30.230.10\"[74-150]Tno description
noIPR
unintegrated
unintegrated
PTHR13718:SF2\"[10-165]T30S RIBOSOMAL PROTEIN S5


","BeTs to 26 clades of COG0098COG name: Ribosomal protein S5Functional Class: JThe phylogenetic pattern of COG0098 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.7e-73) to 2/2 blocks of the IPB000851 family, which is described as \"Ribosomal protein S5\". Interpro entry for IP:IPR000851. IPB000851A 15-68 1.9e-40 IPB000851B 85-135 7.1e-32","Residues 10 to 76 match (2e-25) PD:PD336298 which is described as RIBOSOMAL S5 30S COMPLETE PROTEOME S2 40S S5P CHLOROPLAST PROBABLE ","","","","","","","","","","","Thu Jan 16 12:04:20 2003","Tue Jan 7 13:03:57 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01235 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 85 to 158 (E-value = 7.3e-42) place AA01235 in the Ribosomal_S5_C family which is described as Ribosomal protein S5, C-terminal domain (PF03719)","","","","","Bjorkman J, Samuelsson P, Andersson DI, Hughes D.Novel ribosomal mutations affecting translational accuracy, antibiotic resistance and virulence of Salmonella typhimurium.Mol Microbiol. 1999 Jan;31(1):53-8.PMID: 9987109Cerretti,D.P., Dean,D., Davis,G.R., Bedwell,D.M. andNomura,M. 1983. The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene. Nucleic Acids Res. 11(9): 2599-2616. PubMed: 6222285.","","Thu Jan 16 12:08:24 2003","1","","","" "AA01235.1","842416","842595","180","ATGGCTAAAACTATTAAAGTAACGCAAGTTCGTAGTTCTATTGCTCGTTTGCCGAAGCATAAAGCTACACTACGTGGTCTTGGTCTTCGCCATATGCATCATACTGTTGAGTTAATTGATACTCTGGTAGTACGAGGAATGATTAACCAGGTTTCATATATGGTTAAAGTGGAGGAGTAA","0.00","0.00","6705","MAKTIKVTQVRSSIARLPKHKATLRGLGLRHMHHTVELIDTLVVRGMINQVSYMVKVEE$","","","50S ribosomal protein L30","Cytoplasm","Nearest neighbor is 15603262, a RpL30 protein from Pasteurella multocida: residues 1-59 are 96% similar to this protein.AA01235.1 has significant similarity to the Haemophilus ducreyi gene HD1960, a 50S ribosomal protein L30 (3e-24)AA01235.1 has significant similarity to the Haemophilus influenzae genes, 16272737, a ribosomal protein L30 (3e-24) and 1573806, a ribosomal protein L30 (3e-27).","
InterPro
IPR000517
Domain
Ribosomal protein L30
PF00327\"[3-55]TRibosomal_L30
PS00634\"[23-55]TRIBOSOMAL_L30
InterPro
IPR005996
Family
Ribosomal protein L30, bacterial
TIGR01308\"[5-59]TrpmD_bact: ribosomal protein L30
noIPR
unintegrated
unintegrated
G3DSA:3.30.1390.20\"[2-59]Tno description


","No hits to the COGs database.","Significant hit ( 1.6e-22) to 1/1 blocks of the IPB000517 family, which is described as \"Ribosomal protein L30\". Interpro entry for IP:IPR000517. IPB000517 11-58 1.3e-22","Residues 10 to 59 match (7e-15) PD:PD005137 which is described as RIBOSOMAL L30 COMPLETE PROTEOME 50S MITOCHONDRIAL MITOCHONDRION 60S PROBABLE BL27 ","Fri Feb 27 10:02:20 2004","Sat Feb 28 16:52:17 2004","Sat Feb 28 16:52:17 2004","Sat Feb 28 16:52:17 2004","Fri Feb 27 10:02:20 2004","Fri Feb 27 10:02:20 2004","Fri Feb 27 10:02:20 2004","Fri Feb 27 10:02:20 2004","Fri Feb 27 10:02:20 2004","Fri Feb 27 10:02:20 2004","Fri Feb 27 10:02:20 2004","Fri Feb 27 10:02:59 2004","Fri Feb 27 10:02:20 2004","Fri Feb 27 10:02:20 2004","Fri Feb 27 10:02:20 2004","Fri Feb 27 10:02:20 2004","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01235.1 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Fri Feb 27 10:02:20 2004","Fri Feb 27 10:02:20 2004","","","","Residues 3 to 55 (E-value = 3e-18) place AA01235.1 in the Ribosomal_L30 family which is described as Ribosomal protein L30p/L7e (PF00327)","Fri Feb 27 10:02:20 2004","","","","Ritter,E. and Wittmann-Liebold,B.The primary structure of protein L30 from Escherichia coliribosomesFEBS Lett. 60 (1), 153-155 (1975)PubMed: 776670 ","","Fri Feb 27 10:02:59 2004","1","Fri Feb 27 10:02:20 2004","","" "AA01236","842599","843030","432","ATGCGCTTAAATACTCTATCTCCGGCTGAAGGTGCTAAGCATAGTGCTAAACTTCTTGGTCGTGGTATTGGTTCAGGTTTAGGTAAAACTGGTGGACGTGGTCATAAAGGTCAAAAATCTCGTACTGGTGGCGGTGTTCGTCGTGGGTTCGAAGGTGGTCAAATGCCTTTATATCGTCGTTTACCTAAATTTGGTTTTACTTCTATGAAATCTGCAGTAACAGCAGAAGTCCGTCTAGACGACCTGAATAAAATTGAAAATGGTATTGTGACTTTAGAAACATTAAAAGCTGCCAATATTTTAACTAAGGATATTCAGTTTGCTAAAGTAATTTTAGCGGGTGAAGTTAAAAATAAATTAGTTATTCGTGGGTTGCGTGTGACTAAAGGCGCCAAAGCAGCTATTGAAGCTGCTGGTGGTTCAATCGAGGAA","","","15152","MRLNTLSPAEGAKHSAKLLGRGIGSGLGKTGGRGHKGQKSRTGGGVRRGFEGGQMPLYRRLPKFGFTSMKSAVTAEVRLDDLNKIENGIVTLETLKAANILTKDIQFAKVILAGEVKNKLVIRGLRVTKGAKAAIEAAGGSIEE","843032","From GenBank (gi:1172965): This protein binds directly to 23s ribosomal RNA.","50S ribosomal protein L15","Cytoplasm, Extracellular","","
InterPro
IPR001196
Family
Ribosomal protein L15
PF00256\"[109-140]TL15
PF01305\"[1-101]TRibosomal_L15
PS00475\"[109-139]TRIBOSOMAL_L15
InterPro
IPR005749
Family
Ribosomal protein L15, bacterial form
PTHR12934\"[40-143]T50S RIBOSOMAL PROTEIN L15
TIGR01071\"[2-143]TrplO_bact: ribosomal protein L15


","BeTs to 19 clades of COG0200COG name: Ribosomal protein L15Functional Class: JThe phylogenetic pattern of COG0200 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.9e-20) to 2/2 blocks of the IPB001196 family, which is described as \"Ribosomal protein L15\". Interpro entry for IP:IPR001196. IPB001196A 17-41 1.8e-12 IPB001196B 119-140 3.3e-06","Residues 1 to 95 match (5e-20) PD:PD003120 which is described as RIBOSOMAL L15 50S PROTEOME COMPLETE RRNA-BINDING CHLOROPLAST SUBUNIT PRECURSOR MITOCHONDRIAL ","","","","","","","","","","","Tue Jan 7 13:05:56 2003","Tue Jan 7 13:05:56 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01236 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 109 to 140 (E-value = 4e-07) place AA01236 in the L15 family which is described as Ribosomal protein L15 (PF00256)","","","","","Cerretti,D.P., Dean,D., Davis,G.R., Bedwell,D.M. andNomura,M. The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a proteinexport gene Nucleic Acids Res. 11 (9), 2599-2616 (1983) PubMed: 6222285 Giorginis,S. and Chen,R. The primary structure of protein L15 located at the peptidyltransferase center of Escherichia coli ribosomes FEBS Lett. 84 (2), 347-350 (1977) PubMed: 340263 ","","Tue Jan 7 13:05:56 2003","1","","","" "AA01237","843037","844359","1323","ATGGCTAAACAACCAGGCTATCAAACAAGAAGTACTCAAGGTGGTACAAGTGAGCTAAAGAGCAGATTGTTATTTGTTTTAGGTGCACTTATTGTTTTCCGAATTGGTTCATTCATTCCGGTTCCTGGTATAGACGCGGCTGTATTAGCTCAGTTGATTGAACAACAAAAAGGCACCATCATTGATATGTTTAATATGTTCTCTGGTGGTGCGTTGAGCCGGGCTTCAATTTTTGCGCTTGGTATTATGCCTTATATTTCGGCATCAATTATTATCCAATTGTTAGCTTCGGTTCATCCGGCACTTGCGGAATTAAGAAAAGAAGGTGAGTCAGGTCGTCGTAAGATTAGTAAATATACCCGTTATTCAACGGTTGTGCTTGCTACTCTACAGGCGGTAGGTATTTCAACTGGCTTGCCTAATATGTTACCTGGCTTGGTTCCTAATTTGGGATTCGGCTTTTACTTTACTGCCGTAATTAGTTTAGTTACAGGAACTATGTTCTTGATGTGGTTAGGTGAACAAATTACAGAGCGTGGTATTGGTAATGGTATTTCTTTGATTATTTTTGCGGGGATTGTGGCCGGCTTGCCTGCAGCTGTAGGTCAAACGATTGAGCAAGCTCGTCTTGGTCAAATGCATTTCCTTGTTCTTCTATTAATTGCTGTAATTGTTTTAGCAGTTACTTACTTTGTGGTCTTTGTAGAAAGAGGGCAGAGAAGAATAAAGGTTGAGTATGCTAAACGTCAACAAGGCAGACAAATCTTGGGTGGCCACTCTACTCACCTTCCACTGAAAGTGAATATGGCGGGGGTTATTCCAGCGATTTTTGCATCAAGTATAATTCTTTTCCCTGCGACATTAACCCAATGGGTAGGTCAGGGTTCTAGTCTAGAATGGTTAACTGATTTATCAATGTTATTACATCCTGGACAGCCTTTATACTTAGTCGTTTATGCTAGTGCCATCATCTTCTTTAGTTTTTTCTATACTGCTATGCAATATAATCCTAGAGATACAGCAGATAATTTGAAAAAATCAGGTGCATTTATACCTGGAATTAGACCAGGGGAACAAACATCTCGGTACATTGATAAGATTATGACCAGACTTACCCTTATTGGTGGTCTTTATGTTACATTTGTTTGTTTAGTTCCGTATATCATGACATCTGCTTGGAATGTACAGTTTTATTTCGGTGGTACATCTTTGCTAATTGTTGTGGTGGTAATTATGGATTTCATCGTTCAGATTCAGAGTCATTTGATGTCTACAAGATATGAGTCTGCGCTGAAAAAAGCAAACCTTAAAGGTTTTGGACAA","","","48182","MAKQPGYQTRSTQGGTSELKSRLLFVLGALIVFRIGSFIPVPGIDAAVLAQLIEQQKGTIIDMFNMFSGGALSRASIFALGIMPYISASIIIQLLASVHPALAELRKEGESGRRKISKYTRYSTVVLATLQAVGISTGLPNMLPGLVPNLGFGFYFTAVISLVTGTMFLMWLGEQITERGIGNGISLIIFAGIVAGLPAAVGQTIEQARLGQMHFLVLLLIAVIVLAVTYFVVFVERGQRRIKVEYAKRQQGRQILGGHSTHLPLKVNMAGVIPAIFASSIILFPATLTQWVGQGSSLEWLTDLSMLLHPGQPLYLVVYASAIIFFSFFYTAMQYNPRDTADNLKKSGAFIPGIRPGEQTSRYIDKIMTRLTLIGGLYVTFVCLVPYIMTSAWNVQFYFGGTSLLIVVVVIMDFIVQIQSHLMSTRYESALKKANLKGFGQ","844361","From GenBank (gi:134413): This proteinis involved in protein export. It interacts iwth SecA and SecE to allow the translocation of proteins across the plasma membrane by forming part of a channel.","preprotein translocase","Inner membrane, Cytoplasm","","
InterPro
IPR002208
Family
SecY protein
PR00303\"[23-41]T\"[75-95]T\"[116-139]T\"[152-177]T\"[178-201]T\"[270-289]T\"[313-335]T\"[368-386]T\"[400-418]TSECYTRNLCASE
PTHR10906\"[16-440]TSECY/SEC61-ALPHA FAMILY MEMBER
PF00344\"[76-417]TSecY
TIGR00967\"[20-427]T3a0501s007: preprotein translocase, SecY su
PS00755\"[76-95]TSECY_1
PS00756\"[171-188]TSECY_2
noIPR
unintegrated
unintegrated
PTHR10906:SF2\"[16-440]TPROTEIN TRANSLOCASE SECY SUBUNIT
signalp\"[1-37]?signal-peptide
tmhmm\"[21-41]?\"[72-92]?\"[122-142]?\"[152-172]?\"[181-201]?\"[215-235]?\"[272-292]?\"[311-329]?\"[372-392]?\"[398-416]?transmembrane_regions


","No hits to the COGs database.","Significant hit (4.5e-116) to 6/6 blocks of the IPB002208 family, which is described as \"SecY protein\". Interpro entry for IP:IPR002208. IPB002208A 22-44 9.1e-13 IPB002208B 69-95 3.6e-20 IPB002208C 112-132 5.9e-08 IPB002208D 162-198 7.6e-31 IPB002208E 262-281 1.4e-11 IPB002208F 323-357 2.6e-26","Residues 162 to 329 match (3e-07) PD:PD459741 which is described as SECY TRANSLOCASE PREPROTEIN ","","","","","","","","","","","Tue Jan 7 13:10:25 2003","Tue Jan 7 13:10:25 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01237 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 76 to 417 (E-value = 1.9e-196) place AA01237 in the SecY family which is described as eubacterial secY protein (PF00344)","","","","","Breyton C, Haase W, Rapoport TA, Kuhlbrandt W, Collinson I.Three-dimensional structure of the bacterial protein-translocation complex SecYEG. Nature. 2002 Aug 8;418(6898):662-5. PMID: 12167867 Mori H, Shimizu Y, Ito K. Super active secY variants that fulfill the essential translocation function with a reduced cellular quantity. J Biol Chem. 2002 Sep 25 [epub ahead of print] PMID: 12351621 van der Sluis E, Nouwen N, Driessen A. SecY-SecY and SecY-SecG contacts revealed by site-specific crosslinking. FEBS Lett. 2002 Sep 11;527(1-3):159. PMID: 12220653Ito,K.Structure, function, and biogenesis of SecY, an integral membraneprotein involved in protein exportJ. Bioenerg. Biomembr. 22 (3), 353-367 (1990)PubMed: 2202723","","Tue Jan 7 13:10:25 2003","1","","","" "AA01238","844388","844498","111","ATGAAAGTTCGTGCTTCCGTTAAGAAATTATGTCGTAACTGTAAGATTGTTAAACGCGAAGGTGTTGTTCGTGTACTTTGTAGCGATCCTAAGCATAAACAACGTCAAGGT","0.00","0.00","4261","MKVRASVKKLCRNCKIVKREGVVRVLCSDPKHKQRQG","844498","AA01238 is part of a cluster of genes that is conserved in the closely related A. actinomycetemcomitans, H. influenzae, and H. ducreyi. The corresponding genes (HD1955, gi:1173040) in H. decreyi and H.influenzae organisms are both 50s ribosomal L36 proteins.","50S ribosomal protein L36","Cytoplasm, Extracellular","This gene has significant similarity to the Haemophilus ducreyi gene HD1759, an orotate phosphoribosyltransferase(7e-17).This gene also has significant similarity to 50S ribosomal L36 proteins: residues 1-114 are 92% similar to HD1955, a 50S ribosomal protein L36 (rpL36).This gene has significant similarity to the Haemophilusinfluenzae Rd gene 1573809, a 50S ribosomal protein L36 (2e-04). Residues 1-37 are 97% similar to this protein.","
InterPro
IPR000473
Family
Ribosomal protein L36
PD002101\"[1-36]TRibosomal_L36
PTHR18804\"[1-37]TRibosomal_L36
PF00444\"[1-37]TRibosomal_L36
TIGR01022\"[1-37]TrpmJ_bact
PS00828\"[11-36]TRIBOSOMAL_L36
noIPR
unintegrated
unintegrated
SSF57840\"[1-37]TSSF57840


","BeTs to 17 clades of COG0257COG name: Ribosomal protein L36Functional Class: JThe phylogenetic pattern of COG0257 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-27) to 1/1 blocks of the IPB000473 family, which is described as \"Ribosomal protein L36\". Interpro entry for IP:IPR000473. IPB000473 1-37 9.7e-28","","","","","","","Fri Feb 27 10:10:42 2004","Fri Feb 27 10:10:42 2004","","","","Fri Feb 27 10:10:42 2004","Fri Feb 27 10:10:42 2004","Fri Feb 27 10:10:42 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01238 is paralogously related to AA02903 (3e-04).","Wed Feb 25 13:12:01 2004","","","","","Residues 1 to 37 (E-value = 7.1e-17) place AA01238 in the Ribosomal_L36 family which is described as Ribosomal protein L36 (PF00444)","","","","","","","","1","","","" "AA01239","844643","844996","354","GTGGCCCGTATTGCAGGCATTAACATTCCTGATCATAAGCACGCTGTAATCGCTTTAACTGCAATTTACGGTATTGGTAAGACCCGCTCAAAAAGCATTTGTGCTGCAGCGGGTATTGCTGAAGATGTTAAGATCAGCGAATTGTCTGAAGAGCAGATTGACAAACTGCGTGACGAAGTTGGTAAATTTACCGTTGAAGGGGATTTACGTCGTGAAGTAACACTTAACATTAAACGCCTATTAGATTTAGGTTGTTATCGTGGTTTACGTCATCGTCGTAGTTTACCGGTACGTGGTCAACGTACTAAAACTAATGCGCGTACCCGTAAGGGTCCTCGTAAGCCGATCAAAAAA","","","13163","VARIAGINIPDHKHAVIALTAIYGIGKTRSKSICAAAGIAEDVKISELSEEQIDKLRDEVGKFTVEGDLRREVTLNIKRLLDLGCYRGLRHRRSLPVRGQRTKTNARTRKGPRKPIKK","844998","From GenBank (gi:1173196): This protein is involved in the binding of Fmet-tRNA and, hence, in the initiation of translation.","30S ribosomal protein S13","Cytoplasm","","
InterPro
IPR001892
Family
Ribosomal protein S13
PD001363\"[57-114]TRS13_RALSO_Q8XV35;
PTHR10871:SF1\"[1-114]T30S RIBOSOMAL PROTEIN S13
PF00416\"[3-108]TRibosomal_S13
PS50159\"[4-111]TRIBOSOMAL_S13_2
PS00646\"[87-100]TRIBOSOMAL_S13_1
InterPro
IPR002198
Family
Short-chain dehydrogenase/reductase SDR
PS00061\"[10-38]?ADH_SHORT
noIPR
unintegrated
unintegrated
G3DSA:1.10.8.50\"[1-71]Tno description
G3DSA:4.10.910.10\"[72-116]Tno description
PTHR10871\"[1-114]T30S/40S RIBOSOMAL PROTEIN


","No hits to the COGs database.","Significant hit ( 3.7e-41) to 2/2 blocks of the IPB001892 family, which is described as \"Ribosomal protein S13\". Interpro entry for IP:IPR001892. IPB001892A 3-26 1.2e-13 IPB001892B 76-108 3.3e-26","Residues 29 to 110 match (7e-07) PD:PD259411 which is described as RIBOSOMAL MITOCHONDRION S13 MITOCHONDRIAL RPS13 ","","","","","","","","","","","Tue Jan 7 13:30:39 2003","Tue Jan 7 13:30:39 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01239 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 108 (E-value = 4.9e-61) place AA01239 in the Ribosomal_S13 family which is described as Ribosomal protein S13/S18 (PF00416)","","","","","Bedwell D, Davis G, Gosink M, Post L, Nomura M, Kestler H, Zengel JM, Lindahl L. Nucleotide sequence of the alpha ribosomal protein operon ofEscherichia coli. Nucleic Acids Res. 13(11): 3891-3903. 1985. PubMed: 2989779.","","Tue Jan 7 13:30:39 2003","1","","","" "AA01240","845015","845401","387","ATGGCAAAAACACCAGTTCGTGCACGTAAACGTGTAAAAAAACAAGTTGTAGATGGCGTTGTACACATTCACGCATCTTTCAATAATACAATCGTTACTATAACTGACCGCCAAGGTAATGCATTAGCTTGGGCTACTGCTGGTGGTTCAGGTTTCCGTGGTTCTCGTAAATCTACCCCGTTCGCTGCACAGGTTGCGGCAGAACGTTGTGCTGAAATTGTAAAAGAATTCGGCTTAAAGAACTTGGAAGTTATGGTAAAAGGACCAGGTCCTGGTCGAGAGTCAACTATTCGTGCATTAAATGCGGCAGGTTTCCGCATTACGAATATTACTGATGTGACTCCGATTCCTCATAACGGTTGTCGTCCACCGAAAAAACGTCGTGTT","","","13911","MAKTPVRARKRVKKQVVDGVVHIHASFNNTIVTITDRQGNALAWATAGGSGFRGSRKSTPFAAQVAAERCAEIVKEFGLKNLEVMVKGPGPGRESTIRALNAAGFRITNITDVTPIPHNGCRPPKKRRV","845403","From GenBank (gi:1173178): s11 plays an essential role for the selection of the correct tRNA in protein biosynthesis. It is located on the large lobe of the small subunit.","30S ribosomal protein S11","Cytoplasm, Extracellular","","
InterPro
IPR001971
Family
Ribosomal protein S11
PD001010\"[20-93]TRS11_PASMU_Q9CL52;
G3DSA:3.30.420.80\"[3-128]Tno description
PTHR11759\"[8-129]T40S RIBOSOMAL PROTEIN S14/30S RIBOSOMAL PROTEIN S11
PF00411\"[19-128]TRibosomal_S11
PS00054\"[97-119]TRIBOSOMAL_S11
noIPR
unintegrated
unintegrated
PTHR11759:SF3\"[8-129]T30S RIBOSOMAL PROTEIN S11


","BeTs to 26 clades of COG0100COG name: Ribosomal protein S11Functional Class: JThe phylogenetic pattern of COG0100 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 3.1e-72) to 2/2 blocks of the IPB001971 family, which is described as \"Ribosomal protein S11\". Interpro entry for IP:IPR001971. IPB001971A 21-67 5.8e-36 IPB001971B 87-128 2.8e-35","Residues 21 to 128 match (5e-09) PD:PD426458 which is described as RIBOSOMAL MITOCHONDRION RPS11 S11 ","","","","","","","","","","","Tue Jan 7 13:34:24 2003","Tue Jan 7 13:34:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01240 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 19 to 128 (E-value = 2.1e-75) place AA01240 in the Ribosomal_S11 family which is described as Ribosomal protein S11 (PF00411)","","","","","Bedwell D, Davis G, Gosink M, Post L, Nomura M, Kestler H, Zengel JM, Lindahl L. Nucleotide sequence of the alpha ribosomal protein operon ofEscherichia coli. Nucleic Acids Res. 13(11): 3891-3903.1985. PubMed: 2989779","","Tue Jan 7 13:34:24 2003","1","","","" "AA01241","845434","846051","618","ATGGCAAGATATTTGGGTCCTAAACTCAAGCTAAGCCGCCGTGAAGGCACTGATTTATTTCTTAAATCAGGTGTTCGTGCGATTGATTCAAAATGTAAAATTGATATCGCGCCTGGTCAACATGGTGCTCGTAAACCGCGTCTGTCTGACTATGGTAGTCAGTTGCGTGAGAAACAAAAAGTTCGCCGTATGTACGGTATTTTGGAACGCCAATTCCGTAATTACTACAAAGAAGCAAACCGCTTAAAGGGTAACACAGGTGAAAATCTATTAGTGTTGCTTGAAGGTCGATTGGATAATATAGTTTATCGTATGGGGTTCGCAGCCACTCGCGCAGAGGCTCGCCAATTGGTAAGTCATAAAGCGATTGTTGTTAATGGTCGTGTGGTAAACATTCCATCTTTCCAGGTTTCAGTTGATGATGTAGTTGCTGTTCGTGAAAAATCTAAGAAACAAGCACGTATTAAAGCATCATTGGAATTGGTAGAACAGAAAGAAAAACCGACATGGTTAGAAGTTGATGCTGCTAAAATGGAAGGTGTATTAAAACGTGTTCCTGAACGTTCTGATTTATCAGCAGACATTAACGAACATCTGATCGTTGAGCTTTATTCTAAA","","","23460","MARYLGPKLKLSRREGTDLFLKSGVRAIDSKCKIDIAPGQHGARKPRLSDYGSQLREKQKVRRMYGILERQFRNYYKEANRLKGNTGENLLVLLEGRLDNIVYRMGFAATRAEARQLVSHKAIVVNGRVVNIPSFQVSVDDVVAVREKSKKQARIKASLELVEQKEKPTWLEVDAAKMEGVLKRVPERSDLSADINEHLIVELYSK","846053","From GenBank (gi:1173260): This protein is one of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. With S5 and S12, it plays an important role in translational accuracy. The interaction surface between S4 and S5 is involved in control of translational fidelity","30S ribosomal protein S4","Cytoplasm","","
InterPro
IPR001912
Family
Ribosomal protein S4
PTHR11831\"[93-141]T30S 40S RIBOSOMAL PROTEIN
PF00163\"[2-95]TRibosomal_S4
PS00632\"[94-118]TRIBOSOMAL_S4
InterPro
IPR002942
Domain
RNA-binding S4
PF01479\"[96-143]TS4
SM00363\"[96-160]TS4
PS50889\"[96-156]TS4
InterPro
IPR005709
Family
Ribosomal protein S4, bacterial and organelle form
TIGR01017\"[3-206]TrpsD_bact: ribosomal protein S4
noIPR
unintegrated
unintegrated
G3DSA:3.10.290.10\"[95-206]Tno description
PTHR11831:SF4\"[93-141]T30S RIBOSOMAL PROTEIN S4P


","No hits to the COGs database.","Significant hit ( 1.8e-35) to 1/1 blocks of the IPB001912 family, which is described as \"Ribosomal protein S4\". Interpro entry for IP:IPR001912. IPB001912 83-137 1.6e-35","Residues 3 to 206 match (2e-98) PD:PD004849 which is described as RIBOSOMAL S4 30S PROTEOME COMPLETE RRNA-BINDING CHLOROPLAST 40S SMALL MITOCHONDRION ","","","","","","","","","","","Tue Jan 7 13:41:44 2003","Tue Jan 7 13:41:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01241 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 96 to 143 (E-value = 6.5e-21) place AA01241 in the S4 family which is described as S4 domain (PF01479)","","","","","Bedwell D, Davis G, Gosink M, Post L, Nomura M, Kestler H, Zengel JM, Lindahl L. Nucleotide sequence of the alpha ribosomal protein operon ofEscherichia coli. Nucleic Acids Res. 13(11): 3891-3903.1985. PubMed: 2989779. Changchien LM, Craven GR.The use of hydroxylamine cleavage to produce a fragment of ribosomal protein S4 which retains the capacity to specifically bind 16S ribosomal RNA.Nucleic Acids Res. 1986 Mar 11;14(5):1957-66.PMID: 3515315 Changchien LM, Schwarzbauer J, Cantrell M, Craven GR.On the role of protein S4 N-terminal residues 1 through 30 in 30S ribosome function.Nucleic Acids Res. 1978 Aug;5(8):2789-99.PMID: 358148","","Tue Jan 7 13:46:35 2003","1","","","" "AA01242","846083","847069","987","ATGCAGGGTGCTGTTACAGAATTTTTAAAGCCGCGCTTAGTTGATATTGAACAAATTAGCTCCACTCAAGCTAAGGTTATCTTGGAGCCATTAGAGCGTGGTTTCGGTCATACTCTAGGAAATGCATTGCGTCGAATTCTTTTATCTTCAATGCCAGGTTGTGCTGTTACTGAAGTAGAGATTGATGGTGTATTGCATGAATATAGTAGTAAAGAGGGTGTACAAGAAGATATTCTGGAAGTACTTTTAAATCTAAAAGGTTTAGCTGTAAAAGTACAGAATAAGGATGATGTTCTTCTTACACTTAGCAAGTCTGGAATTGGCCCTGTTGTTGCTGCAGATATTACCCATGATGGTGATGTTGAAGTTATTAATCCGGAGCATGTAATCTGTCATCTAACCGATGAAAACGCCTCTATTAGTATGCGAATTCGTGTTCGGCGTGGTAGAGGATATGTGCCGGCATCAGTTCGTGCTCAAATTCAGGATGAAGAGCGCCCTATTGGTCGTTTATTAGTAGATGCCTGTTATAGCCCGATTGAGCGTATTGCTTACAATGTTGAAGCGGCACGTGTTGAACAACGTACCGATTTAGACAAATTGGTTATTGAGCTGGAGACAAATGGTACTATTGATCCGGAAGAAGCTATTCGTCGGGCAGCAACAATTTTAGCAGAGCAACTCGATGCATTCGTTGATTTACGTGATGTTCGTCAACCTGAAGTTAAGGAGGAGAAGCCGGAATTTGATCCAATCCTTCTTCGCCCTGTAGATGATTTAGAGTTGACAGTTCGTTCTGCTAACTGTTTGAAAGCAGAAACAATTCACTATATCGGTGATTTAGTTCAACGTACAGAAGTTGAGTTACTTAAAACTCCTAATTTAGGTAAGAAATCGCTTACTGAGATTAAGGATGTACTCGCTTCAAGAGGCTTATCACTAGGTATGCGCCTTGAGAATTGGCCACCAGCAAGTATTGCTGAAGAC","","","36484","MQGAVTEFLKPRLVDIEQISSTQAKVILEPLERGFGHTLGNALRRILLSSMPGCAVTEVEIDGVLHEYSSKEGVQEDILEVLLNLKGLAVKVQNKDDVLLTLSKSGIGPVVAADITHDGDVEVINPEHVICHLTDENASISMRIRVRRGRGYVPASVRAQIQDEERPIGRLLVDACYSPIERIAYNVEAARVEQRTDLDKLVIELETNGTIDPEEAIRRAATILAEQLDAFVDLRDVRQPEVKEEKPEFDPILLRPVDDLELTVRSANCLKAETIHYIGDLVQRTEVELLKTPNLGKKSLTEIKDVLASRGLSLGMRLENWPPASIAED","847071","","DNA-directed RNA polymerase alpha subunit","Cytoplasm","","
InterPro
IPR011260
Domain
RNA polymerase, alpha subunit, C-terminal
PD001179\"[256-329]TRPOA_PASMU_P57941;
PF03118\"[242-309]TRNA_pol_A_CTD
InterPro
IPR011261
Domain
RNA polymerase, dimerisation
PF01193\"[25-233]TRNA_pol_L
InterPro
IPR011262
Domain
RNA polymerase, insert
G3DSA:2.170.120.12\"[53-177]Tno description
PF01000\"[59-178]TRNA_pol_A_bac
InterPro
IPR011263
Domain
RNA polymerase, RpoA/D/Rpb3-type
SM00662\"[23-234]TRPOLD
InterPro
IPR011773
Family
DNA-directed RNA polymerase, alpha subunit
TIGR02027\"[23-317]TrpoA: DNA-directed RNA polymerase, alpha su
noIPR
unintegrated
unintegrated
G3DSA:1.10.150.20\"[246-329]Tno description


","BeTs to 22 clades of COG0202COG name: DNA-directed RNA polymerase alpha subunit/40 kD subunitFunctional Class: KThe phylogenetic pattern of COG0202 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-90) to 5/5 blocks of the IPB001700 family, which is described as \"Bacterial RNA polymerase, alpha chain\". Interpro entry for IP:IPR001700. IPB001700A 23-67 2.9e-32 IPB001700B 131-147 0.0061 IPB001700C 173-187 3.2e-05 IPB001700D 199-231 1.3e-17 IPB001700E 257-299 2.5e-27","Residues 55 to 166 match (2e-07) PD:PD587897 which is described as RNA POLYMERASE ALPHA DNA-DIRECTED CHAIN TRANSCRIPTASE TRANSCRIPTION COMPLETE SUBUNIT TRANSFERASE ","","","","","","","","","","","","Tue Jan 7 13:54:59 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01242 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 242 to 309 (E-value = 8.6e-35) place AA01242 in the RNA_pol_A_CTD family which is described as Bacterial RNA polymerase, alpha chain C terminal domain (PF03118)","","","","","Peck MC, Gaal T, Fisher RF, Gourse RL, Long SR. The RNA polymerase alpha subunit from Sinorhizobium melilotican assemble with RNA polymerase subunits from Escherichia coliand function in basal and activated transcription both in vivoand in vitro. J Bacteriol. 2002 Jul;184(14):3808-14. PMID: 12081950 Olekhnovich IN, Kadner RJ. Mutational scanning and affinity cleavage analysis ofUhpA-binding sites in the Escherichia coli uhpT promoter. J Bacteriol. 2002 May;184(10):2682-91. PMID: 11976297 Bedwell D, Davis G, Gosink M, Post L, Nomura M, Kestler H, Zengel JM, Lindahl L. Nucleotide sequence of the alpha ribosomal protein operon ofEscherichia coli. Nucleic Acids Res. 13(11): 3891-3903.1985. PubMed: 2989779. Lombardo,M.J., Bagga,D. and Miller,C.G. Mutations in rpoA affect expression of anaerobically regulated genes in Salmonella typhimurium J. Bacteriol. 173 (23), 7511-7518 (1991) PubMed: 1938946 ","","Tue Jan 7 13:54:59 2003","1","","","" "AA01243","847114","847500","387","ATGCGCCATCGTAAGAGTGGTCGTCAACTAAACCGTAATAGTAGTCATCGCCAAGCGATGTTCCGTAATATGGCAAGTTCTTTAATTGGTCACGAGATTATTAAAACAACTTTGCCTAAAGCAAAAGAATTACGTCGAGTAGTTGAGCCGTTAATTACTTTAGCAAAAGTAGATAGTGTGGCAAATCGCCGCCTAGCTTTTGCTCGTACACGCAACACAGAAACTGTTGCTAAATTATTTAATGAATTAGGTCCACGTTTTGCACAACGTGCTGGTGGCTACACCCGCATCCTTAAATGTGGTTTCCGTGCTGGCGATAATGCTCCAATGGCTTACATTGAGTTAGTAGATCGTCCAGAAGTTTCAAGTAAAGAAGCTACAGCGGAA","","","14549","MRHRKSGRQLNRNSSHRQAMFRNMASSLIGHEIIKTTLPKAKELRRVVEPLITLAKVDSVANRRLAFARTRNTETVAKLFNELGPRFAQRAGGYTRILKCGFRAGDNAPMAYIELVDRPEVSSKEATAE","847502","","50S ribosomal protein L17","Cytoplasm","","
InterPro
IPR000456
Family
Ribosomal protein L17
PD004277\"[22-111]TQ7VKF9_HAEDU_Q7VKF9;
PTHR14413\"[1-129]TRIBOSOMAL PROTEIN L17
PF01196\"[20-116]TRibosomal_L17
TIGR00059\"[6-117]TL17: ribosomal protein L17
PS01167\"[34-56]TRIBOSOMAL_L17
noIPR
unintegrated
unintegrated
G3DSA:3.90.1030.10\"[1-117]Tno description
PTHR14413:SF3\"[1-129]TRIBOSOMAL PROTEIN L17


","BeTs to 19 clades of COG0203COG name: Ribosomal protein L17Functional Class: JThe phylogenetic pattern of COG0203 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 3e-70) to 2/2 blocks of the IPB000456 family, which is described as \"Ribosomal protein L17\". Interpro entry for IP:IPR000456. IPB000456A 19-62 4.9e-31 IPB000456B 63-116 3.1e-38","Residues 14 to 117 match (1e-46) PD:PD004277 which is described as RIBOSOMAL L17 50S PROTEOME COMPLETE MITOCHONDRIAL BL21 PROTEIN YML8 L26 ","","","","","","","","","","","","Tue Jan 7 14:01:26 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01243 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 20 to 116 (E-value = 5e-66) place AA01243 in the Ribosomal_L17 family which is described as Ribosomal protein L17 (PF01196)","","","","","Peck MC, Gaal T, Fisher RF, Gourse RL, Long SR.The RNA polymerase alpha subunit from Sinorhizobium meliloti can assemble with RNA polymerase subunits from Escherichia coli and function in basal and activated transcription both in vivo and in vitro.J Bacteriol. 2002 Jul;184(14):3808-14.PMID: 120819Arnold,R.J. and Reilly,J.P. Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry Anal. Biochem. 269 (1), 105-112 (1999) PubMed: 10094780Meek DW, Hayward RS.Nucleotide sequence of the rpoA-rplQ DNA of Escherichia coli: a second regulatory binding site for protein S4?Nucleic Acids Res. 1984 Jul 25;12(14):5813-21.PMID: 6379605 ","","Tue Jan 7 14:01:26 2003","1","","","" "AA01244","847887","848153","267","ATGAAAGAGCATATTCATATGCTTCTAAAAATTCCGCCGAAATTATCGGTATCAAGTTTTATGGGGTATTTAAAGGGAAAATCATTTGAAAGGCACGCAAACCTAAAATACAACTATGGTAACCGACATTTTTGGTCGAAAGGCTATTATGTAAGCACGGTAGGGCTAAATACAAAGACAGTGGAGGAGTATATAAGGAATCAGGAAAAGGAAGACATGATTCAGGATAATTTATCGAAGAAAGGATATGTGGACCCCTTTAAGGGG","","","10474","MKEHIHMLLKIPPKLSVSSFMGYLKGKSFERHANLKYNYGNRHFWSKGYYVSTVGLNTKTVEEYIRNQEKEDMIQDNLSKKGYVDPFKG","848153","","transposase","Periplasm, Cytoplasm","This sequence is similar to many transposase sequences, for example see gi|29375219 from [Enterococcus faecalis V583. ","
InterPro
IPR002686
Family
Transposase IS200-like
PF01797\"[1-61]TTransposase_17


","BeTs to 8 clades of COG1943COG name: Predicted transposaseFunctional Class: LThe phylogenetic pattern of COG1943 is -o-p----vd--b-efgh-nuj----Number of proteins in this genome belonging to this COG is","","Residues 8 to 61 match (5e-22) PD:PD588153 which is described as TRANSPOSASE PROTEOME COMPLETE IS200 INSERTION SEQUENCE ELEMENT FOR FROM PLASMID ","","","","","","","","","","","","Wed Feb 25 13:17:10 2004","Wed Feb 25 13:17:10 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA0823, AA0232, AA0807.AA01244 is paralogously related to AA00357 (1e-50), AA01226 (1e-32) and AA02040 (3e-30).","Wed Feb 25 13:17:10 2004","","","","","Residues 1 to 61 (E-value = 4.8e-19) place AA01244 in the Transposase_17 family which is described as Transposase IS200 like (PF01797)","","","","","","","","1","","","" "AA01245","849741","848515","1227","ATGTTATTAAAAAATAAAACCTTCGGCAGCGCCTTAATTATCGCCGGAACCGCCATTGGTGCCGGAATGCTCGCCATGCCGTTAACCTCCGCCGGCATGGGATTCGCCTTTACCGCGGCACTTCTCATCGGACTTTGGTTACTCCTTGCTTACAGTGGACTACTTTTCGTTGAAGTTTATCAAACTGCCAAACGCAAAGATGATGGCGTAGCAACCTTGGCGGAAAAATATTTCGGTATTCCCGGACGTATTATTTCAACACTCTCACTTTTCATTTTGTTATATGCATTATCAGCCGCCTACATGGCCGGTGGTGGTACTTTACTTGCAAACGCCCTGCCGAAAGATTTCTTAGGTTCCGCCGATATTACATTAAAAATTTCTATTTTAATTTTCACCTTTATTTTAGGTGCTTTCGTAGTTATCGGTACCAAGGGCGTAGACAATATCACACGTGTATTATTTTCAGGTAAAATCATCGCCTTTATTCTCGTACTTGCCATAATGTTACCGAAGGTCATCGGCGAGAATTTAACGGCGATGCCTTTGGAATATACCCTCATTCTCTCCGCAGGCCCGATTTTCTTTACCTCATTTGGCTTTCATGTAGTGATGGGCAGCATCAATAATTACCTGGAAGGCGATGTGAAACGTTTCCGTTCCGCCATTATTATCGGCACCGCTATTCCACTCATGGCCTATTTATTGTGGCAACTCGCCACGCACGGCATATTAAGCCAAAATGAATTTGTCGCCGTACTCAAAGATGATCCGACATTAAGCGGCTTGATTAACGCCACTAAAACTCTACGAGACACTACCTTGCTAAGCCAAGTTTTACCGATATTCTACTCATTTGCGCTCATCACCTCATTTTTAGGGGTCGCACTCGGTTTATTTGAAGGGCTAAACGATTTATTCAAACGCACTAAAATGCCGGCAAACCGTGTAAGTTTGACCATCGCGACATTCACTCCGCCGTTAATTTTCGCTTTGTTCTACCCAAACGGGTTCCTCTCTGCACTCAGCTACGCCGGACTATTATGTGCTTTTTATTGCTTAATCCTACCTATTGGTCTGGCATGGCGCACAAGAAAGCAATACCAAGATCTCCCTTACCGCGTTGCCGGCGGAAACCTCATGTTAGTCGTCACATTAATTATCGGCATCATCATTATCATCATCCCATTCCTCACCGAAGCCGGCATCTTGCCGAGGGTTGTTAGC","","","44067","MLLKNKTFGSALIIAGTAIGAGMLAMPLTSAGMGFAFTAALLIGLWLLLAYSGLLFVEVYQTAKRKDDGVATLAEKYFGIPGRIISTLSLFILLYALSAAYMAGGGTLLANALPKDFLGSADITLKISILIFTFILGAFVVIGTKGVDNITRVLFSGKIIAFILVLAIMLPKVIGENLTAMPLEYTLILSAGPIFFTSFGFHVVMGSINNYLEGDVKRFRSAIIIGTAIPLMAYLLWQLATHGILSQNEFVAVLKDDPTLSGLINATKTLRDTTLLSQVLPIFYSFALITSFLGVALGLFEGLNDLFKRTKMPANRVSLTIATFTPPLIFALFYPNGFLSALSYAGLLCAFYCLILPIGLAWRTRKQYQDLPYRVAGGNLMLVVTLIIGIIIIIIPFLTEAGILPRVVS","848517","","tyrosine-specific transport protein 2","Inner membrane, Cytoplasm","","
InterPro
IPR002091
Family
Aromatic amino acid permease
PR00166\"[12-35]T\"[39-58]T\"[85-105]T\"[153-173]T\"[187-209]T\"[226-245]T\"[287-306]T\"[321-339]T\"[342-361]TAROAAPRMEASE
PF03222\"[6-396]TTrp_Tyr_perm
InterPro
IPR013059
Family
Tryptophan/tyrosine transporter
TIGR00837\"[9-389]TaraaP: aromatic amino acid transport protei
InterPro
IPR013061
Family
Tryptophan/tryrosine permease
PS00594\"[19-35]TAROMATIC_AA_PERMEASE_1
noIPR
unintegrated
unintegrated
signalp\"[1-52]?signal-peptide
tmhmm\"[9-29]?\"[35-55]?\"[84-104]?\"[123-143]?\"[153-171]?\"[185-205]?\"[220-240]?\"[279-299]?\"[314-334]?\"[340-360]?\"[375-395]?transmembrane_regions


","BeTs to 8 clades of COG0814COG name: Amino acid permeasesFunctional Class: EThe phylogenetic pattern of COG0814 is ------y-------efgh-nu--i--Number of proteins in this genome belonging to this COG is","Significant hit (7.1e-119) to 6/6 blocks of the IPB002091 family, which is described as \"Aromatic amino acids permease\". Interpro entry for IP:IPR002091. IPB002091A 10-53 2.7e-25 IPB002091B 72-109 6.3e-17 IPB002091C 193-208 1.4e-06 IPB002091D 223-265 1.8e-21 IPB002091E 283-307 2.4e-14 IPB002091F 315-365 6.5e-28Significant hit ( 6e-06) to 2/2 blocks of the IPB002422 family, which is described as \"Permeases for amino acids and related compounds, family II\". Interpro entry for IP:IPR002422. IPB002422A 17-27 0.00028 IPB002422B 293-299 11","Residues 5 to 87 match (1e-11) PD:PD407890 which is described as PROTEOME COMPLETE TYROSINE-SPECIFIC TYROSINE PERMEASE AMINO-ACID INNER MEMBRANE TRANSMEMBRANE TYRP ","","","","","","","","","","","","Tue Jan 7 14:17:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01245 is paralogously related to AA01704 (1e-128), AA02973 (1e-124), AA00468 (7e-62) and AA00092 (8e-10).","","","","","","Residues 6 to 396 (E-value = 1.4e-169) place AA01245 in the Trp_Tyr_perm family which is described as Tryptophan/tyrosine permease family (PF03222)","","","","","Wookey,P.J. and Pittard,A.J. DNA sequence of the gene (tyrP) encoding the tyrosine-specific transport system of Escherichia coli. J. Bacteriol. 170(10): 4946-4949.1988. PubMed: 3049553. Sarsero,J.P., Wookey,P.J., Gollnick,P., Yanofsky,C. and Pittard,A.J. . A new family of integral membrane proteins involved intransport of aromatic amino acids in Escherichia coli. J. Bacteriol. 173(10): 3231-3234.1991 PubMed: 2022620.","","Tue Jan 7 14:18:16 2003","1","","","" "AA01247","850004","849804","201","ATGGACATCACCACGAAAATTTTGATTACCGCACCTTACCTCAACAGAATTACCAAATTATCAACGTGGGATTTCGTAGCTTATGTGATGAAGCGGGAAATTATCTTTATATCGGCGTTGATAACAGAGAATAATAAAATTCACTTTCCATTTAAAAAACGCTCTCAAAAAAGACCGCACTTTATAACAAAATCGGCGCAT","","","7946","MDITTKILITAPYLNRITKLSTWDFVAYVMKREIIFISALITENNKIHFPFKKRSQKRPHFITKSAH","849804","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:18:45 2004","Wed Feb 25 13:18:45 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01247 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 13:18:45 2004","","","","","","","","","","","","","1","","","" "AA01248","850362","849874","489","TTGAGTCCATTTGGGGGACAGAATGGAAAACGCGCAATTTACATGGACGCGTGCAACAAATTCAGAATAAAAGAATTGCCGGTTTGGGCGGGGTATTTCGCGGACAAATCTGGATGCCGCCAAATAAGCCGTTATTTTTTGATCCGATCCACTATTGCCAATATTGCCCACAGGAAAAAAATCTGGCGTGGCGGAGTGCCTTTGCGTCACCGCACGTCGATCTTTCCTTCCGATATTGAAATTTTCGAGCAACAACAAGCCGATATTTTAATTTGCCATGAAGCGCCGAAACCACACCCTTCCGGCTTTGATGTGATCAATCAACTGGCAAAAAAATTAGGTGTAACACAAATCTATCATGGACATCACCACGAAAATTTTGATTACCGCACCTTACCTCAACAGAATTACCAAATTATCAACGTGGGATTTCGTAGCTTATGTGATGAAGCGGGAAATTATCTTTATATCGGCGTTGATAACAGAGAA","9.70","7.72","18786","LSPFGGQNGKRAIYMDACNKFRIKELPVWAGYFADKSGCRQISRYFLIRSTIANIAHRKKIWRGGVPLRHRTSIFPSDIEIFEQQQADILICHEAPKPHPSGFDVINQLAKKLGVTQIYHGHHHENFDYRTLPQQNYQIINVGFRSLCDEAGNYLYIGVDNRE","","","conserved hypothetical protein (possible phosphoesterase)","Cytoplasm","AA01248 has significant similarity to the Haemophilus ducreyi gene HD0277, a probable phosphoesterase (8e-41).AA01248 has significant similarity to the Haemophilus influenzae Rd gene 16272703 (1e-42).","No hits reported.","No hits to the COGs database.","","Residues 58 to 162 match (2e-42) PD:PD114920 which is described as PROTEOME COMPLETE HI0762 PM1388 ","Fri Feb 27 10:32:55 2004","Sat Feb 28 16:53:16 2004","Sat Feb 28 16:53:16 2004","Sat Feb 28 16:53:16 2004","Fri Feb 27 10:32:55 2004","Fri Feb 27 10:32:55 2004","Fri Feb 27 10:32:55 2004","Fri Feb 27 10:32:55 2004","Fri Feb 27 10:32:55 2004","Fri Feb 27 10:32:55 2004","Fri Feb 27 10:32:55 2004","Fri Feb 27 10:32:55 2004","Fri Feb 27 10:32:55 2004","Fri Feb 27 10:32:55 2004","Fri Feb 27 10:32:55 2004","Fri Feb 27 10:32:55 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01248 has no significant similarity (blastp p-value < 1e-03) to any other gene in this genome.AA01248 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Fri Feb 27 10:32:55 2004","Fri Feb 27 10:32:55 2004","No hits to the PDB database.","","","No significant hits to the Pfam 7.7 database.","Fri Feb 27 10:32:55 2004","","","","","","","1","Fri Feb 27 10:32:55 2004","","" "AA01249","850483","850127","357","GTGGCGCTCATCATCCTGGGCGATTTACAACTCACCAATCCCGAACCTTTAGAAAAATTGGCGCAATACGCGGATATTTGGTTTATTCACGGCAATCACGACAGCAAAACCGTAGCAGCATTTGAGTCCATTTGGGGGACAGAATGGAAAACGCGCAATTTACATGGACGCGTGCAACAAATTCAGAATAAAAGAATTGCCGGTTTGGGCGGGGTATTTCGCGGACAAATCTGGATGCCGCCAAATAAGCCGTTATTTTTTGATCCGATCCACTATTGCCAATATTGCCCACAGGAAAAAAATCTGGCGTGGCGGAGTGCCTTTGCGTCACCGCACGTCGATCTTTCCTTCCGATAT","","","13747","VALIILGDLQLTNPEPLEKLAQYADIWFIHGNHDSKTVAAFESIWGTEWKTRNLHGRVQQIQNKRIAGLGGVFRGQIWMPPNKPLFFDPIHYCQYCPQEKNLAWRSAFASPHVDLSFRY","850129","","conserved hypothetical protein (possible phosphoesterase)","Periplasm, Cytoplasm","","No hits reported.","No hits to the COGs database.","","Residues 1 to 112 match (1e-46) PD:PD114920 which is described as PROTEOME COMPLETE HI0762 PM1388 ","","","","","","","","","","","","Tue Jan 7 14:22:19 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01249 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01250","851840","850572","1269","ATGTCAGCATTCCAATATTTACAAGAAAAACGTAAAAAATTGAATCTCAAAGTAAATGATGTTTGCCAAAGAGCGAATATTACCCGTGCTTATTTCAATCAATTAGTCAGCGGAAAAATTAAAAGCCCGAGTGCGACAAAACTGACTGCGCTACATCGTGTGCTACAAATTGATGCGCCGAATAATAAAAAAGTCGGTGTGATTTTCGGTAAATTTTATCCGGTTCACACCGGGCATATTAATATGATCTATGAAGCCTTCAGTAAAGTGGATGAAGTGCATGTGATTGTTTGTAGCGATACGGAACGGGATTTAAAACTGTTTTACGACAGTAAAATGAAGCGTATGCCCACCGTACAAGATCGTTTGCGTTGGATGCAACAGATCTTTAAATATCAGAAAAATCAAATTTTTATCCACCACTTAATCGAGGACGGCTTACCAAATTACCCGAACGGCTGGCAAGCGTGGGCTGAACGGGTTAAAGACTTATTTAAAGAAAAAGGATTTACGCCAAGTATCGTCTTCAGTAGCGAAATTCAAGACAAAGCTCCTTATGAAAAATATCTCAATTTGGACGTATCTTTAGTCGATCCCGAACGCGTATTTTTTAATGTGTCCGCTACAAAAATTCGTAACGAACCATTCCATTATTGGAAGTTTATCCCAAAAGAAGTACGTCCGTTTTTCGCAAAAACCATTGCCATCTTAGGTGGTGAGAGCAGCGGTAAAACCGTATTGGTGAACAAATTGGCAACGGTCTTCAACACCACTTCCGCTTGGGAATACGGGCGCGAATTCGTATTTGAAAAACTGGGCGGTGACGAACAGGCCATGCAATATTCCGATTATCCTCAAATGGCGTTAGGACATCAACGTTACATCGATTATGCTGTGCGACACGCCCACAAAGTCGCCATTATTGATACGGATTTCATCACCACACAGGCATTTTGTATTCAATACGAAGGCAAAGCACACCCGTTTTTGGATTCCATGATTAAAGAATATCCTTTTGATGTCACCATTTTGTTAAACAATAACACGCAATGGGTTGATGACGGTTTGCGTAGCCTGGGCAATCAAAAACAGCGACAACGTTTCCAACAGTTACTCAAAAAATTGTTAGATAAATACAATGTCCCATACATTGAAATTGAATCGCCAAGTTATTTGGAGCGCTATAATCGGGTAAAAGAAATTGTGGAAAAAATCCTCAATGAAGAAGAACTGCCTGAATTAAGCAGCGATCACGGCAATTCTATTTTT","","","49474","MSAFQYLQEKRKKLNLKVNDVCQRANITRAYFNQLVSGKIKSPSATKLTALHRVLQIDAPNNKKVGVIFGKFYPVHTGHINMIYEAFSKVDEVHVIVCSDTERDLKLFYDSKMKRMPTVQDRLRWMQQIFKYQKNQIFIHHLIEDGLPNYPNGWQAWAERVKDLFKEKGFTPSIVFSSEIQDKAPYEKYLNLDVSLVDPERVFFNVSATKIRNEPFHYWKFIPKEVRPFFAKTIAILGGESSGKTVLVNKLATVFNTTSAWEYGREFVFEKLGGDEQAMQYSDYPQMALGHQRYIDYAVRHAHKVAIIDTDFITTQAFCIQYEGKAHPFLDSMIKEYPFDVTILLNNNTQWVDDGLRSLGNQKQRQRFQQLLKKLLDKYNVPYIEIESPSYLERYNRVKEIVEKILNEEELPELSSDHGNSIF","850574","","nadAB transcriptional regulator","Cytoplasm","","
InterPro
IPR001387
Domain
Helix-turn-helix type 3
PF01381\"[7-62]THTH_3
SM00530\"[6-62]THTH_XRE
PS50943\"[7-62]THTH_CROC1
InterPro
IPR004821
Domain
Cytidyltransferase-related
TIGR00125\"[65-136]Tcyt_tran_rel: cytidyltransferase-related do
InterPro
IPR006417
Domain
Nicotinamide-nucleotide adenylyltransferase
TIGR01526\"[63-395]TnadR_NMN_Atrans: nicotinamide-nucleotide ad
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620\"[62-230]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[231-399]Tno description


","BeTs to 3 clades of COG3172COG name: Predicted ATPase/kinase involved in NAD metabolismFunctional Class: HThe phylogenetic pattern of COG3172 is ----------rl--ef-h--------Number of proteins in this genome belonging to this COG is","","Residues 66 to 230 match (1e-11) PD:PD448851 which is described as REGULATOR PROTEOME COMPLETE TRANSCRIPTIONAL ","","","","","","","","","","","","Tue Jan 7 14:24:08 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01250 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 62 (E-value = 4.7e-06) place AA01250 in the HTH_3 family which is described as Helix-turn-helix (PF01381)","","","","","Singh SK, Kurnasov OV, Chen B, Robinson H, Grishin NV,Osterman AL, Zhang H. Crystal structure of Haemophilus influenzae NadR protein. Abifunctional enzyme endowed with NMN adenyltransferase andribosylnicotinimide kinase activities. J Biol Chem. 2002 Sep 6;277(36):33291-9. PMID: 12068016 Mushegian A. The Purloined Letter: bacterial orthologs of archaeal NMNadenylyltransferase are domains within multifunctionaltranscription regulator NadR. J Mol Microbiol Biotechnol. 1999 Aug;1(1):127-8. PMID: 10941793 Raffaelli N, Lorenzi T, Mariani PL, Emanuelli M, Amici A,Ruggieri S, Magni G. The Escherichia coli NadR regulator is endowed withnicotinamide mononucleotide adenylyltransferase activity. J Bacteriol. 1999 Sep;181(17):5509-11. PMID: 10464228 ","","Tue Jan 7 14:24:08 2003","1","","","" "AA01251","852054","851965","90","GTGGAAGCCAAAATTAAACAGGTTTTACAAACCAATTATCCAAACCGGATATTGCATCCCGCGAAGAATTTGATTTACAAACACAAGTGT","","","3543","VEAKIKQVLQTNYPNRILHPAKNLIYKHKC","851965","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:20:15 2004","Wed Feb 25 13:20:15 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01251 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 13:20:15 2004","","","","","","","","","","","","","1","","","" "AA01252","852342","852163","180","ATGTTAATACGCAAACAAATTCGCCATTTACAAGAAGGCGATGTACTTTTGATGCTGGCGGATGATCCCGCAACTACCCGTGATATTCCGAGTTTCTGCCAATTTATGGATCATACTTTGCTACATAGCGAAACAACTCAGATCCCCTATCGTTACTGGGTTAAAAAAGGGAAATCAGTT","","","9382","MLIRKQIRHLQEGDVLLMLADDPATTRDIPSFCQFMDHTLLHSETTQIPYRYWVKKGKSV","852165","","conserved hypothetical protein (probable SirA homolog)","Cytoplasm","","
InterPro
IPR001455
Family
SirA-like
PF01206\"[1-56]TSirA
noIPR
unintegrated
unintegrated
G3DSA:3.30.110.40\"[1-58]Tno description


","No hits to the COGs database.","","Residues 1 to 55 match (3e-15) PD:PD488602 which is described as PROTEOME COMPLETE SIRA HOMOLOG REGULATORY GROWTH BMEI0037 NORMAL REQUIRED RSC0810 ","","","","","","","","","","","","Thu Feb 20 08:36:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01252 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 56 (E-value = 6.2e-14) place AA01252 in the UPF0033 family which is described as Uncharacterized protein family UPF0033 (PF01206)","","","","","Lawhon SD, Maurer R, Suyemoto M, Altier C.Intestinal short-chain fatty acids alter Salmonella typhimurium invasion gene expression and virulence through BarA/SirA.Mol Microbiol. 2002 Dec;46(5):1451-64.PMID: 12453229Goodier RI, Ahmer BM.SirA orthologs affect both motility and virulence.J Bacteriol. 2001 Apr;183(7):2249-58.PMID: 11244064Ahmer BM, van Reeuwijk J, Watson PR, Wallis TS, Heffron F.Salmonella SirA is a global regulator of genes mediating enteropathogenesis.Mol Microbiol. 1999 Feb;31(3):971-82.PMID: 1004803","","Tue Jan 7 14:33:55 2003","1","","","" "AA01253","852329","852445","117","TTGCGTATTAACATGACCGGTTCGGGACAACGCAGACCAACGGTATCAAGTGTTTGGGTGATTTTTATATTATCCATTTTTGTTATTTATTACGAAAAATTACGGGGTATAATACAA","","","4538","LRINMTGSGQRRPTVSSVWVIFILSIFVIYYEKLRGIIQ","852445","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-31]?signal-peptide
tmhmm\"[15-30]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:21:56 2004","Wed Feb 25 13:21:56 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01253 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 13:21:56 2004","","","","","","","","","","","","","1","","","" "AA01254","852493","852762","270","ATGATTGAATATCAAATTCCTAAAAGTGCGGTGGATTTTAGCGAAGGAATTAAAAAGAACTATTTTGCTACGGTCGCCGGTCAACTCAACGATTCGCATCAATTCGGTTTTTCTGATGACGGCAAACCGAGCGGCACGGCGGGTAAGCCGATGTTAGCCGCGCTGCAAGGCAGTGGTGTGGGCGAAATCAGTGCCGTGGTGGTGCGCTATTATGGCGGTGTTTTGTTGGGTACAGGCGGATCGGTACGCGCTTATAGCGGTGGCGTTCAA","","","13689","MIEYQIPKSAVDFSEGIKKNYFATVAGQLNDSHQFGFSDDGKPSGTAGKPMLAALQGSGVGEISAVVVRYYGGVLLGTGGSVRAYSGGVQ","852764","","conserved hypothetical protein (possible proline dipeptidase)","Extracellular, Cytoplasm","","
InterPro
IPR001498
Domain
Protein of unknown function UPF0029, N-terminal
PF01205\"[6-90]TUPF0029
PS00910\"[48-77]TUPF0029
noIPR
unintegrated
unintegrated
G3DSA:3.30.230.30\"[3-90]Tno description


","BeTs to 13 clades of COG1739COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG1739 is -o----y-vd-lb-efgh-nu---twNumber of proteins in this genome belonging to this COG is","Significant hit ( 8.4e-25) to 1/2 blocks of the IPB001498 family, which is described as \"Uncharacterized protein family UPF0029\". Interpro entry for IP:IPR001498. IPB001498B 47-89 7.3e-25","Residues 22 to 90 match (1e-13) PD:PD006754 which is described as PROTEOME COMPLETE PROLINE FAMILY PEPQ DIPEPTIDASE YIGZ YVYE UNCHARACTERIZED PM1497 ","","","","","","","","","","","","Tue Jan 7 14:57:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01254 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 6 to 90 (E-value = 7.6e-16) place AA01254 in the UPF0029 family which is described as Uncharacterized protein family UPF0029 (PF01205)","","","","","","","","1","","","" "AA01255","852796","852933","138","GTGGCGTATTTACATTACGCCGTGTGCTGTGATTACACCCAAATTAATGAGTTACAAACGCTGTGCGAACAATGTGCTATTTTGATCCAAGCACAGGGCTTTCAGGGTGGATATTACTTTGCGTTTGGCAATTCGACC","","","5142","VAYLHYAVCCDYTQINELQTLCEQCAILIQAQGFQGGYYFAFGNST","852933","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:24:53 2004","Wed Feb 25 13:24:53 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01255 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 13:24:53 2004","","","","","","","","","","","","","1","","","" "AA01256","852914","853009","96","TTGCGTTTGGCAATTCGACCTGATAAATTAGCGCGTTTCCAACAAGCATTGACGGAACGCTCTGCCGGGCAACTGGTTTTAAACGAAATTAAAAAT","","","3645","LRLAIRPDKLARFQQALTERSAGQLVLNEIKN","853009","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:23:24 2004","Wed Feb 25 13:23:24 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01256 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 13:23:24 2004","","","","","","","","","","","","","1","","","" "AA01258","853031","854491","1461","GTGCATTTTTTATCCATCTTACGCATCGTCGGCATTTTAGTGATGTGCTTTTCCTGTACCATGCTGCTGCCGGCATTTGTTGCATTATTATATGGCGACGGTGGTGGTAAAGCTTTCAGCCAATCCTTTGTAATGAGCGCCATTGCCGGCGTAATCCTATGGTGGGCTTGTCATCACCATAAGGAAGAATTGCGCTCGCGAGAAGGATTTCTGATTGTTGTTGCCTTTTGGGTGGTTATGGGGAGCCTTGGGGCAATTCCTTTTATGTTATTTGAGGACCCCTATTTAACCGTTTCTTCCGCATTTTTTGAATCCTTCTCCGGTTTAACTACGACAGGCGCGACCACTATTGTCGGTTTAGACAACTTGCCAAAAGCGATTTTATTTTATCGCCAGTTATTGCAATGGCTCGGCGGCATGGGGATCATCGTGTTAGCAGTGGCGATCATCCCATTGTTTGGGATCGGTGGAATGTCGCTTTACCGAGCGGAAATTTCCGGTCCGTTAAAAGAGAATAAAATGCGCCCGCGTATCACCGAAACCGCTAAGACATTATGGATCATTTATGCTTCATTAACCCTGCTTTGCGCTTTTTCTTATTGGCTTGCGGGAATGTCGCCTTTTGATGCCATTAGCCATAGTTTTTCCACCGTGTCTATCGGCGGTTTTTCCACTCACGATAGAAGTATGGCGTATTTTGCCAGTTCGACGGTTAATATCATCACTATTGTCTTTTTATTGATTTCCGCCTGTAACTACGTGTTGCATTTCAATGCTTTTTCGCAATTAGGTAAACGAAATATTTTCCTTAGCTATTTTCGCGATCCGGAATTTCGCTTCTTTATGCTGATTCAGTTTTCTTTAGTATTGATTTGCTTTGCCATGTTATTGGCAAATCATCATTTTGATGAAACCTTCCAAAACCTTGAACAAGCGCTATTTCAATCAGTTTCCATTTCAACTACGGCGGGCTACACTACCTCCAGTTTTGAACAATGGCCACTATTCTTGCCGATCCTCCTGTTATTTGCTTCTTGTATAGGCGGCTGTGCAGGATCCACTGGTGGCGGTCTCAAAGTGGTGCGTGTTTTGGTGCTTTATTTACAGGCTAAACGTGAACTCAAACGGCTAATCCATCCCAATTTAGTGTACCCGATTAAATTAGGCAAAAGGGTGTTGGACGAACGGGTTATACAAAGTATTTGGGCTTTTTTTTCCGCCTATTTACTGGTTTTTGTAATTTGTCTGCTGGGGGTCATTAGTTGTGGCGTAGAAACTTTTGATGCCTTTAATGCCGTTATTGCCTGCTTAAATAATGTCGGACCGGCACTGGGGACGGTTAGCAGCAATTTTGTTGGCATCCCTGATAGCGCAAAATGGATCCTGACCTTAGCCATGGTTTGCGGTCGTTTGGAAATTTTCTCCTTATTGGTATTATTCACTCCTGCATTTTGGAAATCC","","","53825","VHFLSILRIVGILVMCFSCTMLLPAFVALLYGDGGGKAFSQSFVMSAIAGVILWWACHHHKEELRSREGFLIVVAFWVVMGSLGAIPFMLFEDPYLTVSSAFFESFSGLTTTGATTIVGLDNLPKAILFYRQLLQWLGGMGIIVLAVAIIPLFGIGGMSLYRAEISGPLKENKMRPRITETAKTLWIIYASLTLLCAFSYWLAGMSPFDAISHSFSTVSIGGFSTHDRSMAYFASSTVNIITIVFLLISACNYVLHFNAFSQLGKRNIFLSYFRDPEFRFFMLIQFSLVLICFAMLLANHHFDETFQNLEQALFQSVSISTTAGYTTSSFEQWPLFLPILLLFASCIGGCAGSTGGGLKVVRVLVLYLQAKRELKRLIHPNLVYPIKLGKRVLDERVIQSIWAFFSAYLLVFVICLLGVISCGVETFDAFNAVIACLNNVGPALGTVSSNFVGIPDSAKWILTLAMVCGRLEIFSLLVLFTPAFWKS","854493","","TRK system potassium uptake protein","Inner membrane, Cytoplasm","","
InterPro
IPR003445
Family
Cation transporter
PF02386\"[152-485]TTrkH
InterPro
IPR004772
Family
K+ transporter Trk
TIGR00933\"[83-470]T2a38: potassium uptake protein, TrkH family
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide
tmhmm\"[10-30]?\"[36-56]?\"[71-91]?\"[133-153]?\"[185-203]?\"[237-257]?\"[278-298]?\"[334-368]?\"[401-421]?\"[460-480]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 2.1e-05) to 1/2 blocks of the IPB003445 family, which is described as \"Cation transport protein\". Interpro entry for IP:IPR003445. IPB003445B 102-115 2.2e-05","Residues 423 to 486 match (8e-14) PD:PD150215 which is described as POTASSIUM COMPLETE PROTEOME UPTAKE TRKH SYSTEM TRK TRANSMEMBRANE INNER MEMBRANE ","","","","","","","","","","","","Tue Jan 7 16:06:27 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01258 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 152 to 485 (E-value = 2.4e-90) place AA01258 in the TrkH family which is described as Cation transport protein (PF02386)","","","","","Nakamura T, Yamamuro N, Stumpe S, Unemoto T, Bakker EP.Cloning of the trkAH gene cluster and characterization of the Trk K(+)-uptake system of Vibrio alginolyticus.Microbiology. 1998 Aug;144 ( Pt 8):2281-9.PMID: 9720051Schlosser A, Meldorf M, Stumpe S, Bakker EP, Epstein W.TrkH and its homolog, TrkG, determine the specificity and kinetics of cation transport by the Trk system of Escherichia coli.J Bacteriol. 1995 Apr;177(7):1908-10.PMID: 7896723","","Tue Jan 7 16:06:27 2003","1","","","" "AA01259","854494","855003","510","ATGAAAACACTTATTTTATATTCAACTCATGATGGACAGACCAAGAAAATAGCCGACTATATTGCCGAACTAATCACCACCAATGTGGAGGTGAAATCGATTAACGCAGAAGTGAATTTTGCCGATTACGAGCGCATTATTATCGGAGCTTCGATCCGCTACGGACATTTCAATAAACAGCTTTATAAAACGCTGGAAAAACACACCGCACTTTTGAATCAAAAGACCACCGCCTTTTTTGGCGTGAACCTGACGGCGCGAAAAGCCGACAAGGCAACGCCTGAAACGAATGTTTATGTGCGTAAATTTTTGCAACGTATCACTTGGCAACCGACGATCTCCGCGGTGTTTGCCGGTGCATTGCTTTATCCGCGCTATGGTTTCTTCGATCGCATGATGATCCAACTTATTATGCGTATCACAGGCGGAGAAACGGATCTTACAAAAGAAATCGAATATACGGATTGGCAAAAAGTGCGGTCGTTTTCAGAAGCGTTTTTGCAGTTGAAA","","","22852","MKTLILYSTHDGQTKKIADYIAELITTNVEVKSINAEVNFADYERIIIGASIRYGHFNKQLYKTLEKHTALLNQKTTAFFGVNLTARKADKATPETNVYVRKFLQRITWQPTISAVFAGALLYPRYGFFDRMMIQLIMRITGGETDLTKEIEYTDWQKVRSFSEAFLQLK","855005","","protoporphyrinogen oxidase","Cytoplasm","","
InterPro
IPR001226
Domain
Flavodoxin, N-terminal
PS00201\"[5-21]TFLAVODOXIN
InterPro
IPR008254
Domain
Flavodoxin/nitric oxide synthase
PS50902\"[3-167]TFLAVODOXIN_LIKE


","BeTs to 3 clades of COG0716COG name: FlavodoxinsFunctional Class: CThe phylogenetic pattern of COG0716 is a-m---y----lbcefghs-uj--t-Number of proteins in this genome belonging to this COG is","","Residues 1 to 170 match (8e-57) PD:PD102179 which is described as COMPLETE PROTEOME PROTOPORPHYRINOGEN OXIDASE OXIDOREDUCTASE PPO PORPHYRIN BIOSYNTHESIS PM1499 ","","","","","Sat Jan 25 14:34:20 2003","","","","","","","Tue Jan 7 16:20:18 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01259 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Kusaba A, Ansai T, Akifusa S, Nakahigashi K, Taketani S, Inokuchi H, Takehara T.Cloning and expression of a Porphyromonas gingivalis gene for protoporphyrinogen oxidase by complementation of a hemG mutant of Escherichia coli.Oral Microbiol Immunol. 2002 Oct;17(5):290-5.PMID: 12354210 [PubMed - in process]Narita S, Taketani S, Inokuchi H.Oxidation of protoporphyrinogen IX in Escherichia coli is mediated by the aerobic coproporphyrinogen oxidase.Mol Gen Genet. 1999 Jul;261(6):1012-20.PMID: 10485293 Xu K, Delling J, Elliott T.The genes required for heme synthesis in Salmonella typhimurium include those encoding alternative functions for aerobic and anaerobic coproporphyrinogen oxidation.J Bacteriol. 1992 Jun;174(12):3953-63.PMID: 1317844","","Sat Jan 25 14:09:23 2003","1","","","" "AA01260","855818","855690","129","ATGCTATTAACACACCAACCTTCCTCAATACCGAAAGAACTTTACAACCCGAAGGCCTTATTCATTCACGCGGCATGGCTGCGTTCAGGGTTGCCCCCATTGCGCAATATTCCCCACTNCTGCCTCCCG","","","4754","MLLTHQPSSIPKELYNPKALFIHAAWLRSGLPPLRNIPHXCLP","855690","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:26:30 2004","Wed Feb 25 13:26:30 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01260 is paralogously related to AA02422 (3e-13), AA02298 (3e-13), AA00622 (3e-13) and AA00413 (3e-13).","Wed Feb 25 13:26:30 2004","","","","","","","","","","","","","1","","","" "AA01261","856583","856783","201","ATGGCGTATACAGAGGGTAACCAACCAGCGATGGGGAGTGAATCTCAGAAAGTGCGTCTAAGTTCGGATTGGAGTCTGCAACTCGACTCCATGAAGTCGGAATCGCTAGTAATCGCGAATCAGAATGTTGCGGTGAATACGTTCCCGGGCCTTGTACACACCGCCCGTCACACCATGGGAGTGGGTTGTACCAGAAGTGGA","","","7166","MAYTEGNQPAMGSESQKVRLSSDWSLQLDSMKSESLVIANQNVAVNTFPGLVHTARHTMGVGCTRSG","856783","","conserved hypothetical protein","Periplasm","This sequence is similar to gi|27359373, a conserved hypothetical from V. vulnificus. See also gi|23015882 from Magnetospirillum magnetotacticum.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:30:00 2004","Wed Feb 25 13:30:00 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01261 is paralogously related to AA02297 (7e-35), AA01566 (7e-35), AA00621 (7e-35), AA00412 (7e-35) and AA02421 (2e-27).","Wed Feb 25 13:30:00 2004","","","","","","","","","","","","","1","","","" "AA01262","860147","859716","432","ATGCTTTCAGCACTTATCTCTCCCGCACTTAGCTACCCGGCTATGCGTCTGGCGACACAACCGGAACACCAGCGGTGCGTCCACTCCGGTCCTCTCGTACTAGGAGCAGCCCCAACCAATTCTCCTACGCCCACGGCAGATAGGGACCGAACTGTCTCACGACGTTCTAAACCCAGCTCGCGTACCACTTTAAATGGCGAACAGCCATACCCTTGGGACCTACTTCAGCCCCAGGATGTGATGAGCCGACATCGAGGTGCCAAACACCGCCGTCGATATGAACTCTTGGGCGGTATCAGCCTGTTATCCCCGGAGTACCTTTTATCCGTTGAGCGATGGCCCTTCCATGCAGAACCACCGGATCACTATGACCTACTTTCGTACCTGCCCGACCTGTCCGTCTCGCAGTTAAGCTTGCTTATACCATTGCAC","","","16179","MLSALISPALSYPAMRLATQPEHQRCVHSGPLVLGAAPTNSPTPTADRDRTVSRRSKPSSRTTLNGEQPYPWDLLQPQDVMSRHRGAKHRRRYELLGGISLLSPEYLLSVERWPFHAEPPDHYDLLSYLPDLSVSQLSLLIPLH","859716","","hydrolase","Periplasm","This sequence is similar to gi|27363940, a predicted cell wall-associated hydrolase from Vibrio vulnificus. See also gi|29337301 from C.muridarum.","
noIPR
unintegrated
unintegrated
PD293281\"[1-104]TQ8CME1_BBBBB_Q8CME1;


","No hits to the COGs database.","","Residues 1 to 122 match (1e-33) PD:PD293281 which is described as PROTEOME COMPLETE TC0114 ","","","","","","","","","","","","Wed Feb 25 13:33:51 2004","Wed Feb 25 13:33:51 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA1579, AA1489, AA0832, AA0404, AA0273, AA1024.AA01262 is paralogously related to AA02296 (8e-83), AA00620 (8e-83), AA00411 (1e-61) and AA01567 (3e-33).","Wed Feb 25 13:33:51 2004","","","","","","","","","","","","","1","","","" "AA01263","860922","861146","225","TTGTTTAATTTCCTTTCCTTAGTTCATATCGGCGTAACGGAAAACGGCGTTATCCAAGGCATGCAGCCTTTCGCCACTGTCTTTTTCGGAATGGCATTTATGCACTTCCGAATGAATCTTTGGCGATGTATTGCATTTATTGTTTCAGCCATATGTATTTATGCCATGAGTGTGGGTCCCATACCGTTGTTGAAGGAGGTGAAGTATGGCTTGGTTACTTATATG","","","8479","LFNFLSLVHIGVTENGVIQGMQPFATVFFGMAFMHFRMNLWRCIAFIVSAICIYAMSVGPIPLLKEVKYGLVTYM","861146","","hypothetical protein","Inner membrane, Extracellular","","
noIPR
unintegrated
unintegrated
signalp\"[1-50]?signal-peptide
tmhmm\"[44-64]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Tue Jan 7 16:23:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01263 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01264","862116","862003","114","ATGGATACCATCAAAGCACAACATTTTTCACCCGCAGTATATCAAACGACCACAATTATTAACGCCGATGATGCGATCTTCGTTCGGCACGTCTTCTTTTGTAAAAAGCAGTGC","","","4371","MDTIKAQHFSPAVYQTTTIINADDAIFVRHVFFCKKQC","862003","","conserved hypothetical protein","Cytoplasm, Periplasm","This sequence is very weakly similar to gi|16272020, a hypothetical from H.influenzae.","No hits reported.","BeTs to 3 clades of COG3054COG name: Predicted transcriptional regulatorFunctional Class: RThe phylogenetic pattern of COG3054 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Wed Feb 25 13:36:21 2004","Wed Feb 25 13:36:21 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01264 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 13:36:21 2004","","","","","","","","","","","","","1","","","" "AA01265","862232","862119","114","TTGAACGGGAACGAAATTAGCTATAAAAGCTGGCAATCGCCTGATCTGACAGGAAAAGTCCGAGTGATCCAACATTTAGCCAGCAGAAGTAGTGTTAAAGAAAAAATGAAGCGT","","","4354","LNGNEISYKSWQSPDLTGKVRVIQHLASRSSVKEKMKR","862119","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database. A very weak similarity might be noted to gi|16132038 from E.coli.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:39:03 2004","Wed Feb 25 13:39:03 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01265 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 13:39:03 2004","","","","","","","","","","","","","1","","","" "AA01266","862311","862216","96","ATGAAAAAAATAGCATTAGCTCTAGGATTAACCTTTCTAAGCATTCTCCGTTACCGTGCAAAAAGATGGCGAATTAATTTTGAACGGGAACGAAAT","","","3947","MKKIALALGLTFLSILRYRAKRWRINFERERN","862216","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-20]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:41:06 2004","Wed Feb 25 13:41:06 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01266 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 13:41:06 2004","","","","","","","","","","","","","1","","","" "AA01267","862407","862670","264","ATGTCTTACTCTTACCAATTTCGTTTAAAAACTATCAAACAGGTCACCGAGCAGGATTTTGGTATCCGTGAGGTGGCGAAACTTCATAAAATCTCCCATTCGCTCGTCATTTATTGGCTAAAAGCATTTCGTGAAAGAGGGCTTAATGGCGTAAAATCCCCTTATATAAACCCTCAACGCCCTAAAATAGTGAAGCCAAAGATGAAAAAGAAAGCGATTGAAATCCCGGAACAAACTACGTCAAATGGGTTTCCATTTGAATCA","","","10650","MSYSYQFRLKTIKQVTEQDFGIREVAKLHKISHSLVIYWLKAFRERGLNGVKSPYINPQRPKIVKPKMKKKAIEIPEQTTSNGFPFES","862670","See BLAST summary in AA01268.","degenerate transposase fragment","Periplasm, Cytoplasm","","No hits reported.","BeTs to 4 clades of COG2963COG name: TransposaseFunctional Class: LThe phylogenetic pattern of COG2963 is ---p-----drlb-efgh---j----Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","Fri Jan 7 17:24:30 2005","Wed Jan 8 18:56:28 2003","","Fri Jan 7 17:22:44 2005","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01267 is paralogously related to AA00535 (1e-28), AA02340 (2e-18), AA02115 (2e-18), AA01289 (2e-18), AA01075 (2e-18), AA00008 (2e-18), AA01445 (6e-16) and AA01549 (2e-07).","Fri Jan 7 17:22:44 2005","","","","","","","","","","","","","1","","","" "AA01268","862663","863277","615","TTGAATCATAAAACGGTGTTAAAACTGATGAATGCGTTAGGTATTCATTCTATTTTACGCAAGAAAAGACATGGAAAACGAGGCAAAACATCGCATATTGCCCCGAATGTGCTAAATCGTGATTTTACAGCGACGGCGCTCAATCAAAAATGGGTAACCGATGTCACTGAGTTTCGAGTTGGGGAAGAAAAGCTCTATTTTTCACCGTTGATGGATTTAGCGAACCGGGAAATTATTGCCTATAATTTTGCGAAACGCCCTAAGTTCTCATTGGTAAAAAGAATGCCGGAAGAAGGACTTGGCAAACTAAAACCGAGCGAATGCCCGATTATTCACAGCGACCAAGGGGTATTGTACGGCTCAGCAGAATGGGTAAAGATGTTGGAAGGCAAGGCGATACAAAGTATGAGTCGCCGAGGGAATTGCTATGATAATGCGGTGATTGAAAGCTTTTTTGCGATATTAAAATCTGAGTGTTTTTACTCACGCACTTATACTTCGATTGCCGAATTACAGGCGGAAATTGAAGAATATTTGGTGTATTACAACCAAGAACGAATTAAACTTGATTTAAAAGGATTAAGCCCGGTGCAATACCGAGCTCAATATTTAAGT","","","23599","LNHKTVLKLMNALGIHSILRKKRHGKRGKTSHIAPNVLNRDFTATALNQKWVTDVTEFRVGEEKLYFSPLMDLANREIIAYNFAKRPKFSLVKRMPEEGLGKLKPSECPIIHSDQGVLYGSAEWVKMLEGKAIQSMSRRGNCYDNAVIESFFAILKSECFYSRTYTSIAELQAEIEEYLVYYNQERIKLDLKGLSPVQYRAQYLS","863277","","transposase","Cytoplasm","Several matches to transposase sequences, for example see gi|28872132 from Pseudomonas syringae.","
InterPro
IPR001584
Domain
Integrase, catalytic core
PF00665\"[43-201]Trve
PS50994\"[31-204]TINTEGRASE


","No hits to the COGs database.","","Residues 4 to 89 match (5e-07) PD:PD006527 which is described as TRANSPOSASE PROTEOME COMPLETE PLASMID TRANSPOSASE-LIKE IS1077A IS1077B IS1077C IS1077D IS1077E ","","","","","","","","","","","","Wed Feb 25 13:44:52 2004","Wed Feb 25 13:44:52 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA0945, AA0835, AA1522, AA0845, AA0709, AA0006, AA1371, AA1578.AA01268 is paralogously related to AA01444 (1e-117), AA02342 (1e-95), AA01287 (1e-95), AA01077 (1e-95), AA00010 (1e-95), AA02117 (3e-89), AA02420 (3e-25), AA00145 (3e-23), AA02341 (1e-11), AA02116 (1e-11), AA01288 (1e-11), AA01076 (1e-11) and AA00009 (1e-11).","Wed Feb 25 13:44:52 2004","","","","","Residues 43 to 201 (E-value = 5.6e-31) place AA01268 in the rve family which is described as Integrase core domain (PF00665)","","","","","","","","1","","","" "AA01269","863473","863312","162","TTGCACACTTCTGCCAAAAAGCGTTCCATTTCCGCGTCGTTGCTGAAAATCTTGCGGTATAAATGGCGCGGGTTCCAATCTACCAGCACGCCGCCCAAATCAAAAACGACGGTCGATATGTTGGGTTTTGGTCATGTTTTCCTCCAATGGATGATGGAAAAG","","","6238","LHTSAKKRSISASLLKILRYKWRGFQSTSTPPKSKTTVDMLGFGHVFLQWMMEK","863312","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:46:45 2004","Wed Feb 25 13:46:45 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01269 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 13:46:45 2004","","","","","","","","","","","","","1","","","" "AA01270","863457","863957","501","TTGGCAGAAGTGTGCAACAGCGAATGGAATGCGCGACAAGATGCCGGGCGCTCCTGGTCGGAAGGCGTTGCCGAAGCCGTCAAACAACATCCACAGTATGAAGCGGAAATCCGCGCCTATCATGAACGCTGGACGGAAACCCTAAACGGTGCCATTGACGACACCGTCGCCCTGCTGGAGCCCCTCAAACGCAGTGGCGTCCGCTTGTTGGCGCTGACCAACTGGTCCAACGAAACCTTCCATTTCGCCGAAGAACGCTTCCCTTTCTTAACCGAATTCGAGGGCATTTTAGTCTCCGGCTACGAACGCCTGGCAAAACCCGACCCACGCATTTTCAATCTGTTAATCGAACGCTACCACCTAAACCCGCAACACACCGTCTTCATCGACGACAACCTGCGCAATGTAGAAGGCGCCCGCAACGTCGGCTTACACACCTTACAATTCACCCATGCCCAAAAACTAAAACAGGATTTAATCACCTTGGGCGTGAAATTTGAT","","","22502","LAEVCNSEWNARQDAGRSWSEGVAEAVKQHPQYEAEIRAYHERWTETLNGAIDDTVALLEPLKRSGVRLLALTNWSNETFHFAEERFPFLTEFEGILVSGYERLAKPDPRIFNLLIERYHLNPQHTVFIDDNLRNVEGARNVGLHTLQFTHAQKLKQDLITLGVKFD","863957","","hydrolase (possible 2-haloalkanoic acid dehalogenase I)","Cytoplasm","","
InterPro
IPR005833
Family
Haloacid dehydrogenase/epoxide hydrolase
PR00413\"[62-75]T\"[93-109]T\"[111-131]T\"[138-151]THADHALOGNASE
InterPro
IPR005834
Domain
Haloacid dehalogenase-like hydrolase
PF00702\"[53-152]THydrolase
InterPro
IPR006402
Domain
HAD-superfamily hydrolase, subfamily IA, variant 3
TIGR01509\"[10-149]THAD-SF-IA-v3: HAD-superfamily hydrolase, su
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1000\"[51-151]Tno description
PTHR12725\"[34-158]THALOACID DEHALOGENASE-LIKE HYDROLASE


","No hits to the COGs database.","Significant hit ( 1.7e-05) to 4/7 blocks of the PR00413 family, which is described as \"Haloacid dehalogenase/epoxide hydrolase family signature\". Prints database entry for PR:PR00413. PR00413D 62-75 13 PR00413E 93-109 9.6 PR00413F 111-131 0.62 PR00413G 138-151 1e+02","Residues 52 to 159 match (6e-07) PD:PD003038 which is described as HYDROLASE EPOXIDE HYDROCARBONS AROMATIC DETOXIFICATION CATABOLISM CYTOSOLIC CEH SOLUBLE HYDRATASE ","","","","","","","","","","","","Wed Jan 8 08:40:38 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01270 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Tsang JS, Sam L.Cloning and characterization of a cryptic haloacid dehalogenase from Burkholderia cepacia MBA4.J Bacteriol. 1999 Oct;181(19):6003-9.PMID: 10498712 Nardi-Dei V, Kurihara T, Park C, Miyagi M, Tsunasawa S, Soda K, Esaki N.DL-2-Haloacid dehalogenase from Pseudomonas sp. 113 is a new class of dehalogenase catalyzing hydrolytic dehalogenation not involving enzyme-substrate ester intermediate.J Biol Chem. 1999 Jul 23;274(30):20977-81.PMID: 10409645 ","","Wed Jan 8 08:38:37 2003","1","","","" "AA01271","864041","863934","108","ATGTATTACAATGTTTCGAGCAACTGTGATTCAAACATGCGTACCATCAACGGTGTAGTGCGAAAAAGTGCGGTCATTTTTCTAATCAAATTTCACGCCCAAGGTGAT","","","4062","MYYNVSSNCDSNMRTINGVVRKSAVIFLIKFHAQGD","863934","","hypothetical protein","Cytoplasm, Extracellular","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:48:04 2004","Wed Feb 25 13:48:04 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01271 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 13:48:04 2004","","","","","","","","","","","","","1","","","" "AA01272","864271","864179","93","TTGTTGATTAACACATTGCCTGCGAATGGTAATGAAACGGTTCGTTCCTGCGCACTTATTGAGCCGCATTTATACGGGCAGAATAGAGTAGTA","","","3388","LLINTLPANGNETVRSCALIEPHLYGQNRVV","864179","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:52:19 2004","Wed Feb 25 13:52:19 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01272 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 13:52:19 2004","","","","","","","","","","","","","1","","","" "AA01273","864502","864648","147","GTGTTGCTTCTTTATTTAATCATCATCGGCGAAGGTTTGCTGTTGCTTTCCGATTCGAGTTCCGCACCTTGGACAGTATTGTCGCAAGGCGTTGCGTTACAAGGGCAATTCAGCGTCGGTTGGGCATCGTGCATTATCAGCCTGACG","","","5116","VLLLYLIIIGEGLLLLSDSSSAPWTVLSQGVALQGQFSVGWASCIISLT","864648","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database. A very weak similarity might be seen to gi|23466606 from Haemophilus somnus.","
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide


","BeTs to 3 clades of COG2364COG name: Uncharacterized membrane proteinFunctional Class: RThe phylogenetic pattern of COG2364 is ---------d--b----h--------Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Wed Feb 25 13:50:12 2004","Wed Feb 25 13:50:12 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01273 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 13:50:12 2004","","","","","","","","","","","","","1","","","" "AA01274","864659","864892","234","GTGGTTTCCGCTAAAGCTCAGGCCGGGGCTCCCACGGTAATGAATATTTTCGTTATCGCCCTTGTCCTCGGCTTAACCACCTATTTACCGGAAAAACCCACCGCACTTTATGTGCGTTTTGCCTACGCCGTTATCGGCATTTTGCTGTCTCGGCATTGGTACGCTGATGTTTGCATTCGGTATCGGTCGGGTGGTGCAATACACGCTGTTATTTATCAGCCGCGTGCCATACTT","","","8516","VVSAKAQAGAPTVMNIFVIALVLGLTTYLPEKPTALYVRFAYAVIGILLSRHWYADVCIRYRSGGAIHAVIYQPRAIL","864892","","hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-24]?signal-peptide
tmhmm\"[10-28]?\"[34-54]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Jan 8 08:59:38 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01274 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01276","865904","864870","1035","ATGAAAAAAGTATTGGTTATTCGTAACGATAAACTGGGTGATTTTATGTTGGCATGGCCGGCGTTTGCCATGTTGAAAGCATCGGATCCGTCGCTAAAACTTACCGCACTTGTGCCGACGTATACGGCGGAAATCGCCCGCGCCTGCCCTTATTTAGATGAGGTCATCATTGACGTGCCGAAGGGGGATAAAGCGGCGTTTCAACGTCTCGTGAATGACATCAAGGCGCAGCGATTTGATGCTATGATTAGTTTTTTTTCCAATACGCACAATGCCAAACTGGCTTGGAAATGCCGTATTCCTTATCGCTTGGCGCCTGCAACTAAATGGGTGCAGTTTTTTTATAATCATCGTCTGGTGCAACGTCGTTCTCAATCTGCCAAGCCAGAGTTTGCCTATAATCTGGATTTAGCCCGTCGTTTTTTACAGGATCAGAGCATTGCGGTGGTGGAACCGCGTCCGCCGTATCTCAGCTTCCCGAAAAGTGCGGTGGATTTTCAGCGTGAATTTTTATGTCTGCAGTTAAACGTGGATTCATCGAAAAAATGGATTTTCGTGCACAGCGGTTCGGGCGGCTCCGCTAATAATTTATCTTTGGCGCAATACGCCGCATTGATTCGGGGGCTGTTGGCGCAGTTTGATGCGTATGTGATTCTCACCGCCGGCCCCAATGAAAGTGAAAAAGCCCATGAATTGGCGGGGCTGGTGCAAGATGCCCGCGTGGTGGTTTATGATAAAAATAAGGGGCTGGTGGATTTTGCACAATCCTTGGCGTGCGCCGATCTGTTTATTGCCGGTTCGACAGGTCCGCTTCATTTGAGCGGCGCGTTAAACGTGCCGACCATCGGCTTTTACCCGAGCCGCCGTTCCGCCACACCGTTGCGCTGGCAACCGATTAATGATGAGGCGAAACATCTGGCATTTTGCCCATCTAACGACAAAGCCAGCCAGACGGATTTAAGCAAAATCTCAATCGAGGAAAAGCTAGCGAAGATGATTCGGTTTATTACTAAAGTATGGCACGCGGCTGATAAA","","","38595","MKKVLVIRNDKLGDFMLAWPAFAMLKASDPSLKLTALVPTYTAEIARACPYLDEVIIDVPKGDKAAFQRLVNDIKAQRFDAMISFFSNTHNAKLAWKCRIPYRLAPATKWVQFFYNHRLVQRRSQSAKPEFAYNLDLARRFLQDQSIAVVEPRPPYLSFPKSAVDFQREFLCLQLNVDSSKKWIFVHSGSGGSANNLSLAQYAALIRGLLAQFDAYVILTAGPNESEKAHELAGLVQDARVVVYDKNKGLVDFAQSLACADLFIAGSTGPLHLSGALNVPTIGFYPSRRSATPLRWQPINDEAKHLAFCPSNDKASQTDLSKISIEEKLAKMIRFITKVWHAADK","864870","","heptosyltransferase III","Periplasm","","
InterPro
IPR002201
Family
Glycosyl transferase, family 9
PF01075\"[67-330]TGlyco_transf_9
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2000\"[3-120]T\"[164-333]Tno description


","No hits to the COGs database.","Significant hit ( 2.5e-23) to 2/2 blocks of the IPB002201 family, which is described as \"Glycosyltransferase family 9\". Interpro entry for IP:IPR002201. IPB002201A 13-37 3.9e-06 IPB002201B 247-290 1.1e-15","Residues 1 to 285 match (5e-07) PD:PD399341 which is described as TRANSFERASE PROTEOME COMPLETE SUGAR HEPTOSYLIII ","","","","","","","","","","","","Wed Jan 8 09:04:57 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01276 is paralogously related to AA01396 (3e-06) and AA01327 (5e-05).","","","","","","Residues 67 to 330 (E-value = 1.5e-06) place AA01276 in the Glyco_transf_9 family which is described as Glycosyltransferase family 9 (heptosyltransferase) (PF01075)","","","","","Filiatrault,M.J., Gibson,B.W., Schilling,B., Sun,S.,Munson,R.S. Jr. and Campagnari,A.A. Construction and Characterization of Haemophilus ducreyiLipooligosaccharide (LOS) Mutants Defective in Expression ofHeptosyltransferase III and beta1,4-Glucosyltransferase:Identification of LOS Glycoforms Containing LactosamineRepeats. Infect. Immun. 68(6): 3352-3361, 2000. PubMed: 10816485 ","","Wed Jan 8 09:04:57 2003","1","","","" "AA01277","867504","866089","1416","ATGACACAATTCAGAAAAGAAGTGGATTTATTAGGTGAACGCGACGTTCCTGCGGACGCGTATTGGGGGATTCATACATTAAGAGCGATAGAAAATTTCAACATTTCTAACACCACCATTTCTGACGTGCCGGAATTCGTACGTGGCATGGTGATGGTGAAAAAAGCTACTGCACTCACCAACGGCGAATTAGGCACGATTTCGAAAAAAATTGCCGATGCTATTGTAAAAGCCTGTGATGAAGTGTTGGTCAACGGCAAATGTTTGGATCAATTCCCGTCCGACGTTTATCAAGGCGGCGCGGGCACTTCCGTCAACATGAATACGAACGAAGTGGTTGCGAATCTGGCATTGGAAATTTTAGGACACAAAAAAGGCGAATATAATTATTTGGATCCGATGGATCATGTGAATGCCAGCCAATCCACCAACGATGCTTACCCGACCGGTTTCCGTATTGCGGTGTATAACAGCATTATGAAATTAGTCAGCAAAGTGTTGTATTTACAACAAGGCTTTGAGAATAAATCAAAAGAATTCGCCAAAGTGTTAAAAATGGGGCGCACCCAATTGCAAGATGCGGTGCCGATGACCGTGGGACAAGAATTCAAAGCCTTTTCCGTATTGTTGGATGAAGAAGTGCGGAACTTAAAACGCACGGCGGAATTGCTGCTTGAAGTGAACTTAGGTGCGACCGCGATCGGTACCGGGTTGAACACCCCGCAAGGCTATGTACCGTTGGTGGTGAAACATTTGTCGGAAGTCAGCGGTTTGCCTTGCGTGGTTGCCGAAAACCTGATTGAAGCCACATCCGACTGCGGCGCTTATGTGATGGTACATGGCGCGTTAAAACGTACGGCGGTAAAATTATCCAAAGTATGTAATGATTTGCGTTTATTGTCTTCCGGTCCGCGTGCAGGCTTGAAAGAAATCAACCTGCCTGAATTACAAGCGGGCTCTTCCATCATGCCGGCGAAAGTCAACCCGGTGGTGCCGGAAGTGGTGAACCAAGTGTGCTTCAAGGTGATCGGTAACGACACCACCGTGACCTTCGCTGCTGAAGCCGGTCAATTGCAATTAAACGTGATGGAACCGGTAATCGGTCAGGCTATGTTCGAATCTATCGACATCTTAACCAACGCGTGCGTGAACTTGCGCGATAAATGTATCGACGGCATCACCGTGAACAAAGAAATTTGCGAAAATTATGTGTTCAATTCTATCGGTATCGTCACCTACTTAAACCCATTCATCGGTCACCATAATGGCGACTTAGTGGGTAAAATATGCGCCCAAACCGGCAAAGGCGTGCGTGAAGTGGTGTTGGAAAAAGGCTTGTTAACCAAAGAAGAATTGGATGATATTCTGTCCGTGGAAAACTTGATGAACCCGACTTACAAAGCGAAATTAAATAAG","","","53298","MTQFRKEVDLLGERDVPADAYWGIHTLRAIENFNISNTTISDVPEFVRGMVMVKKATALTNGELGTISKKIADAIVKACDEVLVNGKCLDQFPSDVYQGGAGTSVNMNTNEVVANLALEILGHKKGEYNYLDPMDHVNASQSTNDAYPTGFRIAVYNSIMKLVSKVLYLQQGFENKSKEFAKVLKMGRTQLQDAVPMTVGQEFKAFSVLLDEEVRNLKRTAELLLEVNLGATAIGTGLNTPQGYVPLVVKHLSEVSGLPCVVAENLIEATSDCGAYVMVHGALKRTAVKLSKVCNDLRLLSSGPRAGLKEINLPELQAGSSIMPAKVNPVVPEVVNQVCFKVIGNDTTVTFAAEAGQLQLNVMEPVIGQAMFESIDILTNACVNLRDKCIDGITVNKEICENYVFNSIGIVTYLNPFIGHHNGDLVGKICAQTGKGVREVVLEKGLLTKEELDDILSVENLMNPTYKAKLNK","866089","","aspartate ammonia-lyase","Cytoplasm","","
InterPro
IPR000362
Domain
Fumarate lyase
PR00149\"[137-155]T\"[182-198]T\"[273-300]T\"[319-335]TFUMRATELYASE
PF00206\"[12-344]TLyase_1
PS00163\"[319-328]TFUMARATE_LYASES
InterPro
IPR003031
Domain
Delta crystallin
PR00145\"[136-158]T\"[177-197]T\"[319-335]TDCRYSTALLIN
InterPro
IPR004708
Family
Aspartate ammonia-lyase
TIGR00839\"[5-472]TaspA: aspartate ammonia-lyase
noIPR
unintegrated
unintegrated
G3DSA:1.10.275.10\"[2-141]Tno description
G3DSA:1.10.40.30\"[410-458]Tno description
G3DSA:1.20.200.10\"[142-409]Tno description
PTHR11444\"[1-464]TASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE
PTHR11444:SF1\"[1-464]TASPARTATE AMMONIA LYASE


","No hits to the COGs database.","Significant hit ( 8.1e-15) to 2/2 blocks of the IPB000362 family, which is described as \"Fumarate lyase\". Interpro entry for IP:IPR000362. IPB000362A 187-200 1.6e-06 IPB000362B 319-329 1.3e-06","Residues 183 to 209 match (2e-07) PD:PD593016 which is described as LYASE ASPARTATE PROTEOME AMMONIA-LYASE COMPLETE ASPARTASE L-ASPARTASE CLASS AMMONIUM FUMC ","","","","","","","","","","","","Wed Jan 8 09:11:01 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01277 is paralogously related to AA01717 (2e-99) and AA00218 (6e-09).","","","","","","Residues 12 to 344 (E-value = 3.1e-160) place AA01277 in the Lyase_1 family which is described as Lyase (PF00206)","","","","","Shi,W., Dunbar,J., Jayasekera,M.M., Viola,R.E. and Farber,G.K.The structure of L-aspartate ammonia-lyase from Escherichia coli Biochemistry 36 (30), 9136-9144 (1997) PubMed: 9230045 Woods,S.A., Miles,J.S., Roberts,R.E. and Guest,J.R. Structural and functional relationships between fumarase and aspartase. Nucleotide sequences of the fumarase (fumC) and aspartase (aspA) genes of Escherichia coli K12 Biochem. J. 237 (2), 547-557 (1986) PubMed: 3541901 Takagi,J.S., Ida,N., Tokushige,M., Sakamoto,H. and Shimura,Y. Cloning and nucleotide sequence of the aspartase gene of Escherichia coli W Nucleic Acids Res. 13 (6), 2063-2074 (1985) PubMed: 2987841 ","","Wed Jan 8 09:11:01 2003","1","","","" "AA01278","867651","867785","135","ATGCGAGATTTGAAGCGCCGACATATTGCACTGCAAAATAAACAGGGTAATATTCATAGCCGATTTATTATTAAGGAGCGCCCATGCCTTTTATTGCCTTTCTTTTCGCCGTTTTCCTGTTTATTTATGCCGAAC","","","5397","MRDLKRRHIALQNKQGNIHSRFIIKERPCLLLPFFSPFSCLFMPN","867785","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
InterPro
IPR013838
Binding_site
Beta tubulin, autoregulation binding site
PS00228\"[1-4]?TUBULIN_B_AUTOREG


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:54:01 2004","Wed Feb 25 13:54:01 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01278 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 13:54:01 2004","","","","","","","","","","","","","1","","","" "AA01279","867827","868213","387","ATGTTGATTCTCTTGCTGATCGGTTCATCGTTGTTGGGTATTTTGATTATTCGCGCCCGCAGTTGGTATGCCTTAACGCGTGTCCGACAACAATTGAAACAGGGCGAATTGCCGACCGAAACAATTTTCAATTCTGCCCGTTGGCTTATTGCCGGCGTGCTTTTCGTAATTCCGGGCTTCGTCACCGATATACTTGCCTGCATTCTACTCAGCCCGCTCGGTAGCCACATCGCGAAAATGCTGTTGGGCAGCCGTTTCATGTTCTTCCGTCAAAACATCTTTAAAAACGATCACACTTTTTATTCGTCACGCCACCACAAGGCGGAAGATGGCGAGGTTTTTGAGGCAGAATTTGAAAAGGAAGTGGATGAACATAAACGGCTCAAA","","","18422","MLILLLIGSSLLGILIIRARSWYALTRVRQQLKQGELPTETIFNSARWLIAGVLFVIPGFVTDILACILLSPLGSHIAKMLLGSRFMFFRQNIFKNDHTFYSSRHHKAEDGEVFEAEFEKEVDEHKRLK","868213","","phage exclusion-related protein","Inner membrane, Cytoplasm","","
InterPro
IPR007313
Family
FxsA cytoplasmic membrane protein
PF04186\"[1-95]TFxsA
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide
tmhmm\"[5-25]?\"[48-70]?transmembrane_regions


","BeTs to 6 clades of COG3030COG name: Protein affecting phage T7 exclusion by the F plasmidFunctional Class: RThe phylogenetic pattern of COG3030 is -o--------r-b-efgh-n-j----Number of proteins in this genome belonging to this COG is","","Residues 18 to 75 match (3e-13) PD:PD020977 which is described as PROTEOME COMPLETE FXSA T7 EXCLUSION F MEMBRANE TRANSMEMBRANE BACTERIOPHAGE SUPPRESSOR ","","","","","","","","","","","","Tue Feb 18 16:11:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01279 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 95 (E-value = 3.8e-09) place AA01279 in the FxsA family which is described as FxsA cytoplasmic membrane protein (PF04186)","","","","","Wang,W.F., Cheng,X. and Molineux,I.J.Isolation and identification of fxsA, an Escherichia coli gene that can suppress F exclusion of bacteriophage T7J. Mol. Biol. 292 (3), 485-499 (1999)PubMed: 10497016Wang,W.F., Margolin,W. and Molineux,I.J.Increased synthesis of an Escherichia coli membrane proteinsuppresses F exclusion of bacteriophage T7J. Mol. Biol. 292 (3), 501-512 (1999)PubMed: 10497017","","Tue Feb 18 16:11:51 2003","1","","","" "AA01280","868303","868590","288","ATGAATATTCGTCCATTACACGACAAAGTCATTTTAAAACGTGAAGACGTGGAAACTAAGTCCGCCGGTGGCATCGTTTTAACCGGTTCCGCTGCCACCAAATCCACTCGCGCCAAAGTATTGGCAGTAGGTCCGGGACGCTTGCTGGAAAATGGTAGTGTACACCCAATGCACGTTAAAGTTGGCGACACCGTGATCTTCAGCGACGGTTATGGCGTGAAAGCGGAGAAAATTGACGGTGAGGAAGTGCTCATCATCTCTGAAAGTGATATTTTGGCGATCGTTGAG","","","10175","MNIRPLHDKVILKREDVETKSAGGIVLTGSAATKSTRAKVLAVGPGRLLENGSVHPMHVKVGDTVIFSDGYGVKAEKIDGEEVLIISESDILAIVE","868590","From GenBank (gi:1705791): This protein binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. ","groES chaperonin","Cytoplasm","","
InterPro
IPR001476
Family
Chaperonin Cpn10
PD000566\"[7-92]TCH10_ACTAC_P46399;
PR00297\"[3-18]T\"[25-46]T\"[60-72]T\"[82-95]TCHAPERONIN10
G3DSA:2.30.33.40\"[1-95]Tno description
PTHR10772\"[1-96]TGROES CHAPERONIN
PF00166\"[2-95]TCpn10
PS00681\"[3-27]TCHAPERONINS_CPN10


","BeTs to 19 clades of COG0234COG name: Co-chaperonin GroES (HSP10)Functional Class: OThe phylogenetic pattern of COG0234 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 3.7e-32) to 2/2 blocks of the IPB001476 family, which is described as \"Chaperonins cpn10 (10 Kd subunit)\". Interpro entry for IP:IPR001476. IPB001476A 3-21 6.9e-08 IPB001476B 38-89 6.4e-23","Residues 3 to 95 match (2e-07) PD:PD595196 which is described as PROTEOME COMPLETE HEAT CHAPERONIN PROTEIN-COCHAPERONIN SHOCK 10KDA ","","","","","","","","","","","Wed Jan 8 09:24:43 2003","Wed Jan 8 09:24:43 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01280 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 96 (E-value = 3.2e-48) place AA01280 in the Cpn10 family which is described as Chaperonin 10 Kd subunit (PF00166)","","","","Nakano,Y., Inai,Y., Yamashita,Y., Nagaoka,S., Kusuzaki-Nagira,T.,Nishihara,T., Okahashi,N. and Koga,T.Molecular and immunological characterization of a 64-kDa protein of Actinobacillus actinomycetemcomitansOral Microbiol. Immunol. 10 (3), 151-159 (1995)PubMed: 7567064","","Wed Jan 8 09:24:43 2003","","1","","","" "AA01284","868714","870354","1641","ATGGCAGCAAAAGACGTAAAATTCGGCAACGACGCACGCGTAAAAATGTTAAACGGCGTAAATATTTTAGCCGATGCAGTAAAAGTTACTCTCGGTCCAAAAGGTCGTAACGTAGTGTTAGACAAATCTTTCGGTGCACCGACCATCACCAAAGACGGGGTTTCCGTGGCGCGTGAAATCGAATTAGAAGATAAATTTGAAAACATGGGCGCCCAAATGGTGAAAGAAGTGGCGTCCAAAGCGAACGACGCGGCAGGGGACGGTACCACAACCGCCACCGTATTGGCTCAAGCCATCGTGAACGAAGGCTTAAAAGCCGTTGCCGCCGGTATGAACCCGATGGATTTAAAACGCGGTATCGACAAAGCTGTCAACTCAGTGGTTGCCGAGCTTAAAAATCTCTCCAAACCATGCGAAACCTCAAAAGAAATCGAACAAGTTGGCACGATCTCTGCAAATTCCGACAGCATTGTGGGTCAATTAATCGCTCAAGCCATGGAAAAAGTGGGTAAAGAAGGCGTAATTACCGTGGAAGACGGCACCGGTTTGGAAGACGAATTGGATGTGGTTGAAGGTATGCAATTCGACCGCGGTTACCTTTCCCCATACTTCATCAACAAGCCTGAAACCGCCACTGTGGAACTGGACAATCCGTTTATCCTGTTAGTAGATAAAAAAATCTCCAACATCCGCGAATTATTGCCGGTATTAGAAGGCGTGGCGAAAGCCGGTAAACCATTGTTAATCATCGCCGAAGATGTGGAAGGCGAAGCTTTGGCAACCTTGGTTGTAAACACCATGCGCGGTATCGTGAAAGTGGCCGCAGTGAAAGCGCCGGGCTTTGGTGACCGCCGTAAAGCGATGTTACAAGATATTGCGATTTTAACCGCCGGTACGGTCATTTCCGAAGAAATCGGTATGGAATTGGAAAAAGCCACACTTGAAGATTTAGGTCAGGCAAAACGTATTGTTATCAACAAAGATAACACCACCATCATCGACGGTATCGGCGATGAAGCACAAATCCAAGGTCGTGTAGCGCAAATTCGTCAACAAATTGAAGAGTCCACTTCCGACTACGACAAAGAGAAATTACAAGAACGCGTGGCGAAATTGGCCGGCGGTGTTGCGGTGATTAAAGTGGGCGCGGCAACCGAAGTGGAAATGAAAGAGAAAAAAGCGCGCGTTGAAGACGCCTTACACGCGACCCGAGCGGCGGTAGAAGAAGGCATCGTTGCCGGTGGTGGCGTGGCGTTAATTCGTGCAGCCGGCAGAGTAGTCGGCTTACAAGGCGAGAACGAAGAGCAAAATGTGGGTATCAAGCTTGCCCTTCGTGCTATGGAAGCACCGTTGCGTCAAATCGTGGCAAATGCCGGTGAAGAAGCTTCCGTGATCGCCAGCGCAGTGAAGAACGGTGAAGGCAATTTCGGTTATAACGCAGGCACTGAACAGTACGGCGACATGATCGCTATGGGTATTTTGGATCCGACGAAAGTCACCCGTTCCGCATTACAATTTGCGGCGTCTGTTGCCGGTTTAATGATCACTACCGAATGTATGGTCACCGAGTTACCGAAAGACGACAAAGCTGACCTCGGCGCTGCCGGAATGGGCGGTATGGGAGGCATGGGCGGGATGATG","","","57436","MAAKDVKFGNDARVKMLNGVNILADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVNSVVAELKNLSKPCETSKEIEQVGTISANSDSIVGQLIAQAMEKVGKEGVITVEDGTGLEDELDVVEGMQFDRGYLSPYFINKPETATVELDNPFILLVDKKISNIRELLPVLEGVAKAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIAILTAGTVISEEIGMELEKATLEDLGQAKRIVINKDNTTIIDGIGDEAQIQGRVAQIRQQIEESTSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGIVAGGGVALIRAAGRVVGLQGENEEQNVGIKLALRAMEAPLRQIVANAGEEASVIASAVKNGEGNFGYNAGTEQYGDMIAMGILDPTKVTRSALQFAASVAGLMITTECMVTELPKDDKADLGAAGMGGMGGMGGMM","870354","From GenBank (gi:1705793): This protein prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.","heat shock protein (hsp60)","Cytoplasm","","
InterPro
IPR001844
Family
Chaperonin Cpn60
PR00298\"[27-53]T\"[83-110]T\"[268-291]T\"[350-375]T\"[398-419]TCHAPERONIN60
PS00296\"[405-416]TCHAPERONINS_CPN60
InterPro
IPR002423
Family
Chaperonin Cpn60/TCP-1
PR00304\"[25-41]T\"[47-65]T\"[81-100]T\"[378-400]T\"[411-423]TTCOMPLEXTCP1
PTHR11353\"[2-547]TCpn60/TCP-1
PF00118\"[23-525]TCpn60_TCP1
InterPro
IPR008950
Domain
GroEL-like chaperone, ATPase
SSF48592\"[10-522]TGroEL-ATPase
InterPro
IPR012723
Family
chaperonin GroEL
TIGR02348\"[3-527]TGroEL
noIPR
unintegrated
unintegrated
G3DSA:3.50.7.10\"[174-376]TG3DSA:3.50.7.10
PTHR11353:SF10\"[2-547]TPTHR11353:SF10
SSF52029\"[184-376]TSSF52029
SSF54849\"[137-193]TSSF54849


","BeTs to 26 clades of COG0459COG name: Chaperonin GroEL (HSP60 family)Functional Class: OThe phylogenetic pattern of COG0459 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit (3.8e-225) to 5/5 blocks of the IPB001844 family, which is described as \"Chaperonin cpn60 (60Kd subunit)\". Interpro entry for IP:IPR001844. IPB001844A 24-73 9.7e-47 IPB001844B 171-225 1.1e-42 IPB001844C 251-304 2.2e-47 IPB001844D 345-396 1.1e-46 IPB001844E 477-523 5.6e-38Significant hit ( 4.5e-63) to 5/5 blocks of the PR00304 family, which is described as \"Tailless complex polypeptide 1 (chaperone) signature\". Prints database entry for PR:PR00304. PR00304A 25-41 1.5e-11 PR00304B 47-65 3.5e-11 PR00304C 81-100 1.5e-12 PR00304D 378-400 4.9e-16 PR00304E 411-423 6.9e-06Significant hit ( 6.9e-08) to 2/2 blocks of the IPB002194 family, which is described as \"Chaperonins TCP-1\". Interpro entry for IP:IPR002194. IPB002194A 59-113 5.4e-05 IPB002194B 477-521 0.46","","","","","","","","","","","","Wed Jan 8 09:30:48 2003","Wed Jan 8 09:30:48 2003","","Tue Feb 8 14:55:37 2005","Tue Feb 8 15:03:52 2005","","yes","Fri Feb 20 15:41:32 MST 1998","AA01284 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Tue Feb 8 14:55:37 2005","","","","","Residues 23 to 525 (E-value = 4.9e-194) place AA01284 in the Cpn60_TCP1 family which is described as TCP-1/cpn60 chaperonin family (PF00118)","Tue Feb 8 14:55:37 2005","","","Nakano,Y., Inai,Y., Yamashita,Y., Nagaoka,S., Kusuzaki-Nagira,T.,Nishihara,T., Okahashi,N. and Koga,T.Molecular and immunological characterization of a 64-kDa protein of Actinobacillus actinomycetemcomitansOral Microbiol. Immunol. 10 (3), 151-159 (1995)PubMed: 96017061Zhang L, Koivisto L, Heino J, Uitto VJ.Bacterial heat shock protein 60 may increase epithelial cell migration through activation of MAP kinases and inhibition of alpha6beta4 integrin expression.Biochem Biophys Res Commun. 2004 Jul;319(4):1088-95.PMID: 15194479Yoshioka M, Grenier D, Hinode D, Fukui M, Mayrand D.Antigenic cross-reactivity and sequence homology between Actinobacillus actinomycetemcomitans GroEL protein and human fibronectin.Oral Microbiol Immunol. 2004 Apr;19(2):124-8.PMID: 14871354Zhang L, Pelech S, Uitto VJ.Long-term effect of heat shock protein 60 from Actinobacillus actinomycetemcomitans on epithelial cell viability and mitogen-activated protein kinases.Infect Immun. 2004 Jan;72(1):38-45.PMID: 14688078","Parsons LM, Waring AL, Shayegani M. Molecular analysis of the Haemophilus ducreyi groE heatshock operon. Infect Immun 1992 Oct;60(10):4111-8. PubMed: 1356926. Valle F, DeRose JA, Dietler G, Kawe M, Pluckthun A, SemenzaG. AFM structural study of the molecular chaperone GroEL and its two-dimensional crystals: an ideal \"living\" calibration sample. Ultramicroscopy. 2002 Oct;93(1):83-9. PMID: 12380652 Miyazaki T, Yoshimi T, Furutsu Y, Hongo K, Mizobata T,Kanemori M, Kawata Y. GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle. J Biol Chem. 2002 Oct 10 [epub ahead of print] PMID: 12377767","Tue Feb 8 15:03:52 2005","Tue Feb 8 15:03:52 2005","1","","","" "AA01286","871303","870449","855","ATGACTGCTCAAATTATTTCCGGCACCGAATTATCACACCAAATTAAAACCCATATTGCCCGCCAAATTGCACATTATGTGGAAAGGGGTAAACGTTCTCCCGGGCTTGCAGTGATTTTGGTCGGTGCCGATCCTGCTTCACAGGTTTATGTGGGAAGTAAGCGCAGAAGCTGTACCGAAGTGGGAATTGTTTCCAAATCCTACGATTTACCGGAAAATACGTCAGAGCAGGAGTTGCTAGGAATCATTGAACAGCTCAATCAGGATAAGGATGTTGATGGCATTCTGGTTCAGCTGCCATTACCAAAACATATTGATAGTACCAAAGTCATTGAAAAAATCTCGTCCGAAAAAGATGTGGACGGCTTCCATCCTTACAATGTCGGGCGTTTATGTCAGCGTATTCCGACGCTACGCGCTTGTACGCCTTATGGCGTGATGAAGCTGTTGGAAACCACCGGTATTGCGTTTCGTGGCAAACATGCGGTGATTGTGGGCGCGTCAAATATCGTTGGTCGTCCGATGGCGTTAGAATTGTTACTTGCAGGTTGTACTGTCACGGTTACCCATCGTTTTACCGAAGATCTGGCACATCATGTGCGTCAGGCGGATATTGTTGTAGTTGCCGTGGGAAAACCGAGATTTATTAAAGGGGAATGGATTAAAGAGGGTGCTGTTGTGGTTGACGTGGGGATTAATCGTATTGATGGCAAACTGGTGGGTGATGTGGAATTCGACGTGGCAGCGGAACGTGCGGCGTATATTACGCCGGTGCCGGGCGGTGTCGGTCCGATGACGGTGGCAATGCTGATGCAAAACACCCTTTCCGCTTATGAAAAACATGAAAATTTAGGC","","","30901","MTAQIISGTELSHQIKTHIARQIAHYVERGKRSPGLAVILVGADPASQVYVGSKRRSCTEVGIVSKSYDLPENTSEQELLGIIEQLNQDKDVDGILVQLPLPKHIDSTKVIEKISSEKDVDGFHPYNVGRLCQRIPTLRACTPYGVMKLLETTGIAFRGKHAVIVGASNIVGRPMALELLLAGCTVTVTHRFTEDLAHHVRQADIVVVAVGKPRFIKGEWIKEGAVVVDVGINRIDGKLVGDVEFDVAAERAAYITPVPGGVGPMTVAMLMQNTLSAYEKHENLG","870449","","5,10-methylenetetrahydrofolate dehydrogenase (bifunctional protein)","Cytoplasm","","
InterPro
IPR000672
Domain
Tetrahydrofolate dehydrogenase/cyclohydrolase
PD002300\"[10-126]TQ9CJR1_PASMU_Q9CJR1;
PR00085\"[34-56]T\"[75-102]T\"[110-131]T\"[155-175]T\"[204-233]T\"[238-254]T\"[255-273]TTHFDHDRGNASE
PF00763\"[4-121]TTHF_DHG_CYH
PF02882\"[124-282]TTHF_DHG_CYH_C
PS00766\"[76-101]TTHF_DHG_CYH_1
PS00767\"[259-267]TTHF_DHG_CYH_2
noIPR
unintegrated
unintegrated
G3DSA:3.40.192.10\"[29-114]Tno description
G3DSA:3.40.50.720\"[133-263]Tno description
PTHR10025\"[14-280]TMETHYLENETETRAHYDROFOLATE DEHYDROGENASE FAMILY MEMBER


","No hits to the COGs database.","Significant hit ( 2e-138) to 5/5 blocks of the IPB000672 family, which is described as \"Tetrahydrofolate dehydrogenase/cyclohydrolase\". Interpro entry for IP:IPR000672. IPB000672A 34-63 6.9e-19 IPB000672B 70-121 2.5e-29 IPB000672C 149-196 5.1e-29 IPB000672D 203-233 1.1e-25 IPB000672E 238-274 5.4e-31","Residues 3 to 126 match (5e-48) PD:PD002300 which is described as METHYLENETETRAHYDROFOLATE DEHYDROGENASE CYCLOHYDROLASE COMPLETE PROTEOME METHENYLTETRAHYDROFOLATE BIFUNCTIONAL FOLD OXIDOREDUCTASE INCLUDES: ","","","","","","","","","","","","Wed Jan 8 09:44:42 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01286 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 123 to 282 (E-value = 1.7e-110) place AA01286 in the THF_DHG_CYH_C family which is described as Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain (PF02882)","","","","","Sundararajan S, MacKenzie RE.Residues involved in the mechanism of the bifunctional methylenetetrahydrofolate dehydrogenase-cyclohydrolase: the roles of glutamine 100 and aspartate 125.J Biol Chem. 2002 May 24;277(21):18703-9.PMID: 11904299 ","","Wed Jan 8 09:44:42 2003","1","","","" "AA01287","872229","871723","507","GTGCTAAATCGTGATTTTACAGCGACGGCGCTCAATCAAAAATGGGTAACCGATGTCACTGAGTTTCGAGTTGGGGAAGAAAAGCTCTATTTTTCACCGTTGATGGATTTAGCGAACCGGGAAATTATTGCCTATAATTTTGCGAAACGCCCTAAGTTCTCATTGGTAAAAAGAATGCCGGAAGAAGGACTTGGCAAACTAAAACCGAGCGAATGCCCGATTATTCACAGCGACCAAGGGGTATTGTACGGCTCAGCAGAATGGGTAAAGATGTTGGAAGGCAAGGCGATACAAAGTATGAGTCGCCGAGGGAATTGCTATGATAATGCGGTGATTGAAAGCTTTTTTGCGATATTAAAATCTGAGTGTTTTTACTCACGCACTTATACTTCGATTGCCGAATTACAGGCGGAAATTGAAGAATATTTGGTGTATTACAACCAAGAACGAATTAAACTTGATTTAAAAGGATTAAGCCCGGTGCAATACCGAGCTCAATATTTAAGT","","","19548","VLNRDFTATALNQKWVTDVTEFRVGEEKLYFSPLMDLANREIIAYNFAKRPKFSLVKRMPEEGLGKLKPSECPIIHSDQGVLYGSAEWVKMLEGKAIQSMSRRGNCYDNAVIESFFAILKSECFYSRTYTSIAELQAEIEEYLVYYNQERIKLDLKGLSPVQYRAQYLS","871723","","transposase","Cytoplasm","This sequence is similar to gi|28872132 of Pseudomonas syringae and to many other transposases.","
InterPro
IPR001584
Domain
Integrase, catalytic core
PF00665\"[7-165]Trve
PS50994\"[7-168]TINTEGRASE


","No hits to the COGs database.","","Residues 55 to 114 match (3e-09) PD:PD001459 which is described as TRANSPOSASE COMPLETE PROTEOME PLASMID ORFB IS629 INSERTION ELEMENT SEQUENCE FOR ","","","","","","","","","","","","Wed Feb 25 13:58:08 2004","Wed Feb 25 13:58:08 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is similar to AA1522, AA0945, AA0845, AA0835, AA0709, AA0006, AA1371, AA1578.AA01287 is paralogously related to AA02342 (1e-95), AA01444 (1e-95), AA01268 (1e-95), AA01077 (1e-95), AA00010 (1e-95), AA02117 (2e-89), AA00145 (2e-23) and AA02420 (4e-17).","Wed Feb 25 13:58:08 2004","","","","","Residues 7 to 165 (E-value = 5.6e-31) place AA01287 in the rve family which is described as Integrase core domain (PF00665)","","","","","","","","1","","","" "AA01288","872348","872226","123","ATGGGTTTCCATTTGAATCATAAAACGGTGTTAAAACTGATGAATGCGTTAGGTATTCATTCTATTTTACGCAAGAAAAGACATGGAAAACGAGGAAAACATCGCATATTGCCCCGAATGTGC","","","4810","MGFHLNHKTVLKLMNALGIHSILRKKRHGKRGKHRILPRMC","872226","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:59:52 2004","Wed Feb 25 13:59:52 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paraloogus sequences are found to this sequence.AA01288 is paralogously related to AA02341 (1e-20), AA02116 (1e-20), AA01076 (1e-20), AA00009 (1e-20), AA01444 (3e-12) and AA01268 (3e-12).","Wed Feb 25 13:59:52 2004","","","","","","","","","","","","","1","","","" "AA01289","872908","872525","384","TTGAGGTGCAGATTATGTCTTACTCTTATCAATTTCGTTAAAAAACTATCAAACAGGTCACCGAGCAGGATTTTGGTATCCGTGAGGTGGCTAAATTTCATCAGATTTCTCGTTCTCAAGTCATTTATTGGAAAAGCCTTTCGTGAAAGAGGGCTTAATGGCGTAAAATCCCCTTATATAAACCCTCAACGCCCTAAAATAGTGAAGCCAAAGATGAAAAAGAAAGCGATTGAAATCCCGGAACAAACAGACTTTTCCCCAAAAGCGTTTAAAAAGCTGCAACGAGAGCTGGCATTAGCACGTGCACAGATTGCTTACCTAAAGGAGTTGGAGGCACTCGACCGTCAAAAACAGCGACAGAAAAAAGAAAAATCATTGAAAGAT","","","15047","LRCRLCLTLINFVKKLSNRSPSRILVSVRWLNFIRFLVLKSFIGKAFRERGLNGVKSPYINPQRPKIVKPKMKKKAIEIPEQTDFSPKAFKKLQRELALARAQIAYLKELEALDRQKQRQKKEKSLKD","872525","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 14:01:49 2004","Wed Feb 25 14:01:49 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is similar to AA0348 and to AA0834, the latter being a degenerate transposase.AA01289 is paralogously related to AA02115 (4e-69), AA01075 (4e-69), AA00008 (4e-69), AA02340 (2e-66), AA00535 (1e-22), AA01267 (4e-18), AA00631 (1e-13), AA00227 (2e-11), AA01404 (6e-11) and AA01549 (0.001).","Wed Feb 25 14:01:49 2004","","","","","","","","","","","","","1","","","" "AA01291","876061","872969","3093","GTGATATTGGCGACGGCTTCGCCGTTCGGCATGGTGCGGACTTCAGGATCGTTACCTAAATTACCGACAATAATCACTTTATTTACTCCAGCCATAATATCCTCTTCTTTTATTCGATTTTGCTGTAAAAAATTTGCCTTATTCTGCCTGAAAATCAGAAAGAAATCCACGCTTTCAACAAAATTAACTGGATATTTGCACAGTTATTTAAGAATATGCGATAATTATCGCAAATTTACACTTCTTTCATTTATAAAATCTATTATGGATACCATCGACATTCGTGGGGCGCGAACCCACAATCTGAAAAATATTAACTTAACCATTCCACGCGACAAACTTATCGTTATCACCGGTTTATCCGGTTCGGGCAAGTCTTCGCTGGCGTTTGATACCCTGTATGCGGAAGGACAACGCCGTTATGTGGAATCCCTTTCTGCCTATGCGCGCCAGTTTCTGTCATTAATGGAAAAGCCTGATGTGGACCACATTGAAGGGCTTTCACCGGCGATTTCCATTGAGCAAAAATCCACCTCCCATAACCCGCGTTCAACGGTGGGGACGATTACCGAAATTCATGATTACCTGCGTTTATTGTTTGCCCGCGTGGGCGAACCGCGCTGTCCGCATCATCATGTTCCGCTCACCGCGCAAACCATCAGCCAAATGGTGGATAAAGTACTTTCCCTGCCGGAAGACAGCAAAATGATGCTGTTGGCACCGGTGGTGAAAGAACGCAAAGGCGAACACGTTAAGCTGTTGCAACAAATTGCCGCACAAGGTTACATTCGCGCCCGTATCGATGGCGAAATTTGTGATTTATCCGATCCACCGAAACTGGAATTACATAAAAAACACACTATTGAAGTGGTGGTGGATCGCTTTAAAGTGCGGTCGGATTTAGCCACAAGATTGGCGGAATCCTTTGAAACCACGTTGGAATTATCGGGCGGCACGGCAGTGGTTGCCTACATGGACGATCCGAAAGCGGAAGAGTTGGTGTTCTCCGCCAACTTTGCCTGCCCCCATTGCGGCTACTCCGTGCCGGAACTGGAACCGCGTCTGTTTTCCTTCAATAACCCGGCAGGGGCGTGTCCGACCTGCGACGGTTTAGGCGTGCAGCAATATTTTGATGAAAAACGCGTGGTGCAAAATCCGAACATTTCCCTTGCCAACGGCGCCATTAAAGGCTGGGATCGCCGTAATTTTTATTATTATCAAATGCTCACTTCCCTCTCGAAACACTACCATTTCGACATAGAAACCCCGTTTGAAGCATTACCGAAAAAAATCCAACAGATTATTTTGAATGGTTCCGGCAAGGAAGAAATCGAGTTTCAATACATGAACGATCGCGGCGATGTGGTGCTGCGTCGCCACGCCTTTGAAGGGATTTTGAACAGCATGGCGCGCCGTTATAAAGAAACGGAATCCATGTCGGTGCGCGAAGAACTCGCCAAACACATCAGCAACCGCCCGTGCGCCGATTGCGGCGGTTCCCGCTTACGCCCGGAAGCGCGCAATGTATATATTGAACAAACCAACCTGCCGGAGGTGTCGGAAAAAAGCATCGGTGAAGCGTTAGATTTCTTCGGCGATTTACAGCTCAGCGGGCAAAAAGCCCAAATCGCCGAAAAAATCCTGAAAGAGATAAAAGAGCGGTTACAATTTTTAGTGAATGTAGGCTTGAATTATCTTTCCCTTTCCCGCTCTGCCGAAACCCTTTCTGGCGGTGAAGCACAACGGATTCGCCTCGCCAGCCAAATCGGCGCAGGATTAGTGGGTGTGATGTACGTGTTGGATGAACCCTCCATCGGCTTGCACCAACGGGACAATGAACGCCTGCTTAACACGCTGATTCATTTGCGTAATTTAGGCAATACAGTAATCGTGGTGGAACATGACGAAGACGCCATTTTGAGCGCCGACCACATTATCGACATCGGACCGGGCGCCGGCGTGCACGGAGGTAGCGTCATCGCCGAAGGCACCGCACAACAAATCATGCAAAATCCGAATTCCCTCACGGGTAAATTTTTATCGGGCACGGAAAAGATCGAAATACCGAAAAAACGTACCGCACTTGATAAGAAAAAAATGCTCAAATTGTTCGGCGCTTCCGGTAACAACCTGAAAAACGTCAATTTAGACATTCCCGTGGGCTTATTTACCTGCATCACCGGCGTGTCCGGTTCAGGTAAATCTACACTGATTAACGACACTCTGTTCCCTATTGCACAAAACGCCTTGAATCGTGCAGAAAATGCCGAGGTATCGCCGTACAAGTCCATTAAAGGTTTGGAATTTTTCGATAAAGTTATTGATATTAACCAAAGCCCGATTGGACGCACGCCACGCTCCAACCCGGCAACTTACACGGGCGTATTCACGCCGATTCGCGAACTGTTTGCCGGCGTACCGGAAGCCCGTGCGCGCGGTTATAACCCGGGGCGTTTCAGTTTTAACGTGCGCGGCGGGCGCTGTGAAGCCTGCCAGGGCGACGGCGTAATCAAAGTGGAAATGCACTTCCTGCCCGATGTGTACGTGCCTTGCGACCAATGTAAAGGCAAGCGTTACAATCGCGAAACCCTGGAAATCCGCTACAAAGGTAAAACCATTCATCAGGTGCTGGACATGACGGTGGAAGATGCGCGCGAGTTTTTCGATGCCATTCCAATGATTGCGCGTAAATTGCAAACCCTGATTGACGTGGGCTTGTCTTATATTCGCTTGGGGCAATCCTCTACCACCCTGTCCGGCGGGGAAGCGCAACGGGTGAAACTGGCGACGGAACTCTCCAAACGGGATACGGGCAAAACCCTGTATATTCTGGACGAACCGACCACAGGGCTGCATTTTGCCGACATTAAACAATTGCTTTCCGTGTTACACCGTTTACGCGATCAAGGCAACACCATCGTGGTCATTGAGCATAATTTAGACGTGATTAAAACCGCCGACTGGATTGTAGATCTCGGCCCTGAAGGCGGCAGCGGCGGCGGACAAATTATCGCGACCGGCACACCGGAACAGGTTGCCAAAATGGAGGGCTCGCACACCGCCCGCTTCCTCAAAGAGATTTTGGCAAAAGGC","","","117008","VILATASPFGMVRTSGSLPKLPTIITLFTPAIISSSFIRFCCKKFALFCLKIRKKSTLSTKLTGYLHSYLRICDNYRKFTLLSFIKSIMDTIDIRGARTHNLKNINLTIPRDKLIVITGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLSLMEKPDVDHIEGLSPAISIEQKSTSHNPRSTVGTITEIHDYLRLLFARVGEPRCPHHHVPLTAQTISQMVDKVLSLPEDSKMMLLAPVVKERKGEHVKLLQQIAAQGYIRARIDGEICDLSDPPKLELHKKHTIEVVVDRFKVRSDLATRLAESFETTLELSGGTAVVAYMDDPKAEELVFSANFACPHCGYSVPELEPRLFSFNNPAGACPTCDGLGVQQYFDEKRVVQNPNISLANGAIKGWDRRNFYYYQMLTSLSKHYHFDIETPFEALPKKIQQIILNGSGKEEIEFQYMNDRGDVVLRRHAFEGILNSMARRYKETESMSVREELAKHISNRPCADCGGSRLRPEARNVYIEQTNLPEVSEKSIGEALDFFGDLQLSGQKAQIAEKILKEIKERLQFLVNVGLNYLSLSRSAETLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLNTLIHLRNLGNTVIVVEHDEDAILSADHIIDIGPGAGVHGGSVIAEGTAQQIMQNPNSLTGKFLSGTEKIEIPKKRTALDKKKMLKLFGASGNNLKNVNLDIPVGLFTCITGVSGSGKSTLINDTLFPIAQNALNRAENAEVSPYKSIKGLEFFDKVIDINQSPIGRTPRSNPATYTGVFTPIRELFAGVPEARARGYNPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDVYVPCDQCKGKRYNRETLEIRYKGKTIHQVLDMTVEDAREFFDAIPMIARKLQTLIDVGLSYIRLGQSSTTLSGGEAQRVKLATELSKRDTGKTLYILDEPTTGLHFADIKQLLSVLHRLRDQGNTIVVIEHNLDVIKTADWIVDLGPEGGSGGGQIIATGTPEQVAKMEGSHTARFLKEILAKG","872969","From Genbak:[gi:13431966] The ABC excision nuclease is a DNA repair enzyme thatcatalyzes the excision reaction of UV-damaged nucleotidesegments producing oligomers having the modified bases.UVRA isan ATPase and a DNA-binding protein tht preferentially bindssingle-stranded or UV-irradiated double-stranded DNA.","excinuclease ABC subunit A","Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PF00005\"[429-651]T\"[721-996]TABC_tran
PS50893\"[695-1025]TABC_TRANSPORTER_2
PS00211\"[575-589]T\"[918-932]TABC_TRANSPORTER_1
InterPro
IPR004602
Family
Excinuclease ABC, A subunit
TIGR00630\"[91-1013]Tuvra: excinuclease ABC, A subunit
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[101-671]T\"[681-1031]Tno description
PTHR19222\"[893-1015]TATP BINDING CASSETE (ABC) TRANSPORTER
tmhmm\"[21-41]?transmembrane_regions


","BeTs to 20 clades of COG0178COG name: Excinuclease ATPase subunitFunctional Class: LThe phylogenetic pattern of COG0178 is -om----qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 3.9e-09) to 2/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 710-756 9.3e-05 IPB001140C 972-1001 0.015 IPB001140C 628-657 0.016","Residues 711 to 739 match (4e-07) PD:PD000005 which is described as ATP-BINDING COMPLETE PROTEOME ABC TRANSPORTER TRANSPORTER PROBABLE TRANSMEMBRANE COMPONENT PLASMID ","","","","","","","","","","","Wed Jan 8 09:58:42 2003","Wed Jan 8 09:58:42 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01291 is paralogously related to AA02320 (2e-09), AA02080 (1e-08), AA00799 (7e-08), AA02805 (2e-06), AA02440 (3e-06), AA01820 (4e-06), AA02225 (5e-06), AA02786 (1e-05), AA02898 (2e-05), AA00934 (2e-05), AA02152 (3e-05), AA01656 (3e-05), AA01524 (5e-05), AA02550 (7e-05), AA01961 (7e-05), AA00858 (9e-05), AA02331 (1e-04), AA01645 (1e-04), AA00415 (1e-04), AA00700 (3e-04), AA02609 (5e-04), AA02146 (5e-04), AA02718 (6e-04), AA02324 (6e-04), AA00207 (6e-04), AA01779 (8e-04), AA01616 (8e-04), AA01051 (8e-04), AA00751 (8e-04), AA01393 (0.001) and AA01684 (0.001).","","","","","","Residues 721 to 993 (E-value = 5.3e-33) place AA01291 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","de la Morena,M.L., Hendrixson,D.R. and St Geme,J.W. 3rd. 1996.Isolation and characterization of the Haemophilus influenzae uvrA gene. Gene 177(1-2):23-28. PubMed: 8921840. Husain,I., Van Houten,B., Thomas,D.C. and Sancar,A. 1986.Sequences of Escherichia coli uvrA gene and protein reveal two potential ATP binding sites. J. Biol. Chem. 261(11):4895-4901. PubMed: 3007478. Backendorf,C., Brandsma,J.A., Kartasova,T. and van de Putte,P.1983. In vivo regulation of the uvrA gene: role of the \"-10\" and \"-35\" promoter regions. Nucleic Acids Res. 11(17):5795-5810. PubMed: 6310514. Myles,G.M. and Sancar,A. 1991. Isolation and characterization of functional domains of UvrA.Biochemistry 30(16):3834-3840. PubMed: 1826851.","","Fri Nov 21 16:43:37 2003","1","","","" "AA01292","875967","876443","477","ATGGCTGGAGTAAATAAAGTGATTATTGTCGGTAATTTAGGTAACGATCCTGAAGTCCGCACCATGCCGAACGGCGAAGCCGTCGCCAATATCACCGTTGCCACCAGTGAAAGCTGGAATGACAAAAACACCGGTGAACGCCGCGAAGTCACCGAATGGCACCGCATCGTATTTTATCGCCGCCAGGCGGAAGTGGCGGGGGAATACCTGCGTAAAGGGTCTAAAGTCTATGTCGAAGGACGCTTAAGAACCCGTAAATGGCAGGATCAAAACGGTCAAGATCGCTACACCACCGAAATCCAGGGCGACGTTTTACAAATGTTAGACAGCCGCGCCGATCGCCAATCCGGCGGAAACTACACACCGACATCCCAACCAAGTTATCCAAACCAACAACAAAGCGCCCCACGCAGTGCGCCGGCAAGTAAACCTGCCGCCGAAGCGCCGATGGATAATTTTGATGATGATATTCCTTTT","","","20955","MAGVNKVIIVGNLGNDPEVRTMPNGEAVANITVATSESWNDKNTGERREVTEWHRIVFYRRQAEVAGEYLRKGSKVYVEGRLRTRKWQDQNGQDRYTTEIQGDVLQMLDSRADRQSGGNYTPTSQPSYPNQQQSAPRSAPASKPAAEAPMDNFDDDIPF","876443","See PVT1 or GI:10954410 for the plasmid version of this gene.","single-stranded DNA binding protein","Extracellular, Cytoplasm","","
InterPro
IPR000424
Family
Single-strand binding protein/Primosomal replication protein n
PF00436\"[4-108]TSSB
PS50935\"[4-109]TSSB
InterPro
IPR011344
Family
Single-strand binding protein
PTHR10302\"[39-159]TSINGLE-STRANDED DNA-BINDING PROTEIN, SSB
TIGR00621\"[2-159]Tssb: single-strand binding protein
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[4-144]Tno description
noIPR
unintegrated
unintegrated
PIRSF002070\"[4-149]TSingle-strand binding protein


","No hits to the COGs database.","Significant hit ( 5.1e-49) to 3/3 blocks of the IPB000424 family, which is described as \"Single-strand binding protein family\". Interpro entry for IP:IPR000424. IPB000424A 4-42 1.2e-23 IPB000424B 68-90 2.2e-19 IPB000424C 153-159 0.0034","Residues 5 to 103 match (2e-09) PD:PD186605 which is described as DNA-BINDING DNA SINGLE-STRANDED PRECURSOR PEPTIDE MITOCHONDRIAL MITOCHONDRION REPLICATION TRANSIT MT-SSB ","","","","","Wed Jun 18 15:39:51 2003","","","","","","Wed Jun 18 15:39:51 2003","Wed Jan 8 10:00:21 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01292 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 109 (E-value = 1.7e-37) place AA01292 in the SSB family which is described as Single-strand binding protein family (PF00436)","","","","","Jarosik,G.P. and Hansen,E.J. Cloning and sequencing of the Haemophilus influenzae ssbgene encoding single-strand DNA-binding protein. Gene 146(1):101-103, 1994. PubMed: 8063092. Meyer,R.R. and Laine,P.S. The single-stranded DNA-binding protein of Escherichia coli.Microbiol. Rev. 54(4)342-380, 1990. PubMed: 2087220. de Vries,J. and Wackernagel,W. Cloning and sequencing of the Serratia marcescens geneencoding a single-stranded DNA-binding protein (SSB) and itspromoter region. Gene 127(1):39-45, 1993. PubMed: 8486286. De Vries,J., Genschel,J., Urbanke,C., Thole,H. andWackernagel,W. The single-stranded-DNA-binding proteins(SSB) of Proteus mirabilis and Serratia marcescens. Eur. J. Biochem. 224(2):613-622,1994. PubMed: 7925378","","Wed Jun 18 15:39:51 2003","1","","","" "AA01294","877427","876555","873","TTGCTCTCAATTCGATTAATTATGCCTGAACCCGCTAAACCCGCTACGCCAGCCAAAAGCCGCCCGTTTCTCAAATGGGCGGGCGGTAAATATCGCCTTATGGACGAAATCAATCGCCTACTACCAAAACGTAAGCAATGCTTGGTCGAACCCTTTGTGGGCGCCGGCGCGGTGTTTCTTAACAGCAATTTCAAACGCTACATTCTGGCGGACATCAACCCCGATTTAATCAACCTCTTTAATATCGTCAAATTGGATGTAGAACGCTATATTCAGGCGTGTAAACCGATTTTTTTCCACCCGGAAGCGAATACTGAAATTTACTACTACGGCAAACGCAAGGAATTTAACCAAAGCACTGACGTTTTCCAGCGCGCCGTGTTATTTCTCTATTTAAACCGCTTCGGTTTCAACGGATTATGCCGTTACAACTCCAAAAACGAATTCAACGTTCCTTTCGGCGATTACAAAACCCACTATTTCCCGGAAGAAGAACTGCGTTTTTTCGCCGCCAAAGCACAAAGTGCGGTCTTTATTTGCGCCGATTTTCAACAAACCTTTGAAATGGCGGACGAAAACTCCGTAATTTACTGCGACCCGCCCTACGCCCCGCTTTCACAAGACAGTAACTTCACCAATTACGCCGGCAATGAGTTCTCCATCGCCCACCAGCGTGATCTCGCCAACCTCGCCAAACACACCATGGAACAACGCAACATTCAAGTGCTGATCTCCAACCACGACACCCCTTTCACCCGCGAAATCTACCAAGGCGCCAAAATCCGTCGCCTAAAAGTACAACGTTCCATCAGCCAAGCACCGCATAAACGCATTAAGGTGAGGGAATTGATTGCGATGTTTAAGCAGGGAAAA","","","33891","LLSIRLIMPEPAKPATPAKSRPFLKWAGGKYRLMDEINRLLPKRKQCLVEPFVGAGAVFLNSNFKRYILADINPDLINLFNIVKLDVERYIQACKPIFFHPEANTEIYYYGKRKEFNQSTDVFQRAVLFLYLNRFGFNGLCRYNSKNEFNVPFGDYKTHYFPEEELRFFAAKAQSAVFICADFQQTFEMADENSVIYCDPPYAPLSQDSNFTNYAGNEFSIAHQRDLANLAKHTMEQRNIQVLISNHDTPFTREIYQGAKIRRLKVQRSISQAPHKRIKVRELIAMFKQGK","876555","","DNA adenine methylase","Cytoplasm","","
InterPro
IPR002052
Domain
N-6 Adenine-specific DNA methylase
PS00092\"[196-202]?N6_MTASE
InterPro
IPR002294
Family
N6 adenine-specific DNA methyltransferase, D12 class
PR00505\"[26-42]T\"[48-62]T\"[67-80]T\"[193-205]TD12N6MTFRASE
InterPro
IPR012263
Family
Adenine modification methylase, M.EcoRV
PIRSF000398\"[20-291]TModification methylase (adenine-specific), M.EcoRV type
InterPro
IPR012326
Domain
DNA adenine methylase
TIGR00571\"[20-287]Tdam: DNA adenine methylase
InterPro
IPR012327
Domain
D12 class N6 adenine-specific DNA methyltransferase
PF02086\"[26-270]TMethyltransfD12
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[10-286]Tno description


","BeTs to 11 clades of COG0338COG name: Site-specific DNA methylaseFunctional Class: LThe phylogenetic pattern of COG0338 is --mpk-------bce-ghsnu---t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-26) to 4/4 blocks of the PR00505 family, which is described as \"D12 class N6 adenine-specific DNA methyltransferase signature\". Prints database entry for PR:PR00505. PR00505A 26-42 2.2e-06 PR00505B 48-62 0.00012 PR00505C 67-80 0.0001 PR00505D 193-205 1.2e-05","Residues 237 to 287 match (1e-07) PD:PD580906 which is described as DNA METHYLTRANSFERASE ADENINE METHYLASE TRANSFERASE REPLICATION PROTEOME COMPLETE DEOXYADENOSYL-METHYLTRANSFERASE M.STYDAM ","","","","","","","","","","","","Wed Jan 8 10:03:42 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01294 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 26 to 270 (E-value = 2e-95) place AA01294 in the MethyltransfD12 family which is described as D12 class N6 adenine-specific DNA methyltransferase (PF02086)","","",""," Wu H, Lippmann JE, Oza JP, Zeng M, Fives-Taylor P, Reich NO.,Abstract Inactivation of DNA adenine methyltransferase alters virulence factors in Actinobacillus actinomycetemcomitans.Oral Microbiol Immunol. 2006 Aug;21(4):238-44.PMID: 16842508Eberhard,J., Oza,J. and Reich,N.O.Cloning, sequence analysis and heterologous expression of the DNAadenine-(N(6)) methyltransferase from the human pathogen Actinobacillus actinomycetemcomitansFEMS Microbiol. Lett. 195 (2), 223-229 (2001)PubMed: 21100291","Brooks,J.E., Blumenthal,R.M. and Gingeras,T.R. The isolation and characterization of the Escherichia coli DNA adenine methylase (dam) gene Nucleic Acids Res. 11 (3), 837-851 (1983) PubMed: 6300769 Lyngstadaas,A., Lobner-Olesen,A. and Boye,E. Characterization of three genes in the dam-containing operon of Escherichia coli Mol. Gen. Genet. 247 (5), 546-554 (1995) PubMed: 7603433 Jonczyk,P., Hines,R. and Smith,D.W. The Escherichia coli dam gene is expressed as a distal gene ofa new operon Mol. Gen. Genet. 217 (1), 85-96 (1989) PubMed: 2549371 Guyot,J.B., Grassi,J., Hahn,U. and Guschlbauer,W. The role of the preserved sequences of Dam methylase Nucleic Acids Res. 21 (14), 3183-3190 (1993) PubMed: 8341592 ","Wed Jan 8 10:03:42 2003","Wed Jan 8 10:03:42 2003","1","","","" "AA01295","878497","877412","1086","ATGTTGTGTGTAAGTGTTGAATTGAAAGAAAGAAGCTACCCGATTCATATCGGCGCCGGATTATTGACGGATCCCCATTGTTATCCGCTGAAACCGGGCAACAAAGTCATGATCGTGACCAATCCGACCGTTGCACAATATTACCTTGCCATCGTCACCGACATGCTGGAAAAAATCGGTTGTCTCGTTGAGCGCGTATTATTGCCGGACGGCGAACAATACAAAACCCTTGACTCTTTAAACCTGATTTTCACCGCACTTTTACAAGCCAATCACGGTCGTGACACTACCATCGTGGCATTGGGCGGCGGAGTAATCGGCGATGTTGCCGGCTATGCGGCGGCGAGCTATCAACGAGGTGTGCGCTTTATTCAAATTCCGACCACCTTATTGGCGCAAGTGGATTCTTCCGTTGGCGGCAAAACTGCCGTGAACCACCCATTAGGGAAAAACATGATCGGCGCTTTTTATCAGCCGAATGCCGTCATCGTGGATACCTTGACCCTAAACACTTTGCCGAAACGTGAAGTGAATGCCGGCTTGGCGGAAGTCATTAAATACGGTGTGATTTTAGATTTCCCTTTCTTTGAATGGCTGGAGCAGCATATTGACGAAGTGGTCGCCCTAGATCAATCCGCGCTCCGGCAATGTATCGCCCGCTGCTGCCAATTAAAAGCGGACATTGTGGCACGGGACGAAACGGAAAAAGGCGATCGTGCGCTGTTAAATCTCGGTCATACTTTTGGTCATGCCATTGAAGCCCATTTGGGTTACGGCAACTGGCTACACGGCGAGTCGATAGCGGCAGGTTGCATGATGGCGGCGGTGTTATCGGAGCGATTAGGCGATTTAACCAAAGCCGATGTGGCGCGCTTGGAGAAACTCCTGGCAAGCGCCAATTTACCAACTGTTTCACCGGACGGCATGACGGCGCAGGATTACTTACCGTTGATGATGCGCGATAAAAAAGTGCTGAACGGTAAATTGCGTTTAGTACTGCTCAAATCTCTCGGTCGGGCTTATGTAGCAACAGATATTAATCAAGATTTAGTTATTGATGCCATCCATCGTTGCTCTCAATTCGAT","","","39408","MLCVSVELKERSYPIHIGAGLLTDPHCYPLKPGNKVMIVTNPTVAQYYLAIVTDMLEKIGCLVERVLLPDGEQYKTLDSLNLIFTALLQANHGRDTTIVALGGGVIGDVAGYAAASYQRGVRFIQIPTTLLAQVDSSVGGKTAVNHPLGKNMIGAFYQPNAVIVDTLTLNTLPKREVNAGLAEVIKYGVILDFPFFEWLEQHIDEVVALDQSALRQCIARCCQLKADIVARDETEKGDRALLNLGHTFGHAIEAHLGYGNWLHGESIAAGCMMAAVLSERLGDLTKADVARLEKLLASANLPTVSPDGMTAQDYLPLMMRDKKVLNGKLRLVLLKSLGRAYVATDINQDLVIDAIHRCSQFD","877412","","3-dehydroquinate synthase","Cytoplasm","","
InterPro
IPR002658
Domain
3-dehydroquinate synthase AroB
PF01761\"[17-325]TDHQ_synthase
TIGR01357\"[13-356]TaroB: 3-dehydroquinate synthase
noIPR
unintegrated
unintegrated
G3DSA:1.20.1090.10\"[172-344]Tno description
G3DSA:3.40.50.1970\"[8-171]Tno description
PTHR21090\"[10-361]TAROM/DEHYDROQUINATE SYNTHASE
PTHR21090:SF1\"[10-361]T3-DEHYDROQUINATE SYNTHASE


","No hits to the COGs database.","","Residues 306 to 360 match (1e-07) PD:PD592465 which is described as COMPLETE PROTEOME SYNTHASE LYASE 3-DEHYDROQUINATE AMINO ACID AROMATIC BIOSYNTHESIS ","","","","","","","","","","","","Wed Jan 8 10:06:52 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01295 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 16 to 356 (E-value = 3e-198) place AA01295 in the DHQ_synthase family which is described as 3-dehydroquinate synthase (PF01761)","","","","","Barker JL, Frost JW. Microbial synthesis of p-hydroxybenzoic acid from glucose. Biotechnol Bioeng. 2001 Dec;76(4):376-90. PMID: 11745165 Skinner MA, Gunel-Ozcan A, Shafiq M, Maskell DJ, Brown KA. Expression of recombinant aroB-encoded dehydroquinate synthasefrom pathogenic microorganisms. Biochem Soc Trans. 1998 Aug;26(3):S280. No abstract available.PMID: 9765999","","Wed Jan 8 10:06:52 2003","1","","","" "AA01296","879012","878524","489","ATGGGGGCAGGCAAAAGCACCATTGGTCGCCAACTTGCTCAGTTGCTCAACATGGATTTTGTAGATACCGACGCAGAAATTGAAGAACGCGCCGGCGCAGATATTGGCTGGATTTTTGATGTTGAGGGCGAAGCCGGTTTCCGTAAAAGAGAAGAACGTATTATTAACGAATTAACGCAACGCCAAGGCATCGTGTTATCTACCGGCGGCGGTGCAGTGTTATCTAAGGACAATCGAAACCAGCTTGCCGCGCGCGGTATTGTGATTTATCTGGAAACCACTGTTGAAAAGCAATATCAACGCACCCAGCGGGATAAAAAGCGCCCGCTTTTGCAAGATGTTGCCGATCCGCGTCAGGTGTTGGAAGATTTGGCGAAAATCCGCAATCCGCTGTATGAAGACGTAGCAGACATTACCCTCCCTACTGATGACCAAAGTGCCAAGGTAATGGCAACGCAGATTATCGACTTGATTGATAACTATAACGGT","","","19574","MGAGKSTIGRQLAQLLNMDFVDTDAEIEERAGADIGWIFDVEGEAGFRKREERIINELTQRQGIVLSTGGGAVLSKDNRNQLAARGIVIYLETTVEKQYQRTQRDKKRPLLQDVADPRQVLEDLAKIRNPLYEDVADITLPTDDQSAKVMATQIIDLIDNYNG","878524","","shikimate kinase (shikimic acid kinase I)","Cytoplasm","","
InterPro
IPR000623
Domain
Shikimate kinase
PR01100\"[19-32]T\"[47-55]T\"[65-74]T\"[86-103]TSHIKIMTKNASE
PF01202\"[1-159]TSKI
PS01128\"[48-73]TSHIKIMATE_KINASE
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[1-158]Tno description
PTHR21087\"[1-156]TSHIKIMATE KINASE


","No hits to the COGs database.","Significant hit ( 6.4e-31) to 5/5 blocks of the IPB000623 family, which is described as \"Shikimate kinase\". Interpro entry for IP:IPR000623. IPB000623A -5-24 1.5e-07 IPB000623B 43-58 1.4e-06 IPB000623C 65-79 4.2e-06 IPB000623D 106-112 0.048 IPB000623E 124-134 0.12","Residues 1 to 150 match (2e-67) PD:PD004326 which is described as KINASE SHIKIMATE COMPLETE PROTEOME TRANSFERASE ACID BIOSYNTHESIS ATP-BINDING AROMATIC AMINO ","","","","","","","","","","","","Wed Jan 8 10:08:34 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01296 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 158 (E-value = 1.1e-72) place AA01296 in the SKI family which is described as Shikimate kinase (PF01202)","","","","","Parish T, Stoker NG. The common aromatic amino acid biosynthesis pathway isessential in Mycobacterium tuberculosis. Microbiology. 2002 Oct;148(Pt 10):3069-77. PMID: 12368440 Filgueira de Azevedo W Jr, Canduri F, Simoes de Oliveira J,Basso LA, Palma MS, Pereira JH, Santos DS. Molecular model of shikimate kinase from Mycobacteriumtuberculosis. Biochem Biophys Res Commun. 2002 Jul 5;295(1):142-8. PMID: 12083781 Gu Y, Reshetnikova L, Li Y, Wu Y, Yan H, Singh S, Ji X. Crystal structure of shikimate kinase from Mycobacteriumtuberculosis reveals the dynamic role of the LID domain incatalysis. J Mol Biol. 2002 Jun 7;319(3):779-89. PMID: 12054870 Romanowski MJ, Burley SK. Crystal structure of the Escherichia coli shikimate kinase I(AroK) that confers sensitivity to mecillinam. Proteins. 2002 Jun 1;47(4):558-62. No abstract available. PMID: 12001235","","Wed Jan 8 10:08:34 2003","1","","","" "AA01297","880671","879265","1407","ATGAAATCGATCCTTTCCCGACGACTAAAGTGCGGTCTGTTTTTCGGGTGTTTTTTAAGTCTTGCGGTGCAGGCGGAACAAAATCCGGTGTTTTCCATTCGGCTGAAACAGGCACCACTGGTTCCGACTTTGCAGCAGTTGGCATTAGCCCACAATACCAATTTGATTATTGACGATGAACTGCAAGGCACGGTGTCGTTACAGTTGGAAAACGTGGATTTGGATCAGCTGTTTCGTTCTGTGGCAAAAATTAAACAACTGGATTTATGGCAGGAAAACGGCATTTATTATTTCACTAAAGGCGACACCAACACGAAATTTGCCGGCAAAATGGAAGAGCCTTTCCCTCTTTCTCTGCCCATGGCGGAAGAACCGGCACAGCTGAACACGGCGACCATTAAATTACACTTTGCCAAAGCGTCGGAAGTGATGAAATCCCTCACCGGGGGGAGTGGTTCCCTGTTGTCGCCTAACGGCAGTATCACTTTCGACGATCGTAGCAATTTGTTGCTGATTCAGGATGAACCGCGCTCCGTCCGCAACATAAAAAAGCTGATTAAGGAACTGGATAAACCCATTGAGCAAATCGCCATTGAAGCGCGCATTGTCACCATTAACGATGAAAGCCTGAAAGAACTGGGCGTGCGCTGGGGCATTTTCAGCCCGACGGACAACGCCCATCGTATCGGTGGCAGTTTGGCGGGCAACGGCTTTGATAACCTTGTCAATCAGTTAAACGTAAATTTTCCCACGACCACGACACCGGCAGGCTCTGTGGCGTTACAGGTTGCGAAAATCAACGGGCGACTTTTAGACTTAGAATTGACCGCACTTGAACGGGAAAATAATGTGGAAATCATCGCAAGCCCACGCCTGCTAACGACAAACAAAAAAAGCGCCAGCATCAAACAGGGGACGGAATTGCCCTATATTCTGGTGAACGAAAAAAGCGGTTCGCAAAGCGTGGAATTTCGTGAGGCGGTACTAGGTTTGGAAGTCACGCCGCACATTTCGCAGGATAAACAAATTCTGTTAGATCTTATCGTCAGCCAAAACTCGCCGGGCAGCCGTGTGGCGTACGGTTTGGGCGAAGTGGTTTCTATTGATAAACAGGAGATTAATACACAAGTCTTCGCCAAGGACGGCGAAACCATTGTGCTGGGCGGTGTATTTAGCGATACCATCACCAAAGGCACCGATAAAGTGCCGGTGCTGGGTGACATTCCGGGTATTAAACATTTATTCAGCAAGGAAAGTGAACGCCATCAAAAACGCGAGCTGGTGATTTTTGTCACACCACATATTTTGCGTAAAGGCGAAACCCCGGACGCTTTCAAACAAAAGCGAATCGGGGTAAATGAGCAAATCATGGCAAAAGGGGAGAATAAAAAGGACCTAAATAGGAAA","","","51723","MKSILSRRLKCGLFFGCFLSLAVQAEQNPVFSIRLKQAPLVPTLQQLALAHNTNLIIDDELQGTVSLQLENVDLDQLFRSVAKIKQLDLWQENGIYYFTKGDTNTKFAGKMEEPFPLSLPMAEEPAQLNTATIKLHFAKASEVMKSLTGGSGSLLSPNGSITFDDRSNLLLIQDEPRSVRNIKKLIKELDKPIEQIAIEARIVTINDESLKELGVRWGIFSPTDNAHRIGGSLAGNGFDNLVNQLNVNFPTTTTPAGSVALQVAKINGRLLDLELTALERENNVEIIASPRLLTTNKKSASIKQGTELPYILVNEKSGSQSVEFREAVLGLEVTPHISQDKQILLDLIVSQNSPGSRVAYGLGEVVSIDKQEINTQVFAKDGETIVLGGVFSDTITKGTDKVPVLGDIPGIKHLFSKESERHQKRELVIFVTPHILRKGETPDAFKQKRIGVNEQIMAKGENKKDLNRK","879265","","competence protein E precursor","Outer membrane, Periplasm, Cytoplasm","","
InterPro
IPR001775
Domain
Bacterial general secretion pathway protein D
PR00811\"[195-205]T\"[273-297]T\"[401-419]T\"[424-438]TBCTERIALGSPD
InterPro
IPR001814
Family
Filamentous bacteriophage Vg4 protein
PR01032\"[257-280]T\"[298-321]T\"[364-392]T\"[417-439]TPHAGEIV
InterPro
IPR003833
Domain
Allophanate hydrolase subunit 1
SM00796\"[127-271]Tno description
InterPro
IPR004846
Domain
Bacterial type II and III secretion system protein
PF00263\"[197-437]TSecretin
InterPro
IPR005644
Domain
NolW-like
PF03958\"[130-195]TSecretin_N
InterPro
IPR013355
Family
Type IV pilus secretin PilQ
TIGR02515\"[28-437]TIV_pilus_PilQ: type IV pilus secretin PilQ
noIPR
unintegrated
unintegrated
signalp\"[1-25]?signal-peptide


","No hits to the COGs database.","Significant hit ( 1.5e-51) to 3/3 blocks of the IPB000016 family, which is described as \"General (type II) secretion pathway (GSP) D protein\". Interpro entry for IP:IPR000016. IPB000016A 186-217 6.5e-14 IPB000016B 275-310 8e-14 IPB000016C 375-416 4e-21Significant hit ( 2.1e-05) to 2/8 blocks of the PR01337 family, which is described as \"Type III secretion system outer membrane G protein family signature\". Prints database entry for PR:PR01337. PR01337E 197-217 0.00025 PR01337H 415-434 42","Residues 382 to 437 match (5e-07) PD:PD525573 which is described as PROTEOME COMPLETE PROBABLE PLASMID II SYSTEM TYPE SECRETION MSHL HEMAGGLUTININ ","","","","","","","","","","","","Tue Jan 21 10:11:53 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01297 is paralogously related to AA00871 (2e-18).","","","","","","Residues 197 to 437 (E-value = 1.3e-87) place AA01297 in the Secretin_C family which is described as Bacterial type II and III secretion system protein (PF00263)","","","","","Ween O, Teigen S, Gaustad P, Kilian M, Havarstein LS.Competence without a competence pheromone in a natural isolate of Streptococcus infantis.J Bacteriol. 2002 Jul;184(13):3426-32. PMID: 12057935 Chen I, Gotschlich EC.ComE, a competence protein from Neisseria gonorrhoeae with DNA-binding activity.J Bacteriol. 2001 May;183(10):3160-8.PMID: 11325945 Busch S, Rosenplanter C, Averhoff B.Identification and characterization of ComE and ComF, two novel pilin-like competence factors involved in natural transformation of Acinetobacter sp. strain BD413.Appl Environ Microbiol. 1999 Oct;65(10):4568-74.PMID: 10508090 ","","Wed Jan 8 10:23:57 2003","1","","","" "AA01298","881083","880694","390","ATGTTACACCCTCTTTTCGTTTTCTTTATCGGCGTGTTGTTCAGCTTGTCTGTCACCGCTAATGATCCTTTTGACAAAACCCAACGCGGAACCACCGCCTCGAACGCATCACTCAAAGACACCACAAGCGTAATCCAGTGCTATAAAGGGACGGAGGCGATTTTTCCGTCCACCGCATTTAATCAAATCCGCATAGTGGGCGTGCTGCAGCACCAAAAAGATTGGCAATTACTCTTGCTTGCCGACAACCAAGTGAACCTCGCCCAACAAGGGGATTTTGTTGCGGCGGAAAATCTGAAAATTGAACACATCGGTAAACAGGAAATTCGTTTTTTACGTTGGGATAACCCGCAAAATTGCGAGCTTTCCACTACATTGAACATAAAATTT","","","14667","MLHPLFVFFIGVLFSLSVTANDPFDKTQRGTTASNASLKDTTSVIQCYKGTEAIFPSTAFNQIRIVGVLQHQKDWQLLLLADNQVNLAQQGDFVAAENLKIEHIGKQEIRFLRWDNPQNCELSTTLNIKF","880694","","competence protein D","Cytoplasm, Periplasm","","
InterPro
IPR010916
Domain
TonB box, N-terminal
PS00430\"[1-21]?TONB_DEPENDENT_REC_1
noIPR
unintegrated
unintegrated
signalp\"[1-20]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","","Residues 7 to 130 match (2e-10) PD:PD396233 which is described as PROTEOME COMD COMPLETE ","","","","","","","","","","","","Tue Jan 21 10:13:19 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01298 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Ween O, Teigen S, Gaustad P, Kilian M, Havarstein LS.Competence without a competence pheromone in a natural isolate of Streptococcus infantis.J Bacteriol. 2002 Jul;184(13):3426-32.PMID: 12057935 JH, Ellen RP, Cvitkovitch DG. A quorum-sensing signaling system essential for genetic competence in Streptococcus mutans is involved in biofilm formation.J Bacteriol. 2002 May;184(10):2699-708.PMID: 11976299","","Wed Jan 8 10:44:52 2003","1","","","" "AA01299","881562","881086","477","TTGACGAGTTGGCAACAAAGGGCATTGCTGATTTTTGTATGTTTATTGGCGCTCTATTTTCCCACATGGGATTATTGGCAACAGCGTTCCCAGGCGGAAGCGATTTCACAACAATTGCAAATCCAACAGGAAAAGCTTGCTCATCAGCAAAAAATCTTAGCCGCGCTGAAAGAAAAAGCGGCGAAGCAATTACTCACACCGGAATTAGCGGGCAAACTCCCGCCGATAAATCAGCAGATTCAACAATTTGCATCGAAATTGCACATTGCGCACAGCCAATGGGATTTTCATCAAAAACCGTTGCTCAAATTGCAACTGCACGGACAGTTTACCGATTTACGGGAATTTTTGACCGCACTTTTCAGTGCTAATGACGAGCTGGAATTACTGGAATGGCACATTATTAAAAACGCCGATACCAATGACGGGCATTCTATTCACAGCGAACTTTTATTTCAATTACATACCAAGGAAAAA","","","20432","LTSWQQRALLIFVCLLALYFPTWDYWQQRSQAEAISQQLQIQQEKLAHQQKILAALKEKAAKQLLTPELAGKLPPINQQIQQFASKLHIAHSQWDFHQKPLLKLQLHGQFTDLREFLTALFSANDELELLEWHIIKNADTNDGHSIHSELLFQLHTKEK","881086","","competence protein C","Cytoplasm, Periplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-24]?signal-peptide
tmhmm\"[9-27]?transmembrane_regions


","No hits to the COGs database.","","Residues 12 to 154 match (1e-09) PD:PD415499 which is described as COMC COMPLETE PROTEOME C DNA TRANSFORMATION COMPETENCE ","","","","","","","","","","","","Tue Jan 21 10:15:17 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01299 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Ween O, Teigen S, Gaustad P, Kilian M, Havarstein LS.Competence without a competence pheromone in a natural isolate of Streptococcus infantis.J Bacteriol. 2002 Jul;184(13):3426-32.PMID: 12057935 [PubMed - indexed for MEDLINE] Echenique JR, Trombe MC.Competence modulation by the NADH oxidase of Streptococcus pneumoniae involves signal transduction.J Bacteriol. 2001 Jan;183(2):768-72.PMID: 11133974 Hakenbeck R.Transformation in Streptococcus pneumoniae: mosaic genes and the regulation of competence.Res Microbiol. 2000 Jul-Aug;151(6):453-6. Review.PMID: 10961458 Link C, Eickernjager S, Porstendorfer D, Averhoff B.Identification and characterization of a novel competence gene, comC, required for DNA binding and uptake in Acinetobacter sp. strain BD413.J Bacteriol. 1998 Mar;180(6):1592-5.PMID: 9515934 ","","Wed Jan 8 10:53:12 2003","1","","","" "AA01301","882155","881607","549","TTGACGCCGACCACAACATTTGAGACGATTACCATGAAAAAAGACATCAATCTCCTGCCGTGGCGCATTCAATTGCAACGTCAACAGAATAAAGCGTTACTTCATCAACTTATCCTTTGCGCGTTGATATGCACAAGCGGCTGGTTAATTCTGGGGTCTTTGGCGGAAAGCCACGCGGAAACCGCAGAAACAATACAAACCGAACTGACCAAAATCCAACCTGAGCAACAGCTTACACAACGACACATTCAACAATTCCGAAGTACACAGACAGATTCGGAGGAATTACACCCCGTTTCAAAAGAAACTGTTTTTTCGCTGTTAAATCAATTAACAGAGTTACCGCTCACACAAGGTGAATTAACGGAATTGTCTCTTAAAACAGCGCAACTAACCTTAACCGGCTACAGCCACAGTCAAGAAGAATTCAGCCGGTTGAATCAATTTCTCACGCAACAACCACTTTTCGCCGAAGTCACACTAGCGGAGTTCAAACCGAATGCCGACGAACTGCAGTTTCAATTTAACTTAACCTTGCGGGACACGCCA","","","20946","LTPTTTFETITMKKDINLLPWRIQLQRQQNKALLHQLILCALICTSGWLILGSLAESHAETAETIQTELTKIQPEQQLTQRHIQQFRSTQTDSEELHPVSKETVFSLLNQLTELPLTQGELTELSLKTAQLTLTGYSHSQEEFSRLNQFLTQQPLFAEVTLAEFKPNADELQFQFNLTLRDTP","881607","","competence protein B","Cytoplasm","","
InterPro
IPR007813
Family
Fimbrial assembly
PF05137\"[16-171]TPilN
noIPR
unintegrated
unintegrated
signalp\"[1-47]?signal-peptide
tmhmm\"[32-52]?transmembrane_regions


","No hits to the COGs database.","","Residues 16 to 173 match (2e-09) PD:PD097629 which is described as COMB COMPLETE PROTEOME B DNA TRANSFORMATION COMPETENCE ","","","","","","","","","","","","Tue Jan 21 10:15:59 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01301 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 16 to 171 (E-value = 8.7e-05) place AA01301 in the PilN family which is described as Fimbrial assembly protein (PilN) (PF05137)","","","","","Smeets LC, Kusters JG.Natural transformation in Helicobacter pylori: DNA transport in an unexpected way.Trends Microbiol. 2002 Apr;10(4):159-62; discussion 162.PMID: 1191201Petersen FC, Scheie AA.Genetic transformation in Streptococcus mutans requires a peptide secretion-like apparatus.Oral Microbiol Immunol. 2000 Oct;15(5):329-34.PMID: 111544267: Herzberg C, Friedrich A, Averhoff B.comB, a novel competence gene required for natural transformation of Acinetobacter sp.BD413: identification, characterization, and analysis of growth-phase-dependent regulation.Arch Microbiol. 2000 Mar;173(3):220-8.PMID: 10763755Havarstein LS.Identification of a competence regulon in Streptococcus pneumoniae by genomic analysis.Trends Microbiol. 1998 Aug;6(8):297-9; discussion 299-300. Review. No abstract available.PMID: 974693","","Wed Jan 8 11:08:04 2003","1","","","" "AA01303","882942","882136","807","ATGTTTATTAGACACATTCCCACACTGCAAGTCGGTCTTTGGTGCCGTGGAGAAACCATCGACGCAGCGTGGATCGACCCGCAAAATCAACCGCACTTTTTGCGCCTCGGCGAACTGGAATTAATGGAACTGACAAGCCATTTAAACCGTCGTTTTAACCATCCGCGCAAAAAATTAGCCTACAAATTTATTACCGCCATCATGCCCCATCAAATCTGGCAGAAAACCTTGATTTTGCCCCATAACCTGAACCTTCAGGAATGTGAGCAACAGTGCCATTTCAGCTTAACCAACGAGCTGCCGATTCCCACCGAAGAGGTGTGGTATGACTACGCAGCCACACCGTTAAAACAGGGCTTTCGGTTAGATATTTTTGCCATTAGACAACAAATCGCCACAGAATATTTGCAACAACTTATGCCTTTACAAATTGACGTGTTAGACAACGCGGCAAAAGCGATGTTACGCGCGGCGGAATATTTTTTGGGGCACGCCTTGCCAAATAACGCCGTGTTTTTATATCAGGACGAAACGGGCTTGCTGGCGGTACAACACAAATTACAGCAAACCCAAACGCTGTTCCAAACGCAGGGAAACCTGACCGCACTTTTGGCGCAATATTGCCAACGTTATGCAGAAGAACCGATGCAGGTGTTCTATTATCAAACCGAAAAAGACGCACAGGCGATACCGCAAAGCTGGCACGCCATTGAAACCGAGCTACCGTTCATCGCGTTAGGTAACGCCTTGTGGCAACGGGAAACGCCGTTGAAATCCACCGCACTTTTTGACGCCGACCACAACATT","","","31655","MFIRHIPTLQVGLWCRGETIDAAWIDPQNQPHFLRLGELELMELTSHLNRRFNHPRKKLAYKFITAIMPHQIWQKTLILPHNLNLQECEQQCHFSLTNELPIPTEEVWYDYAATPLKQGFRLDIFAIRQQIATEYLQQLMPLQIDVLDNAAKAMLRAAEYFLGHALPNNAVFLYQDETGLLAVQHKLQQTQTLFQTQGNLTALLAQYCQRYAEEPMQVFYYQTEKDAQAIPQSWHAIETELPFIALGNALWQRETPLKSTALFDADHNI","882136","","competence protein A","Cytoplasm","","
noIPR
unintegrated
unintegrated
PD123385\"[9-251]TQ9CLJ9_PASMU_Q9CLJ9;


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Jan 8 11:32:18 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01303 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Graupner S, Wackernagel W.Identification and characterization of novel competence genes comA and exbB involved in natural genetic transformation of Pseudomonas stutzeri.Res Microbiol. 2001 Jun;152(5):451-60.PMID: 11446513Kim SB, Shin BS, Choi SK, Kim CK, Park SH.Involvement of acetyl phosphate in the in vivo activation of the response regulator ComA in Bacillus subtilis.FEMS Microbiol Lett. 2001 Feb 20;195(2):179-83.PMID: 1117964912: Petersen FC, Scheie AA.Genetic transformation in Streptococcus mutans requires a peptide secretion-like apparatus.Oral Microbiol Immunol. 2000 Oct;15(5):329-34.PMID: 11154426Havarstein LS.Identification of a competence regulon in Streptococcus pneumoniae by genomic analysis.Trends Microbiol. 1998 Aug;6(8):297-9; discussion 299-300. Review. No abstract available.PMID: 9746937 ","","Tue Jan 21 10:16:59 2003","1","","","" "AA01304","883076","885640","2565","ATGCGGATCGCAAAATTAATATTAAGTTCCTTATTAACTTTATTTATTCTTGGCGGCATTGTGGCGGGTATGTTCTATATCCAGCTCAAATCCGATTTACCGGATGTGGAAACGCTGAAAACCGTTGAGCTGCAACAGCCGATGCAAATTTACACTTCCGACGGCAAACTTATCGGGGAAGTAGGGGAGCAACGCCGAATTCCGGTGAAACTGGCGGATATTCCGGAAAAACTCATTCAAGCCGTGTTGGCAACGGAAGACAGCCGTTTCTATGAACACCACGGGCTGGATCCGATCGGCATCGGGCGTGCGTTAATGGTTGCCGTGACCAAAGGCGGCGCGTCTCAAGGGGCAAGTACCATCACCCAACAGTTGGCGCGTAACTTCTTCTTAACGCCGGAAAAAAGCCTGATCCGTAAAGCCAAAGAAGCGATTTTGGCAATTGATATTGAAAATGCGTTGGATAAAAACGAAATTCTCGAACTGTATTTAAATAAAATTTACTTGGGCTACCGTTCTTATGGTGTCGCGGCGGCGGCAAAAACCTATTTTGGTAAAGAATTGAATCAATTAACCCTATCCGAAATGGCGGTGATTGCGGGCTTGCCGAAAGCGCCTTCCACAATGAATCCGCTGTTTTCGCCGAAACGTGCGCTGGAGCGCCGTAATGTGGTGTTGGGGCGTATGTTGGACCAAAAATACATTTCCAAAGAAGAATATGATGCGGCATTAAAAGCGCCGATTGTCGCCAGTTATCACGGGGCGCAAATGGATTTCCGTGCGGATTATGTGACGGAAATGGTGCGTCAGGAAATGGTGAGACGCTTTGGTGAGGAAAATGCCTATACCAAAGGTTACAAAGTTTACACCACTGTGCTTTCCAAAGATCAGGAAACCGCACAAAAAGCGGTACGTGATAACTTAATCGCTTACGATATGCGCCATGGTTATCGTGGCGGCGCGCCTTTATGGAAAAAAGACGAAGCGCCTTGGGACAACGACACCATTATCGGTTTCCTGAAAAAATTACCGAATTCCGAACCCTTCATTCCGGCGGCGGCAGTCGGCGTTGCCAAATCCGGCGCGGAGCTCCTACTGGCTTCCGGTGATAAAATTACGCTGCCGAGCAGCGCAATGCGTTGGACAGGGCAAGCTAATCCGGTGAAAGTGGGTGATCAAATCTGGATTCGTAAAAATGACAAAGGTGGCTGGATGCTGGGGCAAATCCCGCAGGCCAACTCCGCTTTGGTTTCCTTAAACAGCGACAACGGCGCTATTGAAGCCATTGTGGGCGGTTTCAGTTTTGAACAAAGCAAATTTAACCGCGCCACTCAATCTTTGGTGCAAGTGGGTTCTTCCATTAAACCGTTTATTTATGCGGCAGCATTGGAAAAAGGGTTAACCTTATCCAGCGTGTTGCAGGATATGCCGATTGTGCTGAAAAAACCGGGACAGAAAGAATGGCGTCCGAAAAACTCGCCGGATCGTTATGACGGTCCGTTGCGTTTGCGCGTGGGATTAGGTCAGTCTAAAAATATGATTGCCATTCGCTCCATGCAAATGGCGGGCATTGATTTCGTGGCAGATTTCTTACAACGTTTCGGTTTCAAACGGGATCAATATTTTGCCAGCGAAGCCCTTGCTTTGGGCGCGGCATCCTTCACGCCGTTAGAAATGGCACGCGGTTATGCGGTGTTTGATAACGGCGGTTATTTGGTCGATCCTTATATTATCAATAAAATTTTAGATAATAGCGGTAAAGAAATTTTCGTGGCGAACCCGAAAGTAGCGTGCCCGACCTGCGACAATATTCCGGTGATTTACGGCGAAACGGAAAAATTGGACGGCTTTAAAAATACCGACTTAACGCCGGCTGACGAATTTGCCCGCACCGATGAATCTACTAACGGCGAAGAAGTAGACCAAGGCGAAAGCGTGCCGGATATTCCGGAATTGCAACCGCGTGTCGATGTGGTGAAAGAGGAAAATCTGAACCTCATGGCGGATGCAAAAACCAATGGTTCCGAAGTGCAATATGCACCACGTGTGATTAGCGGTGAATTAGCGTTCTTAATTCGTAGTGCGTTAAGTACCGCAATTTACGGCGAACAGGGGCTTGGCTGGAAAGGTACCAGCTGGCGCATGGCAAATGACATTAAACGTAAAGACATCGGCGGCAAAACCGGTACGACGAATAACTCCAAAGTGGCGTGGTATGCCGGCTTCGGGGCAAATCTGACTACGGCGGTGTATATCGGTTTTGACGATAATCGCTTTAATTTAGGTCGCGGTGAAGCCGGTGCGAAAAGTGCGATGCCGGCGTGGATTGCTTATATGAAGCCGATCTTGCAGGATATTCCGGAACGTGCATTGCCGATGCCTGCCAATATCGTAGAAAAACACATTGATTTACGCTCCGGCTTACTGGCTAACGATGGGCGCGTGGAATATTTCATTAAAGGAACGGAACCAACCCGTGCTTATGTGGAAGAACGCGGCTACTATGTACCAAGCGAACTTCTCGATGGCGACAGTTCACCGGGCGGTCAACCGGAAGAATTGTTC","","","94109","MRIAKLILSSLLTLFILGGIVAGMFYIQLKSDLPDVETLKTVELQQPMQIYTSDGKLIGEVGEQRRIPVKLADIPEKLIQAVLATEDSRFYEHHGLDPIGIGRALMVAVTKGGASQGASTITQQLARNFFLTPEKSLIRKAKEAILAIDIENALDKNEILELYLNKIYLGYRSYGVAAAAKTYFGKELNQLTLSEMAVIAGLPKAPSTMNPLFSPKRALERRNVVLGRMLDQKYISKEEYDAALKAPIVASYHGAQMDFRADYVTEMVRQEMVRRFGEENAYTKGYKVYTTVLSKDQETAQKAVRDNLIAYDMRHGYRGGAPLWKKDEAPWDNDTIIGFLKKLPNSEPFIPAAAVGVAKSGAELLLASGDKITLPSSAMRWTGQANPVKVGDQIWIRKNDKGGWMLGQIPQANSALVSLNSDNGAIEAIVGGFSFEQSKFNRATQSLVQVGSSIKPFIYAAALEKGLTLSSVLQDMPIVLKKPGQKEWRPKNSPDRYDGPLRLRVGLGQSKNMIAIRSMQMAGIDFVADFLQRFGFKRDQYFASEALALGAASFTPLEMARGYAVFDNGGYLVDPYIINKILDNSGKEIFVANPKVACPTCDNIPVIYGETEKLDGFKNTDLTPADEFARTDESTNGEEVDQGESVPDIPELQPRVDVVKEENLNLMADAKTNGSEVQYAPRVISGELAFLIRSALSTAIYGEQGLGWKGTSWRMANDIKRKDIGGKTGTTNNSKVAWYAGFGANLTTAVYIGFDDNRFNLGRGEAGAKSAMPAWIAYMKPILQDIPERALPMPANIVEKHIDLRSGLLANDGRVEYFIKGTEPTRAYVEERGYYVPSELLDGDSSPGGQPEELF","885640","From Genbank:[gi:1172033] This protein is involved in cell wall formation and in the synthesis of cross-linked peptidoglycan from the lipid intermediates. This enzyme has a penicillin-insensitive transglycosylase N-terminal domain and a penicillin-sensitive transpeptidase C-terminal domain. ","penicillin-binding protein 1A","Inner membrane, Periplasm, Cytoplasm","","
InterPro
IPR001264
Domain
Glycosyl transferase, family 51
PD001895\"[136-186]TPBPA_HAEIN_P31776;
PF00912\"[48-215]TTransgly
InterPro
IPR001460
Domain
Penicillin-binding protein, transpeptidase
PF00905\"[414-780]TTranspeptidase
InterPro
IPR011816
Domain
Penicillin-binding protein 1A
TIGR02074\"[65-785]TPBP_1a_fam: penicillin-binding protein, 1A
noIPR
unintegrated
unintegrated
G3DSA:3.40.710.10\"[411-779]Tno description
signalp\"[1-22]?signal-peptide
tmhmm\"[7-27]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 7e-68) to 3/3 blocks of the IPB001264 family, which is described as \"Glycosyltransferase family 51\". Interpro entry for IP:IPR001264. IPB001264A 69-108 2.3e-22 IPB001264B 117-169 3.8e-30 IPB001264C 174-200 7e-13Significant hit ( 2.1e-07) to 2/3 blocks of the IPB001460 family, which is described as \"Penicillin binding protein transpeptidase domain\". Interpro entry for IP:IPR001460. IPB001460B 467-475 1.2e+02 IPB001460C 555-570 7.4e-07","Residues 724 to 803 match (2e-07) PD:PD041950 which is described as PENICILLIN-BINDING COMPLETE PROTEOME 1B PEPTIDOGLYCAN 2.4.2.- PBP1B TRANSPEPTIDASE TGASE POLYMERASE ","","","","","","","","","","","Wed Jan 15 07:55:15 2003","Wed Jan 8 12:21:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01304 is paralogously related to AA02432 (2e-44), AA01690 (1e-18), AA00780 (1e-17) and AA00258 (2e-05).","","","","","","Residues 414 to 780 (E-value = 4.1e-07) place AA01304 in the Transpeptidase family which is described as Penicillin binding protein transpeptidase domain (PF00905)","","","","","Broome-Smith,J.K., Edelman,A., Yousif,S. and Spratt,B.G. The nucleotide sequences of the ponA and ponB genes encoding penicillin-binding protein 1A and 1B of Escherichia coli K12 Eur. J. Biochem. 147 (2), 437-446 (1985) PubMed: 3882429 Ropp PA, Hu M, Olesky M, Nicholas RA. Mutations in ponA, the gene encoding penicillin-bindingprotein 1, and a novel locus, penC, are required forhigh-level chromosomally mediated penicillin resistance inNeisseria gonorrhoeae. Antimicrob Agents Chemother. 2002 Mar;46(3):769-77. PMID: 11850260 Ropp PA, Nicholas RA. Cloning and characterization of the ponA gene encodingpenicillin-binding protein 1 from Neisseria gonorrhoeae andNeisseria meningitidis. J Bacteriol. 1997 Apr;179(8):2783-7. PMID: 9098083 ","","Wed Jan 8 12:21:40 2003","1","","","" "AA01305","885738","886580","843","ATGCTCAGTTATCGTCATAGTTTTCATGCGGGCAATCATGCGGATGTGTTGAAGCACATTGTGTTAATGCTGATTATCGAAAGCCTGCAACAAAAAGAAAAAGGGTTTTATTATTTAGATACGCATTCCGGTGCGGGGCGTTATCGCTTGCTTAGTGCGGAAGCGGAGAAAACGGCGGAATATGTGGACGGCATTGGTCGTTTGTGGGCGCGTGAGGACTTGCCCGCAGAAGTGGCACGTTATGTGGCGTTAATTAAAAAGCTCAATTATAGCGGCAAGGAATTGCGCTATTATGCGGGTTCGCCGTTGTTGGCGGCGAATTTATTGCGTCCGCAGGATCGTGCGTTGCTGGTGGAACTTCATCCGAGCGAGTTTCCGCTGTTACGCAATAATTTTAAAGAATTTGATAATGTGACGGTAAAAATCGGTGACGGTTTTCAACAGGTCAAAGTCACCCTGCCGCCAAAAGAGCGGCGAGGGCTGGTGTTGATTGATCCGCCATATGAGTTAAAAGAAGATTACGATTTGGTGGTGAAAGCCGTTGAAGAGGGCTATAAGCGCTTTGCTACGGGCATTTATGTTATTTGGTATCCGGTGGTGCTGCGTCAGCAAACCAAGCGGATAGTGAAAGGTTTGGAAGCCACGGGGATTCGTAAAATCCTGCAAATCGAACTGGCAGTGCGCCCGGATTCCGATCAACGCGGGATGACGGCGAGCGGGATGATTGTGGTGAATCCGCCTTGGACGCTGGAGCAACAAATGAAATCCATTTTACCTTATTTAACCACCGCACTTATACCGCAAGGTACCGGTAGTTGGTCGGTAAATTGGATTACGCCGGAA","","","31995","MLSYRHSFHAGNHADVLKHIVLMLIIESLQQKEKGFYYLDTHSGAGRYRLLSAEAEKTAEYVDGIGRLWAREDLPAEVARYVALIKKLNYSGKELRYYAGSPLLAANLLRPQDRALLVELHPSEFPLLRNNFKEFDNVTVKIGDGFQQVKVTLPPKERRGLVLIDPPYELKEDYDLVVKAVEEGYKRFATGIYVIWYPVVLRQQTKRIVKGLEATGIRKILQIELAVRPDSDQRGMTASGMIVVNPPWTLEQQMKSILPYLTTALIPQGTGSWSVNWITPE","886580","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR002052
Domain
N-6 Adenine-specific DNA methylase
PS00092\"[162-168]?\"[242-248]?N6_MTASE
InterPro
IPR007473
Family
Protein of unknown function DUF519
PF04378\"[33-279]TDUF519


","BeTs to 6 clades of COG2961COG name: Protein involved in catabolism of external DNAFunctional Class: RThe phylogenetic pattern of COG2961 is --------------efghsn-j----Number of proteins in this genome belonging to this COG is","","Residues 159 to 265 match (1e-18) PD:PD473786 which is described as PROTEOME COMPLETE RSC3368 NMA1260 CC1096 NMB1061 XF0043 ","","","","","","","","","","","","Wed Jan 8 12:30:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01305 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 33 to 279 (E-value = 1.3e-152) place AA01305 in the DUF519 family which is described as Protein of unknown function (DUF519) (PF04378)","","","","","","","","1","","","" "AA01306","886678","888045","1368","ATGAGCAGACATTATGATTACCTTGCTATCGGCGGTGGTAGCGGCGGTATTGCCTCCATTAACCGCGCGGCGAGTTATGGCAAAAAATGTGCCATTATTGAGGCGAAACATTTGGGCGGAACCTGTGTAAATGTGGGTTGTGTACCGAAAAAAGTGATGTTTTACGGCGCACAAATTGCGGAAGCGATTAATCATTATGCACTAGATTACGGTTTTGATGTGGAGGTAAAAAAATTTGATTTCGCCAAGTTGGTGGAAAGCCGTCAAGCCTACATTGATCGTATTCATACTTCTTATAACAATGTATTGGCGAAAAATAACGTCGATGTGATTCACGGCTTCGCTAAATTTGTGAATAAAAACACCGTTGAAGTGACCCTTGCAGACGGTTCCACCGAACAAGTGACCGCTGACCATATTTTAATCGCGACCGGTGGTCGTCCGAGCCATCCGCCGGTAAAAGGCGTGGAATACGGCATTGATTCTGATAGGGTATTTGCTTTGAATGCGCTACCAAAACGCGTTGCCATTATCGGGGCGGGTTATATCGCGGTGGAACTTGCCGGCGTATTCAATAGTTTAGGTTCCGACACTCACTTGGTAGTGCGTCGTCACGCGCCGATGCGTAATCAGGATCCGTTGATCGTTGAAACGCTGGTGGAAGTGTTGGAGCAAGACGGCATTCATTTGCATAAACACACCACGGTGCAAGAAGTCATCAAAAATGCAGATGGATCTTTAACCGTGAAATTCGATCACGATGGAGAAATTATCGTAGATTGTTTGGTTTGGACAATCGGGCGTGATCCGGCAACGGATAAAATCGGTTTGGAAAACATCGGCGTGGAAACCAACGATCGCGGTTTCATTAAAGTGGATAAATATCAAAATACCAATGTACCCGGCATTTACGCAGTGGGCGATATTATTGACGGCGGTATCGAATTAACACCGGTTGCCGTTGCCGCCGGGCGTCGTTTATCCGAGCGTTTGTTCAATAATAAACCAAACGAGTATTTGGATTACAACCTTGTGCCGACAGTGGTATTCAGCCACCCGCCAATCGGCACCGTAGGTTTAACGGAACCGCAAGCTATTGAACAATACGGCGCGGAAAACGTGAAAGTGTATAAATCCAGCTTCACCCCGATGTACAGCGCAGTGACCCAACGCCGCCAACCTTGTCGCATGAAATTGGTTTGCGCGGGTAAAGAAGAGAAAATCGTCGGCTTGCACGGCATCGGCTTCGGTGTGGACGAAATGATCCAAGGCTTTGCTGTCGCCATCAAAATGGGTGCCACCAAAGCCGATTTCGACAACACCGTGGCAATCCACCCGACAGGTTCGGAAGAGTTTGTAACGATGCGT","","","49599","MSRHYDYLAIGGGSGGIASINRAASYGKKCAIIEAKHLGGTCVNVGCVPKKVMFYGAQIAEAINHYALDYGFDVEVKKFDFAKLVESRQAYIDRIHTSYNNVLAKNNVDVIHGFAKFVNKNTVEVTLADGSTEQVTADHILIATGGRPSHPPVKGVEYGIDSDRVFALNALPKRVAIIGAGYIAVELAGVFNSLGSDTHLVVRRHAPMRNQDPLIVETLVEVLEQDGIHLHKHTTVQEVIKNADGSLTVKFDHDGEIIVDCLVWTIGRDPATDKIGLENIGVETNDRGFIKVDKYQNTNVPGIYAVGDIIDGGIELTPVAVAAGRRLSERLFNNKPNEYLDYNLVPTVVFSHPPIGTVGLTEPQAIEQYGAENVKVYKSSFTPMYSAVTQRRQPCRMKLVCAGKEEKIVGLHGIGFGVDEMIQGFAVAIKMGATKADFDNTVAIHPTGSEEFVTMR","888045","","glutathione reductase","Cytoplasm","","
InterPro
IPR000815
Family
Mercuric reductase
PR00945\"[16-34]T\"[174-191]T\"[194-209]THGRDTASE
InterPro
IPR001100
Family
Pyridine nucleotide-disulphide oxidoreductase, class I
PR00411\"[6-28]T\"[38-53]T\"[140-149]T\"[174-199]T\"[260-274]T\"[303-310]T\"[341-362]T\"[408-423]T\"[430-450]TPNDRDTASEI
InterPro
IPR001327
Domain
Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PD000139\"[144-212]TGSHR_HAEIN_P43783;
PF00070\"[174-267]TPyr_redox
InterPro
IPR004099
Domain
Pyridine nucleotide-disulphide oxidoreductase dimerisation region
G3DSA:3.30.390.30\"[345-456]Tno description
PF02852\"[345-456]TPyr_redox_dim
InterPro
IPR006322
Family
Glutathione reductase, animal and bacterial
TIGR01421\"[3-456]Tgluta_reduc_1: glutathione-disulfide reduct
InterPro
IPR012999
Active_site
Pyridine nucleotide-disulphide oxidoreductase, class I, active site
PS00076\"[39-49]TPYRIDINE_REDOX_1
InterPro
IPR013027
Domain
FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PR00368\"[6-28]T\"[140-149]T\"[174-199]T\"[260-274]T\"[303-310]TFADPNR
PF07992\"[6-314]TPyr_redox_2
noIPR
unintegrated
unintegrated
G3DSA:3.50.50.60\"[2-336]Tno description
PTHR22912\"[8-456]TDISULFIDE OXIDOREDUCTASE
PTHR22912:SF27\"[8-456]TGLUTATHIONE REDUCTASE


","No hits to the COGs database.","Significant hit ( 1.4e-32) to 5/5 blocks of the PR00368 family, which is described as \"FAD-dependent pyridine nucleotide reductase signature\". Prints database entry for PR:PR00368. PR00368A 6-28 2.3e-06 PR00368B 140-149 0.029 PR00368C 174-199 4.4e-12 PR00368D 260-274 0.0023 PR00368E 303-310 0.12Significant hit ( 4.8e-12) to 5/5 blocks of the IPB000103 family, which is described as \"Pyridine nucleotide-disulphide oxidoreductase class-II\". Interpro entry for IP:IPR000103. IPB000103A 6-26 0.69 IPB000103B 39-53 58 IPB000103C 163-211 1.5e+02 IPB000103D 261-272 1.4e+02 IPB000103E 298-335 4.8e-07Significant hit ( 5.9e-10) to 1/1 blocks of the IPB001100 family, which is described as \"Pyridine nucleotide-disulphide oxidoreductase, class I\". Interpro entry for IP:IPR001100. IPB001100 39-53 6e-10","Residues 366 to 428 match (1e-06) PD:PD461502 which is described as FAD FLAVOPROTEIN OXIDOREDUCTASE THIOREDOXIN REDUCTASE REDOX-ACTIVE CENTER NADP GLUTATHIONE GR ","","","","","","","","","","","","Wed Jan 8 12:32:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01306 is paralogously related to AA01988 (4e-43), AA02604 (3e-11) and AA02023 (3e-05).","","","","","","Residues 345 to 456 (E-value = 1.8e-55) place AA01306 in the Pyr_redox_dim family which is described as Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain (PF02852)","","","","","Greer,S. and Perham,R.N. Glutathione reductase from Escherichia coli: cloning andsequence analysis of the gene and relationship to other flavoprotein disulfide oxidoreductases Biochemistry 25 (9), 2736-2742 (1986) PubMed: 3521741 Ermler,U. and Schulz,G.E. The three-dimensional structure of glutathione reductase from Escherichia coli at 3.0 A resolution Proteins 9 (3), 174-179 (1991) PubMed: 2006135 Mittl,P.R. and Schulz,G.E. Structure of glutathione reductase from Escherichia coli at1.86 A resolution: comparison with the enzyme from human erythrocytesProtein Sci. 3 (5), 799-809 (1994) PubMed: 8061609 ","","Wed Jan 8 12:32:14 2003","1","","","" "AA01308","888792","888184","609","ATGGATCCGACACTTGAGTGGTTTTTATCCCACTGCCACATCCATAAATATCCGTCTAAAAGCACATTAATCAACGCCGGCGAAAAAGCCGAGACACTTTATTATTTAATTCAAGGCTCCGTGTCCGTTTTGGTCAAAGATGAAGACGGCAAAGAAATGATCCTCACCTATTTAAGCCAAGGGGATTTTTTCGGCGAAGCGGGCTTATTTGAAGAAGGACAACGCCGTTCTGCGTGGATTAAAGCAAAATCCTCCTGCGAAGTGGCGGAAATTTCTTATCGTAAATTTCGCCAGCTGATTCAAGTCAACCCTGAAATCCTGATGTATCTTACTGCCCAATTAGCGTATCGGTTACAAAACACTTCGCGCCAAGTAAGTAATTTAGCCTTTTTAGATGTCACCGGTCGCATTGCGCAAACCTTGCTCAATCTGGCAAAAATGCCGGAAGCGATGACTCACCCGGACGGTATGCAAATTAAAATCACCCGCCAGGAAATCGGACAAATGGTCGGTTGTTCGCGGGAAACCGTCGGGCGTATTCTGAAAATGCTGGAAGATCAACACCTCATCTCGGCACACGGCAAAACCATCGTAGTTTACGGCACCCGC","","","24185","MDPTLEWFLSHCHIHKYPSKSTLINAGEKAETLYYLIQGSVSVLVKDEDGKEMILTYLSQGDFFGEAGLFEEGQRRSAWIKAKSSCEVAEISYRKFRQLIQVNPEILMYLTAQLAYRLQNTSRQVSNLAFLDVTGRIAQTLLNLAKMPEAMTHPDGMQIKITRQEIGQMVGCSRETVGRILKMLEDQHLISAHGKTIVVYGTR","888184","","cyclic AMP receptor protein","Cytoplasm","","
InterPro
IPR000595
Domain
Cyclic nucleotide-binding
PF00027\"[14-105]TcNMP_binding
SM00100\"[1-115]TcNMP
PS50042\"[17-117]TCNMP_BINDING_3
PS00888\"[23-39]TCNMP_BINDING_1
PS00889\"[64-82]TCNMP_BINDING_2
InterPro
IPR001808
Domain
Bacterial regulatory protein, Crp
PR00034\"[159-175]T\"[175-190]THTHCRP
PF00325\"[159-190]TCrp
SM00419\"[153-201]THTH_CRP
PS00042\"[161-184]THTH_CRP_1
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[132-203]Tno description
InterPro
IPR012318
Domain
Helix-turn-helix motif, Crp-type
PS51063\"[131-203]THTH_CRP_2
InterPro
IPR014710
Domain
RmlC-like jelly roll fold
G3DSA:2.60.120.10\"[2-131]Tno description
noIPR
unintegrated
unintegrated
PTHR10217\"[17-127]TVOLTAGE AND LIGAND GATED POTASSIUM CHANNEL


","BeTs to 15 clades of COG0664COG name: cAMP-binding domains - Catabolite gene activator and regulatory subunit of cAMP-dependent protein kinasesFunctional Class: TThe phylogenetic pattern of COG0664 is ------yqvdrlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-39) to 2/2 blocks of the IPB001808 family, which is described as \"Bacterial regulatory proteins, Crp family\". Interpro entry for IP:IPR001808. IPB001808A 27-78 1.5e-20 IPB001808B 159-190 7.3e-18Significant hit ( 1.1e-05) to 2/3 blocks of the IPB000595 family, which is described as \"Cyclic nucleotide-binding domain\". Interpro entry for IP:IPR000595. IPB000595B 20-43 0.0033 IPB000595C 61-86 1.5","Residues 5 to 200 match (2e-07) PD:PD415998 which is described as TRANSCRIPTION REGULATOR ","","","","","","","","","","","","Wed Jan 8 12:36:30 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01308 is paralogously related to AA02124 (3e-09).","","","","","","Residues 159 to 190 (E-value = 1.5e-14) place AA01308 in the Crp family which is described as Bacterial regulatory proteins, crp family (PF00325)","","","","","McKay,D.B., Weber,I.T. and Steitz,T.A. Structure of catabolite gene activator protein at 2.9-A resolution. Incorporation of amino acid sequence and interactions with cyclic AMP J. Biol. Chem. 257 (16), 9518-9524 (1982) PubMed: 6286624 Weber,I.T. and Steitz,T.A. Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 A resolution J. Mol. Biol. 198 (2), 311-326 (1987) PubMed: 2828639 Schultz,S.C., Shields,G.C. and Steitz,T.A. Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees Science 253 (5023), 1001-1007 (1991) PubMed: 1653449 Gent,M.E., Gartner,S., Gronenborn,A.M., Sandulache,R. and Clore,G.M. Site-directed mutants of the cAMP receptor protein--DNA binding of five mutant proteins Protein Eng. 1 (3), 201-203 (1987) PubMed: 3333845 ","","Wed Jan 8 12:36:30 2003","1","","","" "AA01310","889081","888866","216","GTGATTATTCCTTGGCAAGAGTTAGCCGAAGAAACATTGGTCAATATCGTGGAAAGCGTTATTTTGCGAGAAGGGACCGATTATGGTTCACATGAACAGACTTTCGAACAAAAAAAGAAAGCATTGCTGAACAGGATCCGCCAGGGAAGCGCGGTGATTGTTTGGTCTGAATTACATGAATCTATCGACATAAAAGATAAAACGGAATTTTTTAGA","","","8395","VIIPWQELAEETLVNIVESVILREGTDYGSHEQTFEQKKKALLNRIRQGSAVIVWSELHESIDIKDKTEFFR","888866","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR008227
Family
Uncharacterised conserved protein UCP006169
PIRSF006169\"[1-72]TUncharacterised conserved protein
InterPro
IPR010648
Family
Protein of unknown function UPF0270
PF06794\"[1-70]TUPF0270
noIPR
unintegrated
unintegrated
PD026997\"[1-65]TYB56_PASMU_Q9CLQ8;
G3DSA:1.10.10.610\"[1-70]Tno description


","No hits to the COGs database.","","Residues 1 to 52 match (2e-11) PD:PD026997 which is described as PROTEOME COMPLETE YHEU CYTOPLASMIC VC2612 YPO0179 HI0956 PA3463 PM1156 ","","","","","","","","","","","","Wed Jan 8 12:39:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01310 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 70 (E-value = 8.6e-35) place AA01310 in the UPF0270 family which is described as Uncharacterised protein family (UPF0270) (PF06794)","","","","","","","","1","","","" "AA01311","889704","889108","597","ATGGAACAGGCGAATAAACGTAGTATCAAAGAACGCCGCCAGCAAGTGCTAACGGTGCTTACCCATATGCTCCATTCCGAACGTGGTATGGAACGCATGACCACCGCCCGTTTGGCGGCGGAAGTGGGCGTGTCGGAAGCGGCGTTATACCGTTATTACCCGAGTAAAACCAAGATTTTTGAAGCCCTTATTGAGAACATCGAAAGCACGTTGCTTAATCGGATTTCGCAGTCCATCAAACACGAAACCAACACCATGCAACGGGTAAAAGACATTATGCAGATGATCTTGGATTTTGCCCGCAAAAACCCCGGTTTAACCCGCGTGTTAACCGGTCACGCGTTGATGTTTGAAGACGCCAAATTACAAGCCCGCGTCGCCACCTTTTTTGACCGCTTGGAATTGCAATTTGTGAACATTCTGCAAATGCGAAAATTGCGTGAAGGACGTGGCTTTAACGTGGATGAACGGATTATCGCCGCCCACTTGGTGACCCTCTGCGAAGGGCAGTTTATGCGTTATGTGCGTTCCAACTTTCGCCATATGCCGAATCAGGGTTTTAACCAGCAATGGCAACTGATGGAAAGCTTATTTGCA","","","23338","MEQANKRSIKERRQQVLTVLTHMLHSERGMERMTTARLAAEVGVSEAALYRYYPSKTKIFEALIENIESTLLNRISQSIKHETNTMQRVKDIMQMILDFARKNPGLTRVLTGHALMFEDAKLQARVATFFDRLELQFVNILQMRKLREGRGFNVDERIIAAHLVTLCEGQFMRYVRSNFRHMPNQGFNQQWQLMESLFA","889108","","transcriptional regulator","Cytoplasm","","
InterPro
IPR001647
Domain
Bacterial regulatory protein, TetR
PF00440\"[17-63]TTetR_N
PS50977\"[11-71]THTH_TETR_2
InterPro
IPR012287
Domain
Homeodomain-related
G3DSA:1.10.10.60\"[10-74]Tno description


","No hits to the COGs database.","Significant hit ( 1.6e-09) to 1/1 blocks of the IPB001647 family, which is described as \"Bacterial regulatory proteins, TetR family\". Interpro entry for IP:IPR001647. IPB001647 29-59 1.6e-09","Residues 4 to 104 match (1e-15) PD:PD482307 which is described as REGULATOR PROTEOME COMPLETE TRANSCRIPTION TETR/ARCR PROBABLE FAMILY TRANSCRIPTIONAL ","","","","","","","","","","","","Wed Jan 8 12:47:01 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01311 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 17 to 63 (E-value = 7.8e-13) place AA01311 in the TetR_N family which is described as Bacterial regulatory proteins, tetR family (PF00440)","","","","","","","","1","","","" "AA01313","890159","889707","453","ATGAAAAAAATTGACGTAAAAATTTTAGATCAACGCATTGGTAAAGAATTTCCTCTGCCGGCTTACGCTACGGAAGGTTCCGCCGGTTTGGATTTACGTGCCTTAATTGACGAATCTATTGCGATTCAACCGGGCGAAACCACACTTATCCCGACGGGATTATCTATTTATATTGCCGATCCTAATTTGGCGGCGGTAATTTTGCCGCGTTCCGGTTTGGGGCATAAACATGGCATTGTGTTGGGCAATTTGGTGGGGTTAATCGACTCCGATTATCAAGGCCCGTTAATGGTTTCCGTGTGGAATCGTGGCGCCGAACCGTTCAAAATTGAAGTAGGCGATCGCATTGCCCAATTGGTTTTCGTGCCGGTGGTGCAAGCGGAATTTAATATCGTCAGCGAATTTAATGCCACGGAGCGTGGTGAGGGCGGCTTTGGGCATTCGGGTAAACAC","","","16169","MKKIDVKILDQRIGKEFPLPAYATEGSAGLDLRALIDESIAIQPGETTLIPTGLSIYIADPNLAAVILPRSGLGHKHGIVLGNLVGLIDSDYQGPLMVSVWNRGAEPFKIEVGDRIAQLVFVPVVQAEFNIVSEFNATERGEGGFGHSGKH","889707","","deoxyuridinetriphosphatase; deoxyuridine 5'-triphosphate nucleotidohydrolase","Cytoplasm","","
InterPro
IPR003232
Domain
dCTP Deaminase
PD004900\"[42-121]TDCD_METKA_Q8TYK5;
InterPro
IPR008180
Domain
DeoxyUTP pyrophosphatase
PF00692\"[15-149]TdUTPase
InterPro
IPR008181
Domain
DeoxyUTP pyrophosphatase subfamily 1
TIGR00576\"[7-150]Tdut: dUTP diphosphatase
noIPR
unintegrated
unintegrated
G3DSA:2.70.40.10\"[4-149]Tno description
PTHR11241\"[10-151]TDEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE


","No hits to the COGs database.","Significant hit ( 5.7e-27) to 4/4 blocks of the IPB001428 family, which is described as \"dUTPase\". Interpro entry for IP:IPR001428. IPB001428A 22-32 0.00024 IPB001428B 80-98 1.4e-07 IPB001428C 112-123 1.4e-05 IPB001428D 140-149 0.00031","Residues 1 to 135 match (4e-65) PD:PD337300 which is described as HYDROLASE DUTPASE DEOXYURIDINE NUCLEOTIDOHYDROLASE 5'-TRIPHOSPHATE POLYPROTEIN PROTEASE DUTP PYROPHOSPHATASE COMPLETE ","","","","","","","","","","","","Fri Jan 24 13:07:13 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01313 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 15 to 149 (E-value = 2.9e-57) place AA01313 in the dUTPase family which is described as dUTPase (PF00692)","","","","","Lundberg,L.G., Thoresson,H.O., Karlstrom,O.H. and Nyman,P.O.Nucleotide sequence of the structural gene for dUTPase ofEscherichia coli K-12. EMBO J. 2(6):967-971, 1983. PubMed: 6139280. Cedergren-Zeppezauer,E.S., Larsson,G., Nyman,P.O., Dauter,Z.and Wilson,K.S. Crystal structure of a dUTPase Nature. 355 (6362), 740-743 (1992) PubMed: 1311056 Larsson,G., Svensson,L.A. and Nyman,P.O. Crystal structure of the Escherichia coli dUTPase in complexwith a substrate analogue (dUDP) Nature structural biology. 3 (6), 532-538 (1996) PubMed: 8646539 Dauter,Z., Wilson,K.S., Larsson,G., Nyman,P.O. and Cedergren-Zeppezauer,E.S. The refined structure of dUTPase from Escherichia coli Acta Crystallogr. D 54, 735-749 (1998)","","Wed Jan 8 12:48:43 2003","1","","","" "AA01314","890161","890256","96","GTGATGTTTACCTTTAAAGAAATCGGTGATTTTTATCATAAAGTGCGGTCATTTTTTACGGCGTTTTTCATTTCCCATAATGCGTTACAATTTCAT","","","3896","VMFTFKEIGDFYHKVRSFFTAFFISHNALQFH","890256","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 09:37:21 2004","Thu Feb 26 09:37:21 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01314 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:37:21 2004","","","","","","","","","","","","","1","","","" "AA01315","891427","890231","1197","ATGATAAATATAGAAAATAAACGCATTGTCGTGGGCATTACGGGCGGAATTGCCGCTTACAAAACCATTGAATTAATTCGTTTATTACGCAAAGCCAATGCGCAGGTTCGAGTAGTATTAACCCCCGCCGCGGCAGAGTTTGTCACACCGCTCACCTTGCAGGCAATTTCCGGCAACGCTGTGGCACAATCCTTATTGGATCCGCAAGCGGAGCTGGCAATGGGTCACATTGAATTGGCAAAATGGGCGGACGCGGTGCTGATCGCCCCTGCCAGTGCAGATTTTATTGCCCGTCTCACCGTGGGCATGGCGAACGATTTATTATCCACCCTTTGTCTTGCCACCAACACACCGATTTTGCTGGCACCGGCAATGAATCAGCAAATGTACCGCCAGGCAATAACGCAGCAAAATCTGACCGCACTTTTAAGCCGAGGCGTGCAACTTATCGGACCGAATAGCGGCGAACAAGCCTGCGGTGATGTCGGTGCCGGGCGAATGTCCGAACCGTCGGAAATTTTCACCGCACTTTGTGACCATTTTGCCATACAACAGGATTTGGCGGGCATAAATGTTGCCATTACCGCCGGTCCGACCCGCGAAGCCATCGATCCCGTGCGTTATATTTCCAATCACAGCTCCGGCAAAATGGGCTTTGCCATTGCCGAAGCCTTCGCCAAACGTGGGGCGAATGTCACCTTAATCGCAGGTCCTGTTAATCTTGCTACGCCGAAAAACACTTCCCGCATTGATGTGACGTCCGCGCAGCAAATGTGGCAAACCTCCCTTGAGTGCGCTGTGAAAAGCCACATCTTTATTGGCTGCGCCGCCGTTGCGGATTATCGCGTTGCCGACATTGCCGAGCAGAAAATCAAAAAATCCGGTGAGGAAATGACATTAAAACTCATTAAAAACCCCGACATTATTACCGACGTTGCCTATCTTGCCGAAAATCGTCCGTTTGTGGTGGGCTTCGCTGCCGAAACGCAACATTTCGCCGATTACGCCAAAGATAAATTACAACGCAAAAATCTCGATATGATTTGCGCCAATGACGTGTCCGGCGGGCAGGTTTTCGGCGCGGATCAAAATGCGTTGCAACTGTTCTGGAAGGGCGGCGAAAAAGCCTTGCCGTTGGCGGATAAAAATACATTAGCGGAAATGTTGGTCAATGAAATTGTAACGCATTATGGGAAA","","","45125","MINIENKRIVVGITGGIAAYKTIELIRLLRKANAQVRVVLTPAAAEFVTPLTLQAISGNAVAQSLLDPQAELAMGHIELAKWADAVLIAPASADFIARLTVGMANDLLSTLCLATNTPILLAPAMNQQMYRQAITQQNLTALLSRGVQLIGPNSGEQACGDVGAGRMSEPSEIFTALCDHFAIQQDLAGINVAITAGPTREAIDPVRYISNHSSGKMGFAIAEAFAKRGANVTLIAGPVNLATPKNTSRIDVTSAQQMWQTSLECAVKSHIFIGCAAVADYRVADIAEQKIKKSGEEMTLKLIKNPDIITDVAYLAENRPFVVGFAAETQHFADYAKDKLQRKNLDMICANDVSGGQVFGADQNALQLFWKGGEKALPLADKNTLAEMLVNEIVTHYGK","890231","","DNA/pantothenate metabolism flavoprotein","Cytoplasm","","
InterPro
IPR003382
Domain
Flavoprotein
G3DSA:3.40.50.1950\"[7-152]Tno description
PF02441\"[7-124]TFlavoprotein
InterPro
IPR005252
Family
Bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate--cysteine ligase
TIGR00521\"[4-394]TcoaBC_dfp: phosphopantothenoylcysteine deca
InterPro
IPR007085
Domain
DNA/pantothenate metabolism flavoprotein, C-terminal
PF04127\"[187-364]TDFP
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.10300\"[182-399]Tno description
PTHR14359\"[13-399]THOMO-OLIGOMERIC FLAVIN CONTAINING CYS DECARBOXYLASE FAMILY
PTHR14359:SF6\"[13-399]TPANTOTHENATE METABOLISM FLAVOPROTEIN DFP


","No hits to the COGs database.","Significant hit ( 4e-12) to 1/1 blocks of the IPB003382 family, which is described as \"Flavoprotein\". Interpro entry for IP:IPR003382. IPB003382 84-118 4e-12","Residues 355 to 399 match (3e-08) PD:PD483655 which is described as COMPLETE PROTEOME FLAVOPROTEIN DNA/PANTOTHENATE HOMOLOG DFP METABOLISM ","","","","","","","","","","","","Wed Jan 8 12:50:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01315 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 187 to 364 (E-value = 1.9e-57) place AA01315 in the DFP family which is described as DNA / pantothenate metabolism flavoprotein (PF04127)","","","","","Kupke T. Molecular characterization of the4'-phosphopantothenoylcysteine synthetase domain ofbacterial dfp flavoproteins. J Biol Chem. 2002 Sep 27;277(39):36137-45. PMID: 12140293","","Wed Jan 8 12:50:35 2003","1","","","" "AA01316","891402","891551","150","ATGCGTTTATTTTCTATATTTATCATGCTTAAACCCCATGGTTTGCCCGGCTGGAAAATGAGTTTGCCTATTCTACTTGAATTATTATTCAATCAAAAATCTTATTTTTGCGATCCCGGTTCCATCTTTTGCACGGGCTTTTCCAATTTT","","","5769","MRLFSIFIMLKPHGLPGWKMSLPILLELLFNQKSYFCDPGSIFCTGFSNF","891551","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-37]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 09:38:47 2004","Thu Feb 26 09:38:47 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01316 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:38:47 2004","","","","","","","","","","","","","1","","","" "AA01317","891605","891799","195","ATGAATGAAGCATTAATGCCAAGGGAAAAGCTATTAAAATACGGTGCTGCCGCTTTGACGGACGATGAACTATTGGCGATCTTTTTGCGTACGGGAATTAAGGACTGCCCGGTGATGCAGTTATCGAAAAATGTATTGCAACATTTTGGTTCTTTACGCGAGTTAATTCGTGCCGACCAAAAGCAGTTTTGCGTG","","","7375","MNEALMPREKLLKYGAAALTDDELLAIFLRTGIKDCPVMQLSKNVLQHFGSLRELIRADQKQFCV","891799","","probable DNA repair protein","Cytoplasm","","No hits reported.","BeTs to 10 clades of COG2003COG name: DNA repair proteinsFunctional Class: LThe phylogenetic pattern of COG2003 is -------qv--lbcefghsn-j----Number of proteins in this genome belonging to this COG is","","Residues 7 to 62 match (6e-08) PD:PD455810 which is described as REPAIR DNA PROTEOME COMPLETE HOMOLOG RADC TRUNCATEDRADC ","","","","","","","","","","","","Wed Jan 8 13:28:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01317 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Katsiou E, Nickel CM, Garcia AF, Tadros MH.Molecular analysis and identification of the radC gene from the phototrophic bacterium Rhodobacter capsulatus B10.Microbiol Res. 1999 Dec;154(3):233-9.PMID: 10652786 Saveson CJ, Lovett ST.Tandem repeat recombination induced by replication fork defects in Escherichia coli requires a novel factor, RadC.Genetics. 1999 May;152(1):5-13.PMID: 10224240 Okaichi K, Mori T, Ihara M, Ohnishi T.Unique DNA repair property of an ultraviolet-sensitive (radC) mutant of Dictyostelium discoideum.Photochem Photobiol. 1995 Mar;61(3):281-4.PMID: 7716189 Felzenszwalb I, Boiteux S, Laval J.Cloning of the Escherichia coli radC gene: identification of the RadC protein.Braz J Med Biol Res. 1993 Dec;26(12):1261-8.PMID: 8136727 ","","Wed Jan 8 13:14:28 2003","1","","","" "AA01318","892473","892222","252","ATGAAAAAAACACTTTTAAGATTTGAAATCTTTCATACAATCAAAAGTGTAGCTGATTATGTAAATAATCGTGATGACATTGCGGACATTATCGCTGCAGATTACGCTTTAATCGCATGCGAAGAAAGCGGGTATGATGACTATTCGAGAGAATGTGCAGACGCACACTTGGATTTTTTACAAGATGCTGGAGCTAAATTTAATAGAGATGGGGCGTTAGATTTATTTGAGCAAGCTGTAGCGGAAAAAGAT","","","9463","MKKTLLRFEIFHTIKSVADYVNNRDDIADIIAADYALIACEESGYDDYSRECADAHLDFLQDAGAKFNRDGALDLFEQAVAEKD","892222","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Jan 8 13:15:18 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01318 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01319","892592","893461","870","ATGAGAATATTAATACACAAAAGTAGTTGTGGCAACTTTAAAAATATTCTTTTAAAGTTAAATGGCTATTTTTTGAACGGTACTTTTATAGATTTTAATCGTAAGTTATTGATATTAATATATATAAAAGTAACTTTAAAAAGTTTGAAAATATATATGGAGTTTTTTAAAGTTATGCGCACGAAGTTTAAAAACTTTTCTCTTATTGGGTCGCGGATAAGAGAAGAAAGAGAAAGGGCGGGAAGAACTAGGAATGAACTGGCTGATGCATTAGGTTTGTCTCTTTCAACACTGCAGTTATATGAAACAAATGAAAGGGAACCTCAAGCCTCTTTAATTCTTACTATTGCGGAAGAATTAGGGGTTGAGCCTAGTTATTTACTAACTGGCGAGAAGAACGGGGATGTTGGTAGTCCTCCGATTAAGCGCGCGCAAACGCACGAAATAAGCGGAGTTTCAATGATTGACTGCTTTTGTTCGGTAAACGTGTCGGCAGGCTTTGGCAGCTTTAACGAGGGCGTAACCGCGCCCGACGGGCAAGTGCCATATTCGGACAGCCTGTTGCAAAAGCTCGGCATTAAATCAACGCACGCCGCCGTATTTTGGGCAGATGGCACATCCATGCGCCCAACCATTGATGACGGCGATCAGATGTTGGTTGACCTCTCTAAAAAAGAGAGCAAGGGCGATAAAATCTATTTAGTGCAAAACCGCGAAAGCGTATGGGTTAAGCGCGTAAAACTCAACTGGAACGGCATAGAGCTCATTTCAGACAACAAAGAAGAGTACGCCCCGATAACGCTAACCAAAGAGGAAGCGGACAAATTGGAGATAATCGGACAAGTTGCCTACATCGGCAAAAGCGTAATT","","","32526","MRILIHKSSCGNFKNILLKLNGYFLNGTFIDFNRKLLILIYIKVTLKSLKIYMEFFKVMRTKFKNFSLIGSRIREERERAGRTRNELADALGLSLSTLQLYETNEREPQASLILTIAEELGVEPSYLLTGEKNGDVGSPPIKRAQTHEISGVSMIDCFCSVNVSAGFGSFNEGVTAPDGQVPYSDSLLQKLGIKSTHAAVFWADGTSMRPTIDDGDQMLVDLSKKESKGDKIYLVQNRESVWVKRVKLNWNGIELISDNKEEYAPITLTKEEADKLEIIGQVAYIGKSVI","893461","","transcriptional regulatory protein","Cytoplasm, Outer membrane","","
InterPro
IPR001387
Domain
Helix-turn-helix type 3
PF01381\"[73-127]THTH_3
SM00530\"[72-127]THTH_XRE
PS50943\"[73-127]THTH_CROC1
InterPro
IPR006198
Domain
Peptidase S24, S26A and S26B
PF00717\"[202-271]TPeptidase_S24
InterPro
IPR011056
Domain
Peptidase S24 and S26, C-terminal region
G3DSA:2.10.109.10\"[194-283]Tno description
noIPR
unintegrated
unintegrated
G3DSA:1.10.260.40\"[69-131]Tno description


","BeTs to 5 clades of COG2932COG name: Predicted transcriptional regulatorFunctional Class: KThe phylogenetic pattern of COG2932 is -----------l--ef-hsn-j----Number of proteins in this genome belonging to this COG is","","Residues 166 to 284 match (3e-07) PD:PD015931 which is described as REPRESSOR PROTEOME TRANSCRIPTION DNA-BINDING COMPLETE REGULATION REGULATOR REGULATORY CI PHAGE-RELATED ","","","","","","","","","","","","Wed Jan 8 13:22:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01319 is paralogously related to AA01763 (2e-08).","","","","","","Residues 158 to 272 (E-value = 1.7e-05) place AA01319 in the Peptidase_S24 family which is described as Peptidase family S24 (PF00717)","","","","","","","","1","","","" "AA01320","893599","893486","114","TTGGCCCTTTTTTATTGGGTGGTTTTGTCGTTAAAGTTAGTTTTAGAAAAAAAGTGGCTAAAATCTAAAAAGGGCGGTTTTAGCCACTTAATTGTAGAAAAACAAAAAGGCGTT","","","4397","LALFYWVVLSLKLVLEKKWLKSKKGGFSHLIVEKQKGV","893486","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-16]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 09:40:05 2004","Thu Feb 26 09:40:05 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01320 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:40:05 2004","","","","","","","","","","","","","1","","","" "AA01321","893714","894175","462","GTGAAAGGCATTGGCGTTACGCAGTTTATTCAGCTGCAAGCCTGTACTGAAATGACCCGCCGTTATTTGTTTGCAGAATTAAAAGAGACCCACTGTTTTACTTCAACCGACATTGTGAAAATGTACTTACAGACGGAGCTGGCAAATATCGAGCGGGAAATTTTTATGGTGCTTTTTCTGGATAACCAACATCGCCTGATTAAGCAGGAACGCCTGTTTCTCGGCACCATTAATAAAGCGATGGTGTACCCGCGTGAAATCATTAAAGAAGCCTTGGCTTGTAATGCGGCGGCGATTATTTTGGCGCATAATCACCCTTCCGGCGTGGCGGAACCGAGCATTTCCGATAAACAAATTACCGACACCATCAGACAGGCGGCGGATTTGGTGGATATTCGCGTGCTGGATCATTTCGTGATCGGCAATGGACGTTATTTTTCCTTTGCGGAACAAAATCTTCTT","","","17568","VKGIGVTQFIQLQACTEMTRRYLFAELKETHCFTSTDIVKMYLQTELANIEREIFMVLFLDNQHRLIKQERLFLGTINKAMVYPREIIKEALACNAAAIILAHNHPSGVAEPSISDKQITDTIRQAADLVDIRVLDHFVIGNGRYFSFAEQNLL","894175","","DNA repair protein","Cytoplasm","","
InterPro
IPR001405
Family
DNA repair protein RadC
PD007415\"[57-117]TRADC_HAEIN_P44952;
PF04002\"[30-154]TRadC
TIGR00608\"[1-154]Tradc: DNA repair protein RadC
PS01302\"[103-108]?RADC


","No hits to the COGs database.","Significant hit ( 1.7e-27) to 1/1 blocks of the IPB001405 family, which is described as \"DNA repair protein radC family\". Interpro entry for IP:IPR001405. IPB001405 76-116 1.6e-27","Residues 106 to 150 match (1e-10) PD:PD253901 which is described as DNA REPAIR COMPLETE PROTEOME RADC HOMOLOG RADC-LIKE PROTEIN INTERGENIC-REGION REPLICATION ","","","","","","","","","","","","Wed Jan 8 13:28:05 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01321 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 30 to 154 (E-value = 5.7e-73) place AA01321 in the RadC family which is described as RadC, DNA repair protein (PF04002)","","","","","Katsiou E, Nickel CM, Garcia AF, Tadros MH. Molecular analysis and identification of the radC gene from thephototrophic bacterium Rhodobacter capsulatus B10. Microbiol Res. 1999 Dec;154(3):233-9. PMID: 10652786 Saveson CJ, Lovett ST. Tandem repeat recombination induced by replication fork defectsin Escherichia coli requires a novel factor, RadC. Genetics. 1999 May;152(1):5-13. PMID: 10224240 Okaichi K, Mori T, Ihara M, Ohnishi T. Unique DNA repair property of an ultraviolet-sensitive (radC)mutant of Dictyostelium discoideum. Photochem Photobiol. 1995 Mar;61(3):281-4. PMID: 7716189 Felzenszwalb,I., Boiteux,S. and Laval,J. 1992. Identification of the radC102 mutation. Order of the genes inthe 81.5-82.0 min region of the Escherichia coli chromosome. Nucleic Acids Res. 20(2):366. PubMed: 1741263.","","Wed Jan 8 13:28:05 2003","1","","","" "AA01323","894387","894620","234","ATGTCTAGAGTCTGTCAAGTAACAGGCAAGCGTCCGGCAGTGGGGAACAACCGCTCACATGCAATGAATGCGACTCGTCGTCGTTTTCTTCCTAACCTTCACACACACCGTTTCTGGGTTGAAAGTGAAAACCGTTTCGTAACATTACGCTTAACTGCAAAAGGTATGCGTATTATTGATAAAAAAGGCATTGATGCAGTTTTAGCTGAAATCCGTGCTCGTGGCGAGAAAATC","","","9437","MSRVCQVTGKRPAVGNNRSHAMNATRRRFLPNLHTHRFWVESENRFVTLRLTAKGMRIIDKKGIDAVLAEIRARGEKI","894620","","50S ribosomal protein L28","Cytoplasm","","
InterPro
IPR001383
Family
Ribosomal protein L28
PF00830\"[3-63]TRibosomal_L28
TIGR00009\"[1-58]TL28: ribosomal protein L28


","BeTs to 18 clades of COG0227COG name: Ribosomal protein L28Functional Class: JThe phylogenetic pattern of COG0227 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 3.8e-30) to 1/1 blocks of the IPB001383 family, which is described as \"Ribosomal protein L28\". Interpro entry for IP:IPR001383. IPB001383 1-39 3.4e-30","Residues 49 to 78 match (4e-07) PD:PD469979 which is described as RIBOSOMAL PROTEOME COMPLETE 50S L28 ","","","","","","","","","","","","Wed Jan 8 13:30:59 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01323 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 63 (E-value = 2e-33) place AA01323 in the Ribosomal_L28 family which is described as Ribosomal L28 family (PF00830)","","","","","Lee,J.S., An,G., Friesen,J.D. and Isono,K. 1981. Cloning and the nucleotide sequence of the genes for Escherichia coli ribosomal proteins L28 (rpmB) and L33 (rpmG). Mol. Gen. Genet. 184(2):218-223. PubMed: 7035835. Wittmann-Liebold,B. and Marzinzig,E. 1977. Primary structure of protein L28 from the large subunit of Escherichia coli ribosomes. FEBS Lett. 81(1):214-217. PubMed: 332524.","","Wed Jan 8 13:30:22 2003","1","","","" "AA01324","894635","894802","168","ATGGCAGCAAAAGGTGCTCGTGAGAAAATCCGTTTAGTTTCTACTGCTGAAACAGGTCATTTCTACACAACAACAAAAAACAAACGTAATATGCCTGAGAAAATGGAAATCAAAAAATTTGATCCTGTAGTGCGTAAACACGTTGTTTATAAAGAAGCAAAAATCAAA","","","6517","MAAKGAREKIRLVSTAETGHFYTTTKNKRNMPEKMEIKKFDPVVRKHVVYKEAKIK","","","50S ribosomal protein L33","Cytoplasm, Periplasm","","
InterPro
IPR001705
Family
Ribosomal protein L33
PD002595\"[7-54]TQ7VN53_HAEDU_Q7VN53;
PF00471\"[7-54]TRibosomal_L33
TIGR01023\"[1-56]TrpmG_bact: ribosomal protein L33
PS00582\"[22-41]TRIBOSOMAL_L33


","No hits to the COGs database.","Significant hit ( 2.5e-21) to 1/1 blocks of the IPB001705 family, which is described as \"Ribosomal protein L33\". Interpro entry for IP:IPR001705. IPB001705 22-54 2.3e-21","Residues 7 to 54 match (1e-09) PD:PD436773 which is described as RIBOSOMAL L33 50S PROTEOME COMPLETE TYPE CHLOROPLAST ","Thu May 29 13:40:37 2003","","","Thu May 29 13:47:14 2003","Thu May 29 13:47:14 2003","","","Thu May 29 13:47:14 2003","Thu May 29 13:47:14 2003","Thu May 29 13:40:37 2003","Thu May 29 13:40:37 2003","Thu May 29 13:50:34 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01324 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 54 (E-value = 3.8e-21) place AA01324 in the Ribosomal_L33 family which is described as Ribosomal protein L33 (PF00471)","","","","","","","","1","","","" "AA01325","894887","895699","813","ATGCCCGAACTGCCTGAAGTGGAAACCGCCGTACGCGGTGTGAGTCCTTATCTGAAAGATTATGTTATTGAAAAAATCGTAGTCCGCCAGCCGAAACTGCGCTGGGCTGTATCGCCTGAATTGGCAGAGTTGCATCATGTAAAAATTTTGGATTTAACCCGTCGCGCCAAATATCTGGTTATTCACACCGAACAGGGTTACATCATCGGACATTTGGGGATGTCGGGAACGGTGCGTATTGTGTTTCATGGCAGCCCGATTGATAAACACGATCATCTTGATATTGTGGTGAATAACGGCAAATTACTGCGTTATAACGATCCCCGCCGTTTCGGTGCCTGGCTCTGGACGGAAAAATTGGATGAATTCCATTTATTCTTAAAACTGGGACCTGAGCCGCTATCAGAGGAATTCAATGCAGAGTACTTGTTTAAAAAATTACACAAAAAAACAACCGCACTTAAAACCGTATTAATGGATAACACCGTGGTGGTTGGTATTGGCAACATTTATGCCAATGAAAGTCTATTTCTGTGCGGGTTACATCCTTTGAAGCTCGCCGCTAATCTAACTCGAAAACAATGCGAACGCTTGGTGGATACCATTAAATCGGTGCTTGCCAAAGCCATTGAACAAGGCGGCACCACGCTAAAAGATTTTCTCCAGCCCGACGGCAGACCGGGGTATTTTGCACAAGAATTGCTGGTTTACGGCAACAAAGGCAAACCATGTCCGAAGTGCGGTACAAAAATCGAGAGTTTAGTCATCGGGCAACGGAATAGTTTTTATTGCCCGACGTGCCAGAAGAAGGGA","","","32409","MPELPEVETAVRGVSPYLKDYVIEKIVVRQPKLRWAVSPELAELHHVKILDLTRRAKYLVIHTEQGYIIGHLGMSGTVRIVFHGSPIDKHDHLDIVVNNGKLLRYNDPRRFGAWLWTEKLDEFHLFLKLGPEPLSEEFNAEYLFKKLHKKTTALKTVLMDNTVVVGIGNIYANESLFLCGLHPLKLAANLTRKQCERLVDTIKSVLAKAIEQGGTTLKDFLQPDGRPGYFAQELLVYGNKGKPCPKCGTKIESLVIGQRNSFYCPTCQKKG","895699","","formamidopyrimidine-DNA glycosylase","Cytoplasm","","
InterPro
IPR000191
Family
Formamidopyrimidine-DNA glycolase
PD003680\"[138-215]TFPG_HAEIN_P44948;
PF01149\"[2-115]TFapy_DNA_glyco
PF06831\"[129-221]TH2TH
TIGR00577\"[1-268]Tfpg: formamidopyrimidine-DNA glycosylase
InterPro
IPR000214
Binding_site
Formamidopyrimidine-DNA glycolase, zinc-binding site
PS51066\"[235-269]TZF_FPG_2
PS01242\"[244-268]TZF_FPG_1
InterPro
IPR010663
Domain
Zinc finger, Fpg-type
PF06827\"[241-270]Tzf-FPG_IleRS
InterPro
IPR012319
Domain
Formamidopyrimidine-DNA glycosylase, catalytic
PS51068\"[2-112]TFPG_CAT
noIPR
unintegrated
unintegrated
PTHR22993\"[19-270]TFORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE
PTHR22993:SF4\"[19-270]TFORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE (FAPY-DNA GLYCOSYLASE)


","No hits to the COGs database.","Significant hit ( 1.9e-68) to 5/5 blocks of the IPB000214 family, which is described as \"Formamidopyrimidine-DNA glycolase, zinc binding domain\". Interpro entry for IP:IPR000214. IPB000214A 1-13 1.9e-07 IPB000214B 54-78 7.9e-09 IPB000214C 103-112 1.5e-06 IPB000214D 158-183 3.3e-19 IPB000214E 237-268 1.2e-20","Residues 2 to 271 match (1e-127) PD:PD003680 which is described as GLYCOSYLASE COMPLETE PROTEOME FORMAMIDOPYRIMIDINE-DNA GLYCOSIDASE HYDROLASE DNA ZINC REPAIR ZINC-FINGER ","","","","","","","","","","","","Wed Jan 8 13:34:34 2003","","Wed Jan 12 10:19:16 2005","Wed Jan 12 10:19:16 2005","Wed Jan 12 10:19:16 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA01325 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Jan 12 10:19:16 2005","","","","","Residues 241 to 270 (E-value = 4.5e-06) place AA01325 in the zf-FPG_IleRS family which is described as Zinc finger found in FPG and IleRS (PF06827)","Wed Jan 12 10:19:16 2005","","","","Boiteux,S., O\"Connor,T.R. and Laval,J. Formamidopyrimidine-DNA glycosylase of Escherichia coli: cloning and sequencing of the fpg structural gene and overproduction of the protein EMBO J. 6 (10), 3177-3183 (1987) PubMed: 3319582 Clementz,T. and Raetz,C.R. A gene coding for 3-deoxy-D-manno-octulosonic-acid transferase in Escherichia coli. Identification, mapping, cloning, and sequencing J. Biol. Chem. 266 (15), 9687-9696 (1991) PubMed: 2033061 O\"Connor,T.R., Graves,R.J., de Murcia,G., Castaing,B. andLaval,J. Fpg protein of Escherichia coli is a zinc finger protein whose cysteine residues have a structural and/or functional role J. Biol. Chem. 268 (12), 9063-9070 (1993) PubMed: 8473347 Duwat P, de Oliveira R, Ehrlich SD, Boiteux S Repair of oxidative DNA damage in gram-positive bacteria: the Lactococcus lactis Fpg protein. Microbiology 1995 Feb;141 ( Pt 2):411-7 PMID: 7704272 ","","Wed Jan 12 10:19:16 2005","1","","","" "AA01327","896757","895708","1050","ATGTCAATAACAAAAAAACTCGTTGCTAAATTAGCCGGAAAACGAAAAGCAGAAAACATAGATTTAATAATGATTAAATCGGTGTTGTTAAAACCCATTGGCGATGCTATTGGCGATGCCGTTGCCCATACCGCGCATTTAAAACAATTAAAACTTGCCAACCCGGAACTGGTGATTGGCGTGATCGTCACAGAAAGGAATCGGGACATTTTTGCTTATTCCGATTTAGTTGATGTTCTCCTGGAGGACAAACCTTTAACCTATATTTCTCAATGTCGCAAATGGGATCTCTATTTGGATTTTCAGCCAACTTACACCACTAAGTCTATTATTTTAGAGAAGCTGTTATCACCGAAGTACATTATTGTGTTTAATAAAAAACATAAGGAAAATTATAATTTAGATACAATCAAAAATTATAATTTCGCTTGTCCACAAAATGACACAACACATATTTCTGAATATTTGAATGATTCTGCCATTTCTGCTTATTTAGATCCAAAGGCTGTGGAATATGCTTTAATAAATCAGGAAACCATTAGATTTGAAGTGCTTTGGGGCGATAAAGTGAGAATTTTATTGGCACCTGAAGGCAGTACCAGAAAAATTCCGGCAAGCGAATTTGCCGAATTATTAAATCCACTTTCCCCAACGATTGTAGAAAATGTACTTTTTGTGCTAACAAATACGAAAGAAAGTGCCACTTATTTCGAAGAATTAATTTCATTATGTGATAACAAAATTCAGATAAAATTATCACCTAAAACCACAATTCAGGAATATATCCAGCTTGTTTCTTCTGCGGATTTAATTATTAGTGTTGATAGCGGAACGGTTCATCTTGCTACAGCCCTGCAGAAAAAAGTCTTGGCATTTTATGCGCGGAATATCGCCAATTTTTGCCGCTGGCAACCTAAAGGCAAAGCAGAAGTGCCTTATAAAGCGATTATGAGCAAAACCGAAAGCGATTCCAACAATCACACCTGCGATTTCCCCATGGACGAAGCGGCAGATTGGGTAAATCACTTATTTCAAACACTGCCGAAACAC","","","39623","MSITKKLVAKLAGKRKAENIDLIMIKSVLLKPIGDAIGDAVAHTAHLKQLKLANPELVIGVIVTERNRDIFAYSDLVDVLLEDKPLTYISQCRKWDLYLDFQPTYTTKSIILEKLLSPKYIIVFNKKHKENYNLDTIKNYNFACPQNDTTHISEYLNDSAISAYLDPKAVEYALINQETIRFEVLWGDKVRILLAPEGSTRKIPASEFAELLNPLSPTIVENVLFVLTNTKESATYFEELISLCDNKIQIKLSPKTTIQEYIQLVSSADLIISVDSGTVHLATALQKKVLAFYARNIANFCRWQPKGKAEVPYKAIMSKTESDSNNHTCDFPMDEAADWVNHLFQTLPKH","895708","From Genbank:[gi:480923]This protein is involved in core oligosaccharide biosynthesis.","possible LOS biosynthesis enzyme (D-glycero-D-manno-heptosyl transferase)","Cytoplasm","","
InterPro
IPR002201
Family
Glycosyl transferase, family 9
PF01075\"[254-294]TGlyco_transf_9
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2000\"[187-344]Tno description


","BeTs to 9 clades of COG0859COG name: ADP-heptose:LPS heptosyltransferaseFunctional Class: MThe phylogenetic pattern of COG0859 is -------q-----cefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-12) to 2/2 blocks of the IPB002201 family, which is described as \"Glycosyltransferase family 9\". Interpro entry for IP:IPR002201. IPB002201A 38-62 1.4 IPB002201B 255-298 2.2e-10","Residues 14 to 310 match (7e-13) PD:PD041405 which is described as TRANSFERASE COMPLETE PROTEOME LIPOPOLYSACCHARIDE BIOSYNTHESIS LBGB YEEL GLYCOSYLTRANSFERASE PM1144 Z3137 ","","","","","","","","","","","Wed Aug 13 11:36:32 2003","Wed Jan 8 14:00:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01327 is paralogously related to AA01329 (4e-09), AA01396 (9e-06), AA01276 (5e-05) and AA00543 (0.001).","","","","","","","","","","","Stevens,M.K., Klesney-Tait,J., Lumbley,S., Walters,K.A., Joffe,A.M., Radolf,J.D. and Hansen,E.J. Identification of tandem genes involved in lipooligosaccharide expression by Haemophilus ducreyi Infect. Immun. 65 (2), 651-660 (1997) PubMed: 9009327 Tullius MV, Phillips NJ, Scheffler NK, Samuels NM, Munson JrRS Jr, Hansen EJ, Stevens-Riley M, Campagnari AA, Gibson BW. The lbgAB gene cluster of Haemophilus ducreyi encodes a beta-1,4-galactosyltransferase and an alpha-1,6-DD-heptosyltransferase involved in lipooligosaccharide biosynthesis. Infect Immun. 2002 Jun;70(6):2853-61. PMID: 12010972 Gibson,B.W., Campagnari,A.A., Melaugh,W., Phillips,N.J., Apicella,M.A., Grass,S., Wang,J., Palmer,K.L. and Munson,R.S.Jr. Characterization of a transposon Tn916-generated mutant of Haemophilus ducreyi 35000 defective in lipooligosaccharidebiosynthesis J. Bacteriol. 179 (16), 5062-5071 (1997) PubMed: 9260947 ","","Wed Jan 8 13:50:29 2003","1","","8","" "AA01329","897789","896770","1020","ATGAAAGCATTACTCCGAAAAATCCGTTTAGCCTTAGGCAAAATGTTGCTAGACAAAAATGTTCAGGGGCAGCCTTTGCCGACAAATCCGAAAATTATTGTGTTACAACAAGACGGAAAAATCGGAGATTATATTGTCAGTTCATTTATCTTCAGAGAATTAAAACGACATAACCCCAAAATACAGATTGATGTTGTATGTTCACCTAAAAATGCCAATTTATTTGAACAAAATCCATCTATTGATCATTGTTTTATTTTAAATAGAAAAGAACATTGCGCTTACAGCAGAATGGGAAAACAGCTTTCACATGAACATTATGATGTATTAATTAATTTACCGGTATTATTACGGAGTCGTGATTTGTGGCTAACCCGATTAATTCATGCAAAAAATAATATCGGCTATAAAAAACAAAACTACAAACTATTTAATTTGAATGTCACTCAAGACCAATTACATTTTTCCCAAGTTTATGCAGAAGCCATTAAATTATGTGGTGTAAAAGATATTAATCTTGAATATGACATTCCAAATCACAGTGATAAAAAAGAAGATATTGCAAATTTCATACAAAAAAATCATCTTGTCGATTGCATCGCTATAAACTTTTTTGGTGCAGCCGGCACCAGAAAATTTACGGAACAAAACATTTATCGGTTTATCGAAAAATTTAAAGCCGAAAATAAAAAAGCGCTGTTACTAACCTACCCCGAAGTAACCCCTTTGTTAAAAACGATAGCAGAAAAATATACCAATGCTTTTATCTATGAAAATACTGAAAATATCTTTGATACGATAACATTACTTCATTATACTAGCCTCGTTATTTCTCCTGATACGTCTATTATTCATATTGCAGCAGGATTAAATAAAAAAATTATTGGATTTTATAAGCTCGCTGATAAAGAAAACTTTACGCATTGGAATCCAAACTGTAAAAATAAAACATATATCCTTAATTTTATTGAAAATGTCAATGAAATCTCTCCCGATGAAATTAAATCAGAATGGTTAAAA","","","39479","MKALLRKIRLALGKMLLDKNVQGQPLPTNPKIIVLQQDGKIGDYIVSSFIFRELKRHNPKIQIDVVCSPKNANLFEQNPSIDHCFILNRKEHCAYSRMGKQLSHEHYDVLINLPVLLRSRDLWLTRLIHAKNNIGYKKQNYKLFNLNVTQDQLHFSQVYAEAIKLCGVKDINLEYDIPNHSDKKEDIANFIQKNHLVDCIAINFFGAAGTRKFTEQNIYRFIEKFKAENKKALLLTYPEVTPLLKTIAEKYTNAFIYENTENIFDTITLLHYTSLVISPDTSIIHIAAGLNKKIIGFYKLADKENFTHWNPNCKNKTYILNFIENVNEISPDEIKSEWLK","896770","","LOS biosynthesis enzyme (D-glycero-D-manno-heptosyl transferase)","Cytoplasm","","
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2000\"[31-150]T\"[198-339]Tno description
signalp\"[1-23]?signal-peptide


","BeTs to 8 clades of COG0859COG name: ADP-heptose:LPS heptosyltransferaseFunctional Class: MThe phylogenetic pattern of COG0859 is -------q-----cefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 7.7e-12) to 2/2 blocks of the IPB002201 family, which is described as \"Glycosyltransferase family 9\". Interpro entry for IP:IPR002201. IPB002201A 42-66 3.2e-05 IPB002201B 260-303 6.9e-05","Residues 1 to 339 match (1e-81) PD:PD041405 which is described as TRANSFERASE COMPLETE PROTEOME LIPOPOLYSACCHARIDE BIOSYNTHESIS LBGB YEEL GLYCOSYLTRANSFERASE PM1144 Z3137 ","","","","","","","","","","","","Wed Jan 8 13:55:50 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01329 is paralogously related to AA01327 (4e-09), AA01396 (2e-05) and AA00543 (5e-04).","","","","","","","","","","Stevens,M.K., Klesney-Tait,J., Lumbley,S., Walters,K.A., Joffe,A.M., Radolf,J.D. and Hansen,E.J. Identification of tandem genes involved in lipooligosaccharide expression by Haemophilus ducreyi Infect. Immun. 65 (2), 651-660 (1997) PubMed: 9009327 Tullius MV, Phillips NJ, Scheffler NK, Samuels NM, Munson JrRS Jr, Hansen EJ, Stevens-Riley M, Campagnari AA, Gibson BW. The lbgAB gene cluster of Haemophilus ducreyi encodes a beta-1,4-galactosyltransferase and an alpha-1,6-DD-heptosyltransferase involved in lipooligosaccharide biosynthesis. Infect Immun. 2002 Jun;70(6):2853-61. PMID: 12010972 Gibson,B.W., Campagnari,A.A., Melaugh,W., Phillips,N.J., Apicella,M.A., Grass,S., Wang,J., Palmer,K.L. and Munson,R.S. Jr. Characterization of a transposon Tn916-generated mutant of Haemophilus ducreyi 35000 defective in lipooligosaccharide biosynthesis J. Bacteriol. 179 (16), 5062-5071 (1997) PubMed: 9260947","","Wed Jan 8 13:55:50 2003","","1","","8","" "AA01330","898482","897793","690","ATGGATAGCGCATACAATCTTCCCCCAATCTTCGTTATCAGCTTAAAAAACTCTCCCCGTCGTGAATTTATAGCAAAGCGTTTAAATGGGCTTGGCTTGCAATTTGAATTTTTTGATGCGGTTTATGGAAAAGCGTTGAGCGAAGAAGAGCTTGCCAAGGTGGATTATCAGTATTATCAGGATTTCGATAATAAACGTCTAACGCTGGGTGAAATCGGATGTGCCTTAAGTCATATTCAAGTATATGAACACATCAAAAAAAATAATATTGCTGAAGCCATCATTTTAGAAGACGATGCAATTGTTTCGACCCACTTTAAAGCGATTTTGCAGGCGGCTATTGAGAAACTGCCTTCGCGTTACGAAATTCTCTTTTTCGATCATGGCAAAGCCAAATCTTACCCGTTAATTAAAAAGTGCCTGCCTGAAGGTTATAAACTGGTTCGTTATCGCTACCCTTCAAAAAATTCCCGTCGCTCGATCATGAAAGCAACCGCTTATATGGTCAATCAGGCTGGCGTAGAAAAACTCTTAAAATACGCCTATCCTTTGCGTATGCCGGCGGACTTCGTTACGGGTTTTATTCAAAAAACACGTATTCACGCGTATGGCGTTGAGCCCTCCTGTGTCTTTGAGGGCTTAGCGGTTGAAAGCGAAATTAATTCTATTGAAGATCGATACAAGAAAGCA","","","26643","MDSAYNLPPIFVISLKNSPRREFIAKRLNGLGLQFEFFDAVYGKALSEEELAKVDYQYYQDFDNKRLTLGEIGCALSHIQVYEHIKKNNIAEAIILEDDAIVSTHFKAILQAAIEKLPSRYEILFFDHGKAKSYPLIKKCLPEGYKLVRYRYPSKNSRRSIMKATAYMVNQAGVEKLLKYAYPLRMPADFVTGFIQKTRIHAYGVEPSCVFEGLAVESEINSIEDRYKKA","897793","","LOS biosynthesis enzyme (beta-1,4-galactosyltransferase)","Cytoplasm","","
InterPro
IPR002654
Family
Glycosyl transferase, family 25
PTHR10730:SF2\"[10-99]TCEREBRAL CELL ADHESION MOLECULE RELATED
PF01755\"[7-192]TGlyco_transf_25
noIPR
unintegrated
unintegrated
PTHR10730\"[10-99]TPROCOLLAGEN/CELL ADHESION MOLECULE RELATED


","BeTs to 3 clades of COG3306COG name: Glycosyltransferase involved in LPS biosynthesisFunctional Class: MThe phylogenetic pattern of COG3306 is -----------------h-nuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 8.4e-12) to 2/4 blocks of the IPB002654 family, which is described as \"Glycosyltransferase family 25\". Interpro entry for IP:IPR002654. IPB002654A 9-43 0.076 IPB002654B 67-110 3e-08","Residues 11 to 117 match (2e-24) PD:PD405664 which is described as TRANSFERASE PROTEOME GLYCOSYLTRANSFERASE COMPLETE BIOSYNTHESIS CLUSTER 2.-.-.- LBGA HI0765 6-DEOXY-L-TALAN ","","","","","","","","","","","","Wed Jan 8 13:59:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01330 is paralogously related to AA02654 (5e-07) and AA01332 (9e-06).","","","","","","Residues 7 to 192 (E-value = 1.5e-60) place AA01330 in the Glyco_transf_25 family which is described as Glycosyltransferase family 25 (LPS biosynthesis protein) (PF01755)","","","","","Stevens,M.K., Klesney-Tait,J., Lumbley,S., Walters,K.A., Joffe,A.M., Radolf,J.D. and Hansen,E.J. Identification of tandem genes involved in lipooligosaccharide expression by Haemophilus ducreyi Infect. Immun. 65 (2), 651-660 (1997) PubMed: 9009327 Gibson,B.W., Campagnari,A.A., Melaugh,W., Phillips,N.J., Apicella,M.A., Grass,S., Wang,J., Palmer,K.L. and Munson,R.S. Jr. Characterization of a transposon Tn916-generated mutant of Haemophilus ducreyi 35000 defective in lipooligosaccharide biosynthesis J. Bacteriol. 179 (16), 5062-5071 (1997) PubMed: 9260947 Tullius MV, Phillips NJ, Scheffler NK, Samuels NM, Munson Jr RS Jr, Hansen EJ, Stevens-Riley M, Campagnari AA, Gibson BW. The lbgAB gene cluster of Haemophilus ducreyi encodes a beta-1,4-galactosyltransferase and an alpha-1,6-DD-heptosyltransferase involved in lipooligosaccharide biosynthesis. Infect Immun. 2002 Jun;70(6):2853-61. PMID: 12010972 ","","Wed Jan 8 13:59:15 2003","1","","8","" "AA01331","898781","898548","234","ATGGCTTCAAATTTGAGGTTTTCTATGAAACAAGGTATTCATCCTGAATATAAAGAGGTTACTGCGACCTGTTCTTGCGGTAACGTGATCAAAACCCGTTCAACCTTAGGCAAAGACATCAACCTTGATGTGTGCGGTAAATGTCACCCATTCTACACAGGAAAACAACGTGTTGTTGACACCGGTGGCCGCGTTGAACGCTTTAACAGCCGTTTTAAAATTCCAGGTACAAAA","","","8693","MASNLRFSMKQGIHPEYKEVTATCSCGNVIKTRSTLGKDINLDVCGKCHPFYTGKQRVVDTGGRVERFNSRFKIPGTK","898548","","50S ribosomal protein L31","Periplasm, Cytoplasm","","
InterPro
IPR002150
Family
Ribosomal protein L31
PR01249\"[10-27]T\"[39-54]T\"[54-72]TRIBOSOMALL31
PF01197\"[9-75]TRibosomal_L31
TIGR00105\"[8-78]TL31: ribosomal protein L31
PS01143\"[43-64]TRIBOSOMAL_L31


","BeTs to 18 clades of COG0254COG name: Ribosomal protein L31Functional Class: JThe phylogenetic pattern of COG0254 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.5e-24) to 1/1 blocks of the IPB002150 family, which is described as \"Ribosomal protein L31\". Interpro entry for IP:IPR002150. IPB002150 42-72 1.4e-24","Residues 9 to 72 match (7e-08) PD:PD413791 which is described as RIBOSOMAL 50S L31 PROTEOME COMPLETE TYPE B COPY L31-LIKE PROBABLE ","","","","","","","","","","","","Wed Jan 8 14:01:50 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01331 is paralogously related to AA02904 (7e-05).","","","","","","Residues 9 to 75 (E-value = 1.2e-43) place AA01331 in the Ribosomal_L31 family which is described as Ribosomal protein L31 (PF01197)","","","","","Stevens,M.K., Klesney-Tait,J., Lumbley,S., Walters,K.A., Joffe,A.M., Radolf,J.D. and Hansen,E.J. Identification of tandem genes involved in lipooligosaccharide expression by Haemophilus ducreyi Infect. Immun. 65 (2), 651-660 (1997) PubMed: 9009327 Gibson,B.W., Campagnari,A.A., Melaugh,W., Phillips,N.J., Apicella,M.A., Grass,S., Wang,J., Palmer,K.L. and Munson,R.S. Jr. Characterization of a transposon Tn916-generated mutant of Haemophilus ducreyi 35000 defective in lipooligosaccharidebiosynthesis J. Bacteriol. 179 (16), 5062-5071 (1997) PubMed: 9260947 ","","Wed Jan 8 14:01:50 2003","1","","8","" "AA01332","899015","899860","846","ATGAATTCCACGGAAAATAAAAATTTTGTTATCAGCATTTCGACGGCTGAACAACGCAGAAACCACATTATTGAACAATTTACTCATCAAAATATTCCCTTTGAATTTTTTGATGCTTTTACGCCATCCGATAAATTGACCGATCATTTGCAGCGCTATCTTCCGAATGTTGCGAACGCCGCTCAGCTCACCATGGGAGAAAAAGGCTGTTTAATGAGCCACTTCATGCTGTGGAAGAAATGTATTTATGAAAACTTAGACTACGTTACGCTTTTTGAAGATGATATTTTGCTTGGCGAGAATGCTAATAAATTTCTTGCCGAAGACGAATGGCTAAAAGTGCGGTTCAATTTTCAAGAGATTTTTGTCCTGCGTTTAGAAACTTTTCTCATGCCCGTTCAGCTTGAAAAACAAGTGCAGATTCCTCCTTTTCAGCAACGTGATATTGATATTTTAACGTCCAAGCATTTTGGCACGGCAGGATATGTAATATCTCAAGGCGCGGCTAAATATCTCATTGCGTTGTTTGAAAAGCTTACCACAGAAGAAATTAAACCGATTGATGAAATAATGTTTAATCAACAGATTAACGCTACCGGCTATCGGATATATCAACTGAATCCGGCGATTTGTGTTCAGGAATTACAATTAAATCAAGAGGCAAGCTTATTAGTGAGCAATTTGGAACAAGAAAGAAAAAATAAACCTAAAATACGAAAAAAGAAAACATTAAAACAACGCCTATCCCGAATAAAAGAGAATATTATACGGGCAATAAATAAAGAAAAATGGAAAGAACAACAACGCATTAGGGAAATACTAGGTAAAGAAATAGTTCGTTTTATG","","","33292","MNSTENKNFVISISTAEQRRNHIIEQFTHQNIPFEFFDAFTPSDKLTDHLQRYLPNVANAAQLTMGEKGCLMSHFMLWKKCIYENLDYVTLFEDDILLGENANKFLAEDEWLKVRFNFQEIFVLRLETFLMPVQLEKQVQIPPFQQRDIDILTSKHFGTAGYVISQGAAKYLIALFEKLTTEEIKPIDEIMFNQQINATGYRIYQLNPAICVQELQLNQEASLLVSNLEQERKNKPKIRKKKTLKQRLSRIKENIIRAINKEKWKEQQRIREILGKEIVRFM","899860","From GenBank (gi:1170778): This protein is involved in extracellular lipooligosacheraides (LOS) biosynthesis and virulence expression, and in the synthesis of the oligosaccharide moiety of the LOS molecule by adding galac.","galactosyltransferase II","Cytoplasm","","
InterPro
IPR002654
Family
Glycosyl transferase, family 25
PTHR10730:SF2\"[9-96]TCEREBRAL CELL ADHESION MOLECULE RELATED
PF01755\"[6-191]TGlyco_transf_25
noIPR
unintegrated
unintegrated
PTHR10730\"[9-96]TPROCOLLAGEN/CELL ADHESION MOLECULE RELATED


","BeTs to 4 clades of COG3306COG name: Glycosyltransferase involved in LPS biosynthesisFunctional Class: MThe phylogenetic pattern of COG3306 is -----------------h-nuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 2.2e-71) to 4/4 blocks of the IPB002654 family, which is described as \"Glycosyltransferase family 25\". Interpro entry for IP:IPR002654. IPB002654A 8-42 1.4e-17 IPB002654B 63-106 3e-30 IPB002654C 147-173 7.4e-14 IPB002654D 205-214 1e-05","Residues 77 to 117 match (2e-09) PD:PD023344 which is described as TRANSFERASE BIOSYNTHESIS GLYCOSYLTRANSFERASE GLYCOSYL LACTO-N-NEOTETRAOSE COMPLETE PROTEOME LGTE LGTB LIPOPOLYSACCHARIDE ","","","","","","","","","","","Wed Jan 8 15:02:09 2003","Wed Jan 8 14:54:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01332 is paralogously related to AA02654 (2e-06) and AA01330 (1e-05).","","","","","","Residues 6 to 191 (E-value = 5e-77) place AA01332 in the Glyco_transf_25 family which is described as Glycosyltransferase family 25 (LPS biosynthesis protein) (PF01755)","","","","","Sun,S., Schilling,B., Tarantino,L., Tullius,M.V.,Gibson,B.W. and Munson,R.S. Jr. Cloning and characterization of the lipooligosaccharide galactosyltransferase II gene of Haemophilus ducreyi J. Bacteriol. 182 (8), 2292-2298 (2000) PubMed: 10735874 ","","Wed Jan 8 14:54:45 2003","1","","8","" "AA01333","899872","900873","1002","ATGAAAAAAGAATATTCCTCACTCTCAACTTTGTTTTCATCTAATGCAACATTTTTTAATGTTATTCATAGAATAAGCAATAAACCTTATAAAATATTCTATACCGGTTTGATTCCAAAACCGATTCGTAGATGGCTCGCCAAAAAAGCTAATTTATCTCAACAAAATCATGTTGCAAATTGTTGGAAAGAGGTCATTTCCCTTTATCTTAATGGTGAATTAGATGAAATTATGGTTAAGCCTAAAAAGGATTTAGGGAATAAGAAAATCATTTGGCAATATTGGGGACAGGGTTGGGAAAGTGAAGAATTGCCTGATATTGTTAAAATCTGTCGTCGTTCAGTTCAAGAAAATAAAGGTGATTATGAGGTCATCTATCTGGATGATAAAAATTTGATTGAATATATTGAATTTTCTGATTTCGTTTCTGAAAAAAGAAAGAATCCTAATTTTCGTCATGCATTTTTCTCAGACCTGCTTAGGTTAGCTTTGTTGGAATGCTATGGTGGAATATGGGTTGATGCAACAATTTTATTTACAGCACCTATTACAAAACAATTAGGCAGTTCAGATTTTTTCATGTTTTCTCGAAGCCCTAAAGCAACTAATAAGGCAATGTGGAAGAATCTAAATAGAGAGTATTTTTTATGGGATAAAGAAAGTCGGGTAAATATTTTAAATAGCTTTATTATCTCTAAAAAAGGAAATGTAACAATACATATCTTACTTCAGTTGCTATTATTTTTTTGGAAAACACAGGAGAATATTCCTCACTACTTCTTTTTTCAAATCCTCTTCGATGAGCTAAAAAAAGAAAATTTGATTGAAGAGTTTGAATTGGTTGATGATACTTTGCCACATTTATTATTTTCTGAGTTGAATAATCCTTTTGATAAAAATAAGTTAGATAAGATTACAGCAAAATGTAATCAGCATAAAATAACTTATGTGGCAAAGTGTGAGACAGGTAGTTTTTATGCGTATTTAAAAAATAAATACCAG","","","39594","MKKEYSSLSTLFSSNATFFNVIHRISNKPYKIFYTGLIPKPIRRWLAKKANLSQQNHVANCWKEVISLYLNGELDEIMVKPKKDLGNKKIIWQYWGQGWESEELPDIVKICRRSVQENKGDYEVIYLDDKNLIEYIEFSDFVSEKRKNPNFRHAFFSDLLRLALLECYGGIWVDATILFTAPITKQLGSSDFFMFSRSPKATNKAMWKNLNREYFLWDKESRVNILNSFIISKKGNVTIHILLQLLLFFWKTQENIPHYFFFQILFDELKKENLIEEFELVDDTLPHLLFSELNNPFDKNKLDKITAKCNQHKITYVAKCETGSFYAYLKNKYQ","900873","","conserved hypothetical protein; possible capsular polysaccharide synthesis protein","Cytoplasm","","
InterPro
IPR008441
Family
Capsular polysaccharide synthesis
PF05704\"[44-329]TCaps_synth


","No hits to the COGs database.","","Residues 56 to 314 match (3e-40) PD:PD039977 which is described as CAPSULAR POLYSACCHARIDE B SEROTYPE WCIW CAPP33FI CJ1137C PROTEOME COMPLETE CAP37I ","","","","","","","","","","","","Tue May 20 17:44:10 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01333 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 44 to 329 (E-value = 2.6e-54) place AA01333 in the Caps_synth family which is described as Capsular polysaccharide synthesis protein (PF05704)","","","","","Kolkman MA, Wakarchuk W, Nuijten PJ, van der Zeijst BA.Capsular polysaccharide synthesis in Streptococcus pneumoniae serotype 14: molecular analysis of the complete cps locus and identification of genes encoding glycosyltransferases required for the biosynthesis of the tetrasaccharide subunit.Mol Microbiol. 1997 Oct;26(1):197-208.PMID: 9383201","","Tue May 20 17:44:10 2003","1","","8","" "AA01334","901746","900886","861","ATGAAAAATCACAATGAAAATCAATCAATTACAATAGTAACGGCATTCTTTGATATTGGTAGGGGTGACCTCCAATCAAAAGAAGAATTTCCTAGTTACCTCACCAGAACAAATGATACCTATTTTGAATATTTTACCAAACTGGCAACTTTAGATAATCCAATGGTAGTTTTTACAAGTTACGAGCATATTGAGAGAGTAAAGAATATTAGAGGAACCAAACCTACAACAATTATCCCATTTGATATTAATAAATTTCGTAAAACCTTAGATTCAATTAAAAATATTCAAAAAAGTGAAAGCTTTACTTCTAAAATCAATCCAGAAGTGATCAAGAACCTTGAGTATTGGCTTCCAGAATATGTCTTAATAAATAACTTAAAACCATACTTTTTATATAAGGCAATAAAGTCAAAACTAGTTAAAACCGAACTTGTAGCATGGGTAGATTTTGGATATGTAAGAAACGATGAAACGCTGAATAATATCAAAGAATGGCGGTATAATTTTGAACTAAATAAAGTAAACTTTTTTACAATAAGAAAAAATTATAAACTAAAATCAAAAGAAGATGTTTATCATGCAATGTTTAATAATATTATATATGTTATTGGTAGCGTAATAGTCAGTTCAAGAGAACAATGGAAAATTTTCTTTAAAGATATTTTATCCACACAAAAGAGGTTACTTAGAACACAAATAGTAGATGATGACCAAGGTGTTTATCTAATGTGCATTTTTAATAAAAAGGATAATTATAAACTAAATTACTTAGGAAAAGACAATTGGTTTCATATATTTAGAAAATATGATAAAACCAGTAAAATATCATTAAAAGAAAAAATAAAAGATATATTTATC","","","34443","MKNHNENQSITIVTAFFDIGRGDLQSKEEFPSYLTRTNDTYFEYFTKLATLDNPMVVFTSYEHIERVKNIRGTKPTTIIPFDINKFRKTLDSIKNIQKSESFTSKINPEVIKNLEYWLPEYVLINNLKPYFLYKAIKSKLVKTELVAWVDFGYVRNDETLNNIKEWRYNFELNKVNFFTIRKNYKLKSKEDVYHAMFNNIIYVIGSVIVSSREQWKIFFKDILSTQKRLLRTQIVDDDQGVYLMCIFNKKDNYKLNYLGKDNWFHIFRKYDKTSKISLKEKIKDIFI","900886","","HtrL protein involved in lipopolysaccharide biosynthesis (ADP-L-glycero-D-mannoheptose-6-epimerase)","Cytoplasm","","
noIPR
unintegrated
unintegrated
PTHR21579\"[178-268]TFAMILY NOT NAMED
PTHR21579:SF3\"[178-268]Tgb def: HtrL protein


","No hits to the COGs database.","","Residues 9 to 287 match (4e-60) PD:PD191347 which is described as COMPLETE PROTEOME LIPOPOLYSACCHARIDE BIOSYNTHESIS HTRL INVOLVED T11F9.12 ","","","","","","","","","","","","Wed Feb 19 15:07:01 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01334 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Pegues,J.C., Chen,L.S., Gordon,A.W., Ding,L. and Coleman,W.G. Jr.Cloning, expression, and characterization of the Escherichia coliK-12 rfaD geneJ. Bacteriol. 172 (8), 4652-4660 (1990)PubMed: 2198271 Aronson,B.D., Ravnikar,P.D. and Somerville,R.L.Nucleotide sequence of the 2-amino-3-ketobutyrate coenzyme A ligase (kbl) gene of E. coliNucleic Acids Res. 16 (8), 3586 (1988)PubMed: 3287333","","Wed Feb 19 15:07:01 2003","1","","8","" "AA01335","902133","904169","2037","GTGCCTGCGGAGCAGTTGAAGACAGTGCTGGCTTGCATTGATGAGGTTTCCTTATTTTCTCCGCAAAGCTGGCAGTTTTTGCAGTGGGCGGCGGGGTATTATCACGCGCCCTTGGGGGAAGTGTTGTCGCAGGCGTTGCCGGTGAAATTGCGGCAGGGCGAAAGTGCGGTGGAAAACCCAAGTGTTTTTTGGAAACCGACCGCACTTGGTGAGCAGGCATTGGCGCAGGGCTTATTGAAACGCGCGAAGAAGCAGCTTGAAGCGTTGCAGGCGGCGAATGATTTGCCGGAGAAAGGCAACAACCCTTTTAGTGCGGCGATTTGGTCGGCGCTGAAAGCCAAAGATTACGTCACGGAAGTTGCTCTGGAAACGGAAATCCAAACCTGGCAGCAACAATTAGGCAATAAGCCGCTTGTGAATAAGGCGGATCGTTTAACCTTAAACAAGTCGCAGGCGTTAGTGTTCAGTCAGTTGAAATTTACTCAGGGTTTTGTCCCGTGGTTGTTGGACGGCGTGACGGGTTCCGGCAAAACGGAAATCTATTTGCAATTTATCGAAGAGATTTTGCAGCAAGGCAAGCAAGTGCTGGTGTTGGTGCCGGAAATCAGTTTAACGCCACAAACGGTGCGGCGTTTTCAGGCGCGTTTTAATGTGGTCATTGACGTGCTGCATTCCAATCTGAACGACACGCAGCGTTTGCAGGTGTGGCAGCGGGCGCGCAACGGGCAAAGTGCGGTCGTTATCGGCACCCGATCTGCGTTGTTCACGCAATTTTCCGAGTTGGGCGTGATTATTATTGATGAAGAACATGATGCCTCTTTCAAACAGCAGGACGGCTGGCGTTATCACGCGCGTGATTTGGCGATTGTGTATGCGAAACAGCTGAATATCCCGATTTTAATGGGGTCGGCAACGCCAAGTTTGGAAAGCCTGAATAATGTGCAAAGCGGTAAATATCGCCATTTGTCGTTGTCGGAAAAAGCCAATAATTCCACCGCACTTAAACAGCAGATTATCGATTTAAAACGTCAACCTATGCACAACGGGCTGTCTGATGTGTTGTTAAAACGTATGCAGGCGCATTTGGAAAAAGGCAATCAGGTGTTGTTGTTTTTGAATCGGCGCGGTTTTGCGCCGGTGCTGTTGTGCCACGAATGCGGCTGGATGGCGGAATGTCGCCATTGCGATAAGCCTTACACCTATCATCAGCAACATCATGTGTTACGCTGCCATCATTGCGCTTCGCAGAAGCCGATTCCACGCCAATGCGGCAATTGCGGTTCCACACAATTAATCACCACGGGCTTGGGTACGGAACAGCTGGAAGCCACCTTAAAAGACGTTTTTCCTCACTACGGCATTGCCCGCATCGACCGCGACACAACGGCACGTAAAGGCAAGCTGGAAGGCTATTTGGAAGATATTAACCAAGGCAAAAGTCAAATTCTTATCGGCACTCAAATGCTGGCGAAAGGGCATCATTTCCCGAATGTCACGCTGGTGGCATTGGTGAATGTGGATAGCGCCTTATTTTCATTGGATTTTCGTGCGGAAGAACGATTGGCGCAGCTTTATATGCAGGTGGCGGGGCGTGCAGGGCGTGGTGTACAGCAAGGCGAAGTGTTACTGCAAACCCATTACCCCGAGCACCCGTTACTGCAAAGTCTGTTACAAAAAGGTTATAACCAATTTGCGCAAAATGCCTTGGCGTTGCGTAAAAGTATGGGTTTGCCGCCTTTCGGTTCGCAGGCATTATTCAAGGCGCAAAGCCGTTATAGCGAAGAAGCTGAACAATTGCTGGCGCAGTTTGTCGAATATTTACAACAGATTAAGCGAAACACGGCGCCCGAGTTGCAAATTCTCGGTCCGATGCCGGCGCCGTTCAGTAAAAAAGCGGGGCAATATCGTTGGCAGCTATTACTGCAGCATCCTTCCAGAGCGGCGTTGCAGCAGGTGTTGATGGAATTTTGGTGTTATCAGGGCGATCAACCCACAAAAGTGCGGTGGATTTTAGACGTGGATCCGTTGGATCTGAGT","","","82300","VPAEQLKTVLACIDEVSLFSPQSWQFLQWAAGYYHAPLGEVLSQALPVKLRQGESAVENPSVFWKPTALGEQALAQGLLKRAKKQLEALQAANDLPEKGNNPFSAAIWSALKAKDYVTEVALETEIQTWQQQLGNKPLVNKADRLTLNKSQALVFSQLKFTQGFVPWLLDGVTGSGKTEIYLQFIEEILQQGKQVLVLVPEISLTPQTVRRFQARFNVVIDVLHSNLNDTQRLQVWQRARNGQSAVVIGTRSALFTQFSELGVIIIDEEHDASFKQQDGWRYHARDLAIVYAKQLNIPILMGSATPSLESLNNVQSGKYRHLSLSEKANNSTALKQQIIDLKRQPMHNGLSDVLLKRMQAHLEKGNQVLLFLNRRGFAPVLLCHECGWMAECRHCDKPYTYHQQHHVLRCHHCASQKPIPRQCGNCGSTQLITTGLGTEQLEATLKDVFPHYGIARIDRDTTARKGKLEGYLEDINQGKSQILIGTQMLAKGHHFPNVTLVALVNVDSALFSLDFRAEERLAQLYMQVAGRAGRGVQQGEVLLQTHYPEHPLLQSLLQKGYNQFAQNALALRKSMGLPPFGSQALFKAQSRYSEEAEQLLAQFVEYLQQIKRNTAPELQILGPMPAPFSKKAGQYRWQLLLQHPSRAALQQVLMEFWCYQGDQPTKVRWILDVDPLDLS","904169","From GenBank (gi:1172617): This protein recognizes a specific hairpin sequence on phiX ssDNA. This structure is then recognized and bound by proteins PriB and PriC. Formation of the primosome proceeds with the subsequent actions of DnaB, DnaC, DnaT, and primase. PriA then functions as a helicase within the primosome.","primosomal protein N'","Cytoplasm, Periplasm","","
InterPro
IPR001650
Domain
Helicase, C-terminal
PF00271\"[446-536]THelicase_C
SM00490\"[439-536]THELICc
PS51194\"[333-576]THELICASE_CTER
InterPro
IPR005259
Family
Primosomal protein n
TIGR00595\"[168-676]TpriA: primosomal protein N'
InterPro
IPR011545
Domain
DEAD/DEAH box helicase, N-terminal
PF00270\"[148-314]TDEAD
InterPro
IPR014001
Domain
DEAD-like helicases, N-terminal
SM00487\"[143-337]TDEXDc
InterPro
IPR014021
Domain
Helicase superfamily 1 and 2 ATP-binding
PS51192\"[158-324]THELICASE_ATP_BIND_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[472-558]Tno description


","No hits to the COGs database.","","Residues 1 to 47 match (5e-07) PD:PD003500 which is described as HELICASE PROTEOME COMPLETE DNA ATP-BINDING FACTOR PRIMOSOMAL REPLICATION COUPLING DNA-BINDING ","","","","","","","","","","","Wed Jan 8 15:20:55 2003","Wed Jan 8 15:20:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01335 is paralogously related to AA00861 (5e-11), AA02303 (4e-06) and AA02480 (5e-04).","","","","","","Residues 137 to 337 (E-value = 1.3e-05) place AA01335 in the DEAD family which is described as DEAD/DEAH box helicase (PF00270)","","","","","Lee,E.H., Masai,H., Allen,G.C. Jr. and Kornberg,A. The priA gene encoding the primosomal replicative n\" protein of Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 87 (12), 4620-4624 (1990) PubMed: 2162050 Nurse,P., DiGate,R.J., Zavitz,K.H. and Marians,K.J. Molecular cloning and DNA sequence analysis of Escherichiacoli priA, the gene encoding the primosomal protein replicationfactor Y Proc. Natl. Acad. Sci. U.S.A. 87 (12), 4615-4619 (1990) PubMed: 2162049 Ouzounis,C.A. and Blencowe,B.J. Bacterial DNA replication initiation factor priA is related to proteins belonging to the \"DEAD-box\" family Nucleic Acids Res. 19 (24), 6953 (1991) PubMed: 1662369 ","","Wed Jan 8 15:20:55 2003","1","","","" "AA01336","904196","904375","180","ATGGCACAATTTTTGCGTAGAATTATCGGCATTTTTTATCATTGTGATTTCATTGTTCATTTGGTTTTATTGAGACAGGTTTTATTGTGGCACAACGTGATTACGCCGCCCGCAATGGCGCGAAGAAAAAGAAGAAACAGAAAAAAAGTAATAAACCCCTATTATTTGTCATTGCCGGCG","","","7240","MAQFLRRIIGIFYHCDFIVHLVLLRQVLLWHNVITPPAMARRKRRNRKKVINPYYLSLPA","904375","","hypothetical protein","Cytoplasm, Periplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-29]?signal-peptide
tmhmm\"[9-29]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 09:41:53 2004","Thu Feb 26 09:41:53 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01336 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:41:53 2004","","","","","","","","","","","","","1","","","" "AA01337","904375","905091","717","GTGATTGTGGCGGCGTTTGCATTCGGTCTTTATTTATTAAAAGAAAAAGCGCCGGAACCGGTGGTGCAACCGGTAGAAACCACAGAAAAAACGCAACCGAAAAGCGTGTTACCGAATCGTCCGGAAGAAGTGTGGAGCTATATTAAAGCCTTGGAAACCCGCACTGTGCCTATTGATGACAACCCGAAATCGTTAGATAAAAATATGCGTTTAACGGAAGAACAACGCAAGATTTTACAGGCAATGGAAAAAGAACAGAAACAGGCAGAGCTGGCGAAAACCAAAGCGGCAGAAGCTCAACAACAAGCGGCACAACAGTCTGGTCAATTTACAGCGCAGCAACCGCCGCAACAACAACCAAAACCGCAGCCTCAAGTGGTAGAAGCGAAGAAAGCTACACCACCGAGAGAAGAGAAAAAAGCGGAGCAAACGGTGAAAGCCGAATCAACAAAGAAACCTGAACCGCAACCTGCGCCACCGCAAACCCCGGCATCCAATGGCGGCGAGCGAAAATACGGTTTACAATGCGGTGCTTTCAAAAACAAAGGGCAAGCAGAAAATTTACAGGCGCGTCTGGCGATACTCGGCTTGCCGGCGAGGGTGAATGAAAGTGCCGATTGGAACCGCGTGGTGGTTGGTCCGGCAGGTGATCGTAATGCCGCGGTGAAGATGCAGGAAAAAGCCAAAAGCGTGATTAGTTGCGTAGTTATCGGGATG","","","29673","VIVAAFAFGLYLLKEKAPEPVVQPVETTEKTQPKSVLPNRPEEVWSYIKALETRTVPIDDNPKSLDKNMRLTEEQRKILQAMEKEQKQAELAKTKAAEAQQQAAQQSGQFTAQQPPQQQPKPQPQVVEAKKATPPREEKKAEQTVKAESTKKPEPQPAPPQTPASNGGERKYGLQCGAFKNKGQAENLQARLAILGLPARVNESADWNRVVVGPAGDRNAAVKMQEKAKSVISCVVIGM","905091","","cell division protein N","Periplasm, Inner membrane","","
InterPro
IPR007730
Domain
Sporulation/cell division region, bacteria
PF05036\"[168-238]TSPOR
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.1070\"[163-237]Tno description


","BeTs to 6 clades of COG3087COG name: Cell division proteinFunctional Class: DThe phylogenetic pattern of COG3087 is ------------b-efghsn------Number of proteins in this genome belonging to this COG is","","Residues 29 to 79 match (3e-14) PD:PD084981 which is described as PROTEOME COMPLETE HI0896 PM1136 ","","","","","","","","","","","","Wed Jan 8 15:40:03 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01337 is paralogously related to AA02832 (3e-06).","","","","","","Residues 168 to 203 (E-value = 1.4e-07) place AA01337 in the SPOR family which is described as Sporulation related repeat (PF05036)","","","","","Hale CA, de Boer PA. ZipA is required for recruitment of FtsK, FtsQ, FtsL, andFtsN to the septal ring in Escherichia coli. J Bacteriol. 2002 May;184(9):2552-6. PMID: 11948172 Chen JC, Beckwith J. FtsQ, FtsL and FtsI require FtsK, but not FtsN, forco-localization with FtsZ during Escherichia coli celldivision. Mol Microbiol. 2001 Oct;42(2):395-413. PMID: 11703663 Addinall SG, Cao C, Lutkenhaus J. FtsN, a late recruit to the septum in Escherichia coli. Mol Microbiol. 1997 Jul;25(2):303-9. PMID: 9282742 Dai K, Xu Y, Lutkenhaus J. Topological characterization of the essential Escherichiacoli cell division protein FtsN. J Bacteriol. 1996 Mar;178(5):1328-34. PMID: 8631709 ","","Wed Jan 8 15:40:03 2003","1","","","" "AA01338","905107","905208","102","ATGAGAAAGTGCGGTAAAAAATCACCGCACTTTTTTTATTTTCAGCTTGCCAAACAAGAAAAAATCAATAAAATGAACGAACGTTCATTCAGCGCAATGTAT","","","4157","MRKCGKKSPHFFYFQLAKQEKINKMNERSFSAMY","905208","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 09:43:55 2004","Thu Feb 26 09:45:39 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01338 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:43:55 2004","","","","","","","","","","","","","1","","","" "AA01339","905294","905857","564","ATGAATCAATCTGAAACGGATATGATCGAGCGGATTTTTACTGCCACCGATGCATTAATGGCAACGGTGGGGCTGCCAAACTTGTCTATGCACAAGATTGCCAGAGAAGCAAAAATCTCGCCGGGGACGATTTATATTTATTTTAAAAATAAAGAGGAATTGCTGACCCAGTTTGCCCGATATATTTTTCAAAATTTCCAGGATGTGTTGAAGGAAGGCTATGATGAGAGGCAGCCGTTTTTTCAGCAATATCGAAAAATGTGGTGGAATATTTGGCATTTCTTAGAAGCGGAACCTACTATCATGGCGAATATGGGGCAATACGAGTCTTTGCCGGGCTTTTCCGATATTTGTCAAAAATGGGAAAGTGACAGCATCTGGTATCATTTTTGCGTCAAAGCAAAGGCGGCGGGAGAACTGGCTGATGTGCCTCCTCCTATTTTATTTGCGATTTCATTGGAAAGTGCTTTCAATATCGCCTTTAAATGCCGACATTTTTGCGCGCAGGTTTCAATGGAAATGCTGGAGGCCGTCATTGAACGGACTTGGCTTGCTATTAAAAAT","","","21988","MNQSETDMIERIFTATDALMATVGLPNLSMHKIAREAKISPGTIYIYFKNKEELLTQFARYIFQNFQDVLKEGYDERQPFFQQYRKMWWNIWHFLEAEPTIMANMGQYESLPGFSDICQKWESDSIWYHFCVKAKAAGELADVPPPILFAISLESAFNIAFKCRHFCAQVSMEMLEAVIERTWLAIKN","905857","","transcriptional regulator, AcrR/TetR family","Cytoplasm","","
InterPro
IPR001647
Domain
Bacterial regulatory protein, TetR
PR00455\"[12-25]T\"[33-56]THTHTETR
PF00440\"[12-58]TTetR_N
PS50977\"[6-66]THTH_TETR_2
PS01081\"[24-55]THTH_TETR_1
InterPro
IPR012287
Domain
Homeodomain-related
G3DSA:1.10.10.60\"[10-69]Tno description


","No hits to the COGs database.","Significant hit ( 7e-13) to 1/1 blocks of the IPB001647 family, which is described as \"Bacterial regulatory proteins, TetR family\". Interpro entry for IP:IPR001647. IPB001647 24-54 6.8e-13","Residues 3 to 55 match (9e-12) PD:PD470553 which is described as TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR PROTEOME COMPLETE FAMILY TETR REGULATOR ","","","","","","","","","","","","Wed Feb 19 14:46:34 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01339 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 12 to 58 (E-value = 8.8e-13) place AA01339 in the TetR_N family which is described as Bacterial regulatory proteins, tetR family (PF00440)","","","","","","","","1","","","" "AA01340","905886","907079","1194","ATGAGTTCAGCTCAAATCAACAGACCAAAGCGTTCCCATGTGTTCTTTTTGAAACTGGCTTTGGGTGTATTCGTATTACTTTTTGCCGCAATGATTGTGATGAATTATATGAAATCAAAAGGCATTGCGGATTTCCTTGCCAATCAAGGCGAATCCCCGTCACCGGTGACAGCAATGACTGTTACTTCGCAACAGTGGACACCGGTTATTGAAACCACCGGTCTGGTGCGTCCGAACCAAGGGGCTATATTAAGTGCACAAAGTGCGGGTACGATTTCAAAAGTTTTAGTGGAGAACGGACAAAACGTCAAGAAAGGTGATGTGTTGGTGGAATTAGATAGTTCCGTTGAACGCGCCGGTTTACGGGCTGCCGAAGCGCAAGTGATTTCGTTGCGTCAAACCTATCAACGTTATGCGAATCTGGCAAAAAGCGGTGGCGTTTCCCGCCAGGAATTGGATAACGCCAAAGCAGCGTATGATGCGCAGGTTGCCAATGTGGAATCTTTAAAAGCCACCGTTGAGCGTCGCCAAATCCTTGCACCGTTTGACGGCAAGGCGGGTATTGTGAAAGTGAATGTGGGGCAATATGTATCAAACGGCACCGAAATCGTGCGTGTGGAAGACCGCAGTTCCATGAAAGTGGATTTTTCCATTGCACAAAATTTGTTGGATGAATTACGTCTTGGTCAAAAAGTGACTGCCACTGCCGATGCCCGCTTAGGGGAAACCTTTGCTGCGAAAGTGACTGCTATCGAACCGGCAATCAGTTCTTCTACCGGTTTAGTTGATGTGCAAGCCACATTCGAGCCGGAGGATGGAGTGAAATTATTATCCGGTATGTTTACCCGTTTAAACGTGGCATTGCAGACGGAATACGATCAAATCGTGGTGCCGCAAGTGGCGGTGAGCTACAACATGTATGGCGAATCACTTTATATTTTGACCGCACTTTCTGATGAAGAAAAAGAAAAATTCGCCTCAAAAGGCGATGTAAACAAAATGTACCGCGCCCATCAAATCACCGTATTTACCAAAGATCGCCAAGGCATCTATTCTCAATTAAAAGGCGATGAAGTGAAAATCGGCGATAAAATCATTACCGGCGGTCAGCAAAGTTTAAGCAACGGCTCGTTAGTGATTGTTGTGGATAAACAAGGCGTGGGTACCACTCAACCGGCAAGTAAAACTAACCTC","","","51867","MSSAQINRPKRSHVFFLKLALGVFVLLFAAMIVMNYMKSKGIADFLANQGESPSPVTAMTVTSQQWTPVIETTGLVRPNQGAILSAQSAGTISKVLVENGQNVKKGDVLVELDSSVERAGLRAAEAQVISLRQTYQRYANLAKSGGVSRQELDNAKAAYDAQVANVESLKATVERRQILAPFDGKAGIVKVNVGQYVSNGTEIVRVEDRSSMKVDFSIAQNLLDELRLGQKVTATADARLGETFAAKVTAIEPAISSSTGLVDVQATFEPEDGVKLLSGMFTRLNVALQTEYDQIVVPQVAVSYNMYGESLYILTALSDEEKEKFASKGDVNKMYRAHQITVFTKDRQGIYSQLKGDEVKIGDKIITGGQQSLSNGSLVIVVDKQGVGTTQPASKTNL","907079","","possible lipoprotein; possible HlyD family secretion domain protein; possible membrane fusion protein","Periplasm, Inner membrane, Outer membrane","","
InterPro
IPR006143
Family
Secretion protein HlyD
PF00529\"[80-174]THlyD
TIGR01730\"[56-382]TRND_mfp: efflux transporter, RND family, MF
noIPR
unintegrated
unintegrated
signalp\"[1-29]?signal-peptide
tmhmm\"[15-37]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.1e-13) to 2/3 blocks of the IPB002215 family, which is described as \"HlyD family secretion protein\". Interpro entry for IP:IPR002215. IPB002215A 78-114 2.3e-10 IPB002215B 177-211 0.12Significant hit ( 5.7e-07) to 1/7 blocks of the PR01490 family, which is described as \"Gram-negative bacterial RTX secretion protein D signature\". Prints database entry for PR:PR01490. PR01490B 92-112 5.7e-07","Residues 76 to 281 match (5e-10) PD:PD405486 which is described as MEMBRANE COMPLETE PROTEOME FUSION EFFLUX TRANSPORTER PREDICTED ACRA/ACRE SYSTEM TYPE ","","","","","Tue Feb 18 16:36:43 2003","","","","","","","Wed Jan 8 15:52:05 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01340 is paralogously related to AA02081 (8e-17), AA01732 (3e-10), AA02139 (2e-08) and AA01986 (4e-04).","","","","","","","","","","","","","","1","","","" "AA01341","907024","910191","3168","TTGTTGTGGATAAACAAGGCGTGGGTACCACTCAACCGGCAAGTAAAACTAACCTCTAATTGGGACCAGCGAATGAAATTTACCGATATATTTATTCGACGCCCGGTACTTGCGGTTTCAATCAGCCTGTTAATTATCATTCTTGGGTTGCAGGCGATTTCCAAATTGACGGTGCGTGAATACCCTAAAATGACCACAACCGTAATTCAGGTTTCCACAGTGTATCCTGGTGCAGATGCCAACTTGATCCAGGCATTTGTAACTTCGAAGCTGAAGGAAGCGGTGGCGCAGGCAGATAACGTGGATTATATGTCTTCCTCTAGTAGCCCGAGCAGCTCTACCATTACGGTAAAAATGAAATTAAATACTGACCCGAACGCAGCACTTGCCGATGTGTTGGCGAAGGTGAACTCGGTACGTTCCGAGTTGCCAAAGGGGATAGAAGACCCGACAGTGAGCTCATCAACCGGTGGTTCGGGGATTATGTATATTAGCTTCCGCTCCGGTAAATTAGATGCCAGCCAGGTGACCGACTACATTGAACGTGTGGTAAAACCGCAGTTCTTCACCGTTGAAGGGGTGGCGAGCGTGCAAATTTTCGGGGCCTCCGAATATGCGCTGCGTATTTGGTTGGATCCGCAAAAAATGGCGGCGCAAAATCTTTCCGCGACACAAGTGATGTCCGCCTTGTCGGCAAATAACGTGCAAACGGCGGCAGGTAACGATAACGGTTTTTATGTGGTATATAAAAACAAAGTGGATACCACCACGAAATCCGTGTATGAATTAAGCAAACTTATTGTGTATTCCAGTGGCGATAAATTGGTTCGCTTACGTGATATTGCGGATATTGAATTGAATAAATCCAGCGATACCGCCCGTGCGGTGGCGAATGGTGCCGATTCGGTGGTGTTGGCGATTAATCCGACCTCTTCCGCAAACCCGTTAACCGTAGCGGAAAAAATTCTGCCGTTGTATGAAAACATTAAAAATAACCTGCCGGATGCCATTCAAACCGACATTTTGTATGACCGCACTATTGCTATCAATAACTCCATTGATGAAGTGGTGAAAACCATCATTGAAGCGACCATTATCGTATTGGTGGTGATTACCATGTTTATCGGTTCCTTCCGTACGATTTTAATTCCGGTAATTACCATTCCGATTTCCCTTATCGGGGTAATCATGATGCTGCAAACCTTGGATTTCTCCATTAACCTGATGACTTTGCTTGCCTTGATTTTGGCGATTGGGTTGGTGGTGGATGATGCTATTGTGGTATTGGAAAACGTTGACCGTCACATTAAACTGGGCGAAACTCCATTCCGCGCAGCGATTATCGGGACCCGTGAAATTGCCGTGCCGGTGATTTCTATGACTATCGCTTTGATTGCGGTGTATTCTCCGATGGCATTGATGGGCGGGATTACCGGTACGTTATTTAAAGAGTTTGCTTTAACCCTTGCCGGTGCGGTGTTCATTTCCGGTATCGTGGCATTAACTCTGTCGCCGATGATGACCAGTAAATTACTGAAAGCACACGATCAACCAAGTAAATTGGAAGAACGTGTGAACCGCACTTTAACGAGGGTTAACAATATTTACGCATCCATTTTGGATTTAGTGATGCAAAACCGTAAATGTATGTTGGTGTTCGCTGCTATTATTTTTGCGACCCTGCCGGTGTTGTTTAAATCGCTATCCAGCGAGTTGACGCCGGCGGAAGATAAGGGCGCATTCTTGGCAATCGGTTCTGCACCTTCTAACGTGAACGTGGATTATGTGCAAGCTGCCATGGCACCGTACCAGGAAATTCTGACCAACACGCCTGAAGTGCAGTTCGCCATGACCATTTCCGGTGTGCCGAGTTCCAACCAATCTCTTAACGTAGTGACCTTAAAAGACTGGAGCGAACGTTCCAAGAGTCAGGCGCAAGTATTGGAAGAATTGAACAACAAAGCGAAATCCATTCCGGAAGTGTCCGTCAGTGGCTTCGCTTTCCCGGAAATTAACACCGGAGAACAAGGACCACCAATTGGTTTTATCATTAGTACATCACAAGGTTATAATGATTTGGCAAGTGTTGCCGGTAAATTTTTGGAAGCGATGCAAAAATCAGGTAAATTCGTTTACACGAACTTGGATTTGAAATTTGATACGGCACAAATGCACATTAAAATAGACCGTGAAAAAGCCGGTACTTACGGCATCACCATGCAACAAATCAGTGCCACATTGGGTAGTTTTCTTTCTGCAGCAACGGTTGAGCGGGTAGATATTGACGGTCGCGCCTATAAAATTATTTCACAGGTAAAACGTGAAAATCGTTTATCGCCGGAAAGCTGGAAAAATTATTATGTCAGCGCAGCCAACGGCAAATCTGTACCGTTAAGTAGCCTGGTTACTATGTCATTAGAACCGCAGCCAAGCTCATTACCACGTTTCAGCCAGTTGAACTCTGCTGTAATCAGTGCTGTGCCAATGCCGGGTTCTTCCATCGGGGATGCCATCCAATGGTTGCAAGACAACGCCCAAGAGTTATTACCACAAGGCTATAACTACGATTTTAAAGGCGAAGCGCGTCAGTTGGTACAAGAGGGCAATGCCTTAGCGGTGACCTTCGTGTTGGCGGTGGTTATCATCTTCTTGGTGCTGGCGATTCAGTTTGAATCCATTCGTGACCCATTGGTGATCATGATTTCCGTACCGCTGGCAATTAGTGGTGCGTTGTTGGCACTCAACTTCTTCGGCTTTATTGGCGTGGCGGGCAGTACCCTGAACATTTATTCGCAGGTGGGCTTGATTACGCTGGTGGGCTTGATCACCAAACACGGTATTTTGATGTGTGAAGTGGCGAAAGAAGAACAGTTAAACCACGGTAAAACCCGTATTGAAGCCATTACCGAGGCGGCGAAAGTGCGGTTGCGTCCGATTCTGATGACTACCGCTGCGATGATTGCCGGTCTTATTCCGTTGCTTTACGCAACCGGTGCCGGCGCGGTGTCCCGTTTCAGTATCGGTATCGTCATCGTTGCCGGTTTGGCAATCGGTACGCTGTTCACCTTGTTCGTGTTGCCGGTGATTTATTCTTACATCGCAAGCGAACACAAACCGCTACCGGAATTTGATGAAAACATCAAACCGATTGAAGGTGAGATAAATCAT","","","114343","LLWINKAWVPLNRQVKLTSNWDQRMKFTDIFIRRPVLAVSISLLIIILGLQAISKLTVREYPKMTTTVIQVSTVYPGADANLIQAFVTSKLKEAVAQADNVDYMSSSSSPSSSTITVKMKLNTDPNAALADVLAKVNSVRSELPKGIEDPTVSSSTGGSGIMYISFRSGKLDASQVTDYIERVVKPQFFTVEGVASVQIFGASEYALRIWLDPQKMAAQNLSATQVMSALSANNVQTAAGNDNGFYVVYKNKVDTTTKSVYELSKLIVYSSGDKLVRLRDIADIELNKSSDTARAVANGADSVVLAINPTSSANPLTVAEKILPLYENIKNNLPDAIQTDILYDRTIAINNSIDEVVKTIIEATIIVLVVITMFIGSFRTILIPVITIPISLIGVIMMLQTLDFSINLMTLLALILAIGLVVDDAIVVLENVDRHIKLGETPFRAAIIGTREIAVPVISMTIALIAVYSPMALMGGITGTLFKEFALTLAGAVFISGIVALTLSPMMTSKLLKAHDQPSKLEERVNRTLTRVNNIYASILDLVMQNRKCMLVFAAIIFATLPVLFKSLSSELTPAEDKGAFLAIGSAPSNVNVDYVQAAMAPYQEILTNTPEVQFAMTISGVPSSNQSLNVVTLKDWSERSKSQAQVLEELNNKAKSIPEVSVSGFAFPEINTGEQGPPIGFIISTSQGYNDLASVAGKFLEAMQKSGKFVYTNLDLKFDTAQMHIKIDREKAGTYGITMQQISATLGSFLSAATVERVDIDGRAYKIISQVKRENRLSPESWKNYYVSAANGKSVPLSSLVTMSLEPQPSSLPRFSQLNSAVISAVPMPGSSIGDAIQWLQDNAQELLPQGYNYDFKGEARQLVQEGNALAVTFVLAVVIIFLVLAIQFESIRDPLVIMISVPLAISGALLALNFFGFIGVAGSTLNIYSQVGLITLVGLITKHGILMCEVAKEEQLNHGKTRIEAITEAAKVRLRPILMTTAAMIAGLIPLLYATGAGAVSRFSIGIVIVAGLAIGTLFTLFVLPVIYSYIASEHKPLPEFDENIKPIEGEINH","910191","","acriflavine resistance protein","Inner membrane, Cytoplasm","","
InterPro
IPR001036
Family
Acriflavin resistance protein
PR00702\"[34-58]T\"[62-80]T\"[352-375]T\"[379-400]T\"[407-431]T\"[460-483]T\"[485-508]T\"[563-580]T\"[626-640]TACRIFLAVINRP
PF00873\"[27-1034]TACR_tran
noIPR
unintegrated
unintegrated
signalp\"[1-52]?signal-peptide
tmhmm\"[30-50]?\"[360-378]?\"[380-398]?\"[404-422]?\"[453-471]?\"[485-505]?\"[549-569]?\"[868-888]?\"[903-923]?\"[929-949]?\"[982-1004]?\"[1010-1030]?transmembrane_regions


","BeTs to 15 clades of COG0841COG name: Cation/multidrug efflux pumpFunctional Class: QThe phylogenetic pattern of COG0841 is -------qvd--bcefghsnujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 2.2e-90) to 9/9 blocks of the PR00702 family, which is described as \"Acriflavin resistance protein family signature\". Prints database entry for PR:PR00702. PR00702A 34-58 1.6e-07 PR00702B 62-80 3.1e-07 PR00702C 352-375 5.8e-09 PR00702D 379-400 7.6e-08 PR00702E 407-431 6.2e-17 PR00702F 460-483 1.2e-11 PR00702G 485-508 7.6e-11 PR00702H 563-580 0.0095 PR00702I 626-640 0.0002","Residues 344 to 396 match (2e-13) PD:PD594374 which is described as PROTEOME COMPLETE EFFLUX TRANSMEMBRANE RESISTANCE SYSTEM TRANSPORTER RND PROBABLE MEMBRANE ","","","","","","","","","","","","Wed Jan 8 15:57:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01341 is paralogously related to AA02780 (4e-04).","","","","","","","","","","","Ma,D., Cook,D.N., Alberti,M., Pon,N.G., Nikaido,H. and Hearst,J.E. Molecular cloning and characterization of acrA and acrE genes of Escherichia coli J. Bacteriol. 175 (19), 6299-6313 (1993) PubMed: 8407802 Ma,D., Cook,D.N., Alberti,M., Pon,N.G., Nikaido,H. and Hearst,J.E. Genes acrA and acrB encode a stress-induced efflux system of Escherichia coli Mol. Microbiol. 16 (1), 45-55 (1995) PubMed: 7651136 Kawabe,T., Fujihira,E. and Yamaguchi,A. Molecular construction of a multidrug exporter system, AcrAB: molecular interaction between AcrA and AcrB, and cleavage of the N-terminal signal sequence of AcrA J. Biochem. 128 (2), 195-200 (2000) PubMed: 10920254 ","","Wed Jan 8 15:58:11 2003","1","","","" "AA01342","910348","911145","798","ATGACTATTGACGACATTGATTTTAACGAACTCTATAAACAACATCTTATCGCCTGCCATCATTACAATTTGCCATCGGAAAAATGGGATAAAAAGGCGACGAAAATGGCGGAAAATCCGGTAGGCAAAACCAGTCGTTACAATCAGCAATTGCTGCAAACCATACAGGTGCAGTCGCATGAAACCGTGCTCGACATCGGTTGCGGACCGGGCACCTTTGCCCTTCCTTTGGCGCAACAATGCCGACAGGTTTACGCGTTGGATTACAGCGTGGGGATGCTTGATGTGCTGGCGGATTATAAGCAAAAGCTGCAACTGGAAAATGTCACCTTAATTCACCGTTCCTGGGTGGAGGATTGGGCAGATGTGCCGCAGGCGGATGTGGTTTTAGCGTCGCGTTCCACTTTGGTGGATGATTTGGACGATATGATCGACAAACTTCGCACCAAAGCGAAAAAACGCGTTTATCTTACGTCTATCACACAACGGCATTTTTTAGATGAAGGGGTTTTCAGCGCCATCGGGCGCGAAGACATCGGCTTTCCGAGTTACATTTATTTGCTTAATCGGCTTTACCAAAAAGGCATTCAAGCCAATCTGAATTTCATCGAAACGGAATCCGGTCGTTTTATGGGCGAGACCTACGAGGATTTACTCAACTCCGTCGAATTTTCGTTAGGACAGTTGAGTGAAAAAGAAAAACAGGGGCTGGCGGCGTTTTATCGTCAAAAACAACAGAACAACGAACCCATTGCGCACGGACAACACAAATGGGCACTGATTTGGTGGAAGGTGGAA","","","30718","MTIDDIDFNELYKQHLIACHHYNLPSEKWDKKATKMAENPVGKTSRYNQQLLQTIQVQSHETVLDIGCGPGTFALPLAQQCRQVYALDYSVGMLDVLADYKQKLQLENVTLIHRSWVEDWADVPQADVVLASRSTLVDDLDDMIDKLRTKAKKRVYLTSITQRHFLDEGVFSAIGREDIGFPSYIYLLNRLYQKGIQANLNFIETESGRFMGETYEDLLNSVEFSLGQLSEKEKQGLAAFYRQKQQNNEPIAHGQHKWALIWWKVE","911145","","conserved hypotheticl protein (possible ribosomal RNA adenine dimethylase)","Cytoplasm","","
InterPro
IPR013217
Domain
Methyltransferase type 12
PF08242\"[64-157]TMethyltransf_12
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[49-132]Tno description
PTHR10108\"[49-112]TMETHYLTRANSFERASE
PTHR10108:SF15\"[49-112]T2-HEPTAPRENYL-1,4-NAPHTHOQUINONE METHYLTRANSFERASE


","BeTs to 12 clades of COG0500COG name: SAM-dependent methyltransferasesFunctional Class: Q,RThe phylogenetic pattern of COG0500 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.2e-06) to 1/3 blocks of the IPB001737 family, which is described as \"Ribosomal RNA adenine dimethylase\". Interpro entry for IP:IPR001737. IPB001737A 48-93 2.1e-06","Residues 65 to 132 match (3e-14) PD:PD074425 which is described as COMPLETE PROTEOME TRANSFERASE METHYLTRANSFERASE PHOSPHOPANTETHEINE PLASMID SMTA SYNTHASE BIOSYNTHETIC YJHP ","","","","","","","","","","","","Thu Feb 20 09:01:39 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01342 is paralogously related to AA01071 (6e-04).","","","","","","","","","","","","","","1","","","" "AA01344","911801","912745","945","ATGATAAATGCCTTTGCCCTTGAAGATGCTCGTCTGGTTCGCATTGATGAAACCACCGAGCCGTTAAATACCGCCATTTGGATCGATTTACTGGAACCGACCGTGGAAGAGCGTGAAATGTTGCAGGAAAGTTTGGGTCAGAGTTTGGCATCCTTTCTGGAATTGGAAGACATCGAGGCATCTGCACGTTTTTTTGAAGACGAAGACGGTTTGCACCTGCACTCGTTCTTTTATTGTGAAGATGAAAACGATTATGCGGATTTAGCCAGCGTGGCGTTCACCATTCGCGACGGGCGTTTGTTTACCCTGCGTGATCGCGAATTACCGGCGTTCCGTTTATATCGTATGCGTTCCCGTAATCAGCGTTTAATTGAATGTAATTCCTATGAATTATTGCTGGATTTGTTTGAAACTAAAATCGAGCAGCTGGCGGATGTGATTGAAAACGTGTACGCGGATTTGGAAAAATTAAGCCGTGTGGTGTTGGACGGCACCCAAGGGGAAGCCTTCGACGAAGCCCTGGCAACCTTAACGGAACAAGAAGACACCAGTTCCAAAGTGCGTTTGTGTTTGATGGATACGCAACGTGCGTTAAGTTTTTTGGTGCGCAAAACCCGCTTACCGGCGAACCAGTTGGAGCAGGCGCGTGAAATTTTACGAGACATTGAGTCCTTACAACCGCATAATGAATCCCTGTTCCAAAAAGTGAACTTCCTACTGCAAGCCGCGATGGGTTTCATTAATATTGAGCAGAACCGCATTATTAAAATCTTCTCCGTTGTGTCGGTAATTTTTCTACCGCCGACATTGGTGGCATCCAACTACGGCATGAACTTCAGCGATATGCCGGAGCTGGGACTGAAATTTGGTTATCCGATGGCATTGGGTTTAATGGCACTGGCGGCGTTTGCGCCGTATTGGTATTTCAAACGTAAAGGCTGGTTA","","","39136","MINAFALEDARLVRIDETTEPLNTAIWIDLLEPTVEEREMLQESLGQSLASFLELEDIEASARFFEDEDGLHLHSFFYCEDENDYADLASVAFTIRDGRLFTLRDRELPAFRLYRMRSRNQRLIECNSYELLLDLFETKIEQLADVIENVYADLEKLSRVVLDGTQGEAFDEALATLTEQEDTSSKVRLCLMDTQRALSFLVRKTRLPANQLEQAREILRDIESLQPHNESLFQKVNFLLQAAMGFINIEQNRIIKIFSVVSVIFLPPTLVASNYGMNFSDMPELGLKFGYPMALGLMALAAFAPYWYFKRKGWL","912745","","magnesium and cobalt transport protein","Cytoplasm, Inner membrane","","
InterPro
IPR002523
Family
Mg2+ transporter protein, CorA-like
PTHR21535:SF1\"[14-315]TMAGNESIUM AND COBALT TRANSPORT PROTEIN
PF01544\"[22-315]TCorA
InterPro
IPR004488
Family
Magnesium and cobalt transport protein CorA
TIGR00383\"[2-315]TcorA: magnesium and cobalt transport protei
noIPR
unintegrated
unintegrated
PTHR21535\"[14-315]TMAGNESIUM AND COBALT TRANSPORT PROTEIN/MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM8
tmhmm\"[257-275]?\"[289-309]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.6e-41) to 4/4 blocks of the IPB002523 family, which is described as \"CorA-like Mg2+ transporter protein\". Interpro entry for IP:IPR002523. IPB002523A 27-37 0.053 IPB002523B 106-137 9.2e-08 IPB002523C 138-161 1.4e-06 IPB002523D 252-284 1.5e-20","Residues 277 to 315 match (2e-08) PD:PD581688 which is described as COMPLETE PROTEOME COBALT MAGNESIUM CORA TRANSMEMBRANE PROBABLE MAGNESIUM/COBALT PLASMID DIVALENT ","","","","","","","","","","","","Thu Jan 9 09:48:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01344 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 22 to 315 (E-value = 7.7e-94) place AA01344 in the CorA family which is described as CorA-like Mg2+ transporter protein (PF01544)","","","","","Pfeiffer J, Guhl J, Waidner B, Kist M, Bereswill S. Magnesium uptake by CorA is essential for viability of the gastricpathogen Helicobacter pylori. Infect Immun. 2002 Jul;70(7):3930-4. PMID: 12065537 Chamnongpol S, Groisman EA. Mg2+ homeostasis and avoidance of metal toxicity. Mol Microbiol. 2002 Apr;44(2):561-71. PMID: 11972791 Smith,R.L., Banks,J.L., Snavely,M.D. and Maguire,M.E. Sequence and topology of the CorA magnesium transport systems of Salmonella typhimurium and Escherichia coli. Identification of a new class of transport protein J. Biol. Chem. 268 (19), 14071-14080 (1993) PubMed: 8314774 ","","Thu Jan 9 09:48:28 2003","1","","","" "AA01345","912764","913321","558","ATGAATTCAATTCAATTTCTTATTGCGACGGCAATTAGCGTATATAGCTTCATTTTAATTTTACGCACTTGGTTTCAACTGGCGGGCGTGGATTTTTATAATCCGTTATCGCAAGCCTTAGTCAAAGCCACTCAGCCGGTGGTGGTGCCGTTAAGCAAATTGGCGCCGACGGTCAAGGGAGTGAACACCGCCACTTTATTAGCGTGTTTTATTTTGGGATTGGTGAAATTCCCGTTGTTGAATCTGTTCAGCACCATCGGAGCCGCGTCCCTGTTTGAATATGCCATTATCGGCGTGTTAAGCGTGGTGCATAGTATCGGCGAAGCGATTTTTTATGTGTTGTTGGTGGGCGCTATTCTAAGCTGGTTTAATCGTGGCGCCGGTCAAACCCAATATCTTTTGTATCAATTAAGCGAACCGGTGTTACGCCTGGTTCGTAAAATCCTGCCGAATACCGGCATGATCGACTTTTCGCCGATGGTAGTGGTTTTTGTGTTGTATCTGCTTAACCGCGTGTTATACGACGTATTCGGCGGACTTTGGGTCGCCGCAGCGTTT","","","20408","MNSIQFLIATAISVYSFILILRTWFQLAGVDFYNPLSQALVKATQPVVVPLSKLAPTVKGVNTATLLACFILGLVKFPLLNLFSTIGAASLFEYAIIGVLSVVHSIGEAIFYVLLVGAILSWFNRGAGQTQYLLYQLSEPVLRLVRKILPNTGMIDFSPMVVVFVLYLLNRVLYDVFGGLWVAAAF","913321","","conserved hypothetical protein (possible membrane protein)","Inner membrane, Cytoplasm","","
InterPro
IPR003425
Family
Protein of unknown function YGGT
PF02325\"[1-82]T\"[96-176]TYGGT
noIPR
unintegrated
unintegrated
signalp\"[1-29]?signal-peptide
tmhmm\"[5-25]?\"[60-80]?\"[95-115]?\"[163-185]?transmembrane_regions


","BeTs to 11 clades of COG0762COG name: Predicted integral membrane proteinFunctional Class: SThe phylogenetic pattern of COG0762 is --------v-rlbcefgh--uj-it-Number of proteins in this genome belonging to this COG is","Significant hit ( 2.4e-17) to 2/2 blocks of the IPB003425 family, which is described as \"YGGT family\". Interpro entry for IP:IPR003425. IPB003425A 8-25 7 IPB003425B 136-166 8e-16","Residues 1 to 82 match (2e-11) PD:PD005585 which is described as COMPLETE PROTEOME TRANSMEMBRANE MEMBRANE INTEGRAL PROC YGGT VC0459 RSP1385 3'REGION ","","","","","","","","","","","","Thu Jan 9 09:54:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01345 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 96 to 176 (E-value = 3.5e-24) place AA01345 in the YGGT family which is described as YGGT family (PF02325)","","","","","","","","1","","","" "AA01347","913349","913639","291","ATGGCGGCAGTAGAACGAAAGGGCGCGAATTTGCGCCTGAGAATTTTCTTACAACCGAAAGCCGCCAAAAATCAGATTGTCGGATTGCATGATGACGAATTGAAAATCAGCATTACCGCCCCGCCTGTAGATGGGCAGGCAAACGCCCATCTTCTCAAGTTCCTCAGTAAACTTTTCAAAGTACCGAAAAGCAGCATTGTATTGGAAAAAGGCGAACTTAATCGCCATAAACAGGTTCTAATTCCTAGTCCCAAAGTCATTCCGCCGCAAATTGAACCTTACTTAACGCCG","","","10747","MAAVERKGANLRLRIFLQPKAAKNQIVGLHDDELKISITAPPVDGQANAHLLKFLSKLFKVPKSSIVLEKGELNRHKQVLIPSPKVIPPQIEPYLTP","913639","","conserved hypothetical protein","Periplasm, Cytoplasm","","
InterPro
IPR003746
Family
Protein of unknown function DUF167
PTHR13420\"[3-91]TUNCHARACTERIZED
PF02594\"[7-83]TDUF167
InterPro
IPR005228
Family
Conserved hypothetical protein 251
TIGR00251\"[4-91]TTIGR00251: conserved hypothetical protein T
noIPR
unintegrated
unintegrated
G3DSA:3.30.1200.10\"[4-92]Tno description


","No hits to the COGs database.","Significant hit ( 4.9e-25) to 2/2 blocks of the IPB003746 family, which is described as \"DUF167\". Interpro entry for IP:IPR003746. IPB003746A 34-56 1.4e-11 IPB003746B 60-83 6.3e-12","Residues 10 to 79 match (6e-09) PD:PD029858 which is described as PROTEOME COMPLETE SIMILAR TC0667 E.COLI CC3622 CT388 MSL4154 ","","","","","","","","","","","","Thu Jan 9 09:56:26 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01347 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 83 (E-value = 7.7e-38) place AA01347 in the DUF167 family which is described as Uncharacterized ACR, YggU family COG1872 (PF02594)","","","","","","","","1","","","" "AA01348","913759","913634","126","TTGCAGTCTCCTTTCAATAACATAATGAGAAATAAGAATAAATTGTCATTCGGCTGCTCATTTTCCGCTTATTTCGTTTTCTGTCCAGTAAAAACGTTGTCATTTTTGACCGCACTTTTACGGCGT","","","4843","LQSPFNNIMRNKNKLSFGCSFSAYFVFCPVKTLSFLTALLRR","913634","","hypothetical protein","Cytoplasm, Extracellular","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
tmhmm\"[19-39]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 09:47:02 2004","Thu Feb 26 09:47:02 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01348 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:47:02 2004","","","","","","","","","","","","","1","","","" "AA01349","913759","914415","657","ATGAGCGTGACCAAACAGCAAGTATTAGACGCGTTCCATTTTCGTTGCGCCACGCGCTATTACGATCCCGCCCGCAAAATCAGCAAAGAAGATTTCGACTATATTTTAGAACTCGGACGCTTGTCGCCAAGCTCAGTAGGCTCCGAACCTTGGCAGTTTTTGGTGATCCAAAATCCTGAATTACGTCAAGCTTTAAAACCGGTGAGCTGGGGCATGGCAACCCAACTGGACGACGCCAGCCATGTGGTAGTGATTTTAGCCAATAAAAATATGCGTTATGATTCCGAAGATTTCCGTGCAAATCTTGAGCGTCGCGGCTTAACGGAGGAGCAAATTCAAACTAACATGGTAACCTACCAGCGTTTCCAAACCCAACATATAAACGTCTTAGAAAACGACCGCACTTTATTCGACTGGGCAAGCAAACAGACCTATATTGCCCTTGCCAACATGATGACCGGCGCTGCACTTATCGGCATCGACAGCTGCCCGATTGAAGGCTTTAACTATGCGGAAGTGAACCGTATTCTGGCGCAAACCGGCGCTTATAATGCGGACAAATATGCGGTTTCCGTGGCGGTAACCTTCGGCTATCGTGCCAAAGACATACGCCCGAAAGCACGCAAACCGCTTAATGAAATTGTTCATTGGATCGAA","","","25117","MSVTKQQVLDAFHFRCATRYYDPARKISKEDFDYILELGRLSPSSVGSEPWQFLVIQNPELRQALKPVSWGMATQLDDASHVVVILANKNMRYDSEDFRANLERRGLTEEQIQTNMVTYQRFQTQHINVLENDRTLFDWASKQTYIALANMMTGAALIGIDSCPIEGFNYAEVNRILAQTGAYNADKYAVSVAVTFGYRAKDIRPKARKPLNEIVHWIE","914415","","NAD(P)H nitroreductase/H-flavin oxidoreductase","Cytoplasm","","
InterPro
IPR000415
Family
Nitroreductase
PF00881\"[12-198]TNitroreductase
noIPR
unintegrated
unintegrated
G3DSA:3.40.109.10\"[4-218]Tno description
PIRSF000232\"[6-218]TNADH dehydrogenase/NAD(P)H nitroreductase
PTHR23026\"[38-217]TNADPH NITROREDUCTASE
PTHR23026:SF43\"[38-217]TNADPH NITROREDUCTASE


","BeTs to 15 clades of COG0778COG name: NitroreductaseFunctional Class: CThe phylogenetic pattern of COG0778 is aompkz-qvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 9e-13) to 2/2 blocks of the IPB000415 family, which is described as \"Nitroreductase family\". Interpro entry for IP:IPR000415. IPB000415A 43-55 0.007 IPB000415B 150-168 4e-08","Residues 170 to 218 match (3e-08) PD:PD467241 which is described as COMPLETE PROTEOME OXIDOREDUCTASE NADP NITROREDUCTASE FLAVOPROTEIN 1.-.-.- NADPH FMN NAD ","","","","","","","","","","","","Thu Jan 9 10:49:33 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01349 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 12 to 198 (E-value = 4.6e-59) place AA01349 in the Nitroreductase family which is described as Nitroreductase family (PF00881)","","","","","Jeong JY, Mukhopadhyay AK, Dailidiene D, Wang Y, Velapatino B, GilmanRH, Parkinson AJ, Nair GB, Wong BC, Lam SK, Mistry R, Segal I, Yuan Y,Gao H, Alarcon T, Brea ML, Ito Y, Kersulyte D, Lee HK, Gong Y, GoodwinA, Hoffman PS, Berg DE. Sequential inactivation of rdxA (HP0954) and frxA (HP0642)nitroreductase genes causes moderate and high-level metronidazoleresistance in Helicobacter pylori. J Bacteriol. 2000 Sep;182(18):5082-90. PMID: 10960091 Kwon DH, Kato M, El-Zaatari FA, Osato MS, Graham DY. Frame-shift mutations in NAD(P)H flavin oxidoreductase encoding gene(frxA) from metronidazole resistant Helicobacter pylori ATCC43504 andits involvement in metronidazole resistance. FEMS Microbiol Lett. 2000 Jul 15;188(2):197-202. PMID: 10913705 ","","Thu Jan 9 10:49:33 2003","1","","","" "AA01351","914483","916453","1971","ATGTCACGTCAACTGTTTAAAACGGAAAAAATGCATTCTTTGCTGTATCCGATTTTTTTCTTTTGTCTTCTTAACCTGATTGTTTTCACCTTATCCCGTCTTGGGCTGTCTTTGTGGCAAATAGAGCGCGTCAACGCCGTCCACGGCTGGGGCGAACTGTTTTTACAAGGCTTACGTATGGACATTGTGTCCTTGTGCTACCTGTTCGGTGTGCCGGCACTATTCAGCGTATTGTTCTATCATGACAACACTTTAGGGCGTATCTGGAAAGGCATTTTACGCGTCTGGTTAACTGTCGGCAGCGTGTTCATTTTATTTATGGAACTCTCCACGCCCGCCTTCATCAATACCTACGATTACCGCCCGAACCGCCTGTTCATCGAATATTTGATTTACCCGAAAGAAGTGTTCACCATGCTGATGGAAGGGCATTTAAGTGCGGTCATTTTGAGCCTCGTTTTCACGGTAATTGCTGCGGTGGTTTATTGGAAGCTTGCCGGTCGCGCGGTGCGAGATATGCAGCAGATGAGTTGGAAATGGCGCCCGTTGGTGGCGTTATTGGTGATTGCCGTTAGTTTTCTCGGCGCCCGTTCCAGCCTGCAACATCGCGGCATTAACCCGGCGATGGTGGCATTTTCTTCCGACGCCATGGTCAATTCCTTGGTGCTGAATTCGGGCTATTCCGTGATTTATGCGGCACAGCAATTTAAAGACGAAGGCACGTCTTCCGAATCTTACGGCAAAATGGAAACGGCGGAAATGCTGGACATTATCAAGAAAAGCGGCAGCCGCCCGGTGGAGGCTTATATTTCCGATGAATTTCCGACGCTGACCCGTAATCAAGCCACTTATCAGGGCAAACCGAAAAATATCGTGATTATTCTGGAAGAAAGTTTCGGCGCGCAATTTATCGGCACCTTAGGCGGTTTGCCGCTTTCGCCGGCATTTGACAAACTGGCGCAGCAAGGCTGGCTTTTTGATAATTTATACGCCACCGGCACCCGCTCCGTACGCGGCATTGAAGCGGTGACCGCAGGCTTCACGCCAACACCGGCGCGCGCCGTGGTGAAACTGAATAACAGCCAAAACGGCTTTTTCACCTTAGCGCAATTATTAAGCCAACGGGGCTATGACACTTCCTTTATTTACGGCGGAGAAAAACACTTCGACAACATGGCGGGCTTTTTCTACGGCAACGGCTTCAAACGCATTATCGACCAAATGGATTATCAAAATCCGACCTTTACCGGCACCTGGGGCGTGAGCGACGAAGACCTGTTCACCAAAGCCAACGAGACCTTCACCCAATTACAAAAAGAAGGCAAGCCGTTCTTCAGTCTGGTGTTCAGTTCCAGCAACCATGACCCGTTTGAATTTCCAGACGGCAAAATTGAGCTTTACGAACAGCCAAAAGCCACCCGCAACAATGCGGCAAAATACGCCGATTACGCCATCGGGCATTTCTTCAAATTGGCGAAGGAATCTAATTACTGGAAAGACACCATTTTCTTGGTGATTGCCGACCACGACTCCCGCGTTGCCCGCGCCAGCCTGATGCCGATTAAACATTTCCACATCCCGGCGTTAATTCTGGGCGACGGCATTGCACCGCACCGCGATGACCGTTTGGTCAGCCAATTCGATATGCCGACCACTTTACTTTCCTTGGCGGACATCAGCGGCGATTACCCGATGATCGGCTACGACCTCACCAAACCGAACGACCCGAACCGCGCCATCATGCAGTATGACCAAGTGCAGGCGCTCATGCGCGGCAACGACGTGGTGCTTCAGTTCCCGAAAGTGGGCGCCAAAACCTACCGCTATGACAAAACCACTGAAACCTTAACGGAAGAGGAAGTCCCGCCAGCCATGGTGAAAGAAGCCTTGGCGCACGCGCTGTTAGGCAGTTATTTGTACAAACATCGCTTATACACCACCCCGGAAATCAAACAGACGGAAGGAAAGCGT","","","74349","MSRQLFKTEKMHSLLYPIFFFCLLNLIVFTLSRLGLSLWQIERVNAVHGWGELFLQGLRMDIVSLCYLFGVPALFSVLFYHDNTLGRIWKGILRVWLTVGSVFILFMELSTPAFINTYDYRPNRLFIEYLIYPKEVFTMLMEGHLSAVILSLVFTVIAAVVYWKLAGRAVRDMQQMSWKWRPLVALLVIAVSFLGARSSLQHRGINPAMVAFSSDAMVNSLVLNSGYSVIYAAQQFKDEGTSSESYGKMETAEMLDIIKKSGSRPVEAYISDEFPTLTRNQATYQGKPKNIVIILEESFGAQFIGTLGGLPLSPAFDKLAQQGWLFDNLYATGTRSVRGIEAVTAGFTPTPARAVVKLNNSQNGFFTLAQLLSQRGYDTSFIYGGEKHFDNMAGFFYGNGFKRIIDQMDYQNPTFTGTWGVSDEDLFTKANETFTQLQKEGKPFFSLVFSSSNHDPFEFPDGKIELYEQPKATRNNAAKYADYAIGHFFKLAKESNYWKDTIFLVIADHDSRVARASLMPIKHFHIPALILGDGIAPHRDDRLVSQFDMPTTLLSLADISGDYPMIGYDLTKPNDPNRAIMQYDQVQALMRGNDVVLQFPKVGAKTYRYDKTTETLTEEEVPPAMVKEALAHALLGSYLYKHRLYTTPEIKQTEGKR","916453","","probable sulfatase","Inner membrane, Cytoplasm","","
InterPro
IPR000917
Domain
Sulfatase
PF00884\"[287-620]TSulfatase
InterPro
IPR001952
Family
Alkaline phosphatase
G3DSA:3.40.720.10\"[286-571]Tno description
InterPro
IPR012160
Family
Membrane sulphatase, HI1246-related
PIRSF005091\"[5-651]TPredicted membrane sulfatase, HI1246 type
noIPR
unintegrated
unintegrated
PTHR10342\"[268-570]TSULFATASE
signalp\"[1-46]?signal-peptide
tmhmm\"[15-35]?\"[60-80]?\"[95-115]?\"[147-167]?\"[182-200]?transmembrane_regions


","BeTs to 8 clades of COG1368COG name: Phosphoglycerol transferase and related proteins, alkaline phosphatase superfamilyFunctional Class: MThe phylogenetic pattern of COG1368 is --------v--lb-efgh-nuj----Number of proteins in this genome belonging to this COG is","","Residues 13 to 296 match (3e-121) PD:PD185409 which is described as PROTEOME COMPLETE HI1246 TRANSMEMBRANE PM1683 PLASMID INTEGRAL MEMBRANE VCA0802 PA1689 ","","","","","","","","","","","","Thu Feb 20 08:04:49 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01351 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 287 to 622 (E-value = 8.3e-79) place AA01351 in the Sulfatase family which is described as Sulfatase (PF00884)","","","","","","","","1","","","" "AA01354","917381","916629","753","ATGAACTGGATTATTAATATGCACGCAATCAACCCCAACTGGAACGCACCGCAGCAGATTCGGGCGTTCACCACCCTACGCCACAGCGGTGTGAGCCTTGCGCCTTATGATAGCTTCAATTTGGGCGATCATGTGGGCGATGATAAAAACGCCGTGAAAACCAACCGCACTTTATTGGTGGAAAAGTTTCACCTGCCGCAAATGCCCGTTTTCTTAAACCAAATTCACAGCACCAAGGTATTAAATCTGCCTTATCAGGGTGAAGATCTTAATGCCGACGCGGTTTACACCGACCAGCAGAACCAAGTCTGTTTAGTCATGACCGCCGATTGCCTACCCGTATTATTTACCAATCAAAACGGCACGGAAGTCGCCGCCGCCCATGCCGGTTGGCGCGGATTATGTGATGGCATATTAGAACAAACCGTCGCCCGATTCCGATGCCCGACCGATGAAATCTTAGCCTGGTTAGGACCGGCAATCGGACCGACTGCGTTCCAAGTGGGGCAGGAGGTGATCGATCAATTCGTGGCGCAGGATCCCAACGCCAAACAGGCATTCATCGCCGATCCGAAAGAAAACGGCAAATTCCTCGGCAACTTATACCAAATCGCCACCCAACGTCTCAACGCCCTCGGCATCACCCAAATCAGTGGTGGAGAACATTGCACTTACCTTGAAGCGGATAAATTCTTTTCGTATCGACGGGATAACGCCACAGGTAGAATGGCGTCGGTGATTTGGATTGGGGAA","","","28487","MNWIINMHAINPNWNAPQQIRAFTTLRHSGVSLAPYDSFNLGDHVGDDKNAVKTNRTLLVEKFHLPQMPVFLNQIHSTKVLNLPYQGEDLNADAVYTDQQNQVCLVMTADCLPVLFTNQNGTEVAAAHAGWRGLCDGILEQTVARFRCPTDEILAWLGPAIGPTAFQVGQEVIDQFVAQDPNAKQAFIADPKENGKFLGNLYQIATQRLNALGITQISGGEHCTYLEADKFFSYRRDNATGRMASVIWIGE","916629","","conserved hypothetical protein","Cytoplasm, Periplasm","","
InterPro
IPR003730
Family
Protein of unknown function DUF152
PF02578\"[34-250]TDUF152
TIGR00726\"[30-250]TTIGR00726: conserved hypothetical protein T
noIPR
unintegrated
unintegrated
G3DSA:3.60.140.10\"[1-251]Tno description


","No hits to the COGs database.","Significant hit ( 1.5e-58) to 5/5 blocks of the IPB003730 family, which is described as \"DUF152\". Interpro entry for IP:IPR003730. IPB003730A 30-42 4.4e-07 IPB003730B 70-81 4.7e-05 IPB003730C 93-133 1.9e-28 IPB003730D 157-168 0.01 IPB003730E 224-242 3.1e-09","Residues 7 to 53 match (4e-14) PD:PD013142 which is described as COMPLETE PROTEOME INNER YPO3276 PA4543 VC0710 PM1718 MEMBRANE HI0175 YFIH ","","","","","","","","","","","","Thu Jan 9 11:14:13 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01354 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 34 to 250 (E-value = 9.4e-94) place AA01354 in the DUF152 family which is described as Uncharacterised ACR, YfiH family COG1496 (PF02578)","","","","","","","","1","","","" "AA01355","918339","917368","972","ATGGCACAAATTACTCTATCGGCGACCGTGCAATCGCATCAAATGGGACAACGTTTAGACCAAACCCTGGCGGAATTGTTCCCCGACTACTCCCGCTCCCGCTTAAAGACTTGGATCGAGGAAGATCTGGTGTTGGTTAACGGTGTTGTGCAAAATGTGCCGCGCAGTAAAGTTTACGGTGACGAGCAAATTGAAATTACCGTAGAAATTGAAGACGAAACCCGCTTCGAGCCGGAAAATATTCCGTTAAATATCGTGTATGAAGACGACGATATTTTAGTTATCAACAAGCCGAAAGATTTGGTGGTTCACCCGGGCGCCGGCAATCCGAGCGGCACGGTGCTGAATGCGTTGTTATACCATTACCCGCCCATCGCCGAAGTGCCGCGCGCCGGCATCGTTCACCGTTTAGACAAAGACACCACCGGCTTAATGGTGGTGGCGAAAACCATTCCCGCGCAAACCCAGTTGGTGCGCGACCTGCAAAAACGCAAAATCATCCGCGAATATGAAGCGGTTGCCTGCGGTATCATGACCAAAGGCGGCACGGTGGACGAACCCATGGCGCGCCACCCCACCAAACGCACGCACATGGCGGTACACCCGATGGGCAAACCGGCAGTGACCCACTATCGCATTATGGAGCGCTTCCGCGATTACACCCGTCTGCGCCTGCGTTTGGAAACCGGACGCACCCACCAAATTCGCGTACACATGGCACATATGGCCCACCCGTTACTCGGCGATCAAACTTACGGCGGTCGTCCTCGTCCACCGAAAAATGCAAGTGAGGAGCTGATGAGCGTATTACGCAACTTCAAACGCCAAGCGCTGCACGCCGTAATGTTACGCCTACAACACCCGATTAGTGGTGAAATGATGGAATGGTATGCGCCGCTGCCGGAGGATTTTGTGGAATTAATCACCGCCCTGAAAGCAGACTATGTGTTACACAAAGATGAACTGGATTAT","","","37027","MAQITLSATVQSHQMGQRLDQTLAELFPDYSRSRLKTWIEEDLVLVNGVVQNVPRSKVYGDEQIEITVEIEDETRFEPENIPLNIVYEDDDILVINKPKDLVVHPGAGNPSGTVLNALLYHYPPIAEVPRAGIVHRLDKDTTGLMVVAKTIPAQTQLVRDLQKRKIIREYEAVACGIMTKGGTVDEPMARHPTKRTHMAVHPMGKPAVTHYRIMERFRDYTRLRLRLETGRTHQIRVHMAHMAHPLLGDQTYGGRPRPPKNASEELMSVLRNFKRQALHAVMLRLQHPISGEMMEWYAPLPEDFVELITALKADYVLHKDELDY","917368","From GenBank (gi:1175998): This protein is responsible for synthesis of pseudourine from uracil at two positions in 23s ribosomal RNA.","large subunit pseudouridylate synthase D","Cytoplasm","","
InterPro
IPR002942
Domain
RNA-binding S4
PF01479\"[17-64]TS4
SM00363\"[17-82]TS4
PS50889\"[17-90]TS4
InterPro
IPR006145
Domain
Pseudouridine synthase
PD001819\"[134-176]TRLUD_HAEIN_P44445;
PF00849\"[91-241]TPseudoU_synth_2
InterPro
IPR006224
Family
Pseudouridine synthase, Rlu
PS01129\"[134-148]TPSI_RLU
InterPro
IPR006225
Domain
Pseudouridine synthase, RluD
TIGR00005\"[12-312]TrluA_subfam: pseudouridine synthase, RluA f
noIPR
unintegrated
unintegrated
PTHR10436\"[1-308]TRIBOSOMAL PSEUDOURIDINE SYNTHASE


","BeTs to 19 clades of COG0564COG name: Pseudouridylate synthases, 23S RNA-specificFunctional Class: JThe phylogenetic pattern of COG0564 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.3e-58) to 4/4 blocks of the IPB000613 family, which is described as \"Pseudouridine synthase\". Interpro entry for IP:IPR000613. IPB000613A 85-105 5.3e-14 IPB000613B 134-173 9.4e-18 IPB000613C 229-253 4.6e-18 IPB000613D 275-288 0.00015Significant hit ( 1.7e-52) to 3/3 blocks of the IPB002990 family, which is described as \"Pseudouridine synthase, Rlu family\". Interpro entry for IP:IPR002990. IPB002990A 85-105 5.4e-13 IPB002990B 134-172 6.2e-19 IPB002990C 229-253 7.1e-18","Residues 78 to 121 match (3e-07) PD:PD171871 which is described as PROTEOME COMPLETE TP0339 ","","","","","","","","","","","Thu Jan 9 11:21:50 2003","Thu Jan 9 11:21:50 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01355 is paralogously related to AA02913 (2e-30), AA00513 (2e-23), AA02276 (4e-17) and AA02063 (4e-13).","","","","","","Residues 91 to 241 (E-value = 3.3e-68) place AA01355 in the PseudoU_synth_2 family which is described as RNA pseudouridylate synthase (PF00849)","","","","","Gutgsell NS, Del Campo MD, Raychaudhuri S, Ofengand J.A second function for pseudouridine synthases: A point mutant of RluD unable to form pseudouridines 1911, 1915, and 1917 in Escherichia coli 23S ribosomal RNA restores normal growth to an RluD-minus strain.RNA. 2001 Jul;7(7):990-8.PMID: 11453071 Wrzesinski J, Bakin A, Ofengand J, Lane BG.Isolation and properties of Escherichia coli 23S-RNA pseudouridine 1911, 1915, 1917 synthase (RluD).IUBMB Life. 2000 Jul;50(1):33-7.PMID: 11087118 Raychaudhuri S, Conrad J, Hall BG, Ofengand J.A pseudouridine synthase required for the formation of two universally conserved pseudouridines in ribosomal RNA is essential for normal growth of Escherichia coli.RNA. 1998 Nov;4(11):1407-17.PMID: 9814761","","Thu Jan 9 11:21:50 2003","1","","","" "AA01356","918446","919231","786","ATGCGTAAACTTAAATCCTTTGCATTGCTTACTGCCATGGCGTTGGCGGTAACAGCATGTTCAAGTTCAAAACAAGATGTGGAACAAGCCCCTGAGCAAACCTTATATACTACCGGTCAAACCTATTTGCAGGATGGCGATTATTCCCAAGCCATTCGTTATTTTAATGCGGTAAGCAACCGCTTCCCGGGCAATTCCTACGGCGAACAGGTGCAACTGAATTTAATTTACGCGTACTACAAATCTCAAGATTATAGCGAAACCTTGCTAACCATTGACCGCTTCATTCAACGTTATCCGAACAGCAGTCACTTGGATTACGCCCTTTACATGGCAGGTTTAACCAATTCCGCCTTGGGCGATAATTTCTTCCAGGATTTCTTCGGCGTGGATCGCGCTACCCGTGAAAATACCTCAATCAAAACCGCCTTTGCCAACTTTCAGAATTTAGTTAATCATTTCCCGAACAGCCCTTATACGCCGGACGCGTTGGCGCGTATGACTTACATTAAAGCCAGTCTTGCCCGTCATGAATTGGAAATTGCCAAGTTCTATTTTAAACGGGATGCCTATGTGGCGACGGCAAATCGCGTGGTGTCGATGTTAAAACTGTATCCGGACACACAAGCTACGTTGGACGCATTGCCGCTTATGAAGGAATCTTATGAAAAGATGAACTTGAAGCATTTGGCGGATCAAACGGCGAAGGTGATTGCCGCGAACGAAGGCAAGAAGTTTGACGAGCCGGAAAAACCGAAAGAGCCGGAACTTCAAGCGCCACAACAA","","","29785","MRKLKSFALLTAMALAVTACSSSKQDVEQAPEQTLYTTGQTYLQDGDYSQAIRYFNAVSNRFPGNSYGEQVQLNLIYAYYKSQDYSETLLTIDRFIQRYPNSSHLDYALYMAGLTNSALGDNFFQDFFGVDRATRENTSIKTAFANFQNLVNHFPNSPYTPDALARMTYIKASLARHELEIAKFYFKRDAYVATANRVVSMLKLYPDTQATLDALPLMKESYEKMNLKHLADQTAKVIAANEGKKFDEPEKPKEPELQAPQQ","919231","","lipooligosaccharide galactosyltransferase II (comL related)","Periplasm, Outer membrane","","
InterPro
IPR011990
Domain
Tetratricopeptide-like helical
G3DSA:1.25.40.10\"[33-172]Tno description
InterPro
IPR013026
Domain
Tetratricopeptide region
SM00028\"[32-65]T\"[69-102]TTPR
PS50005\"[32-65]T\"[69-102]TTPR
PS50293\"[32-102]TTPR_REGION
InterPro
IPR013105
Repeat
Tetratricopeptide TPR_2
PF07719\"[32-65]TTPR_2
noIPR
unintegrated
unintegrated
PS51257\"[1-20]TPROKAR_LIPOPROTEIN
signalp\"[1-22]?signal-peptide


","BeTs to 11 clades of COG0457COG name: TPR-repeat-containing proteinsFunctional Class: RThe phylogenetic pattern of COG0457 is aompk-yqvd-lbcefghsnujxit-Number of proteins in this genome belonging to this COG is","","Residues 1 to 197 match (4e-54) PD:PD013537 which is described as LIPOPROTEIN COMPLETE PROTEOME SIGNAL MEMBRANE PRECURSOR COMPETENCE REPEAT COML TPR ","","","","","","","","","","","","Thu Jan 9 11:49:31 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01356 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 243 (E-value = 2.2e-122) place AA01356 in the UPF0169 family which is described as Uncharacterised protein family (UPF0169) (PF03696)","","","","","Sun,S., Schilling,B., Tarantino,L., Tullius,M.V., Gibson,B.W. and Munson,R.S. Jr. Cloning and characterization of the lipooligosaccharide galactosyltransferase II gene of Haemophilus ducreyi J. Bacteriol. 182 (8), 2292-2298 (2000) PubMed: 10735874 ","","Thu Jan 9 11:49:31 2003","1","","","" "AA01357","919845","919273","573","ATGCAAGCACATCCTTCAACCGCCACAGTTCGTCAACAACTTCGTCAGCAAATGCGAAAAACGCGCAGAAAACTGGCCGCACTTCAACAGCAACAAGTCGCTAAAAACATCACCGAACAGGCGTTAGCGCTCATTGAACAGCATCATGCGCAACATATCGGACTTTATCTTGCCTTTGACGGCGAAATTTCCACCCAACCGCTCATTGAACGATTATGGCAGCAAGGCAAAAATGTTTATTTACCGGTGTTACATCCGTTCTGTCGCGGGTATTTATTGTTTCTGCGCTATTTGCCGGACACCCCAATGAAACAAAATAAATTCGGCATTTTAGAACCGCATTTGAATGTGCAAAATGTGCTGCCGTTGGCGCAATTAGACATGATTTTCACCCCGCTGGTGGCGTTTGACAAACAGGGCAATCGCCTCGGCATGGGCGGCGGGTTTTATGATCGCACGTTACAACACCGACAACATCGTTTCATCGCCGTGGGTTTGGCGCATCAATGTCAGCAGGTAGAAACGTTGCCGGTAGAAAGCTGGGATGTGCCGTTAGAACACATTCTGGCGGGA","","","21940","MQAHPSTATVRQQLRQQMRKTRRKLAALQQQQVAKNITEQALALIEQHHAQHIGLYLAFDGEISTQPLIERLWQQGKNVYLPVLHPFCRGYLLFLRYLPDTPMKQNKFGILEPHLNVQNVLPLAQLDMIFTPLVAFDKQGNRLGMGGGFYDRTLQHRQHRFIAVGLAHQCQQVETLPVESWDVPLEHILAG","919273","","5-formyltetrahydrofolate cyclo-ligase-family protein","Cytoplasm","","
InterPro
IPR002698
Family
5-formyltetrahydrofolate cyclo-ligase
PTHR23407:SF1\"[1-189]T5-FORMYLTETRAHYDROFOLATE CYCLO-LIGASE
PF01812\"[11-191]T5-FTHF_cyc-lig
TIGR02727\"[11-191]TMTHFS_bact: 5,10-methenyltetrahydrofolate s
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.10420\"[11-189]Tno description
PTHR23407\"[1-189]TATPASE INHIBITOR/5-FORMYLTETRAHYDROFOLATE CYCLO-LIGASE


","No hits to the COGs database.","Significant hit ( 4.4e-18) to 1/1 blocks of the IPB002698 family, which is described as \"5-formyltetrahydrofolate cyclo-ligase\". Interpro entry for IP:IPR002698. IPB002698 127-155 4.3e-18","Residues 11 to 189 match (3e-10) PD:PD096264 which is described as PROTEOME COMPLETE RELATED ML0181 5-FORMYLTETRAHYDROFOLATE CYCLO-LIGASE- ","","","","","Thu Feb 13 15:47:15 2003","","","","","","","Thu Jan 9 11:56:03 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01357 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 11 to 191 (E-value = 1.3e-63) place AA01357 in the 5-FTHF_cyc-lig family which is described as 5-formyltetrahydrofolate cyclo-ligase family (PF01812)","","","","","Holmes WB, Appling DR.Cloning and characterization of methenyltetrahydrofolate synthetase from Saccharomyces cerevisiae.J Biol Chem. 2002 Jun 7;277(23):20205-13.PMID: 119233043: ","","Thu Jan 9 12:05:39 2003","1","","","" "AA01358","920447","920142","306","ATGTCATCGACGAAAAGTATTGAAATCTCCGTATTAGGGCAGCTGTTACGTTTAAATTGCCCGGAAGAACAACATGACGCATTACGCAGTGCCGCCCGGGAATTGGATCAGCGCGTGTCGGAAATGAAAGAACGCACCGGCATTCTGCAAGTGGATAAAGTGCTCTCCATCGTTGCCCTGAATTTAAGTTTTGAACTCATGCAGGAACAGAAAAAAACGCATTTAATTGAGGATGTATTGAAAAATAAAATCCTGCGTCCGCTGGATCATTCTCTCGAAAATATCGGTGCGCCGAAGTTCAATTCC","","","12235","MSSTKSIEISVLGQLLRLNCPEEQHDALRSAARELDQRVSEMKERTGILQVDKVLSIVALNLSFELMQEQKKTHLIEDVLKNKILRPLDHSLENIGAPKFNS","920142","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR007838
Family
Protein of unknown function DUF710
PF05164\"[7-101]TZapA


","BeTs to 6 clades of COG3027COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3027 is ------------b-efghsn-jxi--Number of proteins in this genome belonging to this COG is","","Residues 3 to 95 match (7e-23) PD:PD029857 which is described as COMPLETE PROTEOME CYTOPLASMIC VC2478 HI0857 PM1722 STY3216 YPO0912 YGFE ","","","","","","","","","","","","Thu Jan 9 12:07:31 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01358 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 101 (E-value = 3.6e-30) place AA01358 in the DUF710 family which is described as Family of unknown function (DUF710) (PF05164)","","","","","","","","1","","","" "AA01359","920624","921169","546","ATGACAACAATTTCTTATCAACATCTGAATCAACAACTCCGTCAAGCTTCCATTCCGCTTTCCGCCGCCGAATTACACGGCTTTTTGAGCGGTTTAATTTGTGACGGTGTTCAGGATCAAAGCTGGCAACCGTTGCTTTACCAATTCACCAATGATAATCACGCCTATCCCATCGCACTTTTGCAGCAAATTAGCGACATTTATCAGCAAATTCGTCGCCAATTAGCCGACAATGAAAGTTTTGATTTTGAGCTTTGCCTGCCGGAAACGGAAAACGTGTTCGAACAGGCAGACGGTTTAGCGGAATGGTCGAACCACTTTTTGCTCGGTTTAGGCTTGGCGCAACCGCATTTGGACAAAGAAAAAGGCGACATCGGCGAAGCGGTGGAAGATTTACGCGACATTTGCCAATTAGGCTATGATGATGAAGATGACCCGGAAGAACTGGCGCAGGCGGTGGAAGAAATCGTGGAGTATGTGCGCACCATCGCCACCTTATTTTTCACCCATTTTAATCAAACTGAAGAAAAACAACCGACTTTACAT","","","23765","MTTISYQHLNQQLRQASIPLSAAELHGFLSGLICDGVQDQSWQPLLYQFTNDNHAYPIALLQQISDIYQQIRRQLADNESFDFELCLPETENVFEQADGLAEWSNHFLLGLGLAQPHLDKEKGDIGEAVEDLRDICQLGYDDEDDPEELAQAVEEIVEYVRTIATLFFTHFNQTEEKQPTLH","921169","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR005356
Family
Protein of unknown function UPF0149
PF03695\"[3-182]TUPF0149
InterPro
IPR011978
Domain
YgfB and YecA
TIGR02292\"[2-167]TygfB_yecA: yecA family protein


","BeTs to 5 clades of COG3079COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3079 is --------------efghs-------Number of proteins in this genome belonging to this COG is","","Residues 5 to 182 match (9e-63) PD:PD035069 which is described as COMPLETE PROTEOME CYTOPLASMIC VC2476 EXPORTED HI0817 PM1723 STY3215 YGFB ORF ","","","","","","","","","","","","Thu Jan 9 12:09:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01359 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 182 (E-value = 4.4e-98) place AA01359 in the UPF0149 family which is described as Uncharacterised protein family (UPF0149) (PF03695)","","","","","","","","1","","","" "AA01360","921187","922485","1299","ATGGATCTCGCGTATATGGCTGCGTTACCGCCGGAAGAATTCGCGCAACGCCGGGCTAAAGTATTTGAGCAAATGCAGGACAATTCCCTGTTTTTGGTGTTTTCCGATATTGAGCGTCGTCGCAACGATGGCTGCGATTACCCGTTCCGTCAGGATAGCTATTTCTGGTATTTAACCGGCTTTAATGAGCCGAATGCCGCTTTATTATTGCGTAAACACCAAGGTGAACAACAAGCGATTATATTTTTACGCCCGTCCGATAAATTGCTGGAAATTTGGAACGGTCGCCGCCTTGGCATGGAAAATGCGCCGCAGACGCTACTAGTGGATAGTGCTTATGCTATTGAAGACTTTATTTCGCAGTTTAAAAATTTAGCGCAAAAACAGACCGCACTCTACTACGCACCGAAGCAACAACCTTGGGGCGATGCGTTGCTGGAGCAAAGTGCAGTGGAATTTTCCGGTGTTTTTAACTGGAAGTACATGCTGGGCGAAATGCGCCTGTTCAAATCGGAAAATGAAATTGCGCTGATGCAACAAGCGGGGCAAATCAGCGCGTTGGCGCACATTAAAGCCATGCAACAAACCCGTCCGAACCGTTTGGAATACGAAGTGGAAAGTGACATTTTACACGAATTTAACCGCTTCGGCGCGCGTTATCCGGCTTACAACAGCATTGTTGCGGGCGGCAAAAATGCCTGCATTTTGCACTATTCGGAAAACAATATGCCGTTGCGCGACGGCGATTTGGTGCTGATTGACGCAGGCTGTGAATTCGCCATGTACGCGGGGGATATTACCCGCACTTTCCCCGTGAACGGTAAATTCAGCGAGGCGCAAAAAGCCATTTATGACATCGTACTGCAAGCGCAAAAACGCGCCATTGAATTGTTGGTGCCCGGCAGCTCCATTGCGAAAGTGAACGAGGAAGTAATTCGCATTAAAACCGAAGGTTTGGTGCGTTTAGGTATTCTGAAAGGCGATGTGGATGAATTGATCGAACAAAAAGCCTATCGTGAATTTTATATGCACGGCTTAGGGCATTGGCTCGGCTTGGATGTGCATGATGTGGGCGAATACGGCGAAAACCGCAGTCGCACGTTGGAACCGGGCATGGTGATTACGGTGGAACCGGGTTTGTATTTATCCAAAGACGCTGATATTCCGGAGCAATACAAAGGCATCGGCATTCGCATTGAAGACGACTTACTGATTACCAACTACGGCAACAAAAACCTCACTTCCGCTGCGCCGAAAGAAATTGCCGATATTGAAAAACTGATGGCGGACACGTGCGCT","","","49200","MDLAYMAALPPEEFAQRRAKVFEQMQDNSLFLVFSDIERRRNDGCDYPFRQDSYFWYLTGFNEPNAALLLRKHQGEQQAIIFLRPSDKLLEIWNGRRLGMENAPQTLLVDSAYAIEDFISQFKNLAQKQTALYYAPKQQPWGDALLEQSAVEFSGVFNWKYMLGEMRLFKSENEIALMQQAGQISALAHIKAMQQTRPNRLEYEVESDILHEFNRFGARYPAYNSIVAGGKNACILHYSENNMPLRDGDLVLIDAGCEFAMYAGDITRTFPVNGKFSEAQKAIYDIVLQAQKRAIELLVPGSSIAKVNEEVIRIKTEGLVRLGILKGDVDELIEQKAYREFYMHGLGHWLGLDVHDVGEYGENRSRTLEPGMVITVEPGLYLSKDADIPEQYKGIGIRIEDDLLITNYGNKNLTSAAPKEIADIEKLMADTCA","922485","","XAA-pro aminopeptidase (X-pro aminopeptidase)","Cytoplasm","","
InterPro
IPR000994
Domain
Peptidase M24, catalytic core
G3DSA:3.90.230.10\"[168-428]Tno description
PTHR10804\"[214-322]T\"[341-418]TPROTEASE FAMILY M24 (METHIONYL AMINOPEPTIDASE, AMINOPEPTIDASE P)
PF00557\"[176-415]TPeptidase_M24
InterPro
IPR001131
Domain
Peptidase M24B, X-Pro dipeptidase, cataltyic core
PS00491\"[344-356]TPROLINE_PEPTIDASE
InterPro
IPR007865
Domain
Peptidase M24B, X-Pro dipeptidase/aminopeptidase N-terminal
PF05195\"[9-143]TAMP_N
noIPR
unintegrated
unintegrated
G3DSA:3.40.350.10\"[7-167]Tno description
PTHR10804:SF18\"[214-322]T\"[341-418]TXAA-PRO DIPEPTIDASE APP(E.COLI)


","No hits to the COGs database.","Significant hit ( 2.3e-53) to 5/5 blocks of the IPB001131 family, which is described as \"Proline dipeptidase\". Interpro entry for IP:IPR001131. IPB001131A 217-237 1.3e-09 IPB001131B 249-270 1.1e-11 IPB001131C 344-356 2.6e-09 IPB001131D 368-381 1.1e-08 IPB001131E 396-414 6.6e-08Significant hit ( 2.2e-12) to 2/6 blocks of the IPB002467 family, which is described as \"Methionine aminopeptidase, subfamily 1\". Interpro entry for IP:IPR002467. IPB002467C 245-273 2.5e-07 IPB002467E 368-380 0.0026Significant hit ( 3.2e-06) to 2/4 blocks of the PR00599 family, which is described as \"Methionine aminopeptidase-1 signature\". Prints database entry for PR:PR00599. PR00599B 249-265 0.22 PR00599D 366-378 0.0068","","","","","","","","","","","","","Thu Jan 9 12:13:36 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01360 is paralogously related to AA02429 (0.001).","","","","","","Residues 343 to 414 (E-value = 1.1e-28) place AA01360 in the Peptidase_M24 family which is described as metallopeptidase family M24 (PF00557)","","","","","Wilce,M.C., Bond,C.S., Dixon,N.E., Freeman,H.C., Guss,J.M., Lilley,P.E. and Wilce,J.A. Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 95 (7), 3472-3477 (1998) PubMed: 9520390 Yoshimoto,T., Tone,H., Honda,T., Osatomi,K., Kobayashi,R. and Tsuru,D. Sequencing and high expression of aminopeptidase P genefrom Escherichia coli HB101 J. Biochem. 105 (3), 412-416 (1989) PubMed: 2659585 ","","Thu Jan 9 12:13:36 2003","1","","","" "AA01363","922797","922645","153","ATGCGGAAAAAGTGCGGTTGTTTTTCCGAGTGTTTTTTAAGGCGTCATTTCTACAGCCCTAACACCTGTTTAATCAGTTGCTCTTTTCGCAGCCCCATTTTATTCGTTGCCGACAAGCCAAGCCCGATGATCGCCACTGAATACCTGCATCAG","","","5943","MRKKCGCFSECFLRRHFYSPNTCLISCSFRSPILFVADKPSPMIATEYLHQ","922645","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 09:48:19 2004","Thu Feb 26 09:48:19 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01363 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:48:19 2004","","","","","","","","","","","","","1","","","" "AA01364","922801","922926","126","TTGCAAAAAATCCTCTTCTCACCGAACCTGAACATGGATTTCAGCTTGCTTTTTATGCGAAAAAGAGTAAAATCCACAGGCTTTTTGTCTATATATACAGAGAAAAAAGTAAGTTTAACTCTCATT","","","4904","LQKILFSPNLNMDFSLLFMRKRVKSTGFLSIYTEKKVSLTLI","922926","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 09:49:53 2004","Thu Feb 26 09:49:53 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01364 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:49:53 2004","","","","","","","","","","","","","1","","","" "AA01365","922983","923228","246","ATGGTAACCATTCGTTTATCTCGTGGCGGAGCTAAAAAACGCCCATTTTACCAAATCGTTGTTGCTGACAGCCGTTCACCGCGTGACGGTCGTTTCATTGAGCGCGTTGGTTTCTTCAATCCAATCGCACAAGGTAAAGCAGAACGTGTTCGTATTGATTTAGACCGTGTTAACCACTGGGTTGGACAAGGTGCTTCATTATCCGATCGCGTCGCGAGTTTAGTAAAAGAAGTGCAAAAAGCCGCT","","","9162","MVTIRLSRGGAKKRPFYQIVVADSRSPRDGRFIERVGFFNPIAQGKAERVRIDLDRVNHWVGQGASLSDRVASLVKEVQKAA","923228","","30S ribosomal protein S16","Cytoplasm, Extracellular","","
InterPro
IPR000307
Family
Ribosomal protein S16
PD003791\"[10-77]TRS16_BUCAI_P57474;
G3DSA:3.30.1320.10\"[1-77]Tno description
PTHR12919\"[1-79]T30S RIBOSOMAL PROTEIN S16
PF00886\"[8-68]TRibosomal_S16
TIGR00002\"[2-81]TS16: ribosomal protein S16
PS00732\"[2-11]TRIBOSOMAL_S16


","BeTs to 19 clades of COG0228COG name: Ribosomal protein S16Functional Class: JThe phylogenetic pattern of COG0228 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 4.7e-27) to 1/1 blocks of the IPB000307 family, which is described as \"Ribosomal protein S16\". Interpro entry for IP:IPR000307. IPB000307 1-37 4.3e-27","Residues 1 to 77 match (4e-31) PD:PD003791 which is described as RIBOSOMAL S16 30S PROTEOME COMPLETE CHLOROPLAST MITOCHONDRION MITOCHONDRIAL PROBABLE 28S ","","","","","","","","","","","","Thu Jan 9 12:15:57 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01365 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 68 (E-value = 2e-35) place AA01365 in the Ribosomal_S16 family which is described as Ribosomal protein S16 (PF00886)","","","","","Bystrom AS, Hjalmarsson KJ, Wikstrom PM, Bjork GR. The nucleotide sequence of an Escherichia coli operon containing genes for the tRNA(m1G)methyltransferase, the ribosomal proteins S16 and L19 and a 21-K polypeptide. Embo J. 2(6): 899-905.1983. PubMed: 6357787.","","Thu Jan 9 12:15:57 2003","1","","","" "AA01366","923257","923781","525","ATGCAACAACAAAGAATCGAAACTGTCGGCAAATTAGGTTCGACTTATGGTATTCGCGGTTGGTTACGCATTTATTCATCCACAGAACAAGCTGAAAGCATTTTTGACTATCAACCTTGGTTTTTAAAAATCAAGGGACAATGGCAACCGACAGAACCGGAAAACTGGCGTCATCATAATCACGAACTGATCGTTAAATTAAAAGGCGTGGATGATCGTGAAGCGGCACAAATTCTGGCAAATGTGGAAATCGGTGTGGATTTATCGGTATTTCCGCAGTTGAAAGAAGGCGACTACTATTGGCATGATTTAATCGGTTGTACGGTGGTGAATCTGGCGGGTTATGCCATGGGAACGGTGACCGAGATGATGGAAACCGGATCCAATGATGTGTTGGTGGTCAAAGCCAACGTAAAAGATGCTTTCGGAAAACAAGAACGGTTAATTCCGTTTTTGTATGAACAAGTAGTTAAAAGAGTCGATCTCGCCACTAAGACGATTACAGTGGATTGGGACGCTGGTTTC","","","20366","MQQQRIETVGKLGSTYGIRGWLRIYSSTEQAESIFDYQPWFLKIKGQWQPTEPENWRHHNHELIVKLKGVDDREAAQILANVEIGVDLSVFPQLKEGDYYWHDLIGCTVVNLAGYAMGTVTEMMETGSNDVLVVKANVKDAFGKQERLIPFLYEQVVKRVDLATKTITVDWDAGF","923781","","16S rRNA processing protein","Cytoplasm","","
InterPro
IPR002676
Domain
RimM protein
PF01782\"[8-90]TRimM
InterPro
IPR007903
Domain
PRC-barrel
PF05239\"[96-174]TPRC
InterPro
IPR011961
Family
16S rRNA processing protein RimM
TIGR02273\"[8-175]T16S_RimM: 16S rRNA processing protein RimM


","BeTs to 16 clades of COG0806COG name: RimM protein, required for 16S rRNA processingFunctional Class: JThe phylogenetic pattern of COG0806 is -------qvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 4.8e-44) to 3/3 blocks of the IPB002676 family, which is described as \"RimM\". Interpro entry for IP:IPR002676. IPB002676A 9-29 2e-12 IPB002676B 92-134 2.6e-27 IPB002676C 148-156 0.19","Residues 22 to 173 match (3e-75) PD:PD358463 which is described as PROCESSING RRNA COMPLETE PROTEOME 16S RIMM PROBABLE RIBOSOMAL RNA 21K ","","","","","","","","","","","","Thu Jan 9 12:20:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01366 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 96 to 174 (E-value = 3.9e-21) place AA01366 in the PRC family which is described as PRC-barrel domain (PF05239)","","","","","Bystrom, A.S., Hjalmarsson, K.J., Wikstrom, P.M., Bjork, G.R. 1983.The nucleotide sequence of an Escherichia coli operon containing genesfor the tRNA(m1G)methyltransferase, the ribosomal proteins S16 and L19and a 21-K polypeptide. Embo J. 2(6): 899-905. PubMed: 6357787 Bylund,G.O., Persson,B.C., Lundberg,L.A. and Wikstrom,P.M. 1997. Anovel ribosome-associated protein is important for efficienttranslation in Escherichia coli. J. Bacteriol. 179(14): 4567-4574. PubMed: 9226267 Bylund,G.O., Wipemo,L.C., Lundberg,L.A. and Wikstrom,P.M. 1998. RimMand RbfA are essential for efficient processing of 16S rRNA inEscherichia coli. J. Bacteriol. 180(1): 73-82. PubMed: 9422595 ","","Thu Jan 9 12:20:55 2003","1","","","" "AA01367","923850","924596","747","ATGTGGATTGGGGTAATAAGTCTGTTCCCTGAAATGTTTAAAGCAATTACGGAATATGGGGTAACCGGCAGGGCTGTTAAGCAAGATCTGTTACAAGTGCGGTGCTGGAATCCGAGGGATTTTACGCACGATAAGCACAAAACCGTAGATGACCGCCCTTACGGCGGAGGTCCCGGAATGCTGATGGTGGTGCAACCGTTAAAGGATGCCATCGACGCAGCAAAAAAGGTAGCAGGCGAAGGCGCAAAAGTGATTTATCTCTCACCGCAAGGTCGCAAACTTGACCAGCCGGGTGTAGAGGGATTAGCCCAAAATCAGAAATTGATTTTGTTATGCGGCCGCTATGAAGGCATTGACGAACGGTTGATTGAAACCGTGGTTGATGAAGAATGGTCGGTAGGTGATTATGTATTAACCGGTGGTGAATTGCCGGCAATGACGTTAATTGATGCCGTTGCCCGTTTTATTCCTGGTGTACTCGGTAAACAGGCTTCCGCGGAGGAAGATTCCTTTGCCGAGGGATTGCTTGATTGTCCGCATTATACGCGCCCCGAAGTGCTTGACGGATTGGCCGTGCCTCCCGTGCTGATGTCAGGACACCATGAAGAAATTCGCAAATGGCGGTTGAAACAATCGTTATTGAGAACATGGTTACGACGCCCTGAGCTACTGGAAGGCCTAGCTCTGACTGACGAACAACGTAAGCTGTTAAAACAGGCGCAAGCCGAATATAACGGTAAACTCAGT","","","27758","MWIGVISLFPEMFKAITEYGVTGRAVKQDLLQVRCWNPRDFTHDKHKTVDDRPYGGGPGMLMVVQPLKDAIDAAKKVAGEGAKVIYLSPQGRKLDQPGVEGLAQNQKLILLCGRYEGIDERLIETVVDEEWSVGDYVLTGGELPAMTLIDAVARFIPGVLGKQASAEEDSFAEGLLDCPHYTRPEVLDGLAVPPVLMSGHHEEIRKWRLKQSLLRTWLRRPELLEGLALTDEQRKLLKQAQAEYNGKLS","924596","","tRNA (Guanine-N(1)-)-methyltransferase (M1G-methyltransferase)","Cytoplasm","","
InterPro
IPR002649
Family
tRNA (guanine-N1-)-methyltransferase
PD004978\"[30-225]TTRMD_HAEIN_P43912;
PF01746\"[22-221]TtRNA_m1G_MT
TIGR00088\"[1-240]TtrmD: tRNA (guanine-N1)-methyltransferase
noIPR
unintegrated
unintegrated
G3DSA:1.10.1270.20\"[170-243]Tno description
G3DSA:3.40.1280.10\"[1-160]Tno description
PIRSF000386\"[1-244]TtRNA-(m1G37) methyltransferase
signalp\"[1-15]?signal-peptide


","No hits to the COGs database.","Significant hit (1.3e-125) to 5/5 blocks of the IPB002649 family, which is described as \"tRNA (guanine-N1-)-methyltransferase\". Interpro entry for IP:IPR002649. IPB002649A 1-13 4e-08 IPB002649B 39-64 1.2e-21 IPB002649C 102-123 2.2e-15 IPB002649D 130-171 1.1e-37 IPB002649E 175-223 4.6e-38","Residues 24 to 235 match (6e-103) PD:PD004978 which is described as METHYLTRANSFERASE TRNA PROTEOME COMPLETE TRANSFERASE GUANINE-N1-METHYLTRANSFERASE GUANINE-N1--METHYLTRANSFERASE M1G- PROCESSING GM37 ","","","","","","","","","","","","Thu Jan 9 12:23:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01367 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 22 to 231 (E-value = 2.9e-133) place AA01367 in the tRNA_m1G_MT family which is described as tRNA (Guanine-1)-methyltransferase (PF01746)","","","","","Hjalmarsson,K.J., Bystrom,A.S. and Bjork,G.R. . Purification and characterization of transfer RNA (guanine-1)methyltransferase from Escherichia coli. J. Biol. Chem. 258(2): 1343-1351.1983 PubMed: 6337136. Bystrom AS, Hjalmarsson KJ, Wikstrom PM, Bjork GR. . The nucleotide sequence of an Escherichia coli operon containing genes for the tRNA(m1G)methyltransferase, the ribosomal proteins S16 and L19 and a 21-K polypeptide. Embo J. 2(6): 899-905.1983 PubMed: 6357787. ","","Thu Jan 9 12:23:15 2003","1","","","" "AA01368","924625","924972","348","ATGTCTAACATCATTAAACAACTTGAACAAGAACAGTTAAAACAAAACGTGCCTAGCTTTCGTCCGGGTGACACATTAGAAGTTAAAGTATGGGTTGTTGAAGGTAGCAAACGTCGTTTGCAAGCGTTCGAAGGCGTGGTTATTGCAGTTCGTAACCGTGGCTTGCATTCCGCATTTACCTTACGCAAAATTTCCAACGGGGTTGGTGTTGAACGGGTATTCCAAACTCACTCTCCGGCTGTTGACAGCATCGTTGTGAAACGTAAAGGTGCTGTGCGTAAAGCGAAACTTTACTACCTGCGTGAACGTTCAGGCAAATCTGCCCGTATCAAAGAACGTTTGGGTGAA","","","13140","MSNIIKQLEQEQLKQNVPSFRPGDTLEVKVWVVEGSKRRLQAFEGVVIAVRNRGLHSAFTLRKISNGVGVERVFQTHSPAVDSIVVKRKGAVRKAKLYYLRERSGKSARIKERLGE","924972","","50S ribosomal protein L19","Cytoplasm","","
InterPro
IPR001857
Family
Ribosomal protein L19
PD002979\"[23-103]TRL19_HAEIN_P44357;
PR00061\"[4-33]T\"[34-63]T\"[88-113]TRIBOSOMALL19
PTHR15680\"[5-115]TRIBOSOMAL PROTEIN L19
PF01245\"[2-114]TRibosomal_L19
TIGR01024\"[2-114]TrplS_bact: ribosomal protein L19
PS01015\"[86-101]TRIBOSOMAL_L19
noIPR
unintegrated
unintegrated
PTHR15680:SF2\"[5-115]T50S RIBOSOMAL PROTEIN L19


","No hits to the COGs database.","Significant hit ( 4.3e-56) to 2/2 blocks of the IPB001857 family, which is described as \"Ribosomal protein L19\". Interpro entry for IP:IPR001857. IPB001857A 17-63 6.6e-29 IPB001857B 74-112 4.3e-26","Residues 23 to 103 match (6e-07) PD:PD219117 which is described as RIBOSOMAL CHLOROPLAST 50S L19 ","","","","","","","","","","","","Thu Jan 9 12:25:59 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01368 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 114 (E-value = 1.7e-73) place AA01368 in the Ribosomal_L19 family which is described as Ribosomal protein L19 (PF01245)","","","","","Bystrom AS, Hjalmarsson KJ, Wikstrom PM, Bjork GR. The nucleotide sequence of an Escherichia coli operon containing genesfor the tRNA(m1G)methyltransferase, the ribosomal proteins S16 and L19 and a 21-K polypeptide. Embo J. 2(6): 899-905.1983 PubMed: 6357787.","","Thu Jan 9 12:25:59 2003","1","","","" "AA01369","925573","925088","486","ATGGAAGGTCGTTTTATTTTTCAATGTTTCGTATTAAGCACGATTTTTATCATCGCCTTGGTGATGGAAATTGCGCCTTGGCCTGTGGGTTTTCAAAGTTTTAAACCGACATGGATCGTGTTGGTTTTCACTTACTGGACATTATCTATTCCACATAGAGTCAACATCGGTCAGGCATTCATTATCGGTATCATTTGGGACATGGTACTTGGTTCAACCCTTGGCATTCACGCATTGGTTCTTTCCGTTTCTGCTTATTTAATCACTACCTACCACCTGATTCTGCGTAACCTTTCCTTATGGATGCAAAGTTTGTTAGTTGTCGCATTAGTGTTTGCCGTTCGTTTAAGTATTTTCTTTATCGAATCACTCCTGCACGACGCCAGCTTTAATTGGCAGGAAATTTTCGGTGCCTTAATCAGTGGCATGCTCTGGCCGTGGATGTTTTTATTATTAAGAAAGGTCCGCTACCGGTTGGGAATTGAT","","","18710","MEGRFIFQCFVLSTIFIIALVMEIAPWPVGFQSFKPTWIVLVFTYWTLSIPHRVNIGQAFIIGIIWDMVLGSTLGIHALVLSVSAYLITTYHLILRNLSLWMQSLLVVALVFAVRLSIFFIESLLHDASFNWQEIFGALISGMLWPWMFLLLRKVRYRLGID","925088","","rod shape-determining protein","Inner membrane, Cytoplasm","","
InterPro
IPR007227
Family
Rod shape-determining protein MreD
PF04093\"[3-155]TMreD
noIPR
unintegrated
unintegrated
signalp\"[1-26]?signal-peptide
tmhmm\"[9-29]?\"[75-95]?\"[105-125]?\"[135-153]?transmembrane_regions


","No hits to the COGs database.","","Residues 35 to 156 match (3e-28) PD:PD034571 which is described as PROTEOME COMPLETE ROD SHAPE-DETERMINING MRED TRANSMEMBRANE SHAPE MEMBRANE INNER CELL ","","","","","","","","","","","","Thu Jan 9 12:27:33 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01369 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 155 (E-value = 2.2e-46) place AA01369 in the MreD family which is described as rod shape-determining protein MreD (PF04093)","","","","","Wachi,M., Doi,M., Okada,Y. and Matsuhashi,M. New mre genes mreC and mreD, responsible for formation of the rod shape of Escherichia coli cells. J. Bacteriol. 171(12): 6511-6516, 1989. PubMed: 2687239.","","Thu Jan 9 12:27:33 2003","1","","","" "AA01370","926646","925576","1071","ATGAAACCCATATTCGGTAAAACCCCTCCCTTAGGATTAAAACTTTTTTTTGCGGTCACCGCCTCTATCGGTTTAATCCTCTCCGACGGTCAAACCGCAGCCATGATTCAAACCCGTGGTTTTCTTGAAACGGCGGTGGGCGGGCTTTATTATTTAGCCAATACGCCGCGTACCGTACTGGACGGTGTGTCCGACAATTTGGTGGATACCAACAAGCTGCAAATCGAAAATAAAGTCTTAAAAACGCAGCTACGCGAAAAAAATGCCGATTTGTTATTGCTTGATCAGCTTAAAGTGGAAAACCAACGTTTACGTTTGCTACTCAATTCGCCCCTACGCATTGACGAATATAAAAAAATTGCCGAAGTGCTTACCGCTGAAATGGACGTTTACCGCCAGCAGGTGGTGATTAATCAAGGGCAGAAAGACGGTGCTTATGTAGGACAACCTATCATTGATGAAAAAGGCGTGGTAGGACAAATTATTTCTGTCGGTGAAAATACCAGCCGCGTGCTGTTGGTTACCGATGTAACCCATGCCATTCCGGTACAGGTATTGCGTAACGATGTGCGCCTGATCGCCAGTGGAACCGGGCATAGCGACGAACTGACGCTGGATAACGTGCCCCGTTCGGTAGATATTGAAAAAGGTGATTTATTGGTAACGTCAGGGCTAGGTGGACGCTTTTTAGAGGGCTACCCTGTTGCCGTTGTAGAGTCAATCTCCCGCGACGGACAAAATTACTTCGCCACCGTCACGGCAAAGCCTTTGGCATCCATTGATAAATTACGCTATGTACTTTTACTCTGGCCAACGAATGAAGATATGCGTAAAGCGAAATCCATCACGCCGGAAGAGGTCCGCAAAGCAGTGCAGCAACGTTTAGAAAATCAAGGTAGCGAAGCCAATAAAGTGAAAAAAGCTGTGGTACCGACTGAGAATAATGAGACGCTAAATACGCCTACTGATACGCCGGAAGATCCCCAACCGGAAACAGCGCCCGATACTTCGGGAGAAAATAATGCACCTGCACCGGTTATTCCGAGCGAACAACCACAGAGAGAAGAAAAT","","","39140","MKPIFGKTPPLGLKLFFAVTASIGLILSDGQTAAMIQTRGFLETAVGGLYYLANTPRTVLDGVSDNLVDTNKLQIENKVLKTQLREKNADLLLLDQLKVENQRLRLLLNSPLRIDEYKKIAEVLTAEMDVYRQQVVINQGQKDGAYVGQPIIDEKGVVGQIISVGENTSRVLLVTDVTHAIPVQVLRNDVRLIASGTGHSDELTLDNVPRSVDIEKGDLLVTSGLGGRFLEGYPVAVVESISRDGQNYFATVTAKPLASIDKLRYVLLLWPTNEDMRKAKSITPEEVRKAVQQRLENQGSEANKVKKAVVPTENNETLNTPTDTPEDPQPETAPDTSGENNAPAPVIPSEQPQREEN","925576","","rod shape-determining protein","Outer membrane, Periplasm, Inner membrane","","
InterPro
IPR005223
Family
Rod shape-determining protein MreC, subtype
TIGR00219\"[1-286]TmreC: rod shape-determining protein MreC
InterPro
IPR007221
Family
Rod shape-determining protein MreC
PF04085\"[121-273]TMreC
noIPR
unintegrated
unintegrated
signalp\"[1-24]?signal-peptide
tmhmm\"[15-33]?transmembrane_regions


","No hits to the COGs database.","","Residues 270 to 310 match (4e-08) PD:PD449233 which is described as PROTEOME COMPLETE MREC ","","","","","","","","","","","","Thu Jan 9 12:28:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01370 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 121 to 273 (E-value = 1e-66) place AA01370 in the MreC family which is described as rod shape-determining protein MreC (PF04085)","","","","","Wachi,M., Doi,M., Okada,Y. and Matsuhashi,M. New mre genes mreC and mreD, responsible for formation of the rodshape of Escherichia coli cells. J. Bacteriol. 171(12): 6511-6516, 1989. PubMed: 2687239.","","Thu Jan 9 12:28:44 2003","1","","","" "AA01371","927771","926719","1053","ATGCTATTTAAAAAAATTCGCGGTCTGTTTTCTAACGATCTTTCCATCGACCTGGGTACGGCAAACACACTTATTTATGTAAAAGGTCAGGGCATTGTCCTTGACGAACCTTCCGTAGTAGCCATTCGCCGCGACCGCAGCGGTTCCCTAAAAAGTATTGCCGCCGTCGGTAAAGAAGCGAAACAAATGTTGGGCCGTACGCCAAAAAGCATTGAAGCCATCCGCCCGATGAAAGACGGGGTTATCGCCGACTTCTTCGTCACCGAAAAAATGTTGCAGTATTTCATTAAACAAGTGCACAGCGGCAATTTCATGCGTCCGAGCCCACGCGTATTAATTTGCGTACCGGCAGGCGCCACCCAAGTAGAACGTCGCGCCATTAAAGAATCCGCAATCGGTGCCGGCGCCCGCGAAGTATATTTAATCGAAGAACCGATGGCGGCGGCAATCGGTGCGAAATTGCCGGTTTCCACTGCAACCGGTTCCATGGTGATCGATATCGGCGGCGGTACCACCGAAGTGGCGATTATTTCCTTAAACGGTATCGTCTATTCTTCTTCCGTACGCATCGGTGGTGACCGTTTTGATGAAGCCATTGTGTCTTATATCCGCAAAACCTTCGGTTCCATTATCGGCGAACAAACCGCCGAACGAATCAAAAAAGAAATCGGTATCGCCTACATTCAGGAAGACGATGAAATCAAAGAAATGGAAATTCACGGTTCTAACATTGCCGAAGGGGCGCCACGTTCCATTACGCTAAGTTCCCGTGATGTGTTAGAAGCGATTCGTCAACCGCTTAGCGGCATCGTTGCCGCCGTACGCACGGCGCTTGAAGAATGCCAACCGGAACACGCCGCCGATATTTTTGAACGCGGCATGGTGCTAACCGGCGGCGGTGCGTTGTTACGTAACATCGATGTGTTATTAGCCAAAGAGTCCGGCGTACCGACTATCGTTGCAGAAGAACCGTTAACCTGTGTGGCACGTGGTGGTGGCGAAGCACTGGATATGATCGATATGCACGGCGGCGATATTTTCAGTGATGAAATT","","","38957","MLFKKIRGLFSNDLSIDLGTANTLIYVKGQGIVLDEPSVVAIRRDRSGSLKSIAAVGKEAKQMLGRTPKSIEAIRPMKDGVIADFFVTEKMLQYFIKQVHSGNFMRPSPRVLICVPAGATQVERRAIKESAIGAGAREVYLIEEPMAAAIGAKLPVSTATGSMVIDIGGGTTEVAIISLNGIVYSSSVRIGGDRFDEAIVSYIRKTFGSIIGEQTAERIKKEIGIAYIQEDDEIKEMEIHGSNIAEGAPRSITLSSRDVLEAIRQPLSGIVAAVRTALEECQPEHAADIFERGMVLTGGGALLRNIDVLLAKESGVPTIVAEEPLTCVARGGGEALDMIDMHGGDIFSDEI","926719","","rod shape-determining protein","Cytoplasm","","
InterPro
IPR001023
Family
Heat shock protein Hsp70
PR00301\"[12-25]T\"[111-131]T\"[170-180]T\"[291-307]THEATSHOCK70
PTHR19375\"[113-205]THEAT SHOCK PROTEIN 70KDA
InterPro
IPR004753
Family
Cell shape determining protein MreB/Mrl
PR01652\"[53-71]T\"[73-96]T\"[137-156]T\"[192-212]T\"[307-333]TSHAPEPROTEIN
PF06723\"[11-344]TMreB_Mbl
TIGR00904\"[10-344]TmreB: cell shape determining protein, MreB/
noIPR
unintegrated
unintegrated
G3DSA:3.30.420.40\"[9-168]Tno description
G3DSA:3.90.640.10\"[191-266]Tno description
PTHR19375:SF11\"[113-205]TMICROSOMAL STRESS 70 PROTEIN ATPASE CORE PRECURSOR


","BeTs to 15 clades of COG1077COG name: HSP70 class molecular chaperones involved in cell morphogenesisFunctional Class: DThe phylogenetic pattern of COG1077 is a-mp--yqv---b-efghs-ujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-09) to 3/6 blocks of the IPB001023 family, which is described as \"Heat shock protein hsp70\". Interpro entry for IP:IPR001023. IPB001023A 14-46 12 IPB001023B 95-148 0.00042 IPB001023C 162-197 0.043","Residues 111 to 183 match (8e-07) PD:PD588656 which is described as MREB3 MREB4 SHAPE-DETERMINING CELL ","","","","","","","","","","","","Thu Jan 9 12:30:52 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01371 is paralogously related to AA00657 (3e-08), AA00713 (8e-08) and AA00830 (0.001).","","","","","","Residues 11 to 344 (E-value = 7.5e-210) place AA01371 in the MreB_Mbl family which is described as MreB/Mbl protein (PF06723)","","","","","Abhayawardhane Y, Stewart GC. Bacillus subtilis possesses a second determinant with extensivesequence similarity to the Escherichia coli mreB morphogene. J Bacteriol. 1995 Feb;177(3):765-73. PMID: 7836311 Wachi M, Matsuhashi M. Negative control of cell division by mreB, a gene that functions in determining the rod shape of Escherichia coli cells. J Bacteriol. 1989 Jun;171(6):3123-7. PMID: 2656641 Doi M, Wachi M, Ishino F, Tomioka S, Ito M, Sakagami Y, Suzuki A,Matsuhashi M. Determinations of the DNA sequence of the mreB gene and of the gene products of the mre region that function in formation of the rod shape of Escherichia coli cells. J Bacteriol. 1988 Oct;170(10):4619-24. PMID: 3049542","","Thu Jan 9 12:30:52 2003","1","","","" "AA01372","928021","930423","2403","ATGGCGAAAAAACACAATAAATCCCCTTTGCAGGATCCGAATTACGCAAAGGAATTGGCGAAATATGACAACCCGATTCCGAGCCGCGAATTTATCCTGCAAATTATCCGCAAGCAAAACTCCCCCATGAGCAAAGAAGAGATTTTTGCAGCCCTGGCGATTTCCAACGATGAACAACAGGAAGCCATGCGTCGCCGTTTACGCGCCATGGAAAACGACGGGCAACTGGTGTTTACCAAGCGTAAACGCTATGCTTTGCCGGAAAAACTGGATTTGCTCAAAGGCATGGTTATCGGGCATCGGGAGGGTTTCGGCTTTTTGCAGGTGGAAGGGAAAAAAGAGGATTTTTTCATTCCGAATGTGCAAATGCAAAAAGTTATGCACGGTGATTACGTACTGGCCCAAGCCAACGGATTTGACCGTAAAGGTCGCCCTGAGGTGCGCATCGTGCGTTTATTGGAGGCGAACAAAAAGCAAATTGTCGGTCGCTTTTTCTTAGAACAGGGCATCGGTTATGTGGTGCCTGATGACAGCCGTATTACACGCGATATTTTAATCCCCGACGAAGCCCGCCTTGGCGCGCGCATGGGGCAGGTTGTGGTGGTGGAACTGAACCCGCGCACCGCCCCGTTCTTCCAGCCGATCGGTAAAATTACCGAAATCCTCGGCGATAACATGGCAAAAGGGATGGAAGTGGAAATTGCCATTCGCAAGCATGACATTCCTCACGCGTTCCCAAGTGCGGTGGAAAAACAACTTAAAAAATGGCAGGAAGAGGTGCCGGAAGAGGCAAAACGCGGGCGCGTGGATTTGCGCGATTTGCCGCTGGTGACCATTGATGGCGAAGATGCCCGCGATTTTGACGACGCCGTATTCTGCCAAAAACAAGGCAAAGGCTGGAAACTGTGGGTGGCGATTGCCGATGTGAGCTATTACGTTCGACCGAAAAGCGCCTTGGATCAGGAAGCGTATAATCGAGGCAACTCTATGTATTTCCCGAATCGGGTGGTGCCGATGTTGCCGGAAAAGCTCTCCAACGGGCTATGTTCCTTAAATCCGCAGGTGGATCGGCTGTGCATGGTGTGTGAAATGACGCTTTCCGCTAAAGGCAAAATGACGGACTACCGATTTTACGAAGCGGTGATGAACTCACACGCCCGTTTAACCTATAACAAAGTCGCAAAAATACTAGAAAAAGACACCGCACTTTACGAGCGTTACGCGCCTTTAGTACCGCATTTACAAGAACTTCACGATATGTATCGGGCGCTGGTGAAAGCCCGTCAGCAGCGGGGCGCCATCGAATTTGAAACCATCGAAAGTAAATTTATTTTTAATGCGTTGGGGCGTATTGAACGTATCGAGCCGGTAGTGCGCAACGATGCCCATAAAATCATTGAAGAATGTATGATTCTGGCGAATATTGCCGCCGCCAATTTTATGGAGAAAAATCAGGAACCGGCGCTGTATCGCATTCATGCGTTGCCGGGGGAAGAAAAACTTACGGCGTTTCGCAGTTTCTTGGCGGAATGTGGCTTAACGCTGGGCGGTGGCAATAAACCGACGCCGATGGATTATGCCGCGTTGCTGGAACAAATCCAAACGCGCCCCGATCGCGAATTAATTCAAACCATGTTATTGCGCTCCATGAGCCAGGCGGTGTATAGCGCCGATAATATCGGACATTTCGGCTTGGCATTGAGCGAATACGCACATTTTACGTCGCCGATCCGCCGTTATCCCGATTTAACTTTACACCGCAGTATCAAATACTTATTGGCGAAAAAGAAAGGTTCCAAACGTAAAACCACCGACACCGGCGGTTATCATTATCAGCTTGACGAAATGGATGTCTGCGGCGTCCATTGTTCCACCACGGAACGTCGTGCCGATGACGCCACCCGGGAAGTGGCGGATTGGCTGAAATGCGAATATATGCAGGATCATGTGGGTGAAGAATTTGACGGCGTGATTTCCTCCGTCACCGGTTTTGGCTTTTTCGTCCGCTTAAACGACTTATTTATTGACGGCTTGGTACATATTTCCGGGCTGGCGAACGATTATTATTTGTTCGATATGCCGAAACAGCGTCTTATCGGTGAAAATAGCGGCATGATTTTCCGTATCGGCGATGTGGTGAAAGTGCGGGTGGACGCGGTGAATCTGGAACAAAAACAAATTGATTTTGCCCTGATTGACAGTGAACGTAAACCAAGACGCAGTGGCAAAACGGCGAGAACCAAAGCGAAGAAAGCCGAAACCGAAGCCTCTAAAAAGTCAGCGAAAAAGCAACCCGTTGAAAAGAAAAAAACGAAACCACAGAAAAGTGCGGTCAAAAATAATGGCGTTTCTAAAACGAACCCGCAAGCCGCAGCTAAGAATAAGAAGGCGAAGAACAAAGCA","","","91137","MAKKHNKSPLQDPNYAKELAKYDNPIPSREFILQIIRKQNSPMSKEEIFAALAISNDEQQEAMRRRLRAMENDGQLVFTKRKRYALPEKLDLLKGMVIGHREGFGFLQVEGKKEDFFIPNVQMQKVMHGDYVLAQANGFDRKGRPEVRIVRLLEANKKQIVGRFFLEQGIGYVVPDDSRITRDILIPDEARLGARMGQVVVVELNPRTAPFFQPIGKITEILGDNMAKGMEVEIAIRKHDIPHAFPSAVEKQLKKWQEEVPEEAKRGRVDLRDLPLVTIDGEDARDFDDAVFCQKQGKGWKLWVAIADVSYYVRPKSALDQEAYNRGNSMYFPNRVVPMLPEKLSNGLCSLNPQVDRLCMVCEMTLSAKGKMTDYRFYEAVMNSHARLTYNKVAKILEKDTALYERYAPLVPHLQELHDMYRALVKARQQRGAIEFETIESKFIFNALGRIERIEPVVRNDAHKIIEECMILANIAAANFMEKNQEPALYRIHALPGEEKLTAFRSFLAECGLTLGGGNKPTPMDYAALLEQIQTRPDRELIQTMLLRSMSQAVYSADNIGHFGLALSEYAHFTSPIRRYPDLTLHRSIKYLLAKKKGSKRKTTDTGGYHYQLDEMDVCGVHCSTTERRADDATREVADWLKCEYMQDHVGEEFDGVISSVTGFGFFVRLNDLFIDGLVHISGLANDYYLFDMPKQRLIGENSGMIFRIGDVVKVRVDAVNLEQKQIDFALIDSERKPRRSGKTARTKAKKAETEASKKSAKKQPVEKKKTKPQKSAVKNNGVSKTNPQAAAKNKKAKNKA","930423","","ribonuclease r, virulence associated protein","Cytoplasm","","
InterPro
IPR001900
Domain
Ribonuclease II and R
PF00773\"[268-595]TRNB
PS01175\"[562-586]TRIBONUCLEASE_II
InterPro
IPR003029
Domain
RNA binding S1
PF00575\"[647-732]TS1
SM00316\"[649-732]TS1
PS50126\"[651-732]TS1
InterPro
IPR004476
Family
RNase II and RNase R, bacteria
TIGR00358\"[75-732]T3_prime_RNase: VacB and RNase II family 3'-
InterPro
IPR011129
Domain
Cold shock protein
SM00357\"[94-153]TCSP
InterPro
IPR011805
Family
Ribonuclease R, bacterial
TIGR02063\"[26-733]TRNase_R: ribonuclease R
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[651-758]Tno description
InterPro
IPR013223
Domain
Ribonuclease B, OB region N-terminal
PF08206\"[95-152]TOB_RNB
InterPro
IPR013668
Domain
Ribonuclease R winged-helix domain
PF08461\"[30-93]THTH_12
noIPR
unintegrated
unintegrated
PTHR23355\"[26-800]TRIBONUCLEASE
PTHR23355:SF9\"[26-800]TRIBONUCLEASE R


","BeTs to 18 clades of COG0557COG name: ExoribonucleasesFunctional Class: KThe phylogenetic pattern of COG0557 is -o----yqvd-lbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.3e-56) to 4/4 blocks of the IPB001900 family, which is described as \"Ribonuclease II domain\". Interpro entry for IP:IPR001900. IPB001900A 278-290 9.2e-07 IPB001900B 302-341 3.2e-26 IPB001900C 465-474 7.5e-06 IPB001900D 570-589 3e-13","Residues 562 to 681 match (2e-07) PD:PD139380 which is described as CHROMOSOME I CONTROL SIMILAR C609.01 II III F48E8.6 NUCLEASE HOMOLOG ","","","","","","","","","","","","Thu Jan 9 12:34:18 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01372 is paralogously related to AA01737 (3e-52) and AA00939 (4e-09).","","","","","","Residues 647 to 732 (E-value = 2.3e-19) place AA01372 in the S1 family which is described as S1 RNA binding domain (PF00575)","","","","","Tobe,T., Sasakawa,C., Okada,N., Honma,Y. and Yoshikawa,M. vacB, a novel chromosomal gene required for expression of virulence genes on the large plasmid of Shigella flexneri J. Bacteriol. 174 (20), 6359-6367 (1992) PubMed: 1400189 Cheng,Z.F., Zuo,Y., Li,Z., Rudd,K.E. and Deutscher,M.P. The vacB gene required for virulence in Shigella flexneri and Escherichia coli encodes the exoribonuclease RNase R J. Biol. Chem. 273 (23), 14077-14080 (1998) PubMed: 9603904 ","","Thu Jan 9 12:34:18 2003","1","","","" "AA01374","930423","931157","735","ATGAGTGAAACCATTTATGGCATCCACGCCGTTAAGGCGTTTGTGACCCATTATCCGGAGCGTTTAATTGAAGTCTGGGCGCTAAAAGGACGCGATGATCAACGTTTGCAACCGTTAATTAATGAAATTCAGCGTTTGGGGATTTCTGTTCAATTTTTAAACCGCCAAACGCTGGATAAAAAAGCCGAAGGCGAAGTGCATCAAGGTATTATTGCGCGCGTGCATTCCTTACCGGAATTAAACGAGCATGATTTGGATCGTTTGCTGGAACAGCAAAATACGCCTTTATTGTTGGTATTGGACGGCGTGACGGATCCGCATAACTTGGGTGCCTGTCTGCGTACTGCCGATGCAGCGGGCGTGAATGCGGTGATTGTGCCGAAAGATAAATCGGCGCAATTGAATTCCACCGCGCGTAAAGTGGCGTGCGGTGCGGCGGAAAATGTGCCGCTTATTCGTGTGACCAACCTTGCCCGCACCTTGCGTGAATTGCAGAAACGGCATAATGTGTGGGTTGTCGGCACCGCGGGCGAAACTACGGAAACGCTGTATCAAACCAAACTGACCGGCGCATTAGCCCTGGTGATGGGCGCGGAAGGCGAGGGAATGCGTCGTTTAACCCGCGAACACTGCGACCAATTAATCAGCATTCCAATGATGGGTTCCGTTTCTTCTCTCAATGTTTCCGTTGCCACCGGCGTGTGTTTATTTGAAATCGTGCGGCAGCGCTTAAAA","","","27034","MSETIYGIHAVKAFVTHYPERLIEVWALKGRDDQRLQPLINEIQRLGISVQFLNRQTLDKKAEGEVHQGIIARVHSLPELNEHDLDRLLEQQNTPLLLVLDGVTDPHNLGACLRTADAAGVNAVIVPKDKSAQLNSTARKVACGAAENVPLIRVTNLARTLRELQKRHNVWVVGTAGETTETLYQTKLTGALALVMGAEGEGMRRLTREHCDQLISIPMMGSVSSLNVSVATGVCLFEIVRQRLK","931157","","tRNA/rRNA methyltransferase","Cytoplasm","","
InterPro
IPR001537
Domain
tRNA/rRNA methyltransferase, SpoU
PD001243\"[88-244]TYJFH_HAEIN_P44906;
PF00588\"[95-237]TSpoU_methylase
InterPro
IPR003833
Domain
Allophanate hydrolase subunit 1
SM00796\"[48-194]Tno description
InterPro
IPR004441
Family
RNA methyltransferase TrmH, group 3
TIGR00186\"[1-243]TrRNA_methyl_3: RNA methyltransferase, TrmH
InterPro
IPR013123
Domain
RNA 2-O ribose methyltransferase, substrate binding
PF08032\"[4-80]TSpoU_sub_bind
noIPR
unintegrated
unintegrated
G3DSA:3.30.1330.30\"[3-78]Tno description
G3DSA:3.40.1280.10\"[79-244]Tno description
PTHR12029\"[49-243]TRNA METHYLTRANSFERASE
PTHR12029:SF7\"[49-243]TRRNA METHYLASE


","No hits to the COGs database.","Significant hit ( 1.7e-26) to 3/3 blocks of the IPB001537 family, which is described as \"tRNA/rRNA methyltransferase (SpoU)\". Interpro entry for IP:IPR001537. IPB001537A 98-122 6.6e-15 IPB001537B 194-202 0.098 IPB001537C 225-238 1.4e-06","Residues 135 to 238 match (3e-07) PD:PD022890 which is described as METHYLTRANSFERASE COMPLETE PROTEOME 2.1.1.- TRANSFERASE TRNA/RRNA YFIF RNA HI0424 PM1857 ","","","","","","","","","","","","Thu Jan 9 12:36:05 2003","","Wed Apr 13 08:47:18 2005","Wed Apr 13 08:47:18 2005","Wed Apr 13 08:47:18 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA01374 is paralogously related to AA01441 (2e-07).","Wed Apr 13 08:47:18 2005","","","","","Residues 95 to 237 (E-value = 1.8e-60) place AA01374 in the SpoU_methylase family which is described as SpoU rRNA Methylase family (PF00588)","Wed Apr 13 08:47:18 2005","","","","Urbonavicius J, Durand JM, Bjork GR.Three modifications in the D and T arms of tRNA influence translation in Escherichia coli and expression of virulence genes in Shigella flexneri.J Bacteriol. 2002 Oct;184(19):5348-57.PMID: 12218021 Hori H, Suzuki T, Sugawara K, Inoue Y, Shibata T, Kuramitsu S, Yokoyama S,Oshima T, Watanabe K.Identification and characterization of tRNA (Gm18) methyltransferase from Thermus thermophilus HB8: domain structure and conserved amino acid sequence motifs.Genes Cells. 2002 Mar;7(3):259-72.PMID: 11918670 Koonin EV, Rudd KE.SpoU protein of Escherichia coli belongs to a new family of putative rRNA methylases.Nucleic Acids Res. 1993 Nov 25;21(23):5519.PMID: 8265370","","Thu Jan 9 12:40:29 2003","1","","","" "AA01375","931160","931264","105","ATGCCATCCAGCGTGAATAAGACGGAAACCTTTTCGTCTTATCGTTTCATATTCTCCTCAAAAAACACCTTGAAAAACAACCGCACTTTTTCTTTGCCAAAAAAC","","","4055","MPSSVNKTETFSSYRFIFSSKNTLKNNRTFSLPKN","931264","","hypothetical protein","Periplasm, Cytoplasm","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 09:51:16 2004","Thu Feb 26 09:51:16 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01375 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:51:16 2004","","","","","","","","","","","","","1","","","" "AA01376","931303","931470","168","ATGCGCAAAAAGGAATATTTCTTTTGGGTTTTTGCGCTTTATCATTTCGCATACAATCAAATGACAGGTATTTTTGTGATACTTCTCACAAAATCCCATAAATATTCTTTTCTGTTTTTGGATTTCTTTTATTATTCCACCGTGCTCTTCATAAAAGACAATTTGACT","","","6981","MRKKEYFFWVFALYHFAYNQMTGIFVILLTKSHKYSFLFLDFFYYSTVLFIKDNLT","931470","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-19]?signal-peptide
tmhmm\"[10-30]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Fri Feb 27 07:02:42 2004","Fri Feb 27 07:02:42 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01376 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Fri Feb 27 07:02:42 2004","","","","","","","","","","","","","1","","","" "AA01378","931493","932932","1440","ATGTTTGGTCCATTTAAACCGGCTCTACACATTGCAGAGTTGCCGGCAGACAAAATTGATTCCACCTATAAACGTCTTCGTTGGCAGGTATTTGCCGGGATCTTTTTTGGCTACGCTGCTTATTATTTTGTGCGTGCAAACTTTGACTTGGCGCAACCGGGCTTAATTCAAGCTGGTTTATACACAAAAGCTGAGTTGGGGGTTATCGGTTCTGCGGCAGGTTTAGCCTATGGTTTATCAAAATTCGTGATGGCGGGGATGTCAGACCGTTCTAACCCGCGTGTATTCTTACCGTTCGGTTTATTACTCTCCGGTTTATGTATGACCTTAATGGGCGTGTTCCCATGGGCAACTTCCGGCATCGCCATTATGTGGGTGATGATCTTCTTAAACGGTTGGTTCCAAGGAATGGGCTGGCCTCCATGTGGTCGTACCATGGTGCACTGGTGGTCTAAATCCGAACGAGGGACTATCGTGTCCATTTGGAATACTGCGCACAACATCGGCGGTATGATGCCGGGTGCGATGGTGTTATTGGCAAGTGCGATTTTCTTCAGCACTCACGGTGTGGAAGCGCAAGCAAAAGACGTATGGCAACAATCCTTATACTATCCTGGTATTGCTGCCATGATCTGTGCAATTCCGGTATATTTCGTGATGCGTGATACCCCACAATCTTGTGGTTTACCCTCCATCGAAAAATGGCGTAACGACTACCCGGATGACTATAACGAAAAAACTTACGAAAATGACTTAACCGCAAAAGAAATCTTCGTAACTTATGTATTGAAAAACAAATTGTTATGGTACATCGCCATTGCTAACGTGTTCGTTTACTTAATCCGCTACGGCGTATTGAAATGGTCTCCGGTTTACTTGAGTGAAGTGAAACACTTCAACATCAAAGGTACCGCATGGGCATACACCATTTATGAATTGGCGGCCGTTCCGGGTACATTACTTTGCGGTTGGGTATCTGACCATGTATTCAAAGGTAAACGTGGCTTAACCGGTTTCATCTTTATGATTTTAACCACCGCAGCGGTAGCCACATACTGGATGAACCCTGCAACACCGGAAGCTGAGCTTGCAAACTACAGCGCATGGTATGAAAACCCATACCAATTAACCGACTTTATTTTGATGACCTTAATCGGTTTCTTAATCTACGGCCCTGTGATGCTAATCGGCTTGCACGCCCTTGAACTTGCACCGAAAAAAGCGGCAGGTACCGCAGCAGGTTTCACCGGTTTATTCGGTTACTTAGGCGGTACCGTGTCTGCATCAGCAGTTATCGGTTGGGCAGCCCAACACTACGGCTGGGACGGCGGTTTTTACGTGATGATCGGCGGTGGTATCTTAGCGGTCATCTTGCTCTTCATCGTGATGATTGAAGAAGGCAAACACAAAGCGAAATTAGGAGATACTTACGGTACCAAA","","","53618","MFGPFKPALHIAELPADKIDSTYKRLRWQVFAGIFFGYAAYYFVRANFDLAQPGLIQAGLYTKAELGVIGSAAGLAYGLSKFVMAGMSDRSNPRVFLPFGLLLSGLCMTLMGVFPWATSGIAIMWVMIFLNGWFQGMGWPPCGRTMVHWWSKSERGTIVSIWNTAHNIGGMMPGAMVLLASAIFFSTHGVEAQAKDVWQQSLYYPGIAAMICAIPVYFVMRDTPQSCGLPSIEKWRNDYPDDYNEKTYENDLTAKEIFVTYVLKNKLLWYIAIANVFVYLIRYGVLKWSPVYLSEVKHFNIKGTAWAYTIYELAAVPGTLLCGWVSDHVFKGKRGLTGFIFMILTTAAVATYWMNPATPEAELANYSAWYENPYQLTDFILMTLIGFLIYGPVMLIGLHALELAPKKAAGTAAGFTGLFGYLGGTVSASAVIGWAAQHYGWDGGFYVMIGGGILAVILLFIVMIEEGKHKAKLGDTYGTK","932932","","glycerol-3-phosphatase transporter","Inner membrane, Cytoplasm","","
InterPro
IPR000849
Family
GlpT transporter
TIGR00881\"[35-445]T2A0104: phosphoglycerate transporter family
PS00942\"[154-170]TGLPT
InterPro
IPR005267
Family
Glycerol-3-phosphate transporter
TIGR00712\"[1-468]TglpT: glycerol-3-phosphate transporter
InterPro
IPR007114
Family
Major facilitator superfamily
PS50850\"[25-467]TMFS
InterPro
IPR011701
Family
Major facilitator superfamily MFS_1
PF07690\"[34-437]TMFS_1
noIPR
unintegrated
unintegrated
PTHR11662\"[5-353]T\"[371-477]TSODIUM-DEPENDENT PHOSPHATE TRANSPORTERS
PTHR11662:SF13\"[5-353]T\"[371-477]TGLYCEROL-3-PHOSPHATE TRANSPORTER (HEXOSE TRANSPORTER)
tmhmm\"[28-46]?\"[60-80]?\"[95-115]?\"[121-141]?\"[162-182]?\"[201-219]?\"[268-286]?\"[305-325]?\"[335-355]?\"[379-401]?\"[416-436]?\"[442-462]?transmembrane_regions


","No hits to the COGs database.","Significant hit (1.1e-185) to 7/7 blocks of the IPB000849 family, which is described as \"GlpT family of transporters\". Interpro entry for IP:IPR000849. IPB000849A 23-55 1.1e-24 IPB000849B 65-105 2.3e-29 IPB000849C 135-170 4.8e-31 IPB000849D 202-238 6.1e-24 IPB000849E 256-293 1.6e-30 IPB000849F 310-327 3.3e-11 IPB000849G 385-417 4.7e-28 IPB000849C 122-157 0.021","Residues 5 to 132 match (6e-11) PD:PD537988 which is described as PROTEOME LIPOPOLYSACCHARIDE CORE COMPLETE HOMOLOG KDTB BIOSYNTHESIS ","","","","","","","","","","","","Thu Jan 9 13:58:03 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01378 is paralogously related to AA02864 (1e-117), AA00497 (3e-72) and AA02792 (6e-51).","","","","","","","","","","","Eiglmeier,K., Boos,W. and Cole,S.T. Nucleotide sequence and transcriptional startpoint of the glpT gene ofEscherichia coli: extensive sequence homology of the glycerol-3-phosphate transport protein with components of the hexose-6-phosphate transport system Mol. Microbiol. 1 (3), 251-258 (1987) PubMed: 3329281 Gott,P. and Boos,W. The transmembrane topology of the sn-glycerol-3-phosphate permease of Escherichia coli analysed by phoA and lacZ protein fusions Mol. Microbiol. 2 (5), 655-663 (1988) PubMed: 3141744 Auer M, Kim MJ, Lemieux MJ, Villa A, Song J, Li XD, Wang DN. High-yield expression and functional analysis of Escherichia coliglycerol-3-phosphate transporter. Biochemistry. 2001 Jun 5;40(22):6628-35. PMID: 11380257 Kaplan,J.B. and Fine,D.H.Codon usage in Actinobacillus actinomycetemcomitansFEMS Micrbiol. Lett. 163 (1), 31-36 (1998)PubMed: 9631542","","Thu Jan 9 13:58:03 2003","1","","","" "AA01379","933169","934248","1080","ATGAAACTTAAAACGTTAGCCCTTAGCTTAATTGCAGCAACCGTTTTAGCCGGTTGTAGCGCAAATTATCACAAAGGTTATGATATGGATAAAATTATTATTGCCCATCGTGGCGCCAGCGGCTATTTACCGGAGCATACACTGGAAGCAAAAGCCCTTGCCTTTGCCCAACACGCGGATTATTTGGAGCAAGATTTAGCGATGACAAAAGACGGTCGTTTAGTGGTAATTCATGATCACTTCTTAGACGGATTAACCGATGTGGCGAAAAAATTCCCGAATCGTCACCGCAAAGATGGTCGTTATTATGTGATCGATTTTACGCTGAAAGAAATTCAAAGTTTGAATATGACAGAAAACTTTGAAACTAAAGATAGCAAACAAGTTGCCGTTTATCCGGGACGTTTCCCGCTTTGGAAATCCCACTTCAAGATTCATACCTTTGAAGATGAGCTTGAATTTATTCAAGGGTTAGAAAAATCGACAGGCAAAAAAGTGGGGATTTATCCTGAAATCAAAGCACCTTGGTTCCACCACAAAAACGGTAAAGACATTGCCGCAGCAACCCTTAAAGTGTTGAAAAAATACGGTTATGACAAAAAAACCGACAGGGTTTACTTGCAAACTTTCGACTTTAATGAGTTAAAACGCATTAAAACCGAATTGTTACCGAAAATGGGCATGGATTTGAAATTGGTTCAATTAGTTGCCTACACCGATTGGCATGAAACCGAAGAAAAAGATGCCAAAGGCAAATGGGTGAACTACGATTACGATTGGATGTTCAAACCGGGCGCCATGGCGGAAGTGGTGAAATATGCCGATGGTGTGGGGCCGGGTTGGTATATGTTGATCGACAAAGAAAAATCCAAACCGGGCAAAATCGAATATACGCCTTTAGTCAAAGAATTAGCGCAGTACAAGATTGAATTACACCCATACACCGTGCGTAAAGATGCCTTACCGGACTTCTTCACCGATGTGAACCAAATGTATGATGCGTTGTTGAATAAATCCGGCGCCACCGGTGTGTTTACCGACTTTCCGGATACCGGCGTGCAATTTTTGAAAAAACAAAAA","","","41660","MKLKTLALSLIAATVLAGCSANYHKGYDMDKIIIAHRGASGYLPEHTLEAKALAFAQHADYLEQDLAMTKDGRLVVIHDHFLDGLTDVAKKFPNRHRKDGRYYVIDFTLKEIQSLNMTENFETKDSKQVAVYPGRFPLWKSHFKIHTFEDELEFIQGLEKSTGKKVGIYPEIKAPWFHHKNGKDIAAATLKVLKKYGYDKKTDRVYLQTFDFNELKRIKTELLPKMGMDLKLVQLVAYTDWHETEEKDAKGKWVNYDYDWMFKPGAMAEVVKYADGVGPGWYMLIDKEKSKPGKIEYTPLVKELAQYKIELHPYTVRKDALPDFFTDVNQMYDALLNKSGATGVFTDFPDTGVQFLKKQK","934248","","glycerophosphoryl diester phosphodiesterase (protein D)","Periplasm, Outer membrane","","
InterPro
IPR004129
Family
Glycerophosphoryl diester phosphodiesterase
PTHR23344\"[32-357]TGLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE
PF03009\"[36-351]TGDPD
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.190\"[30-359]Tno description
PS51257\"[1-19]TPROKAR_LIPOPROTEIN
signalp\"[1-21]?signal-peptide
tmhmm\"[5-23]?transmembrane_regions


","BeTs to 14 clades of COG0584COG name: Glycerophosphoryl diester phosphodiesteraseFunctional Class: CThe phylogenetic pattern of COG0584 is -o-pkzy-vdrlb-efgh---j--twNumber of proteins in this genome belonging to this COG is","","Residues 217 to 255 match (8e-14) PD:PD584033 which is described as PHOSPHODIESTERASE GLYCEROPHOSPHODIESTER LIPOPROTEIN COMPLETE PROTEOME DIESTER GLYCEROL D PRECURSOR GLYCEROPHOSPHORYL ","","","","","","","","","","","","Thu Jan 9 14:02:39 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01379 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 36 to 351 (E-value = 5.6e-106) place AA01379 in the GDPD family which is described as Glycerophosphoryl diester phosphodiesterase family (PF03009)","","","","","Ahren IL, Janson H, Forsgren A, Riesbeck K.Protein D expression promotes the adherence and internalization of non-typeable Haemophilus influenzae into human monocytic cells.Microb Pathog. 2001 Sep;31(3):151-8.PMID: 11500100 Janson,H., Heden,L.O., Grubb,A., Ruan,M.R. and Forsgren,A. Protein D, an immunoglobulin D-binding protein of Haemophilusinfluenzae: cloning, nucleotide sequence, and expression in Escherichia coli Infect. Immun. 59 (1), 119-125 (1991) PubMed: 1987023 Janson,H., Ruan,M. and Forsgren,A. Limited diversity of the protein D gene (hpd) among encapsulated and nonencapsulated Haemophilus influenzae strains Infect. Immun. 61 (11), 4546-4552 (1993) PubMed: 8104899 Song,X.M., Forsgren,A. and Janson,H. The gene encoding protein D (hpd) is highly conserved among Haemophilus influenzae type b and nontypeable strains Infect. Immun. 63 (2), 696-699 (1995) PubMed: 7822043 Janson,H., Heden,L.O. and Forsgren,A. Protein D, the immunoglobulin D-binding protein of Haemophilus influenzae, is a lipoprotein Infect. Immun. 60 (4), 1336-1342 (1992) PubMed: 1548059 ","","Thu Jan 9 14:05:25 2003","1","","","" "AA01383","935426","934311","1116","ATGAACAAACATTTAGCACTTTTACTGCGCCTATTACAAATTCCCAAACTGGGTCCTACCACAATTCATAAAATCCTTGCGCAAATCAATTTATTCGAATTGCAATATTACGACGCGGCTGCATTTACGCAAATGGGCTGGAACGCACAGCAAATTCAAGCATGGTTTCATCCGGAACAGCGCTACATTGAACCGGCACTCTTGTGGGGAGAAAAAGAAGGGAATCATATTCTTGATTATTTTCACCCTGATTATCCCGAATTATTAAAACAAATCGAAAGCGCGCCGCCGGTATTGTTCGTCAAAGGCGCGACAAGTGCGCTATCACAGCAACAAATCGCTATTGTCGGCAGCCGCCAATGTTCAAGTTACGGTGAATATTGGGCGAAATATTTTGCCACGGAATTAACCACCAATGGTTTCATCATTACCAGCGGGTTAGCATTAGGCATTGATGGTTTCTGTCATCAGGCTGTGGTCGATTTAAAACAACCGACCATCGCGGTTTTAGGTAGCGGATTGGAAGAAGTGTATCCCGCCAAACATCTCAAATTAGCGCAGAATATTATTGAACATGGCGGTGCGTTGGTTTCTGAATTTTTTCCGCTACAACCGCCTATTGCAGAAAATTTTCCCCGCCGCAATCGCATTATCAGTGGGTTATCATTAGCAACCTTAATTATTGAAGCCACCGAACGTAGCGGATCATTAATTACAGCACGCTATGCATTAGAACAAAAGAGAGAAATTTTTGCACTACCGGGCAATATTCAAAGTCAGTTCAGCCAAGGTTGCCATAAGCTTATTAAACAGGGCGCAATGCTGGTCGAAAACGTGGAAGATATTTTAGAAAATCTTGCGCCACAAATGACATGGAAAAAACGCCCGCAAAATCGACCGCACTTTCCCGCTATAACGAAAACGACGTCCGCCTCATTACCACCCCCGGTCACACCGTCTCATCCTGAGTTATATAATTTGATCGGTTATAATCCGATAAGCGCGGATAACTTATCAACCACCCTTAATTTGTCTATTGATCAAATTCTCATTCAACTGTTGGAACTGGAATTACAGGATTTAATTATCAGTGAGAACGGGTTATATCGGCGGGTT","","","41623","MNKHLALLLRLLQIPKLGPTTIHKILAQINLFELQYYDAAAFTQMGWNAQQIQAWFHPEQRYIEPALLWGEKEGNHILDYFHPDYPELLKQIESAPPVLFVKGATSALSQQQIAIVGSRQCSSYGEYWAKYFATELTTNGFIITSGLALGIDGFCHQAVVDLKQPTIAVLGSGLEEVYPAKHLKLAQNIIEHGGALVSEFFPLQPPIAENFPRRNRIISGLSLATLIIEATERSGSLITARYALEQKREIFALPGNIQSQFSQGCHKLIKQGAMLVENVEDILENLAPQMTWKKRPQNRPHFPAITKTTSASLPPPVTPSHPELYNLIGYNPISADNLSTTLNLSIDQILIQLLELELQDLIISENGLYRRV","934311","","DNA processing chain A","Cytoplasm","","
InterPro
IPR003488
Family
SMF protein
PF02481\"[69-277]TSMF
TIGR00732\"[67-286]TdprA: DNA protecting protein DprA
noIPR
unintegrated
unintegrated
signalp\"[1-19]?signal-peptide


","BeTs to 15 clades of COG0758COG name: Predicted Rossmann fold nucleotide-binding protein involved in DNA uptakeFunctional Class: L,NThe phylogenetic pattern of COG0758 is -------qvdrlbcefghsnuj--t-Number of proteins in this genome belonging to this COG is","","Residues 227 to 286 match (3e-07) PD:PD394808 which is described as COMPLETE PROTEOME AQ_1191 PROCESSING DNA SMF ","","","","","","","","","","","","Thu Jan 9 14:07:37 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01383 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 69 to 277 (E-value = 2.6e-107) place AA01383 in the SMF family which is described as SMF family (PF02481)","","","","","Smeets LC, Bijlsma JJ, Kuipers EJ, Vandenbroucke-Grauls CM, Kusters JG. The dprA gene is required for natural transformation of Helicobacter pylori. FEMS Immunol Med Microbiol. 2000 Feb;27(2):99-102. PMID: 10640603 Ando T, Israel DA, Kusugami K, Blaser MJ. HP0333, a member of the dprA family, is involved in natural transformation in Helicobacter pylori. J Bacteriol. 1999 Sep;181(18):5572-80. PMID: 10482496","","Thu Jan 9 14:07:37 2003","1","","","" "AA01384","935600","935460","141","TTGCCGAGGAAAGTGCGGTCGTTTTATAGCGCGTTTTTAATCCTCATATCACCACCGATATTTCTTTCTATTTTTTTACTAAATTACGATCCGGATCACAAATTCCACCTTTATTTCTTCAGTTTCTTTTTTCTCTGCCTA","","","5717","LPRKVRSFYSAFLILISPPIFLSIFLLNYDPDHKFHLYFFSFFFLCL","935460","","hypothetical protein","Cytoplasm","No sequence similarities are found to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-23]?signal-peptide
tmhmm\"[9-29]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 09:52:36 2004","Thu Feb 26 09:52:36 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01384 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:52:36 2004","","","","","","","","","","","","","1","","","" "AA01385","936095","935649","447","ATGCAAGTAATTCTTTTAGATAAAATTGCACACTTAGGTAAAGTGGGCGATCAAGTAAATGTTAAATCCGGTTATGCCCGTAACTACTTAATCCCACAAGGAAAAGCGGTTATGGCAACCAAAGCTAACATTGAACACTTCGAAGCACGTCGTGCCGAATTAGAAGAAAAAGCAGCCAAAGTATTAGCCGCCGCTGTTGACCGCGCAGAACGTTTAGAAGCCTTAGGTTCCGTAACCATCGCCTCTAAAGCCGGTGATGAAGGTCGTTTATTCGGTTCTATCGGTACCCGCGACATCGCTGATGCAATCACTGCAAAAGGCGTTGAAGTGGCGAAAAGTGAAGTTCGTTTACCAAACGGTTTAATCCGTACTTTAGGCGAACATGAAGTAACTTTCCAATTCCATGGCGAAGTTCTCTCTCACTTAAACGTGATTATCGTTGCCGAA","","","16007","MQVILLDKIAHLGKVGDQVNVKSGYARNYLIPQGKAVMATKANIEHFEARRAELEEKAAKVLAAAVDRAERLEALGSVTIASKAGDEGRLFGSIGTRDIADAITAKGVEVAKSEVRLPNGLIRTLGEHEVTFQFHGEVLSHLNVIIVAE","935649","","50S ribosomal protein L9","Cytoplasm","","
InterPro
IPR000244
Family
Ribosomal protein L9
PTHR21368\"[1-149]T50S RIBOSOMAL PROTEIN L9
PF01281\"[1-48]TRibosomal_L9_N
PF03948\"[62-149]TRibosomal_L9_C
TIGR00158\"[1-149]TL9: ribosomal protein L9
PS00651\"[13-40]TRIBOSOMAL_L9
noIPR
unintegrated
unintegrated
G3DSA:3.10.430.100\"[60-146]Tno description
G3DSA:3.40.5.10\"[1-59]Tno description
PTHR21368:SF17\"[1-149]T50S RIBOSOMAL PROTEIN L9


","BeTs to 18 clades of COG0359COG name: Ribosomal protein L9Functional Class: JThe phylogenetic pattern of COG0359 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 4.1e-40) to 3/3 blocks of the IPB000244 family, which is described as \"Ribosomal protein L9\". Interpro entry for IP:IPR000244. IPB000244A 1-31 3.6e-22 IPB000244B 85-99 4.8e-07 IPB000244C 122-146 5.7e-08","Residues 1 to 47 match (3e-07) PD:PD460289 which is described as RIBOSOMAL 50S PROTEOME L9 COMPLETE RRNA-BINDING ","","","","","","","","","","","","Thu Jan 9 14:09:25 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01385 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 62 to 149 (E-value = 1.4e-37) place AA01385 in the Ribosomal_L9_C family which is described as Ribosomal protein L9, C-terminal domain (PF03948)","","","","","amp,R.M. and Wittmann-Liebold,B. The primary structure of protein L9 from the Escherichia coli ribosome FEBS Lett. 149, 313-319 (1982) Arnold,R.J. and Reilly,J.P. Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry Analytical biochemistry. 269 (1), 105-112 (1999) PubMed: 10094780 ","","Thu Jan 9 14:09:25 2003","1","","","" "AA01386","936341","936114","228","ATGGCACGTTATTTCCGTCGTCGTAAGTTCTGCCGTTTTACAGCGGAAAATGTTGTTGAAATCGATTACAAAGATATCGCTACATTAAAGAACTACATTTCAGAAAGCGGCAAAATTGTACCAAGCCGCATTACCGGTACTCGTGCGAAGTACCAACGCCAATTAGCCCGCGCAATCAAACGCGCACGTTATTTAGCGTTATTACCTTACTCTGACACGCATCATCAC","","","9044","MARYFRRRKFCRFTAENVVEIDYKDIATLKNYISESGKIVPSRITGTRAKYQRQLARAIKRARYLALLPYSDTHHH","936114","","30S ribosomal protein S1","Cytoplasm, Extracellular","","
InterPro
IPR001648
Family
Ribosomal protein S18
PD002239\"[21-72]TRS18_HAEIN_P44384;
PR00974\"[28-38]T\"[38-45]T\"[46-60]T\"[60-70]TRIBOSOMALS18
G3DSA:4.10.640.10\"[4-70]Tno description
PTHR13479\"[3-75]T30S RIBOSOMAL PROTEIN S18
PF01084\"[15-68]TRibosomal_S18
TIGR00165\"[4-73]TS18: ribosomal protein S18
PS00057\"[21-44]TRIBOSOMAL_S18
noIPR
unintegrated
unintegrated
PTHR13479:SF16\"[3-75]T30S RIBOSOMAL PROTEIN S18
signalp\"[1-2]?signal-peptide


","BeTs to 19 clades of COG0238COG name: Ribosomal protein S18Functional Class: JThe phylogenetic pattern of COG0238 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.5e-29) to 1/1 blocks of the IPB001648 family, which is described as \"Ribosomal protein S18\". Interpro entry for IP:IPR001648. IPB001648 28-70 2.1e-29","Residues 6 to 70 match (1e-08) PD:PD027370 which is described as RIBOSOMAL RNA-BINDING PROTEOME 30S COMPLETE S18 ","","","","","","","","","","","","Thu Jan 9 14:11:34 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01386 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 15 to 68 (E-value = 1.8e-31) place AA01386 in the Ribosomal_S18 family which is described as Ribosomal protein S18 (PF01084)","","","","","Schnier,J., Kitakawa,M. and Isono,K. The nucleotide sequence of an Escherichia coli chromosomalregion containing the genes for ribosomal proteins S6, S18, L9 andan open reading frame Mol. Gen. Genet. 204 (1), 126-132 (1986) PubMed: 3528756 Yaguchi,M. Primary structure of protein S18 from the small Escherichiacoli ribosomal subunit FEBS Lett. 59 (2), 217-220 (1975) PubMed: 776663 Urlaub,H., Kruft,V., Bischof,O., Muller,E.C. and Wittmann-Liebold,B. Protein-rRNA binding features and their structural andfunctional implications in ribosomes as determined by cross-linking studies EMBO J. 14 (18), 4578-4588 (1995) PubMed: 7556101 ","","Thu Jan 9 14:11:34 2003","1","","","" "AA01387","936701","936357","345","TTGAATCCAACGATTTTGAGGATGCTGAAGAGTAATTTAAACATTGATAACCGTTTATCCATTATCGGTATCGTTGCCGGTAATCTTAAACGACGCAAAAGTCCGAGCGGAATCGAACATTGCCAATTTTTATTGGAACATCGTTCAAACCGGGTAGAAGCGAATTTAACGCGGCAAGCCTGGTGCAAAATTCCGGTTCAGGTGAGCGGCAATCAATTAGTAGAAAAAACTCAAGGCATTACGGTCGGCAGTAAAGTATTAATTCAAGGTTTTTTAACCACCCATCAGTTAAATAATGGGTCAGTACAATTAGTTTTACACGCCGAGCAAATCGAATTTATAGAT","","","12846","LNPTILRMLKSNLNIDNRLSIIGIVAGNLKRRKSPSGIEHCQFLLEHRSNRVEANLTRQAWCKIPVQVSGNQLVEKTQGITVGSKVLIQGFLTTHQLNNGSVQLVLHAEQIEFID","936357","","primosomal protein N","Cytoplasm","","
InterPro
IPR000424
Family
Single-strand binding protein/Primosomal replication protein n
PF00436\"[16-114]TSSB
PS50935\"[15-115]TSSB
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[12-114]Tno description


","BeTs to 4 clades of COG2965COG name: Primosomal replication protein NFunctional Class: LThe phylogenetic pattern of COG2965 is --------------e-gh-n------Number of proteins in this genome belonging to this COG is","Significant hit ( 2e-06) to 3/3 blocks of the IPB000424 family, which is described as \"Single-strand binding protein family\". Interpro entry for IP:IPR000424. IPB000424A 16-54 0.0054 IPB000424B 78-100 1.8 IPB000424C 107-113 70","Residues 22 to 115 match (9e-32) PD:PD029409 which is described as COMPLETE PROTEOME REPLICATION N PRIMOSOMAL PRIMOSOME PRIB ","","","","","","","","","","","","Thu Jan 9 14:22:02 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01387 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 16 to 115 (E-value = 4.2e-25) place AA01387 in the SSB family which is described as Single-strand binding protein family (PF00436)","","","","","Yamazaki T, Yasuda T, Miyazaki Y, Okada K, Kajiwara S, Shishido K.A promoter activity in Saccharomyces cerevisiae of the 39-noncoding region of the basidiomycetous mushroom gene.J Gen Appl Microbiol. 2002 Aug;48(4):223-31.PMID: 12469321 Flores MJ, Ehrlich SD, Michel B.Primosome assembly requirement for replication restart in the Escherichia coli holDG10 replication mutant.Mol Microbiol. 2002 May;44(3):783-92.PMID: 11994158 Sandler SJ, McCool JD, Do TT, Johansen RU.PriA mutations that affect PriA-PriC function during replication restart.Mol Microbiol. 2001 Aug;41(3):697-704.PMID: 11532137Zavitz KH, DiGate RJ, Marians KJ.The priB and priC replication proteins of Escherichia coli. Genes, DNA sequence, overexpression, and purification.J Biol Chem. 1991 Jul 25;266(21):13988-95.PMID: 1856227 ","","Thu Jan 9 14:22:02 2003","1","","","" "AA01388","937044","936670","375","ATGCGTCACTACGAAATCGTGTTTATGGTTCATCCGGACCAAAGCGAGCAAGTACCGGGCATGATTGAACGTTACACCGGTTCTGTAAAAGAAGCCGGCGGTCAAGTTCATCGCCTAGAAGATTGGGGTCGCCGTCAATTAGCATACCCAATTAACAAATTACATAAAGCACACTATGTGCTTATGAATGTAGAAGCGCCTCAACAAGTAATCGACGAGCTAGAAAAGACTTTCCGTTATAACGATGCTGTGTTGCGCAGCCTTGTTATTCACACTAAGCACGCCGTAACCGAAGCGTCCCCAATGGTTAAAGCAAAAGACGATCGTAAAGCTTTAACTGAAGTTGAATCCAACGATTTTGAGGATGCTGAAGAG","","","14472","MRHYEIVFMVHPDQSEQVPGMIERYTGSVKEAGGQVHRLEDWGRRQLAYPINKLHKAHYVLMNVEAPQQVIDELEKTFRYNDAVLRSLVIHTKHAVTEASPMVKAKDDRKALTEVESNDFEDAEE","936670","","30S ribosomal protein S6","Cytoplasm","","
InterPro
IPR000529
Family
Ribosomal protein S6
PD003809\"[40-86]TRS6_HAEIN_P44375;
PF01250\"[2-92]TRibosomal_S6
TIGR00166\"[1-94]TS6: ribosomal protein S6
PS01048\"[43-52]TRIBOSOMAL_S6
InterPro
IPR014717
Domain
Translation elongation factor EF1B/ribosomal protein S6, conserved
G3DSA:3.30.70.60\"[2-104]Tno description


","No hits to the COGs database.","Significant hit ( 3.3e-21) to 2/2 blocks of the IPB000529 family, which is described as \"Ribosomal protein S6\". Interpro entry for IP:IPR000529. IPB000529A 4-17 3.3e-07 IPB000529B 43-59 2.2e-12","Residues 92 to 125 match (3e-08) PD:PD065614 which is described as RIBOSOMAL 30S PROTEOME S6 COMPLETE RRNA-BINDING ","","","","","","","","","","","","Thu Jan 9 14:23:49 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01388 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 92 (E-value = 5.3e-50) place AA01388 in the Ribosomal_S6 family which is described as Ribosomal protein S6 (PF01250)","","","","","Kang,W.K., Icho,T., Isono,S., Kitakawa,M. and Isono,K. Characterization of the gene rimK responsible for the addition of glutamic acid residues to the C-terminus of ribosomal protein S6 in Escherichia coli K12 Molecular & general genetics : MGG. 217 (2-3), 281-288(1989) PubMed: 2570347","","Thu Jan 9 14:23:49 2003","1","","","" "AA01389","937096","937218","123","TTGTGGAAGCAAGGAACTAATTCGGATGTGACTGAGGGCGCAAATTATACACTGAATCAGGGCGTTTGCAATAAAAGTGCGGTGGATTTTTCCGATGTTTTTACATCCACGCGTTATTGCGAA","","","4532","LWKQGTNSDVTEGANYTLNQGVCNKSAVDFSDVFTSTRYCE","937218","","hypothetical protein","Cytoplasm, Extracellular","No sequence similarities are found to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 09:54:09 2004","Thu Feb 26 09:54:09 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01389 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:54:09 2004","","","","","","","","","","","","","1","","","" "AA01390","937819","937199","621","ATGAAACCACTTACAGCACGACAACAAGAAGTCTATGATTTTCTTAAACACCATCTTGAAACCACCGGTATGCCGCCAACCCGTGCGGAAATTTCCAAAGAGCTGGGATTCCGCTCTCCTAATGCGGCAGAAGAACACCTAAAAGCCCTGGCAAAAAAAGGCGTCATTGAAATCGTTTCCGGCACCTCGCGCGGCATTCGTTTATTGCTGGAAGATCATTCACAAGAAGAAGCCGGTTTGCCATTAATCGGACGCGTTGCAGCGGGTGAACCGATTTTAGCCGAACAGCATATTGAGGGCACTTATCATGTGGATCCCAATATGTTTAAACCGCAAGCAGATTTCCTGCTGAAAGTGTATGGTCAATCCATGAAAGATGTCGGCATTCTGGACGGTGACTTGTTGGCGGTGCACAGCACCAAAGACGTGCGTAACGGGCAAATTGTGGTAGCGCGCATTGAAGATGAAGTGACGGTAAAACGTTTGGAACGTAAAGGTTCCGTGGTTTATTTGCACGCAGAAAACGAAGAATTTTCCCCGATTGTCGTGGATCTCACCCAACCGACGCATTTTGAAATTGAGGGCATTGCCGTGGGGATTATTCGCAATAACGCGTGGATG","","","23004","MKPLTARQQEVYDFLKHHLETTGMPPTRAEISKELGFRSPNAAEEHLKALAKKGVIEIVSGTSRGIRLLLEDHSQEEAGLPLIGRVAAGEPILAEQHIEGTYHVDPNMFKPQADFLLKVYGQSMKDVGILDGDLLAVHSTKDVRNGQIVVARIEDEVTVKRLERKGSVVYLHAENEEFSPIVVDLTQPTHFEIEGIAVGIIRNNAWM","937199","From HD0545: This protein represses a number of genes involved in the response to DNA damage (SOS damage), including RECA andLEXA.It has been shown to bind to the 16 bp palindromic sequence 5\"-CTGT-AT(4)-ACAG-3\".In the presence of single-stranded DNA,RECA interacts with LEXA causing an autocatalytic cleavage which disrupts the DNA-binding part of LEXA,leading to derepression of the SOS regulon and eventually DNA repair.","LexA repressor","Cytoplasm","","
InterPro
IPR006197
Family
Peptidase S24, LexA/MucA/RumA/RuvA
PR00726\"[115-125]T\"[126-137]T\"[154-166]TLEXASERPTASE
InterPro
IPR006198
Domain
Peptidase S24, S26A and S26B
PF00717\"[118-186]TPeptidase_S24
InterPro
IPR006199
Domain
LexA DNA-binding region
PF01726\"[1-65]TLexA_DNA_bind
InterPro
IPR006200
Family
Peptidase S24, LexA repressor
TIGR00498\"[1-206]TlexA: LexA repressor
InterPro
IPR011056
Domain
Peptidase S24 and S26, C-terminal region
G3DSA:2.10.109.10\"[84-207]Tno description
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[1-70]Tno description


","BeTs to 10 clades of COG1974COG name: SOS-response transcriptional repressors (RecA-mediated autopeptidases)Functional Class: K,TThe phylogenetic pattern of COG1974 is --------vdrlbcefghs--j----Number of proteins in this genome belonging to this COG is","Significant hit ( 5.9e-90) to 4/4 blocks of the IPB002865 family, which is described as \"LexA DNA binding domain\". Interpro entry for IP:IPR002865. IPB002865A 4-54 2.5e-35 IPB002865B 80-94 8.1e-11 IPB002865C 115-161 1.9e-36 IPB002865D 193-202 0.0012Significant hit ( 2.9e-17) to 3/3 blocks of the PR00726 family, which is described as \"Repressor LexA serine protease (S24) family signature\". Prints database entry for PR:PR00726. PR00726A 115-125 0.00087 PR00726B 126-137 7.4e-05 PR00726C 154-166 4.8e-05","Residues 2 to 72 match (2e-21) PD:PD004865 which is described as REPRESSOR DNA LEXA SOS HYDROLASE TRANSCRIPTION REGULATION PROTEOME COMPLETE REPLICATION ","","","","","","","","","","","Thu Jan 9 14:31:58 2003","Thu Jan 9 14:31:58 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01390 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 79 to 187 (E-value = 4.3e-55) place AA01390 in the Peptidase_S24 family which is described as Peptidase family S24 (PF00717)","","","","","Bunny K, Liu J, Roth J. Phenotypes of lexA Mutations in Salmonella enterica: Evidencefor a Lethal lexA Null Phenotype Due to the Fels-2 Prophage. J Bacteriol. 2002 Nov;184(22):6235-49. PMID: 12399494 Knegtel,R.M., Fogh,R.H., Ottleben,G., Ruterjans,H.,Dumoulin,P., Schnarr,M., Boelens,R. and Kaptein,R. A model for the LexA repressor DNA complex Proteins. 21 (3), 226-236 (1995) PubMed: 7784426 Lamerichs,R.M., Padilla,A., Boelens,R., Kaptein,R.,Ottleben,G., Ruterjans,H., Granger-Schnarr,M., Oertel,P. and Schnarr,M. The amino-terminal domain of LexA repressor is alpha-helical but differs from canonical helix-turn-helix proteins: a two-dimensional 1H NMR study Proceedings of the National Academy of Sciences of the United States of America. 86 (18), 6863-6867 (1989) PubMed: 2780544 Miki,T., Ebina,Y., Kishi,F. and Nakazawa,A. Organization of the lexA gene of Escherichia coli andnucleotide sequence of the regulatory region Nucleic acids research. 9 (3), 529-543 (1981) PubMed: 6261224 ","","Thu Jan 9 14:31:58 2003","1","","","" "AA01391","938027","940462","2436","ATGGCTGCTTTTCTGAATGCTTATCGAAAATTGCTTGAGTTGCCGTTATCGATCTTAGTAAAGAACAATCCGATTCCCCATAATCCCATTGAAGAATTGGAACTGAATACCTCCCAACCTATCGTTTATGTCTTGCCTTACACCTCTGAAACCGACTTTTTGATTTTCCGAAAAAATTGTTTAAGTATAGGATTGCCGGATCCGTTAGAGCAAAATGAAATCAACGGCAATTTCTTACCGCGCTTTGTGTTTCTGGATGAAGGTCGACGCTTTTTTAAATCCAAAGGCGCGAAAAAAGAAACTACGGCGATTTTCAATAAATACCTGGAATTGCACCGCACTTCTCCTCAGTTAGATGTGCAACTGATCCCTGTTTCCGTGTTGTGGGGGCGTGCACCGGGGCGTGAAGATAAATCGGGCCTGCCGAATTTACGTTTGTTAAACGGGCTGCAAAAAACCATTGCCGCCTTATGGTTCGGGCGGGACACCTTCGTGCGTTTTTCACAGGCGGTATCGTTACGTTATATGGCGCGTGAACATGGTTTTGACCAGAAAATCGCACAAAAATTAGCCCGCGTAGCAAAAATGCACTTTGCCAAACAGCGTATCTCCGCCACGGGCCCGCGCCTGCCGAATCGTCAGGCAATGTTTAATAAATTATTACAACAGCCGGTGATTCTAGCCGCTATTGAAGACGAGGCGAAAAGCAAAAGTATCAGCGTGGAGAAAGCGCGCAAAGAAGCGGAAAAAATTCTTGATGAAATTGCCGCAAACGTCAGTTACGAAGGTTTGCGCGTGGCAGATCGTTTCCTACGTTGGTTGTGGAATAAATTGTATCAGGGCATCGAAGTGGAAAATGCCGATCGTGTGCGTAAACTGGCGTTGGAAGGACATGAAATCGTCTATGTGCCTTGCCATCGCAGCCATATCGACTATTTATTGCTTTCCTATGTTTTGTACCATCAAGGCTTAGTGCCACCTCATATCGCCGCAGGGATTAACCTGAATTTCTGGCCGGTGGGCGGTATGTTCCGCCGTGGCGGGGCGTTTTTTATCCGTCGCACGTTTAAAGGCAATCGTCTGTATTCCACCATTTTCCGCGAATATCTGGCGGAATTGTTCTATCGCGGTTATTCCGTGGAATATTTTATTGAGGGCGGACGTTCCCGTACCGGTAGATTGCTTGCACCGAAAACCGGCATGATGTCCATGACCTTACAGGCGTTACAACAGCAACAAAGCCGTTCGATTACCGTTGTGCCGGTGTATGTGGGTTATGAACACGTGTTGGAAGTAGATACTTACGCGAAAGAATTGCGTGGTGCAGCAAAAGAAAAAGAGAATGCCGGCTTGGTACTGCGCGTGATTAAAAAATTGCGCAACTTAGGCAAAGGCTATGTGAACTTCGGCGAGCCGATTACTTTGAGCAACTATTTAAATCAGCATTTCCCGGAATGGAAAGAGCCTTTGGAAGACCGTCCGCAATGGTTTAACAAAGCGGTAGATGCCGTTTCCAATCAGGTGATGGTGAATATTAACAAAGCCGCCGCCGTGAACGCCATGAACTTAACCGGCACGGCGTTATTGTCCTCCCGCCAACGTGCCTTATCCCGCGAGCAACTGTTGGAGCAACTTTCCAGTTATCAACAATTCCTGCAAAACGTGCCTTATTCCAATGATGTGGTGGTGCCGACGGAAAAAGCGGAAATCATGCTCGACCATGTGTTAAGCTTGGATCGCGTGGGCATTTTGCCGGAAAAAGACAATTTCGGCGAAATCGTTCGTTTAGAGCGTTCTTCTGCGGTGTTGATGACCTATTACCGCAACAATATTCAGCATTTATTTGTACTGCCGTCGCTTGTGGCTAATATCGTGCTGCATTATGAAGCCATTCAGAAAAATTTGGTGTTAGTAGCAATGCTGAAAATTTATCCATTCCTGCGTAGCGAACTGTTCCTGCATTTTACCCAAGAACAGCTGGCGGAACGGGTAGAGCACATTATTGCCGAATTACAACGTCAAAATATCATCAAGTGCAGTGAAAATATGTTGGCGATTAATAAACCAAACATTCGGATGTTGCAACTTTGGTCGGCAGGTGTACGTGAAATCCTACAGCGTTATTACATCACCGTGAATTTACTGCAAAATAACCCATTGATTTCCCGTGTGAATCTGGAAAAAGAAAGTCAATCTGTGGCACAACGCCTTTCCGTCCTACACGGCATTAATGCGCCGGAATTTTTTGATAAAGCCGTTTTCTCTGCGTTTACCAACAGCTTGAAAGAACAGGGTTATTTCAACGAAAGCGGCACCGCTAACACGGAAAAATTACAGGAATTGGCGGACATTCTCACTCATCTCATTTCCACCGAAATTTGCTTAACCATCAACGGCGCCGTGACCAAAGCGGAAGAAAAGGAGCACGAGGAAAAT","","","92968","MAAFLNAYRKLLELPLSILVKNNPIPHNPIEELELNTSQPIVYVLPYTSETDFLIFRKNCLSIGLPDPLEQNEINGNFLPRFVFLDEGRRFFKSKGAKKETTAIFNKYLELHRTSPQLDVQLIPVSVLWGRAPGREDKSGLPNLRLLNGLQKTIAALWFGRDTFVRFSQAVSLRYMAREHGFDQKIAQKLARVAKMHFAKQRISATGPRLPNRQAMFNKLLQQPVILAAIEDEAKSKSISVEKARKEAEKILDEIAANVSYEGLRVADRFLRWLWNKLYQGIEVENADRVRKLALEGHEIVYVPCHRSHIDYLLLSYVLYHQGLVPPHIAAGINLNFWPVGGMFRRGGAFFIRRTFKGNRLYSTIFREYLAELFYRGYSVEYFIEGGRSRTGRLLAPKTGMMSMTLQALQQQQSRSITVVPVYVGYEHVLEVDTYAKELRGAAKEKENAGLVLRVIKKLRNLGKGYVNFGEPITLSNYLNQHFPEWKEPLEDRPQWFNKAVDAVSNQVMVNINKAAAVNAMNLTGTALLSSRQRALSREQLLEQLSSYQQFLQNVPYSNDVVVPTEKAEIMLDHVLSLDRVGILPEKDNFGEIVRLERSSAVLMTYYRNNIQHLFVLPSLVANIVLHYEAIQKNLVLVAMLKIYPFLRSELFLHFTQEQLAERVEHIIAELQRQNIIKCSENMLAINKPNIRMLQLWSAGVREILQRYYITVNLLQNNPLISRVNLEKESQSVAQRLSVLHGINAPEFFDKAVFSAFTNSLKEQGYFNESGTANTEKLQELADILTHLISTEICLTINGAVTKAEEKEHEEN","940462","","glycerol-3-phosphate acyltransferase","Inner membrane, Cytoplasm","","
InterPro
IPR002123
Domain
Phospholipid/glycerol acyltransferase
PF01553\"[281-425]TAcyltransferase
SM00563\"[300-427]TPlsC
InterPro
IPR012082
Family
Glycerol-3-phosphate O-acyltransferase/dihydroxyacetone phosphate acyltransferase
PIRSF000437\"[1-809]TGlycerol-3-phosphate O-acyltransferase/dihydroxyacetone phosphate acyltransferase
InterPro
IPR012124
Family
Glycerol-3-phosphate acyltransferase
PIRSF500064\"[2-809]TGlycerol-3-phosphate acyltransferase
noIPR
unintegrated
unintegrated
PTHR12563\"[214-543]TGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE
PTHR12563:SF3\"[214-543]TDIHYDROXYACETONE PHOSPHATE ACYLTRANSFERASE


","No hits to the COGs database.","","Residues 264 to 299 match (6e-13) PD:PD584611 which is described as ACYLTRANSFERASE GLYCEROL-3-PHOSPHATE PHOSPHOLIPID PROTEOME COMPLETE GPAT MEMBRANE TRANSFERASE BIOSYNTHESIS ","","","","","","","","","","","","Thu Jan 9 14:34:58 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01391 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 281 to 425 (E-value = 7.8e-40) place AA01391 in the Acyltransferase family which is described as Acyltransferase (PF01553)","","","","","Heath,R.J. and Rock,C.O. A missense mutation accounts for the defect in the glycerol-3-phosphate acyltransferase expressed in the plsB26 mutant J. Bacteriol. 181 (6), 1944-1946 (1999) PubMed: 10074094 Green,P.R., Vanaman,T.C., Modrich,P. and Bell,R.M. Partial NH2- and COOH-terminal sequence and cyanogen bromide peptide analysis of Escherichia coli sn-glycerol-3-phosphate acyltransferase J. Biol. Chem. 258 (18), 10862-10866 (1983) PubMed: 6350296 Lewin TM, Wang P, Coleman RA. Analysis of amino acid motifs diagnostic for the sn-glycerol-3-phosphate acyltransferase reaction. Biochemistry. 1999 May 4;38(18):5764-71. PMID: 10231527 ","","Thu Jan 9 14:34:58 2003","1","","","" "AA01393","942089","940509","1581","ATGGGAATGGCGGGCTTGCTGATCCTCAGCATTCTCTCGCTGTTTTTAGCCACTGCCGTGCGCCTGCAAACCCTACAGGGAGTATTTCCGATGCGCTTGCGTTGGAATTTCCACCGCTTAATGTTGGGACAGAGTCTGAGTTTCTATCAGGATGAATTTGCCGGACGGGTGTCTGCCAAAGTGATGCAAACTGCCCTTGCCGTACGCGATACTGTGCTGACCATCGCTGATGTTTTAGTGTATGTAGTAGTGTATTTCGTCACATCAGGTCTGGTTCTTGCTTCATTAGATAGTTGGTTCCTCCTGCCTTTTATCGTCTGGATTGTGTTGTTTGTCACGATTTTGCGTTTATTGATCCCGCGCCTTGCCAAAACAGCAGAACGGCAGGCAGATGCGCGCTCGCTTATGACCGGACGCATCACCGACGCGTATTCTAACATTGCCACGGTGAAACTGTTCTCCCACGGTTCCCGTGAAGCAGGTTATGCCAAGCGTTCTATGGAAGAATTTATGGTAACGGTACACGACCAGATGCGTTTGGCGACCTCGCTGGATACCTTGACCTATATTACCAATGTGATGCTTATTTTAAGTACCGCCGTCATCGGCGTATTGTTATGGCAACAAGGGCTGGTGGGTGTCGGTGCCATTGCCACCGCTACTGCCATGGCGTTGCGCGTACATGGACTATCACGCTGGATTATGTGGGAGTCTGCACGCCTGTTTGAAAATATCGGTACGGTGAATGACGGTATGAATACATTAACCAAACAGCAAACCATTTTGGATAAACCGAATTGTCCGTCGTTAAAGGTTACCCATGGTGAAATTAAATTCGACGACGTGAGCTTTGCCTATGATCCGGTTAAACCGTTGTTGACGCACTTTAATTTAACCATTAAACCGGGCGAAAAAGTGGGCTTAATCGGACGTTCCGGCGCCGGTAAATCCACCATCGTCAATCTATTGTTGCGTTTCTATGAAGCGCAGCAGGGTGCTATTACCATTGATGGGCAAAATATCATCGACGTGCAACAGGAAAGTTTGCGCAGTCAAATTGGCTTGGTGACGCAGGATACGTCATTGTTGCACCGTTCCGTGCGCGATAATATTGTGTACGGCAGACCAACCGCCACCGAGCAGGAAATGTTGGATGCCGCGGAACGCGCTGAAGCGGCGTATTTTATCCCGTATCTAAGCGACGCACAGGGACGTCACGGCTATGATGCTCATGTGGGCGAGCGTGGGGTGAAATTGTCCGGCGGACAACGTCAACGTATCGCCATCGCCCGCGTGATGCTCAAAGACGCACCGATTTTGTTGTTGGACGAAGCCACCAGCGCGCTGGATTCCGAAGTGGAGGCGGCAATTCAGGAAAGTCTGGATAAAATGATGGAAAATAAAACCGTGATTGCCATCGCTCACCGTTTGTCCACCATCGCCGCCATGGATCGTCTGATTGTGCTGGATCACGGACAAATCGTGGAACAGGGCACCCACGCCGAACTGCTGGCACAAAATGGCTTATACGCCAAATTATGGCAACACCAAAGCGGCGGCTTCCTGAGTGAGCACGTGGAT","","","68303","MGMAGLLILSILSLFLATAVRLQTLQGVFPMRLRWNFHRLMLGQSLSFYQDEFAGRVSAKVMQTALAVRDTVLTIADVLVYVVVYFVTSGLVLASLDSWFLLPFIVWIVLFVTILRLLIPRLAKTAERQADARSLMTGRITDAYSNIATVKLFSHGSREAGYAKRSMEEFMVTVHDQMRLATSLDTLTYITNVMLILSTAVIGVLLWQQGLVGVGAIATATAMALRVHGLSRWIMWESARLFENIGTVNDGMNTLTKQQTILDKPNCPSLKVTHGEIKFDDVSFAYDPVKPLLTHFNLTIKPGEKVGLIGRSGAGKSTIVNLLLRFYEAQQGAITIDGQNIIDVQQESLRSQIGLVTQDTSLLHRSVRDNIVYGRPTATEQEMLDAAERAEAAYFIPYLSDAQGRHGYDAHVGERGVKLSGGQRQRIAIARVMLKDAPILLLDEATSALDSEVEAAIQESLDKMMENKTVIAIAHRLSTIAAMDRLIVLDHGQIVEQGTHAELLAQNGLYAKLWQHQSGGFLSEHVD","940509","","ABC transporter, ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[419-461]TQ9K1A3_NEIMB_Q9K1A3;
PF00005\"[303-492]TABC_tran
PS50893\"[277-516]TABC_TRANSPORTER_2
PS00211\"[419-433]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[302-499]TAAA
InterPro
IPR011527
Domain
ABC transporter, transmembrane region, type 1
PS50929\"[1-236]TABC_TM1F
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[242-517]Tno description
PTHR19242\"[1-527]TATP-BINDING CASSETTE TRANSPORTER
PTHR19242:SF91\"[1-527]TLIPID A EXPORT ATP-BINDING/PERMEASE PROTEIN MSBA
signalp\"[1-19]?signal-peptide
tmhmm\"[10-30]?\"[72-94]?\"[100-120]?\"[186-206]?\"[212-230]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.4e-69) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 292-338 4.2e-26 IPB001140B 416-454 2.3e-24 IPB001140C 469-498 1.2e-16","Residues 462 to 498 match (9e-09) PD:PD375591 which is described as ATP-BINDING ABC COMPLETE PROTEOME TRANSPORTER TRANSMEMBRANE MULTIDRUG RESISTANCE P-GLYCOPROTEIN GLYCOPROTEIN ","","","","","","","","","","","","Thu Jan 9 14:38:05 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01393 is paralogously related to AA02805 (4e-62), AA01961 (3e-56), AA01510 (3e-45), AA01509 (8e-44), AA02609 (4e-40), AA02606 (4e-39), AA01867 (1e-25), AA02331 (7e-25), AA02718 (1e-21), AA00415 (6e-21), AA00700 (1e-19), AA01524 (7e-19), AA01645 (9e-19), AA01422 (2e-18), AA02353 (2e-18), AA01656 (6e-18), AA01824 (2e-17), AA02440 (3e-17), AA02080 (5e-17), AA00858 (1e-16), AA00799 (4e-16), AA01779 (6e-16), AA02786 (9e-16), AA02899 (4e-15), AA01616 (6e-15), AA02320 (8e-15), AA01684 (1e-14), AA02898 (4e-14), AA00207 (4e-14), AA01051 (2e-13), AA02484 (3e-13), AA02573 (6e-13), AA02140 (1e-12), AA00751 (1e-12), AA00591 (2e-12), AA02152 (3e-12), AA02550 (2e-11), AA01555 (1e-10), AA01947 (6e-10), AA00933 (1e-09), AA01820 (2e-09), AA01568 (3e-09), AA02324 (7e-09), AA01456 (7e-09), AA02225 (4e-08), A02145 (2e-07), AA01757 (2e-07), AA00061 (2e-07), AA02642 (1e-05), AA01569 (2e-05), AA00934 (4e-05), AA01291 (5e-04) and AA02146 (8e-04).","","","","","","Residues 303 to 492 (E-value = 1.1e-57) place AA01393 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","Guthmiller JM, Kolodrubetz D, Kraig E. Mutational analysis of the putative leukotoxin transport genes inActinobacillus actinomycetemcomitans. Microb Pathog. 1995 May;18(5):307-21. PMID: 7476096 Spitznagel J Jr, Kraig E, Kolodrubetz D. Regulation of leukotoxin in leukotoxic and nonleukotoxic strains of Actinobacillus actinomycetemcomitans. Infect Immun. 1991 Apr;59(4):1394-401. PMID: 2004819 Guthmiller JM, Kolodrubetz D, Cagle MP, Kraig E. Sequence of the lktB gene from Actinobacillus actinomycetemcomitans. Nucleic Acids Res. 1990 Sep 11;18(17):5291. No abstract available. PMID: 2402457","Davies RL, Campbell S, Whittam TS. Mosaic structure and molecular evolution of the leukotoxin operon (lktCABD) in Mannheimia (Pasteurella) haemolytica, Mannheimia glucosida, and Pasteurella trehalosi. J Bacteriol. 2002 Jan;184(1):266-77. PMID: 11741868 Schmitt L. The first view of an ABC transporter: the X-ray crystal structure of MsbA from E. coli. Chembiochem. 2002 Mar 1;3(2-3):161-5. Review. No abstract available. PMID: 11921393 Ko J, Splitter GA.Brucella abortus tandem repeated ATP-binding proteins, BapA and BapB, homologs of haemophilus influenzae LktB, are not necessary for intracellular survival.Microb Pathog. 2000 Oct;29(4):245-53.PMID: 10993743 ","Wed Feb 5 15:21:44 2003","Wed Feb 5 15:21:44 2003","1","","","" "AA01394","943271","942441","831","GTGCGACATGATGCCGACGAAAACCAATATGTGGGCGCTTTTCACTTAATTGAACAAGGTGATTGCTGGCTGACCTTAGAAAATCAACAGATTCATTTACAAGCCGGCGAGCTCTTTTTTCTCCCGCAAAATCGACCGCACTTTATTGCCAGTAAGGCGCAGGACAATGTTATTCAAACCCGAATTACGCCGTCTGATGCACAGGAAGATCAGCAGGATTTATTTAAGGTTTACCATATCGGTCAGAATTCGCCGGATTTAAAAATGTTCTGTGGGATGCTGTACTACAACAAACCATCACTGTTAATTGATGCATTGCCGTCGTATTTGCATTTATCTTTGCGCGATACGCCGTTGTTGCCGCTTATTCAGGTGTTACAACAGGAAGCGGATAAAACGCGTAGTGGCGCGAAATCCTTGATTGATTCGCTGGTCACTGTGTTATTTATTTATATTCTGCGTCATGGATTGCAAAACGAACAACTAAATCAAGGCGTACTCGCCGGTTTTCAGGATAAGCGTTTGAACCCGGTGTTGACACAATTGTTAAACGCACCGCAACAGGCGTGGAATATGGACACCTTGGCGGCACTGGCGGCAATGTCACGAGCGAATTTTATGCGCGTATTTCAACACACTATCGGCATGGCACCGGGCAAGTTTCTGACTCAACTGCGTTTGCAGCAGGCAGCGTTATTATTAAATAAAACGCAGAAAAGCATATTGGCGATTGCGCTGGAGGTGGGCTATCAATCGGAGGCGCATTTCAGTAAGGCTTTTAAAATTGCTTACGGTATGACGCCAAGTCAATATCGAAAGCGAGAAGCCCTT","","","34594","VRHDADENQYVGAFHLIEQGDCWLTLENQQIHLQAGELFFLPQNRPHFIASKAQDNVIQTRITPSDAQEDQQDLFKVYHIGQNSPDLKMFCGMLYYNKPSLLIDALPSYLHLSLRDTPLLPLIQVLQQEADKTRSGAKSLIDSLVTVLFIYILRHGLQNEQLNQGVLAGFQDKRLNPVLTQLLNAPQQAWNMDTLAALAAMSRANFMRVFQHTIGMAPGKFLTQLRLQQAALLLNKTQKSILAIALEVGYQSEAHFSKAFKIAYGMTPSQYRKREAL","942441","","transcriptional regulator (mtr efflux pump)","Cytoplasm, Inner membrane","","
InterPro
IPR000005
Domain
Helix-turn-helix, AraC type
PR00032\"[241-256]T\"[256-272]THTHARAC
PF00165\"[177-223]T\"[229-273]THTH_AraC
SM00342\"[189-272]THTH_ARAC
PS01124\"[176-274]THTH_ARAC_FAMILY_2
PS00041\"[174-218]?HTH_ARAC_FAMILY_1
InterPro
IPR012287
Domain
Homeodomain-related
G3DSA:1.10.10.60\"[173-226]T\"[227-275]Tno description


","No hits to the COGs database.","Significant hit ( 1e-15) to 1/1 blocks of the IPB000005 family, which is described as \"AraC type helix-turn-helix\". Interpro entry for IP:IPR000005. IPB000005 241-272 9.8e-16 IPB000005 191-222 0.14Significant hit ( 1.2e-08) to 2/6 blocks of the IPB003313 family, which is described as \"Arac arabinose-binding and dimerisation domain\". Interpro entry for IP:IPR003313. IPB003313E 190-235 0.52 IPB003313F 236-276 7.6e-06","Residues 236 to 273 match (4e-07) PD:PD402035 which is described as COMPLETE PROTEOME TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR ACTIVATOR FAMILY REGULATORY ","","","","","Wed Feb 19 07:43:40 2003","","","","","","","Wed Feb 19 07:43:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01394 is paralogously related to AA01161 (8e-53).","","","","","","Residues 229 to 273 (E-value = 4.1e-14) place AA01394 in the HTH_AraC family which is described as Bacterial regulatory helix-turn-helix proteins, araC family (PF00165)","","","","","Rouquette C, Harmon JB, Shafer WM. Induction of the mtrCDE-encoded efflux pump system of Neisseriagonorrhoeae requires MtrA, an AraC-like protein. Mol Microbiol. 1999 Aug;33(3):651-8. PMID: 10417654 Gallegos MT, Michan C, Ramos JL The XylS/AraC family of regulators. Nucleic Acids Res 1993 Feb 25;21(4):807-10 PMID: 8451183","","Thu Jan 9 16:00:46 2003","1","","","" "AA01395","943459","943797","339","ATGTTTGCAGATTGGAAAAATGATGTTGCCCATGTGAAAAAATCATTCGGCGAATTAGGTAAAAATTATCCGAAAATGTTACAAGCCTACGGTGCATTAGACGCAGCTGCCTGTGAAGGCAATGTGTTAGATGCTAAAACCCGTGAATTAATTGCCCTCGCCGTGGCGGTTACCACCCGCTGTGAAAGCTGTATCGGCGTACACGCCGCCGAAGCGGTCAAAGCCGGCGCAACGGAGGAAGAGGTCGCCGCCGCACTTGCTATGTCTATCGCGTTAAACGCAGGCGCCGCTTACACTTATTCATTACGCGCATTAGAAGCTTACAATACACAAAAAGAC","","","11897","MFADWKNDVAHVKKSFGELGKNYPKMLQAYGALDAAACEGNVLDAKTRELIALAVAVTTRCESCIGVHAAEAVKAGATEEEVAAALAMSIALNAGAAYTYSLRALEAYNTQKD","943797","","conserved hypothetical protein","Periplasm, Cytoplasm","","
InterPro
IPR003779
Domain
Carboxymuconolactone decarboxylase
PF02627\"[24-107]TCMD
InterPro
IPR004675
Domain
Alkylhydroperoxidase AhpD core
TIGR00778\"[41-91]TahpD_dom: alkylhydroperoxidase AhpD family
noIPR
unintegrated
unintegrated
G3DSA:1.20.1290.10\"[4-109]Tno description


","No hits to the COGs database.","Significant hit ( 8e-11) to 3/3 blocks of the IPB003779 family, which is described as \"Carboxymuconolactone decarboxylase\". Interpro entry for IP:IPR003779. IPB003779A 41-54 0.0017 IPB003779B 70-86 0.00041 IPB003779C 94-105 26","Residues 24 to 82 match (2e-11) PD:PD009108 which is described as PROTEOME COMPLETE DNA-BINDING TA0244 RV1767 PA0565 YURZ TV1372 BH3473 ","","","","","","","","","","","","Thu Jan 9 17:04:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01395 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 19 to 107 (E-value = 8.3e-25) place AA01395 in the CMD family which is described as Carboxymuconolactone decarboxylase family (PF02627)","","","","","","","Thu Jan 9 17:04:14 2003","1","","","" "AA01396","944940","943900","1041","ATGGCTCTTTTCACTAAAGCTCCCAAATCCCTTTGTATTCTGCGTTTGTCCGCCATCGGCGATGTTTGCCATGCGTTGGCAGCGGTGCAACATATTCAACACTATTGGAAGGACACCAAAATCACTTGGATTATCGGCAAAACCGAAGCGCAATTGTTGCGCAACGTGCCGGGCATTGAGTTTATCGTGTATGACAAAAAGTGCGGTTGGCGTGGCGTGTGGAATTTATGGCGGCAGCTGAAACATCGCCGATTTGACGCGCTGCTCAATATGCAAACGGCGTTTCGCGCATTGATTTTATCCCTCGGGATTCATGCCGACTATCGTATCGGTTTTGGCAAACAGCGGGCGCGGGAAGGACAGTGGCTGTTTACGAATCGGCGAATTCAGGATCCCGCTAATCCGCATGTGCTGGACGGTTTTATGGCATTTGCCGATGAGCTCGGCGTGCCGCCTGCGCCGGCGCAATGGGATTTATCGGTGACGGAAGCGGATCTGGCGACAGTGCGGCGCTACCTTGATCCGAATCGCAAAAATCTGCTGATTTCTCCGTGTTCCAGCAAAAAAGAAAAAGATTGGCTGGCGGAACGTTATGCTGCAGTTGCAAATATTGCTCATCAGCATGGCGTGAATGTGATTTTATGCAGCTCGCCCGCACCACGCGAATTGGCGATGATTGAGGAAATCAAAGCACTATGTAATTTTGAACCGACGGATGCATCGGGCAAGCTAACCTTGACCGAACTTACCGCTTTAATTCGCGAAGTGGATTTGGTGATTTCGCCGGATTCCGGTCCCGCGCACATCGCTACCACACAAGGCACGCCGGTTATTGGTTTATACGCCTACCACAACCCACTACGCACCGGCCCCTACTGTAACCTCACCAATGTGGTTTCCGTGTATGAACAAAATGTGCAACAAGAATATGGTAAGCCTTCCTCCCAACTGCCATGGGCAACGAAGCTAAAAGGGAAGAATCTGATGGCGCAAATTGACGTGCAGGATGTGATTGCGCAGATGAAGGCATTGAATTTACTG","","","38899","MALFTKAPKSLCILRLSAIGDVCHALAAVQHIQHYWKDTKITWIIGKTEAQLLRNVPGIEFIVYDKKCGWRGVWNLWRQLKHRRFDALLNMQTAFRALILSLGIHADYRIGFGKQRAREGQWLFTNRRIQDPANPHVLDGFMAFADELGVPPAPAQWDLSVTEADLATVRRYLDPNRKNLLISPCSSKKEKDWLAERYAAVANIAHQHGVNVILCSSPAPRELAMIEEIKALCNFEPTDASGKLTLTELTALIREVDLVISPDSGPAHIATTQGTPVIGLYAYHNPLRTGPYCNLTNVVSVYEQNVQQEYGKPSSQLPWATKLKGKNLMAQIDVQDVIAQMKALNLL","943900","","saccharide biosynthesis regulatory protein","Cytoplasm","","
InterPro
IPR002201
Family
Glycosyl transferase, family 9
PF01075\"[73-320]TGlyco_transf_9
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2000\"[10-157]T\"[160-344]Tno description
signalp\"[1-27]?signal-peptide


","BeTs to 9 clades of COG0859COG name: ADP-heptose:LPS heptosyltransferaseFunctional Class: MThe phylogenetic pattern of COG0859 is -------q-----cefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 2.7e-28) to 2/2 blocks of the IPB002201 family, which is described as \"Glycosyltransferase family 9\". Interpro entry for IP:IPR002201. IPB002201A 20-44 1.2e-08 IPB002201B 243-286 3.2e-18","Residues 76 to 285 match (4e-09) PD:PD565705 which is described as PROTEOME LIPOPOLYSACCHARIDE CORE COMPLETE BIOSYNTHESIS ","","","","","","","","","","","","Fri Jan 10 09:03:53 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01396 is paralogously related to AA00543 (1e-06), AA01276 (3e-06), AA01327 (9e-06) and AA01329 (2e-05).","","","","","","Residues 73 to 320 (E-value = 2.5e-78) place AA01396 in the Glyco_transf_9 family which is described as Glycosyltransferase family 9 (heptosyltransferase) (PF01075)","","","","","Kingsley MT, Gabriel DW, Marlow GC, Roberts PD. The opsX locus of Xanthomonas campestris affects host rangeand biosynthesis of lipopolysaccharide and extracellular polysaccharide. J Bacteriol. 1993 Sep;175(18):5839-50. PMID: 8376331","","Fri Jan 10 09:03:53 2003","1","","","" "AA01398","945029","945751","723","ATGCTTGAATTTCAACTCAAAAACGATTTTTTTCTGTTTAATTTCGACCAACCTTTGACAAACCAAACGCAATTTTTCGAGGCGGCTTTCTGGCAACAACAAAACCGCGTTATCGGTTCGGCAAAAGGTCGTGGCACCACGTGGTTTCTGCAAACGGCGGATTTATTCGGCGTGAACACGGCGCTACGTCACTATTATCGTGGCGGCTTGTGGGGCAAAATCAACAAAGATCGTTATCCTTTCAGCAAACTGAAAAACACCCGTAGTGTTGCCGAATTTAATCTGTTAAATCAATTACATCAGGCAGGCTTACCGGTTCCTAAACCTATCGGGGCGCGGGTACGCAAAGGCAACTTAGGCATTTGTTATCAGGCGGATTTATTAAGCGAAAAAGTCGAAAATGCCCGCGATCTGACCGCACTTTTACAGACACAAAACCTTGAATCAACCCAATGGCGACAAATCGGTGCGCTCATCCGTCACTTGCACGATTTGCAAATCTGCCACACGGATCTTAACGCTCACAATATTCTGTGCCAACAAACGGACAACGGCAATCCATTCTGGCTTATCGACTTCGATAAGTGCGGTGAAAAATCCGGGCATTTTTGGAAAGAAGCCAACCTGCAACGGCTACATCGCTCATTCACCAAAGAGGTAGAATGTATGCATATTCATTTTACCAAGCAGAATTGGCGGGAAGTGTTGGAGGGGTATTCGGGG","","","29469","MLEFQLKNDFFLFNFDQPLTNQTQFFEAAFWQQQNRVIGSAKGRGTTWFLQTADLFGVNTALRHYYRGGLWGKINKDRYPFSKLKNTRSVAEFNLLNQLHQAGLPVPKPIGARVRKGNLGICYQADLLSEKVENARDLTALLQTQNLESTQWRQIGALIRHLHDLQICHTDLNAHNILCQQTDNGNPFWLIDFDKCGEKSGHFWKEANLQRLHRSFTKEVECMHIHFTKQNWREVLEGYSG","945751","","KDO kinase","Cytoplasm","","
InterPro
IPR010440
Family
Lipopolysaccharide kinase
PF06293\"[28-239]TKdo


","BeTs to 7 clades of COG0515COG name: Serine/threonine protein kinasesFunctional Class: TThe phylogenetic pattern of COG0515 is -o-p-zyq-drlbcefghs--j-i-wNumber of proteins in this genome belonging to this COG is","","Residues 1 to 239 match (2e-89) PD:PD180638 which is described as KINASE TRANSFERASE BIOSYNTHESIS LIPOPOLYSACCHARIDE 3-DEOXY-D-MANNO-OCTULOSONIC MEMBRANE ATP-BINDING ACID 2.7.1.- KDO ","","","","","","","","","","","","Fri Jan 10 09:10:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01398 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 28 to 239 (E-value = 9.3e-110) place AA01398 in the Kdo family which is described as Lipopolysaccharide kinase (Kdo/WaaP) family (PF06293)","","","","","Brabetz W, Muller-Loennies S, Brade H. 3-Deoxy-D-manno-oct-2-ulosonic acid (Kdo) transferase (WaaA)and kdo kinase (KdkA) of Haemophilus influenzae are both required to complement a waaA knockout mutation of Escherichiacoli. J Biol Chem. 2000 Nov 10;275(45):34954-62. PMID: 10952982 White KA, Lin S, Cotter RJ, Raetz CR. A Haemophilus influenzae gene that encodes a membrane bound3-deoxy-D-manno-octulosonic acid (Kdo) kinase. Possible involvement of kdo phosphorylation in bacterial virulence. J Biol Chem. 1999 Oct 29;274(44):31391-400. PMID: 10531340 ","","Fri Jan 10 09:10:06 2003","1","","","" "AA01400","946301","945819","483","ATGACCACGGTAATTTATCCCGGCACCTTTGACCCGTTAACCAACGGGCATTTGAACATTATCGAACGAAGTGCGGTGCTTTTTCCGCGCGTTTTAGTGGCGGTGGCGGAAAGCCCGAGCAAAAAGCCGTTATTCAGCTTGACGGAACGGGTGGAACTGGTGCGCCAAGCCGCTGCCCATTTGCCGAACGTGGAAGTCATCGGTTTCGATAATTTACTGGCGCACACCATCGCCCAATATGACGTTAAAGCCATTATTCGCGGCGTGCGCAGCACCACGGATTTTGAATACGAAGTTCAGTTAGCCCATCTTAACCGCCTGCTTACCCACGGCGTCGAAAGCCTGTTTTTCCCGCCGGTGGAACAATGGTCGTACGTCTCCTCCACCATGATCCGCGAAATTTACCTACACAACGGCGATATGAGTCAACTGGTTCCACCGGCGGTATTAAAGGCGTTACAGGCAAAGCGTGAGTTGCGTGGG","","","18046","MTTVIYPGTFDPLTNGHLNIIERSAVLFPRVLVAVAESPSKKPLFSLTERVELVRQAAAHLPNVEVIGFDNLLAHTIAQYDVKAIIRGVRSTTDFEYEVQLAHLNRLLTHGVESLFFPPVEQWSYVSSTMIREIYLHNGDMSQLVPPAVLKALQAKRELRG","945819","","phosphopantetheine adenylyltransferase","Cytoplasm","","
InterPro
IPR001980
Family
Coenzyme A biosynthesis protein
PR01020\"[2-20]T\"[20-41]T\"[49-73]T\"[85-101]T\"[112-134]TLPSBIOSNTHSS
TIGR01510\"[3-157]TcoaD_prev_kdtB: pantetheine-phosphate adeny
InterPro
IPR004820
Domain
Cytidylyltransferase
PF01467\"[5-134]TCTP_transf_2
InterPro
IPR004821
Domain
Cytidyltransferase-related
TIGR00125\"[3-63]Tcyt_tran_rel: cytidyltransferase-related do
InterPro
IPR013166
Domain
Citrate lyase ligase, C-terminal
SM00764\"[12-153]Tno description
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620\"[1-158]Tno description
noIPR
unintegrated
unintegrated
PTHR21342\"[1-161]TPHOSPHOPANTETHEINE ADENYLYLTRANSFERASE


","BeTs to 15 clades of COG0669COG name: Phosphopantetheine adenylyltransferaseFunctional Class: HThe phylogenetic pattern of COG0669 is -------qvdrlbcefghsnuj--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1e-63) to 5/5 blocks of the PR01020 family, which is described as \"Lipopolysaccharide core biosynthesis protein signature\". Prints database entry for PR:PR01020. PR01020A 2-20 4.4e-12 PR01020B 20-41 1.3e-10 PR01020C 49-73 1.8e-14 PR01020D 85-101 5.5e-10 PR01020E 112-134 1e-10","","","","","","","","","","","","","Fri Jan 10 09:16:05 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01400 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 134 (E-value = 1.6e-38) place AA01400 in the CTP_transf_2 family which is described as Cytidylyltransferase (PF01467)","","","","","Roncero,C. and Casadaban,M.J. Genetic analysis of the genesinvolved in synthesis of the lipopolysaccharide core inEscherichia coli K-12: three operons in the rfa locus J. Bacteriol. 174 (10), 3250-3260 (1992) PubMed: 1577693 Clementz,T. and Raetz,C.R. A gene coding for 3-deoxy-D-manno-octulosonic-acid transferase in Escherichia coli. Identification, mapping,cloning, and sequencing J. Biol. Chem. 266 (15), 9687-9696 (1991) PubMed: 2033061 ","","Fri Jan 10 09:16:05 2003","1","","","" "AA01401","947585","946305","1281","ATGTTACGTTTTTTTTATACCTGTTTAATGTATCTTGTGCAGCCTTTTTTGTGGCTTTCGGCGCTGTTTCGAGGCTTCAAAGCGCCTAATTACCGCAAACGTTTAGGCGAACGTTACGCGTTTTACGGCGAATTGCCCGCACCGAAACCCAACGGCGTGCTTATTCATGCCGCGTCGGTGGGCGAAGTGATCGCCGCCGTGCCGTTAATTAAACGTATTCAGCAAGATTACCCGCATTTGGCGATCACCGTGACGACCATGACGCCCACCGGCTCCGATCGTGTCAAGGCGGTTTTCGGTGAGAGCGTCACCCACGTTTATTTGCCTTATGATTTACCCGATGCGGTCGCCCGTTTTATTCGCTTTGTGCAACCGCGCCCGGTGCTCGTCATTGAAACGGAACTGTGGTTTAACCTGATTCATCACTTATCGCAACGAAAAATTCCGTTTATTATCGTGAATGCTCGCTTATCGGCACGTTCTGCCAAGCGTTACGGCTGGTTTAAAAATCAGTTAAAACCATTGTTGGATAACATCAGCTTGATTGCACCGCAGGATGACGTGAGTCTGGCGCGTTATGCCCAATTAGGCATTGCACCCGAACGTTTAACGCTGATGGGCAATATTAAATACGATTTAAATTTAACGGACGATTTGCTGAATAACATCACTGCGTTAAAAGCGCAATGGAATACCCGACGCCCTATTTGGATTGCCGCCAGCACTCATGAAAGCGAAGATGAAATCATCTTAAAAAGCCACCGCACTTTATTGGCGCATTATCCCGATTTATTGTTGATTCTGGTGCCGCGCCACCCCGAGCGTTTTAATTCGGTGGCGCAGCTCATTGAACAGCAGGGCTTTCATTATATCCGACGTAGCAGCCATACTGCGCCACAGGCGGAAATACAAGTGCTGCTCGGCGATACTATGGGCGAGTTGATGTTGCTGTATGGCATGGCGAACGTGGCATTGGTGGGCGGCAGTTTGGTAGCGCACGGCGGACATAATCCGTTAGAACCTCTGGCATTTAAATTGCCGGTGATCAGCGGCAAGCACACGTTTAATTTCCCTGAAGTCTTCAGTAAATTAATTGAACGCCAAGGCGTCGTGATAACGGAAGATAGCCCGCAGGCAGTGGTGGAGGCGGTGGCGCAGTTTTTATCATCGCCGACATTGGGCGAATGCTACGGCAATGCCGGTTATGCGGTATTAAATGAGAATCGCGGCGCATTGCAACGCGTCATGGATTTATTAAAACCTTATTTAGACGAGGTGAAT","","","48097","MLRFFYTCLMYLVQPFLWLSALFRGFKAPNYRKRLGERYAFYGELPAPKPNGVLIHAASVGEVIAAVPLIKRIQQDYPHLAITVTTMTPTGSDRVKAVFGESVTHVYLPYDLPDAVARFIRFVQPRPVLVIETELWFNLIHHLSQRKIPFIIVNARLSARSAKRYGWFKNQLKPLLDNISLIAPQDDVSLARYAQLGIAPERLTLMGNIKYDLNLTDDLLNNITALKAQWNTRRPIWIAASTHESEDEIILKSHRTLLAHYPDLLLILVPRHPERFNSVAQLIEQQGFHYIRRSSHTAPQAEIQVLLGDTMGELMLLYGMANVALVGGSLVAHGGHNPLEPLAFKLPVISGKHTFNFPEVFSKLIERQGVVITEDSPQAVVEAVAQFLSSPTLGECYGNAGYAVLNENRGALQRVMDLLKPYLDEVN","946305","","3-deoxy-D-manno-octulosonic-acid transferase","Inner membrane, Cytoplasm","","
InterPro
IPR001296
Domain
Glycosyl transferase, group 1
PF00534\"[300-404]TGlycos_transf_1
InterPro
IPR007507
Domain
Three-deoxy-D-manno-octulosonic-acid transferase, N-terminal
PF04413\"[31-215]TGlycos_transf_N
noIPR
unintegrated
unintegrated
PTHR23417\"[27-425]T3-DEOXY-D-MANNO-OCTULOSONIC-ACID TRANSFERASE/TRNA (GUANINE-N(7)-)-METHYLTRANSFERASE
PTHR23417:SF2\"[27-425]T3-DEOXY-D-MANNO-OCTULOSONIC-ACID TRANSFERASE (KDO TRANSFERASE)
signalp\"[1-20]?signal-peptide


","BeTs to 11 clades of COG1519COG name: 3-Deoxy-D-manno-octulosonic-acid transferaseFunctional Class: MThe phylogenetic pattern of COG1519 is -------q------efghsnujxi--Number of proteins in this genome belonging to this COG is","","Residues 1 to 46 match (1e-08) PD:PD041572 which is described as TRANSFERASE PROTEOME COMPLETE 3-DEOXY-D-MANNO-OCTULOSONIC-ACID KDO TRANSMEMBRANE BIOSYNTHESIS INNER 2.-.-.- LIPOPOLYSACCHARIDE ","","","","","","","","","","","","Fri Jan 10 09:19:11 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01401 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 234 to 404 (E-value = 2.6e-07) place AA01401 in the Glycos_transf_1 family which is described as Glycosyl transferases group 1 (PF00534)","","","","","Tzeng YL, Datta A, Strole C, Kolli VS, Birck MR, Taylor WP,Carlson RW, Woodard RW, Stephens DS. KpsF is the arabinose-5-phosphate isomerase required for 3-deoxy-D-manno-octulosonic acid biosynthesis and for bothlipooligosaccharide assembly and capsular polysaccharideexpression in Neisseria meningitidis. J Biol Chem. 2002 Jul 5;277(27):24103-13. PMID: 11956197 Tzeng YL, Datta A, Kolli VK, Carlson RW, Stephens DS. Endotoxin of Neisseria meningitidis composed only of intactlipid A: inactivation of the meningococcal3-deoxy-D-manno-octulosonic acid transferase. J Bacteriol. 2002 May;184(9):2379-88. PMID: 11948150 White KA, Kaltashov IA, Cotter RJ, Raetz CR. A mono-functional 3-deoxy-D-manno-octulosonic acid (Kdo)transferase and a Kdo kinase in extracts of Haemophilusinfluenzae. J Biol Chem. 1997 Jun 27;272(26):16555-63. PMID: 9195966 ","","Fri Jan 10 09:19:11 2003","1","","","" "AA01402","947684","948442","759","ATGCCTACCATCAGCGTTGCAATGATTGTCAAAAACGAAGCGCACCACCTCGCATCGTGCCTGGATACGGTGAAAGATTGGGTGGATGAAATCGTCATTTTAGATTCCGGCAGCACGGACGACACGCAACGCATCGCCGAGCAATATCACGCCAAGTTTTATCAAAACACCAACTGGCCGGGCTTCGGCAAACAACGGCAATTAGCCCAGAACTATGTCACCGGCGATTATGTATTGTGGCTGGACGCGGACGAACGGGTCACGCCGGCATTACGTCAATCCATTCAAAATGCCATCGCACAAGACGCGCCGAATACGGCATACAAAATCCCGCGCTTAAGTGAAGTGTTCGGCAGCAAAATTCGCCATTCCGGCTGGTATCCCGATTATGTCATTCGCCTGTATCGCACGGATTTCGCGCGTTACGGCGATCAATTGGTCCATGAAAAAGTAGAATTGCCCGCCAATGCCGACATTCAAAAATTAAACGGAGATCTGTTGCACTACACTTATCAAGATATTCATCATTATTTAGTGAAATCCGCCGGCTACGCCAAAGCCTGGGCGGAACAACGGGAAAAATCCGGTAAAAAAGCCACCTTATGGCAAGGTGTCAGTCACGCCATCGGTTGTTTTGTGAAAATGTATTTTATCCGATTGGGATTTTTAGACGGCAAAGCAGGGTTACTGCTGGCAATTCTCTCGGCGCATTCAACGTTTATAAAATATGCGGATTTGTGGGTGCGGACGAGAGGGAAA","","","32033","MPTISVAMIVKNEAHHLASCLDTVKDWVDEIVILDSGSTDDTQRIAEQYHAKFYQNTNWPGFGKQRQLAQNYVTGDYVLWLDADERVTPALRQSIQNAIAQDAPNTAYKIPRLSEVFGSKIRHSGWYPDYVIRLYRTDFARYGDQLVHEKVELPANADIQKLNGDLLHYTYQDIHHYLVKSAGYAKAWAEQREKSGKKATLWQGVSHAIGCFVKMYFIRLGFLDGKAGLLLAILSAHSTFIKYADLWVRTRGK","948442","","beta 1-4 glucosyltransferase","Cytoplasm","","
InterPro
IPR001173
Domain
Glycosyl transferase, family 2
PF00535\"[5-89]TGlycos_transf_2
noIPR
unintegrated
unintegrated
G3DSA:3.90.550.10\"[2-89]Tno description
PTHR22916\"[10-142]TGLYCOSYLTRANSFERASE


","No hits to the COGs database.","","Residues 52 to 84 match (2e-08) PD:PD576756 which is described as TRANSFERASE LIPOPOLYSACCHARIDE BIOSYNTHESIS COMPLETE PROTEOME GLYCOSYL CORE 2.-.-.- GLYCOSYLTRANSFERASE GLUCOSYLTRANSFERASE ","","","","","","","","","","","","Fri Jan 10 09:24:22 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01402 is paralogously related to AA02332 (1e-07) and AA02649 (0.001).","","","","","","Residues 5 to 153 (E-value = 3.8e-20) place AA01402 in the Glycos_transf_2 family which is described as Glycosyl transferase (PF00535)","","","","","Filiatrault,M.J., Gibson,B.W., Schilling,B., Sun,S.,Munson,R.S. Jr. and Campagnari,A.A. Construction and Characterization of Haemophilus ducreyi Lipooligosaccharide (LOS) Mutants Defective in Expression of Heptosyltransferase III and beta 1,4-Glucosyltransferase: Identification of LOS Glycoforms Containing LactosamineRepeats JOURNAL Infect. Immun. 68 (6), 3352-3361 (2000) PubMed: 10816485 Guasch,J.F., Pique,N., Climent,N., Ferrer,S., Merino,S.,Rubires,X., Tomas,J.M. and Regue,M. Cloning and characterization of two Serratia marcescens genesinvolved in core lipopolysaccharide biosynthesis. J. Bacteriol. 178(19): 5741-5747, 1996. PubMed: 8824620.","","Fri Jan 10 09:24:22 2003","1","","","" "AA01404","948718","948894","177","TTGAAGTGGCTTGAAACAAGCGACTTTTCACCACAAGCCTTTAAAAAACTGAAACGGGAACCTGCCCTTGCAAAAGAGGAGATTGATTATCTAAAAAAGTTAGTGGAATTAGACAATCAAAAACGACGGCAGAAAAAGAAAAGTCATCGAAAAGTTAAAGGAAAAACATGCCTTAAA","","","7066","LKWLETSDFSPQAFKKLKREPALAKEEIDYLKKLVELDNQKRRQKKKSHRKVKGKTCLK","948894","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 14:15:39 2004","Thu Feb 26 17:10:06 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA0227.AA01404 is paralogously related to AA00227 (1e-21), AA00631 (1e-14), AA00535 (1e-12), AA02340 (5e-12), AA02115 (3e-11), AA01289 (3e-11), AA01075 (3e-11) and AA00008 (3e-11).","Thu Feb 26 14:15:39 2004","","","","","","","","","","","","","1","","","" "AA01407","950311","949145","1167","ATGAAAAGCTCTTTTTTACTGTTACCGATCAGCATTGCCGTGTTAGCGGCCTGTACTTCGAATACACCGGCACCGGTGGAAAACGCCGACGGTACCTTATCCCCGGGACTCATGCAACCGGTGGACGGTTCAACCGATGGCGGCAATAGCACATGGGAACCGCAAATCCAACAAGGCAATGTACCCGCTTCGATGAACGGTCCGATTGCCCAGTCGAACAATCTACAGGCGACCGGCGCACAATCTACTCCGCAGCCGAATTTTCAACCGATGTATCAACAGTCTGCACTGCAAGCACAGCCGGTTCAGCAAACCCAACCTGCCGCGCAAAATCAACCGCAACAGGCATCCCAGGATTTCACCATTCCACGTAACCCGACCACTAACGCACCGGATTACAGCCAAATCAACAAAGGTTTCTACAAAGGTGAAACCTATACCGTACGCAAAGGTGACACCATGTTCCTTATCGCCTACATTTCTGGTTTGGATGTGAAAGAATTGGCGGCGTTGAATAATATGTCCGAACCTTACAGCTTAAGCGTCGGACAAACCTTAAAGGTGAGCCGCGGCACAACGGCTACGGTGCAAACGAAAGCTGCACCGCAAATGCAACCGACGGTCACCCAACCGGCTACGCAAGGTGGTGAACCGACCGTAACTTACACCCCGGGCGCAAACGGCACACAATATGGTTCCGACGGCACGATTACCGGCCCGATTAAAGCCGGCGTAGGTACTGCTGCACCGGCAACCAATCAGCCGATAACCCAAGCGGGCACCGCACCGGCAGTATCCAACGTGGCATGGCGCTGGCCGACCAACGGCAATGTGATTCAAGGTTTCTCTAACGCCGACGGCGGTAACAAAGGCATCGACATCAGTGGTTCTCGCAGACAAGCAGTCAATGCCGCCGCCGCAGGTCGAGTGGTTTACGCGGGTAACGCCTTACGCGGTTACGGCAACCTGATCATCATCAAACACAATGATGATTTCCTCAGCGCCTACGCCCACAACGACAGTATTTTGGTAAAAGACCAGCAGGAAATCAAAGCCGGTCAGCAAATCGCAAAAATGGGCAGCACCGGCACCAACGGCGTGAAACTGCACTTTGAAATTCGTTACAAAGGCAAATCCGTGGATCCGTTGCGTTATCTCCCACGTCGT","","","40952","MKSSFLLLPISIAVLAACTSNTPAPVENADGTLSPGLMQPVDGSTDGGNSTWEPQIQQGNVPASMNGPIAQSNNLQATGAQSTPQPNFQPMYQQSALQAQPVQQTQPAAQNQPQQASQDFTIPRNPTTNAPDYSQINKGFYKGETYTVRKGDTMFLIAYISGLDVKELAALNNMSEPYSLSVGQTLKVSRGTTATVQTKAAPQMQPTVTQPATQGGEPTVTYTPGANGTQYGSDGTITGPIKAGVGTAAPATNQPITQAGTAPAVSNVAWRWPTNGNVIQGFSNADGGNKGIDISGSRRQAVNAAAAGRVVYAGNALRGYGNLIIIKHNDDFLSAYAHNDSILVKDQQEIKAGQQIAKMGSTGTNGVKLHFEIRYKGKSVDPLRYLPRR","949145","","outer membrane antigenic lipoprotein b precursor","Outer membrane, Periplasm","","
InterPro
IPR002482
Domain
Peptidoglycan-binding LysM
PF01476\"[146-189]TLysM
SM00257\"[145-189]TLysM
InterPro
IPR002886
Family
Peptidase M23B
PTHR21666:SF7\"[139-212]T\"[248-386]TM23/M37 PEPTIDASE FAMILY MEMBER
PF01551\"[287-382]TPeptidase_M23
noIPR
unintegrated
unintegrated
PTHR21666\"[139-212]T\"[248-386]TPEPTIDASE-RELATED
PS51257\"[1-18]TPROKAR_LIPOPROTEIN
signalp\"[1-16]?signal-peptide


","BeTs to 16 clades of COG0739COG name: Membrane proteins related to metalloendopeptidasesFunctional Class: MThe phylogenetic pattern of COG0739 is -------qvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 6.5e-30) to 2/2 blocks of the IPB002886 family, which is described as \"Peptidase family M23/M37\". Interpro entry for IP:IPR002886. IPB002886A 289-314 4.4e-08 IPB002886B 323-363 2.1e-20","Residues 133 to 192 match (9e-10) PD:PD545455 which is described as LIPOPROTEIN PROTEOME COMPLETE ","","","","","","","","","","","","Fri Jan 10 09:26:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01407 is paralogously related to AA00450 (5e-19), AA01822 (3e-10) and AA01408 (5e-08).","","","","","","Residues 303 to 385 (E-value = 1.5e-42) place AA01407 in the Peptidase_M37 family which is described as Peptidase family M23/M37 (PF01551)","","","","","Ichikawa,J.K., Li,C., Fu,J. and Clarke,S. A gene at 59 minutes on the Escherichia coli chromosomeencodes a lipoprotein with unusual amino acid repeat sequences J. Bacteriol. 176 (6), 1630-1638 (1994) PubMed: 8132457 ","","Fri Jan 10 09:26:28 2003","1","","","" "AA01408","950519","950331","189","ATGAAGAAACTGATTCTGTTACTATCTATGTCGTTAACGTTAGCGGCTTGTTCTTCACATGATGAGATACCGAAAGACGAAAACGATCTGCCGCCGGGCATTATGCAACCGGTGGAAGGCACCGGCGCCATCGCAGGCGGCAGCTGGGTGCCTGAAATTCAACAACAAAGTATGCCAATCAATATGCAA","","","9090","MKKLILLLSMSLTLAACSSHDEIPKDENDLPPGIMQPVEGTGAIAGGSWVPEIQQQSMPINMQ","950331","","conserved hypothetical protein","Outer membrane, Periplasm, Cytoplasm","","
noIPR
unintegrated
unintegrated
PS51257\"[1-17]TPROKAR_LIPOPROTEIN
signalp\"[1-17]?signal-peptide


","No hits to the COGs database.","","Residues 22 to 63 match (2e-07) PD:PD052959 which is described as PROTEOME HI0704 COMPLETE ","","","","","","","","","","","","Fri Jan 10 09:30:21 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01408 is paralogously related to AA01407 (5e-09).","","","","","","","","","","","","","","1","","","" "AA01409","951109","950537","573","ATGAAGCTATTTGGCGCCATGTACGACAAAACCATGCAATGGTCGAAACACCGTTTCGCGCCTTTCTGGTTGTCTTTCGTGAGTTTTATTGAGGCGATTTTCTTCCCAATTCCGCCGGATGTGATGTTAATTCCGATGTCCATGTCAAAACCGCAAAGTGCGGTGAAATTTGCCATGTTTACCGCCACAGCCTCCGTACTCGGCGGGATGATAGGTTACGCGTTAGGCTATTATGCTTTTAATTTGGTCGAACATTACATTACCCAATGGGGCTATCAGGCATCATGGCAAACCACCATTCACTGGTTTGAACGCTGGGGCATGTTGGTGGTGTTCGTGGCAGGCTTTTCGCCGATTCCGTACAAAGTGTTTACCATTTGCGCCGGCGTGATGCAAATGGCGTTTATACCATTCGTAATTACTGCGTTTATTTCCCGTACGGCGCGGTTCTTACTGGTCGCCAAATTAGCCGCCTGGGGTGGTGAAAAATTTGCCGCCAAATTACGTAAATCTATCGAATTCATCGGTTGGTCGGTGGTGGCATTAGCCGTCGTCGCGTATTTAATTTTACGT","","","21693","MKLFGAMYDKTMQWSKHRFAPFWLSFVSFIEAIFFPIPPDVMLIPMSMSKPQSAVKFAMFTATASVLGGMIGYALGYYAFNLVEHYITQWGYQASWQTTIHWFERWGMLVVFVAGFSPIPYKVFTICAGVMQMAFIPFVITAFISRTARFLLVAKLAAWGGEKFAAKLRKSIEFIGWSVVALAVVAYLILR","950537","","lipoprotein B","Inner membrane, Cytoplasm","","
InterPro
IPR015414
Domain
SNARE associated Golgi protein
PF09335\"[44-159]TSNARE_assoc
noIPR
unintegrated
unintegrated
signalp\"[1-32]?signal-peptide
tmhmm\"[19-37]?\"[58-80]?\"[99-119]?\"[134-153]?\"[172-190]?transmembrane_regions


","No hits to the COGs database.","","Residues 100 to 154 match (4e-15) PD:PD430523 which is described as COMPLETE PROTEOME HI0703 DEDA AQ_2066 HOMOLOG FAMILY MJ0201 MJ0374 ","","","","","Tue Feb 18 16:32:29 2003","","","","","","","Tue Feb 18 16:32:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01409 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 22 to 176 (E-value = 1.9e-56) place AA01409 in the DedA family which is described as DedA family (PF00597)","","","","","Ichikawa,J.K., Li,C., Fu,J. and Clarke,S.A gene at 59 minutes on the Escherichia coli chromosome encodes alipoprotein with unusual amino acid repeat sequencesJ. Bacteriol. 176 (6), 1630-1638 (1994)PubMed: 8132457Padmalayam I, Kelly T, Baumstark B, Massung R.Molecular cloning, sequencing, expression, and characterization of an immunogenic 43-kilodalton lipoprotein of Bartonella bacilliformis that has homology to NlpD/LppB.Infect Immun. 2000 Sep;68(9):4972-9.PMID: 10948113 Theisen,M., Rioux,C.R. and Potter,A.A.Molecular cloning, nucleotide sequence, and characterization oflppB, encoding an antigenic 40-kilodalton lipoprotein of Haemophilus somnusInfect. Immun. 61 (5), 1793-1798 (1993)PubMed: 8478068","","Tue Feb 18 16:32:29 2003","1","","","" "AA01411","951877","951140","738","ATGAATATTTTATTAAGTAACGATGACGGCATTCACGCGCCGGGCATTCGTGTGATGGCAGAAGCATTGCGTAAGATTGCCAATGTGACCATCGTCGCGCCGGACAGCAACCGCAGCGCCGCCTCCAGTTCCTTAACCTTGGTGAAGCCGTTGTATCCGTTACATTTGGAAAGCGGTGATTATTGCGTCAACGGCACGCCGGCGGATTGCGTGCATATTGCGCTGAACGGTTTTCTTTCCGGGCGCATCGATTTGGTGATTTCCGGCATCAACGCCGGGGCGAACCTGGGCGATGATGTGCTATATTCCGGCACGGTCGCGGCAGCATTTGAAGGGCGTCATCTGGGCTTGCCGTCTATTGCGGTATCGCTCGATGGTCGTCAACATTTTGAAACGGCGGCGCGCGTGGTATGCGATTTGGTGCCGAAATTACACGCCCAATTATTAGGCAAACACGAAATTCTGAATATTAACGTGCCCGATGTGCCTTACGAAGAACTGAAAGGCATTAAAGTGTGCCATTTGGGCTACCGTTCTTCCGCTTCTGAAGTGATTAAACAGCAAAGCCCGCGTGGCGAAGACATGTATTGGATCGGGCTCAGCGGCTTGCCGGAATATGAAAGCGAAGGCACCGATTTCCACGCGGTGAAAAACGGCTATGTTTCCATTACGCCGATTCAGGTGGACATGACCGCGCACCACTCAATCAACGCTTTACAACGTTGGTTAGAAAGTGAA","","","26499","MNILLSNDDGIHAPGIRVMAEALRKIANVTIVAPDSNRSAASSSLTLVKPLYPLHLESGDYCVNGTPADCVHIALNGFLSGRIDLVISGINAGANLGDDVLYSGTVAAAFEGRHLGLPSIAVSLDGRQHFETAARVVCDLVPKLHAQLLGKHEILNINVPDVPYEELKGIKVCHLGYRSSASEVIKQQSPRGEDMYWIGLSGLPEYESEGTDFHAVKNGYVSITPIQVDMTAHHSINALQRWLESE","951140","","stationary-phase survival protein","Cytoplasm","","
InterPro
IPR002828
Family
Survival protein SurE
PD005378\"[9-243]TSURE_PASMU_P57955;
PF01975\"[1-184]TSurE
TIGR00087\"[1-231]TsurE: 5'/3'-nucleotidase SurE
noIPR
unintegrated
unintegrated
G3DSA:3.40.1210.10\"[1-242]Tno description


","BeTs to 20 clades of COG0496COG name: Survival protein, predicted acid phosphataseFunctional Class: RThe phylogenetic pattern of COG0496 is aom--zyqvd---cefghsnuj-it-Number of proteins in this genome belonging to this COG is","Significant hit ( 3e-66) to 6/6 blocks of the IPB002828 family, which is described as \"Survival protein SurE\". Interpro entry for IP:IPR002828. IPB002828A 1-23 1.6e-13 IPB002828B 28-52 2.6e-10 IPB002828C 61-71 1.2e-06 IPB002828D 84-109 1.8e-21 IPB002828E 149-160 0.12 IPB002828F 221-231 4.7e-05","Residues 1 to 240 match (1e-108) PD:PD005378 which is described as ACID MAGNESIUM PHOSPHATASE HYDROLASE PROTEOME COMPLETE SURE SURVIVAL STATIONARY-PHASE SLL1459 ","","","","","","","","","","","","Fri Jan 10 09:45:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01411 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 184 (E-value = 3.3e-94) place AA01411 in the SurE family which is described as Survival protein SurE (PF01975)","","","","","Li,C., Ichikawa,J.K., Ravetto,J.J., Kuo,H.C., Fu,J.C. andClarke,S. 1994. A new gene involved in stationary-phase survival located at59 minutes on the Escherichia coli chromosome. J. Bacteriol.176(19):6015-6022. PubMed: 7928962","","Fri Jan 10 09:45:14 2003","1","","","" "AA01413","952920","951913","1008","ATGATGGAACTCGCCTATTTGCAAAAAACGCCGCCAAAACAGACCGCACTTTTAAAAGCGGAATGCGCGGATTTTGTCGTCAAAGAGCAACTGGGCTACGACATGAGCGGCGACGGCGAATTCGTGGCGGTGAAAATACGCAAAACCGATTGCAACACCTTGTTTGTAGGCGAGCAACTGGCGAAATTCGCCGGCATTTCGGCACGCAACATGAGTTATGCCGGTTTGAAAGATCGCAAAGCTGTCACCGAACAATGGTTCAGCCTGCAAATGCCCGGGCAACCGACGCCGGATTTCAGCCAATTTCACCTTGACGGCGTGGATATTCTTGAAGTGACCCGCCACCAACGCAAAATCCGTATCGGCAGCCTGCAAGGCAATCATTTTGAGATTTTGCTGCGCCACGCGGAAGAAACCGACGAGCTCAAAGTGCGGTTGGATTTTCTGGCAAAAAACGGCTTCCCCAATTATTTCACCGAACAGCGTTTCGGGCGCGACGGCAACAATCTCACCCAAGCCCTACGCTGGGCGGCGGGCGAAATCAAAGTGAAAGATCGCAACAAGCGCAGTTTCTATATTTCCGCCGCCCGCAGTGAGATTTTCAATTTAATCGTTGCCAAACGTATTGAACTCAGTCTGGCGCAGCAGGTCTTAAATGGAGACGTTTTGCAACTGAACGGTTCGCACAGTTGGTTTGTGGCGGACGCATCGGAAGATTTGACGCAACTGCAACAACGCTTGGCACAACGGGATATTTTGCTTACCGCACCGCTTATCGGCGAAGAGGACAAAAGTGCGGTGGATTTTGAGAATGAAATTTTTGTCGCGCACCAAGCCTTGTTCCATTTGATGCGGCAAGAACGCGTGAAAGCCGCCCGCCGTCCGATTTTAATGCAGGCGCAACAGTTTCAATGGCAATTTGAACCGAACGGTTTGCGCCTTAAATTTTATTTGCCGGCAGGCAGTTACGCCACGGCGTTGGTACGCGAGCTGGTGAATGTTGAAAAC","","","38352","MMELAYLQKTPPKQTALLKAECADFVVKEQLGYDMSGDGEFVAVKIRKTDCNTLFVGEQLAKFAGISARNMSYAGLKDRKAVTEQWFSLQMPGQPTPDFSQFHLDGVDILEVTRHQRKIRIGSLQGNHFEILLRHAEETDELKVRLDFLAKNGFPNYFTEQRFGRDGNNLTQALRWAAGEIKVKDRNKRSFYISAARSEIFNLIVAKRIELSLAQQVLNGDVLQLNGSHSWFVADASEDLTQLQQRLAQRDILLTAPLIGEEDKSAVDFENEIFVAHQALFHLMRQERVKAARRPILMQAQQFQWQFEPNGLRLKFYLPAGSYATALVRELVNVEN","951913","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR001656
Family
tRNA pseudouridine synthase D, TruD
PTHR13326\"[1-165]TTRNA PSEUDOURIDINE SYNTHASE D
PF01142\"[2-336]TTruD
TIGR00094\"[2-335]TTIGR00094: conserved hypothetical protein T
PS01268\"[75-88]TUPF0024
InterPro
IPR011760
Domain
TRUD
PS50984\"[153-309]TTRUD


","BeTs to 15 clades of COG0585COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG0585 is aompkzyq-d----efgh--u-----Number of proteins in this genome belonging to this COG is","Significant hit ( 2.3e-24) to 3/3 blocks of the IPB001656 family, which is described as \"Uncharacterized protein family UPF0024\". Interpro entry for IP:IPR001656. IPB001656A 73-85 3.1e-07 IPB001656B 119-134 2.7e-06 IPB001656C 153-164 1.7e-07","Residues 238 to 333 match (9e-30) PD:PD563057 which is described as PROTEOME COMPLETE HYDROGENASE SUBUNIT VC0530 STY3053 HI0701 PM1610 YGBO PARAL ","","","","","","","","","","","","Fri Jan 10 09:46:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01413 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 336 (E-value = 2.8e-152) place AA01413 in the TruD family which is described as tRNA pseudouridine synthase D (TruD) (PF01142)","","","","","","","","1","","","" "AA01416","953396","952920","477","ATGATACGAATCGGCCATGGTTTTGACGTGCACGCTTTCGGCACCAACAACCCGCTCATTATCGGCGGTGTCACCATTCCCTTTGATAAAGGCTTTATCGCCCATTCCGACGGCGATGTGGCATTGCACGCGCTAACCGATGCGTTGCTCGGCGCGGCGGCATTGGGCGACATCGGCAAACTGTTCCCCGACACGGATATGCAATACAAAGGCGCGGACAGTCGCGTATTGTTGCGCGAAGCCTACCGTCAGGTTCAGGAAAAGGGCTATTGCGTAGGCAACGTAGATGTCACCATCATCGCCCAAGCGCCGAAAATGCGCCCACATATTGACGCCATGCGCGCGCTGATTGCGCAGGATTTGGCGTGCGATATAGAACAGGTGAATGTCAAAGCCACCACCACTGAAAAACTCGGGTTTACCGGTCGCGGTGAAGGCATTGCCTGCGAAGCGGTGGCGTTGCTGGTGCGTAAACCA","","","16969","MIRIGHGFDVHAFGTNNPLIIGGVTIPFDKGFIAHSDGDVALHALTDALLGAAALGDIGKLFPDTDMQYKGADSRVLLREAYRQVQEKGYCVGNVDVTIIAQAPKMRPHIDAMRALIAQDLACDIEQVNVKATTTEKLGFTGRGEGIACEAVALLVRKP","952920","","2C-methyl-D-erythritol 2,4-cyclodiphosphate","Cytoplasm, Periplasm","","
InterPro
IPR003526
Domain
MECDP-synthase
PF02542\"[2-158]TYgbB
TIGR00151\"[3-157]TispF: 2C-methyl-D-erythritol 2,4-cyclodipho
PS01350\"[36-51]TISPF
InterPro
IPR010925
Family
2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
PIRSF005911\"[2-159]T2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
noIPR
unintegrated
unintegrated
G3DSA:3.30.1330.50\"[2-153]Tno description


","No hits to the COGs database.","Significant hit (7.2e-104) to 4/4 blocks of the IPB003526 family, which is described as \"YgbB family\". Interpro entry for IP:IPR003526. IPB003526A 3-13 2.9e-08 IPB003526B 20-64 4.9e-34 IPB003526C 73-121 5.8e-37 IPB003526D 128-155 4.3e-21","Residues 2 to 156 match (1e-58) PD:PD006214 which is described as SYNTHASE 2-C-METHYL-D-ERYTHRITOL 24-CYCLODIPHOSPHATE COMPLETE PROTEOME MECDP-SYNTHASE ISOPRENE MECPS BIOSYNTHESIS LYASE ","","","","","","","","","","","","Fri Jan 10 09:47:46 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01416 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 158 (E-value = 8.8e-99) place AA01416 in the YgbB family which is described as YgbB family (PF02542)","","","","","Kemp LE, Bond CS, Hunter WN. Structure of 2C-methyl-D-erythritol 2,4- cyclodiphosphatesynthase: an essential enzyme for isoprenoid biosynthesis and target for antimicrobial drugdevelopment. Proc Natl Acad Sci U S A. 2002 May 14;99(10):6591-6. PMID: 11997478 Steinbacher S, Kaiser J, Wungsintaweekul J, Hecht S,Eisenreich W, Gerhardt S, Bacher A, Rohdich F. Structure of 2C-methyl-d-erythritol-2,4-cyclodiphosphatesynthase involved in mevalonate-independent biosynthesis ofisoprenoids. J Mol Biol. 2002 Feb 8;316(1):79-88. PMID: 11829504Palmer,K.L. and Munson,R.S. Jr. Cloning and characterization of the genes encoding thehemolysin of Haemophilus ducreyi. Mol. Microbiol. 18(5): 821-830, 1995. PubMed: 8825086.","","Fri Jan 10 09:47:46 2003","1","","","" "AA01417","954088","953396","693","ATGACCTCAACCCGCAAGATTATCGCCGTCGTTCCCGCCGCCGGCATCGGCAGTCGAATGCAGGCGGACAAACCGAAACAATATCTTCACATTCACGGACAGCCGATTTTACAGCACACCTTAAACGTACTGTTGGCTTATCCGCACATCAGCCGAATCGTGCTGGCGGTCGCCGCCGATGATCCTTATATTGACCAACTTAAGCTCAGCCAAAACCCGAAAATTCAGTTGGTGGAAGGCGGTGAAACCCGTGCCGATTCCGTACTCAACGGTTTAAATGCCGTGCAGGACGCGGGCGCCGACGTTTGGGTGATGGTGCACGACGCGGCGCGCCCTTGTTTAACTCACGGCGATTTAGAAAAATTACTTGAAATTCAAGATGATAACGGCGCTATTCTCGCCATTCCGGCAACGGACACCATTAAGCGCGCCCTGCCTTCGCAACAAATTGCCCACACGGAAGATCGTAGCCAATTATGGTTGGCACAAACCCCGCAGTTTTTCCGTGCAGATTTATTACGCGACGCTTTAACCCGCGCCAAACAGCAGCAGTTTGCCGTCACCGACGAAGCTTCCGCCATGGAACTCGCGGGATTTCGACCGCACTTGGTGGCGGGGCGTAGTGATAACATTAAAGTCACCCGCCCGGAAGATTTGGCGCTGGCGGAATTTTACTTAACGAGGAAGACAATA","","","25432","MTSTRKIIAVVPAAGIGSRMQADKPKQYLHIHGQPILQHTLNVLLAYPHISRIVLAVAADDPYIDQLKLSQNPKIQLVEGGETRADSVLNGLNAVQDAGADVWVMVHDAARPCLTHGDLEKLLEIQDDNGAILAIPATDTIKRALPSQQIAHTEDRSQLWLAQTPQFFRADLLRDALTRAKQQQFAVTDEASAMELAGFRPHLVAGRSDNIKVTRPEDLALAEFYLTRKTI","953396","","probable 4-diphosphocytidyl-2C-methyl-D-erthyritol synthase (MEP cytidyltransferase) (MCT)","Cytoplasm, Periplasm","","
InterPro
IPR001228
Domain
4-diphosphocytidyl-2C-methyl-D-erythritol synthase
PF01128\"[7-228]TIspD
TIGR00453\"[8-226]TispD: 2-C-methyl-D-erythritol 4-phosphate c
PS01295\"[104-111]TISPD
InterPro
IPR008233
Family
4-diphosphocytidyl-2-methyl-D-erythritol synthase
PIRSF006765\"[7-229]T4-diphosphocytidyl-2-methyl-D-erythritol synthase
noIPR
unintegrated
unintegrated
G3DSA:3.90.550.10\"[6-227]Tno description


","BeTs to 17 clades of COG1211COG name: 4-diphosphocytidyl-2-methyl-D-erithritol synthaseFunctional Class: IThe phylogenetic pattern of COG1211 is ----k--qvdr-bcefghsnuj-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 5.5e-83) to 6/6 blocks of the IPB001228 family, which is described as \"4-diphosphocytidyl-2C-methyl-D-erythritol synthase\". Interpro entry for IP:IPR001228. IPB001228A 9-41 2.1e-21 IPB001228B 80-92 1.8e-07 IPB001228C 103-112 4.3e-06 IPB001228D 130-142 8.8e-07 IPB001228E 153-177 3.7e-14 IPB001228F 188-219 6.3e-20","Residues 130 to 231 match (2e-09) PD:PD523158 which is described as CYTIDYLYLTRANSFERASE ISOPRENE COMPLETE PROT NUCLEOTIDYLTRANSFERASE 4-PHOSPHATE 2-C-METHYL-D-ERYTHRITOL MCT MEP SYNTHASE ","","","","","","","","","","","","Fri Jan 10 09:56:37 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01417 is paralogously related to AA01539 (2e-05).","","","","","","Residues 7 to 228 (E-value = 4.3e-119) place AA01417 in the IspD family which is described as Uncharacterized protein family UPF0007 (PF01128)","","","","","","","","1","","","" "AA01418","954366","954091","276","ATGCGTTTATTTATTTCTCTTTTAATAGCGGTTTTATTGCTGTTTCAGTACGATTTTTGGTTCGGTAAGAATGGGTATACGGACTACAAAAACACCACCAAAGAAATCGCCGTACACCAGCAGGAAAATGAAAAACTTTCCCAGCGCAATCAAATTATTGCAGCGGAAATCAAAGATTTAAAAGAAGGTGTGGATGCCATCGAAGAGCGCGCCCGTCTGCAGCATGAAATGGTAAAACCGAACGAAACCTTTTATCACATCGTCAAAGAACACAAA","","","10949","MRLFISLLIAVLLLFQYDFWFGKNGYTDYKNTTKEIAVHQQENEKLSQRNQIIAAEIKDLKEGVDAIEERARLQHEMVKPNETFYHIVKEHK","954091","","conserved hypothetical protein","Cytoplasm, Inner membrane","","
InterPro
IPR007060
Family
Septum formation initiator
PF04977\"[11-90]TDivIC
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide
tmhmm\"[4-22]?transmembrane_regions


","No hits to the COGs database.","","Residues 16 to 64 match (1e-13) PD:PD331736 which is described as PROTEOME COMPLETE VC0527 YPO3362 PM1607 YGBQ BU421 ","","","","","","","","","","","","Fri Jan 10 09:58:30 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01418 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 90 (E-value = 3.7e-39) place AA01418 in the DivIC family which is described as Septum formation initiator (PF04977)","","","","","","","","1","","","" "AA01419","954518","955189","672","ATGAAACCCTATTTAATTGCGCCGTCCATTCTTTCCGCCGACCTTGCCCGCTTGGGTGAAGACGTGGAAAAGGTATTAAAGTGCGGTGGCGATGTGATTCATTTTGATGTGATGGATAACCATTATGTGCCGAATTTAACCTTCGGTCCCGCCGTGTGCAAAGCCTTACGCGATTACGGCATCACAGCACCCATTGATGTGCATTTGATGGTGAAACCGGTGGATCGCATTATTCCCGATTTCGCCAAAGCCGGCGCCAGCTACATTACTTTCCACCCCGAAGCATCCGAACATATCGACCGCACTTTACAGCTCATTCGCGACTGCGGTTGCAAATCCGGTTTGGTTTTCAACCCCGCCACGCCGTTAAGCTATTTGGATTATGTGATGGATAAAGTGGATATTATTCTGCTGATGTCGGTGAACCCGGGTTTTGGCGGACAATCTTTCATTCCGGCGACATTGGATAAACTCAAACAGGCGAGAAAACGCATTGATGACAGCGGCTTTGATATTCGTTTGGAAGTGGATGGCGGCGTGAAAGTCTCCAACATCGCCGAGGTGGCACGCGCCGGGGCGGATATGTTTGTTGCCGGTTCGGCGATTTTCGACCAGCCGGATTATCAAAAAGTCATTGATGAAATGCGTCAACAATTAGCCACAGTAGGGAAA","","","24498","MKPYLIAPSILSADLARLGEDVEKVLKCGGDVIHFDVMDNHYVPNLTFGPAVCKALRDYGITAPIDVHLMVKPVDRIIPDFAKAGASYITFHPEASEHIDRTLQLIRDCGCKSGLVFNPATPLSYLDYVMDKVDIILLMSVNPGFGGQSFIPATLDKLKQARKRIDDSGFDIRLEVDGGVKVSNIAEVARAGADMFVAGSAIFDQPDYQKVIDEMRQQLATVGK","955189","","D-ribulose-phosphate-3 epimerase","Cytoplasm","","
InterPro
IPR000056
Family
Ribulose-phosphate 3-epimerase
PTHR11749\"[16-219]TRIBULOSE-5-PHOSPHATE-3-EPIMERASE
PF00834\"[5-206]TRibul_P_3_epim
TIGR01163\"[5-216]Trpe: ribulose-phosphate 3-epimerase
PS01085\"[33-47]TRIBUL_P_3_EPIMER_1
PS01086\"[136-158]TRIBUL_P_3_EPIMER_2
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[4-218]Tno description


","No hits to the COGs database.","Significant hit (1.9e-101) to 4/4 blocks of the IPB000056 family, which is described as \"Ribulose-phosphate 3-epimerase\". Interpro entry for IP:IPR000056. IPB000056A 6-38 6.8e-19 IPB000056B 64-92 4e-21 IPB000056C 106-158 1.3e-39 IPB000056D 174-203 2.8e-18","Residues 5 to 212 match (1e-107) PD:PD003683 which is described as PROTEOME COMPLETE 3-EPIMERASE RIBULOSE-PHOSPHATE ISOMERASE CARBOHYDRATE METABOLISM PPE R5P3E PENTOSE-5-PHOSPHATE ","","","","","","","","","","","","Fri Jan 10 10:00:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01419 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 206 (E-value = 4.7e-135) place AA01419 in the Ribul_P_3_epim family which is described as Ribulose-phosphate 3 epimerase family (PF00834)","","","","","10: Maleszka R, Hanes SD, Hackett RL, de Couet HG, Miklos GL.The Drosophila melanogaster dodo (dod) gene, conserved in humans, is functionally interchangeable with the ESS1 cell division gene of Saccharomyces cerevisiae.Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):447-51.PMID: 8552658","","Fri Jan 10 10:04:23 2003","1","","","" "AA01421","955195","955866","672","ATGACAGGACAATTTAAATTAATCGGTTTTGATTTGGACGGCACGCTGGTGGACAGCCTGCCGGATTTGACGTTATCGGTGAATTCGGCGTTGGCGGAATTCGATTTGCCGCAAGCGCCGGAAGCGTTGGTGCTGACCTGGATTGGCAATGGCGCGCAGATTTTAATCGCCCGCGCCTTGGAATGGGCGACGGCGCAATCGGGTAAAACTTTGACGGAAGCGCAGATTGCCACGCTAAAAGAACGTTTTAATGTGTTTTACGGCGAAAATATTTGTAACCGTAGCCGTTTATTTCCTAACGTCAAAGACACCCTGCAAAAACTCAAAGCCAAAGGCTACCGCTTGGCGGTGGTCACCAATAAACCGACCCAACACACCCGTCCCGTGTTAAAGGCGTTCGGCATTGAAGACTTGTTCGATGAAGTGCTGGGCGGTCAATCCTTACCGGCAATCAAACCGCATCCCGGTCCGTTGTTCTATTTATGTGGCAAATTCGGTTTGTATCCGAAACAAGTGTTGTTCGTGGGCGATTCCCGCAATGACATTATTGCCGCGCACAATGCCGGCTGCCCGGTGGTGGGATTAACCTACGGTTATAACTACAACATCCCGATTGCCGAATCCCACCCGGATTGGGTGTTTGAAGATTTTGCGGAATTGTTGACGATGGTT","","","24625","MTGQFKLIGFDLDGTLVDSLPDLTLSVNSALAEFDLPQAPEALVLTWIGNGAQILIARALEWATAQSGKTLTEAQIATLKERFNVFYGENICNRSRLFPNVKDTLQKLKAKGYRLAVVTNKPTQHTRPVLKAFGIEDLFDEVLGGQSLPAIKPHPGPLFYLCGKFGLYPKQVLFVGDSRNDIIAAHNAGCPVVGLTYGYNYNIPIAESHPDWVFEDFAELLTMV","955866","","phosphoglycolate phosphatase","Cytoplasm","","
InterPro
IPR005833
Family
Haloacid dehydrogenase/epoxide hydrolase
PR00413\"[5-16]T\"[108-121]T\"[139-155]T\"[157-177]THADHALOGNASE
InterPro
IPR005834
Domain
Haloacid dehalogenase-like hydrolase
PF00702\"[5-198]THydrolase
InterPro
IPR006346
Family
2-phosphoglycolate phosphatase, prokaryotic
TIGR01449\"[8-224]TPGP_bact: phosphoglycolate phosphatase, bac
InterPro
IPR006402
Domain
HAD-superfamily hydrolase, subfamily IA, variant 3
TIGR01509\"[43-195]THAD-SF-IA-v3: HAD-superfamily hydrolase, su
InterPro
IPR006439
Family
HAD-superfamily hydrolase, subfamily IA, variant 1
TIGR01549\"[7-189]THAD-SF-IA-v1: HAD-superfamily hydrolase, su
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1000\"[5-224]Tno description
PTHR18901\"[1-224]T2-DEOXYGLUCOSE-6-PHOSPHATE PHOSPHATASE 2


","BeTs to 16 clades of COG0546COG name: Predicted phosphatasesFunctional Class: RThe phylogenetic pattern of COG0546 is aom-k-yq-drlbcefghsnuj--twNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.2e-10) to 4/7 blocks of the PR00413 family, which is described as \"Haloacid dehalogenase/epoxide hydrolase family signature\". Prints database entry for PR:PR00413. PR00413A 5-16 0.08 PR00413D 108-121 0.044 PR00413E 139-155 0.64 PR00413F 157-177 15","Residues 152 to 221 match (6e-11) PD:PD470828 which is described as PROTEOME COMPLETE HYDROLASE PHOSPHATASE PHOSPHOGLYCOLATE PGP METABOLISM CARBOHYDRATE CHROMOSOME FAMILY ","","","","","","","","","","","","Fri Jan 10 10:08:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01421 is paralogously related to AA02446 (3e-10) and AA01201 (4e-07).","","","","","","Residues 5 to 198 (E-value = 6.5e-38) place AA01421 in the Hydrolase family which is described as haloacid dehalogenase-like hydrolase (PF00702)","","","","","Lyngstadaas A, Lobner-Olesen A, Grelland E, Boye E.The gene for 2-phosphoglycolate phosphatase (gph) in Escherichia coli is located in the same operon as dam and at least five other diverse genes.Biochim Biophys Acta. 1999 Oct 18;1472(1-2):376-84.PMID: 10572959","","Fri Jan 10 10:08:28 2003","1","","","" "AA01422","956149","956796","648","ATGATTCGATTTGCAAATGTGAGTAAAGCTTATTTGGGCGGGAAGCCTGCCCTGCAAGGGTTAAGCTTTCATTTACCGGCGGGCAGTATGACCTATCTGGTGGGGCATTCCGGCGCGGGGAAAAGTACCCTGTTAAAATTAATTATGGGCATGGAGCGCGCCAATGGCGGACAAATTTGGTTTAACGGGCACGACATCACCCGTTTATCTCGTCACGAAGTGCCGTTTTTGCGCCGTCAAATCGGCATGGTGCACCAGGATTACCGCTTATTGCCCGATCGTTCGGTATTGGATAACGTCGCTTTACCGTTGATTATTGCCGGGCAACATCCGAAAGATGCGAACAGTCGCGCCTTGGCGGCGTTAGATCGTGTGGGGTTGCGCGATCGAGCCAATCATTTGCCGGCGCATTTGTCCGGTGGGGAACAGCAACGCATTGATATTGCCCGCGCGGTGGTGCATAAGCCACAATTATTGTTGGCGGATGAACCGACCGGCAACTTGGATGGCGCCTTATCCTTAGAAATTTTCAATTTATTTGAAGAATTTAACCGCCTCGGCATGACGGTGTTAATCGCCACCCATGACATCGGCATCGTGCAACAAAAACCGAAACCTTGCTTAGTGCTTGAGCAAGGCTATTTACGC","","","23770","MIRFANVSKAYLGGKPALQGLSFHLPAGSMTYLVGHSGAGKSTLLKLIMGMERANGGQIWFNGHDITRLSRHEVPFLRRQIGMVHQDYRLLPDRSVLDNVALPLIIAGQHPKDANSRALAALDRVGLRDRANHLPAHLSGGEQQRIDIARAVVHKPQLLLADEPTGNLDGALSLEIFNLFEEFNRLGMTVLIATHDIGIVQQKPKPCLVLEQGYLR","956796","","cell division protein E, ABC system ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[138-179]TQ9CKT6_PASMU_Q9CKT6;
PF00005\"[28-213]TABC_tran
PS50893\"[2-216]TABC_TRANSPORTER_2
PS00211\"[138-152]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[27-216]TAAA
InterPro
IPR005286
Family
Cell division ATP-binding protein FtsE
TIGR02673\"[1-214]TFtsE: cell division ATP-binding protein Fts
InterPro
IPR013505
Family
Cell division protein FtsE
TIGR00960\"[1-215]T3a0501s02: Type II (General) Secretory Path
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[1-215]Tno description
PTHR19222\"[2-215]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF36\"[2-215]TFILAMENTATION TEMPERATURE SENSITIVE CELL DIVISION PROTEIN FTSE


","No hits to the COGs database.","Significant hit ( 6.6e-35) to 2/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 17-63 2.6e-19 IPB001140B 135-173 2.8e-14","Residues 76 to 136 match (3e-07) PD:PD267517 which is described as ATP-BINDING COMPLETE PROTEOME ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE PROBABLE PLASMID ","","","","","","","","","","","","Fri Jan 10 10:22:19 2003","","","Thu May 13 11:04:12 2004","Thu May 13 11:04:12 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01422 is paralogously related to AA00415 (1e-39), AA01616 (4e-39), AA00858 (5e-33), AA01524 (2e-31), AA02440 (3e-31), AA02080 (5e-30), AA02718 (4e-28), AA00700 (1e-27), AA02353 (9e-27), AA02324 (1e-25), AA01645 (2e-25), AA01867 (3e-25), AA01656 (3e-25), AA02899 (7e-24), AA01051 (5e-22), AA02805 (4e-21), AA01779 (1e-19), AA01393 (5e-19), AA01509 (9e-19), AA01961 (1e-18), AA02140 (3e-18), AA01757 (4e-18), AA02898 (6e-18), AA01568 (7e-18), AA01824 (1e-17), AA01820 (1e-17), AA01684 (1e-17), AA02606 (3e-17), AA02609 (5e-17), AA02320 (6e-17), AA02152 (2e-16), AA02786 (9e-16), AA02331 (9e-16), AA00933 (9e-16), AA00207 (9e-16), AA00751 (3e-15), AA00799 (6e-15), AA01456 (8e-15), AA01510 (2e-14), AA02550 (4e-14), AA01569 (7e-14), AA01947 (2e-13), AA02573 (2e-12), AA02484 (2e-12), AA01555 (5e-11), AA00591 (9e-11), AA00061 (2e-10), AA02225 (3e-10), AA02146 (2e-08), AA02642 (4e-08), A02145 (5e-08), AA02226 (1e-06), AA00934 (2e-06) and AA01291 (8e-04).","Thu May 13 11:04:12 2004","","","","","Residues 28 to 213 (E-value = 7.8e-62) place AA01422 in the ABC_tran family which is described as ABC transporter (PF00005)","Thu May 13 11:04:12 2004","","","","Gill,D.R., Hatfull,G.F. and Salmond,G.P. A new cell division operon in Escherichia coli Mol. Gen. Genet. 205 (1), 134-145 (1986) PubMed: 3025556 Ramirez-Arcos S, Salimnia H, Bergevin I, Paradis M, Dillon JA. Expression of Neisseria gonorrhoeae cell division genes ftsZ, ftsEand minD is influenced by environmental conditions. Res Microbiol. 2001 Nov;152(9):781-91. PMID: 11763238 Bernatchez S, Francis FM, Salimnia H, Beveridge TJ, Li H, Dillon JA. Genomic, transcriptional and phenotypic analysis of ftsE and ftsX of Neisseria gonorrhoeae. DNA Res. 2000 Apr 28;7(2):75-81. PMID: 10819322 ","","Fri Jan 10 10:22:19 2003","1","","","" "AA01423","956808","957740","933","ATGAATTCCCGTCGTATGCGTTTTCCTTCTGGCGTGCAAAGTGCGTATGTGTTGCGCGCCGTGCTGGCGGATTTGTTGAAACGCAAGTTCGCCACATTGTTGACGGTGTTGGTGATTGCCGTATCGTTCACGATTCCTACCGTCAGTTATCTGCTTAGGAAAAACATTCACCACGCCACCACGCAGTTTTATCCGGAAAGCGAATTGACCGTGTATTTGCATAAAAATCTGTCGGAAGACGATGCCAATTTGGTGGTGGAGAAAATCCGTCAGCAAGAAGGCGTGGAGTCTCTTAATTACATTTCCCGTCAGGAAAGCCTGAATGAATTTCGCCATTGGTCGGGTTTTAGCGAAGAACTGGACGTATTGGACGACAACCCGCTGCCTGCCGTGGTGATGATTAAGCCGACGAAGGCATTTAACGAATCGCAAAAACGTAACGAATTGCGCGCAACGTTAGATAAAATCAAAGGCGTGCAGGAAGTGCGGTTGGATAACGACTGGCTGGAAAAACTGACTGCGCTGACTTGGCTGGTGGCGCATGTGGCGATTTTCTGTACCGTACTCATGGCGCTCGCCGTTTTCTTAGTCATCGGCAACAGCATCCGCGCCGATGTGTACAGCAACCAAGCCAACATTGAAGTGATGAAACTGCTCGGCGCCACCGATCAATTCATCCTCCGCCCGTTCCTCTACACCGGCATGATTTACGCCGTGTTCGGCGGTCTGTTTGCCTGCATTTTCAGCAGCCTGACCATCGGCTACTTCACCGGCGCCGTGAAATACGTCACCGACATTTTCGCCGTCAGCTTCAATTTAAACGGCTTAGGCTTAGTAGAATTTTTATTCCTGCTGATCGTCTGCACCATCATGGGCTACATCGGCGCCTGGTTATCGGCAACGCGCTATATTCAGTTGTTGGATAAGAAAGGT","","","35116","MNSRRMRFPSGVQSAYVLRAVLADLLKRKFATLLTVLVIAVSFTIPTVSYLLRKNIHHATTQFYPESELTVYLHKNLSEDDANLVVEKIRQQEGVESLNYISRQESLNEFRHWSGFSEELDVLDDNPLPAVVMIKPTKAFNESQKRNELRATLDKIKGVQEVRLDNDWLEKLTALTWLVAHVAIFCTVLMALAVFLVIGNSIRADVYSNQANIEVMKLLGATDQFILRPFLYTGMIYAVFGGLFACIFSSLTIGYFTGAVKYVTDIFAVSFNLNGLGLVEFLFLLIVCTIMGYIGAWLSATRYIQLLDKKG","957740","","cell division protein X, ABC system permease","Inner membrane, Cytoplasm","","
InterPro
IPR003838
Domain
Protein of unknown function DUF214, permase predicted
PF02687\"[129-304]TFtsX
InterPro
IPR004513
Family
ABC transporter, FtsX cell division permease
TIGR00439\"[3-311]TftsX: putative protein insertion permease F
noIPR
unintegrated
unintegrated
signalp\"[1-44]?signal-peptide
tmhmm\"[30-50]?\"[177-199]?\"[236-256]?\"[281-301]?transmembrane_regions


","BeTs to 9 clades of COG2177COG name: Cell division proteinFunctional Class: DThe phylogenetic pattern of COG2177 is ---------drlb-efghsn-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 6.5e-09) to 1/2 blocks of the IPB003838 family, which is described as \"DUF214\". Interpro entry for IP:IPR003838. IPB003838A 198-245 6.1e-09","Residues 185 to 304 match (9e-08) PD:PD406731 which is described as DIVISION CELL FTSX PROTEOME TRANSMEMBRANE COMPLETE FTSX HOMOLOG ","","","","","","","","","","","","Fri Jan 10 10:24:45 2003","","","Thu May 13 11:14:15 2004","Thu May 13 10:43:36 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01423 is paralogously related to AA01618 (3e-04).","Thu May 13 10:43:36 2004","","","","","Residues 129 to 304 (E-value = 7e-26) place AA01423 in the FtsX family which is described as Predicted permease (PF02687)","Thu May 13 10:43:36 2004","","","","Schmidt KL, Peterson ND, Kustusch RJ, Wissel MC, Graham B, Phillips GJ, Weiss DS.A predicted ABC transporter, FtsEX, is needed for cell division in Escherichia coli.J Bacteriol. 2004 Feb;186(3):785-93.PMID: 14729705Bernatchez S, Francis FM, Salimnia H, Beveridge TJ, Li H, Dillon JA.Genomic, transcriptional and phenotypic analysis of ftsE and ftsX of Neisseria gonorrhoeae.DNA Res. 2000 Apr;7(2):75-81.PMID: 10819322Kempf MJ, McBride MJ.Transposon insertions in the Flavobacterium johnsoniae ftsX gene disrupt gliding motility and cell division.J Bacteriol. 2000 Mar;182(6):1671-9.PMID: 10692373de Leeuw E, Graham B, Phillips GJ, ten Hagen-Jongman CM, Oudega B, Luirink J.Molecular characterization of Escherichia coli FtsE and FtsX.Mol Microbiol. 1999 Feb;31(3):983-93.PMID: 10048040","","Thu May 13 11:14:15 2004","1","","","" "AA01424","958293","957880","414","ATGGTGCTGGTGGACAGCAATGAAGTGTGCGCCGCGATGAAAGATCTGTTTGAAAACGTGCGTGCAGTGACCGAATTCAGCTACCGCTATGCCGATGACAAACGGGCTTGCGTGTTCATCGGGGTTCGTACCTTAGATGAAGCGGAAAAAGCGAACATCATCGTCGATCTCACACAAAACAGCTTCGATGTGGAAGATATTTCCGACGATGACATCGCCAAAACCCATGTACGCTATTTAATGGGCGGATGGGTCGCCGACCATGGCGAACGCCTTTACACCTTTGAATTCCCGGAACAAAAAGGCGCATTGCTGAAATTCCTCGAAACCCTCGGCACCCGCTGGAAAATTTCCCTGTTCCACGACCGCGCCCACGGGGCGGATTGCGGCAACATTCTTGCCGGCTTCCAGTTA","","","15638","MVLVDSNEVCAAMKDLFENVRAVTEFSYRYADDKRACVFIGVRTLDEAEKANIIVDLTQNSFDVEDISDDDIAKTHVRYLMGGWVADHGERLYTFEFPEQKGALLKFLETLGTRWKISLFHDRAHGADCGNILAGFQL","957880","From GenBank (gi:20140770): This protein catalyzes the formation of alpha-ketobutyrate from threonine in a two-step reaction. The first step is a dehydration of threonine, followed by rehydration and liberation of ammonia.","threonine deaminase (dehydratase)","Cytoplasm","","
InterPro
IPR001721
Domain
Threonine dehydratase, C-terminal
PF00585\"[21-77]T\"[90-138]TThr_dehydrat_C
noIPR
unintegrated
unintegrated
G3DSA:3.40.1020.10\"[21-138]Tno description


","BeTs to 9 clades of COG1171COG name: Threonine dehydrataseFunctional Class: EThe phylogenetic pattern of COG1171 is -o-p-zy-vdrlbcefghsnujx---Number of proteins in this genome belonging to this COG is","","Residues 82 to 138 match (1e-19) PD:PD007543 which is described as THREONINE COMPLETE PROTEOME DEHYDRATASE DEAMINASE LYASE BIOSYNTHETIC PYRIDOXAL BIOSYNTHESIS PHOSPHATE ","","","","","","","","","","","Fri Jan 10 10:40:02 2003","Wed Feb 19 07:53:39 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01424 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 81 to 138 (E-value = 3.4e-05) place AA01424 in the Thr_dehydrat_C family which is described as C-terminal regulatory domain of Threonine dehydratase (PF00585)","","","","","Eisenstein E.Cloning, expression, purification, and characterization of biosynthetic threonine deaminase from Escherichia coli.J Biol Chem. 1991 Mar 25;266(9):5801-7.PMID: 2005118Guillouet S, Rodal AA, An GH, Gorret N, Lessard PA, Sinskey AJ. Metabolic redirection of carbon flow toward isoleucine by expressing a catabolic threonine dehydratase in a threonine-overproducing Corynebacterium glutamicum. Appl Microbiol Biotechnol. 2001 Dec;57(5-6):667-73. PMID: 11778876 ","","Wed Feb 19 07:53:39 2003","1","","","" "AA01426","958715","958347","369","GTGCGTGGGTTCGGTGGCGAAGTGTTGCTACATGACGCCAATTTCGATGAAGCCAAAGCAAAAGTCGTTGAGCTTGCCGAAAAAAAACACATGACCTTTATCACGCCTTTTGATCACCCGCTGGTGATTGCCGGGCAAGGCACGCTCGCTATGGAAATGTTACAGCAAGTGGCAGACTTAGATTATATGTTCGTGCAAGTGTGCGACGGCGGTTTGGCGGCTGGTGTAGCGATTTTATTGAAGCAGTTTATGCCGGACATTAAAGTCATCGGCGTGGAATCGAAAGATTCAGCCTGTCTCAATGCCGCGTTGGAAAAAGGTGAACCGACAGATTTGGCGTACGTGGGCTTATTTGCCGACGGCGTGGCG","","","14407","VRGFGGEVLLHDANFDEAKAKVVELAEKKHMTFITPFDHPLVIAGQGTLAMEMLQQVADLDYMFVQVCDGGLAAGVAILLKQFMPDIKVIGVESKDSACLNAALEKGEPTDLAYVGLFADGVA","958347","","threonine deaminase (dehydratase)","Cytoplasm","","
InterPro
IPR001926
Domain
Pyridoxal-5'-phosphate-dependent enzyme, beta subunit
PF00291\"[1-123]TPALP
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1100\"[1-123]Tno description
PTHR10314\"[1-123]TSER/THR DEHYDRATASE, TRP SYNTHASE
PTHR10314:SF17\"[1-123]TTHREONINE DEHYDRATASE-RELATED


","BeTs to 17 clades of COG1171COG name: Threonine dehydrataseFunctional Class: EThe phylogenetic pattern of COG1171 is -o-p-zy-vdrlbcefghsnujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 7.2e-35) to 2/5 blocks of the IPB001721 family, which is described as \"C-terminal domain of threonine dehydratase\". Interpro entry for IP:IPR001721. IPB001721B 34-56 3.3e-16 IPB001721C 63-98 2.7e-17","Residues 1 to 57 match (2e-07) PD:PD098598 which is described as DEHYDRATASE THREONINE LYASE PROTEOME COMPLETE DEAMINASE PHOSPHATE PYRIDOXAL ISOLEUCINE BIOSYNTHESIS ","","","","","","","","","","","","Wed Feb 19 07:54:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01426 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Eisenstein E. Cloning, expression, purification, and characterization ofbiosynthetic threonine deaminase from Escherichia coli. J Biol Chem. 1991 Mar 25;266(9):5801-7. PMID: 2005118Guillouet S, Rodal AA, An GH, Gorret N, Lessard PA, Sinskey AJ.Metabolic redirection of carbon flow toward isoleucine by expressing a catabolic threoninedehydratase in a threonine-overproducing Corynebacterium glutamicum.Appl Microbiol Biotechnol. 2001 Dec;57(5-6):667-73.PMID: 11778876","","Wed Feb 19 07:50:04 2003","1","","","" "AA01428","959685","958828","858","ATGTCCGCGCGTCGGGGAAAATCGGTGTGTATCGCTACCTCAGGGACGGGCGCCACCAACCTCATCACCAGGCTCGGCGATGCTTTAATGGATTCCATTCCTATCGTCGCCATTACCGGACAGGTCGCTTCCCTGCTCATCGGCACCGATGCCTTTCAGGAAGCGGATGTACTCGGTTTATCCCTTGCCTGCACCAAACACAGTTTCATCGTGCAACATATTGATGAGTTGTCGGAAATTCCCGCCAACGCTTTTGGGATCGCACAAAGCGGCAGACCGGGTCCGGTGCTGGTGGACGTACCGGAAGACGTACAAATTGCACCGACCACGGCGAAGCCAAGAATAAATCCGCCGCCAAAAGCCACCGCACTTCATGAGGAACATTTAACCCAAACTTTAACGTTATTACGCGAAGCACAACGCCCGGTCATCTATATCGGCGGCGTTAGTATGGCAGGAACTGTGCCTGCGTTACGCTATTTTCTGCACAGCACCCAAATGCCAAGCCGTAGTGACCTTAAAAGGCTTGGGTGCCGTCTCCGCCGACGATTCTTATTATTTGGGCATGCTCGGAATGCACGCACCAAAGCCGCCAACTACATCACCCAAGAAGCGGATTTATTACTGGTATTCGGCACCCGCTTTGATGATCGCGTCACCGGCAAACTCGACACCTTCGCCCCGCACGTCAAAGTGATTCATGTGGATATTGACGGTGCCGAATTAGGCAAATTGTCCGAACGTCTGCACAACAATATCTGGATTAAACGGGAAGATCGCCAGCCGGTAAACAGCTTTAAACTGCGCGGTGCATACGCCATGATTTCCAGCCTTTTGCGGAGCAAAAAGCGGCGGGCG","","","32294","MSARRGKSVCIATSGTGATNLITRLGDALMDSIPIVAITGQVASLLIGTDAFQEADVLGLSLACTKHSFIVQHIDELSEIPANAFGIAQSGRPGPVLVDVPEDVQIAPTTAKPRINPPPKATALHEEHLTQTLTLLREAQRPVIYIGGVSMAGTVPALRYFLHSTQMPSRSDLKRLGCRLRRRFLLFGHARNARTKAANYITQEADLLLVFGTRFDDRVTGKLDTFAPHVKVIHVDIDGAELGKLSERLHNNIWIKREDRQPVNSFKLRGAYAMISSLLRSKKRRA","958828","","acetolactate synthase","Cytoplasm","","
InterPro
IPR000634
Binding_site
Serine/threonine dehydratase, pyridoxal-phosphate-binding site
PS00165\"[258-271]TDEHYDRATASE_SER_THR
InterPro
IPR001926
Domain
Pyridoxal-5'-phosphate-dependent enzyme, beta subunit
PF00291\"[244-285]TPALP
InterPro
IPR012000
Domain
Thiamine pyrophosphate enzyme, central region
PF00205\"[129-244]TTPP_enzyme_M
InterPro
IPR012001
Domain
Thiamine pyrophosphate enzyme, N-terminal TPP binding region
PF02776\"[9-113]TTPP_enzyme_N
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.970\"[9-131]Tno description
PTHR18968\"[195-244]TTHIAMINE PYROPHOSPHATE ENZYMES
PTHR18968:SF13\"[195-244]TACETOLACTATE SYNTHASE


","BeTs to 20 clades of COG0028COG name: Thiamine pyrophosphate-requiring enzymes acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylaseFunctional Class: E,HThe phylogenetic pattern of COG0028 is a-mpkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-18) to 2/5 blocks of the IPB000399 family, which is described as \"Thiamine pyrophosphate dependent enzyme\". Interpro entry for IP:IPR000399. IPB000399C 13-36 3.6e-08 IPB000399D 191-220 6.7e-09Significant hit ( 9.9e-07) to 1/3 blocks of the IPB000634 family, which is described as \"Serine/threonine dehydratase pyridoxal-phosphate attachment site\". Interpro entry for IP:IPR000634. IPB000634A 256-270 1e-06","Residues 241 to 283 match (3e-14) PD:PD000323 which is described as COMPLETE PROTEOME SYNTHASE LYASE TRYPTOPHAN PYRIDOXAL PHOSPHATE CYSTEINE BIOSYNTHESIS THREONINE ","","","","","","","","","","","","Fri Jan 10 10:55:08 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01428 is paralogously related to AA02800 (4e-10).","","","","","","Residues 128 to 263 (E-value = 2.4e-13) place AA01428 in the TPP_enzyme_M family which is described as Thiamine pyrophosphate enzyme, central domain (PF00205)","","","","","Lopes JM, Soliman N, Smith PK, Lawther RP.Transcriptional polarity enhances the contribution of the internal promoter, ilvEp, in the expression of the ilvGMEDA operon in wild-type Escherichia coli K12.Mol Microbiol. 1989 Aug;3(8):1039-51.PMID: 2691839","","Fri Jan 10 10:55:08 2003","1","","","" "AA01429","959852","959721","132","ATGAACGGTGCAAATTTAATAATCGAGTGCTTAAAAGCACATAATGTGGACACCATTTTCGGCTTCCCGGCGGCGCCATCATGCCAACCTACGATGCCATTTATGATTCCGGTTAGATCATCTGCTTTGTCG","","","4674","MNGANLIIECLKAHNVDTIFGFPAAPSCQPTMPFMIPVRSSALS","959721","","conserved hypothetical protein","Periplasm, Cytoplasm","This sequence is similar to gi|23467934, a predicted thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase] from Haemophilus somnus 129PT.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 17:08:23 2004","Thu Feb 26 17:08:23 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No sequence paralogous to this sequence was found.AA01429 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 17:08:23 2004","","","","","","","","","","","","","1","","","" "AA01431","959996","960811","816","ATGCAAAAACTGCCTTATCGCGCCATCGTTTCTGACATGGACGGCACGTTGCTCAACGGACATCATGTGGTGGGCGATTTTACCGCACAAACCCTGGAATGCTTATATGACAACAAGGTGGACATTATTCTTGCTACGGGGCGTAACTATTTTGACGTGTCGAGTATTTTGAAGAAAACCAAGGTGAAAGAGGCGGTGCTGATTACCTCAAACGGCGCGCAGGCGCATAATTTGCAAGGCGAGTTGCTGCTCAATAATTTCCTGCCTGAAAGCATTGCCTATGAAATCATGAACCTTCCCTTTGACGATACGCGGGTTTGCGTGAACAGTTATCAGGCGGAAGGCTGGTTTATCAATAAAGATATTCCCGAGCTTTATAAATATCATAAAGATTCCGGTTTTGTTTACGACGTGGTTGATTTTAAACAACATCACGGCAGAGATACGGAAAAAGTCTTTTTTATCGGACGCACACCGGCGGATTTGGTGGCACTGGAAGAACAGTTACGCACACGTTTTGGCACGCTTGCCAACATTACTTATTCTACACCGATTTGCTTGGAAGTCATGGGGGAAGGCGTATCGAAGGCTTCCACGCTTGCTCAAGTCGTGCAACAAAAAGATTATGATTTGCAGGATTGCATCGCTTTCGGTGATGGTATGAATGATGTGGAAATGTTAACGGAAGTGGGCAAAGGCTGCGTTATGGGGAACGCCGATCCTCGTCTGAAACAAGCCGCGCCGCAACTGGAAGTTATCGGTCGCCACGGACATGAAGCAGTGGCATCGTATTTGCGTGCCATTTACGGCATTTAC","","","30367","MQKLPYRAIVSDMDGTLLNGHHVVGDFTAQTLECLYDNKVDIILATGRNYFDVSSILKKTKVKEAVLITSNGAQAHNLQGELLLNNFLPESIAYEIMNLPFDDTRVCVNSYQAEGWFINKDIPELYKYHKDSGFVYDVVDFKQHHGRDTEKVFFIGRTPADLVALEEQLRTRFGTLANITYSTPICLEVMGEGVSKASTLAQVVQQKDYDLQDCIAFGDGMNDVEMLTEVGKGCVMGNADPRLKQAAPQLEVIGRHGHEAVASYLRAIYGIY","960811","","conserved hypothetical protein (possible hydrolase)","Cytoplasm","","
InterPro
IPR000150
Family
Cof protein
TIGR00099\"[8-265]TCof-subfamily: Cof-like hydrolase
PS01228\"[8-19]?COF_1
PS01229\"[217-239]TCOF_2
InterPro
IPR006379
Family
HAD-superfamily hydrolase, subfamily IIB
TIGR01484\"[8-236]THAD-SF-IIB: HAD-superfamily hydrolase, subf
InterPro
IPR013200
Domain
HAD superfamily hydrolase-like, type 3
PF08282\"[9-265]THydrolase_3
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1000\"[2-268]Tno description
PTHR10000\"[187-253]TPHOSPHOSERINE PHOSPHATASE


","No hits to the COGs database.","Significant hit ( 6.1e-29) to 3/3 blocks of the IPB000150 family, which is described as \"Cof protein\". Interpro entry for IP:IPR000150. IPB000150A 5-19 3.9e-06 IPB000150B 39-48 4.6 IPB000150C 215-247 1.5e-19","Residues 211 to 269 match (5e-20) PD:PD001342 which is described as PROTEOME COMPLETE HYDROLASE HAD FAMILY COF SUPERFAMILY THE DEHALOGENASE-LIKE YIGL ","","","","","","","","","","","","Fri Jan 10 10:57:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01431 is paralogously related to AA00316 (1e-14), AA00482 (1e-14) and AA01216 (2e-07).","","","","","","","","","","","","","","1","","","" "AA01432","961826","960855","972","TTGTGTTTTACGCCTTGGTTAAACAGCTTAGTGCCGCTGCAGAGAACCGCCATGAATAACACCGAACTGTTGCAATTTGCCGCGCAATTTCCGTTGCAATATCTTCAGGGCGAACGCCAATGCCGCTTGGCTTATCGGCATTTTATGCACCACCCCGCCGCCCGTAAATTAGTGATTATGGTGAACGGCAGGGCGGAAAACCTGCTGAAATGGACGGAAATTGCGCAGGATTTTTATCATCAAGGCTACGATGTGTTACTGTTTGATCATCGCGGGCAGGGTTATTCGCAACGTTTATTGAAAGATGGCGAGAAAGGGCATTTAGACGAATTTCGGTTTTACCCGCAGGACATGGCAAAAATCATTGAAAATCTGACCGCACTTTATCCTTATCCGCAGCAATACCTGATCGCCCATTCCCTCGGCGCGCTGATTTCCGCCTATTATTTGGCGAATTTTGATCATCGTATTGAACGGGCAGTCTTCTCCGCGCCCTTTTTCGGGGGGCCACTCAAAAAGCCGACGCGCGACGAATTATTGCTGAATTTAATGATGTTATGGGGACAAGGTGAACGTTATGTGTTCGGCAAAAGCGCCTACAAGCCAGTGGATACGGCACAGAACGAGTTAAGTCACAGTGTGGCGCGGATGCAATGGATGAATGACGTGAATCGGGACAACCCGTCAATTCGACTGGGCGGACCGACCTTCCGTTGGGTACATTTGTGTCTCGCCGCCATTAAGCGTCTGCCGAAAATTCTGCCTCGTATCGAAACGCCGGTGTTAGTGTTGGAGGCCGAACAGGAAAAGATCGTGAACAATAAAACGCTGAAAAAACTGACCGCACTTTTGCCCCACGGAGAGCGGCGAAAAATTCACGGCGCCAAACACGAAATTCTGTTTGAAAGCGATGAAATTCGTACCCCGGTACTACAACGCATTTATGCGTTTTTTAATCCAAACAAGCACGCA","","","37679","LCFTPWLNSLVPLQRTAMNNTELLQFAAQFPLQYLQGERQCRLAYRHFMHHPAARKLVIMVNGRAENLLKWTEIAQDFYHQGYDVLLFDHRGQGYSQRLLKDGEKGHLDEFRFYPQDMAKIIENLTALYPYPQQYLIAHSLGALISAYYLANFDHRIERAVFSAPFFGGPLKKPTRDELLLNLMMLWGQGERYVFGKSAYKPVDTAQNELSHSVARMQWMNDVNRDNPSIRLGGPTFRWVHLCLAAIKRLPKILPRIETPVLVLEAEQEKIVNNKTLKKLTALLPHGERRKIHGAKHEILFESDEIRTPVLQRIYAFFNPNKHA","960855","","lysophospholipase L2","Inner membrane, Cytoplasm","","
InterPro
IPR000073
Domain
Alpha/beta hydrolase fold-1
PF00561\"[83-313]TAbhydrolase_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1820\"[39-318]Tno description
PTHR11614\"[56-319]TPHOSPHOLIPASE-RELATED
PTHR11614:SF2\"[56-319]Tgb def: Lysophospholipase L2 (EC 3.1.1.5) (Lecithinase B)


","No hits to the COGs database.","Significant hit ( 7.4e-05) to 2/3 blocks of the PR00793 family, which is described as \"Prolyl aminopeptidase (S33) family signature\". Prints database entry for PR:PR00793. PR00793B 85-96 0.043 PR00793C 136-150 0.97","Residues 55 to 321 match (7e-10) PD:PD421834 which is described as PROTEOME COMPLETE LYSOPHOSPHOLIPASE L2 ","","","","","","","","","","","","Fri Jan 10 11:02:26 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01432 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 83 to 313 (E-value = 5.4e-34) place AA01432 in the Abhydrolase_1 family which is described as alpha/beta hydrolase fold (PF00561)","","","","","Cox GM, McDade HC, Chen SC, Tucker SC, Gottfredsson M, Wright LC, Sorrell TC, Leidich SD, Casadevall A, Ghannoum MA, Perfect JR.Extracellular phospholipase activity is a virulence factor for Cryptococcus neoformans.Mol Microbiol. 2001 Jan;39(1):166-75.PMID: 11123698Karasawa K, Kudo I, Kobayashi T, Sa-Eki T, Inoue K, Nojima S.Purification and characterization of lysophospholipase L2 of Escherichia coli K-12.J Biochem (Tokyo). 1985 Oct;98(4):1117-25.PMID: 390844Kobayashi T, Kudo I, Karasawa K, Mizushima H, Inoue K, Nojima S.Nucleotide sequence of the pldB gene and characteristics of deduced amino acid sequence of lysophospholipase L2 in Escherichia coli.J Biochem (Tokyo). 1985 Oct;98(4):1017-25.PMID: 3908445","","Mon Feb 17 14:57:12 2003","1","","","" "AA01434","963081","961771","1311","ATGCCGATGATAAAGTGCGGTCATTTTTTTAAGCGTTTTTTGCCGACGATGAAGATGACAACATACAAACTCCCCCTGGCAGGGTTTATTAACGCAACGCTGGTGTTCTTTTTTACCTGCCTGCTTGTGTTGAAACACGGCTATAACTATACCCCGGCAATCTTGTCGCTGATGGGCGTAATTTTTTTCATTTACCGCCAATTATGCAAACCGAAGGGCAATCTCACCTATGATGGCAATGAGAAATGGTTTGTTGCCACCCTGCTCTTTTACGTGCTGCTCTTTGCCCTTTCGATTCTGTACCATCAGGGCAAAATTCGGGAATTTGATAACCCGAGCCGCATTCTCTTTTTTCTGACCTTGTTGCCGTTACTGGCGCATTATCCGATATGTTTTAATTGGCTTTTACACGCCATTCCATGGGGCAGCCTGATTGCGGGCATCACCGCTATTATTCATCGTTTTATCTTGAATTATTACATGGCATTTGAGTATCAAATGCACATTCAGTCCGGCGATATTGCCATGTCGTTGGGCATGTTTTCCCTGGCGATTAGCTTTTACTTTTTCATCAAAAGGCAATATCACTTCGGTGCCTTATATTTTGTATTCAGTCTGATGGGCGTGTTCGCCAGTTTGTTATCCACCGCGCGCGGCGGCTGGATTGGTATCCCTTTTGTTCTCCTGTTAATCCTCTTTGCTTATCGTCGTTATTTATCGAAAAAATTCGTCGCCGGCTTTTTTATTGTGCTTGCCCTGATTGTAACAACCGTTGCGATGTTGCCAAATACCAAAATTAAAGAACGCATTGCCGCCGCAGAATACGACATCATCGCCTATTTTCAACAAAATAACGGTTCTACCTCCGTCGGCGCCCGTTTTGATATGTGGAAAAGCGTGATGTTAATGACGCAGGAAAAACCGATTTTCGGTTGGGGCGTACAAGGGGTCAGCGAAAAACGCAAACTGCAATATGAGCAAGGTTTGATAAGCCAATATGCCGCCGCCTTTAACCACGCGCACAACCAATATTTTGATGATTTATCCAAACGCGGCGCATTAGGTTTACTCGCCTTACTCGGCGTATTTTTAGTGCCGTTGCGTTTCTTTATACGGCATCTCAAAAGCGTCGATTTAGAACTGAAACTCGTTTCGTTGTTAGGTGCGGTTCATATTGTCTCCGTGATGTTCTACTGTTTCAGCCAAGGCTTTTTCAGCCATAACTCGGGCAATATTTTCTATTTTTTCCCGGTGATTGTGTTTTACGCCTTGGTTAAACAGCTTAGTGCCGCTGCAGAGAACCGCCATGAA","","","50166","MPMIKCGHFFKRFLPTMKMTTYKLPLAGFINATLVFFFTCLLVLKHGYNYTPAILSLMGVIFFIYRQLCKPKGNLTYDGNEKWFVATLLFYVLLFALSILYHQGKIREFDNPSRILFFLTLLPLLAHYPICFNWLLHAIPWGSLIAGITAIIHRFILNYYMAFEYQMHIQSGDIAMSLGMFSLAISFYFFIKRQYHFGALYFVFSLMGVFASLLSTARGGWIGIPFVLLLILFAYRRYLSKKFVAGFFIVLALIVTTVAMLPNTKIKERIAAAEYDIIAYFQQNNGSTSVGARFDMWKSVMLMTQEKPIFGWGVQGVSEKRKLQYEQGLISQYAAAFNHAHNQYFDDLSKRGALGLLALLGVFLVPLRFFIRHLKSVDLELKLVSLLGAVHIVSVMFYCFSQGFFSHNSGNIFYFFPVIVFYALVKQLSAAAENRHE","961771","","conserved hypothetical protein (possible o-antigen ligase)","Inner membrane, Cytoplasm","","
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[143-269]Tno description
InterPro
IPR007016
Family
O-antigen polymerase
PF04932\"[287-357]TWzy_C
noIPR
unintegrated
unintegrated
signalp\"[1-47]?signal-peptide
tmhmm\"[24-44]?\"[49-69]?\"[83-101]?\"[116-136]?\"[142-162]?\"[171-191]?\"[201-233]?\"[243-261]?\"[351-371]?\"[383-401]?\"[411-431]?transmembrane_regions


","BeTs to 6 clades of COG3307COG name: Lipid A core - O-antigen ligase and related enzymesFunctional Class: MThe phylogenetic pattern of COG3307 is -------------cefghsnujx---Number of proteins in this genome belonging to this COG is","","Residues 47 to 169 match (1e-09) PD:PD415446 which is described as PROTEOME COMPLETE TRANSMEMBRANE HI0874 PM1862 ","","","","","","","","","","","","Fri Jan 10 11:15:26 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01434 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 287 to 357 (E-value = 1.2e-16) place AA01434 in the Wzy_C family which is described as O-Antigen Polymerase (PF04932)","","","","","","","","1","","","" "AA01436","964197","963121","1077","ATGGCTAAATTATTAGATATCGTAAAACCGGGCGTACTTACCGGTGAAGATGTACAAAAAGTATTCGCATACGCAAAGGAACACGGCTTTGCCATTCCCGCCGTGAACTGCGTCGGTTCCGATTCTGTGAATGCCGTATTGGAAACCGCCGCCCGTGTAAAAGCGCCGGTCATCATTCAGTTCTCTAACGGCGGTGCGGCATTCTACGCAGGTAAAGGCATTAAACCCGCCGGCGGCGCCCGTCCTGACGTATTAGGCGCCATTGCCGGTGCGAAACATGTTCATGCTTTAGCCAAAGAATACGGCGTGCCGGTGATTTTACACACCGACCACGCAGCGAAAAAATTACTGCCTTGGATAGACGGCTTACTTGATGCCGGTGAAAAACACTTCGCCGAAACCGGACGCCCGCTGTTCTCCTCCCACATGATTGACCTTTCCGAAGAACCGATGGAAGAAAACATGGCAATCTGCCGTGAATACCTTGCTCGTATGAGCAAAATGGGCATGACCCTTGAAATCGAAATCGGTATCACCGGCGGTGAAGAAGACGGCGTGGATAACTCCGATGTGGATGAATCCCGTCTTTACACCCAACCGTCCGACGTGCTTTATGTTTACGACCAATTACACCCGGTAAGCCCGAACTTCACCGTAGCGGCGGCATTTGGTAACGTACACGGTGTGTACAAGCCGGGTAATGTGAAATTAAAACCGTCTATTCTGGGGGCAAGCCAAGAATTCGTGGCGAAAGAACGTAACCTTCCGGCAAAACCGATTAACTTCGTCTTCCACGGCGGTTCCGGTTCCAGCCGCGAAGAAATCCGTGAAGCCATCGGTTACGGTGCAATTAAAATGAATATCGACACCGACACTCAATGGGCATCCTGGAATGGTATTTTAAATTTCTACAAAGCCAATGAAGCGTATTTGCAAGGTCAACTAGGCAACCCGTCAGGTCCTGATGCACCGAACAAAAAATACTACGATCCGCGCGTTTGGTTACGCAAAATGGAAGAATCCATGTCTAAACGTTTAGAGCAATCTTTCGAAGACTTAAACTGCGTAGATGTTTTA","","","39039","MAKLLDIVKPGVLTGEDVQKVFAYAKEHGFAIPAVNCVGSDSVNAVLETAARVKAPVIIQFSNGGAAFYAGKGIKPAGGARPDVLGAIAGAKHVHALAKEYGVPVILHTDHAAKKLLPWIDGLLDAGEKHFAETGRPLFSSHMIDLSEEPMEENMAICREYLARMSKMGMTLEIEIGITGGEEDGVDNSDVDESRLYTQPSDVLYVYDQLHPVSPNFTVAAAFGNVHGVYKPGNVKLKPSILGASQEFVAKERNLPAKPINFVFHGGSGSSREEIREAIGYGAIKMNIDTDTQWASWNGILNFYKANEAYLQGQLGNPSGPDAPNKKYYDPRVWLRKMEESMSKRLEQSFEDLNCVDVL","963121","","fructose-bisphosphate aldolase class II","Cytoplasm","","
InterPro
IPR000771
Family
Ketose-bisphosphate aldolase, class-II
PD002376\"[10-350]TQ7VMV1_HAEDU_Q7VMV1;
PIRSF001359\"[13-359]TFructose-bisphosphate aldolase II
PF01116\"[14-359]TF_bP_aldolase
TIGR00167\"[13-359]TcbbA: ketose-bisphosphate aldolases
PS00602\"[101-112]TALDOLASE_CLASS_II_1
PS00806\"[172-183]TALDOLASE_CLASS_II_2
InterPro
IPR006411
Family
Fructose-bisphosphate aldolase, class II, yeast/E. coli subtype
TIGR01520\"[4-359]TFruBisAldo_II_A: fructose-bisphosphate aldo
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[2-359]Tno description


","BeTs to 16 clades of COG0191COG name: Fructose/tagatose bisphosphate aldolaseFunctional Class: GThe phylogenetic pattern of COG0191 is ------yqvdrlbcefgh-nuj--twNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.9e-92) to 6/6 blocks of the IPB000771 family, which is described as \"Fructose-bisphosphate aldolase, class-II\". Interpro entry for IP:IPR000771. IPB000771A 25-63 5e-22 IPB000771B 103-114 4.8e-05 IPB000771C 150-186 1.9e-21 IPB000771D 219-231 2.9e-07 IPB000771E 264-295 7.2e-21 IPB000771F 325-342 6.6e-09","Residues 2 to 359 match (5e-196) PD:PD002376 which is described as ALDOLASE PROTEOME COMPLETE FRUCTOSE-BISPHOSPHATE LYASE ZINC GLYCOLYSIS FRUCTOSE-16-BISPHOSPHATE II TAGATOSE-BISPHOSPHATE ","","","","","","","","","","","","Fri Jan 10 11:18:19 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01436 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 14 to 359 (E-value = 1.5e-217) place AA01436 in the F_bP_aldolase family which is described as Fructose-bisphosphate aldolase class-II (PF01116)","","","","","Berry,A. and Marshall,K.E. Identification of zinc-binding ligands in the class IIfructose-1,6-bisphosphate aldolase of Escherichia coli. FEBS Lett. 318(1): 11-16, 1993 PubMed: 8436219. Alefounder,P.R. and Perham,R.N Identification, molecular cloning and sequence analysis of a genecluster encoding the class II fructose 1,6-bisphosphate aldolase,3-phosphoglycerate kinase and a putative second glyceraldehyde3-phosphate dehydrogenase of Escherichia coli. Mol. Microbiol. 3(6): 723-732, . 1989. PubMed: 2546007. Alefounder,P.R., Baldwin,S.A., Perham,R.N. and Short,N.J. Cloning, sequence analysis and over-expression of the gene for theclass II fructose 1,6-bisphosphate aldolase of Escherichia coli.Biochem. J. 257(2): 529-534, 1989. PubMed: 2649077.","","Fri Jan 10 11:18:19 2003","1","","","" "AA01437","965425","964265","1161","ATGTCAGTAATTAAAATGACCGATTTAGATTTGAACGGTAAACGCGTATTTATCCGAGCCGACCTGAATGTGCCGGTAAAAGACGGTAAAATCACTTCCGATGCGCGTATTCGTGCCACCATCCCAACCTTAAAATTAGCCTTGGAAAAAGGCGCCAAAGTGATGGTTACCTCCCACTTAGGTCGTCCGACCGAAGGTGAATTCAAACCTGAAGATTCCCTCCAACCCGTTGTTGATTATTTAAACGAACATCTTGATGTGCCGGTACGTTTAGTACGTGATTACCTCGACGGCGTAGATGTTAAACCCGGCGAAATCGTTGTATTGGAAAACGTTCGCATGAACAAAGGCGAAAAGAAAAACGATCCTGAATTAGGCAAAAAATACGCCGCACTTTGTGATGTATTCGTGATGGATGCGTTCGGTACGGCTCACCGCGCCCAAGCGTCCACTTACGGCGTTGCCGAATTCGCCCCGATTGCCTGTGCCGGCCCATTACTTGCGGCTGAATTGGATGCCCTCGGTAAAGCGTTAAAAGAACCTGCACGTCCGATGGTGGCGATTGTAGGCGGTTCTAAAGTCTCCACCAAATTGGAAGTATTGAACTCCCTGTCTAAAATTGCCGACCAAATTATCGTAGGCGGCGGTATCGCCAACACCTTCATCGCCGCAGCCGGTCATAATGTAGGTAAATCCTTATACGAGGCGGATTTAATCCCGGTTGCTAAAGAACTCGCGGCAAGCACCGATATTCCTGTGCCGGTTGATGTTCGCGTCGGCACCGAATTCTCCGAAACCGCACCGGCAACAGAAAAATCCGTGACCGAAGTAAAAGATGATGAATCCATTTTCGACATCGGCGACAAATCCGCAGAGCAACTGGCAGACATCATCAAAAACGCCAAAACCGTATTATGGAACGGCCCGGTGGGCGTGTTTGAATTCCCGAACTTCCGCAAAGGAACTGAAATCATTTCTCGTGCTATCGCCAACAGTGACGCGTTCTCCATTGCGGGCGGCGGTGATACGTTAGCGGCTATCGATCTTTTCGGTATTGCAGATAAAATCTCTTACATCTCAACCGGTGGTGGTGCGTTCTTAGAATTCGTCGAAGGTAAAGTCTTACCAGCGGTAGAAATTCTTGAAAAACGCGCGAAAAAC","","","41158","MSVIKMTDLDLNGKRVFIRADLNVPVKDGKITSDARIRATIPTLKLALEKGAKVMVTSHLGRPTEGEFKPEDSLQPVVDYLNEHLDVPVRLVRDYLDGVDVKPGEIVVLENVRMNKGEKKNDPELGKKYAALCDVFVMDAFGTAHRAQASTYGVAEFAPIACAGPLLAAELDALGKALKEPARPMVAIVGGSKVSTKLEVLNSLSKIADQIIVGGGIANTFIAAAGHNVGKSLYEADLIPVAKELAASTDIPVPVDVRVGTEFSETAPATEKSVTEVKDDESIFDIGDKSAEQLADIIKNAKTVLWNGPVGVFEFPNFRKGTEIISRAIANSDAFSIAGGGDTLAAIDLFGIADKISYISTGGGAFLEFVEGKVLPAVEILEKRAKN","964265","","phosphoglycerate kinase","Cytoplasm","","
InterPro
IPR001114
Family
Adenylosuccinate synthetase
SM00788\"[77-222]Tno description
InterPro
IPR001576
Family
Phosphoglycerate kinase
PR00477\"[10-26]T\"[31-53]T\"[104-119]T\"[132-154]T\"[163-185]T\"[186-205]T\"[303-328]T\"[336-347]T\"[359-376]TPHGLYCKINASE
PIRSF000724\"[3-387]TPhosphoglycerate kinase
PTHR11406\"[3-385]TPHOSPHOGLYCERATE KINASE
PF00162\"[2-381]TPGK
PS00111\"[15-25]TPGLYCERATE_KINASE
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1260\"[2-166]Tno description
G3DSA:3.40.50.1270\"[173-384]Tno description


","BeTs to 25 clades of COG0126COG name: 3-phosphoglycerate kinaseFunctional Class: GThe phylogenetic pattern of COG0126 is aompkzyqvdrlbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is","Significant hit (1.5e-135) to 8/8 blocks of the IPB001576 family, which is described as \"Phosphoglycerate kinase family\". Interpro entry for IP:IPR001576. IPB001576A 10-36 2.3e-17 IPB001576B 54-63 0.00074 IPB001576C 104-118 9.2e-07 IPB001576D 134-154 2.3e-16 IPB001576E 163-209 2.5e-24 IPB001576F 243-263 0.0014 IPB001576G 284-322 9.4e-25 IPB001576H 337-381 3.1e-29","Residues 285 to 382 match (1e-08) PD:PD565936 which is described as PROTEOME KINASE PHOSPHOGLYCERATE COMPLETE ","","","","","","","","","","","","Fri Jan 10 11:21:57 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01437 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 385 (E-value = 1.7e-198) place AA01437 in the PGK family which is described as Phosphoglycerate kinase (PF00162)","","","","","Alefounder,P.R. and Perham,R.N. Identification, molecular cloning and sequence analysis of a genecluster encoding the class II fructose 1,6-bisphosphate aldolase,3-phosphoglycerate kinase and a putative second glyceraldehyde3-phosphate dehydrogenase of Escherichia coli. Mol. Microbiol. 3(6): 723-732. 1989. PubMed: 2546007. Bond CS, White MF, Hunter WN. Mechanistic implications for Escherichia coli cofactor-dependentphosphoglycerate mutase based on the high-resolution crystal structure of a vanadate complex. J Mol Biol. 2002 Mar 8;316(5):1071-81. PMID: 11884145 Bond CS, White MF, Hunter WN. High resolution structure of the phosphohistidine-activated form of Escherichia coli cofactor-dependent phosphoglycerate mutase. J Biol Chem. 2001 Feb 2;276(5):3247-53. PMID: 11038361 ","","Wed Jan 29 13:00:16 2003","1","","","" "AA01438","966233","965541","693","ATGAACGAAAAACGTATGTTGCTGCTGTCATTTTTTGTGGTGGCGTTTTTAATGTTTTTACTTGCCGGCTGGTATTATTTTTCCAAGCAGAAACAAGCGGTTGGCGTGTTAATCGATCGGGATTACGATTACATCATGAAAAACGATCCCATCGGGCAAAATAAAAAGGTCCGCACCGATTATTACACGCTGGTGTTGTCCTGGTCACCGGCGTTTTGTGAGCGTCAACGTAAGCAATACGGCGATGACTTACCGAATTCCTTGCAATATCAATGCGGTTTGACTCAACAATTCGGTTGGATTGTACACGGATTATGGTCACAAAACGAACAGGCACGACGGGTTTCCGATCATCCGCGTTTCTGTCAGGGCGATTTGCCGAAATTGCCGCAGGAGCTCATCGAACAATATCTGCCAGAGATGCCCGGCGCCAATTTAATTCAGGGCGAATGGGAAAAACACGGTTCGTGTATGTTCAACAATGCGCAGGATTATTTGGAAAAGATCAAAAATTTATACCGCACTTTAAAGCTGCCGAACTACGAATTAAGCCGTAACGAGTTGTTTACCTGGATAAAGAAAAATAATCCGCAACTCAAAGGTCGCTATCTTGGCGCGGCGCGTAACGAATTATTCATTTGTTACGGCTTAGATTGGCAACCGATTGATTGTCCGCGCAATCGCACCGGTTAT","","","27393","MNEKRMLLLSFFVVAFLMFLLAGWYYFSKQKQAVGVLIDRDYDYIMKNDPIGQNKKVRTDYYTLVLSWSPAFCERQRKQYGDDLPNSLQYQCGLTQQFGWIVHGLWSQNEQARRVSDHPRFCQGDLPKLPQELIEQYLPEMPGANLIQGEWEKHGSCMFNNAQDYLEKIKNLYRTLKLPNYELSRNELFTWIKKNNPQLKGRYLGAARNELFICYGLDWQPIDCPRNRTGY","965541","","conserved hypothetical protein (possible ribonuclease )","Periplasm, Cytoplasm","","
InterPro
IPR001568
Family
Ribonuclease T2
G3DSA:3.90.730.10\"[55-226]Tno description
PF00445\"[59-230]TRibonuclease_T2
PS00531\"[146-157]?RNASE_T2_2
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide
tmhmm\"[7-27]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.3e-08) to 3/3 blocks of the IPB001568 family, which is described as \"Ribonuclease T2 family\". Interpro entry for IP:IPR001568. IPB001568A 100-109 0.1 IPB001568B 146-157 0.00072 IPB001568C 207-216 50","Residues 1 to 59 match (2e-11) PD:PD384667 which is described as PROTEOME COMPLETE PM1859 ","","","","","","","","","","","","Thu Jan 23 10:56:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01438 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 59 to 230 (E-value = 3.6e-07) place AA01438 in the Ribonuclease_T2 family which is described as Ribonuclease T2 family (PF00445)","","","","","","","","1","","","" "AA01439","966301","966558","258","GTGGCACTATTCATCACTGACAAATGCACAAACTGCGATATGTGCCTGCCGGAATGCCCGAATGAAGCCATTTCAATCGGCGATGAGATCTATGTCATCGATCCTAATTTATGCACCGAATGTGTCGGTCACTACGACACCCCAACCTGCCAAAAAGTTTGCCCCATCAGCAAATGTATCATCACCGATCCCGACCATATCGAAACCGAAGAGCAGCTTTGGGAACGCTTTGTGCTGATTCATCACGCGGATAAGTTG","","","9735","VALFITDKCTNCDMCLPECPNEAISIGDEIYVIDPNLCTECVGHYDTPTCQKVCPISKCIITDPDHIETEEQLWERFVLIHHADKL","966558","","probable ferredoxin (fdx-2)","Cytoplasm, Periplasm","","
InterPro
IPR001450
Domain
4Fe-4S ferredoxin, iron-sulfur binding
PR00353\"[2-13]T\"[14-25]T4FE4SFRDOXIN
PF00037\"[2-25]TFer4
PS00198\"[9-20]T4FE4S_FERREDOXIN
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.20\"[2-84]Tno description


","BeTs to 15 clades of COG1145COG name: Ferredoxin 2Functional Class: CThe phylogenetic pattern of COG1145 is a-mpkz--vd--bcefghsnuj----Number of proteins in this genome belonging to this COG is","","Residues 61 to 86 match (1e-07) PD:PD051290 which is described as PROTEOME COMPLETE PM1858 ","","","","","","","","","","","","Fri Jan 10 11:31:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01439 is paralogously related to AA01807 (3e-04) and AA02677 (6e-04).","","","","","","Residues 2 to 25 (E-value = 1e-05) place AA01439 in the Fer4 family which is described as 4Fe-4S binding domain (PF00037)","","","","","","","","1","","","" "AA01441","967703","966630","1074","ATGAATCAACATTCAAATAAACCAACCTTCAAATCCACAAATAAGACTTTCCAAGAAACATCTTTCAATGAACGCAGCGTCGGTGCAGACCGCAAAAAACGCGATAAAAACCGACTGCACTTTAACGCACCGAATGCCGCACGCCCCGAATTCAAAAAAAGCCAAGGCAAGAATCCACCCTTCAAGCGTGCCGACAGCCAAGAAAAAACCTTGCGCATTTCCGAAAGCACTATGAAAAAAGCCGGCGGTGCGGAAGGCGGCGTGAAAGTGATGGTGAAAAGCAGCCAATTCGACGACAAACCGAGAGAGAAAAAAACCGGTCCGTTGTCGCCGCGCGCACCGGAAAAAATCAAGAAAAATCGTGCCGAAGAAATGAAGGTTTATGGTGAAAATGCCTGTTTAGCCCTTTTTGAACAACGTCCCGCCAGTATAGTTCGCTTGTGGGCGAAGGTGCAAATGGCGCACAAAATCGGCGATATTTGCAGCTATTTAGCTGCCAACAAAAAGGTTTATCACATCGTGGAGAGTGACGAGCTCACCAAAGTCAGCGGCACCGAACATCACGGCGGTATTTGTATGTTGGTGAAAAAATCCTATCCGTTCACTTTGCAAGGGTATTTGGACGTCCCTCACCAAGAAGATTGTCTGGTGCTGTTAGACGGCGTCAATAACGCGCAAAACATCGGCGGTATTTTGCGCACCTGCGCGTTCTTCGGTGTGAAAAATATGGTATTGGAAGAAGCGGAAAGCCTCAATTCCGCCGTCACCCTGCGCGTGGCGGAAGGCGGTGCGGAATACGTCCGCGTGCTGGAAACCGACGACAGCCGCAACGCCCTCGCCCAATTACGCCACGCCGGTTATCAAATTATCCATGTAAGCAATGACAAAAACTCCACCGCATTGGATAAAGTGCGGTTAAAAAATAAAACGGTTTTCGTGCTAAGCGAAGGTTCAACGGAAACCTTGGCAGAGAAATCCGACGAACAAGTCCGCCTGTCTTTCGGCAACCCGCTGAAAAACGGATTAAATGTCTCGGTGAACGCGGGGATTTTATTGGCGAAATGGTATTTTAGA","","","39871","MNQHSNKPTFKSTNKTFQETSFNERSVGADRKKRDKNRLHFNAPNAARPEFKKSQGKNPPFKRADSQEKTLRISESTMKKAGGAEGGVKVMVKSSQFDDKPREKKTGPLSPRAPEKIKKNRAEEMKVYGENACLALFEQRPASIVRLWAKVQMAHKIGDICSYLAANKKVYHIVESDELTKVSGTEHHGGICMLVKKSYPFTLQGYLDVPHQEDCLVLLDGVNNAQNIGGILRTCAFFGVKNMVLEEAESLNSAVTLRVAEGGAEYVRVLETDDSRNALAQLRHAGYQIIHVSNDKNSTALDKVRLKNKTVFVLSEGSTETLAEKSDEQVRLSFGNPLKNGLNVSVNAGILLAKWYFR","966630","","tRNA/rRNA methylase","Periplasm, Cytoplasm","","
InterPro
IPR001537
Domain
tRNA/rRNA methyltransferase, SpoU
PD001243\"[209-330]TQ9CJY1_PASMU_Q9CJY1;
PF00588\"[214-353]TSpoU_methylase
InterPro
IPR013123
Domain
RNA 2-O ribose methyltransferase, substrate binding
PF08032\"[126-201]TSpoU_sub_bind
noIPR
unintegrated
unintegrated
G3DSA:3.30.1330.30\"[113-199]Tno description
G3DSA:3.40.1280.10\"[211-356]Tno description
PTHR12029\"[170-352]TRNA METHYLTRANSFERASE
PTHR12029:SF7\"[170-352]TRRNA METHYLASE


","BeTs to 18 clades of COG0566COG name: rRNA methylasesFunctional Class: JThe phylogenetic pattern of COG0566 is a-----yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 5.3e-13) to 2/3 blocks of the IPB001537 family, which is described as \"tRNA/rRNA methyltransferase (SpoU)\". Interpro entry for IP:IPR001537. IPB001537A 217-241 2.7e-10 IPB001537C 341-354 0.57","Residues 1 to 143 match (1e-18) PD:PD174113 which is described as METHYLTRANSFERASE COMPLETE PROTEOME 2.1.1.- TRANSFERASE TRNA/RRNA YFIF RNA HI0424 PM1857 ","","","","","","","","","","","","Wed Feb 19 14:36:38 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01441 is paralogously related to AA01374 (3e-07).","","","","","","Residues 214 to 353 (E-value = 2.3e-37) place AA01441 in the SpoU_methylase family which is described as SpoU rRNA Methylase family (PF00588)","","","","","Anantharaman V, Koonin EV, Aravind L.SPOUT: a class of methyltransferases that includes spoU and trmD RNA methylase superfamilies, and novel superfamilies ofpredicted prokaryotic RNA methylases.J Mol Microbiol Biotechnol. 2002 Jan;4(1):71-5. PMID: 11763972Persson BC, Jager G, Gustafsson C.The spoU gene of Escherichia coli, the fourth gene of the spoT operon, is essential for tRNA (Gm18) 2'-O-methyltransferaseactivity.Nucleic Acids Res. 1997 Oct 15;25(20):4093-7.PMID: 9321663","","Wed Feb 19 14:37:18 2003","1","","","" "AA01442","967889","969253","1365","ATGTTTACAGATAAAATCGAACGTGCGCGCAAACGTCTTGAAAGCCTGCCATGTTTGCCATTACAGCCGGAGCAAGTGGAATTTATTTATAGCCCGGCTGCCTTTAAAAGCGAAATTATTCAGCTGACTCGACAAGCAAAAACGCGGATTATTGTGACCGCACTTTATTGGCAAAATGACGAGGCGGGACAAGAAATTCTGGATGAAATTTATCGTGCGAAGCAGGATAAACCGGAACTGGAAGTGAAAATTTTAATTGATTGGCATCGGGCGCAACGCAATTTGTTGGGTGCGGAGAAAAGCGCCACCAATGCTGATTGGTACTACGAAACCCGCCAGAAATATCAACTCGCGGAAGATCCGCATATGTTCTTCGGCGTACCGATTAACACCCGCGAAGTGTTCGGCGTGCTGCACATTAAAGGTTTTGTGTTCGACGATACCGTGTTATACAGCGGCGCCAGCATTAATAACGTGTATTTGCAAAAAAATGAGAAATACCGTTACGACCGCTATCAAAAAATCACCCATCCCGTATTAGCCAACACCATGGTGAATTTCGTGCGCCAAAATCTGTTAGATGCCGATGTGGTGTTGCCGTTGGATGCCGCCAATCCGCCGAAAACCAAAGAAATTCGCGGCAATATTCGTGCGTTCCGTAAAAATCTTGCTGCGTACGGGCAATATCAACTGCCAAGTGCGGTGTCTTTTGGCGATGAATTAACGATCACACCGTTATTCGGTTTAGGCGGCGCAGGCAATATTCTTAATTCGACCATAGAAGATTTGTTCCAGCTGGTGGAAGAAAAACTGACCATTTGTACGCCATATTTCAACTTTCCGAACACGTTGCAACAAAAAATTCGCTATTTGCTCGGCAAAGGCAAGCAAATTGAAATTATCGTCGGCAATAAAGTAGCGAACGATTTTTATATTCCGCCGGATCAACCGTTTAAAATGGCGGGTGCGTTGCCGTATTTGTACGAAAGCAATTTGCGCCGTTTCAGCAAAAAATTTGAACGGGAAATTACCCAAGGGCAGCTTACCGTACGCACCTGGAAAGACGGCGATAATACTTATCACCTGAAAGGCGTTTGGGTGGACAAGAGTTATATTTTGCTCACCGGCAATAACCTCAACCCGCGCGCTTGGCGTTTGGATGCGGAAAACGGTTTGTTCATTCACGATCCGAAACAGCAACTGCGTCCTCAAGTATTAAACGAACTGGAACACATCCGCCGCCACACCACCGTGCTGAGACATTACACCGAGCTGGAAGAATTAAACCAATACCCGGCACCGGTACAAAAACTCCTGAAAAAATTCGCCCATATTAAAGCGGATAAACTGGTGAAAATGATTTTG","","","52835","MFTDKIERARKRLESLPCLPLQPEQVEFIYSPAAFKSEIIQLTRQAKTRIIVTALYWQNDEAGQEILDEIYRAKQDKPELEVKILIDWHRAQRNLLGAEKSATNADWYYETRQKYQLAEDPHMFFGVPINTREVFGVLHIKGFVFDDTVLYSGASINNVYLQKNEKYRYDRYQKITHPVLANTMVNFVRQNLLDADVVLPLDAANPPKTKEIRGNIRAFRKNLAAYGQYQLPSAVSFGDELTITPLFGLGGAGNILNSTIEDLFQLVEEKLTICTPYFNFPNTLQQKIRYLLGKGKQIEIIVGNKVANDFYIPPDQPFKMAGALPYLYESNLRRFSKKFEREITQGQLTVRTWKDGDNTYHLKGVWVDKSYILLTGNNLNPRAWRLDAENGLFIHDPKQQLRPQVLNELEHIRRHTTVLRHYTELEELNQYPAPVQKLLKKFAHIKADKLVKMIL","969253","","phosphatidylserine synthetase","Cytoplasm","","
InterPro
IPR001736
Domain
Phospholipase D/Transphosphatidylase
PF00614\"[134-160]T\"[356-383]TPLDc
SM00155\"[134-160]T\"[356-383]TPLDc
PS50035\"[356-383]TPLD
noIPR
unintegrated
unintegrated
PTHR12586\"[16-455]TCDP-DIACYLGLYCEROL--SERINE O-PHOSPHATIDYLTRANSFERASE


","No hits to the COGs database.","","Residues 16 to 188 match (2e-74) PD:PD014389 which is described as SYNTHASE PHOSPHATIDYLSERINE PROTEOME TRANSFERASE COMPLETE O-PHOSPHATIDYLTRANSFERASE CDP-DIACYLGLYCEROL--SERINE PHOSPHOLIPID PHOSPHATIDYLGLYCEROPHOSPHATE BIOSYNTHESIS ","","","","","","","","","","","","Fri Jan 10 11:58:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01442 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 356 to 383 (E-value = 4.1e-07) place AA01442 in the PLDc family which is described as Phospholipase D. Active site motif (PF00614)","","","","","Dowhan,W. Phosphatidylserine synthase from Escherichia coli Meth. Enzymol. 209, 287-298 (1992) PubMed: 1323044 Saha SK, Nishijima S, Matsuzaki H, Shibuya I, Matsumoto K. A regulatory mechanism for the balanced synthesis of membranephospholipid species in Escherichia coli. Biosci Biotechnol Biochem. 1996 Jan;60(1):111-6. PMID: 8824831 ","","Fri Jan 10 11:58:15 2003","1","","","" "AA01444","969913","969299","615","TTGAATCATAAAACGGTGTTAAAACTGATGAATGCGTTAGGTATTCATTCTATTTTACGCAAGAAAAGACATGGAAAACGAGGCAAAACATCGCATATTGCCCCGAATGTGCTAAATCGTGATTTTACAGCGACGGCGCTCAATCAAAAATGGGTAACCGATGTCACTGAGTTTCGAGTTGGGGAAGAAAAGCTCTATTTTTCACCGTTGATGGATTTAGCGAACCGGGAAATTATTGCCTATAATTTTGCGAAACGCCCTAAGTTCTCATTGGTAAAAAGAATGCCGGAAGAAGGACTTGGCAAACTAAAACCGAGCGAATGCCCGATTATTCACAGCGACCAAGGGGTATTGTACGGCTCAGCAGAATGGGTAAAGATGTTGGAAGGCAAGGCGATACAAAGTATGAGTCGCCGAGGGAATTGCTATGATAATGCGGTGATTGAAAGCTTTTTTGCGATATTAAAATCTGAGTGTTTTTACTCACGCACTTATACTTCGATTGCCGAATTACAGGCGGAAATTGAAGAATATTTGGTGTATTACAACCAAGAACGAATTAAACTTGATTTAAAAGGATTAAGCCCGGTGCAATACCGAGCTCAATATTTAAGT","","","25196","LNHKTVLKLMNALGIHSILRKKRHGKRGKTSHIAPNVLNRDFTATALNQKWVTDVTEFRVGEEKLYFSPLMDLANREIIAYNFAKRPKFSLVKRMPEEGLGKLKPSECPIIHSDQGVLYGSAEWVKMLEGKAIQSMSRRGNCYDNAVIESFFAILKSECFYSRTYTSIAELQAEIEEYLVYYNQERIKLDLKGLSPVQYRAQYLS","969299","","ISRS011/IS150 related transposase, orfB","Cytoplasm","","
InterPro
IPR001584
Domain
Integrase, catalytic core
PF00665\"[43-201]Trve
PS50994\"[31-204]TINTEGRASE


","BeTs to 10 clades of COG2801COG name: Putative transposaseFunctional Class: LThe phylogenetic pattern of COG2801 is ---p-----drlbcefgh-n-j---wNumber of proteins in this genome belonging to this COG is","","Residues 4 to 89 match (5e-07) PD:PD006527 which is described as TRANSPOSASE PROTEOME COMPLETE PLASMID TRANSPOSASE-LIKE IS1077A IS1077B IS1077C IS1077D IS1077E ","","","","","","","","","","","","Fri Jan 10 12:05:32 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01444 is paralogously related to AA01268 (1e-117), AA02342 (1e-95), AA01287 (1e-95), AA01077 (1e-95), AA00010 (1e-95), AA02117 (3e-89), AA02420 (3e-25), AA00145 (3e-23), AA02341 (1e-11), AA02116 (1e-11), AA01288 (1e-11), AA01076 (1e-11) and AA00009 (1e-11).","","","","","","Residues 43 to 201 (E-value = 5.6e-31) place AA01444 in the rve family which is described as Integrase core domain (PF00665)","","","","","","","","1","","","" "AA01445","970167","970039","129","ATGTCTTACTCTTACCAATTTCGTTTAAAAACTATCAAACAGGTCACCGAGCAGGATTTTGGTATCCGTGAGGTGGCTAAATTTCATCAGATTTCTCGTTCTCAAGTCATTTATTGGAAAAGCCTTTCG","","","5210","MSYSYQFRLKTIKQVTEQDFGIREVAKFHQISRSQVIYWKSLS","970039","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 17:04:33 2004","Thu Feb 26 17:04:33 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA01267.AA01445 is paralogously related to AA01267 (8e-16) and AA00535 (6e-11).","Thu Feb 26 17:04:33 2004","","","","","","","","","","","","","1","","","" "AA01446","970386","970291","96","TTGATTGCCGACTATCAGCTTCGGTTGCAGCGTTGTCACCCGATAGAAGCCATCGCATGGTTACATTTGGCATTTGAATCCATTCACCCATTTTGT","","","3787","LIADYQLRLQRCHPIEAIAWLHLAFESIHPFC","970291","","conserved hypothetical protein","Cytoplasm","This sequence is similar to gi|23467214, a predicted uncharacterized conserved protein from Haemophilus somnus 129PT.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 17:01:53 2004","Thu Feb 26 17:01:53 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01446 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 17:01:53 2004","","","","","","","","","","","","","1","","","" "AA01448","970348","970452","105","GTGACAACGCTGCAACCGAAGCTGATAGTCGGCAATCAATTTCGGTCAAAAGTGCGGTCATTTTATGAAGTGTTTTTTAAAAATAAAATTGAGTGGCGGAGATCG","","","4285","VTTLQPKLIVGNQFRSKVRSFYEVFFKNKIEWRRS","970452","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 16:59:17 2004","Thu Feb 26 16:59:17 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01448 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 16:59:17 2004","","","","","","","","","","","","","1","","","" "AA01449","971629","970709","921","TTGATGGTACTAAAATTTATGGCACGCATAATTAAACCCTTAACCGACAAAGAAATTCGCACTGCCAAAGCGGGTAAATTCCCACTCAGAGACGGCAACGGATTATCTCTAGAACTTACCACCACCGGCGCGAAAATATGGCGTTTTAATTACTTCAAACCTTTTACCCAAAAAAGAACCAATATCAGCCTAGGCAAACTATCTGATATGACATTGACACAAGCACGGGCAAAGCGTGAAGAATATCGGCAACTCTTAGCAAAGAATATCGATCCACGCACCTACGAAGCCCAAGCTAAACAAGAAAGCACCGACAAACAGAACCGTACTTTTGAGCGCATGGCAGAAGCATGGTTTAAGGATAGACAGCTTAAAGCCAATTTCACCGAGCGCACCGCAAAAGACACATGGGCTTTATTTGAACGGCATATTCTCCCCGCTATCGGTAAATATCCAATCGACCAACTGACCGCACTTATCGGCATTAATGCTTTCAAGCCATTAGAGCGTGCAGGAAAATTAGAGACCGTTAGAAAAATATTAAACAACGTGAATCATGTAATGCGCTATGCCTTGCACCGTGGATTAATTGCCACCAACAACTTAGCCGAAATTCAACGAGAATTTGATAAACCGCGCGTAAAAGGTATGAACACCATAGAACCTGACGAACTGGCGGAATTTTTAGCGAAATTCTATCAAGCAAGAGATGACGGCAGATTTTCTCTATTGTCGTTCTATGCCGTGATGTTGGCAGTGTTAACCGGAAGCAGACCAAGCGAAATAGCGCGGGCGCAATGGGAAGATATAGACACCACAGCGCAGACATGGAGCTACCGAGTAGAGGAACATATAACAAGGCTTACTATATCAATCAGCGGGCGGAAATGTTGCAAGCGTGGGCGGATTATGTGGAATCAT","","","35649","LMVLKFMARIIKPLTDKEIRTAKAGKFPLRDGNGLSLELTTTGAKIWRFNYFKPFTQKRTNISLGKLSDMTLTQARAKREEYRQLLAKNIDPRTYEAQAKQESTDKQNRTFERMAEAWFKDRQLKANFTERTAKDTWALFERHILPAIGKYPIDQLTALIGINAFKPLERAGKLETVRKILNNVNHVMRYALHRGLIATNNLAEIQREFDKPRVKGMNTIEPDELAEFLAKFYQARDDGRFSLLSFYAVMLAVLTGSRPSEIARAQWEDIDTTAQTWSYRVEEHITRLTISISGRKCCKRGRIMWNH","970709","","prophage CP4-57 integrase","Cytoplasm","","
InterPro
IPR002104
Domain
Integrase, catalytic core, phage
PF00589\"[232-277]TPhage_integrase


","BeTs to 6 clades of COG0582COG name: IntegraseFunctional Class: LThe phylogenetic pattern of COG0582 is aompkz-qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 64 to 290 match (3e-07) PD:PD119784 which is described as INTEGRASE COMPLETE PROTEOME PLASMID PHAGE DNA INTEGRASE PRBABLE SIMILAR PROPHAGE: ","","","","","","","","","","","","Fri Jan 10 12:12:03 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01449 is paralogously related to AA00785 (9e-07).","","","","","","","","","","","Kirby,J.E., Trempy,J.E. and Gottesman,S.Excision of a P4-like cryptic prophage leads to Alp protease expression in Escherichia coliJ. Bacteriol. 176 (7), 2068-2081 (1994)PubMed: 7511583","","Fri Jan 10 12:14:40 2003","1","","","" "AA01450","972000","972092","93","TTGGAAATTGATGCGAACTTTAGCGCAAAAGCCCGTGCGATTCAAGTGAAGCGGAAAAATAATCCATTAATTTTATACGGAATATTGGGCGTT","","","3408","LEIDANFSAKARAIQVKRKNNPLILYGILGV","972092","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 16:57:54 2004","Thu Feb 26 16:57:54 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01450 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 16:57:54 2004","","","","","","","","","","","","","1","","","" "AA01451","973544","972075","1470","ATGTATCTTGGCGTCGATTGCGGCACGCAAGGCACGAAAGTGATTGTTGTAGATAGTCAACAGCATAAGGTATTGGGTAGCGGTTATGTCGCCCATCAACTCATTGAAAACTCCGACGGACGGCGCGAGCAAGCGCCGGATTGGTGGATTACGGCGTTTAAAAATGCTTTTGCCGACGCCATAAAACACGCCGAAATTCAACCGCACTTGATTCGTGGCATCGGTATTTCCGGGCAGCAACACGGCTTGGTGGTGCTGGATAAAAACGATCATCCGTTGTACCATGCCAAACTCTGGTGCGACACGGAAACCGCCGCGGAAAATGCGGAGATTTTAGCGTTGCTCGGTGGCGAACAAGCCTGTTTTGAACGCCTCGGCATTGTTTGCCAAAGCGGTTATACGGCATCCAAAATCCGTTGGCTGCGTAAATATCAACCGGATATTTATCAACAAATCGACAAAATCATGCTACCTCATGATTATCTCAATTATTGGCTCACGGGCAAATTCTGTACCGAATACGGTGATGCGTCCGGCACCGGCTATTTTGATGTGGTGCGACGTTGTTGGGACGAGGAGGTGTTGCGCCTTATTGCCCCGGAAAAATGCCTGGAAAATCTACCGCACTTAATCGACGCTGACCAAATTCTCGGCACGGTGAAAGCAGATGTCGCGCGCCAATTAGGACTGGAGAATGACGTCATTGTTTCCGCCGGCGGCGGCGACAACATGATGGGCGCCATCGGTACCGGCAATATTCAACAAGGCATCGTCACCATGAGCTTAGGCACGTCGGGCACGCTCTATGCCTACAGCGATAAACCGCTCCCCGATTTGCCGCCGATGATTGCCGATTTTTGTTCCTCTTCCGGCGGCTGGTTGCCGTTGGTTTGCACCATGAACGTGACGTCCGCTAACAAAAATCTCATGCAACTGCTGGAAATTAACGTGAGCGAATTCAATGAATTGGTACAACAAGCCAATATCGGCGCCGACGGCGTGACCATTCTGCCCTTCTTTAACGGCGAACGGGTGCCGGCATTGCCGAATAGCAAAGCGGCGATTTTGGGCTTGGATGCGGGCAATTTCACCCGCGCCAATTTATCCCGCGCCGTGATGGAAAGCGCCAGTTTTACCTTGCGCTACGGCTTGGATTTATTTGAACAGGCGGGGCTGGCCGCCACCGAAATCCGCCTGATTGGCGGCGGGGCGAAAAGTGCCGTATGGCGGCAAATGATTGCCGACATTATGAACGTCAACGTAGTGTGCCTGATGGAGGAAGAAGCTGCCGCATTGGGCGCCGCAATTCAAGCCATGTGGGCAAATAAACAGGGTTCGCTGGCGGAATTATGCCGAGCTTTCGTACAGTTAAATGAAGCGACGCGCACAGCGCCGATAGCGGAAAATGCGGAACAATATCAATCCGTTTACCAACGCTATCGCCAACATTTAAACGCCCAATATTCCGTA","","","53630","MYLGVDCGTQGTKVIVVDSQQHKVLGSGYVAHQLIENSDGRREQAPDWWITAFKNAFADAIKHAEIQPHLIRGIGISGQQHGLVVLDKNDHPLYHAKLWCDTETAAENAEILALLGGEQACFERLGIVCQSGYTASKIRWLRKYQPDIYQQIDKIMLPHDYLNYWLTGKFCTEYGDASGTGYFDVVRRCWDEEVLRLIAPEKCLENLPHLIDADQILGTVKADVARQLGLENDVIVSAGGGDNMMGAIGTGNIQQGIVTMSLGTSGTLYAYSDKPLPDLPPMIADFCSSSGGWLPLVCTMNVTSANKNLMQLLEINVSEFNELVQQANIGADGVTILPFFNGERVPALPNSKAAILGLDAGNFTRANLSRAVMESASFTLRYGLDLFEQAGLAATEIRLIGGGAKSAVWRQMIADIMNVNVVCLMEEEAAALGAAIQAMWANKQGSLAELCRAFVQLNEATRTAPIAENAEQYQSVYQRYRQHLNAQYSV","972075","","D-xylulokinase","Cytoplasm","","
InterPro
IPR000577
Family
Carbohydrate kinase, FGGY
PTHR10196\"[48-488]TXYLULOSE KINASE
PF00370\"[1-249]TFGGY_N
PF02782\"[252-474]TFGGY_C
PS00445\"[353-374]?FGGY_KINASES_2
InterPro
IPR006000
Family
Xylulokinase
TIGR01312\"[3-485]TXylB: xylulokinase
noIPR
unintegrated
unintegrated
PTHR10196:SF10\"[48-488]TXYLULOSE KINASE


","BeTs to 9 clades of COG1070COG name: Sugar (pentulose and hexulose) kinasesFunctional Class: GThe phylogenetic pattern of COG1070 is a----zy-v-rlbcef-h---j--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 6.2e-32) to 6/9 blocks of the IPB000577 family, which is described as \"Carbohydrate kinase, FGGY family\". Interpro entry for IP:IPR000577. IPB000577B 73-88 4.7e-05 IPB000577C 90-99 20 IPB000577D 125-144 0.43 IPB000577E 170-208 0.00026 IPB000577H 333-374 0.003 IPB000577I 397-433 5.1e-10","Residues 3 to 386 match (2e-07) PD:PD576421 which is described as KINASE POSSIBLE PROTEOME COMPLETE KINASE SUGAR XYLULOSE ","","","","","","","","","","","","Fri Jan 10 15:46:04 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01451 is paralogously related to AA02230 (2e-26), AA00937 (7e-21) and AA00938 (1e-10).","","","","","","Residues 252 to 474 (E-value = 8.7e-81) place AA01451 in the FGGY_C family which is described as FGGY family of carbohydrate kinases, C-terminal domain (PF02782)","","","","","Jin YS, Jones S, Shi NQ, Jeffries TW.Molecular cloning of XYL3 (D-xylulokinase) from Pichia stipitis and characterization of its physiological function.Appl Environ Microbiol. 2002 Mar;68(3):1232-9.PMID: 11872473 vanKuyk PA, de Groot MJ, Ruijter GJ, de Vries RP, Visser J. The Aspergillus niger D-xylulose kinase gene is co-expressed with genesencoding arabinan degrading enzymes, and is essential for growth on D-xylose and L-arabinose. Eur J Biochem. 2001 Oct;268(20):5414-23. PMID: 1160626 Johansson B, Christensson C, Hobley T, Hahn-Hagerdal B. Xylulokinase overexpression in two strains of Saccharomyces cerevisiaealso expressing xylose reductase and xylitol dehydrogenase and its effecton fermentation of xylose and lignocellulosic hydrolysate. Appl Environ Microbiol. 2001 Sep;67(9):4249-55. PMID: 11526030 Erlandson KA, Park JH, Wissam, El Khal, Kao HH, Basaran P, Brydges S, Batt CA.Dissolution of xylose metabolism in Lactococcus lactis.Appl Environ Microbiol. 2000 Sep;66(9):3974-80.PMID: 10966417 ","","Fri Jan 10 12:37:41 2003","1","","","" "AA01453","974913","973597","1317","ATGACAAACTACTTCAACAACATTGACAAAGTTCGCTACGAAGGTCCTGACTCAACCAATCCCTTCGCGTATAAATACTACGACGCCAATCAGGTCATTCTTGGCAAAACCATGGCGGAGCATTTGCGTTTGGCGGTATGTTATTGGCATACGTTTTGCTGGAACGGTACCGATATGTTCGGCTTGGGTTCGCTGGATCGAAGCTGGCAGAAAAATGCCGGCACGTTAGAGGCGGCAAAACAAAAAGCGGATATTGCTTTTGAGTTTTTCACCAAATTAGGCGTGCCTTATTATTGTTTCCACGATGTGGATGTGGCGCCGGAAGGCAATTCCATTAAGGATTACATTCATAATTTCAACACAATAACGGACATTCTTGAGCGTAAACAGGCGGAAACCGGCGTGAAGTTGCTGTGGGGCACGGCAAACTGTTTCAGCAATCCGCGTTATATGTCCGGCGCCTCCACCAACCCGAATCCGGAAGTGTTCGCCTGGGCGGCAACGCAGGTATATCACGCCATGAATGCTACCAAGCGTTTGGGCGGCGAAAACTATGTGCTCTGGGGCGGTCGCGAAGGTTATGAAACCCTGCTCAATACGGACTTAAAACGTGAACGCGAGCAAATCGGACGCTTCATGCAAATGGTGGTGGAACATAAACATAACATCGGCTTTAACGGCACATTGCTTATCGAACCGAAACCACAGGAACCAACCAAACATCAATACGATTATGACGTGGCGACGGTTTACGGTTTCTTAAAACAATTCGGCTTGGAAAATGAAATTAAAGTGAACATTGAAGCCAACCACGCCACCTTGGCGGGGCACACCTTCCAGCATGAAGTGGCGACGGCGTTCGCGCTGGATATTTTCGGCTCCATCGACGCCAACCGCGGCGACCCGCAATCAGGCTGGGACACCGACCAATTCCCGAACAGCGTGGAAGAAAACACGTTGGTGATGTACGAAATCCTGAAAAACGGCGGTTTTACCACCGGCGGTTTCAATTTTGATGCGAAAATCCGCCGTCAAAGTACCGATCCTTATGATTTGTTCTATGCCCATATCGGCGCTATCGACGTATTGGCGTTATCCCTCAAACGGGCGGCACAAATGCTGGAAGAACAACGGCTGCAACAGCTTGTGGACGAACGTTATGCCGGTTGGCGGCAATCCCTCGGTCAGCAAATTTTGCTGGGTAACGCTTCTTTGGCACAGCTCGCGCAGGCGGTTGAGCAACAAGGCTTGGATCCGCAACCGGTGTCCGGTAAACAGGAGTATCTGGAAAACTTGGTGAACGGTTACATTTACCGT","","","49786","MTNYFNNIDKVRYEGPDSTNPFAYKYYDANQVILGKTMAEHLRLAVCYWHTFCWNGTDMFGLGSLDRSWQKNAGTLEAAKQKADIAFEFFTKLGVPYYCFHDVDVAPEGNSIKDYIHNFNTITDILERKQAETGVKLLWGTANCFSNPRYMSGASTNPNPEVFAWAATQVYHAMNATKRLGGENYVLWGGREGYETLLNTDLKREREQIGRFMQMVVEHKHNIGFNGTLLIEPKPQEPTKHQYDYDVATVYGFLKQFGLENEIKVNIEANHATLAGHTFQHEVATAFALDIFGSIDANRGDPQSGWDTDQFPNSVEENTLVMYEILKNGGFTTGGFNFDAKIRRQSTDPYDLFYAHIGAIDVLALSLKRAAQMLEEQRLQQLVDERYAGWRQSLGQQILLGNASLAQLAQAVEQQGLDPQPVSGKQEYLENLVNGYIYR","973597","","D-xylose isomerase","Cytoplasm, Extracellular","","
InterPro
IPR001998
Family
Xylose isomerase
PR00688\"[92-114]T\"[133-153]T\"[156-175]T\"[180-201]T\"[207-226]T\"[229-253]T\"[271-298]T\"[300-311]T\"[333-344]TXYLOSISMRASE
PS00172\"[231-238]TXYLOSE_ISOMERASE_1
PS00173\"[100-109]TXYLOSE_ISOMERASE_2
InterPro
IPR012307
Domain
Xylose isomerase-like TIM barrel
PF01261\"[128-286]TAP_endonuc_2
InterPro
IPR013452
Family
Xylose isomerase, bacterial type
TIGR02630\"[4-437]Txylose_isom_A: xylose isomerase
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.150\"[2-438]Tno description


","BeTs to 4 clades of COG2115COG name: Xylose isomeraseFunctional Class: GThe phylogenetic pattern of COG2115 is --------v--lb-e--h---j----Number of proteins in this genome belonging to this COG is","Significant hit ( 3e-130) to 7/7 blocks of the IPB001998 family, which is described as \"Xylose isomerase\". Interpro entry for IP:IPR001998. IPB001998A 48-61 9.4e-11 IPB001998B 87-114 8.6e-18 IPB001998C 126-175 6.3e-28 IPB001998D 215-254 1.5e-27 IPB001998E 255-281 3.6e-17 IPB001998F 282-312 6.3e-16 IPB001998G 334-344 2.3e-05","Residues 4 to 437 match (7e-217) PD:PD003353 which is described as ISOMERASE XYLOSE PENTOSE SHUNT METABOLISM MAGNESIUM PROTEOME COMPLETE 3D-STRUCTURE D-XYLOSE ","","","","","","","","","","","","Fri Jan 10 15:44:27 2003","","","Tue Mar 16 08:49:06 2004","Tue Mar 16 08:48:33 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01453 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Tue Mar 16 08:48:33 2004","","","","","Residues 29 to 437 (E-value = 2.7e-255) place AA01453 in the Xylose_isom family which is described as Xylose isomerase (PF00259)","Tue Mar 16 08:48:33 2004","","","","Erbeznik M, Dawson KA, Strobel HJ.Cloning and characterization of transcription of the xylAB operon in Thermoanaerobacter ethanolicus.J Bacteriol. 1998 Mar;180(5):1103-9.PMID: 9495747Lawlis VB, Dennis MS, Chen EY, Smith DH, Henner DJ.Cloning and sequencing of the xylose isomerase and xylulose kinase genes of Escherichia coli.Appl Environ Microbiol. 1984 Jan;47(1):15-21.PMID: 6320721Schellenberg GD, Sarthy A, Larson AE, Backer MP, Crabb JW, Lidstrom M, Hall BD, Furlong CE.Xylose isomerase from Escherichia coli. Characterization of the protein and the structural gene.J Biol Chem. 1984 Jun;259(11):6826-32.PMID: 6327696","","Tue Mar 16 08:49:06 2004","1","","","" "AA01455","975171","976166","996","ATGAAAATCAAATTTGCTTTATTATCTCTTGCTACCGCACTTGCCTTATGCAGCACCACCGGCTTCGCCAAAGACTTAAAAATCGGTATGTCCATTGACGATTTACGTTTAGAAAGATGGCAAAAAGACAGCAGTATTTTCGTTAAAAAAGCGGAAGCGTTAGGCGCCAAAGTTTATGTTCAATCCGCCAACGGCGATGATTCGGCACAAATTTCACAAATCGAAAACATGATTAATAAAAATATTGATGTGCTGGTGATTATTCCACATAACGGTGAAGTATTAAGCAATGTCATTGCAGAGGCGAAAAAAGAAGGCATCAAAGTTTTAGCCTATGACCGTTTAATTAATAACGCGGATCTGGACTTTTACGTTTCCTTTGATAATGAAAAAGTCGGTGAATTACAAGCGCAAAGTGTTATTGAGAAAAAACCGGAAGGTAACTATTTCTTAATGGGTGGTTCGCCGGTAGATAACAACGCGAAACTTTTCCGCAAAGGTCAAATGAAAGTATTACAACCGTTAATTGATAGCGGAAAAATTAAAGTGGTGGGCGATCAATGGGTCGATTCTTGGTTACCGGAAAAAGCCTTACAAATTATGGAAAATGCACTAACCGCCAACAAAAATAATATTGATGCCGTTGTTGCTTCGAACGATGCCACCGCCGGCGGGGCAATTCAGGCGCTTTCCGCGCAGGGTTTATCCGGCAAAGTAGCGATTTCCGGTCAGGATGCCGACTTGGCGGCAATTAAACGCATTGTGGAAGGCACACAAACCATGACCGTGTATAAACCGATAGCCTTATTGGCGGATAAAGCGGCTGAAATTTCCGTTGCCTTGGCTAAGGATGAAAAACCGCAATCCAATGCGGAATTAAATAACGGCTTGAAAAACGTGCCATCCTACCTACTTGAACCTATCGTCGTTGATAAAAATAATATTGAAACCACGATTATTAAGGACGGGTTCCATTCTAAAGATAGCATTTATAAA","","","35919","MKIKFALLSLATALALCSTTGFAKDLKIGMSIDDLRLERWQKDSSIFVKKAEALGAKVYVQSANGDDSAQISQIENMINKNIDVLVIIPHNGEVLSNVIAEAKKEGIKVLAYDRLINNADLDFYVSFDNEKVGELQAQSVIEKKPEGNYFLMGGSPVDNNAKLFRKGQMKVLQPLIDSGKIKVVGDQWVDSWLPEKALQIMENALTANKNNIDAVVASNDATAGGAIQALSAQGLSGKVAISGQDADLAAIKRIVEGTQTMTVYKPIALLADKAAEISVALAKDEKPQSNAELNNGLKNVPSYLLEPIVVDKNNIETTIIKDGFHSKDSIYK","976166","","D-xylose ABC transporter, periplasmic-binding protein","Periplasm","","
InterPro
IPR001761
Domain
Periplasmic binding protein/LacI transcriptional regulator
PF00532\"[25-308]TPeripla_BP_1
InterPro
IPR013456
Family
D-xylose ABC transporter, substrate-binding protein
TIGR02634\"[28-330]TxylF: D-xylose ABC transporter, substrate-b
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2300\"[128-280]Tno description
signalp\"[1-23]?signal-peptide
tmhmm\"[5-23]?transmembrane_regions


","BeTs to 7 clades of COG1879COG name: Periplasmic sugar-binding proteinsFunctional Class: GThe phylogenetic pattern of COG1879 is --------v-rlb-efgh---j--t-Number of proteins in this genome belonging to this COG is","","Residues 293 to 329 match (6e-09) PD:PD583468 which is described as PERIPLASMIC COMPLETE PROTEOME D-XYLOSE-BINDING SUGAR SIGNAL PRECURSOR SYSTEM BINDING SUGAR-BINDING ","","","","","","","","","","","","Fri Jan 10 15:30:20 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01455 is paralogously related to AA00932 (3e-23), AA00209 (6e-20), AA02788 (3e-18), AA02787 (8e-17), AA00750 (8e-10) and AA00749 (5e-04).","","","","","","Residues 25 to 308 (E-value = 4.3e-05) place AA01455 in the Peripla_BP_1 family which is described as Periplasmic binding proteins and sugar binding domain of the LacI family (PF00532)","","","","","Sumiya M, Davis EO, Packman LC, McDonald TP, Henderson PJ.Molecular genetics of a receptor protein for D-xylose, encoded by the gene xylF, in Escherichia coli.Receptors Channels. 1995;3(2):117-28.PMID: 8581399","","Fri Jan 10 15:30:20 2003","1","","","" "AA01456","976229","977737","1509","ATGGCTCTATTAGAAATGAAAAATATCACCAAGAAATTCGGCGATGTTGTAGCATTAAACAACATTTCCATTTCCTTGGAAAAAGCGGAGATTCTGTCTTTATGTGGTGAAAACGGCTCCGGTAAATCCACCTTAATGAAGGTATTATGCGGCATTTATCCTTTCGGCGATTATGAAGGCGATATTTATTTCAGTTATGAAAAAATCGTTGCCAAAAACATTAAAGATACGGAAGAAAAAGGCATTTCCATTATTCACCAGGAATTAACCTTGGTAAAAAATATGTCCATTTTGGAAAATATGTTTTTGGGCAACGAAATCACCAAAGGCGGCATTACCGACGACAACGAAATGTATTTACGCTGTAAAAAACTGTTGGAACAAGTCCAACTGGATATTGACCCGCACACCAAAGTCGGTGAATTAGGTTTGGGGCAGCAACAACTTGTTGAAATTGCCAAAGCCTTAAATAAACAGGTTCGTTTGCTGATTTTAGACGAACCGACAGCATCATTAACCGAAAAAGAAACGGCGATTTTATTAAATCTGGTAAAAGATTTACGCGCCCATAATATCGCCTGCATTTACATTTCCCACAAACTCAATGAAGTTAAAGAAATCTCCGACAAAATCTGTGTGATTCGCGACGGTGAGCATATCGGTACCCGTGATGCGAAAACCATGACGGAAGATGACATCATCACCATGATGGTAGGCCGTGAAATCACGTCTTTATATCCCCATGAAGCACATGAAATCGGTGAGGAAATCCTGCGGGTGGAACATATTACCGCTTGGCATCCCATTAATACCCATATTAAACGGGTAAGTAACGCGTCGTTTACGCTCCATAAAGGTGAGATTTTAGGGGTTGCCGGTTTAGTCGGCTCCGGACGAACAGAAATGGTGCAATGTATTTTTGGTTCCTACCCGGGTAAACATGAAGGTGAGATTTTTATTCATAACCATAAAGTAAAAATTCGTAATTGCAGCGAAGCCATTAAACACAATATCGTAATGGTGCCGGAAGATCGCAAAAAACACGGTATCGTTGCCATTATGGGCGTGGGAAAAAATATTACGCTACCTTCATTACGCAATTATTGTTTCGGTAAACGGGTCATCAATGAAGCCTTGGAAGAAACGGTAATTAACCAAGCTATCGCCCAGTTAAAAGTCAAAACGTCTTCACCGCACTTAGCCATCGGGCGTTTAAGCGGCGGCAATCAGCAAAAAGCGATTCTTGCCAAATCCTTATTACTTAAACCTCAAATTCTGATTTTGGATGAACCTACACGCGGGATCGATGTGGGCGCCAAATATGAAATTTATAAACTTATCAACCAACTGGCACAAGAAGGCATCGCGATTATTGTCATTTCCTCCGAATTGCCGGAAGTGCTTGGCATTAGCGATCGGGTTTTAGTGATGCACCAAGGTCAGATTAAAGCGGATTTAATCAATAATCATCTGACACAGGAACAGGTCATGGAAGCGGCGCTAAAGGAG","","","55900","MALLEMKNITKKFGDVVALNNISISLEKAEILSLCGENGSGKSTLMKVLCGIYPFGDYEGDIYFSYEKIVAKNIKDTEEKGISIIHQELTLVKNMSILENMFLGNEITKGGITDDNEMYLRCKKLLEQVQLDIDPHTKVGELGLGQQQLVEIAKALNKQVRLLILDEPTASLTEKETAILLNLVKDLRAHNIACIYISHKLNEVKEISDKICVIRDGEHIGTRDAKTMTEDDIITMMVGREITSLYPHEAHEIGEEILRVEHITAWHPINTHIKRVSNASFTLHKGEILGVAGLVGSGRTEMVQCIFGSYPGKHEGEIFIHNHKVKIRNCSEAIKHNIVMVPEDRKKHGIVAIMGVGKNITLPSLRNYCFGKRVINEALEETVINQAIAQLKVKTSSPHLAIGRLSGGNQQKAILAKSLLLKPQILILDEPTRGIDVGAKYEIYKLINQLAQEGIAIIVISSELPEVLGISDRVLVMHQGQIKADLINNHLTQEQVMEAALKE","977737","","D-xylose ABC transporter, ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[141-184]T\"[405-447]TXYLG_HAEIN_P45046;
PF00005\"[29-217]T\"[402-480]TABC_tran
PS50893\"[4-241]T\"[258-499]TABC_TRANSPORTER_2
PS00211\"[405-419]?ABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[28-218]T\"[285-481]TAAA
InterPro
IPR013455
Family
D-xylose ABC transporter, ATP-binding protein
TIGR02633\"[3-501]TxylG: D-xylose ABC transporter, ATP-binding
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[3-232]T\"[251-495]Tno description
PTHR19222\"[4-309]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF12\"[4-309]TSUGAR ABC TRANSPORTER


","BeTs to 7 clades of COG1129COG name: ABC-type sugar (aldose) transport system, ATPase componentFunctional Class: GThe phylogenetic pattern of COG1129 is -----z--v--lb-efgh---j--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 7.3e-21) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 18-64 3.9e-08 IPB001140B 139-177 1.1e-07 IPB001140C 457-486 0.11","Residues 236 to 308 match (8e-09) PD:PD586243 which is described as PROTEOME COMPLETE TRANSPORTER ABC NUCLEOTIDE BINDING/ATPASE ATP-BINDING SUGAR SYSTEM ","","","","","","","","","","","","Fri Jan 10 15:39:52 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01456 is paralogously related to AA00207 (1e-109), AA00751 (1e-107), AA02786 (6e-97), AA02225 (6e-60), AA00933 (2e-56), AA00934 (4e-24), AA00700 (2e-21), AA01524 (7e-21), AA02140 (9e-21), AA01051 (4e-20), AA02320 (6e-20), AA01645 (6e-20), AA02440 (2e-19), AA02718 (4e-19), AA01656 (4e-18), AA02080 (7e-18), AA02152 (1e-17), AA01820 (3e-17), AA00858 (4e-17), AA01568 (6e-17), AA01616 (2e-16), AA00415 (4e-16), AA01824 (7e-16), AA02898 (9e-16), AA02899 (2e-15), AA02550 (3e-15), AA02353 (1e-14), AA01422 (2e-14), AA01510 (4e-14), AA01961 (2e-13), AA02805 (4e-13), AA01684 (9e-13), AA00799 (1e-12), AA02331 (2e-12), AA01509 (8e-12), AA02606 (1e-11), AA02324 (1e-11), AA02573 (2e-11), AA01867 (7e-11), AA02484 (1e-10), AA01779 (1e-10), AA01569 (2e-10), AA01947 (6e-10), AA00061 (2e-09), AA01757 (5e-09), AA01393 (6e-09), AA02642 (8e-09), AA02146 (2e-08), AA02226 (1e-07), AA02609 (3e-07), AA00591 (5e-06), A02145 (3e-04), AA01555 (6e-04) and AA01291 (8e-04).","","","","","","Residues 286 to 480 (E-value = 1.8e-21) place AA01456 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Sumiya M, Davis EO, Packman LC, McDonald TP, Henderson PJ.Molecular genetics of a receptor protein for D-xylose, encoded by the gene xylF, in Escherichia coli.Receptors Channels. 1995;3(2):117-28.PMID: 8581399","","Fri Jan 10 15:39:52 2003","1","","","" "AA01457","977744","978868","1125","ATGTCTAAATTGAAATCAATAAATTTACAGGTTTATATTATGCTTATTGCCATTGTGGTGATTATGGCATTCTTCTTTGTCGCCACCGACGGCGCTTACCTGAGTGCGCGTAATATTTCCAATCTATTACGCCAAACCTCCATTACGGGCATTCTCGCCATCGGCATGATTTTCGTGATTATCTCTGCCGAGATTGACTTATCCGTCGGTTCATTAATGGGATTACTCGGCGGTTTTGCCGCCATCGCCGATGTTTGGTGGGGCTGGCCGTTACCGTTAACCATTATAACAACGTTGCTTATCGGCATTGTGCTCGGCGCTTGCACCGGCTGGTGGGTTGCCTATCGAAAAGTACCCTCTTTTATTGTCACATTGGCGGGAATGCTGATTTTCCGCGGGATGTTGGTCGGCGCAACCAACGGCACCACGGTTTCACCGATTAGCAAAGACATGACAATCATCGGTCAAGGCTACCTTCCCGATACCACCGGCATTATTTTAGGTTGTGTTGCCGTTATTTGTTTCTTCCTATGGGGTTCTTATCAACGTAAAACCCGCAAAAATCTTAACTTAAGCGTTACCGGCACAGGTAAAGAAACCATGAAATACGGTTTATTCGCCATTGGTGTACTGGGTGCGATCTATCTCTTAAATGATTATCGGGGCATTCCGTTCCCGGTGTTGCTTCTGGCGATTTTAGCGGTTATCGGTATGTTCATTGCACGAAAAACCGCATTCGGACGACACATTTATGCCATTGGCGGTAATATTGAGGCTGCCAGATTATCAGGCATCAATGTTGAAAAAATCAAACTCATGATTTTCTCCATTAACGGCTTAATGGTCGCCATCGCCGGGTTAATTCTCAGTGCCCGTTTAGGTGCCGGCGCGCCGTCCGCCGGTCAAAATGCCGAACTGGACGCCATCGCCGCCTGTGTTATCGGCGGTGCAAGCCTCGCCGGCGGTGTCGGTAGCGTTTACGGCGTGGTTATCGGTGCATTGATTATCGCCTTATTGGACAACGGTATGAGTATGTTAGACGTGCCGACCTTCTGGCAATACATTGTGAAAGGTACCATTTTATTACTCGCCGTATGGATGGATACGATGAGTAAGAAAAAAATG","","","39745","MSKLKSINLQVYIMLIAIVVIMAFFFVATDGAYLSARNISNLLRQTSITGILAIGMIFVIISAEIDLSVGSLMGLLGGFAAIADVWWGWPLPLTIITTLLIGIVLGACTGWWVAYRKVPSFIVTLAGMLIFRGMLVGATNGTTVSPISKDMTIIGQGYLPDTTGIILGCVAVICFFLWGSYQRKTRKNLNLSVTGTGKETMKYGLFAIGVLGAIYLLNDYRGIPFPVLLLAILAVIGMFIARKTAFGRHIYAIGGNIEAARLSGINVEKIKLMIFSINGLMVAIAGLILSARLGAGAPSAGQNAELDAIAACVIGGASLAGGVGSVYGVVIGALIIALLDNGMSMLDVPTFWQYIVKGTILLLAVWMDTMSKKKM","978868","","D-xylose ABC transporter, membrane spanning protein","Inner membrane, Cytoplasm","","
InterPro
IPR001851
Family
Bacterial inner-membrane translocator
PF02653\"[38-365]TBPD_transp_2
noIPR
unintegrated
unintegrated
signalp\"[1-31]?signal-peptide
tmhmm\"[10-28]?\"[49-83]?\"[89-109]?\"[118-138]?\"[157-179]?\"[200-215]?\"[221-241]?\"[274-294]?\"[308-339]?\"[348-366]?transmembrane_regions


","BeTs to 7 clades of COG1172COG name: Ribose/xylose/arabinose/galactoside ABC-type transport systems, permease componentsFunctional Class: GThe phylogenetic pattern of COG1172 is --------v-rlb-efgh---j--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.8e-14) to 2/2 blocks of the IPB001851 family, which is described as \"Binding-system dependent bacterial transporters (araH, livH/limM families)\". Interpro entry for IP:IPR001851. IPB001851A 246-260 3.3e-07 IPB001851B 305-316 1.5e-05","Residues 333 to 374 match (4e-10) PD:PD409969 which is described as COMPLETE PROTEOME PERMEASE ABC SUGAR TRANSPORTER TRANSPORTER MEMBRANE SYSTEM PLASMID ","","","","","","","","","","","","Fri Jan 10 15:49:08 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01457 is paralogously related to AA00208 (2e-52), AA00753 (1e-44), AA00936 (7e-39), AA02785 (2e-36), AA02224 (5e-30), AA02220 (2e-21) and AA00935 (2e-13).","","","","","","Residues 38 to 365 (E-value = 1.2e-67) place AA01457 in the BPD_transp_2 family which is described as Branched-chain amino acid transport system / permease component (PF02653)","","","","","","","","1","","","" "AA01458","978960","980153","1194","ATGGAAATCAAATTTGATCAATGGGTTAATCGAATCGGAACGGATAGTGCCAAATGGGATGTCCCTTATTCAAAATATGGTTCCGATATTATTCCTCTGTCGGTAGCGGATATGGATCTTCCTGCGCCGCAGGAAATTATTGAATTATTGAACGAACGTAATTGGTTGGGCATATACGGATATACAATAATATCGGATGATTATTATCCGCTCATAACCGATTATTTCAAAAGACATTACGCTTACTATGCAAGCCCTGAAGATATTGTATTTTGCCCGCGAATAATTCAAGCGGTATCAATTTATATCAGAGAATTTACAACCGAGAACGATACTATTTGCTTATTTACGCCTTCTTATTCGCCTATGCTTAATGCCGTATTACTAAATAACCGAAAGCTGTCGCAATTTCCTTTAGTTTACTACAATCAAAAATATCATATTGATTTTAAAAAACTGGAAATATGTTTTAGTCATTCCGACGTATTTATTCTGATTTCTCCACATAATCCCACCGGTTTGGTGTTTAGCATTCAGGATCTCAATCGAATTGCATTACTGGCGGAAAAGTATCATGTCTTTATTATTTCGGATGATATTCATGCAGATTTTGATTTTTCAGGCGAGAAACATCATATTATTTCTTCGATTAATCATTATGTAAAAGAACATTCGATTATTTGCACTTCCCCGTCAAAAACCTTTAATTTAGCCGGTTTAGAAATTTCAAATCTGATTATTCATAATCACGTCATACGAAATAAATTTAATCGATTACTGCAACAATTAGGCATCCATAATCCTAATTACTTCTCCATTCCCGCCATAAAAGCAGCTTACCGAAACGGTGATGTCTGGCTGAGAGAATTACAACAATATATCCTTGAGAATAAGCAGTTTGTTAAACGTTTCTTTACAGCGCATATTCCTGAACTGGACGTCGCTGATACAACCGGTACCTATCTGGTATGGGTTAATTATTCCCGCTTAAAAATAGACGAACAGCTATTGAAACATTGGCTATTGCATTTAGCCCGCGTTGAAATGTCTTGGGGAAGTGACTTCGGGGAAGATGGGAATAGATTCTTTCGTATGAATATTGCAGTACCACGCTCCTGTTTGATTAGTTGTTTAAACAGAATTAAGCAGGCTTTTCTTTTATTAAAAAAAGAGGGATATTGCTATGCAGCACAG","","","46505","MEIKFDQWVNRIGTDSAKWDVPYSKYGSDIIPLSVADMDLPAPQEIIELLNERNWLGIYGYTIISDDYYPLITDYFKRHYAYYASPEDIVFCPRIIQAVSIYIREFTTENDTICLFTPSYSPMLNAVLLNNRKLSQFPLVYYNQKYHIDFKKLEICFSHSDVFILISPHNPTGLVFSIQDLNRIALLAEKYHVFIISDDIHADFDFSGEKHHIISSINHYVKEHSIICTSPSKTFNLAGLEISNLIIHNHVIRNKFNRLLQQLGIHNPNYFSIPAIKAAYRNGDVWLRELQQYILENKQFVKRFFTAHIPELDVADTTGTYLVWVNYSRLKIDEQLLKHWLLHLARVEMSWGSDFGEDGNRFFRMNIAVPRSCLISCLNRIKQAFLLLKKEGYCYAAQ","980153","","aminotransferase","Cytoplasm","","
InterPro
IPR004839
Domain
Aminotransferase, class I and II
PF00155\"[28-240]TAminotran_1_2
InterPro
IPR015422
Domain
Pyridoxal phosphate-dependent transferase, major region, subdomain 2
G3DSA:3.90.1150.10\"[224-394]Tno description
noIPR
unintegrated
unintegrated
PTHR11751\"[45-389]TSUBGROUP I AMINOTRANSFERASE RELATED
PTHR11751:SF21\"[45-389]TAMINOTRANSFERASE RELATED


","BeTs to 5 clades of COG1168COG name: PLP-dependent aminotransferaseFunctional Class: EThe phylogenetic pattern of COG1168 is ---------drlb-e--h--------Number of proteins in this genome belonging to this COG is","Significant hit ( 7.3e-06) to 2/3 blocks of the IPB001511 family, which is described as \"Aminotransferases class-I\". Interpro entry for IP:IPR001511. IPB001511B 163-177 0.0019 IPB001511C 230-243 1.9","Residues 106 to 237 match (1e-07) PD:PD535992 which is described as SYSTEM PROTEOME IIC COMPLETE PTS TRANSFERASE PHOSPHOTRANSFERASE ENZYME ","","","","","Thu Feb 13 17:24:39 2003","","","","","","","Fri Jan 10 16:01:56 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01458 is paralogously related to AA00084 (2e-06) and AA02757 (8e-04).","","","","","","Residues 74 to 386 (E-value = 1.7e-07) place AA01458 in the Aminotran_1_2 family which is described as Aminotransferase class I and II (PF00155)","","","","","","","","1","","","" "AA01459","980143","981552","1410","ATGCAGCACAGTAACACACAAATAAAAATACCGACTTTAGCACAAGCACTATCACCAATAATCGTTATGTTACTATTATTGGGCTTAGGTTATGCGCTGTTTGATCTGCCGCCGGAACCACTCATGGTAGTTTCTTGTGTGTTTGCCGGCTTTTTAGTGAAATATTTAGGCTTTCGCTATAATGATATGCTGAACGCTATTGCAGGGAAAATTGCTAAAACTATGCCGGCATTATTGATTTTAATCACCGTCGGTTTACTCATCGGGACTTGGATTGCAGGTGGTACGATTCCGATGATGATTTATTATGGGTTGAAGGTAATTGATCCTAAATTTTTATACATTACCGCCTTGTTTTTGACTTCTGTGGTTTCTATTTGTACTGGCACATCTTGGGGTTCGGCCGGAACCGTAGGCGTGGCTTTTATGGGGGTCGCGACCGGATTAAACGCCAACCTTGCCGCCACCGCAGGTGCTGTCGTAGCAGGAGCCTATTTCGGGGATAAGCTTTCACCGTTATCCGACACCACAAATATCGCATCGGCAGCAACCGGTGTGGATTTATATGAGCATATTACCCATCTGTTATATACCACACTCCCGTCTTTTATACTGGCAGCGATAGTTTATATCATATATGGAATGAATGCGGATTTTCAGAACGTAGCAACGCCGGAAAAAGTTGCACTCATGCTATCCGGTTTGGAGTCAATTTATCATTTCAACTTGTTATTATTAATTCCTGTCATCATTATTTTATGGGGCTCCATTACCAAAAAACCGACCATTCCGGTCATGTTATTATCGGCATTCGTTGCAATGTCAAATGCATTTTTTATCCAACACGTTGCGTTGCATGACATTGTAAACAGTGCGGTTAATGGTTTTAATGTATCAATGGTCCATAGTGATGTTCAAATTAGTTCGGATTTAAACCGTCTGTTAAATCGTGGCGGGATGAATTCAATGATGGGAACTTTACTGATCTGCTTTTGCGCATTATCGTTCGCCGGTGTTTTATCATTAAGCGGCGCATTGGATGTCATTATTAACAATCTATTGAAATTGGTAAAATCCACTGCGTCACTCATTGTCGCGACGATTATCTGCGGCTTAACCATGATAGGTGTAACCAGCAACGGGCAGGTTTCCATCCTGATTCCGGGTGAAATGCTACGGGATGCCTATATCGAACGTGATCTGCACCCCAAAAATCTCAGCCGGACGATAGAAGACTCGGCGACTATCATTGAACCGATCCTACCTTGGACAGCTGCCGGCGCTTATATGGCCGGCACTTTAGGCGTAGCGACATTGTCTTATTTACCTTGGGCCGTGCTATGCTGGAGCGGTATCGTCTTTGCGACAATTTGGGGAATTACCAGTTTCGGTATAGCTAAATTAAATCAA","","","50023","MQHSNTQIKIPTLAQALSPIIVMLLLLGLGYALFDLPPEPLMVVSCVFAGFLVKYLGFRYNDMLNAIAGKIAKTMPALLILITVGLLIGTWIAGGTIPMMIYYGLKVIDPKFLYITALFLTSVVSICTGTSWGSAGTVGVAFMGVATGLNANLAATAGAVVAGAYFGDKLSPLSDTTNIASAATGVDLYEHITHLLYTTLPSFILAAIVYIIYGMNADFQNVATPEKVALMLSGLESIYHFNLLLLIPVIIILWGSITKKPTIPVMLLSAFVAMSNAFFIQHVALHDIVNSAVNGFNVSMVHSDVQISSDLNRLLNRGGMNSMMGTLLICFCALSFAGVLSLSGALDVIINNLLKLVKSTASLIVATIICGLTMIGVTSNGQVSILIPGEMLRDAYIERDLHPKNLSRTIEDSATIIEPILPWTAAGAYMAGTLGVATLSYLPWAVLCWSGIVFATIWGITSFGIAKLNQ","981552","From GenBank (gi:2498052): This protein is an integral membrane protein.","Na(+)/H(+) antiporter","Inner membrane, Cytoplasm","","
InterPro
IPR004770
Family
Na+/H+ antiporter NhaC
PF03553\"[163-463]TNa_H_antiporter
TIGR00931\"[9-469]Tantiport_nhaC: Na+/H+ antiporter NhaC
noIPR
unintegrated
unintegrated
signalp\"[1-32]?signal-peptide
tmhmm\"[9-31]?\"[37-57]?\"[78-98]?\"[112-134]?\"[149-167]?\"[197-217]?\"[238-258]?\"[262-280]?\"[327-349]?\"[355-375]?\"[420-440]?\"[446-466]?transmembrane_regions


","No hits to the COGs database.","","Residues 9 to 60 match (6e-08) PD:PD426282 which is described as HI1107 SYMPORT PROTEOME TRANSMEMBRANE SODIUM COMPLETE ANTIPORTER NA/H ","","","","","","","","","","","Mon Jan 13 10:10:37 2003","Mon Jan 13 10:10:37 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01459 is paralogously related to AA02294 (6e-09) and AA00143 (1e-04).","","","","","","Residues 163 to 463 (E-value = 8.3e-89) place AA01459 in the Na_H_antiporter family which is described as Na+/H+ antiporter family (PF03553)","","","","","Pragai Z, Eschevins C, Bron S, Harwood CR.Bacillus subtilis NhaC, an Na+/H+ antiporter, influences expression of the phoPR operon and production of alkaline phosphatases.J Bacteriol. 2001 Apr;183(8):2505-15.PMID: 112741107: Krulwich TA, Guffanti AA, Ito M.pH tolerance in Bacillus: alkaliphiles versus non-alkaliphiles.Novartis Found Symp. 1999;221:167-79; discussion 179-82.PMID: 10207919 Ito M, Guffanti AA, Zemsky J, Ivey DM, Krulwich TA.Role of the nhaC-encoded Na+/H+ antiporter of alkaliphilic Bacillus firmus OF4.J Bacteriol. 1997 Jun;179(12):3851-7.PMID: 9190799 ","","Mon Jan 13 10:10:37 2003","1","","","" "AA01460","981656","981552","105","TTGCGGCAACTGATATTAGCATACACAAATTCGCCGCGAAGAAAACTGCTTTATTTCATCTCTGTGATTTCACTCAAAAAACCGACCGCACTTTTTAACGGCTAT","","","4081","LRQLILAYTNSPRRKLLYFISVISLKKPTALFNGY","981552","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 16:56:19 2004","Thu Feb 26 16:56:19 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01460 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 16:56:19 2004","","","","","","","","","","","","","1","","","" "AA01462","981670","982839","1170","ATGAATAATCAAAAATATTACCGCATTGCGTTGTTATTCAACGCGAACAAAGTCTATGACCGGGAAGTGGTTGAGGGTGTGGGGCAGTATTTGCAGGCATCGCAATGTATGTGGGATATTTTTGTGGAAGATGAGTTTATTTATCATAAAGATACCATCAACAACCTGTCTATTGACGGCATCATCGCCGATTTCGATGATGCCGAAACCGTCGAGTTACTTAAAAATATATCGATTCCGCTCATTGCCGTGGGCGGCTCTTATCAAAATCCCGCGTTTTATCCCAATCTGCCTTACGTCGCCACCGATAATTATGCCTTGGTGGAAACCGCTTTTTTACATTTGAAACAAAAAGGCATTACCAGCTTTGCGTTTTATGGTTTGGAGACGGAAGAAACCAAGCATTGGGCAAATGAAAGAAAAGACGCGTTTCTTGCATTAATGCAGAAATATGAATTCCAAAGTGCGGTCTATTTAGGCGACAAAACTGACTCACAGAACTGGGCGCAGGAACAGGCGAAAGTCACCGACTGGCTTAAAACTTTGCCACCCCACACCGGCATTATCGCCGTCACCGACGCCCGCGCACGGCATATTCTGCAAGCCTGCGAAACCGCCGGCATTGCCGTGCCGGAGCAACTCTGCGTGATCGGCATTGATAACGAAGAACTGATTCAATATTTATCCCGTGTCTCCCTTTCTTCTGTGGCACAAGGCACGCGGGAAATCGGTTACCAGGCAGCGAAACTGCTGCACCGTTTATTAACTGGGCAAAAAGTCGCCGCCACACCGCTTCTGATCCCGCCGGTAAAAGTTATCGAACGCAGCTCCACCGATTACCGCTCCCTGCGCGACCCGCTGGTGATGCAAGCCATGCACTACATCCGCCACCGCGCCTGCCAAGGCATTAAAGCGGAACAGGTGCTGGATTACCTGCGCACCTCCCGTTCCAATTTAGAAGCCCGTTTTAAAGCGGAAATGAACAAAACCATTCATCAGGTCATCCACGAAGAAAAAATCACCCGCGCCAAACAGCTACTGCGTCGCAGCGATATTCCCATTCAGGAAATCTCCGACATTTGCGGCTACCCGTCACTACAATACTTTTACTCGGTATTCAAAAAAGAATTTAATCAAACCCCGAAAGAGTTTCGAAATCGTGAAGGGAAG","","","46092","MNNQKYYRIALLFNANKVYDREVVEGVGQYLQASQCMWDIFVEDEFIYHKDTINNLSIDGIIADFDDAETVELLKNISIPLIAVGGSYQNPAFYPNLPYVATDNYALVETAFLHLKQKGITSFAFYGLETEETKHWANERKDAFLALMQKYEFQSAVYLGDKTDSQNWAQEQAKVTDWLKTLPPHTGIIAVTDARARHILQACETAGIAVPEQLCVIGIDNEELIQYLSRVSLSSVAQGTREIGYQAAKLLHRLLTGQKVAATPLLIPPVKVIERSSTDYRSLRDPLVMQAMHYIRHRACQGIKAEQVLDYLRTSRSNLEARFKAEMNKTIHQVIHEEKITRAKQLLRRSDIPIQEISDICGYPSLQYFYSVFKKEFNQTPKEFRNREGK","982839","","xylose operon regulatory protein","Cytoplasm","","
InterPro
IPR000005
Domain
Helix-turn-helix, AraC type
PR00032\"[354-369]T\"[369-385]THTHARAC
PF00165\"[290-336]T\"[342-386]THTH_AraC
SM00342\"[302-385]THTH_ARAC
PS01124\"[289-387]THTH_ARAC_FAMILY_2
PS00041\"[339-381]THTH_ARAC_FAMILY_1
InterPro
IPR012287
Domain
Homeodomain-related
G3DSA:1.10.10.60\"[340-388]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2300\"[103-244]Tno description
PTHR11019\"[315-387]TTHIJ/PFPI
PTHR11019:SF11\"[315-387]TARAC FAMILY TRANSCRIPTIONAL REGULATORY PROTEIN


","BeTs to 4 clades of COG1609COG name: Transcriptional regulatorsFunctional Class: KThe phylogenetic pattern of COG1609 is --------vdrlb-efghs--j----Number of proteins in this genome belonging to this COG is","Significant hit ( 2.8e-12) to 1/1 blocks of the IPB000005 family, which is described as \"AraC type helix-turn-helix\". Interpro entry for IP:IPR000005. IPB000005 354-385 2.8e-12Significant hit ( 5.6e-06) to 2/6 blocks of the IPB003313 family, which is described as \"Arac arabinose-binding and dimerisation domain\". Interpro entry for IP:IPR003313. IPB003313E 303-348 1.9 IPB003313F 349-389 0.0013","Residues 339 to 382 match (1e-09) PD:PD597285 which is described as REGULATION DNA-BINDING TRANSCRIPTION PLASMID ACTIVATOR PERA TRANSCRIPTIONAL OPERON COMPLETE VIRULENCE ","","","","","","","","","","","","Mon Jan 13 10:11:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01462 is paralogously related to AA02003 (3e-04) and AA02673 (0.001).","","","","","","Residues 342 to 386 (E-value = 9.1e-15) place AA01462 in the HTH_AraC family which is described as Bacterial regulatory helix-turn-helix proteins, araC family (PF00165)","","","","","Devos D, Garmendia J, de Lorenzo V, Valencia A.Deciphering the action of aromatic effectors on the prokaryotic enhancer-binding protein XylR: a structural model of its N-terminal domain.Environ Microbiol. 2002 Jan;4(1):29-41.PMID: 11966823 Garmendia J, Devos D, Valencia A, de Lorenzo V.A la carte transcriptional regulators: unlocking responses of the prokaryoticenhancer-binding protein XylR to non-natural effectors.Mol Microbiol. 2001 Oct;42(1):47-59.PMID: 11679066 9: Fraile S, Roncal F, Fernandez LA, de Lorenzo V.Monitoring intracellular levels of XylR in Pseudomonas putida with a single-chain antibody specific for aromatic-responsive enhancer-binding proteins.J Bacteriol. 2001 Oct;183(19):5571-9. PMID: 11544219 ","","Mon Jan 13 10:20:25 2003","1","","","" "AA01463","984260","982872","1389","ATGAGTGAGCGTCAACATTACCGTAATTTAGCCCTAATTGCCGCCATGGCATTGTTTATGCAATCCCTTGACGCTACCATTTTGAACACCGCGCTACCCGCCATTTCCGCCGATTTGCATGAATCGCCGCTGGAAATGCAAATGACGATCATCAGTTATTCCCTCACCGTTGCCCTGTTTATTCCGCTCACCGGATGGATCGCCGATAAATACGGCACGCTCAATGTGTTTCGGGTGGCAGTGACGATTTTTGTACTCGGTTCCGTCGCCTGTGCGGTATCCAATTCATTGAATGCGCTGATTTGGTCGCGTGTGTTGCAGGGGCTGGGCGGCGCGCTGATGATGCCGGTGGCGCGTTTGGCAATTATTCGCAACGTGCCGAAAACCCAGCTGGTTGCTGCGTGGAATGCCATGGCGATGGCAGGGCTTATCGGTCCGGTGCTGGGACCGATTGTGGGCGGTTGGCTGGTGACGCACGCCACATGGCATTGGATTTTCTTGATTAACATTCCTATCGGTTTGCTCGGCGTTTGGTTTGCCGGACGACATATGCCGAACAGTACGGGCAATATCGGTAAACTGGATTGGCGGGGCTTCGTACTGTTTGCCGGCGGCTTGGCAGGCTTGACCCTCGGTTTGGATTTGTTGTCCGAAGATCGTGTCAGCCAATGGATGACCGCCTTGATTCTGGCTGCCGGAATCGGTTGTTTTTCCATTTATTATTTTTATGCCCGACGGGCACAATATCCCTTATTGTCGCTCAATATATTTGCGGTTCGCACCTTTCGGGTAGGCATCGTCGCCAACCTCTTCATTCGCTTGAGTGGTTCCGGCATTCCATTTTTAATGCCGCTTATGTTGCAGGTGGTGTTTAATTATGGCGCCGATGCTGCCGGTTGGTTACTCGCGCCGATCGCCGTGAGTTCGGTGTTGACCAAATCCTTCGCAGGGAAAGTTCTGTCGCGCTTCGGCTACAAAACGACGTTAATTTTGACCGCACTTTCCATGACCTTCGCCATCGCCACCATGAGCCTCTTAGATCAGCAAAGCCCGATTTGGCTGTTGGTGCTGATTCTGGCGTGGTACGGTTGTTCCATGTCGATTATTTTCACCGCCGTCAACACCCTCACCATTAGCGACTTAAACGACCACAATGCCAGCACCGGTTCCACTTATCTCAGCGTCATCCAACAAGTGGGGATTGGTATCAGCATCGCCGTCTCTTCCGTCATCTTAGACCTCTACCGCCACTTCATCGGCGAAAACGGCACACAACTGCAACACGCCTTCAGCGCCACTTTCCTCACCTCCGCCCTCTTCGGCATCGCCCTGTTGTGGGTCTTGAGTTATCTTAAAAGCGAGGATGGTGAGGGGAATTTTCGGAAGGGG","","","52706","MSERQHYRNLALIAAMALFMQSLDATILNTALPAISADLHESPLEMQMTIISYSLTVALFIPLTGWIADKYGTLNVFRVAVTIFVLGSVACAVSNSLNALIWSRVLQGLGGALMMPVARLAIIRNVPKTQLVAAWNAMAMAGLIGPVLGPIVGGWLVTHATWHWIFLINIPIGLLGVWFAGRHMPNSTGNIGKLDWRGFVLFAGGLAGLTLGLDLLSEDRVSQWMTALILAAGIGCFSIYYFYARRAQYPLLSLNIFAVRTFRVGIVANLFIRLSGSGIPFLMPLMLQVVFNYGADAAGWLLAPIAVSSVLTKSFAGKVLSRFGYKTTLILTALSMTFAIATMSLLDQQSPIWLLVLILAWYGCSMSIIFTAVNTLTISDLNDHNASTGSTYLSVIQQVGIGISIAVSSVILDLYRHFIGENGTQLQHAFSATFLTSALFGIALLWVLSYLKSEDGEGNFRKG","982872","","probable transport protein","Inner membrane, Cytoplasm","","
InterPro
IPR001411
Family
Tetracycline resistance protein TetB
PR01036\"[13-37]T\"[104-124]T\"[134-158]T\"[353-373]TTCRTETB
InterPro
IPR004638
Family
Drug resistance transporter EmrB/QacA subfamily
TIGR00711\"[10-451]Tefflux_EmrB: drug resistance MFS transporte
InterPro
IPR007114
Family
Major facilitator superfamily
PS50850\"[10-455]TMFS
InterPro
IPR011701
Family
Major facilitator superfamily MFS_1
PF07690\"[14-413]TMFS_1
noIPR
unintegrated
unintegrated
PTHR10074\"[1-198]T\"[248-453]TMAJOR FACILITATOR SUPERFAMILY MEMBER
PTHR10074:SF57\"[1-198]T\"[248-453]TDRUG RESISTANCE TRANSPORTER, EMRB/QACA FAMILY-RELATED
signalp\"[1-25]?signal-peptide
tmhmm\"[10-28]?\"[50-68]?\"[73-93]?\"[99-117]?\"[132-154]?\"[160-178]?\"[199-217]?\"[221-243]?\"[264-284]?\"[290-310]?\"[325-345]?\"[351-371]?\"[392-412]?\"[431-451]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Jan 13 10:22:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01463 is paralogously related to AA01731 (8e-48), AA00062 (3e-09) and AA00266 (3e-06).","","","","","","","","","","","","","","1","","","" "AA01464","984463","984350","114","GTGTCCGCAATGCCGTTGTGTGAAAAAAACAATCGTCCGATTTGTCGTTGGTACAATAAAATCGGATTAAAATTGCATGCAATAGGCGCGAATCATGTAGAATACGGGCAAAAT","","","4321","VSAMPLCEKNNRPICRWYNKIGLKLHAIGANHVEYGQN","984350","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 16:54:54 2004","Thu Feb 26 16:54:54 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01464 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 16:54:54 2004","","","","","","","","","","","","","1","","","" "AA01465","984612","985607","996","ATGACCATTGCTATTATTATCGCAACACATGGGGTCGCGGCGGAGCAGCTGTTAAAAACCACAGAAATGCTCATCGGCGAACAGGAAAATGTGGCGACCATTGATTTTGTGCCCGGTGAAAACGCCGAGACCATCATGGAAAAATATCAGGCGAAACTCAGCGGCGATCTTGCCCATTGCGACAAAGTGCTGTTTTTGGTGGATACCTGGGGCGGCAGTCCGTTTAATGCGGCAAACCGCGTGTCGGAAGGCAAGGACAACATGGATATCGTCACCGGTGTGAACGTGCCAATGTTGGTGGAAACCTTCATGGCGCGAGATGACGGTCCAAGTTTGGATGAATTGGTGGCAATCGCCTTAGAAACCGGCCGTACCGGCGTACGTGCGCTGCGTTATCAGGAGCCGGAAACCGAACCGACCGCGCCAACATCCGAGGTTCCAGCACAACCCGCCGCATCACAAGCGGAACCGCAACCGGCGATGGTCACACCGAATCAGGAAGGGCATTTGGAAATCGGTTTGGCGCGTATTGACGACCGATTGATTCACGGGCAAGTGGCAACCCGTTGGACGAAAGAAAGCCGTGTATCGCGCATTGTGGTGGTGAGCGACGAAGTGGCGAAAGACACCGTGCGCGCGACCATGCTAAAAAGCGTTGCACCGCCCGGGGTCACCGCCCACGTGGTAAACGTGGATAAAATGGTGCGGGTTTACAACAACCCTGAATATGCCGGCGAACGCATGATGTTGCTGTTTACCAATCCGACGGACGTATTGCGTCTTTCCGATGCGGGCGTTGATTTTAAATCCATCAATGTGGGTGGCATGGCGTATCGCGATGGTAAAAAAATGATTACCAATGCGGTATCCGTGGACGACAAAGATATTGCCGCCTTCAAAGCCCTTGATGCCAAAGGCATTGAGCTGGACGTGCGTAAAGTTTCAAATGACAACCGCCAGTACATGATGGATTTATTGAAGAAAAATAACTTACTT","","","36223","MTIAIIIATHGVAAEQLLKTTEMLIGEQENVATIDFVPGENAETIMEKYQAKLSGDLAHCDKVLFLVDTWGGSPFNAANRVSEGKDNMDIVTGVNVPMLVETFMARDDGPSLDELVAIALETGRTGVRALRYQEPETEPTAPTSEVPAQPAASQAEPQPAMVTPNQEGHLEIGLARIDDRLIHGQVATRWTKESRVSRIVVVSDEVAKDTVRATMLKSVAPPGVTAHVVNVDKMVRVYNNPEYAGERMMLLFTNPTDVLRLSDAGVDFKSINVGGMAYRDGKKMITNAVSVDDKDIAAFKALDAKGIELDVRKVSNDNRQYMMDLLKKNNLL","985607","","mannose-specific phosphotransferase element","Cytoplasm","","
InterPro
IPR004701
Domain
Phosphotransferase system, fructose subfamily IIA component
G3DSA:3.40.50.510\"[2-137]Tno description
PF03610\"[3-120]TEIIA-man
PS51096\"[2-127]TPTS_EIIA_TYPE_4
InterPro
IPR004720
Domain
Phosphotransferase system, sorbose subfamily IIB component
PD008332\"[178-317]TQ9CMJ0_PASMU_Q9CMJ0;
G3DSA:3.40.35.10\"[170-328]Tno description
PF03830\"[171-321]TPTSIIB_sorb
TIGR00854\"[171-321]Tpts-sorbose: PTS system, mannose/fructose/s
PS51101\"[168-332]TPTS_EIIB_TYPE_4
InterPro
IPR013789
Domain
Phosphotransferase system, fructose subfamily IIA component, subgroup
TIGR00824\"[2-119]TEIIA-man: PTS system, mannose/fructose/sorb
noIPR
unintegrated
unintegrated
signalp\"[1-14]?signal-peptide


","No hits to the COGs database.","","Residues 1 to 127 match (7e-58) PD:PD328938 which is described as PROTEOME COMPLETE PTS COMPONENT SYSTEM IIA TRANSFERASE SYSTEM IIAB PHOSPHOTRANSFERASE ","","","","","","","","","","","","Mon Jan 13 10:26:31 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01465 is paralogously related to AA00478 (8e-73).","","","","","","Residues 171 to 321 (E-value = 3.7e-93) place AA01465 in the PTSIIB_sorb family which is described as PTS system sorbose subfamily IIB component (PF03830)","","","","","Lortie,L.A., Pelletier,M., Vadeboncoeur,C. and Frenette,M. The gene encoding IIABLMan in Streptococcus salivarius is part of a tetracistronic operon encoding a phosphoenolpyruvate:mannose/glucose phosphotransferase system.Microbiology 146:677-685,2000. Nunn,R.S., Markovic-Housley,Z., Genovesio-Taverne,J.C., Flukiger,K., Rizkallah,P.J., Jansonius,J.N., Schirmer,T. and Erni,B. Structure of the IIA domain of the mannose transporter from Escherichia coli at 1.7 angstroms resolution Journal of molecular biology. 259 (3), 502-511 (1996) PubMed: 8676384 Markovic-Housley,Z., Balbach,J., Stolz,B. and Genovesio-Taverne,J.C. Predicted topology of the N-terminal domain of the hydrophilic subunit of the mannose transporter of Escherichia coli FEBS letters. 340 (3), 202-206 (1994) PubMed: 8131846 Gschwind,R.M., Gemmecker,G., Leutner,M., Kessler,H., Gutknecht,R., Lanz,R., Flukiger,K. and Erni,B. Secondary structure of the IIB domain of the Escherichia coli mannose transporter, a new fold in the class of alpha/beta twisted open-sheet structures FEBS letters. 404 (1), 45-50 (1997) PubMed: 9074635 ","","Mon Jan 13 10:26:31 2003","1","","","" "AA01466","985622","986422","801","ATGGAAATTACCACTTTACAAATTATTCTGGTGTTTCTGGTCGCCTGTATTTGCGGCGCAGGATCGATTCTTGACGAATGGCAAACCCAACGCCCGTTAATTGCCTGTACCTTAATCGGCTTAGTGTTGGGCGATATTCAAACCGGTATCATTATCGGCGGGACCTTGGAATTATTGGCGTTAGGCTGGATGAATATCGGCGCGGCCGTGGCACCTGATGCGGCACTGGCCTCCGTGATTTCAACCATTTTGGTTATCGTCGGTAAACAAGAAATCTCTACCGGAATTGCGGTGGCGATTCCGCTTGCCGCCGCCGGTCAGGTGTTGACCTATATCGTGCGCGCCATCACCGTGGGTTTCCAACATGCCGCGGATAAATCAGTGGAAGACGGCAACCTAACGCGTTTAGACTGGTTACATTGCAGTGCGCTAATGTTACAAGCCATGCGGATCGCCATTCCGGCGCTGATCGTCGCCTTAACCGCCGGTACTGATGAGGTACAAAGCATGCTGAACGCCATTCCTGACGTAGTGACAACCGGGCTTAAAATCGCCGGTGGCTTCATCGCTGTGGTCGGTTATGCCATGGTAATCAACATGATGCGTGCAGGGCATTTAATGCCATTCTTCTATGCGGGCTTTGTCATCGCCGCTTATACCGAATTCAATCTGGTTGCCCTCGGTGTGTTAGGCATCGTGATGGCGGTGTTATATATTCAAATGCACCCGAAATATAACCAAAGCAAGCAAGTGGTGCAGGTAACAACTGCCGCCGGCAATGACTTGGACAATAGACTGGAT","","","28364","MEITTLQIILVFLVACICGAGSILDEWQTQRPLIACTLIGLVLGDIQTGIIIGGTLELLALGWMNIGAAVAPDAALASVISTILVIVGKQEISTGIAVAIPLAAAGQVLTYIVRAITVGFQHAADKSVEDGNLTRLDWLHCSALMLQAMRIAIPALIVALTAGTDEVQSMLNAIPDVVTTGLKIAGGFIAVVGYAMVINMMRAGHLMPFFYAGFVIAAYTEFNLVALGVLGIVMAVLYIQMHPKYNQSKQVVQVTTAAGNDLDNRLD","986422","","mannose-specific phosphotransferase system IIC","Inner membrane, Cytoplasm","","
InterPro
IPR004700
Family
Phosphotransferase system, sorbose-specific IIC subunit
PF03609\"[3-238]TEII-Sor
TIGR00822\"[1-266]TEII-Sor: PTS system, mannose/fructose/sorbo
PS51106\"[3-237]TPTS_EIIC_TYPE_4
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide
tmhmm\"[4-24]?\"[39-61]?\"[67-87]?\"[144-164]?\"[178-198]?\"[208-239]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Jan 13 10:30:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01466 is paralogously related to AA00479 (6e-89).","","","","","","Residues 3 to 238 (E-value = 1.4e-139) place AA01466 in the EII-Sor family which is described as PTS system sorbose-specific iic component (PF03609)","","","","","Erni,B., Zanolari,B. and Kocher,H.P. The mannose permease of Escherichia coli consists of three different proteins. Amino acid sequence and function in sugar transport, sugar phosphorylation, and penetration of phage lambda DNA. J. Biol. Chem. 262(11):5238-5247,1987. PubMed: 2951378. Wehmeier,U.F. and Lengeler,J.W. Sequence of the sor-operon for L-sorbose utilization from Klebsiella pneumoniae KAY2026. Biochim. Biophys. Acta 1208(2):348-351,1994. PubMed: 7947968. Martin-Verstraete,I., Debarbouille,M., Klier,A. and Rapoport,G. Levanase operon of Bacillus subtilis includes a fructose-specific phosphotransferase system regulating the expression of the operon. J. Mol. Biol. 214(3):657-671,1990.PubMed: 2117666.","","Mon Jan 13 10:30:09 2003","1","","","" "AA01467","986441","987274","834","ATGACAACCGAAGTCAGAAAAGTAACAAAAAGTGATTTGAACGCCGTCGTAATGCGCTCCAACCTGTTCCAAGGGTCATGGAACTTCGAACGTATGCAGGCGTTGGGCTTTGCCTATTCCATGGTACCGGTAATCAAACGGTTATACCCAGTACAGGATTCCCAAGAGCGCAAAGACGCCATTAAACGCCACCTGGAATTTTTCAACACCCAGCCTTTCGTCGGCGCACCCGTATTAGGCGTGGCAATTGCCATGGAAGAACAACGTGCCAACGGCAAACCGGTGGAAGATGCCGCCATCAACGGGATTAAAGTGGGTCTCATGGGACCGCTTGCCGGCGTGGGCGACCCGATTTATTGGGGGACCGCGCGTCCGGTCTTCGCTGCACTCGGCGCAGGCTTAGCGTTAAACGGCAGCATTTTAGGTCCGATTCTGTTCTTCGTTTTATTTAACCTCGTGCGTCTCGCCACCCGTTACTACGGCGTAATTTACGGCTACCGCAAAGGGCTGGACGTGGTCAGCGACATGAGTGGCGGCTTATTGCAAAAACTTACCGAAGGCGCATCAATCCTCGGTTTGTTCATCATGGGCGCCCTAGTGCAAAAATGGACCAGCATTAATGTACCGTTAGTAGTTTCCACCATCAAAAAACAAAACGGCACCGTTGAAGTCACCACCGTACAAAGCATCTTGGACAGTCTCATGCCAGGCTTACTGGCGATACTGCTCACCTTCGCCTGTATGTGGCTGCTGCGCAATCGGGTAAACGCCCTGTGGATCATCGTTGGCTTCTTCGTCATCGGCATCTTCGGCGCCTGGACGGGCACCCTCGCG","","","30275","MTTEVRKVTKSDLNAVVMRSNLFQGSWNFERMQALGFAYSMVPVIKRLYPVQDSQERKDAIKRHLEFFNTQPFVGAPVLGVAIAMEEQRANGKPVEDAAINGIKVGLMGPLAGVGDPIYWGTARPVFAALGAGLALNGSILGPILFFVLFNLVRLATRYYGVIYGYRKGLDVVSDMSGGLLQKLTEGASILGLFIMGALVQKWTSINVPLVVSTIKKQNGTVEVTTVQSILDSLMPGLLAILLTFACMWLLRNRVNALWIIVGFFVIGIFGAWTGTLA","987274","","mannose-specific phosphotransferase system IID","Inner membrane, Cytoplasm","","
InterPro
IPR004704
Family
Phosphotransferase system, mannose/fructose/sorbose family IID component
PF03613\"[6-277]TEIID-AGA
TIGR00828\"[6-277]TEIID-AGA: PTS system, mannose/fructose/sorb
PS51108\"[6-277]TPTS_EIID
noIPR
unintegrated
unintegrated
tmhmm\"[126-148]?\"[230-250]?\"[255-275]?transmembrane_regions


","No hits to the COGs database.","","Residues 143 to 258 match (1e-20) PD:PD242695 which is described as PROTEOME COMPLETE PTS IID SYSTEM COMPONENT MANNOSE-SPECIFIC PERMEASE TRANSFERASE PHOSPHOTRANSFERASE ","","","","","","","","","","","","Mon Jan 13 10:32:04 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01467 is paralogously related to AA00480 (6e-95).","","","","","","Residues 6 to 277 (E-value = 8.7e-173) place AA01467 in the EIID-AGA family which is described as PTS system mannose/fructose/sorbose family IID component (PF03613)","","","","","Erni,B., Zanolari,B. and Kocher,H.P. The mannose permease of Escherichia coli consists of three different proteins. Amino acid sequence and function in sugar transport, sugar phosphorylation, and penetration of phage lambda DNA. J. Biol. Chem. 262(11):5238-5247, 1987. PubMed: 2951378. Martin-Verstraete,I., Debarbouille,M., Klier,A. and Rapoport,G. Levanase operon of Bacillus subtilis includes a fructose-specific phosphotransferase system regulating theexpression of the operon.J. Mol. Biol.214(3):657-671,1990. PubMed: 2117666.","","Mon Jan 13 10:32:04 2003","1","","","" "AA01471","989062","987461","1602","ATGACCGAACTGTATTTCACCGAACAAACCAAAACCCTGATTGACAGCCTGAAAACCATCTGCGCCCACTACGGCTTGGGCAACGACGGCAATGAGTTCAAAATCATCAGTCAGGCTTTTCTGTATAAATTCTTAAACGACAAATATGATTTCGAAGTCAAAAAAATCCTTGAAGAAAAGCCCGGCGAGCCGATGGAATTTGTCGATATGGAGATTCAGAGCAAAACGGCGGTATTGAAGCCGGAGCATTCCATCCGCTATCTGTCGCAAAGGCAAAACGATGCGGATTTTGCCAAATTGTTCGACGATACGCTGATAGACATTGCCGCGCATAATGCCGAAGTGTTCGCGGTGAAAACCGAGGGCGGGGCGAAAATCGTGTTGTTCGAGCGTATCAGCCAATATATCGCTGATGAAAACCGCCGCGACGATTTCTGCCGCGCGCTGATTTCCAAATTGGCGGATTTCAGCTTCGAGGCGGTGTTTGCCCAAAAATTCGATTTTTTCGCGACGATTTTCGAATACCTGATTAAGGACTACGACAGCAATTCGGGCGGCAAATACGCCGAATACTACACGCCGCACGCGGTGGCGCGGATTATGGCGGATATTTTGGTGCCTCAAGATGTGCGCGGACAAATCCGCAGTGTGGACGTGTACGACCCGTCGGCAGGTTCGGGAACGCTGCTGATGAATGTGGCGCACGCCATCGGCGAAGACAAATGTATGATTTATACGCAGGATATTTCGCAAAAATCGTCCAACCTGTTGCGCTTGAACCTGGTTCTGAACAATCTGGTGCATTCTTTGAATAATGTGATTCAGGGCAATACGATTTTGTCGCCTTACCATAAGGATAAAGTAGGTCGTCTGAAAAAATTCGATTTCATCGTGTCCAATCCGCCGTTTAAGTTGGATTTCAGCGATTTCCGCGACCAATTGGACAGCGCGGAAAACCGCGAACGCTTTTTTGCGGGGATTCCGAAAATCAAGGCGAAAGACAAGGATAAGATGGAAATCTACCAGCTTTTTATCCAGCATATCCTGTTCAGCCTGAAAGAAAACGGCAAGGCGTCGATTGTGTTGCCAACGGGCTTTATCACCGCTCAATCGGGCATAGACAGAAAAATCCGCGAATATCTGGTGGAAAATAAAATGCTCGCCGGCGTGGTGTCTATGCCTTCCAATATTTTCGCCACCACGGGAACCAATGTTTCCATCCTGTTTATTGACAAAGCCAATAAAGACAAAGTGGTATTAATCGACGCGTCTGGCTTGGGCGAAAAAATCAAAGACGGCAAAAACCAAAAAACCGTACTTTCCCGCGAGGAAGAGCAAAAAATCTGCCAAACGTTTACGGACAAACAGGTGGTGGAAAATTTCAGCGTGGTGGTCGGCTACGATGAAATCCAAGCGAAAAACTACAGCCTCTCGGCAGGGCAGTATTTCGAGGTGAAGATTGATTATGTGGATATTTCCGCCGATGAATTCGAGCAGAAAATGGCGGGGTTTTCAGCGGATTTAGACCGGCTTTTTGCGGAGTCTGCCGAATTGGGACGGGAGATTGGGGAGCGGTTGCGGGTGTTGAGGCTTGGGGGGAAA","","","60511","MTELYFTEQTKTLIDSLKTICAHYGLGNDGNEFKIISQAFLYKFLNDKYDFEVKKILEEKPGEPMEFVDMEIQSKTAVLKPEHSIRYLSQRQNDADFAKLFDDTLIDIAAHNAEVFAVKTEGGAKIVLFERISQYIADENRRDDFCRALISKLADFSFEAVFAQKFDFFATIFEYLIKDYDSNSGGKYAEYYTPHAVARIMADILVPQDVRGQIRSVDVYDPSAGSGTLLMNVAHAIGEDKCMIYTQDISQKSSNLLRLNLVLNNLVHSLNNVIQGNTILSPYHKDKVGRLKKFDFIVSNPPFKLDFSDFRDQLDSAENRERFFAGIPKIKAKDKDKMEIYQLFIQHILFSLKENGKASIVLPTGFITAQSGIDRKIREYLVENKMLAGVVSMPSNIFATTGTNVSILFIDKANKDKVVLIDASGLGEKIKDGKNQKTVLSREEEQKICQTFTDKQVVENFSVVVGYDEIQAKNYSLSAGQYFEVKIDYVDISADEFEQKMAGFSADLDRLFAESAELGREIGERLRVLRLGGK","987461","","type I restriction enzyme M (modification chain)","Cytoplasm","","
InterPro
IPR002052
Domain
N-6 Adenine-specific DNA methylase
PS00092\"[297-303]?N6_MTASE
InterPro
IPR002296
Family
N6 adenine-specific DNA methyltransferase, N12 class
PR00507\"[189-205]T\"[219-233]T\"[294-306]T\"[339-363]TN12N6MTFRASE
InterPro
IPR003356
Domain
N-6 DNA methylase
PF02384\"[164-491]TN6_Mtase
InterPro
IPR013212
Domain
Mad3/BUB1 homology region 1
SM00777\"[316-426]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[191-417]Tno description


","BeTs to 15 clades of COG0286COG name: Type I restriction-modification system methyltransferase subunitFunctional Class: LThe phylogenetic pattern of COG0286 is aom-k-----rl--efghsnuj---wNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.4e-22) to 4/4 blocks of the PR00507 family, which is described as \"N12 class N6 adenine-specific DNA methyltransferase signature\". Prints database entry for PR:PR00507. PR00507A 189-205 0.00093 PR00507B 219-233 0.0016 PR00507C 294-306 0.0028 PR00507D 339-363 1.7e-06","Residues 285 to 430 match (7e-08) PD:PD567698 which is described as PROTEOME TRANSMEMBRANE COMPLETE MODIFICATION TRANSFERASE ENZYME METHYLTRANSFERASE ","","","","","","","","","","","","Mon Jan 13 10:58:20 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01471 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 313 to 476 (E-value = 6.9e-43) place AA01471 in the N6_Mtase family which is described as N-6 DNA Methylase (PF02384)","","","","","Beck C, Jeltsch A.Probing the DNA interface of the EcoRVDNA-(adenine-N6)-methyltransferase by site-directed mutagenesis, fluorescence spectroscopy, and UV cross-linking.Biochemistry. 2002 Dec 3;41(48):14103-10.PMID: 12450373Szczelkun MD.Kinetic models of translocation, head-on collision, and DNA cleavage by type I restriction endonucleases.Biochemistry. 2002 Feb 12;41(6):2067-74.PMID: 11827554 Smith MA, Read CM, Kneale GG.Domain structure and subunit interactions in the type I DNA methyltransferase M.EcoR124I.J Mol Biol. 2001 Nov 16;314(1):41-50.PMID: 11724530 Lucchini,S., Sidoti,J. and Brussow,H.Broad-range bacteriophage resistance in Streptococcus thermophilus by insertional mutagenesisVirology 275 (2), 267-277 (2000)PubMed: 10998327","","Mon Jan 13 10:48:48 2003","1","","","" "AA01472","989036","989218","183","TTGTTCGGTGAAATACAGTTCGGTCATTTTTTGTCTCGTTTGTTTTTTATTTCGGTTTTAGTTTCACGTGGCAGACTGAAAAGCGCGGTCGGATTTGGAAGAGTAAGTCGGGCATTTATGCCCGACCTACTCTTCCGCCACGGCTACCTGCCCATTCATCAGCATGGGCAGCAGGAAATCGCG","","","6969","LFGEIQFGHFLSRLFFISVLVSRGRLKSAVGFGRVSRAFMPDLLFRHGYLPIHQHGQQEIA","989218","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-26]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 16:53:22 2004","Thu Feb 26 16:53:22 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01472 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 16:53:22 2004","","","","","","","","","","","","","1","","","" "AA01473","990292","989165","1128","ATGAATGAATTACAAGATTGTATTTTAGGTGATTTGGTAGAGTTCCAACGTGGATATGATTTACCAAAAGATGCTTTTGTAAAAGGCGAATATCCTGTTCAATCTTCCAACGGAATTTTGGGTTATCACAATGAATATAAAGTTAAAGCGCCTGGAATTACGATTGGGAGAAGTGGAACAGTCGGTATTCCACATTTAATAACAAAAAACTTTTTTCCGCATAATACAGCATTGTATGTAAAAGATTTTAAGGGAAATAACGTCCAATATATTTATTACCTATTGAAAAATTTAAAATTAAATGAATATAAAACTGGTTCTGGTGTTCCAACCATGAACCGAAATCATCTGCATCCGTTAAAAATCAGAGCGTTCACCAACCTCAAAACCCAACAATCCATCGCCGCCGTTCTCTCTGCCTTGGATAAAAAAATCGCCCTGAACAAACAAATCAACGCGCGCTTGGAAGAGATGGCGAAAACCCTGTACGACTACTGGTTCGTGCAGTTCGACTTCCCCGACGCAAACGGCAAACCCTACAAATCCTCCGGCGGCGAAATGGTGTTTGACGAAACTCTGAAACGAGAAATTCCGAAGGGGTGGGAAGTGAAGAGTTTGGGAGATTGGGCTGAAATTAAAAAAGGGACTTTAATTACAGAAAAAACTGCTAATACCAATGGAGATATTAAAGTGATTTCGGCAGGATTGGATTTCTCTTATTATCACGATGTAGCTAATCGTCCAAAGAATACCATTACAATTAGTGCTTCGGGTGCAAACGCAGGTTTTGTTAATTTTTGGAGAGAACCGATTTTTGTCTGCGATTGTACAACTATTACAAATAGTGTTATTGGCAGCACATTATATATATTAAACTTTTTAAGAATTGTTCAAGATTTTATTTACCAACAAGCTAGAGGATCGGCGCAGCCCCATGTATATCCAAAAGATATTGAAGGATTAAAAATAATTGTACCGCCTGATTTCCTTTTAAAGAGATTTAGTGAGTTTGTAGAAAATTGGAATTTAAAGATTGTAAATAGCGAAAAACAAAACCACCAGCTGACCCAACTACGCGATTTCCTGCTGCCCATGCTGATGAATGGGCAGGTAGCCGTGGCGGAAGAG","","","42606","MNELQDCILGDLVEFQRGYDLPKDAFVKGEYPVQSSNGILGYHNEYKVKAPGITIGRSGTVGIPHLITKNFFPHNTALYVKDFKGNNVQYIYYLLKNLKLNEYKTGSGVPTMNRNHLHPLKIRAFTNLKTQQSIAAVLSALDKKIALNKQINARLEEMAKTLYDYWFVQFDFPDANGKPYKSSGGEMVFDETLKREIPKGWEVKSLGDWAEIKKGTLITEKTANTNGDIKVISAGLDFSYYHDVANRPKNTITISASGANAGFVNFWREPIFVCDCTTITNSVIGSTLYILNFLRIVQDFIYQQARGSAQPHVYPKDIEGLKIIVPPDFLLKRFSEFVENWNLKIVNSEKQNHQLTQLRDFLLPMLMNGQVAVAEE","989165","","type I restriction-modification system S (specificity subunit)","Cytoplasm","","
InterPro
IPR000055
Domain
Restriction modification system DNA specificity domain
PF01420\"[4-143]T\"[201-265]TMethylase_S


","BeTs to 10 clades of COG0732COG name: Restriction endonuclease S subunitsFunctional Class: LThe phylogenetic pattern of COG0732 is aompk-----rl--efghs-uj---wNumber of proteins in this genome belonging to this COG is","","Residues 170 to 335 match (1e-07) PD:PD554845 which is described as I S PROTEOME DEOXYRIBONUCLEASE CHAIN COMPLETE TYPE SITE-SPECIFIC ","","","","","","","","","","","","Mon Jan 13 11:04:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01473 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 201 to 339 (E-value = 3.7e-05) place AA01473 in the Methylase_S family which is described as Type I restriction modification DNA specificity domain (PF01420)","","","","","Titheradge AJ, King J, Ryu J, Murray NE.Families of restriction enzymes: an analysis prompted by molecular and genetic data for type ID restriction and modification systems.Nucleic Acids Res. 2001 Oct 15;29(20):4195-205.PMID: 11600708 Lucchini,S., Sidoti,J. and Brussow,Broad-range bacteriophage resistance in Streptococcus thermophilusby insertional mutagenesis.Virology 275 (2), 267-277 (2000)PubMed: 10998327Titheradge,A.J., Ternent,D. and Murray,N.E.A third family of allelic hsd genes in Salmonella enterica: sequence comparisons with related proteins identify conserved regions implicated in restriction of DNAMol. Microbiol. 22 (3), 437-447 (1996)PubMed: 8939428","","Mon Jan 13 13:33:20 2003","1","","","" "AA01474","990399","990491","93","TTGTTTATCGGTGGGCAGGAATGCCCACCCTACAATAAAGGTCGTTTGAAAAACATTTCAAAATCCGACCGCACTTTTTCAAGTAGCCTACAT","","","3463","LFIGGQECPPYNKGRLKNISKSDRTFSSSLH","990491","","hypothetical protein","Cytoplasm, Periplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 16:51:43 2004","Thu Feb 26 16:51:43 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01474 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 16:51:43 2004","","","","","","","","","","","","","1","","","" "AA01475","991490","990504","987","ATGCACGACAACGACATCATCATTTACACTACGGAAGACGGACTATCCGAATTCACCCTGCGCGAGCTTGACGGCGAACTGTGGCTGACCCAAAAAGAAATTGCCGAACTCTACCAAACCAGCAAACAAAACATCAGCAAGCACATTAAAACCATTTTTGACGAAAACGAAATGGACGAACAGGCAACTGTCAACTTTCAGTTGACAGTTCAAAATGAAAGCGGGCGGGAGGTAAGCCGAAAAATTGCCCTTTACCCCCTGTCCCTGATCATTGCCATCGGTTACCGCGTCCGCTCCACACGCGGCACACAATTCCGCCAATGGGCAACACGGACATTGGGCGAATACATCAGCAAAGGCTTCGTACTCAATGATGACCGCCTCAAAAACCCGCCCGTCGGCACAAGTCGCGCCGAAGATCAGTTTGAACAGCTGCTTAACCGCATCAGGGACATCCGCAGCAGCGAGCGGCGGATGTATCTGCGCGTGCGCGAAATCTTTGCAATGGCGGCGGATTACCAGCACAGCTTCAAAGAAACCAACGCATTTTTCAAAACCATACAAAATAAACTCCACTACGCTTGCACCCTGCATACCGCGCCCGAAATCATCTATCAGCGCGCAGATGCAGAAAAACCCAATATGGGGCTGACTCATTGGCGGGGGAAAGCCGATACAACCGTTGCCAAAAACTACCTGAACGAGGCAGAAATCGATGCCCTCAACCGCATTGTTTCCATGTGGCTGGACTTTGCCGAAGACCAGGCAACCCGGAAAAAACAAATATTCCTGCAAGACTGGACGGAAAAACTGGATGCCTTTCTTACCTTCAACGACCGCCGTGTGCTGCAAAACGCAGGCACAGTCAGCAAAACTCAAGCAGACGAAAAAGCCTGCATCGAATACGAAAAATTCGCCGCTGCACGCAGACTGGAAAAAGAACGCGAGGGCGAACGCCATATTGCCGAACTGCTGAACCTAAAGAAA","","","38474","MHDNDIIIYTTEDGLSEFTLRELDGELWLTQKEIAELYQTSKQNISKHIKTIFDENEMDEQATVNFQLTVQNESGREVSRKIALYPLSLIIAIGYRVRSTRGTQFRQWATRTLGEYISKGFVLNDDRLKNPPVGTSRAEDQFEQLLNRIRDIRSSERRMYLRVREIFAMAADYQHSFKETNAFFKTIQNKLHYACTLHTAPEIIYQRADAEKPNMGLTHWRGKADTTVAKNYLNEAEIDALNRIVSMWLDFAEDQATRKKQIFLQDWTEKLDAFLTFNDRRVLQNAGTVSKTQADEKACIEYEKFAAARRLEKEREGERHIAELLNLKK","990504","","conserved hypothetical protein (possible cytoplasmic protein; DNA binding protein)","Cytoplasm","","
InterPro
IPR011204
Family
Virulence protein RhuM
PIRSF015268\"[1-329]TPredicted virulence protein, RhuM type


","No hits to the COGs database.","","Residues 89 to 124 match (3e-07) PD:PD355478 which is described as PROTEOME DNA-BINDING COMPLETE GP8 RC1095 ","","","","","","","","","","","","Thu Jan 23 10:57:21 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01475 is paralogously related to AA02244 (2e-23).","","","","","","","","","","","","","","1","","","" "AA01476","992321","991542","780","TTGCTCACCCTTAAAAAAGCCCTGCAAACCGCCAAAGAGCTGTACAACATCCTGCGCCTGCAAGGCGACTATGAATTTCTCGAGCATCTCGATTTTGACAAACTCAACCTCCTATACCGTGAAACCGCCGCCCGCATCGACACCCTGAACCTTGCCGAAAAACTGCAGCAGGGCGACACCGCACACCTGCTCAACGAAGCCTTGGAAGACATCTACTTCCAATTTGTCAAAACCGGCGAAGCCGAGCTCAAACTCGCCGACGACTTGAAAGACATCATGCGCAAAGTCCGCGAAGGGCTGGCGGGCAACTTCGACCAAGTAGACCCCGAATTCATCAGCCTGCGCGAAGAATTGGAACGCATCTTCAAGAAAAAGAACCTCGCCGAAGTCGGACAAGACGACATGAAAACCAACATCGGCATACTCGAAACCGTCTATGCCAAAATCAAAGAGCTCAACCGAAAAAACGACCTCCTGCGGCACAAATACGGCGGCGACGCAAAATACGCCCGCACCCACAAACGCCTGCTGGAAAATCCCGTCCTCTACGGCGACAAACAAAAAGTCTTCGACGCGCTCAACGGCGTCAAAACCGACGCCGACCAAAAAGTGCTGGATATGGCGCAGATTTTGGACAACCAGAATTACTTTGAAAAACAAATGCAGGGCATCGTCTTAAAACGCTTCCGCACAGAACAAAAATTCCCCGTTCAGCCCGCAGACATCCAAGTCATCAACCGCCTGCTGGTGCGCGAATATTTAAAAGAAAGCGGACGGATT","","","30289","LLTLKKALQTAKELYNILRLQGDYEFLEHLDFDKLNLLYRETAARIDTLNLAEKLQQGDTAHLLNEALEDIYFQFVKTGEAELKLADDLKDIMRKVREGLAGNFDQVDPEFISLREELERIFKKKNLAEVGQDDMKTNIGILETVYAKIKELNRKNDLLRHKYGGDAKYARTHKRLLENPVLYGDKQKVFDALNGVKTDADQKVLDMAQILDNQNYFEKQMQGIVLKRFRTEQKFPVQPADIQVINRLLVREYLKESGRI","991542","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Jan 13 15:03:49 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01476 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01477","994539","992389","2151","ATGTTCCAAACCCACAACGAAAACTCCCGTGTCAAAATTCCCGCCGTATTGCACCTGATGCGACTGGGCTACCGCTATCTTTCGCTAAAAACCGCAACATGGGATAGGCAGACCAACATCTTTCCCGACATCTTCACCGAAAGCCTGTGCCGCATCAATGCGGGACTATCCGAAGACGACGCGCGCCGCCTGCTGACCGACATCACCATCGAGCTGGACAACGAAGACTTGGGACGGCAATTTTACGAACGCCTCATCAGCCGCTCCGGCATCAAGCTGATCGATTTCCAAAATTTCGACAACAACCGCTTCCATGTCGTAACCGAACTGCCCTGCATCAACGGCGACGAAGAATTCCGCCCGGACATCACCCTGCTGGTAAACGGCATGCCGTTGATATTTGTCGAAGTTAAAAAGCCCAATAACAAAGGCGGTATAGGCGCAGAACGCGAGCGGATGGCAAAGCGCGCGCAAAATCCCAAATTCCGCCGCTTTATCAACATCACCCAATTCATGATTTTTTCCAACAACATGGAATACGACGACGGCGCGACCGAGCCGGTGCAGGGCGCATTCTACTCCTCATCCGCCTATGGCAGCCCCGCTTTCAACTATTTCCGCGAAGAACATAAGCTCAACCTTGCCGAACTTTTAAACACCCTTTCAGACGACCTTGAAAACACCGTCCTGCAAGACAACAACCTGTCCGTCATCAAACATAACCCCGAATTTATCAGCAACAAATCCCCCGACACGCCTACCAACCGAATCCTGACCTCGCTGCTGTGCCGCGACCGCCTCGCCTTTCTCCTGCAATACGGCTTTGCATACGTCGAAACACAAAACGGCATAAAAAAACACATCATGCGCTATCCGCAGCTTTTCGCCGCCTACGCCACCGAAAAACACCTGACCAACGGCGGCAAAAAAGGCGTCATCTGGCACACCCAAGGCTCCGGCAAAACCGCGCTCGCCTACTACAGCACCCGCTATCTAACCCGCTATCTAACCCGCTATTACGCCAAACAAGGTATCGTGCCAAAATTCTATTTCATCGTGGACAGGCTCGACCTCTTGAAACAGGCGCAGCAGGAATTCACCGCCCGTGACCTCATCGTCCACACCATCGACAGCCGCGAAGCCTTCGCCGCCGACATCAAATCCGCCCAAACCCTGCACAACCATTCCGGCAAAGCGGAAATCACCGTCGTCAACATCCAAAAATTCAAAGACGACCCCGACGTCGTCACCAAAAGCGACTACGACCTGAGCATCCAGCGCGTCTATTTCCTCGACGAAGTACACCGCAGCTACAACCCCAAAGGTTCGTTTCTTGCCAACCTCAACCAGTCCGACGTAAACGCCGTCAAAATCGGGCTGACCGGCACGCCGCTTATCGGAGTAACCGCCGGCAGCGTCAACACCCGCGAACTCTTCGGCGACTACATCCACAAATATTATTACAACGCCTCCATCGCCGACAGCTACACCCTGCGCCTCATCCGCGAAGCCATCAGCAGCCAATACAAAGCCCAATTGCAGGCAACATTGGCGCAGCTTGAAATCGAAAAAGGCAGCATAGAGCGCAAAGCCATCTACGCCCATCCGCATTTCGTCCGCCCGATGCTCGACTACATCCTTGACGACTTTGCCAAATTCCGCAAAACCAACCAAGACGACAGCCTCGGCGCCATGATTATCTGCGACAGCGCAGAGCAGGCGCGGCAGATGTACGCCTATTTTCAGACGACCTCGGACCACAAGCTCACCGCCGCCCTGATACTGCACGACGTCGGCACCAAAGACGAGCGCGACCAATGGGTCAAAGACTTCAAAGCCAGCAAAACAGACCTCCTCTTCGTGTACAACATGCTGCTGACCGGCTTTGACGCCCCGCGCCTGAAAAAACTCTATTTGGGCAGACTCATCAAAGCCCACAACCTTTTACAGACCCTCACCCGCGTACAAACACTACCGCTACGGCTACGTCGTCGATTTCGCCGACATACAAAGCGAATTCGACAAAACCAACCGCGCCTATTGGGACGAACTAACCAACGAACTGGGCGACGAAATCGGCAGCTACAGCCAACTTTTCAAAACCGCCGAAGAAATCGAACAGGAAATCGCCGGCATCAAAGCCGCCCTCTT","","","83061","MFQTHNENSRVKIPAVLHLMRLGYRYLSLKTATWDRQTNIFPDIFTESLCRINAGLSEDDARRLLTDITIELDNEDLGRQFYERLISRSGIKLIDFQNFDNNRFHVVTELPCINGDEEFRPDITLLVNGMPLIFVEVKKPNNKGGIGAERERMAKRAQNPKFRRFINITQFMIFSNNMEYDDGATEPVQGAFYSSSAYGSPAFNYFREEHKLNLAELLNTLSDDLENTVLQDNNLSVIKHNPEFISNKSPDTPTNRILTSLLCRDRLAFLLQYGFAYVETQNGIKKHIMRYPQLFAAYATEKHLTNGGKKGVIWHTQGSGKTALAYYSTRYLTRYLTRYYAKQGIVPKFYFIVDRLDLLKQAQQEFTARDLIVHTIDSREAFAADIKSAQTLHNHSGKAEITVVNIQKFKDDPDVVTKSDYDLSIQRVYFLDEVHRSYNPKGSFLANLNQSDVNAVKIGLTGTPLIGVTAGSVNTRELFGDYIHKYYYNASIADSYTLRLIREAISSQYKAQLQATLAQLEIEKGSIERKAIYAHPHFVRPMLDYILDDFAKFRKTNQDDSLGAMIICDSAEQARQMYAYFQTTSDHKLTAALILHDVGTKDERDQWVKDFKASKTDLLFVYNMLLTGFDAPRLKKLYLGRLIKAHNLLQTLTRVQTLPLRLRRRFRRHTKRIRQNQPRLLGRTNQRTGRRNRQLQPTFQNRRRNRTGNRRHQSRPL","992389","","type I restriction enzyme R protein","Outer membrane, Cytoplasm","","
InterPro
IPR006935
Family
Type III restriction enzyme, res subunit
PF04851\"[286-466]TResIII
InterPro
IPR007409
Domain
Type I restriction enzyme R protein N terminus
PF04313\"[4-188]THSDR_N
InterPro
IPR014001
Domain
DEAD-like helicases, N-terminal
SM00487\"[285-499]TDEXDc
InterPro
IPR014021
Domain
Helicase superfamily 1 and 2 ATP-binding
PS51192\"[302-482]THELICASE_ATP_BIND_1
noIPR
unintegrated
unintegrated
signalp\"[1-29]?signal-peptide


","BeTs to 13 clades of COG0610COG name: Restriction enzymes type I helicase subunits and related helicasesFunctional Class: LThe phylogenetic pattern of COG0610 is aom-k------l--efghsnuj---wNumber of proteins in this genome belonging to this COG is","","Residues 76 to 159 match (5e-13) PD:PD003712 which is described as COMPLETE PROTEOME RESTRICTION TYPE I ENZYME R SUBUNIT HYDROLASE HSDR ","","","","","","","","","","","","Mon Jan 13 15:17:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01477 is paralogously related to AA01640 (2e-05).","","","","","","Residues 4 to 188 (E-value = 6.8e-24) place AA01477 in the HSDR_N family which is described as Type I restriction enzyme R protein N terminus (HSDR_N) (PF04313)","","","","","Piekarowicz A, Klyz A, Kwiatek A, Stein DC.Analysis of type I restriction modification systems in the Neisseriaceae: genetic organization and properties of the gene products.Mol Microbiol. 2001 Sep;41(5):1199-210.PMID: 11555298Hubacek J, Holubova I, Weiserova M.The effect of recA mutation on the expression of EcoKI and EcoR124I hsd genes cloned in a multicopy plasmid.Folia Microbiol (Praha). 1998;43(4):353-9.PMID: 9821288","","Mon Jan 13 15:20:45 2003","1","","","" "AA01478","994840","994691","150","TTGTCCTCCGGAGCTAAAAATAGCGAGCGGTTAAATTTTATCAGCAAACTGAGTAAAAACTCGGCGGGCAGTATAGCAGATTTTAAGCGCTTGTCCCTTAGTTTTGTGAAAGCACTGCGCCGTTTTGCTCATAAAGTGCGGTGGGTTTTT","","","5652","LSSGAKNSERLNFISKLSKNSAGSIADFKRLSLSFVKALRRFAHKVRWVF","994691","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 16:50:09 2004","Thu Feb 26 16:50:09 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01478 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 16:50:09 2004","","","","","","","","","","","","","1","","","" "AA01479","994845","995888","1044","TTGAAAAACTTGTTTGCAAAAACATTAAAATCCCTTTGTTTCGCCTTGACTTTCCTTTCCATCACTGCCTTTGCGCAAGAAAAACTTTACGTTTATAACTGGACCGATTACGTGCCTTCCAATCTCATTGCCGAATTTACCAAAGAGACCGGCATTGAAGTGATTTATTCCACCTTTGAAAGCAACGAAGAAATGTATGCCAAACTTAAGCTTATTTCCGACAATGCCGGTTATGACTTGGTTTTCCCGTCCAGCTATTATGTGAACAAAATGGTGCAAGACGGTATGTTGCAAAAATTGGATCATGGCAAGTTAAGCAATTTCAAACAAATTCCGGACAATTTATTGCACAAAGATTTCGACCCGAATAACGACTATTCCCTGCCTTATGTGTATGGTTTAACCGGTATCGCCGTGAACTCGGAAGATGTTGACGTCAGCAAAATCACTAGCTGGTCAGATTTGTGGAACCCGGAATACAAAGGCAAAGTGTTGCTCACTAGTGATGCGCGCGAAGTGTTTCATGTGGCGTTATTGTTGGACGGAAAATCACCGAACACCACCAACGAAGACGAAATCAAAGCTGCTTACGAACGGTTGGAAAAATTATTGCCGAACGTCGCCGTTTTTAACTCCGACTCGCCGGAAGTGCCTTATGTGCAGGGCGAAGTAGCACTAGGCATGATTTGGAACGGTTCCGCCTACATGGCACACCGTGAAAACGAAAACATTCAGTTCGTCTATCCGAAAGAAGGCGCAATTTTCTGGATGGATAACTACGCTATTCCGAAAAGCGCGAAAAACGTCGAAAACGCCTATAAATTTATCAATTTCCTGCTACGTCCGGAAAACGCCAAAGTGGTTTTGGAACGCTTGGGCTATTCCATGCCAAACAACGGCGTAAAAGCCTTAATCTCACCGGAAATGGCAAACAACCCGACCTTATTCCCGCCGGAGGAACAAGTGAAAAAAGGCATTATTCAAGGTGACGTAGGTAACGCCATTGATATTTATGAAAAATATTGGAATAAGTTGAAAACTAAT","","","41554","LKNLFAKTLKSLCFALTFLSITAFAQEKLYVYNWTDYVPSNLIAEFTKETGIEVIYSTFESNEEMYAKLKLISDNAGYDLVFPSSYYVNKMVQDGMLQKLDHGKLSNFKQIPDNLLHKDFDPNNDYSLPYVYGLTGIAVNSEDVDVSKITSWSDLWNPEYKGKVLLTSDAREVFHVALLLDGKSPNTTNEDEIKAAYERLEKLLPNVAVFNSDSPEVPYVQGEVALGMIWNGSAYMAHRENENIQFVYPKEGAIFWMDNYAIPKSAKNVENAYKFINFLLRPENAKVVLERLGYSMPNNGVKALISPEMANNPTLFPPEEQVKKGIIQGDVGNAIDIYEKYWNKLKTN","995888","","spermidine/putrescine-binding periplasmic protein","Periplasm, Cytoplasm","","
InterPro
IPR001188
Family
Bacterial periplasmic spermidine/putrescine-binding protein
PR00909\"[32-48]T\"[48-69]T\"[77-91]T\"[93-106]T\"[124-140]T\"[150-164]T\"[168-187]T\"[205-224]T\"[249-268]T\"[294-320]TSPERMDNBNDNG
InterPro
IPR006059
Family
Bacterial extracellular solute-binding protein, family 1
PF01547\"[42-286]TSBP_bac_1
InterPro
IPR011587
Domain
Prokaryotic extracellular metal-binding protein
PD008688\"[222-294]TQ9Z3S7_RHIME_Q9Z3S7;
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[133-273]Tno description
signalp\"[1-25]?signal-peptide
tmhmm\"[12-32]?transmembrane_regions


","BeTs to 12 clades of COG0687COG name: Spermidine/putrescine-binding periplasmic proteinFunctional Class: EThe phylogenetic pattern of COG0687 is ao---z--vd-l-cefgh-n-j--twNumber of proteins in this genome belonging to this COG is","Significant hit (6.9e-118) to 10/10 blocks of the PR00909 family, which is described as \"Bacterial periplasmic spermidine/putrescine-binding protein signature\". Prints database entry for PR:PR00909. PR00909A 32-48 9.5e-10 PR00909B 48-69 5.5e-19 PR00909C 77-91 9.8e-10 PR00909D 93-106 0.0015 PR00909E 124-140 1.1e-09 PR00909F 150-164 2.4e-07 PR00909G 168-187 1.1e-11 PR00909H 205-224 3.1e-10 PR00909I 249-268 2.5e-14 PR00909J 294-320 2.3e-09","Residues 102 to 160 match (7e-07) PD:PD371140 which is described as LPP38 ","","","","","","","","","","","","Mon Jan 13 15:26:56 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01479 is paralogously related to AA02721 (3e-84), AA01642 (2e-10), AA00696 (2e-10), AA01048 (6e-07) and AA00698 (6e-07).","","","","","","Residues 12 to 286 (E-value = 6.7e-13) place AA01479 in the SBP_bac_1 family which is described as Bacterial extracellular solute-binding protein (PF01547)","","","","","Sugiyama,S., Vassylyev,D.G., Matsushima,M., Kashiwagi,K., Igarashi,K. and Morikawa,K. Crystal structure of PotD, the primary receptor of the polyamine transport system in Escherichia coli J. Biol. Chem. 271 (16), 9519-9525 (1996) PubMed: 8621624 Sugiyama,S., Matsuo,Y., Maenaka,K., Vassylyev,D.G., Matsushima,M.,Kashiwagi,K., Igarashi,K. and Morikawa,K. The 1.8-A X-ray structure of the Escherichia coli PotD protein complexed with spermidine and the mechanism of polyamine binding Protein Sci. 5 (10), 1984-1990 (1996) PubMed: 8897598 Matsuo,Y. and Nishikawa,K. Prediction of the structural similarity between spermidine/putrescine-binding protein and maltose-binding protein FEBS Lett. 345 (1), 23-26 (1994) PubMed: 8194593 ","","Mon Jan 13 15:51:17 2003","1","","","" "AA01480","996380","995955","426","ATGGCAACATTTAATTTAACAGTGGTAAGTGCAGAACAACAAATCTTTTCCGGCAATGTGAAAAGCGTTCAAGCAACTGGTATTGAAGGCGAGCTCGGTGTTTTACCGGGTCATGCCCCGTTACTAACGGCAATCAAGCCGGGTATTGTTAAGCTGACGTTGGAAAATGATAGCGAGGAAGTTATCTACGTTTCCGGTGGTTTCTTAGAAGTACAACCGACAGCGGTTATTGTCCTTGCGGATATCGCTATTCGAGGCCAAGAACTTGACAGCGAACGCATTCTTGCTGCGAAGAAACGTGCTGAAGAAAACATTCGTCAGCATCACCACGATGCAGATTACGAAGTATTAATGTCCAAACTTTCTAAAGAATTGGCAAAACTTCGTGCTTATGAACTGACAGAACAATTAGTCAAATCTAAGCGC","","","16173","MATFNLTVVSAEQQIFSGNVKSVQATGIEGELGVLPGHAPLLTAIKPGIVKLTLENDSEEVIYVSGGFLEVQPTAVIVLADIAIRGQELDSERILAAKKRAEENIRQHHHDADYEVLMSKLSKELAKLRAYELTEQLVKSKR","995955","From GenBank (gi:1168590):This protein produces ATP from ADP in the presence of a proton gradient across the membrane.F-type ATPases have two components, CF(1), the catalytic core, and CF(0), the membrane proton channel. CF(1) has five subunits: ALPHA(3), BETA(3), GAMMA(1), DELTA(1), and EPSILON(1). CF(0) has three main subunits: A, B and C","ATP synthase F1, epsilon","Cytoplasm","","
InterPro
IPR001469
Family
ATPase, F1 complex, delta/epsilon subunit
PD000944\"[9-89]TATPE_PASMU_Q9CKW0;
G3DSA:2.60.15.10\"[1-89]Tno description
PTHR13822\"[3-132]TATP SYNTHASE DELTA/EPSILON CHAIN
PF02823\"[3-85]TATP-synt_DE_N
TIGR01216\"[3-132]TATP_synt_epsi: ATP synthase F1, epsilon sub
noIPR
unintegrated
unintegrated
G3DSA:1.20.5.440\"[90-138]Tno description
PTHR13822:SF2\"[3-132]TATP SYNTHASE EPSILON CHAIN


","BeTs to 16 clades of COG0355COG name: F0F1-type ATP synthase epsilon subunit (mitochondrial delta subunit)Functional Class: CThe phylogenetic pattern of COG0355 is ------yqv-rlbcefghsnujx--wNumber of proteins in this genome belonging to this COG is","Significant hit ( 6.3e-31) to 2/2 blocks of the IPB001469 family, which is described as \"ATP synthase, Delta/Epsilon chain\". Interpro entry for IP:IPR001469. IPB001469A 15-52 1.7e-21 IPB001469B 64-84 4.9e-08","Residues 90 to 142 match (6e-10) PD:PD438860 which is described as ATP EPSILON SYNTHASE PROTEOME SUBUNIT F1 ION SECTOR CHAIN COMPLETE ","","","","","","","","","","","Tue Jan 21 10:27:50 2003","Tue Jan 21 10:26:43 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01480 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 85 (E-value = 4e-32) place AA01480 in the ATP-synt_DE_N family which is described as ATP synthase, Delta/Epsilon chain, beta-sandwich domain (PF02823)","","","","","Hausrath,A.C., Gruber,G., Matthews,B.W. and Capaldi,R.A.Structural features of the gamma subunit of the Escherichia coliF(1) ATPase revealed by a 4.4-A resolution map obtained by x-raycrystallography. Proceedings of the National Academy of Sciences of the UnitedStates of America. 96 (24), 13697-13702 (1999) PubMed: 10570135 Nielsen,J., Hansen,F.G., Hoppe,J., Friedl,P. and von Meyenburg,K.The nucleotide sequence of the atp genes coding for the F0subunits a, b, c and the F1 subunit delta of the membrane boundATP synthase of Escherichia coli. Mol. Gen. Genet. 184 (1), 33-39 (1981) PubMed: 6278247. Kanazawa,H., Mabuchi,K., Kayano,T., Noumi,T., Sekiya,T. andFutai,M. Nucleotide sequence of the genes for F0 components of theproton-translocating ATPase from Escherichia coli: prediction ofthe primary structure of F0 subunits. Biochem. Biophys. Res. Commun. 103 (2), 613-620 (1981) PubMed: 6277311.","","Sat Feb 15 07:24:38 2003","1","","","" "AA01482","997795","996425","1371","ATGGCGACAGGTAAAATTGTACAAATCATCGGTGCGGTGATTGACGTCGAATTTCCACAAGATGCAGTACCAAAAGTTTATGATGCATTAAAAGTTGAAACAGGTTTAACCCTTGAAGTTCAACAACAATTAGGCGGTGGTGTGGTACGTTGTATCGCACTGGGTGCCTCCGACGGTTTAAAACGCGGTTTGAAAGTAGAAAATACCAATGACCCGATTCAAGTACCGGTAGGCACAAAAACCCTTGGTCGTATTATGAACGTATTGGGCGAACCAATCGATGAACAAGGTCCAATCGGTGAAGAAGAACGTTGGTCAATCCACCGTTCGGCACCAAGCTATGAAGAACAATCCAACAGTACCGAATTATTAGAAACCGGTATTAAAGTTATCGACTTAATTTGCCCATTCGCGAAAGGGGGTAAAGTCGGTTTATTCGGTGGTGCGGGTGTAGGTAAAACCGTAAATATGATGGAATTAATCCGTAATATTGCTATTGAGCACTCAGGTTATTCCGTATTCGCCGGTGTAGGTGAACGTACCCGTGAAGGTAACGACTTCTACCACGAAATGAAAGATTCCAATGTATTGGATAAAGTATCTCTGGTTTATGGTCAAATGAATGAACCACCGGGTAACCGTTTACGTGTTGCCTTAACCGGTTTGACTATGGCGGAAAAATTCCGTGATGAAGGTCGTGACGTATTATTCTTCGTGGATAATATCTATCGTTATACCCTTGCCGGTACCGAAGTATCCGCCCTTTTAGGTCGTATGCCGTCAGCGGTAGGTTATCAACCGACACTTGCGGAAGAAATGGGTGTGTTACAAGAACGTATCACCTCAACCAAAACCGGTTCTATCACCTCCGTACAAGCGGTTTATGTTCCTGCGGATGACTTAACCGACCCGTCTCCGGCAACTACCTTTGCGCACTTAGATTCCACCGTCGTATTGAGTCGTCAAATTGCGTCTTTGGGGATTTATCCGGCGGTTGACCCGTTAGATTCTACATCCCGTCAATTGGATCCGTTGGTTGTCGGTCAAGAACACTATAATGTCGCTCGTGGCGTCCAAGGTATCTTGCAACGTTACAAAGAATTGAAAGACATCATCGCAATTCTTGGTATGGATGAATTATCCGAAGAAGATAAATTAGTGGTAGCGCGCGCGCGTAAAATCGAACGTTTCTTATCACAACCATTCTTTGTTGCTGAAGTCTTTACAGGTTCACCGGGTAAGTATGTTCCGTTAAAAGAAACTATTCGCGGCTTTAAAGGTATTTTAAGCGGTGAGTACGACCATATTCCGGAACAGGCGTTCTATATGGTCGGTTCTATCGACGAAGCGCTAGAAAAAGCCAAAAATATG","","","51717","MATGKIVQIIGAVIDVEFPQDAVPKVYDALKVETGLTLEVQQQLGGGVVRCIALGASDGLKRGLKVENTNDPIQVPVGTKTLGRIMNVLGEPIDEQGPIGEEERWSIHRSAPSYEEQSNSTELLETGIKVIDLICPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDSTVVLSRQIASLGIYPAVDPLDSTSRQLDPLVVGQEHYNVARGVQGILQRYKELKDIIAILGMDELSEEDKLVVARARKIERFLSQPFFVAEVFTGSPGKYVPLKETIRGFKGILSGEYDHIPEQAFYMVGSIDEALEKAKNM","996425","From GenBank (gi:114546): AtpG produces ATP from ADP in the presence of a proton gradient across the membrane. The beta chain is the catalytic subunit. F-type ATPases have two components, CF(1), the catalytic core, and CF(0), the membrane proton channel. CF(1) has five subunits: ALPHA(3), BETA(3), GAMMA(1), DELTA(1), and EPSILON(1). CF(0) has three main subunits: A, B and C. ","ATP synthase F1, subunit beta","Cytoplasm, Inner membrane","","
InterPro
IPR000194
Domain
ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding
PF00006\"[126-339]TATP-synt_ab
PS00152\"[330-339]TATPASE_ALPHA_BETA
InterPro
IPR000793
Domain
ATPase, F1/V1/A1 complex, alpha/beta subunit, C-terminal
PF00306\"[352-457]TATP-synt_ab_C
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[139-324]TAAA
InterPro
IPR004100
Domain
ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal
PF02874\"[6-70]TATP-synt_ab_N
InterPro
IPR005722
Family
ATPase, F1 complex, beta subunit
PTHR15184:SF8\"[1-371]TATP SYNTHASE BETA SUBUNIT
TIGR01039\"[2-457]TatpD: ATP synthase F1, beta subunit
noIPR
unintegrated
unintegrated
G3DSA:2.40.10.170\"[1-72]Tno description
G3DSA:3.40.50.300\"[72-346]Tno description
PTHR15184\"[1-371]TATP SYNTHASE


","BeTs to 16 clades of COG0055COG name: F0F1-type ATP synthase beta subunitFunctional Class: CThe phylogenetic pattern of COG0055 is ------yqv-rlbcefghsnujx--wNumber of proteins in this genome belonging to this COG is","Significant hit (6.5e-106) to 5/5 blocks of the IPB000194 family, which is described as \"ATP synthase alpha and beta subunit, N-terminal\". Interpro entry for IP:IPR000194. IPB000194A 63-94 1.1e-15 IPB000194B 126-163 6.9e-19 IPB000194C 199-230 4.2e-18 IPB000194D 240-281 1.5e-23 IPB000194E 286-333 9.6e-25Significant hit ( 1.3e-16) to 3/10 blocks of the IPB003255 family, which is described as \"ATP synthase beta subunit, C-terminal\". Interpro entry for IP:IPR003255. IPB003255B 67-111 1.2e-07 IPB003255C 112-157 0.42 IPB003255H 297-332 0.00023Significant hit ( 2.9e-12) to 4/6 blocks of the IPB000790 family, which is described as \"ATP synthase alpha subunit, C-terminal\". Interpro entry for IP:IPR000790. IPB000790B 116-159 0.0076 IPB000790C 195-240 5.8e-05 IPB000790D 241-282 1.2e+02 IPB000790E 312-349 4.7","Residues 286 to 403 match (5e-10) PD:PD032612 which is described as SUBUNIT ATP B HYDROLASE HYDROGEN ION VACUOLAR SYNTHASE V-TYPE SYNTHESIS ","","","","","","","","","","","Tue Jan 21 10:39:24 2003","Tue Jan 21 10:31:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01482 is paralogously related to AA01486 (1e-29) and AA00265 (2e-07).","","","","","","Residues 352 to 457 (E-value = 1.8e-52) place AA01482 in the ATP-synt_ab_C family which is described as ATP synthase alpha/beta chain, C terminal domain (PF00306)","","","","","Nielsen,J., Hansen,F.G., Hoppe,J., Friedl,P. and von Meyenburg,K.The nucleotide sequence of the atp genes coding for the F0 subunitsa, b, c and the F1 subunit delta of the membrane bound ATP synthaseof Escherichia coli. Mol. Gen. Genet. 184 (1), 33-39 (1981) PubMed: 6278247. Kanazawa,H., Mabuchi,K., Kayano,T., Noumi,T., Sekiya,T. andFutai,M. Nucleotide sequence of the genes for F0 components of theproton-translocating ATPase from Escherichia coli: prediction ofthe primary structure of F0 subunits. Biochem. Biophys. Res. Commun. 103 (2), 613-620 (1981) PubMed: 6277311.Kumamoto,C.A. and Simoni,R.D. Genetic evidence for interaction between the a and b subunits ofthe F0 portion of the Escherichia coli proton translocating ATPase.J. Biol. Chem. 261 (22), 10037-10042 (1986) PubMed: 2874136. ","","Mon Jan 13 15:54:20 2003","1","","","" "AA01484","998681","997815","867","ATGGCAGGTGCAAAAGAGATAAAAACCAAAATTGCCAGCGTGCAGAGTACGCAGAAAATCACCAAGGCAATGGAAATGGTTGCAACCTCGAAAATGCGTAAAACGCAGGATCGTATGGCGGCATCTCGTCCGTATTCTGAAACTATCCGTAATGTTATCAGTCATGTGTCTAAAGCCAGTATCGGTTACAAACACCCGTTCTTAGTGGAACGTGAAGTGAAAAATGTCGGCATTTTAGTTATTTCTACCGATGGTGGAATGTGCGGTGGTTTAAACGTTAATTTGTTTAAAGCCACGCTTAACCAAATTAAGGACTGGAAAGCGCAGAATGCCGCTACCGTACTTGGTTTAATCGGTTCTAAAGGGATTAGTTTTTTCCGTTCTCTTGGCTTTAATGTCAAAGGACAACTTTCCGGTTTGGGCGATAACCCGGCTTTGGAAGAATTAATTGGTGTGGCGAATGCCATGTTTGATGCTTATCGTAATGGTGAAATTGATGCGATTTATATTGCGTACAATAAATTCATTAATACGATGTCGCAAAAACCGGTTATACAACAATTAGTTCCTTTACCGGAAATGGAAAACGATCACCTAAGCGAAAGACAACAGGCATGGGATTATATTTATGAACCTGATCCAAAAGTATTATTAGACAGTCTTTTAGTTCGTTATTTAGAATCTCAGGTTTATCAAGCGGTTGTAGATAATTTAGCTTCAGAACAAGCGGCTCGAATGGTAGCGATGAAAGCAGCAACGGATAACGCAGGTAATTTAATTAATGATTTGCGGTTGGTGTATAACAAAGCTCGTCAAGCAAGTATCACAAATGAATTAAATGAAATTGTTGCCGGCGCGGCAGCGATT","","","31717","MAGAKEIKTKIASVQSTQKITKAMEMVATSKMRKTQDRMAASRPYSETIRNVISHVSKASIGYKHPFLVEREVKNVGILVISTDGGMCGGLNVNLFKATLNQIKDWKAQNAATVLGLIGSKGISFFRSLGFNVKGQLSGLGDNPALEELIGVANAMFDAYRNGEIDAIYIAYNKFINTMSQKPVIQQLVPLPEMENDHLSERQQAWDYIYEPDPKVLLDSLLVRYLESQVYQAVVDNLASEQAARMVAMKAATDNAGNLINDLRLVYNKARQASITNELNEIVAGAAAI","997815","From GenBank (gi:114639): AtpG produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the F0 complex. F-type ATPases have two components, CF(1), the catalytic core, and CF(0), the membrane proton channel. CF(1) has five subunits: ALPHA(3), BETA(3), GAMMA(1), DELTA(1), and EPSILON(1). CF(0) has three main subunits: A, B and C.","ATP synthase F1, subunit gamma","Cytoplasm","","
InterPro
IPR000131
Family
ATPase, F1 complex, gamma subunit
PR00126\"[73-92]T\"[166-183]T\"[236-255]T\"[267-288]TATPASEGAMMA
PTHR11693\"[1-289]TATP SYNTHASE GAMMA CHAIN
PF00231\"[2-289]TATP-synt
TIGR01146\"[1-289]TATPsyn_F1gamma: ATP synthase F1, gamma subu
PS00153\"[275-288]TATPASE_GAMMA
noIPR
unintegrated
unintegrated
G3DSA:3.40.1380.10\"[27-248]Tno description
PTHR11693:SF10\"[1-289]TATP SYNTHASE GAMMA CHAIN, SODIUM ION SPECIFIC


","BeTs to 16 clades of COG0224COG name: F0F1-type ATP synthase gamma subunitFunctional Class: CThe phylogenetic pattern of COG0224 is ------yqv-rlbcefghsnujx--wNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.2e-97) to 5/5 blocks of the IPB000131 family, which is described as \"ATP synthase gamma subunit\". Interpro entry for IP:IPR000131. IPB000131A 4-35 9.6e-23 IPB000131B 73-97 1.9e-11 IPB000131C 118-128 0.0049 IPB000131D 166-191 4e-13 IPB000131E 234-286 6.9e-42","Residues 5 to 126 match (2e-07) PD:PD000146 which is described as ORF SUBUNIT POLYMERASE RNA ATP SYNTHASE GAMMA DNA-DIRECTED MITOCHONDRION GENE ","","","","","","","","","","","Tue Jan 21 10:43:30 2003","Tue Jan 21 10:43:30 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01484 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 289 (E-value = 1.4e-169) place AA01484 in the ATP-synt family which is described as ATP synthase (PF00231)","","","","","Hausrath,A.C., Gruber,G., Matthews,B.W. and Capaldi,R.A. Structural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by x-ray crystallography. Proceedings of the National Academy of Sciences of the United States of America. 96 (24), 13697-13702 (1999) PubMed: 10570135Kanazawa,H., Mabuchi,K., Kayano,T., Noumi,T., Sekiya,T. and Futai,M.Nucleotide sequence of the genes for F0 components of the proton-translocating ATPase from Escherichia coli: prediction of the primary structure of F0 subunits. Biochem. Biophys. Res. Commun. 103 (2), 613-620 (1981) PubMed: 6277311. ","","Tue Jan 14 10:24:35 2003","1","","","" "AA01486","1000238","998700","1539","ATGCAACTAAATTCAACTGAAATTAGTGAATTAATAAAAAAACGCATTGCCCAGTTTAATGTAGAAAGCGAAGCGCGTAATACGGGAACAATCGTTTCAGTCAGCGATGGTATCATTCGTATTCACGGTTTAAGTGAAGTGATGCAAGGTGAGATGATTGCATTACCGGGAAATCGCTACGCAATGGCATTAAACTTAGAAAGAGATTCTGTTGGTGCAGTGGTAATGGGGCCTTATGCCGATCTTGCAGAAGGCATGGAAGTCCAATGTACCGGCCGTATTCTTGAAGTGCCTGTAGGTCGCGGTTTATTAGGTCGTGTGGTAAATACCCTTGGTCAACCGATTGACGGCAAAGGTGAAATTGAAAATGACGGTTTTTCTCCAATTGAAGTCATTGCACCGGGTGTAATTGAACGTAAGTCCGTTGATCAACCTGTTCAAACCGGTTATAAAGCCGTTGACTCCATGGTACCAATCGGTCGTGGACAACGTGAGTTAATTATCGGTGACCGTCAAACCGGTAAAACCGCATTGGCTATCGATACTATCATCAACCAACGTAATTCCGGTATTAAATGTATCTATGTTGCAATCGGTCAAAAAGCATCAACCATTGCCAATGTGGTACGTAAATTAGAAGAACACGGCGCATTAGCCAACACTATCGTGGTTGCTGCTTCTGCTTCCGAATCTGCCGCATTACAATATTTAGCGCCTTATGCCGGTTGTGCAATGGGTGAATATTTCCGCGATCGTGGTGAAGATGCATTAATCGTTTACGATGACCTTTCCAAACAAGCGGTGGCTTATCGTCAAATTTCCTTGTTATTACGTCGTCCGCCGGGTCGTGAAGCTTATCCGGGTGACGTATTCTACCTACACTCACGTTTACTTGAACGTGCCTCTCGTGTAAATGAAGAATATGTAGAAAAATTCACTAACGGTGAAGTTAAAGGTAAAACCGGTTCTTTAACCGCACTTCCGATTATCGAAACACAAGCGGGTGACGTTTCCGCCTTCGTTCCAACCAACGTAATTTCGATTACTGACGGTCAGATTTTCTTGGAATCCAACCTATTTAACTCCGGCATTCGTCCTGCGGTAAACCCGGGTATTTCCGTTTCCCGTGTAGGTGGTTCGGCACAAACTAAAGTCATCAAAAAATTAGCCGGTGGTATTCGTACCGCACTTGCCCAATATCGTGAATTAGCGGCGTTTGCACAGTTTGCATCCGATCTTGATGATGCAACCCGTAAACAACTTTCTCACGGTGAAAAAGTAACTGAATTGCTAAAACAAAAACAATTTGCGCCGCTTTCGGTTGCGGAACAGGCTGTTGTGTTATTTGCTGTTGAGTTCGGTTATTTGGAAGATGTGGAGTTATCAAAAATAGCAAGTTTTGAGACCGCACTTTTAGATTATGCAAATCGTAATTATGCCGAGTTTATGCAAGAACTAACCAAAACCGGTAACTATAATGACGAAATCAAAGATACGTTAAAAGGTATTTTAGATAGTTTTAAAGCTAACAGTGCTTGG","","","55621","MQLNSTEISELIKKRIAQFNVESEARNTGTIVSVSDGIIRIHGLSEVMQGEMIALPGNRYAMALNLERDSVGAVVMGPYADLAEGMEVQCTGRILEVPVGRGLLGRVVNTLGQPIDGKGEIENDGFSPIEVIAPGVIERKSVDQPVQTGYKAVDSMVPIGRGQRELIIGDRQTGKTALAIDTIINQRNSGIKCIYVAIGQKASTIANVVRKLEEHGALANTIVVAASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASRVNEEYVEKFTNGEVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESNLFNSGIRPAVNPGISVSRVGGSAQTKVIKKLAGGIRTALAQYRELAAFAQFASDLDDATRKQLSHGEKVTELLKQKQFAPLSVAEQAVVLFAVEFGYLEDVELSKIASFETALLDYANRNYAEFMQELTKTGNYNDEIKDTLKGILDSFKANSAW","998700","From GenBank (gi:1168566): AtpA produces ATP from ADP in the presence of a proton gradient across a membrane. The alpha chain is a regulatory subunit. F-type ATPases have two components, CF(1), the catalytic core, and CF(0), the membrane proton channel. CF(1) has five subunits: ALPHA(3), BETA(3), GAMMA(1), DELTA(1), and EPSILON(1). CF(0) has three main subunits: A, B and C. ","ATP synthase F1, subunit alpha","Cytoplasm, Inner membrane","","
InterPro
IPR000194
Domain
ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding
PF00006\"[148-375]TATP-synt_ab
PS00152\"[366-375]TATPASE_ALPHA_BETA
InterPro
IPR000793
Domain
ATPase, F1/V1/A1 complex, alpha/beta subunit, C-terminal
PF00306\"[387-488]TATP-synt_ab_C
InterPro
IPR004100
Domain
ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal
PF02874\"[24-92]TATP-synt_ab_N
InterPro
IPR005294
Family
ATPase, F1 complex, alpha subunit
PTHR15184:SF3\"[194-510]TATP SYNTHASE ALPHA SUBUNIT MITOCHONDRIAL
TIGR00962\"[2-513]TatpA: ATP synthase F1, alpha subunit
noIPR
unintegrated
unintegrated
G3DSA:1.20.150.20\"[383-513]Tno description
G3DSA:2.40.30.20\"[24-93]Tno description
G3DSA:3.40.50.300\"[94-382]Tno description
PTHR15184\"[194-510]TATP SYNTHASE


","BeTs to 16 clades of COG0056COG name: F0F1-type ATP synthase alpha subunitFunctional Class: CThe phylogenetic pattern of COG0056 is ------yqv-rlbcefghsnujx--wNumber of proteins in this genome belonging to this COG is","Significant hit (1.5e-223) to 6/6 blocks of the IPB000790 family, which is described as \"ATP synthase alpha subunit, C-terminal\". Interpro entry for IP:IPR000790. IPB000790A 27-77 1.2e-30 IPB000790B 138-181 2.3e-41 IPB000790C 216-261 1.4e-36 IPB000790D 262-303 5.1e-40 IPB000790E 348-385 1.1e-32 IPB000790F 386-439 3.2e-37Significant hit (1.1e-124) to 5/5 blocks of the IPB000194 family, which is described as \"ATP synthase alpha and beta subunit, N-terminal\". Interpro entry for IP:IPR000194. IPB000194A 85-116 8.9e-19 IPB000194B 148-185 5.7e-24 IPB000194C 220-251 9.4e-18 IPB000194D 261-302 3.6e-30 IPB000194E 322-369 2.8e-29Significant hit ( 1.1e-19) to 5/10 blocks of the IPB003255 family, which is described as \"ATP synthase beta subunit, C-terminal\". Interpro entry for IP:IPR003255. IPB003255B 89-133 1.1e-08 IPB003255C 134-179 0.44 IPB003255D 188-221 2.7 IPB003255G 292-332 1.3e+02 IPB003255H 333-368 0.0012","Residues 179 to 217 match (7e-07) PD:PD507040 which is described as ATP HYDROLASE CF1 ION SYNTHESIS HYDROGEN ALPHA ATP-BINDING SYNTHASE MITOCHONDRION ","","","","","","","","","","","Tue Jan 14 10:21:48 2003","Tue Jan 21 10:47:11 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01486 is paralogously related to AA01482 (1e-29).","","","","","","Residues 387 to 488 (E-value = 1.4e-26) place AA01486 in the ATP-synt_ab_C family which is described as ATP synthase alpha/beta chain, C terminal domain (PF00306)","","","","","Nielsen,J., Hansen,F.G., Hoppe,J., Friedl,P. and von Meyenburg,K.The nucleotide sequence of the atp genes coding for the F0 subunits a, b, c and the F1 subunit delta of the membrane bound ATP synthase of Escherichia coli. Mol. Gen. Genet. 184 (1), 33-39 (1981) PubMed: 6278247. Kanazawa,H., Mabuchi,K., Kayano,T., Noumi,T., Sekiya,T. and Futai,M.Nucleotide sequence of the genes for F0 components of theproton-translocating ATPase from Escherichia coli: prediction of the primary structure of F0 subunits. Biochem. Biophys. Res. Commun. 103 (2), 613-620 (1981) PubMed: 6277311. Cain,B.D. and Simoni,R.D. Impaired proton conductivity resulting from mutations in the asubunit of F1F0 ATPase in Escherichia coli. J. Biol. Chem. 261 (22), 10043-10050 (1986) PubMed: 2874137. Kumamoto,C.A. and Simoni,R.D. Genetic evidence for interaction between the a and b subunits of the F0 portion of the Escherichia coli proton translocating ATPase. J. Biol. Chem. 261 (22), 10037-10042 (1986) PubMed: 2874136. Cain,B.D. and Simoni,R.D. Proton translocation by the F1F0ATPase of Escherichia coli.Mutagenic analysis of the a subunit. J. Biol. Chem. 264 (6), 3292-3300 (1989) PubMed: 2536742. Yamada,H., Moriyama,Y., Maeda,M. and Futai,M. Transmembrane topology of Escherichia coli H(+)-ATPase (ATP synthase) subunit a. FEBS Lett. 390 (1), 34-38 (1996) PubMed: 8706824. Valiyaveetil,F.I. and Fillingame,R.H. Transmembrane topography of subunit a in the Escherichia coli F1F0ATP synthase. J. Biol. Chem. 273 (26), 16241-16247 (1998) PubMed: 9632683. ","","Tue Jan 14 10:23:23 2003","1","","","" "AA01487","1000799","1000254","546","ATGTCAGAATTAACTACCATAGCTCGCCCTTATGCAAAAGCAGCATTTGATTTTGCCGTAGAACAGCGTTCGGTTGACAAAAGTGCGGTGGGAAAATGGGGAGAAATGTTAGGTTTTCTTGCTGAAGTCGTTGAAAATGACACCATGAAAGATTTCTTAACAAGCTCTTTTTCGGCACAAAAACTGGCGGATACGGTGATCGCAATTTGTGGTGAACAAATAAATCAATATGGGCAAAATTTGATTCGGTTAATGGCTGAAAATAAGCGTTTAACTGTCCTTCCGGCAGTATTCAAAGAATTCCGGCATTATGTTGAGGAATATAACGCAATTACGGAAGTTCAGGTCACCTCAGCTCAACCATTAAGTGTCGCGCAACAAGAAAAAATTGCTGCCGCAATGGAAAAGAAATTAGCCCGTAAAATTAAGTTAAATTGCAACATTGATAACTCACTGATTGCCGGAGTTATCATTCGTACAGATGATTTTGTGATTGACGGAAGTAGCCGTGGGCAACTTACCCGTCTGGCAAATGAGTTGCAATTA","","","21350","MSELTTIARPYAKAAFDFAVEQRSVDKSAVGKWGEMLGFLAEVVENDTMKDFLTSSFSAQKLADTVIAICGEQINQYGQNLIRLMAENKRLTVLPAVFKEFRHYVEEYNAITEVQVTSAQPLSVAQQEKIAAAMEKKLARKIKLNCNIDNSLIAGVIIRTDDFVIDGSSRGQLTRLANELQL","1000254","From GenBank (gi:114580): This protein seems to be part of the stalkthat links F0 to F1. It either transmits conformational changes fromF0 into F1 or is implicated in proton conduction. F-type ATPaseshave two components, CF(1), the catalytic core, and CF(0), themembrane proton channel. CF(1) has five subunits: ALPHA(3), BETA(3),GAMMA(1), DELTA(1), and EPSILON(1). CF(0) has three main subunits:A, B and C. ","ATP synthase F1, subunit delta","Cytoplasm","","
InterPro
IPR000711
Family
ATPase, F1 complex, OSCP/delta subunit
PR00125\"[7-26]T\"[79-90]T\"[90-104]T\"[140-155]T\"[155-173]TATPASEDELTA
G3DSA:1.10.520.20\"[2-111]Tno description
PTHR11910\"[7-182]TATP SYNTHASE DELTA CHAIN
PF00213\"[7-180]TOSCP
TIGR01145\"[7-180]TATP_synt_delta: ATP synthase F1, delta subu


","No hits to the COGs database.","Significant hit ( 1e-12) to 1/1 blocks of the IPB000711 family, which is described as \"ATP synthase, delta (OSCP) subunit\". Interpro entry for IP:IPR000711. IPB000711 148-176 1e-12","Residues 1 to 97 match (2e-13) PD:PD582529 which is described as SYNTHASE DELTA PROTEOME COMPLETE ATP CHAIN HYDROLASE SUBUNIT PROBABLE F1 ","","","","","","","","","","","Tue Jan 14 10:27:46 2003","Tue Jan 21 10:51:08 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01487 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 180 (E-value = 8.2e-49) place AA01487 in the OSCP family which is described as ATP synthase delta (OSCP) subunit (PF00213)","","","","","Mabuchi,K., Kanazawa,H., Kayano,T. and Futai,M. Nucleotide sequence of the gene coding for the delta subunit ofproton translocating ATPase of Escherichia coli. Biochemical and biophysical research communications. 102 (1),172-179 (1981) PubMed: 6458296. Nielsen,J., Hansen,F.G., Hoppe,J., Friedl,P. and von Meyenburg,K.The nucleotide sequence of the atp genes coding for the F0 subunits a, b, c and the F1 subunit delta of the membrane bound ATP synthase of Escherichia coli. Mol. Gen. Genet. 184 (1), 33-39 (1981) PubMed: 6278247","","Tue Jan 14 10:27:46 2003","1","","","" "AA01488","1001283","1000816","468","GTGAATTTAAATGCAACATTAATTGGTCAACTCATTTCATTCGCACTTTTTGTGTGGTTCTGTATGAAATTTGTTTGGCCGCCAATTATTAAGGCAATTGAAACGCGTCAAAGCCAAATTGCAAATGCTTTAGCTTCGGCGGAAGTGGCAAAAAAAGAACAGGCGGATACCAAAGCCCTTGTTGAACAAGAAATTTCTAAAGCCAAAATTCAGGCACAAGAAATTTTGGATGATGCCAATAAACGTCGTAACGAAGTATTGGACGAAGTTAAAAACGAAGCTGAAGAACTTAAAGCGAAAATTATTGAACAAGGCTATGCGGAAGTGGAAGCCGAGCGTAAGCGTGTTCAGGAAGAATTGCGTGTTAAAGTGGCGTCTTTGGCTGTTGCCGGTGCAGAAAAAATTGTGGGTCGTTCTATTGATGAAGCGGCAAACAATGACATTATTGATAAATTAGTTGCAGAACTA","","","17341","VNLNATLIGQLISFALFVWFCMKFVWPPIIKAIETRQSQIANALASAEVAKKEQADTKALVEQEISKAKIQAQEILDDANKRRNEVLDEVKNEAEELKAKIIEQGYAEVEAERKRVQEELRVKVASLAVAGAEKIVGRSIDEAANNDIIDKLVAEL","1000816","From GenBank (gi:114618):F-type ATPases have 2 components, CF(1)- the catalytic core- and CF(0)- the membrane protein channel. CF91) has five subunits: alpha(3), beta(3), gamma (1), delta(1), epsilon(1). CF(0) has three main subunits: a, b, and c.","ATP synthase F0, subunit b","Cytoplasm, Periplasm, Inner membrane","","
InterPro
IPR002146
Family
ATPase, F0 complex, subunit B/B', bacterial and chloroplast
PF00430\"[6-137]TATP-synt_B
InterPro
IPR005864
Family
ATPase, F0 complex, subunit B, bacterial
TIGR01144\"[10-156]TATP_synt_b: ATP synthase F0, B subunit
noIPR
unintegrated
unintegrated
signalp\"[1-32]?signal-peptide
tmhmm\"[10-30]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.5e-16) to 1/1 blocks of the IPB002146 family, which is described as \"ATP synthase B/B' CF(0)\". Interpro entry for IP:IPR002146. IPB002146 11-49 1.4e-16","Residues 5 to 156 match (9e-07) PD:PD415730 which is described as ATP HYDROLASE PROTEOME ION CHAIN COMPLETE CF1 SYNTHESIS DELTA SYNTHASE ","","","","","","","","","","","Tue Jan 21 11:00:10 2003","Tue Jan 21 11:00:10 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01488 is paralogously related to AA02832 (3e-05) and AA02347 (3e-04).","","","","","","Residues 6 to 137 (E-value = 7.6e-29) place AA01488 in the ATP-synt_B family which is described as ATP synthase B/B' CF(0) (PF00430)","","","","","Nielsen,J., Hansen,F.G., Hoppe,J., Friedl,P. and von Meyenburg,K.The nucleotide sequence of the atp genes coding for the F0 subunits a, b, c and the F1 subunit delta of the membrane bound ATP synthase of Escherichia coli. Mol. Gen. Genet. 184 (1), 33-39 (1981) PubMed: 6278247. Kanazawa,H., Mabuchi,K., Kayano,T., Noumi,T., Sekiya,T. and Futai,M.Nucleotide sequence of the genes for F0 components of theproton-translocating ATPase from Escherichia coli: prediction of the primary structure of F0 subunits. Biochem. Biophys. Res. Commun. 103 (2), 613-620 (1981) PubMed: 6277311. Kumamoto,C.A. and Simoni,R.D. Genetic evidence for interaction between the a and b subunits of the F0 portion of the Escherichia coli proton translocating ATPase. J. Biol. Chem. 261 (22), 10037-10042 (1986) PubMed: 2874136. ","","Tue Jan 14 10:34:38 2003","1","","","" "AA01489","1001587","1001336","252","ATGGAAACTGTAATTACAGCTACAATTATCGGTGCATCTATCCTTCTTGCATTCGCTGCATTGGGCACGGCAATCGGCTTTGCTATCTTAGGCGGTAAATTCTTAGAATCATCCGCCCGTCAGCCGGAACTAGCTTCAAGCCTACAAACTAAAATGTTTATCGTGGCAGGTCTTTTAGATGCGATTGCGATGATTGCAGTTGGTATTTCTTTACTTTTCATTTTTGCAAACCCATTCATCGGTTTATTACAA","","","9108","METVITATIIGASILLAFAALGTAIGFAILGGKFLESSARQPELASSLQTKMFIVAGLLDAIAMIAVGISLLFIFANPFIGLLQ","1001336","From GenBank (gi:1168602):This is one of the three chains of the nonenzymatic component (CF(0) subunit) of the ATPase complex. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF91) has five subunits: alpha(3), beta(3), gamma(1), delta(1), and epsilon(1). CF(0) has three main subunits: a, b, and c.","ATP synthase F0, subunit c","Inner membrane, Cytoplasm","","
InterPro
IPR000454
Family
ATPase, F0 complex, subunit C
PR00124\"[11-30]T\"[32-47]T\"[49-74]TATPASEC
PS00605\"[39-60]TATPASE_C
InterPro
IPR002379
Family
ATPase, F0/V0 complex, subunit C
G3DSA:1.20.20.10\"[2-78]Tno description
PF00137\"[7-76]TATP-synt_C
InterPro
IPR005953
Family
ATPase, F0 complex, subunit C, bacterial and chloroplast
TIGR01260\"[19-76]TATP_synt_c: ATP synthase F0, C subunit
noIPR
unintegrated
unintegrated
signalp\"[1-26]?signal-peptide
tmhmm\"[10-32]?\"[53-75]?transmembrane_regions


","BeTs to 15 clades of COG0636COG name: F0F1-type ATP synthase c subunit/Archaeal/vacuolar-type H+-ATPase subunit KFunctional Class: CThe phylogenetic pattern of COG0636 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.5e-17) to 1/1 blocks of the IPB000454 family, which is described as \"Eubacterial and plasma membrane ATP synthase subunit C\". Interpro entry for IP:IPR000454. IPB000454 15-68 2e-17","Residues 16 to 73 match (8e-13) PD:PD186061 which is described as ATP LIPID-BINDING SYNTHASE SUBUNIT TRANSMEMBRANE ION C HYDROGEN CHAIN CF0 ","","","","","","","","","","","Tue Jan 21 11:10:03 2003","Tue Jan 21 11:10:03 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01489 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 76 (E-value = 9.9e-25) place AA01489 in the ATP-synt_C family which is described as ATP synthase subunit C (PF00137)","","","","","Secondary Laboratory Evidence:Nielsen,J., Hansen,F.G., Hoppe,J., Friedl,P. and von Meyenburg,K.The nucleotide sequence of the atp genes coding for the F0 subunits a, b, c and the F1 subunit delta of the membrane bound ATP synthase of Escherichia coli. Mol. Gen. Genet. 184 (1), 33-39 (1981) PubMed: 6278247. Kanazawa,H., Mabuchi,K., Kayano,T., Noumi,T., Sekiya,T. andFutai,M. Nucleotide sequence of the genes for F0 components of the proton-translocating ATPase from Escherichia coli: prediction ofthe primary structure of F0 subunits. Biochem. Biophys. Res. Commun. 103 (2), 613-620 (1981) PubMed: 6277311Kumamoto,C.A. and Simoni,R.D. Genetic evidence for interaction between the a and b subunits ofthe F0 portion of the Escherichia coli proton translocating ATPase.J. Biol. Chem. 261 (22), 10037-10042 (1986) PubMed: 2874136. ","","Tue Jan 14 10:55:47 2003","1","","","" "AA01490","1002429","1001644","786","ATGTCTGAACAAACAACTTCAGAATATATCGGTCACCACTTATCTTTCCTTAAAACGGGGGACGGTTTCTGGAATATTCACGTTGATACCTTATTTTTCTCTATTCTGTCTGCCGTTATTTTCCTTTTCATTTTCAGACGGGTTGCTAAAAAGGCAACGCCGGGTGTACCGGGAAAATTACAATGTCTGGTGGAAATCCTGGTAGGTTGGGTTAACGGCATCGTTAAAGAAAATTTCCATGGTCCGCGCGAGGTGGTGGCACCGATTGCCCTGACCATTTTCTGTTGGGTATTCATTATGAATGCCATCGACTTAATCCCTGTTGATTTCCTTCCGCAACTTGCCGGATTATTCGGTATTCACTATTTAAGAACCGTCCCTACGGCAGATATTAGCGCTACTTTGGGGATGTCGATTTGCGTCTTCTTCCTGATTCTTTTCTATACGGTTAAATCCAAAGGGGTTAGCGGTTTAGTTAAGGAATATACCTTACATCCGTTTAATTACTGGGCATTTATCCCTGTTAACTTTATTCTCGAAACTGTTACTTTACTGGCTAAACCGATTTCTCTCGGCTTCCGTTTGTTCGGTAACATGTATGCGGGCGAATTAATCTTTATTCTTATTGCCGTTATGTATTCCGCCAATATGGCGATTGCGGCACTGGGAATTCCATTACACCTTGCTTGGGCGATTTTCCATATTTTGGTTATCACGTTACAAGCATTCATTTTTATGATGTTGACGGTGGTTTATTTGAGTATTGCTTATAACAAAGCAGAACAT","","","29328","MSEQTTSEYIGHHLSFLKTGDGFWNIHVDTLFFSILSAVIFLFIFRRVAKKATPGVPGKLQCLVEILVGWVNGIVKENFHGPREVVAPIALTIFCWVFIMNAIDLIPVDFLPQLAGLFGIHYLRTVPTADISATLGMSICVFFLILFYTVKSKGVSGLVKEYTLHPFNYWAFIPVNFILETVTLLAKPISLGFRLFGNMYAGELIFILIAVMYSANMAIAALGIPLHLAWAIFHILVITLQAFIFMMLTVVYLSIAYNKAEH","1001644","From GenBank (gi:1168558): AtpB is a key component of the protonchannel and may play a direct role in the translocation of protonsacross the membrane. F-type ATPases have two components, CF(1), the catalytic core, and CF(0), the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), and epsilon(1). CF(0) has three main subunits: a, b and c. ","ATP synthase F0, subunit a","Inner membrane, Cytoplasm","","
InterPro
IPR000568
Family
ATPase, F0 complex, subunit A
PR00123\"[89-105]T\"[187-209]T\"[240-255]TATPASEA
PTHR11410\"[29-109]T\"[125-234]TATP SYNTHASE SUBUNIT 6
PF00119\"[24-255]TATP-synt_A
TIGR01131\"[5-257]TATP_synt_6_or_A: ATP synthase F0, A subunit
PS00449\"[190-199]TATPASE_A
noIPR
unintegrated
unintegrated
tmhmm\"[25-45]?\"[85-107]?\"[126-146]?\"[167-185]?\"[204-226]?\"[236-256]?transmembrane_regions


","BeTs to 16 clades of COG0356COG name: F0F1-type ATP synthase a subunitFunctional Class: CThe phylogenetic pattern of COG0356 is ------yqv-rlbcefghsnujx--wNumber of proteins in this genome belonging to this COG is","Significant hit ( 3.5e-35) to 3/3 blocks of the IPB000568 family, which is described as \"ATP synthase A subunit\". Interpro entry for IP:IPR000568. IPB000568A 92-113 2.3e-06 IPB000568B 174-209 2.1e-17 IPB000568C 233-253 2.2e-08","Residues 5 to 55 match (1e-15) PD:PD015851 which is described as A ION CHAIN CF0 SYNTHASE HYDROGEN TRANSMEMBRANE ATP PROTEOME COMPLETE ","","","","","","","","","","","Tue Jan 21 11:14:40 2003","Tue Jan 21 11:13:03 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01490 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 83 to 255 (E-value = 4.3e-64) place AA01490 in the ATP-synt_A family which is described as ATP synthase A chain (PF00119)","","","","","Nielsen,J., Hansen,F.G., Hoppe,J., Friedl,P. and von Meyenburg,K. The nucleotide sequence of the atp genes coding for the F0 subunits a,b, c and the F1 subunit delta of the membrane bound ATP synthase ofEscherichia coli. Mol. Gen. Genet. 184 (1), 33-39 (1981) PubMed: 6278247. Kanazawa,H., Mabuchi,K., Kayano,T., Noumi,T., Sekiya,T. and Futai,M. Nucleotide sequence of the genes for F0 components of the proton-translocating ATPase from Escherichia coli: prediction of theprimary structure of F0 subunits. Biochem. Biophys. Res. Commun. 103 (2), 613-620 (1981) PubMed: 6277311. Cain,B.D. and Simoni,R.D. Impaired proton conductivity resulting from mutations in the a subunit of F1F0 ATPase in Escherichia coli. J. Biol. Chem. 261 (22), 10043-10050 (1986) PubMed: 2874137. Kumamoto,C.A. and Simoni,R.D. Genetic evidence for interaction between the a and b subunits of the F0portion of the Escherichia coli proton translocating ATPase. J. Biol. Chem. 261 (22), 10037-10042 (1986) PubMed: 2874136. Cain,B.D. and Simoni,R.D. Proton translocation by the F1F0ATPase of Escherichia coli. Mutagenic analysis of the a subunit. J. Biol. Chem. 264 (6), 3292-3300 (1989) PubMed: 2536742. Yamada,H., Moriyama,Y., Maeda,M. and Futai,M. Transmembrane topology of Escherichia coli H(+)-ATPase (ATP synthase)subunit a. FEBS Lett. 390 (1), 34-38 (1996) PubMed: 8706824. Valiyaveetil,F.I. and Fillingame,R.H. Transmembrane topography of subunit a in the Escherichia coli F1F0 ATP synthase. J. Biol. Chem. 273 (26), 16241-16247 (1998) PubMed: 9632683. ","","Tue Jan 14 11:01:55 2003","1","","","" "AA01491","1002831","1002457","375","ATGTCCAGAGTTTTAGCACAAGCCCGAGCCAAATATAAAAAATCCATTTACATTGAATTTTTCGTCGGTCTTGTTTTGAGCTCTATTATTGCGTTGTTAGCCAATACCCAAAGTGCGGTTGATTTCTGCTTAGGATTTTTTGCCGCGTTCATACCTTTTTTTATCTTTGTGTATGTTGTTTTTTATCGCAATCAGGATTTATCAAAAAAATTAACCGCACTTTATCGTGGTGAAGCCATTAAATTCGTATTGACGATTCTACTGATTATTTTTTCGTTCAAATGGCTTTCGGTAACATATTTTATTGTTTTCTTTACAGGTTTTTTTACAGCATTAATGCTAAATAATATTATCCCATTTCTGCTGAATAGGTCT","","","14431","MSRVLAQARAKYKKSIYIEFFVGLVLSSIIALLANTQSAVDFCLGFFAAFIPFFIFVYVVFYRNQDLSKKLTALYRGEAIKFVLTILLIIFSFKWLSVTYFIVFFTGFFTALMLNNIIPFLLNRS","1002457","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-38]?signal-peptide
tmhmm\"[12-34]?\"[40-62]?\"[72-92]?\"[102-122]?transmembrane_regions


","No hits to the COGs database.","","Residues 1 to 124 match (2e-14) PD:PD174571 which is described as PROTEOME COMPLETE HI0485.1 PM1487 TRANSMEMBRANE ","","","","","","","","","","","","Tue Jan 14 11:17:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01491 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01492","1003626","1002946","681","ATGCATAGAATACTGACCGCACTTTCAAGTAGAATGTGCGGTGTTCCTAAAGAGAGTATCTCATCAATGAAAGCTAAATTAGATAGCCTCCTTGCACAAGCGAAGATTCAACCAAACGATCAACAAAAACAGCAATTGATCGACTTCGTCAATTTATTAAACAAATGGAATAAAGCCTATAATTTAACCTCCGTGCGCGATCCGCAAGACATGTTGGTGAAACATATTTTGGATAGCCTCGTGGTTAGCCTTCATTTACAAGGTGATCGTTTTATTGATGTAGGTACCGGTCCTGGCTTGCCCGGCTTGCCGTTGGCGATCATTAACCCTGATAAGCAGTTTGTACTGTTGGATAGCCTGGGCAAGCGTATCAGCTTTATTCGTAATGCGGTTCGTGAGTTGGGACTAACAAACGTTAAGCCTGTTCTAAGCCGTGTGGAAGAATATCAACCAGAAGAAAAATTCGACGGCGTATTAAGCCGCGCTTTTGCTTCCTTAAAAGACATGACAGAATGGTGCTGGCATTTACCCAAACCTGATGGTATGTTTTATGCGTTAAAAGGTATTTATCAGCAGGAAGAAGCACAAAATTTAAGTGATCAATTTCAGATTGAAAATGTGATTTCTATTGAGGTTCCAACACTTATCGGTGAACGCCATTTAATACTTTTGACTAAAAAG","","","25687","MHRILTALSSRMCGVPKESISSMKAKLDSLLAQAKIQPNDQQKQQLIDFVNLLNKWNKAYNLTSVRDPQDMLVKHILDSLVVSLHLQGDRFIDVGTGPGLPGLPLAIINPDKQFVLLDSLGKRISFIRNAVRELGLTNVKPVLSRVEEYQPEEKFDGVLSRAFASLKDMTEWCWHLPKPDGMFYALKGIYQQEEAQNLSDQFQIENVISIEVPTLIGERHLILLTKK","1002946","From GenBank (gi:12518597): The function of this protein may bemacromolecule synthesis. It may be involved in modification of DNA -replication, repair, restriction/modification. It is a glucose-inhibited division protein and is possibly involved inchromosome replication.From GenBank (gi:1169897): This protein is a probable S-adenosyl-L-methionine dependent methyltransferase specific for a sterol and/or lipid substrate.","glucose inhibited division protein B","Cytoplasm","","
InterPro
IPR003682
Family
Glucose inhibited division protein
PD004441\"[52-126]TGIDB_PASMU_P57946;
PF02527\"[42-222]TGidB
TIGR00138\"[46-226]TgidB: methyltransferase GidB
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[23-227]Tno description


","No hits to the COGs database.","Significant hit ( 1.1e-52) to 3/3 blocks of the IPB003682 family, which is described as \"Glucose inhibited division protein\". Interpro entry for IP:IPR003682. IPB003682A 53-80 2.1e-14 IPB003682B 93-118 8.3e-15 IPB003682C 155-195 9.2e-21","Residues 46 to 194 match (7e-66) PD:PD004441 which is described as INHIBITED GLUCOSE DIVISION B COMPLETE PROTEOME ","","","","","","","","","","","Tue Jan 21 11:20:20 2003","Tue Jan 14 11:19:21 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01492 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 42 to 222 (E-value = 2.8e-88) place AA01492 in the GidB family which is described as Glucose inhibited division protein (PF02527)","","","","","Walker,J.E., Gay,N.J., Saraste,M. and Eberle,A.N. DNA sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and phoS. The Biochemical journal. 224 (3), 799-815 (1984). PubMed: 6395859. Romanowski MJ, Bonanno JB, Burley SK. Crystal structure of the Escherichia coli glucose-inhibited division protein B (GidB) reveals a methyltransferase fold. Proteins. 2002 Jun 1;47(4):563-7. . PMID: 12001236","","Wed Feb 5 13:28:22 2003","1","","","" "AA01494","1003981","1003622","360","ATGGAAAATATTTTTGAACGTGGCAATGTTTTGGCTTCAGATTGTCCTTCACGCCAAATTTTACAGCATTTAACCAACCGTTGGGGCGTTTTGGTGTTGGTGAGTCTGTATTCCGGTACTAAACGTTTTAGCGAATTGCGTCGCGCCATTGACGGTGTGAGTGAGCGAATGCTGACGAAGACCTTACAAGAATTGGAAGCGGACGGTATGTTAGTTCGCAAATCCTATAACACAGTGCCGCCGCAAGTGGATTACACGCTGACGGAATTTGGTTCGGAGGCGTCAAGTAAAATGTTTGAATTGGTGGATTGGCTGGAAACGAATTTAACCGGGATTTTGCAGCAACAGGCGAAAAATGCA","","","14481","MENIFERGNVLASDCPSRQILQHLTNRWGVLVLVSLYSGTKRFSELRRAIDGVSERMLTKTLQELEADGMLVRKSYNTVPPQVDYTLTEFGSEASSKMFELVDWLETNLTGILQQQAKNA","1003622","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR002577
Domain
Helix-turn-helix, HxlR type
PD004032\"[42-77]TQ9K3V3_STRCO_Q9K3V3;
PF01638\"[23-113]TDUF24
PS51118\"[15-113]THTH_HXLR


","No hits to the COGs database.","","Residues 21 to 81 match (3e-16) PD:PD589677 which is described as COMPLETE PROTEOME PLASMID HYDROLASE RSP0843 REGULATOR ESTER MLR2600 ATU2000 AGR_C_1731P ","","","","","","","","","","","","Tue Jan 14 11:20:25 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01494 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 23 to 113 (E-value = 9.8e-30) place AA01494 in the DUF24 family which is described as Transcriptional regulator (PF01638)","","","","","","","","1","","","" "AA01495","1004232","1004987","756","GTGCGTTCTCCGGAAAAAATTTCAGGTGCGCAAGCCCGCAAATTTGACTATTTAAAAGTGGAAGGTCAAGTAGAAGCACTACGAGGCATAGACACTTTAATTCTAGTATCAAGCAATGAAATCGGGCAACGTTTCGTACAACACAATAATGTCATTGAATCAGCCAAAAAAGCAGGCGTGAAGCGTATCATCTATATTAGTTTTATCAATGTTAACAAAGAAAACAATGTACGTTTATTATCAGATGAATATGTACAAACCGAAGCTGCATTAAAAGCATCAGGTATTACTTACACCATTCTACGCAACGGCTGGTACACCGAAAACCATACCGCCTCTATTCCTGCAGCATTGGAAAATAACGCTTTCTACGGTTCTGCAAAAGAAGGACGTATTTCATCCGCCCTTCGTGCAGAACTTGCTGAAGCCGCGGTAAATGTGACATTAGGCGAAGGTCACGACAACCAAACTTACGAACTTGCCGGCTCAACCAGTTGGACATTAGCGGATTTAGCCGCAGAAATCAGTAAACAAACAGGCAAAGACATTCCCTATGTCGATCTTCCTGCCGCAGATTATTCAGCAGCACTTATAAAAGCAGGCTTGCCTGAAGATTTTGCAAGGTTAACTGCAGAATGTGATGTAGACGCATCAAACGGTGCATTATTTTCAGAGGATAAAACCCTTGAAAAATTAATCGGTCGCCCAACCACAAGATTAGATGTGGCAGTGCAACAGGCATTGCAACTTTTACCA","","","27342","VRSPEKISGAQARKFDYLKVEGQVEALRGIDTLILVSSNEIGQRFVQHNNVIESAKKAGVKRIIYISFINVNKENNVRLLSDEYVQTEAALKASGITYTILRNGWYTENHTASIPAALENNAFYGSAKEGRISSALRAELAEAAVNVTLGEGHDNQTYELAGSTSWTLADLAAEISKQTGKDIPYVDLPAADYSAALIKAGLPEDFARLTAECDVDASNGALFSEDKTLEKLIGRPTTRLDVAVQQALQLLP","1004987","","probable oxidoreductase","Cytoplasm","","
InterPro
IPR008030
Family
NmrA-like
PF05368\"[6-187]TNmrA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[1-185]Tno description
PTHR14194\"[9-251]TNITROGEN METABOLIC REGULATION PROTEIN NMR-RELATED
PTHR14194:SF2\"[9-251]TUNCHARACTERIZED


","No hits to the COGs database.","","Residues 101 to 132 match (1e-06) PD:PD071844 which is described as PROTEOME COMPLETE HI0742 YPO1645 ","","","","","","","","","","","","Tue Jan 14 12:11:48 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01495 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01496","1007151","1005265","1887","ATGTTTTATACAGAAACCTATGATGTCATCGTAATCGGTGGCGGTCATGCAGGAACCGAAGCCGCCTTGGCACCTGCGCGCATGGGGTTAAAAACCCTGTTGCTTACCCATAATATCGATACTTTAGGGCAAATTTCTTGTAACCCGGCGATTGGTGGGATCGGAAAAGGGCATTTGGTCAAAGAAATTGATGCCATGGGCGGTTTAATGGCAACCGCAGCAGATAAGGCGGGTATTCAATTTCGCACCTTAAATAGCAGCAAAGGTCCTGCCGTACGCGCTACTCGCGCACAAACGGATCGCGTGTTATATCGCCAAGCGGTCAGAATCGCATTGGAAAATCAACCGAATTTGGATATTTTCCAACAAGAAGCCACAGATATTTTAATCGAACAGGATCGCGCCACGGGTGTGGTCACCAAAATGGGGCTAAAATTTCACGCCAAAGCTGTGATTCTCACTGCCGGCACTTTCCTCGCCGGCAAGATCCATATTGGTTTGGAAAATTATACCGGCGGGCGTGCAGGTGATCCTGCTTCCGTCACATTAGCCCAGCGTTTGCGCGATCTCAATTTACGGGTGGATCGCTTAAAAACCGGTACACCACCGCGTATTGATGCGCGTACGATCAATTTTGATGTGCTTGCTAAACAACATGGCGATGCCGTATTGCCAGTGTTCTCGTTTATGGGATCTGTTTCCGATCTCCCACAACAAATTCCTTGTTATATCACCCATACTAACGAGCAAACTCATGACGTGATCCGCAATAATTTGGATCGCAGCCCAATGTACACCGGTGTGATTGAAGGCATCGGTCCACGTTACTGTCCGTCTATTGAAGATAAAGTGATGCGTTTTGCGGATCGCAATTCTCATCAGATTTACCTTGAACCGGAAGGCTTAACCAGTAATGAAATTTATCCGAACGGAATCTCCACCAGTTTGCCGTTTGATGTGCAAATGGGGATCGTGAATTCCATGAAAGGTTTGGAAAAGGCACGAATCGTCAAACCGGGTTACGCCATTGAATACGATTATTTTGATCCGCGTGATCTCAAACCGACCTTAGAAACCAAAGCGATCTCCGGTTTATTCTTTGCCGGTCAAATTAACGGCACAACCGGTTATGAAGAAGCAGCGGCACAAGGTTTACTTGCCGGGATCAACGCCGGGCTTTATGTGCAGGAAAAAGATGCCTGGTTCCCACGTCGTGATCAGGCTTATATTGGTGTGTTGGTGGATGATCTTTGCACCCTTGGTACTAAAGAACCATATCGCGTGTTTACTTCCCGTGCGGAATATCGCTTGTTGTTACGTGAAGATAACGCCGATATTCGTTTAACGCCGATTGCGCACGAATTAGGTTTAATTGATGAAGCGCGTTGGGCGCGTTTTAATCAAAAAATGGAAAATATTGAGCTTGAACGCCAACGTTTACGCAGCATTTGGTTGCACCCGCGTTCAGAATATTTGGAAGAAGCGAATAAAGTGTTGGGTAGTCCATTGGTGCGCGAAGCCAACGGTGAAGATTTATTGCGTCGCCCGGAAATGAACTATGAGATTTTAACTTCTTTGACGCCTTATCAACCAGCAATGGAAGATAAAGAAGCAGTGGAACAAGTGGAAATTGCTATTAAATATCAAGGTTATATTGAACATCAAGAAGAAGAAATCGAAAAACAAAAACGCCACGAAAACACAGCGATTCCTGCACAGTTTGATTATGCTAAAGTCTCCGGTTTATCAAACGAAGTACGTGCTAAGTTAGAACAACATCGTCCGGTGTCTATCGGGCAAGCAAGCCGTATTTCCGGCATCACGCCAGCAGCTATTTCCATCATTTTAGTGAACTTGAAAAAACAAGGGATGTTAAAGCGTGGGGAG","","","69930","MFYTETYDVIVIGGGHAGTEAALAPARMGLKTLLLTHNIDTLGQISCNPAIGGIGKGHLVKEIDAMGGLMATAADKAGIQFRTLNSSKGPAVRATRAQTDRVLYRQAVRIALENQPNLDIFQQEATDILIEQDRATGVVTKMGLKFHAKAVILTAGTFLAGKIHIGLENYTGGRAGDPASVTLAQRLRDLNLRVDRLKTGTPPRIDARTINFDVLAKQHGDAVLPVFSFMGSVSDLPQQIPCYITHTNEQTHDVIRNNLDRSPMYTGVIEGIGPRYCPSIEDKVMRFADRNSHQIYLEPEGLTSNEIYPNGISTSLPFDVQMGIVNSMKGLEKARIVKPGYAIEYDYFDPRDLKPTLETKAISGLFFAGQINGTTGYEEAAAQGLLAGINAGLYVQEKDAWFPRRDQAYIGVLVDDLCTLGTKEPYRVFTSRAEYRLLLREDNADIRLTPIAHELGLIDEARWARFNQKMENIELERQRLRSIWLHPRSEYLEEANKVLGSPLVREANGEDLLRRPEMNYEILTSLTPYQPAMEDKEAVEQVEIAIKYQGYIEHQEEEIEKQKRHENTAIPAQFDYAKVSGLSNEVRAKLEQHRPVSIGQASRISGITPAAISIILVNLKKQGMLKRGE","1005265","From GenBank (gi:12518597): The function of this protein may bemacromolecule synthesis. It may be involved in modification of DNA - replication, repair, restriction/modification. It is a glucose-inhibited division protein and is possibly involved in chromosome replication.","glucose inhibited division protein A","Cytoplasm","","
InterPro
IPR002218
Family
Glucose-inhibited division protein A
PD003738\"[330-396]TGIDA_PASMU_P57945;
PTHR11806\"[12-620]TGLUCOSE INHIBITED DIVISION PROTEIN A
PF01134\"[8-399]TGIDA
PS01280\"[273-287]TGIDA_1
PS01281\"[368-391]TGIDA_2
InterPro
IPR004416
Family
Glucose-inhibited division protein A subfamily
TIGR00136\"[7-623]TgidA: glucose-inhibited division protein A
noIPR
unintegrated
unintegrated
G3DSA:3.50.50.60\"[3-156]Tno description


","BeTs to 18 clades of COG0445COG name: NAD/FAD-utilizing enzyme apparently involved in cell divisionFunctional Class: DThe phylogenetic pattern of COG0445 is ------yqvd-lbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit (1.4e-283) to 9/9 blocks of the IPB002218 family, which is described as \"Glucose inhibited division protein A family\". Interpro entry for IP:IPR002218. IPB002218A 26-75 1.3e-41 IPB002218B 137-174 1.2e-26 IPB002218C 176-221 2.8e-27 IPB002218D 239-267 5.8e-24 IPB002218E 273-301 3e-25 IPB002218F 311-365 1.8e-42 IPB002218G 371-391 9.9e-19 IPB002218H 405-448 1.8e-39 IPB002218I 570-612 1.2e-29Significant hit ( 2e-07) to 1/5 blocks of the PR00368 family, which is described as \"FAD-dependent pyridine nucleotide reductase signature\". Prints database entry for PR:PR00368. PR00368A 8-30 2e-07 PR00368C 8-33 0.0022Significant hit ( 3.9e-06) to 2/6 blocks of the IPB000447 family, which is described as \"FAD-dependent glycerol-3-phosphate dehydrogenase\". Interpro entry for IP:IPR000447. IPB000447A 7-59 0.00026 IPB000447C 140-162 6.7Significant hit ( 1.3e-05) to 1/5 blocks of the IPB000103 family, which is described as \"Pyridine nucleotide-disulphide oxidoreductase class-II\". Interpro entry for IP:IPR000103. IPB000103A 8-28 1.3e-05","Residues 273 to 309 match (3e-10) PD:PD581259 which is described as II CHROMOSOME F52H3.2 MITOCHONDRIAL MITOCHONDRION 2310039H01RIK MTO1 TRANSLATION OPTIMIZATION C30B4.06 ","","","","","","","","","","","Tue Jan 14 12:14:39 2003","Tue Jan 14 12:14:39 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01496 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 406 (E-value = 2.1e-266) place AA01496 in the GIDA family which is described as Glucose inhibited division protein A (PF01134)","","","","","White DJ, Merod R, Thomasson B, Hartzell PL. GidA is an FAD-binding protein involved in development of Myxococcus xanthus. Mol Microbiol. 2001 Oct;42(2):503-17. PMID: 11703671 ","","Wed Feb 5 13:29:16 2003","1","","","" "AA01497","1008037","1007597","441","ATGCAGCCTAAAATTTGCTTAATTACCGGCAGCACATTAGGTGGCGCCGAATATGTTGCCGAACACTTGGAAGGCGTATTACAACAGCAGGGTTTCAGCACCGCACTTCTGCACGGACCCTCTTTAGACGAAGTTATTAACGAAAAACTATGGTTAGTGGTCACCTCCACCCACGGCGCCGGCGAATTACCGGATAACCTAAAACCGCTATTTGATGAACTCAAAACCGGTGATGCGGATCTTTCAGAGTTACGATTTGCCGTCATCGGCTTGGGCAATTCCGACTATGATACCTTCTGTTTTGCGGTGGATACGGTAGAACAGACCTTGCAGGCAAAAAGTGCGGTCAAAATTATCGACGCTTTGCGTATTGATGTCTTAACGGAAACCGATCAGGAACAATGTGCGGAAGACTGGCTGCCTAACTTTCTGCACCATCTT","","","16093","MQPKICLITGSTLGGAEYVAEHLEGVLQQQGFSTALLHGPSLDEVINEKLWLVVTSTHGAGELPDNLKPLFDELKTGDADLSELRFAVIGLGNSDYDTFCFAVDTVEQTLQAKSAVKIIDALRIDVLTETDQEQCAEDWLPNFLHHL","1007597","","MioC protein","Cytoplasm","","
InterPro
IPR001094
Domain
Flavodoxin-like
PR00369\"[6-19]T\"[52-63]T\"[83-93]TFLAVODOXIN
InterPro
IPR008254
Domain
Flavodoxin/nitric oxide synthase
PF00258\"[7-139]TFlavodoxin_1
PS50902\"[5-144]TFLAVODOXIN_LIKE
InterPro
IPR014357
Family
Flavodoxin
PIRSF000088\"[2-146]TFlavodoxin
InterPro
IPR015702
Domain
NADPH Cytochrome P450 Reductase
PTHR19384:SF17\"[46-147]TNADPH CYTOCHROME P450 REDUCTASE
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.360\"[4-147]Tno description
PTHR19384\"[46-147]TFLAVODOXIN-RELATED


","BeTs to 6 clades of COG0716COG name: FlavodoxinsFunctional Class: CThe phylogenetic pattern of COG0716 is a-m---y----lbcefghs-uj--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.7e-09) to 4/4 blocks of the PR00369 family, which is described as \"Flavodoxin signature\". Prints database entry for PR:PR00369. PR00369A 6-19 73 PR00369B 52-63 0.024 PR00369C 83-93 0.03 PR00369D 107-126 6.9","Residues 5 to 52 match (2e-07) PD:PD498430 which is described as ELECTRON PROTEOME COMPLETE HOMOLOG FLAVOPROTEIN MIOC FMN ","","","","","","","","","","","","Tue Jan 14 12:17:17 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01497 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 139 (E-value = 3.5e-32) place AA01497 in the Flavodoxin_1 family which is described as Flavodoxin (PF00258)","","","","","Lobner-Olesen,A. and Boye,E. Different effects of mioC transcription on initiation of chromosomal and minichromosomal replication in Escherichia coli Nucleic Acids Res. 20 (12), 3029-3036 (1992) PubMed: 1620598 Birch,O.M., Hewitson,K.S., Fuhrmann,M., Burgdorf,K., Baldwin,J.E., Roach,P.L. and Shaw,N.M. MioC is an FMN-binding protein that is essential for Escherichia coli biotin synthase activity in vitro J. Biol. Chem. 275 (41), 32277-32280 (2000) PubMed: 10913144 ","","Tue Jan 14 12:17:17 2003","1","","","" "AA01498","1008312","1008097","216","ATGTCACTAGAAATTCTAGACCAGTTAGAAAACAAGATTAAACAAGCTGTCGAAACCATTCAGTTGCTTCAATTGGAAGTGGATGAATTAAGAGAAAAAAGCAGCAGAGCACAACAAGAAAATGATGCACTACGTGGTGAAAACGAACAATTAAGAGGCGAACACCAAAATATTCAAGAACGTTTACGTTCACTCTTAGGTATCACCGACAGCATC","","","8338","MSLEILDQLENKIKQAVETIQLLQLEVDELREKSSRAQQENDALRGENEQLRGEHQNIQERLRSLLGITDSI","1008097","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR009252
Family
Protein of unknown function DUF904
PF06005\"[1-72]TDUF904


","BeTs to 3 clades of COG3074COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3074 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 1 to 72 match (1e-10) PD:PD019455 which is described as PROTEOME COMPLETE CYTOPLASMIC PM1483 HI0668 STS164 STY3782 VC2686 YPO0093 YIIU ","","","","","","","","","","","","Tue Jan 14 12:20:27 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01498 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 72 (E-value = 3.3e-27) place AA01498 in the DUF904 family which is described as Protein of unknown function (DUF904) (PF06005)","","","","","","","","1","","","" "AA01499","1008497","1009507","1011","ATGAACAGAGCATTAGCCATTGAATTTTCAAGAGTTACGGAAGTTGCCGCGTTAGCCGGTTTTGCCTGGTTGGGGCGCGGGGATAAAAATGCAGCGGATGATGCGGCGGTGAAAGCCATGCGTTATATGCTGAACTTAATTCATATGGATGCGGAAATAGTGATTGGTGAAGGAGAAATTGATCAGGCACCTATGTTGTATATCGGTGAAAAAGTCGGTTCGGGCATGGGTGAGCTGGTGTCCATTGCCGTTGATCCTATTGACGGTACGCGAATGACGGCAATGGGACAGTCTAATGCCATTTCTGTGTTGGCGGCGGGCGGTAAAAATACCTTTTTAAAAGCGCCGGATATGTACATGGAAAAACTGGTGGTCGGCCCGGAAGTGAAAGGCTTGATTGATTTAAATTTACCTATTGAACAAAATTTACGCCGTGTTGCTTCTAAATTAGGCAAATTACTCTCCGATTTAAGTGTCATGGTCTTGGATAAACCCCGTCATAGCGCGGTGATTGAAAAAATGCACGAGTTGGGTGTACGCGTATTTACCGTTCCTGACGGCGATGTTACCGCTTCCGTTTTATGTTGTTTGCCGGAAGCGGAAGTAGACATGGTTTATGGTATTGGTGGTACGCCGGAAGGTGTTGTGGCGGCAGCTGCCATTCGCGCACTGGGCGGTGATATGCAGGTTCGTTTGTTGCCACGTGATCAGGTGAAAGGCGACACGCCGGAAAATAACGCTTTGGCGGCGGAGGAAATTCGCCGTTGTCAGGAAATGGGCGTGGAAGTGAACGCCGTATTGCAATTGGAACAATTGGTGCGTGATGATAATTTGGTGTTTGCCGCAACGGGCATTACTAACGGCGATTTATTAAAAGGTATCCACCGCAAAGGTAATTTGGCGACAACGGAAACTTTATTAATTCGTGGTAAATCCAGAACCATTCGTCGTATTCAATCCACCCATTATTTAGACCGAAAAGACACCGCACTTTATCGTTTAATTAATGCT","","","36359","MNRALAIEFSRVTEVAALAGFAWLGRGDKNAADDAAVKAMRYMLNLIHMDAEIVIGEGEIDQAPMLYIGEKVGSGMGELVSIAVDPIDGTRMTAMGQSNAISVLAAGGKNTFLKAPDMYMEKLVVGPEVKGLIDLNLPIEQNLRRVASKLGKLLSDLSVMVLDKPRHSAVIEKMHELGVRVFTVPDGDVTASVLCCLPEAEVDMVYGIGGTPEGVVAAAAIRALGGDMQVRLLPRDQVKGDTPENNALAAEEIRRCQEMGVEVNAVLQLEQLVRDDNLVFAATGITNGDLLKGIHRKGNLATTETLLIRGKSRTIRRIQSTHYLDRKDTALYRLINA","1009507","From GenBank (gi:1169957):The GlpX protein is of unknown function, but is probably involved in glycerol metabolism.","fructose 1,6-bisphosphatase protein","Cytoplasm","","
InterPro
IPR004464
Family
GlpX
PD007014\"[4-59]TGLPX_HAEIN_P44811;
PIRSF004532\"[1-333]TFructose-1,6-bisphosphatase, GlpX type
PF03320\"[2-322]TFBPase_glpX
TIGR00330\"[1-335]TglpX: fructose-1,6-bisphosphatase, class II
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.90\"[110-276]Tno description
signalp\"[1-27]?signal-peptide


","BeTs to 7 clades of COG1494COG name: Fructose-1,6-bisphosphatase/sedoheptulose 1,7-bisphosphatase and related proteinsFunctional Class: GThe phylogenetic pattern of COG1494 is ---------dr-bce-gh---j----Number of proteins in this genome belonging to this COG is","","Residues 1 to 319 match (2e-139) PD:PD007014 which is described as COMPLETE PROTEOME GLPX GLYCEROL METABOLISM FRUCTOSE-16-BISPHOSPHATASE GLYCEROL-INDUCIBLE METABOLIC METABIOLISM HOMOLOG ","","","","","Mon Feb 17 08:38:55 2003","","","","","","Mon Feb 17 08:38:55 2003","Mon Feb 17 08:38:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01499 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 322 (E-value = 7.1e-224) place AA01499 in the FBPase_glpX family which is described as Bacterial fructose-1,6-bisphosphatase, glpX-encoded (PF03320)","","","","","Donahue JL, Bownas JL, Niehaus WG, Larson TJ;Purification and characterization of glpX-encoded fructose 1,6-bisphosphatase, a new enzyme of the glycerol 3-phosphate regulon of Escherichia coli. J Bacteriol 2000;182:5624-5627. PMID: 10986273Truniger V, Boos W, Sweet G.Molecular analysis of the glpFKX regions of Escherichia coli and Shigella flexneri.J Bacteriol. 1992 Nov;174(21):6981-91.PMID: 1400248 ","","Mon Feb 17 08:38:55 2003","1","","","" "AA01500","1009951","1009856","96","ATGCAAAATCAATCTCTATTTTCAAATAGAAAATTTCTATTTGCCCTTTTTATCAGTTTATTTTTTGTTTTTCCTGCAGAAATAATACGGATAAAT","","","3835","MQNQSLFSNRKFLFALFISLFFVFPAEIIRIN","1009856","","hypothetical protein","Cytoplasm, Periplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-28]?signal-peptide
tmhmm\"[12-31]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 16:48:34 2004","Thu Feb 26 16:48:34 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01500 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 16:48:34 2004","","","","","","","","","","","","","1","","","" "AA01501","1009972","1010100","129","TTGGTTTTTAAGTTTAAAAATAACAAAAAAACTAACCGCACCTTAATACGCCTAAAGTGCGGTTATAAAATCCAACGGATTTTGAAAGTTGGCTTTGTCAACGGCCCCATTGGGACGAACAATCGAACT","","","4975","LVFKFKNNKKTNRTLIRLKCGYKIQRILKVGFVNGPIGTNNRT","1010100","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 16:46:57 2004","Thu Feb 26 16:46:57 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01501 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 16:46:57 2004","","","","","","","","","","","","","1","","","" "AA01502","1010948","1010154","795","ATGTCGTTAGAAGTTTGGCAAAATATTCGTCAGGAAGCGAAACAGCTCGTCGATAACGAACCTATGCTTGCCAGTTTTTTTCATTCGACGATTTTAAAACATCACAATTTAGGCAGTGCATTAAGCTACATTTTAGCCAATAAATTAGCCAATACCATCATGCCCGCCATCGCGTTACGTGAAATCATCGAAGAAACCTATCAGGCAAAACCCGGCATTATCGAATGTGCCGCCTGCGACATCATGGCTGTGCGTCAGCGTGACCCGGCGGTTGAATTATTATCCACGCCGTTGCTTTATTTAAAAGGCTTTCACGCTTTACAAAGTTATCGCATCACCCATTATTTATGGCAACAAAATCGCAAAGCCCTGGCGATTTATCTGCAAAACCAAATTTCTGTCGCGTTTGACGTGGATATTCACCCCGCGGCAAAAATCGGACATGGTATTATGTTTGACCATGCCACCGGCATTGTAGTGGGTGAAACCTCGGTCATTGAAAATAATGTATCCATTTTACAAGGGGTTACCTTAGGCGGAACGGGAAAAGAATCCGGTGATCGGCATCCAAAAGTGCGCGAAGGCGTGATGATCGGCGCTGGTGCAAAAATTTTAGGCAACATTGAAATCGGAAAATATGCTAAAATTGGTTCCAATTCCGTAGTGTTGCAACCAGTGCCGGAATATGCCACCGCAGCGGGCGTACCTGCACGAATCATTGGTAAAGATAAAGATGCCAAACCGGCGTTCGATATGAACCAAAACTTTATTGATCTTGGTATGGAACTGAATATC","","","28966","MSLEVWQNIRQEAKQLVDNEPMLASFFHSTILKHHNLGSALSYILANKLANTIMPAIALREIIEETYQAKPGIIECAACDIMAVRQRDPAVELLSTPLLYLKGFHALQSYRITHYLWQQNRKALAIYLQNQISVAFDVDIHPAAKIGHGIMFDHATGIVVGETSVIENNVSILQGVTLGGTGKESGDRHPKVREGVMIGAGAKILGNIEIGKYAKIGSNSVVLQPVPEYATAAGVPARIIGKDKDAKPAFDMNQNFIDLGMELNI","1010154","","serine acetyltransferase","Cytoplasm","","
InterPro
IPR001451
Repeat
Bacterial transferase hexapeptide repeat
PF00132\"[131-148]T\"[163-180]T\"[189-206]T\"[207-224]THexapep
PS00101\"[198-226]THEXAPEP_TRANSFERASES
InterPro
IPR005881
Family
Serine O-acetyltransferase
TIGR01172\"[77-238]TcysE: serine O-acetyltransferase
InterPro
IPR010493
Domain
Serine acetyltransferase, N-terminal
PF06426\"[5-109]TSATase_N
noIPR
unintegrated
unintegrated
G3DSA:1.10.3130.10\"[4-138]Tno description
G3DSA:2.160.10.10\"[139-254]Tno description
PTHR23416\"[140-240]TSIALIC ACID SYNTHASE-RELATED
PTHR23416:SF2\"[140-240]TSERINE ACETYLTRANSFERASE


","No hits to the COGs database.","Significant hit ( 1.6e-13) to 1/1 blocks of the IPB001451 family, which is described as \"Bacterial transferase hexapeptide repeat\". Interpro entry for IP:IPR001451. IPB001451 192-227 1.6e-13","Residues 134 to 240 match (5e-07) PD:PD102549 which is described as (see also SP:P70729_AZOBR_P70729).","","","","","","","","","","","","Wed Jan 15 13:44:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01502 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 109 (E-value = 2.8e-61) place AA01502 in the SATase_N family which is described as Serine acetyltransferase, N-terminal (PF06426)","","","","","Hindson,V.J., Moody,P.C., Rowe,A.J. and Shaw,W.V. Serine acetyltransferase from Escherichia coli is a dimer oftrimers The Journal of biological chemistry. 275 (1), 461-466 (2000)PubMed: 10617639 Tei,H., Murata,K. and Kimura,A. Structure and expression of cysX, the second gene in the Escherichia coli K-12 cysE locus Biochemical and biophysical research communications. 167(3), 948-955 (1990) PubMed: 2108679 Wigley,D.B., Derrick,J.P. and Shaw,W.V. The serine acetyltransferase from Escherichia coli. Over-expression, purification and preliminarycrystallographic analysis FEBS letters. 277 (1-2), 267-271 (1990) PubMed: 2125278 Denk,D. and Bock,A. L-cysteine biosynthesis in Escherichia coli: nucleotidesequence and expression of the serine acetyltransferase (cysE) gene from the wild-type and a cysteine-excreting mutant Journal of general microbiology. 133 (Pt 3), 515-525 (1987) PubMed: 3309158 ","","Wed Jan 15 13:44:44 2003","1","","","" "AA01503","1011964","1010954","1011","ATGAATACGACCATAGCCGATTTCCCTATCACCGTGCTGGGTGCCGGTTCTTTTGGTACGGCATTGGCTATCGCTTTTTCGCGCAACGGGCATTCCACCTATCTGTGGGGACACAACCCGGCAAAAATGCAACAACTTCAGGCAGATCGTCAAAATAAAGTATTTTTACCCGAGATTGTTTTTCCTTCATCTTTGGTTATTGAAGCCAATTTAGGCAAAGTGATTCAAGCCTCAAAGGATTTATTACTTGCCGTGCCAAGCCATTGCTTCGGTGAAATTCTCGATGAAATTCGACCGCACTTACGCCCCGATCATCGTATTATATGGGCAACCAAAGGCTTGGAGCGGGATACGGGTCGTTTACTGGAAGAGGTAATTAAAGAAAAACTTGGCGAACAGTACCCGCTGGCGGTACTTTCCGGCCCGACATTTGCCAAAGAACTGGCTTCCGGTTTACCTACCGCCATTACGCTGGCGTCCGATAACGACGACTTTGCCCGGCAATTTCAGGCGCGCATTCATTGCAGTAAACATTTTCGGGTTTATATCAATAATGATATGCTCGGCGTACAACTGGGCGGGGCGATTAAAAACGTGATTGCCATCGGTGCGGGTATTTCCGACGGTATGGGTTTCGGTGCCAATGCCAGAACCGCCTTAATTACCCGTGGCATTGCGGAAATATCCCGTTTAGGTGCCGCACTTGGCGCTAATCCGAATACTTTCATGGGAATGTCCGGTTTAGGTGATTTGGTATTGACCTGCACCGATAACCAATCACGCAACCGCCGTTTCGGTATAATGCTTGGGCAAGGCGTTTCGGCACAAGCGGCGATGGAAAATATCGGACAGGTGGTGGAAGGCTTTTATAACACCAAAGAAGCCCATTTATTGGCGCAACGGCATGACATAGAAATGCCAATTACCGAACAAATTTATCAAGTGCTGTTCTGCGGCAAAGCAGCAAAAGATGCCGCCGTTAATTTACTCGGCAGAGAACGTAAAGGGGAA","","","36597","MNTTIADFPITVLGAGSFGTALAIAFSRNGHSTYLWGHNPAKMQQLQADRQNKVFLPEIVFPSSLVIEANLGKVIQASKDLLLAVPSHCFGEILDEIRPHLRPDHRIIWATKGLERDTGRLLEEVIKEKLGEQYPLAVLSGPTFAKELASGLPTAITLASDNDDFARQFQARIHCSKHFRVYINNDMLGVQLGGAIKNVIAIGAGISDGMGFGANARTALITRGIAEISRLGAALGANPNTFMGMSGLGDLVLTCTDNQSRNRRFGIMLGQGVSAQAAMENIGQVVEGFYNTKEAHLLAQRHDIEMPITEQIYQVLFCGKAAKDAAVNLLGRERKGE","1010954","","glycerol-3-phosphate dehydrogenase","Cytoplasm, Periplasm, Inner membrane","","
InterPro
IPR006109
Domain
NAD-dependent glycerol-3-phosphate dehydrogenase, C-terminal
PD001278\"[211-317]TQ8CP64_STAEP_Q8CP64;
PF07479\"[185-329]TNAD_Gly3P_dh_C
InterPro
IPR006168
Family
NAD-dependent glycerol-3-phosphate dehydrogenase
PR00077\"[12-29]T\"[62-89]T\"[138-158]T\"[179-203]T\"[204-228]T\"[244-261]TGPDHDRGNASE
PTHR11728\"[10-337]TGLYCEROL-3-PHOSPHATE DEHYDROGENASE
PS00957\"[194-215]TNAD_G3PDH
InterPro
IPR011128
Domain
NAD-dependent glycerol-3-phosphate dehydrogenase, N-terminal
PF01210\"[8-167]TNAD_Gly3P_dh_N
InterPro
IPR013328
Domain
Dehydrogenase, multihelical
G3DSA:1.10.1040.10\"[195-337]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[9-193]Tno description
PIRSF000114\"[10-333]TGlycerol-3-phosphate dehydrogenase (NAD)
signalp\"[1-23]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","BeTs to 21 clades of COG0240COG name: Glycerol 3-phosphate dehydrogenaseFunctional Class: CThe phylogenetic pattern of COG0240 is a-m---yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 6.7e-42) to 6/8 blocks of the IPB001652 family, which is described as \"NAD-dependent glycerol-3-phosphate dehydrogenase\". Interpro entry for IP:IPR001652. IPB001652A 10-27 0.067 IPB001652C 43-88 0.031 IPB001652E 138-154 0.00053 IPB001652F 189-228 7.5e-19 IPB001652G 241-262 5.2e-06 IPB001652H 277-313 1.4","Residues 10 to 170 match (2e-07) PD:PD547303 which is described as DEHYDROGENASE GLYCEROL-3-PHOSPHATE PHOSPHOLIPID PROBABLE PROTEOME NADP COMPLETE NADPH-DEPENDENT OXIDOREDUCTASE NAD ","","","","","","","","","","","","Wed Jan 15 13:47:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01503 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 9 to 329 (E-value = 1.3e-149) place AA01503 in the NAD_Gly3P_dh family which is described as NAD-dependent glycerol-3-phosphate dehydrogenase (PF01210)","","","","","Arcari,P., Russo,A.D., Ianniciello,G., Gallo,M. andBocchini,V. Nucleotide sequence and molecular evolution of the genecoding for glyceraldehyde-3-phosphate dehydrogenase in thethermoacidophilic archaebacterium Sulfolobus solfataricus Biochem. Genet. 31 (5-6), 241-251 (1993) PubMed: 8259927 Jones,C.E., Fleming,T.M., Cowan,D.A., Littlechild,J.A. and Piper,P.W. The phosphoglycerate kinase and glyceraldehyde-3-phosphate dehydrogenase genes from the thermophilic archaeonSulfolobus solfataricus overlap by 8-bp. Isolation, sequencing of the genes and expression in Escherichia coli Eur. J. Biochem. 233 (3), 800-808 (1995) PubMed: 8521845 Shimizu H, Nishiyama K, Tokuda H. Expression of gpsA encoding biosynthetic sn-glycerol3-phosphate dehydrogenase suppresses both the LB- phenotypeof a secB null mutant and the cold-sensitive phenotype of asecG null mutant. Mol Microbiol. 1997 Dec;26(5):1013-21. PMID: 9426138 ","","Wed Jan 15 13:47:40 2003","1","","","" "AA01506","1012554","1012045","510","ATGACCGAAGAAAACAAAGAAGTGACAAACCAAGAACAGGAAGTTCAAGCGGTGTTGCAAATTCAACGCATTTATGTGAAAGACGTTTCTTTTGAAGCACCAAACCTACCGCATATTTTCAACCAAGAATGGAAACCGCGTTTAAGTTTTGATTTATCTACCGAAACCGCTAAATTAGACGATGATTTATATGAAGTCTGCTTAAATATTTCAGTGGAAACTACATTGGAAGATTCCGGTGATGTGGCATTCATCTGTGAAGTGAAACAAGCAGGCGTGTTTACCATCAGTGGCTTGGAAGAAATGCAAATGGCGCATTGCTTAACTTCACAATGCCCGAATATGTTATTCCCGTATGCGCGCGAATTGGTTTCCAACTTAGTAAACCGCGGTACTTTCCCGGCATTAAATCTTTCTCCGGTAAATTTTGACGCGCTATTTGTTGAATATTTACAACGTCAGGAACAACAAGCGCAAGAGGCCGGCGAGCAAAGCGAACCAACAGTAAAT","","","19295","MTEENKEVTNQEQEVQAVLQIQRIYVKDVSFEAPNLPHIFNQEWKPRLSFDLSTETAKLDDDLYEVCLNISVETTLEDSGDVAFICEVKQAGVFTISGLEEMQMAHCLTSQCPNMLFPYARELVSNLVNRGTFPALNLSPVNFDALFVEYLQRQEQQAQEAGEQSEPTVN","1012045","From Genbank (gi:1173413):This is one of the proteins required for the normal export of envelope proteins out of the cell cytoplasm; it may be involved in the initiation of the exporting process, by binding to the nascent prolypeptide via a signal sequence, maintaining a stable and pre-translocation conformation.","protein-export protein","Cytoplasm","","
InterPro
IPR003708
Family
Bacterial protein export chaperone SecB
PD021849\"[24-151]TSECB_HAEIN_P44853;
PR01594\"[21-38]T\"[83-103]T\"[107-129]T\"[133-151]TSECBCHAPRONE
G3DSA:3.10.420.10\"[2-170]Tno description
PF02556\"[1-156]TSecB
TIGR00809\"[13-157]TsecB: protein-export chaperone SecB


","BeTs to 8 clades of COG1952COG name: Preprotein translocase subunit SecBFunctional Class: NThe phylogenetic pattern of COG1952 is --m-----------efghsn-jx---Number of proteins in this genome belonging to this COG is","Significant hit ( 8.3e-52) to 2/2 blocks of the IPB003708 family, which is described as \"Bacterial protein export chaperone SecB\". Interpro entry for IP:IPR003708. IPB003708A 19-52 1.6e-21 IPB003708B 112-147 4.3e-29","Residues 16 to 151 match (4e-65) PD:PD021849 which is described as COMPLETE PROTEOME SECB PROTEIN-EXPORT TRANSLOCATION PROTEIN-TRANSPORT PROBABLE MOLECULAR TRANSLOCASE OR ","","","","","","","","","","","Wed Jan 15 13:52:13 2003","Wed Jan 15 13:52:13 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01506 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 156 (E-value = 4.9e-92) place AA01506 in the SecB family which is described as Preprotein translocase subunit SecB (PF02556)","","","","","Kumamoto,C.A. and Nault,A.K. Characterization of the Escherichia coli protein-exportgene secB Gene. 75 (1), 167-175 (1989) PubMed: 2656409 Miller A, Wang L, Kendall DA. SecB modulates the nucleotide-bound state of SecA andstimulates ATPase activity. Biochemistry. 2002 Apr 23;41(16):5325-32. PMID: 11955083 Sapriel G, Wandersman C, Delepelaire P. The N terminus of the HasA protein and the SecB chaperonecooperate in the efficient targeting and secretion of HasAvia the ATP-binding cassette transporter. J Biol Chem. 2002 Feb 22;277(8):6726-32. PMID: 11698405 Kononova SV, Khokhlova OV, Zolov SN, Nesmeyanova MA. Effect of export-specific cytoplasmic chaperone, proteinSecB, on secretion of Escherichia coli alkalinephosphatase. Biochemistry (Mosc). 2001 Jul;66(7):803-7. PMID: 11563962 ","","Wed Jan 15 13:52:13 2003","1","","","" "AA01507","1013070","1012573","498","ATGACTCAAGTAAAGTTATACTTGAGCCCTTATTTTTTAAACCTAATTATTGAGAAAAAAATGCAAGAATTTATACCCATGGCAACCGCTTTTGCCAAAAATCATACCTTGATCGTCGTCGCTTGGGTAGCTGTCTTTTTGATGGTGATCTATAATTTCGTAAAATCTGCCACCAGTAAAACCAAACTTATTGATAATGCGGAAGCGATTTCTTTAATGAACAACCAAAATGCCGTGGTTATCGACTTACGCTCCATTGATGAGTTTAACAAAGGCCATATCATAAACAGTTTAAACATCCTGCCTTCCGAAATTAAAAACAACAATATCGGAAAAATTGAACAGCACAAAGACATTCCGGTAATTTTAGCCTGTGCCGATTTCGTTTCTTCCCGTTCTTCCGGTGAAATTCTGGCAAAACAAGGTTTCAATCATGTTTATGTGCTAAGAGAAGGCATCGGCGGCTGGCGTGCAGCAAATTTACCTTTAGTTAAAAAA","","","18584","MTQVKLYLSPYFLNLIIEKKMQEFIPMATAFAKNHTLIVVAWVAVFLMVIYNFVKSATSKTKLIDNAEAISLMNNQNAVVIDLRSIDEFNKGHIINSLNILPSEIKNNNIGKIEQHKDIPVILACADFVSSRSSGEILAKQGFNHVYVLREGIGGWRAANLPLVKK","1012573","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR001763
Domain
Rhodanese-like
PF00581\"[65-159]TRhodanese
SM00450\"[64-162]TRHOD
PS50206\"[74-165]TRHODANESE_3
noIPR
unintegrated
unintegrated
G3DSA:3.40.250.10\"[40-165]Tno description
signalp\"[1-47]?signal-peptide
tmhmm\"[36-54]?transmembrane_regions


","BeTs to 14 clades of COG0607COG name: Rhodanese-related sulfurtransferasesFunctional Class: PThe phylogenetic pattern of COG0607 is aomp--yq-drlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 2.5e-07) to 2/2 blocks of the IPB001763 family, which is described as \"Rhodanese/cdc25 fold\". Interpro entry for IP:IPR001763. IPB001763A 81-94 0.00024 IPB001763B 145-156 0.5","Residues 21 to 58 match (4e-09) PD:PD033278 which is described as PROTEOME COMPLETE PM1433 HI0744 ","","","","","","","","","","","","Wed Jan 15 13:59:11 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01507 is paralogously related to AA00581 (5e-10) and AA02249 (0.001).","","","","","","Residues 65 to 159 (E-value = 7.9e-15) place AA01507 in the Rhodanese family which is described as Rhodanese-like domain (PF00581)","","","","","","","","1","","","" "AA01508","1013338","1014657","1320","ATGTCTGCTATGTTTTTATTTCAGTTCGCCATTGTGTTGCTCTGCATTTTAATCGGTGCGCGTGTTGGCGGAATCGGTTTAGGTGTATTTGGTGGCTTGGGGCTTACAATTTTGTCCTTTGGGTTCGGTTTAAAACCTGCCGGCTTGCCAATTGATGTGATGTTTATGATTATGGCGGTAGTTGCAGCGGCAGCGGCAATGCAGGCTGCCGGTGGGTTAGATTACATGATCAAAATTGCCACTAATATTTTACGTCGTAATCCGAAATACATTACTTTTATGGCACCTGCGGTAACTTGGACATTTACGCTGTTAGCAGGAACCGGTCACGTGGCTTACTCCGTATTACCGGTTATCGCTGAAGTGAGCCGTCAAAATGGTATTCGCCCGGAGCGTCCGTTATCCATGGCGGTTATCGCATCACAATTTGCTATTGTTGCAAGCCCGATTGCGGCGGCGGTGGTAGCCGTGGTTGCCTACCTTGAACCGCAGGGTATTCACCTGGGGGATGTCCTGATTGTTACCATTCCTTCTACTATAATCGGTCTTTTCCTTGCTTGTATCTTTGTGAACAAAATGGGCAAAGAATTAAAAGATGATCCGGAATATCAACGTCGTTTAAACGATCCTAAATATGCGGAAGCTTTCAATTCAACCACTAGCAGTAAAGAACTTGAAATCAGCAAAACCGCAAAAATTTCCGTCTCACTATTCTTATTCGGTGCATTACTTGTGGTTTTAATGGGGGCAATGCCTTCATTACGTCCGGTGTTCGACGGCAAACCGATGGGTATGGCACACACCATTGAAATTATTATGTTAACCATCGGTGCATTAATTATCTTAACCTGTAAACCGGACGGTACGGAAATTACCAAGGGTTCGGTATTTCATGCCGGTATGCGTGCAGTTATCGCCATTTTCGGTATCGCATGGTTAGGTGATACGTTAATGCAGGCGCATCTTGAAGAAGTGAAAGGTATGGTGAGGGGTTTGGTAGAAACTGCGCCTTGGACATTTGCAATCGCCTTATTTATCCTGTCCGTATTGGTAAACAGCCAAGGGGCAACGGTGGCAACATTATTCCCGCTTGGTATTGCCCTTGGCATTCCGCCGGCAGTATTAGTTGGTGTGTTTGTGGCGGTAAACGGTTATTTCTTCATTCCGAACTACGGTCCGATCATTGCCTCTATCGACTTTGACACTACGGGCACCACACGCATCGGTAAATACATTTTCAATCACAGCTTCATGTTGCCGGGCTTATTGAGTATGGCATTCAGCTTAGCCTTAGGCTTATTATTTGCAAATATTTTCCTA","","","46743","MSAMFLFQFAIVLLCILIGARVGGIGLGVFGGLGLTILSFGFGLKPAGLPIDVMFMIMAVVAAAAAMQAAGGLDYMIKIATNILRRNPKYITFMAPAVTWTFTLLAGTGHVAYSVLPVIAEVSRQNGIRPERPLSMAVIASQFAIVASPIAAAVVAVVAYLEPQGIHLGDVLIVTIPSTIIGLFLACIFVNKMGKELKDDPEYQRRLNDPKYAEAFNSTTSSKELEISKTAKISVSLFLFGALLVVLMGAMPSLRPVFDGKPMGMAHTIEIIMLTIGALIILTCKPDGTEITKGSVFHAGMRAVIAIFGIAWLGDTLMQAHLEEVKGMVRGLVETAPWTFAIALFILSVLVNSQGATVATLFPLGIALGIPPAVLVGVFVAVNGYFFIPNYGPIIASIDFDTTGTTRIGKYIFNHSFMLPGLLSMAFSLALGLLFANIFL","1014657","From GenBank (gi:1169253): This protein is responsible forthe transport of C4-dicarboxylates from the periplasmaccross the inner membrane. Belongs to the DcuA/DcuB familyof transporters.","anaerobic C4-dicarboxylate transporter","Inner membrane, Cytoplasm","","
InterPro
IPR004668
Family
Anaerobic c4-dicarboxylate membrane transporter
PD014334\"[214-425]TQ7VPN1_HAEDU_Q7VPN1;
PIRSF004539\"[4-440]TAnaerobic C4-dicarboxylate transporter
PF03605\"[8-372]TDcuA_DcuB
TIGR00770\"[8-440]TDcu: transporter, anaerobic C4-dicarboxylat
noIPR
unintegrated
unintegrated
signalp\"[1-24]?signal-peptide
tmhmm\"[5-23]?\"[29-49]?\"[54-72]?\"[97-117]?\"[138-160]?\"[170-190]?\"[234-254]?\"[264-284]?\"[294-314]?\"[333-351]?\"[361-381]?\"[419-439]?transmembrane_regions


","BeTs to 5 clades of COG2704COG name: Anaerobic C4-dicarboxylate transporterFunctional Class: RThe phylogenetic pattern of COG2704 is --------------e-gh--u-----Number of proteins in this genome belonging to this COG is","","Residues 4 to 440 match (5e-169) PD:PD014334 which is described as COMPLETE PROTEOME ANAEROBIC C4-DICARBOXYLATE TRANSPORTER MEMBRANE INNER TRANSMEMBRANE DCUA DCUB ","","","","","","","","","","","Wed Jan 15 14:02:17 2003","Wed Jan 15 14:02:17 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01508 is paralogously related to AA02726 (3e-61).","","","","","","Residues 8 to 372 (E-value = 1.8e-247) place AA01508 in the DcuA_DcuB family which is described as Anaerobic c4-dicarboxylate membrane transporter (PF03605)","","","","","Six,S., Andrews,S.C., Unden,G. and Guest,J.R. Escherichia coli possesses two homologous anaerobicC4-dicarboxylate membrane transporters (DcuA and DcuB)distinct from the aerobic dicarboxylate transport system(Dct). J. Bacteriol. 176 (21), 6470-6478 (1994) PubMed: 7961398. Six,S., Andrews,S.C., Roberts,R.E., Unden,G. and Guest,J.R.Construction and properties of Escherichia coli mutantsdefective in two genes encoding homologous membrane proteinswith putative roles in anaerobic C4-dicarboxylic acidtransport. Biochem. Soc. Trans. 21 (4), 342S (1993) PubMed: 8131924 ","","Wed Jan 15 14:02:17 2003","1","","","" "AA01509","1014832","1016574","1743","ATGATTGATAAACAGCTGATAAATACGGTCGCCAACAGCAAAAAATGGATTGCGATTAATGTATTGTGGAACTGGGTTGCATTAATTGGCGGCATTATTAGCGCAGTGGTGTTTGCCGTTTGTTTGCAATGGGCGTTTGAGCGTTCGCTTACCCTCCAAAGTGCGGTTATTTTTACCGTCGTTTTAATTGCCTGTTTGGCACTACGTGCCTGGGCGGGCAAAATGGCAGTGAAAGCGTCCTATAAAGCCAGTACGCAGGTGAAACACAAATTACGCACGCTGATTTATCAAAAACTGTCTTCCATGCCGCTTAATCAAGTAAATCAACAATCAACCTCTTCCGTAATTCAAGTGGCTTCCGAAGGGGTAGAACAGCTGGAAATTTATTTCGGGCGTTATCTCCCGCAGCTTTTTTACAGCCTGCTTGCGCCACTCACGTTGTTTATTTTTTTGGTTTTTTTCAACGCGCCAACGTCCCTCATTCTGTTGGTTTGCGTACCGTTAATTCCTATGTCCATTATTGCCGTGAATAAAATCGCGAAACGTTTATTAGCGAAATATTGGTCCATTTATGTGGGTTTAGGCAGCAGTTTTTTGGATAACTTACAAGGCTTGATTACTTTAAAAATCTATCAGGACGACGATTACAAAGCTAAACAAATGGACATTGAAGCGGAAAATTTCCGCACTATTACCATGAAAGTGCTCACTATGCAGCTGAACTCCGTTTCGCTAATGGATTTATTGGCTTACGGCGGCGCTGCGCTGGGTATTTTGACCGCACTTTTACAATTTCAGGACGGCAATTTATCCATTTTCGGCGTGGTGTTGTTTATTTTACTGGCTTCCGAATTTTTCATTCCATTGCGCTTGCTTGGTTCCTTCTTCCATGTGGCGATGAACGGCAAAGCTGCTTCGGAAAAAATCTTTACGCTGTTGGATACGCCGGTGGAAGAAAATAAAAGTGCGGTGGATTTTCCGGTTAAAAATGAAGTCACCGTGCAAATTAACGATTTACATTTTGCCTATTCCGAGGAAAAACCCGCCATTAACGGCTTAACCCTCAGCATCCAGCCGAAACAGTTAACGGTTTTCGTGGGCAAAAGCGGTTGTGGCAAATCGACCTTGGTATCTTTACTAATGGGGTTCTATCAGGCGCAACAAGGCGAAATTTTGTTTAACGGCATCGATATTAAACAGATTAACCGCCATTCCTTATATCGCCACATTTCGCTGGTAAGTCACAGCAGTTACATTTTCAAAGGCAGCTTGCGGGAAAATATGCTAATGATGTTATCAAATGCCTCCGACGAAGTCATTTATCAATGTTTGGAACAAGTGAATCTGGCGAATTTTGTGCGGGAAAACGGCGGTTTGGAGATGCCGTTGCTCAGTCGCGGAAGCAATTTGTCCGGCGGGCAAATTCAACGTTTAGCGCTTGCCCGCGCCCTTTTGCATAACGCTGATGTCTATATTTTCGATGAAGCTACCAGTAACATCGATGTAGAAAGCGAAGAAATTATTCTGCAATTTATTCAACAGCTTAAACACAGCAAAACCATTGTGATGATTTCTCATCGGTTGGCAAACGCAATGAACGCGGATCAGATTTATGTGCTACAAAGCGGTCGCTTGATGGAATCCGGCGATCATGCCTCTTTAATGGCAGAAAACGGAATTTATGCAGAAATGTTCAATCAACAAAAGAATTTAGAAAATATCAGAATGGGGGCAAATCATGCG","","","64845","MIDKQLINTVANSKKWIAINVLWNWVALIGGIISAVVFAVCLQWAFERSLTLQSAVIFTVVLIACLALRAWAGKMAVKASYKASTQVKHKLRTLIYQKLSSMPLNQVNQQSTSSVIQVASEGVEQLEIYFGRYLPQLFYSLLAPLTLFIFLVFFNAPTSLILLVCVPLIPMSIIAVNKIAKRLLAKYWSIYVGLGSSFLDNLQGLITLKIYQDDDYKAKQMDIEAENFRTITMKVLTMQLNSVSLMDLLAYGGAALGILTALLQFQDGNLSIFGVVLFILLASEFFIPLRLLGSFFHVAMNGKAASEKIFTLLDTPVEENKSAVDFPVKNEVTVQINDLHFAYSEEKPAINGLTLSIQPKQLTVFVGKSGCGKSTLVSLLMGFYQAQQGEILFNGIDIKQINRHSLYRHISLVSHSSYIFKGSLRENMLMMLSNASDEVIYQCLEQVNLANFVRENGGLEMPLLSRGSNLSGGQIQRLALARALLHNADVYIFDEATSNIDVESEEIILQFIQQLKHSKTIVMISHRLANAMNADQIYVLQSGRLMESGDHASLMAENGIYAEMFNQQKNLENIRMGANHA","1016574","","ABC system transport protein, ATP binding/permease","Inner membrane, Cytoplasm","","
InterPro
IPR001140
Domain
ABC transporter, transmembrane region
PF00664\"[78-289]TABC_membrane
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[469-512]TQ9CKX7_PASMU_Q9CKX7;
PF00005\"[360-543]TABC_tran
PS50893\"[334-567]TABC_TRANSPORTER_2
PS00211\"[470-484]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[359-543]TAAA
InterPro
IPR011527
Domain
ABC transporter, transmembrane region, type 1
PS50929\"[26-301]TABC_TM1F
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[297-575]Tno description
PTHR19242\"[1-570]TATP-BINDING CASSETTE TRANSPORTER
PTHR19242:SF55\"[1-570]TABC TRANSPORTER (CYDD)
signalp\"[1-72]?signal-peptide
tmhmm\"[21-41]?\"[55-73]?\"[136-154]?\"[160-180]?\"[243-265]?\"[271-293]?transmembrane_regions


","BeTs to 20 clades of COG1132COG name: ABC-type multidrug/protein/lipid transport system, ATPase componentFunctional Class: QThe phylogenetic pattern of COG1132 is -o--k-yqvdrlbcefghsnujxi-wNumber of proteins in this genome belonging to this COG is","Significant hit ( 3.6e-56) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 349-395 4.1e-20 IPB001140B 467-505 1.8e-22 IPB001140C 520-549 6e-11","Residues 514 to 549 match (6e-07) PD:PD375591 which is described as ATP-BINDING ABC COMPLETE PROTEOME TRANSPORTER TRANSMEMBRANE MULTIDRUG RESISTANCE P-GLYCOPROTEIN GLYCOPROTEIN ","","","","","","","","","","","","Thu May 13 11:53:43 2004","","","Thu May 13 11:53:43 2004","Thu May 13 11:53:43 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01509 is paralogously related to AA02606 (1e-62), AA02805 (1e-47), AA01510 (3e-47), AA01961 (4e-46), AA02609 (1e-44), AA01393 (9e-44), AA02331 (6e-24), AA02440 (7e-20), AA01616 (5e-19), AA01645 (1e-18), AA01422 (3e-18), AA02324 (5e-18), AA01867 (4e-17), AA00799 (4e-17), AA02899 (1e-16), AA00700 (1e-16), AA02718 (2e-16), AA02550 (6e-16), AA01656 (1e-15), AA00415 (1e-15), AA02080 (7e-15), AA01051 (7e-15), AA00858 (9e-15), AA01524 (3e-14), AA02353 (6e-14), AA02152 (2e-13), AA02573 (4e-13), AA01820 (4e-13), AA00751 (8e-13), AA01824 (1e-12), AA01568 (2e-12), AA02140 (3e-12), AA02786 (5e-12), AA02320 (7e-12), AA01456 (9e-12), AA01779 (3e-11), AA01947 (3e-11), AA00933 (3e-11), AA02898 (5e-11), AA00591 (2e-10), A02145 (4e-10), AA01684 (1e-09), AA00207 (1e-09), AA01555 (3e-09), AA00061 (5e-08), AA02484 (6e-08), AA00934 (2e-07), AA02225 (2e-06), AA02642 (4e-05) and AA02146 (0.001).","Thu May 13 11:53:43 2004","","","","","Residues 360 to 543 (E-value = 3.2e-49) place AA01509 in the ABC_tran family which is described as ABC transporter (PF00005)","Thu May 13 11:53:43 2004","","","","Winstedt L, Yoshida K, Fujita Y, von Wachenfeldt C. Cytochrome bd biosynthesis in Bacillus subtilis:characterization of the cydABCD operon. J Bacteriol. 180(24):6571-80, 1998. PubMed: . Cook GM, Membrillo-Hernandez J, Poole RK. Transcriptional regulation of the cydDC operon, encoding aheterodimeric ABC transporter required for assembly ofcytochromes c and bd in Escherichia coli K-12: regulation byoxygen and alternative electron acceptors. J Bacteriol. 179(20):6525-30, 1997. PubMed: . Poole,R.K., Hatch,L., Cleeter,M.W., Gibson,F., Cox,G.B. andWu,G. Cytochrome bd biosynthesis in Escherichia coli: thesequences of the cydC and cydD genes suggest that theyencode the components of an ABC membrane transporter. Mol. Microbiol. 10(2): 421-430, 1993. PubMed: 7934832. Pittman MS, Corker H, Wu G, Binet MB, Moir AJ, Poole RK. Cysteine is exported from the Escherichia coli cytoplasm byCydDC, an ABC-type transporter required for cytochromeassembly. J Biol Chem. 2002 Oct 21 PMID: 12393891 ","","Wed Jan 15 14:11:22 2003","1","","","" "AA01510","1016570","1018225","1656","ATGCGTAAGAACGGATTTGTCGTCATGTGGCAGCTCATGAAATTGGTTACGCCGTTAGCCCACATCATGAGTTTCACCATCATTATGGGCACCCTCGGTTTCCTCAGCGCGATTTTCATTATGGTGCTGGGCGCCATGGGATTGGCGGAACTGCTCAATTTCCACGTTCACTTAAATTTATCGCAAATTTTGACCGCACTTATCGTGTTGGCGGTAGCACGCGGCATTTTGCGTTATCTGGAACAAATGTCCGGGCATTACATCGCTTTCAAATTATTGGCATTATTGCGCGATAAAGTGTTTGGCGCATTGCGTCGCCTGGCGTTCGTTAAATTGCAGGATAAACAATCCGGGCAATTGCTCTCTTTAGTCACCAACGACATTGAATTGTTGGAAGTGTTTTACGCACACACCATCGCCCCCATCGCTATTGCCTTTCTCACTTCCGCCATTTTATTGGCGGTATTCGCTCACATTTCCTGGTGGTTCGTGTTGGTGGCTCTGTTGGCGTATGTGACCATCGGCATTATTCTGCCTATCGTCACTACCCAAATGGCGCGCGAAGACGGGCGCAAATACCGCGAGCTGGTGGGCGAAATGAACGATTTCTTTCTCGACAGCATTCGTGGCATGAAAGAAATTCAGTTATTCGGCAACGAACAAAAACGCCTACAGGAAATTCACCAACGCAGCAAAAAAATCGATCAGGCATTCTTAAAAATCAAACAACAGGAAGGCAATGTGCGTTCCTTTACGGAAATCGCCGTATCGTTTTTTAATATCGTGATTTTACTGGTGGGCTTAACGTTATTTGCTTATGATAAAATTGATTTTGTCGGCTTGTTAGTGGCGGTGATTTTGCTTATGTCCGGCTACGGACCGGTGATTGCCTTAAGTAATCTCTCCAATAACCTGCTGCAAACCCTTGCCAGCGGCGAGCGGGTATTGGCGTTGCTGGCGGAACAGCCTGAATTGAAAGACGTGGAAAATGGAGTAAGTATCACCGATGTGCAGCAAATTAAGGTAGAAAATGTCAGTTTTGCTTATGCGCAGGAACAGATTTTGTCCGATGTGAATTTGCACATAAATAAAGGCGAAATCCTCGGCATTCACGGACGCAGCGGCAGCGGAAAAAGCACGCTGTTAAAATTGATTATGCGTTTTTACGATCCGCAACAAGGCAGCATCTGTATTAACGATACCGACTTAAAACACATTAACACCGTGAATTTGCGCGATAATATCGCTTACATCACGCAACAAACCTATATTTTCAACGAAACCATTTATGAAAATATTTTGTTGGCGAACCGCAACGCGACCAAAGAACAAGTGATTGAAGCGGCGAAAAAAGCGTCTATTCATGAATTTATCATGAGCCTGCCGGAAGTCTATGACACCAAAATTACCGAAATGGGGAACAACCTTTCTGACGGCGAAAAACAACGCATCGGTATTGCCCGCGCTTTCTTGCACAACGCGCCGATTATTTTGCTGGACGAACCTACCAGCAATCTGGACAGCTTAAACGAAGCCATGATTTTGCAATCTTTATTGAATGTAAAAGCGGAAAAATTAATCATCCTCGTCAGCCATCGCGCCTCCACCATGGCGATTTGCGATCAGGTGATCCCGATTGCCAACGGCCGAATGTCA","","","61699","MRKNGFVVMWQLMKLVTPLAHIMSFTIIMGTLGFLSAIFIMVLGAMGLAELLNFHVHLNLSQILTALIVLAVARGILRYLEQMSGHYIAFKLLALLRDKVFGALRRLAFVKLQDKQSGQLLSLVTNDIELLEVFYAHTIAPIAIAFLTSAILLAVFAHISWWFVLVALLAYVTIGIILPIVTTQMAREDGRKYRELVGEMNDFFLDSIRGMKEIQLFGNEQKRLQEIHQRSKKIDQAFLKIKQQEGNVRSFTEIAVSFFNIVILLVGLTLFAYDKIDFVGLLVAVILLMSGYGPVIALSNLSNNLLQTLASGERVLALLAEQPELKDVENGVSITDVQQIKVENVSFAYAQEQILSDVNLHINKGEILGIHGRSGSGKSTLLKLIMRFYDPQQGSICINDTDLKHINTVNLRDNIAYITQQTYIFNETIYENILLANRNATKEQVIEAAKKASIHEFIMSLPEVYDTKITEMGNNLSDGEKQRIGIARAFLHNAPIILLDEPTSNLDSLNEAMILQSLLNVKAEKLIILVSHRASTMAICDQVIPIANGRMS","1018225","","ABC transporter, ATP-binding protein/permease","Inner membrane, Cytoplasm","","
InterPro
IPR001140
Domain
ABC transporter, transmembrane region
PF00664\"[27-295]TABC_membrane
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[475-518]TY664_HAEIN_Q57538;
PF00005\"[365-549]TABC_tran
PS50893\"[340-552]TABC_TRANSPORTER_2
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[364-550]TAAA
InterPro
IPR011527
Domain
ABC transporter, transmembrane region, type 1
PS50929\"[25-307]TABC_TM1F
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[334-551]Tno description
PTHR19242\"[9-551]TATP-BINDING CASSETTE TRANSPORTER
PTHR19242:SF91\"[9-551]TLIPID A EXPORT ATP-BINDING/PERMEASE PROTEIN MSBA
signalp\"[1-37]?signal-peptide
tmhmm\"[15-49]?\"[55-77]?\"[138-156]?\"[162-182]?\"[254-274]?\"[278-298]?transmembrane_regions


","BeTs to 18 clades of COG1132COG name: ABC-type multidrug/protein/lipid transport system, ATPase componentFunctional Class: QThe phylogenetic pattern of COG1132 is -o--k-yqvdrlbcefghsnujxi-wNumber of proteins in this genome belonging to this COG is","Significant hit ( 5.9e-52) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 354-400 1.6e-25 IPB001140B 473-511 8.6e-21 IPB001140C 526-552 0.0061","Residues 40 to 241 match (7e-07) PD:PD108249 which is described as ATP-BINDING PROTEOME COMPLETE CYDD ABC TRANSPORTER TRANSMEMBRANE MEMBRANE TRANSPORTER INNER ","","","","","","","","","","","","Thu May 13 11:47:28 2004","","","Thu May 13 11:47:28 2004","Thu May 13 11:47:28 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01510 is paralogously related to AA01961 (1e-55), AA02609 (5e-55), AA01509 (3e-47), AA01393 (3e-45), AA02805 (1e-44), AA02606 (3e-39), AA02331 (4e-31), AA02320 (5e-22), AA02440 (2e-21), AA00415 (1e-20), AA01824 (4e-20), AA01867 (1e-19), AA02353 (3e-19), AA01051 (1e-18), AA01684 (5e-18), AA00858 (5e-18), AA02080 (8e-18), AA02718 (1e-17), AA01524 (1e-17), AA00933 (4e-17), AA01645 (7e-17), AA02140 (1e-16), AA02152 (2e-16), AA01820 (3e-16), AA02550 (1e-15), AA01616 (1e-15), AA01656 (6e-15), AA00700 (1e-14), AA00207 (2e-14), AA01779 (3e-14), AA00799 (3e-14), AA01456 (4e-14), AA01422 (5e-14), AA00751 (2e-13), AA02899 (8e-13), AA02786 (3e-12), AA02324 (4e-12), AA01568 (5e-12), AA02898 (6e-11), AA02484 (2e-10), AA00061 (2e-10), AA02573 (8e-10), AA00591 (8e-10), AA01757 (4e-09), AA01569 (7e-09), A02145 (3e-08), AA01555 (8e-08), AA02642 (1e-07), AA02225 (1e-05), AA01947 (1e-05) and AA02146 (6e-05).","Thu May 13 11:47:28 2004","","","","","Residues 365 to 549 (E-value = 5.3e-59) place AA01510 in the ABC_tran family which is described as ABC transporter (PF00005)","Thu May 13 11:47:28 2004","","","Guthmiller JM, Kolodrubetz D, Kraig E. Mutational analysis of the putative leukotoxin transport genes inActinobacillus actinomycetemcomitans. Microb Pathog. 1995 May;18(5):307-21. PMID: 7476096 Spitznagel J Jr, Kraig E, Kolodrubetz D. Regulation of leukotoxin in leukotoxic and nonleukotoxic strains of Actinobacillus actinomycetemcomitans. Infect Immun. 1991 Apr;59(4):1394-401. PMID: 2004819 Guthmiller JM, Kolodrubetz D, Cagle MP, Kraig E. Sequence of the lktB gene from Actinobacillus actinomycetemcomitans. Nucleic Acids Res. 1990 Sep 11;18(17):5291. No abstract available. PMID: 2402457","Davies RL, Campbell S, Whittam TS. Mosaic structure and molecular evolution of the leukotoxin operon(lktCABD) in Mannheimia (Pasteurella) haemolytica, Mannheimia glucosida, and Pasteurella trehalosi. J Bacteriol. 2002 Jan;184(1):266-77. PMID: 11741868 Schmitt L. Chang G, Roth CB.Structure of MsbA from E. coli: a homolog of themultidrug resistance ATP binding cassette (ABC) transporters. Science. 2001 Sep 7;293(5536):1793-800. PMID: 11546864 Schmitt L.The first view of an ABC transporter: the X-ray crystal structure of MsbA from E. coli.Chembiochem. 2002 Mar;3(2-3):161-5. Review. No abstract available.PMID: 11921393","Wed Jan 15 14:21:06 2003","Thu Jan 23 10:53:27 2003","1","","","" "AA01511","1018960","1018343","618","ATGGTCGGTATTCGGGCGCAGCAAAAAGAAAAAACCCGTCGTGCCTTAATTGATGCGGCTTTTAACCAGCTGACGGCAGAAAAGAGTTTTTCCAATTTGAGTTTGCGGGAAGTCTCCCGCGAGGCCGGTATTGCTCCGACCTCATTTTATCGCCATTTTCGCGATATGAATGAGCTTGGTCTCACCATGGTGGATGAAGCAGGTTTAATCCTACGTCAACTCATGCGTCAAGCACGTAAACGCATTGCCAACGGCGGAAGCGTTATCGTCATCTCAGTGGAAACCTTCTTTGAATTTATCAACAACAGTCCAAACATATTCCGCCTACTATTGCGTGAAAGTTCAGGCACATCACAGGCTTTCCGCACTGCCGCTGCCCGTGAAATAAAGCATTTTATCGACGAACTGTCAGAATACATTGCCCACAAAAACCACTATTCCCAATATATCGCTTATGTGCAGGCTGAAGGGATGGTCACCATTGTATTTACTACTGGCGCCAGTGCCTTAGACATGAGTAAGGCGGAACGGGAACAGTTAAAAGCGCGGTTGATTTTACAACTCAGAATGTTGGCAAAAGGGGCTAAATATGAAACCAGGGATAAATACAAGCCTGGC","","","23399","MVGIRAQQKEKTRRALIDAAFNQLTAEKSFSNLSLREVSREAGIAPTSFYRHFRDMNELGLTMVDEAGLILRQLMRQARKRIANGGSVIVISVETFFEFINNSPNIFRLLLRESSGTSQAFRTAAAREIKHFIDELSEYIAHKNHYSQYIAYVQAEGMVTIVFTTGASALDMSKAEREQLKARLILQLRMLAKGAKYETRDKYKPG","1018343","","probable transcriptional regulator","Cytoplasm","","
InterPro
IPR001647
Domain
Bacterial regulatory protein, TetR
PF00440\"[16-63]TTetR_N
PS50977\"[11-71]THTH_TETR_2
PS01081\"[29-59]?HTH_TETR_1
InterPro
IPR012287
Domain
Homeodomain-related
G3DSA:1.10.10.60\"[10-67]Tno description


","No hits to the COGs database.","Significant hit ( 1e-09) to 1/1 blocks of the IPB001647 family, which is described as \"Bacterial regulatory proteins, TetR family\". Interpro entry for IP:IPR001647. IPB001647 29-59 1e-09","Residues 5 to 59 match (9e-18) PD:PD000384 which is described as TRANSCRIPTION DNA-BINDING REGULATION TRANSCRIPTIONAL COMPLETE PROTEOME REGULATOR FAMILY TETR REGULATOR ","","","","","","","","","","","","Wed Jan 15 14:30:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01511 is paralogously related to AA02137 (1e-04).","","","","","","Residues 16 to 63 (E-value = 1.5e-10) place AA01511 in the TetR_N family which is described as Bacterial regulatory proteins, tetR family (PF00440)","","","","","","","","1","","","" "AA01513","1019871","1018975","897","ATGAATATTCGTGATTTAGAATACCTTGTAGCGCTTGCCGAACACAAGCACTTTCGTCGTGCGGCGGATTCTTGTCATGTAAGCCAACCGACATTAAGCGGACAAATTCGTAAACTGGAAGATGAGTTGGGTATTATTCTGTTGGAACGTACCAGCCGTAAAGTATTGTTTACCCAATCGGGTTTATTATTGGTGGATCAGGCTAAAACCGTCTTGCGCGAAGTAAAGTTATTAAAAGAAATGGCAAGCAACCAAGGCAAAGACATGACCGGTCCGCTACATATAGGCATTATTCCTACTGTAGGACCTTATCTAATGCCTCATATCGTACCGACCTTACAGCAAAATTTCCCTGATCTGGAATTATTCCTTTATGAAGCACAAACCTATAGGTTGTTAGAACAACTGGAAACCGGTCGATTGGATTGTGCTATTGTAGCGTCCGTACCGGAAACTGAAGCCTTTATTGAAGTCCAACTATTTAATGAAAAAATGCTTCTTGCCGTTGCTGAGCAGCACCCATGGGCTAATGAAAATTCAGTCTCAATGTCCTTACTAAAAGACTGTGAAATATTAATGTTGGACGATGGGCATTGCTTACGCAACCAAGCATTAGGTTATTGCTTCACTGCCGGCGCACGGGAAAACGCCCACTTTCAGGCAACCAGCTTAGAAACTCTACGCAACATGGTCGCTGCCAATACCGGCGTCACTTTAATGCCACAGCTTGCTGTGCTCAGTGAAGGCAATCGTAGTGGCGTAAAATACCTGCCTTGTGATGAACCGGAACCATCCCGCGACATTACCTTGGTTTATCGCCCGGGTTCACCATTACGTGCACGTTATGAGCGAGTAGCAAATACGGTGAGTCAATCGGTTAAATCTATCTTATCTTCT","","","33389","MNIRDLEYLVALAEHKHFRRAADSCHVSQPTLSGQIRKLEDELGIILLERTSRKVLFTQSGLLLVDQAKTVLREVKLLKEMASNQGKDMTGPLHIGIIPTVGPYLMPHIVPTLQQNFPDLELFLYEAQTYRLLEQLETGRLDCAIVASVPETEAFIEVQLFNEKMLLAVAEQHPWANENSVSMSLLKDCEILMLDDGHCLRNQALGYCFTAGARENAHFQATSLETLRNMVAANTGVTLMPQLAVLSEGNRSGVKYLPCDEPEPSRDITLVYRPGSPLRARYERVANTVSQSVKSILSS","1018975","From GenBank: (gi:1171941)This protein is required for the induction of a regulon of hydrogen peroxide inducible genes such as atalase, glutathione-reductase, etc. It belongs to the LysR family of transcriptional regulators.From GenBank: (gi:129310)OxyR is a hydrogen peroxide sensor. Activates the expression of a regulon of hydrogen peroxide-inducible genes such as katG, gor, ahpC, ahpF, oxyS (a regulatory RNA), dps, fur and grxA. OxyR expression is negatively autoregulated by binding to a 43 bp region upstream of its own coding sequence. OxyR is inactivated by reduction of its essential disulfide bond by the product of grxA, itself positively regulated by OxyR. Has also a positive regulatory effect on the production of surface proteins that control the colony morphology and auto-aggregation ability. Oxidized OxyR can be reduced and inactivated by glutaredoxin 1, the product of grxA, whose expression is regulated by OxyR itself. ","hydrogen peroxide-inducible activator","Cytoplasm","This sequence corresponds to gi:38488592 in Genbank.Its nearest neighbor in the NR database is gi:15603211 from Pasteurella multocida subsp. multocida str. Pm70.","
InterPro
IPR000847
Domain
Bacterial regulatory protein, LysR
PR00039\"[18-29]T\"[29-39]T\"[39-50]THTHLYSR
PF00126\"[3-62]THTH_1
PS50931\"[1-58]THTH_LYSR
InterPro
IPR005119
Domain
LysR, substrate-binding
PF03466\"[86-294]TLysR_substrate
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[87-201]TG3DSA:3.40.190.10
SSF46785\"[1-105]TSSF46785
SSF53850\"[87-294]TSSF53850


","No hits to the COGs database.","Significant hit ( 8.7e-16) to 1/1 blocks of the IPB000847 family, which is described as \"Bacterial regulatory protein, LysR family\". Interpro entry for IP:IPR000847. IPB000847 17-50 8.5e-16Significant hit ( 4.5e-06) to 1/2 blocks of the IPB001583 family, which is described as \"NodD transcription activator carboxyl terminal region\". Interpro entry for IP:IPR001583. IPB001583A 5-55 4.2e-06Significant hit ( 6.7e-05) to 1/1 blocks of the IPB000792 family, which is described as \"Bacterial regulatory protein, LuxR family\". Interpro entry for IP:IPR000792. IPB000792 1-47 6.3e-05","Residues 93 to 260 match (2e-07) PD:PD488793 which is described as TRANSCRIPTIONAL REGULATOR PROTEOME LYSR COMPLETE FAMILY ","","","","","","","","","","","Mon Apr 4 14:14:57 2005","Wed Jan 15 14:35:47 2003","Mon Apr 4 14:14:57 2005","Mon Apr 4 14:14:57 2005","Mon Apr 4 14:14:57 2005","Mon Apr 4 14:14:57 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA01513 is paralogously related to AA01999 (2e-17), AA00940 (1e-16), AA02539 (3e-12), AA00371 (1e-11), AA00985 (7e-09) and AA01794 (2e-05).","Mon Apr 4 14:14:57 2005","","","","","Residues 86 to 294 (E-value = 6.7e-50) place AA01513 in the LysR_substrate family which is described as LysR substrate binding domain (PF03466)","Mon Apr 4 14:14:57 2005","","","","Kikuchi Y, Ohara N, Sato K, Yoshimura M, Yukitake H, Sakai E, Shoji M, Naito M, Nakayama K.Novel stationary-phase-upregulated protein of Porphyromonas gingivalis influences production of superoxide dismutase, thiol peroxidase and thioredoxin.Microbiology. 2005 Mar;151(Pt 3):841-53.PMID: 15758230Lee C, Lee SM, Mukhopadhyay P, Kim SJ, Lee SC, Ahn WS, Yu MH, Storz G, Ryu SE.Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction path.Nat Struct Mol Biol. 2004 Dec;11(12):1179-85.PMID: 15543158Rocha ER, Smith CJ.Transcriptional regulation of the Bacteroides fragilis ferritin gene (ftnA) by redox stress.Microbiology. 2004 Jul;150(Pt 7):2125-34.PMID: 15256555Herren CD, Rocha ER, Smith CJ.Genetic analysis of an important oxidative stress locus in the anaerobe Bacteroides fragilis.Gene. 2003 Oct;316:167-75.PMID: 14563563Ueshima J, Shoji M, Ratnayake DB, Abe K, Yoshida S, Yamamoto K, Nakayama K.Purification, gene cloning, gene expression, and mutants of Dps from the obligate anaerobe Porphyromonas gingivalis.Infect Immun. 2003 Mar;71(3):1170-8.PMID: 12595429Rocha ER, Owens G, Smith CJ.The redox-sensitive transcriptional activator OxyR regulates the peroxide response regulon in the obligate anaerobe Bacteroides fragilis.J Bacteriol. 2000 Sep;182(18):5059-69.PMID: 10960088","","Mon Apr 4 14:14:57 2005","1","","","" "AA01514","1020030","1020755","726","ATGTCTAATATGGAAGGTAAAAAAGTTCCTCAAGTGACATTCCGTACGCGTCAAGGCGACCAATGGATTGATGTCACTACATCCGAATTATTTGATAATAAAACCGTTATCGTTTTCTCTTTACCGGGTGCATTCACCCCGACTTGTTCTTCTTCCCATTTACCACGTTATAACGAATTAGCGCCGGTATTCAAAAAATACGGTGTTGATGATATTCTTGTGATTTCCGTGAATGATACATTCGTGATGAATGCATGGAAAGAAGATGAAAAATCCGACAACATTACTTTCATTCCTGACGGTAATGGCGAGTTCACCGAAGGCATGGGCATGTTGGTAGGGAAAGAAGATTTAGGTTTTGGCAAACGTTCATGGCGTTATTCTATGCTGGTGAAAAATGGCGTAGTAGAAAAAATGTTTATCGAACCAAACGAACCGGGTGATCCGTTTAAAGTGTCCGATGCCGATACCATGTTGAAGTATCTTGCACCGCAACACCAAGTTCAAGAATCTATTACGATCTTCACTAAACCGGGTTGTCCATTCTGTGCAAAAGCAAAACAAATGTTACACGAAAAAGGCTTGAGCTTTGAGGAAATCGTGTTAGGTCACGATGCGACTATCGTGAGCGTACGTGCGGTTTCCGGTCGTGCGACTGTGCCGCAAGTATTCATCGGTGGTAAACACATCGGTGGTAGTGATGATTTAGAAGCGTATTTTGCGAAA","","","28178","MSNMEGKKVPQVTFRTRQGDQWIDVTTSELFDNKTVIVFSLPGAFTPTCSSSHLPRYNELAPVFKKYGVDDILVISVNDTFVMNAWKEDEKSDNITFIPDGNGEFTEGMGMLVGKEDLGFGKRSWRYSMLVKNGVVEKMFIEPNEPGDPFKVSDADTMLKYLAPQHQVQESITIFTKPGCPFCAKAKQMLHEKGLSFEEIVLGHDATIVSVRAVSGRATVPQVFIGGKHIGGSDDLEAYFAK","1020755","From GenBank (gi:1723174):The N-terminal section belongs to the peroxiredoxin 2 family. The c-terminal section belongs to the glutaredoxin family.","peroxiredoxin 2 family protein/glutaredoxin","Periplasm, Cytoplasm","","
InterPro
IPR002109
Domain
Glutaredoxin
PF00462\"[172-230]TGlutaredoxin
InterPro
IPR011767
Active_site
Glutaredoxin active site
PS00195\"[174-190]TGLUTAREDOXIN
InterPro
IPR011906
Domain
Glutaredoxin-like region
TIGR02190\"[163-241]TGlrX-dom: Glutaredoxin-family domain
InterPro
IPR012335
Domain
Thioredoxin fold
G3DSA:3.40.30.10\"[1-164]T\"[170-241]Tno description
InterPro
IPR013740
Domain
Redoxin
PF08534\"[4-162]TRedoxin
InterPro
IPR014025
Domain
Glutaredoxin subgroup
PR00160\"[172-190]T\"[213-226]T\"[227-240]TGLUTAREDOXIN
noIPR
unintegrated
unintegrated
PTHR10430\"[6-161]TPEROXIREDOXIN-5


","BeTs to 6 clades of COG0678COG name: PeroxiredoxinFunctional Class: OThe phylogenetic pattern of COG0678 is ------y------c--gh-n-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-21) to 2/2 blocks of the IPB002109 family, which is described as \"Glutaredoxin\". Interpro entry for IP:IPR002109. IPB002109A 172-186 5.5e-07 IPB002109B 216-235 3.9e-13Significant hit ( 1.6e-10) to 2/3 blocks of the IPB000866 family, which is described as \"AhpC/TSA family\". Interpro entry for IP:IPR000866. IPB000866A 37-52 8.5e-06 IPB000866B 72-86 0.0069","Residues 172 to 238 match (4e-07) PD:PD467627 which is described as GLUTAREDOXIN COMPLETE PROTEOME REDOX-ACTIVE CENTER ELECTRON SYNTHESIS GRX1 DEOXYRIBONUCLEOTIDE GRX ","","","","","","","","","","","Tue Jan 21 11:39:20 2003","Wed Jan 15 14:38:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01514 is paralogously related to AA01708 (3e-05).","","","","","","Residues 171 to 242 (E-value = 1.9e-15) place AA01514 in the Glutaredoxin family which is described as Glutaredoxin (PF00462)","","","","","Xia B, Vlamis-Gardikas A, Holmgren A, Wright PE, Dyson HJ. Solution structure of Escherichia coli glutaredoxin-2 showssimilarity to mammalian glutathione-S-transferases. J Mol Biol. 2001 Jul 20;310(4):907-18. PMID: 11453697 ","","Wed Jan 15 14:38:16 2003","1","","","" "AA01515","1021094","1020822","273","TTGGATAGGGTAAAACGGATTCAACAAATTCACAACAGTTATTTAGGAAATATTATGTCGATGCAACAAAATTTAGCACAGCGTATCACCGAATTGGAGATGAAAGCGACCTTTCAGGAAACTGTCATTGAAGAATTGAATCAGGCATTGGTTGAACAACAATTTATTCTGGATAAAATTCAGCTCCAGTTACGTTATCTGGCGAATAAAATACAAGATATGCAGCCTTCCAATATCGCCAGCCAAGCGGAAGAAACCCCACCACCGCATTAT","","","10650","LDRVKRIQQIHNSYLGNIMSMQQNLAQRITELEMKATFQETVIEELNQALVEQQFILDKIQLQLRYLANKIQDMQPSNIASQAEETPPPHY","1020822","","SlyX family protein","Cytoplasm","","
InterPro
IPR007236
Family
SlyX
PF04102\"[24-91]TSlyX
noIPR
unintegrated
unintegrated
PD336571\"[25-91]TQ75TM3_ACTAC_Q75TM3;


","BeTs to 6 clades of COG2900COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG2900 is --------------efghsn-j----Number of proteins in this genome belonging to this COG is","","Residues 24 to 91 match (3e-09) PD:PD446763 which is described as PROTEOME COMPLETE SLYX CYTOPLASMIC ","","","","","","","","","","","","Wed Jan 15 14:44:20 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01515 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 24 to 91 (E-value = 1.2e-39) place AA01515 in the SlyX family which is described as SlyX (PF04102)","","","","","","","","1","","","" "AA01517","1021129","1021851","723","ATGTTAAAAATGAAGAAAATTTCAGTGCCGGTGCTGATTTTAAGTGCGGTCGTTTCTAGCGGTGTTTTGGCGGAAAGCAAAACTGATGCAAAATTTACCGATGATTCCTCTTACGCGGTAGGCGTATTATTCGGTTCCGATTTACAAGGCTTAATTAACGCACAAAAAGGCATGATTGATTACAACAATGCGAAAGTGATTGCCGGGATTTCCGACGTGTTAAACGGCAAAGTAAAATTGGAAGGCAACAAAGAAATCGCCTCTACCTTGCAAGGCATTAATGCCAAGTTAAAAGCGGAAAATGAAAAACGTGTCGCCGTCATGGTGAAAAAAGCGGAAGAAGAAGGCAAAAAATTCACGGCAGAATTTGCTAAGAAAGATAGCGTGAAGAAAACTGCTTCCGGTTTGTTATATCGTGTGGAAAAAGAAGGGTCCGGTGATGCCATTAAAGCTGCCGATGTGGTTAAAGTTCACTATACCGGTAAATTGCCGGATGGTACCGTATTTGACAGCTCCCGTGAGCGTGGAACGCCTGCCGAGTTTCCATTAAATCAAGTGATTAAAGGTTGGACCGAAGGTCTGCAATTAGTTAAAAAAGGCGGACAAATTGAGTTGGTCATTCCGGCGGACTTGGGGTACGGTGAGGACGGTGCGGGCGATAAAATTCCACCGCATTCCACACTTTACTTTGATATTGAAGTATTGGACGTCACCCCGGCGAAA","","","25741","MLKMKKISVPVLILSAVVSSGVLAESKTDAKFTDDSSYAVGVLFGSDLQGLINAQKGMIDYNNAKVIAGISDVLNGKVKLEGNKEIASTLQGINAKLKAENEKRVAVMVKKAEEEGKKFTAEFAKKDSVKKTASGLLYRVEKEGSGDAIKAADVVKVHYTGKLPDGTVFDSSRERGTPAEFPLNQVIKGWTEGLQLVKKGGQIELVIPADLGYGEDGAGDKIPPHSTLYFDIEVLDVTPAK","1021851","From GenBank (gi:1169691):PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. ","peptidyl-prolyl cis-trans isomerase; macrophage infectivity protein","Periplasm","","
InterPro
IPR000774
Domain
Peptidyl-prolyl cis-trans isomerase, FKBP-type, N-terminal
PD001516\"[95-147]TQ8L3M3_ACTAC_Q8L3M3;
PF01346\"[13-140]TFKBP_N
InterPro
IPR001179
Domain
Peptidyl-prolyl cis-trans isomerase, FKBP-type
PTHR10516\"[139-241]TFK506 BINDING PROTEIN
PF00254\"[144-235]TFKBP_C
PS50059\"[152-238]TFKBP_PPIASE
noIPR
unintegrated
unintegrated
G3DSA:3.10.50.40\"[98-237]Tno description
PTHR10516:SF17\"[139-241]TFKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE
signalp\"[1-24]?signal-peptide


","No hits to the COGs database.","Significant hit ( 1.4e-54) to 4/4 blocks of the IPB000774 family, which is described as \"Domain amino terminal to FKBP-type peptidyl-prolyl isomerase\". Interpro entry for IP:IPR000774. IPB000774A 106-146 1.7e-09 IPB000774B 157-184 1.5e-16 IPB000774C 185-214 3.1e-18 IPB000774D 222-237 5.1e-06Significant hit ( 1.6e-13) to 1/1 blocks of the IPB001179 family, which is described as \"FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase)\". Interpro entry for IP:IPR001179. IPB001179 181-214 1.6e-13","Residues 134 to 173 match (2e-08) PD:PD407729 which is described as INFECTIVITY MACROPHAGE POTENTIATOR ISOMERASE ROTAMASE CIS-TRANS MEMBRANE PEPTIDYL-PROLYL OUTER MIP ","","","","","","","","","","","Tue Jan 21 12:17:40 2003","Tue Jan 28 14:34:41 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01517 is paralogously related to AA00282 (2e-38).","","","","","","Residues 144 to 235 (E-value = 9.6e-46) place AA01517 in the FKBP_C family which is described as FKBP-type peptidyl-prolyl cis-trans isomerase (PF00254)","","","","","Bumbaugh AC, McGraw EA, Page KL, Selander RK, Whittam TS.Sequence polymorphism of dotA and mip alleles mediating invasion and intracellular replication of Legionella pneumophila.Curr Microbiol. 2002 May;44(5):314-22.PMID: 11927981Pereira PJ, Vega MC, Gonzalez-Rey E, Fernandez-Carazo R, Macedo-Ribeiro S, Gomis-Ruth FX, Gonzalez A, Coll M.Trypanosoma cruzi macrophage infectivity potentiator has a rotamase core and a highly exposed alpha-helix.EMBO Rep. 2002 Jan;3(1):88-94.PMID: 11751578Ramm K, Pluckthun A.High enzymatic activity and chaperone function are mechanistically related features of the dimeric E. coli peptidyl-prolyl-isomerase FkpA.J Mol Biol. 2001 Jul 6;310(2):485-98.PMID: 11428902Horne SM, Kottom TJ, Nolan LK, Young KD.Decreased intracellular survival of an fkpA mutant of Salmonella typhimurium Copenhagen.Infect Immun. 1997 Feb;65(2):806-10.PMID: 900934","","Tue Jan 21 12:36:37 2003","1","","","" "AA01519","1021934","1022599","666","ATGTTAACGGATAAACGACCTTTTACTGACGAAGATCGCACCATTTTAAATTCTTATATTGCCGTGGTTGACGGCGTGAGTGCGCTTATCGGGCAACATTGCGAAATTGTTTTACATTCCTTTGAGGATTTAGAACATTCCGCCATTTATATCGCCAACGGGCATAACACCAACTGTCAGGTGGGTTCGCCCATAACGGATTTTGCTTTGCGTTCATTGCACGAGATGAAATCAGACAGCGTCAGTAAACCTTATTTTCTCCATGAGGAGAAAAACAGCGGTTTGATGAAGTCGGTAACCATCGCTATTCGCAACAGCACAAAGCGTATTATTGGTTTGCTTTGTATAAACATTAATTTAGACGTGCCGGTGTCGCAATTTCTGCAAAATTTTATCCCAATCCCCGATCATCAAGAAACCTCAGCGGTGAATTTTGCCAGCTCGGTGGAAGAACTGGTAGTGCAAACTGTGGGTAAAACCATTGAGGAGATTACTGCCGATCGCATGGTGGCGAATAATAACAAAAATCGCCAAATTGTCGTTTCTCTGTATGAAAAAGGCATTTTCGACATTAAAGACGCTATCAATTTAGTGGCGGAGCGTCTCAATATTTCTCGTCATACCGTGTATTTATATATTCGTCAAATTAAACAAGATCAGGATGAA","","","25027","MLTDKRPFTDEDRTILNSYIAVVDGVSALIGQHCEIVLHSFEDLEHSAIYIANGHNTNCQVGSPITDFALRSLHEMKSDSVSKPYFLHEEKNSGLMKSVTIAIRNSTKRIIGLLCININLDVPVSQFLQNFIPIPDHQETSAVNFASSVEELVVQTVGKTIEEITADRMVANNNKNRQIVVSLYEKGIFDIKDAINLVAERLNISRHTVYLYIRQIKQDQDE","1022599","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR013559
Domain
YheO-like
PF08348\"[15-130]TPAS_6


","No hits to the COGs database.","","Residues 151 to 222 match (1e-26) PD:PD336696 which is described as PROTEOME COMPLETE DNA-BINDING YHEO HI0575 REGULATOR VC0355 ORF PM1350 ","","","","","","","","","","","","Wed Jan 15 14:51:50 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01519 is paralogously related to AA02974 (1e-12).","","","","","","","","","","","","","","1","","","" "AA01519.1","1022606","1022980","375","ATGGATTATGTGTTGGTGGTGAAACAACCGGTTTACGGTAGTCAAGGCGCGTTTCTGGCGTACCAACTGGCACAAGTACTGGTGCAAAAGCATCATATCAGCCAAATCTTTTTTTATCAGGATGGCGTAACCAACGGCAACGCCTTGGTTTATCCCGCTAATGACGAATTTAATTTGGTCCAAGCCTGGCAGGCATTTTCCCGTCAATTTAACGTGCCGCTGCATTTGTGCGTTGCCGCCGCTCAACGGCGTGGCGTGGTGGATAGCTATTCTGCCGCCGATAAAAGTGCGGTTAACCTGGCGGACGTTTTTCAACTTGCCGGCTTGGGTGAATTCAGCCAAGCCTTATTACAAGCCGATCGGGTGATAACCCTA","6.20","-1.35","13762","MDYVLVVKQPVYGSQGAFLAYQLAQVLVQKHHISQIFFYQDGVTNGNALVYPANDEFNLVQAWQAFSRQFNVPLHLCVAAAQRRGVVDSYSAADKSAVNLADVFQLAGLGEFSQALLQADRVITL","","","conserved hypothetical protein","Periplasm","AA01519.1 has significant similarity to the Haemophilus ducreyi gene HD1902, a conserved hypothetical protein (2e-37).AA01519.1 has significant similarity to the Haemophilus influenzae Rd gene 16272519 (5e-44).","
InterPro
IPR003787
Family
DsrE-like protein
PF02635\"[1-125]TDrsE
noIPR
unintegrated
unintegrated
G3DSA:3.40.1260.10\"[3-125]Tno description


","BeTs to 6 clades of COG1553COG name: Uncharacterized ACR involved in intracellular sulfur reductionFunctional Class: PThe phylogenetic pattern of COG1553 is --m-----v-----efgh--------Number of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-46) to 4/5 blocks of the IPB003787 family, which is described as \"DsrE-like protein\". Interpro entry for IP:IPR003787. IPB003787A 1-22 1.6e-07 IPB003787C 37-59 3.9e-16 IPB003787D 71-84 1.5e-07 IPB003787E 94-125 7.9e-11","Residues 1 to 102 match (3e-32) PD:PD331614 which is described as COMPLETE PROTEOME YHEN SULFUR INTRACELLULAR BU532 ACR DSRE PA2605 TM0981 ","Fri Feb 27 11:01:59 2004","Sat Feb 28 17:06:08 2004","Sat Feb 28 17:06:08 2004","Sat Feb 28 17:06:08 2004","Fri Feb 27 11:01:59 2004","Fri Feb 27 11:01:59 2004","Fri Feb 27 11:01:59 2004","Fri Feb 27 11:01:59 2004","Fri Feb 27 11:01:59 2004","Fri Feb 27 11:01:59 2004","Fri Feb 27 11:01:59 2004","Fri Feb 27 11:01:59 2004","Fri Feb 27 11:01:59 2004","Fri Feb 27 11:01:59 2004","Fri Feb 27 11:01:59 2004","Fri Feb 27 11:01:59 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01519.1 has no significant similarity (blastp p-value < 1e-03) to any other gene in this genome.AA01519.1 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Fri Feb 27 11:01:59 2004","Sat Feb 28 17:06:08 2004","pdb1JX71JX7-A CRYSTAL STRUCTURE OF YCHN PROTEIN FROM E.COLI 42.6 3e-05","","","Residues 1 to 125 (E-value = 1.1e-42) place AA01519.1 in the DrsE family which is described as DsrE/DsrF-like family (PF02635)","Fri Feb 27 11:01:59 2004","","","","","","","1","Fri Feb 27 11:01:59 2004","","" "AA01520","1022947","1022567","381","TTGGCTGAATTCACCCAAGCCGGCAAGTTGAAAAACGTCCGCCAGGTTAACCGCACTTTTATCGGCGGCAGAATAGCTATCCACCACGCCACGCCGTTGAGCGGCGGCAACGCACAAATGCAGCGGCACGTTAAATTGACGGGAAAATGCCTGCCAGGCTTGGACCAAATTAAATTCGTCATTAGCGGGATAAACCAAGGCGTTGCCGTTGGTTACGCCATCCTGATAAAAAAAGATTTGGCTGATATGATGCTTTTGCACCAGTACTTGTGCCAGTTGGTACGCCAGAAACGCGCCTTGACTACCGTAAACCGGTTGTTTCACCACCAACACATAATCCATGACTTATTCATCCTGATCTTGTTTAATTTGACGAATATA","","","14284","LAEFTQAGKLKNVRQVNRTFIGGRIAIHHATPLSGGNAQMQRHVKLTGKCLPGLDQIKFVISGINQGVAVGYAILIKKDLADMMLLHQYLCQLVRQKRALTTVNRLFHHQHIIHDLFILILFNLTNI","1022567","","hypothetical protein","Cytoplasm, Inner membrane","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Jan 15 14:54:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01520 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01522","1022980","1023339","360","ATGAGTAAACTTGCCTTTATTTTCCGTCACGCGCCTTATGGTTCGGCAAATACACGCGAAGGATTAGACGCGCTGCTTGCCGCCACGGCATTTTGCGCCGAAGAGGACATTGCGGTGTTTTTCTTGGATGACGGCGTGTTGAATTTGCAAAAAAATCAACAGGCGGAATTGATTTTGCAAAAAGACACGGCAAGCGCATTAAAATTATTGAATTTATACGATATTGAACAGCGTTATGTGTGCGCCGATTCCCTGCAACAATTTCAACTTAAGCCGCTGGATTTATCCTTAAACTGTGAGGCACTGCCGCGTGAACAGCTGATGAGAATCCTGCAACAAAGTAAAAAAATTCTGACGTTC","","","13563","MSKLAFIFRHAPYGSANTREGLDALLAATAFCAEEDIAVFFLDDGVLNLQKNQQAELILQKDTASALKLLNLYDIEQRYVCADSLQQFQLKPLDLSLNCEALPREQLMRILQQSKKILTF","1023339","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003787
Family
DsrE-like protein
PF02635\"[2-120]TDrsE
noIPR
unintegrated
unintegrated
G3DSA:3.40.1260.10\"[1-120]Tno description


","No hits to the COGs database.","","Residues 3 to 120 match (7e-30) PD:PD031378 which is described as COMPLETE PROTEOME INTRACELLULAR OXIDATION YHEM SULFUR BU531 DSRF PA2606 VC0357 ","","","","","","","","","","","","Wed Jan 15 14:55:41 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01522 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 120 (E-value = 2.1e-32) place AA01522 in the DrsE family which is described as DsrE/DsrF-like family (PF02635)","","","","","","","","1","","","" "AA01523","1023345","1023629","285","ATGCTTTATACCTTTTCCCAAGCCCATTATTCCCAAGCCGAACTGGCACGTTATTTGCTGAATGCCACCGCGCGGGATGCGGTCGTGTTATGGCAGGACGGCGTGTTATTGGCGTTAAAACAGGCGGATTTATTGGCGCGCTGTAAAGCGCAATGTATGATGTTGCAGGAAGATATTTTGGCGAGAAATTTAACCGCACTTTTGCCGTCACCAACAAAAGTGCGGTTGATTTCTTTGACGGATTTTGTGGCAATCAGCGAACAATATTCTCCGCAAATTGCCCTT","","","10610","MLYTFSQAHYSQAELARYLLNATARDAVVLWQDGVLLALKQADLLARCKAQCMMLQEDILARNLTALLPSPTKVRLISLTDFVAISEQYSPQIAL","1023629","","conserved hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
PD065630\"[1-94]TY577_HAEIN_P44017;


","No hits to the COGs database.","","Residues 1 to 95 match (4e-25) PD:PD065630 which is described as PROTEOME COMPLETE HI0577 PM1353 ","","","","","","","","","","","","Wed Jan 15 14:57:11 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01523 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01524","1024404","1023640","765","ATGTTAGACGTTCGCAACATTCATAAAACATTTAACGGCAATCAGGTGCTGAAAGGGATCGATTTTCAGATTCAAAAAGGCGAAATGGTGGCGATGCTCGGCCCTTCCGGCTCCGGCAAAACCACGTTTTTACGCTGTTTAAATTTACTGGAACGCGCCGAACAGGGCACGTTGCACTTCACCGACGGCAGCCTTGCGTTGGATTTTGCCAAAAAAATCAGCAAAGCCGATGAATTAAAACTGCGTCGCCGCTCTTCCATGGTGTTTCAACAATACAATTTATTTCCCCATCGCACCGCACTTGAGAACGTGATGGAAGGCATGCTTGTGGTGCAAAAGAAAAGCAAGGAGGAAGCGGAACAGCGCGCCGTGGAATTGCTCACCAAAGTGGGCTTAAAAGACAAAATGCATTTGTATCCGTCCCAATTATCCGGCGGTCAGCAGCAACGTGTCGGTATTGCGCGCGCGTTGGCGGTGCAACCGGACATTATTCTGCTGGACGAACCCACCTCCGCGCTGGATCCGGAATTGGTCGGTGAAGTGCTACAAACTTTGAAATTACTGGCGCAGGAAGGCTGGACGATGATTATCGTCACCCATGAATTGCAGTTTGCCCGCGACGTGGCGGATCGGGTGATTTTAATGGCAGACGGCAATGTGGTGGAACAAAACGGCGCGCGTGAATTTTTTGAAAACCCGCAACAGGAACGCACCAAACAATTCTTGTTACAGGCAAAAATTCCGGTCTGCGTGGAGTATGAAATT","","","28732","MLDVRNIHKTFNGNQVLKGIDFQIQKGEMVAMLGPSGSGKTTFLRCLNLLERAEQGTLHFTDGSLALDFAKKISKADELKLRRRSSMVFQQYNLFPHRTALENVMEGMLVVQKKSKEEAEQRAVELLTKVGLKDKMHLYPSQLSGGQQQRVGIARALAVQPDIILLDEPTSALDPELVGEVLQTLKLLAQEGWTMIIVTHELQFARDVADRVILMADGNVVEQNGAREFFENPQQERTKQFLLQAKIPVCVEYEI","1023640","","amino acid ABC transporter, ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[142-185]TYA78_HAEIN_P45022;
PF00005\"[27-218]TABC_tran
PS50893\"[2-242]TABC_TRANSPORTER_2
PS00211\"[143-157]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[26-219]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[1-242]Tno description
PTHR19222\"[2-242]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF33\"[2-242]TGLUTAMATE / GLUTAMINE ABC TRANSPORTER


","BeTs to 14 clades of COG1126COG name: ABC-type polar amino acid transport system, ATPase componentFunctional Class: EThe phylogenetic pattern of COG1126 is a----z--vd-lbcefgh-nujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 5.3e-33) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 16-62 1.1e-11 IPB001140B 140-178 3.1e-18 IPB001140C 195-224 4.6Significant hit ( 1.8e-05) to 1/5 blocks of the IPB001324 family, which is described as \"Phosphoribulokinase family\". Interpro entry for IP:IPR001324. IPB001324A 26-47 1.9e-05","Residues 89 to 185 match (6e-07) PD:PD476601 which is described as ATP-BINDING PROTEOME COMPLETE BRANCHED-CHAIN AMINO ACID HIGH-AFFINITY LIVG / PERMEASE ","","","","","","","","","","","","Wed Jan 15 15:05:01 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01524 is paralogously related to AA00858 (4e-48), AA00415 (3e-43), AA02718 (4e-39), AA00700 (2e-36), AA02080 (5e-34), AA02440 (3e-32), AA02353 (9e-32), AA01051 (9e-32), AA01616 (2e-31), AA01422 (2e-31), AA01656 (2e-30), AA01645 (1e-28), AA02899 (3e-28), AA01867 (8e-27), AA02324 (2e-26), AA02898 (7e-24), AA02320 (1e-23), AA01684 (2e-23), AA01779 (4e-23), AA01947 (2e-22), AA01456 (3e-21), AA00933 (3e-21), AA02805 (5e-21), AA02786 (2e-20), AA01568 (3e-20), AA02609 (1e-19), AA02550 (1e-19), AA01393 (3e-19), AA00207 (4e-19), AA02152 (5e-19), AA02573 (4e-18), AA01510 (5e-18), AA02606 (5e-17), AA00799 (5e-17), AA00751 (5e-17), AA01961 (8e-17), AA01824 (7e-16), AA02140 (3e-15), AA01509 (1e-14), AA01569 (4e-14), AA01820 (5e-14), AA02484 (3e-13), AA01757 (2e-12), AA02331 (2e-12), AA02225 (4e-11), AA01555 (4e-11), AA02642 (8e-11), AA02146 (2e-10), AA00061 (4e-10), AA00934 (1e-09), AA02226 (2e-08), AA00591 (7e-07), AA01291 (1e-05) and A02145 (1e-05).","","","","","","Residues 27 to 218 (E-value = 1.4e-66) place AA01524 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Rodriguez,F. and Grandi,G. An operon encoding a novel ABC-type transport system in Bacillussubtilis. Microbiology 141(Pt 7): 1781-1784.1995. PubMed: 7551042. Blight MA, Holland IB. Structure and function of haemolysin B,P-glycoprotein and other members of a novel family of membrane translocators. Mol Microbiol. 4:873-880.1990. PubMed: 1977073.","","Wed Jan 15 15:08:45 2003","1","","","" "AA01525","1025139","1024417","723","GTGATGATATTACTCAATAATTTTCTTGCCTCCCTTCCCTTTATGAATGCAGAAAGAGCCAATGCAGCCATCAGCGCTTTTTGGCCTATGTTGGAAGCGGCAATTGATAAAACCATTCCGTTGGCAATTATCTCTTTCTTTGCCGGTTTAGTGATTGCGTTGGGCGTGGCGGTGATTCGTACCATGCCGAAAAGCGGCATCGGTTTACTTGTGTTGCAACTGCTTTGTCGCATCTATGTTTCCATCATTCGCGGTACGCCGATGTTGGTGCAGATTTTCATTATTTTCTACGGCTTGCCGGAAGTGGGCATTAAACTGGATCCCTTTCCGACGGCGATTATCGCCTTTTCCATTAATATCGGTGCCTACGCGTCGGAAACCATTCGTGCGGCGATTTTGTCCATTCCGAAAGGGCAATGGGAAGCCTCCTATTCTATTGGCATGAACTATTTCCAAACCTTCACCCGCACCATCATGCCGCAAGCTTTGCGCGTGTCCGTGCCGCCGCTATCCAACACCTTCATCAGCAACGTGAAAGACACGTCGTTAGCGTCTTTGGTGTTGGTGACCGAAATGTTCCGCGTGGCGCAAAATATCACAGCGGAAAACTATGAATTTATTATGATTTATAGCGAAGCGGCGTTAATTTACTGGTGCATTTGTCTGGTTTTGTCATTTGCTCAGGAACGCTTGGAAAAACGCCTGTCCCGTCACTTACAAGCC","","","26721","VMILLNNFLASLPFMNAERANAAISAFWPMLEAAIDKTIPLAIISFFAGLVIALGVAVIRTMPKSGIGLLVLQLLCRIYVSIIRGTPMLVQIFIIFYGLPEVGIKLDPFPTAIIAFSINIGAYASETIRAAILSIPKGQWEASYSIGMNYFQTFTRTIMPQALRVSVPPLSNTFISNVKDTSLASLVLVTEMFRVAQNITAENYEFIMIYSEAALIYWCICLVLSFAQERLEKRLSRHLQA","1024417","","amino acid ABC transporter, permease component","Inner membrane, Cytoplasm","","
InterPro
IPR000515
Family
Binding-protein-dependent transport systems inner membrane component
PF00528\"[31-237]TBPD_transp_1
PS50928\"[35-228]TABC_TM1
InterPro
IPR010065
Domain
Amino acid ABC transporter, permease protein, 3-TM region, His/Glu/Gln/Arg/opine
TIGR01726\"[27-130]THEQRo_perm_3TM: amino acid ABC transporter,
noIPR
unintegrated
unintegrated
signalp\"[1-17]?signal-peptide
tmhmm\"[39-59]?\"[80-100]?\"[207-227]?transmembrane_regions


","No hits to the COGs database.","","Residues 104 to 205 match (2e-12) PD:PD545085 which is described as PROTEOME COMPLETE PERMEASE SYSTEM TRANSMEMBRANE HISTIDINE HISQ TRANSPORTER INNER ABC ","","","","","","","","","","","","Wed Jan 15 15:07:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01525 is paralogously related to AA00855 (9e-28), AA00854 (1e-21) and AA00416 (2e-07).","","","","","","Residues 31 to 237 (E-value = 1.2e-24) place AA01525 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component (PF00528)","","","","","Rodriguez,F. and Grandi,G. An operon encoding a novel ABC-type transport system inBacillus subtilis. Microbiology 141(Pt 7): 1781-1784.1995. PubMed: 7551042. Turner,M.S., Timms,P., Hafner,L.M. and Giffard,P.M.Identification and characterization of a basic cellsurface-located protein from Lactobacillus fermentum BR11. J.Bacteriol. 179(10): 3310-3316.1997. PubMed: 9150229.","","Wed Jan 15 15:07:45 2003","1","","","" "AA01526","1025899","1025123","777","ATGAAAAAATCCATTTTAGCAAAAACATTACTGTTAACCGGTTTAGCCCTCGGCATCGCCACGCAGGCGGCAGCAGGCGAAATTTCCGATCGGGTAGAAAAAACCAAAACCTTATTAGTGGGTACGGAAGGCACTTACGCTCCGTTCACCTTCCACGATGACAGCGGCAAATTAACCGGTTTTGACGTGGAAGTTATCGAATCTGTGGCGCAACGTTTAGGCTTAAAAATTCAATTTAACGAAACCCAATGGGATTCCATGTACGCCGGGTTAAACGCCAAACGTTTCGATTTAATCGCCAACCAAACCAGCCCAAGTCTGGAACGCTTGAAAAAGTACCTTTACACCACACCTTATAACTACTCCACGGCGGTTATCGTGACCAAAGAAGGCGATGACAGCATTAAGGCATTTGAAGATTTAAAAGGCAAAAAAGCGGCGCAATCCTTAACCAGTAACTACGGCAAAATCGCCAAAGCCAACGGCGCGGAATTGATCGTGGTGGACGGTTTGGCGCAAGCCTTGAAACTCATCACACAAGATCGTGCACAAACCGTAGTAAACGACCAATTAGCAGTGTTGGATTACTTCAAAAAACAACCAAATGCCGGCTTAAAAATTGCAGTAAAACGCGATGAAAAAGTGCCTTCCGGTTTTGCCGTGTTAAAAGGTGAAGAACCGTTGGCGGAAAAAATCAATCAGGCGCTGGAAGAATTACGAAAAGACGGCACCTTGAAGCAAATCTCAATTAAATGGTTCGGTGATGATATTACTCAA","","","28363","MKKSILAKTLLLTGLALGIATQAAAGEISDRVEKTKTLLVGTEGTYAPFTFHDDSGKLTGFDVEVIESVAQRLGLKIQFNETQWDSMYAGLNAKRFDLIANQTSPSLERLKKYLYTTPYNYSTAVIVTKEGDDSIKAFEDLKGKKAAQSLTSNYGKIAKANGAELIVVDGLAQALKLITQDRAQTVVNDQLAVLDYFKKQPNAGLKIAVKRDEKVPSGFAVLKGEEPLAEKINQALEELRKDGTLKQISIKWFGDDITQ","1025123","","amino acid ABC transporter, periplasmic amino acid-binding protein","Periplasm","","
InterPro
IPR001638
Family
Bacterial extracellular solute-binding protein, family 3
PF00497\"[38-255]TSBP_bac_3
SM00062\"[37-256]TPBPb
PS01039\"[60-73]TSBP_BACTERIAL_3
InterPro
IPR008893
Domain
WGR
SM00773\"[121-186]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[33-159]Tno description
signalp\"[1-25]?signal-peptide


","BeTs to 17 clades of COG0834COG name: ABC-type amino acid transport system, periplasmic componentFunctional Class: EThe phylogenetic pattern of COG0834 is a----z--vdrlbcefgh-nujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 9.1e-13) to 2/2 blocks of the IPB001638 family, which is described as \"Bacterial extracellular solute-binding proteins, family 3\". Interpro entry for IP:IPR001638. IPB001638A 56-65 0.0017 IPB001638B 88-119 1.5e-07","Residues 101 to 255 match (3e-08) PD:PD578442 which is described as PROTEOME COMPLETE AMINO ABC ACID TRANSPORTER TRANSPORTER BINDING SUBSTRATE PROTEIN ","","","","","","","","","","","","Thu Jan 2 15:22:05 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01526 is paralogously related to AA00856 (2e-18).","","","","","","Residues 38 to 255 (E-value = 4.8e-87) place AA01526 in the SBP_bac_3 family which is described as Bacterial extracellular solute-binding proteins, family 3 (PF00497)","","","","","","","","1","","","" "AA01527","1025844","1025993","150","ATGCCGAGGGCTAAACCGGTTAACAGTAATGTTTTTGCTAAAATGGATTTTTTCATAATTCGTTCCTTTATTTTGCTTAATAAGAGGAAAAGTGCGGTGGATTATTACAGTAAATCTGCGCCGAATAAAATAATCATTTTCTCTATTGTA","","","5762","MPRAKPVNSNVFAKMDFFIIRSFILLNKRKSAVDYYSKSAPNKIIIFSIV","1025993","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 16:45:33 2004","Thu Feb 26 16:45:33 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01527 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 16:45:33 2004","","","","","","","","","","","","","1","","","" "AA01528","1027320","1026028","1293","ATGCTAGCGTTTTCACATCAGGAACATATTGAATCCTATTATTCCGTCACTCGTAACCAATATTTTGAGTTACCATCGCTAAGTCAAAAAGCATCTGCCGACGTTTGCGTGGTGGGCGCGGGCTTTTTCGGTTTATCCACTGCGTTGGAACTTGCCGAGCAAGGAAAAAGCGTGATCGTGCTGGAAGGCGCGCGGGTGGGCTTTGGCGCGTCGGGGCGTAGCGGCGGGCAGGCGATTAACGGGTTTGAAGACGGCATCGACGATTATATTGCGCAAGTGGGGCTGGACACCGCCCGCAAGCTCTGGCAGATGTCGCTGGAAGCCATTGAGATTATTGATGAGCGTATTGCCAAATACAGCATTCAATGCGATTGGAAGAAAGGCTATGCTACCTTGGCGTTAAATGAGCGCCGCATGGACGATCTCATCGCTATCGAAAAAGCCAGCCATGAGATTTTCGGCTACCAAAATATGCAACTGTGGGATAAAGCTAAGCTGGAACAACATCTGGGCAGCAAAATTTATTACGGCGCGTTGTACGACAGTAATTCCGGGCATTTACACCCGCTCAATTATTGTCTCGGTTTGGCGAAAGCCTGTTTGGAGCTGGGCGTGCGCATTTATGAACAGTCGCCGGTAGTGGATTTGCAGGAAAAAGCCACGAAAATTGAAGTGATCACCGATCAAAGTTCGGTCATCGCCAAAGATGTGGTATTAGCGACCAACGCCTATATTGACGCCTTGCCGAAAAGCATTCACCACGGCATTGCGCGCAAAATTCTGCCGGTGGAAAGTTTTATTATCGCCACCGAACCGTTGGATCAAGCCACCGCCGATTCAGTGATTAATAACGGGATGTCCGTGTGCGACAGCAATTATTTACTGGATTATTATCGTTTAAGCGCCGATAATCGCTTGTTGTTCGGCAGTGACTCCAGTTCGGAAAAAGATATGATTGAAGTCATGCGCGGCAATATGTTGCATGTTTTTCCACAGTTGGAACAGGTCAAAATTGACTACGGCTGGGGTGGACCTATCGACATGACTATCAATTCCAACCCGCATTTCGGCCGGATTTCGCCGCATATTTATTTCGCGCAAGGCTATTCCGGACACGGCGTCGCGCTCACCGGTTTGGCGGGGCGCATTGTAGCGGAAGCCATTTTAGGCAACGACGAGCGTTTGAAGATTTTCAGTAAATTAAAAGTGCCTTCCGTGTTCGGCGGCAAATTAGTGAAGAATCTGGCATTAAAAATCGGCGTTAATTATTATCGTTTCTTAGATAAATACCGT","","","50444","MLAFSHQEHIESYYSVTRNQYFELPSLSQKASADVCVVGAGFFGLSTALELAEQGKSVIVLEGARVGFGASGRSGGQAINGFEDGIDDYIAQVGLDTARKLWQMSLEAIEIIDERIAKYSIQCDWKKGYATLALNERRMDDLIAIEKASHEIFGYQNMQLWDKAKLEQHLGSKIYYGALYDSNSGHLHPLNYCLGLAKACLELGVRIYEQSPVVDLQEKATKIEVITDQSSVIAKDVVLATNAYIDALPKSIHHGIARKILPVESFIIATEPLDQATADSVINNGMSVCDSNYLLDYYRLSADNRLLFGSDSSSEKDMIEVMRGNMLHVFPQLEQVKIDYGWGGPIDMTINSNPHFGRISPHIYFAQGYSGHGVALTGLAGRIVAEAILGNDERLKIFSKLKVPSVFGGKLVKNLALKIGVNYYRFLDKYR","1026028","","probable oxidoreductase","Cytoplasm","","
InterPro
IPR006076
Family
FAD dependent oxidoreductase
PF01266\"[34-387]TDAO
noIPR
unintegrated
unintegrated
G3DSA:3.50.50.60\"[29-411]Tno description
PTHR13847\"[34-398]TFAD NAD BINDING OXIDOREDUCTASES
PTHR13847:SF13\"[34-398]TDAO, FAD DEPENDENT OXIDOREDUCTASE


","BeTs to 15 clades of COG0665COG name: Glycine/D-amino acid oxidases (deaminating)Functional Class: EThe phylogenetic pattern of COG0665 is ao-pkzyq--rlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is","Significant hit ( 3.4e-08) to 2/6 blocks of the IPB000447 family, which is described as \"FAD-dependent glycerol-3-phosphate dehydrogenase\". Interpro entry for IP:IPR000447. IPB000447A 33-85 5.3e-08 IPB000447C 226-248 2.4e+02Significant hit ( 5.6e-08) to 1/5 blocks of the IPB000171 family, which is described as \"Bacterial-type phytoene dehydrogenase\". Interpro entry for IP:IPR000171. IPB000171A 36-66 5.5e-08Significant hit ( 9.8e-07) to 1/6 blocks of the PR00420 family, which is described as \"Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature\". Prints database entry for PR:PR00420. PR00420A 34-56 9.9e-07","Residues 256 to 394 match (4e-07) PD:PD579483 which is described as COMPLETE OXIDOREDUCTASE PROTEOME PROBABLE 1.-.-.- PA3424 ","","","","","","","","","","","Wed Feb 19 15:19:17 2003","Thu Jan 2 15:26:25 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01528 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Jovanovic G, Model P.The RIB element in the goaG-pspF intergenic region of Escherichia coli.J Bacteriol. 1997 May;179(10):3095-102.PMID: 9150200 ","","Mon Nov 25 14:10:40 2002","1","","","" "AA01530","1028809","1027448","1362","ATGAAACGCGCGAACTTTCCTTTCCGATTGACCTTTCTCGCCGCCGGTTTAGCGTTGCTAACCGCTTGCCACTCCATCATTTATCAACCTGCCAAAACCATTGAACACATCTATCTGCAAAGCGGTTATCGTTTGGAAAACGTCATGCAGCAGGCGTTGCAAAAAGAGAATCTGGTGATTATGACCTTTTCCGGCGGCGGTTCGCGGGCGGCATCTTTGGGCTACGGCGTGTTGGAGCAATTCAAAAACGCCTCGGTGCGACCGACGGAAAAAGGCGATACTCTGTTGCAAAATATTGATGTGGTGTACGGCGTGTCGGGCGGTTCGGTGTTGGCGGCATATTTTGCACAGGAAGGGCAGGATGTGATCCCGAAATTTAACGAATCCTTTTTGAAAAAGGACTTTCAAAAGAAAGTAATTAACGAAGTGTTCTCCATGAGCAACGTGCCTCGGCTAACCTCCCCGCAATTCGGGCGGAGCGATTTGTTGCAGGAGCAGTTGAATCTTGCGTTATATAAAGGGAAAAAATTTGCCGACCTCGCCCAACATAGAAAAGGTCCTTTTGCGGTGATCAATGCCACGGACATGGCCATGGGGCAAAAAATCTCCTTTACCCAAGATTTCTTTGATTGGCTTTGTCTGGATTTAAACGATATTGAAATTGCCCGCGCGGTGGCGGCGTCCAGCGCCGTGCCGTTAATTTTTTCGCCGGTGACGCTCAATAATCATGGTGGATCTTGCCATATCCATAACAAAAAAGCGATGTTGACCGAACAGCCGGGTTATTGGCTCCTACTGAATAATTTTAATGCTATGGAAAAACGTTTTGCCCGCTATCAAAATAATCCCGAAAAAACCTATTTACATTTGGTAGACGGCGGTTTGACAGACAATTTGGGCTTGGCGAGTTTATTGGATATGTCGAATTTATTGAGTATGCATGAGTTATATACAGAATTGAAAAAGTCCAATTTGCGCAATATTGTGGTGGTGAATGTGAATGCGCAAAACGAAAATACCAGTCAGATAGATAAATCGGCGGATGTGCCGGGCGTGAAAGAAGTGGTTAATACAGTTATCAGTGTGCCTATTGATAAAGCGACGGAATCCACATTGCAATATTCACAAAAATTTGCCGACCAATGGAATGCTTACACCAAGCGCAAAAAAGACGTAAAAATTAAGATTTATTTTGTGAATTTGAGTTTGCGGAATCTGCCTGAAGGACAGTTAAAAACCGATGTGTTACATATCGGCACCTCTTTCTATTTGCCTGAATCTGATGTGGATAAACTGCGCGAAGCCGCTAAGATTTTGTTAGAGCAATCGAAAGAATATCAAGAAGCGCTGAAGGCATTGCAA","","","55690","MKRANFPFRLTFLAAGLALLTACHSIIYQPAKTIEHIYLQSGYRLENVMQQALQKENLVIMTFSGGGSRAASLGYGVLEQFKNASVRPTEKGDTLLQNIDVVYGVSGGSVLAAYFAQEGQDVIPKFNESFLKKDFQKKVINEVFSMSNVPRLTSPQFGRSDLLQEQLNLALYKGKKFADLAQHRKGPFAVINATDMAMGQKISFTQDFFDWLCLDLNDIEIARAVAASSAVPLIFSPVTLNNHGGSCHIHNKKAMLTEQPGYWLLLNNFNAMEKRFARYQNNPEKTYLHLVDGGLTDNLGLASLLDMSNLLSMHELYTELKKSNLRNIVVVNVNAQNENTSQIDKSADVPGVKEVVNTVISVPIDKATESTLQYSQKFADQWNAYTKRKKDVKIKIYFVNLSLRNLPEGQLKTDVLHIGTSFYLPESDVDKLREAAKILLEQSKEYQEALKALQ","1027448","","conserved hypothetical protein","Outer membrane, Periplasm, Inner membrane, Cytoplasm","","
InterPro
IPR002641
Family
Patatin
PF01734\"[61-305]TPatatin
noIPR
unintegrated
unintegrated
PS51257\"[1-23]TPROKAR_LIPOPROTEIN
signalp\"[1-25]?signal-peptide
tmhmm\"[10-28]?transmembrane_regions


","No hits to the COGs database.","","Residues 58 to 454 match (3e-29) PD:PD575346 which is described as PROTEOME COMPLETE BMEI0401 ","","","","","","","","","","","","Mon Nov 25 14:31:48 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01530 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 61 to 305 (E-value = 4.4e-10) place AA01530 in the Patatin family which is described as Patatin-like phospholipase (PF01734)","","","","","","","","1","","","" "AA01531","1028937","1028845","93","TTGTTCCTTAATTGCCACACCGATCACATTTTCAAAATAAAAACACCGAAAAAATCCACCGCACTTTCCCCTTTCTTGCTAAGCGTTGTAGAA","","","3510","LFLNCHTDHIFKIKTPKKSTALSPFLLSVVE","1028845","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 16:43:55 2004","Thu Feb 26 16:43:55 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01531 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 16:43:55 2004","","","","","","","","","","","","","1","","","" "AA01532","1028911","1029006","96","GTGATCGGTGTGGCAATTAAGGAACAAAATGTGAAGATACGCATGGTGTATTTACTCAAATTTACAAAGAAAATGGTGGTATACAGTATTGGTTTA","","","3665","VIGVAIKEQNVKIRMVYLLKFTKKMVVYSIGL","1029006","","hypothetical protein","Cytoplasm, Extracellular","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 16:42:01 2004","Thu Feb 26 16:42:01 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01532 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 16:42:01 2004","","","","","","","","","","","","","1","","","" "AA01533","1029071","1029511","441","GTGGGTTATTCATCTATTGCTATCGCCAACTCATTCATTGGCAAGGCTAATATTGGAGAAATTTCTAATTTAACTCCAATGAAACTACAAAAATTAATGTTTTATACGCAATCTTGGTATATTAAGCTTTATGGTAAGCCTTTGTTTGAGGGGGGGTTTGAAAGATGGCAATTTGGTCCGGTGCTACCGGAAATTTACCATGAGTTCAAACCATTTGGTTCTCGAATTATCTCTAGTTTTGGTACTGATATATGGGGGAAACAGCAAATTATTAAAGAAAGTGATAAAGATACTCTGTTGTTTTTAGATAAGATCATTGAAATATACGGTAAATTTGATGGACCTCAGTTATCTTGGATGACTCATCAACCTGAAACGGCATGGTCTATGGGACGTTTAGGAAGTGTTATTACTCAAGATGAGCTTTTTAATGGAAAAGTA","","","16808","VGYSSIAIANSFIGKANIGEISNLTPMKLQKLMFYTQSWYIKLYGKPLFEGGFERWQFGPVLPEIYHEFKPFGSRIISSFGTDIWGKQQIIKESDKDTLLFLDKIIEIYGKFDGPQLSWMTHQPETAWSMGRLGSVITQDELFNGKV","1029511","","conserved hypothetical protein","Cytoplasm","","No hits reported.","BeTs to 3 clades of COG3600COG name: Uncharacterized phage-associated proteinFunctional Class: SThe phylogenetic pattern of COG3600 is -----------l------s--j---wNumber of proteins in this genome belonging to this COG is","","Residues 8 to 128 match (3e-08) PD:PD092804 which is described as PROTEOME COMPLETE CC3515 PS3 ORF21 PROPHAGE BMEII0458 UU033 GEPA ","","","","","","","","","","","","Thu Jan 2 15:30:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01533 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01534","1029517","1030638","1122","ATGTCCAGTATTGAGAATATAAAAACAGAATTTGAATTTAATTATGTTCAAAAAGGTGAGGCTGGTATCGAAAGTCCACCTTTTTTATTGCCTTCAAAATCATCAGTAGCCAAGGCTGGCGATTATTTAAGAAAAATATCTCAAAGCAATAATGAAGAAATAGATCAAAAAAAATTAATACGCTTTATTACTATACTAGAAACATATAGAAGTTACCACTCATATAATATTTCAGTTTTTGAAAGACTACTGAATAAGAAAATTCAGAGATTAAATCTATATGATAAATGTATCATATCTTCGCGCTCAAAAAGGTTTTCTTCAATTATACAAAAATTAAAAAGATTTCCTGATATGAAATTATCTCGAATGGGAGATTTAGCTGGAGTTAGAATAATTTTAAAGAATATGGATGCATTGAGAGTGTTTGTTAGTGATAATTCAAATACAATCTGTGAACTTAGGAAGGAAAATTTCTTCTGTTATGTAAATAAAACGCATGATTATATAGAAACTCCTAAAAAAGATGGGTATAGAAGTGTACATCAAGTATTTGAAGATAAAAATTATAAACTAAAATTAGAGTTGCAAATTAGAACTCAGTTACAACATGAGTGGGCAACCATAGTTGAAATATTGGGCTCTTTGATGAAAACATCATTTAAAGTTGGACAAGGTGATGAGGGAATAAGATTATTTTTGAAATTATGTAGTGCATTATTTTCTTATCAGGAAGATACTCCAATAATAGAAGAGTTTAATAATTTTTCTGTTGTGCAAATATGTGAAAAAATAAAAGAGTTAGATTCAAAATTAGGTGTAATAGATACACTAAAAAGCGTTAGTGCTATTGATGTAGAACATAACCCTAGCGCAGCATATTATTTGTTAATATTAGATTTAAAAAAACATAATACTGAAATTAAAACTTTTAATGAGAATGAGAAATTTAAAGCTGAGCAGGTATACTCCCATTATGAACAAGATTCTTTTAAGAATGAATTTCTTGATGTGGTGCTAGTTTCGGTTGATGATGTAAACCAATTAAAAGATGCGTACCCTAATTATTTCTTAGATACAACTAGCTTCATAAATAGAATGGAAAACTTACTAATGAATAGA","","","43684","MSSIENIKTEFEFNYVQKGEAGIESPPFLLPSKSSVAKAGDYLRKISQSNNEEIDQKKLIRFITILETYRSYHSYNISVFERLLNKKIQRLNLYDKCIISSRSKRFSSIIQKLKRFPDMKLSRMGDLAGVRIILKNMDALRVFVSDNSNTICELRKENFFCYVNKTHDYIETPKKDGYRSVHQVFEDKNYKLKLELQIRTQLQHEWATIVEILGSLMKTSFKVGQGDEGIRLFLKLCSALFSYQEDTPIIEEFNNFSVVQICEKIKELDSKLGVIDTLKSVSAIDVEHNPSAAYYLLILDLKKHNTEIKTFNENEKFKAEQVYSHYEQDSFKNEFLDVVLVSVDDVNQLKDAYPNYFLDTTSFINRMENLLMNR","1030638","","conserved hypothetical protein (possible GTP pyrophosphokinase)","Cytoplasm","","
InterPro
IPR007685
Domain
RelA/SpoT
PF04607\"[101-208]TRelA_SpoT
noIPR
unintegrated
unintegrated
PTHR21262\"[80-207]TGUANOSINE-3',5'-BIS(DIPHOSPHATE) 3'-PYROPHOSPHOHYDROLASE


","No hits to the COGs database.","","Residues 65 to 213 match (7e-11) PD:PD124962 which is described as PROTEOME COMPLETE RV1366 ","","","","","","","","","","","","Fri Jan 31 15:32:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01534 is paralogously related to AA01072 (2e-07).","","","","","","Residues 101 to 215 (E-value = 2.5e-19) place AA01534 in the RelA_SpoT family which is described as Region found in RelA / SpoT proteins (PF04607)","","","","","","","","1","","","" "AA01537","1031667","1030756","912","ATGAGCGAACAAAATTTAGTAAACAGCCTCGAAAAAATGTTAAGCGAACAGCGCAATCCGAACACCATGCACATTGATTCCCTGTCGACGTTGGAGGTCGTTACCTTATTAAATAAGGAAGACAAATTGGTGGCGTTGGCGGTGGAAAAAAATCTGCCGCAAATTGCACAAGCGGTAGAACGCATTGAGGAGGCATTTCAGGCGGGCGGACGCTTGGTTTACCTGGGTGCCGGCACCAGCGGTCGCCTTGGCGTATTAGATGCCTCCGAATGCCCGCCCACCTTCGGCGTGCCATCCGGCATGGTGGTGGGGTTAATTGCCGGCGGGGACACGGCGTTGCGTAACGCGGTGGAAGGCGCGGAAGATAATGCCGCCGCAGGCGAACAGGATTTACGCCACATCAATTTCAGCGCTAAAGACGTACTGGTGGGCATCGCCGCCAGCGGACGTACGCCTTATGTGATCGGCGGTTTGAACTACGCCAAACAGCTCGGTGCAACCACAGTGTCCTTGGTCAGCAACCCGAACGCTGTTATGAGCGATATCGCGGACATCGCCATCACCACCGCCGTCGGCCCTGAAGCTCTCACCGGCTCCAGCCGCTTAAAATCCGGCACAGCGCAAAAAATGGTGCTGAATATGCTCACCGCCGCCGCCATGATCCGCCTCGGCAAATGCTACCAAAACCTGATGGTGGACGTGCAAGCCACTAACCAAAAACTCAAAGCCCGCGCCATCCGCATTGTCATGCAAGCCACCGACTGCGATGCCACCACCGCCGAACAAACCCTACACACCACCAACGGCAATGCCAAACTCGCGATCATGATGTTGTTAAGCGGATTGGATAAAACGCAGGCGGAAGCCGTGTTAGTGCAACATAAGGGAAGATTACAGAACGCCTTGGTGGGG","","","31910","MSEQNLVNSLEKMLSEQRNPNTMHIDSLSTLEVVTLLNKEDKLVALAVEKNLPQIAQAVERIEEAFQAGGRLVYLGAGTSGRLGVLDASECPPTFGVPSGMVVGLIAGGDTALRNAVEGAEDNAAAGEQDLRHINFSAKDVLVGIAASGRTPYVIGGLNYAKQLGATTVSLVSNPNAVMSDIADIAITTAVGPEALTGSSRLKSGTAQKMVLNMLTAAAMIRLGKCYQNLMVDVQATNQKLKARAIRIVMQATDCDATTAEQTLHTTNGNAKLAIMMLLSGLDKTQAEAVLVQHKGRLQNALVG","1030756","","possible glucokinase regulatory protein","Cytoplasm","","
InterPro
IPR001347
Domain
Sugar isomerase (SIS)
PF01380\"[123-221]TSIS
InterPro
IPR005486
Family
Glucokinase regulatory protein
PS01272\"[192-209]TGCKR
InterPro
IPR005488
Family
Glucokinase regulatory-like protein
TIGR00274\"[13-303]TTIGR00274: glucokinase regulator homolog
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.10490\"[10-257]Tno description
PTHR10937\"[126-215]TGLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE


","No hits to the COGs database.","Significant hit ( 2.6e-71) to 3/3 blocks of the IPB001741 family, which is described as \"Glucokinase regulatory protein\". Interpro entry for IP:IPR001741. IPB001741A 14-35 1.1e-07 IPB001741B 71-109 8.4e-31 IPB001741C 209-249 2.2e-30Significant hit ( 6.3e-08) to 1/2 blocks of the IPB001347 family, which is described as \"SIS domain\". Interpro entry for IP:IPR001347. IPB001347B 140-165 6.3e-08Significant hit ( 3.1e-05) to 1/3 blocks of the IPB000281 family, which is described as \"Helix-turn-helix domain, RpiR family\". Interpro entry for IP:IPR000281. IPB000281B 125-172 2.9e-05","Residues 14 to 209 match (1e-11) PD:PD340219 which is described as GLUCOKINASE REGULATORY REGULATOR SIMILAR KINASE POLYMORPHISM ","","","","","","","","","","","","Thu Jan 2 15:44:08 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01537 is paralogously related to AA02468 (3e-04).","","","","","","","","","","","","","","1","","","" "AA01538","1032794","1031667","1128","ATGCAACAGGAATATTATCTCGGCATCATGTCCGGCACCAGTTTGGACGGTGTGGACGTTGCCCTGATGGCATTCACCGAACAACCGCAATTCATTGCCGGGCAATTCACGCCAATGCCGACGCATTTACGACAAGATTTATTGCAATTAGTTTCTCACGGCACCACCACATTACAGCAACTGGGCGAGCTAGATCAACGTTTAGCCCTGTTATACGCCGACGCCGTCAACCGCTTCCTCACCACCCACAACCTATCTCCGCAACATATCCGCGCCATCGGCTGCCACGGGCAAACCGTGTGGCACGCGCCGCAGGGGGATTTTCCGTTTACCCTGCAAATTGGCGATATGCATCTGCTTGCAGCGCGCACCGGCATTGACGTGGTGGGCGATTTTCGGCGTAAGGATATGGCATTCGGCGGACAAGGGGCGCCGCTGGTGCCTGCTTTTCATCAAGCGCTGTTTTATGATGAACGTTGGGCGACGGTGGTGTTGAACATCGGCGGGATCAGCAATATTTCCGTGCTGTTTCCCCATCAGCCGATTATCGGCTACGGCACCGGCGCGGGCAACGCCTTAATGGACGGTTGGATTGAGCGCCATCTGGGCAAATCCTACGACGCCGACGGGCAATGGGCGCGCAGCGGAAAAGTGCGGTCGGCATTATTGGGGGAAATGCTGAAAGAGCCTTATTTCCAACTACCGCCGCCGAAAAGCACCGGGCGCGAATTGTTCAACCTTGCGTGGCTTGAAAAAACGCTGGCAAAAACGACCGCACTTTTAGGCGAGATACCGCCGCAAGACGTGCAAGCCACCTTATTGGAATTCACCGCGCAAAGCATTGCCCTTGCTTTAAATCAGCTTGAAACCGAACTGCCGCGCCGTTTGTTGGTGTGTGGCGGCGGCGCGAAAAACGGCTTGCTGATGGAGCGCCTGCAAGCGCTGCTGCCAAATTGGCAATGCCGTCCGACCAACGACGTGGGCTTAGATGTGGATTATGTGGAAGCCGCCGCCTTCGCTTGGCTTTCCTATCGTCGCATTCACAACCTACCATCCAATTTACCCAGCGTGACCGGCGCCAAAAGTGCGGTCAGTTTGGGCGCCATTTTTCCTGCGGAGAAGATCTCA","","","43551","MQQEYYLGIMSGTSLDGVDVALMAFTEQPQFIAGQFTPMPTHLRQDLLQLVSHGTTTLQQLGELDQRLALLYADAVNRFLTTHNLSPQHIRAIGCHGQTVWHAPQGDFPFTLQIGDMHLLAARTGIDVVGDFRRKDMAFGGQGAPLVPAFHQALFYDERWATVVLNIGGISNISVLFPHQPIIGYGTGAGNALMDGWIERHLGKSYDADGQWARSGKVRSALLGEMLKEPYFQLPPPKSTGRELFNLAWLEKTLAKTTALLGEIPPQDVQATLLEFTAQSIALALNQLETELPRRLLVCGGGAKNGLLMERLQALLPNWQCRPTNDVGLDVDYVEAAAFAWLSYRRIHNLPSNLPSVTGAKSAVSLGAIFPAEKIS","1031667","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR005338
Family
Protein of unknown function UPF0075
PF03702\"[4-372]TUPF0075


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Jan 2 15:46:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01538 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 372 (E-value = 1e-236) place AA01538 in the UPF0075 family which is described as Uncharacterised protein family (UPF0075) (PF03702)","","","","","","","","1","","","" "AA01539","1032880","1034247","1368","ATGACAACTCAAGCACTCAGCGTAGTAATTCTGGCCGCCGGCAAAGGCACCCGTATGTATTCCGATTTGCCGAAAGTGTTGCACCCTATTGCGGGCAAACCCATGGTGAAACACGTCATCGACACCGCTAAACAACTCGGCGCGCGCAATATTCATTTGGTTTACGGACACGGCGGCGATTTAATACAACAACGCTTGGCGGGCGAACCGGTGAACTGGGTGTTGCAAACGGAACAACTCGGCACAGGTCATGCCATGCAACAGGCGGCGCCGTTTTTTGCCGATGACGAAAACATTTTAATGCTCTATGGCGATGCGCCTTTGATTACTAAAGACACCTTGGAAAAACTCATTGCCGCCAAACCGGACAACGGCATTGCCTTGTTAACGGTCGTGTTGGACAACCCGACGGGTTACGGTCGCATTTTGCGCGAAAATGGCAATGTCGTTGGCATTGTGGAACAAAAAGATGCCAACGTGGAACAGCTTAACATTCAGGAAGTGAACACCGGCGTGATGGTGTCCGACGGCGCATCCTTCAAAAAATGGCTGGCGCAGCTGGATAACAACAACGCGCAAGGCGAATACTACATGACCGATGTTATCGCCTTGGCAAATCGCGACGGTTGCCAAGTGGCGGCGGTGCAAGCGGTGGATTTAATGGAAGTGGAAGGCGCGAATAATCGCCTGCAACTGACCGCACTTGAGCAATATTTCCAACAAAAACAGGCACGCGAATTATTGCTGGCGGGCGTGATGTTATTGGATCCGAACAGCTTCAAACTGCGCGGCGAATTGAGCCACGGCAAAGACGTGGAAATCGACATGAACGTGATTTTAAACGGCAAAGTGCGGTTAGGAAATCGGGTGAAAATCGGTGCAGGTTGTGTGTTGACTAACTGCGACATCGGCGATGACGTGGAAATCAAACCGTATTCCGTGCTGGAAGATGCCTCCGTAGGCGCCAATGCCGCCATCGGACCGTTCTCCCGCTTACGTCCGGGCGCCGACTTGGCGGAAAACACCCACGTGGGCAATTTCGTGGAAATCAAAAAAGCGTACATCGGCAAAGGCTCCAAAGTGAACCACTTAACCTATGTGGGCGACGCGGAAATCGGCAAAGATTGTAACATAGGCGCAGGCGTGATCACCTGTAACTACGACGGCGCCAACAAATTCAAAACCACTATCGGTGACAACGTGTTTGTCGGCTCCGACAGCCAACTCGTCGCCCCGGTCACCATCGAAAGCGGCGCTACCATCGGCGCAGGCTCCACCATCCGCTACGACGTCAAACGCGACGAACTGGTCACCACCCGCGTTCCGCAAAAACACGTCCAAGGCTGGGAAAGACCGACGAAGAAAAAA","","","49170","MTTQALSVVILAAGKGTRMYSDLPKVLHPIAGKPMVKHVIDTAKQLGARNIHLVYGHGGDLIQQRLAGEPVNWVLQTEQLGTGHAMQQAAPFFADDENILMLYGDAPLITKDTLEKLIAAKPDNGIALLTVVLDNPTGYGRILRENGNVVGIVEQKDANVEQLNIQEVNTGVMVSDGASFKKWLAQLDNNNAQGEYYMTDVIALANRDGCQVAAVQAVDLMEVEGANNRLQLTALEQYFQQKQARELLLAGVMLLDPNSFKLRGELSHGKDVEIDMNVILNGKVRLGNRVKIGAGCVLTNCDIGDDVEIKPYSVLEDASVGANAAIGPFSRLRPGADLAENTHVGNFVEIKKAYIGKGSKVNHLTYVGDAEIGKDCNIGAGVITCNYDGANKFKTTIGDNVFVGSDSQLVAPVTIESGATIGAGSTIRYDVKRDELVTTRVPQKHVQGWERPTKKK","1034247","[FUNCTION] Bifunctional enzyme responsible for the acetylation of glc-N-1-P to give glcNAC-1-PP and the synthesis of UDP-glcNAC (by similarity). [CATALYTIC ACTIVITY] Acetyl-CoA + D-glucosamine 1-phosphate =CoA + N-acetyl-D-glucosamine 1-phosphate. [CATALYTIC ACTIVITY] UTP + N-acetyl-alpha-D-glucosamine1-phosphate = diphosphate + UPD-N-acetyl-D-glucosamine. [PATHWAY] Peptidoglycan and lipopolysaccharide biosynthesis. [SIMILARITY] In the c-terminal section; belongs to the CysE/LacA/LpxA/NodL family of acetyltransferases. Composed of multiple repeats of [liv]-G-X(4). ","UDP-N-acetylglucosamine pyrophosphorylase (bifunctional enzyme)","Cytoplasm","","
InterPro
IPR001228
Domain
4-diphosphocytidyl-2C-methyl-D-erythritol synthase
PF01128\"[6-38]TIspD
InterPro
IPR001451
Repeat
Bacterial transferase hexapeptide repeat
PF00132\"[283-300]T\"[303-317]T\"[317-334]T\"[335-352]T\"[352-369]T\"[369-386]T\"[394-411]T\"[412-429]THexapep
PS00101\"[403-431]THEXAPEP_TRANSFERASES
InterPro
IPR005882
Family
UDP-N-acetylglucosamine pyrophosphorylase
TIGR01173\"[6-455]TglmU: UDP-N-acetylglucosamine pyrophosphory
noIPR
unintegrated
unintegrated
G3DSA:2.160.10.10\"[228-456]Tno description
G3DSA:3.90.550.10\"[1-227]Tno description
PTHR22572\"[14-309]T\"[327-451]TSUGAR-1-PHOSPHATE GUANYL TRANSFERASE
PTHR22572:SF17\"[14-309]T\"[327-451]TUDP-N-ACETYLGLUCOSAMINE PYROPHOSPHORYLASE-RELATED


","BeTs to 15 clades of COG1207COG name: N-acetylglucosamine-1-phosphate uridyltransferase (contains nucleotidyltransferase and I-patch acetyltransferase domains)Functional Class: MThe phylogenetic pattern of COG1207 is -------qvdrlbcefghsnujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 9.9e-12) to 1/1 blocks of the IPB001451 family, which is described as \"Bacterial transferase hexapeptide repeat\". Interpro entry for IP:IPR001451. IPB001451 397-432 9.7e-12 IPB001451 268-303 5.6e-08 IPB001451 314-349 0.0052 IPB001451 320-355 0.01 IPB001451 274-309 0.17Significant hit ( 1e-11) to 1/6 blocks of the IPB001228 family, which is described as \"4-diphosphocytidyl-2C-methyl-D-erythritol synthase\". Interpro entry for IP:IPR001228. IPB001228A 8-40 1e-11","Residues 305 to 442 match (8e-07) PD:PD016268 which is described as N-SUCCINYLTRANSFERASE 2345-TETRAHYDROPYRIDINE-2-CARBOXYLATE TRANSFERASE PROTEOME COMPLETE ACYLTRANSFERASE TETRAHYDRODIPICOLINATE SUCCINYLTRANSFERASE SUCCINYLASE LYSINE ","","","","","","","","","","","Thu Jan 2 15:53:18 2003","Thu Jan 2 15:53:18 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01539 is paralogously related to AA02000 (4e-09), AA01956 (9e-07), AA00610 (1e-06), AA01417 (5e-05) and AA00612 (2e-04).","","","","","","Residues 7 to 230 (E-value = 4.6e-09) place AA01539 in the NTP_transferase family which is described as Nucleotidyl transferase (PF00483)","","","","","Olsen LR, Roderick SL. Structure of the Escherichia coli GlmUpyrophosphorylase and acetyltransferase active sites. Biochemistry. 2001 Feb 20;40(7):1913-21. PMID: 11329257 Olsen LR, Tian Y, Roderick SL. Purification, crystallization and preliminary X-raydata for Escherichia coli GlmU: a bifunctionalacetyltransferase/uridyltransferase. Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt2):296-7. PMID: 11173485 Sulzenbacher G, Gal L, Peneff C, Fassy F, Bourne Y. Crystal structure of Streptococcus pneumoniaeN-acetylglucosamine-1-phosphate uridyltransferase boundto acetyl-coenzyme A reveals a novel active site architecture. J Biol Chem. 2001 Apr 13;276(15):11844-51. PMID: 11118459 Kostrewa D, D'Arcy A, Takacs B, Kamber M. Crystal structures of Streptococcus pneumoniaeN-acetylglucosamine-1-phosphate uridyltransferase,GlmU, in apo form at 2.33 A resolution and in complex with UDP-N-acetylglucosamine and Mg(2+) at 1.96 Aresolution. J Mol Biol. 2001 Jan 12;305(2):279-89. PMID: 11124906 Pompeo F, Bourne Y, van Heijenoort J, Fassy F,Mengin-Lecreulx D. Dissection of the bifunctional Escherichia coliN-acetylglucosamine-1-phosphate uridyltransferaseenzyme into autonomously functional domains andevidence that trimerization is absolutely required forglucosamine-1-phosphate acetyltransferase activity andcell growth. J Biol Chem. 2001 Feb 9;276(6):3833-9. PMID: 11084021","","Thu Jan 2 15:53:18 2003","1","","","" "AA01543","1034315","1034410","96","ATGCCGGACATAAAAAGTGCGGTGAAAATTCACAGCGTTTTTCAACCGCACTTTGGCTCGGGATGCGACCCAATTTGCATTACAGAATTAATCTTG","","","3479","MPDIKSAVKIHSVFQPHFGSGCDPICITELIL","1034410","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
PS51257\"[1-22]TPROKAR_LIPOPROTEIN


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 16:40:14 2004","Thu Feb 26 16:40:14 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01543 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 16:40:14 2004","","","","","","","","","","","","","1","","","" "AA01544","1035493","1034405","1089","ATGAATAAAACCTTAAAAATTTCATTGTTTGCCATGATTTCCGCGTTAGCTTTTAATACCATGGCAAATACACAACCGTTAGCCGTGTTGGAACCGCAGGTAAACTATCAACAGTTACTCACCCAACGGCAGGTGGTGGATGATTTAATCGCGCAGGCGGTGAAAATCCAAAATTCACCGGCGCGGGTGTCCAATGCGGGCTTTACCGCAAAATTGCCAAGCAACATGGAACGCATTGCCGCGATTTTGTTGGAAGCCTATGAATTGGAACCTTACCGCGTTGATTTTCTGTTCGGCGCAGCAAATGCCAACATTTACAACGGCAATACGGACAAAGCCATCGAGCTTTACCAAAAAGTGCTCACGGTGGCGCCTGATGATGTGAAAGCACATATTTATTTAACCGCGTGGAATCGTTTTAAACAAAACCAAGGGGAAACCGACAAATACTTCACCCGCTTAAAAGCGCTGGCACCGCAAAAAGCAGCGGAACTGGAGCAGGTCTTCAAGATTATTGATAACGCCGCAAGCCAACCGATTAGCGATAAATTGGCGAATAAATTGCCGGCGGATTCCGCCATTATTACCTTGGGTTATGCGTTAAATCCGGACGGCAGTATGCACGACATTTTGATTCAGCGTTTGGAAAAAACCTTGGAAATCGCCAAACAAAATCCTGATGCATTGATTATTGTCACCGGCGGCATGCCGCAAAATAATCGTACGGAAGGGGCATTAATGAAACAATGGCTGATTAACAAAGGCATCGATGCCAAACGCATTTATGCCGACAATTACGCCCGTTCAACGGTGGAAAATGCGTTATTTTCCCGTTACGCCTTGGCGAAACACCATATCAAACACGCCTCCCTCATCAGCTCCGGTAGCCATGTGCGGCGCGGTCAGGCGTTGTTTGAAATCGCCGCCTTGGAATCCGGTCCGCAAAACATCAAAATCGAAACGGTGGCGGCGCTAGACAAACCGTTAGACGAATTACAAAAAGTGAGTGAAAAAGATTTATTGGGAATCTATCGCGACAGCCTGAAAACCATGGGCTTGCCAATGTTTAATAGCGGAGCACTACAAGAT","","","40181","MNKTLKISLFAMISALAFNTMANTQPLAVLEPQVNYQQLLTQRQVVDDLIAQAVKIQNSPARVSNAGFTAKLPSNMERIAAILLEAYELEPYRVDFLFGAANANIYNGNTDKAIELYQKVLTVAPDDVKAHIYLTAWNRFKQNQGETDKYFTRLKALAPQKAAELEQVFKIIDNAASQPISDKLANKLPADSAIITLGYALNPDGSMHDILIQRLEKTLEIAKQNPDALIIVTGGMPQNNRTEGALMKQWLINKGIDAKRIYADNYARSTVENALFSRYALAKHHIKHASLISSGSHVRRGQALFEIAALESGPQNIKIETVAALDKPLDELQKVSEKDLLGIYRDSLKTMGLPMFNSGALQD","1034405","","conserved hypothetical protein","Periplasm","","
InterPro
IPR003848
Domain
Protein of unknown function DUF218
PF02698\"[190-335]TDUF218
InterPro
IPR011990
Domain
Tetratricopeptide-like helical
G3DSA:1.25.40.10\"[57-160]Tno description
InterPro
IPR013026
Domain
Tetratricopeptide region
PS50005\"[94-127]TTPR
PS50293\"[60-127]TTPR_REGION
InterPro
IPR013105
Repeat
Tetratricopeptide TPR_2
PF07719\"[94-127]TTPR_2
noIPR
unintegrated
unintegrated
signalp\"[1-24]?signal-peptide
tmhmm\"[9-29]?transmembrane_regions


","BeTs to 5 clades of COG1434COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG1434 is -------qvd-l-cefghsn-jx---Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Thu Jan 2 15:55:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01544 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01546","1036380","1035634","747","ATGGAGAAAAAACAAACCTCACGGGTACAAAAACTGGAATTTTTGCTCAAACAAACAGATAAAATCCATCTGCGCGACGCGGCACAAATGCTTGATGTGTCGGAAATGACTTTACGTCGGGATTTAAGTTCCGACAGCGGCAATGTGGTGTTATTGGGCGGCTATATCGTGATGAACCCACAAAAAAGCGGCAATCATTATCAGATTTTTGACCAACAAACGCGCCACATTACGGAAAAAATGTGGCTCGGTAAACTCGCCGCCAATCTCGTCAAGGACGGAGATACCGTGTTCTTCGATTGCGGTAGCACCATTCCGTTTATCATTTCGCAAATCGATCCGCAGATAAAATTCACCGCACTTTTTTGCTCCATCAATAGTTTTATGGCGTTGCAGGACAAACCGCACTGCGAAGTGATTCTGTGCGGCGGACATTATTCGCGCCACAATTCTTTCCTGACTTCCGTGCAATTACACAGCGAACTGGACGCCATTTGCACCACCAAAGCCTTTATTTCCGCCTCAGGTATCGATATAAAAAAAGGTGTGACCTGCTTTAGCGTGGATGAAGCGAAAGTGAAGCAAAAAGCCATGGCAAAAACCCAACTGGCCATTTTGGTTTTTGATCACCATAAAGTGCATAAAATCCAACAAGCCTATATCGGCGAATTGGCACAATTTGATCTGCTGATCTCCAACCAACCGCTACCGGCGGGCTTTGGTGAGGTGCCGAAGATGTTAGTGAAA","","","27871","MEKKQTSRVQKLEFLLKQTDKIHLRDAAQMLDVSEMTLRRDLSSDSGNVVLLGGYIVMNPQKSGNHYQIFDQQTRHITEKMWLGKLAANLVKDGDTVFFDCGSTIPFIISQIDPQIKFTALFCSINSFMALQDKPHCEVILCGGHYSRHNSFLTSVQLHSELDAICTTKAFISASGIDIKKGVTCFSVDEAKVKQKAMAKTQLAILVFDHHKVHKIQQAYIGELAQFDLLISNQPLPAGFGEVPKMLVK","1035634","[FUNCTION] This protein is one of the repressors that regulate the expression of deocabd genes, which encode nucleotide and deoxy ribonucleotide catabolizing enzymes. It also negatively regulates the expression of nupG (a transport protein) & tsx (a pore-forming protein). The inducer is deoxyribose-5-phosphate. [SUBUNIT] Octamer (probable). [SIMILARITY] Belongs to the DeoR family of transcriptional regulators. ","deoxyribose operon repressor","Cytoplasm","","
InterPro
IPR001034
Domain
Bacterial regulatory protein, DeoR N-terminal
PF08220\"[8-61]THTH_DeoR
SM00420\"[8-57]THTH_DEOR
PS51000\"[5-57]THTH_DEOR_2
PS00894\"[8-42]THTH_DEOR_1
InterPro
IPR014036
Domain
Bacterial regulatory protein, DeoR
PF00455\"[77-233]TDeoR


","No hits to the COGs database.","Significant hit ( 5.5e-24) to 4/5 blocks of the IPB001034 family, which is described as \"Bacterial regulatory protein, DeoR family\". Interpro entry for IP:IPR001034. IPB001034A 22-57 2.4e-09 IPB001034B 80-104 7.2e-10 IPB001034D 143-155 7.6 IPB001034E 205-215 11","Residues 1 to 109 match (1e-09) PD:PD031012 which is described as PROTEOME COMPLETE REGULATOR OPERON PLASMID DEOXYRIBOSE DEOR FAMILY TRANSCRIPTIONAL REPRESSOR ","","","","","","","","","","","Thu Jan 2 15:59:23 2003","Thu Jan 2 15:59:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01546 is paralogously related to AA02048 (4e-13), AA00973 (1e-12), AA00308 (2e-10) and AA00585 (2e-05).","","","","","","Residues 8 to 233 (E-value = 9.2e-53) place AA01546 in the DeoR family which is described as Bacterial regulatory proteins, deoR family (PF00455)","","","","","Valentin-Hansen,P., Hojrup,P. and Short,S. The primary structure of the DeoR repressor from Escherichia coli K-12. Nucleic Acids Res. 13 (16): 5927-5936 (1985) [PubMed: 2994018].Mortensen,L., Dandanell,G. and Hammer,K. Purification and characterization of the deoR repressor of Escherichia coli. EMBO J. 8 (1): 325-331 (1989) [PubMed: 2653814].","","Thu Jan 2 15:59:23 2003","1","","","" "AA01547","1037079","1036411","669","ATGAACGCAAAACAAATCGCCCATTATATCGACCACACCGCCCTCACAGCCGAGAAAACCGAGGCGGATATTTTGAAACTGTGTGATGAAGCCCTTGAACATCATTTCTTTTCCGTTTGTATTAATTCCTGCCATATTCCGTTGGCAAAACAAAAACTTGCCGGTTCCGATGTGAAAATTTGTACGGTAGTAGGGTTTCCGTTGGGAGCGAATCTCACCTCCGTGAAAGCCTTTGAAACCAAAGAAGCCATTGCCGCCGGCGCCAATGAAATCGATATGGTGATCAACGTGGGGTGGATTAAATCCGGTAAGTGGGACGCGGTAAAAGCGGATATTCAGGGCGTACTTGCCGCCTGCTATGGCACGCCGTTAAAAGTGATCTTGGAAACCTGTCTGCTAACCAAAAAAGAAATCGTACGCGCCTGCGAAATCTGCAAAGGGTTAAATGTGGCGTTTGTGAAAACCTCTACCGGTTTCAATAAAGGCGGCGCCACCGTGGAAGATGTAGCGTTAATGAAACAAACCGTGGGTAACATCGGCGTAAAAGCCTCCGGCGGGATTCGCGATACGCAAACCGCGTTAGCCATGATTGAAGCGGGCGCAACCCGTATCGGCGCCAGCGCAGGCATCGCCATTATTCACGGCTTACAGGACTCCGGCAGCCCTTAT","","","23399","MNAKQIAHYIDHTALTAEKTEADILKLCDEALEHHFFSVCINSCHIPLAKQKLAGSDVKICTVVGFPLGANLTSVKAFETKEAIAAGANEIDMVINVGWIKSGKWDAVKADIQGVLAACYGTPLKVILETCLLTKKEIVRACEICKGLNVAFVKTSTGFNKGGATVEDVALMKQTVGNIGVKASGGIRDTQTALAMIEAGATRIGASAGIAIIHGLQDSGSPY","1036411","[CATALYTIC ACTIVITY] 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde.[PATHWAY] Nucleotide and deoxyribonucleotide catabolism.[SUBCELLULAR LOCATION] Cytoplasmic (By similarity).","deoxyribose-phosphate aldolase","Cytoplasm","","
InterPro
IPR002915
Family
Deoxyribose-phosphate aldolase/phospho-2-dehydro-3-deoxyheptonate aldolase
PF01791\"[5-215]TDeoC
InterPro
IPR011343
Family
Deoxyribose-phosphate aldolase
PIRSF001357\"[4-223]TDeoxyribose-phosphate aldolase
PTHR10889\"[1-220]TDEOXYRIBOSE-PHOSPHATE ALDOLASE
TIGR00126\"[5-214]TdeoC: deoxyribose-phosphate aldolase
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[4-222]Tno description


","BeTs to 15 clades of COG0274COG name: Deoxyribose-phosphate aldolaseFunctional Class: FThe phylogenetic pattern of COG0274 is -omp-z-qvdrlbce-gh---j--twNumber of proteins in this genome belonging to this COG is","Significant hit ( 4.1e-43) to 3/3 blocks of the IPB002915 family, which is described as \"Deoxyribose-phosphate aldolase\". Interpro entry for IP:IPR002915. IPB002915A 11-31 2.9e-09 IPB002915B 61-94 3e-18 IPB002915C 181-207 9.7e-13","Residues 1 to 56 match (2e-18) PD:PD383658 which is described as PROTEOME COMPLETE DEOXYRIBOSE-PHOSPHATE BASE SCHIFF DEOXYRIBOALDOLASE LYASE ALDOLASE PHOSPHODEOXYRIBOALDOLASE ","","","","","","","","","","","Thu Jan 2 16:06:22 2003","Thu Jan 2 16:06:22 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01547 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 214 (E-value = 5.2e-116) place AA01547 in the DeoC family which is described as Deoxyribose-phosphate aldolase (PF01791)","","","","","Saxild,H.H., Andersen,L.N. and Hammer,K. Dra-nupC-pdp operon of Bacillus subtilis: nucleotide sequence, induction by deoxyribonucleosides, and transcriptional regulationby the deoR-encoded DeoR repressor protein. J. Bacteriol. 178 (2): 424-434 (1996) [PubMed: 8550462]. Yoshida,K., Fujimura,M., Yanai,N. and Fujita,Y. Cloning and sequencing of a 23-kb region of the Bacillus subtilis genome between the iol and hut operons. DNA Res. 2 (6): 295-301 (1995) [PubMed: 8867804].","","Thu Jan 2 16:06:22 2003","1","","","" "AA01549","1037940","1037584","357","ATGGGTAAGCATTATTCAATCGAATTCAAATATCACACTGTCAAGCTTGTCTTAGAAGAACATTGGGGCATTCGCGAAGCCGCACAGCACTTCCATATCGCCACCCATCCTTCCGTTGTCGTCCGGTTGCAACGCTTTGAAAAATACGGTATCAATGGGTTACATCGTCAACACACCACAGCGAGAAAAGCGAAAATGCCAAAGCGAAAAGAAACGCCACTTTACGATAATCCTCAAAATATCAAAGCGTTACTAAAACGCATTGAATATTTGGAAGCGGAGAACACCATCTTAAAAAAGTTCAAGGAGCTGGACGAACAAAAAGCCCGACAGAAAAAAGGAATATCGCCAACGCGT","","","14645","MGKHYSIEFKYHTVKLVLEEHWGIREAAQHFHIATHPSVVVRLQRFEKYGINGLHRQHTTARKAKMPKRKETPLYDNPQNIKALLKRIEYLEAENTILKKFKELDEQKARQKKGISPTR","1037584","","hypothetical protein","Cytoplasm","","No hits reported.","BeTs to 4 clades of COG2963COG name: TransposaseFunctional Class: LThe phylogenetic pattern of COG2963 is ---p-----drlb-efgh---j----Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Thu Jan 2 16:14:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01549 is paralogously related to AA01267 (5e-07), AA00535 (3e-06), AA02340 (9e-04), AA02115 (9e-04), AA01289 (9e-04), AA01075 (9e-04) and AA00008 (9e-04).","","","","","","","","","","","","","","1","","","" "AA01550","1038352","1038176","177","ATGGCATTAAAAGCCTTTAACACGCAAACGGCAAACGCCGCCATTAAGCGAGTAAAAGCCGCGTATGACAGAGGGGAGAGATTAAAACAACGATTTCAGCTATTACAAACATGGGCGGATTTTGTAGAGCAATCCGTGCAAGGTGCTTTACCGCAATTTCATTTGAAGATTGTGGCT","","","7636","MALKAFNTQTANAAIKRVKAAYDRGERLKQRFQLLQTWADFVEQSVQGALPQFHLKIVA","1038176","","hypothetical protein","Periplasm, Cytoplasm","","No hits reported.","BeTs to 3 clades of COG0582COG name: IntegraseFunctional Class: LThe phylogenetic pattern of COG0582 is aompkz-qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Thu Jan 2 16:15:56 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01550 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01551","1038330","1038434","105","GTGTTAAAGGCTTTTAATGCCATAGGTGCGGTAATCTGCGTGATAGGCAAATGCCCAAAGTGCGGTAATCGTATAACTAAAATTCAAGGCTTTGGTAGTATCTTA","","","3615","VLKAFNAIGAVICVIGKCPKCGNRITKIQGFGSIL","1038434","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-16]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 16:37:52 2004","Thu Feb 26 16:37:52 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01551 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 16:38:38 2004","","","","","","","","","","","","","1","","","" "AA01552","1039360","1039133","228","ATGAAAAAACATCTTAAAAAATCACCGCACTTTTTTTGCCTGACCGCCACCATATTGGCGCTTGCCGGCTGCACACCAACCATTCAGCTTGATACGCCCAAAGAAGGCATTACTATCAATATGAACGTGATTGTGGATCACAATATTAACGTCAAAATAGATGAAAAAACCAAAGTGACTGCCGGAGAAAATAGCGCAGTTGAAGCGAACAAAACGCCGGCGGAAAAA","","","8255","MKKHLKKSPHFFCLTATILALAGCTPTIQLDTPKEGITINMNVIVDHNINVKIDEKTKVTAGENSAVEANKTPAEK","1039133","","hypothetical protein","Outer membrane, Periplasm, Cytoplasm","","
noIPR
unintegrated
unintegrated
PD052969\"[14-58]TQ7VNE3_HAEDU_Q7VNE3;
PS51257\"[1-24]TPROKAR_LIPOPROTEIN
signalp\"[1-24]?signal-peptide
tmhmm\"[10-30]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Jan 2 16:16:47 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01552 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01553","1042092","1039360","2733","GTGGGAAAACGTTGGCTATTCTTATTGCTGTTATTCATCTTGGCGGGGATCGGTTCTCTACCGTGGTGGATTACGTCTCAACAATTGGAACAACTTGCCAACTATTTCTTAGCGCCGGGTTATACGCTGCAAATCGGCAATGAGCGTTCGCTTAATATGGACGGTTTACAAGTATCCCAATTACGCCTCGGCGCAACACAATGCAACCTCGTGACCCTCAACAACATTCAATTGAATTGGTGGGCTCCCCGTCGCCTTGAAGTAGAACAGGCGACACTGGATTATGCCTGCCTGAACAGCCTGCATATCAACGACAATGGAAAAACATCGCCAAAATTGACCGCACTTTTTTCCTCCCTGCCTACCGCAGAAGTGGTAATCAAACACCTAAAGGTACTCAATACCGAAAACGTCACCCAACCGTTGTTAAATCAGCTAATCACCGCCGACCTTAGCGTCGTGGCAAATTATGACGGCAAGCGGCTGCAAATTAACACTGAAGCCACAGAGGAAGCTACAAAGAATGGGACGCTGATATTGCAACACCGTTCCACCCTCACGCCGCAAAACGGGCAGTTCCACTGGCAGGGACGAACGGATTTTCAACCCACAGAAAAACAAGCCTATCACCTGACGTTCTCCACAAAAATGAATAATGAATTATTGCGCCTGAAACCTCGCGGCGAGATTACGCTGAACTGGCAAAATCCCGAGTTTGTTGTGGCGAAAGGGGAAATCAAATGGACTTGGGATGGCGAGAAAGGACAAATCAATGCGCAGGATTTGGTACGCAGCGAGCCATTGCTTGACGTGCCTTTTATTCTCACCCCAAACAGTTTGGAAGTCAGCTGGGGGACATTTTATTGGACCTTCGACGGTTATCAGCCGGTGAAGGGCTTCCTTGGTTTGACATTGCGCAAACCGCAGGATAACTGGTTTCCGCTCAATATTGATTTGGATGTCATTCTGCAAACCTTAGGCGAACAAGGCAAGGGTGAAATCGTGTTTGCCGGTAAAGGCGGACAAATTGGCGGCGGTACGCAGCAGAACGAACTCAACTTTGACCTGAAAACCCGCGGCGATCTGCGTTATAACAATACCGTCGCGCAAACCAATCTGGATTATCATATCGGCGGCACATTCAGCGATCCGATCTTGCAATTCCGCCCTGGGTCAATTTTCAAAATGGATAACCTGCAACCGGATGCCAAAATTCATGTTCGCCTGCCGTTGGACGATGTGTTAATCGGGCGCTATGGACTGGAAGGACGGCTACAGGCAACTTTGCAAGGCTTCACCCCGCAATTTGAGAACCTCAATTTGAAATTGGACGGACAGGCACACGAGTTCATCGCCGGCATTAAAACCGTCTTTGAATTGCGTGACGAACAACAAAATCTGCACAATGCAGAAATGCGTGCGGCAAACCGGTGGGATTGGACGATTAGCGGCAGCGCACAATGGAAAGCGCTAAAAACTGCCGTCACCATGCAAGGCATCGGCTTTTGGCAGGCGAATTATATTGAATTGAACCAACTTTCGGCGCATTCCGGCAACGTATATACCGGTGGGGTAAAAATGGCACCGCTGTCACTGGAGCTGAAAGACCGACTGCGTTGGAATTATGAAAAAGAGCATATCCGCGGGCTGATGCAGGCAAAAACCGACTGGATCGAATTTGACTACGGCGGGTGGTTTGTAAAGCCGGTGTTCGGCGTCGGACTAAACGGCAAAAGTATCAATCATTTTACCATCGCCGGTGAGTTGAAAGCCGGTTCGCTCGGCCCATTAGATCTTACTGCCCGTTATCAAAATCAGACGCTGACGGGACAAATCGGTTGGAAGGAGCAATCCGCCAACGTATTCCAATCGCTGTTTCCGCAACAATGGGAATGGATTATCCACCAAGGCACCATCAAAGGCGCCAGCAACTTCGTTATTAACGGCGACGGAGTGGCGCTGCACGGTGAACTGAACCTGCGCGGTGGTGAAATCACCATGCCCGACGGCGAAATTCAAGGGCTGAATATTCGTTTTCCGTTAAATTATCAGGATCTGGCGTTGAAAGCCTCGCGCAACAAACCTATTCGTGTGTCGGCAAACAATATCCGTAAAGGTGCGCTGTTGATGAATAAAGCGGTGTTCAACCTGTTCGGGACCTACCCAAATTCAGCAAAATCGCCACTCACCTTGAGCAATGCGCGGATAAATGTCTTTGACGGTGAGTTGCAAATTCCGAGTTTAAGTTTCCCGCAACAAAAAATAGCAACCTTGAGTTTCAAGAATATCGACTTGGCGCAGGTCATCAACATGGCGCAATATAATCAAATCAGCCTGCGCGGAAGGGTCAATGCCACCTTGCCGTTTTGGCTCGGACACCAGGAATGCCTGATCTGTAACGGCACCATTGAACAGGTAAATAACCTGCATATTAAACTCAACGACGAAATCGTCACCGGCTTAAAAAAGGGCGGCTGGACGGAAAACATTTTAGTGGATTTATTAAAAGAAATGGAATTGGAAAAATCCCGTGCCAACTTGAATCTTGCGCCAGACGGGCAAATGAAATTACATTCCAGCCTGACCGCGTTCAACCCGACCAAGCGCACACGTAGCCCGATCACCCTGAATTACACTCACCAAGAAAATATGTTTGAGCTGTGGAATATGATTGACTACGGCTCGCAATTTGAACAGAATTTGCAATATCGACTTTACCGACATTTGGAACAA","","","102977","VGKRWLFLLLLFILAGIGSLPWWITSQQLEQLANYFLAPGYTLQIGNERSLNMDGLQVSQLRLGATQCNLVTLNNIQLNWWAPRRLEVEQATLDYACLNSLHINDNGKTSPKLTALFSSLPTAEVVIKHLKVLNTENVTQPLLNQLITADLSVVANYDGKRLQINTEATEEATKNGTLILQHRSTLTPQNGQFHWQGRTDFQPTEKQAYHLTFSTKMNNELLRLKPRGEITLNWQNPEFVVAKGEIKWTWDGEKGQINAQDLVRSEPLLDVPFILTPNSLEVSWGTFYWTFDGYQPVKGFLGLTLRKPQDNWFPLNIDLDVILQTLGEQGKGEIVFAGKGGQIGGGTQQNELNFDLKTRGDLRYNNTVAQTNLDYHIGGTFSDPILQFRPGSIFKMDNLQPDAKIHVRLPLDDVLIGRYGLEGRLQATLQGFTPQFENLNLKLDGQAHEFIAGIKTVFELRDEQQNLHNAEMRAANRWDWTISGSAQWKALKTAVTMQGIGFWQANYIELNQLSAHSGNVYTGGVKMAPLSLELKDRLRWNYEKEHIRGLMQAKTDWIEFDYGGWFVKPVFGVGLNGKSINHFTIAGELKAGSLGPLDLTARYQNQTLTGQIGWKEQSANVFQSLFPQQWEWIIHQGTIKGASNFVINGDGVALHGELNLRGGEITMPDGEIQGLNIRFPLNYQDLALKASRNKPIRVSANNIRKGALLMNKAVFNLFGTYPNSAKSPLTLSNARINVFDGELQIPSLSFPQQKIATLSFKNIDLAQVINMAQYNQISLRGRVNATLPFWLGHQECLICNGTIEQVNNLHIKLNDEIVTGLKKGGWTENILVDLLKEMELEKSRANLNLAPDGQMKLHSSLTAFNPTKRTRSPITLNYTHQENMFELWNMIDYGSQFEQNLQYRLYRHLEQ","1039360","","conserved hypothetical protein","Outer membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","","Residues 671 to 902 match (4e-19) PD:PD148240 which is described as COMPLETE PROTEOME EXPORTED YDBH PERIPLASMIC ORF ","","","","","","","","","","","","Thu Jan 2 16:19:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01553 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01554","1042815","1042201","615","ATGTTTGATTCTCTTATCGTTCAATTTGTCGTACTGTGGGCGGTTATCGATCCCATCGGTTCCATTCCCGTTTACTTAACGAAAACCGTCGGGTTATCGGTGGAAGATCGGCGCAAGATTGCGTTAAAAGCCGTCATGATTTCCGCCGGAATATTAATTTTCTTCCTCATTGCCGGACAGGCACTGTTAGAAGCCATGCAAATTCCGTTGACCGCCTTCCAAATCGCCGGCGGCCTGGTGCTATTGTTATTCGCGCTCACTATGATTTTCGGTGAGGGCAAGGCGGAGCAGGAAATTAAGCTGTCCTCCAACTTAAACGAACTGGCGGTGTATCCGTTAGCTGTGCCGTCCATCGCCTCACCGGGGGCGATGATGGCGATTGTGTTGCTAACCGACAACCACCGTTTCAGCCTGTTCGACCAAACCATGACCACCTTAATTATGTTGTCCGTTCTGGCAATCACTTACCTTTTGCTCCTCGCGGCAAATCGCATTCAACGCTGGCTCGGCAACACCGGTGCGGCGGTGATCAGTCGAGTGATGGGATTAATCCTGGCAGCGGTTGCTATCAACAATATGTTGGTGGGGATTCGCGATTTCTTTACGCAAATGAGT","","","22565","MFDSLIVQFVVLWAVIDPIGSIPVYLTKTVGLSVEDRRKIALKAVMISAGILIFFLIAGQALLEAMQIPLTAFQIAGGLVLLLFALTMIFGEGKAEQEIKLSSNLNELAVYPLAVPSIASPGAMMAIVLLTDNHRFSLFDQTMTTLIMLSVLAITYLLLLAANRIQRWLGNTGAAVISRVMGLILAAVAINNMLVGIRDFFTQMS","1042201","","conserved hypothetical protein; hypothetical membrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR002771
Family
Multiple antibiotic resistance (MarC)-related proteins
PF01914\"[2-201]TMarC
TIGR00427\"[1-197]TTIGR00427: conserved hypothetical protein T
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide
tmhmm\"[5-25]?\"[44-62]?\"[71-91]?\"[110-130]?\"[145-165]?\"[175-195]?transmembrane_regions


","BeTs to 16 clades of COG2095COG name: Integral membrane proteins of the MarC familyFunctional Class: SThe phylogenetic pattern of COG2095 is a-mpkz-q-d--b-efghsnuj-it-Number of proteins in this genome belonging to this COG is","Significant hit ( 7.1e-27) to 3/3 blocks of the IPB002771 family, which is described as \"Uncharacterised protein family UPF0056\". Interpro entry for IP:IPR002771. IPB002771A 71-89 9.3e-05 IPB002771B 112-125 2.4e-05 IPB002771C 165-197 1.5e-13","Residues 3 to 90 match (3e-07) PD:PD006289 which is described as PROTEOME COMPLETE TRANSMEMBRANE MEMBRANE MARC PM0044 AQ_540 PROBABLE PAB0863 RESISTANCE ","","","","","","","","","","","","Thu Jan 2 16:20:53 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01554 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 201 (E-value = 8.5e-44) place AA01554 in the MarC family which is described as MarC family integral membrane protein (PF01914)","","","","","","","","1","","","" "AA01555","1042896","1044383","1488","ATGCTTTTTTTCATTAACTTAACATTAAAACGTGGTTTAACCACCTTGCTCGAAAATGCCAACGCTACCATCAACCCCGGACAGAAAGTCGGGTTGGTCGGAAAAAACGGTTGCGGTAAGTCTTCTCTGTTCGCCTTGCTGAAAAATGAAATGAGCGCCGAAGGCGGCGAAATGTCTTTTCCGCCGAATTGGGCATTGGCATGGGTGAATCAGGAAACTCCCTCGCTGGATTGCCGCGCCATCGATTATGTGATTCAGGGCGATCGCGAATACAGCCGCCTGCAACAGGTATTACAACAGGCGAATACCGCCAATGACGGCAATGCTATCGCGGTGTTGCACAATCAGTTAGACGCCATTGATGCTTGGACCATTGAAGCCCGTGCCGGCGAATTATTGCACGGCTTAGGTTTCACCCAAGCGGAACTGGAACAACCGGTGAAGGCCTTTTCCGGTGGTTGGCGGATGCGCTTGAACTTGGCGCAGGCGCTGATTTGTCGCTCTGATTTATTGTTATTGGACGAGCCCACCAACCACTTGGATTTGGACGCGGTGATTTGGCTGGAACGTTGGTTAAAGCAATATCCCGGCACCTTGATCCTGATTTCGCACGATCGCGACTTTTTAGACCCTATTGTCGGCAAAATTCTACACATTGAACAACAAAAGCTGAACGAATATACCGGCGATTATTCTTCTTTCGAACAGCAACGGGCGACCAAATTGGCACAACAAAACGCCATGTATCGCCAGCAACAACTGAAAATCGACCATCTGCAACGTTATATCGATCGCTTCAAAGCCAAAGCCACCAAGGCGAAACAGGCGCAAAGCCGCATCAAGGCATTGGAGCGTATGGAAAAAATCGCGCCGGCGTATGTGGATAATCCGTTTCATTTTGAATTTCGCGAACCGTTGTCGCTGCCCAACCCGTTATTAATGATGGAAAACGCCTCGGTAGGCTACGGCGAGGGCGAAAAAAGTGCGGTGGAAATTTTAAGTAAAATTAAACTCAATCTGGTGCCCGGCTCGCGCATTGGTCTGCTGGGGAAAAACGGTGCGGGGAAATCTACTTTAATCAAATTATTGGCGGGCGAAATCGCGCCTACCGGCGGCACCATTCAGTTGGCAAAAGGCGTACAGTTGGGCTATTTCGTGCAGCACCAATTGGATACGTTGCGCGCCGACGAAAGCGCCCTGTGGCATTTACAAAAAATTGCCCCGCAACAGACGGAACAGCAACTGCGCGATTATTTGGGCGGATTTGCGTTTCACGGCGATAAAGTGAATCAACCGGTTGCTTCTTTTTCCGGCGGCGAAAAAGCGCGTCTGGTGCTGGCGCTCATCGTGTGGCAACGCCCGAATTTGCTGCTGCTGGACGAGCCGACCAACCACTTGGATTTTAGATATGCGTCAGGCGTTAACGGAAGCCTTGGTGGATTATCAGGGCTCTTTGGTGTTGGTGTCGCACGATCGCCATTTATTGCG","","","54961","MLFFINLTLKRGLTTLLENANATINPGQKVGLVGKNGCGKSSLFALLKNEMSAEGGEMSFPPNWALAWVNQETPSLDCRAIDYVIQGDREYSRLQQVLQQANTANDGNAIAVLHNQLDAIDAWTIEARAGELLHGLGFTQAELEQPVKAFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLERWLKQYPGTLILISHDRDFLDPIVGKILHIEQQKLNEYTGDYSSFEQQRATKLAQQNAMYRQQQLKIDHLQRYIDRFKAKATKAKQAQSRIKALERMEKIAPAYVDNPFHFEFREPLSLPNPLLMMENASVGYGEGEKSAVEILSKIKLNLVPGSRIGLLGKNGAGKSTLIKLLAGEIAPTGGTIQLAKGVQLGYFVQHQLDTLRADESALWHLQKIAPQQTEQQLRDYLGGFAFHGDKVNQPVASFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDFRYASGVNGSLGGLSGLFGVGVARSPFIA","1044383","","ABC transporter, ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[150-192]T\"[435-467]TQ9KNX2_VIBCH_Q9KNX2;
PF00005\"[27-222]T\"[343-467]TABC_tran
PS50893\"[2-246]TABC_TRANSPORTER_2
PS00211\"[150-164]?\"[436-450]?ABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[26-223]T\"[342-493]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[1-287]T\"[328-481]Tno description
PTHR19211\"[120-468]TATP-BINDING TRANSPORT PROTEIN-RELATED
PTHR19211:SF13\"[120-468]TABC TRANSPORTER ATP-BINDING PROTEIN YHES-RELATED
signalp\"[1-22]?signal-peptide


","No hits to the COGs database.","Significant hit ( 7.6e-21) to 2/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 332-378 1.8e-13 IPB001140B 433-471 7.8e-06 IPB001140B 147-185 1.3e-05","Residues 1 to 47 match (9e-07) PD:PD261979 which is described as ATP-BINDING PROBABLE ABC PROTEOME COMPONENT COMPLETE TRANSPORTER ","","","","","","","","","","","","Thu Jan 2 16:24:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01555 is paralogously related to AA02573 (5e-61), AA02484 (5e-53), AA01820 (2e-14), AA02140 (6e-14), AA01616 (1e-11), AA02080 (1e-11), AA02898 (2e-11), AA00415 (5e-11), AA01524 (9e-11), AA02609 (1e-10), AA01824 (1e-10), AA01393 (1e-10), AA01422 (1e-10), AA00858 (2e-10), AA01568 (3e-10), AA00700 (7e-10), AA01961 (1e-09), AA01757 (1e-09), AA01509 (3e-09), AA00799 (5e-09), AA01051 (8e-09), AA02550 (1e-08), AA02440 (1e-08), AA02331 (1e-08), AA02320 (1e-08), AA02642 (2e-08), AA01867 (2e-08), AA01656 (4e-08), AA01684 (5e-08), AA02805 (7e-08), AA01510 (7e-08), AA02606 (9e-08), AA01645 (2e-07), AA02718 (3e-07), AA02899 (4e-07), AA02152 (4e-07), AA01779 (8e-07), AA00207 (8e-07), AA00061 (3e-06), AA02225 (4e-06), AA02353 (1e-05), AA02226 (2e-05), AA00934 (2e-05), AA01569 (3e-05), AA02786 (4e-05), AA01947 (4e-05), A02145 (2e-04), AA02146 (5e-04), AA00933 (5e-04), AA00591 (5e-04), AA01456 (6e-04) and AA02324 (0.001).","","","","","","Residues 343 to 486 (E-value = 1.2e-16) place AA01555 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","","","","1","","","" "AA01556","1044358","1044819","462","GTGTCGCACGATCGCCATTTATTGCGTAACACAGTAGATGAATTTTATTTGGTGCACGATAAGCAGGTGGAGGAATTTAAAGGGGATTTGGGCGATTATCAAAAATGGCTGAACGAACAAAACGCCCAACCGACCATCACAAAAGCACAAACCGCGCCTGTTGAAAATGAAAACTCCGCCGCTAATCGTAAGGAACAAAAACGCAAAGAAGCGGAATTGCGCCAACAGCTCGCGCCGTTACGCAAACAGGCAACGCAGCTGGAAAATCAAATGGAAAAGCTGGGCGCGCAGTTACAACACATTGAAACAGCGCTGGCGGATCCGAATGTGTATGATGCCGAAATGAAAGCAAAACTGACCGCACTTTTAAACGATCAGGTGCAGACGAAAAAGCAACTGGAAGAAGTAGAAGCGGCATGGTTAGTCTTGCAGGAAGATATGGAAAACATCACAGCACAAGCA","","","17816","VSHDRHLLRNTVDEFYLVHDKQVEEFKGDLGDYQKWLNEQNAQPTITKAQTAPVENENSAANRKEQKRKEAELRQQLAPLRKQATQLENQMEKLGAQLQHIETALADPNVYDAEMKAKLTALLNDQVQTKKQLEEVEAAWLVLQEDMENITAQA","1044819","","ABC transporter ATP-binding protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
PTHR19211\"[1-94]TATP-BINDING TRANSPORT PROTEIN-RELATED
PTHR19211:SF13\"[1-94]TABC TRANSPORTER ATP-BINDING PROTEIN YHES-RELATED


","No hits to the COGs database.","","Residues 1 to 35 match (1e-10) PD:PD467395 which is described as ATP-BINDING ABC COMPLETE PROTEOME TRANSPORTER PROBABLE COMPONENT REPEAT TRANSPORTER ATPASE ","","","","","","","","","","","","Thu Jan 2 16:27:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01556 is paralogously related to AA02573 (2e-06).","","","","","","","","","","","","","","1","","","" "AA01557","1045051","1046025","975","ATGAAACTCGGCGACAGCCAAAAACTGGACATTGAAGCGATTTCCACCGGTTCTTTCGGTCTTGACCTAGCACTAGGCATCGGCGGTTTGCCGATGGGGCGTATCGTGGAGATTTTCGGGCCGGAATCTTCAGGTAAAACTACTTTAACCCTTTCTGTGATTGCGGAAGCGCAAAAAACCGGCAAAACCTGTGCCTTTATTGATGCGGAACATGCTTTAGACCCGATTTATGCCTCCAAACTCGGCGTGGATGTAAAAGAACTTTTAGTTTCCCAGCCGGACAACGGCGAACAGGCGCTGGAAATTTGTGATGCGTTGGTGCGTTCCGGTGCGGTGGATGTAATTATCGTTGACTCCGTTGCCGCCTTAACGCCGAAAGCGGAAATTGAAGGCGACATGGGCGATTCCCACATGGGATTACAAGCGCGTTTAATGTCTCAAGCATTGCGTAAACTTACCAGCCAAATTAAAAACGCCAACTGCTTGGTGATTTTCATCAACCAAATTCGGATGAAAATCGGCGTGATGTTCGGTAATCCGGAAACCACCACCGGCGGTAACGCGTTGAAATTCTATGCCTCCGTGCGTTTGGATATTCGCCGCGTGGGTTCTATCAAAGAGGGTGATGAAGTTATCGGTAATGAAACTCGTGTGAAAGTGGTGAAAAACAAAGTGGCGCCACCGTTCCGCCAAGTGGATTTCCAAATTCTGTACGGCGAAGGTATTTCCAAAGAAAGCGAACTGATTGAGCTCGGCGTGAAACATAAACTCATCAGCAAAGCAGGTGCGTGGTACGCTTACCAAAACGAGAAAATCGGTCAGGGCAAAACCAATGCTATGAAATGGTTGAAAGACAATCCTGAACAAGCCAAATTTATCGAAAGCACCTTGCGTGATGAATTGTTGGCACATCCGGAATCTGCCATCACTGCGGAAGTAGAAAACGAAGCGGGTAATGGCGAAGGCGATTTCGAA","","","37965","MKLGDSQKLDIEAISTGSFGLDLALGIGGLPMGRIVEIFGPESSGKTTLTLSVIAEAQKTGKTCAFIDAEHALDPIYASKLGVDVKELLVSQPDNGEQALEICDALVRSGAVDVIIVDSVAALTPKAEIEGDMGDSHMGLQARLMSQALRKLTSQIKNANCLVIFINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRRVGSIKEGDEVIGNETRVKVVKNKVAPPFRQVDFQILYGEGISKESELIELGVKHKLISKAGAWYAYQNEKIGQGKTNAMKWLKDNPEQAKFIESTLRDELLAHPESAITAEVENEAGNGEGDFE","1046025","[FUNCTION] Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the atp-dependent hybridization of homologous single-stranded DNAs. It interacts with lexa causing its activation and leading to its autocatalyticcleavage. [SUBCELLULAR LOCATION] Cytoplasmic (by similarity). [SIMILARITY] Belongs to the RecA family. For other \"rec\" genes, see HD1076 (recB), HD1342(recJ), HD1604 (recO), HD1921 (recG), HD0325 (recR),HD0411 (recX), HD0475 (recQ), HD0815 (recN), HD0849(recF), HD0626 (recD).","recombinase A","Cytoplasm","","
InterPro
IPR001553
Family
RecA bacterial DNA recombination
PD000229\"[131-179]TRECA_ACTAC_Q9JRP9;
PR00142\"[11-33]T\"[37-66]T\"[68-97]T\"[102-131]T\"[140-169]T\"[185-213]T\"[218-247]T\"[272-289]TRECA
TIGR02012\"[1-299]Ttigrfam_recA: protein RecA
PS50162\"[10-173]TRECA_2
PS50163\"[174-247]TRECA_3
PS00321\"[188-196]TRECA_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[32-203]TAAA
InterPro
IPR013765
Domain
RecA
PF00154\"[1-303]TRecA
noIPR
unintegrated
unintegrated
G3DSA:3.30.250.10\"[244-302]Tno description
G3DSA:3.40.50.300\"[1-243]Tno description
PTHR22942\"[2-302]TRECA/RAD51/RADA DNA STRAND-PAIRING FAMILY MEMBER
PTHR22942:SF1\"[2-302]TDNA REPAIR PROTEIN RECA


","No hits to the COGs database.","Significant hit (3.4e-139) to 3/4 blocks of the IPB001553 family, which is described as \"RecA bacterial DNA recombination protein\". Interpro entry for IP:IPR001553. IPB001553B 24-77 1.5e-50 IPB001553C 128-182 2.5e-52 IPB001553D 241-294 1.7e-34","Residues 218 to 301 match (8e-07) PD:PD597639 which is described as P0660F12.22 RECA ","","","","","","","","","","","Fri Nov 21 17:00:06 2003","Mon Jan 13 18:22:59 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01557 is paralogously related to AA02735 (2e-05).","","","","","","Residues 1 to 303 (E-value = 4.5e-220) place AA01557 in the RecA family which is described as recA bacterial DNA recombination protein (PF00154)","","","","","Horii,T., Ogawa,T. and Ogawa,H. Organization of the recA gene of Escherichia coli . Proc. Natl. Acad. Sci. U.S.A. 77 (1): 313-317 (1980) PubMed: 6244554.Sancar,A., Stachelek,C., Konigsberg,W. and Rupp,W.D. Sequences of the recA gene and protein . Proc. Natl. Acad. Sci. U.S.A. 77 (5): 2611-2615 (1980) PubMed: 6930655.Zhao,X.J. and McEntee,K. DNA sequence analysis of the recA genes from Proteus vulgaris, Erwinia carotovora, Shigella flexneri and Escherichia coli B/r. Mol. Gen. Genet. 222 (2-3): 369-376 (1990) [PubMed: 2274037].Yu,X. and Egelman,E.H. The RecA hexamer is a structural homologue of ring helicases . Nat. Struct. Biol. 4 (2): 101-104 (1997) [PubMed: 9033586].","","Tue Jan 28 15:07:41 2003","1","","","" "AA01559","1046110","1046565","456","ATGTCTTCTCTTGCGCTCAATTATGTGATGAATTTACTTTCCCGCCGTGAATACAGCGAGTTTGAACTGCGTTGCAAAATGCAGGAAAAAGCCTTTTCCGAAAACGACATCGATCAGGTAATTGCCCATTGTCAGCAAAAAAACTGGCAAAGCGATGTACGATTCACGGAAAGCTATTTGCACAGCCGTGCCCAGCGGGGTTATGGTGCCAATCAAATCAAACAGGAATTACGCCAGTTAAAAGGGGTTGAAAGCGCAACCATTGAATCGGTAATGCGCGAATGTGAAATTGATTGGTCCGAGTTGGCGTTAACCGTATTACGCAAAAAATTTCCCGATTACAAAGCAAAACAACCGCCGAAGATGCGACAAAAGATCTGGCAATATATGCTGTCGCACGGTTTTCATGGCGATGATTTTGCCGATTATGTGGGATCGGAGCCCGATGAATTTGAT","","","17954","MSSLALNYVMNLLSRREYSEFELRCKMQEKAFSENDIDQVIAHCQQKNWQSDVRFTESYLHSRAQRGYGANQIKQELRQLKGVESATIESVMRECEIDWSELALTVLRKKFPDYKAKQPPKMRQKIWQYMLSHGFHGDDFADYVGSEPDEFD","1046565","[FUNCTION] May play a regulatory role possibly by interacting with recA (by similarity). [SIMILARITY] Belongs to the recX family. ","RecA regulatory protein, RecX","Cytoplasm","","
InterPro
IPR003783
Family
Regulatory protein RecX
PF02631\"[27-150]TRecX


","BeTs to 8 clades of COG2137COG name: Uncharacterized BCRFunctional Class: RThe phylogenetic pattern of COG2137 is --------vdrlb-efgh-n----t-Number of proteins in this genome belonging to this COG is","Significant hit ( 9.3e-06) to 2/2 blocks of the IPB003783 family, which is described as \"RecX regulatory protein\". Interpro entry for IP:IPR003783. IPB003783A 16-26 0.44 IPB003783B 65-79 0.012","Residues 5 to 60 match (9e-08) PD:PD512217 which is described as RECX ","","","","","","","","","","","Thu Jan 2 16:39:56 2003","Tue Jan 28 15:50:01 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01559 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 27 to 150 (E-value = 1.9e-43) place AA01559 in the RecX family which is described as RecX family (PF02631)","","","","","Venkatesh R, Ganesh N, Guhan N, Reddy MS,Chandrasekhar T, Muniyappa K. RecX protein abrogates ATP hydrolysis and strandexchange promoted by RecA: insights into negativeregulation of homologous recombination. Proc Natl Acad Sci U S A. 2002 Sep 17;99(19):12091-6.PMID: 12218174 Stohl EA, Blount L, Seifert S. Differential cross-complementation patterns ofEscherichia coli and Neisseria gonorrhoeae RecAproteins. Microbiology. 2002 Jun;148(Pt 6):1821-31. PMID: 12055302De Mot,R., Schoofs,G. and Vanderleyden,J. A putative regulatory gene downstream of recA is conserved in gram-negative and gram-positive bacteria. Nucleic Acids Res. 22 (7): 1313-1314 (1994) [PubMed: 8165147].","","Thu Jan 2 16:38:50 2003","1","","","" "AA01561","1046645","1047031","387","ATGACTAAAATAATTCATACCGATAAAGCACCGGCAGCCATTGGTCCTTATGTACAAGCGGTGGATTTAGGCAATTTGGTGTTGACATCCGGACAAATTCCGGTCAATCCGGTAACAGGCGAGGTGCCGAAAGAGATTGTGGCGCAGGCCCGTCAGTCTTTAGAAAACGTAAAAGCCATTATTGAACAGGCGGGTTTGAAGGTTGCCGATATTGTGAAAACCACGGTGTTTGTGAAAGACTTGAATGATTTTGCTGCGGTAAACGCCGAATATGAGCGTTTCTTCAAAGAAAACAATCACCCGAACTTCCCGGCGCGTTCTTGCGTAGAAGTTGCCCGCTTGCCGAAAGATGTGGGCTTGGAAATTGAGGCGATTGCGGTAAGAGCC","","","13960","MTKIIHTDKAPAAIGPYVQAVDLGNLVLTSGQIPVNPVTGEVPKEIVAQARQSLENVKAIIEQAGLKVADIVKTTVFVKDLNDFAAVNAEYERFFKENNHPNFPARSCVEVARLPKDVGLEIEAIAVRA","1047031","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR006056
Family
YjgF-like protein
TIGR00004\"[2-128]TTIGR00004: endoribonuclease L-PSP, putative
PS01094\"[104-122]TUPF0076
InterPro
IPR006175
Domain
Endoribonuclease L-PSP
PF01042\"[7-128]TRibonuc_L-PSP
InterPro
IPR013813
Domain
Endoribonuclease L-PSP/chorismate mutase-like
G3DSA:3.30.1330.40\"[1-129]Tno description
noIPR
unintegrated
unintegrated
PTHR11803\"[5-129]TTRANSLATION INITIATION INHIBITOR


","BeTs to 18 clades of COG0251COG name: Putative translation initiation inhibitorFunctional Class: JThe phylogenetic pattern of COG0251 is -o--kzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 6.7e-57) to 3/3 blocks of the IPB000543 family, which is described as \"YER057c/YjgF/UK114 family\". Interpro entry for IP:IPR000543. IPB000543A 10-37 8.3e-15 IPB000543B 49-95 5.6e-27 IPB000543C 104-126 1.6e-12","Residues 2 to 128 match (1e-56) PD:PD002429 which is described as PROTEOME COMPLETE INHIBITOR TRANSLATION PLASMID INITIATION ORF TRANSLATIONAL PROBABLE LIPOPROTEIN ","","","","","","","","","","","","Thu Jan 2 16:41:57 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01561 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 128 (E-value = 8.2e-60) place AA01561 in the Ribonuc_L-PSP family which is described as Endoribonuclease L-PSP (PF01042)","","","","","","","","1","","","" "AA01563","1049103","1047109","1995","ATGTCAAATCGTCAACAACTCGCCAATGCAATTCGTTTTTTAAGTATGGATGCGGTACAAAAAGCGAAATCCGGTCACCCGGGCGCACCTATGGGCATGGCGGATATCGCCGAAGTATTATGGCGTGATTTTTTACACCACAACCCGACCAACCCGCAATGGGCTAACCGCGACCGTTTTGTGCTGTCCAACGGACACGGTTCCATGCTGATTTACAGCTTATTACACCTCAGCGGTTACGATTTATCCATCGAAGATTTAAAACAATTCCGTCAACTGCACTCCAAAACACCGGGCCATCCTGAATACGGCTACACTCCGGGCGTAGAAACCACCACCGGTCCGTTAGGACAAGGTATTACCAATGCGGTGGGGATGGCAATTGCGGAAAAAACCCTTGCCGGTCAATTTAACCGTGACGGTCATAACATCGTTGATCACTATACTTACGCCTTTTTAGGCGATGGTTGTTTAATGGAAGGAATTTCCCACGAAGCCTGTTCTTTAGCGGGTACCTTAGGTTTGGGTAAATTGATCGCATTCTATGATGACAACAATATCTCTATCGACGGACACGTTGACGGCTGGTTCACCGACGATACACAAAAACGCTTTGAAGCATACGGCTGGCAAGTGATTCCGGCAATTGACGGTCACAATCCGGCACAAATTGCCGAAGCCATCAAACAAGCGCAAGCGGAAACCGCCAAACCAACATTAATTATCTGTAAAACCATTATCGGTTTCGGTTCACCAAATAAATCCAACTCTCATGACAGCCACGGCGCGCCGTTAGGCGACGAAGAAATCGCTTTAACCCGCAAAGCGTTACATTGGGATTATGCCCCGTTTGAAATTCCGGCGGACATTTATGCGCAATGGGATGCCAAAGCAAAAGGCGCGGAATGGGAAAAAGCCTGGGATGAAAAATTTTCCGCGTATGCCAAAGCCTATCCTGAATTAGCGGCTGAATTCACCCGCCGCATAGCGAAAAAACTGCCGGCCGACTGGGCAAAAGACTCTCAAGCATTTGTTGAGCATTTACAAGCCAATCCGGCAAGCATTGCAAGCCGCAAAGCCTCACAAAATGCCATTGAAGCCTACGCCAAAATTTTACCTGAATTACTGGGCGGTTCTGCCGACTTGGCAAGTTCCAACTTAACCCTTTGGTCCGGTTCCAAACCAATCCGTGCCACCCAAAACGTTGATGGTAACTACATCAACTACGGCGTGCGCGAATTCGGTATGGCGGGGATCATGAACGGTATCGCCTTGCACGGCGGCTTCATTCCTTACGGCGCCACCTTCCTGATGTTCATGGAATACGCCCACAACGCCATTCGCATGGCGGCCCTAATGAAGCAACGTTCCTTATTTGTGTTCACCCACGATTCCATCGGCTTAGGCGAAGACGGCCCGACCCACCAACCGGTAGAACAAACTGCGGCATTACGTTTAATTCCTAACTTGAACACATGGCGTCCTTGCGACCAAGTGGAATCCGCCATTGCGTGGAAAGCGGCGATTGAAAGAACGGATGGTCCAAGCGCCTTAATTTTTACCCGCCAAAACTTGGCGCAGATGGACCGCACTTCCGAGCAACTGGCAAATGTGGCGCGCGGGGCGTATGTCTTAAAAGATTGTGCCGGTACGCCGGAACTGATCTTTATCGCCACCGGTTCTGAAGTGGAATTAGCAGTGAAAGCAGCAGAACAATTAACCGCGGAAGGCAAAAAAGTTCGTGTGGTTTCCATGCCAAGCACCAACGTGTTTGATAAACAAGATGAAGCTTATCGCGAATCCGTGTTGCCTGTCGCCGTGACTAAACGTGTCGCCATTGAAGCCGGAATTTCCGACTTCTGGTACAAATATGTCGGCTTCAACGGCCGAATCATCGGTATGCACAGCTTCGGCGAATCTGCACCGGCAGACCAATTATTCAAACTCTTTGGTTTTACGGTGGATAACGTCGTCGCCAAGGCAAAAGAAATACTC","","","72805","MSNRQQLANAIRFLSMDAVQKAKSGHPGAPMGMADIAEVLWRDFLHHNPTNPQWANRDRFVLSNGHGSMLIYSLLHLSGYDLSIEDLKQFRQLHSKTPGHPEYGYTPGVETTTGPLGQGITNAVGMAIAEKTLAGQFNRDGHNIVDHYTYAFLGDGCLMEGISHEACSLAGTLGLGKLIAFYDDNNISIDGHVDGWFTDDTQKRFEAYGWQVIPAIDGHNPAQIAEAIKQAQAETAKPTLIICKTIIGFGSPNKSNSHDSHGAPLGDEEIALTRKALHWDYAPFEIPADIYAQWDAKAKGAEWEKAWDEKFSAYAKAYPELAAEFTRRIAKKLPADWAKDSQAFVEHLQANPASIASRKASQNAIEAYAKILPELLGGSADLASSNLTLWSGSKPIRATQNVDGNYINYGVREFGMAGIMNGIALHGGFIPYGATFLMFMEYAHNAIRMAALMKQRSLFVFTHDSIGLGEDGPTHQPVEQTAALRLIPNLNTWRPCDQVESAIAWKAAIERTDGPSALIFTRQNLAQMDRTSEQLANVARGAYVLKDCAGTPELIFIATGSEVELAVKAAEQLTAEGKKVRVVSMPSTNVFDKQDEAYRESVLPVAVTKRVAIEAGISDFWYKYVGFNGRIIGMHSFGESAPADQLFKLFGFTVDNVVAKAKEIL","1047109","[CATALYTIC ACTIVITY] Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.[COFACTOR] Thiamine pyrophosphate. [SIMILARITY] Belongs to the transketolase family. ","transketolase isozyme 1","Cytoplasm","","
InterPro
IPR005474
Domain
Transketolase, N-terminal
PF00456\"[3-334]TTransketolase_N
PS00801\"[12-32]TTRANSKETOLASE_1
InterPro
IPR005475
Domain
Transketolase, central region
PF02779\"[353-527]TTransket_pyr
PS00802\"[469-485]TTRANSKETOLASE_2
InterPro
IPR005476
Domain
Transketolase, C-terminal
PF02780\"[542-657]TTransketolase_C
InterPro
IPR005478
Family
Bacterial transketolase
PIRSF000418\"[1-665]TTransketolase
PTHR11624:SF1\"[16-660]TTRANSKETOLASE
TIGR00232\"[5-665]Ttktlase_bact: transketolase
InterPro
IPR009014
Domain
Transketolase, C-terminal-like
G3DSA:3.40.50.920\"[540-665]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.970\"[5-331]T\"[332-538]Tno description
PTHR11624\"[16-660]TDEHYDROGENASE RELATED
tmhmm\"[60-80]?transmembrane_regions


","BeTs to 22 clades of COG0021COG name: TransketolaseFunctional Class: GThe phylogenetic pattern of COG0021 is --mpkzyqvdrlbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-51) to 3/3 blocks of the IPB000360 family, which is described as \"Transketolase\". Interpro entry for IP:IPR000360. IPB000360A 25-36 1.7e-05 IPB000360B 38-77 1.5e-24 IPB000360C 468-497 7.2e-19","Residues 386 to 448 match (1e-28) PD:PD469151 which is described as TRANSKETOLASE PROTEOME COMPLETE TRANSFERASE PYROPHOSPHATE THIAMINE TK FAMILY MULTIGENE PROBABLE ","","","","","","","","","","","Thu Jan 2 16:47:37 2003","Thu Jan 2 16:47:37 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01563 is paralogously related to AA02564 (5e-14), AA02565 (2e-07), AA01985 (6e-07) and AA02050 (4e-06).","","","","","","Residues 542 to 657 (E-value = 2e-16) place AA01563 in the Transketolase_C family which is described as Transketolase, C-terminal domain (PF02780)","","","","","Katayama A, Tsujii A, Wada A, Nishino T, Ishihama A. Systematic search for zinc-binding proteins in Escherichia coli. Eur J Biochem. 2002 May;269(9):2403-13. PMID: 11985624 Tatarko M, Romeo T. Disruption of a global regulatory gene to enhance central carbon flux into phenylalanine biosynthesis in Escherichia coli. Curr Microbiol. 2001 Jul;43(1):26-32. PMID: 11375660 Sprenger GA, Schorken U, Sprenger G, Sahm H. Transketolase A of Escherichia coli K12. Purification and properties of the enzyme from recombinant strains. Eur J Biochem. 1995 Jun 1;230(2):525-32. PMID: 7607225 Zhao G, Winkler ME. An Escherichia coli K-12 tktA tktB mutant deficient in transketolase activity requires pyridoxine (vitamin B6) as well as the aromatic amino acids and vitamins for growth. J Bacteriol. 1994 Oct;176(19):6134-8. PMID: 7928977","","Thu Jan 2 16:47:37 2003","1","","","" "AA01564","1050189","1049239","951","ATGACTAACCAGCTAGATTCTCTTCGTGAACTTACTACTGTGGTCGCCGATACCGGCGATATTGATGCAATTCGCCAATACAAACCGGAAGATGCGACAACTAACCCATCCCTGATTCTTAGTGCAGCAGCACTTCCACAATATGCCGCACTGATTGATGAAGCCATTACTTACGGCAAACAGAAAAGCCAAGATAAATCACAACAACTTATTGATGCGGAAGATAAATTAGCGGTAAACATCGGCTTAGAAATCTTAAAACTGGTGCCGGGTCGTGTTTCTACCGAAGTGGATGCCCGTCTTTCTTATGACACGCAAGCCACCGTTGCGAAAGCCAGAAAACTTATTGCCCTTTATGAAGCGGCAGGCATTAATAAAAACCGTATTTTGATTAAAATTGCGTCCACCTGGCAGGGTATCCGTGCCGCGGAAATTTTAGAAAAAGAAGGCATTAACTGTAACCTAACCCTATTATTCTCCGAAGCCCAAGCCCGTGCCTGTGCGGAAGCCGGTGTTTACTTAATTTCGCCGTTTGTCGGTCGTATTTTAGACTGGTATAAAGCCAATTCCGATAAGAAAGAATACGCACCGGCTGAAGATCTGGGCGTGATTTCCGTCACCAAAATCTACAATTATTACAAACAATACGGCTATAAAACAGTGGTCATGGGCGCCAGCTTCCGTAATGTCGGCGAAATCATCGAATTAGCCGGTTGTGACCGTTTAACCATCGCCCCGCCATTATTGAAAATCTTACACGAAACGCCAAATGCCGTTGTCAGAAAATTAGATTTCCAAGGTGAAGTTAAAGCTAAACCGCAGCCGTTAACCGAAACAGAGTTCTATTGGCAGCATAACAGCGATGCCATGGCGGTAGAAAAACTGGCGGAAGGTATTCGCAAATTTGCCGTTGACCAAGGCAAATTGGAAGAAATGTTACTGTCCAAATGG","","","35147","MTNQLDSLRELTTVVADTGDIDAIRQYKPEDATTNPSLILSAAALPQYAALIDEAITYGKQKSQDKSQQLIDAEDKLAVNIGLEILKLVPGRVSTEVDARLSYDTQATVAKARKLIALYEAAGINKNRILIKIASTWQGIRAAEILEKEGINCNLTLLFSEAQARACAEAGVYLISPFVGRILDWYKANSDKKEYAPAEDLGVISVTKIYNYYKQYGYKTVVMGASFRNVGEIIELAGCDRLTIAPPLLKILHETPNAVVRKLDFQGEVKAKPQPLTETEFYWQHNSDAMAVEKLAEGIRKFAVDQGKLEEMLLSKW","1049239","[FUNCTION] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway (by similarity). [CATALYTIC ACTIVITY] Sedoheptulose 7-phosphate + d-glyceraldehyde 3-phosphate = d-erythrose 4-phosphate + d-fructose 6-phosphate. [PATHWAY] Pentose phosphate pathway; nonoxidative part. [SUBCELLULAR LOCATION] Cytoplasmic (probable). [SIMILARITY] Belongs to the transaldolase family. subfamily 1. ","transaldolase B","Cytoplasm","","
InterPro
IPR001585
Family
Transaldolase
PTHR10683\"[1-317]TTRANSALDOLASE
PF00923\"[13-313]TTransaldolase
PS00958\"[129-146]TTRANSALDOLASE_2
PS01054\"[31-39]TTRANSALDOLASE_1
InterPro
IPR004730
Family
Transaldolase AB
PTHR10683:SF3\"[1-317]TTRANSALDOLASE 1
TIGR00874\"[3-317]TtalAB: transaldolase
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[2-317]Tno description


","BeTs to 17 clades of COG0176COG name: TransaldolaseFunctional Class: GThe phylogenetic pattern of COG0176 is --mp--yqvdrlbcefgh-nuj-i--Number of proteins in this genome belonging to this COG is","Significant hit (1.6e-105) to 6/6 blocks of the IPB001585 family, which is described as \"Transaldolase\". Interpro entry for IP:IPR001585. IPB001585A 24-39 2.2e-09 IPB001585B 90-112 4.5e-18 IPB001585C 129-142 4.6e-09 IPB001585D 149-184 3.1e-29 IPB001585E 200-228 2.4e-19 IPB001585F 286-309 9e-14","Residues 8 to 160 match (7e-08) PD:PD009632 which is described as TRANSALDOLASE TRANSFERASE SHUNT PENTOSE COMPLETE PROTEOME TRANSALDOLASE-LIKE ","","","","","","","","","","","Thu Jan 2 16:52:34 2003","Thu Jan 2 16:52:34 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01564 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 13 to 313 (E-value = 2.7e-162) place AA01564 in the Transaldolase family which is described as Transaldolase (PF00923)","","","","","Sprenger,G.A., Schorken,U., Sprenger,G. and Sahm,H. Transaldolase B of Escherichia coli K-12: cloning of its gene, talB, and characterization of the enzyme from recombinant strains.J. Bacteriol. 177 (20): 5930-5936 (1995) [PubMed: 7592346].Jia,J., Huang,W., Schorken,U., Sahm,H., Sprenger,G.A., Lindqvist,Y. and Schneider,G. Crystal structure of transaldolase B from Escherichia coli suggests a circular permutation of the alpha/beta barrel within the class Ialdolase family. Structure 4 (6): 715-724 (1996) [PubMed: 8805555].","","Thu Jan 2 16:52:34 2003","1","","","" "AA01565","1051027","1050851","177","GTGTGGCTGGCCATCCTCTCAGACCAGCTAGCGATCGTCGGCTTGGTAGGCCCTTACCCCACCAACTACCTAATCACACTTGGGTTCATCTCATGGCATGCGGCCATAAAGTCCCGCACTTTCGTCTCCCGACCCTACGCGGTATTAGCGACAGTTTCCCGTCGTTATCCCCCTCCA","","","6540","VWLAILSDQLAIVGLVGPYPTNYLITLGFISWHAAIKSRTFVSRPYAVLATVSRRYPPP","1050851","","conserved hypothetical protein","Cytoplasm","This sequence matches to gi|24113929, a predicted orf, partial conserved hypothetical protein from Shigella flexneri 2a str. 301. ","
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide
tmhmm\"[16-36]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 16:22:12 2004","Thu Feb 26 16:35:07 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA02422, AA02298, AA00622 and AA00413 all conserved hypothetical proteins.AA01565 is paralogously related to AA02422 (1e-30), AA02298 (1e-30), AA00622 (1e-30) and AA00413 (7e-30).","Thu Feb 26 16:35:07 2004","","","","","","","","","","","","","1","","","" "AA01566","1051951","1052151","201","ATGGCGTATACAGAGGGTAACCAACCAGCGATGGGGAGTGAATCTCAGAAAGTGCGTCTAAGTTCGGATTGGAGTCTGCAACTCGACTCCATGAAGTCGGAATCGCTAGTAATCGCGAATCAGAATGTTGCGGTGAATACGTTCCCGGGCCTTGTACACACCGCCCGTCACACCATGGGAGTGGGTTGTACCAGAAGTGGA","","","7166","MAYTEGNQPAMGSESQKVRLSSDWSLQLDSMKSESLVIANQNVAVNTFPGLVHTARHTMGVGCTRSG","1052151","","conserved hypothetical protein","Periplasm","This sequence is similar to gi|27359373, a predicted conserved hypothetical protein from Vibrio vulnificus CMCP6.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 16:17:20 2004","Thu Feb 26 16:17:20 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA02297 and to AA01261.AA01566 is paralogously related to AA02297 (7e-35), AA01261 (7e-35), AA00621 (7e-35), AA00412 (7e-35) and AA02421 (2e-27).","Thu Feb 26 16:17:20 2004","","","","","","","","","","","","","1","","","" "AA01567","1055275","1055084","192","ATGAGCCGACATCNAGGTGCCAAACACCGCCGTCGATATGAACTCTTGGGCGGTATCAGCCTGTTATCCCCGGAGTACCTTTTATCCGTTGAGCGATGGCCCTTCCATGCAGAACCACCGGATCACTATGACCTACTTTCGTACCTGCCCGACCTGTCCGTCTCGCAGTTAAGCTTGCTTATACCATTGCAC","","","7304","MSRHXGAKHRRRYELLGGISLLSPEYLLSVERWPFHAEPPDHYDLLSYLPDLSVSQLSLLIPLH","1055084","","conserved hypothetical protein (possible cell-wall-associated hydrolase)","Cytoplasm, Periplasm","This sequence is similar to gi|27363940, predicted cell wall-associated hydrolase from Vibrio vulnificus CMCP6.","
noIPR
unintegrated
unintegrated
PD293281\"[1-24]TQ8CME1_BBBBB_Q8CME1;


","No hits to the COGs database.","","Residues 1 to 42 match (8e-07) PD:PD293281 which is described as PROTEOME COMPLETE TC0114 ","","","","","","","","","","","","Thu Feb 26 16:12:35 2004","Thu Feb 26 16:14:53 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA02296.AA01567 is paralogously related to AA02296 (1e-33), AA01262 (1e-33), AA00620 (1e-33) and AA00411 (2e-12).","Thu Feb 26 16:09:19 2004","","","","","","","","","","","","","1","","","" "AA01568","1056992","1056177","816","ATGCCGTTATTACAAGTGGAAGATTTAACAAAATCCTTTAAGGGTAGCCTCGGCCTCTTTAGCTCCGGCTATTTTCACGCTGTGGAACAAATCAGCTTTAGTCTTGAAGCAGGTAACACCCTGGCAATTATCGGAAGAAACGGTTCAGGAAAATCAACCCTAGCAAAAATGATTGTAGGTATCACAAAACCCACATCAGGAAACATCTTGTTTAAAGACAATCCCCTCGTATTCGGCGATTATCATTATCGTGCCAAGCATATTCGCATGGTATTCCAAGATCCGAATACCGCCTTTAATCCGCGTCTAAATGTTGGTCAAGTGCTGGATGCCCCCCTACTTCTCACGACAAAATTTGATGAGCAGCAACGCAATCAGAAAATTTTTGATATTTTAAAACTCGTAGGAATGCACCCGGATCACACTAATATAAAAATCAATACGCTTTCCGTCAGCCAAAAGCAACGTATCGCCCTAGCCCGCGCACTGATTTTAAATCCGGAGGTCGTTATTATTGATGATGCACTTGGTTCATTAGATGCCACGGTAAAAACACAACTGACTAATCTCGTGTTGGAATTACAGAAAAAACTCAAACTTGCCTATATTTATGTCGGACAAAATCTCGGCATCATCAAACATATTGCCGATACGATTCTCGTGATGGAAGACGGGAAAATGATTGAATATGGCGACACGCATTCCTTATTTACTGCGCCTAAAACCGATGTAACCAAACGCCTCATTGAAAGCCATTTTGGTAAAATTCTGGATAATTCATCTTGGAAAAATGAAGATTTAGCCAATAAAGTGCGG","","","30284","MPLLQVEDLTKSFKGSLGLFSSGYFHAVEQISFSLEAGNTLAIIGRNGSGKSTLAKMIVGITKPTSGNILFKDNPLVFGDYHYRAKHIRMVFQDPNTAFNPRLNVGQVLDAPLLLTTKFDEQQRNQKIFDILKLVGMHPDHTNIKINTLSVSQKQRIALARALILNPEVVIIDDALGSLDATVKTQLTNLVLELQKKLKLAYIYVGQNLGIIKHIADTILVMEDGKMIEYGDTHSLFTAPKTDVTKRLIESHFGKILDNSSWKNEDLANKVR","1056175","[FUNCTION] Involved in a peptide intake transport system that plays a role in the resistance to antimicrobialpeptides. [SUBCELLULAR LOCATION] Inner membrane-associated (potential). [SIMILARITY] Belongs to the ABC transporter family","dipeptide transport system ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[148-191]TQ9CMB7_PASMU_Q9CMB7;
PF00005\"[38-225]TABC_tran
PS50893\"[4-249]TABC_TRANSPORTER_2
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[37-226]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[2-258]Tno description
PTHR19222\"[4-251]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF28\"[4-251]TOLIGOPEPTIDE ABC TRANSPORTER


","BeTs to 16 clades of COG1124COG name: ABC-type dipeptide/oligopeptide/nickel transport system, ATPase componentFunctional Class: E,PThe phylogenetic pattern of COG1124 is ao-pkz-qvd-lb-efgh--uj-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 6.8e-30) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 27-73 1.7e-16 IPB001140B 146-184 1.7e-11 IPB001140C 202-231 81","Residues 194 to 249 match (2e-09) PD:PD259958 which is described as ATP-BINDING COMPLETE PROTEOME ABC TRANSPORTER OLIGOPEPTIDE PEPTIDE TRANSPORTER NUCLEOTIDE BINDING/ATPASE ","","","","","","","","","","","Thu Jan 2 17:13:06 2003","Thu Jan 2 17:13:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01568 is paralogously related to AA02899 (4e-41), AA02898 (4e-33), AA00415 (8e-29), AA01051 (3e-24), AA00700 (3e-24), AA01656 (6e-23), AA02353 (1e-21), AA01645 (2e-21), AA02718 (1e-20), AA01524 (3e-20), AA02805 (1e-19), AA00858 (4e-19), AA01867 (6e-18), AA01779 (6e-18), AA01422 (1e-17), AA01616 (2e-17), AA00751 (2e-17), AA01456 (3e-17), AA00207 (5e-17), AA01569 (7e-17), AA00933 (1e-16), AA02786 (3e-16), AA02140 (3e-16), AA02320 (1e-14), AA02550 (2e-14), AA01820 (2e-14), AA02573 (3e-14), AA02225 (2e-13), AA02080 (3e-13), AA01961 (6e-13), AA01947 (1e-12), AA01509 (1e-12), AA02606 (1e-12), AA02642 (2e-12), AA02440 (2e-12), AA01510 (2e-12), AA02152 (8e-12), AA02324 (1e-11), AA01824 (7e-11), AA02331 (9e-11), AA01555 (2e-10), AA01684 (3e-10), AA02484 (6e-10), AA00799 (1e-09), AA01393 (1e-09), AA02609 (1e-08), AA01757 (4e-08), AA00591 (2e-07), AA00061 (2e-07), AA02226 (1e-06) and A02145 (5e-06).","","","","","","Residues 38 to 225 (E-value = 1.6e-47) place AA01568 in the ABC_tran family which is described as ABC transporter (PF00005)","","","",""," Parra-Lopez,C., Baer,M.T. and Groisman,E.A. Molecular genetic analysis of a locus required for resistance to antimicrobial peptides in Salmonella typhimurium. EMBO J. 12 (11): 4053-4062 (1993)[PubMed: 8223423].","","Thu Jan 2 17:13:06 2003","1","","","" "AA01569","1058048","1056999","1050","ATGGCTTTATTGGATATTCGTAACTTACGCATTGATATAAAAACGCCGGCAGGGTTTATTCGGATTGTTGATAACGTAAGTCTAACATTAAACGAAGGGGAAATTTGCGGCTTGGTCGGCGAATCCGGTTCCGGTAAAAGTTTAATTGCTAAAGTCATTTGCAATGCATTCAAAGATTCCTGGATTGTCACAGCTGACCGCTTTCGCTTTAACGACATCGAATTACTCAAGCTCACACCGCCCCAACGACGTAAAATCGTCGGTAAAGAAATTTCCATGGTATTTCAGGATCCGCTCACCTGTCTTGATCCCAGCCAAAAAATCGGCAAGCAACTGATTGAAAGTATCCCGAACTGGACGTTTAAAGGGCACTGGTGGCAGCGTTTATTCAATTGGAAAAAACGTCGCGCCATCGAATTATTGCATCGCGTAGGGATCAAAGAACACAAAGACATCATGGCCAGCTACCCGCACGAACTGACCGAAGGGGAAGGGCAAAAAGTGATGGTTGCCATCGCTGTGGCAAACCAACCGCGTTTACTTATTGCCGACGAACCGGCAAATTCCGTGGAATCCATTACAAGGGTACAAATATTCCGCCTTCTATCCAGCATGAATCAAAACCAAGGCACTTCTATTTTGCTTGCCAGCAATGATATTAATAGTATTAGTGAATGGTGTGATTCTTTTATTGTGCTTTATTCCGGGCAAAACGCGGAATCAGGACCAAAAGAAAATATTTTGGAAAACCCTCATCATCCTTACACGCAAGCCTTGTTGCATTCCATCCCGGATTTTACACAGCCCTTACCGTTTAAAGGCTATCTGGGTACATTAAAGGGGTCGGTACCATTATTGGAGCAAATGCCGATCGGTTGTCGTCTCGGTCCGCGTTGCCCTTTCGCGCAAAAAAAATGTATCGTAAAACCGACCGCACTTCGTATTAAACAACATGAATTTTTCTGCCATTTCCCGATTAATTTACGGGAAAAGAAAATCAAAGAAAAAGAGCAAATTCAACCGCTCACCCTAAACACCGATAAACAGGAA","","","39709","MALLDIRNLRIDIKTPAGFIRIVDNVSLTLNEGEICGLVGESGSGKSLIAKVICNAFKDSWIVTADRFRFNDIELLKLTPPQRRKIVGKEISMVFQDPLTCLDPSQKIGKQLIESIPNWTFKGHWWQRLFNWKKRRAIELLHRVGIKEHKDIMASYPHELTEGEGQKVMVAIAVANQPRLLIADEPANSVESITRVQIFRLLSSMNQNQGTSILLASNDINSISEWCDSFIVLYSGQNAESGPKENILENPHHPYTQALLHSIPDFTQPLPFKGYLGTLKGSVPLLEQMPIGCRLGPRCPFAQKKCIVKPTALRIKQHEFFCHFPINLREKKIKEKEQIQPLTLNTDKQE","1056997","[FUNCTION] Involved in a peptide intake transport system thatplays a role in the resistance to antimicrobial peptides. [SUBCELLULAR LOCATION] Inner membrane-associated (potential).[SIMILARITY] Belongs to the ABC transporter family","dipeptide transport ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[163-202]TQ9CMB8_PASMU_Q9CMB8;
PF00005\"[33-236]TABC_tran
PS50893\"[4-260]TABC_TRANSPORTER_2
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[32-236]TAAA
InterPro
IPR010066
Domain
Oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal
TIGR01727\"[237-324]Toligo_HPY: oligopeptide/dipeptide ABC trans
InterPro
IPR013563
Domain
Oligopeptide/dipeptide ABC transporter, C-terminal
PF08352\"[239-306]Toligo_HPY
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[3-269]Tno description
PTHR19222\"[4-329]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF28\"[4-329]TOLIGOPEPTIDE ABC TRANSPORTER


","BeTs to 16 clades of COG0444COG name: ABC-type dipeptide/oligopeptide/nickel transport system, ATPase componentFunctional Class: E,PThe phylogenetic pattern of COG0444 is ao-pkz-qvd-lb-efgh--uj-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 6.2e-13) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 22-68 7.1e-07 IPB001140B 157-195 0.00067 IPB001140C 213-242 1.6e+02","Residues 80 to 116 match (1e-08) PD:PD000720 which is described as ATP-BINDING PROTEOME COMPLETE ABC TRANSPORTER OLIGOPEPTIDE TRANSPORTER PEPTIDE DIPEPTIDE PLASMID ","","","","","","","","","","","Thu Jan 2 17:17:13 2003","Thu Jan 2 17:17:13 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01569 is paralogously related to AA02898 (5e-54), AA02899 (2e-31), AA00415 (5e-21), AA01568 (9e-17), AA01684 (4e-16), AA01616 (4e-14), AA01524 (5e-14), AA01422 (1e-13), AA02353 (2e-13), AA00858 (2e-13), AA02320 (1e-12), AA01051 (1e-12), AA00207 (2e-12), AA02080 (2e-12), AA02550 (3e-12), AA02225 (3e-12), AA02718 (5e-12), AA01820 (7e-12), AA01656 (9e-12), AA01779 (2e-11), AA02805 (3e-11), AA02440 (3e-11), AA00700 (1e-10), AA01456 (1e-10), AA01824 (5e-10), AA02152 (1e-09), AA02786 (2e-09), AA00799 (3e-09), AA01510 (4e-09), AA02140 (1e-08), AA02324 (3e-08), AA00933 (1e-07), AA01961 (2e-07), AA00751 (2e-06), AA01645 (3e-06), AA01867 (5e-06), AA01393 (9e-06), AA01947 (1e-05), AA01555 (2e-05), AA02642 (5e-05), AA01757 (8e-05), AA00934 (1e-04) and AA02484 (4e-04).","","","","","","Residues 33 to 236 (E-value = 5.3e-42) place AA01569 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Parra-Lopez,C., Baer,M.T. and Groisman,E.A. Molecular genetic analysis of a locus required for resistanceto antimicrobial peptides in Salmonella typhimurium. EMBO J. 12 (11): 4053-4062 (1993) [PubMed: 8223423].Abouhamad,W.N. and Manson,M.D. The dipeptide permease of Escherichia coli closely resembles other bacterial transport systems and shows growth-phase-dependent expression Molecular microbiology. 14 (5), 1077-1092 (1994) PubMed: 7536291 ","","Thu Jan 2 17:17:13 2003","1","","","" "AA01571","1058943","1058059","885","ATGCAAGATAGAGAACCGAAAGACTTTCGTGAAACTGCGACCTTAAAACATATTTGGCAGTTATTTCGTAAAGACCGCATTGCGTTATTCGGCTTCTACGCATTTTTACTGCTAATTTTGACCGCACTTTTCGGACCATTACTTGCGCCTTATCCAAGTGAAATGCAATTTGTCGGCAAAGAACTGACACCGCCTTCTTGGGCAAGTGATGGGCAAATAGCCTACTTCTTTGGCACCGATGATATTGGACGCGACGTATTCAGTCGTATACTTATCGGCACCAGCTATACCGTCGGCGCCGCGGTTATTGTCGCCATGATGACCGCCCTTGTCGGTGGTGGACTGGGCATTTTGGCAGGAATGTCACAAGGGATTAAATCCCGTGTTTTAGGACATTTTCTTGATGCGTTTCTCACTATTCCGGTACTTTTAGTGGCAATTATTATTGCGACACTCATGGAACCGAGTTTAATCAACGCAATGTTATCAATAGGATTGGCGTTATTGCCGTATTTCGTACATGAAATTTATCTCAGCATTCAGCAGGAATTAAAGAAAGAATACGTGCTTATGTTGCGTCTGGATGGCATTTCAAAGCGACTTTTGTTAAAGGATACCATCTTACCAAATATTGCCACCCGCTATATTCAGGAAATTTCCCGTGCCTTCAATATTGCCATTCTGGATATCAGCGCATTAAGTTTTATCGCCCTCGGCGCACAACGTCCCGCACCGGAATGGGGCGCGATAATCCAAGATTCTTTAGAGCTGATTTACCTCGCTCCTTGGACTGTGATTTTACCCGGGCTGGCGATCATTCTGAGCGTATTAATCAGCTTAATTTTCACCAACGGGCTCTGCAAAGCCATTGATAAATATTATGAG","","","32655","MQDREPKDFRETATLKHIWQLFRKDRIALFGFYAFLLLILTALFGPLLAPYPSEMQFVGKELTPPSWASDGQIAYFFGTDDIGRDVFSRILIGTSYTVGAAVIVAMMTALVGGGLGILAGMSQGIKSRVLGHFLDAFLTIPVLLVAIIIATLMEPSLINAMLSIGLALLPYFVHEIYLSIQQELKKEYVLMLRLDGISKRLLLKDTILPNIATRYIQEISRAFNIAILDISALSFIALGAQRPAPEWGAIIQDSLELIYLAPWTVILPGLAIILSVLISLIFTNGLCKAIDKYYE","1058057","[FUNCTION] Involved in a peptide intake transport system that plays a role in the resistance to antimicrobial peptides. [SUBCELLULAR LOCATION] Integral membrane protein. inner membrane (potential). [SIMILARITY] Belongs to the binding-protein-dependent transport system permease family. OppBC subfamily. ","peptide transport system permease","Inner membrane, Cytoplasm","","
InterPro
IPR000515
Family
Binding-protein-dependent transport systems inner membrane component
PF00528\"[94-295]TBPD_transp_1
PS50928\"[94-283]TABC_TM1
noIPR
unintegrated
unintegrated
signalp\"[1-49]?signal-peptide
tmhmm\"[29-49]?\"[96-118]?\"[133-153]?\"[259-281]?transmembrane_regions


","No hits to the COGs database.","","Residues 96 to 155 match (7e-07) PD:PD383691 which is described as COMPLETE PEPTIDE SAPC PROTEOME INNER PERMEASE SYSTEM TRANSMEMBRANE MEMBRANE ","","","","","","","","","","","Thu Jan 2 17:26:00 2003","Thu Jan 2 17:26:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01571 is paralogously related to AA02897 (1e-20).","","","","","","Residues 94 to 295 (E-value = 2.9e-36) place AA01571 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component (PF00528)","","","","","Lopez-Solanilla,E., Garcia-Olmedo,F. and Rodriguez-Palenzuela,P. Inactivation of the sapA to sapF locus of Erwinia chrysanthemi reveals common features in plant and animal bacterial pathogenesis. Plant Cell 10(6): 917-924, 1998. PubMed: 9634580. Chen HY, Weng SF, Lin JW. Identification and analysis of the sap genes from Vibrio fischeri belonging to the ATP-binding cassette gene family required for peptide transport and resistance to antimicrobial peptides. Biochem Biophys Res Commun. 2000 Mar 24;269(3):743-8. PMID: 10720487 ","","Thu Jan 2 17:26:00 2003","1","","","" "AA01572","1059898","1058936","963","ATGTTTAATTCACTGATTCGGCAATGTGTTTTTCTCGTTTTAACGTCAATTATCCTCACATTGATAAGTTACGTTATTTTAATGCAGGATCCATTAAATGCCGAACTGGCGACACCGTATTTTTACAATGGCTACCTTAATTATTTAGGCAACCTTACCCGTGGTGATTTAGGTATCAGTTACAATGGCGGGCAGCTGTTAAAATCCACGATTTTTACTGTTTTACCCCCCACCCTTGAATTGTGCTTTTGTGCCATTTTGTTGGCGGTGCTGTTCGGCATTCCTCTTGGTTTATTAGGTGCCATTTACCAATCACATTTCATCGGAAAAACCACCCGCACTTTATCTTCCATGGGATTGGCCATGCCAGTCTTCTGGATTGCACCGATTTTATTATACGCCTCCGCGATAAATGGTTGGGAAATCGCCGCAATCGGGCAATACAATTTACTCTATGAAATTAAACCGATAACCGGTTTCCCTATTATTGACGTATGGTTTGTCGAAGCGCCTTATCGGCTCAAAATCATTCAAAACGTGCTGCAACATTTGGCATTGCCCAGCTTAGTGTTAACCATCCTGCCGACAATGGAAATTGTCCGTTTTGTGCAGCAACAAGCGGAAACTATTTTTCAGCAAAATTACGTTAAAGTGGCCGCCACTCGCGGTTGGTCAAAATTTAAGATGCTACGCAAATATATTTTACGCAATACCCTGCCTCTGCTTATTCCGCAAATGACCCGTTTATTCACCTTGGTCATCACACAATGTATGCTGGTAGAAAGCACCCTCGGCTGGCCGGGGATCGGGCGCTGGCTTATTGATTCGGTCACCCAGCAGGATTACAACAGTATTTCGGCAGGTATTATTACTATCGGATCATGTATTATCTTCATCAAATTATTCTCCGAAAGCTTAATCTTTATTTTGGATCCGTTAAATAAGAAGGGTTGGTATGCAAGA","","","36191","MFNSLIRQCVFLVLTSIILTLISYVILMQDPLNAELATPYFYNGYLNYLGNLTRGDLGISYNGGQLLKSTIFTVLPPTLELCFCAILLAVLFGIPLGLLGAIYQSHFIGKTTRTLSSMGLAMPVFWIAPILLYASAINGWEIAAIGQYNLLYEIKPITGFPIIDVWFVEAPYRLKIIQNVLQHLALPSLVLTILPTMEIVRFVQQQAETIFQQNYVKVAATRGWSKFKMLRKYILRNTLPLLIPQMTRLFTLVITQCMLVESTLGWPGIGRWLIDSVTQQDYNSISAGIITIGSCIIFIKLFSESLIFILDPLNKKGWYAR","1058934","[FUNCTION] Involved in a peptide intake transport system thatplays a role in the resistance to antimicrobial peptides. [SUBCELLULAR LOCATION] Inner membrane-associated (potential).[SIMILARITY] Belongs to the binding-protein-dependenttransport system permease family. OppBC subfamily. ","peptide ABC transporter, permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR000515
Family
Binding-protein-dependent transport systems inner membrane component
PF00528\"[75-316]TBPD_transp_1
PS50928\"[75-308]TABC_TM1
noIPR
unintegrated
unintegrated
signalp\"[1-27]?signal-peptide
tmhmm\"[10-28]?\"[81-103]?\"[124-144]?\"[282-302]?transmembrane_regions


","No hits to the COGs database.","","Residues 148 to 187 match (3e-11) PD:PD077001 which is described as PEPTIDE COMPLETE PROTEOME SAPB PERMEASE SYSTEM INNER MEMBRANE TRANSMEMBRANE ABC ","","","","","","","","","","","Thu Jan 2 17:29:53 2003","Thu Jan 2 17:29:53 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01572 is paralogously related to AA02895 (2e-17).","","","","","","Residues 75 to 316 (E-value = 3.3e-42) place AA01572 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component (PF00528)","","","","","Lopez-Solanilla,E., Garcia-Olmedo,F. andRodriguez-Palenzuela,P. Inactivation of the sapA to sapF locus of Erwinia chrysanthemi reveals common features in plant and animal bacterial pathogenesis. Plant Cell 10(6): 917-924, 1998. PubMed: 9634580. Chen HY, Weng SF, Lin JW. Identification and analysis of the sap genes from Vibrio fischeri belonging to the ATP-binding cassette gene family required for peptide transport and resistance to antimicrobial peptides. Biochem Biophys Res Commun. 2000 Mar 24;269(3):743-8. PMID: 10720487 ","","Thu Jan 2 17:29:53 2003","1","","","" "AA01573","1061514","1059901","1614","GTGCCGGAAGAGTTGACAAACAACGGATTGATTTATTGTACTCATGCTTCCGGTTTTTCTTTTAATCCGCAAACCGCCGATGCCGGCACCAGCATGAATGTAGTCACCGAGCAGATTTATAATAAACTTTTTGAAATATCCAATACCAGTGCGGCGCCAACGCCGGTATTGGCGCAATCCTATTCTCTCTCGCCTGACGGCAAAGTCATTACAATTCATTTACGCAGGGGCATTAAATTTCATCACACCGATTGGTTTAAACCGACCCGTGATTTCAATGCCGATGATGTGGTTTTTTCGCTAAATCGCGTGCTGGGCTATGAAACCTATTTACCGACCTTAGAACAGACCTCGGTCAGCTATAAAAATCCTCAGTATCGCATCTTTCACGAACAGGCAAAAAAGGTGCGTTTTCCTTATTTTGAAAGCATTAAATTGAATCAAAAAATCGAATCGGTAAAAGCCATTAATCCGCATACAGTGGAAATTATCTTATTTAAACCGGATTCCTCCATTTTGTCCCATTTGGCAAGCCAGTACGCCATTATTTTCTCGCAGGAATATGCCGTACAGCTCAATGCGGACGACAACTTGGTACAATTGGATACATTGCCCGTGGGAACCGGTCCGTATAAAGTGAAAAATTACTTTCGTAACCAATATGTGCGTTTAGAAAAAAATACAGATTATTGGAAAAAAGACGCCAAAATTAACGACATCATTATTGACCTCTCAACGGATCGTACGGGGCGGTTGATTAAATTTTTCAATGGCGAATGCCAGATTGCGTCCTATCCCGAAGTCAGCCAACTGGGCTTATTACGGGAAAATGACGAACGTTATTACATTAAAAGTGTCGAAGGCATGAATTTGGCGTATCTGGCGTTTAATTTCCAAAAAACTGCCCTTCAAGACGAGCAATTACGCCGCGCTATCTCGCAAGCGATTAATCGACAAAGGATTATTAAAACCATTTATCACAATACGGCAACCGTGGCGAATAATATCATCCCGAACATTTCTTGGGCTTCCGCGGTGAATACTCCCGATTTTGACTATGATTATAATCCGCAACAGGCGAAGAGAATCTTACAGGATAAAAAGTTAAGCCTGAGTATGTGGGTGATTAATGAAGAACAGGTGTATAACCCTGCGCCATTAAAAACCGCAGAACTCATCAAAGCAGATTTAACAAATGCTGGTGTTGAGGTTAATATTCGTTCTGTCACCCGCACCTTTTTAATCGAGCAATTACATAAAAAAGCCGAAGATTACGACATGATTTTAACCGGTTGGCTGGGGGGAAATTTAGATCCGGACAGTTTTATGCGCCCGATTTTAAGTTGCAGCACCTCAAATGAAATTACCAACTTATCCAACTGGTGCAGCGAAAAATTTGATCAAATTATGGATGAGGCATTGGATACTTCCAATCAGCGCGTACGCTCCGCTGCTTATAATCAGGCACAGACGTTAATTTTATCGGAGTTACCAATCATTCCGATCGCGAACGTTAAGCGGGTTCTCGTCGCCAGTTCGCGTGTTCAAAATATCGACATGAGTCCGTTCGGTAGCCTGAACTTTTCAACCCTCTCCCTGCGAAAAGGGCACAAA","","","63970","VPEELTNNGLIYCTHASGFSFNPQTADAGTSMNVVTEQIYNKLFEISNTSAAPTPVLAQSYSLSPDGKVITIHLRRGIKFHHTDWFKPTRDFNADDVVFSLNRVLGYETYLPTLEQTSVSYKNPQYRIFHEQAKKVRFPYFESIKLNQKIESVKAINPHTVEIILFKPDSSILSHLASQYAIIFSQEYAVQLNADDNLVQLDTLPVGTGPYKVKNYFRNQYVRLEKNTDYWKKDAKINDIIIDLSTDRTGRLIKFFNGECQIASYPEVSQLGLLRENDERYYIKSVEGMNLAYLAFNFQKTALQDEQLRRAISQAINRQRIIKTIYHNTATVANNIIPNISWASAVNTPDFDYDYNPQQAKRILQDKKLSLSMWVINEEQVYNPAPLKTAELIKADLTNAGVEVNIRSVTRTFLIEQLHKKAEDYDMILTGWLGGNLDPDSFMRPILSCSTSNEITNLSNWCSEKFDQIMDEALDTSNQRVRSAAYNQAQTLILSELPIIPIANVKRVLVASSRVQNIDMSPFGSLNFSTLSLRKGHK","1059899","[FUNCTION] Involved in a peptide intake transport systemthat plays a role in the resistance to antimicrobial peptides. [SUBCELLULAR LOCATION] Integral membrane protein. inner membrane (potential). [SIMILARITY] Belongs to the binding-protein-dependent transport system permease family. OppBC subfamily. ","peptide transport periplasmic protein","Periplasm, Outer membrane, Cytoplasm","","
InterPro
IPR000463
Domain
Cytosolic fatty-acid binding
PS00214\"[97-114]?FABP
InterPro
IPR000914
Family
Bacterial extracellular solute-binding protein, family 5
PF00496\"[52-454]TSBP_bac_5
PS01040\"[58-80]TSBP_BACTERIAL_5
noIPR
unintegrated
unintegrated
G3DSA:3.10.105.10\"[287-502]Tno description
G3DSA:3.90.76.10\"[8-204]Tno description


","BeTs to 20 clades of COG0747COG name: ABC-type dipeptide/oligopeptide/nickel transport systems, periplasmic componentsFunctional Class: E,PThe phylogenetic pattern of COG0747 is ao-pkz-qvdrlbcefgh--uj-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 4.7e-06) to 2/3 blocks of the IPB000914 family, which is described as \"Bacterial extracellular solute-binding protein, family 5\". Interpro entry for IP:IPR000914. IPB000914A 55-62 1.5e+02 IPB000914B 66-83 1.5e-05","Residues 461 to 529 match (5e-08) PD:PD003939 which is described as PROTEOME COMPLETE PERIPLASMIC ABC PEPTIDE DIPEPTIDE BINDING PROBABLE COMPONENT TRANSPORTER ","","","","","","","","","","","Thu Jan 2 17:33:22 2003","Thu Jan 2 17:33:22 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01573 is paralogously related to AA00458 (2e-28), AA02891 (2e-07), AA01607 (9e-06) and AA02892 (8e-04).","","","","","","Residues 1 to 533 (E-value = 1e-179) place AA01573 in the SBP_bac_5 family which is described as Bacterial extracellular solute-binding proteins, family 5 (PF00496)","","","","","Chen HY, Weng SF, Lin JW. Identification and analysis of the sap genes from Vibrio fischeri belonging to the ATP-binding cassette gene family required for peptide transport and resistance to antimicrobial peptides. Biochem Biophys Res Commun. 2000 Mar 24;269(3):743-8.PMID: 10720487 Lopez-Solanilla,E., Garcia-Olmedo,F. and Rodriguez-Palenzuela,P. Inactivation of the sapA to sapF locus of Erwinia chrysanthemi reveals common features in plant and animal bacterial pathogenesis. Plant Cell 10(6): 917-924, 1998. PubMed: 9634580. ","","Thu Jan 2 17:33:22 2003","1","","","" "AA01575","1061804","1063207","1404","ATGCTAAATCATTTGCAAAAAGAATTAAACGATCTGGTTAATCGCGGATTAGACCGCACTTTACGCATTGCTGTGACAGGGTTGAGTCGAAGCGGGAAAACTGCTTTTATCACCAGCCTTATTAACCAATTGTTACATATCAATCGCGTGGATAATAGCCATCTGCCGCTCTTTGATGCGGCGCGGCGGCGCGGGATTATTGCGGTAAAACGTATTCCTCAACCGGATTTATCCGTTCCCCGTTTTGATTATGATGGCAATCTCAATGCCTTGTCGCAGCAACCGCCTGTTTGGCCGCAATCTACCAGAAGTGTAAGCGAAACCCGACTGGCGATTCGTTATCAGCGTAGTTCGGGCTTATTGCGTCATGTTAAAGAAAAAGGCACGTTGTATCTGGATATTTTTGACTATCCGGGCGAATGGCTGTTGGATTTGCCTTTGCTGGAACTGGATTTTCAACAGTGGTCGCAGGAATTGCAACGACAGCTCAATGCGACTCATCTGCAACTGGCGCAACCTTGGTTGGAGAAAACAAAGAAAATCAATTTAACCGATGTTGCCGATGAAGACATTTTGGCGCAACTTGCCAAAGACTACACGGACTATCTATGGCAGTGTAAAAAACACGGATTGCATTTTATTCAGCCAGGGCGATTTGTGTTACCCGGTGAATTGGATGGCGCACCTGCCTTGCAATTCTTTCCTTTGTTACATTTAACCGAGTCACAATGGCAGCAGCTGAAAAAAGAGGCAAAAGAGAACAGTTATTTTGTCGTGCTACGAAAACGCTACGATTATTACCGTCGGCGTATTGTGAAAGATTTCTATGAAAATTACTTTTCCACTTTTGATCGGCAGGTGATTCTGGCGGATTGTTTAACGCCCTTGAATCACAGCCGTGAAGCCTTCGGCGATATGCAGCTGGCGTTACATCAGCTGTTTCGGAATTTTCACTATGGAAAGCGCCATTTTCTTAATCGCCTTTTTTCACCGAAAATCGATAAATTGATGTTTATCGCAACCAAGGCGGATCACATCACGACCGATCAATTTCCCAATTTAGTCAATCTTATGCGCCAATTAGTCCAGGAAGGCGGGCGCTATGTGGAATTTGCCGATATTGCCACCGATTACACCGCCATTGCTGCCATTCGGGCGACGCAACAGGTGGTGGTGAACCAAAACGGTCGCCAATTTAAAGCTATTCAGGGCGTTCGTAGTAGCGATCAGCAGAAGGTGACGCTTTATCCCGGTAGCGTACCGAGTAAATTGCCGAGCGCCGATTTTTGGCAAACCCGGAAATTTGAATTTGACCAATTTGAACCACACCGTTTAGAACAGGGCGAAAATATACCGCACTTACGTATGGATGCCGTGTTGCAGTTTTTGCTGGGCGATAAGTTA","","","54909","MLNHLQKELNDLVNRGLDRTLRIAVTGLSRSGKTAFITSLINQLLHINRVDNSHLPLFDAARRRGIIAVKRIPQPDLSVPRFDYDGNLNALSQQPPVWPQSTRSVSETRLAIRYQRSSGLLRHVKEKGTLYLDIFDYPGEWLLDLPLLELDFQQWSQELQRQLNATHLQLAQPWLEKTKKINLTDVADEDILAQLAKDYTDYLWQCKKHGLHFIQPGRFVLPGELDGAPALQFFPLLHLTESQWQQLKKEAKENSYFVVLRKRYDYYRRRIVKDFYENYFSTFDRQVILADCLTPLNHSREAFGDMQLALHQLFRNFHYGKRHFLNRLFSPKIDKLMFIATKADHITTDQFPNLVNLMRQLVQEGGRYVEFADIATDYTAIAAIRATQQVVVNQNGRQFKAIQGVRSSDQQKVTLYPGSVPSKLPSADFWQTRKFEFDQFEPHRLEQGENIPHLRMDAVLQFLLGDKL","1063205","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR007413
Family
Protein of unknown function DUF463, YcjX-like protein
PF04317\"[2-468]TDUF463
noIPR
unintegrated
unintegrated
PD042940\"[306-467]TQ9CMC2_PASMU_Q9CMC2;


","BeTs to 3 clades of COG3106COG name: Predicted ATPaseFunctional Class: RThe phylogenetic pattern of COG3106 is --------------e-gh---j----Number of proteins in this genome belonging to this COG is","","Residues 5 to 467 match (3e-183) PD:PD042940 which is described as COMPLETE PROTEOME ATP-BINDING YCJX REGULATED PM0910 ATU1357 R01806 MLR0775 VC1306 ","","","","","","","","","","","","Thu Jan 2 17:35:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01575 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01577","1063224","1064300","1077","ATGGATAAAAAAATGTTTGACCAAGCCGATGACCTAGAACAACAAGATGCCTTTATTGCCAAACAGGAATTCCGTGAAGAGCAGGCAGTGCCGGATACGGAAGCGGAAAATGTCGTATTGGACGGGGAACTGTTGGAAGATCAATTTGAACAAAGCATTCAACCGACACCCCGCTGGTGGAAACGCGTACTTACCGGCACCGCATTTTTGTTTTTGACGGCGACGGTGGCGCAATCGGTGCAATGGCTGATCGATACCTGGCAACAAAATCAGTGGATCTATTTTGTGTTTTCCTTGGTGTTGTGTTTGGCGGTATTGCTTGGTTTATCCGCAATCATCGGCGAATGGCGACGCTTGGTGCTGCTACGGAAACGTGGCGAAATGCAAAATCAAAGCCGCGAATTGCTCAAAAGTGCGGTCGTTTTTCCGGGGGAATTTTCAAGTGCAAGCAATCAACAAGCGGTTGGGCTATGTGAACAAATCGGCAAACTGATGCACCTTGAATCACAGCAAGATGGCTTCACTCAATGGCGACAGCAGGTGAATGAATCTTATTCGGCTCCTGAAGTGTTGCATTTGTTTAGCCAGAATGTACTGCAATCTTTTGATAAACAAGCAAAAAAACTGGTTAACAAAGCCACTGCTGAATCGGCGGCTTTGGTGGCAATCAGCCCATTGGCGTTGGCGGATATGTTTTTTATCGCGTGGCGTAATATTCGCTTGGTAAATCAAATTGCGTGTCTTTACGGCATTGAGCTGGGCTATATCAGTCGTCTCCGTTTATTGCGTATAGTATTGGTGAATATGGCATTTGCCGGTGCGACAGAATTAATTCAGGATCTTGGCGTGAATTGGCTTTCGCAAGATCTTACTGCCAAACTTTCTGCCCGAATGGCACAGGGCATTGGCGTCGGTTTGCTAACCGCCCGTTTGGGGATTAAAGCCATGGAATTTTGTCGTCCGCTGGCATTTCAAGCCGATGAAAAACCGCGTTTATTGCAAATTCATAAGGAATTATTAAGCCATCTCGGCTCAACTATTTTTGATAATGTAAAATTTAAACAGAAAGATAAAGTG","","","42731","MDKKMFDQADDLEQQDAFIAKQEFREEQAVPDTEAENVVLDGELLEDQFEQSIQPTPRWWKRVLTGTAFLFLTATVAQSVQWLIDTWQQNQWIYFVFSLVLCLAVLLGLSAIIGEWRRLVLLRKRGEMQNQSRELLKSAVVFPGEFSSASNQQAVGLCEQIGKLMHLESQQDGFTQWRQQVNESYSAPEVLHLFSQNVLQSFDKQAKKLVNKATAESAALVAISPLALADMFFIAWRNIRLVNQIACLYGIELGYISRLRLLRIVLVNMAFAGATELIQDLGVNWLSQDLTAKLSARMAQGIGVGLLTARLGIKAMEFCRPLAFQADEKPRLLQIHKELLSHLGSTIFDNVKFKQKDKV","1064298","","conserved hypothetical transmembrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR002345
Domain
Lipocalin
PS00213\"[108-119]?LIPOCALIN
InterPro
IPR006507
Family
Conserved hypothetical protein 1620
PF05128\"[47-344]TDUF697
TIGR01620\"[47-344]Thyp_HI0043: conserved hypothetical protein
noIPR
unintegrated
unintegrated
PD041583\"[2-352]TY909_PASMU_Q9CMC3;
tmhmm\"[63-83]?\"[93-113]?\"[241-259]?transmembrane_regions


","No hits to the COGs database.","","Residues 39 to 346 match (5e-86) PD:PD041583 which is described as PROTEOME COMPLETE MEMBRANE TRANSMEMBRANE YCJF PM0909 ATU1356 SMC00466 HI0043 MLR0776 ","","","","","","","","","","","","Thu Jan 2 17:40:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01577 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 47 to 344 (E-value = 9.3e-153) place AA01577 in the DUF697 family which is described as Family of unknown function (DUF697) (PF05128)","","","","","","","","1","","","" "AA01579","1064387","1065343","957","ATGGCAACTTCTTCAACCACCGATCCTTTTTCACACATCGTCAGCCGAAATCCGCGAATGCGGGATGTTATTGCGAAAGCCAGAAAATTTGCGTTATTGGATGCGCCGTTGGTGATTCAAGGTGAAACCGGCACGGGAAAAGACGTGATTGCCAAAGCCTGCCATGATTTTAGTGCGCGCCGAAATAAAGCATTTCTCGCCGTAAACTGTGCCGGCATTCCCGGCGAAGACGCGGAAACGGAAATGTTCGGGCGGCGTAATAAAGATGGTGAATTTATCGGTTTTTTTGAATATGCCGATGGCGGCACGGTGTTGTTAGATGGTGTTGAGGAGTTGCCTCTGACTTTGCAGGCGAAGCTTCTGCGTTTTTTAAGCGACGGTACTTTCCGCCGTGTCGGAGAGGAAGAGGAGCATTATGCCAATGTACGTGTGATTTGCACGGCGCAGCAGCCGTTACAGCATTATGTCGAGCAGGGTAAAATGCGTAGCGATTTGTTCCATCGGCTAAACGTGCTGACGTTAAACCTGCCGTTGCTGCGTGAGCGCGTGGAAGATATTGAGCCTCTTGCCTGCCAATTTATTGCTGAAATCAGTGAAAAACTCGGCATTTCCGCACCGCACTTTGATGCCGAATTTTTGCATTATCTTCAACAATATCCTTGGTTTGGTAACATTCGTGAACTTTATAACGCGCTGTATCGTGCCGTTTCGTTAGCCAAAGAAAATCGTTTACTTATTGAAGATTTAGGGCTGGAGACGCAAGTTTCTACATCTCAGGCTATAGATGATCTTGTTCTGGAAGGTGAAACTTTAGAGGAAATCATGGGGCGATTTGAAGCGGCGGTGTTAAATAAATTTTATGCGAAATATCCCAGCTCCAGAAAACTTGCCGCCCGTTTAGGCGTATCTCACACGGCAATCGCCAATAAATTACGCCAATATGGCATTGGCAAATCT","","","35813","MATSSTTDPFSHIVSRNPRMRDVIAKARKFALLDAPLVIQGETGTGKDVIAKACHDFSARRNKAFLAVNCAGIPGEDAETEMFGRRNKDGEFIGFFEYADGGTVLLDGVEELPLTLQAKLLRFLSDGTFRRVGEEEEHYANVRVICTAQQPLQHYVEQGKMRSDLFHRLNVLTLNLPLLRERVEDIEPLACQFIAEISEKLGISAPHFDAEFLHYLQQYPWFGNIRELYNALYRAVSLAKENRLLIEDLGLETQVSTSQAIDDLVLEGETLEEIMGRFEAAVLNKFYAKYPSSRKLAARLGVSHTAIANKLRQYGIGKS","1065341","[FUNCTION] Involved in transcriptional regulation of aromatic amino acid biosynthesis and transport. Modulates the expression of at least 8 unlinked operons. Seven of these operons are regulated in response to changes in the concentration of the three aromatic amino acids (phenylalanine, tyrosine and tryptophan). These amino acids are suggested to act as co-effectors which bind to the tyrR protein to form an active regulatory protein. In most cases tyrR causes negative regulation, but positive effects on the tyrP gene have been observed at high phenylalanine concentrations (by similarity). [SUBUNIT] Homodimer. In presence of tyrosine (to the lesser extent, phenylalanine or tryptophan) and excess of ATP it undergoes a ligand-induced hexamerization. It is suggested that the hexameric form of tyrR is the active repressing species, interacting with two or three tyrR boxes in the targeted regulatory DNA (By similarity).","transcriptional regulatory protein","Cytoplasm","","
InterPro
IPR002078
Domain
RNA polymerase sigma factor 54, interaction
PF00158\"[13-229]TSigma54_activat
PS50045\"[13-237]TSIGMA54_INTERACT_4
PS00675\"[37-50]TSIGMA54_INTERACT_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[33-179]TAAA
InterPro
IPR012287
Domain
Homeodomain-related
G3DSA:1.10.10.60\"[258-318]Tno description
noIPR
unintegrated
unintegrated
G3DSA:1.10.8.60\"[181-256]Tno description
G3DSA:3.40.50.300\"[11-180]Tno description


","No hits to the COGs database.","Significant hit ( 4.9e-38) to 3/3 blocks of the IPB002078 family, which is described as \"Sigma-54 factor interaction protein family\". Interpro entry for IP:IPR002078. IPB002078A 37-71 3.2e-18 IPB002078B 159-189 4.6e-13 IPB002078C 221-230 0.00088","Residues 99 to 133 match (7e-08) PD:PD587784 which is described as TRANSCRIPTION REGULATION DNA-BINDING ATP-BINDING PROTEOME COMPLETE REGULATOR TRANSCRIPTIONAL SENSORY TRANSDUCTION ","","","","","","","","","","","Thu Jan 2 17:47:40 2003","Thu Jan 2 17:47:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01579 is paralogously related to AA02281 (9e-05).","","","","","","Residues 13 to 229 (E-value = 5.6e-106) place AA01579 in the Sigma54_activat family which is described as Sigma-54 interaction domain (PF00158)","","","","","Cornish,E.C., Argyropoulos,V.P., Pittard,J. and Davidson,B.E. Structure of the Escherichia coli K12 regulatory gene tyrR. Nucleotide sequence and sites of initiation of transcription and translation. J. Biol. Chem. 261(1): 403-410,1986. PubMed: 3001057. Yang,J., Ganesan,S., Sarsero,J. and Pittard,A.J. A genetic analysis of various functions of the TyrR protein of Escherichia coli. J. Bacteriol. 175(6): 1767-1776,1993. PubMed: 8449883. Cui,J. and Somerville,R.L. The TyrR protein of Escherichia coli, analysis by limited proteolysis of domain structure and ligand-mediated conformational changes. J. Biol. Chem. 268(7): 5040-5047,1993. PubMed: 8444880. Argaet,V.P., Wilson,T.J. and Davidson,B.E. Purification of the Escherichia coli regulatory protein TyrR and analysis of its interactions with ATP, tyrosine, phenylalanine, and tryptophan. J. Biol. Chem. 269(7): 5171-5178, 1994. PubMed: 8106498. Wilson,T.J., Maroudas,P., Howlett,G.J. and Davidson,B.E. Ligand-induced self-association of the Escherichia coli regulatory protein TyrR. J. Mol. Biol. 238(3): 309-318, 1994. PubMed: 8176727. Bailey,M.F., Davidson,B.E., Minton,A.P., Sawyer,W.H. and Howlett,G.J. The effect of self-association on the interaction of the Escherichia coli regulatory protein TyrR with DNA. J. Mol. Biol. 263(5): 671-684, 1996. PubMed: 8947567. Pittard,A.J. and Davidson,B.E. TyrR protein of Escherichia coli and its role as repressor and activator. Mol. Microbiol. 5(7): 1585-1592, 1991. PubMed: 1943694.","","Thu Jan 2 17:47:40 2003","1","","","" "AA01581","1065578","1065405","174","GTGCATTGCCTTTTTGATTCACAAAAAAATACGGATGATTTAAATGAATTTCAACTGCTCACGAAATCCGCTCAAGACAATATTTTATTGGTCAGCGCGAAATGGACAATAAAGAAGAGATCAACCAATTCGGTGAGTTTTTGCCGAATATTCGTATTGAAAAAATGGAGTGTC","","","10818","VHCLFDSQKNTDDLNEFQLLTKSAQDNILLVSAKWTIKKRSTNSVSFCRIFVLKKWSV","1065403","","possible GTP-binding protein","Periplasm, Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Jan 2 17:50:50 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01581 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01582","1065711","1065565","147","TTGAACCCTTTACTCAATAATTTAAGCCAAAGTGCGGTGGATTCTGCGGAAATTTCCACCGCACTTTTTGCGTCTGATAAGCCTGATAATCCCTCATCACATGAAAAATCATGGATTGAATCATGCCACTATCGTGCATTGCCTTTT","","","5384","LNPLLNNLSQSAVDSAEISTALFASDKPDNPSSHEKSWIESCHYRALPF","1065565","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 15:43:11 2004","Thu Feb 26 15:43:11 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01582 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 15:43:11 2004","","","","","","","","","","","","","1","","","" "AA01584","1066025","1065729","297","ATGGCAAAAGGACAATCTTTACAAGATCCTTACTTGAACGCACTTCGTCGTGAACGCATTCCCGTTTCAATTTATTTGGTAAACGGTATCAAATTACAGGGGCAAATCGAGTCATTCGATCAATTCGTGATTTTACTGAAAAACACAGTAAATCAAATGGTTTATAAACACGCCATCTCGACTGTTGTACCGGCGCGTTCCGTCGCCCATCACAATGCTAACCAACAGCAGCAGCAACATCAGGGACAACAGCAAGAAACTACTCCTGCCGAAAACAATGTTGAAGCTCAGGCAGAA","","","11161","MAKGQSLQDPYLNALRRERIPVSIYLVNGIKLQGQIESFDQFVILLKNTVNQMVYKHAISTVVPARSVAHHNANQQQQQHQGQQQETTPAENNVEAQAE","1065727","[FUNCTION] RNA-binding protein that stimulates the elongation of poly(A) tails Required for phage qBeta RNA genome replication; function by destabilizing an RNA secondary structure on the 3'end of the Qbeta phage. Binds tightly to Qbeta RNA, poly(A) RNA, oxyS RNA and the untranslated RNA dsrA. Targets several mRNAs for degradation possibly by increasing polyadenylation or by interfering with ribosome binding. (By similarity).[SUBUNIT] Homohexamer (By similarity).","host factor-I protein","Cytoplasm, Extracellular","","
InterPro
IPR001163
Family
Like-Sm ribonucleoprotein, core
PF01423\"[5-64]TLSM
InterPro
IPR005001
Family
Host factor Hfq
PD009059\"[9-71]THFQ_HAEIN_P44437;
TIGR02383\"[5-64]THfq: RNA chaperone Hfq
noIPR
unintegrated
unintegrated
G3DSA:2.30.30.100\"[1-76]Tno description


","BeTs to 9 clades of COG1923COG name: Uncharacterized ACR, host factor I proteinFunctional Class: RThe phylogenetic pattern of COG1923 is --m----qv---b-efghsn-j----Number of proteins in this genome belonging to this COG is","","Residues 8 to 62 match (2e-23) PD:PD009059 which is described as COMPLETE PROTEOME HFQ RNA-BINDING HOST REGULATOR YERSINIA FACTOR-I PROBABLE HF-I ","","","","","","","","","","","Tue Feb 4 17:17:55 2003","Thu Jan 2 17:57:08 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01584 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 64 (E-value = 6.1e-11) place AA01584 in the LSM family which is described as LSM domain (PF01423)","","","","","Nakao,H., Watanabe,H., Nakayama,S. and Takeda,T. 1995. yst gene expression in Yersinia enterocolitica is positively regulated by a chromosomal region that is highly homologous to Escherichia coli host factor 1 gene (hfq). Mol. Microbiol. 18(5):859-865. PubMed: 8825090. Kajitani,M. and Ishihama,A. 1991. Identification and sequence determination of the host factor gene for bacteriophage Q beta. Nucleic Acids Res. 19(5):1063-1066. PubMed: 2020545. Carmichael,G.G., Weber,K., Niveleau,A. and Wahba,A.J. 1975. The host factor required for RNA phage Qbeta RNA replication in vitro. Intracellular location, quantitation, and purification bypolyadenylate-cellulose chromatography. J. Biol. Chem. 250(10):3607-3612. PubMed: 805130. ","","Thu Jan 2 17:57:08 2003","1","","","" "AA01585","1067133","1066147","987","TTGGCAGCCTTATTTAACCCAACTGACATAACCGCCCCACTAACTATGCAAGATTCCGAACAAAAACCTTTGGCGATTTTTTTAATGGGTCCCACCGCTTCCGGCAAAACGGATTTAGCCATTCAACTGCGCCAACATCTGCCGGTGGAAGTAATAAGCGTGGATTCAGCTCTCATTTATCGCGGCATGGATATTGGCACGGCAAAGCCCTCAAAAGCCGAGTTGGCACTGGCGCCCCACCGTTTAATTGATATTTGCGACCCGGCAGAAAGCTATTCCGCCGCCAATTTCCGCACCGACGCCCTACGTGAAATGCAGGACATTACCTCGTTGGGTAAAATCCCGTTATTGGTGGGTGGCACGATGTTGTATTACAAAGCGTTGCTCGAAGGCTTATCGCCATTGCCCTCCGCCGATGAAAAAGTGCGGTCAGAAATTGAAGCGAAAGCGGAACGTATCGGCTGGGCGGCATTACATCAGGAACTGAACAAAATCGACCCCATCTCGGCGCAACGCATTAACCCGAATGATTCGCAACGGATTAACCGCGCACTGGAAGTGTTTTATTTAAGCGGCAAAACCTTAACGGAATTAACCGAACAAAAAGGCGACGCGCTGCCCTATGAGATTCTGCAATTCGCCATTGCACCGGAGCAGAGAGATCTGTTGCATCAACGCATTGAGCAACGTTTTCATAAAATGATTGAACTTGGCTTTCAACAAGAGGTCGAAAAACTGTACCGACGCGCTGATTTGCACGAGAATTTGCCCTCCATTCGCTGTGTGGGGTATCGTCAAATGTGGGAATATTTGCGTGGTGACTATAGCCATGATGAAATGGTTTTTCGTGGCATCTGCGCCACCCGCCAATTAGCCAAGCGTCAGATTACTTGGTTACGCGGTTGGAAATCACCGATTCAATGGCTGGACAGTTTACAACCGGCTCAAGCGCTTGAGAAAGTGTTAAGTTTGCTTTCAAATAAAGCG","","","37232","LAALFNPTDITAPLTMQDSEQKPLAIFLMGPTASGKTDLAIQLRQHLPVEVISVDSALIYRGMDIGTAKPSKAELALAPHRLIDICDPAESYSAANFRTDALREMQDITSLGKIPLLVGGTMLYYKALLEGLSPLPSADEKVRSEIEAKAERIGWAALHQELNKIDPISAQRINPNDSQRINRALEVFYLSGKTLTELTEQKGDALPYEILQFAIAPEQRDLLHQRIEQRFHKMIELGFQQEVEKLYRRADLHENLPSIRCVGYRQMWEYLRGDYSHDEMVFRGICATRQLAKRQITWLRGWKSPIQWLDSLQPAQALEKVLSLLSNKA","1066145","[FUNCTION] Catalyzes the first step in the biosynthesis of 2-methylthio-N6-(delta(2)-isopentenyl)-adenosine (MS[2]I[6]A]) adjacent to the anticodon of several tRNA species (By similarity).[CATALYTIC ACTIVITY] Isopentenyl diphosphate + tRNA = diphosphate + tRNA containing 6-isopentenyladenosine.","tRNA delta(2)-isopentenylpyrophosphate","Cytoplasm","","
InterPro
IPR002627
Family
tRNA isopentenyltransferase
PD004674\"[83-139]TMIAA_PASMU_Q9CMC7;
PTHR11088\"[56-319]TTRNA DELTA(2)-ISOPENTENYLPYROPHOSPHATE TRANSFERASE-RELATED
PF01715\"[57-312]TIPPT
TIGR00174\"[25-314]TmiaA: tRNA delta(2)-isopentenylpyrophosphat
InterPro
IPR011593
Domain
Isopentenyl transferase-like
PD005388\"[22-82]TMIAA_HAEIN_P44495;
noIPR
unintegrated
unintegrated
PTHR11088:SF21\"[56-319]TTRNA DELTA(2)-ISOPENTENYLPYROPHOSPHATE TRANSFERASE


","BeTs to 18 clades of COG0324COG name: tRNA delta(2)-isopentenylpyrophosphate transferaseFunctional Class: JThe phylogenetic pattern of COG0324 is ------yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.5e-83) to 5/5 blocks of the IPB002627 family, which is described as \"IPP transferase\". Interpro entry for IP:IPR002627. IPB002627A 50-85 5.9e-24 IPB002627B 108-138 3.8e-18 IPB002627C 166-193 5.7e-16 IPB002627D 223-246 2.2e-12 IPB002627E 288-300 1.1e-07Significant hit ( 5e-05) to 1/5 blocks of the IPB000623 family, which is described as \"Shikimate kinase\". Interpro entry for IP:IPR000623. IPB000623A 26-55 4.9e-05","Residues 26 to 298 match (2e-130) PD:PD004674 which is described as TRANSFERASE TRNA ISOPENTENYLTRANSFERASE COMPLETE DELTA2-ISOPENTENYLPYROPHOSPHATE IPP ATP-BINDING IPPT IPTASE PROCESSING ","","","","","","","","","","","Thu Jan 2 18:03:15 2003","Thu Jan 2 18:03:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01585 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 57 to 312 (E-value = 2.4e-150) place AA01585 in the IPPT family which is described as IPP transferase (PF01715)","","","","","Connolly,D.M. and Winkler,M.E. 1991. Structure of Escherichia coli K-12 miaA and characterization of the mutator phenotype caused by miaA insertion mutations. J. Bacteriol. 173(5): 1711-1721. PubMed: 1999389. Connolly,D.M. and Winkler,M.E. 1989. Genetic and physiological relationships among the miaA gene, 2-methylthio-N6-(delta 2-isopentenyl)-adenosine tRNA modification, and spontaneous mutagenesis in Escherichia coli K-12. J. Bacteriol. 171(6): 3233-3246. PubMed: 2656644.","","Thu Jan 2 18:03:15 2003","1","","","" "AA01586","1068953","1067106","1848","ATGACCATACGCATTTTATCGCCACAATTAGCTAACCAAATTGCCGCCGGGGAAGTGGTTGAACGCCCTGCTTCGGTGGTGAAAGAATTGGTGGAAAACAGCCTTGATGCCGGTGCCGATAAAATTCAAATTGATATTGAAAACGGGGGCGCCGGGCTGATTCGCATTCGTGACAATGGCATCGGCATTGCTAAAGAGGAGCTAGCTTTAGCCCTTGCCCGCCATGCCACCAGCAAAATTGCCGATTTAGCAGATTTGGAAGCCATTTTAAGCCTGGGATTTCGCGGTGAAGCGCTCGCCAGTATCAGTTCTGTCTCCCGCTTAACCCTCACCTCCCGCACAGCCGAACAAAGCGAAGCTTGGCAAGTTTATGCCCAAGGGCGGGATATGAAAACCATCATTCAACCCGCCTCTCATCCTGTGGGCACTACCGTTGAAGTGGCAAATTTATTTTTTAACACGCCTGCCCGTCGCAAATTTTTACGTTCGGAAAAAACCGAATTTTCCCATATTGATGAAGTTATTCGTCGCATTGCATTAGCCAAATTTCACATTAACTTTACTCTGACACACAATGGGAAAGTGCTTCGCCAGTATAAAAGTGCGGTCACCCATGAACAAAAATTAAAGCGCGTCGCTGCTATTTGCGGTCAGGATTTTATTCAAAACGCGTTACAAATCGACTGGAAACACGATGACCTGCATTTATCCGGCTGGGTGGCGTTGCCGCAGTTTAACCGTCCGCAAAACGACCTGAATTATTGCTATGTCAACGGGCGCATGGTGCGTGATAAAACCATTACGCACGCGATCCGCCAAGCCTATGCGGATTATTTAACCACTGAACAATATCCCGCTTTTGTGTTGTTTATTGATCTCAATCCGAATGAGGTGGATGTGAATGTGCACCCGACCAAACACGAAGTGCGTTTCCAGCAATCCCGATTGGTGCATGATTTCATCACCCAAGGCATTAGTAACGCGCTGGCTTCAGAACAAATACACTTGACCCCGTCATCAATGGAAAATGCCGTAGAAGAACCTGCGGGTGTGTGGGAAGCGCCGACTTACACCAAACCGAATCGCTCGGCGGCAGGGCAAAATATATTCGCACCGACTACCGGTTATTCCGCCACTGCCTACGCCGAAAAAAAGAATGACGGCACGCAAAAACACCGGCAAAGTTCACCGCACTTTTATCGTGAAAATGCCCATCGTGAACAAATTACGCAGAACGTATTGAATGCCCACAAAACCTTGTGGACGGCGTTAAAAAATCAGCCTCAAACGGAAATGACCATAGCGGAAGTCAGCAAACCCAATACCGATTTTTTACACGCGCTTGCGCTTATCAACGACGAGGCATTATTGTTACAGCAAGGACAGCATTTTTATTTGTTGTCATTAGCCCGTTTGCAGCATTTAAAATTGGAGTTGAATTTAACCTTGGCGCCAACACCTCAGCCATTGTTAATCCCGATTATTTTTCGCTTATCTAATGACCAATGGCAGGCATGGTTACAACAAAAAACGTTCTTTGAGCAAATCGGTTTTACTTTTACGGAAGAGGCGACACAACATAAAATAACGCTGCAAAAAGTATCGGCACATTTACGCCAACAAAATTTACAGCAGATAATTATCTCGCTATTAAATCACTCCATCGAAAATTTACCTGAATTTTTGACCGCACTTTTGGCGTCCTTAGAATTCGCGCCCATCACCGTGCTTGCCGATGCGGTAAGTTTGCTGACCGATACGGAACAATTACTTGCCAAACAAGCGCAAACCTGCCTGATGGATTTGCTTGTGGAAATCGATTGGCAGCCTTATTTAACCCAACTGACA","","","69292","MTIRILSPQLANQIAAGEVVERPASVVKELVENSLDAGADKIQIDIENGGAGLIRIRDNGIGIAKEELALALARHATSKIADLADLEAILSLGFRGEALASISSVSRLTLTSRTAEQSEAWQVYAQGRDMKTIIQPASHPVGTTVEVANLFFNTPARRKFLRSEKTEFSHIDEVIRRIALAKFHINFTLTHNGKVLRQYKSAVTHEQKLKRVAAICGQDFIQNALQIDWKHDDLHLSGWVALPQFNRPQNDLNYCYVNGRMVRDKTITHAIRQAYADYLTTEQYPAFVLFIDLNPNEVDVNVHPTKHEVRFQQSRLVHDFITQGISNALASEQIHLTPSSMENAVEEPAGVWEAPTYTKPNRSAAGQNIFAPTTGYSATAYAEKKNDGTQKHRQSSPHFYRENAHREQITQNVLNAHKTLWTALKNQPQTEMTIAEVSKPNTDFLHALALINDEALLLQQGQHFYLLSLARLQHLKLELNLTLAPTPQPLLIPIIFRLSNDQWQAWLQQKTFFEQIGFTFTEEATQHKITLQKVSAHLRQQNLQQIIISLLNHSIENLPEFLTALLASLEFAPITVLADAVSLLTDTEQLLAKQAQTCLMDLLVEIDWQPYLTQLT","1067104","[FUNCTION] This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair and may act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex (by similarity).[SIMILARITY] Belongs to the DNA mismatch repair MutL/HexB family. ","DNA mismatch repair protein","Cytoplasm","","
InterPro
IPR002099
Family
DNA mismatch repair protein
PTHR10073\"[64-338]TDNA MISMATCH REPAIR PROTEIN (MLH, PMS, MUTL)
InterPro
IPR003594
Domain
ATP-binding region, ATPase-like
G3DSA:3.30.565.10\"[2-216]Tno description
PF02518\"[18-79]THATPase_c
SM00387\"[18-153]THATPase_c
InterPro
IPR013507
Domain
DNA mismatch repair protein, C-terminal
PF01119\"[217-330]TDNA_mis_repair
InterPro
IPR014721
Domain
Ribosomal protein S5 domain 2-type fold
G3DSA:3.30.230.10\"[217-330]Tno description
InterPro
IPR014762
Domain
DNA mismatch repair, MutL/HexB/PMS1
PS00058\"[93-99]?DNA_MISMATCH_REPAIR_1
InterPro
IPR014763
Domain
DNA mismatch repair protein, N-terminal
TIGR00585\"[1-310]Tmutl: DNA mismatch repair protein MutL
InterPro
IPR014790
Domain
MutL, C-terminal, dimerisation
PF08676\"[440-574]TMutL_C
noIPR
unintegrated
unintegrated
PTHR10073:SF12\"[64-338]TDNA MISMATCH REPAIR PROTEIN MUTL


","BeTs to 16 clades of COG0323COG name: DNA mismatch repair enzyme (predicted ATPase)Functional Class: LThe phylogenetic pattern of COG0323 is -o----yqvd-lbcefghsn-jxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.9e-93) to 5/6 blocks of the IPB002099 family, which is described as \"DNA mismatch repair proteins mutL/hexB/PMS1\". Interpro entry for IP:IPR002099. IPB002099A 3-50 6e-36 IPB002099B 60-107 1.2e-28 IPB002099C 142-159 4.2e-12 IPB002099D 253-265 0.00014 IPB002099E 298-309 6.3e-07","Residues 310 to 615 match (4e-42) PD:PD398696 which is described as DNA REPAIR MUTL COMPLETE MISMATCH PROTEOME ","","","","","","","","","","","Tue Jan 28 15:52:02 2003","Thu Jan 2 18:07:27 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01586 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 217 to 330 (E-value = 2.8e-49) place AA01586 in the DNA_mis_repair family which is described as DNA mismatch repair protein, C-terminal domain (PF01119)","","","","","Secondary Laboratory Evidence: Tsui,H.T., Mandavilli,B.S. and Winkler,M.E. 1992. Nonconserved segment of the MutL protein from Escherichia coli K-12 and Salmonella typhimurium. Nucleic Acids Res. 20(9):2379. PubMed: 1594459. Mankovich,J.A., McIntyre,C.A. and Walker,G.C. 1989. Nucleotide sequence of the Salmonella typhimurium mutL gene required for mismatch repair: homology of MutL to HexB of Streptococcus pneumoniae and to PMS1 of the yeast Saccharomyces cerevisiae. J. Bacteriol. 171(10):5325-5331. PubMed: 2676972.","","Thu Jan 2 18:07:27 2003","1","","","" "AA01588","1070440","1068956","1485","ATGAAACTCGGCAATATCTTTAAATTATTTCTTGTCAACAGCGTTTTTTTCTTTGCAATGCCCGTTCTCGCCGGTAACGCATGGACAATTGCCGTTGATCCCGGTCATGGCGGGAAAGACCCCGGCGCTATCGGGCGCAACCTAAAAATTTATGAAAAAAATGTAACCCTTTCTATCGCCCGTGAATTAAAAGCGCTTTTAGATAAGGATCCGCGTTTTCATGCCGTATTAACCCGCAACGGCGATTACTTTATTTCCGTGCCGCAACGTTCCGAAATTGCGCGTAAGCACAAAGCCAATTATTTGGTTTCCATTCATGCAGATTCCTCAGAAACCCCGAATTTACGCGGCGCTTCCGTATGGGTGTTGTCAAACCGTCGCGCCAATGACGAAATGGGGCAATGGCTGGAAGATCATGAAAAACGTTCGGAGCTGTTGGGCGGAGCGGGTAGCGTGCTCGCTTCACATAATGAAAAATACTTGGATCAAACGGTGTTAGATTTACAATTCGGACATAGCCAACGGGTGGGTTATGAATTAGGCAATATCGTGCTGCGCCATTTTTCCCAAATTGCTTCTTTAAGCCGCCCGACACCACGCCATGCAAGCCTTGGCGTCTTACGTTCGCCGGATATTCCATCCATTTTGGTAGAAACGGGCTTTCTCTCCAATCAAGATGAAGAACTGAAATTAAGCACGCCCGCCTACCGCAAAAAAATTGCAAAAGCCATTTATAACGGTTTGGTCGAATATCGTCGTCAAAATTATAAAGAAGAGCCAAAAATTCCGACCGTAAAAACACCTGAAAAATCCACCGCACTTGAAGTGACGGACAGTGGCATTCGTCATAAGGTGAAATCAGGCGAAGGCTTAGGCAAACTGGCTGAAAAATACCATGTTAACATCGCGGATGTCATTGCGTTAAACAAATTAAAACGCAAAAAATTGTGGGTGGGCGAAACCATTAAAATCCCTGATAATGGCAAAAACAACGCGACCAACACGAAGGAAAACACCGAAACTAAACCGGTGAAAAGTGCGGAAATTAAAGACAGCGGCATTCGCCATAAAGTGAAAAAAGGCGAAACTTTAACTAAACTTGCGGCAAGATATAAAGTTTCCGGTAACGATATTCTTACGCTCAATAAGCTAAAACGTAAAGAACTGCAACTGGGTGAAACCATTAAAATTCCTGCCGTTGCCAAAGCGGAAGATACCATGAAAACCGAAGCCAAAACGGAAAAAGGGAAAGCTGCAGAAAATACGAAAAGCAAGGACGAAAACACCTCGGGGAAAGGCAAAGCGGAAGTAAAACAAGCTGTGCCGACTTTCCATGTGGTGAAAAAAGATCAAACGCTCTACTCCATTGCACGTGAGTATAATCTTTCGCCAAATACCTTGCTAAAACTGAACCCGCAATTAAAAAACGGCAAAGTGTTAAGCGGGCAAAAAATCCGACTGGTTGAAAACAAACACGGGAAAAAA","","","55069","MKLGNIFKLFLVNSVFFFAMPVLAGNAWTIAVDPGHGGKDPGAIGRNLKIYEKNVTLSIARELKALLDKDPRFHAVLTRNGDYFISVPQRSEIARKHKANYLVSIHADSSETPNLRGASVWVLSNRRANDEMGQWLEDHEKRSELLGGAGSVLASHNEKYLDQTVLDLQFGHSQRVGYELGNIVLRHFSQIASLSRPTPRHASLGVLRSPDIPSILVETGFLSNQDEELKLSTPAYRKKIAKAIYNGLVEYRRQNYKEEPKIPTVKTPEKSTALEVTDSGIRHKVKSGEGLGKLAEKYHVNIADVIALNKLKRKKLWVGETIKIPDNGKNNATNTKENTETKPVKSAEIKDSGIRHKVKKGETLTKLAARYKVSGNDILTLNKLKRKELQLGETIKIPAVAKAEDTMKTEAKTEKGKAAENTKSKDENTSGKGKAEVKQAVPTFHVVKKDQTLYSIAREYNLSPNTLLKLNPQLKNGKVLSGQKIRLVENKHGKK","1068954","[FUNCTION] Cell-wall hydrolase probably involved in cell-wall hydrolysis, septation or recycling (by similarity). [CATALYTIC ACTIVITY] Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain bacterial cell-wall glycopeptides. [DOMAIN] LysM repeats are thought to be involved in peptidoglycan binding. [SIMILARITY] Belongs to the N-acetylmuramoyl-L-alanine amidase family 3.[SIMILARITY] Contains 2 LysM repeats. ","N-acetylmuramoyl-L-alanine amidase II","Periplasm, Outer membrane","","
InterPro
IPR002482
Domain
Peptidoglycan-binding LysM
PF01476\"[283-325]T\"[356-398]T\"[445-488]TLysM
SM00257\"[282-325]T\"[355-398]T\"[444-488]TLysM
InterPro
IPR002508
Family
Cell wall hydrolase/autolysin
PF01520\"[30-250]TAmidase_3
SM00646\"[91-249]TAmi_3
noIPR
unintegrated
unintegrated
G3DSA:3.10.350.10\"[352-400]Tno description
G3DSA:3.40.630.40\"[27-251]Tno description
PTHR21666\"[346-416]T\"[454-485]TPEPTIDASE-RELATED
PTHR21666:SF8\"[346-416]T\"[454-485]TLYSM CONTAINING PEPTIDASE
signalp\"[1-24]?signal-peptide
tmhmm\"[10-30]?transmembrane_regions


","BeTs to 15 clades of COG0860COG name: N-acetylmuramoyl-L-alanine amidaseFunctional Class: MThe phylogenetic pattern of COG0860 is -------q-dr-bcefghsnuj-it-Number of proteins in this genome belonging to this COG is","Significant hit ( 2.5e-41) to 4/4 blocks of the IPB002508 family, which is described as \"Cell wall hydrolase/autolysin\". Interpro entry for IP:IPR002508. IPB002508A 32-44 7.4e-09 IPB002508B 48-71 8.5e-08 IPB002508C 99-108 0.012 IPB002508D 202-241 2.3e-17","Residues 284 to 325 match (2e-07) PD:PD407905 which is described as PROTEOME COMPLETE PRECURSOR HYDROLASE CELL REPEAT SIGNAL LIPOPROTEIN WALL ENZYME ","","","","","","","","","","","Thu Jan 2 18:11:31 2003","Thu Jan 2 18:11:31 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01588 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 445 to 488 (E-value = 8.6e-12) place AA01588 in the LysM family which is described as LysM domain (PF01476)","","","","","Wilson SA, Williams RJ, Pearl LH, Drew RE. Identification of two new genes in the Pseudomonas aeruginosa amidase operon, encoding an ATPase (AmiB) and a putative integral membrane protein (AmiS). J Biol Chem. 1995 Aug 11;270(32):18818-24. PMID: 7642533 Alloing G, Trombe MC, Claverys JP. The ami locus of the gram-positive bacterium Streptococcus pneumoniae is similar to binding protein-dependent transport operons of gram-negative bacteria. Mol Microbiol. 1990 Apr;4(4):633-44. PMID: 2352474","","Thu Jan 2 18:11:31 2003","1","","","" "AA01589","1070931","1070440","492","ATGATCGATAGATTTAGCCAATACATTTCTGATGAAAATGCCATGTGCGCCTTTGGAGCAAAACTTATCAATGCGATAAGCCATGTTCCGAATCAACAAGGCATTGCACTTTATTTGAACGGTGATCTTGGCGCTGGGAAAACGACCTTAAGCCGTGGGATGATTCAAGCTTTGGGGTATCAAGGTAAAGTAAAAAGCCCGACTTACACGTTAGTGGAAGAATATCGATTCCGCAACAAAACCGTTTACCATTTTGATTTGTATCGTCTTGCCGATCCTGAAGAGCTGGAATTTATGGGCATTCGTGATTATTTTAGTGAAAACACGCTTTGCTTGATTGAGTGGGCTGAGAAAGGAACAGGCATGCTTATGGCGGCAGATTTGTTGGTCAACATTGCCTATGCGGAAACTGCCCATCACATTGAATTGGTTGCTCAATCGCCAATCGGCAGACAGATTATTGAACAATTAAATAACGATGATGTACCACAA","","","20104","MIDRFSQYISDENAMCAFGAKLINAISHVPNQQGIALYLNGDLGAGKTTLSRGMIQALGYQGKVKSPTYTLVEEYRFRNKTVYHFDLYRLADPEELEFMGIRDYFSENTLCLIEWAEKGTGMLMAADLLVNIAYAETAHHIELVAQSPIGRQIIEQLNNDDVPQ","1070438","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003442
Domain
Protein of unknown function UPF0079, ATPase bacteria
PF02367\"[15-142]TUPF0079
TIGR00150\"[8-147]TTIGR00150: conserved hypothetical protein T
InterPro
IPR012298
Family
ATPase, cell wall biosynthesis
PIRSF006361\"[6-158]TATPase likely involved in cell wall biosynthesis
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[2-159]Tno description


","No hits to the COGs database.","Significant hit ( 1.3e-33) to 3/3 blocks of the IPB003442 family, which is described as \"Uncharacterised P-loop hydrolase UPF0079\". Interpro entry for IP:IPR003442. IPB003442A 31-59 5.7e-14 IPB003442B 66-90 8.7e-14 IPB003442C 108-117 0.0087","Residues 21 to 134 match (6e-40) PD:PD006723 which is described as PROTEOME COMPLETE ATP-BINDING KINASE YJEE NUCLEOTIDE-BINDING PREDICTED FAMILY CC3534 BB0186 ","","","","","","","","","","","","Thu Jan 2 18:13:58 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01589 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 15 to 142 (E-value = 2.6e-46) place AA01589 in the UPF0079 family which is described as Uncharacterised P-loop hydrolase UPF0079 (PF02367)","","","","","","","","1","","","" "AA01590","1070906","1071031","126","ATGTATTGGCTAAATCTATCGATCATGCTGTTTGTCAGTTTAAAAAGTAGTAAGGAATTGTACCGCACTTTGGCGGGATTATGTAGTGGCTTTGAATTGATGTATGGTTACAGTGGGCATTTGGAA","","","4835","MYWLNLSIMLFVSLKSSKELYRTLAGLCSGFELMYGYSGHLE","1071031","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-16]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 15:41:12 2004","Thu Feb 26 15:41:12 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01590 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 15:41:12 2004","","","","","","","","","","","","","1","","","" "AA01592","1072880","1071090","1791","ATGTATAATAAATTATTTATAAATAATAACATAAAAAAATTAGTTTATATCGCTTGTATTATTTGGATATTATGTGCCACTTTTTTAATTATACGGAACTGGAGTGATGTCGCAAATTTCGCATTGAGTGATACTGATGATCTTATGCGCTATCATCAATATAGTGAGTGGTTAAAAAATGGGAATTGGTATTTACTGCCGGATCCTCAATTTAACCCACAAGACGGCGTTATCATGCACTGGTCCAGAGTTGTGGATATTCCATTAGCCGGGGTAGCCCTGCTTGCTTCTATTTTCACCGATTGGAACACCGCATTCACCATATCGAATGTTATAACACCACTCCTTTATCTATTAATTTTTTTATTAATTATATCACTAATATCTTACCGTTTATTTGGGCTGGAGACAGCTAAAATAGCAATGCTGTTTCCACTATTAGCACCAATTAGTTATCGTTTTCTTCCGGGCGCTTTAGATCACCATAATCTTCAGTTTATTTTATTAATATCTTTTTGCATTTTCTCTATAGCAAAAAATAAACAAAATCAAAACGGGCAGCCATTCTTTATAGCGATAAGTATAGTTTTATCATTATGGATAGGGCTAGAAAACATATATAGCTTTGTTGCCATTTTAATGCTATTTGTTTTATATGGTTTACTGAATAATTTATATTACTTAGAATTAGCCAAAAAAATATGCCTGCATAGTAGTATTCTATCTTTTGCAGTATTAATACTAAACAGACCTGCAAATGAATTATTTATCCCACAATATGACGCTTTATCATTTCCATTCTTACTTTGTTTTATTGCAGGATCTATTCTTTGTACTTTATTGATTAAGTTTTCTATTCATTTTACTAACAAAATTAAAAAAATTGCTTTTTTGTGTGTAACAGGTATTGCTTTAGTTCTGCCTATCATAATTATTTATCCAAACCTAATAAAAGGAGGGTATGCCGACTACCCTATTTTCCTTAAGGATAACTGGCTATCTTTTGTCTCTGAAGCAAGACCATTAACTGTGACAATATCTCAGGATATCGGAGATATAGGTTATTTTATTGCGATTCTTCCCGCTATCCTTTCTCCATTATTTTTATCTGATAAAAAGGAATTAAATTACTGGATTATATATATCGCTTTAATCACTAATTTATTACTGGCAATATTTTGGCAAGTAAGAATGTTCTATACAGCAATGTCTGTTGCAATTCCTTTACAAGCTTATACTTGCTACTCATTAAGAGAGAAATATTCATTACCGATAACAAAAACTATCATTTTATTTTTATCAATACCTACATTTCTATTAATTTCAACTAAAATAATCATAAATTTCAACGATGAAAATGAATCCAAAGAGATTTATGACGAAAAATATAATAATAGCTACTATGCGACGAAAAAATTACTTAATAAAAACAATTTAGAAAATAAAATTATATTACCTCCTATTGATTTAGGTGCTGCCGTTATTGCTACAACATCCAATGCTTCTATTTCTGCGCCTTACCACAGAAATATAAGAGGAAATTCTGATACAATGCGGTTTTATACGTCAGTTAATACAGATGATGCAGAAAAATACTTGATTAAAAATAATGTGGATTATATTCTGATTGAGAAAAATTTTGCCAATGTTTTAGCCGATAAATATAAGGGGAAAGAAATCATGGCTCAAAAATTAATAGATAAGAAAGATATACCTGATTATCTTGAATTTATTGATGCCAATGAAAACACCAATATTATTTTATATAAATTTATTAAACCCGAACTCAAA","","","68491","MYNKLFINNNIKKLVYIACIIWILCATFLIIRNWSDVANFALSDTDDLMRYHQYSEWLKNGNWYLLPDPQFNPQDGVIMHWSRVVDIPLAGVALLASIFTDWNTAFTISNVITPLLYLLIFLLIISLISYRLFGLETAKIAMLFPLLAPISYRFLPGALDHHNLQFILLISFCIFSIAKNKQNQNGQPFFIAISIVLSLWIGLENIYSFVAILMLFVLYGLLNNLYYLELAKKICLHSSILSFAVLILNRPANELFIPQYDALSFPFLLCFIAGSILCTLLIKFSIHFTNKIKKIAFLCVTGIALVLPIIIIYPNLIKGGYADYPIFLKDNWLSFVSEARPLTVTISQDIGDIGYFIAILPAILSPLFLSDKKELNYWIIYIALITNLLLAIFWQVRMFYTAMSVAIPLQAYTCYSLREKYSLPITKTIILFLSIPTFLLISTKIIINFNDENESKEIYDEKYNNSYYATKKLLNKNNLENKIILPPIDLGAAVIATTSNASISAPYHRNIRGNSDTMRFYTSVNTDDAEKYLIKNNVDYILIEKNFANVLADKYKGKEIMAQKLIDKKDIPDYLEFIDANENTNIILYKFIKPELK","1071088","","hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[88-223]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-35]?signal-peptide
tmhmm\"[15-35]?\"[79-99]?\"[114-134]?\"[163-178]?\"[188-222]?\"[262-282]?\"[297-317]?\"[350-370]?\"[375-393]?\"[399-417]?\"[429-449]?\"[483-503]?transmembrane_regions


","No hits to the COGs database.","","Residues 44 to 589 match (5e-07) PD:PD416990 which is described as PROTEOME COMPLETE MLR4739 MLL5209 ","","","","","","","","","","","","Thu Jan 2 18:15:02 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01592 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01593","1074188","1073271","918","ATGAATGAATCAATCAATCAATCAATTGCAATATTAATTCCTTGTTATAATGAAGAACATAGTATATCCGATACTGTTCTCTCATTTAGATCCGCTTTGCCTTTGGCAAAAATCTACGTTTATGATAATAATTCGACAGATAAAACTTTTGAAATTGCAAGTAAACTAGATTGTATTGTACGCAATGAACCTAAACAAGGAAAAGGTGCCGTCGTTCGCAGAATGTTTGCAGATATTGATGCAGACATTTATATTCTGGTGGATGGAGATAATACCTATGATGCCAACATTGCTCCGGATTTAGTTAACACCCTGATTCAGGAAAACTTAGATATGATAATCGGGGCGCGAAATAGAAAATCAGAATCCTACCCTAAAGGTCATATACTGGGTAATAAAATTTTTTCAAAAATAATTAGTTATTTTTTTAATTCAACTATAAATGATCTTTTTTCCGGCTATAGAATAATGACGAAACGCTTTGTCAAATCTTTACCATTAATCAGTAATGGGTTTGAAATTGAAACAGAGATGACGGTATTAGCATTACAATTAAATATGCCAATAAAGGAAATTCCCACTAACTATAGTTCAAGAAAAGAAAATAGTAAGAGCAAGTTAAGAACATATAGAGATGGGTTTAAAATATTAAGTTTTATTTTCTTCTTAATTAGAGAGCAAAAACCGCTATTATTTTTTATGACACTCTCTTTAATTTGCACACTATTTTCACTGATTACCGGTACTTCCGTTATCTTCCAGTATCTCAAGCTTGGTACGGTACTAAAAATATCTACTGCTGTATTCGCTACCGGCATGGGGATTCTGGCTATATTATTTTTTGCAATTGCATTAATTCTAGACTCAATATCCAATGCAAGAAAAGAACTTAAAAGAATGAATTATCTCAATATTAAA","","","34708","MNESINQSIAILIPCYNEEHSISDTVLSFRSALPLAKIYVYDNNSTDKTFEIASKLDCIVRNEPKQGKGAVVRRMFADIDADIYILVDGDNTYDANIAPDLVNTLIQENLDMIIGARNRKSESYPKGHILGNKIFSKIISYFFNSTINDLFSGYRIMTKRFVKSLPLISNGFEIETEMTVLALQLNMPIKEIPTNYSSRKENSKSKLRTYRDGFKILSFIFFLIREQKPLLFFMTLSLICTLFSLITGTSVIFQYLKLGTVLKISTAVFATGMGILAILFFAIALILDSISNARKELKRMNYLNIK","1073269","","glycosyltransferase; rfbJ protein","Inner membrane, Cytoplasm","","
InterPro
IPR001173
Domain
Glycosyl transferase, family 2
PF00535\"[10-166]TGlycos_transf_2
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[187-298]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.90.550.10\"[9-162]Tno description
PTHR10859\"[15-287]TGLYCOSYLTRANSFERASE RELATED
tmhmm\"[231-253]?\"[267-287]?transmembrane_regions


","BeTs to 20 clades of COG0463COG name: Glycosyltransferases involved in cell wall biogenesisFunctional Class: MThe phylogenetic pattern of COG0463 is aompkzyqvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is","","Residues 9 to 93 match (1e-08) PD:PD395383 which is described as TRANSFERASE COMPLETE PROTEOME SYNTHASE GLYCOSYLTRANSFERASE MANNOSYLTRANSFERASE DOLICHOL-PHOSPHATE MANNOSE GLYCOSYL DOLICHYL-PHOSPHATE ","","","","","","","","","","","","Mon Jan 27 15:21:05 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01593 is paralogously related to AA02636 (3e-07) and AA01190 (3e-06).","","","","","","Residues 10 to 166 (E-value = 6.6e-18) place AA01593 in the Glycos_transf_2 family which is described as Glycosyl transferase (PF00535)","","","","","","","","1","","","" "AA01594","1075704","1074199","1506","ATGACAATCACTAAAAAAGCAATAATATTATCTTTTCTAAGTGGCTTCCTAAGCTTAGGATTAGAAGTGATTTGGATTAGACTTTTTGGTTTCTATGGTATTTCTCTACCCCAAATATTTTCTTTAACGCTTGCCTTATTTTTATTGGGTATCGCTTGTGGTTCTTTAATTGGCAAGCGCTTATGCCAATCAGAAAAAGGAACTGTTCAATATATTGGGTATTCTTTTCTGCTATCTTCAATTTTTGATTGCTTAACAATCTCACTAATAGTTAATTTCCCTATTGAGGGTATGTTAGGCATCTTTATCGTATGCATATTTTACAGCGCACTACTAAGAGGAATTGTGTTCCCAATTGTTCATCATTTAGGTGCGGAACAGAAAAAAACAGGTGCAGCAATTTCTAATGTCTATTTTGCTAATGTTCTGGGATGTACAATTTCTCCGATATTAATTGGATTTTACCTCCTTGACATTTTTACTACACAACAAACATATTTTATCATCACTTTTATTACCCTGGTTACAGCTGCATTCTGTATACAAGAAAAATGGCTAAAAAGCACAACCGCTCTTATAGCTACTATTATTATAGCGATAACCTTCGTTTTACCTGAAAATATAATTCATTCATTAGCCAAGAAAAAAGATGAAAACGGGAAATATTTAAAATTAGAGAAACTGATTGAAAATAAACACGGTTTTATTCAAGTATATTTAAGCGAAAACAATGACAAACTCGTATTCGGCGGTAATGCTTATGATGGTATGCTAAATACAAATTTGAATCACAGTCATAATGGCATTGAAAGAGCTTATTTATTACCGGTTATTGCACCTCATGCGAAAAACATTCTTGTTATCGGTTTAAGTACAGCCTCTTGGACAAGAGTTTTAACATCAATGCCCGAATTGGAATCAATGACTGTTATTGAATTAAATCCGGGCTATCCTCAGCTAGCCGGAATGTACTCTGAAATGGGCAAATTTCTGCAGGACAAGCGGGTCAATCTCATCACTGATGATGGTCGCCGTTGGTTAAACCGTAATCCTGAGAAAAAATTTGACTTTATTCTAATGAATACCACATTCCATTGGAGAAATTATGCATCTAATTTACTTAGTAAAGAGTTTTTAGAATTAACAAAATCGCATTTAAATGAAAATGGTTTTATCTATTTCAACACAACGGAATCATATGATGCATACTACACCTCAAAAGAAGTTTTCCCTCATGTTTATCAATATATGAATATGTCACTAGCTTCATTGAATCCGATCAGCGCACTAACCAAAGATCAAATTACGTCCGGATTATCAAGATTAAAATGGGAAAATGGAAGTCATGTCTTCAATTCACAAGAAGAGTTAGAGAAAGGCGTTAATACTATTTTTATAAAACCTCTAATTCGTTATGAAGAGATAAATTTCCAAAATTTAGGACGCCCATTAGAAATAATTACAGATGGAAACATGATCACAGAATATAAATATGGATTTTTTAAT","","","56907","MTITKKAIILSFLSGFLSLGLEVIWIRLFGFYGISLPQIFSLTLALFLLGIACGSLIGKRLCQSEKGTVQYIGYSFLLSSIFDCLTISLIVNFPIEGMLGIFIVCIFYSALLRGIVFPIVHHLGAEQKKTGAAISNVYFANVLGCTISPILIGFYLLDIFTTQQTYFIITFITLVTAAFCIQEKWLKSTTALIATIIIAITFVLPENIIHSLAKKKDENGKYLKLEKLIENKHGFIQVYLSENNDKLVFGGNAYDGMLNTNLNHSHNGIERAYLLPVIAPHAKNILVIGLSTASWTRVLTSMPELESMTVIELNPGYPQLAGMYSEMGKFLQDKRVNLITDDGRRWLNRNPEKKFDFILMNTTFHWRNYASNLLSKEFLELTKSHLNENGFIYFNTTESYDAYYTSKEVFPHVYQYMNMSLASLNPISALTKDQITSGLSRLKWENGSHVFNSQEELEKGVNTIFIKPLIRYEEINFQNLGRPLEIITDGNMITEYKYGFFN","1074197","[CATALYTIC ACTIVITY] S-adenosylmethioninamine + putrescine = 5'-methylthioadenosine + spermidine.[PATHWAY] Spermidine biosynthesis; fifth (last) step.","probable spermidine synthase","Inner membrane, Cytoplasm","","
InterPro
IPR001045
Family
Spermine synthase
PTHR11558\"[333-392]TSPERMIDINE/SPERMINE SYNTHASE
PF01564\"[210-437]TSpermine_synth
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[278-428]Tno description
signalp\"[1-54]?signal-peptide
tmhmm\"[9-29]?\"[39-59]?\"[71-93]?\"[99-119]?\"[134-154]?\"[160-180]?\"[185-205]?transmembrane_regions


","No hits to the COGs database.","","Residues 22 to 499 match (2e-102) PD:PD361077 which is described as PROTEOME COMPLETE NMB0240 INTEGRAL MEMBRANE ","","","","","","","","","","","Thu Jan 2 18:53:47 2003","Thu Jan 2 18:53:47 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01594 is paralogously related to AA01595 (6e-10).","","","","","","","","","","","Tabor,C.W. and Tabor,H. The speEspeD operon of Escherichia coli. Formation and processing of a proenzyme form of S-adenosylmethionine decarboxylase. J. Biol. Chem. 262 (33): 16037-16040 (1987) [PubMed: 3316212].Xie,Q.W., Tabor,C.W. and Tabor,H. Spermidine biosynthesis in Escherichia coli: promoter and termination regions of the speED operon. J. Bacteriol. 171 (8): 4457-4465 (1989) [PubMed: 2666401].Tabor,C.W., Tabor,H. and Xie,Q.W. Spermidine synthase of Escherichia coli: localization of the speE gene. Proc. Natl. Acad. Sci. U.S.A. 83 (16): 6040-6044 (1986) [PubMed: 3526348].","","Thu Jan 2 18:53:47 2003","1","","","" "AA01595","1076308","1075694","615","ATGGATAAATATTCTGCCGGAACGGTAAAATCTGTATTTTTTATGTCGGGCTTTGCTGCCTTAATTTATCAAATAGCATGGCAAAGAATGTTATTTACTGCTTTTGGAGTAGACTTAGAATCAATCACTGTTATTATTGCCGTCTTTATGGCCGGATTAGGCATAGGTGCTTATTTTGGCGGACGCATTGCCGATAAATTTCCTAAACAAATTATTTTACTCTTCGCATTAACAGAAATCGGGATTGGTACATTCGGTTTCTTAAGCCCCACACTAATTAATTTAACCCAAGCGTTATTTTTACATTCGGCACTTCTTACTGTCGCGTTCTCTAACTTTGTTTTATTGCTATTCCCTACGTTTCTAATGGGAAGCACTCTTCCCCTGCTGACACAATATTTAAATCAACACTTTGATAATATTGGCAATAATATAGGCTGGTTATACTTTACCAATACTTTAGGCGCGGCATTTGCCTGTATAACAACCGGGTTTATCTTATTCAATTATTTTACAATCACACAAGTAATCTACTTGGCAGCAATTATTAATTATCTTGTAGCGACAGTTATATTCTTAAAATACGGGAAAAAAGGAATCAGTCATGACAATCAC","","","22637","MDKYSAGTVKSVFFMSGFAALIYQIAWQRMLFTAFGVDLESITVIIAVFMAGLGIGAYFGGRIADKFPKQIILLFALTEIGIGTFGFLSPTLINLTQALFLHSALLTVAFSNFVLLLFPTFLMGSTLPLLTQYLNQHFDNIGNNIGWLYFTNTLGAAFACITTGFILFNYFTITQVIYLAAIINYLVATVIFLKYGKKGISHDNH","1075692","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-28]?signal-peptide
tmhmm\"[9-27]?\"[41-61]?\"[71-93]?\"[99-130]?\"[145-165]?\"[171-193]?transmembrane_regions


","BeTs to 11 clades of COG0477COG name: Permeases of the major facilitator superfamilyFunctional Class: G,E,P,RThe phylogenetic pattern of COG0477 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 1 to 201 match (2e-38) PD:PD309202 which is described as PROTEOME COMPLETE INTEGRAL MEMBRANE ","","","","","","","","","","","","Thu Jan 2 19:07:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01595 is paralogously related to AA01594 (2e-10).","","","","","","","","","","","","","","1","","","" "AA01596","1078007","1076340","1668","TTGTCTTTTCTGTTATCTTCAGTCTTAAACCTAAAGAACCAATTTATGTTTAAAAAATTTCTTAATTATCTAAATAGCCGAATCTTTTGGATTTGGCTACTCTTTTTCTCATTTATTACGCTTATTATATCACCTGAGAATACTATTTATTATGGCATGTTTGTAATATACATTATCTATTATTTAATATTCTCACTAAATCAGAAATTATTCTGGAGCCTTATTACATTCGTTATCATAACGTTATCTATTTATCAGCCTATATATTTATCTTATGGAAACTTAAACTCCGGAGTTGTTGCTGCTTTTTTTGAAACCAACCCGGAAGAATCTTTTGAATTTTTAGGAAAATTAAAATTTAGCCAATTTTTACTGCCATTCTTATTTATTTTATCCGGATATATTTTATATAGACTAAGAAAACAAGCAATACCGGAAACCCCACCGACTCAACAAGAAATGAAACATCAAAAGATCTTAAAGTATGCATTAACGGCAGTAGCAATTCTGAGTATTATTTGGCTCCCTACAAAACATCATTTCGATTATGCTTCCACAGAACAAGTAGATTCCCGTTGGACTTTAGCCAACAGCCCAATAAATCTGATTTCGTTTTATGCGAATATAATAGACAGTGTGAGCGAATATTATAGTGATAAAGAAGACTTAGAATCAGCTAAAAGTATGCGATCTCCTTGGCATATTATTTCCAGTCATCCTAAATATAAAAATTATGTGTTAATTATCGGCGAAAGTGAGAGAAAGGATTATATGTCAAGCTACGGTTTTAAGTTGCCGACAACACCATTCCTGGATAAAACGAATGGATATATTAATGCAGGTTATATTTCTGCTGCGCCGGCAACATACCATTCACTATTAAATACATTATATTTTAAACCCAAAGATAAGGGCGAAAAAAATTATTCTTTTAATATTATCACGTTAGCGAAGGCGGCCGGTATAAAAACCTTCTGGCTATCAAATCAAGGGTGTATAGGAAAATATGACACTCTTGCCAGCAGATCAGGTGCAAGTGCAGATTTTCATTACTTCACGAAAAAAGGTGGATTTATTACCAATAATACCGATGATTTCAAATTACTGGATGAACTTAAAGTCAAATTTAAAGAGAAAAGTTATGCAAATAATACACGACTATTTGTCATTCATTTGATGGGATCTCATCGTAATTTTTGCCAGAGAATCACAAAAGATGAAAAGAAATACGAATTTATAAATGAAAGTTTATCCTGTTATGTCAATAGTATTTTAAAAACGGATAAATTAATTGAAGAGATCGTCTATTTATTAAAAGCACAGAATGAAAGTTATTCTTTAATTTATTTTTCAGATCATGGATTATCGCACAAAAATAAAGAAAGCAAAGAAGAAATAGATTTAGATTTTGGTGAAGAATCAAAACAAAATTTTGAAGTACCCTTTGTTAAACTTTCCAGTGATGACACATCAAGAAATTTAGTGAATGTGAAGCGAAGTGCATTTAATTTTATCTATGGTTATGCCGAATGGTTAGGAATAAAAACAGAAGAATTAAATAATGGCTATGAGTTTTTCTCAAATAAAGATGATAAAGACATTAAAGTATTTAATTTCAGAGAAAATATTTCTTATGACACATTAAAAAACGACAATATACCGAATTTT","","","64853","LSFLLSSVLNLKNQFMFKKFLNYLNSRIFWIWLLFFSFITLIISPENTIYYGMFVIYIIYYLIFSLNQKLFWSLITFVIITLSIYQPIYLSYGNLNSGVVAAFFETNPEESFEFLGKLKFSQFLLPFLFILSGYILYRLRKQAIPETPPTQQEMKHQKILKYALTAVAILSIIWLPTKHHFDYASTEQVDSRWTLANSPINLISFYANIIDSVSEYYSDKEDLESAKSMRSPWHIISSHPKYKNYVLIIGESERKDYMSSYGFKLPTTPFLDKTNGYINAGYISAAPATYHSLLNTLYFKPKDKGEKNYSFNIITLAKAAGIKTFWLSNQGCIGKYDTLASRSGASADFHYFTKKGGFITNNTDDFKLLDELKVKFKEKSYANNTRLFVIHLMGSHRNFCQRITKDEKKYEFINESLSCYVNSILKTDKLIEEIVYLLKAQNESYSLIYFSDHGLSHKNKESKEEIDLDFGEESKQNFEVPFVKLSSDDTSRNLVNVKRSAFNFIYGYAEWLGIKTEELNNGYEFFSNKDDKDIKVFNFRENISYDTLKNDNIPNF","1076338","","conserved hypothetical protein; possible membrane protein","Outer membrane, Inner membrane, Cytoplasm","","
InterPro
IPR000917
Domain
Sulfatase
PF00884\"[241-548]TSulfatase
noIPR
unintegrated
unintegrated
signalp\"[1-45]?signal-peptide
tmhmm\"[21-41]?\"[47-65]?\"[70-90]?\"[120-138]?\"[159-177]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.3e-20) to 3/3 blocks of the IPB003371 family, which is described as \"Integral membrane protein of unknown function\". Interpro entry for IP:IPR003371. IPB003371A 246-269 1.3e-11 IPB003371B 312-326 0.0002 IPB003371C 367-396 0.34","Residues 240 to 519 match (2e-63) PD:PD005703 which is described as COMPLETE PROTEOME MEMBRANE TRANSMEMBRANE INTEGRAL PLASMID PRECURSOR OUTER DCA SIGNAL ","","","","","","","","","","","","Thu Jan 2 19:09:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01596 is paralogously related to AA00116 (1e-93).","","","","","","Residues 241 to 550 (E-value = 5.4e-48) place AA01596 in the Sulfatase family which is described as Sulfatase (PF00884)","","","","","","","","1","","","" "AA01597","1078996","1078373","624","TTGCTCATAAAAGTGCGGTCGTTTTTTGGGGCGTTTTTCGCTAGAATAACAAAAATTTTGCATAGGATACCTTATATCATGTCATTCGATAAACAAAATCTGATTTGGATTGATTTAGAAATGACCGGACTTGATCCGGAAAAAGAACGTATTATTGAAATCGCCACCATCGTGACCGATAAAAATTTAAACATCCTTGCCGAGGGCCCTGTCCTTGCTATTCGCCAGCCCGATGCGTTACTGAATAAAATGAGTGAATGGTGTGTAAAAACCCACACGGCAAACGGCTTGATAGAACGTGTTAAAGCCAGCAAACTCACCAAACACGCGGCAGAGCTACAAACACTTGATTTCTTAAAAAAATACGTTCCGAAAGGCGCCTCCCCGATTTGTGGCAACAGCGTTGCGCAGGACAAACGCTTCCTGTTTAAATACATGCCTGAACTTGCCGACTATTTTCATTATCGCCACCTTGACGTCAGCACCTTAAAAGAACTTGCCGCCCGCTGGAGACCGGACATTTTAAACGGCTTTAATAAGCAAAATACGCATTTGGCGCTGGACGATATTCGTGAATCTATCAAAGAGTTAGCCTATTATCGTGAACATTTTTTGAAGATGGAC","","","24161","LLIKVRSFFGAFFARITKILHRIPYIMSFDKQNLIWIDLEMTGLDPEKERIIEIATIVTDKNLNILAEGPVLAIRQPDALLNKMSEWCVKTHTANGLIERVKASKLTKHAAELQTLDFLKKYVPKGASPICGNSVAQDKRFLFKYMPELADYFHYRHLDVSTLKELAARWRPDILNGFNKQNTHLALDDIRESIKELAYYREHFLKMD","1078371","[FUNCTION] 3'-to-5' exoribonuclease specific for small oligoribonucleotides (by similarity). [SUBCELLULAR LOCATION] Cytoplasmic (potential). [SIMILARITY] Belongs to the oligoribonuclease family. ","oligoribonuclease","Cytoplasm","","
InterPro
IPR006055
Domain
Exonuclease
SM00479\"[33-206]TEXOIII
InterPro
IPR013520
Domain
Exonuclease, RNase T and DNA polymerase III
PF00929\"[34-197]TExonuc_X-T
noIPR
unintegrated
unintegrated
G3DSA:3.30.420.10\"[25-208]Tno description
PTHR11046\"[1-206]TOLIGORIBONUCLEASE, MITOCHONDRIAL
signalp\"[1-28]?signal-peptide


","BeTs to 8 clades of COG1949COG name: Oligoribonuclease (3'->5' exoribonuclease)Functional Class: FThe phylogenetic pattern of COG1949 is ------y---r---efghsn------Number of proteins in this genome belonging to this COG is","Significant hit ( 1.6e-05) to 2/2 blocks of the IPB000520 family, which is described as \"Exonuclease\". Interpro entry for IP:IPR000520. IPB000520A 34-45 0.00034 IPB000520B 184-189 26","Residues 32 to 69 match (5e-14) PD:PD477405 which is described as NUCLEASE 3.1.-.- HYDROLASE OLIGORIBONUCLEASE EXONUCLEASE COMPLETE PROTEOME PROBABLE SMALL MITOCHONDRION ","","","","","","","","","","","Thu Jan 2 19:15:45 2003","Thu Jan 2 19:15:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01597 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 34 to 197 (E-value = 1.5e-35) place AA01597 in the Exonuc_X-T family which is described as Exonuclease (PF00929)","","","","","Zhang,X., Zhu,L. and Deutscher,M.P. Oligoribonuclease is encoded by a highly conserved gene in the 3'-5' exonuclease superfamily. J. Bacteriol. 180 (10): 2779-2781 (1998) [PubMed: 9573169].","","Thu Jan 2 19:15:45 2003","1","","","" "AA01598","1079094","1080026","933","ATGTTGGGCGCGTCGCAAGAAGGCTTGGTGGTGACCCGCTATGCCCGTCATGCGGATGTCGAAAATGAGCGGGGTGAGATTTTCCGTTGTAATTTGCGTCGGACCTTAGCTGGTGTAGTGGTCGGTGACCGTGTAATTTGGCGACAAGGCAACGAACAATTGCAGGGCGTGAGTGGGGTAATTGAAGGTGTTCATCCGCGCCAAAATGAAATTTCCCGCCCGGATTATTATGATGGAATGAAAGTGATCGCCGCCAATATTGATCGCATTATTATCATTTCTTCCGTATTGCCGAGTTTATCGTTAAATATTATCGATCGTTATTTAGTGGTGTGTGAAGAAGCCAAAATTGAACCGATTATCGTGTTAAATAAGGCGGATATGTTGACGGAGTTGCAGTGGCAGGAGGTGGATTCGCAACTGGAAATTTACCGTAAAATCGGTTACCAAACGTTGATGGTGTCTGCTCAGAGCGGAAAAAATCTGGAAAAACTGACCGCACTTTTATCCGACGGTGTATCTATTTTTGTCGGGCAATCCGGTGTGGGAAAATCCAGTTTGATTAATGCGGTGCTACCTCATGTTGAAGCGCAAGTCGGGGAAATCAGTTCCACTTCAGGTTTGGGACAGCATACCACCACATCATCCCGTTTATATCATTTGCCGCAAGGCGGCAGTCTGATTGATTCGCCGGGAATTCGGGAATTCGGTTTGTGGCATCTGGAAGATGAGCAGATTACAAGAGGTTATCGTGAATTTCAGACCGTGTTGGGAACTTGTAAATTCCGTGATTGTAAGCATTTAAATGACCCGGGGTGCGCTTTGCGACAAGCCGTGGAAGAAGGAAAAATTAGCGCTGTGCGCTACGAAAATTATCACCGCTTACTCACCAGCCGAAGGGACATGAAATCACAACGGCATTTTTCTATTGAG","","","39144","MLGASQEGLVVTRYARHADVENERGEIFRCNLRRTLAGVVVGDRVIWRQGNEQLQGVSGVIEGVHPRQNEISRPDYYDGMKVIAANIDRIIIISSVLPSLSLNIIDRYLVVCEEAKIEPIIVLNKADMLTELQWQEVDSQLEIYRKIGYQTLMVSAQSGKNLEKLTALLSDGVSIFVGQSGVGKSSLINAVLPHVEAQVGEISSTSGLGQHTTTSSRLYHLPQGGSLIDSPGIREFGLWHLEDEQITRGYREFQTVLGTCKFRDCKHLNDPGCALRQAVEEGKISAVRYENYHRLLTSRRDMKSQRHFSIE","1080024","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR004881
Family
GTPase EngC
PF03193\"[7-297]TDUF258
TIGR00157\"[39-298]TTIGR00157: ribosome small subunit-dependent
InterPro
IPR010914
Domain
EngC GTPase
PS50936\"[85-234]TENGC_GTPASE
noIPR
unintegrated
unintegrated
G3DSA:1.10.40.50\"[239-306]Tno description
G3DSA:3.40.50.300\"[75-238]Tno description
PTHR11089\"[87-243]TGTP-BINDING PROTEIN-RELATED


","BeTs to 13 clades of COG1162COG name: Predicted GTPasesFunctional Class: RThe phylogenetic pattern of COG1162 is -------qv-rlbcefghsn-j--twNumber of proteins in this genome belonging to this COG is","","Residues 175 to 232 match (2e-10) PD:PD001145 which is described as PROTEOME COMPLETE GTP-BINDING GTPASE TRNA HFLX PROBABLE SIMILAR CHLOROPLAST ENVELOPE ","","","","","","","","","","","","Thu Jan 2 19:11:37 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01598 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 144 to 297 (E-value = 1.1e-83) place AA01598 in the DUF258 family which is described as Protein of unknown function, DUF258 (PF03193)","","","","","","","","1","","","" "AA01599","1080250","1080504","255","ATGTATTCAAAAGATGTTGAAATTACTGCAGCTAATGGTTTACACACGCGTCCGGCAGCGCAATTTGTAAAAGAAGCGAAAGCGTTTGCTTCTGACATTACGGTCACATCCGCCGGTAAAAGTGCCAGTGCGAAAAGTTTGTTTAAATTACAGACACTGGCGTTAACTCAGGGAACTGTGATTACTATCTCGGCAGAAGGTGAGGACGCGGAAAAAGCGGTTGAGCATCTTGTTGCATTAATTCCTACATTAGAG","","","10189","MYSKDVEITAANGLHTRPAAQFVKEAKAFASDITVTSAGKSASAKSLFKLQTLALTQGTVITISAEGEDAEKAVEHLVALIPTLE","1080502","[FUNCTION] This is a component of the phosphoenolpyruvate dependent sugar phosphotransferase system (PTS), a majorcarbohydrate active transport system. the phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein hpr by enzyme I. phospho-HPR then transfers it to the permease (enzymes II/III). HPR is common to all PTS (by similarity). [SUBCELLULAR LOCATION] Cytoplasmic (by similarity). [SIMILARITY] Belongs to the HPR family.","phosphocarrier protein HPr","Cytoplasm, Periplasm","","
InterPro
IPR000032
Family
Phosphotransferase system, phosphocarrier HPr protein
PD002238\"[10-80]TQ9CMD2_PASMU_Q9CMD2;
PR00107\"[13-29]T\"[38-53]T\"[53-70]TPHOSPHOCPHPR
G3DSA:3.30.1340.10\"[1-85]Tno description
PF00381\"[1-84]TPTS-HPr
InterPro
IPR001020
PTM
Phosphotransferase system, HPr histidine phosphorylation site
PS00369\"[13-20]TPTS_HPR_HIS
InterPro
IPR002114
PTM
Phosphotransferase system, HPr serine phosphorylation site
PS00589\"[39-54]TPTS_HPR_SER
InterPro
IPR005698
Family
Phosphotransferase system, HPr
TIGR01003\"[1-82]TPTS_HPr_family: phosphocarrier, HPr family


","BeTs to 11 clades of COG1925COG name: Phosphotransferase system, HPr-related proteinsFunctional Class: GThe phylogenetic pattern of COG1925 is ---------d-lb-efghsn-j-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 5.4e-38) to 2/2 blocks of the IPB001020 family, which is described as \"Histidine phosphorylation site in HPr protein\". Interpro entry for IP:IPR001020. IPB001020A 8-35 8.5e-16 IPB001020B 39-77 6.7e-21Significant hit ( 4.6e-27) to 3/3 blocks of the PR00107 family, which is described as \"Phosphocarrier protein signature\". Prints database entry for PR:PR00107. PR00107A 13-29 1.1e-09 PR00107B 38-53 2.1e-05 PR00107C 53-70 1.2e-08Significant hit ( 1.6e-06) to 2/2 blocks of the IPB002114 family, which is described as \"Serine phosphorylation site in HPr protein\". Interpro entry for IP:IPR002114. IPB002114A 2-32 0.0071 IPB002114B 44-85 0.083","Residues 1 to 80 match (6e-26) PD:PD002238 which is described as HPR PHOSPHOTRANSFERASE PHOSPHOCARRIER PROTEOME COMPLETE SYSTEM PHOSPHORYLATION HISTIDINE-CONTAINING SUGAR PTS ","","","","","","","","","","","Thu Jan 2 19:21:10 2003","Thu Jan 2 19:21:10 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01599 is paralogously related to AA00332 (5e-11).","","","","","","Residues 1 to 84 (E-value = 2.1e-39) place AA01599 in the PTS-HPr family which is described as PTS HPr component phosphorylation site (PF00381)","","","","","e Reuse,H. and Danchin,A. The ptsH, ptsI, and crr genes of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: acomplex operon with several modes of transcription J. Bacteriol. 170 (9), 3827-3837 (1988) PubMed: 2457575 De Reuse,H., Roy,A. and Danchin,A. Analysis of the ptsH-ptsI-crr region in Escherichia coliK-12: nucleotide sequence of the ptsH gene Gene 35 (1-2), 199-207 (1985) PubMed: 2411636 Saffen,D.W., Presper,K.A., Doering,T.L. and Roseman,S. Sugar transport by the bacterial phosphotransferase system. Molecular cloning and structural analysis of the Escherichia coli ptsH, ptsI, and crr genes J. Biol. Chem. 262 (33), 16241-16253 (1987) PubMed: 2960675 ","","Thu Jan 2 19:21:10 2003","1","","","" "AA01600","1080621","1082345","1725","ATGATTTCAGGAATTCCGGCCTCTCCGGGTATTGTTTTTGGCAAAGCACTTGTGCTTAAAGAAGAAAAAATTGTACTTGATACGCAAAAAATTAAAGACAGCCAAATTGAAGATGAAGTGGCACGCTTTTATGCGGGACGCGATGCTGCGGTTGAACAGTTAAATTCTATTAAAGATGGGGCCTATCAATCTTTGGGGGAAGAGAAGGCGGCTATCTTTGAAGGTCATTTAATGATTTTGGAAGATGAGGAACTGGAAGAAGAAATCATTGATTACCTTCGTTCAAATCATGTCAATGCTGCAGTTGCCGCGAATGTGATTATCGATCAGCAAGTGGCGATGTTATCGGAAATTGATGATGAATATTTGAAAGAACGTGCCGGCGATATTCGCGATATTGGTAATCGTTTAATTAAAAATATTTTAGGTATGCATATCGTTGATTTAGGTGAAATTAACGAAGAAGCGATTTTGGTTGCCTATGATTTAACCCCTTCCGAAACCGCACAGTTAAATTTGGATAAAGTGTTAGGCTTTGTTACCGACATTGGTGGTCGCACCTCCCATACTTCAATTATGGCGCGCTCTTTGGAATTGCCGGCAATCGTGGGAACCAATAACGTTACCCATAAAGTGAATACCGGGGATTACCTGATCCTGGATGCGCTAAATAACGTAGTTTATGTCAATCCTTCTCAAGAAGATATTCAACGCTTGAAAGCATTACAAGCGAAATTGGTGGAAGAAAAAGCCGAATTAGCAAAATTAAAAGACTTACCGGCGCTCACGTTAGATGGTCACCGTGTCGATGTGGTGGCGAATATCGGTACAATCCGTGATGTGGAAGGCGCTGAACGTAACGGCGCGGAAGGTGTTGGTTTATACCGTACCGAATTTTTGTTCATGGACCGCGACCAGCTACCAACCGAAGAAGAACAGTTTATTGCGTATAAAGAAGTGGTAGAAGCCATGAATGGGAATCTCGTGGTGTTGCGTACCATGGATATCGGTGGCGATAAAGAACTGCCATATTTGAATCTGCCGAAAGAAATGAACCCGTTCCTTGGCTGGCGTGCAATTCGCATTGCGTTGGATCGTCGTGAGATTCTACATGCGCAATTAAGAGCCGTGTTGCGCGCTTCTGCTTACGGAAAACTAGCGGTGATGTTCCCGATGATTATTTCCGTGGAAGAAATTCGCGAATTAAAATCGGTGGTTGAAAAATTAAAAGTTGAATTGCGTAACGAAGGCAAAGCCTTTGATGAAGATATTCAAATCGGTGTAATGGTTGAAACCCCGGCGGCGGCCGTCAATGCCGGATTCTTAGCAAAAGAAGTGGATTTCTTTAGTATCGGTACCAATGATTTAGCACAATACACTTTGGCGGTTGACCGTGGTAACGAGTTAATTTCCCATCTCTATAACCCAATGAGTCCATCGGTGCTGAACTTAATTAAACAGGTGATTGATGCCTCTCATGCAGAAGGAAAATGGACCGGTATGTGTGGTGAGTTGGCAGGTGATGAACGCGCGACGATTCTATTGTTGGGTATGGGCTTGGATGAGTTCAGTATGAGTGCCATTTCTGTGCCGCGCATTAAGAAATTAATCCGTAATGTGAATTTCCAAGATGCAAAAGCCTTAGCTGAAAAAGCGTTACAGCAACCGACGGCTGCCGAAATTGAAAGTTTGGTCTCTGATTTTTTGTATGAAAAAGCATTAAAT","","","64847","MISGIPASPGIVFGKALVLKEEKIVLDTQKIKDSQIEDEVARFYAGRDAAVEQLNSIKDGAYQSLGEEKAAIFEGHLMILEDEELEEEIIDYLRSNHVNAAVAANVIIDQQVAMLSEIDDEYLKERAGDIRDIGNRLIKNILGMHIVDLGEINEEAILVAYDLTPSETAQLNLDKVLGFVTDIGGRTSHTSIMARSLELPAIVGTNNVTHKVNTGDYLILDALNNVVYVNPSQEDIQRLKALQAKLVEEKAELAKLKDLPALTLDGHRVDVVANIGTIRDVEGAERNGAEGVGLYRTEFLFMDRDQLPTEEEQFIAYKEVVEAMNGNLVVLRTMDIGGDKELPYLNLPKEMNPFLGWRAIRIALDRREILHAQLRAVLRASAYGKLAVMFPMIISVEEIRELKSVVEKLKVELRNEGKAFDEDIQIGVMVETPAAAVNAGFLAKEVDFFSIGTNDLAQYTLAVDRGNELISHLYNPMSPSVLNLIKQVIDASHAEGKWTGMCGELAGDERATILLLGMGLDEFSMSAISVPRIKKLIRNVNFQDAKALAEKALQQPTAAEIESLVSDFLYEKALN","1082343","[FUNCTION] This is a component of the phosphoenolpyruvate dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (pep) tothe phosphoryl carrier protein (hpr). Enzyme i is common to all pts (by similarity). [CATALYTIC ACTIVITY] phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine. [subunit] homodimer (by similarity). [SUBCELLULAR LOCATION] Cytoplasmic. [SIMILARITY] Belongs to the pep-utilizing enzymes family. ","phosphotransferase system enzyme I","Cytoplasm","","
InterPro
IPR000121
Domain
PEP-utilizing enzyme
PD000940\"[268-531]TQ9CMD3_PASMU_Q9CMD3;
PF02896\"[250-542]TPEP-utilizers_C
PS00742\"[447-465]TPEP_ENZYMES_2
InterPro
IPR006318
Domain
Phosphoenolpyruvate-protein phosphotransferase
PR01736\"[293-312]T\"[447-462]T\"[464-479]T\"[500-512]TPHPHTRNFRASE
TIGR01417\"[2-566]TPTS_I_fam: phosphoenolpyruvate-protein phos
InterPro
IPR008279
Domain
PEP-utilising enzyme, mobile region
PF00391\"[145-225]TPEP-utilizers
PS00370\"[184-195]TPEP_ENZYMES_PHOS_SITE
InterPro
IPR008731
Domain
phosphotransferase system, PEP-utilising enzyme, N-terminal
PF05524\"[2-127]TPEP-utilisers_N
noIPR
unintegrated
unintegrated
G3DSA:1.10.274.10\"[21-146]Tno description
G3DSA:3.20.20.60\"[250-573]Tno description
G3DSA:3.50.30.10\"[146-229]Tno description
PTHR22931\"[1-569]TPHOSPHOENOLPYRUVATE DIKINASE-RELATED
PTHR22931:SF10\"[1-569]TPHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE


","No hits to the COGs database.","Significant hit ( 9.5e-81) to 7/7 blocks of the IPB000121 family, which is described as \"PEP-utilizing enzyme\". Interpro entry for IP:IPR000121. IPB000121A 76-86 0.48 IPB000121B 178-204 1.4e-18 IPB000121C 288-300 3e-08 IPB000121D 350-361 1.2e-07 IPB000121E 388-398 0.00052 IPB000121F 431-467 5.3e-25 IPB000121G 496-509 3e-07Significant hit ( 3.8e-44) to 6/12 blocks of the IPB002192 family, which is described as \"Pyruvate phosphate dikinase, PEP/pyruvate binding domain\". Interpro entry for IP:IPR002192. IPB002192E 178-204 9.3e-08 IPB002192G 270-301 1.4e-09 IPB002192I 350-359 0.11 IPB002192J 373-398 1.4 IPB002192K 433-467 1.5e-16 IPB002192L 496-513 9.8Significant hit ( 2.2e-12) to 1/2 blocks of the IPB002114 family, which is described as \"Serine phosphorylation site in HPr protein\". Interpro entry for IP:IPR002114. IPB002114B 496-539 2.2e-12","","","","","","","","","","","","Thu Jan 2 19:43:57 2003","Thu Jan 2 19:39:59 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01600 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 250 to 542 (E-value = 1.2e-189) place AA01600 in the PEP-utilizers_C family which is described as PEP-utilising enzyme, TIM barrel domain (PF02896)","","","","","De Reuse,H. and Danchin,A. The ptsH, ptsI, and crr genes of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: a complex operon with several modes of transcription J. Bacteriol. 170 (9), 3827-3837 (1988) PubMed: 2457575 Saffen,D.W., Presper,K.A., Doering,T.L. and Roseman,S. Sugar transport by the bacterial phosphotransferase system. Molecular cloning and structural analysis of the Escherichia coli ptsH, ptsI, and crr genes J. Biol. Chem. 262 (33), 16241-16253 (1987) PubMed: 2960675 ","","Thu Jan 2 19:43:57 2003","1","","","" "AA01601","1082409","1082906","498","ATGGGTTTATTTGACAAATTATTTGGTTCAAAAGACAAGAAAGCGATGGATGTGGAAATCTATGCGCCACTTTCCGGAGAAATCGTGAACATTGAAGATGTTCCGGATGTCGTATTCTCTGAAAAAATCGTTGGTGACGGTGTTGCAATTCGCCCGACCGGTAACAAACTGGTTGCACCGGTGGATGGCGTAGTTGGTAAAATCTTTGAAACTAATCATGCCTTTTCAATGGAATCAAAAGAAGGCGTTGAATTGTTTGTACACTTCGGCATTGATACCGTTGAATTGAAAGGCGAAGGATTTACCCGTGTTGCAAAAGAAGGTCAAACCGTAAAACGTGGTGATACCATTATTGAATTGGATCTTCCGTTATTAGAAGCAAAAGCCAAATCTGTATTAACGCCGGTGGTGATCTCTAATATGGACGAAATCAGTAATATGGAGAAAAAATCCGGTGAAGTGGTTGCCGGTGATTCCGTTGTATTGGTTCTGAAAAAA","","","17875","MGLFDKLFGSKDKKAMDVEIYAPLSGEIVNIEDVPDVVFSEKIVGDGVAIRPTGNKLVAPVDGVVGKIFETNHAFSMESKEGVELFVHFGIDTVELKGEGFTRVAKEGQTVKRGDTIIELDLPLLEAKAKSVLTPVVISNMDEISNMEKKSGEVVAGDSVVLVLKK","1082904","[CATALYTIC ACTIVITY] Protein N-phosphohistidine + sugar = proteinhistidine + sugar phosphate.[SUBCELLULAR LOCATION] Cytoplasmic.[FUNCTION] This is a component of the phosphoenolpyruvate dependent sugar phosphotransferase system (P[TS), a majorcarbohydrate active -transport system. The IICD domains contain the sugar binding site and the transmembrane channel; the IIA domain contains the primary phosphorylation site (the donor is phospho-hpr); IIA transfers its phosphoryl group to the iib domain which finally transfers it to the sugar. [MISCELLANEOUS] The nonphosphorylated factor III is an inhibitor for uptake of certain sugars such as maltose, melibiose, lactose, & glycerol. Phosphorylated factor III, however, may be an activator for adenylate cyclase. It is an important regulatory protein for cell metabolism. [SIMILARITY] Contains 1 pts EIIA domain. ","PTS system, glucose-specific IIA componen","Cytoplasm","","
InterPro
IPR001127
Domain
Phosphotransferase system, sugar-specific permease EIIA 1 domain
PD002243\"[11-166]TPTGA_HAEIN_P45338;
PF00358\"[15-147]TPTS_EIIA_1
TIGR00830\"[20-140]TPTBA: PTS system, glucose subfamily, IIA co
PS51093\"[36-140]TPTS_EIIA_TYPE_1
PS00371\"[82-94]TPTS_EIIA_TYPE_1_HIS
noIPR
unintegrated
unintegrated
G3DSA:2.70.70.10\"[6-166]Tno description


","No hits to the COGs database.","Significant hit ( 2.9e-51) to 2/2 blocks of the IPB001127 family, which is described as \"Sugar-specific permease, EIIA 1 domain\". Interpro entry for IP:IPR001127. IPB001127A 20-54 2.3e-21 IPB001127B 59-101 1e-28","Residues 2 to 166 match (1e-69) PD:PD002243 which is described as COMPONENT PTS PHOSPHOTRANSFERASE COMPLETE PROTEOME IIABC SYSTEM ENZYME SYSTEM TRANSFERASE ","","","","","","","","","","","Thu Jan 2 19:50:15 2003","Thu Jan 2 19:50:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01601 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 36 to 140 (E-value = 8.7e-61) place AA01601 in the PTS_EIIA_1 family which is described as phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 1 (PF00358)","","","","","De Reuse,H. and Danchin,A. The ptsH, ptsI, and crr genes of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: a complex operon with several modes of transcription J. Bacteriol. 170 (9), 3827-3837 (1988) PubMed: 2457575 Hall,B.G. and Sharp,P.M. Molecular population genetics of Escherichia coli: DNA sequence diversity at the celC, crr, and gutB loci of naturalisolates Mol. Biol. Evol. 9 (4), 654-665 (1992) PubMed: 1630305 Saffen,D.W., Presper,K.A., Doering,T.L. and Roseman,S. Sugar transport by the bacterial phosphotransferase system. Molecular cloning and structural analysis of the Escherichia coli ptsH, ptsI, and crr genes. J. Biol. Chem. 262 (33): 16241-16253 (1987) [PubMed: 2960675].Hall,B.G. and Sharp,P.M. Molecular population genetics of Escherichia coli: DNA sequence diversity at the celC, crr, and gutB loci of natural isolates. Mol. Biol. Evol. 9 (4): 654-665 (1992) [PubMed: 1630305].","","Thu Jan 2 19:50:15 2003","1","","","" "AA01603","1085074","1083038","2037","ATGACAAATCCATTACTCACACCCACCACCTTACCCGCATTTTCCAAAATCGAGCCGCAATATATCGAACCTGCCATCAAGCAACTGATTCAAGAAAATCGTGAAACCATCGAACGCGTGGTAAAACAACCGCACTTTACTTGGGAAAATTTCATCCTGCCGTTAACGGAAGCCGGCGATCGTTTAAGCAAAGTTTGGTCGCCGATTTCGCATTTGAATTCGGTAAAAAATAGCTCCGAATTACGCGAAGCCTACCAAGCCTGTCTGCCGCTATTGGCGGAATACAGCACGTGGGTCGGCCAACATCAGGGGTTATATGAAGCCTATTTGCAATTAAAAAACAGCCCTGAATTTGCCGGTTACAGCCAAGCACAGAAAAAAGCCATTGAAAACAGCCTGCGTGATTTCAAATTATCGGGCATCTCCTTGCCGCCGGAAAAACAACAACGTTATGGCGAAATCACCGCGCGATTATCTGAGCTCACCTCCCAATTCAGCAATAACGTGCTGGACGCCACCATGGGCTGGGAGAAAGTCATTGAAGACGTAAACCTTCTTAAAGGCTTGCCGGAATCCGCACTGGAAGCGGCAAAACAATCGGCGGAAAGCAAAGGGTTAAGCGGCTATCGCTTTACCTTGGAATTTCCGAGCTACATTCCGGTGATGACATATTGTGAAAACCGTGAATTGCGCGAAGAGATGTATCGTGCTTTCGCCACCCGCGCCTCCGATCAAGGTCCGAATGCGGGCAAATGGGATAATTCTGCAATTATGCAGGAAATTTTGAGTCTGCGCGTTGAATTAGCAAAATTGCTGGATTTCAACACCTATACCGAATTATCCCTTGCCACCAAAATGGCGGAAAATCCACAACAGGTGTTGGACTTCTTAGAAAATCTCGCTACCCGCGCCAAAGCACAAGGCGAACATGAATTACAGGAATTAAAAGATTTCTGCAAAACACACTATAATTTGACCGCACTTGAGCTTTGGGATTTGTCCTTTTACAGCGAGAAACAAAAACAACATTTATATGCCATTAGCGATGAAGAATTGCGCCCTTATTTCCCGGAAGATCGTGTCCTTAACGGCTTATTTGAACTGATTAAACGCATTTTCAACATTCGTGCCGTAGAACGTCATGATGTGGAAACCTGGCATAAAGATGTGCGCTTCTTTGACTTAATTGATGAAAATGATGAAGTTCGCGGCAGCTTCTATTTAGATTTGTATGCCCGTGAACATAAACGCGGCGGCGCATGGATGGACGATTGTATCGGTCGTCGCAAAACCATCGACGGTAGTCTACAAAAACCGGTCGCCTATTTAACCTGTAACTTCAATCGTCCGCTCGGTGATCAACCGGCATTATTCACCCATGATGAAGTCACTACCCTGTTCCATGAATTCGGGCATGGGTTACATCATATGCTCACCAAAATCGATGTGGCGGATGTCGCCGGCATTAACGGTGTGCCTTGGGATGCCGTGGAATTGCCAAGTCAATTTATGGAAAACTGGTGCTGGGAAGAAGAAGCGTTGCAGTTTATTTCCGGTCATTATCAAACGGGTGAACCGTTACCAAAAGAGAAACTGACCCAATTACTCAAAGCGAAAAATTTCCAAGCGGCGATGTTTGTTTTGCGTCAGCTGGAATTCGCGTTGTTTGATTTCCGTTTGCATCATACTTTTGAACCGAATAAACAGAATCAAGTATTGGATATGCTACACGCCGTGAAACGCCAAGTTGCGGTGATTCCGGGTGCACAATGGGGAAGAATGCCGCACAGCTTCAGCCACATTTTTGCCGGCGGTTATGCGGCGGGCTATTACAGCTATTTATGGGCGGAAGTGTTATCGGCAGATGCTTATTCTCGCTTTGAGGAAGAAGGCATTTTCAATGCGAAAACCGGTCAATCTTTCTTGGATGAAATCCTCACCAAAGGCGGTTCCGAAGAGCCGATGACGTTATTCAAAAACTTCCGTGGTCGTGAACCGCAATTAGATGCGCTACTCCGCCACAAAGGCATTGCAAAT","","","78045","MTNPLLTPTTLPAFSKIEPQYIEPAIKQLIQENRETIERVVKQPHFTWENFILPLTEAGDRLSKVWSPISHLNSVKNSSELREAYQACLPLLAEYSTWVGQHQGLYEAYLQLKNSPEFAGYSQAQKKAIENSLRDFKLSGISLPPEKQQRYGEITARLSELTSQFSNNVLDATMGWEKVIEDVNLLKGLPESALEAAKQSAESKGLSGYRFTLEFPSYIPVMTYCENRELREEMYRAFATRASDQGPNAGKWDNSAIMQEILSLRVELAKLLDFNTYTELSLATKMAENPQQVLDFLENLATRAKAQGEHELQELKDFCKTHYNLTALELWDLSFYSEKQKQHLYAISDEELRPYFPEDRVLNGLFELIKRIFNIRAVERHDVETWHKDVRFFDLIDENDEVRGSFYLDLYAREHKRGGAWMDDCIGRRKTIDGSLQKPVAYLTCNFNRPLGDQPALFTHDEVTTLFHEFGHGLHHMLTKIDVADVAGINGVPWDAVELPSQFMENWCWEEEALQFISGHYQTGEPLPKEKLTQLLKAKNFQAAMFVLRQLEFALFDFRLHHTFEPNKQNQVLDMLHAVKRQVAVIPGAQWGRMPHSFSHIFAGGYAAGYYSYLWAEVLSADAYSRFEEEGIFNAKTGQSFLDEILTKGGSEEPMTLFKNFRGREPQLDALLRHKGIAN","1083036","[FUNCTION] May play a specific role in the degradation of signal peptides after they are released from precursor forms ofsecreted proteins. can cleave n-acetyl-l-ala4 (by similarity). [CATALYTIC ACTIVITY] Hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-Pro-Ala is cleaved, but not Z-(Gly)5.[COFACTOR] Binds 1 zinc ion (By similarity).[SIMILARITY] Belongs to peptidase family M3. ","oligopeptidase A","Cytoplasm, Extracellular","","
InterPro
IPR001567
Domain
Peptidase M3A and M3B, thimet/oligopeptidase F
PF01432\"[221-677]TPeptidase_M3
InterPro
IPR006025
Binding_site
Peptidase M, neutral zinc metallopeptidases, zinc-binding site
PS00142\"[465-474]?ZINC_PROTEASE
noIPR
unintegrated
unintegrated
G3DSA:1.10.1370.10\"[139-677]Tno description
G3DSA:1.20.1050.40\"[5-134]Tno description
PTHR11804\"[352-678]TPROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED
PTHR11804:SF7\"[352-678]TOLIGOPEPTIDASE A


","BeTs to 9 clades of COG0339COG name: Zn-dependent oligopeptidasesFunctional Class: EThe phylogenetic pattern of COG0339 is ------y--d---cefghsn-j----Number of proteins in this genome belonging to this COG is","","Residues 199 to 286 match (3e-07) PD:PD432198 which is described as COMPLETE CARBOXYPEPTIDASE PROTEOME PEPTIDYL-DIPEPTIDASE DIPEPTIDYL DCP HYDROLASE II ZINC METALLOPROTEASE ","","","","","","","","","","","Fri Nov 21 17:04:25 2003","Thu Jan 2 19:56:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01603 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 221 to 677 (E-value = 4.8e-225) place AA01603 in the Peptidase_M3 family which is described as Peptidase family M3 (PF01432)","","","","","Conlin,C.A., Trun,N.J., Silhavy,T.J. and Miller,C.G. Escherichia coli prlC encodes an endopeptidase and is homologous to the Salmonella typhimurium opdA gene J. Bacteriol. 174 (18), 5881-5887 (1992) PubMed: 1325967 Conlin,C.A. and Miller,C.G. Location of the prlC (opdA) gene on the physical map of Escherichia coli J. Bacteriol. 175 (17), 5731-5732 (1993) PubMed: 8366062 ","","Thu Jan 2 19:56:55 2003","1","","","" "AA01604","1085186","1085578","393","TTGCGAATAATTTTTATTTTGAGGTTCTCAATGAAGTATTTTTACATCGGACTTGGCTTTATCTTTTTGGCATTAGGTATTGTCGGTATTGTCCTTCCTCTTTTGCCTACTACGCCGTTTTTGCTGCTGACCTTATTTTGTTTTGCCAAGGGGTCTGACCGTTTGCATAACTGGTTCATCGGCACAAAAATCTATCAAAACCATCTGAAAGATTTCCAGCAACAACGCGCACTAACCAAGAAAGCGAAAATCTATATTTTGAGCTTTTCTACCTCTATGCTATTGCTAGGCTTTTATTTTACGCCGAGTATCATTGGTAAAAGTATTATTATTGCTGTCCTCCTGATTAAATATTGGTGCTTCTTTTTCTGGATCAAAACCCTCAAAGAAGAG","","","15343","LRIIFILRFSMKYFYIGLGFIFLALGIVGIVLPLLPTTPFLLLTLFCFAKGSDRLHNWFIGTKIYQNHLKDFQQQRALTKKAKIYILSFSTSMLLLGFYFTPSIIGKSIIIAVLLIKYWCFFFWIKTLKEE","1085576","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR007401
Family
Protein of unknown function DUF454
PF04304\"[52-126]TDUF454
noIPR
unintegrated
unintegrated
signalp\"[1-29]?signal-peptide
tmhmm\"[15-33]?\"[39-59]?\"[79-99]?\"[105-125]?transmembrane_regions


","BeTs to 5 clades of COG2832COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG2832 is ---------d----efgh-n------Number of proteins in this genome belonging to this COG is","","Residues 11 to 121 match (1e-21) PD:PD079045 which is described as COMPLETE PROTEOME MEMBRANE PHAGE SP1261 SAV0166 NMB0571 PA1439 CPE0228 DR1457 ","","","","","","","","","","","","Thu Jan 2 20:04:33 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01604 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 52 to 126 (E-value = 1.7e-23) place AA01604 in the DUF454 family which is described as Protein of unknown function (DUF454) (PF04304)","","","","","","","","1","","","" "AA01605","1085714","1085589","126","TTGGGGTTGGTCATCACATCCGTTCAACCCAAAAACACTGAAAAAAAGCACCGCACTTTTAAAGTGGAAAATACGCATTTAAATGAATTCAATGAAATAAATGCGCACATTATACATCAGTCTGTT","","","4848","LGLVITSVQPKNTEKKHRTFKVENTHLNEFNEINAHIIHQSV","1085589","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 15:39:04 2004","Thu Feb 26 15:39:04 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01605 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 15:39:04 2004","","","","","","","","","","","","","1","","","" "AA01607","1085784","1087172","1389","TTGCTGGTGCGTGGTGTTTATTCCGACTTATTCTTGAACCCATTGCAAGCTTCAAATATTGAGCAAATCGCCTTTTTGCGCGATATTTTTGAAGGTTTGGTGATTTATGATCCTCAAGGCAATGTGGTGCCGGCAGTGGCGGAAAGCTGGCAAACCAAAGACAACAAAATCTGGCACTTCACCTTACGAAAAGAAGCAATATGGTCTAACGGCGAACCGGTGACTGCGCAGCAATTTGTTGCAAGCTGGCAACGGCTGGCGCAATCGGATTCTCCTTTAAAGCACTATTTACGCTACCTTAACTTAGTCAACGCGGAGAAAGTGTTACAGCAAACTCTGCTGCCAGAGCAGTTGGGAATTGTCGCGGAAAATGACCGCACTTTACGCTTAACTTTAGATAAAGCGACCCCTTACTTGCCGCAAATGCTGGCGCATATCAGCCTGTTGCCACAATATTTGTCGCCACATGAAGGCATTGTGACCAACGGGGCGTATCAAGTGATGGGGCAGCAAGGCAATCTCATCCATTTGGAAAAGAACCCGCAATATTGGGCGAAAGAAAAAGTGGCGTTTAAAAATGTGGATTATCAGAAAATCGCACTGCAACAGGACGTCAGCGCCTTAGATGTGGTGTGGCAGCCGCAGCAACAAACGGATCAAACGCAATACTTCCCGCAACTTTGCACCTATTTTTACACCTTTAATTTTAACATGCCACAACTGGCGCAAAGCCCGGTGCGTAAGGCATTGGCAATGATGACATCTGCCCGCAGTTTATTGCCGGAAAGTAAAAACAGGATTCCTTTAACGGATAATTTTTTACCAATTTCCATGCAAACCATCGATAGCCGGTGGGAGCAAACGCCGGTTGAACAATTATTAAGCCAAGCGCGAATTGGAGAGAAGGCACCGCTCAAACTGACCCTAAGTTACGATCAATCAGAAGTGCAAAGTCAACTGGTGCAGGGGTTGATTCGCACGTGGTCGCAATCGGACATGATTCAGATTATCGGCGAAGGGATGCCGAAACAACAATTGCTGGAGAACATTGCTAAAGGCGAGTTTCAAATCGCCCGCGCCGGTTGGTGTGCCGATTATAACGAACCATCCGCATTTTTAAGCCTGTTCTACAGCCGTAGCCCGGATAACAAAAGCGGTTATAGTAACGACGAACTGGATGGCTTATTTGAACAAAGCCTGAAAGTCATTCTACCGGCAGAACGCACCGCACTTTACGGACGAATCGAGCAAATCCTGCAAGAGGAAAATGTGGTTCTGCCGTTATATCAATCCACCGTTCCCGTCTATCTCAACCCCACACTAAACGGCTACGACCCCGCCAACCCGACGGAAGTTATTTATAGCAAGGATTTGTTTCGTAAGGTTAGA","","","58339","LLVRGVYSDLFLNPLQASNIEQIAFLRDIFEGLVIYDPQGNVVPAVAESWQTKDNKIWHFTLRKEAIWSNGEPVTAQQFVASWQRLAQSDSPLKHYLRYLNLVNAEKVLQQTLLPEQLGIVAENDRTLRLTLDKATPYLPQMLAHISLLPQYLSPHEGIVTNGAYQVMGQQGNLIHLEKNPQYWAKEKVAFKNVDYQKIALQQDVSALDVVWQPQQQTDQTQYFPQLCTYFYTFNFNMPQLAQSPVRKALAMMTSARSLLPESKNRIPLTDNFLPISMQTIDSRWEQTPVEQLLSQARIGEKAPLKLTLSYDQSEVQSQLVQGLIRTWSQSDMIQIIGEGMPKQQLLENIAKGEFQIARAGWCADYNEPSAFLSLFYSRSPDNKSGYSNDELDGLFEQSLKVILPAERTALYGRIEQILQEENVVLPLYQSTVPVYLNPTLNGYDPANPTEVIYSKDLFRKVR","1087170","[FUNCTION] This protein is a component of the oligopeptide permease, a binding protein-dependent transport system, itbinds peptides up to five amino acids long with high affinity. [SUBCELLULAR LOCATION] periplasmic. [SIMILARITY] Belongs to the bacterial extracellular solute-binding protein family 5. ","oligopeptide transporter, periplasmic-binding protein","Periplasm","","
InterPro
IPR000914
Family
Bacterial extracellular solute-binding protein, family 5
PF00496\"[41-384]TSBP_bac_5
noIPR
unintegrated
unintegrated
G3DSA:3.10.105.10\"[228-429]Tno description
G3DSA:3.90.76.10\"[1-171]Tno description


","No hits to the COGs database.","Significant hit ( 4.6e-07) to 2/3 blocks of the IPB000914 family, which is described as \"Bacterial extracellular solute-binding protein, family 5\". Interpro entry for IP:IPR000914. IPB000914A 44-51 1.7 IPB000914B 54-71 0.00012","Residues 304 to 373 match (2e-07) PD:PD430398 which is described as COMPLETE PROTEOME BINDING ABC OLIGOPEPTIDE TRANSPORTER DIPEPTIDE DPPA PERIPLASMIC ANTIGEN ","","","","","","","","","","","Fri Jan 3 12:06:10 2003","Fri Jan 3 12:06:10 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01607 is paralogously related to AA02891 (6e-30), AA02892 (3e-17), AA00458 (5e-11) and AA01573 (8e-06).","","","","","","Residues 1 to 460 (E-value = 2.9e-71) place AA01607 in the SBP_bac_5 family which is described as Bacterial extracellular solute-binding proteins, family 5 (PF00496)","","","","","Hiles,I.D., Gallagher,M.P., Jamieson,D.J. and Higgins,C.F. Molecular characterization of the oligopeptide permease of Salmonella typhimurium. J. Mol. Biol. 195 (1): 125-142 (1987) [PubMed: 2821267].Hiles,I.D. and Higgins,C.F. Peptide uptake by Salmonella typhimurium. The periplasmic oligopeptide-binding protein. Eur. J. Biochem. 158 (3): 561-567 (1986) [PubMed: 3525163].Tame,J.R., Murshudov,G.N., Dodson,E.J., Neil,T.K., Dodson,G.G., Higgins,C.F. and Wilkinson,A.J. The structural basis of sequence-independent peptide binding by OppA protein. Science 264 (5165): 1578-1581 (1994) [PubMed: 8202710].Tame,J.R., Dodson,E.J., Murshudov,G., Higgins,C.F. and Wilkinson,A.J. The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands. Structure 3 (12): 1395-1406 (1995) [PubMed: 8747465].Davies,T.G., Hubbard,R.E. and Tame,J.R. Relating structure to thermodynamics: the crystal structures and binding affinity of eight OppA-peptide complexes. Protein Sci. 8 (7): 1432-1444 (1999) [PubMed: 10422831].","","Fri Jan 3 12:06:10 2003","1","","","" "AA01608","1088037","1087453","585","ATGGAATTTCCCCTATTTGAAACCCTTGCCATAGCACAAGGCAAAGTACGCAACATTAAACTTCATCAACAACGCTACGAACGCAGTTTACAGACGTTTTACGGCAAAAGTGCGGTCATTTTTCCAAACGTTTTTCAGCTTGCCAAACAGATCCATGTACCGGCGGAATTGCGAGCCGAACCGCTGATTCGCTGCCGAATTAATTACAACGCTGAACAAATCCTTTGTCGCTATTTTCCCTACACGCGCAAAACCTACCGCACTTTTAAGCCTATCGTCTGCGACCACATTGACTACGGATTAAAATACGCCGACCGCACCTTGTTAAATGCACTGTTCGCACAAAAAGGCGATTGTGACGAAATCATGATCATCAAAAACGGCTATGTCACCGATTGTTCCATCGGCAACCTCATCTTCCGCCAAAACACCCAATGGTTCACCCCCGACACGCCCCTGCTCGAAGGCACCCAACGGGCAACATTACTTACCCAAGGACGCATAAAAGTGCGGTCGATTTTAGCCACGGATTTGCACTTATTTGAGGAAGTGAGATTGATTAATGCGTTGAATGGATTGGATGAT","","","22646","MEFPLFETLAIAQGKVRNIKLHQQRYERSLQTFYGKSAVIFPNVFQLAKQIHVPAELRAEPLIRCRINYNAEQILCRYFPYTRKTYRTFKPIVCDHIDYGLKYADRTLLNALFAQKGDCDEIMIIKNGYVTDCSIGNLIFRQNTQWFTPDTPLLEGTQRATLLTQGRIKVRSILATDLHLFEEVRLINALNGLDD","1087451","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR001544
Family
Aminotransferase, class IV
PD001961\"[119-190]TQ9CKY5_PASMU_Q9CKY5;
PTHR11825\"[120-168]TSUBGROUP IIII AMINOTRANSFERASE
noIPR
unintegrated
unintegrated
G3DSA:3.20.10.10\"[102-193]Tno description
PTHR11825:SF3\"[120-168]T4-AMINO-4-DEOXYCHORISMATE LYASE RELATED


","BeTs to 6 clades of COG0115COG name: Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyaseFunctional Class: E,HThe phylogenetic pattern of COG0115 is aom---yqvdrlbcefghsnujx---Number of proteins in this genome belonging to this COG is","","Residues 3 to 193 match (1e-61) PD:PD104370 which is described as PROTEOME COMPLETE HI1169 PM1465 ","","","","","","","","","","","","Fri Jan 3 12:10:57 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01608 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01609","1088882","1088043","840","GTGCAATTTCCAGGCTATACCAACGTGAATTGGCAAAAAGAACCACCGGAAGCCTTTTATTTACACAAGAAACCCATGGATTTTATGGCGTATCAACAAGGTTTTGATTTAGTGCAACGGGAATTGCGCTTCGGCAATTCTTATTTGCTGAATCTCACCTATCCAACGCCCATTGAAACCAATTATTCTCTACGACAGCTGTTTTGGCAAAGTCAGGCGAAATATAAATTGTTATTCAAAGATCAGTTCGTTTGCTTCTCGCCCGAATGTTTTGTCAATTTGCGTGACAACCGCATTTTCACTTACCCCATGAAAGGCACTATTGACGCTACCCTGCCCGACGCGCAAGCCCTCTTGCTCAATAATCAAAAGGAACAACGGGAGCATTACACCATCGTGGATTTAATGCGTAATGATTTAGCCACAGTGGCGAAAAATATTCAGGTAACACGTTTTCGTTATGTGGAAAAAATCCAAACGGAACAAGGCGCTATTTTGCAAACCAGCTCGGAAATCTGCGGCGAATTGGCGGAAAACTGGCAGGGACAGATTGGATCTATACTTGCCAACTTATTGCCGGCGGGTTCCATCAGCGGCGCGCCGAAAGAAAAAACCGTGCAAATCATTCAACAGGCAGAACAACAACCACGTGGGTATTACACAGGCATTTTCGGCATTTTTGACGGCGAATCATTGCAAAGCGCGGTGGCAATTCGTTTTATCGAACAGACGGGAAAGGGGTTGTTCTTCCGCAGTGGTGGCGGCATTACTATTCAAAGTGATGCGCAGGAAGAATATCGTGAGCTGATTCAAAAAGTATATGTGCCGTTACAACGAGGT","","","37355","VQFPGYTNVNWQKEPPEAFYLHKKPMDFMAYQQGFDLVQRELRFGNSYLLNLTYPTPIETNYSLRQLFWQSQAKYKLLFKDQFVCFSPECFVNLRDNRIFTYPMKGTIDATLPDAQALLLNNQKEQREHYTIVDLMRNDLATVAKNIQVTRFRYVEKIQTEQGAILQTSSEICGELAENWQGQIGSILANLLPAGSISGAPKEKTVQIIQQAEQQPRGYYTGIFGIFDGESLQSAVAIRFIEQTGKGLFFRSGGGITIQSDAQEEYRELIQKVYVPLQRG","1088041","[FUNCTION] Catalyzes the biosynthesis of 4-amino-4-deoxychorismate (adc) from chorismate and glutamine.[PATHWAY] Folate biosynthesis pathway. first step in the biosynthesis of p-aminobenzoate (pabA). [SUBUNIT] Consists of two nonidentical chains: component i catalyzes the formation of adc by binding chorismate and ammonia; component II provides the glutamine amidotransferase activity. [SIMILARITY] Belongs to the anthranilate synthase component i family. ","p-aminobenzoate synthase component I homolog","Cytoplasm","","
InterPro
IPR005801
Domain
Anthranilate synthase component I and chorismate binding protein
PD000779\"[50-272]TYE64_PASMU_Q9CKY6;
PR00095\"[117-130]T\"[131-144]T\"[215-229]TANTSNTHASEI
PF00425\"[27-280]TChorismate_bind
noIPR
unintegrated
unintegrated
G3DSA:3.60.120.10\"[26-278]Tno description
PTHR11236\"[28-273]TAMINOBENZOATE/ANTHRANILATE SYNTHASE
PTHR11236:SF4\"[28-273]Tgb def: Putative para-aminobenzoate synthase component I


","No hits to the COGs database.","Significant hit ( 7.4e-10) to 3/4 blocks of the PR00095 family, which is described as \"Anthranilate synthase component I signature\". Prints database entry for PR:PR00095. PR00095A 117-130 2.1 PR00095B 131-144 0.0011 PR00095C 215-229 0.071","Residues 5 to 77 match (3e-16) PD:PD127102 which is described as PROTEOME PABA-LIKE COMPLETE HI1170 PM1464 ","","","","","","","","","","","Fri Jan 3 12:15:50 2003","Fri Jan 3 12:15:50 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01609 is paralogously related to AA02173 (4e-10) and AA00085 (1e-06).","","","","","","Residues 27 to 280 (E-value = 2.1e-18) place AA01609 in the Chorismate_bind family which is described as chorismate binding enzyme (PF00425)","","","","","Rayl EA, Green JM, Nichols BP. Escherichia coli aminodeoxychorismate synthase: analysis of pabB mutations affecting catalysis and subunit association. Biochim Biophys Acta. 1996 Jun 7;1295(1):81-8. PMID: 8679677Slock,J., Stahly,D.P., Han,C.Y., Six,E.W. and Crawford,I.P. An apparent Bacillus subtilis folic acid biosynthetic operon containing pab, an amphibolic trpG gene, a third gene required forsynthesis of para-aminobenzoic acid, and the dihydropteroatesynthase gene. J. Bacteriol. 172 (12): 7211-7226 (1990) [PubMed: 2123867].","","Fri Jan 3 12:15:50 2003","1","","","" "AA01610","1089040","1088951","90","TTGTCGTTTTTTCACGAGATAACGTTATGTGGCAAAATTTTATTCAACACGCAAACCGATTTGGCAAAACAAAAACGCCCTTCTTCTTTT","","","3453","LSFFHEITLCGKILFNTQTDLAKQKRPSSF","1088951","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 15:37:02 2004","Thu Feb 26 15:37:02 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01610 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 15:37:02 2004","","","","","","","","","","","","","1","","","" "AA01611","1089116","1089679","564","ATGTCCTTACTGATTATCAACAACCACGATTCCTTTACTTTCAATTTAGTGGATTTAATCCGCCGTTTGGCAGTGCCGTTTCAGGTGGTGAATGTGGAAGACCTGGATTTGGACGCGGTGGAAAATTTCTCCCATTTGCTTATTTCTCCCGGCCCCGATGTGCCGCGTGCGTATCCGCAATTATTTGCCTTGTTGGAACGTTATCACCGGTGCAAATCCATTTTCGGCGTGTGTTTAGGACATCAAATATTGTGCGAATTTTTCGGTGCGGCATTATATAACCTGCCGTCGCCCCGCCACGGGCAGGCAAAGCTGTTGTATCTTGTGTCGGATTCGCCGTTATTCAAAAACTTGCCGCCAAGCTTTCAAATCGGTTTATACCATTCCTGGGCGGTGGGCGAACCGCATTGCCCCACGCAACTACAGATTACTGCCCGTTGTAGCGATAACATCATCATGGCAATGCAGCACAAAACTTTGCCCATTTACGGCGTACAGTTTCATCCCGAATCCTACATTTCCGAATACGGCGAGCAGATTTTACGAAACTGGTTGCAGGCGTCA","","","22898","MSLLIINNHDSFTFNLVDLIRRLAVPFQVVNVEDLDLDAVENFSHLLISPGPDVPRAYPQLFALLERYHRCKSIFGVCLGHQILCEFFGAALYNLPSPRHGQAKLLYLVSDSPLFKNLPPSFQIGLYHSWAVGEPHCPTQLQITARCSDNIIMAMQHKTLPIYGVQFHPESYISEYGEQILRNWLQAS","1089677","[CATALYTIC ACTIVITY] Chorismate + L-glutamine = anthranilate +pyruvate + L-glutamate.[PATHWAY] Tryptophan biosynthesis; first step.[SUBUNIT] Tetramer of two components i and two components II. [SIMILARITY] Contains 1 type-1 glutamine amidotransferase domain. ","anthranilate synthase component II","Cytoplasm","","
InterPro
IPR000991
Domain
Glutamine amidotransferase class-I
PF00117\"[4-187]TGATase
InterPro
IPR006220
Domain
Anthranilate synthase component II/delta crystallin
PR00097\"[3-17]T\"[46-55]T\"[73-84]T\"[98-106]T\"[119-131]T\"[164-177]TANTSNTHASEII
InterPro
IPR006221
Domain
Glutamine amidotransferase of anthranilate synthase
TIGR00566\"[2-187]TtrpG_papA: glutamine amidotransferase of an
InterPro
IPR011702
Domain
Glutamine amidotransferase superfamily
PR00096\"[46-55]T\"[73-84]T\"[164-177]TGATASE
InterPro
IPR012998
Active_site
Glutamine amidotransferase, class I, active site
PS00442\"[73-84]?GATASE_TYPE_I
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.880\"[2-185]Tno description
PIRSF001375\"[2-187]TGMP synthase/anthranilate synthase component II
PTHR11922\"[2-185]TGMP SYNTHASE-RELATED


","BeTs to 22 clades of COG0512COG name: Anthranilate/para-aminobenzoate synthases component IIFunctional Class: E,HThe phylogenetic pattern of COG0512 is aompkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.6e-13) to 2/10 blocks of the IPB001674 family, which is described as \"GMP synthase C terminal domain\". Interpro entry for IP:IPR001674. IPB001674B 73-82 0.04 IPB001674D 163-184 1.2e-09Significant hit ( 2.8e-10) to 2/2 blocks of the IPB000991 family, which is described as \"Glutamine amidotransferase class-I\". Interpro entry for IP:IPR000991. IPB000991A 73-82 0.0012 IPB000991B 162-172 9.2e-05","Residues 4 to 55 match (8e-15) PD:PD002064 which is described as SYNTHASE ANTHRANILATE GLUTAMINE PROTEOME COMPLETE AMIDOTRANSFERASE COMPONENT II LYASE BIOSYNTHESIS ","","","","","","","","","","","Fri Jan 3 12:20:23 2003","Fri Jan 3 12:20:23 2003","","Fri May 20 08:17:34 2005","Fri May 20 08:17:34 2005","Fri May 20 08:17:34 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA01611 is paralogously related to AA02175 (7e-22) and AA01913 (7e-06).","Fri May 20 08:17:34 2005","","","","","Residues 4 to 187 (E-value = 1.3e-50) place AA01611 in the GATase family which is described as Glutamine amidotransferase class-I (PF00117)","Fri May 20 08:17:34 2005","","","","","","","1","","","" "AA01614","1089838","1090779","942","ATGAATATTGTTTTTTTAGACCGCACCGGCATTCCCGCCGGCCATGACATTCCACGCCCGAGTTTTCCACACACCTGGACTGAATATGACCGCACTTTGCCGCAAGAAACCTTTGAACGCACCAAAGATGCCGACATTGTGGTGACCAGCAAAGTGGTGTTCGACCGTGACTTATTAAGCCGCTTACCGAAATTAAAACTCATCGCCATCACCGCCACCGGCACCAATAACATTGATTTAGAGGCGGCGAAAGCGCTGGGTATCGCCGTGAAGAACGTTACGGGTTATTCCAGCGTCACCGTGCCGGAGCACGTTTTAGGTATGATTTTTGCGCTGAAACATAGCCTCATGAGCTATCACCGCGATCAAGTCACTTCTGATCGTTGGGCGACCTGCGGGCAATTTTGTTATACCGATTACCCGATTACCGATGTGCGTGGCGCGACTCTCGGCGTATTCGGCAAAGGCAACATCGGCACGGAAATCGGGCGCTTGGCGCAGTTGTTGGGCATGAAAATATTGTATGCGGAACACAAAGGCGCAAGCCAAATTCGGGACGGCTATACCGATTTTGAAACCGTGCTGAAACAAGCGGACATCGTCACGCTGCATTGCCCGCTCACCGACACCACCAAAAATCTTATTAACTCCGATACCTTGGCATTAATGAAACCGACGGCTTATTTAATTAACACAGGTCGCGGTCCGTTGGTGGACGAAACCGCATTATTGGCGGCCTTAGAAAGCGGTAAAATTGCCGGGGCGGCGTTGGACGTGTTGGTGAAAGAACCGCCGGAAAAAGAAAATCCGCTCATTCAAGCGGCAAAACGCTTACCGAATCTTTTGCTTACCCCGCACGTTGCCTGGGCGAGCGATTCTGCTGTCACCACGCTGGTGAATAAAGTAGCGCAAAATATCGAAGATTTTGTGGCGAACGGTAAG","","","34335","MNIVFLDRTGIPAGHDIPRPSFPHTWTEYDRTLPQETFERTKDADIVVTSKVVFDRDLLSRLPKLKLIAITATGTNNIDLEAAKALGIAVKNVTGYSSVTVPEHVLGMIFALKHSLMSYHRDQVTSDRWATCGQFCYTDYPITDVRGATLGVFGKGNIGTEIGRLAQLLGMKILYAEHKGASQIRDGYTDFETVLKQADIVTLHCPLTDTTKNLINSDTLALMKPTAYLINTGRGPLVDETALLAALESGKIAGAALDVLVKEPPEKENPLIQAAKRLPNLLLTPHVAWASDSAVTTLVNKVAQNIEDFVANGK","1090777","[CATALYTIC ACTIVITY] 3-phosphoglycerate + NAD(+) = 3-phosphohydroxypyruvate + NADH.[PATHWAY] Serine biosynthesis; first step.[SIMILARITY] Belongs to the D-isomer specific 2-hydroxyacid dehydrogenases family. ","D-isomer specific 2-hydroxyacid dehydrogenase family protein","Cytoplasm","","
InterPro
IPR006139
Domain
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic region
PF00389\"[29-314]T2-Hacid_dh
InterPro
IPR006140
Domain
D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding
PF02826\"[106-288]T2-Hacid_dh_C
PS00670\"[194-216]TD_2_HYDROXYACID_DH_2
PS00671\"[223-239]TD_2_HYDROXYACID_DH_3
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[100-289]Tno description
PTHR10996\"[36-313]T2-HYDROXYACID DEHYDROGENASE


","BeTs to 8 clades of COG1052COG name: Lactate dehydrogenase and related dehydrogenasesFunctional Class: C,H,RThe phylogenetic pattern of COG1052 is ---pkzyq---lbcefgh-nuj--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 4.3e-63) to 5/5 blocks of the IPB002162 family, which is described as \"D-isomer specific 2-hydroxyacid dehydrogenase\". Interpro entry for IP:IPR002162. IPB002162A 77-114 3.8e-15 IPB002162B 147-159 0.0063 IPB002162C 191-204 0.0012 IPB002162D 211-260 2.4e-30 IPB002162E 275-294 3.4e-05","Residues 100 to 216 match (1e-10) PD:PD349508 which is described as PROTEOME COMPLETE DEHYDROGENASE OXIDOREDUCTASE REDUCTASE 2-HYDROXYACID HYDROXYPYRUVATE PYRUVATE D-ISOMER SPECIFIC ","","","","","","","","","","","Mon Jan 6 07:37:51 2003","Wed Jan 22 16:18:22 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01614 is paralogously related to AA02375 (2e-35) and AA02916 (5e-30).","","","","","","Residues 101 to 286 (E-value = 1.9e-75) place AA01614 in the 2-Hacid_dh_C family which is described as D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain (PF02826)","","","","","Chistoserdova,L.V. and Lidstrom,M.E. Genetics of the serine cycle in Methylobacterium extorquens AM1: identification of sgaA and mtdA and sequences of sgaA, hprA, and mtdA. J. Bacteriol. 176 (7): 1957-1968 (1994) [PubMed: 8144463].Chistoserdova,L.V. and Lidstrom,M.E. Cloning, mutagenesis, and physiological effect of a hydroxypyruvate reductase gene from Methylobacterium extorquens AM1.J. Bacteriol. 174 (1): 71-77 (1992) [PubMed: 1729225].Chistoserdova,L.V. and Lidstrom,M.E. Purification and characterization of hydroxypyruvate reductase from the facultative methylotroph Methylobacterium extorquens AM1. J. Bacteriol. 173 (22): 7228-7232 (1991) [PubMed: 1657886].","","Mon Jan 6 07:37:51 2003","1","","","" "AA01615","1091326","1092507","1182","ATGACTTTATCTACACCTCTTTTTATCGCGTTACGCTATTGGCGGGCGAAAAGTGCCGATCGTTTCGGGCGTTTGGTGACGAATTTGGCCGGCTTCGGGATCTTTCTCGGCGTGATGGCACTAATCATTGTGCTGTCCGTGATGAACGGATTGGAGGGCTACCAGAAGCAACAAGTGCTATCCACCATTCCGCACGCCATTGTCAGCCCGAACGGTAACGCCAAAATTGACGACGCACCGCCGACAATGCCGGATTTCGTGCAAAAAGCCGTGCCAATTAACATGACCAATGTGATTTTCCAGACAGCAGGCGGTGTCAGTGCGGGACAGGTGATTGGTATTCGGCAGTTTTCCGATGATCCGCTTTTGTTTGATTTTCCCGAGCAGGAATTCGACAAAATGCTGCCGACAGGCGGGTTTAGAATCATTATCGGTGATCAGCTGGCGCAGAAATTAAATCTGCATGTGGGCGATAAAGTGCGGTTGATGATCACCGAGAATAGCCAATATACGCCTTTCGGACGAGTACCTTTACAGCGCTTATTTACCGTGAGCGAAATCTATTTTGACAACAGCGAAGTGTCTGGCTATGAAGCCTTTACCAATCTAACGGACATCGGGCGTTTAATGCGTATTCAACCGGGCGAGGTGCAGGGCTTTCGCTTATTCTTAGCGGATCCTTTCCAGATTACAGCCTTGCCGACTGCGTTTCCGGCGGACTATCAAATCAGCGATTGGCGCACTCAAAAAGGCGAGTTTTTCCAAGCGGTGCGTATGGAAAAAAACATGATGGGCTTGTTGGTGAGCCTGATTATCGTGGTGGCGATTTCCAATATTATTACGTCTTTAAGCCTGATGGTGGTGGACAAACAGGGTGAAATCGCCATTTTGCAAACCCAAGGGCTGACCAAAGGGCAGGTACGTTCCATCTTTATTTATCAAGGTTTGTTGGTGGGCTTGATGGGAACGCTGCTAGGCTCGATTTTAGGTGTGCTGGTGACGTTAAATTTAGACGGCATTGTGAATTTATTCGGCGCACAAACGATGTATTTACCGACCGCACTTGAGCCTTGGCAAATTCTGACGATTATCGCCTTTTCTTTATTATTGTCTTTCTTATCCACCATTTATCCGGCATATCGGGCGGCAAAAGTTGAACCGGCGGAAGCCTTGCGTTACGAA","","","43532","MTLSTPLFIALRYWRAKSADRFGRLVTNLAGFGIFLGVMALIIVLSVMNGLEGYQKQQVLSTIPHAIVSPNGNAKIDDAPPTMPDFVQKAVPINMTNVIFQTAGGVSAGQVIGIRQFSDDPLLFDFPEQEFDKMLPTGGFRIIIGDQLAQKLNLHVGDKVRLMITENSQYTPFGRVPLQRLFTVSEIYFDNSEVSGYEAFTNLTDIGRLMRIQPGEVQGFRLFLADPFQITALPTAFPADYQISDWRTQKGEFFQAVRMEKNMMGLLVSLIIVVAISNIITSLSLMVVDKQGEIAILQTQGLTKGQVRSIFIYQGLLVGLMGTLLGSILGVLVTLNLDGIVNLFGAQTMYLPTALEPWQILTIIAFSLLLSFLSTIYPAYRAAKVEPAEALRYE","1092505","[FUNCTION] Part of an ATP-dependent transport system lolCDE responsible for the release of lipoproteins targeted to theouter membrane from the inner membrane. Such a release is dependent of the sorting-signal (absence of an asp atposition 2 of the mature lipoprotein) and of lolA (by similarity).[SUBCELLULAR LOCATION] Integral membrane protein. inner membrane (by similarity). [SIMILARITY] Belongs to the lolC/E family. ","lipoprotein releasing system transmembrane","Inner membrane, Cytoplasm","","
InterPro
IPR003838
Domain
Protein of unknown function DUF214, permase predicted
PF02687\"[217-387]TFtsX
InterPro
IPR011925
Family
Lipoprotein releasing system, transmembrane protein, LolC/E family
TIGR02212\"[4-394]TlolCE: lipoprotein releasing system, transm
noIPR
unintegrated
unintegrated
signalp\"[1-40]?signal-peptide
tmhmm\"[25-45]?\"[268-288]?\"[309-329]?\"[360-380]?transmembrane_regions


","BeTs to 20 clades of COG0577COG name: ABC-type transport systems, involved in lipoprotein release, permease componentsFunctional Class: RThe phylogenetic pattern of COG0577 is aom----qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 7.2e-26) to 2/2 blocks of the IPB003838 family, which is described as \"DUF214\". Interpro entry for IP:IPR003838. IPB003838A 279-326 1.2e-18 IPB003838B 378-391 9.8e-06","Residues 7 to 266 match (6e-22) PD:PD314920 which is described as TRANSMEMBRANE INNER LIPOPROTEIN PROTEOME RELEASING COMPLETE MEMBRANE SYSTEM LOLC ","","","","","","","","","","","Mon Jan 6 07:46:26 2003","Mon Jan 6 07:46:26 2003","","","Tue Mar 16 09:34:40 2004","Tue Mar 16 09:34:40 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01615 is paralogously related to AA01618 (3e-43), AA02080 (5e-08), AA02438 (1e-07) and AA02439 (3e-07).","Tue Mar 16 09:34:40 2004","","","","","Residues 217 to 387 (E-value = 1.9e-45) place AA01615 in the FtsX family which is described as Predicted permease (PF02687)","Tue Mar 16 09:34:40 2004","","","","Yakushi T, Masuda K, Narita S, Matsuyama S, Tokuda H.A new ABC transporter mediating the detachment of lipid-modified proteins from membranes.Nat Cell Biol. 2000 Apr;2(4):212-8.PMID: 10783239","","Tue Mar 16 09:34:40 2004","1","","","" "AA01616","1092525","1093208","684","ATGACTACAGCATTATTATCCTGCCAAAATATCAGTAAATTTTATCAAGAAGGCACGCAACAAACGGAAGTGTTGAAACAGGTTTCTTTCGCGATGCAACAGGGCGAATTGGTTGCTATTGTGGGCAGTTCCGGTTCGGGTAAAAGCACCTTGTTACACACTTTGGGCGGTTTAGATCAACCGAGCGGCGGAGAGGTGTTTATTAAAGGGCAGTCGCTGCAACAGATGACGCCGAATGCCTTGGCGAAATTGCGCAACCAGTATTTAGGCTTTGTTTATCAGTTTCATCATTTGATGGCGGATTTCACCGCACTTGAGAATGTCATGATGCCGATGTTAATCGGGCGACAAAATAAAAGTGAAGCGCAAGCACGCGCCGAGCAGATGTTAAGTGCGGTCGGTTTACAGCACAGAATTTCACATCGCCCATCCGCCTTGTCCGGTGGCGAGCGTCAACGTGTGGCGATTGCCCGTGCGCTGGTGAATAACCCGGCGCTCGTGCTGGCGGATGAACCCACGGGGAATTTGGATCATAAAACCACGGAAAGCATTTTTGAGTTGATTCAACAGTTAAACCAAGAAAAACACATCGCCTTTTTATTGGTAACGCATGATTTGAGTTTGGCGGAAAAACTCAATCGCCGTTTAATTATGCAAGACGGCGTGCTACGCGAGGAACATGCC","","","25157","MTTALLSCQNISKFYQEGTQQTEVLKQVSFAMQQGELVAIVGSSGSGKSTLLHTLGGLDQPSGGEVFIKGQSLQQMTPNALAKLRNQYLGFVYQFHHLMADFTALENVMMPMLIGRQNKSEAQARAEQMLSAVGLQHRISHRPSALSGGERQRVAIARALVNNPALVLADEPTGNLDHKTTESIFELIQQLNQEKHIAFLLVTHDLSLAEKLNRRLIMQDGVLREEHA","1093206","[FUNCTION] Part of an ATP-dependent transport system lolcde responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane. such a release is dependent of the sorting-signal (absence of an asp at position 2 of the mature lipoprotein) and of lola (by similarity). [SUBCELLULAR LOCATION] Inner membrane-associated (by similarity). [SIMILARITY] Belongs to the ABC transporter family. LolD subfamily. ","lipoprotein releasing system ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[146-188]TLOLD_HAEIN_P45247;
PF00005\"[35-221]TABC_tran
PS50893\"[6-228]TABC_TRANSPORTER_2
PS00211\"[146-160]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[34-222]TAAA
InterPro
IPR011924
Family
Lipoprotein releasing system, ATP-binding protein
TIGR02211\"[5-225]TLolD_lipo_ex: lipoprotein releasing system,
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[3-227]Tno description
PTHR19222\"[6-226]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF32\"[6-226]TABC TRANSPORTER


","No hits to the COGs database.","Significant hit ( 6.7e-39) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 24-70 3.8e-18 IPB001140B 143-181 1.7e-16 IPB001140C 198-227 0.22Significant hit ( 3.1e-06) to 1/5 blocks of the IPB001324 family, which is described as \"Phosphoribulokinase family\". Interpro entry for IP:IPR001324. IPB001324A 34-55 3.1e-06","Residues 90 to 143 match (3e-07) PD:PD267517 which is described as ATP-BINDING COMPLETE PROTEOME ABC TRANSPORTER TRANSPORTER COMPONENT ATPASE PROBABLE PLASMID ","","","","","","","","","","","Mon Jan 6 08:00:10 2003","Mon Jan 6 08:00:10 2003","","","Tue Mar 16 09:33:29 2004","Tue Mar 16 09:33:29 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01616 is paralogously related to AA02080 (5e-47), AA02440 (3e-42), AA01422 (5e-39), AA00415 (5e-37), AA01524 (2e-31), AA01645 (9e-30), AA01051 (3e-28), AA01656 (4e-28), AA00858 (7e-28), AA02718 (2e-27), AA01867 (4e-27), AA02353 (8e-26), AA00700 (1e-25), AA01684 (7e-25), AA02805 (1e-23), AA02899 (1e-22), AA01779 (3e-22), AA02324 (7e-22), AA02898 (1e-20), AA02152 (2e-20), AA00933 (2e-20), AA02550 (9e-20), AA01961 (9e-20), AA01820 (1e-19), AA01509 (1e-19), AA02609 (4e-19), AA02320 (9e-19), AA02606 (1e-18), AA02140 (1e-18), AA01568 (1e-17), AA01456 (7e-17), AA01757 (2e-16), AA01510 (3e-16), AA02786 (6e-16), AA02331 (7e-16), AA01393 (2e-15), AA01947 (4e-15), AA00799 (8e-15), AA00207 (8e-15), AA02225 (1e-14), AA01569 (2e-14), AA01824 (1e-13), AA00751 (2e-13), AA02484 (3e-13), AA01555 (4e-12), AA00591 (9e-12), AA02573 (1e-11), A02145 (5e-10), AA00061 (5e-10), AA02642 (7e-09), AA02146 (3e-08), AA02226 (4e-08), AA00934 (4e-06) and AA01291 (1e-04).","Tue Mar 16 09:33:29 2004","","","","","Residues 35 to 221 (E-value = 8.1e-60) place AA01616 in the ABC_tran family which is described as ABC transporter (PF00005)","Tue Mar 16 09:33:29 2004","","","","Yakushi T, Masuda K, Narita S, Matsuyama S, Tokuda H.A new ABC transporter mediating the detachment of lipid-modified proteins from membranes.Nat Cell Biol. 2000 Apr;2(4):212-8.PMID: 10783239","","Tue Mar 16 09:33:29 2004","1","","","" "AA01618","1093211","1094458","1248","ATGAATACGCCATTTTTTATTAGCTGGCGTTATCAGCGCAGTAAACATAGAAATCGCCTGGTATCGCTGATTGCTTTTTTTTCCAGCATGGGCATTGCCTTGGGCGTGGCGGTACTCATTGTCGGCTTAAGTGCCATGAATGGTTTTGAGCGCGAGTTGAATCAACGTATTTTGGCGGTGGTGCCACACGCGGAAATTATTTCCGCCCCGGGGCAAGGGGATGCGCCCATCGATCATTGGCAGAATTTGGCGGCGAAACTTAAACAAAATCCGCAAATTCGCGGTATTTCACCTTTCGTAAGTTTTACCGCGTTGGTGGAAAACGGCGCAAAATTAAAAGTCGTGCAAATTAAAGGGGTGGAAACGGCGTTGCAGGATCAAGTGAGTTCTCTCGGGCGCTTCGTGTTAAATGCCGGTTGGCAGAATTTTGCGCAAAACGGCGGATTGGTCCTCGGTTCCGGTATTGCGCGGGATTTGGACGTGCAGGAAGGGGATTGGGTATCTTTGTTAATTTCCCAGCAAAAAGGTTCGGAAAATCTCACCCAGCCGTTGCGTGAACGTATTCAAGTGACCGGTATTCTACGTTTGGACGGTCAGTTGGATCACAGTTATGCTTTGATGCCGTTGGCACAGGCGCAGCAATTGATGAATTATCAGGCGGATCAGGTCACCGGCGTGGAACTGAAAACCGCAGATCCGTTTAGTGTGCAAAATATGGATTATTCCATGTTGCAGGATTATCCGCAGATGCTGTACCTGCAAAACTGGATCAGCAAATTTGGTTATATGTACCGCGATATTCAGCTGATCCGCACGGTGATGTATATCGCCATGGTGTTGGTTATCGGGGTCGCCTGTTTTAACATTGTTTCCACTTTAATTATGGCGGTAAAAGACAAAGCCGGCGATATTGCCATTATGCGCACCCTCGGCGCCAATAACCGTTTCATTAAACGGATTTTTATTTGGTACGGCTTGCAGGCGGGCATGAAAGGCTGCCTGATTGGCATTGTGTTTGGCATGATTTTAGCCTTGAATCTGACTCAATTAATTCAGTTATTGGAAAACGCCATTGGTAAGAAATTGTTGTCCGACGGTATTTATTTCGTGGATTTTCTGCCGACGGAACTACATTGGCAAGATGTGCTTTTGGTGTTGTTGTCCGCGTTAATTTTAAGTTTATTCGCCAGTCTTTATCCGGCAAACCGCGCGGCGAAATTACAACCGGCACAGGTGTTAAGCGGTCAT","","","46187","MNTPFFISWRYQRSKHRNRLVSLIAFFSSMGIALGVAVLIVGLSAMNGFERELNQRILAVVPHAEIISAPGQGDAPIDHWQNLAAKLKQNPQIRGISPFVSFTALVENGAKLKVVQIKGVETALQDQVSSLGRFVLNAGWQNFAQNGGLVLGSGIARDLDVQEGDWVSLLISQQKGSENLTQPLRERIQVTGILRLDGQLDHSYALMPLAQAQQLMNYQADQVTGVELKTADPFSVQNMDYSMLQDYPQMLYLQNWISKFGYMYRDIQLIRTVMYIAMVLVIGVACFNIVSTLIMAVKDKAGDIAIMRTLGANNRFIKRIFIWYGLQAGMKGCLIGIVFGMILALNLTQLIQLLENAIGKKLLSDGIYFVDFLPTELHWQDVLLVLLSALILSLFASLYPANRAAKLQPAQVLSGH","1094456","[FUNCTION] Part of an ATP-dependent transport system lolCDE responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane. such a release is dependent of the sorting-signal (absence of an asp at position 2 of the mature lipoprotein) and of lola (by similarity). [SUBCELLULAR LOCATION] Inner membrane-associated (by similarity). [SIMILARITY] Belongs to the ABC transporter family. LolD subfamily. ","lipoprotein releasing system transmembrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR003838
Domain
Protein of unknown function DUF214, permase predicted
PF02687\"[223-409]TFtsX
InterPro
IPR011925
Family
Lipoprotein releasing system, transmembrane protein, LolC/E family
TIGR02212\"[2-416]TlolCE: lipoprotein releasing system, transm
InterPro
IPR011926
Family
Lipoprotein releasing system, transmembrane protein LolE
TIGR02213\"[2-416]TlolE_release: lipoprotein releasing system,
noIPR
unintegrated
unintegrated
signalp\"[1-35]?signal-peptide
tmhmm\"[21-43]?\"[275-297]?\"[320-340]?\"[379-399]?transmembrane_regions


","BeTs to 19 clades of COG0577COG name: ABC-type transport systems, involved in lipoprotein release, permease componentsFunctional Class: RThe phylogenetic pattern of COG0577 is aom----qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 3.7e-24) to 2/2 blocks of the IPB003838 family, which is described as \"DUF214\". Interpro entry for IP:IPR003838. IPB003838A 289-336 4.5e-18 IPB003838B 400-413 0.00014","Residues 6 to 276 match (7e-08) PD:PD314920 which is described as TRANSMEMBRANE INNER LIPOPROTEIN PROTEOME RELEASING COMPLETE MEMBRANE SYSTEM LOLC ","","","","","","","","","","","Mon Jan 6 08:15:38 2003","Mon Jan 6 08:20:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01618 is paralogously related to AA01615 (3e-43), AA02439 (2e-04), AA02080 (2e-04) and AA01423 (5e-04).","","","","","","Residues 223 to 409 (E-value = 2e-48) place AA01618 in the FtsX family which is described as Predicted permease (PF02687)","","","","","Yakushi,T., Masuda,K., Narita,S., Matsuyama,S. andTokuda,H. A new ABC transporter mediating the detachment of lipid-modified proteins from membranes. Nat. Cell Biol. 2 (4): 212-218 (2000) [PubMed: 10783239].","","Mon Jan 6 08:15:38 2003","1","","","" "AA01619","1094562","1095638","1077","ATGAAAAAAAAAGATATTAATATTAAAAACGATGATACTCGAATCGGTAAGATTGAACAGGTATTGCCGCCCATCGCGTTATTAGAAAAATTTCCTGCCAGCGAGGTTGCGGTAAAAACCGTAGAACAAGCCCGCGAAGAAGCACACGACATTATTCATGGCAAAGATGATCGCCTGTTGGTGGTGATCGGGCCTTGCTCCATTCACGATCCGAAAGCGGCATTGGAATATGCGCAACGCATTAAATTAATGCGTGAAAAATTCAAAGATACCTTACAAATCATCATGCGCGTGTATTTTGAAAAGCCGCGTACCACCGTGGGTTGGAAAGGCTTAATTAATGACCCGCACTTAAATAATACTTATGCCTTGAACGACGGTTTGCGTATGGCGCGTAAATTATTATCCGACATTAACGATTTAACCGTGCCTTCCGCCGGTGAGTTTTTGGATATGATCACACCGCAGTATTTAGCGGATTTCATGAGCTGGGGTGCCATCGGTGCAAGAACCACCGAATCCCAAGTACACCGTGAACTGGCTTCCGGTTTATCCTGCGCGGTGGGCTTTAAAAATGCCACTAACGGTTGCGTGAAAATTGCTTTAGATGCTATCGGCGCTGCAGAAGCACCGCACCATTTTTTATCCGTAACCAAATTCGGTCATTCCGCCATTGTTTCTACCAAAGGCAACGAAGACTGCCACATTATTTTACGTGGTGGCGACAACGGTCCTAATTACAGTGAAGAAGATGTTTCCGACGTGTGTGCAAAACTTGCCAAAGCCGGTTACACACCGCATGTTATGGTGGATTTCAGCCATGCCAACAGCAGCAAACAATTCAAAAGACAATTAGACGTTAGCCATGAAGTGGCGCGCCAAATTGCCGGCGGCTCAAAACAAATCTTCGGCGTTATGATTGAAAGCCATTTGGTGGAAGGTCGTCAGGATTTGGTAGAAGGCAAAGAATTGACATACGGGCAAAGTATCACCGACAGTTGTATTGGCTGGGACGACAGTGAAAAAGTCTTGCAGGAATTATCTGACGCGGTAGCGGCAAGACGTAAATTAAACGGC","","","39533","MKKKDINIKNDDTRIGKIEQVLPPIALLEKFPASEVAVKTVEQAREEAHDIIHGKDDRLLVVIGPCSIHDPKAALEYAQRIKLMREKFKDTLQIIMRVYFEKPRTTVGWKGLINDPHLNNTYALNDGLRMARKLLSDINDLTVPSAGEFLDMITPQYLADFMSWGAIGARTTESQVHRELASGLSCAVGFKNATNGCVKIALDAIGAAEAPHHFLSVTKFGHSAIVSTKGNEDCHIILRGGDNGPNYSEEDVSDVCAKLAKAGYTPHVMVDFSHANSSKQFKRQLDVSHEVARQIAGGSKQIFGVMIESHLVEGRQDLVEGKELTYGQSITDSCIGWDDSEKVLQELSDAVAARRKLNG","1095636","","phospho-2-dehydro-3-deoxyheptonate aldolase (DAHP synthase)","Cytoplasm","","
InterPro
IPR001531
Family
Phospholipase C zinc-binding, prokaryotic
SM00770\"[84-319]Tno description
InterPro
IPR006218
Domain
DAHP synthetase I/KDSA
PF00793\"[30-345]TDAHP_synth_1
InterPro
IPR006219
Family
Phospho-2-dehydro-3-deoxyheptonate aldolase, subtype 1
PIRSF001361\"[7-359]T3-deoxy-7-phosphoheptulonate synthase
PTHR21225\"[1-354]TPHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE (DAHP SYNTHETASE)
TIGR00034\"[11-355]TaroFGH: phospho-2-dehydro-3-deoxyheptonate
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[13-355]Tno description


","BeTs to 8 clades of COG0722COG name: 3-Deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthaseFunctional Class: EThe phylogenetic pattern of COG0722 is ------y--d-l--efghsn-j----Number of proteins in this genome belonging to this COG is","Significant hit (3.6e-189) to 7/7 blocks of the IPB001785 family, which is described as \"DAHP synthetase class I\". Interpro entry for IP:IPR001785. IPB001785A 11-34 9.7e-08 IPB001785B 45-78 1.1e-29 IPB001785C 94-134 1.5e-36 IPB001785D 142-193 4.4e-43 IPB001785E 212-240 4.6e-22 IPB001785F 268-311 2.4e-29 IPB001785G 326-347 6.9e-14 IPB001785B 48-81 0.45","","","","","","Tue Feb 18 14:49:48 2003","","","","","","Tue Feb 18 14:49:48 2003","Mon Jan 6 08:22:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01619 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 30 to 345 (E-value = 5.7e-164) place AA01619 in the DAHP_synth_1 family which is described as DAHP synthetase I family (PF00793)","","","","","Davies,W.D. and Davidson,B.E. The nucleotide sequence of aroG, the gene for 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase (phe) in Escherichia coli K12. Nucleic Acids Res. 10 (13): 4045-4048 (1982) [PubMed: 6125934].Parish T, Stoker NG. The common aromatic amino acid biosynthesis pathway is essential in Mycobacterium tuberculosis. Microbiology. 2002 Oct;148(Pt 10):3069-77. PMID: 12368440 Jiang PH, Liu AM, Ge HP, Zhang YY, Fan CS, Huang WD. Cloning and Expression of aroG Gene of E. coli and Its Co-expression with pheA and tyrB Genes. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 1998;30(6):593-596. PMID: 12167994 Jiang PH, Shi M, Qian ZK, Li NJ, Huang WD. Effect of F209S Mutation of Escherichia coli AroG on Resistance to Phenylalanine Feedback Inhibition. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2000;32(5):441-444. PMID: 12058188 Kikuchi Y, Tsujimoto K, Kurahashi O. Mutational analysis of the feedback sites of phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase of Escherichia coli. Appl Environ Microbiol. 1997 Feb;63(2):761-2. PMID: 9023954","","Tue Feb 18 14:49:48 2003","1","","","" "AA01620","1095772","1095653","120","GTGGAAAAAAGTCGCTATATGATATACCAAATCCGGGGGCGGTTTAACTTAAAAATACAAAAAAGTGCGGTGGAAATTCTCCGTAAAAATCCACCGCACTTTTCTTTAGAAAGGCACAAT","","","4880","VEKSRYMIYQIRGRFNLKIQKSAVEILRKNPPHFSLERHN","1095653","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 15:34:53 2004","Thu Feb 26 15:34:53 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01620 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 15:34:53 2004","","","","","","","","","","","","","1","","","" "AA01621","1095787","1097190","1404","ATGGCGTCTAAGAATTCACCTCCTGCAAAAGAAAAAAATACCACCAATTTAAATATTCCCCCTCATTCCATTGAAGCCGAACAAGCGGTGTTAGGCAGTATTTTATTGAACAATTTTTATTGGGATGATGTAGCGGAAAATGTGGTGAAAGAGGATTTTTACCGCTTTGAGCATCGCCTGATTTTTGAGGAAATGGAAAAGCTCATTGCGCAACAGGCGCCGGTGGATTTAATCACTTTGGAACAAGCCCTCAAAAGCCGTGAAGTGATTGAACAGGTAGGCGGCTTCGCTTATTTGGCGGAACTTTCCAATAACACGCCAAGTGCCGCCAACGTGGTGGCGTATGCGAATGTGGTGCGGGAAAAAGCCATTATGCGCGAATTGATTTCCGTGGGGAATAAAATCGCGCAGAACAGTTATTCACCGAAAGGGCAGGATGTGAAACATTTGCTGGACGAAGCGGAACGGGAAGTGTTTGCCATCGCGGAAAAACGTACCTCGGGCAATGAAGGTCCGCAAAATATTATCGCCATTCTGGAAAATACTATCAGTAAAATCGAACAACTCAGTCAAGCCAAAGATCATTCCGGCGTCACCGGCGTTTCTACCGGCTTTAAAGATTTGGATAAAAAAACCGCCGGCTTGCAAAAATCCGATTTGATTATTGTGGCGGCGCGTCCTTCCATGGGGAAAACCACGTTTGCTATGAATCTGTGTGAAAATGCGGCGTTAGGCAGTGAAAAACCGGTGTTGGTATTCAGTTTGGAGATGCCGGCGGAACAAATTATGATGCGTAGCCTTGCGTCACTTTCCCGCGTGGACCAAACTAAAATTCGTACCGGTCAGGGGTTGGACGATAACGACTGGGCGAAAATTTCCAGTACCATGGGCGTACTTGCTAAAAAGCCGAATTTATTTATTGATGACTCCTCAGGGTTAACGCCAACAGAGCTACGTTCCCGTGCCAGACGGGTGTATCGGGAAAACGGCGGATTAAGTTTAATCATGGTGGACTATCTTCAATTAATGCGCGCACCGGCATTTTCTGATAATCGAACGTTGGAAATTGCGGAAATTTCGCGTTCTTTAAAAGCCTTGGCAAAAGAATTGGAAGTGCCGGTGATCGCCCTGTCACAATTAAACCGTACGTTGGAAAACCGTCAGGATAAACGCCCCGTGAACTCGGATTTACGGGAATCTGGCTCCATTGAGCAGGATGCGGATTTGATCATGTTTATTTATCGTGATGAAGTGTATAACCGCGAGTCGGAAGAAAAAGGCATTGCGGAAATTATTATCGGTAAACAGCGTAACGGCCCTATCGGGCGCGTAAAACTGGCGTTCCAAGGACAATTTTCCCGGTTTGATAATTTGGCGGAACATCATTATTACGATGATGAATAT","","","52257","MASKNSPPAKEKNTTNLNIPPHSIEAEQAVLGSILLNNFYWDDVAENVVKEDFYRFEHRLIFEEMEKLIAQQAPVDLITLEQALKSREVIEQVGGFAYLAELSNNTPSAANVVAYANVVREKAIMRELISVGNKIAQNSYSPKGQDVKHLLDEAEREVFAIAEKRTSGNEGPQNIIAILENTISKIEQLSQAKDHSGVTGVSTGFKDLDKKTAGLQKSDLIIVAARPSMGKTTFAMNLCENAALGSEKPVLVFSLEMPAEQIMMRSLASLSRVDQTKIRTGQGLDDNDWAKISSTMGVLAKKPNLFIDDSSGLTPTELRSRARRVYRENGGLSLIMVDYLQLMRAPAFSDNRTLEIAEISRSLKALAKELEVPVIALSQLNRTLENRQDKRPVNSDLRESGSIEQDADLIMFIYRDEVYNRESEEKGIAEIIIGKQRNGPIGRVKLAFQGQFSRFDNLAEHHYYDDEY","1097188","[FUNCTION] Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with dnaC protein, primase, and other prepriming proteins (by similarity). [SUBUNIT] Homohexamer (by similarity). [SIMILARITY] Belongs to the helicase family. DnaB subfamily.","replicative DNA helicase","Cytoplasm","","
InterPro
IPR001114
Family
Adenylosuccinate synthetase
SM00788\"[43-385]Tno description
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[217-424]TAAA
InterPro
IPR007692
Family
DnaB helicase
TIGR00665\"[15-455]TDnaB: replicative DNA helicase
InterPro
IPR007693
Domain
DnaB-like helicase, N-terminal
G3DSA:1.10.860.10\"[20-122]Tno description
PF00772\"[19-121]TDnaB
InterPro
IPR007694
Domain
DnaB-like helicase, C-terminal
PD332834\"[304-414]TDNAB_PASMU_Q9CNL6;
PF03796\"[197-397]TDnaB_C
PS51199\"[194-462]TSF4_HELICASE
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[193-446]Tno description


","BeTs to 18 clades of COG0305COG name: Replicative DNA helicaseFunctional Class: LThe phylogenetic pattern of COG0305 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit (2.5e-143) to 7/7 blocks of the IPB001198 family, which is described as \"DnaB helicase\". Interpro entry for IP:IPR001198. IPB001198A 21-31 3.9e-06 IPB001198B 107-123 5.6e-06 IPB001198C 203-241 2.4e-32 IPB001198D 249-288 2.2e-23 IPB001198E 331-344 5e-08 IPB001198F 350-398 5e-41 IPB001198G 430-455 6.9e-19","Residues 403 to 459 match (5e-15) PD:PD003017 which is described as HELICASE DNA REPLICATIVE PROTEOME COMPLETE ATP-BINDING HYDROLASE REPLICATION DNA-BINDING PRIMOSOME ","","","","","","","","","","","Mon Jan 6 09:45:20 2003","Mon Jan 6 09:45:20 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01621 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 197 to 397 (E-value = 5.8e-138) place AA01621 in the DnaB_C family which is described as DnaB-like helicase C terminal domain (PF03796)","","","","","ong,A., Kean,L. and Maurer,R. Sequence of the dnaB gene of Salmonella typhimurium J. Bacteriol. 170 (6), 2668-2675 (1988) PubMed: 2836367 Nakayama,N., Arai,N., Bond,M.W., Kaziro,Y. and Arai,K. Nucleotide sequence of dnaB and the primary structure of the dnaB protein from Escherichia coli J. Biol. Chem. 259 (1), 97-101 (1984) PubMed: 6323420 ","","Mon Jan 6 09:45:20 2003","1","","","" "AA01623","1097217","1098296","1080","ATGCACATGAAGCCCGCGACAGCCAAAATCAGTTCTGTTGCTTTGAAGCACAATATTCAAACTATCAAACAAAAAGCTCCGGAAAGCAAAATTATTGCGGTAGTCAAAGCCAACGCCTACGGCCATGGCGTCGTGTTCGTGTCTTCTGCCGTAGAAAATCTGGTGGATTGCTTCGGCGTGGCGCGTTTGGAAGAAGCGTTAAAATTGCGTTCCAACGGTATTACCAAGCCGATTTTATTGCTGGAAGGTTTTTTCTCTGCTAAAGATTTACCCGTTCTGGCGGTGAACAACATTCAAACCGTGGTGCACAGCCAAGAACAGCTGGACGCGCTGGAACAGGCGAAAACCCCGAATCCGATCAAAGTCTGGTTAAAAATTGATACCGGTATGCACCGTTTAGGGGTACATTTAGACGAAGTGGATGCCTTTTATCAAAAATTAAAATCGTTACCCTGTGTTGACCCGAATATCGGTTTTGTTAGTCATTTTAGTCGCGCCGATGAATTGGCATGCGGTTATACCGAAAAACAATTGGCGCGTTTTTTACAGGCGACGGAAGGTAAAGGCGGTGAGCGTAGTATTTCCGCATCCGGCGGTATTTTATTCTGGCAGGACGCGCATTTGGATTGGATCCGCCCTGGTATTATTATGTACGGCATTTCACCGAATAATACCGCCGGCAAAGAATACGGTTTAATTCCGGTGATGAATCTTACGTCTTCCCTAATTGCCGTACGCGAACATAAAAAAGGCGAGCCGGTGGGCTACGGCGGCGTTTGGATGAGTGACAAAGATACCAAAATCGGCGTGGTGGCAATCGGCTACGGCGACGGTTATCCGCGTGACGTGCCGGAAGGTACGCCGGTTTACCTTAATGGTCGACGTGTGCCTATTGTCGGAAAGGTTTCCATGGATATGCTTACCGTGGATCTTGGTGCAGACAGTCAGGATAAGGTCGGTGATGAAGTGATCTTGTGGGGCAAAGAATTGCCTATTGAAGAAATTGCAGCAATTACCGGCGTTATCAGTTATGAATTAATCACCAAATTGACCCCGCGTGTTTTAACTGAATACATAGAT","","","39261","MHMKPATAKISSVALKHNIQTIKQKAPESKIIAVVKANAYGHGVVFVSSAVENLVDCFGVARLEEALKLRSNGITKPILLLEGFFSAKDLPVLAVNNIQTVVHSQEQLDALEQAKTPNPIKVWLKIDTGMHRLGVHLDEVDAFYQKLKSLPCVDPNIGFVSHFSRADELACGYTEKQLARFLQATEGKGGERSISASGGILFWQDAHLDWIRPGIIMYGISPNNTAGKEYGLIPVMNLTSSLIAVREHKKGEPVGYGGVWMSDKDTKIGVVAIGYGDGYPRDVPEGTPVYLNGRRVPIVGKVSMDMLTVDLGADSQDKVGDEVILWGKELPIEEIAAITGVISYELITKLTPRVLTEYID","1098294","[FUNCTION] Provides the D-alanine required for cell wall biosynthesis (By similarity).[CATALYTIC ACTIVITY] L-alanine = D-alanine.[COFACTOR] Pyridoxal phosphate (By similarity).[PATHWAY] Along with D-alanine--D-alanine ligase, it makes up the D-alanine branch of the peptidoglycan biosynthetic route.","alanine racemase 1","Cytoplasm","","
InterPro
IPR000821
Domain
Alanine racemase region
PR00992\"[28-44]T\"[63-81]T\"[123-135]T\"[158-169]T\"[195-222]T\"[251-266]T\"[268-283]T\"[289-306]T\"[341-354]TALARACEMASE
TIGR00492\"[4-360]Talr: alanine racemase
PS00395\"[33-43]TALANINE_RACEMASE
InterPro
IPR001608
Domain
Alanine racemase, N-terminal
PF01168\"[5-223]TAla_racemase_N
InterPro
IPR011079
Domain
Alanine racemase, C-terminal
PF00842\"[235-359]TAla_racemase_C
InterPro
IPR012155
Family
Alanine racemase
PIRSF001401\"[8-360]TAlanine racemase
noIPR
unintegrated
unintegrated
G3DSA:2.40.37.10\"[222-358]Tno description
G3DSA:3.20.20.10\"[3-217]Tno description


","No hits to the COGs database.","Significant hit ( 1.8e-82) to 6/6 blocks of the IPB000821 family, which is described as \"Alanine racemase\". Interpro entry for IP:IPR000821. IPB000821A 33-43 7e-08 IPB000821B 54-81 1.1e-13 IPB000821C 122-134 2.5e-10 IPB000821D 196-222 8.6e-15 IPB000821E 251-281 4.9e-20 IPB000821F 333-358 1.3e-08","Residues 9 to 144 match (6e-09) PD:PD430024 which is described as ALANINE PHOSPHATE PYRIDOXAL ISOMERASE CELL PROTEOME PEPTIDOGLYCAN COMPLETE SYNTHESIS WALL ","","","","","","","","","","","Mon Jan 6 09:50:31 2003","Mon Jan 6 09:50:31 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01623 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 235 to 359 (E-value = 2e-67) place AA01623 in the Ala_racemase_C family which is described as Alanine racemase, C-terminal domain (PF00842)","","","","","Strych U, Huang HC, Krause KL, Benedik MJ. Characterization of the alanine racemases from Pseudomonas aeruginosa PAO1. Curr Microbiol. 2000 Oct;41(4):290-4. PMID: 10977898 Tauch A, Gotker S, Puhler A, Kalinowski J, Thierbach G. The alanine racemase gene alr is an alternative to antibiotic resistance genes in cloning systems for industrial Corynebacterium glutamicum strains. J Biotechnol. 2002 Oct 9;99(1):79-91. PMID: 12204559 Patrick WM, Weisner J, Blackburn JM. Site-directed mutagene sis of Tyr354 in Geobacillus stearothermophilus alanine racemase identifies a role in controlling substrate specificity and a possible role in the evolution of antibiotic resistance. Chembiochem. 2002 Aug 2;3(8):789-92. PMID: 12203980 Strych U, Benedik MJ. Mutant analysis shows that alanine racemases fromPseudomonas aeruginosa and Escherichia coli are dimeric.J Bacteriol. 2002 Aug;184(15):4321-5. PMID: 12107154Kuramitsu,S., Inoue,K., Ogawa,T., Ogawa,H. and Kagamiyama,H. Aromatic amino acid aminotransferase of Escherichia coli: nucleotide sequence of the tyrB gene. Biochem. Biophys. Res. Commun. 133 (1): 134-139 (1985) [PubMed: 3907634].Yokoigawa,K., Hirasawa,R., Ueno,H., Okubo,Y., Umesako,S. and Soda,K. Gene cloning and characterization of alanine racemases from Shigella dysenteriae, Shigella boydii, Shigella flexneri, andShigella sonnei. Biochem. Biophys. Res. Commun. 288 (3): 676-684 (2001) [PubMed: 11676496].","","Mon Jan 6 09:50:31 2003","1","","","" "AA01624","1098315","1099961","1647","ATGCAAAATCTTAATCCAACCCAAACTAGCGCATGGAAAGCACTAACGCAACATCATGCACAATGCAAAAACGCTACGATTCAGGAATTATTTGCGCAAGAAAAAGATCGCTTTGCGCATTATTCTTTAACCTTCAACAATGAAATCTTAGTGGATTTTTCTAAAAATAATCTGACTCAGGAAACCCTCGACTTGTTGCGCCAACTCACCGAAGAGTGCGGTCTGGCGCAAGCGAAAGAAGCCATGTTCAACGGGGAAAAAATCAACCGTACGGAGAATCGTGCCGTTTTACACACCGCACTGCGTAATCGAGCCAATACGCCTGTCTTGGTGGATGGCAAAGACGTGATGCCGGAAGTGAATGCGGTGCTTGCGAAAATGAAATCTTTCTGTGAACGCGTGATTTCCGGCGAATGGAAAGGTTACACCGGCAAAGCCATTACCGACGTGATCAATATCGGGATCGGCGGTTCGGATCTCGGTCCTTATATGGTGACCGAAGCGTTGCGTCCGTATAAAAATCATTTAACCATGCACTTCGTGTCTAACGTGGACGGCACGCACATTGCGGAAACCTTAAAGAAAGTTAATCCGGAAACCACCCTTGTGTTGGTTGCCTCCAAAACTTTCACCACTCAAGAAACCATGACCAACGCCAACTCCGCCCGCGATTGGTTCTTAGCTACCGCAAAAGACGAAAAACACGTTGCAAAACATTTTGCGGCGCTTTCTACCAACGCCAAAGAAGTGGAAAAATTCGGTATCGACACCGACAATATGTTCGGTTTCTGGGATTGGGTCGGCGGACGTTATTCCTTATGGTCAGCCATCGGTTTATCCATCGCGCTTTCCATCGGCTTTGAAAACTTTGAAGCGCTTTTAAGCGGTGCGCACGAAATGGATAAACATTTCCGCAATGCGCCGTTGGAACAAAACATTCCGACCACATTGGCATTAGTGGGCTTGTGGAACACGAACTTCCTCGGCGCACAAACAGAAGCCATTTTGCCTTACGACCAATATTTACACCGTTTTGCCGCCTATTTCCAACAAGGCAACATGGAATCCAACGGTAAATACGTAGGACGTGACGGTAAAGTCATCGACAACTACCAAACCGGTCCGATTATCTGGGGTGAACCGGGCACTAACGGTCAACACGCGTTCTATCAATTGATTCACCAAGGTACCACATTAATTCCTTGTGATTTCATCGCGCCGGCGCAAACCCACAATCCGTTGTCCGATCATCACAACAAATTGCTTTCCAATTTCTTCGCGCAAACCGAAGCCTTGGCTTTCGGTAAAACCAAAGAGCAAGTGGAAGCGGAATTCCTGAAAGCGGGCAAAACCTTAGCGGAAGTTGAAGACATCGTGCCGTTCAAAGTATTCAACGGCAATAAACCGACCAACTCCATCTTGCTACAAAAAATCACCCCGTTCAGCCTTGGTGCCCTTATCGCCATGTATGAACACAAAATTTTCGTACAAGGCGTGCTGTTCAATATTTACAGCTTCGACCAATGGGGTGTGGAATTAGGGAAACAACTCGCCAACCGCATCCTGCCGGAATTGGTGAATAACGATAAAATCGAAAGCCACGACAGTTCAACCAATGGCTTGATTAATCAATTCAAAGCCTGGCGT","","","61484","MQNLNPTQTSAWKALTQHHAQCKNATIQELFAQEKDRFAHYSLTFNNEILVDFSKNNLTQETLDLLRQLTEECGLAQAKEAMFNGEKINRTENRAVLHTALRNRANTPVLVDGKDVMPEVNAVLAKMKSFCERVISGEWKGYTGKAITDVINIGIGGSDLGPYMVTEALRPYKNHLTMHFVSNVDGTHIAETLKKVNPETTLVLVASKTFTTQETMTNANSARDWFLATAKDEKHVAKHFAALSTNAKEVEKFGIDTDNMFGFWDWVGGRYSLWSAIGLSIALSIGFENFEALLSGAHEMDKHFRNAPLEQNIPTTLALVGLWNTNFLGAQTEAILPYDQYLHRFAAYFQQGNMESNGKYVGRDGKVIDNYQTGPIIWGEPGTNGQHAFYQLIHQGTTLIPCDFIAPAQTHNPLSDHHNKLLSNFFAQTEALAFGKTKEQVEAEFLKAGKTLAEVEDIVPFKVFNGNKPTNSILLQKITPFSLGALIAMYEHKIFVQGVLFNIYSFDQWGVELGKQLANRILPELVNNDKIESHDSSTNGLINQFKAWR","1099959","[CATALYTIC ACTIVITY] D-glucose 6-phosphate = D-fructose 6-phosphate.[PATHWAY] Involved in glycolysis and in gluconeogenesis.[SUBCELLULAR LOCATION] Cytoplasmic (By similarity).","glucose-6-phosphate isomerase","Cytoplasm","","
InterPro
IPR001672
Family
Phosphoglucose isomerase (PGI)
PR00662\"[150-169]T\"[261-279]T\"[338-359]T\"[466-484]T\"[484-498]T\"[498-511]TG6PISOMERASE
PTHR11469\"[1-549]TGLUCOSE-6-PHOSPHATE ISOMERASE
PF00342\"[52-542]TPGI
PS00174\"[498-515]TP_GLUCOSE_ISOMERASE_2
PS00765\"[265-278]TP_GLUCOSE_ISOMERASE_1
noIPR
unintegrated
unintegrated
G3DSA:1.10.1390.10\"[512-549]Tno description
G3DSA:3.40.50.10490\"[3-511]Tno description


","BeTs to 19 clades of COG0166COG name: Glucose-6-phosphate isomeraseFunctional Class: GThe phylogenetic pattern of COG0166 is -omp-zyqvdrlbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is","Significant hit (2.8e-220) to 8/8 blocks of the IPB001672 family, which is described as \"Phosphoglucose isomerase (PGI)\". Interpro entry for IP:IPR001672. IPB001672A 82-102 1e-17 IPB001672B 134-170 3.9e-30 IPB001672C 183-225 2.3e-35 IPB001672D 239-274 5.1e-29 IPB001672E 319-365 7.6e-37 IPB001672F 378-396 4.4e-19 IPB001672G 417-440 1.8e-16 IPB001672H 483-515 9.7e-28","Residues 417 to 478 match (5e-08) PD:PD491846 which is described as ISOMERASE GPI PROTEOME GLUCOSE-6-PHOSPHATE PGI PHI PHOSPHOHEXOSE GLYCOLYSIS PHOSPHOGLUCOSE COMPLETE ","","","","","Wed Feb 19 14:52:57 2003","","","","Wed Feb 19 14:52:57 2003","","Mon Jan 6 10:16:01 2003","Mon Jan 6 10:16:01 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01624 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Arsenieva D, Jeffery C. Conformational changes in phosphoglucose isomerase induced by ligand binding. J Mol Biol. 2002 Oct 11;323(1):77. PMID: 12368100 Froman,B.E., Tait,R.C. and Gottlieb,L.D. Isolation and characterization of the phosphoglucose isomerase gene from Escherichia coli. Mol. Gen. Genet. 217 (1): 126-131 (1989) PubMed: 2549364.Smith,M.W. and Doolittle,R.F. Anomalous phylogeny involving the enzyme glucose-6-phosphate isomerase. J. Mol. Evol. 34 (6): 544-545 (1992) PubMed: 1593646.Morita T, El-Kazzaz W, Tanaka Y, Inada T, Aiba H.Accumulation of glucose-6-phosphate or fructose-6-phosphate is responsible for destabilization of glucose transporter mRNA in Escherichia coli.J Biol Chem. 2003 Feb 10 PMID: 12578824","","Wed Feb 19 14:52:57 2003","1","","","" "AA01625","1100104","1100574","471","ATGAAAGTTTTAGAAGGTCATATCGCAACGCCGGAAGCTAAAGTCGCCGTGGTTATCAGCCGTTTCAACAGTTTTATCAACGAAAGCCTGCTTGAAGGCGCTCTGGATGCGTTAAAACGTGTCGGTCAAGTGAAAGATGAAAATATCACTTTAGTGCGCGTACCGGGTGCATATGAACTGCCGTTAGTAGCGCGCCGTTTGGCGGAAAGCAAAAAATTCGATGCCATTGTTGCTCTGGGTACGGTAATCCGTGGCGGCACGGCGCATTTTGAATATGTGGCGGGTGAGGCCAGCAGCGGTTTAGGCAAAGTGGCGATGGAATCCGAAATTCCGGTGGCATTCGGCGTATTAACTACCGAAAACATCGAACAAGCCATTGAACGTGCAGGCACCAAAGCCGGTAATAAAGGTGCGGAAGCTGCCTTAGTTGCGTTAGAAATGGTGAATCTGTTAAATCAAATTCAGGCTGCG","","","16539","MKVLEGHIATPEAKVAVVISRFNSFINESLLEGALDALKRVGQVKDENITLVRVPGAYELPLVARRLAESKKFDAIVALGTVIRGGTAHFEYVAGEASSGLGKVAMESEIPVAFGVLTTENIEQAIERAGTKAGNKGAEAALVALEMVNLLNQIQAA","1100572","From GenBank (gi:1172948):Riboflavin synthase is a bifunctional enzyme complex catalyzing the formation of riboflavin from 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione and L-3,4-dihydrohy-2-butanone-4-phosphate via 6,7-dimethyl-8-lumazine. The beta subunit catalyzes the condensation of 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione with L-3,4-dihydrohy-2-butanone-4-phosphate yielding 6,7-dimethyl-8-lumazine.Riboflavin synthase catalyzes 2 6,7-dimethyl-8-(1-D-ribityl)lumazine =riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine.This protein is the last step in Riboflavin biosynthesis. ","riboflavin synthase, beta chain","Cytoplasm","","
InterPro
IPR002180
Family
6,7-dimethyl-8-ribityllumazine synthase
PD003664\"[14-142]TRISB_HAEIN_P45149;
G3DSA:3.40.50.960\"[2-155]Tno description
PF00885\"[10-154]TDMRL_synthase
TIGR00114\"[13-151]Tlumazine-synth: 6,7-dimethyl-8-ribityllumaz
noIPR
unintegrated
unintegrated
PTHR21058\"[2-156]T6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE (DMRL SYNTHASE) (LUMAZINE SYNTHASE)


","No hits to the COGs database.","Significant hit ( 5.6e-66) to 5/5 blocks of the IPB002180 family, which is described as \"6,7-dimethyl-8-ribityllumazine synthase\". Interpro entry for IP:IPR002180. IPB002180A 14-38 3.1e-12 IPB002180B 54-68 3.4e-09 IPB002180C 73-93 2.1e-15 IPB002180D 111-130 9.1e-16 IPB002180E 135-147 1.6e-07","Residues 30 to 156 match (9e-52) PD:PD003664 which is described as SYNTHASE RIBOFLAVIN 67-DIMETHYL-8-RIBITYLLUMAZINE TRANSFERASE BETA CHAIN PROTEOME DMRL COMPLETE LUMAZINE ","","","","","","","","","","","Tue Jan 21 16:17:27 2003","Mon Jan 6 10:23:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01625 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 10 to 154 (E-value = 1.8e-85) place AA01625 in the DMRL_synthase family which is described as 6,7-dimethyl-8-ribityllumazine synthase (PF00885)","","","","","","","","1","","","" "AA01626","1100584","1101006","423","ATGGCTGAACAAACAAAAAAAATCTCTCCTCGTCGCCGCGCCCGTGAATGCGCCGTTCAGGCGTTATATTCTTGGGCGATTTCAAAAAATTCCCCGGAAATAGTGGAACTGAATTTCATCACCGAACAGGATATGAAAGGCGTTGATACACCGTATTTCCGCAAATTATTCCGTCAAACGGTGGAAAATGTGGAAGCGGTGGATGCCACCATGCAATGCTATTTGGATCGCACGTTAGAAGAATTGGATCCTATCGAAAAAGCCATTTTGCGTTTGGCGGTGTATGAGCTGCAATTTGAAGCGAACGTGCCTTACAAAGTGGTCATCAACGAAGCCATTGAAGTGGCGAAAGTGTTCGGCGCAGACGAAAGCCATAAATATATCAACGGTGTATTAGACAAAATTGCACCGGTTGTGCGTGCG","","","16135","MAEQTKKISPRRRARECAVQALYSWAISKNSPEIVELNFITEQDMKGVDTPYFRKLFRQTVENVEAVDATMQCYLDRTLEELDPIEKAILRLAVYELQFEANVPYKVVINEAIEVAKVFGADESHKYINGVLDKIAPVVRA","1101004","From GenBank (gi:13431742):This protein is involved in the transcription termination process (by similarity). ","N utilization substance protein B","Cytoplasm","","
InterPro
IPR006027
Domain
NusB/RsmB/TIM44
G3DSA:1.10.940.10\"[2-135]Tno description
PF01029\"[12-139]TNusB
InterPro
IPR011605
Family
NusB antitermination factor
TIGR01951\"[11-137]TnusB: transcription antitermination factor


","BeTs to 18 clades of COG0781COG name: Transcription termination factorFunctional Class: KThe phylogenetic pattern of COG0781 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 4e-38) to 3/3 blocks of the IPB000139 family, which is described as \"Antitermination protein NusB\". Interpro entry for IP:IPR000139. IPB000139A 11-22 1e-07 IPB000139B 85-97 5.3e-06 IPB000139C 103-135 2.2e-21","Residues 7 to 139 match (3e-52) PD:PD241318 which is described as PROTEOME COMPLETE B SUBSTANCE UTILIZATION N TRANSCRIPTION TERMINATION NUSB HOMOLOG ","","","","","","","","","","","Tue Jan 21 16:14:25 2003","Mon Jan 6 10:28:59 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01626 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 12 to 139 (E-value = 7.5e-47) place AA01626 in the NusB family which is described as NusB family (PF01029)","","","","","Luttgen H, Robelek R, Muhlberger R, Diercks T, SchusterSC, Kohler P, Kessler H, Bacher A, Richter G. Transcriptional regulation by antitermination. Interaction of RNA with NusB protein and NusB/NusE protein complex of Escherichia coli. J Mol Biol. 2002 Mar 1;316(4):875-85. PMID: 11884128 Imamoto,F. and Nakamura,Y. Escherichia coli proteins involved in regulation of transcription termination: function, structure, and expression of the nusA and nusB genes Adv. Biophys. 21, 175-192 (1986) PubMed: 3019094 Carlomagno MS, Nappo A. The antiterminator NusB enhances termination at a sub-optimal Rho site. J Mol Biol. 2001 May 25;309(1):19-28. PMID: 11491288 Taura,T., Ueguchi,C., Shiba,K. and Ito,K. Insertional disruption of the nusB (ssyB) gene leads to cold-sensitive growth of Escherichia coli and suppression of the secY24 mutation Mol. Gen. Genet. 234 (3), 429-432 (1992) PubMed: 1406588 ","","Mon Jan 6 10:28:59 2003","1","","","" "AA01628","1101028","1102008","981","ATGAGCGAAGGTGAATTTGACATCATTCAACGTTATTTTACTGCTTCCAAGCGTCCTCCGCGCAAAGATGTAGTGCTTTCGGTGGGCGATGATTGTGCCATCACCGAATTGAACACCAATCAGCATTTAGCCATCACCACCGACACCATGGTGGAAAACGTTCACTTCTTATCGACCATTCGCCCTGCTGATTTAGCCTACAAAGCGGTCGCCACTAATTTAAGCGATCTTGCCTCTATGGGTGCCGAACCCGCTTGGATTTCCCTCGCTTTAACCTTGCCGAAAATCGATCATGATTGGCTGGCGGAATTCAGTGAAAGTTTCTTTGCCATTTTGGATCATTACAACGTCGATTTAATCGGTGGCGACACCACGAAAGGCCCGTTAGGGTTGACCATTACCGCGCAAGGCATTATTGCGAAAAATAAAGGGTTATGTCGCCATCAGGCGAAAGTGGGGGATTGGATTTACGTTTCCGGCACCTTGGGCGACAGCGCGGCAGGCTTATCTTTTATCTTGCAGGGCAAAAGTGCGGTGAATTCTGCGCAAGAATTTTTAATTCAACGCCATCTGCGCCCGACACCAAGGGTGCTGCTGGGATTGGAACTTTCCGTTTCCGGTTTAGCAAATGCGGCAATCGACATCTCAGACGGGCTGGTTGCCGATTTAGGGCATATTTTAGAACGCAGCCAATGCGGTGCGATGATTGAATTGGATAAATTGCCCCTTTCCGCCGAGTTGGTCGCCGAAGTCGGTTTGGCGAAAGCGGAACAGTTTGCCTTGTCCGGCGGCGAAGACTACGAACTTTGTTTCACCGTACCTGACAACAATATCGTCAAATTAGAAAAAGCCCTGGCGCATCTCGGCGTGCCATATACCTGTATCGGGCAAATTCGTCACGCGGGCAAAAAACGTATTCAGTTTCAACGCAACGGGCTGGCGGTCGAGCTTGAGTTGCCATACGGTTTTGATCATTTCAAA","","","36071","MSEGEFDIIQRYFTASKRPPRKDVVLSVGDDCAITELNTNQHLAITTDTMVENVHFLSTIRPADLAYKAVATNLSDLASMGAEPAWISLALTLPKIDHDWLAEFSESFFAILDHYNVDLIGGDTTKGPLGLTITAQGIIAKNKGLCRHQAKVGDWIYVSGTLGDSAAGLSFILQGKSAVNSAQEFLIQRHLRPTPRVLLGLELSVSGLANAAIDISDGLVADLGHILERSQCGAMIELDKLPLSAELVAEVGLAKAEQFALSGGEDYELCFTVPDNNIVKLEKALAHLGVPYTCIGQIRHAGKKRIQFQRNGLAVELELPYGFDHFK","1102006","From GenBank (gi:6226713]):This protein cataltyzes ATP + thiamine phosphate = ADP + thiamine diphosphate. Its pathway is thiamine biosynthesis.","thiamin-monophosphate kinase","Cytoplasm","","
InterPro
IPR006283
Family
Thiamine-monophosphate kinase
PIRSF005303\"[3-327]TThiamine monophosphate kinase
TIGR01379\"[4-326]TthiL: thiamine-monophosphate kinase
InterPro
IPR010918
Domain
AIR synthase related protein, C-terminal
PF02769\"[151-309]TAIRS_C
noIPR
unintegrated
unintegrated
G3DSA:3.30.1330.10\"[4-143]Tno description
G3DSA:3.90.650.10\"[146-326]Tno description


","No hits to the COGs database.","","Residues 230 to 326 match (4e-19) PD:PD518803 which is described as KINASE PROTEOME COMPLETE THIAMINE-MONOPHOSPHATE TRANSFERASE THIAMINE THIAMINE-PHOSPHATE BIOSYNTHESIS THIAMIN-MONOPHOSPHATE MONOPHOSPHATE ","","","","","","","","","","","Tue Jan 21 16:21:47 2003","Tue Jan 21 16:21:47 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01628 is paralogously related to AA01206 (9e-06) and AA01760 (1e-04).","","","","","","Residues 151 to 309 (E-value = 1.7e-07) place AA01628 in the AIRS_C family which is described as AIR synthase related protein, C-terminal domain (PF02769)","","","","","Webb E, Downs D. Characterization of thiL, encoding thiamin-monophosphate kinase, in Salmonella typhimurium. J Biol Chem. 1997 Jun 20;272(25):15702-7. PMID: 9188462 Shikata H, Egi Y, Koyama S, Yamada K, Kawasaki T. Properties of the thiamin triphosphate-synthesizing activity catalyzed by adenylate kinase (isoenzyme 1). Biochem Int. 1989 May;18(5):943-9. PMID: 2551298 ","","Mon Jan 6 10:31:40 2003","1","","","" "AA01629","1102021","1102509","489","ATGACGTCATTACAACATCCGCTCGAACGGGTGAATTTGCGCAATCCTATTCATTTTTTCGCGCTGGGGTTCGGCTCCGGTTTATTGCGTCCCGCGCCCGGCACTTGGGGCAGTTTGGTCGGCGTGATTTTAGGCGCGTTATTGCTGCCGGTACTCGGCGCAAAAACATTTTTTATTTTGACCGCACTTTGCTTCTTCATCGGCATTTGGCTATGCGAACGCACCAGTCATGACATGGGCGTGCACGATCACGGCAGCATTGTGTGGGATGAAATCGTGGCGGTTTTCCTTGTGTTATTAGCCGTGCCGCAAGTGTCATTATTATGGTGCGCCATCGCTTTCGTGACTTTCCGTCTGTTTGATATTTTAAAACCTTATCCTATTCGCTATTTTGACGAAAAACTCACCAACGGCTTTGGCATTATGGTGGACGATATTTTGGCAGCAGGCTACAGCATCGTTGTTATTTTTGTATTAGCACATTTTATC","","","18071","MTSLQHPLERVNLRNPIHFFALGFGSGLLRPAPGTWGSLVGVILGALLLPVLGAKTFFILTALCFFIGIWLCERTSHDMGVHDHGSIVWDEIVAVFLVLLAVPQVSLLWCAIAFVTFRLFDILKPYPIRYFDEKLTNGFGIMVDDILAAGYSIVVIFVLAHFI","1102507","From GenBank (gi:1175729):PgpA specifically hydrolyzes phosphphatidylglycerophosphate. Its catalytic activity is phosphatidylglycerophosphate + H(2)O = phosphatidylglycerol + phosphate. It is an integral membrane protein, inner membrane (potential).","phosphatidylglycerophosphatase A","Inner membrane, Cytoplasm","","
InterPro
IPR007686
Family
Phosphatidylglycerophosphatase A
PF04608\"[17-160]TPgpA
noIPR
unintegrated
unintegrated
PD016242\"[17-159]TQ9CMT1_PASMU_Q9CMT1;
signalp\"[1-53]?signal-peptide
tmhmm\"[32-50]?\"[56-71]?\"[92-112]?\"[141-161]?transmembrane_regions


","BeTs to 9 clades of COG1267COG name: Phosphatidlglycerophosphatase A and related proteinsFunctional Class: IThe phylogenetic pattern of COG1267 is --m-kz-q---lb-efgh-nu-x---Number of proteins in this genome belonging to this COG is","","Residues 17 to 159 match (6e-45) PD:PD016242 which is described as COMPLETE PROTEOME PHOSPHATIDYLGLYCEROPHOSPHATASE A HYDROLASE TRANSMEMBRANE MEMBRANE DEGRADATION INNER PHOSPHOLIPID ","","","","","","","","","","","Tue Jan 21 16:25:51 2003","Mon Jan 6 10:35:19 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01629 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 16 to 161 (E-value = 6.9e-78) place AA01629 in the PgpA family which is described as Phosphatidylglycerophosphatase A (PF04608)","","","","","Funk CR, Zimniak L, Dowhan W. The pgpA and pgpB genes of Escherichia coli are not essential: evidence for a third phosphatidylglycerophosphate phosphatase. J Bacteriol. 1992 Jan;174(1):205-13. PMID: 1309518 Icho T. Membrane-bound phosphatases in Escherichia coli: sequence of the pgpA gene.J Bacteriol. 1988 Nov;170(11):5110-6. PMID: 2846510Icho T, Raetz CR.Multiple genes for membrane-bound phosphatases in Escherichia coli and their action on phospholipid precursors.J Bacteriol. 1983 Feb;153(2):722-30.PMID: 6296050 ","","Tue Feb 18 14:47:12 2003","1","","","" "AA01630","1102521","1103141","621","ATGTTAAATTTAATGTTCGTTCATTTGGTGGGATTGCTTTCCCCCGGACCGGATTTTTTCTATGTGAGCCGTGTCGCGGCAATCCGTTCACGACGTACCGCTATTTACGGCGTTATGGGCATTACGCTCGGCGTGTTCCTCTGGGCAACCGCTGCCGTGTTGGGGCTTGCTATCGTCTTTAAAACCTCGCCGGCATTGCAAGGCGTGGTGATGGCATTGGGGGGCAGTTATTTGTTTTATCTTGGCGTGAAAATGACGCGCGTTAAAACCAATGCGGTGTTTAATGATTCGGCGGAAGGGCAAAAAAGCGTGGGTGCCAAAAGTGAGTTACTGAAAGGGTTATTGGTCAATTTATCCAATGCCAAAGTGGTGATTTATTTCAGTAGCGTAATGTCTTTTGTGTTGGTCAACATCACCGAAACGTGGCAAATTCTGACCGCACTTTTGATTATCACGGTGGAAACTTTTTTGTATTTTTACGTCATTTCCATTTTATTCTCACGCCCTTTCGCCAGACAGTTTTACAGTCGATACAGTCACTATATTGATAACGTTTCGGGCGTAATTTTTATTTTATTCGGCATCTACTTAATTTATAGTGGTGCGCTGAAAGTGTTAGGC","","","22830","MLNLMFVHLVGLLSPGPDFFYVSRVAAIRSRRTAIYGVMGITLGVFLWATAAVLGLAIVFKTSPALQGVVMALGGSYLFYLGVKMTRVKTNAVFNDSAEGQKSVGAKSELLKGLLVNLSNAKVVIYFSSVMSFVLVNITETWQILTALLIITVETFLYFYVISILFSRPFARQFYSRYSHYIDNVSGVIFILFGIYLIYSGALKVLG","1103139","From GenBank (gi:2851443):RhtC Conducts the efflux of threonine. It is an integral membrane protein (potential), and belongs to the rht family. ","threonine efflux protein","Inner membrane, Cytoplasm","","
InterPro
IPR001123
Family
Lysine exporter protein (LYSE/YGGA)
PF01810\"[9-201]TLysE
noIPR
unintegrated
unintegrated
signalp\"[1-15]?signal-peptide
tmhmm\"[37-57]?\"[63-83]?\"[118-138]?\"[144-164]?\"[185-203]?transmembrane_regions


","No hits to the COGs database.","","Residues 162 to 201 match (6e-07) PD:PD475646 which is described as PROTEOME COMPLETE TRANSMEMBRANE HI1307 PM0727 ","","","","","","","","","","","Tue Jan 21 16:37:19 2003","Mon Jan 6 10:41:13 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01630 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 9 to 201 (E-value = 9.9e-53) place AA01630 in the LysE family which is described as LysE type translocator (PF01810)","","","","","Kruse D, Kramer R, Eggeling L, Rieping Influence of threonine exporters on threonine production in Escherichia coli.Appl Microbiol Biotechnol. 2002 Jul;59(2-3):205-10.PMID: 12111147Irino,N., Nakayama,K. and Nakayama,H. The recQ gene of Escherichia coli K12: primary structure and evidence for SOS regulation. Mol. Gen. Genet. 205 (2): 298-304 (1986) PubMed: 3027506].2. Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and Livshits,V.A. The novel transmembrane Escherichia coli proteins involved in the amino acid efflux. FEBS Lett. 452 (3): 228-232 (1999) PubMed: 10386596].","","Fri Jan 31 13:36:01 2003","1","","","" "AA01631","1103166","1103975","810","ATGACATTAAAAATTGCTGTAGTGGGCGCAGGCGGACGTATGGGTCGCCAATTAATTCAGGCGGTACATAACGCGGAAGGCGTGGAATTAGGTGCGGCGTTTGAGCGCAAAGGTTCCTCATTGGTGGGCGCCGATGCCGGCGAATTGGCGGGGATCGGCAACTTAGGCATTAAGGTCGGCGATGACTTAAACGCGGTGAAAGATCGTTTCGATTTACTGATTGATTTCACCCGCCCGGAAGGCACATTGGAACATTTGGCATTTTGTGTTGCCAACCATAAAAAAATCGTTATCGGTACCACGGGTTTTGATGACGCCGGCAAAGCGGCAATTAAATCGGCAGCCGAAAAGACCGCTATCGTGTTTGCTTCAAATTTCAGTGTCGGCGTGAATTTGGTCTTTAAATTATTGGAAAAAGCCGCCAAGGTGATGGGCGATTATTGCGACATCGAAATCATCGAAGCGCACCACCGCTATAAAGTCGATGCGCCGTCCGGTACCGCGCTTTCCATGGGCGAACATATTGCCAAAACCCTCGGACGGGATCTGAAAACCCACGGCGTATTTTGTCGCGATGGTATTATCGGTGAACGTAAACGTGATGAAATTGGCTTTTCCACCATTCGCGCCTCCGATGTGGTGGGCGAGCACAGCGTCTGGTTTGCCGACATCGGTGAACGGGTAGAAATAGCCCACAAAGCCTCCAGCCGCATGACCTTCGCCAACGGAGCCGTACGTGCCGCCAAATGGCTTGAAGGTAAAAACAACGGCTTGTTCGACATGACGGACGTGTTGGATTTGAATAATTTA","","","28849","MTLKIAVVGAGGRMGRQLIQAVHNAEGVELGAAFERKGSSLVGADAGELAGIGNLGIKVGDDLNAVKDRFDLLIDFTRPEGTLEHLAFCVANHKKIVIGTTGFDDAGKAAIKSAAEKTAIVFASNFSVGVNLVFKLLEKAAKVMGDYCDIEIIEAHHRYKVDAPSGTALSMGEHIAKTLGRDLKTHGVFCRDGIIGERKRDEIGFSTIRASDVVGEHSVWFADIGERVEIAHKASSRMTFANGAVRAAKWLEGKNNGLFDMTDVLDLNNL","1103973","From GenBank (gi:13431431):The catalytic activity of this protein is 2,3,4,5-tetrahydrodipicolinate + NAD(P)(+) = 2,3-dihydrodipicolinate + NAD(P)H.The pathway of DapB is the second step in the biosynthesis of diaminopimelate and lysine from aspartate semialdehyde.Its subcellular location is cytoplasmic (By similarity).","dihydrodipicolinate reductase","Cytoplasm","","
InterPro
IPR000846
Family
Dihydrodipicolinate reductase
PD004105\"[68-265]TDAPB_HAEIN_P45153;
PF01113\"[3-126]TDapB_N
PF05173\"[129-266]TDapB_C
PS01298\"[151-168]TDAPB
InterPro
IPR011770
Family
Dihydrodipicolinate reductase, bacterial and plant
PIRSF000161\"[3-267]TDihydrodipicolinate reductase
TIGR00036\"[2-268]TdapB: dihydrodipicolinate reductase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[3-150]T\"[171-270]Tno description
PTHR20836\"[2-267]TDIHYDRODIPICOLINATE REDUCTASE


","BeTs to 18 clades of COG0289COG name: Dihydrodipicolinate reductaseFunctional Class: EThe phylogenetic pattern of COG0289 is a-m----qv-rlbcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 2.1e-75) to 5/5 blocks of the IPB000846 family, which is described as \"Dihydrodipicolinate reductase\". Interpro entry for IP:IPR000846. IPB000846A 4-15 1e-05 IPB000846B 71-103 4.4e-21 IPB000846C 118-133 3e-06 IPB000846D 149-168 3.5e-16 IPB000846E 207-244 1.3e-20","Residues 3 to 53 match (3e-08) PD:PD510971 which is described as BIOSYNTHESIS DIHYDRODIPICOLINATE REDUCTASE NADP LYSINE DIAMINOPIMELATE DHPR OXIDOREDUCTASE COMPLETE PROTEOME ","","","","","","","","","","","Wed Jan 22 08:25:31 2003","Mon Jan 6 11:03:44 2003","","Mon May 23 08:10:39 2005","Mon May 23 08:10:39 2005","Mon May 23 08:10:39 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA01631 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon May 23 08:10:39 2005","","","","","Residues 129 to 266 (E-value = 2.7e-79) place AA01631 in the DapB_C family which is described as Dihydrodipicolinate reductase, C-terminus (PF05173)","Mon May 23 08:10:39 2005","","","","Liu,L. and Shaw,P.D. Characterization of dapB, a gene required by Pseudomonas syringae pv. tabaci BR2.024 for lysine and tabtoxinine-beta-lactam biosynthesis J. Bacteriol. 179 (2), 507-513 (1997) PubMed: 8990304 Bouvier,J., Richaud,C., Richaud,F., Patte,J.C. and Stragier,P. Nucleotide sequence and expression of the Escherichia coli dapB gene. J. Biol. Chem. 259 (23): 14829-14834 (1984) [PubMed: 6094578].Bouvier,J., Patte,J.C. and Stragier,P. Multiple regulatory signals in the control region of the Escherichia coli carAB operon. Proc. Natl. Acad. Sci. U.S.A. 81 (13): 4139-4143 (1984) [PubMed: 6377309].Scapin,G., Blanchard,J.S. and Sacchettini,J.C. Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase. Biochemistry 34 (11): 3502-3512 (1995) [PubMed: 7893645].Scapin,G., Reddy,S.G., Zheng,R. and Blanchard,J.S. Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor2,6-pyridinedicarboxylate. Biochemistry 36 (49): 15081-15088 (1997) [PubMed: 9398235].","","Mon Jan 6 11:03:44 2003","1","","","" "AA01633","1104393","1104148","246","ATGAAAATCCATTTATTACTCCGCCAACAAACCATCGAACACGATAACCGAATTCCGCTTCTCAACCGTCTGGAACAACACGGCGTTCATCACGAATACCAATGTCGCAGTGGCTACTGTGGTTCCTGTCGGGTAAAAATCAAAAAAGGCAAGGTGTCCTACGCAGAAACACCGTTAGCCTTTTTACAAAAAGATGAGATTTTATTGTGTTGTTGTCGGGTGGAAGAAGATTTGGAAATTGAATTG","","","9617","MKIHLLLRQQTIEHDNRIPLLNRLEQHGVHHEYQCRSGYCGSCRVKIKKGKVSYAETPLAFLQKDEILLCCCRVEEDLEIEL","1104146","[FUNCTION] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. [COFACTOR] Binds 1 2Fe-2S cluster. ","probable ferredoxin-like protein","Cytoplasm","","
InterPro
IPR001041
Domain
Ferredoxin
PF00111\"[24-76]TFer2
PS51085\"[1-82]T2FE2S_FER_2
InterPro
IPR006058
Binding_site
2Fe-2S ferredoxin, iron-sulfur binding site
PS00197\"[35-43]T2FE2S_FER_1
InterPro
IPR012675
Domain
Beta-grasp fold, ferredoxin-type
G3DSA:3.10.20.30\"[9-82]Tno description


","BeTs to 8 clades of COG0633COG name: FerredoxinFunctional Class: CThe phylogenetic pattern of COG0633 is ao----yq-dr--cefgh-n-jxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 4.8e-11) to 2/2 blocks of the IPB000564 family, which is described as \"2Fe-2S Ferredoxin\". Interpro entry for IP:IPR000564. IPB000564A 32-50 1.2e-07 IPB000564B 68-77 0.16","Residues 1 to 82 match (5e-26) PD:PD000232 which is described as IRON-SULFUR ELECTRON FERREDOXIN CHLOROPLAST COMPLETE PROTEOME OXIDOREDUCTASE REDUCTASE I COMPONENT ","","","","","","","","","","","Mon Jan 6 11:15:28 2003","Mon Jan 6 11:15:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01633 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 76 (E-value = 5.9e-11) place AA01633 in the Fer2 family which is described as 2Fe-2S iron-sulfur cluster binding domain (PF00111)","","","","","Carlson,J., Fuchs,J.A. and Messing,J. Primary structure of the Escherichia coli ribonucleoside diphosphate reductase operon. Proc. Natl. Acad. Sci. U.S.A. 81 (14): 4294-4297 (1984) [PubMed: 6087316].","","Mon Jan 6 11:15:28 2003","1","","","" "AA01634","1104730","1104464","267","ATGTACCCACCCTTTTTATATTCGATTTTCGAGCAGGTACATCCCCCAAAAACGCCTCTAAAAGTCACCGCACTTTCTACCACCCTCCAACCGCTTAACATCCGCCACAAACTTGAACCTATTACCAAACCGAAACAACTTTTTTCTCAATATAACAGCCTGATTATTTTCATTTTAGATTTCGATTTTATTTTGATGTTGGTGTTAATTAACGCCCCTCCTTTCTCTCCACAGGAAAATCACGAACCGGCGTATTCCGCGTCGATC","","","10649","MYPPFLYSIFEQVHPPKTPLKVTALSTTLQPLNIRHKLEPITKPKQLFSQYNSLIIFILDFDFILMLVLINAPPFSPQENHEPAYSASI","1104462","","hypothetical protein","Cytoplasm, Inner membrane","","
noIPR
unintegrated
unintegrated
tmhmm\"[53-73]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Jan 6 11:17:50 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01634 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01635","1105882","1104755","1128","ATGGCATACACCACTTTCTCACAAAACAAAAACGACCAATTAAAAGAACCGATGTTCTTTGGTCAAAACGTCAACGTAGCGCGTTACGATCAACAAAAATATGAGACTTTTGAAAAGCTCATTGAAAAACAACTTTCCTTCTTCTGGCGTCCGGAAGAAGTGGATGTGTCGCAAGACCGTATCGACTACGCGGCGTTGCCTGAACATGAAAAACACATTTTCATCAGCAACTTAAAATATCAAACCTTGTTGGATTCCATTCAAGGCAGAAGCCCGAATGTGGCGTTGTTGCCGTTGGTGTCCATTCCGGAATTGGAAACCTGGATCGAGACCTGGACCTTCTCCGAAACCATCCATTCCCGTTCTTACACCCACATTATTCGTAACATCGTAAACGATCCGTCCATCGTGTTTGATGACATCGTGACCAACGAAGAAATCATCAAACGCGCACGCGATATTTCTTCTTACTACGACGATTTAATCCGCGACAGCCAGCTTTACAGCCTCTACGGCGAAGGCACTTACACTGTGGACGGTAAAGAATGCGTGGTGAGCCTGCGTAACCTGAAAAAACAACTTTACCTGTGCTTAATGAGCGTCAACGCCTTGGAAGCCATTCGCTTCTATGTGTCTTTTGCCTGTTCCTTCGCTTTTGCAGAACGCCAATTAATGGAAGGTAATGCAAAAATCATTAAATTCATCGCTCGTGATGAAGCATTACACTTAACCGGTACGCAGCACATTTTGAACATTATGGCGGCGGGTCAGGACGATCCTGAAATGGCGGAAATTGCCGAAGAATGCAAACAGGAAGCCTACGATTTGTTCCTCGCCGCGGCGGAACAGGAAAAAGACTGGGCGGATTATTTGTTTAAAGACGGTTCCATGATCGGTTTGAACAAAGACATTTTGGTGCAATATGTGGAATACATCACCAATATCCGTATGCAGGCGGTAGGCTTGCCGTTGCCGTTCCAAGCGCGCTCTAATCCGATTCCTTGGATCAACGCCTGGTTGGTTTCCGACAACGTACAGGTGGCACCGCAAGAAGTGGAAGTGAGTTCTTATCTTGTGGGTCAAATCGATTCCAAAGTCGATACCAAAGATTTTGATGATTTTGATTTG","","","43399","MAYTTFSQNKNDQLKEPMFFGQNVNVARYDQQKYETFEKLIEKQLSFFWRPEEVDVSQDRIDYAALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLVSIPELETWIETWTFSETIHSRSYTHIIRNIVNDPSIVFDDIVTNEEIIKRARDISSYYDDLIRDSQLYSLYGEGTYTVDGKECVVSLRNLKKQLYLCLMSVNALEAIRFYVSFACSFAFAERQLMEGNAKIIKFIARDEALHLTGTQHILNIMAAGQDDPEMAEIAEECKQEAYDLFLAAAEQEKDWADYLFKDGSMIGLNKDILVQYVEYITNIRMQAVGLPLPFQARSNPIPWINAWLVSDNVQVAPQEVEVSSYLVGQIDSKVDTKDFDDFDL","1104753","[FUNCTION] Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides, precursors that are necessary for dna synthesis (by similarity). [catalytic activity] 2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H(2)O = ribonucleoside diphosphate + reduced thioredoxin. [COFACTOR] Binds 2 iron ions (by similarity). [PATHWYA] DNA replication pathway; first step. [SUBUNIT] Tetramer of two alpha and two beta chains (by similarity). [SIMILARITY] Belongs to the ribonucleoside diphosphate reductase small chain family. ","ribonucleoside diphosphate reductase, beta chain","Cytoplasm","","
InterPro
IPR000358
Family
Ribonucleotide reductase
PTHR23409\"[19-159]T\"[189-366]TRIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN
PF00268\"[203-314]TRibonuc_red_sm
PS00368\"[115-131]TRIBORED_SMALL
InterPro
IPR012348
Family
Ribonucleotide reductase-related
G3DSA:1.10.620.20\"[2-340]Tno description


","BeTs to 19 clades of COG0208COG name: Ribonucleotide reductase beta subunitFunctional Class: FThe phylogenetic pattern of COG0208 is -o----yq-drlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-45) to 5/5 blocks of the IPB000358 family, which is described as \"Ribonucleotide reductase\". Interpro entry for IP:IPR000358. IPB000358A 33-87 1.3e-16 IPB000358B 108-133 3.2e-07 IPB000358C 211-251 3.4e-15 IPB000358D 318-328 1.3e+02 IPB000358E 347-357 0.11","Residues 30 to 158 match (8e-08) PD:PD006930 which is described as REDUCTASE COMPLETE PROTEOME RIBONUCLEOTIDE SUBUNIT RIBONUCLEOSIDE-DIPHOSPHATE BETA CHAIN OXIDOREDUCTASE SMALL ","","","","","","","","","","","Thu Jan 23 09:15:19 2003","Mon Jan 6 11:24:52 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01635 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 16 to 339 (E-value = 2.4e-147) place AA01635 in the Ribonuc_red_sm family which is described as Ribonucleotide reductase, small chain (PF00268)","","","","","Carlson,J., Fuchs,J.A. and Messing,J. Primary structure of the Escherichia coli ribonucleoside diphosphate reductase operon. Proc. Natl. Acad. Sci. U.S.A. 81 (14): 4294-4297 (1984) [PubMed: 6087316]. Salowe,S.P. and Stubbe,J. Cloning, overproduction, and Purification of the B2 subunit of ribonucleoside-diphosphate reductase. J. Bacteriol. 165 (2): 363-366 (1986) [PubMed: 3511029].Nordlund,P., Sjoberg,B.M. and Eklund,H. Three-dimensional structure of the free radical protein of ribonucleotide reductase. Nature 345 (6276): 593-598 (1990) [PubMed: 2190093].Nordlund,P. and Eklund,H. Structure and function of the Escherichia coli ribonucleotide reductase protein R2. J. Mol. Biol. 232 (1): 123-164 (1993) [PubMed: 8331655].Logan,D.T., Su,X.D., Aberg,A., Regnstrom,K., Hajdu,J., Eklund,H. and Nordlund,P. Crystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at adinuclear iron site. Structure 4 (9): 1053-1064 (1996) [PubMed: 8805591].Guzman EC, Caballero JL, Jimenez-Sanchez A. Ribonucleoside diphosphate reductase is a component of the replication hyperstructure in Escherichia coli. Mol Microbiol. 2002 Jan;43(2):487-95. PMID: 11985724 Gallardo-Madueno R, Leal JF, Dorado G, Holmgren A,Lopez-Barea J, Pueyo C. In vivo transcription of nrdAB operon and of grxA and fpg genes is triggered in Escherichia coli lacking both thioredoxin and glutaredoxin 1 or thioredoxin and glutathione, respectively. J Biol Chem. 1998 Jul 17;273(29):18382-8. PMID: 9660805 ","","Mon Jan 6 11:24:52 2003","1","","","" "AA01636","1106740","1106087","654","ATGAATGAATTGACAATAAAAATTGTAATGCTTTTATTACCTGGCATTATAATTACAATGCTTATAGATAAGTTCACTGAACATAAAGAATGGAATAACTATAAATATTCATTGTTTGTTATTTCATATGGAATATTATCTTACTTAATATTACAAATTCTATCGCTATTAAATCAATGTGCCAAAATCGGGTACGAAAATTTCACATTAAATAATGCAGAGTATCTTCAAGTATGGGATGTTAATTCAAGTATTAACCTACCTTATAATGAAGTAATTGCTTCAGGAATAGTGTCATTTTTTCTTGGTTTATTATTTGTTTACATAGATCACAAAGAATACCTTGCCAAATTTCTTCTTAAATTTAATATTTCTAGAAAATATGGTGATTATGGAGTATTCCCCCAGTTATTAAAAGATAACAAAGATCAATACATAGATATCACTATTTGGGATAAAAATTTATTTATTAGGGGTATTGTAAATTCCTTTCATGAAGATAAAGAACTATTCGAAATATACATTGAAAATGCTGATGTTTATAAAACATCAAAAGGTAAAGCAACAAAAATTTACACAGCTCTTAGACTTTCAATATGTGAGCCATATAAAAACCTTATAATTTCAACTACACAACAACCTTCAAAAGGAGAA","","","25404","MNELTIKIVMLLLPGIIITMLIDKFTEHKEWNNYKYSLFVISYGILSYLILQILSLLNQCAKIGYENFTLNNAEYLQVWDVNSSINLPYNEVIASGIVSFFLGLLFVYIDHKEYLAKFLLKFNISRKYGDYGVFPQLLKDNKDQYIDITIWDKNLFIRGIVNSFHEDKELFEIYIENADVYKTSKGKATKIYTALRLSICEPYKNLIISTTQQPSKGE","1106085","","conserved hypothetical protein","Cytoplasm, Inner membrane","","
noIPR
unintegrated
unintegrated
signalp\"[1-19]?signal-peptide
tmhmm\"[4-22]?\"[37-57]?\"[89-109]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Jan 6 12:44:46 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01636 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01637","1109064","1106797","2268","ATGAACAAGGCATTGATGGTCACCAAACGTGACGGAAAACCGGAACCGATTAATCTTGATAAAATTCACCGCGTGATCACTTGGGCGGCGGAAGGGTTGGACAATGTGTCCGTGTCTCAAGTGGAATTGCGTTCTCACATTCAGTTTTATGAAGGGATTCGCACCTCCGACATTCACGAAACCATTATTAAAGCGGCGGCGGATCTGATCAGCAAAGATTCCCCGGATTATCAATACCTTGCCGCGCGCCTTGCGGTGTTCCATTTGCGTAAAAAAGCGTACGGGCATTTTGATCCGCCGCGTTTATACGATCACGTGAAAAAACTGGTACGTATGGGCAAATACGATCCGTCTTTATTGGATGACTACACTCGCGAAGAATGGGATGAAATGGACGGTTTTATCGACCATTGGCGCGATATGACCTTCTCTTATGCGGCAGTGAAGCAATTAGAAGGCAAATATTTAGTCCAAAACCGTGTGACCGGTGAGATCTACGAATCCGCCCAATTCCTCTATTTATTGGTAGCGGCGAGCCTGTTCTCCAAATACCCGCAGGAAACCCGTTTGGATTATGTGCGCCGTTTTTACGATGCCACCTCCACCTTTAAAATTTCCCTGCCGACCCCAATCATGGCAGGCGTGCGCACCCCAACCCGTCAATTCAGCTCTTGCGTGCTGATCGAATGCGGCGACAGCCTAGATTCCATTAACGCGACCGCCTCCGCCATTGTGAAATACGTTTCCCAACGCGCCGGTATCGGGATCAACGCGGGCGCTATTCGCGCTCTTGGCAGCCCGATTCGTGGCGGCGAAGCCTTCCATACCGGTTGTATTCCATTCTACAAACACTTCCAAACTGCCGTCAAATCCTGCTCACAGGGCGGTGTGCGCGGCGGTGCGGCAACGGTGTATTACCCGATTTGGCACTTGGAAGTGGAAAGCCTGTTGGTGTTGAAAAACAACCGTGGCGTGGAAGACAACCGTGTGCGTCACATGGACTACGGTGTGCAACTCAACAAATTAATGTATCAACGCTTAATTAAAGGCGGCGACATTACCCTATTCAGCCCGTCCGATGTGCCGGGGCTTTATGAAACGTTCTTTGCCGATCAAGATAAATTCGAGCAACTTTATGTGCAATACGAACAGGATCCAAACATTCGTAAACGCACCGTGAAAGCCGTGGAATTATTCTCCTTATTAATGCAGGAGCGTGCTTCCACCGGTCGTATTTATATTCATAACGTGGACCACTGTAACACCCATTCACCGTTCGATCCGAAAGTAGCACCGGTGCGTCAATCCAATCTTTGCCTGGAAATCGCCCTGCCGACCAAACCGTTACAACATTTCCACGATGAAAATGGCGAAATAGCCCTTTGTACCCTTTCCGCCTTTAACTTAGGCAAACTGGAAAACTTAGACGAGTTAGACAACCTGGCAGATCTTGCTGTTCGCACCTTAGATGCCTTATTGGATTACCAAGATTATCCGGTGATTGCGGCGAAACGCAGTTCCCTTGCCCGTCGTTCTTTGGGTATCGGCGTGATTAACTATGCATATTACTTGGCGAAACACGGCGTGCGTTATTCCGACGGCAGCGCCAACGATTTAACCCACCGCACTTTTGAAGCCATTCAATATTATTTACTGAAAGCCTCCATGAATTTGGCAAAAGAACAAGGCGCGTGCGAGTATTTCAACGAAACCACTTACGCCCAAGGCATTTTGCCAATCGATACTTACAAAAAAGACATCGACAGCCTAACCACCGAACCGCTGCATTACGACTGGGAAAGCCTGCGCCGCGACATCCAAGAATTCGGCTTGCGTAACTCCACCCTCACCGCCTTAATGCCGTCGGAAACCTCTTCCCAGATTTCCAACGCCACCAACGGCATCGAACCGCCACGCGGTCATGTGAGCGTGAAAGCCTCCAAAGACGGCATTTTGAAACAAGTGGTGCCGGATTACGAAAACCTCGGCGAAAACTACGAATTGCTTTGGGATATTCCAAGCAATGACGGTTACTTACACTTAGTGGGCATCATGCAAAAATTCGTGGATCAAGCGATTTCCGCTAATACCAATTACGATCCGAAACGTTTTGAAGACGGCAAAGTGCCGATGAAAGTGTTGTTAAAAGATCTCTTAACCGCTTACAAATACGGCTTAAAAACCCTCTACTACCAGAACACCCGCGACGGCGCCGAAGACAGCCAAGAAGATTTGGATGATGGTTGTGCCGGTGGGGCGTGTAAGATT","","","85435","MNKALMVTKRDGKPEPINLDKIHRVITWAAEGLDNVSVSQVELRSHIQFYEGIRTSDIHETIIKAAADLISKDSPDYQYLAARLAVFHLRKKAYGHFDPPRLYDHVKKLVRMGKYDPSLLDDYTREEWDEMDGFIDHWRDMTFSYAAVKQLEGKYLVQNRVTGEIYESAQFLYLLVAASLFSKYPQETRLDYVRRFYDATSTFKISLPTPIMAGVRTPTRQFSSCVLIECGDSLDSINATASAIVKYVSQRAGIGINAGAIRALGSPIRGGEAFHTGCIPFYKHFQTAVKSCSQGGVRGGAATVYYPIWHLEVESLLVLKNNRGVEDNRVRHMDYGVQLNKLMYQRLIKGGDITLFSPSDVPGLYETFFADQDKFEQLYVQYEQDPNIRKRTVKAVELFSLLMQERASTGRIYIHNVDHCNTHSPFDPKVAPVRQSNLCLEIALPTKPLQHFHDENGEIALCTLSAFNLGKLENLDELDNLADLAVRTLDALLDYQDYPVIAAKRSSLARRSLGIGVINYAYYLAKHGVRYSDGSANDLTHRTFEAIQYYLLKASMNLAKEQGACEYFNETTYAQGILPIDTYKKDIDSLTTEPLHYDWESLRRDIQEFGLRNSTLTALMPSETSSQISNATNGIEPPRGHVSVKASKDGILKQVVPDYENLGENYELLWDIPSNDGYLHLVGIMQKFVDQAISANTNYDPKRFEDGKVPMKVLLKDLLTAYKYGLKTLYYQNTRDGAEDSQEDLDDGCAGGACKI","1106795","[FUNCTION] Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides, precursors that are necessary for DNA synthesis (by similarity). [CATALYTIC ACTIVITY] 2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H(2)O = ribonucleoside diphosphate + reduced thioredoxin. [PATHWAY] DNA replication pathway; first step. [SUBUNIT] Tetramer of two alpha and two beta chains (by similarity). [SIMILARITY] Belongs to the ribonucleoside diphosphate reductaselarge chain family. ","ribonucleoside diphosphate reductase","Cytoplasm","","
InterPro
IPR000788
Domain
Ribonucleotide reductase large subunit, C-terminal
PR01183\"[298-317]T\"[433-444]T\"[473-496]T\"[511-533]T\"[539-562]T\"[610-637]TRIBORDTASEM1
PTHR11573\"[206-751]TRIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN
PF02867\"[222-736]TRibonuc_red_lgC
PS00089\"[599-621]TRIBORED_LARGE
InterPro
IPR005144
Domain
ATP-cone
PF03477\"[5-94]TATP-cone
PS51161\"[5-95]TATP_CONE
InterPro
IPR013346
Domain
Ribonucleoside-diphosphate reductase, alpha subunit
TIGR02506\"[145-735]TNrdE_NrdA: ribonucleoside-diphosphate reduc
InterPro
IPR013509
Domain
Ribonucleotide reductase large subunit, N-terminal
PF00317\"[141-220]TRibonuc_red_lgN
noIPR
unintegrated
unintegrated
G3DSA:1.10.395.10\"[96-200]Tno description
G3DSA:1.10.40.20\"[1-95]Tno description
G3DSA:3.90.244.10\"[201-324]T\"[438-737]Tno description
PTHR11573:SF5\"[206-751]TRIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN


","BeTs to 25 clades of COG0209COG name: Ribonucleotide reductase alpha subunitFunctional Class: FThe phylogenetic pattern of COG0209 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit (8.7e-121) to 10/10 blocks of the IPB000788 family, which is described as \"Ribonucleotide reductase large subunit\". Interpro entry for IP:IPR000788. IPB000788A 12-22 0.02 IPB000788B 145-156 0.0096 IPB000788C 197-227 7.3e-18 IPB000788D 247-283 9.1e-21 IPB000788E 298-320 3.1e-12 IPB000788F 374-383 0.1 IPB000788G 431-450 2.7e-09 IPB000788H 549-577 7.4e-15 IPB000788I 599-637 1.3e-21 IPB000788J 722-731 0.00036","Residues 222 to 322 match (1e-16) PD:PD012935 which is described as REPLICATION CHAIN RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE DNA OXIDOREDUCTASE ALPHA ","","","","","","","","","","","Mon Jan 6 12:52:20 2003","Mon Jan 6 12:52:20 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01637 is paralogously related to AA02210 (2e-20).","","","","","","Residues 222 to 736 (E-value = 3.7e-248) place AA01637 in the Ribonuc_red_lgC family which is described as Ribonucleotide reductase, barrel domain (PF02867)","","","","","Guzman EC, Caballero JL, Jimenez-Sanchez A. Ribonucleoside diphosphate reductase is a component of the replication hyperstructure in Escherichia coli. Mol Microbiol. 2002 Jan;43(2):487-95. PMID: 11985724 Gallardo-Madueno R, Leal JF, Dorado G, Holmgren A, Lopez-Barea J, Pueyo C. In vivo transcription of nrdAB operon and of grxA and fpg genes is triggered in Escherichia coli lacking both thioredoxin and glutaredoxin 1 or thioredoxin and glutathione, respectively. J Biol Chem. 1998 Jul 17;273(29):18382-8. PMID: 9660805 Nilsson,O., Aberg,A., Lundqvist,T. and Sjoberg,B.M. Nucleotide sequence of the gene coding for the large subunit of ribonucleotide reductase of Escherichia coli. Correction. Nucleic Acids Res. 16 (9): 4174 (1988) [PubMed: 3287341].Carlson,J., Fuchs,J.A. and Messing,J. Primary structure of the Escherichia coli ribonucleoside diphosphate reductase operon. Proc. Natl. Acad. Sci. U.S.A. 81 (14): 4294-4297 (1984) [PubMed: 6087316].","","Mon Jan 6 12:52:20 2003","1","","","" "AA01639","1109413","1109276","138","TTGCGGAATTTGTTGAGAAATTTAAGGGCATCGGTGGAAGTATCTAATCACCTTTCCCCTAAAAAGTGCGGTGGAAATTTAAGGTGTTTTTTCACCGCACTTTTTTCTTTCAAAACGCCCTACCCTCATCATTTCGCA","","","5271","LRNLLRNLRASVEVSNHLSPKKCGGNLRCFFTALFSFKTPYPHHFA","1109276","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 15:30:34 2004","Thu Feb 26 15:30:34 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01639 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 15:30:34 2004","","","","","","","","","","","","","1","","","" "AA01640","1110899","1109370","1530","TTGAACAACTTCAAACAAAAGACACATCGTTTCAACGCCGGCAATCAAGGCTTTAATGCGATGTTTGCGGTGAGTAGTGTGGAGGCGGCAAAGTTTTATTATGAAGCATTTAAAAAGCAACAAAGTGCGGTAGAAAATCCGCTTAAAATTGCCACTATCTTTTCTTTTGCCGCTAATGAAGAACAAGACGCGGTAGGCGATATTACCGATGAAAGTTTTGAAGTGGAAGCCATGAATTCGAGCGCCAAAGAATTCTTAAAATCTGCTATTGATGACTACAACAAGTATTTTGCAACCAACTATGATGTAGATGGAAAATCCTTCCAAAATTATTATCGAGATTTGGCAAAACGGGTAAAAAATAAAGAAATTGACCTGCTTATTGTTGTCGGTATGTTTTTAACCGGGTTTGATGCGCCAACGCTAAACACCTTGTTTGTCGATAAAAATCTACGTTATCACGGGTTAATTCAAGCTTTTTCCCGCACCAATCGAATTTATAATGCGACCAAAACCTTTGGCAATATCGTTACTTTCCGCGATTTGGAGCAAAACACCATTGATGCCATTACGCTTTTTGGCAACGCCAATACGCGTAACGTAGTACTGGAAAAAAGCTATCAAGAATATATGGAAGGCTATACCGATGCAGGCATCGATCGCCGCGGCTATTTAGACGTCATTACCGAACTCAGCGATCGTTTTCCTGATCCAACTGAAATTGAAACGGAAAAAGGCAAAAAAGCCTTTGTTAAATTATTCGGTGAATATTTACGCGTTGAAAATATCCTGCAAAATTATGATGAATTTTCCGCTTTGCAGGCATTTCAATCCGTTGATAAAACTGATGAACAAGCAATACAAGCATTTAAAGAAAAGTATTATCTTAGCGATGAAGCCCTTGCTGAAATACAAAAAATTGATATACCAAGCGAACGCGCTATTCAAAATTATCGATCTACTTATAATGACATTCGTGATTGGCTTCGCCGGCAAAAAGATGGCGAAGAAAAAGGCAAATCAACCATTGATTGGGATGATGTAGTCTTTGAGGTGGATTTATTAAAATCCCAAGAAATCAATCTGGATTATATTTTAGAGCTGATTTTTGAGCACAATAAAAAAACCAAAGACAAAGAAACCTTGGTTGAAGAAATTCGTTCAATTATCCGCTCAAGTTTGGGAAACCGCGCCAAAGAAAGTTTAATCATCGATTTTATTCATCAAACAGATTTAGATGCTATTGCCGACAAGGCAAGTATCATTGAAGCGTTCTTTAAATTTGCTCAAACAGAGCAACAAAAAGAGGCTAATGAACTCATTGCTTCGGAAAACTTAAACATAGAAGCGGCTAAACGTTATATTAGTGTTTCATTAAAACGCGAGTACGCCAGCGAAAACGGCACGGATTTAAATGAAGCCCTGCCTAAGATGAGTCCGCTCAATCCGGAATATCTGAAGAAAAAGAAAAGTATTTTCCAAAAAATTGCGGAATTTGTTGAGAAATTTAAGGGCATCGGTGGAAGTATC","","","58648","LNNFKQKTHRFNAGNQGFNAMFAVSSVEAAKFYYEAFKKQQSAVENPLKIATIFSFAANEEQDAVGDITDESFEVEAMNSSAKEFLKSAIDDYNKYFATNYDVDGKSFQNYYRDLAKRVKNKEIDLLIVVGMFLTGFDAPTLNTLFVDKNLRYHGLIQAFSRTNRIYNATKTFGNIVTFRDLEQNTIDAITLFGNANTRNVVLEKSYQEYMEGYTDAGIDRRGYLDVITELSDRFPDPTEIETEKGKKAFVKLFGEYLRVENILQNYDEFSALQAFQSVDKTDEQAIQAFKEKYYLSDEALAEIQKIDIPSERAIQNYRSTYNDIRDWLRRQKDGEEKGKSTIDWDDVVFEVDLLKSQEINLDYILELIFEHNKKTKDKETLVEEIRSIIRSSLGNRAKESLIIDFIHQTDLDAIADKASIIEAFFKFAQTEQQKEANELIASENLNIEAAKRYISVSLKREYASENGTDLNEALPKMSPLNPEYLKKKKSIFQKIAEFVEKFKGIGGSI","1109368","[FUNCTION] The ecor124/3 I enzyme recognizes 5'gaan(7)rtcg. subunit R is required for both nuclease and ATPase activities, but not for modification. [CATALYTIC ACTIVITY] Endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphate; ATP is simultaneously hydrolysed. [SUBUNIT] The type I restriction/modification system is composed of three polypeptides R, M and S. [MISCELLANEOUS] Type I restriction and modification enzymes are complex, multifunctional systems which require ATP, s-adenosyl methionine and Mg(2+) as co-factors and, in addition to their endonucleolytic and methylase activities, are potent DNA-dependent ATPases. ","restriction enzyme type I helicase subunit","Cytoplasm","","
noIPR
unintegrated
unintegrated
PD047574\"[309-344]TQ9JZZ7_NEIMB_Q9JZZ7;
tmhmm\"[126-146]?transmembrane_regions


","BeTs to 14 clades of COG0610COG name: Restriction enzymes type I helicase subunits and related helicasesFunctional Class: LThe phylogenetic pattern of COG0610 is aom-k------l--efghsnuj---wNumber of proteins in this genome belonging to this COG is","","Residues 156 to 369 match (2e-07) PD:PD041105 which is described as PLASMID RESTRICTION TYPE SUBUNIT IC DEOXYRIBONUCLEASE HSDR COMPLETE PROTEOME SITE-SPECIFIC ","","","","","","","","","","","Tue Jan 28 15:11:46 2003","Mon Jan 6 13:16:38 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01640 is paralogously related to AA01477 (1e-05).","","","","","","","","","","","Price,C., Lingner,J., Bickle,T.A., Firman,K. and Glover,S.W. Basis for changes in DNA recognition by the EcoR124 and EcoR124/3 type I DNA restriction and modification enzymes. J. Mol. Biol. 205 (1): 115-125 (1989) PubMed: .","","Tue Jan 28 15:09:23 2003","1","","","" "AA01641","1110959","1111096","138","GTGCGGTTAGTTTTTTCCGTGTTTTTAGCCGGTGATTGGTTGTACCTGTTTTTCATCAGCGCAAAAAATAAACGTGATTTATTTAGTATTTTGCATTCAATGGCATATAATCCTGAGCAATCAATGATGATTAATTTA","","","5410","VRLVFSVFLAGDWLYLFFISAKNKRDLFSILHSMAYNPEQSMMINL","1111096","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 15:27:48 2004","Thu Feb 26 15:27:48 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01641 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 15:27:48 2004","","","","","","","","","","","","","1","","","" "AA01642","1111110","1112135","1026","ATGCAAAAATGGTTTAAACGCAGTTTAGGTTTGGTTTGTCTTTCGCCTTTTTTCTTCGCCCAGCAGGCACAGGCGGAAGGGCGCTTGACGGTGTATTGCACGGTGCAAAATAAAGTGTGTGAAAAAGTGACGCAGGATTTCGGCGCGAAATACAACGTGGAAACGCAATTCGTACACGGCGGCACGGAAACCATTTTTGGCAAGATCAAAGCGGAAAAAGACAATCCGCAGGCGGATTTTTGGTATGGCGGAACTATCGAACCACATTTTCAGGCGGGGGAATTAGGTTTATTGGAAGCCTACCGTTCTCCGAAACAGGCGGAAATCCTACCGCAGTTTAAAACCTTGATGGCAGAAAAAGGCGAGTTTACGTCCGTGGCGTATATGCTGGTGTTAGGTTTCGGCGTGAATACGCAAAAATTAGCCCAACTCGGTTTGCCGACACCGCAAACCTGGGAAGATTTGTTAAAGCCGGAATACAAAGGCGAGGTTCAACTGCCGGATCCGCGCGCTTCCGGCACTACTTATACAATTATGGCGACTTTAATTCAGCTTTGGGGCGAAGAAAAAGCTTTTGATTACCTCAAAAAACTCAATGAAAACGTGTCGCAATATGTGAAAAGCAATTTGGTGACGGCGAATTTATCCCGTGGCGAAACGGCGATCAGTATTGGATTCGTGCATTCTTACGCCACGGAAAAAGAAAAAGGCGCGCCGGTAGAGGCGGTGATTCCGCAAGGCAAAACGGGTTACGCCTTGGGCGGTGCGAGCATCATCAAAGGTGCGCGTAATTTGGATAACGCCAAACTGTTCATGGATTATGTGCTTTCCAAAGAGGTGGAAGAAATTCCGTGGCGTGAATTCGGTTTGTATCAAATTCCGACAAACGTGAACGCTGAAGCCTCACCGAAATCTGTTAATCCGAAAACCTTACAATTACTGGATTTTGATTTTGTGAAATTCGGTTCCAGCGAAGAAGGCAAACGCTTGATTAATAAATGGTTGGCGGAAATTAAATTGGCGAAA","","","38407","MQKWFKRSLGLVCLSPFFFAQQAQAEGRLTVYCTVQNKVCEKVTQDFGAKYNVETQFVHGGTETIFGKIKAEKDNPQADFWYGGTIEPHFQAGELGLLEAYRSPKQAEILPQFKTLMAEKGEFTSVAYMLVLGFGVNTQKLAQLGLPTPQTWEDLLKPEYKGEVQLPDPRASGTTYTIMATLIQLWGEEKAFDYLKKLNENVSQYVKSNLVTANLSRGETAISIGFVHSYATEKEKGAPVEAVIPQGKTGYALGGASIIKGARNLDNAKLFMDYVLSKEVEEIPWREFGLYQIPTNVNAEASPKSVNPKTLQLLDFDFVKFGSSEEGKRLINKWLAEIKLAK","1112133","","possible iron(III) ABC transporter","Periplasm, Cytoplasm","","
InterPro
IPR006059
Family
Bacterial extracellular solute-binding protein, family 1
PF01547\"[5-282]TSBP_bac_1
InterPro
IPR011587
Domain
Prokaryotic extracellular metal-binding protein
PD008688\"[218-283]TQ8U777_AGRT5_Q8U777;
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[28-303]Tno description
signalp\"[1-25]?signal-peptide


","BeTs to 14 clades of COG1840COG name: ABC-type iron/thiamine transport systems, periplasmic componentFunctional Class: HThe phylogenetic pattern of COG1840 is -o--kz---d-lbcefghsnuj--t-Number of proteins in this genome belonging to this COG is","","Residues 120 to 158 match (9e-08) PD:PD583936 which is described as PROTEOME AFUA COMPLETE ABC IRON-COMPOUND-BINDING IRONIII PERIPLASMIC TRANSPORTER ","","","","","","","","","","","","Tue Mar 16 09:42:19 2004","","","","Tue Mar 16 09:42:19 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01642 is paralogously related to AA00696 (1e-102), AA00698 (1e-101), AA01048 (3e-14), AA01479 (2e-10), AA02286 (5e-10), AA02721 (1e-06) and AA02285 (4e-04).","Tue Mar 16 09:42:19 2004","","","","","Residues 5 to 282 (E-value = 4.9e-07) place AA01642 in the SBP_bac_1 family which is described as Bacterial extracellular solute-binding protein (PF01547)","Tue Mar 16 09:42:19 2004","",""," James D, Shao H, Lamont RJ, Demuth DR.,The Actinobacillus actinomycetemcomitans ribose binding protein RbsB interacts with cognate and heterologous autoinducer 2 signals.Infect Immun. 2006 Jul;74(7):4021-9.PMID: 16790775Willemsen PT, Vulto I, Boxem M, de Graaff J.Characterization of a periplasmic protein involved in iron utilization of Actinobacillus actinomycetemcomitans.J Bacteriol. 1997 Aug;179(15):4949-52.PMID: 9244288","Chin N, Frey J, Chang CF, Chang YF. Identification of a locus involved in the utilization of iron by Actinobacillus pleuropneumoniae. FEMS Microbiol Lett. 1996 Sep 15;143(1):1-6. PMID: 8807793","Tue Feb 11 14:57:15 2003","Tue Feb 11 14:57:15 2003","1","","","" "AA01644","1112190","1114220","2031","ATGCTAAAAAAACAATTTCGTCACAACCTCACCTGGATTTTGCTTGCATTTACGGCATTTGCGCTATTGCCTGTGCGAGCTTTGGATTACGGCATTTTCGGCGCCACCCGCAGCGAATATTTCGCGGCGCTGGGCTGGGTTCAACCGAATATCAGCTGGCTGTGGTTTGCGGCGTTATTGTTTTTCCCTTTTCTTTCCCGCAGTGCCTTCGGGCGACCTAAAATTACTTTATTTTTAGCCGTTTCACTCGGTGTCTTCATTTGGTTTTCCGCCGAATTTTTCCGTTTTCGTTTTGGCTACGCCGTTATTTTTCTGACATTGGCGCTAGGCGCCATTTTGGTGGATGCCTTGGCACGCCTGCGATTTATGCAGGTCGATCGTTTTTTATTAAGTGTCGCCTTGGGGCTATCTTGTTTAGTCATCGGTTTTATTTTTTATCCCATCGGCAAATTGTTCGCTGTCTTTTTTTGCGCAGAGCAGAGTGATTGGCAGAATATCTCTGCCTTAATGGCGAACGCCGGCTTGTGGCAGGTGGTGGGGAATTCTTTGGCGGTGTCTGCTTCCGTGGGTGTTTTTTCCGTCGTCTTCGGCTTGATTTTCGCCCTTTATACCACCCGTATCGCTAAACGCAGTGTATGGATCAGCAAACTCTTTTCGATTTTACCCATGATTACGCCGCCCTTTGTGGTGAGCCTCGGCGTGATGCTCATGTTCGGACGCAACGGTTCCGTCACACTGTTTTTAACGCAACATTTCGGTATTACGGCAAATTGGCTGTACGGCTTCAACGGCATTTTAATTTCCCACACGCTGGCGCTCACGCCCATGGCATTTATGCTTATTGAAGGCGCGTTAAAAGCCTTGTCGCCCAAACTGGAAGAAGCGGGCGTGATGTTAGGGGCAAACCGTTGGCAAAGTTTCCGTTTTATTGTATTGCCGCTACTCAAACAGGCGTTAGCCAATGCGTTTTTGATCGTGATGGTGCAATCGCTGGCGGATTTCAGCGCTCCCTTCGTGCTGGGGGGCAATTTTGATGTGTTGGCAACGCAGATTTATTTTTATATTGTCGGCGCACAAAATGATTATTTAGCCGCCAGCACCCTGGGCGTGATTTTGCTTGCTATCTCGTTGAGCATATTCTGGCTGCAATACCGTTTTATCGGCAGCCAAAACTATGTCACGGTATCGGGCAAATCTTTTGAAGGGCGGGTAACGCCGCTGGCTACCGGTTTGAACGTGTTGGTGACGACGGTTTTTATCCTTTGGGTGGGCTTTAACGGTATTTTGTACGGTAGCATTTTTTACGGCAGTTTCATGCAAAGCTGGGGCATTAATAATCAATTTACCTTTCAGCATTACATCACCTTATTCGGACAAGGCTGGAACAGCGGCGCCATTCCGTCTTTAGTGCAAACCGTATTATTCGCGTTAATTGCCGCACCCTTTACCGCCATCAGCGGTTTTCTGTTAGCCTATTTTTTCGCCCGTCGGCATTTTTTCGGCAAAAAATACGCGGAATTTTTCACTTTATTAAGTTTTGCCGTGCCCGGCACGGTGGCGGGTGTTTCTTACATTCTGGCGTTTAATAACGTGCCATTGTATTTGACCGGCACCGGCGTCATCATTGTGCTTTCCATGATTACGCGCAATATGCCTATCGGCTTGCGTGCGGCGTTAGTGAATTTCAAACAGTTGGATCCGACTTTGGATGAAGCGGGTTATACGCTAAAAGCGAGCAGTTTTCAGGTATTACGCTTTATTATTCTGCCTTTATCAAAACCGGCGTTATTATCCGCCTTGGTGACCGGTTTCGTGCGCGCCATGACCACCATCAGCGCCATTATTTTCTTAGTCACACCAAGCACCCGCGTTGCCACGTCTTATATTTTAAATCGCGTGGAAGACGGCGATTACGGACTTGCGGTGGCATACGGCGCAACCCTCATTGTGGTGATGATGCTGGTGATTGGATTATTCGGGCGCTGGGTCGGCGATCTCAATTTGCAGAGAAAACAACATGACAGAACAGAT","","","74860","MLKKQFRHNLTWILLAFTAFALLPVRALDYGIFGATRSEYFAALGWVQPNISWLWFAALLFFPFLSRSAFGRPKITLFLAVSLGVFIWFSAEFFRFRFGYAVIFLTLALGAILVDALARLRFMQVDRFLLSVALGLSCLVIGFIFYPIGKLFAVFFCAEQSDWQNISALMANAGLWQVVGNSLAVSASVGVFSVVFGLIFALYTTRIAKRSVWISKLFSILPMITPPFVVSLGVMLMFGRNGSVTLFLTQHFGITANWLYGFNGILISHTLALTPMAFMLIEGALKALSPKLEEAGVMLGANRWQSFRFIVLPLLKQALANAFLIVMVQSLADFSAPFVLGGNFDVLATQIYFYIVGAQNDYLAASTLGVILLAISLSIFWLQYRFIGSQNYVTVSGKSFEGRVTPLATGLNVLVTTVFILWVGFNGILYGSIFYGSFMQSWGINNQFTFQHYITLFGQGWNSGAIPSLVQTVLFALIAAPFTAISGFLLAYFFARRHFFGKKYAEFFTLLSFAVPGTVAGVSYILAFNNVPLYLTGTGVIIVLSMITRNMPIGLRAALVNFKQLDPTLDEAGYTLKASSFQVLRFIILPLSKPALLSALVTGFVRAMTTISAIIFLVTPSTRVATSYILNRVEDGDYGLAVAYGATLIVVMMLVIGLFGRWVGDLNLQRKQHDRTD","1114218","[FUNCTION] Part of the binding-protein-dependent transport system for iron; probably responsible for the translocation of the substrate across the membrane. [SUBCELLULAR LOCATION] Integral membrane protein. inner membrane (potential). [SIMILARITY] Belongs to the binding-protein-dependent transportsystem permease family. ","ferric transport system permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR000515
Family
Binding-protein-dependent transport systems inner membrane component
PF00528\"[175-392]T\"[465-673]TBPD_transp_1
PS50928\"[179-383]T\"[469-659]TABC_TM1
InterPro
IPR002198
Family
Short-chain dehydrogenase/reductase SDR
PS00061\"[133-161]?ADH_SHORT
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[147-294]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-27]?signal-peptide
tmhmm\"[10-28]?\"[47-65]?\"[70-90]?\"[96-118]?\"[128-148]?\"[183-203]?\"[218-240]?\"[259-281]?\"[312-332]?\"[362-382]?\"[418-438]?\"[472-492]?\"[507-527]?\"[531-553]?\"[574-594]?\"[600-618]?\"[639-659]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 5.4e-08) to 1/1 blocks of the IPB000515 family, which is described as \"Binding-protein-dependent transport systems inner membrane component\". Interpro entry for IP:IPR000515. IPB000515 294-313 5.5e-08 IPB000515 571-590 0.0014","Residues 601 to 672 match (2e-16) PD:PD015756 which is described as COMPLETE PROTEOME PERMEASE ABC TRANSPORTER TRANSMEMBRANE SYSTEM MEMBRANE TRANSPORTER INNER ","","","","","","","","","","","Mon Jan 6 13:29:17 2003","Mon Jan 6 13:29:17 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01644 is paralogously related to AA00699 (0.0), AA01050 (2e-23), AA01780 (5e-17), AA01650 (2e-14), AA01950 (1e-11), AA02720 (3e-10), AA02719 (3e-10), AA01866 (4e-10), AA01948 (5e-10), AA01682 (1e-09), AA01649 (6e-07) and AA00416 (8e-05).","","","","","","Residues 465 to 673 (E-value = 8e-10) place AA01644 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component (PF00528)","","",""," James D, Shao H, Lamont RJ, Demuth DR.,The Actinobacillus actinomycetemcomitans ribose binding protein RbsB interacts with cognate and heterologous autoinducer 2 signals.Infect Immun. 2006 Jul;74(7):4021-9.PMID: 16790775","Dugourd,D., Martin,C., Rioux,C.R., Jacques,M. and Harel,J. Characterization of a periplasmic ATP-binding cassette iron import system of Brachyspira (Serpulina) hyodysenteriae. J. Bacteriol. 181 (22): 6948-6957 (1999) [PubMed: 10559160].","","Mon Jan 6 13:29:17 2003","1","","","" "AA01645","1114156","1115244","1089","TTGGATTATTCGGGCGCTGGGTCGGCGATCTCAATTTGCAGAGAAAACAACATGACAGAACAGATTGAATTAAAACACATCTATAAATCCTTCGGGCAAACCAAGGTGTTGCAGGATTTCAATTTATCTTTTCAAAAGCATAAATTCACCACTTTGCTTGGTGCCTCCGGCTGTGGCAAAACCACCATTTTGCGTCTGATTGCGGGGCTAGAAGAGCCGGATAAAGGGCAGATTTTGTGCGACGGACGGGATCTCAGTCGGCTTGCTCCGCAACAACGTGGCGTGGGCTTCGTATTTCAGTCTTATGCCTTATTTCCCCATTTAACGGTGAGTGAAAACGTGGCGTTCGGCTTAAAAATGCAGGATGAAAACGCAACGAACATTGCCGCTAAAGTGAGGAATGCGTTGAAAATGGTGGAGTTGGACGGTTTTGAAACGCGTCGTATTGAGCAGCTTTCCGGCGGGCAACAACAGCGGGTGGCGCTTGCCCGTGCCTTGGTTATCGCGCCGCAGATTTTATTGTTTGATGAGCCTTTGAGCAACCTGGATACCAATTTACGCCGCACATTACGCGAAATGATTCGTCATTTACAGCAACAACTGAATATCACTACCTTATATGTCACCCACGATCAAAGCGAAGCCTTTGCCATTTCTGATGAAGTGGTGGTGATGAATCAAGGCAAAGTGGAACAAATCGGCACCCTAAGCGAGCTCTACCGCGCGCCGACCTCCCGCTTCACGGCGACCTTCATGGGCGATGCCTCATTCTTTCCCGTGCAATCAAAAAACGGCAAATTATTCATGGATAAAAATCCATTATCATTAGTCTCTCAAACAGGGGCGACGGATGGCAATTATCAGCTGGGCATTCGCCCGGAAGGGGTGTTGCTTGGTTTGCAAGGTGAGTCGGCTGCACAATGCACGATTCAGTCGGCGGTATTCATGGGAAATTACTGGGAAATTCGCGCCTTATGGCAGGGCTTGCCGCTATTGATTCACCTTAACCCGAACGATTACATTCCGAACCAACCGCGTTATTTCGTGCAACTACGCCCCATAGGCTGGTTTTTGCTGCCGGCAGAAGGG","","","40487","LDYSGAGSAISICRENNMTEQIELKHIYKSFGQTKVLQDFNLSFQKHKFTTLLGASGCGKTTILRLIAGLEEPDKGQILCDGRDLSRLAPQQRGVGFVFQSYALFPHLTVSENVAFGLKMQDENATNIAAKVRNALKMVELDGFETRRIEQLSGGQQQRVALARALVIAPQILLFDEPLSNLDTNLRRTLREMIRHLQQQLNITTLYVTHDQSEAFAISDEVVVMNQGKVEQIGTLSELYRAPTSRFTATFMGDASFFPVQSKNGKLFMDKNPLSLVSQTGATDGNYQLGIRPEGVLLGLQGESAAQCTIQSAVFMGNYWEIRALWQGLPLLIHLNPNDYIPNQPRYFVQLRPIGWFLLPAEG","1115242","[FUNCTION] Part of the binding-protein-dependent transport system for iron. probably responsible for energy coupling to the transport system. [MISCELLANEOUS] In E.coli, the afu system seems to have been deleted by an insertion sequence. afua is totally lost, afuB is partially present and afuC is totally conserved. [SIMILARITY] Belongs to the ABC transporter family. ","ferric transport ABC-related ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[151-194]TQ9KLQ5_VIBCH_Q9KLQ5;
PF00005\"[47-228]TABC_tran
PS50893\"[22-252]TABC_TRANSPORTER_2
PS00211\"[152-166]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[46-229]TAAA
InterPro
IPR013611
Domain
Transport-associated OB
PF08402\"[289-359]TTOBE_2
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[19-255]Tno description
PTHR19222\"[22-269]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF44\"[22-269]TSULFATE-TRANSPORTING ATPASE


","BeTs to 3 clades of COG3841COG name: ABC-type iron transport systems, ATPase componentsFunctional Class: PThe phylogenetic pattern of COG3841 is ------------b-efgh-n----t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.8e-36) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 36-82 4.6e-18 IPB001140B 149-187 1.2e-14 IPB001140C 205-234 0.83","Residues 103 to 246 match (2e-07) PD:PD387048 which is described as ATP-BINDING 250AA PROTEOME COMPLETE III DICITRATE IRON LONG ","","","","","Mon Feb 17 08:18:13 2003","","","","","","Mon Jan 6 13:33:33 2003","Mon Feb 17 08:18:13 2003","","","Tue Mar 16 09:38:40 2004","Tue Mar 16 09:38:28 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01645 is paralogously related to AA00700 (5e-98), AA02718 (7e-65), AA01656 (2e-59), AA01051 (4e-48), AA01947 (2e-47), AA00415 (8e-35), AA02353 (1e-34), AA00858 (8e-34), AA02324 (9e-33), AA01867 (1e-31), AA02440 (3e-31), AA01779 (3e-31), AA01616 (2e-29), AA02899 (5e-29), AA01524 (2e-28), AA01684 (5e-27), AA01824 (1e-26), AA02080 (1e-25), AA01422 (4e-25), AA00933 (6e-25), AA01820 (6e-24), AA00799 (6e-24), AA02805 (1e-22), AA02320 (7e-22), AA02140 (2e-21), AA01568 (2e-21), AA02152 (4e-21), AA01456 (4e-20), AA00751 (2e-19), AA02898 (6e-19), AA01393 (6e-19), AA01961 (8e-19), AA01509 (8e-19), AA02331 (2e-18), AA00207 (7e-18), AA02786 (4e-17), AA01510 (4e-17), AA02606 (1e-16), AA02573 (2e-16), AA02484 (3e-15), AA02642 (2e-14), AA02225 (2e-14), AA01757 (3e-14), AA02550 (3e-14), AA00591 (5e-12), AA00061 (7e-12), AA02609 (1e-11), AA00934 (1e-10), AA01555 (1e-07), AA02146 (2e-07), A02145 (2e-06), AA02226 (3e-06), AA01569 (3e-06) and AA01291 (4e-05).","Tue Mar 16 09:38:28 2004","","","","","Residues 47 to 228 (E-value = 7.9e-66) place AA01645 in the ABC_tran family which is described as ABC transporter (PF00005)","Tue Mar 16 09:38:28 2004","",""," James D, Shao H, Lamont RJ, Demuth DR.,The Actinobacillus actinomycetemcomitans ribose binding protein RbsB interacts with cognate and heterologous autoinducer 2 signals.Infect Immun. 2006 Jul;74(7):4021-9.PMID: 16790775","Volkert MR, Loewen PC, Switala J, Crowley D, Conley M.The delta (argF-lacZ)205(U169) deletion greatly enhances resistance to hydrogen peroxide in stationary-phase Escherichia coli.J Bacteriol. 1994 Mar;176(5):1297-302.PMID: 8113168Furuchi T, Kashiwagi K, Kobayashi H, Igarashi K.Characteristics of the gene for a spermidine and putrescine transport system that maps at 15 min on the Escherichia coli chromosome.J Biol Chem. 1991 Nov;266(31):20928-33.PMID: 1939142Kashiwagi K, Innami A, Zenda R, Tomitori H, Igarashi K.The ATPase activity and the functional domain of PotA, a component of the sermidine-preferential uptake system in Escherichia coli.J Biol Chem. 2002 Jul;277(27):24212-9.PMID: 11976340","","Tue Mar 16 09:38:40 2004","1","","","" "AA01646","1115322","1115209","114","TTGGGCAGGAGAGTAAGATTACTGCAAAAAGTGCGGTCATTTCAAAAAACGTTTTTTAAATCGACCGCACTTTTTTTACCCTTCTGCCGGCAGCAAAAACCAGCCTATGGGGCG","","","4470","LGRRVRLLQKVRSFQKTFFKSTALFLPFCRQQKPAYGA","1115209","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 15:25:56 2004","Thu Feb 26 15:25:56 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01646 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 15:25:56 2004","","","","","","","","","","","","","1","","","" "AA01648","1117358","1115310","2049","ATGCAAAAATCCATTCTCTATTTTTCTCTGTTCTGCGCCGGCAATACCTTTGCCGCGTGGCAGCATCCGCAGTTTAACGAACTGAACGACAACGCCGAAAAGCAACTCTTCCAAGGGCAGGCAACGCTGGACAAAGGCAATTATTCGTTACAATTCCAACGCGACGGCAAATGCTTCCAGCCTCAAACTGCCGTGAAACTCAATCAAACCGCCTCCCTCGAACCTTGCCACGGCGACGCGCCGCAATTACGTATTTTCCGTCACGGCAATTATCTCGCCCAAATCGACACCCGCAGCGGCACGCCGACTTTACGTATCAGCATTGAACGACAGCCGGAACCGGAAGCCGTAGCAAAAACTTGTCCGAAGTGGGATCAGAAACCGTTGGAAATTGACGTGAGCCAAACCTTCGCCGAGGGCGATACCGTGCGCGATGCTTATTCGGGCAAAAGTGCGGTGGTGAAAAACGGTAAAGTGACCTTGACGCCGGATCCGCTGGCGGGCGGATTGCTGCTCTTGGAAAAAAGTGCGGTTAAAAATCCAAGTGTTTTTCACTGGAAAAACGCCACCGTCTATTTTGTGTTGACCGATCGCTTTCATAACGGCAACCCGCACAACGATCACAGCTACGGACGACAAAAAGACGGTATGCAGGAAATCGGTACGTTCCATGGTGGCGATTTAAAAGGCTTAACGGAAAAACTGGATTACCTGCAACAGCTCGGCGTGAACGTCATCTGGATTTCCTCGCCACTAGAACAAATGCACGGCTGGGTCGGCGGTGGGGATAAAGGCGATTTTCCGCATTACGCCTATCACGGCTATTATCATCAGGACTGGACGAAAATTGACGCCAACATGGGGACGGAGCAAGATCTCAGCCATTTCATTGAGCAAGCCCATAAACGCGGCATGAAAGTGATTTTCGACGTGGTGATGAATCACACCGGCTACGCTACTCTTGCGGATATGCAGGAATTCGGTTTCGGTTCGTTTTACCTGAAACCGGAAGAAATGCAATCCGTATTAGGTGAAAAATGGACGAACTGGAAACCGAAACGCGGTCAGAATTGGCATAGTTTTAACGACTACATCAATTTCGGCGATAGCGTCAGCTGGGCGAAATGGTGGGGTAAGGATTGGGTGCGATCCGACATTGGCGATTACGACAGCCCGAAATTCGACGATCTGAAAATGTCCCTCGCTTCATTGCCCGATCTCAAAACCGAAAGCGATAATGCAGTGGGTTTGCCGCCTTTTTATCACCACAAACAAACCCATGCCAAAGCTCTGCAAAATGCCAAAGTGCGTGATTATCTCATCGGCTGGTTGTCTGATTGGGTGCGTAACTACGGCGTAGACGGCTTTCGCGTGGATACCGCCAAACACGTTGAAAAATCCACTTGGCTGGCATTAAAACAATCGGCGGACGCGGCATTACACCAGTGGCAGCAAAAACATCCTTCCGAGAGCAGCGGTGAACCCTTTTGGATGACGGGTGAAGCCTGGGGACACGGCGTGCTGAAAAGCGATTACTACCAAAACGGCTTCGACGCCATGATCAATTTCGACTTTCAGGACCAAGCAAAAAATGCGTTGGATTGTTTCGCCCACATTGATCCCGTGTATCAGAACATGAGCGACAAACTGAAAGATTTCAATGTGTTGAGTTACCTTTCCTCCCACGATACCCGTTTTTTCTATCATTCGGATAGCCAAGGCAACAACGCGAAACAAAAAATCGCCGCTAACCTGTTATTACTGGCGCCGGGCGCTGTACAAATCTATTACGGCGATGAAAGCGGACGGGACTTTGGACCCACCGGTTCCGACCCGATGCAAGGCACGCGTTCCGATATGAATTGGCAGGACCTCGGCACAAACGGCGACAAACAAGCCCTGCTCACCCACTGGCAAACACTCGCCCGCTTCCGCCAAGCGCATCCGGCAATCGGCGCAGGTAAACAAACCACTGCGAAAACGGAGAAATATTACGCCTTTAGCCGTGAATTGGACGGCGATAAAGTGATGGTCGTTTGGGCAGGAGAG","","","78318","MQKSILYFSLFCAGNTFAAWQHPQFNELNDNAEKQLFQGQATLDKGNYSLQFQRDGKCFQPQTAVKLNQTASLEPCHGDAPQLRIFRHGNYLAQIDTRSGTPTLRISIERQPEPEAVAKTCPKWDQKPLEIDVSQTFAEGDTVRDAYSGKSAVVKNGKVTLTPDPLAGGLLLLEKSAVKNPSVFHWKNATVYFVLTDRFHNGNPHNDHSYGRQKDGMQEIGTFHGGDLKGLTEKLDYLQQLGVNVIWISSPLEQMHGWVGGGDKGDFPHYAYHGYYHQDWTKIDANMGTEQDLSHFIEQAHKRGMKVIFDVVMNHTGYATLADMQEFGFGSFYLKPEEMQSVLGEKWTNWKPKRGQNWHSFNDYINFGDSVSWAKWWGKDWVRSDIGDYDSPKFDDLKMSLASLPDLKTESDNAVGLPPFYHHKQTHAKALQNAKVRDYLIGWLSDWVRNYGVDGFRVDTAKHVEKSTWLALKQSADAALHQWQQKHPSESSGEPFWMTGEAWGHGVLKSDYYQNGFDAMINFDFQDQAKNALDCFAHIDPVYQNMSDKLKDFNVLSYLSSHDTRFFYHSDSQGNNAKQKIAANLLLLAPGAVQIYYGDESGRDFGPTGSDPMQGTRSDMNWQDLGTNGDKQALLTHWQTLARFRQAHPAIGAGKQTTAKTEKYYAFSRELDGDKVMVVWAGE","1115308","MalS has also been assigned as a gene name to malate dehydrogenase.[FUNCTION] Since only maltooligosaccharides up to a chain length of 6 glucose units are actively transported through thecytoplasmic membrane via the membrane-bound complex of three proteins, malF, malG, and malK, longer maltooligosaccharides must first be degraded by the periplasmic alpha-amylase, the malS protein. [CATALYTIC ACTIVITY] Endohydrolysis of 1,4-alpha-glucosidic linkages in oligosaccharides and polysaccharides. [SUBUNIT] Monomer.[SUBCELLULAR LOCATION] Periplasmic. [INDUCTION] Under the regulatory control of the malT protein. [SIMILARITY] Belongs to family 13 of glycosyl hydrolases, also known as the alpha-amylase family","alpha-amylase protein; 1,4-alpha-D-glucan glucanohydrolase","Periplasm, Extracellular","","
InterPro
IPR006047
Domain
Glycosyl hydrolase, family 13, catalytic region
PF00128\"[193-645]TAlpha-amylase
InterPro
IPR006589
Domain
Glycosyl hydrolase, family 13, subfamily, catalytic region
SM00642\"[193-645]TAamy
InterPro
IPR013781
Domain
Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80\"[181-654]Tno description
noIPR
unintegrated
unintegrated
PTHR10357\"[186-202]T\"[221-255]T\"[272-377]T\"[449-680]TAMYLASE
PTHR10357:SF11\"[186-202]T\"[221-255]T\"[272-377]T\"[449-680]TALPHA-AMYLASE
signalp\"[1-18]?signal-peptide


","BeTs to 10 clades of COG0366COG name: GlycosidasesFunctional Class: GThe phylogenetic pattern of COG0366 is ---p--y-vdrlbcefg----j----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-08) to 3/5 blocks of the PR00110 family, which is described as \"Alpha-amylase signature\". Prints database entry for PR:PR00110. PR00110B 304-315 0.038 PR00110C 453-464 0.00027 PR00110D 497-515 2.6e+02","Residues 192 to 253 match (3e-07) PD:PD303886 which is described as HYDROLASE COMPLETE PROTEOME GLYCOSIDASE CYCLOMALTODEXTRINASE GLUCANOHYDROLASE 14-ALPHA-D-GLUCAN ALPHA-AMYLASE NEOPULLULANASE PULLULANASE ","","","","","Wed Feb 19 16:33:47 2003","","","","Wed Feb 19 16:33:47 2003","","Thu Feb 13 17:13:47 2003","Mon Jan 6 14:26:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01648 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 193 to 645 (E-value = 2.1e-81) place AA01648 in the Alpha-amylase family which is described as Alpha amylase, catalytic domain (PF00128)","","","","","Kawazu,T., Nakanishi,Y., Uozumi,N., Sasaki,T., Yamagata,H., Tsukagoshi,N. and Udaka,S. Cloning and nucleotide sequence of the gene coding for enzymatically active fragments of the Bacillus polymyxabeta-amylase. J. Bacteriol. 169 (4): 1564-1570 (1987) [PubMed: 2435707].Uozumi,N., Sakurai,K., Sasaki,T., Takekawa,S., Yamagata,H., Tsukagoshi,N. and Udaka,S. A single gene directs synthesis of a precursor protein with beta- and alpha-amylase activities in Bacillus polymyxa. J. Bacteriol. 171 (1): 375-382 (1989) [PubMed: 2464578].Rhodes,C., Strasser,J. and Friedberg,F. Sequence of an active fragment of B. polymyxa beta amylase. Nucleic Acids Res. 15 (9): 3934 (1987) [PubMed: 2438660].Uozumi,N., Matsuda,T., Tsukagoshi,N. and Udaka,S. Structural and functional roles of cysteine residues of Bacillus polymyxa beta-amylase. Biochemistry 30 (18): 4594-4599 (1991) [PubMed: 1827035].Jones CH, Dexter P, Evans AK, Liu C, Hultgren SJ, Hruby DE.Escherichia coli DegP protease cleaves between paired hydrophobic residues in a naturalsubstrate: the PapA pilin.J Bacteriol. 2002 Oct;184(20):5762-71.PMID: 12270835","","Thu Feb 13 17:13:47 2003","1","","","" "AA01649","1118343","1117456","888","ATGGCTATCGTACAATCCAAATCTGCCCGCTACCGTTTATGGGTGACCCATTTGCTGCTGATTGCATTTATTTGTCTGATTATTTTCCCGTTACTGATGGTGATCGGCATTTCCCTGCGCCCGGGCAACCTCGCTTTGGGCGATTTGATTCCGAAACAAATTTCCTGGGAACACTGGCAGGCGGCGCTTGGCTTTTATGTGGTACACGCCGACGGTTCTGTCACACCACCGCCGTTCCCGGTGTTGTTGTGGTTGTGGAACTCCATTAAAGTGGCGACCATCACCTCCGTGGGTATCGTTGTTATGTCCACCACTTGCGCCTACGCTTTCGCGCGGATGAAATTCAAAGGCAAAAAAACCATCTTGCAAGGCATGTTAATTTTCCAAATGTTCCCTGCGGTGTTGTCTTTGGTCGCCTTATACGCCTTATTCGATCGCCTCGGTCAATATATCCCGTTCCTCGGCTTAAACACCCACGGCGGCGTGATTTTCGCTTACTTGGGCGGTATCGCCTTGCACGTTTGGACCATCAAAGGCTATTTTGAAACCATCGACGGATCCCTGGAAGAAGCTGCCGCCTTAGACGGCGCTACCCCATGGCAGGCATTCCGCTTAATTTTACTACCTCTCTCCGTACCGATTCTGGCGGTGGTCTTCATTCTTTCCTTCATCGCCGCCATTACCGAAGTGCCGGTCGCCTCGCTATTATTACGCGATGTCAACAGCTACACCCTGGCGGTGGGAATGCAACAATATCTCTACCCGCAAAACTACCTTTGGGGCGACTTCGCCGCTGCAGCGGTGCTTTCCGCTATTCCTATTACCCTCGTGTTCTTACTGGCACAACGCTGGTTAATCGGCGGATTAACGGCAGGTGGGGTGAAGGGG","","","32355","MAIVQSKSARYRLWVTHLLLIAFICLIIFPLLMVIGISLRPGNLALGDLIPKQISWEHWQAALGFYVVHADGSVTPPPFPVLLWLWNSIKVATITSVGIVVMSTTCAYAFARMKFKGKKTILQGMLIFQMFPAVLSLVALYALFDRLGQYIPFLGLNTHGGVIFAYLGGIALHVWTIKGYFETIDGSLEEAAALDGATPWQAFRLILLPLSVPILAVVFILSFIAAITEVPVASLLLRDVNSYTLAVGMQQYLYPQNYLWGDFAAAAVLSAIPITLVFLLAQRWLIGGLTAGGVKG","1117454","[FUNCTION] Part of the binding-protein-dependent transport system for maltose; probably responsible for the translocation of the substrate across the membrane. [SUBCELLULAR LOCATION] Integral membrane protein. inner membrane.[SIMILARITY] Belongs to the binding-protein-dependent transport system permease family. MalfG subfamily. ","maltose ABC transporter, permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR000515
Family
Binding-protein-dependent transport systems inner membrane component
PF00528\"[85-291]TBPD_transp_1
PS50928\"[85-281]TABC_TM1
noIPR
unintegrated
unintegrated
signalp\"[1-36]?signal-peptide
tmhmm\"[15-37]?\"[91-111]?\"[126-144]?\"[154-174]?\"[205-227]?\"[258-280]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 5.6e-10) to 1/1 blocks of the IPB000515 family, which is described as \"Binding-protein-dependent transport systems inner membrane component\". Interpro entry for IP:IPR000515. IPB000515 190-209 5.7e-10","Residues 1 to 100 match (2e-25) PD:PD557258 which is described as MALTOSE COMPLETE MALG PERMEASE PROTEOME TRANSMEMBRANE MEMBRANE INNER SYSTEM SUGAR ","","","","","","","","","","","Mon Jan 6 14:57:18 2003","Mon Jan 6 14:57:18 2003","","","Tue Mar 16 10:11:53 2004","Tue Mar 16 10:11:53 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01649 is paralogously related to AA01780 (8e-14), AA01950 (7e-10), AA02720 (2e-08), AA01650 (6e-08), AA01948 (2e-07), AA01644 (2e-07), AA01050 (1e-06), AA00699 (5e-05) and AA02719 (1e-04).","Tue Mar 16 10:11:53 2004","","","","","Residues 85 to 291 (E-value = 6.7e-14) place AA01649 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component (PF00528)","Tue Mar 16 10:11:53 2004","","","","Dahl MK, Francoz E, Saurin W, Boos W, Manson MD, Hofnung M.Comparison of sequences from the malB regions of Salmonella typhimurium and Enterobacter aerogenes with Escherichia coli K12: a potential new regulatory site in the interoperonic region.Mol Gen Genet. 1989 Aug;218(2):199-207.PMID: 2674653","","Tue Mar 16 10:11:53 2004","1","","","" "AA01650","1119909","1118368","1542","ATGCAACAATCTCCGACTCAAGCGACATCGCAATCCCCGTGGCTGAAATATTTGTTAGCCGGCGTCGTATTGTTGATTGACTTATATTTAGTGGTTTTAATGTATTCGCAGGGAGAATATTTGTTCGCCATTTTAACCTTGGTGATTCTGACTTCCGGCGTGTACATTTTCAGCAGCAAAAAAGTGTACGCATGGCGTTATGTGTATCCCGGCTTAACGGGCATGGCGATTTTTATTTTATTCCCGTTGGTCGCCACCATCGCCATCGCCTTCACCAATTACAGCGGCACCAACCAGCTTTCCTTTGAACGTGCCGTTGCCGTATTAGGCGAACAACGTTACTTCGCCGGTGATAAATACGATTTCAAACTCTACCCGCAACAGGACAACAGCTATATCCTTGCCCTACACAATAACAATACCGGACAGGATTTCGCTTCCGTTCCTATTAAACTCACCGATAAGGAAATCACGGTAACCGAACAAGCCGCACCGCAAAGCGAAGCGGCACCGCTTAAAGTGATTACGCAAAACCGCAGCGCCTTACAAGCCATGCGCGTGACCTTGCCAAGCGGCAATGAATTGACCATGAGTTCATTACGTCAATTTTCCGAACAAAAACCGCGTTACACCTTTAACAGCGAAACCAATACCTTAACCAACAACGAAAACGGCAAAATCTACAAAGCCAACAATGATATCGGCTTTTTCCAAGCGGTTAATGAAACCGGCGAATGGTTAAATGAAACCTTAGAGCCGGGTTATACGGTGTCTGTGGGCTGGCTGAATTTCGTGAAAATCTTCACCGATGAAGGTATCCAAAAACCGTTCATTCAAATTTTTATCTGGACGGTGATTTTCTCCTTACTCACCGTTGTTTTCACCGTTATTCTCGGCATGGTGTTGGCTTGCGTGGTGCAATGGGAAGCGCTGAAAGGCAAAGGCGTATATCGCTTGCTGTTAATCTTGCCGTATGCCGTGCCGTCCTTTATTTCCATCTTGATTTTCAAAGGGTTATTCAACCAAAGTTTCGGGGAAATCAATGTCATTCTGAATCAATTATTCGGCATTAGCCCGGAATGGTTTAACGATCCGTTCCTGGCGAAAACCATGATTCTTATCGTCAATACCTGGTTGGGTTATCCGTACATGATGATTTTGTGCATGGGCTTGTTGAAAGCCATTCCGTCGGATTTATACGAAGCCTCTGCCATGGACGGCGCGTCCACCTGGCAGAACTTCAGCAAAATCACCTTCCCGTTGTTGTTAAAACCGTTAACCCCGTTAATGATTGCGTCCTTCGCCTTTAACTTTAACAACTTCGTGTTGATTCAACTATTAACCAACGGTCGCCCGGACATGATCGGCACCACCACGCCGGCAGGTTACACCGACTTGCTCGTCAGCTACACCTACCGCATCGCCTTTGAAGGCAGCGGCACGCAAGACTTCGGCTTGGCGGCAGCGATTGCCACCATCATCTTCTTGCTCGTAGGCGGCTTGGCATTACTCAACATCAAAGCCACTAAAATGAAATTAGAC","","","57387","MQQSPTQATSQSPWLKYLLAGVVLLIDLYLVVLMYSQGEYLFAILTLVILTSGVYIFSSKKVYAWRYVYPGLTGMAIFILFPLVATIAIAFTNYSGTNQLSFERAVAVLGEQRYFAGDKYDFKLYPQQDNSYILALHNNNTGQDFASVPIKLTDKEITVTEQAAPQSEAAPLKVITQNRSALQAMRVTLPSGNELTMSSLRQFSEQKPRYTFNSETNTLTNNENGKIYKANNDIGFFQAVNETGEWLNETLEPGYTVSVGWLNFVKIFTDEGIQKPFIQIFIWTVIFSLLTVVFTVILGMVLACVVQWEALKGKGVYRLLLILPYAVPSFISILIFKGLFNQSFGEINVILNQLFGISPEWFNDPFLAKTMILIVNTWLGYPYMMILCMGLLKAIPSDLYEASAMDGASTWQNFSKITFPLLLKPLTPLMIASFAFNFNNFVLIQLLTNGRPDMIGTTTPAGYTDLLVSYTYRIAFEGSGTQDFGLAAAIATIIFLLVGGLALLNIKATKMKLD","1118366","[FUNCTION] Part of the binding-protein-dependent transport system for maltose; probably responsible for the translocation of the substrate across the membrane. [SUBCELLULAR LOCATION] integral membrane protein. inner membrane.a substantial portion of it protrudes into the periplasmic space. [SIMILARITY] Belongs to the binding-protein-dependent transport system permease family. MalfG subfamily. ","maltose transport inner membrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR000515
Family
Binding-protein-dependent transport systems inner membrane component
PF00528\"[281-513]TBPD_transp_1
PS50928\"[281-505]TABC_TM1
noIPR
unintegrated
unintegrated
signalp\"[1-38]?signal-peptide
tmhmm\"[15-35]?\"[41-59]?\"[74-94]?\"[286-306]?\"[316-336]?\"[372-392]?\"[421-441]?\"[486-506]?transmembrane_regions


","BeTs to 7 clades of COG3834COG name: ABC-type maltose transport systems, permease componentFunctional Class: GThe phylogenetic pattern of COG3834 is ---pk---vd-lb-e-g---------Number of proteins in this genome belonging to this COG is","Significant hit ( 4.8e-06) to 1/1 blocks of the IPB000515 family, which is described as \"Binding-protein-dependent transport systems inner membrane component\". Interpro entry for IP:IPR000515. IPB000515 401-420 4.9e-06","Residues 339 to 401 match (1e-08) PD:PD557254 which is described as COMPLETE PROTEOME TRANSMEMBRANE PERMEASE MALTODEXTRIN SYSTEM MALC ABC LIN2229 SA0208 ","","","","","","","","","","","Mon Jan 6 15:06:06 2003","Mon Jan 6 15:06:06 2003","","","Tue Mar 16 10:17:48 2004","Tue Mar 16 10:17:28 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01650 is paralogously related to AA01644 (1e-14), AA01948 (2e-10), AA01649 (1e-07), AA02719 (3e-07), AA00699 (5e-07), AA01866 (1e-05), AA01950 (1e-05) and AA01780 (0.001).","Tue Mar 16 10:17:28 2004","","","","","Residues 281 to 513 (E-value = 1.1e-13) place AA01650 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component (PF00528)","Tue Mar 16 10:17:28 2004","","","","Dahl MK, Francoz E, Saurin W, Boos W, Manson MD, Hofnung M.Comparison of sequences from the malB regions of Salmonella typhimurium and Enterobacter aerogenes with Escherichia coli K12: a potential new regulatory site in the interoperonic region.Mol Gen Genet. 1989 Aug;218(2):199-207.PMID: 2674653Froshauer S, Beckwith J.The nucleotide sequence of the gene for malF protein, an inner membrane component of the maltose transport system of Escherichia coli. Repeated DNA sequences are found in the malE-malF intercistronic region.J Biol Chem. 1984 Sep;259(17):10896-903.PMID: 6088520Dassa E, Hofnung M.Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems.EMBO J. 1985 Sep;4(9):2287-93.PMID: 3000770Ehrmann M, Boyd D, Beckwith J.Genetic analysis of membrane protein topology by a sandwich gene fusion approach.Proc Natl Acad Sci U S A. 1990 Oct;87(19):7574-8.PMID: 2170984","","Tue Mar 16 10:17:48 2004","1","","","" "AA01651","1120064","1119936","129","ATGCCCGCGCACGTATCCAAAAACAACAATAAACCAAGCCTGATGTGCCGAGCCGAATTGACGGTTCGGCACATTAACAATTCAAAAAGTGCGGTGCAAATTTTTAGTGTTTTCTATGCCGTAGCCGAT","","","4772","MPAHVSKNNNKPSLMCRAELTVRHINNSKSAVQIFSVFYAVAD","1119936","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 15:24:13 2004","Thu Feb 26 15:24:13 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01651 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 15:24:13 2004","","","","","","","","","","","","","1","","","" "AA01654","1121223","1120036","1188","ATGAAAAACAAACTCGTTAAATTCACTTTAACCGCCGTGGCGGGCTTAGTTATGTCTTCCGCTGTAATGGCAAAAATGACCGAAGGAAAATTGGTTATTTGGATCAACGGCGACAAAGGCTATAACGGCTTGGCTGAAGTGGGTAAAAAATTTGAAAAAGACACCGGCATTTCCGTTTTGGTAGAACATCCGGACAGACTGGAAGAAAAATTTGCTCAAGTGGCGTCCACCGGTGACGGCCCGGACATTATCTTCTGGGCACATGACCGTTTTGGCGGCTATGCGCAAGCGGGTTTATTGACCGAACTTACCCCAAGCAAAGAATTTAAAGATAAATTCGTAGATTTTGCCTGGGATGCGGAAACCTATAACGGCAAAGTCATCGGCTATCCGGTGGCGATTGAATCCCTGTCTTTAATCTACAACAAAGACTTGGTTCCTACCCCGCCGAAATCCTGGGAAGAAATTCTTGAGCTGGATGCCAAACTCAAAAAAGACAAGAAAAACGCCATTATGTGGAACCTGTCCGAGCCGTATTTCACTTGGCCTATCGTCGCTTCTAACGGCGGTTATGCCTTCAAATTTGTCAACGGCAAATATGACATTAACGACATCGGCGTAAACAACGAAGGTTCACAAAAAGCCCTGCAATTCGTGGTGAATATGGTGAAAAATAAAGTCATCAGCGCCGATATGGACTATGCCATCGCGGAAGCGGCATTTAACAAAGGCGATGCGGCGTTAACCATTAATGGTCCTTGGTCTTGGGGCAACATTGAGAAAAGCAAAATCAATTACGGCGTTGCCGTGTTGCCGACCTTAAACGGTCACAATGCCAAACCGTTCGTCGGCGTGTTAAGTGCCGGTATTAACTCCGCCAGCCCGAACAAAGATCTCGCGGTGGAATTCATGGAAAACTACCTGTTGACCGATGACGGTTTGGAAACCGTCAATAAAGACAAACCACTAGGCGCTGTGGCATTGAAATCCTACCAAGAAAAATTAGCGAAAGATCCGCGTATCGCCGCCACCATGGAAAATGCGAAAAACGGTGAAATCATGCCGAATATCGCGCAAATGAGTGCTTTCTGGTATGCCGAAAAAGCGGCAATCGGCAATGCCGTCAGCGGTCGTCAAAGCGTAAAACAAGCCTTGGACGATGCCCGCGCACGTATCCAAAAACAACAA","","","43394","MKNKLVKFTLTAVAGLVMSSAVMAKMTEGKLVIWINGDKGYNGLAEVGKKFEKDTGISVLVEHPDRLEEKFAQVASTGDGPDIIFWAHDRFGGYAQAGLLTELTPSKEFKDKFVDFAWDAETYNGKVIGYPVAIESLSLIYNKDLVPTPPKSWEEILELDAKLKKDKKNAIMWNLSEPYFTWPIVASNGGYAFKFVNGKYDINDIGVNNEGSQKALQFVVNMVKNKVISADMDYAIAEAAFNKGDAALTINGPWSWGNIEKSKINYGVAVLPTLNGHNAKPFVGVLSAGINSASPNKDLAVEFMENYLLTDDGLETVNKDKPLGAVALKSYQEKLAKDPRIAATMENAKNGEIMPNIAQMSAFWYAEKAAIGNAVSGRQSVKQALDDARARIQKQQ","1120034","From InterPro: IPR006060Maltose binding protein.Bacterial high affinity transport systems are involved in active transport of solutes across the cytoplasmic membrane. The protein components of these traffic systems include one or two transmembrane protein components, one or two membrane-associated ATP-binding proteins and a high affinity periplasmic solute-binding protein. In Gram-positive bacteria, which are surrounded by a single membrane and therefore have no periplasmic region, the equivalent proteins are bound to the membrane via an N-terminal lipid anchor. These homologue proteins do not play an integral role in the transport process per se, but probably serve as receptors to trigger or initiate translocation of the solute through the membrane by binding to external sites of the integral membrane proteins of the efflux system. In addition at least some solute-binding proteins function in the initiation of sensory transduction pathways.Maltodextrin binding protein (MBP) is the primary component of bacterial high-affinity active transport and chemotaxis. It is a monomeric protein, with 2 globular domains separated by a 2- or 3-stranded hinge. MBP binds and transports linear oligosaccharides (of up to 7 glucosyl units), as well as 2 cyclic maltodextrins which, although binding tightly, cannot be transported nor initiate a chemotactic response. It is thought that the hinge region is critical for the correct functioning of MBP, not just in the binding and recognition of sugars, but also in allowing and maintaining the integrity of initiation of both active transport and chemotaxis. ","periplasmic maltose-binding protein precursor","Periplasm","","
InterPro
IPR006059
Family
Bacterial extracellular solute-binding protein, family 1
PF01547\"[9-314]TSBP_bac_1
InterPro
IPR006060
Family
Maltose binding protein
PR00181\"[34-52]T\"[68-86]T\"[128-147]T\"[149-168]T\"[169-188]T\"[231-250]T\"[297-318]T\"[355-374]TMALTOSEBP
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[136-394]Tno description
signalp\"[1-24]?signal-peptide
tmhmm\"[5-23]?transmembrane_regions


","BeTs to 7 clades of COG2182COG name: Maltose-binding periplasmic proteins/domainsFunctional Class: GThe phylogenetic pattern of COG2182 is ---pkz--vd-lb-e-g---------Number of proteins in this genome belonging to this COG is","Significant hit (7.5e-103) to 8/8 blocks of the PR00181 family, which is described as \"Maltose binding protein signature\". Prints database entry for PR:PR00181. PR00181A 34-52 4e-18 PR00181B 68-86 1.3e-14 PR00181C 128-147 2.4e-13 PR00181D 149-168 3.7e-05 PR00181E 169-188 3.8e-09 PR00181F 231-250 9.6e-11 PR00181G 297-318 2.8e-12 PR00181H 355-374 2.3e-09","Residues 238 to 384 match (7e-11) PD:PD314168 which is described as SUGAR PROTEOME COMPLETE SUGAR-BINDING LIPOPROTEIN ABC TRANSPORTER SOLUTE-BINDING BINDING TRANSPORTER ","","","","","","","","","","","Tue Mar 16 10:28:39 2004","Mon Jan 6 15:14:28 2003","","","Thu May 13 12:15:54 2004","Tue Mar 16 10:28:39 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01654 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Tue Mar 16 10:28:39 2004","","","","","Residues 9 to 314 (E-value = 7.2e-36) place AA01654 in the SBP_bac_1 family which is described as Bacterial extracellular solute-binding protein (PF01547)","Tue Mar 16 10:28:39 2004","","","","Duplay P, Bedouelle H, Fowler A, Zabin I, Saurin W, Hofnung M.Sequences of the malE gene and of its product, the maltose-binding protein of Escherichia coli K12.J Biol Chem. 1984 Aug;259(16):10606-13.PMID: 6088507Spurlino JC, Lu GY, Quiocho FA.The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis.J Biol Chem. 1991 Mar;266(8):5202-19.PMID: 2002054Sharff AJ, Rodseth LE, Spurlino JC, Quiocho FA.Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis.Biochemistry. 1992 Nov;31(44):10657-63.PMID: 1420181Bedouelle H, Hofnung M.A DNA sequence containing the control regions of the malEFG and malK-lamB operons in Escherichia coli K12.Mol Gen Genet. 1982;185(1):82-7.PMID: 6283312Bedouelle H, Schmeissner U, Hofnung M, Rosenberg M.Promoters of the malEFG and malK-lamB operons in Escherichia coli K12.J Mol Biol. 1982 Nov;161(4):519-31.PMID: 6185687","","Tue Mar 16 10:36:24 2004","1","","","" "AA01655","1121327","1121446","120","GTGGCGGTATTTTCCAGTGAGCATGAAACACTTAAAAAGCCTTTTTACACATTATTGGCATTATCCGTAAATATTTTATTTTGTTATCCTCCCCCTGACTACTCCTTGTCTGTAACACTG","","","4486","VAVFSSEHETLKKPFYTLLALSVNILFCYPPPDYSLSVTL","1121446","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
tmhmm\"[15-33]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 15:18:29 2004","Thu Feb 26 15:18:29 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01655 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 15:18:29 2004","","","","","","","","","","","","","1","","","" "AA01656","1121680","1122795","1116","ATGGCAAGTGTAACATTGCGCAATGTGGGCAAATCTTACGGAAACGTACATATTTCCAAAGATATTAATTTGGATATTGAAGAAGGCGAATTTGTCGTCTTTGTCGGACCGTCCGGTTGCGGTAAATCCACATTATTGCGAATGATTGCCGGACTTGAGGATATTACCACCGGTGAACTTTACATCGGTGAAAAACGGATGAACGATGTGCCGCCGGCAAAGCGCGGTATCGGTATGGTGTTCCAATCTTACGCCCTGTACCCGCACTTGGATGTGGCAGAAAATATGTCTTTCGGGCTGAAATTAGCCGGTGTAAATAAAACGGAACGGGATCAGCGCGTTAATCAGGTTGCCGAAATTTTACAGCTTGCCCATTTGCTTGAACGTAAACCGAAAGCCTTGTCGGGCGGTCAGCGTCAACGTGTGGCGATTGGGCGAACCCTTGTTTCCCAGCCAGAAGTATTCTTGCTGGACGAACCGCTTTCCAACTTAGATGCCGCCTTGCGCGTACAAATGCGGGTGGAAATCTCCAAATTACACAAAAAACTCAACCGCACCATGATTTATGTTACCCATGACCAAGTGGAAGCCATGACCCTGGCGGACAAAATCGTGGTGTTGAATGCGGGCGGTATTGCGCAGGTGGGGAAACCGCTGGAACTTTACCATTATCCGCAAAATCGTTTCGTGGCCGGTTTTATCGGTTCACCGAAAATGAATTTCCTGCCGGTGAAAGTGACTGCTGTGGAAAAAGAGCGGGTGCAAATCGAATTGCCCGACGCCAACCATCATAACTTCTGGATCCCGGTTTCCGGTAATGGCGTGAAAGTGGGTGAAAACCTTTCATTAGGTATACGCCCTGAGCATTTAATTCCGTCTGATGAGGCAGAAGTTACGTTGCGCAGCAATGTGCAGGTGGTGGAATTGCTTGGTAACGAAACGCAAATTCACCTTGAAATCCCTGAAATTAAACAACCGACCTTAATTTATCGCCAAAATGATGTGGTGTTGGTGAAGGAGGGGGAAACGATGGACATCGGCATCATTCCGGAACGTTGCCATCTGTTTAAAGAAGACGGCACCGCCTGCCAACGTTTGTATAAAGAAAAAGGCGTT","","","41394","MASVTLRNVGKSYGNVHISKDINLDIEEGEFVVFVGPSGCGKSTLLRMIAGLEDITTGELYIGEKRMNDVPPAKRGIGMVFQSYALYPHLDVAENMSFGLKLAGVNKTERDQRVNQVAEILQLAHLLERKPKALSGGQRQRVAIGRTLVSQPEVFLLDEPLSNLDAALRVQMRVEISKLHKKLNRTMIYVTHDQVEAMTLADKIVVLNAGGIAQVGKPLELYHYPQNRFVAGFIGSPKMNFLPVKVTAVEKERVQIELPDANHHNFWIPVSGNGVKVGENLSLGIRPEHLIPSDEAEVTLRSNVQVVELLGNETQIHLEIPEIKQPTLIYRQNDVVLVKEGETMDIGIIPERCHLFKEDGTACQRLYKEKGV","1122793","[FUNCTION] This is one of the five proteins essential to the active binding protein-dependent transport system for maltoseand maltodextrin. MalK is the target for inducer exclusion, mediated by the unphosphorylated enzyme III of thephosphotransferase system for glucose and resulting in the inhibition of maltose transport. MalK has also a regulatoryfunction on mal gene expression. [SUBCELLULAR LOCATION] Inner membrane-associated. [SIMILARITY] Belongs to the ABC transporter family. ","maltose/maltodextrin transport ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[134-176]TQ9L531_VIBCH_Q9L531;
PF00005\"[29-210]TABC_tran
PS50893\"[4-234]TABC_TRANSPORTER_2
PS00211\"[134-148]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[28-219]TAAA
InterPro
IPR013611
Domain
Transport-associated OB
PF08402\"[283-356]TTOBE_2
noIPR
unintegrated
unintegrated
G3DSA:2.40.50.100\"[239-304]Tno description
G3DSA:3.40.50.300\"[1-237]Tno description
PTHR19222\"[4-246]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF42\"[4-246]TSUGAR ABC TRANSPORTER


","BeTs to 15 clades of COG3839COG name: ABC-type sugar transport systems, ATPase componentsFunctional Class: NThe phylogenetic pattern of COG3839 is -o-pkz-qvdrlbcefghs--j--twNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.7e-35) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 18-64 2.4e-17 IPB001140B 131-169 3.4e-14 IPB001140C 187-216 0.85Significant hit ( 5.1e-05) to 1/5 blocks of the IPB001324 family, which is described as \"Phosphoribulokinase family\". Interpro entry for IP:IPR001324. IPB001324A 28-49 5.1e-05","Residues 223 to 362 match (4e-07) PD:PD532859 which is described as ATP-BINDING PROTEOME COMPLETE MANNITOL ","","","","","","","","","","","Mon Jan 6 15:19:50 2003","Mon Jan 6 15:19:50 2003","","","Wed Mar 10 14:04:31 2004","Wed Mar 10 14:04:31 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01656 is paralogously related to AA02718 (3e-63), AA01645 (2e-59), AA00700 (4e-59), AA01947 (5e-48), AA01051 (7e-47), AA02353 (2e-46), AA01867 (9e-34), AA00858 (1e-33), AA01779 (5e-32), AA01524 (3e-30), AA02080 (3e-29), AA01684 (4e-28), AA00415 (6e-28), AA01616 (7e-28), AA02320 (5e-27), AA02899 (3e-26), AA02440 (7e-26), AA01422 (6e-25), AA02140 (1e-23), AA01824 (4e-23), AA01568 (9e-23), AA01820 (2e-22), AA00933 (1e-21), AA00799 (2e-21), AA02152 (2e-19), AA02324 (1e-18), AA02898 (2e-18), AA02805 (2e-18), AA01456 (3e-18), AA01393 (4e-18), AA02786 (2e-17), AA02331 (7e-17), AA01509 (6e-16), AA00207 (1e-15), AA01961 (2e-15), AA02573 (3e-15), AA02484 (4e-15), AA01510 (4e-15), AA01757 (7e-15), AA02642 (3e-14), AA00751 (8e-14), AA00591 (8e-14), AA02609 (2e-13), AA02550 (7e-13), AA00061 (1e-12), AA02606 (6e-12), AA01569 (9e-12), AA02225 (1e-10), AA02226 (2e-08), AA01555 (3e-08), AA00934 (4e-08), A02145 (8e-06), AA01291 (1e-05) and AA02146 (1e-05).","Wed Mar 10 14:04:31 2004","","","","","Residues 294 to 355 (E-value = 3.2e-07) place AA01656 in the TOBE family which is described as TOBE domain (PF03459)","Wed Mar 10 14:04:31 2004","","","","Gilson,E., Nikaido,H. and Hofnung,M. Sequence of the malK gene in E.coli K12 . Nucleic Acids Res. 10(22): 7449-7458 (1982) [PubMed: 6296778].Dahl,M.K., Francoz,E., Saurin,W., Boos,W., Manson,M.D. and Hofnung,M. Comparison of sequences from the malB regions of Salmonella typhimurium and Enterobacter aerogenes with Escherichia coli K12: apotential new regulatory site in the interoperonic region. Mol. Gen. Genet. 218 (2): 199-207 (1989) [PubMed: 2674653].Bedouelle,H. and Hofnung,M. A DNA sequence containing the control regions of the malEFG and malK-lamB operons in Escherichia coli K12. Mol. Gen. Genet. 185 (1): 82-87 (1982) [PubMed: 6283312].","","Mon Jan 6 15:19:50 2003","1","","","" "AA01657","1122875","1124155","1281","ATGAAAATTCAAAAAACACTTCTGACAATTGCCATTAGCGGCACATTATTTGCAACAAGCGCAAGTGCGGTGGATTTCCACGGTTACGCCCGTTCCGGTATTGGTTGGACATCGGGCGGTGGCGAACTGACCGCATTTTCCGCCAACGGCGCACCGGCAAAATACCGTTTAGGTAACGAATCCGATACCTATGCGGAATTAGGCTTCGGTCAAGAATTATGGAAAGAAGGCAACAAACGCTTCTATTTCGACAGCTTAATTGCCTATGGTGGTAATTTGCATAAAGGCGACTGGACCGAAACCAGCCCGGCAGTGCGTGAATTAAATGTGAAATTTGAAAACTTCGCTGACAGCTTACCGGGCGCCACATTATGGGCAGGTAAACGTTTCTACCAACGTCATGACGTACACATGAACGACTTCTACTACTGGGATATTTCCGGTCCGGGTGCGGGGGTTGAAGGCATTGATTTGGGTTTTGGTAAATTATCTCTTGCGGTAACCCGTAATACAGAAGCAGGCGGTGCATTTAGCTACTACTATGATCGCGCAAATAAAAGATGGGATACTACCCGTAAAGTACAAAAAGATGTTTACAACGATGTATTCGATGTTCGTTTAGCTGAAGTTCAAGTTAGCGAAAACGGTAAATTAGAATTCGGTTTTGATTACGCCCGATCTCATAAAAAAGACGATGCCCGCTATGTAAATGATGACGCGACCAAAAACGGTCACATGTTCACTATCGAACATACTCAAAGCGAGTTCTTCGGCGGCTTCAATAAATTCACCGTGCAATATGCCAAAGATTCCATGGCATCTGACGGTTGGAACTACGGTCATGCGCAAGGTTCATTAACCAGCAACCGTGGTCACATGATCCGTTTAATTGACCAAGGTACCGTTCAATTCAGCGATAAAGTTGAAATGATGTACGCCTTGATTTATCAAAAAACCGATTTAAATAACAAACAAGGCAAAACCTGGTACTCCGCCGGTGTTCGTCCGATGTATAAATGGACTAATACCATGAGTACCTTAATGGAACTCGGTTATGACCGCGTGAAAGATCAAGCCACCGGTAAGAAAAATGATTTAGCCAAAGTTACTCTTGCGCAACAATGGCAGGCAGGTAGTAGCATCTGGGCGCGTCCGGCAATTCGTGTGTTCGGAACTTACGCGCACTGGAATGATAAATTCAACACTGAGAATCGTATTGAACATGGTTACAAAGCAAAAGATGGCGAATTTATCGCTGGTGTTCAATTTGAAGCATGGTGG","","","49014","MKIQKTLLTIAISGTLFATSASAVDFHGYARSGIGWTSGGGELTAFSANGAPAKYRLGNESDTYAELGFGQELWKEGNKRFYFDSLIAYGGNLHKGDWTETSPAVRELNVKFENFADSLPGATLWAGKRFYQRHDVHMNDFYYWDISGPGAGVEGIDLGFGKLSLAVTRNTEAGGAFSYYYDRANKRWDTTRKVQKDVYNDVFDVRLAEVQVSENGKLEFGFDYARSHKKDDARYVNDDATKNGHMFTIEHTQSEFFGGFNKFTVQYAKDSMASDGWNYGHAQGSLTSNRGHMIRLIDQGTVQFSDKVEMMYALIYQKTDLNNKQGKTWYSAGVRPMYKWTNTMSTLMELGYDRVKDQATGKKNDLAKVTLAQQWQAGSSIWARPAIRVFGTYAHWNDKFNTENRIEHGYKAKDGEFIAGVQFEAWW","1124153","From InterPro:IPR003192Porin, LamB type.Maltoporin (LamB protein) forms a trimeric structure which facilitates the diffusion of maltodextrins across the outer membrane of Gram-negative bacteria. The membrane channel is formed by an antiparallel beta-barrel. ","maltose high-affinity receptor","Outer membrane, Extracellular","","
InterPro
IPR003192
Family
Porin, LamB type
PD008788\"[30-414]TLAMB_KLEPN_P31242;
G3DSA:2.40.170.10\"[24-427]Tno description
PF02264\"[26-427]TLamB
noIPR
unintegrated
unintegrated
signalp\"[1-23]?signal-peptide


","No hits to the COGs database.","Significant hit ( 1e-83) to 7/7 blocks of the IPB003192 family, which is described as \"LamB porin\". Interpro entry for IP:IPR003192. IPB003192A 25-36 8.6e-10 IPB003192B 55-67 1.8e-06 IPB003192C 125-164 3.7e-30 IPB003192D 197-231 5.1e-07 IPB003192E 295-308 1.7 IPB003192F 335-352 4.9e-10 IPB003192G 380-399 6.2e-11","","","","","","","","","","","","Tue Mar 16 10:49:01 2004","Tue Mar 16 10:49:01 2004","","","Tue Mar 16 11:38:16 2004","","yes","Fri Feb 20 15:41:32 MST 1998","AA01657 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Tue Mar 16 10:49:01 2004","","","","","Residues 26 to 427 (E-value = 1.1e-154) place AA01657 in the LamB family which is described as LamB porin (PF02264)","Tue Mar 16 10:49:01 2004","","","","Schirmer T, Keller TA, Wang YF, Rosenbusch JP.Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution.Science. 1995 Jan;267(5197):512-4.PMID: 7824948Werts C, Charbit A, Bachellier S, Hofnung M.DNA sequence analysis of the lamB gene from Klebsiella pneumoniae: implications for the topology and the pore functions in maltoporin.Mol Gen Genet. 1992 Jun;233(3):372-8.PMID: 1535683","","Tue Mar 16 10:50:15 2004","1","","","" "AA01658","1124244","1125140","897","ATGAAAAAAACGATAAAATTTTTGACCGCACTTTTATTGGCGAATATCGCAGTAGCCTCGCCAAGCCGGGCTAATACGCCTGTTCATATTAACTCAACGGCACTGGCAAATCTGCAATGGCAGGACGTATCCTTTTCCGAAAAAGTCACCACCAATTTATCCGAACAACAAAAACAAGCCTTTACCGCCTCTTTTGCCGGTGTAGAAAGCCCGATTGCCGCCTATCGCATTCCGGCGAACCAAGGCACTTTGGAAGTGGAAATTATCAGTCCTATTGAAAACAAAAGCGCATTCGTCCCAAGTGCGGTGGTTTTAGATAGCAATTTTAATGTGGCGGCGACTTACCCTTCATCCGAATTCAAATTCCAAGAAGAACGCGGTATGCAACCGAATCGCTTTGCCGCCGAGCTAAACCTTACGCCTGCCGCTTCACAAAGTTATATTTACCTGTTGATTTACACCACCCAACAAGATTTGGCAAAAACCACCATGATCCCGCATCCGGCGAAACTGTATGCCAAAGGCACCGGGCACCAACCGCCGGCATTGAATGATATTGAAGTGAAACACAGTTTGAATGGTCAGATTATCGTGAACGTCACTAACGCTAACGGCACGCGCTTTATCGGTATGCCAACCAATATTTTCTCCTCTTCCGATAAAAAAGCGGTTCAACCGGTAGGGGCAGCGCCTACACCGGCGCCGACAGCAAACATTGTGTCGTCTAAAGCGGTGAATGTGCCGGTGGATCGAGACACTGAAGCCTACTTCAATCAGGCAATCACCAAAGCGTTAAAAGGCGGTGATGTAAACAAAGCGATGAATTTAGTTAACGAAGCAGAAAAACTTGGCTTAACCTCACCGCGCCAAACCTTCTTAAAACAGGTTTCCTCGAAA","","","32206","MKKTIKFLTALLLANIAVASPSRANTPVHINSTALANLQWQDVSFSEKVTTNLSEQQKQAFTASFAGVESPIAAYRIPANQGTLEVEIISPIENKSAFVPSAVVLDSNFNVAATYPSSEFKFQEERGMQPNRFAAELNLTPAASQSYIYLLIYTTQQDLAKTTMIPHPAKLYAKGTGHQPPALNDIEVKHSLNGQIIVNVTNANGTRFIGMPTNIFSSSDKKAVQPVGAAPTPAPTANIVSSKAVNVPVDRDTEAYFNQAITKALKGGDVNKAMNLVNEAEKLGLTSPRQTFLKQVSSK","1125138","[FUNCTION] Not yet known. Might function in the uptake of a still unidentified substrate. [SUBCELLULAR LOCATION] periplasmic. ","maltose operon periplasmic protein precursor","Periplasm","","
InterPro
IPR010794
Family
Maltose operon periplasmic
PF07148\"[7-299]TMalM
noIPR
unintegrated
unintegrated
signalp\"[1-19]?signal-peptide


","No hits to the COGs database.","","Residues 20 to 299 match (1e-36) PD:PD040315 which is described as PERIPLASMIC PROTEOME COMPLETE MALTOSE OPERON PRECURSOR SUGAR SIGNAL PROTEIN MAL ","","","","","","","","","","","Mon Jan 6 15:57:09 2003","Mon Jan 6 15:57:09 2003","","","","Tue Mar 16 11:33:01 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01658 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Tue Mar 16 11:33:01 2004","","","","","Residues 7 to 299 (E-value = 6.9e-64) place AA01658 in the MalM family which is described as Maltose operon periplasmic protein precursor (MalM) (PF07148)","Tue Mar 16 11:33:01 2004","","","","Gilson,E., Rousset,J.P., Charbit,A., Perrin,D. and Hofnung,M. malM, a new gene of the maltose regulon in Escherichia coli K12. I. malM is the last gene of the malK-lamB operon and encodes a periplasmic protein. J. Mol. Biol. 191 (3): 303-311 (1986) PubMed: 2434655.Clement,J.M. and Hofnung,M. Gene sequence of the lambda receptor, an outer membrane protein of E. coli K12. Cell 27 (3 Pt 2): 507-514 (1981) PubMed: 6086106.","","Tue Feb 4 14:07:33 2003","1","","","" "AA01660","1125175","1125342","168","TTGCCACCGATTTTCGGTGGCTTTTTTATGATTGGAATAATGCAATTGCAGGAAAAGTGCGGTGGTTCTTGGCGGTGTTTTTTAGGAACGGGGCCTGGGGAGTTGAAAAATGATATTTACGAAGAAAAGAATCGATTGAATACAGGTGCGCTGATGGCGCGCGTTTCC","","","6176","LPPIFGGFFMIGIMQLQEKCGGSWRCFLGTGPGELKNDIYEEKNRLNTGALMARVS","1125342","","hypothetical protein","Cytoplasm, Extracellular","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-16]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 15:12:24 2004","Thu Feb 26 15:12:24 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01660 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 15:12:24 2004","","","","","","","","","","","","","1","","","" "AA01661","1126252","1125524","729","ATGGAATTAACCCATCAGGAAGAATTACGCTACAACCGCCAGATCGTGTTGAAAGACATTGATTTTGACGGACAGGAAACGCTGAAAGACAGCAAAATGCTCATCGTCGGTTTGGGCGGTTTAGGTTGCGCTGCCAGCCAATATTTAGCCGTCGCCGGTGTGGGACATTTGACGCTGCTGGATTTCGACACCGTAGATATATCCAACTTACAACGTCAGGTGTTGCATGATGACAGTCGTCTCGGCATGCCGAAAGTGGACTCGGCAAAACGTTCTTTAGCGCGTTTAAATCCGCATATTGAAGTGGACGCTATCAATCAGTTATTGGACGAACAACAGCTCAAGGAATTGGTCAGCAAATTTGATGTGGTGCTGGATTGCACCGATAACGTCACCACCCGAAACCAATTAGACAGCGCCTGTTCAGCTCATAAAATCCCGCTAGTTTCCGGTGCGGCGATTCGTCTGGAAGGACAGGTTTCCGTGTTCACTTACGAAGACGACACTCCAACCTATCACAGCCTCAGCCGTTTGTTCGGCGATAACGCCTTAAGTTGTGTAGAAGCCGGCGTACTAGCACCTATCGTAGGTTTGATCGGTTCCATTCAGGCCTTGGAAGCTATCAAAGTGCGGTTAAAAATCGGCACGAATTTATGCGGTCGGTTGTTGTTAATTGATGGGATGACGATGTCGGTAAGGGAAGTGAAGTTGACGGGGAAGGGTAATATA","","","26482","MELTHQEELRYNRQIVLKDIDFDGQETLKDSKMLIVGLGGLGCAASQYLAVAGVGHLTLLDFDTVDISNLQRQVLHDDSRLGMPKVDSAKRSLARLNPHIEVDAINQLLDEQQLKELVSKFDVVLDCTDNVTTRNQLDSACSAHKIPLVSGAAIRLEGQVSVFTYEDDTPTYHSLSRLFGDNALSCVEAGVLAPIVGLIGSIQALEAIKVRLKIGTNLCGRLLLIDGMTMSVREVKLTGKGNI","1125522","[FUNCTION] Involved in biosynthesis of a demolybdo cofactor (molybdopterin), necessary for molybdoenzymes. Plays arole in the activation of the small subunit of the molybdopterin converting factor (moaD) (by similarity). [PATHWAY] Molybdenum cofactor biosynthesis. [SIMILARITY] belongs to the HesA/MoeB/ThiF family. ","molybdopterin biosynthesis protein","Cytoplasm","","
InterPro
IPR000594
Domain
UBA/THIF-type NAD/FAD binding fold
PF00899\"[29-163]TThiF
InterPro
IPR007901
Domain
MoeZ/MoeB
PF05237\"[167-242]TMoeZ_MoeB
InterPro
IPR012730
Family
Molybdopterin synthase sulfurylase MoeB
TIGR02355\"[7-242]TmoeB: molybdopterin synthase sulfurylase Mo
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[2-242]Tno description
PTHR10953\"[2-237]TUBIQUITIN-ACTIVATING ENZYME E1


","BeTs to 20 clades of COG0476COG name: Dinucleotide-utilizing enzymes involved in molybdopterin and thiamine biosynthesis family 2Functional Class: HThe phylogenetic pattern of COG0476 is aompkzyq-dr-bcefghsnuj----Number of proteins in this genome belonging to this COG is","","Residues 11 to 142 match (5e-07) PD:PD590278 which is described as SIMILAR 5730525G14 RIKEN 5730525G14RIK CDNA GENE ","","","","","","","","","","","Mon Jan 6 16:02:23 2003","Mon Jan 6 16:02:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01661 is paralogously related to AA02933 (4e-16).","","","","","","Residues 167 to 243 (E-value = 2e-26) place AA01661 in the MoeZ_MoeB family which is described as MoeZ/MoeB domain (PF05237)","","","","","Nohno T, Kasai Y, Saito T. Cloning and sequencing of the Escherichia coli chlENoperon involved in molybdopterin biosynthesis. J Bacteriol 1988 Sep;170(9):4097-102. PubMed: 3045084.Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H. Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex. Nature 414 (6861): 325-329 (2001) [PubMed: 11713534].","","Mon Jan 6 16:02:23 2003","1","","","" "AA01662","1127482","1126271","1212","ATGTTGCCGTTATCCCAAGCCCTTGAGCAAATGTTAAACCAACTTCCCTTTCCCACTTCTACGGAAGCACTGCCGACTCACCTGGCAAGCCAACGCATTTGCGCTGAAAATATTATTTCCCCTATTAACGTTCCCTCTTTCGACAATTCCGCCATGGACGGTTATGCCGTGCGGTTGGCGGATTTGCAACAATCCATGACGCTTACTGTGGCGGGCAAAGCCTTTGCCGGTGCGCCATTTGAGGGTGAATGGACGGCGCAAAGTGCGGTCAGAATTATGACCGGTGCCATGATTCCACAGGATGCGGACGCGGTGGTGATGCAAGAAGAGGTTCAGGTGAACGATGACGGCACGGTAACCTTCCAAAATCTGCCGAAATTAAATCAAAATATTCGTCGTATCGGGGAAGATGTTAAACAGGGGGATGTGGTGTTGCGACAAGGCGCCTTATTAAATGCGATTTCCCTGCCGTTACTCGCCTCCCTTGGTATTGAAAACGTGAAGGTTTTCCCGCGTTTAAAAGTGGCGGTGCTTTCTACCGGTGATGAATTGGTGCCGGTGGGCAAACCGCTACAAACCGGGCAAATTTATGACACCAACCGTTTCGCCGTGAAATTATTATTGGAAAAATTAAACTGCGAAGTGTTGGATTTCGGTATTTTGCCAGATAACGAGGCGCAATTTGAAAACGCCTTTATTGAAGCGCAACAACAGGCGGATTTGGTGATTACCAGCGGCGGTGTTTCCGTGGGCGAAGCGGATTTCACCAAACATATTTTAGAGAAAGTGGGCAAAATCAATTTCTGGAAAATCGCCATTAAACCGGGTAAACCTTTTGCTTTCGGCAAATTAAAAAACGCCTGGTTCTGCGGTTTGCCGGGCAACCCGGTGTCGGCGTTGGTGACATTTTATCAATTAGTGCAACCCGCCATCGCCAAACTCAGCGGCTACAGCCAATGGAAAGCGCCGATTCGCTTCCCTGCCGTCGCCGCCGTGAATTTGAAAAAAGCGCCGGGACGATTAGATTTCCAACGCGGGTATTATCACGTCAACGCTCAAGGGCAAATTGAAGTGCAACCGGTGGGTTTCCAAGGCTCCCATTTATTCAGCTCCTTTGTGAAAAGTAATTGTTTTATCGTGCTGGAACAGGAACGCGGTAATGTTGCAGCGGGCGAAACGGTCACCATTGAGCCTTTTACCGATTTATTACAC","","","43978","MLPLSQALEQMLNQLPFPTSTEALPTHLASQRICAENIISPINVPSFDNSAMDGYAVRLADLQQSMTLTVAGKAFAGAPFEGEWTAQSAVRIMTGAMIPQDADAVVMQEEVQVNDDGTVTFQNLPKLNQNIRRIGEDVKQGDVVLRQGALLNAISLPLLASLGIENVKVFPRLKVAVLSTGDELVPVGKPLQTGQIYDTNRFAVKLLLEKLNCEVLDFGILPDNEAQFENAFIEAQQQADLVITSGGVSVGEADFTKHILEKVGKINFWKIAIKPGKPFAFGKLKNAWFCGLPGNPVSALVTFYQLVQPAIAKLSGYSQWKAPIRFPAVAAVNLKKAPGRLDFQRGYYHVNAQGQIEVQPVGFQGSHLFSSFVKSNCFIVLEQERGNVAAGETVTIEPFTDLLH","1126269","[FUNCTION] Involved in the biosynthesis of a demolybdo-cofactor (molybdopterin), necessary for molybdo-enzymes. Seems to be involved in a step of activation of molybdenum in the form of thiomolybdenum (by similarity). [PATHWAY] Molybdenum cofactor biosynthesis. [SIMILARITY] To the C-terminal of cinnamon/gephyrin","molybdopterin biosynthesis protein","Periplasm","","
InterPro
IPR001453
Domain
Molybdopterin binding domain
PD002460\"[181-316]TQ9CMW0_PASMU_Q9CMW0;
PF00994\"[176-313]TMoCF_biosynth
TIGR00177\"[172-309]Tmolyb_syn: molybdenum cofactor synthesis do
InterPro
IPR005110
Domain
MoeA, N-terminal, domain I and II
PF03453\"[1-163]TMoeA_N
InterPro
IPR005111
Domain
MoeA, C-terminal, domain IV
PF03454\"[327-400]TMoeA_C
InterPro
IPR008284
Family
Molybdenum cofactor biosynthesis protein
PS01079\"[249-282]TMOCF_BIOSYNTHESIS_2
InterPro
IPR012088
Family
Molybdenum cofactor molybdenum incorporation protein MoeA
PIRSF004870\"[1-401]TMolybdenum cofactor molybdenum incorporation protein MoeA
noIPR
unintegrated
unintegrated
G3DSA:2.170.190.11\"[45-137]Tno description
G3DSA:3.40.980.10\"[145-332]Tno description
PTHR10192\"[1-399]TMOLYBDOPTERIN BIOSYNTHESIS PROTEIN


","BeTs to 18 clades of COG0303COG name: Molybdopterin biosynthesis enzymeFunctional Class: HThe phylogenetic pattern of COG0303 is aompkz-q-dr-bcefgh--uj----Number of proteins in this genome belonging to this COG is","Significant hit ( 7.5e-31) to 3/3 blocks of the IPB001453 family, which is described as \"Molybdenum cofactor biosynthesis protein\". Interpro entry for IP:IPR001453. IPB001453A 45-56 1.3e-07 IPB001453B 89-109 1.8e-13 IPB001453C 174-189 1.3e-06","Residues 33 to 172 match (4e-14) PD:PD550876 which is described as BIOSYNTHESIS PROTEOME MOLYBDENUM COMPLETE COFACTOR MOLYBDOPTERIN ","","","","","","","","","","","Mon Jan 6 16:09:13 2003","Mon Jan 6 16:09:13 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01662 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 327 to 400 (E-value = 1.4e-23) place AA01662 in the MoeA_C family which is described as MoeA C-terminal region (domain IV) (PF03454)","","","","","Hasona A, Ray RM, Shanmugam KT. Physiological and genetic analyses leading to identification of a biochemical role for the moeA (molybdate metabolism) gene product in Escherichia coli. J Bacteriol 1998 Mar;180(6):1466-72. PubMed: 9515915. ","","Mon Jan 6 16:09:13 2003","1","","","" "AA01663","1127611","1128264","654","ATGAACGATATTTCACCTGAAGCAGAGAAAGTCCGTACGGCGCTGGTTCAGAAAGGAATTGAAACACCGATGATTGTGTCGGACGAGAGCAAAGATGAACGTCGCACAAGAATCGAACAACATATGCGCGAAGTGTTGCGTTTAATCGGCTTGGATTTACGTGACGACAGTATTGAAGAAACCCCGTCACGTCTTGCAAAAATGTTCGTTGATGAAATTTTTAGCGGCTTGGATTACGTCAATTTTCCTAAGATTACGAACATTGCTAATCGTATGAAAGTGAGTGAAATGGTGTTGGTCAATGATGTCACATTAACCAGCACCTGCGAACATCATTTTGTTACCATCGGCGGAAAAGTTTCCGTGGCGTATTACCCGAAGAAATGGGTTATCGGCTTATCTAAAATTAATCGCATAGTGACATTTTTCGCTCAACGTCCGCAAGTGCAGGAGCGTTTAACGGAACAAATTTTGTTGGCATTCCAAACCATTTTGGAAACGGAAGATGTGGCGGTTTATGTAAAAGCAACCCATTTCTGCGTGAAATGCCGTGGCATTAAAGATGCCAACAGCTACACCGTCACCTCCGCTTTCGGCGGCGTGTTCTTAGAAGATCGCGAAACACGCAAAGAGTTTTTGAGTTTAATTAATAAA","","","24936","MNDISPEAEKVRTALVQKGIETPMIVSDESKDERRTRIEQHMREVLRLIGLDLRDDSIEETPSRLAKMFVDEIFSGLDYVNFPKITNIANRMKVSEMVLVNDVTLTSTCEHHFVTIGGKVSVAYYPKKWVIGLSKINRIVTFFAQRPQVQERLTEQILLAFQTILETEDVAVYVKATHFCVKCRGIKDANSYTVTSAFGGVFLEDRETRKEFLSLINK","1128262","[CATALYTIC ACTIVITY] GTP + 2 H(2)O = formate + 2-amino-4-hydroxy-6-(erythro-1,2, 3-trihydroxypropyl)dihydropteridine triphosphate.[PATHWAY] Tetrahydrofolate biosynthesis; first step.[SUBUNIT] Homopolymer.","GTP cyclohydrolase I","Cytoplasm","","
InterPro
IPR001474
Family
GTP cyclohydrolase I
PD003330\"[11-216]TGCH1_PASMU_P57865;
PF01227\"[96-200]TGTP_cyclohydroI
TIGR00063\"[38-218]TfolE: GTP cyclohydrolase I
PS00859\"[96-112]TGTP_CYCLOHYDROL_1_1
PS00860\"[144-154]TGTP_CYCLOHYDROL_1_2
noIPR
unintegrated
unintegrated
G3DSA:1.10.286.10\"[2-84]Tno description
G3DSA:3.30.1130.10\"[85-218]Tno description
PTHR11109\"[43-217]TGTP CYCLOHYDROLASE I


","BeTs to 14 clades of COG0302COG name: GTP cyclohydrolase IFunctional Class: HThe phylogenetic pattern of COG0302 is ------yq-drlbcefghs-ujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 1.6e-51) to 3/3 blocks of the IPB001474 family, which is described as \"GTP cyclohydrolase I\". Interpro entry for IP:IPR001474. IPB001474A 49-66 5.2e-06 IPB001474B 94-146 2.1e-33 IPB001474C 165-185 2.1e-09","Residues 4 to 216 match (7e-102) PD:PD003330 which is described as GTP CYCLOHYDROLASE HYDROLASE I PROTEOME COMPLETE GTP-CH-I METABOLISM ONE-CARBON ENZYME ","","","","","","","","","","","Mon Jan 6 16:12:27 2003","Mon Jan 6 16:12:27 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01663 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 96 to 200 (E-value = 1.3e-51) place AA01663 in the GTP_cyclohydroI family which is described as GTP cyclohydrolase I (PF01227)","","","","","Katzenmeier,G., Schmid,C., Kellermann,J., Lottspeich,F. and Bacher,A. Biosynthesis of tetrahydrofolate. Sequence of GTP cyclohydrolase I from Escherichia coli Biol. Chem. Hoppe-Seyler 372 (11), 991-997 (1991) PubMed: 1665332 Schmid,C., Meining,W., Weinkauf,S., Bachmann,L., Ritz,H., Eberhardt,S., Gimbel,W., Werner,T., Lahm,H.W., Nar,H. and Bacher,A. Studies on GTP cyclohydrolase I of Escherichia coli Adv. Exp. Med. Biol. 338, 157-162 (1993) PubMed: 8304099 Schoedon,G., Redweik,U., Frank,G., Cotton,R.G. and Blau,N. Allosteric characteristics of GTP cyclohydrolase I from Escherichia coli Eur. J. Biochem. 210 (2), 561-568 (1992) PubMed: 1459137 Nar,H., Huber,R., Meining,W., Schmid,C., Weinkauf,S. and Bacher,A. Atomic structure of GTP cyclohydrolase I Structure 3 (5), 459-466 (1995) PubMed: 7663943 ","","Mon Jan 6 16:12:27 2003","1","","","" "AA01666","1129681","1128371","1311","TTGGCATTCATCGCCAAAAACATCAATCAAGATAACATTATCGCCGATTATAACGGACAAACGTTCATGCTCCCCGCCAGCACGCAAAAAGTATTTACCGCTTTGGCGGCAAAATTGGCGCTCGGCGATTCATTTCAATTTCAAACCGCACTTTTAACCAACGGCAAAGTACAAAACGGTCAACTCAACGGCGATTTAATTGTGCGTTTTACCGGCGACCCGGATTTAACCAGCGGGCAATTATTCAATTTATTATCGGAATTAAAGAAGCAAAACATTAATAAAATCACCGGTAATCTGATTTTAGATACGTCGGTGTTTATCGGTCACGATCGCGGTTTAGGCTGGATCTGGAATGATCTGACCATGTGCTTTAACGCTCCGCCTGCCGCGGTAAATATTGATAATAACTGCTTTTATGTGGATATTGATGCCAACCAGCCGGAAGGGCAACCGGTAAAATTCAACGTGCCGTCGCAATACCCGATTCAGGTGTTCGGGCAGGTTTATGTGGCAGGTAAAGAGGAAGCCGGTTATTGCCAGTTGGATGCTATCGTGCATGATAACAACCGCTATCAGGTGAAAGGCTGTCTGGTGCGTCAAAGCAAGCCTTTCGGGTTAAGTTTCGCCGTGCAGGATCCCAACGCTTACGCAGCGGCGATTATTCAACGCCAGCTAAAACGCCTGAATATCGAATTTAACGGGCAAGTGCAACAACCTTATCGCCAACAACAAGGTCAGGTGTTGGCGCAACATTTGTCCAAACCGCTGCCCGATCTCATCAAAAAAATGATGAAAAAATCTGACAACCAAATTGCCGATGCGTTGTTCCGCACCATCGCTTACAACCAATACAAACGCCCCGCGTCCTTCCAATTAGGCACTCTGGCAATGAAAAGGGTGTTATCGCAGGTGGGTATTAAATTCGGCAACAGCGTTATCGCCGACGGTTCAGGCTTATCCCGCCATAATTTAGTGGCGCCGCAAACCATGTTGCAGGTGTTGGATTACATCGCAAAAAATGAAGAAAAATTGCATTTATTGGATAGCTTCCCTATCGCCGGCGTGGACGGCACCTTAAGCGGGCGCGGGTCATTAATCAATCCGCCGTTGGTGAAAAACGTCATCGCCAAAACCGGCGCATTAAAAGGCGTGTACAATCTGGCGGGCTATCTCACCAACGCGCGCGGAGAAAAAGTGGCGTTCGTGCAATTTATCAACGGCTACTCCACCGGCGATCCGGAAAGCAAAACCAAGCGTGCCCCGCTAGTGCAATTTGAAAGCGGCGTGTATAACGCGCTGTATCAGGAT","","","52795","LAFIAKNINQDNIIADYNGQTFMLPASTQKVFTALAAKLALGDSFQFQTALLTNGKVQNGQLNGDLIVRFTGDPDLTSGQLFNLLSELKKQNINKITGNLILDTSVFIGHDRGLGWIWNDLTMCFNAPPAAVNIDNNCFYVDIDANQPEGQPVKFNVPSQYPIQVFGQVYVAGKEEAGYCQLDAIVHDNNRYQVKGCLVRQSKPFGLSFAVQDPNAYAAAIIQRQLKRLNIEFNGQVQQPYRQQQGQVLAQHLSKPLPDLIKKMMKKSDNQIADALFRTIAYNQYKRPASFQLGTLAMKRVLSQVGIKFGNSVIADGSGLSRHNLVAPQTMLQVLDYIAKNEEKLHLLDSFPIAGVDGTLSGRGSLINPPLVKNVIAKTGALKGVYNLAGYLTNARGEKVAFVQFINGYSTGDPESKTKRAPLVQFESGVYNALYQD","1128369","[FUNCTION] Not involved in transpeptidation but exclusively catalyses a DD-carboxypeptidase and DD-endopeptidasereaction (by similarity). [CATALYTIC ACTIVITY] D-alanyl-D-alanine + H(2)O = 2 D-alanine. [PATHWAY] Final stages in peptidoglycan synthesis. [SUBCELLULAR LOCATION] Periplasmic (potential). [SIMILARITY] Belongs to peptidase family s13; alsoknown as the D-alanyl-D-alanine carboxypeptidase 3 family. ","penicillin-binding protein 4; D-alanyl-D-alanine carboxypeptidase; D-alanyl-D-alanine-endopeptidase","Periplasm","","
InterPro
IPR000667
Family
Peptidase S13, D-Ala-D-Ala carboxypeptidase C
PR00922\"[23-42]T\"[248-270]T\"[306-320]T\"[321-335]T\"[385-398]TDADACBPTASE3
PF02113\"[25-407]TPeptidase_S13
TIGR00666\"[10-408]TPBP4: D-alanyl-D-alanine carboxypeptidase/D


","No hits to the COGs database.","Significant hit ( 1.1e-47) to 5/5 blocks of the PR00922 family, which is described as \"D-Ala-D-Ala carboxypeptidase 3 (S13) family signature\". Prints database entry for PR:PR00922. PR00922A 23-42 1e-11 PR00922B 248-270 2.5e-12 PR00922C 306-320 8.2e-05 PR00922D 321-335 1.5e-07 PR00922E 385-398 5.3e-05","Residues 364 to 436 match (1e-28) PD:PD489338 which is described as CARBOXYPEPTIDASE DD- SYNT PENICILLIN-BINDING PROTEOME ALANINE PEPTIDOGLYCAN DD-PEPTIDASE COMPLETE D-ALANYL-D-ALANINE-ENDOPEPTIDASE ","","","","","","","","","","","Mon Jan 6 16:18:14 2003","Mon Jan 6 16:18:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01666 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 25 to 407 (E-value = 2e-176) place AA01666 in the Peptidase_S13 family which is described as D-Ala-D-Ala carboxypeptidase 3 (S13) family (PF02113)","","","","","McDonough MA, Anderson JW, Silvaggi NR, Pratt RF, Knox JR, Kelly JA. Structures of two kinetic intermediates reveal species specificity of penicillin-binding proteins. J Mol Biol. 2002 Sep 6;322(1):111-22. PMID: 12215418 ","","Mon Jan 6 16:19:02 2003","1","","","" "AA01668","1129970","1130443","474","ATGCAACAAATTCCAATGACTGTTCGCGGCGCACAATTACTGCGTGAAGAACTGGATTATCTTAAAAAAGAACGTCGCCCGGAAATCATCAAAGCCATTGCGGAAGCCCGTGAATATGGCGATTTAAAAGAAAATGCGGAATATCACGCCGCCCGTGAGCAACAAGGTTTCTGCGAAGGACGCATTCAGGAAATCGAAGGCAAATTAGCCAATAGCCAAGTGATCGACGTCACTAAAATCCCGAATAACGGCAAAGTAATCTTCGGTGCCACTGTAGTGTTGCTTAACACCAATACGGACGAAGAAGTGAGTTACCGCATTGTGGGCGATGACGAAGCAGACATCAAAAACGGCTTAATTTCCGTTAATTCACCGATTGCTCGCGGTTTGGTCGGCAAAGAAGTGGACGATGTGGTCAATATCTCGACGCCGGGTGGCACGGTGGAATTTGAAATCATTGAAGTGGATTACGTT","","","17530","MQQIPMTVRGAQLLREELDYLKKERRPEIIKAIAEAREYGDLKENAEYHAAREQQGFCEGRIQEIEGKLANSQVIDVTKIPNNGKVIFGATVVLLNTNTDEEVSYRIVGDDEADIKNGLISVNSPIARGLVGKEVDDVVNISTPGGTVEFEIIEVDYV","1130441","[FUNCTION] Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as greA or greB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides (By similarity).","transcription elongation factor","Cytoplasm","","
InterPro
IPR001437
Domain
Transcription elongation factor, GreA/GreB region, prokaryotic
PD004918\"[90-157]TQ7VL00_HAEDU_Q7VL00;
G3DSA:1.10.287.180\"[1-75]Tno description
G3DSA:3.10.50.30\"[76-158]Tno description
PF01272\"[80-157]TGreA_GreB
PF03449\"[1-74]TGreA_GreB_N
PS00829\"[17-48]TGREAB_1
PS00830\"[121-137]TGREAB_2
InterPro
IPR006359
Domain
Prokaryotic transcription elongation factor GreA
TIGR01462\"[5-156]TgreA: transcription elongation factor GreA
InterPro
IPR012243
Family
Prokaryotic transcription elongation factor GreA, GreB
PIRSF006092\"[1-158]TTranscription elongation factor GreA/GreB


","No hits to the COGs database.","Significant hit ( 1.4e-60) to 2/2 blocks of the IPB001437 family, which is described as \"Prokaryotic transcription elongation factor GreA/GreB\". Interpro entry for IP:IPR001437. IPB001437A 17-66 2e-39 IPB001437B 105-137 4.8e-20","Residues 112 to 155 match (9e-08) PD:PD582765 which is described as FACTOR ELONGATION TRANSCRIPTION PROTEOME COMPLETE GREA DNA-BINDING COILED TRANSCRIPT REGULATION ","","","","","","","","","","","Wed Feb 5 14:00:26 2003","Mon Jan 6 16:23:38 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01668 is paralogously related to AA00944 (8e-23).","","","","","","Residues 80 to 157 (E-value = 7.3e-42) place AA01668 in the GreA_GreB family which is described as Prokaryotic transcription elongation factor, GreA/GreB, C-terminal domain (PF01272)","","","","","Stebbins,C.E., Borukhov,S., Orlova,M., Polyakov,A., Goldfarb,A. and Darst,S.A. Crystal structure of the GreA transcript cleavage factor from Escherichia coli. Nature 373 (6515): 636-640 (1995) PubMed: 7854424.Sparkowski,J. and Das,A. The nucleotide sequence of greA, a suppressor gene that restores growth of an Escherichia coli RNA polymerase mutant at high temperature. Nucleic Acids Res. 18 (21): 6443 (1990) PubMed: 2243801.","","Wed Feb 5 14:00:26 2003","1","","","" "AA01670","1130821","1130522","300","ATGTCAATTACATTATCAACCAAACAAAAACAGTATCTAAAAGGACTGGCCCATCATTTAAGCCCGGTGGTGATGCTCGGTGGCAATGGTTTAACGGAAGGCGTGCTGGCAGAAATTGATTTATCGTTGAATCATCATGAATTAATTAAGGTGAAAATCAGCGGTTCCGATCGTGAAACCAAACAACTTATTATTGATGCGATTGTGCGGGAAACCGGCGCTACGGCGGTGCAAACCATCGGTCATGTGCTGGTGCTATATCGTCCGAGTGAAGAAAATAAAATTCAGCTTCCGCGCAAA","","","10974","MSITLSTKQKQYLKGLAHHLSPVVMLGGNGLTEGVLAEIDLSLNHHELIKVKISGSDRETKQLIIDAIVRETGATAVQTIGHVLVLYRPSEENKIQLPRK","1130520","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR001890
Domain
CRS1/YhbY
PD010559\"[12-98]TQ74DQ2_GEOSL_Q74DQ2;
PF01985\"[5-88]TCRS1_YhbY
TIGR00253\"[5-99]TTIGR00253: conserved hypothetical protein T
PS01301\"[5-30]TUPF0044
noIPR
unintegrated
unintegrated
G3DSA:3.30.110.60\"[3-100]Tno description


","BeTs to 12 clades of COG1534COG name: Predicted RNA-binding protein containing KH domain, possibly ribosomal proteinFunctional Class: JThe phylogenetic pattern of COG1534 is aom-kz-----lb-efghsn------Number of proteins in this genome belonging to this COG is","Significant hit ( 5.6e-23) to 1/1 blocks of the IPB001890 family, which is described as \"Uncharacterized protein family UPF0044\". Interpro entry for IP:IPR001890. IPB001890 5-44 5.1e-23","Residues 4 to 92 match (1e-33) PD:PD010559 which is described as COMPLETE PROTEOME RNA-BINDING KH CONTAINING DOMAIN YQEI SP1748 NMA1009 PREDICTED ","","","","","","","","","","","","Mon Jan 6 16:34:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01670 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 88 (E-value = 2.4e-38) place AA01670 in the CRS1_YhbY family which is described as CRS1 / YhbY domain (PF01985)","","","","","Filiatrault,M.J., Gibson,B.W., Schilling,B., Sun,S., Munson,R.S. Jr. and Campagnari,A.A. Construction and Characterization of Haemophilus ducreyi Lipooligosaccharide (LOS) Mutants Defective in Expression of Heptosyltransferase III and beta 1,4-Glucosyltransferase: Identification of LOS Glycoforms Containing Lactosamine Repeats. Infect. Immun. 68(6): 3352-3361, 2000. PubMed: 10816485 ","","Mon Jan 6 16:34:07 2003","1","","","" "AA01671","1130989","1131285","297","ATGATGATACAAATTAAGACGACTTTTCTTTTTGATGAATGGTTGAAGAAACTCAAAAACCTAAGAGCTAAAGCAAAAATCAACGCACGAATTAAACGGTTACAGTTTGGTAATTTCGGTGATTTAAAAAGCGTTAATGACGGCATATTTGAAATGCGGATTGATAAAGGTCAGGGGTATCGGGTTTATCTGAAAAATCAAAATGGCATACTTGTTATCCTGCTTTGTGGCGGAGACAAATCCACTCAAGAGAAAGATATCAAGAAAGCAAAACAACTTGCACAGGAAATGGGACTA","","","11390","MMIQIKTTFLFDEWLKKLKNLRAKAKINARIKRLQFGNFGDLKSVNDGIFEMRIDKGQGYRVYLKNQNGILVILLCGGDKSTQEKDIKKAKQLAQEMGL","1131283","","conserved hypothetical protein","Periplasm, Extracellular","","
InterPro
IPR009241
Family
Protein of unknown function DUF891
PF05973\"[46-97]TGp49
InterPro
IPR014056
Family
Addiction module killer protein, HI1419
TIGR02683\"[3-97]Tupstrm_HI1419: probable addiction module ki


","No hits to the COGs database.","","Residues 40 to 97 match (7e-20) PD:PD067155 which is described as COMPLETE PROTEOME PLASMID RSP0077 XFA0045 R01829 HI1419 CC3038 XF2764 PROPHAGE ","","","","","","","","","","","","Mon Jan 6 16:35:17 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01671 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 98 (E-value = 9.8e-61) place AA01671 in the DUF891 family which is described as Bacterial protein of unknown function (DUF891) (PF05973)","","","","","","","","1","","","" "AA01672","1131285","1131578","294","ATGAGTGAACAATTGAAAGATTTTGATCCTGCAGAATATTTATCTACCGAAGAAGATATTCGGCTTTATTTAAATGAAGTGCTACAAGAAAATAATATTGAGCTTATTTTGTCTGCGTTAGGCGATATCGCACGAACCAGAAATATGAGCCAAATTGCCCGCGAAACCGGTATGAGTAGAGAAGGGCTTTATAAAGCCCTGTCCGGTACGGGCAATCCTACCTTTGCCACCGTGATTAAAGTCATGAAAGCCTTAAATTTACAACTCCAAGTGCAACCTTCCGGTTATGTTTCT","","","13813","MSEQLKDFDPAEYLSTEEDIRLYLNEVLQENNIELILSALGDIARTRNMSQIARETGMSREGLYKALSGTGNPTFATVIKVMKALNLQLQVQPSGYVS","1131576","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR001387
Domain
Helix-turn-helix type 3
PF01381\"[40-92]THTH_3
InterPro
IPR014057
Family
Addiction module antidote protein, HI1420
TIGR02684\"[4-92]Tdnstrm_HI1420: probable addiction module an


","No hits to the COGs database.","","Residues 1 to 87 match (2e-33) PD:PD066355 which is described as COMPLETE PROTEOME PLASMID DNA-BINDING RSP0076 R01829 HI1420 CC3037 XF2763 PROPHAGE ","","","","","","","","","","","","Mon Jan 6 16:36:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01672 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 40 to 92 (E-value = 5.2e-05) place AA01672 in the HTH_3 family which is described as Helix-turn-helix (PF01381)","","","","","","","","1","","","" "AA01673","1132153","1131617","537","GTGGAAATGCCACAAGAAATGCTGAAAGGATTACAAATCGGCGCCTCCGTTGCCCATAACGGCGTATGTTTAACCGTAACGGAAATTAAAGATAATCTGGTGAGCTTCGATTTAATGCAGGAAACGTTGAAGATCACCAATTTAGGCGAATTAAAGGTCGGAGATCCCGTGAATATCGAACGCGCCATGCAAATGGGTACGGAAATCGGCGGGCATATTTTATCCGGTCATGTGTATTGCACGGCGGAAATCATCGAACGCCTGCCTTCCGAAAACAACCTGCAAATTTGGTTCAAACTGCCGAATAAAGAGGTGATGAAATATGTGCTGACCAAAGGTTTTATCGCCGTAGACGGCATTAGCTTAACCATCGGCAAAGTACGCGAACAAAGCTTCTGCGTGAACCTGATCCCGGAAACCCTCCACCGCACCCTTATCGGTAAGAAAGCGGAGGGTGACAAAGTGAATATCGAAATCGACCCGCAAACCCAGGCAATTGTGGATACCGTTGAACGTTACTTAGCGCAGAAAGAGGCG","","","22620","VEMPQEMLKGLQIGASVAHNGVCLTVTEIKDNLVSFDLMQETLKITNLGELKVGDPVNIERAMQMGTEIGGHILSGHVYCTAEIIERLPSENNLQIWFKLPNKEVMKYVLTKGFIAVDGISLTIGKVREQSFCVNLIPETLHRTLIGKKAEGDKVNIEIDPQTQAIVDTVERYLAQKEA","1131615","[FUNCTION] Riboflavin synthase is a bifunctional enzyme complex catalyzing the formation of riboflavin from5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione and l-3,4-dihydrohy-2-butanone-4-phosphate via6,7-dimethyl-8-lumazine. the alpha subunit catalyzes the dismutation of 6,7-dimethyl-8-lumazine to riboflavin and5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione (by similarity). [CATALYTIC ACTIVITY] 2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine.[PATHWAY] Final steps of riboflavin synthesis. [SUBUNIT] Oligomer that consist of 3 alpha subunits and 60 beta subunits (by similarity). [DOMAIN] Composed of two homologous domains. [SIMILARITY] To bioluminescence antenna proteins luxY (yfp)and luxL (lumP). ","riboflavin synthase, alpha chain","Cytoplasm","","
InterPro
IPR001783
Family
Lumazine-binding protein
PD004110\"[1-69]T\"[76-168]TRISA_HAEIN_P45273;
PIRSF000498\"[1-178]TRiboflavin synthase, alpha subunit
PTHR21098\"[3-178]TRIBOFLAVIN SYNTHASE ALPHA CHAIN
PF00677\"[1-62]T\"[75-160]TLum_binding
TIGR00187\"[1-179]TribE: riboflavin synthase, alpha subunit
PS51177\"[1-72]T\"[73-170]TLUMAZINE_BIND
noIPR
unintegrated
unintegrated
G3DSA:2.40.30.20\"[1-72]T\"[77-179]Tno description


","BeTs to 17 clades of COG0307COG name: Riboflavin synthase alpha chainFunctional Class: HThe phylogenetic pattern of COG0307 is -o----yqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 4.1e-66) to 4/5 blocks of the IPB001783 family, which is described as \"Riboflavin synthase alpha chain family lumazine binding domain\". Interpro entry for IP:IPR001783. IPB001783B 14-26 4.8e-07 IPB001783C 41-84 4.1e-30 IPB001783D 112-124 2.1e-08 IPB001783E 132-160 1.9e-16 IPB001783B 112-124 0.76 IPB001783E 34-62 3.4e-05","Residues 73 to 160 match (1e-12) PD:PD493784 which is described as RIBOFLAVIN ALPHA SYNTHASE COMPLETE PROTEOME CHAIN TRANSFERASE SUBUNIT FLAVOPROTEIN BIOSYNTHESIS ","","","","","","","","","","","Mon Oct 4 14:30:37 2004","Mon Oct 4 14:30:37 2004","","Mon Oct 4 14:30:37 2004","Mon Oct 4 14:30:37 2004","Mon Oct 4 14:30:37 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01673 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Oct 4 14:30:37 2004","","","","","Residues 75 to 160 (E-value = 4.9e-41) place AA01673 in the Lum_binding family which is described as Lumazine binding domain (PF00677)","Mon Oct 4 14:30:37 2004","","","","Eberhardt,S., Richter,G., Gimbel,W., Werner,T. and Bacher,A. Cloning, sequencing, mapping and hyperexpression of the ribC gene coding for riboflavin synthase of Escherichia coli. Eur. J. Biochem. 242 (3): 712-719 (1996) [PubMed: 9022701].Hensel,M., Shea,J.E., Baumler,A.J., Gleeson,C., Blattner,F. and Holden,D.W. Analysis of the boundaries of Salmonella pathogenicity island 2 and the corresponding chromosomal region of Escherichia coli K-12.J. Bacteriol. 179 (4): 1105-1111 (1997) [PubMed: 9023191].","","Mon Jan 6 16:45:24 2003","1","","","" "AA01674","1132157","1132255","99","GTGTGTTCTAAAATTAGCCTTTTCCGTGATCGTCTTAATTTGTGCGGTACCTTGCACAATGCCTGTAAACATAATTACCTCGAAATTTATCTATTTTTA","","","3881","VCSKISLFRDRLNLCGTLHNACKHNYLEIYLFL","1132255","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 15:08:44 2004","Thu Feb 26 15:08:44 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01674 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 15:08:44 2004","","","","","","","","","","","","","1","","","" "AA01675","1132255","1133649","1395","ATGAAGTTAACAACCGTCAAAGAATATCATATTGAAGCTAAAAAATTAATTGCTATTGCCCTCCCGATTTTGCTCGCGCAAATTGCGCAGAATTCCATGGGATTGGTGGACACCATTATGGCAGGACGTGTCAGTGCGGTGGACATGGCAGCGATTTCCGTGGGGGCGTCCATCTGGCTGCCGTTGGTGTTGTTCGGGTATGGCTTATTGCTTGCGTTGCCGCCGACCATTTCCTATTTGAACGGTTCGGGGCAACGCCGGCGCATTGCCCATCAGGTGCGCCAAGGTATTTGGATTGTGCTTTTTAGCTGCATTCCGCTGGTGTGGCTGATTTATAGCAGCGATTTCGTACTACAAAAAATGGACATGGAACAACGCTTGGCGGACATTACTATCGGTTATTTGCACGCCATGGTTTGGGGCTTGCCGGGCTATTTGTTGATGGTGAATTTTCGTTGTTTAAATGACGGCATCGCGAAAACTAAACCAGCGATGGTGATCACCTTTCTCGGCTTGCTGATCAATATTCCTCTTAATTATATTTTTATTTACGGCAAATTGGGTGTGCCGGCATTCGGCGCCGTGGGCTGTGGCATTGCCACGGCAATTGTAAACTGGGTGATGTGTCTGTTGATGTTGGCATACTGTATGCGGGCGAAAAATCAACGTGATTTGAAGGTTTTCGCAAATATCATTGAACGCCCGAATAGACGCACGCTGGGGAAATTGCTGAAGCTGGGTTTCCCCATTGCTATGGCGTTGTGCTGTGAAGTAGCATTGTTTGCGCTAACCTCTTTATTCTTATCGCCTTTGGGCGCCGACGTGGTGGCAAGTCATCAAATTGCACTAAATACCGGTTCTTTTGTATTTATGTTGCCTATGTCTCTCGGCATGGCAACGACCATTTTGGTGGGGCAGCGTTTGGGTGAAAAATCCCCGGAAGGCGCAAAGCAGGTGACCTATTCTGCGCTGGTTATGGGGTTATTTATTGCGGTGATAACGGCATTTTTAATCGTAATTTTGAAGGAGCAAATTGCTAACATTTTCGTGAAAGATGCCGAAGTCATTGCCATGGCGGGCACCCTGTTGCTATTGGCGGCGTTGTATCAATTCTCCGACACCATACAAGTGATTATTGGCAGTGTGTTGCGCGGCTACAAGGACACGCAAGCGATTTTATACATCACCTTATTTTGTTATTGGGTTGTAGGAATGCCGCTCGGTTACGTTCTGGCACGCACGGATCTCATCGTTCCCGGCGGCATTGCGGCAAAAGGCTTCTGGATTGCTTTCGTGGTGAGCCTGACGATTGCGGCAGTTTTACTGTTTTTCCGTCTGCGAAAAACACAAGGGCAGCCGGACGATATTTTATTGGCAAGGCTGGAGAAATTGAAA","","","50889","MKLTTVKEYHIEAKKLIAIALPILLAQIAQNSMGLVDTIMAGRVSAVDMAAISVGASIWLPLVLFGYGLLLALPPTISYLNGSGQRRRIAHQVRQGIWIVLFSCIPLVWLIYSSDFVLQKMDMEQRLADITIGYLHAMVWGLPGYLLMVNFRCLNDGIAKTKPAMVITFLGLLINIPLNYIFIYGKLGVPAFGAVGCGIATAIVNWVMCLLMLAYCMRAKNQRDLKVFANIIERPNRRTLGKLLKLGFPIAMALCCEVALFALTSLFLSPLGADVVASHQIALNTGSFVFMLPMSLGMATTILVGQRLGEKSPEGAKQVTYSALVMGLFIAVITAFLIVILKEQIANIFVKDAEVIAMAGTLLLLAALYQFSDTIQVIIGSVLRGYKDTQAILYITLFCYWVVGMPLGYVLARTDLIVPGGIAAKGFWIAFVVSLTIAAVLLFFRLRKTQGQPDDILLARLEKLK","1133647","[FUNCTION] Functions as a Na(+)/drug antiporter (by similarity).[SUBCELLULAR LOCATION] Integral membrane protein. innermembrane (potential). [SIMILARITY] Belongs to the multi antimicrobial extrusion (mate) family. norm (tc 2.a.66.1.1) subfamily. ","probable multidrug resistance protein; multidrug-efflux transporter","Inner membrane, Cytoplasm","","
InterPro
IPR002528
Family
Multi antimicrobial extrusion protein MatE
PTHR11206\"[36-452]TMULTIDRUG RESISTANCE PUMP
PF01554\"[22-181]T\"[249-410]TMatE
TIGR00797\"[22-428]TmatE: MATE efflux family protein
noIPR
unintegrated
unintegrated
PTHR11206:SF7\"[36-452]TMULTIDRUG RESISTANCE PUMP
signalp\"[1-34]?signal-peptide
tmhmm\"[21-43]?\"[49-71]?\"[96-116]?\"[130-149]?\"[164-184]?\"[194-214]?\"[246-268]?\"[321-341]?\"[362-384]?\"[390-412]?\"[427-447]?transmembrane_regions


","No hits to the COGs database.","","Residues 115 to 203 match (4e-09) PD:PD387377 which is described as COMPLETE PROTEOME DNA-DAMAGE-INDUCIBLE PROBABLE TRANSMEMBRANE MULTIDRUG PLASMID EFFLUX RESISTANCE PUMP ","","","","","","","","","","","Mon Jan 6 16:51:46 2003","Fri Jan 24 13:37:57 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01675 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 249 to 410 (E-value = 2.2e-53) place AA01675 in the MatE family which is described as MatE (PF01554)","","","","","Morita,Y., Kodama,K., Shiota,S., Mine,T., Kataoka,A., Mizushima,T. and Tsuchiya,T. NorM, a putative multidrug efflux protein, of Vibrio parahaemolyticus and its homolog in Escherichia coli. Antimicrob. Agents Chemother. 42 (7): 1778-1782 (1998) [PubMed: 9661020].Brown,M.H., Paulsen,I.T. and Skurray,R.A. The multidrug efflux protein NorM is a prototype of a new family of transporters. Mol. Microbiol. 31 (1): 394-395 (1999) [PubMed: 9987140].","","Mon Jan 6 16:51:46 2003","1","","","" "AA01678","1134435","1133959","477","ATGACACCGGCGATTGACTTATTGAAAAAGCAAAAAGTCCCTTTCACCTTACATCATTACGATCACGACCCGGACAACACCCATTTCGGCGATGAAGCCGCCGAGAAATTAGGCATAAATCCCGATCAATCTTTCAAGACTTTATTGGTTGCGGAAAACGGCGATCAGAAAAAGCTCGCCTGTTTCGTGCTGCCCACCAGCCATCTGTTAAGCCTGAAAAAAGCGGCAAAAGCCTTGGGCGTCAAAAAAGTGGAAATGGCGGACAAAGACGCGGCACAAAAAAGTACCGGCTACTTGGTGGGCGGAATCAGCCCATTAGGTCAAAAGAAACGCCTAACCACCATCATTGAACAATCTGCGCTGAATTTCGACAAGATTTTCGTCTCCGGCGGTAAACGCGGATTAAGCGTTGAAATCGCCCCGCAGGATTTGGCGAAAATATTGAATGCGACGTTTTTGGATATTGTGGATGAGGGG","","","17236","MTPAIDLLKKQKVPFTLHHYDHDPDNTHFGDEAAEKLGINPDQSFKTLLVAENGDQKKLACFVLPTSHLLSLKKAAKALGVKKVEMADKDAAQKSTGYLVGGISPLGQKKRLTTIIEQSALNFDKIFVSGGKRGLSVEIAPQDLAKILNATFLDIVDEG","1133957","[FUNCTION] This protein may be involved in transcriptional controlor may also play a role in nucleotide or oligonucleotidebinding, the nature of which is yet to be determined. ","possible transcriptional regulator","Periplasm, Cytoplasm","","
InterPro
IPR004369
Family
Conserved hypothetical protein 11
TIGR00011\"[2-156]TYbaK_EbsC: ybaK/ebsC protein
InterPro
IPR007214
Domain
YbaK/prolyl-tRNA synthetase associated region
PF04073\"[10-155]TYbaK
noIPR
unintegrated
unintegrated
G3DSA:3.90.960.10\"[1-158]Tno description


","BeTs to 8 clades of COG2606COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG2606 is -----z----rlb-efgh-n-j----Number of proteins in this genome belonging to this COG is","","Residues 2 to 158 match (2e-60) PD:PD009524 which is described as PROTEOME COMPLETE TRANSCRIPTION REGULATION TRANSCRIPTIONAL REGULATOR REGULATORY YBAK YJDI ALL0659 ","","","","","","","","","","","Mon Jan 6 16:57:12 2003","Mon Jan 6 16:57:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01678 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 10 to 155 (E-value = 7.7e-74) place AA01678 in the YbaK family which is described as YbaK / prolyl-tRNA synthetases associated domain (PF04073)","","","","","Zhang,H., Huang,K., Li,Z., Banerjei,L., Fisher,K.E., Grishin,N.V., Eisenstein,E. and Herzberg,O. Crystal structure of YbaK protein from Haemophilus influenzae (HI1434) at 1.8 A resolution: functional implications. Proteins 40 (1): 86-97 (2000) [PubMed: 10813833]. Burns,D.M. and Beacham,I.R. Nucleotide sequence and transcriptional analysis of the E. coli ushA gene, encoding periplasmic UDP-sugar hydrolase (5'-nucleotidase): regulation of the ushA gene, and the signal sequence of its encoded protein product. Nucleic Acids Res. 14 (10): 4325-4342 (1986) [PubMed: 3012467].","","Thu Jan 23 11:01:04 2003","1","","","" "AA01679","1134496","1135296","801","ATGAGTACAAGATTAAATATCGCCCTGGTCGCCGAATTCGATTTATGCGAGAAATTGGCGGAGGCGTTGGAGCAGAGCAGTTTAGCCATTGAGACCCTGTCCGTGGTCGAACTTTTCCCTTTTAGCGAAGAACAGGGCATTCGATTCAACAACAAAAGCGTGGCGCAAATTCCGTTAGAGGAAACGGAATGGTCAGAATTTAATTATGTGTTATTTGCCGGTGAATTTGCTCATGCGACACATATTGCCAATACGGCGCAAGCGGGTTGTGTGGTGATTGATTTGAAAGGCGTGTGCGCTTCGCTAAATGATGTGCCGCTTATCGTCCCGAGCATTAACGATGAACAGTTGGTTTTATTGAAACGTAACATTGTGTCTTTGCCAGATCCGCAGGTTACACAATTCATTTTCTCTGTGTCACAATTTGCCCGCGAAAATACATTGTCTCAAGTGTTGGTTACGTCATTATTACCGGCATCTTATGTTGACAGCGACACCGTGAATAAACTTGCCGGACAAACCGCGCAACTATTGAACGGCATTCCGTTAGATGAAGATCAACAACGTTTGGCATTTGATGTGTTCCCGCTCGCCAAGCCGACCAAAAACCTTGCTGCACAAGTAGAAAAAATTTTTCCGCAACTGCCGAATGTGATTTTTCATCAGGCGCAAGTGCCGGTGTTTTATGGCATGGCGCAAATGGTCACGCTGCTTTCCGAGTATGAATTTGATGAACAGCCGCAGATCCAGGCATGGCAGGCGAAACTAAAGCCACCGCACCGGTGGTGTTGCATATTCCGG","","","31175","MSTRLNIALVAEFDLCEKLAEALEQSSLAIETLSVVELFPFSEEQGIRFNNKSVAQIPLEETEWSEFNYVLFAGEFAHATHIANTAQAGCVVIDLKGVCASLNDVPLIVPSINDEQLVLLKRNIVSLPDPQVTQFIFSVSQFARENTLSQVLVTSLLPASYVDSDTVNKLAGQTAQLLNGIPLDEDQQRLAFDVFPLAKPTKNLAAQVEKIFPQLPNVIFHQAQVPVFYGMAQMVTLLSEYEFDEQPQIQAWQAKLKPPHRWCCIFR","1135294","[CATALYTIC ACTIVITY] L-aspartate-semialdehyde + orthophosphate + nadp(+) = L-aspartyl phosphate + NADPH. [PATHWAY] Second step in the common biosynthetic pathway leading from asp to the cell wall precursor meso-diaminopimelate, tolys, to met, to ile and to thr. [SUBUNIT] Homodimer (by similarity). [SIMILARITY] Belongs to the aspartate-semialdehyde dehydrogenase family. ","aspartate-semialdehyde dehydrogenase; PTS system enzyme II A component","Cytoplasm","","No hits reported.","BeTs to 15 clades of COG0136COG name: Aspartate-semialdehyde dehydrogenaseFunctional Class: EThe phylogenetic pattern of COG0136 is aompkzyqvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is","","Residues 1 to 117 match (9e-09) PD:PD001262 which is described as DEHYDROGENASE ASPARTATE-SEMIALDEHYDE BIOSYNTHESIS COMPLETE PROTEOME OXIDOREDUCTASE ASADH ASA DIAMINOPIMELATE NADP ","","","","","","","","","","","Mon Jan 6 17:04:55 2003","Mon Jan 6 17:04:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01679 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01681","1135299","1135730","432","ATGGCAATTAGTCGGGATAAAAGCGCCGGCATTGATTCTTTTAAAGCCTTAGCGGAAAGCAAATTACGTTTAGGCGTTGGCGATAGCAAAGCGATGGCGTTGGGCAAAGGTGCGGAGAAGATCTTTGAATTGTCGGGCTATCAACAGCAGTTGAATGACAAAGTGGTGGTGAGAGCCGCGACGGTAAAACAGTTGATGTTATATTTATTGAATGGGGATGTGGATGCGGCAGTTGTCGGACGTTCAGGGGCATGGAAAGTGCGCGATAAAGTCACCATTTTGCCTAATCCGCAAGGCACCCCGGAAGAAAAAGTCACGGTAGCGTTGCTTTCTTCTTCGAAACATACGGCGGAAGCGCAACAATTATTTGATCTTTTTAAATCCGAGCAAGGTGTGAAATATTTTGTTGATGAAGGCTTCTTACCTGTTAAA","","","17300","MAISRDKSAGIDSFKALAESKLRLGVGDSKAMALGKGAEKIFELSGYQQQLNDKVVVRAATVKQLMLYLLNGDVDAAVVGRSGAWKVRDKVTILPNPQGTPEEKVTVALLSSSKHTAEAQQLFDLFKSEQGVKYFVDEGFLPVK","1135728","","molybdate-binding periplasmic protein","Periplasm","","
InterPro
IPR011587
Domain
Prokaryotic extracellular metal-binding protein
PD008688\"[62-142]TQ9CLU7_PASMU_Q9CLU7;


","No hits to the COGs database.","","Residues 1 to 144 match (1e-62) PD:PD589204 which is described as PROTEOME COMPLETE PERIPLASMIC MOLYBDATE-BINDING MODB HI1525 BINDING SIGNAL PRECURSOR ","","","","","","","","","","","Tue Mar 16 12:54:05 2004","Mon Jan 6 17:09:04 2003","","","","Tue Mar 16 12:46:09 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01681 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Tue Mar 16 12:46:09 2004","","","","","","","","","","","","","1","","","" "AA01682","1135708","1136502","795","ATGAAGGCTTCTTACCTGTTAAATAAAAGCCTTGGTTTAAAGTTAGCACTGATTCCGTTGATGATTTTGTTATTGATTGTGATAGGCTCGGTGCTTTCTTTAATGACGCAACTGGATTTTCATTTTTTCAAACAGGTGCTTTTTGATGCCGAGCTTCATTTTGCCTTGGGAATGTCGTTGGGTTCCTCTTTAATTTCGCTGTTTCTCGCATTTTGCCTATCTGTGCCGAGCGCGTGGTTGATGAGCCAAGTGCGGTTACCTTTGCAAAAGTTTATTGATACCTTTCTTGATTTACCCATGGTTTTGCCGCCTTTGGTCACCGGGTTAAGTTTGCTGCTTCTCTTTAATTCACAAGGCATTTTGAGTCAGTGGATTCCTTCGATCAGCCAATGGATTTTTAGCCCCGTTGGCATTGTGGTGGCACAAACGTATATCGTGTCGTCCATTTTATTGCGTGGCACAAGAGGGATTTTTTCGTCTTTTGATCAAGGCTATCGGTTTGCGGCATATAGTCTGGGGTTATCGCCTTTCAAAACCTTATGGAAAATTGAATTGCCCATGTGCTGGAAGCCATTATTAGGCTGTGTGATTTTGGCGTGGTCGCGGGCGATCGGGGAATTTGGCACCACGTTGATGCTTGCCGGTGCAACGCGATTTAAAACGGAAACCTTGCCGATGGCGGTGTATTTGAATATTTCCAGCGGCGATTTTGAAATCGCTATCGGCGCATCATTGTGGCTGCTGTTTATTTCCGCCTGTTTATTGATGCTTTTACGGATTGTGAATCGAAATGTG","","","29589","MKASYLLNKSLGLKLALIPLMILLLIVIGSVLSLMTQLDFHFFKQVLFDAELHFALGMSLGSSLISLFLAFCLSVPSAWLMSQVRLPLQKFIDTFLDLPMVLPPLVTGLSLLLLFNSQGILSQWIPSISQWIFSPVGIVVAQTYIVSSILLRGTRGIFSSFDQGYRFAAYSLGLSPFKTLWKIELPMCWKPLLGCVILAWSRAIGEFGTTLMLAGATRFKTETLPMAVYLNISSGDFEIAIGASLWLLFISACLLMLLRIVNRNV","1136500","","molybdate ABC transporter protein","Inner membrane, Cytoplasm","","
InterPro
IPR000515
Family
Binding-protein-dependent transport systems inner membrane component
PF00528\"[52-265]TBPD_transp_1
PS50928\"[56-258]TABC_TM1
InterPro
IPR006469
Family
NifC-like ABC-type porter
TIGR01581\"[34-257]TMo_ABC_porter: NifC-like ABC-type porter
noIPR
unintegrated
unintegrated
signalp\"[1-33]?signal-peptide
tmhmm\"[15-35]?\"[54-74]?\"[95-115]?\"[131-151]?\"[196-216]?\"[239-261]?transmembrane_regions


","BeTs to 19 clades of COG0555COG name: ABC-type sulfate/molybdate transport systems, permease componentsFunctional Class: PThe phylogenetic pattern of COG0555 is aompkz-q-dr-bcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 7.6e-06) to 1/1 blocks of the IPB000515 family, which is described as \"Binding-protein-dependent transport systems inner membrane component\". Interpro entry for IP:IPR000515. IPB000515 167-186 7.7e-06","Residues 78 to 152 match (1e-18) PD:PD002244 which is described as PROTEOME COMPLETE PERMEASE SULFATE ABC SYSTEM TRANSMEMBRANE MEMBRANE TRANSPORTER TRANSPORTER ","","","","","","","","","","","","Mon Jan 6 17:12:04 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01682 is paralogously related to AA01780 (5e-20), AA00699 (2e-11), AA01644 (4e-10), AA02352 (4e-06), AA01948 (5e-06), AA02719 (9e-06), AA01950 (3e-05) and AA02720 (1e-04).","","","","","","Residues 52 to 265 (E-value = 2.2e-09) place AA01682 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component (PF00528)","","","","","","","","1","","","" "AA01684","1136442","1137119","678","GTGGCTGCTGTTTATTTCCGCCTGTTTATTGATGCTTTTACGGATTGTGAATCGAAATGTGTAATGATGTTGAAGATTGAACATTTATCTGCCGGCATTCTGCGAAATATTTCCCTGTCGGTAGAGGCAGGCGAATGTGTCGCCATTGTGGGGGAATCGGGCAGCGGCAAAACCACGTTATTAAACGCCATTGCCGGTTATATTGATTATGCCGGCACCATCCGATTAGCCAATCAATCGTTGGACAACTTGGCGCCATGGCAACGCAATTGTCGTTATTTAAATCAGCGGCTTTATTTGTTTCCCCATAAAACCGTTAGCGGCAATTTAGCGTTGGCGAATCCTGATGCCACATTCGAGGCACAAATCGCCTTATTGGAAAAATTAAAAATTGCCCATTTAATCAATCGCTATCCTCATCAATTATCCGGCGGAGAACAACAACGGGCGGCATTTGCCCGCGTGTTAATTAACCCACCGAATTTGTTATTGCTTGATGAGCCTTTTTCTTCCCTGGATTGGCAAACCCGTGTCCATATTTGGCAGATGTTAAACGCATTAAGGCAGGAATATCAAATGACGACCCTTTTGGTCACGCATGAACTCAAAGAAGCCGAATATTTGGCAAACCGAACAATTTCGCTTAAGCAAGGACAATTTCTTGATAAGGACAAGCCA","","","25443","VAAVYFRLFIDAFTDCESKCVMMLKIEHLSAGILRNISLSVEAGECVAIVGESGSGKTTLLNAIAGYIDYAGTIRLANQSLDNLAPWQRNCRYLNQRLYLFPHKTVSGNLALANPDATFEAQIALLEKLKIAHLINRYPHQLSGGEQQRAAFARVLINPPNLLLLDEPFSSLDWQTRVHIWQMLNALRQEYQMTTLLVTHELKEAEYLANRTISLKQGQFLDKDKP","1137117","","ABC transporter, ATP-binding protein; possible ATP-binding component of sulfate permease A protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[141-181]TQ9CLU5_PASMU_Q9CLU5;
PF00005\"[44-218]TABC_tran
PS50893\"[18-226]TABC_TRANSPORTER_2
PS00211\"[142-156]?ABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[43-219]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[21-221]Tno description
PTHR19222\"[24-219]TATP BINDING CASSETE (ABC) TRANSPORTER


","No hits to the COGs database.","Significant hit ( 1.5e-30) to 2/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 33-79 2.3e-16 IPB001140B 139-177 8.2e-13Significant hit ( 7.2e-05) to 1/4 blocks of the PR00364 family, which is described as \"Disease resistance protein signature\". Prints database entry for PR:PR00364. PR00364A 46-61 7.5e-05","Residues 125 to 200 match (5e-07) PD:PD241888 which is described as ATP-BINDING PROTEOME COMPLETE ABC TRANSPORTER HOMOLOG COBALT COMPONENT A2 EXPORTER ","","","","","","","","","","","Tue Mar 16 13:34:25 2004","Tue Mar 16 13:49:35 2004","","","Tue Mar 16 13:49:35 2004","Tue Mar 16 13:34:25 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01684 is paralogously related to AA01051 (1e-29), AA01867 (3e-29), AA01656 (2e-28), AA02718 (3e-28), AA01645 (2e-27), AA01779 (8e-26), AA02080 (3e-25), AA01616 (7e-25), AA00700 (1e-23), AA01524 (2e-23), AA02353 (8e-23), AA00858 (2e-22), AA02609 (5e-22), AA02440 (9e-22), AA02899 (6e-21), AA00415 (3e-20), AA02606 (5e-20), AA02805 (2e-19), AA01820 (3e-19), AA01961 (7e-19), AA01510 (2e-18), AA02320 (6e-18), AA01757 (6e-18), AA01422 (1e-17), AA01824 (4e-17), AA02898 (5e-17), AA02152 (3e-16), AA01569 (3e-16), AA02550 (4e-16), AA02140 (4e-16), AA01947 (1e-15), AA01393 (5e-15), AA00591 (4e-14), AA02573 (7e-14), AA00207 (7e-14), AA02324 (1e-13), AA02484 (2e-13), AA01456 (3e-13), AA02225 (6e-13), AA00799 (1e-12), AA00933 (2e-12), AA02786 (3e-11), AA01568 (2e-10), AA01509 (4e-10), AA00061 (5e-10), AA02331 (2e-09), AA01555 (2e-08), AA00751 (3e-08), AA02146 (4e-08), A02145 (5e-07), AA02642 (3e-06), AA00934 (3e-05), AA01291 (2e-04) and AA02226 (0.001).","Tue Mar 16 13:34:25 2004","","","","","Residues 44 to 218 (E-value = 2.9e-56) place AA01684 in the ABC_tran family which is described as ABC transporter (PF00005)","Tue Mar 16 13:34:25 2004","","","","","","Tue Mar 16 13:34:25 2004","1","","","" "AA01685","1137119","1137976","858","ATGATTTACTTTTCAGACAAAGAACTTAATGATTTTTTATTGGAAGATATTTACCGAGGTGATCTCACTACCCATGCTTTAGGATTGGATGATGTTCCTGCAAGGATTTTGTTTAAGCGTAAAAACACAGGAAGAGTGGCGGGCGTGAGCATCGCGGAAAAGCTGTTACGTAAGCTGGATGTTCAAGTGAAAGTTCATATTGCGGACGGTGAAAATGTGGCTGCCGGCACATTGCTGTTGAGTGGAGATGGGCATGCCGATAAATTACATCAGGCGTGGAAAGTGGTTCAACTGGTGTTGGAATGGTCTTGTGGCGTGGCGCAATACACCGCCGAAATGATTGCCAATGCGAAAGCACTCAATCCACAGGCTATTGTGGCGTGTACCCGTAAAAGTATTCCGAATACGCGTAAATTGGCAACTGCTGCGGTGCTTGCCGCCGGCGGGCATATTCATCGCCAGGGACTAAGCGAAACCTTACTTGTGTTTACCAACCATCGCAATTTGCTGGATAACCCCACTGATTATCAAGCAATCGTTTCCCAATTGAGACTGGAAGCTCCGGAAAATAAAATCACCTTGGAAGCTGATAATTTTTCGCAATTTGAACAAATGCTTGCAGCCGAACCGGATATTATTCAGTTGGATAAATGGTCGCCGGAACAGGTTCAACAGGCATTGGCTTTGTTAAAAAAGCAAAGTAAAAAAACGCTCCTTTCTGTTGCCGGCGGGGTGAATAAAAACAACATAGCAGATTATGCCAAGTTAGGGATAAATTTATTTATCATCTCCGTGCCTTACTATGCACCGCCGGAAGATATTAAAGTGGTGATTGAGCGGATGCAGAACAAAAACACT","","","31586","MIYFSDKELNDFLLEDIYRGDLTTHALGLDDVPARILFKRKNTGRVAGVSIAEKLLRKLDVQVKVHIADGENVAAGTLLLSGDGHADKLHQAWKVVQLVLEWSCGVAQYTAEMIANAKALNPQAIVACTRKSIPNTRKLATAAVLAAGGHIHRQGLSETLLVFTNHRNLLDNPTDYQAIVSQLRLEAPENKITLEADNFSQFEQMLAAEPDIIQLDKWSPEQVQQALALLKKQSKKTLLSVAGGVNKNNIADYAKLGINLFIISVPYYAPPEDIKVVIERMQNKNT","1137974","From InterPro: IPR002638Quinolinate phosphoribosyl transferase (QPRTase) or nicotinate-nucleotide pyrophosphorylase EC: 2.4.2.19 is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to give rise to nicotinic acid mononucleotide (NaMN), pyrophosphate and carbon dioxide. Unlike Nicotinate-nucleotide pyrophosphorylase , this family also includes the molybdenum transport system protein ModD. ","molybdenum ABC transporter, ATP-binding protein","Cytoplasm","","
InterPro
IPR002638
Family
Quinolinate phosphoribosyl transferase
PD003988\"[126-258]TMODD_PASMU_Q9CLU4;
PF01729\"[106-277]TQRPTase_C
PF02749\"[17-104]TQRPTase_N
InterPro
IPR006242
Family
Putative molybdenum utilization protein ModD
TIGR01334\"[2-278]TmodD: modD protein
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[109-278]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.90.1170.20\"[9-108]Tno description


","BeTs to 18 clades of COG0157COG name: Nicotinate-nucleotide pyrophosphorylaseFunctional Class: HThe phylogenetic pattern of COG0157 is aom-k-yqv-rlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 4.5e-14) to 1/1 blocks of the IPB002638 family, which is described as \"Quinolinate phosphoribosyl transferase\". Interpro entry for IP:IPR002638. IPB002638 130-166 4.4e-14","Residues 129 to 221 match (2e-08) PD:PD235616 which is described as PYROPHOSPHORYLASE GLYCOSYLTRANSFERASE MODD 2.4.2.- TRANSFERASE ","","","","","","","","","","","Tue Mar 16 13:18:35 2004","Tue Mar 16 13:14:43 2004","","","Tue Mar 16 13:18:35 2004","Tue Mar 16 13:14:43 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01685 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Tue Mar 16 13:14:43 2004","","","","","Residues 106 to 277 (E-value = 1.3e-63) place AA01685 in the QRPTase_C family which is described as Quinolinate phosphoribosyl transferase, C-terminal domain (PF01729)","Tue Mar 16 13:14:43 2004","","","","Maupin-Furlow JA, Rosentel JK, Lee JH, Deppenmeier U, Gunsalus RP, Shanmugam KT.Genetic analysis of the modABCD (molybdate transport) operon of Escherichia coli.J Bacteriol. 1995 Sep;177(17):4851-6.PMID: 7665460Walkenhorst HM, Hemschemeier SK, Eichenlaub R.Molecular analysis of the molybdate uptake operon, modABCD, of Escherichia coli and modR, a regulatory gene.Microbiol Res. 1995 Nov;150(4):347-61.PMID: 8564363Grunden AM, Shanmugam KT.Molybdate transport and regulation in bacteria.Arch Microbiol. 1997 Nov;168(5):345-54.PMID: 9325422","","Tue Mar 16 13:18:35 2004","1","","","" "AA01686","1138053","1138196","144","GTGCGGTTAAAAAACAAATTAAAAATTCACCGTACTTTTTATTCCCCTCCACAATTCAACAAAATAGAATTTATACCCTTAAATAAATTGCGGATAAACCGCTCTTTTTCTTTGGAAAATATCGGATTTATTGCCATTTTCAGG","","","5801","VRLKNKLKIHRTFYSPPQFNKIEFIPLNKLRINRSFSLENIGFIAIFR","1138196","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 14:54:54 2004","Thu Feb 26 14:54:54 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01686 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 14:54:54 2004","","","","","","","","","","","","","1","","","" "AA01687","1138183","1139721","1539","TTGCCATTTTCAGGTAACTTTCCTTTTCGGTTTTGGCGGAAAATACGTTATAATCCCGACCAATTTTTTATCGATAAAATGACCGAGATTTCTATGTTAAAAAAAGTGACCGAAAGTTTATTGGTGCAGAGCCATTTGACGCTTGCGGATTTGCCGAATGTGTTTGATACCTTGGCGCAGCGCAATGTGGATTATGCGGATTTGTATTTTCAGCTCAGTCAGGACGAGAACTGGGTGTTGGAAGACGGGATTATTAAGGAAGGCGGGTTTCATATTGATCGCGGCGTGGGCGTGCGTGCGGTGAGCGGTGAGAAAACCGGTTTCGCTTATTCCGACCAGATTAATTTAGCCAATTTACAGCAATGTGCGCAGGCAGTGCGTGGCATTGCGCAACCTTCTCAATGTAATTTTATTCTGCCGGTGAAGTTTAACCCGGTGGACGCGACTTTGCGTTATCAGCCGATTAACCCGTTGCACAGTTTAAGTCAGGAACAAAAAATCGAACTCTTGCGTTTGGTGGACAGAACCGCCCGTGCGGAAGATCCGCGTGTGGTGCAGGTGAACGCCGGGTTAAGCATGGTGTATGAAGAAATGCTGGTAGCGGCGACCGACGGCACGTTAGCGGCGGATATTCGTCCGTTGATTCGGTTGTCCGTTTCCGTGTTGGTGGAACAAGACGGCAAACGTGAACGGGGCGGCGCAGGCGCAGGCGGACGTTTTGCTTTGGATTGGTTCTTTGAAAACTATAACGGCGAGCAAAGTGCGGTCTATTTTGCCAAAGAAGCGGTGCGCCAGGCGTTGGTGAATTTAAGCGCGGTTGCGGCACCGGCAGGGTTAATGCCGGTGGTGTTAGGCGCAGGTTGGCCCGGCGTGTTGTTGCATGAGGCGGTTGGACACGGTTTGGAAGGCGATTTTAATCGCAAAGAAAGCTCTTTGTTTACCGGCAAAATCGGTGAATTGGTGACATCGCCGCTGTGTACCATTGTGGATGACGGCACGTTAATGGATCGTCGCGGTTCTGTTACCGTGGACGATGAAGGTGTGCCGAGCCAACATAATGTTTTAATTAAAAACGGCATTTTGCAGAAATATATGCAGGATAAAATGAATGCCCGTTTGATGGGCGTGCAACCGACAGGGAACGGTCGCCGTGAATCTTATGCTCATTTGCCGATGCCGCGCATGACCAACACTTATATGCTGGCGGGCAAAGATAAATTTGAGGATTTGGTGGCATCGGTGGAACAAGGGATTTTCGCACCGCACTTTGGTGGCGGACAAGTGGATATTACCTCCGGCAAATTTGTGTTTTCCACCTCTGAAGCCTATTTGATCGAAAAAGGAAAAATCACCAAGCCGGTGAAAGGGGCAACCCTCATCGGCAGCGGCATCGAAGTAATGCAAAATGTGTCTATGGTTGCCGACGAAGTGGAATTGGATCACGGTGTAGGCACTTGCGGTAAAGAAGGTCAAAGCGTACCGGTAGGCGTGGGGCAGCCGGCGTTGAAAATCGATCAGATTACCGTGGGCGGCACAAAC","","","55940","LPFSGNFPFRFWRKIRYNPDQFFIDKMTEISMLKKVTESLLVQSHLTLADLPNVFDTLAQRNVDYADLYFQLSQDENWVLEDGIIKEGGFHIDRGVGVRAVSGEKTGFAYSDQINLANLQQCAQAVRGIAQPSQCNFILPVKFNPVDATLRYQPINPLHSLSQEQKIELLRLVDRTARAEDPRVVQVNAGLSMVYEEMLVAATDGTLAADIRPLIRLSVSVLVEQDGKRERGGAGAGGRFALDWFFENYNGEQSAVYFAKEAVRQALVNLSAVAAPAGLMPVVLGAGWPGVLLHEAVGHGLEGDFNRKESSLFTGKIGELVTSPLCTIVDDGTLMDRRGSVTVDDEGVPSQHNVLIKNGILQKYMQDKMNARLMGVQPTGNGRRESYAHLPMPRMTNTYMLAGKDKFEDLVASVEQGIFAPHFGGGQVDITSGKFVFSTSEAYLIEKGKITKPVKGATLIGSGIEVMQNVSMVADEVELDHGVGTCGKEGQSVPVGVGQPALKIDQITVGGTN","1139719","[FUNCTION] Suppresses inhibitory activity of CsrA","TldD protein","Cytoplasm","","
InterPro
IPR002510
Family
Peptidase U62, modulator of DNA gyrase
PF01523\"[64-364]TPmbA_TldD


","BeTs to 18 clades of COG0312COG name: Predicted Zn-dependent proteases and their inactivated homologsFunctional Class: RThe phylogenetic pattern of COG0312 is a-mpkz-qvdr-bcefghsn-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 6.3e-32) to 2/2 blocks of the IPB002510 family, which is described as \"Putative modulator of DNA gyrase\". Interpro entry for IP:IPR002510. IPB002510A 290-302 1.2e-06 IPB002510B 339-381 7.1e-24","Residues 395 to 510 match (3e-54) PD:PD002987 which is described as COMPLETE PROTEOME TLDD PMBA PROTEASE MATURATION HOMOLOG GYRASE DNA MODULATOR ","","","","","","","","","","","Tue Jan 7 10:19:23 2003","Tue Jan 7 10:19:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01687 is paralogously related to AA00139 (1e-14).","","","","","","Residues 64 to 364 (E-value = 1.4e-95) place AA01687 in the PmbA_TldD family which is described as Putative modulator of DNA gyrase (PF01523)","","","","","Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H., Horiuchi,T., Sekimizu,K. and Miki,T. Evidence for involvement of Escherichia coli genes pmbA, csrA and a previously unrecognized gene tldD, in the control of DNA gyrase by letD (ccdB) of sex factor F. J. Mol. Biol. 256 (3), 483-502 (1996) PubMed: 8604133.Allali N, Afif H, Couturier M, Van Melderen L.The highly conserved TldD and TldE proteins of Escherichia coli are involved in microcin B17 processing and in CcdA degradation.J Bacteriol. 2002 Jun;184(12):3224-31.PMID: 12029038","","Tue Feb 4 17:15:34 2003","1","","","" "AA01688","1139775","1145543","5769","ATGCAGAGCAAAATAAAATTTTCAGTACTTGGCGCACTCGTGCTGGCTGCCGCAGCAGGTGGTGCTTATTGGTATCAACACCAAAAAACCGATGGCGGCAATACGATTAAAGTGAAATTTAATCCGATTGAGCAAACGTCTTACGGTCAATCCGGTGAAGGGCAAACGACAAATACGATTTACCCGTTAAGCGTGGAATTCAGCGGCGCGGCGGCACCTATTGACAAAGTAAAAAGCGAAATCACCCAGGGTATAAAAATGGAACCTGCCATTGAGGGGAAATGGATCTGGTCAAGCGACTATTTGCTTAGCTTTACCCCGACGCAGGATTGGCCGACAGGGCAAGAATATAAAATTACCTTGGATAAGAAAGTATTAAATCCAAGTTTGACTTACGCGAAATCCGTTACGGATACCCATTCCGTGAAAACTCAGCCTTTTAGTGTGGTGGAATCCGAATCGGAATTTTATAAGGATCCGAATTTATCCCATATTCGCCATGCGTTGACTCATTTGGTGTTTTCCAACCCGGTGGATCCGAAAGATTTGGAAAAAGCGGTTGAAGTGAACTTGGTGCATAAAAATCAAGATCAGTCGCTGAATTTGATTAACCCGTTGAAATTTAAAATTCGTTATTCCGATAATAAGCTGGAAGCTTGGATTAGGTCCGATGAACTTTCTTTGTCCACCCAGCCGAATCAATTTGTACAGACCAAAATCAGCCGGGCATTACGCGCGAAAACCGGGGCGAATACTTTAGAAAGAGAAATTACCAAACTGGTGCAAGTGCCGTCGAAATATAGTCTGCAAAATTCCCACAACAGCTTCAAAATCGTTAACAATCAGAAAAATGAAGCAGATCAGGTATTAACTTTCAACTTTAATTATGGGGTGAAAGGGAAAGACATTGCCGATAATTTAAGCGCAGTGTTACTGCCTGAACCGCCGGAAGGTAAAAGCTGGGAAGTGGAAAAATTAACCGAGGCCGTAGTGAAGCGTGGTGAACGCATTCAACCGGAGCTTATTCCAAGTGAACGTCCGTATGCCAACAATCAATCCTTCCGTTTTAATATTCCGGAAGGGCGTTGTCTTTATTTGCAGTTGGATAATAAATTCACCGCATTAGGCGGCTACCAATTGAAAAAAGCTATCGGTAGCCTGGAATGTGCACCGAATTATCCGACTTATGTGAACTTTGTGGGGAAAGGTTCCTTATTGTCTCAATACGGCGATGGCAAAGTTACACTTGCTGTGCGTAATACAGATCGTGTGCGATTGGATATTGGTCGTGTGCAGGCGGAACAATTGCGCCATGTGGCAAATTTGAATAGCAAAAATTTCCAAAAACCGGATTTAGGCAACTTGAAATTTGATGACATCGCAACCTTTAAAACGGAAACTCTGACCGTTGCCAATCGCGATCCTCGCAAATCCGATTACCTCAGCGTGGATTTATCACAAAGAGGTTTACCGAAGCAAGGGATCTTCTGGGTGAAGGCAAGTGCGGTCAATGCTAAGGATAAATCTGAAGGCGGTAGTTTAAAAGACCGTGGTGATGACGATGGCTATTATTTTGATGCTGATCCGGATTCACAAAAAAGTGATTACCGTTTAATCATCTTGACAGATTTAGGTATCATTACCAAAAAAGCGGCGGACGGCACACAATCCGTATTTGTACAATCAATTGCAAGCGGCGCGCCGGTTTCAAGTGCTCTGGTGAAAGTGATTTCCCGCAATAACACCGTTATCGCCAGCCAATACACTAACAGACTTGGCGTTGCCCAACTCCCTTCTTTAGAGAATTATAAGCAGGAGCTTGAGCCGGTGATGTATTTGGTGGCACGCGGGCAAGATCAGTCATTCTTGCCGATTGATAAATCCGACCGTACATTAGATTTCTCCCGTTTTGATATTCGCGGTCAGGAAATGTCACAGGAACAAAATGCTATTAAAACGTTCCTGTTTAATGATCGTGGTATTTATCGCCCGGGCGAATCTGTCCATATTGGCATGATCAGTAAGGCCTTGGATTGGAAGAAATCCTTAGCCAATGTGCCGTTGACGTTGGAAGTTACCTCGCCGTCCGGTAAAACCCAATGGCAAAAGAATATTCGTGTGAGCGAAAGCAGCTTTAATGAGCTGACTTACCCGCTATCGGATAGTGCGGAAACCGGCGAATGGCTGGCACATATTTATATTGGTCAGCAACAGGAGAAAATTGATGTAGGTTCCATGACATTCCAAGTGCAGGAATTTGAACCGGATACCTTAAGAATCAATACGATGTTTGATAACAGCCAACAGCTGGGCTGGGTTTCGCCACAAGATTTGAATGCTACCGTGCATTTAACCAATTTATTCGGCACACCGGCACAAAAACGCAGAGTGGCAGCGAATATCATGCTGCATGCTATTTTCCCAAGTTTTCCGCAGTATAAAAATTATCAATTCTATGATAATCAGCGTAACAAAAATGCCATTTTGTTAGAAACTGAATTGCAGGATCAAACGACAGATAATAACGGTAATGCGATTTTTGCCTTGAATTTGGAGCATGAAGCGGAAAATACCGTACAAATGTTGTATTTCACGGCGGATGGTTATGAAAATAACAGCGGTCGCGGTGTGTCTAAAGTGCAATCGATATTGGTTTCTGCGCAACCTTGGTTAGTGGGCTACAGCAGCGCGCAAGACTTAAATTATTTAAGAGAAAAGAGCGAGAGCAAGGTAAATTTAATCGCTATTAATCCAAGCCTGCAAAAAACCTCAGTGCGAGGATTAAGTGCGGTGCTAATGGAACGTAAATATGTTTCCGTGCTAACCGAGCAGCGTTCCGGTGCCTATAAATATGAATCCAAAATGGTAGAAAGCCAGCTGGATGAAAAACCGCTTAATATCGATCAGAACGGTTCGGATTTTGCTTTGAATACCGAGCGTAGCGGCGATTTCGTGTTAGTGATTAATAATCAATACGGCGAAACCGTCAACCGTATTCCTTATACGGTTATCGGTAACAGCAATGTTACGGTTGCCATGGATAAAAACACCGAACTTAAGTTGAATCTGAACAAAAAACAATTTATGCCGGGTGAAGAAATCGAAGTAGCAATTAACGCGCCTTATGCAGGCAGCGGTTTAATCACTATCGAACGCGAGCGTGTGTATACTCATAAATGGTTTAAATCCACAACCAATCGTTCGGTACAAAAAATCAGAATCCCGGAGAATTTTGAAGGCAGCGGTTACATTAATGTGCAATTCTCCCGCGATATGCAATCTGATGACATTTTCACCAGCCCGCTAAGTTATGGTGTGGCACCATTTAGTGTTAATGTAGATAACCACCGTTTGAAGGTAAATCTGAGTGCGCCGCAACAAGTGAAATCCGGCGAGAAAGTCAAATTTACGTTATCTACTGACAGACCAAGTAAAGCCGTGATTTATGCGGTGAACGAAGGCATTTTGCAGGTAGCGGGGCATAGACAGGAGGATCCGTTACAATTTTTCTTCCCGAAATATGCGTTGCAAGTGGAAACTTTGCAAATTCTGGATCTGATTTTGCCGGAATTCCGTAAAGTGTTGCAGTTTGCGCAAACCGGTGGTGACGCCGAAGAGACAGCTGCACTAGCAAAGGCCATCGCAGCGAATACTAATCCGTTTAAACGTAAAACCGACAAACCGGCGGTGTTCTGGTCAAATATTATCGATGTGGACGGCACAAAAACCGTGACTTATCAAGTGCCGCAAGGTTTTAACGGCAATCTTAAAGTGATGGCGATTGCTGTGACAAACGATGGTTTGCAAATGAATATCGGTCAAACGGAAACCTTAGTGCGTGATGATATGGTTTTGTCACCAACTGCTCCGATTACTTTAGCGCCGAATGACGAAACCAAAGTGAGTCTGACTGTTTCCAATAACACGAAAAGCAAGCAAAACGTTCTGGTTCAACTCAATGTGGCACCGCAATTCCAAGTGTTGAGTAATGCGCAAACCGCGATTATGTTGGAGCCGATGAGCGAAGGTGTCGTGAATTTCCAGTTGAAAGCCACGGACCAGCTCGGTAGCGGTATTTTATACTTCACTGCCGCGTATTTGGATGAACAGCAACAACCGGCGCAGGTTGAGCGAAAATACGGTATTTCCGTTCGTCCATTAACGGCAAAACAGCAATTCATCAAAGTGGGTGAAGTGGCGGCGAATCAACAGGCTCAAAGCGGCTTTCCGAATGTATTATTCCCGCAACTACGCGAGCAAACCGCGCTGATTTCGCCTGCACCGTTAGCCTTGGCGCAAGGCATAAGCAGTTATTTAGGCAATTACGACAACTTATGCACGGAGCAGATTATCAGCGCTGCCATACCGAATTTGTTATTTGCCAATAATCCTGAATACCAAAGCTTGCTCGGTATCTTGTCGCAAGTGGGAGATAACACCGCGACACAAAGTAGCAAACAGCAAATTCAGAGTAATCTGAACCGCGTCTTTAGTTTGTTGCCGGCACGTCAAACTGTTAACGAAGGTTTTGGCTTGTGGTCGGGATTAGATGAGGATGACGGATTTTTAACCGCTTATGTGGCACATTTCCTAATTGAAGCGCAAGAACACGGTGTGCAATTGCCGGCGGCATGGATTACGCCAAATGGTTTATTTAATAAATCCATCACAGCGTTAGAGCGTTTAAGCCGCCCTGAAAGTGAAGATGATTTAGCCATGTTGCGCCAGCGTGCTTATGCTACTTATCTATTAGCACGTTTAGGGCAAGTGCCAAGTGACAGTTTGCTGTCTATTCGCAGCCTATTGGAACGCAATTTCAAAGCGGAAGAATGGCGATTTGATTTAACTGTAGCTTGGCTGGCAGGCGCTTATCAATTGGTGAAACAGGAAGAAGATGCGGATAATCTAATTAGCAATGTGATGGCGAAATTTAATAATTTGCAGCCTAAAAACGCGTGGTTCTACCGAGATTATTTGGATCCGTTGATTGAGAAGGGGGCTGTTTTGTATGTATTAGCGCGTCATTTCCCTGAACAGGCGGAACAATTATCCGACACCTTATTAAGTAGCATCGTGAAGGATTTAAACGACAATCGTTATAACACCTTGTCTTCCGCTATGGTGTTGTTGGCGTTAGATGCTTATAGTAAGCAACATGCCGAACAAATTGCAAACCTGCATATTCAGCAGGACGGGCAAAATATTGGCGGCGTGCAGGGGGCCTTCGTGTTAGCCAATATCAATGCGGATAAAGCGCAATTAAATTTCGTCAACCAAAGCACGCAAAAAGCCTGGTATGCCATTAGTCAATCCGGTTATGTACAGCAGGCGCCTGCCGAAGCAATTAAAAACGGTGTGGAAATCGACCGCACTTATTTAGATCAAGAAGGCAAACCGGTGACTTCAGTGAAACTTGGCGATGTGATTAACGTACAAGTTAGGGTGCGTTCATTACAAAATGAACTGGATAATATGGTGATTACCGATCTCTATCCGGCAGGTTTTGAAGTGGTGAACAGTAATGGCGATGAAACCGTGAATGTCAAAGAAGGTGACATAATTTATATGTTTAACTTCATTCATCGCGATTTGCGTGAAGATCGTATGTTGAGTTACGGTTCAGTGGGTGATACTACTACGGTGATTAACTACCAATTAAAAGCCGTAAACGCGGGTAAATTCCAAATTCCGCGCGCCTATACGGAAAATATGTACAACCGCACGGTGAACGCACAGTCTGCCGATAAAGGTTATATTGAAGTTATACAA","","","214722","MQSKIKFSVLGALVLAAAAGGAYWYQHQKTDGGNTIKVKFNPIEQTSYGQSGEGQTTNTIYPLSVEFSGAAAPIDKVKSEITQGIKMEPAIEGKWIWSSDYLLSFTPTQDWPTGQEYKITLDKKVLNPSLTYAKSVTDTHSVKTQPFSVVESESEFYKDPNLSHIRHALTHLVFSNPVDPKDLEKAVEVNLVHKNQDQSLNLINPLKFKIRYSDNKLEAWIRSDELSLSTQPNQFVQTKISRALRAKTGANTLEREITKLVQVPSKYSLQNSHNSFKIVNNQKNEADQVLTFNFNYGVKGKDIADNLSAVLLPEPPEGKSWEVEKLTEAVVKRGERIQPELIPSERPYANNQSFRFNIPEGRCLYLQLDNKFTALGGYQLKKAIGSLECAPNYPTYVNFVGKGSLLSQYGDGKVTLAVRNTDRVRLDIGRVQAEQLRHVANLNSKNFQKPDLGNLKFDDIATFKTETLTVANRDPRKSDYLSVDLSQRGLPKQGIFWVKASAVNAKDKSEGGSLKDRGDDDGYYFDADPDSQKSDYRLIILTDLGIITKKAADGTQSVFVQSIASGAPVSSALVKVISRNNTVIASQYTNRLGVAQLPSLENYKQELEPVMYLVARGQDQSFLPIDKSDRTLDFSRFDIRGQEMSQEQNAIKTFLFNDRGIYRPGESVHIGMISKALDWKKSLANVPLTLEVTSPSGKTQWQKNIRVSESSFNELTYPLSDSAETGEWLAHIYIGQQQEKIDVGSMTFQVQEFEPDTLRINTMFDNSQQLGWVSPQDLNATVHLTNLFGTPAQKRRVAANIMLHAIFPSFPQYKNYQFYDNQRNKNAILLETELQDQTTDNNGNAIFALNLEHEAENTVQMLYFTADGYENNSGRGVSKVQSILVSAQPWLVGYSSAQDLNYLREKSESKVNLIAINPSLQKTSVRGLSAVLMERKYVSVLTEQRSGAYKYESKMVESQLDEKPLNIDQNGSDFALNTERSGDFVLVINNQYGETVNRIPYTVIGNSNVTVAMDKNTELKLNLNKKQFMPGEEIEVAINAPYAGSGLITIERERVYTHKWFKSTTNRSVQKIRIPENFEGSGYINVQFSRDMQSDDIFTSPLSYGVAPFSVNVDNHRLKVNLSAPQQVKSGEKVKFTLSTDRPSKAVIYAVNEGILQVAGHRQEDPLQFFFPKYALQVETLQILDLILPEFRKVLQFAQTGGDAEETAALAKAIAANTNPFKRKTDKPAVFWSNIIDVDGTKTVTYQVPQGFNGNLKVMAIAVTNDGLQMNIGQTETLVRDDMVLSPTAPITLAPNDETKVSLTVSNNTKSKQNVLVQLNVAPQFQVLSNAQTAIMLEPMSEGVVNFQLKATDQLGSGILYFTAAYLDEQQQPAQVERKYGISVRPLTAKQQFIKVGEVAANQQAQSGFPNVLFPQLREQTALISPAPLALAQGISSYLGNYDNLCTEQIISAAIPNLLFANNPEYQSLLGILSQVGDNTATQSSKQQIQSNLNRVFSLLPARQTVNEGFGLWSGLDEDDGFLTAYVAHFLIEAQEHGVQLPAAWITPNGLFNKSITALERLSRPESEDDLAMLRQRAYATYLLARLGQVPSDSLLSIRSLLERNFKAEEWRFDLTVAWLAGAYQLVKQEEDADNLISNVMAKFNNLQPKNAWFYRDYLDPLIEKGAVLYVLARHFPEQAEQLSDTLLSSIVKDLNDNRYNTLSSAMVLLALDAYSKQHAEQIANLHIQQDGQNIGGVQGAFVLANINADKAQLNFVNQSTQKAWYAISQSGYVQQAPAEAIKNGVEIDRTYLDQEGKPVTSVKLGDVINVQVRVRSLQNELDNMVITDLYPAGFEVVNSNGDETVNVKEGDIIYMFNFIHRDLREDRMLSYGSVGDTTTVINYQLKAVNAGKFQIPRAYTENMYNRTVNAQSADKGYIEVIQ","1145541","","conserved hypothetical protein; possible membrane protein","Outer membrane, Periplasm","","
InterPro
IPR002890
Domain
Alpha-2-macroglobulin, N-terminal
PF01835\"[539-823]TA2M_N
InterPro
IPR011625
Domain
Alpha-2-macroglobulin, N-terminal 2
PF07703\"[1015-1161]TA2M_N_2
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","BeTs to 6 clades of COG2373COG name: Large extracellular alpha-helical proteinFunctional Class: RThe phylogenetic pattern of COG2373 is --------vd----ef-hs--jx---Number of proteins in this genome belonging to this COG is","","Residues 392 to 502 match (4e-07) PD:PD591043 which is described as PROTEOME COMPLETE SIGNAL PRECURSOR RC0835 YP02573 RP558 ","","","","","","","","","","","","Tue Jan 7 10:21:52 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01688 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01689","1145640","1146725","1086","GTGAGAATCAACTGCATTTTTTTATTTTCTCGGCGTATAATGAAGCCTCTTTTCCCTTTTATAATAAATAAAATGAAAAATCGAACATTATACTTAGGGCTAATTTGTGTCGCTTTTTTAGCACTAATAGCCGAAAAAATAAGCCAAACGACATTTGCTCTTCAGTTACATTTAAGTGCATTAATCATCGCAATTTTGCTGGGGATGATATTTGGTAACAGTGTTTATAAAGGATATGAGAAGCACCTTGAAAAAGGCATTTTATTTGCAAAAGGACAAATTTTACGGATAGGGATTGTATTGTATGGCTTTCGGCTTACTTTGCATGACATTGCGCAGGTCGGCATGAATGCGATTTTAACGAATGCCCTGATGTTACTCTCTACGTTTTTTCTGACCTGCTTCATCGGGATCCGTTACCTTAAAATGGATAAACAACTTGTTTATCTCACAGCTTCCGGTTGTAGCATTTGTGGCGCTGCTGCAGTGATGGCGGTAGCGCCGGTCACTAAAGCGGAATCTCATAAAGTTTCGGTAGCAATTGCTGTGGTGGTGATTTTTGGTACACTTTCCATTTTTCTTTATCCGTCTTTATATTCTTGGGTAGGCGTATTGATTACCCCGCACCAGTTTGGTATTTATGTGGGTTCCAGTGTGCATGAGGTAGCTCAGGTGTATGCCATAGGTGGCAATATTAGCCCCGTTGTAGCGAACACGGCAGTCATTACCAAAATGATTCGGGTAATGATGTTGGCGCCATTCTTGTTGGGATTGTCTTGGTTGCTTAACAAAGATTCTCAAGGCGGGGAACAACGTAAAATTATCATTCCATGGTTTGCCCTTTGGTTTATTGCGGTTGCGGTATTCAATTCTTTCAATTTATTGCCGGATTTTTTAGTGAAACTTTTAGTCGAACTGGATTCTTTGTTACTCGTTACTGCGATGGCGGCATTAGGATTAACTACACACCTCGGCGCAATTAAACAGGCAGGATTAAAACCGTTAATTCTCGGCACATTGATTTATATTTGGTTAATCGTCGGCGGATTCTTTTTGAACTATGAAGCAGCTCTCTTTTTCTCGTTG","","","39804","VRINCIFLFSRRIMKPLFPFIINKMKNRTLYLGLICVAFLALIAEKISQTTFALQLHLSALIIAILLGMIFGNSVYKGYEKHLEKGILFAKGQILRIGIVLYGFRLTLHDIAQVGMNAILTNALMLLSTFFLTCFIGIRYLKMDKQLVYLTASGCSICGAAAVMAVAPVTKAESHKVSVAIAVVVIFGTLSIFLYPSLYSWVGVLITPHQFGIYVGSSVHEVAQVYAIGGNISPVVANTAVITKMIRVMMLAPFLLGLSWLLNKDSQGGEQRKIIIPWFALWFIAVAVFNSFNLLPDFLVKLLVELDSLLLVTAMAALGLTTHLGAIKQAGLKPLILGTLIYIWLIVGGFFLNYEAALFFSL","1146723","","conserved hypothetical protein (possible inner membrane protein)","Inner membrane, Cytoplasm","","
InterPro
IPR004630
Family
Conserved hypothetical protein 698
PF03601\"[32-338]TCons_hypoth698
TIGR00698\"[28-360]TTIGR00698: conserved hypothetical protein
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[94-234]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-44]?signal-peptide
tmhmm\"[30-48]?\"[54-76]?\"[119-139]?\"[149-169]?\"[179-199]?\"[240-262]?\"[274-294]?\"[308-327]?\"[334-354]?transmembrane_regions


","BeTs to 6 clades of COG2855COG name: Uncharacterized membrane proteinFunctional Class: SThe phylogenetic pattern of COG2855 is a----------l--ef-h-nuj----Number of proteins in this genome belonging to this COG is","","Residues 227 to 334 match (2e-14) PD:PD528249 which is described as COMPLETE PROTEOME MEMBRANE PLASMID INNER ATU0671 CC0425 YEIH PA5383 MLR2225 ","","","","","","","","","","","","Fri Jan 31 14:41:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01689 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 32 to 338 (E-value = 2.1e-149) place AA01689 in the Cons_hypoth698 family which is described as Conserved hypothetical protein 698 (PF03601)","","","","","","","","1","","","" "AA01690","1146848","1149202","2355","ATGTCACAGATATCCCGTAAAAGTCTTTATTTTGTTCTATGCGGCTTATTGCTTACCTGCATAGGGGGGCGTTTTTTACCTCACATTCCGTTAAAACAGCGTTTCCCTTATTCCGTCGCGGTGTATGATGAACAGCAGAATCTGTTACGCCTGACCACGGCAAAGGATCAGAAATATCGTCTTTGGACGCCGTTGGAAGAACTTTCACCACAACTGGTGGATGCAGTGTTATTTCAGGAAGACGAATGGTTTTATTATCATTTCGGGGTCAATCCTTACGGTTTATTGCGCGGGGCGACACAAACCTATTTATTCGGCGGCTCACCGCAAGGCGGTTCGACTATCACCATGCAACTGGCGCGAATATTGTGGAGTATTGATAGCCGCAACATCGGCGGGAAAATCGAGCAGATTCTACGCGCCGTTCAGCTGGAATTACAGTATTCCAAACGGGAAATTCTGGAAGCCTATTTCAACTTTGCTCCTTATGGACGGAACATTGAAGGGGCGGGCACAGCGAGCCTGATTTATTTTAACCGTGCCAATAAGAACCTGAATTTGGCGGAAGCCATGACCTTGGCGATTTTACCGAAAAATCCGAACGCTTACATTCAGCAGAACAATCAGCAACTTAATCCGCAGCTTTTTAATGCGCGTAATAAACTTTATGCCCGCTGGGTGGAAAGCCATCCGAAAGATCGTCAATGGCAGTCGCATTTCAAATTAAATTACCCGTTGCGCCCGCTTGAAAAACTCCCGTTTTTTGCACCGCACTTTACCGATCAAGTGTTGCAACAATACGTCGAAAGCGAGGCGATTCAAAACGGACGAATCATTACCGGCTTAAACAGCGGTTTACAGCGTTTGGTGGAGCGCATTAGTTTGCGTTATCTGCAACAGCAAAAACCGTATGGCGTGAATAATCTTGCCGTTCTGCTGGTGAATAATCGCACCATGCAAATTAAGGCGCTGGTGGGTTCCGGCGATTATTTTAATCAACATATCAGCGGGCAGATTAACGGCACGCTGGCAAAGCGATCTTACGGTTCCACGTTAAAACCGTTTATTTATGGCTTGGCGTTTGATCAAGGTTTGGTACACCCCAAAACGATTTTAAAAGATTTGCCTACCACCTTCGCCGATTATCAACCGGAAAATTATGAAGGCAATTTTCTGGGACCGGTAAGCGTTACGCAGGCGTTACTGCAAAGCCGTAATATTCCGGCGGTAGGCATGGCGCAAAGGCTGAAATATCCCGATCTTTACGATTTACTTAAACAGGCAAAGATCACCTTGCCGAAGGAGAAAGCACATTACGGGTTGTCATTAGTGCTGGGCGGCGCGGAGCTTTCCATGCAACAATTGGCGGGGCTATATGCCGCCCTTGCCAATGGCGGGCAATGGCAACCATTACAAACATTAAAGCATTCGCCGGCGACGCAAAGCGCGACCTTACTAAGCTCCGAAAGCAGCTATATGCTGGGCGATATTTTGTCGCAGAATATTCGTACCGATATTTACAACAAAGCCATCAAAACCAAACTGCCGATTTATTGGAAAACCGGTACGTCAAACGGCTTGCGCGATGCCTGGACGGCAGGCTATTTCGGCAATTACACGCTGGTGGTGTGGTTCGGCAATTTTAACAATAAAAGTAACCCGCACTTTATCGGTCGCCGCCTTGCCGCGCCGTTATTTTTACAACTGGCGGACAGCATTATTGCGCAATACCCGAACATGAAAGACCCGCTTAGCCGTGACAAGCTGAACTTAACGGAAGTTGCTGTGTGTGCCGCCGACGGCAACCTGCCGAACAAATATTGTCAGCAGCTCACGAAGACGTTGTTTATCCCGGGTAAATCGCCTATTCAGGTGAGCAATATCTATCAACAATTACGCGTGCGCAAAGGCACAGACGTCCTGGCTTGCGCAACGGATCCGAATGCGCAAACGGAGCAAAAAATTTATGAAATCTGGGGCAGTGACTATCAAAAAATGTTTGCGCAGGCGGGCATCATGAAACGCAATCCCATCGTCAACGTCGAATGCCCTTACGAGCAACAAAACCAGTCCTTGCAACACATTACGCATAATCCGCTGAAGATGACATCGCCACTGGAAAACCGCACTTACTACATCAATATGAACAGCCCGGAAAACCACATTCCGCTGACCGCGACAACCTCCGGCGAAGTTCAACACCTTTATTGGTTCGTGAATAACGTCTACTTAGGCGAAAGCCCCGCCTCCAAAGCCTTCTTATGGCAACCCACCAAAAGCGGCACCTACCAAATCACCGTCGCCGATGAACAAGGACACAGAACCGGTGTGAGCGTGGTGGTGAGTGTGGTGAGG","","","89676","MSQISRKSLYFVLCGLLLTCIGGRFLPHIPLKQRFPYSVAVYDEQQNLLRLTTAKDQKYRLWTPLEELSPQLVDAVLFQEDEWFYYHFGVNPYGLLRGATQTYLFGGSPQGGSTITMQLARILWSIDSRNIGGKIEQILRAVQLELQYSKREILEAYFNFAPYGRNIEGAGTASLIYFNRANKNLNLAEAMTLAILPKNPNAYIQQNNQQLNPQLFNARNKLYARWVESHPKDRQWQSHFKLNYPLRPLEKLPFFAPHFTDQVLQQYVESEAIQNGRIITGLNSGLQRLVERISLRYLQQQKPYGVNNLAVLLVNNRTMQIKALVGSGDYFNQHISGQINGTLAKRSYGSTLKPFIYGLAFDQGLVHPKTILKDLPTTFADYQPENYEGNFLGPVSVTQALLQSRNIPAVGMAQRLKYPDLYDLLKQAKITLPKEKAHYGLSLVLGGAELSMQQLAGLYAALANGGQWQPLQTLKHSPATQSATLLSSESSYMLGDILSQNIRTDIYNKAIKTKLPIYWKTGTSNGLRDAWTAGYFGNYTLVVWFGNFNNKSNPHFIGRRLAAPLFLQLADSIIAQYPNMKDPLSRDKLNLTEVAVCAADGNLPNKYCQQLTKTLFIPGKSPIQVSNIYQQLRVRKGTDVLACATDPNAQTEQKIYEIWGSDYQKMFAQAGIMKRNPIVNVECPYEQQNQSLQHITHNPLKMTSPLENRTYYINMNSPENHIPLTATTSGEVQHLYWFVNNVYLGESPASKAFLWQPTKSGTYQITVADEQGHRTGVSVVVSVVR","1149200","[FUNCTION] Cell wall formation. the enzyme has a penicillin-insensitive transglycosylase n-terminal domain (formation of linear glycan strands) and a transpeptidase C-terminal domain which may not be functional. [ENZYME REGULATION] Transglycosylase activity can be inhibited by moenomycin. [PATHWAY] Final stages in peptidoglycan synthesis. [SUBCELLUAR LOCATION] Type II membrane protein. inner membrane (by similarity). [MISCELLANEOUS] Due to the fact that pbp-1c can neither substitute for pbp-1a or pbp-1b, nor rescue a pbp-1a/pbp-1b double mutant, it is possible that pbp-1c has its own distinct function. Moreover it does not bind to most of the beta-lactams known to bind to otherbinding proteins, suggesting that the penicillin-binding domain must be different from those present in pbp-1a andpbp-1b. it may function as a tranglycosylase only. [SIMILARITY] In the N-terminal section; belongs to the transglycosylase family. [SIMILARITY] In the C-terminal section; belongs to the transpeptidase family. ","penicillin-binding protein 1C","Inner membrane, Outer membrane, Periplasm","","
InterPro
IPR001264
Domain
Glycosyl transferase, family 51
PD001895\"[134-177]TQ9CN05_PASMU_Q9CN05;
PF00912\"[39-209]TTransgly
InterPro
IPR001460
Domain
Penicillin-binding protein, transpeptidase
PF00905\"[309-466]TTranspeptidase
InterPro
IPR009647
Domain
Penicillin-binding, C-terminal
PF06832\"[689-779]TBiPBP_C
InterPro
IPR011815
Family
Penicillin-binding protein 1C
TIGR02073\"[28-782]TPBP_1c: penicillin-binding protein 1C
noIPR
unintegrated
unintegrated
G3DSA:3.40.710.10\"[285-571]Tno description
signalp\"[1-22]?signal-peptide
tmhmm\"[9-27]?transmembrane_regions


","BeTs to 16 clades of COG0744COG name: Membrane carboxypeptidase (penicillin-binding protein)Functional Class: MThe phylogenetic pattern of COG0744 is -------qvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.5e-41) to 3/3 blocks of the IPB001264 family, which is described as \"Glycosyltransferase family 51\". Interpro entry for IP:IPR001264. IPB001264A 63-102 4.3e-13 IPB001264B 111-163 7.5e-20 IPB001264C 168-194 9.6e-06","Residues 9 to 59 match (3e-08) PD:PD385740 which is described as PONC PROTEOME COMPLETE ","","","","","","","","","","","Tue Jan 7 10:33:16 2003","Tue Jan 7 10:33:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01690 is paralogously related to AA02432 (2e-39), AA01304 (1e-18) and AA00780 (9e-16).","","","","","","Residues 689 to 779 (E-value = 6.8e-22) place AA01690 in the BiPBP_C family which is described as Penicillin-Binding Protein C-terminus Family (PF06832)","","","","","Schiffer,G. and Holtje,J.V. Cloning and characterization of PBP 1C, a third member of the multimodular class A penicillin-binding proteins of Escherichia coli. J. Biol. Chem. 274 (45): 32031-32039 (1999) [PubMed: 10542235].Goffin,C. and Ghuysen,J.M. Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol. Mol. Biol. Rev. 62 (4): 1079-1093 (1998) [PubMed: 9841666].","","Tue Jan 7 10:33:16 2003","1","","","" "AA01692","1149989","1149318","672","ATGAACAAACCATTACTTCAAATCGCCTTAGATTCACTGAGCTTAGAAAAAGCCGTGTCCGACGCCAAACAAGCGGAAAATTTAGTGGAAATTATTGAAGTGGGCACCATTCTTGCCTGCGCCGAAGGCATGAAAGCGGTGTCCACCCTACGCGCCCTTCACCCGAATCACATTATCGTATGCGATTTAAAAACCACCGACGGCGGCGCCATTTTAGCCAAAATGGCATTTGAAGCCGGTGCCGACTGGCTCACCGTCTCCGCCGCCGCCCACCCGGCCACCAAAGCAGCATGCAAAAAAGTTGCCGACGAATTCAACGCAGAGCACCCGGATCTCAAAGTGAAAAAAGAAATCCAAATCGAAATTTACGGCAACTGGACATTAGATGACGCCAAAGACTGGGTTGCGTTGGGTGTGACGCAAGCCATTTACCACCGCTCACGGGATGCCGAACTTGCCGGCAAAGGTTGGACAGCGGAAGACGTGGAGCTCATGAAGCAATTATCGGTTTTAGGGCTTGAACTCTCCATCACCGGCGGCATCGTGCCAAAAGACATTCATTTATTCAAAGACATCAAAAACGCCAAAGCCTTCATCGCAGGCCGCGCATTAGTGGGCGAAAACGGCAAAGCTACCGCCGAAGCCATCCGCGAACAAATCAATCAATACTGG","","","24224","MNKPLLQIALDSLSLEKAVSDAKQAENLVEIIEVGTILACAEGMKAVSTLRALHPNHIIVCDLKTTDGGAILAKMAFEAGADWLTVSAAAHPATKAACKKVADEFNAEHPDLKVKKEIQIEIYGNWTLDDAKDWVALGVTQAIYHRSRDAELAGKGWTAEDVELMKQLSVLGLELSITGGIVPKDIHLFKDIKNAKAFIAGRALVGENGKATAEAIREQINQYW","1149316","[FUNCTION] Condensation of D-ribulose 5-phosphate with formaldehyde to form D-arabino-6-hexulose 3-phosphate.[PATHWAY] Probably part of a sugar metabolic pathway along with sgbu. ","hexulose-6-phosphate synthase","Cytoplasm","","
InterPro
IPR001754
Domain
Orotidine 5'-phosphate decarboxylase, core
PF00215\"[4-216]TOMPdecase
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[1-224]Tno description


","No hits to the COGs database.","","Residues 9 to 206 match (7e-11) PD:PD001042 which is described as DECARBOXYLASE SYNTHASE PYRIMIDINE LYASE BIOSYNTHESIS OROTIDINE OMPDECASE 5'-PHOSPHATE OMP OMPDCASE ","","","","","","","","","","","Tue Jan 7 10:58:24 2003","Tue Jan 7 10:58:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01692 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 216 (E-value = 3.3e-54) place AA01692 in the OMPdecase family which is described as Orotidine 5'-phosphate decarboxylase / HUMPS family (PF00215)","","","","","Reizer,J., Reizer,A. and Saier,M.H. Jr. Is the ribulose monophosphate pathway widely distributed in bacteria?. Microbiology 143 (Pt 8): 2519-2520 (1997) [PubMed: 9274005].Reizer,J., Charbit,A., Reizer,A. and Saier,M.H. Jr. Novel phosphotransferases system genes revealed by bacterial genome analysis: operons encoding homologues of sugar-specific permeasedomains of the phosphotransferase system and pentose catabolic enzymes. Genome Sci. Technol. 1, 53-75 (1996) ","","Tue Jan 7 10:58:24 2003","1","","","" "AA01694","1150527","1150069","459","ATGCTAAAAGAATCCCTTATCGAAAATAATTCCATCAGACTCAACCAATCTGCATCCAACTGGGAAGAAGCCATTAAAATCGGTACGGATTTACTGGTCGCTTCAGGTGCCATAGAACCGCGTTATTATGACAATATTGTCAACAACATCAAAAAGTTCGGGCCTTATATCGTTCTCGCCCCGGGGCTTGCCATGCCGCACGCCCGCCCGGAAGAAGGTGTAATTAAAACCGCATTCGGCTTAACCACATTAAGCGTGCCGGTAGATCTCGACGGCGAATCCATTTCCGTGCTACTCACTCTTGCCGGCAGCGATTCCAATTCCCACATGGAAGGCATTATGGAAATCACCCAAATCTTCGACGATCCCAACAGCGATGACGGTGTGAACATCCAAAAATTCCTGGATTGCAAAACTACGGAAGAGGTGCTTGCCGTAATTGATGCCACACTGAATGCT","","","16547","MLKESLIENNSIRLNQSASNWEEAIKIGTDLLVASGAIEPRYYDNIVNNIKKFGPYIVLAPGLAMPHARPEEGVIKTAFGLTTLSVPVDLDGESISVLLTLAGSDSNSHMEGIMEITQIFDDPNSDDGVNIQKFLDCKTTEEVLAVIDATLNA","1150067","[CATALYTIC ACTIVITY] Protein N-phosphohistidine + sugar = protein histidine + sugar phosphate.[SUBCELLULAR LOCATION] Cytoplasmic (Probable).","PTS system, IIA component","Cytoplasm","","
InterPro
IPR002178
Domain
Phosphotransferase system, phosphoenolpyruvate-dependent sugar EIIA 2
PD001689\"[12-142]TQ9CMQ0_PASMU_Q9CMQ0;
G3DSA:3.40.930.10\"[6-147]Tno description
PF00359\"[5-150]TPTS_EIIA_2
PS51094\"[5-150]TPTS_EIIA_TYPE_2


","No hits to the COGs database.","","Residues 6 to 122 match (1e-09) PD:PD546790 which is described as COMPLETE PROTEOME LIN2817 LMO0501 LIN2203 SAV0244 LMO0630 LMO2668 LMO2099 LIN0501 ","","","","","","","","","","","Tue Jan 7 12:06:14 2003","Tue Jan 7 12:06:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01694 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 150 (E-value = 2.8e-36) place AA01694 in the PTS_EIIA_2 family which is described as Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2 (PF00359)","","","","","Reizer,J., Charbit,A., Reizer,A. and Saier,M.H.Jr. Novel phosphotransferases system genes revealed by bacterial genome analysis: operons encoding homologues of sugar-specific permease domains of the phosphotransferase system and pentose catabolicenzymes. Genome Sci. Technol. 1, 53-75 (1996) ","","Tue Jan 7 12:06:14 2003","1","","","" "AA01695","1152354","1150585","1770","ATGGAAATCTTCATGTGGATCAACGAACAGATCCTATCTAAAGCGCCCTTACTGCTCGGTATCGTAGCCTGTATCGGTTATATTCTGTTAAGAAAAGACACAGCAACTATTATCAAAGGCACGATTAAAACCATCGTGGGCTTTATGTTGGTACAAGTGGGGGCGGCCACATTGGTTGCCGGTTTTAAACCAATTATTGAAAATCTGGCAAAGTTCCATAATTTAACCGGTGCAGTCATTGACCCTTACACCAGCATGCAGGCGACCATCCAAACCATGGGAGATAACTACGGTTGGGTCGGCTATGCCGTATTATTGGCACTGGCATTGAACATTTTATTAGTGGTATTCAGACGCTTTACCGGTATTCGTACCATCATGCTTACCGGCCATATCATGTTCCAGCAGGCGGGTTTGGTTGCGGTGTTCTATATGATCATCGGTGCTTCCATGTGGGAAACCATCGTTTATACAGCAGTCATCATGGCATTATATTGGGGGATTTCCTCTAACATTATGTATAAAGCAACCCAATCAGTTACCGGCGGTGCGGGCTTCTCCATTGGTCACCAACAACAGGTCGCCTCATGGATTGCCACCAAAATCGCACCGAAACTGGGTGATAAAAATGACAACGTGGATCACATGGATTTACCGAAATGGTTACATATTTTCCACGACAGCATCTCCGCCACCGCTATTGTTATGTCCGTCTTCTTCGGGATTATTTTACTTTCCTTCGGACTGGATAATCTGCAAACCATGGCGGGCAAAACTCACTGGTCAATTTACATTTTGGAAACCGGTTTAAAATTCGCCGTCGCCATTCAAATTATCGTTATGGGTGTGCGTATGTTCGTCGCCGAATTATCGGAAGCCTTTAAGGGGATTTCCGAACGGGTGATTCCAAATGCGGTACTCGCCATTGACTGTGCAGCGATTTACGCCTTCTCCCCTAACGCCATGGTATTCGGTTTCATGTGGGGTGCCATCGGTCAATTCGTGGCGGTAGGTATCCTGCTCGGCTTCAGCGCACCGATTTTAATCATTACGGGCTTTATCCCGATGTTCTTCTCTAACGCCACCATCGGCGTCTTTGCCAACCACTTCGGCGGCTGGAAAGCGGTCATGAAAATCTGTTTCGTGATGGGGATCATTGAAGTATTAGGTTCCGCCTGGGTTATTCAACTCTTAGCAACCCAAGGCACTACCTTCAACGGTTGGATGGGTATGGCGGACTGGGCGTTATTATTCCCACCTGTTTTGCAAGGTATTGTGAGCATTCCGTTCTTCTTCTTTGTTATCGTCGCCCTTTCCTTGGTTTATATGTTCTTCGCTTCTAAAAAATTGCGTGCCGACGAAGCTGCTGCCGCTGCTGCAGGCAAAACCTTGGAGCAAATGGACGGTTACAACTTAGACGACGAACCGGTGACCGAAATACAACGTGAAGCGCAACCTGCCGAACAAAGCGGTGAGTGCCCGATTCGTATCTTAGCCGTATGCGGTTCCGGTCAAGGTTCTTCTATGATGATGAAAATGAAGATCAAAGGTTATCTGGACAAACGTGGCATTCCAAATATTATGGATTCCTGCGCAGTGACCGACTATAAAGGTAAACTCAACGAAGTGGATATTATCGTTGCATCCAAACACTTAGCCGGCGAAATTGAAGTGGGCGAAGGCAAAGCCGTACTCGGCGTGCAAAATATGCTTAACCCTAACTCTTTCGGCGATGAATTGGTCGAGTTAATCAATAAACATCATTCTGCC","","","64170","MEIFMWINEQILSKAPLLLGIVACIGYILLRKDTATIIKGTIKTIVGFMLVQVGAATLVAGFKPIIENLAKFHNLTGAVIDPYTSMQATIQTMGDNYGWVGYAVLLALALNILLVVFRRFTGIRTIMLTGHIMFQQAGLVAVFYMIIGASMWETIVYTAVIMALYWGISSNIMYKATQSVTGGAGFSIGHQQQVASWIATKIAPKLGDKNDNVDHMDLPKWLHIFHDSISATAIVMSVFFGIILLSFGLDNLQTMAGKTHWSIYILETGLKFAVAIQIIVMGVRMFVAELSEAFKGISERVIPNAVLAIDCAAIYAFSPNAMVFGFMWGAIGQFVAVGILLGFSAPILIITGFIPMFFSNATIGVFANHFGGWKAVMKICFVMGIIEVLGSAWVIQLLATQGTTFNGWMGMADWALLFPPVLQGIVSIPFFFFVIVALSLVYMFFASKKLRADEAAAAAAGKTLEQMDGYNLDDEPVTEIQREAQPAEQSGECPIRILAVCGSGQGSSMMMKMKIKGYLDKRGIPNIMDSCAVTDYKGKLNEVDIIVASKHLAGEIEVGEGKAVLGVQNMLNPNSFGDELVELINKHHSA","1150583","[FUNCTION] Could act as the transport protein for the unknown pentitol substrate of the sga operon. [SUBCELLUAR LOCATION] Integral membrane protein. inner membrane (potential). ","carbohydrate transport protein","Inner membrane, Cytoplasm","","
InterPro
IPR003501
Domain
Phosphotransferase system, lactose/cellobiose-specific IIB subunit
PF02302\"[496-585]TPTS_IIB
InterPro
IPR007333
Family
Putative sugar-specific permease, SgaT/UlaA
PF04215\"[1-417]TSgaT_UlaA
InterPro
IPR013011
Domain
Phosphotransferase system, EIIB component, type 2
PS51099\"[495-588]TPTS_EIIB_TYPE_2
noIPR
unintegrated
unintegrated
signalp\"[1-30]?signal-peptide
tmhmm\"[10-30]?\"[45-65]?\"[97-117]?\"[126-144]?\"[150-168]?\"[229-249]?\"[263-283]?\"[304-324]?\"[330-350]?\"[379-399]?\"[425-445]?transmembrane_regions


","No hits to the COGs database.","","Residues 378 to 462 match (9e-23) PD:PD142911 which is described as COMPLETE PROTEOME SGAT INNER IISGA SUBUNIT PTS TRANSMEMBRANE MEMBRANE ENZYME ","","","","","","","","","","","Tue Jan 7 12:10:51 2003","Tue Jan 7 12:10:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01695 is paralogously related to AA02566 (5e-37) and AA02568 (1e-06).","","","","","","Residues 496 to 585 (E-value = 3.8e-29) place AA01695 in the PTS_IIB family which is described as PTS system, Lactose/Cellobiose specific IIB subunit (PF02302)","","","","","Reizer, J., Charbit, A., Reizer, A., and Saier, M. H. J. R. Novel phosphotransferases system genes revealed by bacterial genome analysis: operons encoding homologues of sugar-specific permease domains of the phosphotransferase system and pentose catabolic enzymes. Genome Sci. Technol. 1: 53-75, 1996.","","Tue Jan 7 12:10:51 2003","1","","","" "AA01696","1152702","1153790","1089","ATGGCTAAAGTTAATGAAATCACCCGTGAAAGTTGGATCCTTTCTACTTTTCCTGAATGGGGCACTTGGTTAAATGAAGAAATTGAGAACGAAGTTGTTCCCGAGGGCAATTTTGCCATGTGGTGGTTAGGTTGTGTCGGTGTGTGGATAAAAACCCCCGCGGGCGCCAATATTTGCATGGACTTATGGTGCAATCGTGGTAAGAGTACTAAAAAAGTAAAAGACATGGTGCGCGGTCACCAAATGGCGAACATGGCAGGCGTGCGTAAATTACAACCGAACCTGCGTGCCCAGCCAATGGTTTTGGATCCGTTTGCCATTAACGAAGTGGATTTCATTTTAGCCTCCCATTATCACAGCGATCATATTGATGTAAACGTTGCGGCGGCAATCGTAAATAACCCGAAATTGGATCATGTGAAATTTGTTGGTCCATGGCATTGCGCCGAATTATGGAAAAATTGGGGTGTACCGGAAGAACGCATCATTATCGTTAAACCGGGTGATATGGTGAAATTAAAAGATGTCGACATTTACGCCTTGGATTCTTTCGACCGCACTTGCCTGGTGACATTGCCGGTTGAAGGTGCGGAAGAACAAGGCGGTGAATTAAAAGGGCTTTGCCCGTCTGATGAAGAAATGGGACGTAAAGCGGTGAACTATGTGTTCAAAACACCGGGCGGTAATATTTACCATGGTGCAGATTCGCATTATTCCATTCAATTCGCCAAGCACGGTAAAGATTTCGATATTGATGTGGCACTGAATAACTATGGTGAAAATCCGGTGGGGATTGCCGATAAAATGACTTCAATTGATTTACTCCGTATGGCAGAATGTTTGCGTACCAATGTTATCATTCCTGTTCATCACGACATTTGGACCAACTTTATGGCGAGTACCGATGAAATTCTTGCGCTATGGCGTATGCGTAAAGATCGTTTGCAGTATAAATTCCATCCGTTTATCTGGGAAGTCGGCGGTAAATATGTGTACCCGCGTGATAAAGATTTGATTGAATATCATCATCCGCGCGGTTTTGATGATTGCTTTGAGCAGGAACCGAACATCCAGTTTAAATCCATGCTT","","","41606","MAKVNEITRESWILSTFPEWGTWLNEEIENEVVPEGNFAMWWLGCVGVWIKTPAGANICMDLWCNRGKSTKKVKDMVRGHQMANMAGVRKLQPNLRAQPMVLDPFAINEVDFILASHYHSDHIDVNVAAAIVNNPKLDHVKFVGPWHCAELWKNWGVPEERIIIVKPGDMVKLKDVDIYALDSFDRTCLVTLPVEGAEEQGGELKGLCPSDEEMGRKAVNYVFKTPGGNIYHGADSHYSIQFAKHGKDFDIDVALNNYGENPVGIADKMTSIDLLRMAECLRTNVIIPVHHDIWTNFMASTDEILALWRMRKDRLQYKFHPFIWEVGGKYVYPRDKDLIEYHHPRGFDDCFEQEPNIQFKSML","1153788","","conserved hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
PD135310\"[1-363]TQ9CMQ2_PASMU_Q9CMQ2;


","BeTs to 10 clades of COG2220COG name: Predicted Zn-dependent hydrolases of the beta-lactamase foldFunctional Class: RThe phylogenetic pattern of COG2220 is aompkzy-vdrlbcefghs-uj----Number of proteins in this genome belonging to this COG is","","Residues 1 to 33 match (1e-10) PD:PD584716 which is described as COMPLETE PROTEOME SP2031 SPY0182 VCA0248 PM0763 ","","","","","","","","","","","","Tue Jan 7 12:13:04 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01696 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01698","1153885","1154631","747","ATGAACGAACGTTATCGTCATAATCAAATATTAGATTTACTGAAAGAGCGAACCCTTCTTTCGACCAACGAAATTATCGATACCTTTAACATCTCGCCGGCAACAGCACGTCGCGATATTAATAAATTAAATGCGCAAGGGTTGCTTAGAAAAGTCCGTAACGGCGCCGAATACCTTGCCTTTAACGGTAAACAATATGCGCAGCCCCGTGTTGTTAATAATGCCGAAGAAAAACAACGCATTGCCGAAGCCGCAGCAAAACTTTGTGAAAACGGGCAAAGCGTCGTACTGACTTGCGGCACCACCATGCAAATGCTGGCGGATAGCCTGTGCGGATGCAATGTACAGATCATTACCAACTATTTGCCTTTGGCTAATTTCCTCATTGAACATAATCATGACGATGTCGTGATTATGGGCGGTCAATATAATAAAAATAAAGCGGTGACTTTATCCCTGAATTCCACTAACGAACCGGCTTATGCCGCCAATATTATGTTTACCAGCGGTAAAGGCATGACCACAGACGGCTTATACAAAACAGATATGATTATCGCCAATTCGGAACAGCATATTTTACCTAAGGTCAGCAAACTGGTTGCTTTGGTTGACAGTTCAAAGCTCGGACGCGAAATGGGCATGCTGTTTAGCGAATTGAAAGATATTGATTTACTGGTGACCGGAAAAGAGGCCGATCCAAAGATTATTCAAGAATTAAAAGACAAAGGATTAGAAGTTATTCTTGCC","","","28703","MNERYRHNQILDLLKERTLLSTNEIIDTFNISPATARRDINKLNAQGLLRKVRNGAEYLAFNGKQYAQPRVVNNAEEKQRIAEAAAKLCENGQSVVLTCGTTMQMLADSLCGCNVQIITNYLPLANFLIEHNHDDVVIMGGQYNKNKAVTLSLNSTNEPAYAANIMFTSGKGMTTDGLYKTDMIIANSEQHILPKVSKLVALVDSSKLGREMGMLFSELKDIDLLVTGKEADPKIIQELKDKGLEVILA","1154629","[FUNCTION] Repressor of the glp operon; ","probable transcriptional regulator (DeoR family)","Cytoplasm","","
InterPro
IPR001034
Domain
Bacterial regulatory protein, DeoR N-terminal
PR00037\"[24-38]T\"[38-56]THTHLACR
PF08220\"[6-62]THTH_DeoR
SM00420\"[6-58]THTH_DEOR
PS51000\"[3-58]THTH_DEOR_2
PS00894\"[6-40]THTH_DEOR_1
InterPro
IPR014036
Domain
Bacterial regulatory protein, DeoR
PF00455\"[75-228]TDeoR


","No hits to the COGs database.","Significant hit ( 5.9e-35) to 5/5 blocks of the IPB001034 family, which is described as \"Bacterial regulatory protein, DeoR family\". Interpro entry for IP:IPR001034. IPB001034A 20-55 8.8e-15 IPB001034B 78-102 9.2e-11 IPB001034C 118-128 0.071 IPB001034D 140-152 1.3e+02 IPB001034E 200-210 0.037Significant hit ( 1.1e-05) to 1/1 blocks of the IPB000524 family, which is described as \"Bacterial regulatory proteins, GntR family\". Interpro entry for IP:IPR000524. IPB000524 19-59 1e-05","Residues 1 to 94 match (6e-10) PD:PD469489 which is described as COMPLETE PROTEOME TRANSCRIPTION REPRESSOR DNA-BINDING REGULATION TRANSCRIPTIONAL REGULATOR LACTOSE PHOSPHOTRANSFERASE ","","","","","","","","","","","Tue Jan 7 12:17:39 2003","Tue Jan 7 12:17:39 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01698 is paralogously related to AA02048 (3e-20), AA00308 (5e-18), AA00973 (4e-14) and AA00585 (1e-13).","","","","","","Residues 6 to 228 (E-value = 3.1e-69) place AA01698 in the DeoR family which is described as Bacterial regulatory proteins, deoR family (PF00455)","","","","","","","","1","","","" "AA01700","1154675","1155532","858","GTGAGAAAACATAAATTGGGTATTTATGAAAAAGCCCTGCCGAAAAATATTAGCTGGCAGGATCGCTTGTCCATCGCCAAAGCCTGCGGTTTTGATTTTGTCGAAATTTCTATCGATGAAAGCGATGAGCGTTTGGCGCGTTTGGATTGGAGCGAAAAAGAACGCATTCAGTTGGTGAAAGCCATTATCAAAACCGGCGTTACCATTCCTTCTATGTGTCTTTCCGGGCATCGTCGTTTTCCTTTCGGCAGCCGTGACGAAGCAACCCGCGCAAAAGCTTATGAAATCATGGAAAAAGCCGTTAAATTAGCCGTCGATTTAGGTATTCGCACCATTCAGTTGGCGGGTTATGACGTGTATTACGAAGAGCAGGACAAAGGCACTATTCAGCGCTTCCAAGAAGGCTTGCAATGGGCGGTGGAATTGGCGGCAAGTAATCAAGTGACCATTGCGGTAGAAATTATGGATACCCAATTTATGAGCTCCATCAGTCGCTGGAAAAAATGGGATGACCTTATCAAATCGCCGTGGTTCACTGTGTATCCGGATCTCGGCAATTTAAGTGCGTGGAATGACAACGTCGCGAAAGAATTGAAGCTGGGCATCGACAAAATCTCCGCCATTCATTTGAAAGACACTTATAAAGTTACCGACACCTGCAAAGGGCAATTCCGTGACGTGCCTTTCGGTGACGGTTGTGTGGATTTTGTTGCCTGTTTCAGAACATTGGCAGAATTGAATTATCGCGGCGCATTTTTAATTGAAATGTGGACGGAAAAAGCGGAAGAACCGATTGCGGAAATTATTAACGCCCGCCGTTGGATTGAACAAAAAATGAAAGAAGGTGGTTTTCCATGT","","","32792","VRKHKLGIYEKALPKNISWQDRLSIAKACGFDFVEISIDESDERLARLDWSEKERIQLVKAIIKTGVTIPSMCLSGHRRFPFGSRDEATRAKAYEIMEKAVKLAVDLGIRTIQLAGYDVYYEEQDKGTIQRFQEGLQWAVELAASNQVTIAVEIMDTQFMSSISRWKKWDDLIKSPWFTVYPDLGNLSAWNDNVAKELKLGIDKISAIHLKDTYKVTDTCKGQFRDVPFGDGCVDFVACFRTLAELNYRGAFLIEMWTEKAEEPIAEIINARRWIEQKMKEGGFPC","1155530","[FUNCTION] Isomerization of D-arabino-6-hexulose 3-phosphate to D-fructose 6-phosphate. [PATHWAY] Probably part of a sugar metabolic pathway along with sgbH. [SIMILARITY] Belongs to the humPI family ","hexulose-6-phosphate isomerase","Cytoplasm","","
InterPro
IPR004560
Family
Putative hexulose-6-phosphate isomerase
TIGR00542\"[2-286]Thxl6Piso_put: hexulose-6-phosphate isomeras
InterPro
IPR012307
Domain
Xylose isomerase-like TIM barrel
PF01261\"[23-234]TAP_endonuc_2
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.150\"[4-282]Tno description
PTHR12110\"[16-277]THYDROXYPYRUVATE ISOMERASE


","BeTs to 4 clades of COG3623COG name: Putative L-xylulose-5-phosphate 3-epimeraseFunctional Class: GThe phylogenetic pattern of COG3623 is -----------l--e-gh-------wNumber of proteins in this genome belonging to this COG is","","Residues 6 to 283 match (2e-143) PD:PD017663 which is described as ISOMERASE PROTEOME COMPLETE HEXULOSE-6-PHOSPHATE 5.-.-.- HUMPI SUGAR-PHOSPHATE ISOMERASE SGAU 3-HEXULOSE-6-PHOSPHATE ","","","","","","","","","","","Tue Jan 7 12:23:44 2003","Tue Jan 7 12:23:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01700 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 285 (E-value = 2.3e-230) place AA01700 in the Hxl6Piso_put family which is described as Putative hexulose-6-phosphate isomerase (PF03809)","","","","","Reizer,J., Charbit,A., Reizer,A. and Saier,M.H. Jr. Novel phosphotransferases system genes revealed by bacterial genome analysis: operons encoding homologues of sugar-specific permease domains of the phosphotransferase system and pentose catabolic enzymes. Genome Sci. Technol. 1, 53-75 (1996) ","","Tue Jan 7 12:23:44 2003","1","","","" "AA01703","1155529","1156221","693","ATGTTAGAAACACTTAAAGAAAAAGTCTTAAAAGCAAATCTGGCGTTACCGAAATACAATTTGGTGACTTTCACTTGGGGCAACGTTTCCGCCATTGATCGCGAAAAAAATCTGGTGGTGATAAAACCTTCCGGCGTGGAATACGATGTCATGACCGCCGAAGATATGGTGGTAGTGGATTTATTCACCGGCAAAGTGGTAGAAGGCAGCAAAAAACCGTCTTCCGACACGCCGACCCACTTGGAATTGTATCGCGAGTTCCCGACCATCGGCGGCATCGTGCACACCCATTCCCGCCACGCTACCATCTGGTCACACGCGGGCGAAGATCTTATCGCCGCAGGCACTACCCATGCCGACTATTTCTATGGTTCCATTCCTTGCACCCGCAAAATGACCCCGGCGGAAATTCAAGGCGAGTATGAATTAGAAACCGGCAAAGTTATCGTGGAGACCTTCCGCAAACGCGGCATCGATCCGAAAGACGTACCTGCCGTATTGGTGCATTCCCACGGCCCATTCGCGTGGGGAACGGACGCCGACAACGCCGTGCATAATGCGGTGGTGCTGGAAGAAATCGGCTACATGAACCTGTTCAGCCGCCAACTCCGCCCGAACCTACAACCGATGCAACAAGAATTACTGGATAAACATTATCTACGCAAACACGGTAAAAATGCTTATTACGGGCAG","","","25903","MLETLKEKVLKANLALPKYNLVTFTWGNVSAIDREKNLVVIKPSGVEYDVMTAEDMVVVDLFTGKVVEGSKKPSSDTPTHLELYREFPTIGGIVHTHSRHATIWSHAGEDLIAAGTTHADYFYGSIPCTRKMTPAEIQGEYELETGKVIVETFRKRGIDPKDVPAVLVHSHGPFAWGTDADNAVHNAVVLEEIGYMNLFSRQLRPNLQPMQQELLDKHYLRKHGKNAYYGQ","1156219","[FUNCTION] Probable pentulose-5-phosphate-4-epimerase. [COFACTOR] Binds one zinc ion per molecule (potential).[SIMILARITY] Belongs to the aldolase class II family. araD/fucA subfamily. [PATHWAY] L-arabinose catabolism; third step.[CATALYTIC ACTIVITY] L-ribulose 5-phosphate = D-xylulose 5-phosphate.","L-ribulose-phosphate 4-epimerase","Cytoplasm","","
InterPro
IPR001303
Domain
Class II aldolase/adducin, N-terminal
G3DSA:3.40.225.10\"[1-231]Tno description
PF00596\"[7-218]TAldolase_II
InterPro
IPR004661
Family
L-ribulose-5-phosphate 4-epimerase
TIGR00760\"[1-231]TaraD: L-ribulose-5-phosphate 4-epimerase
noIPR
unintegrated
unintegrated
PTHR22789\"[78-231]TFUCULOSE PHOSPHATE ALDOLASE


","BeTs to 16 clades of COG0235COG name: Ribulose-5-phosphate 4-epimerase and related epimerases and aldolasesFunctional Class: GThe phylogenetic pattern of COG0235 is aompkzyqv-rlb-efghs-ujx--wNumber of proteins in this genome belonging to this COG is","Significant hit ( 9e-44) to 4/4 blocks of the IPB001303 family, which is described as \"Class II Aldolase and Adducin N-terminal domain\". Interpro entry for IP:IPR001303. IPB001303A 22-31 2.6e-05 IPB001303B 35-60 7.9e-16 IPB001303C 80-98 4.9e-09 IPB001303D 166-183 5.6e-09","Residues 1 to 223 match (4e-118) PD:PD001906 which is described as PROTEOME COMPLETE ALDOLASE ISOMERASE 4-EPIMERASE ADDUCIN ZINC II L-RIBULOSE-5-PHOSPHATE PHOSPHATE ","","","","","","","","","","","Tue Jan 7 12:28:29 2003","Tue Jan 7 12:28:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01703 is paralogously related to AA00311 (1e-07).","","","","","","Residues 7 to 218 (E-value = 1.4e-107) place AA01703 in the Aldolase_II family which is described as Class II Aldolase and Adducin N-terminal domain (PF00596)","","","","","Lee,N., Gielow,W., Martin,R., Hamilton,E. and Fowler,A. The organization of the araBAD operon of Escherichia coli. Gene 47(2-3): 231-244, 1986. PubMed: 3549454. Mineno,J., Fukui,H., Ishino,Y., Kato,I. and Shinagawa,H. Nucleotide sequence of the araD gene of Escherichia coli K12 encoding the L-ribulose 5-phosphate 4-epimerase. Nucleic Acids Res. 18(22): 6722, 1990. PubMed: 2251150. Lin,H.C., Lei,S.P., Studnicka,G. and Wilcox,G. The araBAD operon of Salmonella typhimurium LT2. III. Nucleotide sequence of araD and its flanking regions, and primary structure of its product, L-ribulose-5-phosphate 4-epimerase. Gene 34(1): 129-134, 1985. PubMed: 3891514.","","Tue Jan 7 12:28:29 2003","1","","","" "AA01704","1157521","1156310","1212","ATGAACAAAACCGTAGGAAGTACGCTGTTAGTGGCAGGAACCATGATTGGCGCCGGCATGCTGGCAATGCCGCTCACCTCCGCCGGCATCGGATTTAGTTTCACTTTACTTTTATTATTAGGCTTGTGGGGATTACTCACCTTTACCGCGCTGTTATTCGTCGAACTTTACCAAACCGCCCCGAGCGACGCCGGCATCGGCACCCTTGCCGAACAATATTTCGGTCGACCGGGACGCATTATCGCCACCGCCGTATTAATCATTTTCTTATACGCCCTCATCGCCGCTTACATCAGTGGCGGCGGTTCCTTATTGGCTGACACCCTACCGACCATCGCCGACAAAGACACCACCGGCAAAATCGCCGTATTAATCTTCACCCTTTTCTTCGGTATGTTTATCGTCATCGGCACGCACAGCGTCGATAAAATCAACCGTTTGTTATTTTTCACTATGATCGGCACATTCATCGTGGTATTGGCGCTCATGTTGCCGGAAATCAAACTGGATAACTTAATGGCAATGCCTATTGATAACGCCCTCATCATTTCCGCCGGCCCGGTGTTTTTCACCGCATTCGGCTTCCATGGCTCCATTCCCAGCCTGAACAAATACCTCGGCGGCAATGTAAAAGCCCTAAGAATCTCCATTTTAGTCGGCTCGGGCATCACCTTATTCGCCTACATTTTATGGCAACTTTCCACCCACGGCTTGCTGACCCAAAACGCGTTTTTACAAGTCTTACAACAAGATCCTACGCTGAACGGTTTGGTCACCGCCACCTTAACCATCACACAAAGCAGCATCATGGCAAACGCGGTGAAAATCTTCTCTACCCTAGCACTCATCACCTCATTTTTAGGTGTCGGCATCGGCTTATTGGAATGTATAGAAGACTTGTTAAAACGCTCATTTAATGTTCACACCAGGCGCTTCTCTTTGGGTTTACTCACGTTCATTCCGCCCATCGTTTTCACCCTGTTCTACCCGCAAGGCTTCATTTTAGCCTTAGGCTACGCCGGACAAATGTTCGCCTTTTACGCCGTCGTCCTACCGGTCGCCCTCGTGTGGAAAGCGCGCAAAATCCACCCGAACCTGCCATATAAAGTCTTGGGTGGCAATTTAACACTGGCGGTGGCGTTGGTCCTGGGCGTGATCATCACCTCCATCCCCTTCGCCATCCGCGCGGGTTATTTGCCGTTTGTAGTGGGC","","","43240","MNKTVGSTLLVAGTMIGAGMLAMPLTSAGIGFSFTLLLLLGLWGLLTFTALLFVELYQTAPSDAGIGTLAEQYFGRPGRIIATAVLIIFLYALIAAYISGGGSLLADTLPTIADKDTTGKIAVLIFTLFFGMFIVIGTHSVDKINRLLFFTMIGTFIVVLALMLPEIKLDNLMAMPIDNALIISAGPVFFTAFGFHGSIPSLNKYLGGNVKALRISILVGSGITLFAYILWQLSTHGLLTQNAFLQVLQQDPTLNGLVTATLTITQSSIMANAVKIFSTLALITSFLGVGIGLLECIEDLLKRSFNVHTRRFSLGLLTFIPPIVFTLFYPQGFILALGYAGQMFAFYAVVLPVALVWKARKIHPNLPYKVLGGNLTLAVALVLGVIITSIPFAIRAGYLPFVVG","1156308","[FUNCTION] Involved in transporting tyrosine across the cytoplasmic membrane (by similarity). [SUBCELLULAR LOCATION] Integral membrane protein. inner membrane (by similarity). [SIMILARITY] Belongs to the mtr/tnaB/tyrO permease family.","tyrosine-specific transport protein","Inner membrane, Cytoplasm","","
InterPro
IPR002091
Family
Aromatic amino acid permease
PR00166\"[9-32]T\"[36-55]T\"[81-101]T\"[147-167]T\"[181-203]T\"[220-239]T\"[281-300]T\"[316-334]T\"[337-356]TAROAAPRMEASE
PF03222\"[3-391]TTrp_Tyr_perm
InterPro
IPR013059
Family
Tryptophan/tyrosine transporter
TIGR00837\"[6-384]TaraaP: aromatic amino acid transport protei
InterPro
IPR013061
Family
Tryptophan/tryrosine permease
PS00594\"[16-32]TAROMATIC_AA_PERMEASE_1
noIPR
unintegrated
unintegrated
signalp\"[1-51]?signal-peptide
tmhmm\"[5-24]?\"[30-52]?\"[80-100]?\"[119-137]?\"[147-167]?\"[177-197]?\"[212-232]?\"[276-294]?\"[309-329]?\"[335-355]?\"[370-390]?transmembrane_regions


","No hits to the COGs database.","Significant hit (5.5e-121) to 6/6 blocks of the IPB002091 family, which is described as \"Aromatic amino acids permease\". Interpro entry for IP:IPR002091. IPB002091A 7-50 7.4e-24 IPB002091B 68-105 1.4e-20 IPB002091C 187-202 7.4e-11 IPB002091D 217-259 8.6e-20 IPB002091E 277-301 1.6e-10 IPB002091F 310-360 4.4e-29Significant hit ( 2.4e-07) to 2/2 blocks of the IPB002422 family, which is described as \"Permeases for amino acids and related compounds, family II\". Interpro entry for IP:IPR002422. IPB002422A 14-24 6.5e-06 IPB002422B 287-293 16","Residues 1 to 83 match (1e-16) PD:PD407890 which is described as PROTEOME COMPLETE TYROSINE-SPECIFIC TYROSINE PERMEASE AMINO-ACID INNER MEMBRANE TRANSMEMBRANE TYRP ","","","","","","","","","","","Tue Jan 7 12:32:54 2003","Tue Jan 7 12:32:54 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01704 is paralogously related to AA02973 (1e-162), AA01245 (1e-128), AA00468 (8e-60) and AA00092 (1e-06).","","","","","","Residues 3 to 391 (E-value = 1.4e-188) place AA01704 in the Trp_Tyr_perm family which is described as Tryptophan/tyrosine permease family (PF03222)","","","","","Wookey,P.J. and Pittard,A.J. DNA sequence of the gene (tyrP) encoding the tyrosine-specific transport system of Escherichia coli. J. Bacteriol. 170 (10): 4946-4949 (1988) [PubMed: ]. Sarsero,J.P., Wookey,P.J., Gollnick,P., Yanofsky,C. and Pittard,A.J. . A new family of integral membrane proteins involved in transport of aromatic amino acids in Escherichia coli. J. Bacteriol. 173(10): 3231-3234.1991 PubMed: 2022620.","","Tue Jan 7 12:32:54 2003","1","","","" "AA01705","1157783","1158040","258","GTGGAAAATCCAAGAGAATTTTACGATTATTTTATGGTGTTGAACGGGCAATTCGTGGGTTATAGCCAAATCAGCCATTGCACCTCTGAACTTGATGTAACGAATTATTTACAGTTAGACGAGAATATCCTCGATATTATCGTGCTGAAATGGTGTGACGGCAGTATTTGGAGGAACAGGATAAATTCCGTATGTCGGGGATTTTTCGTGATGTTTATCTGCTGTAACGGGATGCGCAGTATTTGCAGGATTTTTCAT","","","8924","VENPREFYDYFMVLNGQFVGYSQISHCTSELDVTNYLQLDENILDIIVLKWCDGSIWRNRINSVCRGFFVMFICCNGMRSICRIFH","1158005","[CATALYTIC ACTIVITY] Hydrolysis of terminal, non-reducing beta-D-galactose residues in beta-D-galactosides.[SIMILARITY] Belongs to family 2 of glycosyl hydrolases. ","beta-galactosidase","Cytoplasm","","
InterPro
IPR006104
Domain
Glycoside hydrolase family 2, carbohydrate-binding
PF02837\"[14-58]TGlyco_hydro_2_N
noIPR
unintegrated
unintegrated
G3DSA:2.60.120.260\"[8-59]Tno description
tmhmm\"[67-85]?transmembrane_regions


","BeTs to 3 clades of COG3250COG name: Beta-galactosidase/beta-glucuronidaseFunctional Class: GThe phylogenetic pattern of COG3250 is --------v--lb-e---s-------Number of proteins in this genome belonging to this COG is","","Residues 11 to 69 match (3e-10) PD:PD002797 which is described as BETA-GALACTOSIDASE HYDROLASE GLYCOSIDASE LACTASE BETA-GLUCURONIDASE COMPLETE PROTEOME PRECURSOR PLASMID LYSOSOME ","","","","","","","","","","","Tue Jan 7 12:39:28 2003","Tue Jan 7 12:39:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01705 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Bassias,J. and Bruckner,R. Regulation of lactose utilization genes in Staphylococcus xylosus. J. Bacteriol. 180 (9): 2273-2279 (1998) [PubMed: 9573174].Nagano,H., Kawaguchi,T., Omori,M., Shoji,Z. and Arai,M. Molecular cloning and nucleotide sequence of the beta-galactosidase gene from Enterobacter cloacae GAO. Biosci. Biotechnol. Biochem. 58 (10): 1866-1869 (1994) [PubMed: 7765512].Buchel,D.E., Gronenborn,B. and Muller-Hill,B. Sequence of the lactose permease gene . Nature 283 (5747): 541-545 (1980) [PubMed: 6444453].Fowler,A.V. and Smith,P.J. The active site regions of lacZ and ebg beta-galactosidases are homologous. J. Biol. Chem. 258 (17): 10204-10207 (1983) [PubMed: 6411710].Herrchen,M. and Legler,G. Identification of an essential carboxylate group at the active site of lacZ beta-galactosidase from Escherichia coli. Eur. J. Biochem. 138 (3): 527-531 (1984) [PubMed: 6420154].Gebler,J.C., Aebersold,R. and Withers,S.G. Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) beta-galactosidase from Escherichia coli. J. Biol. Chem. 267 (16): 11126-11130 (1992) [PubMed: 1350782]. ","","Tue Jan 7 12:39:28 2003","1","","","" "AA01708","1158653","1158276","378","TTGTGTAGCACATTAAACTCGCCATATCTTACACTAATTACAAGAATGCCGAAAAACACTTTATTGTTTTTTCGCGAATCCTTAAAATCAGCACAAATTCACTCAAAAGGAAACATTATGTTCGTTACAATTTATGGTCGCCTAAGCTGCCCTTATTGCGTTCGCGCCAAAACCTTAGCGGAAAAATTAAAAAATACTGTGGAAAATTTTGATTATCGTTACATCGACATCATCGAGCAAGGCATGAGCAAAGAAGACATCGCCAACATCATCGGCAAGCCGGTGCAAACCGTGCCGCAGGTTCTGATTGGTGACAAGCCGATCGGCGGTTGCACCGATTTTGAGGCCTTAATGGCCGAACAGTTTGGCGATATTGAT","","","14153","LCSTLNSPYLTLITRMPKNTLLFFRESLKSAQIHSKGNIMFVTIYGRLSCPYCVRAKTLAEKLKNTVENFDYRYIDIIEQGMSKEDIANIIGKPVQTVPQVLIGDKPIGGCTDFEALMAEQFGDID","1158275","[FUNCTION] Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins (by similarity)[SUBUNIT] Monomer (by similarity). [SUBCELLULAR LOCATION] Cytoplasmic (by similarity). [SIMILARITY] Belongs to the glutaredoxin family. ","glutaredoxin","Cytoplasm","","
InterPro
IPR002109
Domain
Glutaredoxin
PF00462\"[42-108]TGlutaredoxin
InterPro
IPR011767
Active_site
Glutaredoxin active site
PS00195\"[44-59]TGLUTAREDOXIN
InterPro
IPR011902
Family
Glutaredoxin, GrxA
TIGR02183\"[41-126]TGRXA: Glutaredoxin, GrxA family
InterPro
IPR012335
Domain
Thioredoxin fold
G3DSA:3.40.30.10\"[40-124]Tno description
InterPro
IPR014025
Domain
Glutaredoxin subgroup
PR00160\"[42-60]T\"[91-104]T\"[105-118]TGLUTAREDOXIN
noIPR
unintegrated
unintegrated
PTHR10168\"[50-118]TGLUTAREDOXIN
PTHR10168:SF16\"[50-118]TGLUTAREDOXIN-1, GRX1


","BeTs to 13 clades of COG0695COG name: Glutaredoxin and related proteinsFunctional Class: OThe phylogenetic pattern of COG0695 is aom-k-y-vdrlbcefghsn-jx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 5.7e-15) to 2/2 blocks of the IPB002109 family, which is described as \"Glutaredoxin\". Interpro entry for IP:IPR002109. IPB002109A 42-56 2.6e-05 IPB002109B 94-113 6.2e-08","Residues 42 to 111 match (1e-18) PD:PD328381 which is described as GLUTAREDOXIN COMPLETE PROTEOME CENTER ELECTRON REDOX-ACTIVE PROBABLE FAMILY THIOLTRANSFERASE ACETYLATION ","","","","","","","","","","","Tue Jan 7 12:45:50 2003","Tue Jan 7 12:45:50 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01708 is paralogously related to AA01514 (1e-05).","","","","","","Residues 41 to 126 (E-value = 3.5e-18) place AA01708 in the Glutaredoxin family which is described as Glutaredoxin (PF00462)","","","","","Hoog,J.O., von Bahr-Lindstrom,H., Jornvall,H. and Holmgren,A. Cloning and expression of the glutaredoxin (grx) gene of Escherichia coli. Gene 43 (1-2): 13-21 (1986) [PubMed: 3530878].2. Hoog,J.O., Jornvall,H., Holmgren,A., Carlquist,M. and Persson,M. The primary structure of Escherichia coli glutaredoxin. Distant homology with thioredoxins in a superfamily of small proteins witha redox-active cystine disulfide/cysteine dithiol. Eur. J. Biochem. 136 (1): 223-232 (1983) [PubMed: 6352262].Sodano,P., Chary,K.V., Bjornberg,O., Holmgren,A., Kren,B., Fuchs,J.A. and Wuthrich,K. Nuclear magnetic resonance studies of recombinant Escherichia coli glutaredoxin. Sequence-specific assignments and secondary structuredetermination of the oxidized form. Eur. J. Biochem. 200 (2): 369-377 (1991) [PubMed: 1889405].Sodano,P., Xia,T.H., Bushweller,J.H., Bjornberg,O., Holmgren,A., Billeter,M. and Wuthrich,K. Sequence-specific 1H n.m.r. assignments and determination of the three-dimensional structure of reduced Escherichia coliglutaredoxin. J. Mol. Biol. 221 (4): 1311-1324 (1991) [PubMed: 1942053]. Xia,T.H., Bushweller,J.H., Sodano,P., Billeter,M., Bjornberg,O., Holmgren,A. and Wuthrich,K. NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins. Protein Sci. 1 (3): 310-321 (1992) [PubMed: 1304339].","","Tue Jan 7 12:45:50 2003","1","","","" "AA01709","1158663","1159394","732","ATGTCTGAGAAAAAATATACCTCCGAAACCTTAGATTGTATTTTAGCCCACCGTTCTATTCGCCGTTTTACCGATGAGCCTGTTGATGACAATATTATCGACCGTTTGGTGAATGCGGCGCGTTTTGCTTCTACGTCCAACCATTTGCAATGTGTTTCCATCGTGCGTATTACCGATCAGGCGATTCGTGAGCAAATGATGGTGTACAGCTCCAATCAGGAGTATGTGAAATCCGCGCCTGAATTTTGGGTATTCTGCGTCGATTTTAATAAGCATAAACAAATTTGCCCGACGGCGCAGCTGGATTATGCGGAAGTGTTGCTGATCGGCGCGGTGGACACCGGCATTATGTCGCAAAACGTGCTGTTGGCGGCGGAAAGTTTAGGATTAGGCGGGGTGTATATCGGATCCTTGCGTAATGAAATGGAAGCAGTGGGCAAATTGCTCAATCTGCCGGAACATTGCCTGCCGATGGTGGGAATGTGTTTGGGCTATCCGGATCAGGATCCGCCGAGCAAGCCACGCCTGCCGAAAGAAACCCTGTTTTTTGAAAACCGTTATCAGCCGTTGGATACCACCAAACTGGACGAATATAACGCGACGGTTGCTGACTATTATTGTCAGCGCAGCAACATTGACATGGATTGGTCGCGCAATGTGATAAAAAGTTTGGATAAGCCGATTCGTCCGAACGTATTGGCTTATTTGCAGCAACAGGGCTTTATTAAAAAA","","","27782","MSEKKYTSETLDCILAHRSIRRFTDEPVDDNIIDRLVNAARFASTSNHLQCVSIVRITDQAIREQMMVYSSNQEYVKSAPEFWVFCVDFNKHKQICPTAQLDYAEVLLIGAVDTGIMSQNVLLAAESLGLGGVYIGSLRNEMEAVGKLLNLPEHCLPMVGMCLGYPDQDPPSKPRLPKETLFFENRYQPLDTTKLDEYNATVADYYCQRSNIDMDWSRNVIKSLDKPIRPNVLAYLQQQGFIKK","1159393","[FUNCTION] Reduction of nitroaromatic compounds using NADH. Reduces nitrofurazone by a ping-pong bi-bi mechanismpossibly to generate a two-electron transfer product. Major component of the oxygen-insensitive nitroreductase activity in E.coli. Involved in bioluminescence. It is a good supplier of reduced flavin mononucleotide (FMNH2) to the bioluminescencereaction.[COFACTOR] FMN. [SIMILARITY] Belongs to the flavin oxidoreductase frp family. ","glutathione-S-transferase-nitroreductase A fusion protein; modulator of drug activity A","Cytoplasm","","
InterPro
IPR000415
Family
Nitroreductase
PF00881\"[14-165]TNitroreductase
noIPR
unintegrated
unintegrated
G3DSA:3.40.109.10\"[7-244]Tno description
PTHR23026\"[39-228]TNADPH NITROREDUCTASE
PTHR23026:SF46\"[39-228]TNAD(P)H-FLAVIN OXIDOREDUCTASE


","No hits to the COGs database.","Significant hit ( 1.2e-05) to 2/2 blocks of the IPB000415 family, which is described as \"Nitroreductase family\". Interpro entry for IP:IPR000415. IPB000415A 75-87 6.6 IPB000415B 120-138 0.00092","Residues 14 to 76 match (5e-08) PD:PD439947 which is described as PROTEOME COMPLETE NADH NITROREDUCTASE DEHYDROGENASE OXIDOREDUCTASE ENTEROBACTER OXIDOREDUCTASE YCND NADPH-FLAVIN ","","","","","Mon Feb 17 11:31:45 2003","","","","","","Tue Jan 7 12:53:51 2003","Tue Jan 7 12:53:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01709 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 14 to 165 (E-value = 6.3e-37) place AA01709 in the Nitroreductase family which is described as Nitroreductase family (PF00881)","","","","","Zenno,S., Kobori,T., Tanokura,M. and Saigo,K. Conversion of NfsA, the major Escherichia coli nitroreductase, to a flavin reductase with an activity similar to that of Frp, a flavinreductase in Vibrio harveyi, by a single amino acid substitution. J. Bacteriol. 180 (2): 422-425 (1998) PubMed: 9440535.Zenno,S., Koike,H., Kumar,A.N., Jayaraman,R., Tanokura,M. and Saigo,K. Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase. J. Bacteriol. 178 (15): 4508-4514 (1996) PubMed: 8755878.Lei,B., Liu,M., Huang,S. and Tu,S.C. Vibrio harveyi NADPH-flavin oxidoreductase: cloning, sequencing and overexpression of the gene and purification and characterization ofthe cloned enzyme. J. Bacteriol. 176 (12): 3552-3558 (1994) PubMed: 8206832.Carroll CC, Warnakulasuriyarachchi D, Nokhbeh MR, Lambert IB.Salmonella typhimurium mutagenicity tester strains that overexpress oxygen-insensitive nitroreductases nfsA and nfsB.Mutat Res. 2002 Apr 25;501(1-2):79-98.PMID: 11934440Paterson ES, Boucher SE, Lambert IB.Regulation of the nfsA Gene in Escherichia coli by SoxS.J Bacteriol. 2002 Jan;184(1):51-8.PMID: 11741843","","Mon Feb 17 11:31:45 2003","1","","","" "AA01710","1159488","1160318","831","ATGGATATTTTGGATCCGAATCGTTGCCTGATAAAACTCCAAAAAAATCCACCGCACTTTGTGTTGTATTATCAAGCGGACGCGGAGAGTGAGGCGCAGCTTTTGCCACATTATGACGCGGTGTTGCCCCGCTTCGGCACCACCAGTATGCTTATGGGCTGTCGCGTGTTGTATTATTTCCAAGCGCAAGGCGTTCCTTGTTTGAATAACGTCGATGCCTTTCGCAACGCCCGCGATAAATGGCTTAGTCTGCAAATGTTGCTGCAACAAGGTGTTGCGGTGCCGGATTCTTTGCTCGCCGGCATTGAAGTCAATGCTAATCATGCGGTGCAACACATCGGCGCGCCAACCATTTTGAAAACCTTGAGCGGTTCTCAGGGCATCGGCGTGATTCTGGCGGAGCGAACAAAAAGTGCGGTCAGTATTTTGGAAACTTTAAAACAAGCGGACGTGCCGGTGTTGTTGCAGGAATTTGTGGCAGAAGCCGACGGCACGGATGTACGCTGTTTTGTGATTGGCGGACGGGTGGTTGCCGCCATGCAACGGGTCGGGCAAAACGGTGAATTTCGCGCCAATTGTCATCGTGGCGCGACAGCAGAAAAAGTGGTGTTGACCGAACAGGAAAAGCAAATCGCCTTGCGTGCGACCAACGCGCTCGGCTTAGATGTTGCCGGTGTGGATTTGATTCGCTCGGCGAAAGGCCCGTTGGTGTTGGAAGTGAATGCCAGCCCGGGGCTTGAAATGATTGAGAAAACCAGCGGTATTAATATCGCGTTACAAATGATTTTATATTTAGAGCAGAAAATCCGTAATCAAGTTGGAGTAATAAAA","","","33476","MDILDPNRCLIKLQKNPPHFVLYYQADAESEAQLLPHYDAVLPRFGTTSMLMGCRVLYYFQAQGVPCLNNVDAFRNARDKWLSLQMLLQQGVAVPDSLLAGIEVNANHAVQHIGAPTILKTLSGSQGIGVILAERTKSAVSILETLKQADVPVLLQEFVAEADGTDVRCFVIGGRVVAAMQRVGQNGEFRANCHRGATAEKVVLTEQEKQIALRATNALGLDVAGVDLIRSAKGPLVLEVNASPGLEMIEKTSGINIALQMILYLEQKIRNQVGVIK","1160317","[FUNCTION] Responsible for the addition of glutamic acid residuesto the C-terminus of ribosomal protein S6 (By similarity).","ribosomal protein S6 modification protein","Cytoplasm","","
InterPro
IPR004666
Family
S6 modification enzyme RimK
TIGR00768\"[1-265]TrimK_fam: alpha-L-glutamate ligases, RimK f
InterPro
IPR011761
Domain
ATP-grasp fold
PS50975\"[84-266]TATP_GRASP
InterPro
IPR013651
Domain
ATP-grasp fold, RimK-type
PF08443\"[77-265]TRimK
InterPro
IPR013816
Domain
ATP-grasp fold, subdomain 2
G3DSA:3.30.470.20\"[138-256]Tno description
noIPR
unintegrated
unintegrated
PTHR21621\"[33-269]TRIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN


","BeTs to 12 clades of COG0189COG name: Glutathione synthase/Ribosomal protein S6 modification enzyme (glutaminyl transferase)Functional Class: H,JThe phylogenetic pattern of COG0189 is aom-kz---d--bcefghsn-j---wNumber of proteins in this genome belonging to this COG is","","Residues 88 to 267 match (4e-11) PD:PD432181 which is described as GLUTATHIONE SYNTHETASE COMPLETE PROTEOME LIGASE GSH GSH-S ATP-BINDING GSHASE SYNTHASE ","","","","","","","","","","","Tue Jan 7 12:56:27 2003","Tue Jan 7 12:56:27 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01710 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 172 (E-value = 9.1e-07) place AA01710 in the ATP-grasp family which is described as ATP-grasp domain (PF02222)","","","","","Kang,W.K., Icho,T., Isono,S., Kitakawa,M. and Isono,K.1989. Characterization of the gene rimK responsible for the addition of glutamic acid residues to the C-terminus of ribosomal protein S6 in. Escherichia coli K12. Mol. Gen. Genet. 217(2-3): 281-288. PubMed: 2570347.","","Tue Jan 7 12:56:27 2003","1","","","" "AA01711","1160374","1160562","189","ATGCAATTAAAATTTATTGACGACGATGTGCGTTTTGTGAATTGCAGCACCCTGCATCCACGTCACGACATGACGTTTTTGCTCAATGAAGTGCATAATTGGTGTCCCAATCTAAAGACGAAAATCCACTCATTTGCGGTGTTGGTTTGTCAGTTATTGGGCGGAACATATCGGCTTTTTGTGCGGCAT","","","7552","MQLKFIDDDVRFVNCSTLHPRHDMTFLLNEVHNWCPNLKTKIHSFAVLVCQLLGGTYRLFVRH","1160561","","conserved hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
tmhmm\"[42-61]?transmembrane_regions


","No hits to the COGs database.","","Residues 1 to 55 match (2e-10) PD:PD107540 which is described as PROTEOME COMPLETE PM0825 VC1892 YCFP STY1250 YPO1616 ESTERASE ","","","","","","","","","","","","Tue Jan 7 12:57:33 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01711 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01715","1161222","1160620","603","ATGAAATTAAAATCGCTGTTATTCATTTTAACTTTATTTCCTACCGCACTTTCGGCGCACTGGCTCAATGTCGGAAACGCCGATTATAACTGGGGTCTGTTCCTCGTTTATACCATCGAGTTAGAAACGGAAAACGGGGCTTATGAAGCCAATCAGTTGCCGTTTATGCTTTCCTTTAAATACGAAAAACCCATTGAAGGCAAAAATTTTGCCATCAGCCTGGCGAAAGAAATGGAACATCTCAACGTGGATAAAGCGCAAGGCGATTTGTGGTTGAAGCAAATGCAGCAGCTTTTTCCCGACTTCTCACCTAACGACATTTTGCGTTTTGTCGCCCTGCCGGAAAAAAGCTATTTCATTTTAAACGACACCATTTTGGATCATGAATTCGAACCGCAATTTGCACAAGCGCTGATTAGCATTTGGTTGTCGCCGAACAGTAACTTTATTCAATTACAACCGCAGTTATTGGGAAAAGAAAAAAATGCAAACTCACCGGAGAAGTTTAAACGCACGCCGGAAGTGGACCCGCTGGGCGAAGATGACGCCAGCCCGCAACTGCCGCCGAATTTTCAATTTCAGGATCAAGATCCGGAATTAGGT","","","23079","MKLKSLLFILTLFPTALSAHWLNVGNADYNWGLFLVYTIELETENGAYEANQLPFMLSFKYEKPIEGKNFAISLAKEMEHLNVDKAQGDLWLKQMQQLFPDFSPNDILRFVALPEKSYFILNDTILDHEFEPQFAQALISIWLSPNSNFIQLQPQLLGKEKNANSPEKFKRTPEVDPLGEDDASPQLPPNFQFQDQDPELG","1160619","","conserved hypothetical protein","Periplasm, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","","Residues 19 to 161 match (3e-47) PD:PD357407 which is described as PROTEOME COMPLETE PM0824 VC1124 HI1399 ","","","","","","","","","","","","Tue Jan 7 13:13:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01715 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01717","1162720","1161329","1392","ATGGCATTTCGCATTGAAAAAGACACTATGGGTGAAGTTCAAGTTCCGGCAGACAAATATTGGGCTGCACAAACCGAACGTTCCCGCAATAATTTTAAAATCGGTCCTGCGGCATCTATGCCACATGAAATTATCGAAGCCTTTGGTTATTTGAAAAAAGCGGCGGCGTTTGCCAATGCGGATCTCGGCGTATTGCCTGCGGAAAAACGCGATTTGATCGCGCAAGCCTGCGATGAAATTTTAGCCAACAAATTAGACGATCAATTCCCGTTGGTTATCTGGCAAACCGGCTCCGGTACGCAATCCAACATGAACGTGAACGAAGTGGTGGCAAACCGCGCACACGTTTTACACGGCGGTAAATTAGGCGAAAAATCCATCATTCACCCGAATGACGATGTGAATAAATCCCAATCCTCCAACGACACCTTCCCGACAGCAATGCACATTGCGGCTTACAAAAAAGTGGTAGAAACTACCATTCCTGCAGTAGAACGTTTGCAAAAAACCTTCGCGGCAAAATCCGAAGCCTTCAAAGATGTGGTGAAAATCGGTCGTACGCATTTAATGGACGCAACCCCGCTCACATTAGGTCAGGAATTCTCCGCTTATGCGGCGCAATTGCACTTCGGTTTAATCGCGTTGAAAAATACCCTGCCGCATTTGCGTCAATTAGCCCTCGGCGGTACTACTGTGGGTACGGGGTTGAATACACCGAAAGGTTATGACGTGAAAGTGGCGGAATACATCGCGAAATTTACCGGTTTGCCGTTCATCACTGCCGAAAACAAATTCGAAGCCTTGGCGGCGCATGATGCCATCGTGGAAACCCACGGTGCATTACGTCAATTAGCCATGAGCTTGTTCAAAATCGCCAACGACATTCGTTTATTGGCATCCGGTCCGCGTTCCGGTATCGGCGAAATCTTAATTCCGGAAAATGAACCGGGCTCTTCCATCATGCCGGGTAAAGTGAATCCGACCCAATGCGAAGCCATGACCATGGTGTGCGCGCAAGTGTTCGGTAACGACACCACCATCTCGTTCGTCGGTTCACAAGGTCATTTCCAATTGAACGTGTTCAACCCGGTGATGATCGCCAACTTCCTGCAATCCGCCCAATTATTGGCAGACGCCTGCGTTTCCTTCGACGAACACTGCGCAACCGGTATCGAGCCGAACTATCTGCGCATTAAACAACAACTTGAAAATTCATTGATGTTGGTGACCGCACTTAATACCCATATCGGCTACGAAAATGCGGCGAAAATCGCAAAAACCGCACACAAAAACGGTACCACCTTGCGTGAAGAAGCCATTAACCTCGGTTTGGTTTCCGCCGAAGACTTCGACAAATGGGTGCGTCCGGAAGATATGGTGGGCAGCTTAAAA","","","50418","MAFRIEKDTMGEVQVPADKYWAAQTERSRNNFKIGPAASMPHEIIEAFGYLKKAAAFANADLGVLPAEKRDLIAQACDEILANKLDDQFPLVIWQTGSGTQSNMNVNEVVANRAHVLHGGKLGEKSIIHPNDDVNKSQSSNDTFPTAMHIAAYKKVVETTIPAVERLQKTFAAKSEAFKDVVKIGRTHLMDATPLTLGQEFSAYAAQLHFGLIALKNTLPHLRQLALGGTTVGTGLNTPKGYDVKVAEYIAKFTGLPFITAENKFEALAAHDAIVETHGALRQLAMSLFKIANDIRLLASGPRSGIGEILIPENEPGSSIMPGKVNPTQCEAMTMVCAQVFGNDTTISFVGSQGHFQLNVFNPVMIANFLQSAQLLADACVSFDEHCATGIEPNYLRIKQQLENSLMLVTALNTHIGYENAAKIAKTAHKNGTTLREEAINLGLVSAEDFDKWVRPEDMVGSLK","1161328","[CATALYTIC ACTIVITY] (S)-malate = fumarate + H(2)O.[PATHWAY] Tricarboxylic acid cycle.[SUBUNIT] Homotetramer (By similarity).","fumarate hydratase, class II","Cytoplasm","","
InterPro
IPR000362
Domain
Fumarate lyase
PR00149\"[134-152]T\"[180-196]T\"[271-298]T\"[317-333]TFUMRATELYASE
PF00206\"[11-342]TLyase_1
PS00163\"[317-326]TFUMARATE_LYASES
InterPro
IPR003031
Domain
Delta crystallin
PR00145\"[133-155]T\"[175-195]T\"[317-333]TDCRYSTALLIN
InterPro
IPR005677
Family
Fumarate hydratase, class II
TIGR00979\"[3-461]TfumC_II: fumarate hydratase, class II
noIPR
unintegrated
unintegrated
PD727516\"[1-26]TFUMC_PASMU_Q9CMK1;
G3DSA:1.10.275.10\"[1-138]Tno description
G3DSA:1.10.40.30\"[408-462]Tno description
G3DSA:1.20.200.10\"[139-407]Tno description
PTHR11444\"[3-462]TASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE
PTHR11444:SF1\"[3-462]TASPARTATE AMMONIA LYASE


","BeTs to 16 clades of COG0114COG name: FumaraseFunctional Class: CThe phylogenetic pattern of COG0114 is -o---zy--dr-bcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 9.1e-15) to 2/2 blocks of the IPB000362 family, which is described as \"Fumarate lyase\". Interpro entry for IP:IPR000362. IPB000362A 185-198 3.1e-06 IPB000362B 317-327 8e-07","Residues 179 to 205 match (7e-08) PD:PD593016 which is described as LYASE ASPARTATE PROTEOME AMMONIA-LYASE COMPLETE ASPARTASE L-ASPARTASE CLASS AMMONIUM FUMC ","","","","","","","","","","","Tue Jan 7 13:18:49 2003","Tue Jan 7 13:18:49 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01717 is paralogously related to AA01277 (2e-99) and AA00218 (2e-10).","","","","","","Residues 11 to 342 (E-value = 1.4e-162) place AA01717 in the Lyase_1 family which is described as Lyase (PF00206)","","","","","Friedberg,D., Peleg,Y., Monsonego,A., Maissi,S., Battat,E., Rokem,J.S. and Goldberg,I. The fumR gene encoding fumarase in the filamentous fungus Rhizopus oryzae: cloning, structure and expression. Gene 163 (1): 139-144 (1995) [PubMed: 7557464]Ueda,Y., Yumoto,N., Tokushige,M., Fukui,K. andOhya-Nishiguchi,H. Purification and characterization of two types of fumarase from Escherichia coli. J. Biochem. 109(5): 728-733, 1991. PubMed: 1917897. Weaver,T. and Banaszak,L. Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli. Biochemistry 35(44): 13955-13965, 1996. PubMed: 8909293. Woods,S.A., Miles,J.S., Roberts,R.E. and Guest,J.R. Structural and functional relationships between fumarase and aspartase. Nucleotide sequences of the fumarase (fumC) and aspartase (aspA) genes of Escherichia coli K12. Biochem. J. 237(2): 547-557, 1986. PubMed: 3541901.","","Tue Jan 7 13:18:49 2003","1","","","" "AA01718","1162930","1163376","447","ATGCCAAAAAATGCGCAATTCTACCTGCTTTCCGATGCCTCTCCCGCACAGACGAATTTGTCTGCGGTGGAAAGCCTTGCCTGCAATTTGGCGGCGTCCGCCTGGCGTTTGGGAAAACGGGTTCTGTTGGCGTGTGAAAATGAAGCGCAGGCGCTCAATATTGATGAAGCCCTTTGGCAACGGGAACCGGACGAATTCGTCCCGCACAACCTTTCCGGCGAAGCCACCACGTATGCCACGCCCATCGAAATCAGCTGGACGGGCAAACGCAACGCACAAAGCCGCGATTTGCTGATTAATTTACAACCGCAGCTGCCGGAATTCATCAACAGCTTTAACCAAATTATCGATTTCGTACCCGCCGAAGAACAACAAAAAGCTTTAGCGCGGGAACGTTATAAACAATTGAGGCAGTTGGGCTGGGAATTGAGTACGGAGCAGGCGGGG","","","16756","MPKNAQFYLLSDASPAQTNLSAVESLACNLAASAWRLGKRVLLACENEAQALNIDEALWQREPDEFVPHNLSGEATTYATPIEISWTGKRNAQSRDLLINLQPQLPEFINSFNQIIDFVPAEEQQKALARERYKQLRQLGWELSTEQAG","1163375","[FUNCTION] DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity (by similarity). [catalytic activity] N deoxynucleoside triphosphate = N diphosphate + {DNA}(N). [SUBUNIT] Contains a core (composed of alpha, epsilon, andtheta chains) that associates with a tau subunit which allow the core dimerization to form the polIII' complex. polIII'associates with the gamma complex (composed of chains gamma, delta, delta', psi, and chi) and with the beta chain(by similarity). ","DNA polymerase III, chi subunit","Periplasm","","
InterPro
IPR007459
Family
DNA polymerase III chi subunit, HolC
PF04364\"[2-148]TDNA_pol3_chi
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.10110\"[2-149]Tno description
PTHR11963\"[26-95]TLEUCINE AMINOPEPTIDASE-RELATED
PTHR11963:SF1\"[26-95]Tgb def: DNA polymerase III, chi subunit (EC 2.7.7.7)


","BeTs to 7 clades of COG2927COG name: DNA polymerase III chi subunitFunctional Class: LThe phylogenetic pattern of COG2927 is --------------efghsn-jx---Number of proteins in this genome belonging to this COG is","","Residues 38 to 147 match (1e-44) PD:PD398238 which is described as COMPLETE PROTEOME SUBUNIT POLYMERASE CHI III DNA HOLC ","","","","","","","","","","","Tue Jan 7 13:24:32 2003","Tue Jan 7 13:24:32 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01718 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 148 (E-value = 1.1e-67) place AA01718 in the DNA_pol3_chi family which is described as DNA polymerase III chi subunit, HolC (PF04364)","","","","","Xiao,H., Crombie,R., Dong,Z., Onrust,R. and O'Donnell,M.DNA polymerase III accessory proteins. III. holC and holD encoding chi and psi J. Biol. Chem. 268 (16), 11773-11778 (1993) PubMed: 8389364 Carter,J.R., Franden,M.A., Lippincott,J.A. and McHenry,C.S. Identification, molecular cloning and characterization of the gene encoding the chi subunit of DNA polymerase III holoenzyme of Escherichia coli Mol. Gen. Genet. 241 (3-4), 399-408 (1993) PubMed: 8246893 O'Donnell,M. Accessory protein function in the DNA polymerase III holoenzyme from E. coli Bioessays 14 (2), 105-111 (1992) PubMed: 1575709 Nwankwo,D.O., Moran,L.S., Slatko,B.E., Waite-Rees,P.A., Dorner,L.F., Benner,J.S. and Wilson,G.G. Cloning, analysis and expression of the HindIII R-M-encoding genes. Gene 150 (1): 75-80 (1994) [PubMed: 7959067].","","Tue Jan 7 13:24:32 2003","1","","","" "AA01720","1163418","1163543","126","ATGAACGACATCACTTTTTATCAATGTTTCCAAGATGATATTCTCGCCGGACGAAAAACCATCACCATTCGGGATAAATCCGAAAGCCACTTTAAAGCCGGTGATATTTTACGTGTCGGGCGGTTT","","","4890","MNDITFYQCFQDDILAGRKTITIRDKSESHFKAGDILRVGRF","1163543","","conserved hypothetical protein","Cytoplasm","This sequence is similar to gi|42631695, a predicted hypothetical protein from Haemophilus influenzae R2866.","
InterPro
IPR008314
Family
Uncharacterised conserved protein UCP029143
PD030073\"[2-42]TYQFB_ECOLI_Q46828;
PF06164\"[1-42]TDUF978


","No hits to the COGs database.","","Residues 3 to 42 match (6e-12) PD:PD030073 which is described as COMPLETE PROTEOME YQFB CYTOPLASMIC HI1394 STY3206 ORF16 VC1576 TEX YPO1778 ","","","","","","","","","","","","Thu Feb 26 14:44:55 2004","Thu Feb 26 14:44:55 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01720 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 14:44:55 2004","","","","","Residues 1 to 42 (E-value = 5.6e-06) place AA01720 in the DUF978 family which is described as Bacterial protein of unknown function (DUF978) (PF06164)","","","","","","","","1","","","" "AA01721","1163452","1163577","126","ATGATATTCTCGCCGGACGAAAAACCATCACCATTCGGGATAAATCCGAAAGCCACTTTAAAGCCGGTGATATTTTACGTGTCGGGCGGTTTTAAGATGATGAATATTTCTGCACAATTGAAGTGT","","","4616","MIFSPDEKPSPFGINPKATLKPVIFYVSGGFKMMNISAQLKC","1163577","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 14:22:01 2004","Thu Feb 26 14:22:01 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01721 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 14:22:01 2004","","","","","","","","","","","","","1","","","" "AA01722","1163574","1163699","126","GTGTTAAGTGTTTCACCGATTACCCTTGATGAACTGACGGAACAACACGCGAAACAAGAAAATATGACGTTGGCGGAGTTGAAAGAGGTGATTAGTGAGATTTATCTGAGTAAAAAAAGTTTTTCA","","","4733","VLSVSPITLDELTEQHAKQENMTLAELKEVISEIYLSKKSFS","1163699","","conserved hypothetical protein","Cytoplasm","This sequence is similar to gi|42629312, a predicted hypothetical protein from Haemophilus influenzae R2846.Also see gi|16273304.","
InterPro
IPR008314
Family
Uncharacterised conserved protein UCP029143
PD030073\"[1-35]TYD94_HAEIN_P44172;
PF06164\"[1-35]TDUF978


","No hits to the COGs database.","","Residues 1 to 35 match (1e-08) PD:PD030073 which is described as COMPLETE PROTEOME YQFB CYTOPLASMIC HI1394 STY3206 ORF16 VC1576 TEX YPO1778 ","","","","","","","","","","","","Thu Feb 26 11:39:15 2004","Thu Feb 26 11:39:15 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01722 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 11:39:15 2004","","","","","","","","","","","","","1","","","" "AA01723","1163909","1164334","426","ATGAATAAAAGTGAGTTTAATATATTCAAATCACTAACAGATCTATTGAATGATGAAAAGTATAAGGGAAAAAATTTTAGACTATTCTCTCAAGTTGGACTTGGTGGCATTATAAATACAAAGACACCTTATAAATCAGCTTCTCAAAATGAGAAAAATGCTTTTTTGGCAATAAATTCATTAAGAGCTGATTTTATTATTGTAGATTGTTTGGGTTATCCTGTAGTACTAATTGAATATAATGGTTACGGACATAATATAGAAAATCCTGCTTATCGAGATATTCGCAAACAATATGCTTGTCAACAGGTTAATTTACCTTTAGTTATCTTTTATTTTAAAGATGATAAGAACGCAGCGATTGAAGAGAATAATAGAAAATTAGAAGAAGTTTCAAGAATTTTGCTTTCTCATACTGTTAGAAAA","","","16368","MNKSEFNIFKSLTDLLNDEKYKGKNFRLFSQVGLGGIINTKTPYKSASQNEKNAFLAINSLRADFIIVDCLGYPVVLIEYNGYGHNIENPAYRDIRKQYACQQVNLPLVIFYFKDDKNAAIEENNRKLEEVSRILLSHTVRK","1164334","","conserved hypothetical protein","Cytoplasm","This sequence matches to gi|16273520, a predicted hypothetical protein from Haemophilus influenzae Rd KW20.","
noIPR
unintegrated
unintegrated
PD031859\"[1-106]TYG31_HAEIN_P44279;


","No hits to the COGs database.","","Residues 1 to 106 match (2e-12) PD:PD031859 which is described as SIGNAL PRECURSOR PROTEOME PLASMID COMPLETE HI1631 Y4BI ","","","","","","","","","","","","Thu Feb 26 11:33:25 2004","Thu Feb 26 11:33:25 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01723 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 11:33:25 2004","","","","","","","","","","","","","1","","","" "AA01724","1164586","1167282","2697","ATGGGGCACGCGTTCCAGCAAACCTTGATGGATACCTTAATTCGTTTTAACCGCATGGAAGGACATAATACCCTCTGGCAAGCGGGAACCGACCATGCGGGCATTGCAACCCAGATGGTGGTGGAGCGCAAAATTGCCGCGGAAGAAAATAAAACCCGTCATGATTATGGTCGTGAGGCCTTTATCGACAAAATTTGGGAATGGAAAGCGCAATCCGGCGGCACCATTAGTCAACAGATTCGCCGCTTGGGTAACTCCGTGGACTGGACGCGTGAGCGCTTCACGATGGATGACGGTCTTTCCGACGCGGTGAAGGAAGTGTTTGTGCGTTTACACGAAGAAGGCTTGATTTATCGCGGCAAGCGTTTAGTGAACTGGGATCCGAAACTGCACACCGCCATTTCTGATCTGGAAGTGGAAAACAAAGAATCCAAAGGCAGCCTGTGGCATTTCCGTTATCCGCTGGCGAACGGTGCGAAAACCGCAGACGGAAAAGATTATTTAGTGGTGGCGACCACCCGTCCGGAAACCATGTTGGGCGATACTGCCGTTGCCGTTCACCCGGAAGATGAACGTTATCAGTCTTTAATCGGCAAAACCGTTGTACTGCCGCTGGCAAATCGTGAAGTTCCTATTATTGCCGATGATTATGTGGATCGTGAGTTCGGTACGGGCGTGGTGAAAATTACCCCGGCGCACGATTTCAATGACTACGAGGTGGGTAAGCGCCATCAGTTGCCGATGGTCAATGTATTGACGCTGAACGCGGATATTCGTGATGAAGCGGAAATTATCGGCACCGATGGTAAGCCTATGGCGGGCTATGAAGCGCTTATTCCGGCAGATTATCGTGGCTTGGAACGTTTCGCCGCGCGGAAGAAAATCGTGGCGGATTTTGAAGCCCTTGGTCTTCTTGATGAAATCAAACCGCACGATTTGAAGGTGCCTTACGGCGATCGCGGCGGCGTGCCGATTGAGCCGATGCTGACCGACCAATGGTATGTGAGAGTGAAACCGCTCGCCGAAGTAGCGATTAAAGCGGTGGAAGACGGCGAAATTCAATTTGTGCCGAAACAATACGAAAACCTGTATTTCTCTTGGATGCGTGACATTCAGGATTGGTGTATTTCCCGCCAACTTTGGTGGGGACACCGCATTCCGGCGTGGTATGACGCGGAAGGCAACATTTATGTGGCGCGCAGTGAAGCGGAAGTGCGGTCAAAATATCAGTTAAATCCTGATGTGGCACTTAAACAAGATGAAGACGTGCTGGACACTTGGTTCTCCTCCGGTTTATGGACGTTCTCCACGCTCGGCTGGCCGCAACAAACCAAAGAATTGAAAATGTTCCATTCAACGGATGTGCTGATTACCGGTTTTGACATTATTTTCTTCTGGGTGGCGCGCATGATTATGTTCACCATGCACTTCATCAAAGACGAAAACGGCAAGCCGCAAGTGCCGTTCAAAACCGTGTATGTGACGGGCTTGATTCGTGACGAAAACGGGAAAAAAATGTCGAAATCCAAAGGCAACGTGATTGACCCGTTAGACATGATTGACGGCATCAGCCTTGAAGATTTGGTGGCAAAACGCACCGGCAACATGATGCAACCGCAATTAGCGGAGAAAATCGCCAAATCCACCCGCAAAGAATTCCCGGAAGGCATTGTGGCGCACGGCACCGACGCCTTACGTTTCACCCTCGCCGCCCTTGCAACGAACGGTCGCGACATTAACTGGGATATGAAACGTTTGGAAGGCTACCGCAACTTCTGCAACAAATTGTGGAACGCCAGCCGCTTCGTGCTTACCAATGAAAAGCTGGATTTAAGCCAAGGCGAAATTGAATTTTCCGTTGCCGATCGTTGGATCCAATCGGAATTCAACCGCACTGTGGAAACCTTCCGCAACGCATTAAGCCAATTCCGTTTTGACTTATGTGCCACCGCGCTTTATGAATTCACTTGGAACCAATTCTGTGACTGGTATTTGGAACTCACCAAGCCGGTATTCGCAAACGGCAACCAAGCGCAAATTCGCGCGGCAAGCCAGACCTTGGTGCATGTGTTAGAGAAATTACTGCGTTTAGCGCACCCGGTTATTCCATTCATTACCGAAGAAATCTGGCAGAAAGTGAAAGGTTTCGTCGGCATTGACGCCGACAGCATTATGTTGCAGCCGTTCCCGCAAGTGGACATGACGGCGTTTGATGTGGACGCGGAAGCCGAAATCGCATGGTTGAAAGAGGTCATCGTCGCCGTACGTAATATTCGCGCCGAATGCAACATTGCGCCGAGCAAAGGTTTGGATTTGTTATTCCGTAATATTCCGGCGGACGAGCAAAAAATACTGGAAAAACAGACCGCACTTTTAACAGCCATGGCGAAGTTGGATAACGTTAGTGTGCTTAAGGAAGGCGAACAAGCCCCGTTAGCGGTGGCAAAACTAGTCGGCAACACCGAGCTTCTCGTGCCGCTGGTGGGCTTCATCAACAAAGATGCCGAGCTTGCCCGTTTGACCAAAGAGATTGAAAAATACCAAAACGAAGTCAAACGCATCGAAAGCAAACTCAGCAACGACGCCTTCGTCGCCAAAGCCCCGGAAGCCGTCATCGCCAAAGAACGCGAAAAAATGGCCGAATACCAATCCGGATTGGAAAAAATCCGTGAGCAGTATAAGGTGATTGAGGCGTTG","","","108761","MGHAFQQTLMDTLIRFNRMEGHNTLWQAGTDHAGIATQMVVERKIAAEENKTRHDYGREAFIDKIWEWKAQSGGTISQQIRRLGNSVDWTRERFTMDDGLSDAVKEVFVRLHEEGLIYRGKRLVNWDPKLHTAISDLEVENKESKGSLWHFRYPLANGAKTADGKDYLVVATTRPETMLGDTAVAVHPEDERYQSLIGKTVVLPLANREVPIIADDYVDREFGTGVVKITPAHDFNDYEVGKRHQLPMVNVLTLNADIRDEAEIIGTDGKPMAGYEALIPADYRGLERFAARKKIVADFEALGLLDEIKPHDLKVPYGDRGGVPIEPMLTDQWYVRVKPLAEVAIKAVEDGEIQFVPKQYENLYFSWMRDIQDWCISRQLWWGHRIPAWYDAEGNIYVARSEAEVRSKYQLNPDVALKQDEDVLDTWFSSGLWTFSTLGWPQQTKELKMFHSTDVLITGFDIIFFWVARMIMFTMHFIKDENGKPQVPFKTVYVTGLIRDENGKKMSKSKGNVIDPLDMIDGISLEDLVAKRTGNMMQPQLAEKIAKSTRKEFPEGIVAHGTDALRFTLAALATNGRDINWDMKRLEGYRNFCNKLWNASRFVLTNEKLDLSQGEIEFSVADRWIQSEFNRTVETFRNALSQFRFDLCATALYEFTWNQFCDWYLELTKPVFANGNQAQIRAASQTLVHVLEKLLRLAHPVIPFITEEIWQKVKGFVGIDADSIMLQPFPQVDMTAFDVDAEAEIAWLKEVIVAVRNIRAECNIAPSKGLDLLFRNIPADEQKILEKQTALLTAMAKLDNVSVLKEGEQAPLAVAKLVGNTELLVPLVGFINKDAELARLTKEIEKYQNEVKRIESKLSNDAFVAKAPEAVIAKEREKMAEYQSGLEKIREQYKVIEAL","1167281","[CATALYTIC ACTIVITY] ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val).[SUBUNIT] Monomer (By similarity).[SUBCELLULAR LOCATION] Cytoplasmic.","valyl-tRNA synthetase","Cytoplasm","","
InterPro
IPR002300
Domain
Aminoacyl-tRNA synthetase, class Ia
PF00133\"[1-582]TtRNA-synt_1
InterPro
IPR002303
Family
Valyl-tRNA synthetase, class Ia
PR00986\"[187-204]T\"[320-333]T\"[420-441]T\"[451-469]TTRNASYNTHVAL
PTHR11946:SF5\"[1-263]T\"[282-522]T\"[560-899]TVALYL-TRNA SYNTHETASE
TIGR00422\"[1-880]TvalS: valyl-tRNA synthetase
InterPro
IPR013155
Domain
tRNA synthetase, valyl/leucyl, anticodon-binding
PF08264\"[622-775]TAnticodon_1
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620\"[1-515]Tno description
noIPR
unintegrated
unintegrated
G3DSA:1.10.730.10\"[560-737]Tno description
PTHR11946\"[1-263]T\"[282-522]T\"[560-899]TISOLEUCYL, LEUCYL, TYROSYL, VALYL AND METHIONYL-TRNA SYNTHETASES


","BeTs to 26 clades of COG0525COG name: Valyl-tRNA synthetaseFunctional Class: JThe phylogenetic pattern of COG0525 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 8.7e-06) to 1/2 blocks of the IPB001412 family, which is described as \"Aminoacyl-transfer RNA synthetases class-I\". Interpro entry for IP:IPR001412. IPB001412B 502-512 8.9e-06","Residues 284 to 361 match (1e-07) PD:PD373849 which is described as CDNA: FIS FLJ21965 HEP05617 MGC:14919 FOR ","","","","","","","","","","","Tue Jan 7 13:28:44 2003","Tue Jan 7 13:28:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01724 is paralogously related to AA02950 (5e-37) and AA01090 (7e-19).","","","","","","Residues 1 to 582 (E-value = 5.2e-293) place AA01724 in the tRNA-synt_1 family which is described as tRNA synthetases class I (I, L, M and V) (PF00133)","","","","","Tardif KD, Horowitz J. Transfer RNA determinants for translational editing by Escherichia coli valyl-tRNA synthetase. Nucleic Acids Res. 2002 Jun 1;30(11):2538-45. PMID: 12034843 Tardif KD, Liu M, Vitseva O, Hou YM, Horowitz J. Misacylation and editing by Escherichia coli valyl-tRNA synthetase: evidence for two tRNA binding sites. Biochemistry. 2001 Jul 10;40(27):8118-25. PMID: 11434781Hartlein,M., Frank,R. and Madern,D. Nucleotide sequence of Escherichia coli valyl-tRNA synthetase gene valS. Nucleic Acids Res. 15 (21): 9081-9082 (1987) [PubMed: 3317277]. Heck,J.D. and Hatfield,G.W. Valyl-tRNA synthetase gene of Escherichia coli K12. Primary structure and homology within a family of aminoacyl-TRNA synthetases. J. Biol. Chem. 263 (2): 868-877 (1988) [PubMed: 3275660].","","Tue Jan 7 13:28:44 2003","1","","","" "AA01725","1167352","1168242","891","ATGAAAGATATTTATTTTGGAAAAATATACCCTTTAGAAAAACATATATCTTTAACAAATAAACCTTCGTTATGTAAACAACAAATTAAATTTTTGAATCCTCTTTTATTACAAACTACGTTTACGGAAGACAATTTTGAACAATATGATCTTAAAGTAACTTTTTTCCAAGGAAATCGATTTGCTCAAACCTTGCATTTCTGTTCTTACTCTCCGAATAAACTATTTGATACTAAAGCAGAATTAAATGCAGTACTTTTTGATAAATTAGATAGAAAAGAAAGTTTAGGAAGTGTTGTTATTGCATCAGGTGTAATTCCTTCGGAAGAAAGCTTAGTCATAAAAAATTCTTCTTGGTTTATCCGTAGTTCTGATACGTTAGATAAAAATGAATTTTTCCATTTGAGCAATGAGTGGCGTGCGATAGATGGCCGAGGTATGGCTATTTTTGAATCTTTTGGTACGGTGACAAATGCTTATAGGCAAGTGTTTTTAATTATGTTGGCTTTAGCATATTACAGCGCGTTACATAAAATTAGCGAAGAGTTAGCAAATGTTTTGGCTAAGCCGAATAATATTCAAGAGTTGGATAAGTTGTATACTGAAGCAGCAATTTTTAATGCGCGTTATTATTTTGATAATCCAATTGAGTTTTCTCGTTATCCGACATTTCGTGCTTGGGAACATATACGAGAGGCATATCATCTTAGAGATAAAAACAATGAGGTTACTTCTCAGTTGGCACAGGTCCACCAAATATTGAGTTATACTCAACAAAAAGCAGAACAGTGTATTAATGAAAAACGTAATTGGAGGTTAGGATTAATCGGGGTTATTTTAGCCGGTGCAGGACTGATTGAGGTTATAGATATACTTATTCAATGGTTGTCT","","","34820","MKDIYFGKIYPLEKHISLTNKPSLCKQQIKFLNPLLLQTTFTEDNFEQYDLKVTFFQGNRFAQTLHFCSYSPNKLFDTKAELNAVLFDKLDRKESLGSVVIASGVIPSEESLVIKNSSWFIRSSDTLDKNEFFHLSNEWRAIDGRGMAIFESFGTVTNAYRQVFLIMLALAYYSALHKISEELANVLAKPNNIQELDKLYTEAAIFNARYYFDNPIEFSRYPTFRAWEHIREAYHLRDKNNEVTSQLAQVHQILSYTQQKAEQCINEKRNWRLGLIGVILAGAGLIEVIDILIQWLS","1168241","","hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
tmhmm\"[273-293]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Tue Jan 7 13:30:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01725 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01726","1168364","1168245","120","ATGTCCCCTACATTCCCCGCTACCAGCCATATTTTTAAATTACCTATCGGTATCGTCGGGCAGGAGCAACTTAATCTTTCCCATAATTGCGAGAACGAATGGCTTTGCCTGAAGTTCGGC","","","4483","MSPTFPATSHIFKLPIGIVGQEQLNLSHNCENEWLCLKFG","1168245","","conserved hypothetical protein (possible HipA-like protein","Cytoplasm","This sequence matches to gi|33593600, a predicted HipA-like protein from Bordetella pertussis Tohama I. Also see gi|22989870 from Burkholderia fungorum.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 11:28:02 2004","Thu Feb 26 11:28:02 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01726 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 11:28:02 2004","","","","","","","","","","","","","1","","","" "AA01727","1168480","1168367","114","GTGTTGAAAAACTACCGCACTTTTCCGTTAGGCATGGAAGAAACCGATGATTTTCTCATTTCGCTTGTCGGCACACAGGAAAAAACGGCTCTACTCTACTATCAAAATCAATGG","","","4508","VLKNYRTFPLGMEETDDFLISLVGTQEKTALLYYQNQW","1168367","","conserved hypothetical protein (possible HipA protein)","Cytoplasm","This sequence matches weakly to gi27377096, a predicted HipA protein from Bradyrhizobium japonicum. Also see gi27365384.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 11:17:16 2004","Thu Feb 26 11:24:56 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01727 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 11:24:56 2004","","","","","","","","","","","","","1","","","" "AA01728","1168725","1168477","249","TTGCCTTTATCCCATAAAGTTTACCGAGAGGATTCGGTTTACAATTTCTTCGATAATCTTTTGCCCGAAAATGAACAAATTCGTTCACGCATTCAGCAACGTTTCCAGACCTCGACCAAATCCCCCTTTGATTTGCTTTCGGCTATTGAGCAGGATTGCGTTGGGGCGATTCAACTTTATCACGGTGAAAGTCGCTCTGTTCGGCAAATTTATGCGGAGCCGTTAAATGATAAGAAGTGTAAAACGTGT","","","13102","LPLSHKVYREDSVYNFFDNLLPENEQIRSRIQQRFQTSTKSPFDLLSAIEQDCVGAIQLYHGESRSVRQIYAEPLNDKKCKTC","1168476","","conserved hypothetical protein(related to HipA protein)","Cytoplasm","","
noIPR
unintegrated
unintegrated
PD563641\"[1-58]TQ7MXZ9_PHOLL_Q7MXZ9;


","No hits to the COGs database.","","Residues 1 to 56 match (2e-10) PD:PD017698 which is described as HIPA PROTEOME COMPLETE TRANSCRIPTION Y4ME REGULATOR PLASMID ID617 CC2735 ","","","","","","","","","","","","Fri Jan 31 14:18:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01728 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01729","1168725","1169087","363","ATGATAATGAAATTGGACGGGAGCGCGCAGAATCAAGCCATTTTGGGGGATATTGAAATTCCGTCGGCCATTTGTGAGCTTTCGCCATTCGCCGACCAGCAAGCCGTTCATTGCGACTTTCAAGATAGCGTTATTCATTACCACGCCTCATCGTCATCGGAAAATGCAGGTGTTGGTTCGCTGATTAAATTTTCCGTAACCGCGGATTTTTTGCGCGGTTGTACGATAAGTTCTAACTCTAATCCTGCCAAAATTTTAAATAACGTTTCTAATTTCGTGCGTTCCGGCTCATTTTCAAAAACCGATATTCTGGCTTGGGTGGTGCTAGCAAGCTTGGCGACATCTGTTTGTGAGAGGTTGCCT","","","16278","MIMKLDGSAQNQAILGDIEIPSAICELSPFADQQAVHCDFQDSVIHYHASSSSENAGVGSLIKFSVTADFLRGCTISSNSNPAKILNNVSNFVRSGSFSKTDILAWVVLASLATSVCERLP","1169086","","hypothetical protein","Periplasm, Extracellular","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Tue Jan 7 13:30:59 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01729 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01730","1169143","1168865","279","ATGGTTATTACCACCGCAAAAATGCTTTCTCATGTTATTCGGGAATTTCGTTATCAAGGCAACCTCTCACAAACAGATGTCGCCAAGCTTGCTAGCACCACCCAAGCCAGAATATCGGTTTTTGAAAATGAGCCGGAACGCACGAAATTAGAAACGTTATTTAAAATTTTGGCAGGATTAGAGTTAGAACTTATCGTACAACCGCGCAAAAAATCCGCGGTTACGGAAAATTTAATCAGCGAACCAACACCTGCATTTTCCGATGACGATGAGGCGTGG","5.00","-2.77","10491","MVITTAKMLSHVIREFRYQGNLSQTDVAKLASTTQARISVFENEPERTKLETLFKILAGLELELIVQPRKKSAVTENLISEPTPAFSDDDEAW","","","conserved hypothetical protein (possible transcriptional regulator)","Cytoplasm","Nearest neighbor is >22969077 from Rhodospirillum rubrum.AA01730 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus ducreyi gene.AA01730 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus influenzae Rd gene.","
InterPro
IPR001387
Domain
Helix-turn-helix type 3
PF01381\"[13-67]THTH_3
SM00530\"[12-67]THTH_XRE
PS50943\"[13-67]THTH_CROC1
noIPR
unintegrated
unintegrated
G3DSA:1.10.260.40\"[8-64]Tno description


","BeTs to 5 clades of COG1396COG name: Predicted transcriptional regulatorsFunctional Class: KThe phylogenetic pattern of COG1396 is --m----qvdrlb-efghsn-jx-t-Number of proteins in this genome belonging to this COG is","","","Fri Feb 27 11:11:05 2004","Sat Feb 28 17:07:17 2004","Sat Feb 28 17:07:17 2004","Sat Feb 28 17:07:17 2004","Fri Feb 27 11:11:05 2004","Fri Feb 27 11:11:05 2004","Fri Feb 27 11:11:05 2004","Fri Feb 27 11:11:05 2004","Fri Feb 27 11:11:05 2004","Fri Feb 27 11:11:05 2004","Fri Feb 27 11:11:05 2004","Fri Feb 27 11:11:05 2004","Fri Feb 27 11:11:05 2004","Fri Feb 27 11:11:05 2004","Fri Feb 27 11:11:05 2004","Fri Feb 27 11:11:05 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01730 has no significant similarity (blastp p-value < 1e-03) to any other gene in this genome.AA01730 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Fri Feb 27 11:11:05 2004","Fri Feb 27 11:11:05 2004","No hits to the PDB database.","","","Residues 13 to 67 (E-value = 4.7e-06) place AA01730 in the HTH_3 family which is described as Helix-turn-helix (PF01381)","Fri Feb 27 11:11:05 2004","","","","","","","1","Fri Feb 27 11:11:05 2004","","" "AA01731","1170735","1169290","1446","ATGCAAGTGTTGGATTCTACCATTGCCAATGTGGCGATTCCCACCATTGCAGGCGATCTCGGCGCGTCATTCAGCCAAGGCACTTGGGTCATCACATCTTTCGGGGTGGCGAACGCCATTTCCATTCCTATCACCGGCTGGCTCGCCAAACGCTTCGGCGAGGTAAAATTATTCTTAATTTCGACCGCACTTTTTGTCTTCGCCTCTTGGCTATGCGGCATTTCCCACAGTTTGGAAATGTTGATTTTATGCCGAATATTCCAAGGGTTGGCGGCAGGTCCGATTATTCCTTTATCCCAAAGTTTACTACTCAATAATTACCCGCCGGAAAAACGCGGAATGGCGCTGGCATTTTGGGCGATGACGGTGGTTGTGGCGCCGATTTTCGGCCCGATTCTCGGTGGCTGGATTAGCGACAACCTGCACTGGGGCTGGATTTTCTTTATTAACGTCCCCATCGGCTTAATCGTCATCGGTTTCAGCTGGAAAATTTTGGCACCACGGGAAAGTGAAATTCAGCACCAACCCATTGATACCGTCGGCTTGATCTTATTGGTATTAGGTGTCGGCTGTTTGCAATTAATGTTGGATCAAGGGCGCGAACAGGACTGGTTCAGTTCCAACGAAATCATTATTCTTGCCGTGGTTTCTGCCGTTACCTTAACCGCGTTGGTGATTTGGGAACTAACTGATGACAACCCTGTGGTGGATATTTCTTTGTTTAAGCAACGCAATTTTACCGTCGGTTGCTTATCCACCAGCCTGGCATTTTTGATCTACCTTGGATCCGTCGTGCTGATCCCATTATTGCTTCAACAAGTGTTCGGCTATACTGCCACTTGGGCAGGCTTGGCTTCCGCACCTGTGGGTTTATTTCCGATTTTGCTATCGCCACTTATCGGCAAATTCGGTTACAAAATCGATATGCGTATTTTGGTCACTATCAGTTTCGTGGTGTACGCCGTCACCTTTTATTGGCGTGCCGTTACCTTTGAGCCGAATATGACGTTCATTAATGTGATATTACCGCAAACGGTGCAGGGCTTGGCTGTTGCCTGTTTCTTTATGCCGTTGACAACCATTACGTTATCGGACTTGCCGGCACATAAAATGGCATCGGCTTCAAGTCTGTTCAACTTTTTGCGCACGCTTGCCGGTTCCGTGGGAACCTCGTTCACTACGTTTTTATGGTATAATCGTGAAGTCGTGCATCATACTCAACTCACCGAAGCCATTACACCGTACAACCTTATCGCACAACAGTATTATTACATGATGGAGCGTTTCGGCATGAGTGAAGAACAAACCTCTTCTATACTTGCCCGCAATATTACTTCACAAGGCTTTATTATCGGTGCCAACGAAATCTTTTGGCTATCTGCGATTATGTTCCTTATTTTGTTCATCTTAGTCTGGTTTGCTAAACCCCCTTTTAGCGGTCGCCAT","","","55709","MQVLDSTIANVAIPTIAGDLGASFSQGTWVITSFGVANAISIPITGWLAKRFGEVKLFLISTALFVFASWLCGISHSLEMLILCRIFQGLAAGPIIPLSQSLLLNNYPPEKRGMALAFWAMTVVVAPIFGPILGGWISDNLHWGWIFFINVPIGLIVIGFSWKILAPRESEIQHQPIDTVGLILLVLGVGCLQLMLDQGREQDWFSSNEIIILAVVSAVTLTALVIWELTDDNPVVDISLFKQRNFTVGCLSTSLAFLIYLGSVVLIPLLLQQVFGYTATWAGLASAPVGLFPILLSPLIGKFGYKIDMRILVTISFVVYAVTFYWRAVTFEPNMTFINVILPQTVQGLAVACFFMPLTTITLSDLPAHKMASASSLFNFLRTLAGSVGTSFTTFLWYNREVVHHTQLTEAITPYNLIAQQYYYMMERFGMSEEQTSSILARNITSQGFIIGANEIFWLSAIMFLILFILVWFAKPPFSGRH","1169289","[FUNCTION] Translocase that confers resistance to substances of high hydrophobicity (by similarity). [SUBCELLULAR LOCATION] Integral membrane protein. inner membrane (potential). [SIMILARITY] Belongs to the major facilitator family (also known as the drug resistance translocase family). ","multidrug resistance protein B","Inner membrane, Cytoplasm","","
InterPro
IPR004638
Family
Drug resistance transporter EmrB/QacA subfamily
TIGR00711\"[1-474]Tefflux_EmrB: drug resistance MFS transporte
InterPro
IPR007114
Family
Major facilitator superfamily
PS50850\"[1-479]TMFS
InterPro
IPR011701
Family
Major facilitator superfamily MFS_1
PF07690\"[4-398]TMFS_1
noIPR
unintegrated
unintegrated
PTHR10074\"[1-181]T\"[232-400]T\"[452-482]TMAJOR FACILITATOR SUPERFAMILY MEMBER
PTHR10074:SF57\"[1-181]T\"[232-400]T\"[452-482]TDRUG RESISTANCE TRANSPORTER, EMRB/QACA FAMILY-RELATED
tmhmm\"[29-49]?\"[54-74]?\"[84-104]?\"[116-138]?\"[144-166]?\"[176-196]?\"[210-230]?\"[251-271]?\"[281-301]?\"[311-329]?\"[348-368]?\"[378-398]?\"[456-474]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.8e-07) to 1/2 blocks of the IPB003662 family, which is described as \"General substrate transporters\". Interpro entry for IP:IPR003662. IPB003662A 81-113 1.8e-07","Residues 1 to 30 match (3e-07) PD:PD427369 which is described as TRANSMEMBRANE COMPLETE PROTEOME RESISTANCE EFFLUX ANTIBIOTIC TRANSPORTER MEMBRANE MULTIDRUG PROBABLE ","","","","","","","","","","","Tue Jan 7 14:07:10 2003","Tue Jan 7 14:07:10 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01731 is paralogously related to AA01463 (8e-48), AA00062 (1e-08), AA00266 (6e-07) and AA00497 (5e-05).","","","","","","","","","","","Tanabe H, Yamasak K, Furue M, Yamamoto K, Katoh A, Yamamoto M, Yoshioka S, Tagami H, Aiba HA, Utsumi R.Growth phase-dependent transcription of emrKY, a homolog of multidrug efflux emrAB genes of Escherichia coli, is induced bytetracycline.J Gen Appl Microbiol. 1997 Oct;43(5):257-263.PMID: 12501312Borges-Walmsley MI, Beauchamp J, Kelly SM, Jumel K, Candlish D, Harding SE, Price NC, Walmsley AR.Identification of oligomerization and drug-binding domains of the membrane fusion protein EmrA.J Biol Chem. 2002 Dec 13 PMID: 12482849Lomovskaya O, Lewis K.Emr, an Escherichia coli locus for multidrug resistance.Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):8938-42.PMID: 1409590 ","","Fri Feb 7 13:18:45 2003","1","","","" "AA01732","1171974","1170817","1158","ATGAGCGAAGTAAGCCAACCACAAGTTGAAAAATCAAAAAACACACGCCGAAAAGCATTAGGTATTTTCTTTTTTATTTTGATTCTTATTAGCTTCTTGAGCGGACTGTACTGGTTCTTTTTTGTAAAAACCTATCAAACTACCGAAGATGCCTATGTAAGTGGCAATCAAGTGATGATTTCCGCACAAATTGCCGGTAATGTGCGCCAAATTAACGCGGAAAATATGGATTTCGTTCACGCCGGCGATGTATTACTGGAGCTTGATGATGCCGATTATCAACTGAGTTTCAGCCAAGCACAAAATACTTTGGCAAGCGCCGTACGTCAAATTTCACAACTGGGTTATACAGTCAAACAGCTTGAAGCTACCGTTCAAGCCAATCAAATTGCACTGAATAAAGTACAGGGTGACTTAGCGCGTCGTGAAATGCTGGGGAAAAGCGGCGCAATTGATAAAGAATCGCTGCAACATGCCAGAGAAGCCGTAGTGATCGCAGAGGCGAATCTGAAAGCGGTTAAAAATCAGCTTGCCGCCAATCAATCCTTACTTCTGAATGTGCCGCTTAAGGAACAACCGGAAATTCAAAAAGCCATTAGTTCGCTAAAACAGGCTTGGTTAAATTTACAACGCACCAAAATTGTCAGCCCGGTGGACGGTTATGTGGCACGTCGCAGCACACAAATCGGGCAAAAAGTCGCTGTTGGCAGTACATTAATGGCTGTTATTTCCAACGACAAAATGTGGGTGGATGCCAATTTCAAAGAAACCCAACTGAAAGATATGCGAATCGGACAACCGGTAAAACTGTCTTTTGATTTATATGGTCATGATGTGAAATTCGATGGCAAAGTAGAAGGCATTGAAATGGGCACCGGCAGCGCATTTTCTTTATTGCCTGCACAAAATGCCACCGGCAACTGGATCAAAGTGATACAACGGGTGCCGGTGCGCGTTAGCTTAGACGCGCAACAACTTGCCCGTTACCCCTTGCGAATCGGCTTATCTACCTTGGTTGAAGTGAATATTGCCGACACGAGCGGTGAAATCTTATCGCAGAAGAAACGCACGACACCGCTCTACTCCACCAACACCCTAGATTACGACCAAAGTGCGCTGGAAAATTTGATTGAAAAAATTATCAGCGACAATACCAAC","","","42774","MSEVSQPQVEKSKNTRRKALGIFFFILILISFLSGLYWFFFVKTYQTTEDAYVSGNQVMISAQIAGNVRQINAENMDFVHAGDVLLELDDADYQLSFSQAQNTLASAVRQISQLGYTVKQLEATVQANQIALNKVQGDLARREMLGKSGAIDKESLQHAREAVVIAEANLKAVKNQLAANQSLLLNVPLKEQPEIQKAISSLKQAWLNLQRTKIVSPVDGYVARRSTQIGQKVAVGSTLMAVISNDKMWVDANFKETQLKDMRIGQPVKLSFDLYGHDVKFDGKVEGIEMGTGSAFSLLPAQNATGNWIKVIQRVPVRVSLDAQQLARYPLRIGLSTLVEVNIADTSGEILSQKKRTTPLYSTNTLDYDQSALENLIEKIISDNTN","1170816","[FUNCTION] The emr locus confers resistance to substances of high hydrophobicity. EmrA probably participate in a transport system to extrude toxins and drugs from the cell (by similarity). [SUBCELLULAR LOCATION] Inner membrane-bound (potential).[SIMILARITY] Belongs to the hlyD family of secretion proteins.","multidrug resistance protein A","Periplasm, Outer membrane, Inner membrane","","
InterPro
IPR005694
Family
Efflux pump membrane protein Emr
TIGR00998\"[16-341]T8a0101: efflux pump membrane protein
InterPro
IPR006143
Family
Secretion protein HlyD
PF00529\"[56-339]THlyD
noIPR
unintegrated
unintegrated
signalp\"[1-35]?signal-peptide
tmhmm\"[21-41]?transmembrane_regions


","BeTs to 8 clades of COG1566COG name: Multidrug resistance efflux pumpFunctional Class: QThe phylogenetic pattern of COG1566 is -------q----b-efgh-n-jx---Number of proteins in this genome belonging to this COG is","Significant hit ( 5.1e-27) to 3/3 blocks of the IPB002215 family, which is described as \"HlyD family secretion protein\". Interpro entry for IP:IPR002215. IPB002215A 54-90 4.5e-13 IPB002215B 213-247 5e-07 IPB002215C 283-305 0.001 IPB002215A 208-244 0.11 IPB002215B 157-191 0.046","Residues 192 to 275 match (2e-07) PD:PD203444 which is described as COMPLETE PROTEOME RESISTANCE MULTIDRUG A EFFLUX EMRA PUMP AQ_1060 ","","","","","","","","","","","Tue Jan 7 14:10:07 2003","Tue Jan 7 14:10:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01732 is paralogously related to AA01340 (2e-10), AA02081 (7e-08) and AA02139 (2e-06).","","","","","","Residues 56 to 339 (E-value = 9.2e-79) place AA01732 in the HlyD family which is described as HlyD family secretion protein (PF00529)","","","","","Tanabe H, Yamasak K, Furue M, Yamamoto K, Katoh A, Yamamoto M, Yoshioka S, Tagami H, Aiba HA, Utsumi R.Growth phase-dependent transcription of emrKY, a homolog of multidrug efflux emrAB genes of Escherichia coli, is induced bytetracycline.J Gen Appl Microbiol. 1997 Oct;43(5):257-263.PMID: 12501312Borges-Walmsley MI, Beauchamp J, Kelly SM, Jumel K, Candlish D, Harding SE, Price NC, Walmsley AR.Identification of oligomerization and drug-binding domains of the membrane fusion protein EmrA.J Biol Chem. 2002 Dec 13 PMID: 12482849Lomovskaya O, Lewis K.Emr, an Escherichia coli locus for multidrug resistance.Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):8938-42.PMID: 1409590 ","","Fri Feb 7 13:18:18 2003","1","","","" "AA01733","1171917","1172051","135","ATGCTTTTCGGCGTGTGTTTTTTGATTTTTCAACTTGTGGTTGGCTTACTTCGCTCATTTATTATCCTTAACTTTAATACTTTGAAAATTATTATTTGTTATTTGATTTTTAAAGTCTATCAATTCTATTTAATG","","","5395","MLFGVCFLIFQLVVGLLRSFIILNFNTLKIIICYLIFKVYQFYLM","1172051","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-19]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 11:14:00 2004","Thu Feb 26 11:14:00 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01733 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 11:14:00 2004","","","","","","","","","","","","","1","","","" "AA01734","1172183","1172662","480","ATGTCAAAAACATTTATTGGTTTAGATACTGCTCAATCAGAAATGTTGGCTTCAAAGTTAAATGAATTATTAGCGACTTACCAAGTTTTTTACACCAACGTGCGTGGCTATCACTGGAATATTAAAGATGTCAATTTCTTTGAATTACATGCAAAATTTGAGGAAGTTTATACTGACCTTGTGGAAAAAGTAGATGGGGTTGCAGAACGCATTTTAACTTTGGGTTATACACCAAATAACGCATTCAGTCAGTATTTAACTCTCGCACGTATTAAAGAAGATATTGCTGTAAGCAACGCAATTACTTGTTTAAAAGGCACGCTAGAAGGCTTTAAAGTGTTGCTTGCCCAACAGCGGGAGATTTTAGCCCTTGCCGGCGAAGCCGGTGATGAAGGCACTGTTTCACAAATGAGTGATTACATAAAAGAGCAAGAAAAACTGGTTTGGATGTTCCAGGCAGCTTGTCAAGCTTGTGCAAGC","","","17935","MSKTFIGLDTAQSEMLASKLNELLATYQVFYTNVRGYHWNIKDVNFFELHAKFEEVYTDLVEKVDGVAERILTLGYTPNNAFSQYLTLARIKEDIAVSNAITCLKGTLEGFKVLLAQQREILALAGEAGDEGTVSQMSDYIKEQEKLVWMFQAACQACAS","1172661","","DNA-binding protein; DPS family protein","Cytoplasm","","
InterPro
IPR002177
Family
DNA-binding protein Dps
PD149803\"[29-93]TDPS
PR01346\"[38-54]T\"[62-78]T\"[133-151]THELNAPAPROT
PIRSF005900\"[6-158]TDps
PS00819\"[64-78]TDPS_2
InterPro
IPR008331
Family
Ferritin and Dps
PF00210\"[17-157]TFerritin
InterPro
IPR009078
Family
Ferritin/ribonucleotide reductase-like
SSF47240\"[2-156]TFerritin/RR_like
InterPro
IPR012347
Family
Ferritin-related
G3DSA:1.20.1260.10\"[6-153]TFerritin_rel


","BeTs to 13 clades of COG0783COG name: Starvation-inducible DNA-binding proteinFunctional Class: LThe phylogenetic pattern of COG0783 is -o-------d-lbcefghs-ujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 2.8e-38) to 3/3 blocks of the IPB002177 family, which is described as \"Dps protein family\". Interpro entry for IP:IPR002177. IPB002177A 20-60 1.4e-20 IPB002177B 61-75 0.00017 IPB002177C 130-155 3e-10","Residues 104 to 153 match (1e-16) PD:PD444422 which is described as PROTEOME COMPLETE DPS DNA-BINDING HI1349 NON-SPECIFIC FAMILY PM0817 ","","","","","","","","","","","","Tue Jan 7 14:18:41 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01734 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 17 to 157 (E-value = 1.5e-19) place AA01734 in the Ferritin family which is described as Ferritin-like domain (PF00210)","","","","","","","","1","","","" "AA01735","1172774","1172673","102","GTGAATCTTAAAGATGTTTTCAAAACGCTCGAAAAAATCACCGCACTTTTGACCAAAAAAATCCTGCTTAACGATTTATTTAAGCAGGATTATTTTTTTAGC","","","4030","VNLKDVFKTLEKITALLTKKILLNDLFKQDYFFS","1172673","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 11:11:57 2004","Thu Feb 26 11:11:57 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01735 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 11:11:57 2004","","","","","","","","","","","","","1","","","" "AA01737","1174763","1172787","1977","ATGTTTCAAGATAATCCCCTACTCGCCCAATTAAAACAACAAATTCACGACAGCAAAGAACGTGTGGAAGGCACGGTAAAAAGCACTGATAAAGCTTACGGTTTTTTAGAATGTGACAAAAAAAGCTATTTTATTGCACCGCCGGCAATGAAAAAAGTGATGCACGGCGACAAAATCAGCGCCACTATTGAAAAACAGGGCGACAAAGAACAAGCGGAACCGGAAGCCCTGATCGAACCGATACTCACCCGTTTTATCGCCAAAGTGCGGTTCAATAAAGACAAGAAATTACAGGTATTGGTCGATCACCCGAATATCAATCAACCCATTGGCGCCGCGCAAAACAAATCCGTAAAAAAAGAGTTACAGGAAGGCGATTGGGTGGTGGCATCACTTAAAACTCATCCGCTGCGTGATGATCGTTTTTTCTATGCGCAAATTACCCAATTCATTTGCCACGCCGATGATGAATTGGCGCCTTGGTGGGTCACCCTTGCCCGTCACGAGCAACCACGTGAGCCTGTTCAGGGGCAAGATCAATATGAAATGCAGGATAAAGAAACGCGCGAAAATCTGACCGCACTTCACTTCGTCACCATCGACTCGGAAACCACGCAGGACATGGATGACGCCTTATATATTGAGCCGTTAACCTCAAATAATGAGCAAACCGGCTGGCAATTGCTTGTGGCGATTGCCGATCCGACGGCTTATATCAGCTTGGATTCGCAAATCGAGAAAGATGCTAAGCAACGCTGTTTCACCAATTATCTGCCGGGCTTCAACATCCCAATGTTACCACGCGAACTCTCCGACGAGCTTTGTTCCTTAAAACCTAACGAAACCCGTCCCGCACTGGTTTGTTATATTCAAACGGATTTACAGGGCAATATCATCGCGCCGGCAAAATTTGTGTTAGCGAATGTACAATCGAAAGCTAAATTGACTTATAGTCGGGTGTCCGATTATTTAGAAGGCAAAGAAAATGCCTGGCAGCCGGAAAACCAAGACATGGCACAGCAAATTCATTGGCTGCATCAATTTAGCCTTGCCAGAACACAATGGCGCAAAACCCATGCCCTATTGTTTAAAGAAAAACCGGATTATTCTTTCGTGTTGGGAGAAAACGGCAAGGTGCAGGAAATTAAGGCGGAATATCGCCGTATTGCCAACCAAATCGTGGAAGAATCCATGATTATCGCCAATATCTGCGCCGCTCAATTTTTACAGAAAAACCTGCAATGCGGTATTTTCAATACGCACAGCGGATTCGACAAAAAATTCCTGGAAAACGCCCATCATTTTCTGTTAGCCAGTTTAGCAAACGAAGAAAACAAAGCGGAACTACAAGCCCGCTATACCGTAGAGCATTTAGCGACGCTAAACGGCTACTGCCAAATGCGTCACGATATTGAACCGATTGAAGGGGATTATTTGGAATTCCGCCTGCGTCGATTCTTAACTTTTGCAGAATTTAAAGCGGAATTGGCACCGCACTTTGGGCTGGGATTGAACGGTTACGCTACTTGGACGTCACCGATTCGGAAATATTCCGACATGGTGAATCATCGCCTGATTAAAGCTTATTTAGCCCATCGCCCTTATGAAAAACCGGAAGAAAGCGTGCTGGTGCGCTTGCAAGAAGCCCGCCGCCAAAATCGCCTGGTGGAACGTGACATTGCCGATTGGCTATATTGTCGCTATCTTGCCGATAAAGTTGCCGAAAAAGTGGAATTTGAAGCAGAAGTACAAGATATTACCCGTGGAGGTTTACGTGTTTTATTGTTGGCAAACGGCGCGTCCATATTTATTCCTGCCTCAACCTTGCACGACAACAAAGAGGAAATTGTTATCAATACCGACGAAATCGCCTTCTATGTCAAAGATCAGCGTCTTTACAAGATCGGAGATATTTTACGCGTGCAACTCACGGAAGTGAAGGAAGCAACACGTAGTATTATGGGGATGGTCATCAAG","","","76002","MFQDNPLLAQLKQQIHDSKERVEGTVKSTDKAYGFLECDKKSYFIAPPAMKKVMHGDKISATIEKQGDKEQAEPEALIEPILTRFIAKVRFNKDKKLQVLVDHPNINQPIGAAQNKSVKKELQEGDWVVASLKTHPLRDDRFFYAQITQFICHADDELAPWWVTLARHEQPREPVQGQDQYEMQDKETRENLTALHFVTIDSETTQDMDDALYIEPLTSNNEQTGWQLLVAIADPTAYISLDSQIEKDAKQRCFTNYLPGFNIPMLPRELSDELCSLKPNETRPALVCYIQTDLQGNIIAPAKFVLANVQSKAKLTYSRVSDYLEGKENAWQPENQDMAQQIHWLHQFSLARTQWRKTHALLFKEKPDYSFVLGENGKVQEIKAEYRRIANQIVEESMIIANICAAQFLQKNLQCGIFNTHSGFDKKFLENAHHFLLASLANEENKAELQARYTVEHLATLNGYCQMRHDIEPIEGDYLEFRLRRFLTFAEFKAELAPHFGLGLNGYATWTSPIRKYSDMVNHRLIKAYLAHRPYEKPEESVLVRLQEARRQNRLVERDIADWLYCRYLADKVAEKVEFEAEVQDITRGGLRVLLLANGASIFIPASTLHDNKEEIVINTDEIAFYVKDQRLYKIGDILRVQLTEVKEATRSIMGMVIK","1172786","[FUNCTION] Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction (By similarity).[CATALYTIC ACTIVITY] Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.[SUBCELLULAR LOCATION] Cytoplasmic (By similarity).","exoribonuclease II","Cytoplasm","","
InterPro
IPR001900
Domain
Ribonuclease II and R
PF00773\"[189-532]TRNB
PS01175\"[499-523]TRIBONUCLEASE_II
InterPro
IPR003029
Domain
RNA binding S1
PF00575\"[572-657]TS1
SM00316\"[574-657]TS1
PS50126\"[574-659]TS1
InterPro
IPR004476
Family
RNase II and RNase R, bacteria
TIGR00358\"[6-658]T3_prime_RNase: VacB and RNase II family 3'-
InterPro
IPR011129
Domain
Cold shock protein
SM00357\"[23-78]TCSP
InterPro
IPR011804
Family
Ribonuclease II, bacterial
PTHR23355:SF6\"[51-649]TRIBONUCLEASE II
TIGR02062\"[1-657]TRNase_B: exoribonuclease II
InterPro
IPR013223
Domain
Ribonuclease B, OB region N-terminal
PF08206\"[24-80]TOB_RNB
noIPR
unintegrated
unintegrated
PTHR23355\"[51-649]TRIBONUCLEASE


","No hits to the COGs database.","Significant hit ( 9.5e-42) to 4/4 blocks of the IPB001900 family, which is described as \"Ribonuclease II domain\". Interpro entry for IP:IPR001900. IPB001900A 199-211 1.2e-05 IPB001900B 228-267 1.8e-17 IPB001900C 393-402 0.059 IPB001900D 507-526 4.8e-12","Residues 143 to 188 match (9e-13) PD:PD492953 which is described as II COMPLETE PROTEOME RNA-BINDING EXORIBONUCLEASE NUCLEASE RIBONUCLEASE RNB EXONUCLEASE RNASE ","","","","","Wed Feb 19 16:35:07 2003","","","","Wed Feb 19 16:35:07 2003","","Wed Feb 19 16:35:07 2003","Tue Jan 7 14:20:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01737 is paralogously related to AA01372 (3e-52).","","","","","","Residues 572 to 657 (E-value = 3.9e-10) place AA01737 in the S1 family which is described as S1 RNA binding domain (PF00575)","","","","","Cheng ZF, Deutscher MP. Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II. J Biol Chem. 2002 Jun 14;277(24):21624-9. PMID: 11948193 Cannistraro VJ, Kennell D. Escherichia coli ribonuclease II. Methods Enzymol. 2001;342:309-30. PMID: 11586905 Zilhao,R., Camelo,L. and Arraiano,C.M. DNA sequencing and expression of the gene rnb encoding Escherichia coli ribonuclease II. Mol. Microbiol. 8(1):43-51. PubMed: 8497196 ","","Mon Feb 17 08:09:10 2003","1","","","" "AA01738","1175624","1174839","786","ATGGGTTTCTTAACAGGTAAACGTATTTTAGTCACAGGTCTCGCCAGCAATCGTTCCATCGCCTACGGCATTGCGAAAGCGATGAAAGAACAAGGTGCGGAACTGGCTTTCACTTATTTAAATGAAAAATTACAACCGCGCGTAGAAGAATTTGCCAAAGAATTCGGTGTGAACATCGTGCTTCCGTTGGACGTTGCCACTGATGAAAGCATTCAAAACTGTTTTGCGGAATTAAGCAAACACTGGGATAAATTTGACGGTTTCGTGCACGCCATTGCATTCGCACCGGGCGATCAACTCGATGGCGATTACGTGAACGCGGCGACCCGTGAAGGCTATCGCATCGCCCACGACATCAGTGCTTACAGCTTCGTGGCAATGGCGCAAGCGGCACGCCCGTATTTGAATCCAAACGCCGCCTTACTTACCCTTTCTTACTTGGGCGCAGAACGTGCTATTCCTAACTACAACGTCATGTGTTTAGCCAAAGCTTCTCTTGAAGCGGCAACCCGCGTAATGGCAGCGGATTTAGGCAAAGACGGCATTCGTGTGAACGCCATTTCTGCCGGCCCGATTCGTACCTTGGCGGCATCCGGCATCAAAAACTTCAAGAAAATGCTTTCTGCTTTTGAGAAAACTGCGGCATTACGCCGCACCGTAACCATTGAAGATGTGGGCAACTCCGCCGCATTCCTATGTTCTGGTTTAGCTTCCGGCATCACCGGTGAAATCGTGCACGTGGATGCCGGTTTCAGCATCACCGCCATGGGAGAATTAGGCGAAGAA","","","30318","MGFLTGKRILVTGLASNRSIAYGIAKAMKEQGAELAFTYLNEKLQPRVEEFAKEFGVNIVLPLDVATDESIQNCFAELSKHWDKFDGFVHAIAFAPGDQLDGDYVNAATREGYRIAHDISAYSFVAMAQAARPYLNPNAALLTLSYLGAERAIPNYNVMCLAKASLEAATRVMAADLGKDGIRVNAISAGPIRTLAASGIKNFKKMLSAFEKTAALRRTVTIEDVGNSAAFLCSGLASGITGEIVHVDAGFSITAMGELGEE","1174838","[CATALYTIC ACTIVITY] Acyl-[acyl-carrier protein] + NAD(+) = trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.[PATHWAY] Fatty acid biosynthesis pathway; second reduction step.[SUBCELLULAR LOCATION] Inner membrane-associated (By similarity).","enoyl-(acyl-carrier-protein) reductase","Cytoplasm, Inner membrane","","
InterPro
IPR002198
Family
Short-chain dehydrogenase/reductase SDR
PTHR19410\"[4-249]TSHORT-CHAIN DEHYDROGENASES/REDUCTASE FAMILY MEMBER
PF00106\"[7-178]Tadh_short
InterPro
IPR002347
Family
Glucose/ribitol dehydrogenase
PR00081\"[159-178]T\"[180-197]T\"[215-235]TGDHRDH
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[6-202]Tno description
PTHR19410:SF12\"[4-249]TENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE


","No hits to the COGs database.","","Residues 4 to 254 match (6e-07) PD:PD563725 which is described as PROTEOME DEHYDROGENASE CHAIN COMPLETE SHORT ","","","","","","","","","","","Tue Jan 7 14:25:51 2003","Tue Jan 7 14:25:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01738 is paralogously related to AA00269 (3e-09).","","","","","","Residues 9 to 251 (E-value = 6.4e-10) place AA01738 in the adh_short family which is described as short chain dehydrogenase (PF00106)","","","","","Bergler,H., Hogenauer,G. and Turnowsky,F. Sequences of the envM gene and of two mutated alleles in Escherichia coli. J. Gen. Microbiol. 138 (Pt 10): 2093-2100 (1992) [PubMed: 1364817]. Kater,M.M., Koningstein,G.M., Nijkamp,H.J. and Stuitje,A.R. 1994. The use of a hybrid genetic system to study the functional relationship between prokaryotic and plant multi-enzyme fatty acid synthetase complexes. Plant Mol. Biol. 25(5):771-790. [PubMed: 8075395] Hoang,T.T. and Schweizer,H.P. Characterization of Pseudomonas aeruginosa enoyl-acyl carrier protein reductase (FabI): a target for the antimicrobial triclosanand its role in acylated homoserine lactone synthesis. J. Bacteriol. 181 (17): 5489-5497 (1999) [PubMed: 10464225]. ","","Tue Jan 7 14:25:51 2003","1","","","" "AA01739","1176572","1175718","855","ATGTCTTTACCAAAAGATCTTTGCACCGGTCATTTTTTTCTTCTTATTCCTCCCCAAAGCCATTATCATTACGCCATTCCTTTCTTTATTCAGAGAATAGTTATGCAAAATTTAGCCCTGGAAAATCTACTTAATCAAAAGCTCAGCAGCCATCTTATCAATGATTACGCGCCGAACGGATTACAGGTAGAAGGCAAACCTGAAGTTAAAAAAATCATCACCGGCGTGACCGCCAGCCAAGCCTTAATTGACTATGCCGTTGCACAAAAAGCCGACGCGCTACTCGTTCATCACGGTTATTTTTGGAAAAGTGAGAACCCTTGTATTCGCGGCATGAAAGGCAGACGTATCAAGGCGTTGCTGGTAAATGACATCAATTTATACGGCTATCATCTGCCACTGGACGTCCACCCCGAACTGGGCAACAACGCCCAATTAGCCCAATTATTAGGCATTGAAAACCTTCAACCATTGGAACAAGGCAGCTTCAGCATCCCGGTTTGGGGCACTTTAAAAGAACCGCTTAGCGCCGAACAATTTGCCCAACGCATTGAGCAAACACTCGCCCGCAAACCGTTAATTTGCACGGAAAACGGACCGCACTTTATTCGCAAAGTCGGTATTTGTACCGGCGGCGGACAGGGTTATATCGATCTTGCCGCCGCACAAGGTTGTGACGCCTTTATCACCGGTGAAGTTTCGGAACAAACCATTCATTCCGCCAGAGAACAAGGGGTTTATTTCTTTTCCTCCGGTCATCACGCCACCGAACGTTACGGGGTGAAAGCATTAGGCGAATGGCTGGCAAACGAATATGGTTTTGAGGTGGAATTTAAGGATATGGATAATCCGGCG","","","32380","MSLPKDLCTGHFFLLIPPQSHYHYAIPFFIQRIVMQNLALENLLNQKLSSHLINDYAPNGLQVEGKPEVKKIITGVTASQALIDYAVAQKADALLVHHGYFWKSENPCIRGMKGRRIKALLVNDINLYGYHLPLDVHPELGNNAQLAQLLGIENLQPLEQGSFSIPVWGTLKEPLSAEQFAQRIEQTLARKPLICTENGPHFIRKVGICTGGGQGYIDLAAAQGCDAFITGEVSEQTIHSAREQGVYFFSSGHHATERYGVKALGEWLANEYGFEVEFKDMDNPA","1175717","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR002678
Family
NGG1p interacting factor 3, NIF3
PTHR13799\"[32-285]TNGG1 INTERACTING FACTOR 3
PF01784\"[44-281]TNIF3
TIGR00486\"[35-285]TTIGR00486: conserved hypothetical protein T


","BeTs to 18 clades of COG0327COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG0327 is aom-k-y--drlb-efgh-nu--itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.8e-52) to 5/5 blocks of the IPB002678 family, which is described as \"Domain of unknown function DUF34\". Interpro entry for IP:IPR002678. IPB002678A 55-65 0.00036 IPB002678B 86-98 2.2e-05 IPB002678C 120-143 2.7e-15 IPB002678D 203-213 0.00017 IPB002678E 225-257 6e-17","Residues 160 to 284 match (3e-08) PD:PD438201 which is described as CPN0137/CP0635/CPJ0137 PROTEOME COMPLETE ","","","","","","","","","","","","Tue Jan 7 14:27:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01739 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 44 to 281 (E-value = 2.3e-115) place AA01739 in the NIF3 family which is described as NIF3 (NGG1p interacting factor 3) (PF01784)","","","","","","","","1","","","" "AA01740","1177303","1176698","606","ATGCCTTCTTACAACATCGTTGAGATTTTTGAAAGCCTGCAAGGCGAAGGTTTTAACACCGGTATGCCGTGCATTTTCGTGCGCTTCGGCAAATGCAATCTCGCCTGTCCTTGGTGTGATACTAATTATAATCAATTCGAACGCATGACGCTGGCGCAAGTGATGGAAGAAGTGCGGTCATTTTCTTCAAAGAATATTATCATCACCGGCGGCGAACCGACGATTGTTCCAAATATTGAAATCCTGCTTGAACAAATGAAATCGGAAGGTTATTTCCTCGCCATTGAAACCAATGGGCTGAAACCGATCCCACCACAAATTGATTACATCGCGACCAGTCCGAAACGCTTGTATCCACACAAATATGAACGACGTTGTATTGATTTTGCCCATGAAGTTCGTATCGTTGCAGATGAAAACGTTATGGCATTTTGTGAACTTATTGAAGACAAAATCCGCGCCGAGCGCTATTACCTTTCTCCTTGTGAAATTAACGGCAAAATGAATTTGCTGGAAACCATCACCCAACTTGGGCAATTAAATCAACGTGTAAACAGACCAAAATGGTTATTAAGTGTACAAACACATAAATTAATTGGCATTGAA","","","25695","MPSYNIVEIFESLQGEGFNTGMPCIFVRFGKCNLACPWCDTNYNQFERMTLAQVMEEVRSFSSKNIIITGGEPTIVPNIEILLEQMKSEGYFLAIETNGLKPIPPQIDYIATSPKRLYPHKYERRCIDFAHEVRIVADENVMAFCELIEDKIRAERYYLSPCEINGKMNLLETITQLGQLNQRVNRPKWLLSVQTHKLIGIE","1176697","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR007197
Domain
Radical SAM
PF04055\"[26-174]TRadical_SAM


","No hits to the COGs database.","Significant hit ( 1.2e-12) to 2/3 blocks of the IPB001989 family, which is described as \"Radical activating enzymes\". Interpro entry for IP:IPR001989. IPB001989A 18-45 1.5e-08 IPB001989B 65-76 0.024","Residues 5 to 53 match (4e-09) PD:PD405600 which is described as HYPE HYDROGENASE EXPRESSION/FORMATION PROTEOME HYPE-LIKE COMPLETE HUPE ","","","","","","","","","","","","Tue Jan 7 14:28:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01740 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 26 to 174 (E-value = 2e-11) place AA01740 in the Radical_SAM family which is described as Radical SAM superfamily (PF04055)","","","","","","","","1","","","" "AA01741","1177755","1177333","423","ATGTTTAAAGTTTCTAAAGAATTTAGCTTTGATATGGCGCATCTGTTGGATGGGCATGATGGGAAGTGTCAGAATTTACACGGGCACACCTATAAATTGCAGGTGGAAGTGCGTGGAGATTTGTATCAAGAAGGCGCGAAACAAGGCATGGTTATTGATTTCAGCGATTTGAAGAAAATCGTCAATCACGCCATATTGGAACCGATGGATCACGCATTTATTTACGATCAAACCAGTGAACGTGAGAGCAAAATCGCATCTCTATTGCAACAGCTTGATTCTAAAACCTTCGGTGTCCCTTTTCGCACTACGGCGGAACAATTGGCTCAATTTATTTTTAATCAGTTGAAATATCAGAAAAACCTTCCCGTTTCCGCCATTCGTCTATGGGAAACGCCCACATCATTTTGCGAATATGGGGAA","","","16232","MFKVSKEFSFDMAHLLDGHDGKCQNLHGHTYKLQVEVRGDLYQEGAKQGMVIDFSDLKKIVNHAILEPMDHAFIYDQTSERESKIASLLQQLDSKTFGVPFRTTAEQLAQFIFNQLKYQKNLPVSAIRLWETPTSFCEYGE","1177332","[SIMILARITY] Belongs to the PTPS family.","6-pyruvoyl tetrahydrobiopterin synthase","Cytoplasm","","
InterPro
IPR007115
Family
6-pyruvoyl tetrahydropterin synthase and hypothetical protein
PD004049\"[6-40]TPTPS_HAEIN_P44123;
PIRSF006113\"[1-141]T6-pyruvoyl tetrahydropterin synthase
PTHR12589\"[1-79]T\"[97-139]TPYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE
PF01242\"[1-141]TPTPS
noIPR
unintegrated
unintegrated
G3DSA:3.30.479.10\"[8-139]Tno description


","BeTs to 19 clades of COG0720COG name: 6-pyruvoyl-tetrahydropterin synthaseFunctional Class: HThe phylogenetic pattern of COG0720 is aompk--qv---bcefghsnujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 6.8e-26) to 4/4 blocks of the IPB001914 family, which is described as \"6-pyruvoyl tetrahydropterin synthase\". Interpro entry for IP:IPR001914. IPB001914A 9-18 0.032 IPB001914B 21-35 1.2e-09 IPB001914C 104-114 0.031 IPB001914D 124-141 1.6e-06","Residues 72 to 139 match (1e-09) PD:PD593190 which is described as COMPLETE PROTEOME SYNTHASE NMA0704 6-PYRUVOYL TETRAHYDROBIOPTERIN ","","","","","","","","","","","Tue Jan 7 14:40:08 2003","Tue Jan 7 14:40:08 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01741 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 141 (E-value = 3e-08) place AA01741 in the PTPS family which is described as 6-pyruvoyl tetrahydropterin synthase (PF01242)","","","","","","","","1","","","" "AA01743","1179411","1177948","1464","ATGTTGGTGCGTCGTGAAAAATTAGCCGCCTTGCGCGCCAAAGGCAATGCCTTCCCGAACCAATTCCGTCGCGATGCGCTTGCACAGGATTTGCACGATAAATATGATGCCGAAGAGGGCGAAGCATTAAAAGAAAAACACATTGAAGTTACCGTTGCCGGACGTATCATGACTCGTCGCGCCATGGGTAAAGCCACCTTTATCACCATTCAAGATATGAGCGGCAAAATTCAGCTTTATGTGGCGCGCGATAACTTGCCTGAAGGCGTGTATAAAGATGATGTAGGTCACTGGGATTTGGGTGACATTGTCGGTATTAAAGGTTCGCTATTCAAAACCAAAACCGACGAACTCACCGTGAAAGCCACCAAAGTTCAGTTATTAACCAAAGCCCTTCGCCCGCTGCCGGACAAATTCCACGGTTTAACCGACCAAGAAGTGCGTTATCGTCAACGTTATTTGGATTTAATTTCTAACGAAGAATCCCGCCGCACTTTCATCATTCGTTCTAAAGTCGTCGCCGGCATTCGTGAATATTTCCTTTCCAAAGGCTTCATGGAAGTGGAAACCCCAATGTTGCAAGTGATTCCAGGTGGTGCAGCGGCTCGTCCGTTTGTCACACATCACAATGCCTTAGACGTGGATATGTATTTGCGTATCGCACCGGAACTTTACTTAAAACGTTTAGTGGTGGGCGGCTTTGAACGCGTATTCGAATTGAACCGCAATTTCCGCAACGAAGGTGTTTCCGTGCGTCACAATCCCGAATTCACCATGCTGGAATACTACCAAGCCTACGCCGATTACCATGATTTAATGGACAACACCGAAGAATTATTGCGCAAATTGGCGATTGATATTTTAGGCACCACCATCGTGAAATATGGCGACTTAGAATTTGATTTCGGCAAACCGTTCGAGCGTATCACCTTACACGACGCCACCATTAAATACGGCGCCGAAAAAGGCATCGTAAAAGAAGATTTATACGACTTCGACCGTGCCAAAGCTACCGCAGAACGCTTAGGCATTGAAGTACAAAAATCCTGGGGCTTAGGCAGCATTGTGAACGCCACCTTTGAAGAAGTGGCAGAACATCACTTAATTCAGCCGACTTTTTTAATGGCTCACCCTGCTGAAATTTCACCGCTCGCCCGTCGTAACGATGAAAATCCGGAAGTCACAGACCGTTTTGAACTCTTCATCGGCGGACGTGAAATCGGTAACGGCTTCTCAGAATTAAACGACGCCGAAGACCAAAACGACCGTTTCGACGCACAAGTCGCCGCCAAAGAAGCCGGTGATGACGAAGCGATGTTTAAAGATGAAGACTTCGTGATCGCACTCGAACACGGCTTACCACCAACAGCTGGCGAGGGCTTAGGCATCGACCGCCTGGCAATGCTCTACGCCAACGCGCCATCTATCCGTGATGTGATTTTATTCCCGGCAATGCGGCAGAGG","","","57038","MLVRREKLAALRAKGNAFPNQFRRDALAQDLHDKYDAEEGEALKEKHIEVTVAGRIMTRRAMGKATFITIQDMSGKIQLYVARDNLPEGVYKDDVGHWDLGDIVGIKGSLFKTKTDELTVKATKVQLLTKALRPLPDKFHGLTDQEVRYRQRYLDLISNEESRRTFIIRSKVVAGIREYFLSKGFMEVETPMLQVIPGGAAARPFVTHHNALDVDMYLRIAPELYLKRLVVGGFERVFELNRNFRNEGVSVRHNPEFTMLEYYQAYADYHDLMDNTEELLRKLAIDILGTTIVKYGDLEFDFGKPFERITLHDATIKYGAEKGIVKEDLYDFDRAKATAERLGIEVQKSWGLGSIVNATFEEVAEHHLIQPTFLMAHPAEISPLARRNDENPEVTDRFELFIGGREIGNGFSELNDAEDQNDRFDAQVAAKEAGDDEAMFKDEDFVIALEHGLPPTAGEGLGIDRLAMLYANAPSIRDVILFPAMRQR","1177947","[CATALYTIC ACTIVITY] ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys).[COFACTOR] Binds 3 magnesium ions per subunit (By similarity).[SUBUNIT] Homodimer (By similarity).[SUBCELLULAR LOCATION] Cytoplasmic.","lysyl-tRNA synthetase","Cytoplasm","","
InterPro
IPR002313
Family
Lysyl-tRNA synthetase, class-2
PR00982\"[181-191]T\"[197-213]T\"[226-239]T\"[244-261]T\"[370-386]TTRNASYNTHLYS
PTHR22594:SF4\"[115-488]TLYSYL-TRNA SYNTHETASE
TIGR00499\"[1-488]TlysS_bact: lysyl-tRNA synthetase
InterPro
IPR004364
Domain
tRNA synthetase, class II (D, K and N)
PF00152\"[144-487]TtRNA-synt_2
InterPro
IPR004365
Domain
Nucleic acid binding, OB-fold, tRNA/helicase-type
PF01336\"[50-128]TtRNA_anti
InterPro
IPR006195
Domain
Aminoacyl-transfer RNA synthetase, class II
PS50862\"[166-483]TAA_TRNA_LIGASE_II
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[1-136]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.30.930.10\"[137-488]Tno description
PTHR22594\"[115-488]TASPARTYL/LYSYL-TRNA SYNTHETASE


","No hits to the COGs database.","Significant hit ( 9.3e-07) to 2/2 blocks of the IPB002106 family, which is described as \"Aminoacyl-transfer RNA synthetases class-II\". Interpro entry for IP:IPR002106. IPB002106A 179-191 0.017 IPB002106B 462-476 0.025","Residues 252 to 290 match (3e-07) PD:PD381293 which is described as SYNTHETASE LIGASE LYSYL-TRNA AMINOACYL-TRNA ATP-BINDING BIOSYNTHESIS PROTEOME COMPLETE LYSINE--TRNA LYSRS ","","","","","","","","","","","Tue Jan 7 14:44:42 2003","Tue Jan 7 14:44:42 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01743 is paralogously related to AA00801 (5e-33), AA02856 (6e-17) and AA02233 (2e-09).","","","","","","Residues 144 to 487 (E-value = 2.1e-199) place AA01743 in the tRNA-synt_2 family which is described as tRNA synthetases class II (D, K and N) (PF00152)","","","","","Leveque,F., Plateau,P., Dessen,P. and Blanquet,S. Homology of lysS and lysU, the two Escherichia coli genes encoding distinct lysyl-tRNA synthetase species. Nucleic Acids Res. 18(2): 305-312.1990. PubMed: 2183178. Commans,S., Plateau,P., Blanquet,S. and Dardel,F. Solution structure of the anticodon-binding domain of Escherichia coli lysyl-tRNA synthetase and studies of its interaction with tRNA(Lys). J. Mol. Biol. 253(1): 100-113. 1995. PubMed: 7473706. Clark,R.L. and Neidhardt,F.C. Roles of the two lysyl-tRNA synthetases of Escherichia coli: analysis of nucleotide sequences and mutant behavior. J. Bacteriol. 172(6): 3237-3243.1990 PubMed: 2188953.","","Tue Jan 7 14:44:42 2003","1","","","" "AA01744","1180412","1179513","900","GTGGTCAACACCATTAAAAATCTGGAACAAGGCTTGGAAGATGTGGACGGACTGTTGGAACTTGCCGTGGAAGCGGGTGATGAAGACACCTTCAACGAAGCCATCACCGAATTAAATGCGCTTGAACAACAACTCGAAAAATTAGAATTCCGCCGTATGTTCAGCGGTGAACACGATGCCTGCGATTGCTATGTGGATTTACAAGCGGGTTCAGGCGGTACGGAAGCGCAGGACTGGACGGAAATGTTATTGCGGATGTATTTGCGTTGGGCGGAAAGCAAAGGCTTCAAAACCGAATTAATGGAAGTTTCCGACGGCGATGTGGCAGGGTTGAAATCCGCCACCATCAAAGTGAGCGGCGAATACGCCTTCGGTTGGTTACGCACCGAAACCGGCATTCACCGTTTGGTGCGCAAAAGCCCGTTCGATTCCAATAACCGTCGCCATACCTCTTTCAGTGCCGCATTTGTGTATCCTGAAATTGACGACGACATTGACATCGAAATCAATCCGGCAGACTTGCGTATCGATGTCTATCGCGCGTCCGGCGCAGGCGGTCAGCACGTAAACAAAACCGAAAGTGCGGTGCGAATTACCCACATACCAAGCGGCATTGTAGTGCAATGTCAAAATGACCGTTCCCAGCACAAGAATAAAGACCAGGCAATGAAGCAGTTAAAAGCGAAGTTGTACGAGCTGGAATTGCAAAAGAAAAACGCCGACAAACAAGCCATGGAAGACAATAAATCCGACATCGGCTGGGGCAGCCAAATTCGTTCTTATGTGTTGGACGATTCCCGCATTAAAGATTTACGCACCGGCATTGAAAACCGCAATACGCAAGCGGTGTTAGACGGCGATTTGGATCGTTTTATTGAAGCGAGTTTAAAGGCCGGCTTG","","","33678","VVNTIKNLEQGLEDVDGLLELAVEAGDEDTFNEAITELNALEQQLEKLEFRRMFSGEHDACDCYVDLQAGSGGTEAQDWTEMLLRMYLRWAESKGFKTELMEVSDGDVAGLKSATIKVSGEYAFGWLRTETGIHRLVRKSPFDSNNRRHTSFSAAFVYPEIDDDIDIEINPADLRIDVYRASGAGGQHVNKTESAVRITHIPSGIVVQCQNDRSQHKNKDQAMKQLKAKLYELELQKKNADKQAMEDNKSDIGWGSQIRSYVLDDSRIKDLRTGIENRNTQAVLDGDLDRFIEASLKAGL","1179512","[FUNCTION] Peptide chain release factor 2 directs the termination of translation in response to the peptide chaintermination codons uga and uaa (by similarity). [SUBCELLULAR LOCATION] Cytoplasmic. [PTM] Methylated by hemK. Methylation increases the termination efficiency of RF2. Is absent when the factor is overproduced (By similarity)[MISCELLANEOUS] The gene for this protein contains a uga in-frame termination codon after leu-25; a naturally occurring frameshift enables complete translation of rf-2. This provides a mechanism for the protein to regulate its own production (by similarity). [SIMILARITY] Belongs to the prokaryotic and mitochondrial release factors family. ","peptide chain release factor RF-2","Cytoplasm","","
InterPro
IPR000352
Domain
Class I peptide chain release factor
PF00472\"[160-272]TRF-1
PS00745\"[180-196]TRF_PROK_I
InterPro
IPR004374
Family
Peptide chain release factor 2
PIRSF500106\"[1-300]TPeptide chain release factor 2
PTHR11075:SF6\"[2-300]TPEPTIDE CHAIN RELEASE FACTOR 2
TIGR00020\"[1-300]TprfB: peptide chain release factor
InterPro
IPR005139
Domain
PCRF
PF03462\"[20-130]TPCRF
InterPro
IPR012086
Family
Protein chain release factor, RF-1/RF-2
PIRSF003056\"[1-300]TProtein chain release factor, RF-1/RF-2
noIPR
unintegrated
unintegrated
PTHR11075\"[2-300]TPEPTIDE CHAIN RELEASE FACTOR


","BeTs to 16 clades of COG1186COG name: Protein chain release factor BFunctional Class: JThe phylogenetic pattern of COG1186 is ------yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit (1.7e-124) to 4/4 blocks of the IPB000352 family, which is described as \"Class I peptide chain release factor\". Interpro entry for IP:IPR000352. IPB000352A 56-102 1.6e-30 IPB000352B 109-160 2.7e-33 IPB000352C 173-219 4.8e-47 IPB000352D 258-285 2.1e-10","","","","","","","","","","","","Tue Jan 7 14:49:00 2003","Tue Jan 7 14:49:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01744 is paralogously related to AA00649 (1e-50).","","","","","","Residues 162 to 272 (E-value = 5.8e-72) place AA01744 in the RF-1 family which is described as Peptidyl-tRNA hydrolase domain (PF00472)","","","","","Craigen,W.J., Cook,R.G., Tate,W.P. and Caskey,C.T. Bacterial peptide chain release factors: conserved primary structure and possible frameshift regulation of release factor 2 Proc. Natl. Acad. Sci. U.S.A. 82 (11), 3616-3620 (1985) PubMed: 3889910 Lee,C.C., Kohara,Y., Akiyama,K., Smith,C.L., Craigen,W.J. and Caskey,C.T. Rapid and precise mapping of the Escherichia coli release factor genes by two physical approaches J. Bacteriol. 170 (10), 4537-4541 (1988) PubMed: 3049538 Kawakami,K., Jonsson,Y.H., Bjork,G.R., Ikeda,H. and Nakamura,Y. Chromosomal location and structure of the operon encoding peptide-chain-release factor 2 of Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 85 (15), 5620-5624 (1988) PubMed: 2456575 ","","Tue Jan 7 14:49:00 2003","1","","","" "AA01745","1180692","1180534","159","TTGGAGTTTCGTTCGCTCTACCCAATTCCCGCAAAATCCCTTATAATCCCGCACTTAATTTACCTTTTTACGACATTCATTATCATGTTTGAAATTAATCCTATCAAAAATAAAATCGCCGATTTAACCGACCGCACTTCCGTGCTTCGGGGGTATCTT","","","6193","LEFRSLYPIPAKSLIIPHLIYLFTTFIIMFEINPIKNKIADLTDRTSVLRGYL","1180534","","conserved hypothetical protein (possible peptide chain release factor 2)","Cytoplasm","This sequence matches to gi|1172913, a predicted peptide chain release factor 2 from Haemophilus influenzae strain Rd KW20. Also see gi|16121194.","
noIPR
unintegrated
unintegrated
signalp\"[1-29]?signal-peptide
tmhmm\"[15-35]?transmembrane_regions


","BeTs to 3 clades of COG1186COG name: Protein chain release factor BFunctional Class: JThe phylogenetic pattern of COG1186 is ------yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Thu Feb 26 11:09:47 2004","Thu Feb 26 11:09:47 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01745 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 11:09:47 2004","","","","","","","","","","","","","1","","","" "AA01746","1180776","1181456","681","ATGAAAAAAATTATTACTACGCTTTCTCTTTTGGCTATATCTATGAGTGTAACGGCAAATGATGTTGCACTGAAAAGTAAATTGGAAAAGCTTGGTGTGAAAGATATTGATATTCAAACTTCACCGATTAAAGGCTTAAAAACTGTCGTAAGCGACCAAGGCATTTTTTACGCAAGTGAAGACGGCGAATATTTATTACAAGGTAAAATCTACAAATTAACCGATAAAGGCATTAGCAACGTCACTAATAAAGTGTTGCTGGATAAATTAAATGCGCTGAAAAATGAAATGATTGTGTATCCGGCAAAAAATGAAAAACACGTCATTACTGTATTTATGGATATTACCTGCCATTACTGCCATTTGTTACATCAACAAGTGAAAGAATATAACGACTTAGGCATTACCGTACGTTATTTGGCGTTCCCGCGTGCAGGTATGGAGAGTCAAACTGCAGGGCAAATGGAAGCGATTTTTACCGCAAAAGACCCAACATTCGCTTTAAACGAAGCGGAAAAAGGCAATCTTCCAAAAGAATTGAAGACCCCGAATGTGGTGAGAAAACATTATTTGCTTGGCGCTCAATTTGGTGTAAACGGAACGCCGACTATCATTACCAGTGAAGGCGAAGTTATTGGTGGTTATCTAAAACCTGCTGATTTACTTGCAGCGTTAGAAGGA","","","24914","MKKIITTLSLLAISMSVTANDVALKSKLEKLGVKDIDIQTSPIKGLKTVVSDQGIFYASEDGEYLLQGKIYKLTDKGISNVTNKVLLDKLNALKNEMIVYPAKNEKHVITVFMDITCHYCHLLHQQVKEYNDLGITVRYLAFPRAGMESQTAGQMEAIFTAKDPTFALNEAEKGNLPKELKTPNVVRKHYLLGAQFGVNGTPTIITSEGEVIGGYLKPADLLAALEG","1181455","[FUNCTION] Required for disulfide bond formation in some periplasmic proteins. acts by transferring its disulfide bond toother proteins and is reduced in the process. DsbC is reoxidized by a yet uncharacterized protein. also acts as a disulfide isomerase (by similarity). [SUBUNIT] Homodimer (by similarity). [SUBCELLULAR LOCATION] Periplasmic (by similarity). [SIMILARITY] Belongs to the thioredoxin family. DsbC subfamily. ","thiol:disulfide interchange protein","Periplasm, Cytoplasm","","
InterPro
IPR009094
Domain
Disulfide bond isomerase, N-terminal
G3DSA:3.10.450.70\"[20-70]Tno description
InterPro
IPR012335
Domain
Thioredoxin fold
G3DSA:3.40.30.10\"[71-225]Tno description
InterPro
IPR014679
Family
Thiol:disulphide interchange DsbC
PIRSF500113\"[1-227]TThiol:disulphide interchange protein DsbC
noIPR
unintegrated
unintegrated
PIRSF001489\"[1-227]TThiol:disulphide interchange protein, DsbG/DsbC types
signalp\"[1-19]?signal-peptide


","BeTs to 7 clades of COG1651COG name: Protein-disulfide isomeraseFunctional Class: OThe phylogenetic pattern of COG1651 is ao-----q-dr-bcefghsnujxi--Number of proteins in this genome belonging to this COG is","","Residues 20 to 76 match (2e-08) PD:PD579730 which is described as THIOL:DISULFIDE INTERCHANGE COMPLETE PROTEOME DSBC PRECURSOR REDOX-ACTIVE PERIPLASMIC CENTER SIGNAL ","","","","","","","","","","","Tue Jan 7 14:55:06 2003","Tue Jan 7 14:55:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01746 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Shevchik,V.E., Condemine,G. and Robert-Baudouy,J. Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity. EMBO J. 13 (8): 2007-2012 (1994) [PubMed: 8168497].Lovett,S.T. and Kolodner,R.D. Nucleotide sequence of the Escherichia coli recJ chromosomal region and construction of recJ-overexpression plasmids J. Bacteriol. 173 (1), 353-364 (1991) PubMed: 1987126 Missiakas,D., Georgopoulos,C. and Raina,S. The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation EMBO J. 13 (8), 2013-2020 (1994) PubMed: 8168498 Zapun,A., Missiakas,D., Raina,S. and Creighton,T.E. Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. Biochemistry 34 (15): 5075-5089 (1995) [PubMed: 7536035].Joly,J.C. and Swartz,J.R. In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC. Biochemistry 36 (33): 10067-10072 (1997) [PubMed: 9254601].McCarthy,A.A., Haebel,P.W., Torronen,A., Rybin,V., Baker,E.N. and Metcalf,P. Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli. Nat. Struct. Biol. 7 (3): 196-199 (2000) [PubMed: 10700276].","","Tue Jan 7 14:55:06 2003","1","","","" "AA01747","1181499","1183190","1692","GTGCCGGCAGGTAATAAACTCTGTGACGATCCGCTCTTGGATCGTCTCTATCGCTCGCGGCACATTAAAAACGCTTGCCAGTTAGACCGCACTTTAGCCGCCATTCACAACCCGAATCTGATGTCCGGTTTGGATGATGCTGTAGCGCTTTTGCTGGAAGCCTACGAAAAACAGCAAAAAATCGTTATCGTCGGCGATTTCGATGCGGACGGTGCGACAAGCACGGCATTGGCGGTGTTGGCGTTGCGCCAGCTTGGTTTTGTCAACGTCGCTTATTTGGTACCGAATCGCTTCGAGCAAGGTTACGGTTTAAGTGTTGCAGTGGCGCAAGAGGCATTGGCGCTGGATGTTGAACTGCTTATCACGGTGGATAATGGTGTGTCTTCTCATGAGGGCGTAGCGTTTCTAAAAGAACGGGGCGTGAATGTTATCGTCACCGACCATCATTTGCCGCCGGAAAGCTTGCCGAGTGCCGATGCCATCATCAATCCGAATCTTGCCCATTGCGGTTTTCCGTCGAAAAATCTTGCCGGTGTGGGCGTGGCGTTTTATCTTATGCTTGCTTTGCGGGCGAAATTTCGTGAATTGGGCATGTTTGACGCCAAAAATCAGCCGAATTTCACCGAACTGCTGGATTTGGTGGCGTTAGGTACGGTGTCTGATGTAGTGCCGTTGGATCAAAACAATCGCATTCTGGTGTATCAGGGCTTGGCGCGTATTAAAGCGCAGCGTTGCCGTTTTGGTATTCGAGCTTTGGCAGAAGTGGCAAAACGGGATTTAGCGGGATTTTCCGCATCGGATTTGGGTTTTTCTATTGCACCGCGATTAAATGCGGCGGGACGTTTGGATAATATGTCCGTAGGCGTTGAATTATTGCTAGCAGAAGACATGGAAAGCGCCCGTGCCTTGGCGTTAGAATTAGACGGCTTAAATCAAGCGCGCAAAGAAATCGAGCAGGGCATGAAGCTGGAAGCTTTAAAAATATGCCAAAATCTCACCGCACTTGAAAACCAATTGCCACATTCCATCGTGCTGTATCAGGCGGATTGGCATCAAGGTGTACTGGGCATTGTGGCATCGCGTATTAAAGACCAATTTCACCGCCCGGTGATTGCCTTTGCACAGGAGCAAGATGGCATTTTAAAAGGTTCCGCACGCTCCATTCCGGGTTTACATATTCGTGATGCGCTGGAACGGGTTTATTCGCAGCACCCGGATTTAATTTTAAAATTCGGCGGTCATGCAATGGCGGCGGGCTTAAGCATTAATGAAAACTATTTTGCCGATTTTCAACGCATTTTTAACGAGACGGTCAGTGAGTTGTTGGCTCAGGAACAATTACAAGGCAGCATTTGGACGGATGGCGAACTGAGCGTGAATGAGCTGAATCTGAATACGGCGGAACGTTTAAAATCTGCCGGCCCTTGGGGGCAAGCCTTCCCCGAACCTTTATTTGACGGCGAGTTTAAAATCCTACAACAGCGCTTGGTAGGGGAAAAACATTTAAAAATGATGGTGGAATCCAAACTGGGCGGACCATTGATGGATGCTATCGCATTTAATGTGGATACGCGCTATTATCCTGATTTATCAATAAAAACAGCAAAACTGGTATATAAGTTAGACATTAATGAATTTCGCGGCAATCGGGATATTCAGTTATTAATTGATTATATTGAACCTTTAGAGAAT","","","63244","VPAGNKLCDDPLLDRLYRSRHIKNACQLDRTLAAIHNPNLMSGLDDAVALLLEAYEKQQKIVIVGDFDADGATSTALAVLALRQLGFVNVAYLVPNRFEQGYGLSVAVAQEALALDVELLITVDNGVSSHEGVAFLKERGVNVIVTDHHLPPESLPSADAIINPNLAHCGFPSKNLAGVGVAFYLMLALRAKFRELGMFDAKNQPNFTELLDLVALGTVSDVVPLDQNNRILVYQGLARIKAQRCRFGIRALAEVAKRDLAGFSASDLGFSIAPRLNAAGRLDNMSVGVELLLAEDMESARALALELDGLNQARKEIEQGMKLEALKICQNLTALENQLPHSIVLYQADWHQGVLGIVASRIKDQFHRPVIAFAQEQDGILKGSARSIPGLHIRDALERVYSQHPDLILKFGGHAMAAGLSINENYFADFQRIFNETVSELLAQEQLQGSIWTDGELSVNELNLNTAERLKSAGPWGQAFPEPLFDGEFKILQQRLVGEKHLKMMVESKLGGPLMDAIAFNVDTRYYPDLSIKTAKLVYKLDINEFRGNRDIQLLIDYIEPLEN","1183189","FUNCTION] Single-stranded-dna-specific exonuclease. Required for many types of recombinational events, although the stringency of the requirement for recj appears to vary with the type of recombinational event monitored and the other recombination gene products which are available (by similarity). ","single-stranded-DNA-specific exonuclease","Cytoplasm","","
InterPro
IPR001667
Domain
Phosphoesterase, RecJ-like
PF01368\"[54-219]TDHH
InterPro
IPR003156
Domain
Phosphoesterase, DHHA1
PF02272\"[367-436]TDHHA1
InterPro
IPR004610
Family
Bacterial RecJ exonuclease
TIGR00644\"[9-559]TrecJ: single-stranded-DNA-specific exonucle


","BeTs to 21 clades of COG0608COG name: Single-stranded DNA-specific exonucleaseFunctional Class: LThe phylogenetic pattern of COG0608 is aompk--qvd-lbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 5.3e-12) to 3/3 blocks of the IPB001667 family, which is described as \"DHH family\". Interpro entry for IP:IPR001667. IPB001667A 66-79 0.011 IPB001667B 143-150 0.0077 IPB001667C 411-419 0.01","Residues 486 to 562 match (3e-32) PD:PD024656 which is described as EXONUCLEASE COMPLETE PROTEOME RECJ SINGLE-STRANDED-DNA-SPECIFIC 3.1.-.- HYDROLASE NUCLEASE SSDNA EXONUCLEASE ","","","","","","","","","","","Tue Jan 7 14:58:46 2003","Tue Jan 7 14:58:46 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01747 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 367 to 436 (E-value = 5e-17) place AA01747 in the DHHA1 family which is described as DHHA1 domain (PF02272)","","","","","Lovett,S.T. and Kolodner,R.D. Nucleotide sequence of the Escherichia coli recJ chromosomal region and construction of recJ-overexpression plasmids J. Bacteriol. 173 (1), 353-364 (1991) PubMed: 1987126 Lovett,S.T. and Kolodner,R.D. Identification and purification of a single-stranded-DNA-specific exonuclease encoded by the recJ gene of Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 86 (8), 2627-2631 (1989) PubMed: 2649886 ","","Tue Jan 7 14:58:46 2003","1","","","" "AA01748","1183202","1183870","669","ATGTTGCGGGTCGGATTGTTTATCATGCTATTATGCGTAGGCGGATTCGCTGCGGCACAAGCCGGTGATGAATCCGTTGCGCCTGATCCTGCTGTTTTGCTTGATGAAGAAAGTCCGGAATTTGAAGATGGCAAAGATTATTTCTCTTACGAATATCCTATCGCCATGCCTGCCCGTAATGATCACCGCGTTATTATTCAGTTCTTTTTTGATTATGACTGCCGTGTTTGTTCCTCCGCACAGGATATTTTAGAACTTTACACGCAAATCAACCGTGATCGTGTAGTGTTGGAAGAATTCCCCGTCGCTACCAACAAAGCGCGCTTCACTGCCGGTGTTTTCTTCAGTTTACAAGCTTTAAATGTGGAGCATCTGTCTTCCGCATTACTGTTTGAAACCTCGGAACGGCAGCGTTATATCAAATTATCCCGCATTGAAAATCTGGTACATTGGCTGCAAAAACAAGGCATTGAGCGCGATAGTTTCTTGGAAATGTATCATTCCGATCAGATTCACCAAAAAGTGAATGACGCCGTGCTGATGACGGAAGAGTATGGTGTGTTCACCTTTCCTTATGTGATCATCAACGGCAAATACGTTTTGACCGCCAGCACGCTGTATAACGATGATTATGCGCTCGCCGTGTTGGATTTTTTAGTAAATAGAAAA","","","25640","MLRVGLFIMLLCVGGFAAAQAGDESVAPDPAVLLDEESPEFEDGKDYFSYEYPIAMPARNDHRVIIQFFFDYDCRVCSSAQDILELYTQINRDRVVLEEFPVATNKARFTAGVFFSLQALNVEHLSSALLFETSERQRYIKLSRIENLVHWLQKQGIERDSFLEMYHSDQIHQKVNDAVLMTEEYGVFTFPYVIINGKYVLTASTLYNDDYALAVLDFLVNRK","1183869","[FUNCTION] Involved in disulfide-bond formation. Acts by transferring its disulfide bond to other proteins. Involved in theproduction of protease and alkaline phosphatase, motility, metal resistance, and multi-drug resistance. [SUBCELLULAR LOCATION] Periplasmic (by similarity). [SIMILARITY] Belongs to the thioredoxin family. dsbA subfamily. ","thiol:disulfide interchange protein","Cytoplasm, Periplasm, Inner membrane","","
InterPro
IPR012335
Domain
Thioredoxin fold
G3DSA:3.40.30.10\"[39-223]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide


","BeTs to 6 clades of COG0526COG name: Thiol-disulfide isomerase and thioredoxinsFunctional Class: O,CThe phylogenetic pattern of COG0526 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 6.3e-06) to 3/4 blocks of the IPB001853 family, which is described as \"DSBA oxidoreductase\". Interpro entry for IP:IPR001853. IPB001853A 38-50 31 IPB001853B 66-80 81 IPB001853D 161-199 0.00092","Residues 41 to 222 match (5e-56) PD:PD415819 which is described as COMPLETE PROTEOME HI1215 PM0193 SIGNAL PRECURSOR ","","","","","","","","","","","Tue Jan 7 15:04:30 2003","Tue Jan 7 15:04:30 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01748 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Grauschopf,U., Winther,J.R., Korber,P., Zander,T., Dallinger,P. and Bardwell,J.C. Why is DsbA such an oxidizing disulfide catalyst? Cell. 83 (6), 947-955 (1995) PubMed: 8521518 Akiyama,Y., Kamitani,S., Kusukawa,N. and Ito,K. In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product The Journal of biological chemistry. 267 (31), 22440-22445 (1992) PubMed: 1429594 Martin,J.L., Bardwell,J.C. and Kuriyan,J. Crystal structure of the DsbA protein required for disulphide bond formation in vivo Nature. 365 (6445), 464-468 (1993) PubMed: 8413591 Guddat,L.W., Bardwell,J.C., Zander,T. and Martin,J.L. The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding Protein science : a publication of the Protein Society. 6 (6), 1148-1156 (1997) PubMed: 9194175 ","","Tue Jan 7 15:04:30 2003","1","","","" "AA01750","1183890","1184579","690","ATGAAAATTGGTATTGTCGGCGCCATGGCGCAGGAAGTGGAAATTTTGGTTGGGTTAATGACGGATAAAAACGTCACAAAATTGGTTTCCGGTACGATTTATGAAGGTAAAATTCATGGCAAAAATATTGCCTTGTTGCAATCGGGTATTGGCAAAGTCGCTGCTGCCATGGGCACCACCGCTTTATTGCAACTTGCTAAGCCGAACCTGGTGATTAACACAGGTTCCGCCGGTGGGGTGGCGGAGGGATTGCACGTCGGTGATGTGATTGTATCCACCGAAACCCAATACCACGACGCCGATGTGACCGCCTTCGGTTATGCCAAAGGACAGCTACCCGCATGCCCTGTCACTTTTGTTTCTGATGCCCGTTTGGTCGAATTGGCGGAACGTACTGCAAAACAACTTGGGCAACGGGTAAAACGCGGTTTAATTTGTTCCGGCGATAGCTTTATTCAAGGCGGAGAACGTTTGGCGCAGATTAAGCAGGATTTCCCAAATGTCATCGCGGTGGAAATGGAAGCCACAGCTATTGCGCAAGTTTGCCATGCGTTTAACGTGCCTTTCGTGGTGGTGCGCGCCATTTCCGATGCGGGCGATGGCAAAGCTAATATGTCTTTTGAAGAATTTCTACCGCTCGCTGCCAAACAATCGTCCGACATGGTTGTCGCCATGTTGGCGGAGTTGAAT","","","24099","MKIGIVGAMAQEVEILVGLMTDKNVTKLVSGTIYEGKIHGKNIALLQSGIGKVAAAMGTTALLQLAKPNLVINTGSAGGVAEGLHVGDVIVSTETQYHDADVTAFGYAKGQLPACPVTFVSDARLVELAERTAKQLGQRVKRGLICSGDSFIQGGERLAQIKQDFPNVIAVEMEATAIAQVCHAFNVPFVVVRAISDAGDGKANMSFEEFLPLAAKQSSDMVVAMLAELN","1184578","[FUNCTION] Responsible for cleavage of the glycosidic bond in both 5'-methylthioadenosine (mta) and s-adenosylhomocysteine (sah) (by similarity). [CATALYTIC ACTIVITY] S-adenosyl-L-homocysteine + H(2)O = adenine + S-D-ribosyl-L-homocysteine. [CATALYTIC ACTIVITY] Methylthioadenosine + H(2)O = adenine + 5-methylthio-D-ribose.","MTA/SAH nucleosidase [Includes: 5'-methylthioadenosine nucleosidase; S-adenosylhomocysteine nucleosidase]","Cytoplasm, Periplasm","","
InterPro
IPR000845
Family
Nucleoside phosphorylase
PF01048\"[2-226]TPNP_UDP_1
InterPro
IPR010049
Family
MTA/SAH nucleosidase
TIGR01704\"[2-229]TMTA/SAH-Nsdase: MTA/SAH nucleosidase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1580\"[1-229]Tno description
PTHR21234\"[1-229]TPURINE NUCLEOSIDE PHOSPHORYLASE
PTHR21234:SF6\"[1-229]TMTA/SAH NUCLEOSIDASE


","BeTs to 13 clades of COG0775COG name: Nucleoside phosphorylaseFunctional Class: FThe phylogenetic pattern of COG0775 is --------vdrlb-efgh-nuj-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2e-12) to 3/4 blocks of the IPB000845 family, which is described as \"Purine and other phosphorylases, family 1\". Interpro entry for IP:IPR000845. IPB000845B 29-63 0.052 IPB000845C 142-152 41 IPB000845D 167-203 1.3e-07","Residues 147 to 226 match (4e-10) PD:PD290266 which is described as NUCLEOSIDASE STORAGE PROTEOME COMPLETE MTA/SAH HYDROLASE 5'-METHYLTHIOADENOSINE MULTIFUNCTIONAL S-ADENOSYLHOMOCYSTEINE FAMILY ","","","","","","","","","","","Mon Feb 17 15:35:37 2003","Mon Feb 17 15:35:37 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01750 is paralogously related to AA00488 (3e-07).","","","","","","Residues 2 to 226 (E-value = 1.8e-85) place AA01750 in the PNP_UDP_1 family which is described as Phosphorylase family (PF01048)","","","","","Cornell,K.A. and Riscoe,M.K. Cloning and expression of Escherichia coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase:identification of the pfs gene product. Biochim. Biophys. Acta 1396 (1): 8-14 (1998) PubMed: 9524204.Wurgler,S.M. and Richardson,C.C. Structure and regulation of the gene for dGTP triphosphohydrolase from Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 87 (7): 2740-2744 (1990) PubMed: 2157212.","","Mon Feb 17 15:35:37 2003","1","","","" "AA01751","1184760","1185452","693","ATGAAATTCGAAAAAACAACCGCTATTTTGACCGCACTTTTCGCGGCATCCGTTGCTAACGCTCACAACGTATGGCTGGAACCCGTCAAGGAGGCGAATTCTACCGGGCAATATGTAGTGAAATTCGGGCATGAACAAACGGAAATTTATCCGGAACACAAGCTAAAAACCGTTAAATTGCTGGATAACAACGGCAACCTCACTAACGCAACCCATCAATTTAAACAAGGCGAAGCCTATCTCAATGCTGAAAATGCGTCACAAGTTTTTATCCGTTTTGATAACGGCGTCTGGTCAAAGCTGCCAAGCGGCAAATATGTAGAAAAAAGCAAACAACAAGAGCCCACTGCGGAATTTGCCGTGAACCCGGTGAAGTTCGGCAAAGCGTTGTTGCGTTGGGACGCGCAGGCGTTGAAAGCCCATGGCATGGAATATGAACTGGTGCCGCAAGAGAAAGCGCAAGCGGGTAAACCGCTACCGATTTTGGTGTTACACAACGGCAAGCCGGTGAAAGATATTAAAGTGGGATTGGGTGAAGACGCGCCGTTCAATCTGACTAATGAAAAAGGCATAGCCGAATTTACACCGCAAAAAGGCAACAACAAAGTTTGGGCAGAATTTTCGGAAAACGTGAAAGGCAACCCCGATTACGATCGCCGTTCGGTGGAATATATGCTGACCTTTGAGGCGGAG","","","28658","MKFEKTTAILTALFAASVANAHNVWLEPVKEANSTGQYVVKFGHEQTEIYPEHKLKTVKLLDNNGNLTNATHQFKQGEAYLNAENASQVFIRFDNGVWSKLPSGKYVEKSKQQEPTAEFAVNPVKFGKALLRWDAQALKAHGMEYELVPQEKAQAGKPLPILVLHNGKPVKDIKVGLGEDAPFNLTNEKGIAEFTPQKGNNKVWAEFSENVKGNPDYDRRSVEYMLTFEAE","1185451","","conserved hypothetical protein","Periplasm","","
noIPR
unintegrated
unintegrated
PD115091\"[1-231]TYG24_HAEIN_P44276;
signalp\"[1-21]?signal-peptide


","No hits to the COGs database.","","Residues 1 to 231 match (1e-83) PD:PD115091 which is described as SIGNAL PRECURSOR COMPLETE CBIK PERIPLASMIC BINDING HI1624 PROTEOME ","","","","","","","","","","","","Tue Jan 7 16:10:58 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01751 is paralogously related to AA02126 (1e-07).","","","","","","","","","","","","","","1","","","" "AA01753","1185462","1185962","501","ATGAAAAAAACGCCGTATTTTTTGACCGCACTTTTGGGCTTATGTGTTGCACCTCACGCTTGGACGCACGCCCTTTATGTATTTGCCCAGTATGACGGGCAAACCGTGACGGGAAAATCCTATTATTCCGACATGACCCCCGCCGTCGAAACCTATGTGGAGGTGTTACGCCAAGGGGAAAATCAGCCGTTGCTGACGGGCAAAACCGACAATGGCGGTTATTTTCACCTGCCGTTAAAAGCGGATCCGAATATGGCGTTGAAAGTGGTGGTGGAAGGTGAGGAAGGGCATCGGGCGACGGTCGTGGCGGATAGAATTACGGCGAATGCCGGCGCAACAACTCGGGCGGGCGATGAAAGTCTGCTGTTGTTACGCGGTGATATTGCGCAGTTGCGCGATAAAATTTATCTGCACGATATTTTAGGCGGAATCGGTTACATTGTGGGAATTGCGGGCATTGCCGCTTGGCTGAAGGCCCGTAAGTTAAGAAAGGGACATCAA","","","18194","MKKTPYFLTALLGLCVAPHAWTHALYVFAQYDGQTVTGKSYYSDMTPAVETYVEVLRQGENQPLLTGKTDNGGYFHLPLKADPNMALKVVVEGEEGHRATVVADRITANAGATTRAGDESLLLLRGDIAQLRDKIYLHDILGGIGYIVGIAGIAAWLKARKLRKGHQ","1185961","","conserved hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide
tmhmm\"[10-30]?\"[135-157]?transmembrane_regions


","No hits to the COGs database.","","Residues 7 to 164 match (3e-39) PD:PD095015 which is described as SIGNAL PRECURSOR PROTEOME TRANSMEMBRANE COMPLETE CBIL MEMBRANE HI1622 CYTOPLASMIC ","","","","","","","","","","","","Tue Jan 7 16:14:26 2003","","","","Thu Mar 11 15:03:46 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01753 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Mar 11 15:03:46 2004","","","","","","","","","","","","","1","","","" "AA01755","1185965","1186615","651","ATGCATTTATCGGAAGGCGTGTTGCATACACCGGTGTTGTTAGCCGGAGTGGCTTTGGCAGTGGTCGGTGTAGCGGTAGGGTTGCGTCGCCTGGATAACGAACGTTTGCCGTTAACGGCACTGTTTGCCGCCGCTTTTTTTGTTGCCGGCACCATCCATGTGCCGGTTGGCATCGGTAGCGTACACTTGATTTTAAACGGCATAGCGGGATTATTTCTTGGTTGGGCGGTGTTTCCCGCCTTTTTTATCGCCTTGTTGTTACAGGTGTTGTTTTTTTCCTTCGGTGGGTTTGCCGTGTTAGGCGTGAATTTGTGCGTGATAGCGTTGCCGGCGGTGGCGGCGCATTATTTATTACGCGGTTATTTGCATCCTGACATGGGAAAAATGGCGAAATTGTTCGCCGGTGTGGGTGTCGGCGTGATTGGTGTAGGTGGCGCGGGCGCGTTGGCGTCTTTGGTTTTAGCCTTGGACGGCGGTAAACATTATCAGGATTTAATCGCCCTGTTGTTGCTGTCCCATTTGCCGGTATTTGTGCTGGACGGCATTATCAGCTACGGCGTGATTTCTTTGCTCGGCAAAATGTATCCCGTCGCACTGCAACCTGTCGCCACCTCACAAAAAGCCGTCGGTTACAGCAAACGGTGTGCGCAA","","","22431","MHLSEGVLHTPVLLAGVALAVVGVAVGLRRLDNERLPLTALFAAAFFVAGTIHVPVGIGSVHLILNGIAGLFLGWAVFPAFFIALLLQVLFFSFGGFAVLGVNLCVIALPAVAAHYLLRGYLHPDMGKMAKLFAGVGVGVIGVGGAGALASLVLALDGGKHYQDLIALLLLSHLPVFVLDGIISYGVISLLGKMYPVALQPVATSQKAVGYSKRCAQ","1186614","","cobalt membrane transport protein","Inner membrane, Cytoplasm","","
InterPro
IPR002751
Family
Cobalamin (vitamin B12) biosynthesis CbiM
PD005331\"[1-107]TYG21_HAEIN_P44274;
PF01891\"[23-197]TCbiM
noIPR
unintegrated
unintegrated
signalp\"[1-27]?signal-peptide
tmhmm\"[10-28]?\"[38-58]?\"[72-92]?\"[97-117]?\"[136-156]?\"[166-188]?transmembrane_regions


","BeTs to 6 clades of COG0310COG name: Cobalamin biosynthesis protein CbiMFunctional Class: HThe phylogenetic pattern of COG0310 is aom----------c---h--------Number of proteins in this genome belonging to this COG is","Significant hit ( 2.7e-36) to 3/3 blocks of the IPB002751 family, which is described as \"Cobalamin synthesis CBIM\". Interpro entry for IP:IPR002751. IPB002751A 1-10 0.008 IPB002751B 37-68 8.5e-17 IPB002751C 83-112 1.2e-13","Residues 89 to 196 match (1e-12) PD:PD486860 which is described as COBALT PROTEOME TRANSMEMBRANE COMPLETE CBIM MEMBRANE HI1621 ","","","","","","","","","","","","Tue Jan 7 16:20:51 2003","","","Tue Mar 16 14:01:26 2004","Tue Mar 16 14:01:26 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01755 is paralogously related to AA02668 (0.001).","Tue Mar 16 14:01:26 2004","","","","","Residues 23 to 197 (E-value = 1.1e-45) place AA01755 in the CbiM family which is described as CbiM (PF01891)","Tue Mar 16 14:01:26 2004","","","","","","","1","","","" "AA01756","1186615","1187277","663","ATGAGTTCTGTTTTTCGTCTTTTTTTTGCACCGCACTTTTTCGCGCCTCATCTACGCCTGATCTATTTGTTTCTTTGGGGCTTAGTCATCAGTGCGTTGCACCAATCGTCTTTGCTATTCTGCTTGAACGGTGCGGCGTTGGTGTTGTTGGCGGCATTCATTTACGGCAATGCAGAACCTTATTCCCCCTATATAAAACGTTGGCTGTGGTTAAATGGATTCACGTTTTTGCTTTGGCTAACATTGAGCTGGCGGATCGGTGCCGAGGGCATGGAGCTTAATCCCGAAGGCATGGAAACGGCGCTGCTCATCACGTTACGTATGAATCTGTTGTTGTTTTCCTTGTGGTTGTTCTTGTGGAAAATGAACGACGCGGTGCTGGTGCAGGCAATAGGTAAATTGCCGTTACCGCCTAAGCTCATTTGGCTTTTTGTGTTGACTGTGCGTTACATTGCATTATTGGGCGAGTTGCGGCAGAAAATGGATCTGGCAATGCGCGCGCGCGGGTATCGCGCGGGACTGAATCGCCGCACGTTATATATCACTGCGCAACGGGTGGCGTTATTGCTTGTTCATGCCTTGTTAAAAGCGGAAACGGCGCAGATTGCGTTGAAATGTCGCAGCTTTCGATTCGGCAATCAACAAACGCTAGGCGGGGAAAAA","","","25632","MSSVFRLFFAPHFFAPHLRLIYLFLWGLVISALHQSSLLFCLNGAALVLLAAFIYGNAEPYSPYIKRWLWLNGFTFLLWLTLSWRIGAEGMELNPEGMETALLITLRMNLLLFSLWLFLWKMNDAVLVQAIGKLPLPPKLIWLFVLTVRYIALLGELRQKMDLAMRARGYRAGLNRRTLYITAQRVALLLVHALLKAETAQIALKCRSFRFGNQQTLGGEK","1187276","From Accession number: PF02361Cobalt transport proteinThis family consists of various cobalt transport proteins Most of which are found in Cobalamin (Vitamin B12) biosynthesis operons. In Salmonella the cbiN cbiQ (product CbiQ in this family) and cbiO are likely to form an active cobalt transport system. Description Cobalt transport proteins are most often found in cobalamin (vitamin B12) biosynthesis operons. Salmonella typhimurium synthesizes cobalamin (vitamin B12) de novo under anaerobic conditions. Not all Salmonella and Pseudomonas cobalamin synthetic genes have apparent homologs in the other species suggesting that the cobalamin biosynthetic pathways differ between the two organisms.","cobalt membrane transport protein","Inner membrane, Cytoplasm","","
InterPro
IPR003339
Family
Cobalt transport protein
PF02361\"[12-217]TCbiQ
noIPR
unintegrated
unintegrated
signalp\"[1-83]?signal-peptide
tmhmm\"[10-30]?\"[36-58]?\"[68-86]?\"[100-120]?\"[135-153]?transmembrane_regions


","BeTs to 4 clades of COG0619COG name: ABC-type cobalt transport system, permease component CbiQ and related transportersFunctional Class: PThe phylogenetic pattern of COG0619 is aom-kz--vdrlbce--h-------wNumber of proteins in this genome belonging to this COG is","","Residues 145 to 209 match (1e-10) PD:PD266966 which is described as COBALT CBIQ PROTEOME COMPLETE MEMBRANE ","","","","","","","","","","","Thu Mar 11 15:52:03 2004","Tue Jan 7 16:27:13 2003","","","","Thu Mar 11 15:52:03 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01756 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Mar 11 15:52:03 2004","","","","","Residues 12 to 217 (E-value = 5.3e-05) place AA01756 in the CbiQ family which is described as Cobalt transport protein (PF02361)","Thu Mar 11 15:52:03 2004","","","","","","","1","","","" "AA01757","1187277","1187897","621","ATGACGGTTTTACAAGTCAAAGGATTGCAAATTAAGCGGGGAGAACGGCGGATTATTGATAATCTGTCCTTTCAACTTGACGCGGGGCAACGTTTTTTTATCCGGGGCGAAATCGGCACAGGAAAAACCACCTTATTACTGGCGTTGCTCGGTTTTGTTCCTATTGCGGGGGGAGAAATTCGCCTGTTCGGGCAGCTTTGTCGGGAAGAACGGGATTTTGCTCCTTTTCGTGGCAGTGTGGGTTTTTGTTTTCAGCACGCCGACGATCAACTGTTCGGTCCGACGGTGTTGGACGATGTGGCGTTCGGTCCGTTAAATCAAGGCTTGCCGCGTCAACAGGCGTATGCCATCGCTTTGCAACAGTTGGAACGGCTGGGAATTGCCCATTTGCAAGACCGCACGGTGCATACCCTGTCCGGCGGCGAAAAAAATTTTACCGCACTGGCGGGCGTGTTGGCGATGCAGCCGAAAATGTTACTGTTAGATGAGCCGACTAACGGCTTGGATAGCAAAAATACCGAAAAACTGACCGCACTTTTGCGCGAATTGTCGTTGCCCATGTTGGTGGCGTCCCATCACCACGGCTTTACTGCACAATTGGCGGACGAAGTTTTGACTTTA","","","31020","MTVLQVKGLQIKRGERRIIDNLSFQLDAGQRFFIRGEIGTGKTTLLLALLGFVPIAGGEIRLFGQLCREERDFAPFRGSVGFCFQHADDQLFGPTVLDDVAFGPLNQGLPRQQAYAIALQQLERLGIAHLQDRTVHTLSGGEKNFTALAGVLAMQPKMLLLDEPTNGLDSKNTEKLTALLRELSLPMLVASHHHGFTAQLADEVLTL","1187896","","cobalt transport ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[138-180]TQ6AQ88_BBBBB_Q6AQ88;
PF00005\"[29-207]TABC_tran
PS50893\"[4-207]TABC_TRANSPORTER_2
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[28-207]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[3-207]Tno description
PTHR19222\"[4-207]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF22\"[4-207]TCOBALT ABC TRANSPORTER


","No hits to the COGs database.","Significant hit ( 2.3e-20) to 2/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 18-64 2.9e-11 IPB001140B 135-173 1.4e-07","Residues 119 to 207 match (4e-07) PD:PD387048 which is described as ATP-BINDING 250AA PROTEOME COMPLETE III DICITRATE IRON LONG ","","","","","","","","","","","","Tue Jan 7 16:30:04 2003","","","Thu Mar 11 14:44:28 2004","Thu Mar 11 14:44:28 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01757 is paralogously related to AA01051 (1e-18), AA01422 (4e-18), AA01684 (5e-18), AA02324 (3e-17), AA02152 (3e-17), AA01616 (1e-16), AA00700 (5e-16), AA02440 (1e-15), AA01656 (3e-15), AA02550 (4e-15), AA02080 (4e-15), AA00858 (4e-15), AA02718 (6e-15), AA01645 (1e-14), AA02320 (3e-14), AA00415 (3e-14), AA02899 (4e-14), AA00207 (5e-14), AA02573 (3e-13), AA01824 (3e-13), AA02146 (7e-13), AA01867 (9e-13), AA01961 (1e-12), AA01524 (1e-12), AA02140 (2e-12), AA01779 (1e-11), AA02898 (2e-11), AA02484 (3e-11), AA01820 (5e-11), AA02786 (4e-10), AA01555 (4e-10), AA02606 (5e-10), AA02331 (9e-10), AA01510 (1e-09), AA02609 (2e-09), AA01456 (2e-09), AA00061 (6e-09), AA02353 (1e-08), AA00933 (2e-08), AA00799 (2e-08), AA01568 (3e-08), AA01393 (7e-08), AA02805 (9e-08), AA00591 (4e-07), AA02225 (9e-07), AA00751 (2e-06), AA01947 (5e-06), AA01569 (4e-05), AA00934 (3e-04), AA01291 (4e-04), AA01509 (6e-04) and A02145 (7e-04).","Thu Mar 11 14:44:28 2004","","","","","Residues 29 to 207 (E-value = 3.4e-37) place AA01757 in the ABC_tran family which is described as ABC transporter (PF00005)","Thu Mar 11 14:44:28 2004","","","","","","","1","","","" "AA01758","1187979","1188785","807","ATGTGTACGACTTGTGGTTGCGGGTATCCCGAACAAGTAAGAATCGGCGAAGTGGCACATTCTCATCATGACAGCCACGACGGCACGCAAAGTGCAGTCAAAAATCCGGACTTTTCTCATTTCAAATTTCACTCGGCGCAGCAGCCGTCCGACACATCCGAGACGCAAAAACGCTTGTTGAAAGTGGAGCAGGACGTATTAGGTAAAAATAATCAAATTGCGGCGCACAACCGTTTTCTTTTCCAACAACAGCACATTCTTGCATTGAATTTGGTGTCTAGCCCGGGTTCCGGCAAAACCACCTTGCTTACTACCACGCTAAACGCGCTGAAAAATGACCGCACTTGTTATGTGATTGAAGGCGATCAACAAACGGAAAACGACGCCGATCGCATTCGCGCCACCGGTGTATCTGCGATTCAGGTGAACACCGGTAAAGGTTGCCATTTGGATGCGCAGATGATCAACGACGCCTTGTTCAAACTGGAACCGAAACAACACAGCCTCTTATTCATTGAAAATGTCGGCAATTTGGTTTGCCCGTCGGAATTTGATTTGGGCGAAAAAGCCAAAGTGGTGATTTTGTCCGTCACCGAGGGCGAAGACAAACCGCTGAAATACCCACATATGTTTGCTGCCTCCAAACTCATGATTTTAAACAAAATCGACTTGCTGCCTTACCTTAATTTCGACGTGGAAAAATGTATCGCCTACGCCAAACAGGTGAACCCGCAAATTGAGGTGATTCAACTTTCCGCTACCACGGGCGAAGGCTTAAAAGACTGGTTAAATTGGTTACAAAACGCC","","","31742","MCTTCGCGYPEQVRIGEVAHSHHDSHDGTQSAVKNPDFSHFKFHSAQQPSDTSETQKRLLKVEQDVLGKNNQIAAHNRFLFQQQHILALNLVSSPGSGKTTLLTTTLNALKNDRTCYVIEGDQQTENDADRIRATGVSAIQVNTGKGCHLDAQMINDALFKLEPKQHSLLFIENVGNLVCPSEFDLGEKAKVVILSVTEGEDKPLKYPHMFAASKLMILNKIDLLPYLNFDVEKCIAYAKQVNPQIEVIQLSATTGEGLKDWLNWLQNA","1188784","[FUNCTION] Is required for the formation of all three hydrogenase isoenzymes. Affects some aspect of the processing of hydrogenases 1 and 2, perhaps nickel incorporation into the apo-enzymes, since hypb gene lesions can be complemented by high nickel ion concentration in the medium. [SIMILARITY] Belongs to the hypB/hupM family. ","hydrogenase isoenzymes nickel incorporation protein","Cytoplasm","","
InterPro
IPR003495
Domain
Cobalamin (vitamin B12) biosynthesis CobW-like
PF02492\"[87-250]TcobW
InterPro
IPR004392
Family
Hydrogenase accessory protein HypB
TIGR00073\"[55-266]ThypB: hydrogenase accessory protein HypB
InterPro
IPR012202
Family
[NiFe]-hydrogenase/urease maturation factor, Ni(2+)-binding GTPase
PIRSF005624\"[1-268]TNi(2+)-binding GTPase ([NiFe]-hydrogenase/urease maturation factor)


","BeTs to 14 clades of COG0378COG name: Ni2+-binding GTPase involved in regulation of expression and maturation of urease and hydrogenaseFunctional Class: O,KThe phylogenetic pattern of COG0378 is a-m----q-dr-bcef-h--uj---wNumber of proteins in this genome belonging to this COG is","Significant hit ( 8.8e-52) to 4/4 blocks of the IPB002894 family, which is described as \"HypB/UreG nucleotide-binding domain\". Interpro entry for IP:IPR002894. IPB002894A 89-100 5.2e-05 IPB002894B 117-129 0.00047 IPB002894C 138-158 7.5e-10 IPB002894D 192-232 1.9e-28","Residues 55 to 133 match (4e-16) PD:PD006124 which is described as NICKEL HYPB HYDROGENASE PROTEOME COMPLETE METAL-BINDING INCORPORATION EXPRESSION/FORMATION ISOENZYMES PROTEIN ","","","","","","","","","","","Tue Jan 7 16:37:27 2003","Tue Jan 7 16:37:27 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01758 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 76 to 203 (E-value = 8.5e-72) place AA01758 in the HypB_UreG family which is described as HypB/UreG nucleotide-binding domain (PF01495)","","","","","Lutz,S., Jacobi,A., Schlensog,V., Bohm,R., Sawers,G. and Bock,A. Molecular characterization of an operon (hyp) necessary for the activity of the three hydrogenase isoenzymes in Escherichia coli. Mol. Microbiol. 5 (1): 123-135 (1991) [PubMed: 1849603].Chen,J.C. and Mortenson,L.E. Identification of six open reading frames from a region of the Azotobacter vinelandii genome likely involved in dihydrogenmetabolism. Biochim. Biophys. Acta 1131 (2): 199-202 (1992) [PubMed: 1610901].","","Tue Jan 7 16:37:27 2003","1","","","" "AA01759","1188815","1189924","1110","ATGCAATTCATTGATGAATTTCGTGATCCCAAACTGGCGAAAAGTTTGGTGGAGCGTTTGCAAAAACTCATGGAAAAACTACCGCACTTTACGCCGGAAAATCCGTTGTATCTTATGGAAGTCTGCGGCGGTCATACCCATACGATTTTTAAATTCGGCTTGGATCGCCTGTTGCCGAAAAGCATTGAGTTTATTCACGGTCCGGGCTGTCCGGTGTGTGTGTTGCCCATGGGGCGCATTGATGTGTGTATTGAAATCGCGCAAAAGCCCAATGTGATTTTCTGCACCTTCGGTGACGCCATGCGGGTGAAAGGACGGTGCGGTTCCTTGCTGGAGGCAAAAGCCAAAGGCGCCGATGTGCGAATCGTTTATTCGCCGTTGGACGCGCTGAATATCGCCGTGAACAATCCCGAAAAAAACGTGGTTTTCTTTTCCCTCGGTTTTGAAACTACTATGCCGAGCGCGGCGGTGACCCTTCAACAGGCGAACAAGCTGAATCTGCAAAATTTCTGGGTGGTATGTCAAAACATCACCATTATCCCCACTTTACACAGCCTGCTTTCGCAAGATTATGTGAAAATTGACGGCTTCATTGCGCCCGGCCATGTGAGCATGGTGATTGGCGCCTCGCCTTATCAATCCATTGTGGATAAATACCATAAGCCTTTTGTGGTTACGGGCTTTGAGCCGTTGGATATTCTGCAAGCCATCGTGATGTTGGTGCAACAATTCGTGGACGGGCGTTGTGAAATCGAAAACCAATATAAACGCATCGTGCATTCCCAAGGCAACCTGCTGGCGCAACAAGCCATGCGTGAAGTGTTCCAATTGAAGAAATCCAGCGAATGGCGCGGTTTGGGCGAAATCGAAGAGTCAGGCGTGGAACTCACCGACGCGTACAAACGTTTTGACGCGGAAATCTATTTCCACAGCCACCCGCAACAAGTGGCGGACGACCCCAATTCCCGCTGCGGCGATGTGCTCACCGGCAAATGTAAACCTTGCGATTGCCCGTTATTCGGCAGCCAATGCAACCCGGATGATGCCTACGGCGCCTTAATGGTGTCTTCAGAAGGGGCGTGCGCCGCCTATTATCAATACCGGAGAGAA","","","43078","MQFIDEFRDPKLAKSLVERLQKLMEKLPHFTPENPLYLMEVCGGHTHTIFKFGLDRLLPKSIEFIHGPGCPVCVLPMGRIDVCIEIAQKPNVIFCTFGDAMRVKGRCGSLLEAKAKGADVRIVYSPLDALNIAVNNPEKNVVFFSLGFETTMPSAAVTLQQANKLNLQNFWVVCQNITIIPTLHSLLSQDYVKIDGFIAPGHVSMVIGASPYQSIVDKYHKPFVVTGFEPLDILQAIVMLVQQFVDGRCEIENQYKRIVHSQGNLLAQQAMREVFQLKKSSEWRGLGEIEESGVELTDAYKRFDAEIYFHSHPQQVADDPNSRCGDVLTGKCKPCDCPLFGSQCNPDDAYGALMVSSEGACAAYYQYRRE","1189923","[FUNCTION] Required for the formation of all three hydrogenase isoenzymes. [SIMILARITY] Belongs to the hypD family. ","hydrogenase isoenzymes formation protein","Cytoplasm","","
InterPro
IPR002780
Family
Hydrogenase formation HypD protein
PIRSF005622\"[1-370]T[NiFe]-hydrogenase maturation factor, HypD type
PF01924\"[9-370]THypD
TIGR00075\"[1-369]ThypD: hydrogenase expression/formation prot


","BeTs to 9 clades of COG0409COG name: Hydrogenase maturation factorFunctional Class: OThe phylogenetic pattern of COG0409 is a-m-k--q-----ce-----u-----Number of proteins in this genome belonging to this COG is","Significant hit (1.1e-166) to 7/7 blocks of the IPB002780 family, which is described as \"Hydrogenase formation hypA\". Interpro entry for IP:IPR002780. IPB002780A 39-72 1.3e-28 IPB002780B 75-106 1.5e-16 IPB002780C 109-143 8.1e-22 IPB002780D 149-190 8.3e-12 IPB002780E 194-242 6.5e-34 IPB002780F 243-276 4e-16 IPB002780G 322-369 9.2e-31","Residues 334 to 367 match (5e-09) PD:PD538491 which is described as HYDROGENASE HYPD COMPLETE PROTEOME EXPRESSION/FORMATION FORMATION ISOENZYMES METAL-BINDING ISOENZYME ON ","","","","","","","","","","","Tue Jan 7 16:41:51 2003","Fri Jan 31 15:51:33 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01759 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 9 to 370 (E-value = 6e-214) place AA01759 in the HypD family which is described as Hydrogenase formation hypA family (PF01924)","","","","","Lutz,S., Jacobi,A., Schlensog,V., Bohm,R., Sawers,G. and Bock,A.Molecular characterization of an operon (hyp) necessary for the activity of the three hydrogenase isoenzymes in Escherichia coli. Mol. Microbiol. 5 (1): 123-135 (1991) PubMed: 1849603.Colbeau,A., Richaud,P., Toussaint,B., Caballero,F.J., Elster,C., Delphin,C., Smith,R.L., Chabert,J. and Vignais,P.M. Organization of the genes necessary for hydrogenase expression in Rhodobacter capsulatus. Sequence analysis and identification of twohyp regulatory mutants. Mol. Microbiol. 8 (1): 15-29 (1993) PubMed: 8497190.","","Fri Jan 31 15:51:33 2003","1","","","" "AA01760","1189927","1190475","549","ATGACAGATTTTATTACCATGGCGCACGGCAACGGCGGCGCGGCAATGCAAAAATTAATTCAGTATTATTTCGTCGAAGCCTTTGACAACCCGATTCTCGCCCAAGGAGAAGATCAAGCCCGTTTGCCGTTGGCGGAATTGATGGCGCAGGGCGAACAGCTTTCTTTCAGCACCGACAGTTTCGTCATTGACCCGATTTTCTTCCCTGGTGGCAACATCGGCAAGCTCGCCGTATGCGGCACGTTAAATGATGTGGCGGTATGCGGCGCTATTCCCAAATACCTTTCCTGCGGCTTTATTTTGGAAGAAGGTTTACCATTAACCGAATTAAAAGAAATCATTCAAGCTATGGCGCAAGCCTGCAAAGCTGCCGGCGTGCAGGTGGTGACGGGCGATACCAAAGTAGTGCAAAAAGGCGCGGTAGATAAAATCTTCATCAACACCAGCGGCATCGGCGTGATCCCGCGTGGTATCGATTGGGGAATGCACCGTATTACAGCAGGCGATAACATCATTGTCAGCGGCACCATCGGTGTAACCAACCACATA","","","20677","MTDFITMAHGNGGAAMQKLIQYYFVEAFDNPILAQGEDQARLPLAELMAQGEQLSFSTDSFVIDPIFFPGGNIGKLAVCGTLNDVAVCGAIPKYLSCGFILEEGLPLTELKEIIQAMAQACKAAGVQVVTGDTKVVQKGAVDKIFINTSGIGVIPRGIDWGMHRITAGDNIIVSGTIGVTNHI","1190474","[FUNCTION] May be involved in the maturation of the nifE hydrogenase.[SIMILARITY] Belongs to the hypE family. ","hydrogenase isoenzymes formation protein","Cytoplasm","","
InterPro
IPR000728
Domain
AIR synthase related protein
PF00586\"[1-155]TAIRS
noIPR
unintegrated
unintegrated
G3DSA:3.30.1330.10\"[9-158]Tno description


","BeTs to 11 clades of COG0309COG name: Hydrogenase maturation factorFunctional Class: OThe phylogenetic pattern of COG0309 is aompkz-q-----ce-----u-----Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","Tue Jan 7 16:47:07 2003","Tue Jan 7 16:47:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01760 is paralogously related to AA01628 (6e-05).","","","","","","Residues 1 to 155 (E-value = 4.6e-41) place AA01760 in the AIRS family which is described as AIR synthase related protein, N-terminal domain (PF00586)","","","","","Colbeau,A., Richaud,P., Toussaint,B., Caballero,F.J., Elster,C., Delphin,C., Smith,R.L., Chabert,J. and Vignais,P.M. Organization of the genes necessary for hydrogenase expression in Rhodobacter capsulatus. Sequence analysis and identification of twohyp regulatory mutants. Mol. Microbiol. 8 (1): 15-29 (1993) [PubMed: 8497190].Lutz,S., Jacobi,A., Schlensog,V., Bohm,R., Sawers,G. and Bock,A. Molecular characterization of an operon (hyp) necessary for the activity of the three hydrogenase isoenzymes in Escherichia coli. Mol. Microbiol. 5 (1): 123-135 (1991) [PubMed: 1849603].Du,L., Stejskal,F. and Tibelius,K.H. Characterization of two genes (hupD and hupE) required for hydrogenase activity in Azotobacter chroococcum. FEMS Microbiol. Lett. 75 (1): 93-101 (1992) [PubMed: 1526470].","","Tue Jan 7 16:47:07 2003","1","","","" "AA01762","1190651","1190526","126","GTGGTTAAATTGCACATTTTTAAATTTAGCCGCTTTTTTTCTAATTTTGATTTTTCCTTTTATCCTCTAAATAAAAAAGGGCTGAAATTTCTTTCAACCCTTGATTTTCTTTACTTTTCGACAATT","","","5086","VVKLHIFKFSRFFSNFDFSFYPLNKKGLKFLSTLDFLYFSTI","1190526","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 11:06:16 2004","Thu Feb 26 11:06:16 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01762 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 11:06:16 2004","","","","","","","","","","","","","1","","","" "AA01763","1190878","1190783","96","GTGCAAAATGGCGCCAGCGTATGGGTTAAACGCGTTAAAATCAACTGGGATGGCTTAGAGCTCATTTCAGACAATAAAGAAGCCCACCGATCCATT","","","3645","VQNGASVWVKRVKINWDGLELISDNKEAHRSI","1190783","","conserved hypothetical protein (possible transcriptional regulatory protein)","Periplasm, Cytoplasm","This sequence is similar to gi16273380, a predicted transcriptional regulatory protein from Haemophilus influenzae Rd KW20. Also see gi33151354.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 11:03:05 2004","Thu Feb 26 11:03:05 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA01319.AA01763 is paralogously related to AA01319 (2e-09).","Thu Feb 26 11:02:36 2004","","","","","","","","","","","","","1","","","" "AA01764","1191758","1191666","93","TTGGGTAATATTTATTTCTTTAAACCAAGCCTTAACTTCCTCTCGTGTTTTTTTCTGCATAAAACCACCTTTTTATGGACTAAAAACAGTTTA","","","3710","LGNIYFFKPSLNFLSCFFLHKTTFLWTKNSL","1191666","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-16]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 10:58:56 2004","Thu Feb 26 10:58:56 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01764 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 10:58:56 2004","","","","","","","","","","","","","1","","","" "AA01765","1191896","1192696","801","ATGTGTGAACTAGAGTCACATTACAGCGCTCAGTCTCTTGTTGAGCTTGGTCTAATAAGTTTACCGAAAACAAAAAAATCCATTTTAACAAAGGCTAAACGCGAAAATTGGAAATGCCGAGTTAGACAAGGTAAAGGCGGTGGTTATGAATATGCCGTTAAATCCATGCCGGAAGACGTACAAGCCGAAATCGTTTTAAAACTTGGTAAACGTGCGGTTAAAAATTTGCCTGTTTCGGTTGATGCCGATATGTCGGCAGATGCGCAAATCTTGTGGGCTGGCTACGAACAAAGCACCGAGAAACAACAAACAAAAGCGCAAATGAAGCTGGGCTTGATGTTGGCAGTGGCTGAATTGGTGAGTGCCGACGTAAAAGTGATGGACGCCTTGGAATTGGTTGCCATGAAACACAACCAAAACAACGCAAAAACCGTCTCGGTTAGCGCCCTGAAAAATTGGTGGTATGCGGTAAAAGACGCGGAACGCAGTTTGTGGTTGCCTTTATTGGTGGGCTATCAAACCGCAAGCGGTGAACACAGAGAAGCTGAATTCACGGCGGAAGCCTGGGCGTTTTTTAAAGCCGATTATTTTCGCAATGAGCGCCCGCAATTCGGCAGTTGTTATGAAAGATTGAAACGCGCGGCAGGTGCAAACGGATGGGTTATCCCAAGCGCGTCCAGCATTAAACGCAAGATTGAACGAGAAGTGCCGAAAACCCATCAGGTTTACTTAAGAAAACCCGCACATTGTACAAGCCCGCTGGGCGTTGTATGTGGTGGCCAATGTGTTGGATGGTCAGCG","","","30316","MCELESHYSAQSLVELGLISLPKTKKSILTKAKRENWKCRVRQGKGGGYEYAVKSMPEDVQAEIVLKLGKRAVKNLPVSVDADMSADAQILWAGYEQSTEKQQTKAQMKLGLMLAVAELVSADVKVMDALELVAMKHNQNNAKTVSVSALKNWWYAVKDAERSLWLPLLVGYQTASGEHREAEFTAEAWAFFKADYFRNERPQFGSCYERLKRAAGANGWVIPSASSIKRKIEREVPKTHQVYLRKPAHCTSPLGVVCGGQCVGWSA","1192695","[FUNCTION] This transposase is essential for integration, replication-transposition, and excision of MU DNA (by similarity).","Mu-like prophage FluMu transposase A","Periplasm, Cytoplasm","","
InterPro
IPR003314
Domain
Transposase MuA/Repressor CI, DNA-binding
PF02316\"[14-161]TMu_DNA_bind
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[4-72]Tno description
InterPro
IPR012287
Domain
Homeodomain-related
G3DSA:1.10.10.60\"[177-252]Tno description
InterPro
IPR015126
Domain
Mu DNA binding, I gamma subdomain
PF09039\"[164-253]TMu_I-gamma


","No hits to the COGs database.","Significant hit ( 2.4e-16) to 3/6 blocks of the IPB003314 family, which is described as \"Mu DNA-binding domain\". Interpro entry for IP:IPR003314. IPB003314A 20-44 9.4e-07 IPB003314B 46-59 0.00082 IPB003314C 145-159 0.033","Residues 4 to 67 match (8e-11) PD:PD145839 which is described as DNA A FLUMU PROTEOME ELEMENT RECOMBINATION INTEGRATION DNA-BINDING EXCISION COMPLETE ","","","","","","","","","","","Tue Jan 7 17:02:15 2003","Tue Jan 7 17:02:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01765 is paralogously related to AA02072 (8e-07) and AA02149 (1e-06).","","","","","","Residues 14 to 161 (E-value = 9.2e-05) place AA01765 in the Mu_DNA_bind family which is described as Mu DNA-binding domain (PF02316)","","","","","Harshey,R.M., Getzoff,E.D., Baldwin,D.L., Miller,J.L. and Chaconas,G. Primary structure of phage mu transposase: homology to mu repressor . Proc. Natl. Acad. Sci. U.S.A. 82 (22): 7676-7680 (1985) [PubMed: 2999776].Priess,H., Kamp,D., Kahmann,R., Brauer,B. and Delius,H. Nucleotide sequence of the immunity region of bacteriophage Mu . Mol. Gen. Genet. 186 (3): 315-321 (1982) [PubMed: 6214696].Toussaint,A., Faelen,M., Desmet,L. and Allet,B. The products of gene A of the related phages Mu and D108 differ in their specificities. Mol. Gen. Genet. 190 (1): 70-79 (1983) [PubMed: 6222246].Clubb,R.T., Omichinski,J.G., Savilahti,H., Mizuuchi,K., Gronenborn,A.M. and Clore,G.M. A novel class of winged helix-turn-helix protein: the DNA-binding domain of Mu transposase. Structure 2 (11): 1041-1048 (1994) [PubMed: 7881904].Schumacher,S., Clubb,R.T., Cai,M., Mizuuchi,K., Clore,G.M. and Gronenborn,A.M. Solution structure of the Mu end DNA-binding ibeta subdomain of phage Mu transposase: modular DNA recognition by two tethereddomains. EMBO J. 16 (24): 7532-7541 (1997) [PubMed: 9405381].","","Tue Jan 7 17:02:15 2003","1","","","" "AA01767","1192668","1193021","354","GTGGTGGCCAATGTGTTGGATGGTCAGCGTGAGGATGATGTCGGCATCTATCAATTGGTCGAGCGTTTACCCGAGCCTTATGTTGCCGTTAAAGGGCAGCCCTATTATTGGGAGATCGGGAGAGAGCATGTTTTTAACTGCTTCATCATCGGTGCCACCAAGGGGCACGGATACCAAACAAGAAATGACCCGTGCAGGTTTACGCACGACGGCAATTTCAATGAAACCGATTTGAAAGGCGTCGCATTTCATTTGGATGGCTCGATCATTGTAGAATCCGCAGTCCCGATGTTAGGTCCTTTCGGTCCGATTTCTTCATACGATAAACGGATAGCTTCCCCGTCGTCATTCAGG","","","13173","VVANVLDGQREDDVGIYQLVERLPEPYVAVKGQPYYWEIGREHVFNCFIIGATKGHGYQTRNDPCRFTHDGNFNETDLKGVAFHLDGSIIVESAVPMLGPFGPISSYDKRIASPSSFR","1193021","","conserved hypothetical protein","Cytoplasm","This sequence is similar to gi|33151389, a predicted conserved hypothetical protein from Haemophilus ducreyi 35000HP.","
noIPR
unintegrated
unintegrated
PD035107\"[1-23]TQ7VPF0_HAEDU_Q7VPF0;


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 10:56:17 2004","Thu Feb 26 10:56:17 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01767 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 10:56:17 2004","","","","","","","","","","","","","1","","","" "AA01769","1193088","1193192","105","GTGGCGATTATCCGAAAAACGCCGTGGCTTACGATTGTAGTAAAAATCATCCATCTGCTGCTCGGTTCATGTAATTTGTGTGCCGTACAGTATCTCGCCGCACCA","","","3814","VAIIRKTPWLTIVVKIIHLLLGSCNLCAVQYLAAP","1193192","","hypothetical protein","Cytoplasm, Periplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-24]?signal-peptide
tmhmm\"[9-29]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 10:52:53 2004","Thu Feb 26 10:52:53 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01769 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 10:52:53 2004","","","","","","","","","","","","","1","","","" "AA01770","1193457","1193251","207","ATGGTAAACACCCATCATTTTGATAGCACCAGCGTCCACGCTGGTGCTATCCTTTTGTCCAAGCGTGGACGCTTGAACTATCACAAAAACAAAAAATGTGCGGTCAAAATCTCAAACGTTTTCAACGCTAAAAAAACAATCCTAAAACTCACCGCACTTCACTCTGATAGCACCAGTATCCAAGCCCTCTTGCCGACGCATATTTCA","","","7590","MVNTHHFDSTSVHAGAILLSKRGRLNYHKNKKCAVKISNVFNAKKTILKLTALHSDSTSIQALLPTHIS","1193250","","hypothetical protein","Cytoplasm, Extracellular","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Tue Jan 7 17:03:53 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01770 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01772","1195002","1194190","813","ATGCTCAACAAAGACACCCAACTCTGTATGTCCCTGTCCGGTCGTCCCGGCAATTTCGGTACACAATTTCACAATTACCTTTATCAAAAACTTGGTTTGAATTTCATTTATAAAGCCTTTACCACCAACGACATCGAACACGCAGTGAAAGGCGTGCGGGCGTTAGGGATTCGCGGTTGTGCGGTGTCCATGCCGTTTAAAGAAAGCTGTATGCCGTTTTTAGATGAAATCCCCCCTTCCGCACAAGCCATCAAATCGGTAAATACCATCGTCAACGACAACGGATTTTTACGTGCCTATAACACCGATTACATCGCCATCGTGAAACTTATCGAAAGATATCAACTGGATAAAAACGATTCCGTGATCGTGCACGGCAGTGGCGGCATGGCAAAAGCGGTGGTTGCCGCCTTTAAAAATTCCGGTTTTGAGAATGTCAAAATCTTTGCCCGTAACGAAAAAACAGGCAATTATTTAGCCGCACTTTATGGCTACGGCTACATCAATTCCCTCAACAACCAAAACGCCGACATTCTCATTAATGTCACCCCCATCGGCATGAAAGGAGGCAAAGAAGCATTCGATCTCGCCTTCCCCGAAACCATGATCCGCCACGCCAAAACCGCTTTTGACGTCGTCGCCCACCCCGCCGACACCCCGTTAATCAAAGCCGCCCAAGCCCTCGGCAAACAAACCATCTCCGGTGCCGAAGTCATCGTCTTACAAGCCGTCGAACAATTTGAACTCTACACCGGCAAACGACCAAGCGAGGAACTCATCGCCGAAGCCGCGGAATATGCAAGAAAGAATGCG","","","29671","MLNKDTQLCMSLSGRPGNFGTQFHNYLYQKLGLNFIYKAFTTNDIEHAVKGVRALGIRGCAVSMPFKESCMPFLDEIPPSAQAIKSVNTIVNDNGFLRAYNTDYIAIVKLIERYQLDKNDSVIVHGSGGMAKAVVAAFKNSGFENVKIFARNEKTGNYLAALYGYGYINSLNNQNADILINVTPIGMKGGKEAFDLAFPETMIRHAKTAFDVVAHPADTPLIKAAQALGKQTISGAEVIVLQAVEQFELYTGKRPSEELIAEAAEYARKNA","1194189","[CATALYTIC ACTIVITY] Shikimate + NADP(+) = 5-dehydroshikimate + NADPH.[PATHWAY] Aromatic amino acids biosynthesis; shikimate pathway; fourth step.","shikimate 5-dehydrogenase protein","Cytoplasm","","
InterPro
IPR006151
Domain
Shikimate/quinate 5-dehydrogenase
PF01488\"[107-222]TShikimate_DH
InterPro
IPR013708
Domain
Shikimate dehydrogenase substrate binding, N-terminal
PF08501\"[12-90]TShikimate_dh_N
noIPR
unintegrated
unintegrated
G3DSA:3.40.192.10\"[1-100]Tno description
G3DSA:3.40.50.720\"[101-271]Tno description
PTHR21089\"[176-269]TSHIKIMATE DEHYDROGENASE


","BeTs to 23 clades of COG0169COG name: Shikimate 5-dehydrogenaseFunctional Class: EThe phylogenetic pattern of COG0169 is aompkzyqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 2e-46) to 6/6 blocks of the IPB002907 family, which is described as \"Shikimate / quinate 5-dehydrogenase\". Interpro entry for IP:IPR002907. IPB002907A 10-37 3.5e-08 IPB002907B 59-90 4.2e-15 IPB002907C 97-106 0.0057 IPB002907D 123-132 0.077 IPB002907E 174-187 1.1e-05 IPB002907F 235-250 0.0002","Residues 126 to 156 match (5e-07) PD:PD199044 which is described as PROTEOME COMPLETE PM1429 HI0607 SHIKIMATE 5-DEHYDROGENASE-LIKE OXIDOREDUCTASE ","","","","","","","","","","","Tue Jan 7 17:07:58 2003","Tue Jan 7 17:07:58 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01772 is paralogously related to AA00575 (4e-16).","","","","","","Residues 23 to 253 (E-value = 7.8e-95) place AA01772 in the Shikimate_DH family which is described as Shikimate / quinate 5-dehydrogenase (PF01488)","","","","","","","","1","","","" "AA01773","1195017","1195172","156","TTGGTGTGGATGGAAAATAATACGGTGAGTATAGCAGTTCCTGATGGCGCGCGCCTTGCGAGGCGTGTGAGCAAGTTGATAAAAAATATTCGGGATATAGATCAAAGTGCGGTCATTTCTTTTTATGTTTTTAACTTACAAACTCGGACGAATGCC","","","5888","LVWMENNTVSIAVPDGARLARRVSKLIKNIRDIDQSAVISFYVFNLQTRTNA","1195172","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 10:49:13 2004","Thu Feb 26 10:49:13 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01773 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 10:49:13 2004","","","","","","","","","","","","","1","","","" "AA01774","1196036","1195155","882","ATGAGTTACGCAAAAGAAATTGATAATCTAAATCAACATTTAGCTGATTTAAACGGCAAAATTAATGTCTCTTTTGAATTTTTCCCGCCGAAAAGTGAAAAAATGGAAAATCTTCTGTGGGAATCCATCCATCGCTTAAAAGTGCTAAAACCGAAATTTGTATCCGTGACTTACGGCGCCAATTCCGGCGAGCGTGAACGCACTCACGGGGTGGTGAAACGCATTAAGCAGGAAACCGGTCTGGAAGCTGCGCCGCATTTAACCGGTATTGACGCTACCTCGGACGAATTGCGTCGCATTGCCAAAGGTTATTGGGATAGCGGCATTCGTCGCATTGTGGCACTGCGCGGTGACGAGCCGAAAGGCTACGAGAAAAAACCATTTTATGCCGCCGATTTAGTAGCATTATTACGTGACGTATCAGATTTTGATATTTCCGTGGCGGCATACCCTGAGGTTCATCCGGAAGCCAAATCGGCGCAAGCGGATTTAATTAATTTAAAACGTAAAATTGATGCCGGTGCCAATCATGTGATCACACAATTCTTTTTCGATATTGACAGCTATCTGCGGTTCCGCGATCGCTGCGCGTCTATCGGTATTGATGCAGAAATCGTGCCGGGGATTCTGCCGGTGACCAACTTCAAACAATTACAAAAAATGGCAGCAATCACTAATGTGAAAATTCCAGCTTGGATGAGCAAAATGTATGAAGGCTTGGATGATGACCAAACCACCCGCAATCTGGTGGCGGCGAGCATCGCCATGGACATGGTGCGTGTACTGTCCCGCGAAGGGGTAAAAGACTTTCATTTCTACACCCTGAATCGCAGTGAACTCACCTATGCTATTTGCCACACGTTAGGCATTCGTCCGAGTTTG","","","36710","MSYAKEIDNLNQHLADLNGKINVSFEFFPPKSEKMENLLWESIHRLKVLKPKFVSVTYGANSGERERTHGVVKRIKQETGLEAAPHLTGIDATSDELRRIAKGYWDSGIRRIVALRGDEPKGYEKKPFYAADLVALLRDVSDFDISVAAYPEVHPEAKSAQADLINLKRKIDAGANHVITQFFFDIDSYLRFRDRCASIGIDAEIVPGILPVTNFKQLQKMAAITNVKIPAWMSKMYEGLDDDQTTRNLVAASIAMDMVRVLSREGVKDFHFYTLNRSELTYAICHTLGIRPSL","1195154","","5,10-methylenetetrahydrofolate reductase","Cytoplasm","","
InterPro
IPR003171
Family
Methylenetetrahydrofolate reductase
PF02219\"[9-289]TMTHFR
InterPro
IPR004620
Family
5,10-methylenetetrahydrofolate reductase
TIGR00676\"[23-289]Tfadh2: 5,10-methylenetetrahydrofolate reduc
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.220\"[18-292]Tno description
PTHR21091\"[86-289]TMETHYLTETRAHYDROFOLATE:HOMOCYSTEINE METHYLTRANSFERASE RELATED
PTHR21091:SF1\"[86-289]TMETHYLENETETRAHYDROFOLATE REDUCTASE


","No hits to the COGs database.","Significant hit (2.2e-104) to 8/8 blocks of the IPB003171 family, which is described as \"Methylenetetrahydrofolate reductase\". Interpro entry for IP:IPR003171. IPB003171A 23-33 1.4e-05 IPB003171B 51-62 1e-05 IPB003171C 80-113 4.1e-16 IPB003171D 129-139 0.016 IPB003171E 143-156 4.9e-09 IPB003171F 163-192 3.6e-22 IPB003171G 229-266 4.9e-17 IPB003171H 267-290 3.8e-16","Residues 19 to 293 match (1e-145) PD:PD406226 which is described as REDUCTASE OXIDOREDUCTASE 510-METHYLENETETRAHYDROFOLATE PROTEOME COMPLETE METHYLENETETRAHYDROFOLATE FAD FLAVOPROTEIN NADP METHIONINE ","","","","","","","","","","","Fri May 20 14:16:56 2005","Tue Jan 7 17:11:35 2003","","Fri May 20 14:16:56 2005","Fri May 20 14:16:56 2005","Fri May 20 14:16:56 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA01774 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Fri May 20 14:16:56 2005","","","","","Residues 9 to 289 (E-value = 5.3e-159) place AA01774 in the MTHFR family which is described as Methylenetetrahydrofolate reductase (PF02219)","Fri May 20 14:16:56 2005","","","","Guenther,B.D., Sheppard,C.A., Tran,P., Rozen,R., Matthews,R.G. and Ludwig,M.L. The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia. Nat. Struct. Biol. 6 (4): 359-365 (1999) [PubMed: 10201405].Saint-Girons,I., Duchange,N., Zakin,M.M., Park,I., Margarita,D., Ferrara,P. and Cohen,G.N. Nucleotide sequence of metF, the E. coli structural gene for 5-10 methylene tetrahydrofolate reductase and of its control region. Nucleic Acids Res. 11 (19): 6723-6732 (1983) [PubMed: 6356036].","","Tue Jan 7 17:11:35 2003","1","","","" "AA01775","1196141","1196242","102","ATGTGCGAAACAAAAGCCCGCGATGTATCACGGGCTTTAAAAACAGCATTTTTTATGACCGCACTTTTGCCTAATTACGTCGTCGTGCCAACAACCACCAAG","","","3787","MCETKARDVSRALKTAFFMTALLPNYVVVPTTTK","1196242","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 10:47:31 2004","Thu Feb 26 10:47:31 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01775 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 10:47:31 2004","","","","","","","","","","","","","1","","","" "AA01776","1197278","1196214","1065","ATGAATACATTAGAACGATATATCGGTAAAAGTATTTTAGGTACGATCTTCGCCACCTTGTTAATGTTGGTGGGGTTGTCCGCTATCATTAAATTCGTGGAACAGTTCCGCAGTGTGGGCAAAGGCACTTATGATATTTTACAAGCCATCGCTTATACCGTGCTGACCATGCCGAAAGACGTGGAAACCTTTTTCCCGATGGCGGCACTACTCGGCGCACTGATTGCTTTAGGTAATCTTGCCAGCCGCAGTGAACTGGTGGTGATGCAATCTTCCGGCTTTTCCCGTATGCGTATTGGTTTTGCGGTGATGAAAACCACGCTCCCTTTAGTGTTGCTGACCATGGTGATCGGTGAGTGGGGCATTCCGCAAACGGAACAATTCGCCCGTGATATGCGTTCCAAAGCTATTTCCGGCGGTTCAATGCTATCGGTGAAAAACGGTATTTGGGCGAAAGACGGCAATAATTTCGTGTATGTGCGTCGCATTACCGATGACGTGGAATTAAATGATATTTATATTTACACCTTTAATGAACAGCGTCAGTTAGAGAAACTCAAACACGCCAACCGGGCAACCTTTAACAGCGGCAAATGGACGTTGCAGCAAGTCAACGAATCACGTATTCAGCCGGAGAACATTCAAACCACCAATCGTTTAAACGAAGAATGGCAAACCAATTTAACACCCGATAAACTTGGTGTGGCGTCGTTACGACCAACTTCTTTATCTATTTCCGGTTTATCCAATTACATTACTTTCTTAAGGGAGACGGGACAGGATTCCAAAAATTTCGAGCTAACCTATTGGCGTAAATTATTCCAGCCGATTTCGGTTGGAGTCATGATGATGTTGGCGCTGTCCTTTATTTTCGGACCGTTGCGCAGCGTGACTGCAGGCGCCCGTATCCTTATCGGGATTTGCTTCGGCTTCCTGTTCTATGTGGTGAATGAATTATTTGGTAAATTCAGTTTAGTTTATAACACCACGCCGCTTATCGGCGCGCTGATGCCGAGTGTGCTGTTCCTAATCATCACTTGGTGGTTGTTGGCACGACGACGTAAT","","","40014","MNTLERYIGKSILGTIFATLLMLVGLSAIIKFVEQFRSVGKGTYDILQAIAYTVLTMPKDVETFFPMAALLGALIALGNLASRSELVVMQSSGFSRMRIGFAVMKTTLPLVLLTMVIGEWGIPQTEQFARDMRSKAISGGSMLSVKNGIWAKDGNNFVYVRRITDDVELNDIYIYTFNEQRQLEKLKHANRATFNSGKWTLQQVNESRIQPENIQTTNRLNEEWQTNLTPDKLGVASLRPTSLSISGLSNYITFLRETGQDSKNFELTYWRKLFQPISVGVMMMLALSFIFGPLRSVTAGARILIGICFGFLFYVVNELFGKFSLVYNTTPLIGALMPSVLFLIITWWLLARRRN","1196213","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR005495
Family
Predicted permease YjgP/YjgQ
PF03739\"[6-352]TYjgP_YjgQ
noIPR
unintegrated
unintegrated
signalp\"[1-28]?signal-peptide
tmhmm\"[12-30]?\"[63-81]?\"[102-122]?\"[274-294]?\"[303-323]?\"[329-351]?transmembrane_regions


","BeTs to 11 clades of COG0795COG name: Predicted permeasesFunctional Class: RThe phylogenetic pattern of COG0795 is --------vd---cefghsnujxit-Number of proteins in this genome belonging to this COG is","","Residues 4 to 342 match (9e-148) PD:PD296042 which is described as PROTEOME COMPLETE TRANSMEMBRANE MEMBRANE INNER PERMEASE NMB1571 YJGQ VC2499 PROBABLE ","","","","","","","","","","","","Tue Jan 7 17:13:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01776 is paralogously related to AA01777 (1e-07).","","","","","","Residues 6 to 352 (E-value = 1.8e-111) place AA01776 in the YjgP_YjgQ family which is described as Predicted permease YjgP/YjgQ family (PF03739)","","","","","","","","1","","","" "AA01777","1198401","1197286","1116","ATGGACGATAAAGTGATTTTAACCCGATATTTAACCAAAGAAATTTTTAAAAGCCAGATTGCGATTTTGTTTATTTTGCTGCTGATCTTTTTCTGTCAGCAATTAGTACGCGTACTGGGCTCTGCCGCAAACGGTAAAGTACCGGCGGATTTAGTCTTTTCTTTACTCGGCTTAGGTATGCCAACCATGGCGCAGCTCATGTTGCCGCTCTGTTTGTTCATCGCCATTTTACTGACGCTGGGGCGTTTGTATGCAGAAAGTGAAATTACCGTGATGCGTGCCTGCGGTGTGGGACAGCCGATTTTAGTCAAAGTTGTACTGCTACTTTCCTTATTAACGTCAGGTGTGGCGGCTTACAACGCACTTTGGTTGACACCTTGGGCGATTCACAAACAGACAGAAATTGTGGAAGATGCCAAAGCCAATCCGAATGTAGGTGCATTGTCCGCCGGGCAATTCGTTAGCGCCAACAACAGCGATTTCGTGCTGTTCATCGATGACATTCAAAATAATCAAATCAATAATGTTTATGTGTTCCAAACGCAACCACGCGGACAAAGCAAGCCGTCGGTGATCGTAGCGGAAAAAGGCGAATTAAAAGCGTTACCGAACGGCGATCAGGTGCTGAATCTACAAAACAGCGAACGCTTTGAAGGCACGGCGGCACTGCCGGATTTTCGCATCACCCATTTTGATGAATATCAGGCGTATTTAGGGCATAAAGCAGTGAATGATGATTCTGCCGAGACGGAAGAATTAAGTTTAAGTCAGTTGTTAAACACCAAAACACCGGCGGCGAAAACCGAGTTTCACTGGCGCCTAACCTTAATTCTCGCCGTGCCGATTATGGCGTTACTTGCCGTGCCGCTAAGCCGTGTGAATCCGCGCCAGGGGCGTTTTGCTAAAGTGTTGCCGGCATTGTTGTTGTATTTAATTTATTTCTTATTGCAAAGCTCGTTAAAATCCGCCGGCGGGGCAGGCAAATTGGATGCCGGGTTATTCATGCCGTTAGTCAATATTGTCTTTTTCTTACTGGCAATTCTCCTGAATAGCTGGGATAGCGCATTTATGTATCGCATTCGTTATTCGTTCAATAAAAAAGCGGTAACACAGGGA","","","41037","MDDKVILTRYLTKEIFKSQIAILFILLLIFFCQQLVRVLGSAANGKVPADLVFSLLGLGMPTMAQLMLPLCLFIAILLTLGRLYAESEITVMRACGVGQPILVKVVLLLSLLTSGVAAYNALWLTPWAIHKQTEIVEDAKANPNVGALSAGQFVSANNSDFVLFIDDIQNNQINNVYVFQTQPRGQSKPSVIVAEKGELKALPNGDQVLNLQNSERFEGTAALPDFRITHFDEYQAYLGHKAVNDDSAETEELSLSQLLNTKTPAAKTEFHWRLTLILAVPIMALLAVPLSRVNPRQGRFAKVLPALLLYLIYFLLQSSLKSAGGAGKLDAGLFMPLVNIVFFLLAILLNSWDSAFMYRIRYSFNKKAVTQG","1197285","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR005495
Family
Predicted permease YjgP/YjgQ
PF03739\"[9-358]TYjgP_YjgQ
InterPro
IPR008893
Domain
WGR
SM00773\"[159-218]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-34]?signal-peptide
tmhmm\"[21-41]?\"[66-84]?\"[105-123]?\"[270-288]?\"[303-323]?\"[329-349]?transmembrane_regions


","BeTs to 11 clades of COG0795COG name: Predicted permeasesFunctional Class: RThe phylogenetic pattern of COG0795 is --------vd---cefghsnujxit-Number of proteins in this genome belonging to this COG is","","Residues 9 to 132 match (3e-24) PD:PD313198 which is described as PROTEOME COMPLETE MEMBRANE TRANSMEMBRANE INTEGRAL YJGP PROBABLE VC2500 CC1691 PA3828 ","","","","","","","","","","","","Tue Jan 7 17:14:10 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01777 is paralogously related to AA01776 (1e-07).","","","","","","Residues 9 to 358 (E-value = 6.3e-104) place AA01777 in the YjgP_YjgQ family which is described as Predicted permease YjgP/YjgQ family (PF03739)","","","","","","","","1","","","" "AA01778","1198538","1200025","1488","ATGAAGTATAGTGCTCAACAATGTGCCATTAATCAGCCTGCGGACTGCCTGATTGTGGGCATTTTTGAAGAGAAAATCCTATCCAAAAGTGCGGTGGAAATTGACAATCTTTCCGGCAATTATCTAAGCGATTTGGTGGAAAACGGCGAAATCAGCGGCAAATTAGGGCAAACCGCCTTGTTACGCCATTTGTCAAATATCGCTGCCAAGCGCGTATTGGTGGTGGGTTGCGGCAAAGCCGGAGAGCTTAGCGAACGTCAATATAAACAACTTATTCAAAAATCCGTACAGGCATTAAAAGAAACCCAAGCCAAAAGTGCGGTCAGTTTTTTAACTGAAATTCAGCTCAACCAACGCGATCTTTATTGGAATATTCGCTTCGCGGTGGAAACCGTCGAACAGGATTTATACCAATTCACCCAATTCAAAAGCCAAAAAACAGCGGAAAAATCCACCGCACTTTGTGAAGTGATTTTTAATGTGGATGCCAAGGATCAAACCACCGCTGAGCAGGCAATTCAGCACGCTTCCGCCATTGCATTGGGCGTGCGCTTTACTAAAGATGTCGCAAATTGCCCGCCAAATGTGTGTACCCCAAACTACCTGGCGGATAAAGCCTTAGACTTGGCAAAACACTCACCTCTCATCAAAACCACAATTATCAACGAAGCCGACATGGAAAAATTAGGCATGGGCGCTTATTTGGCGGTGTCTCGCGGTTCCCGTAATGAAGCAAAACTTTCCATTATGGAATACCGTAATGCGCCGAATCCGAACGCGAAACCTATCGTACTGGTGGGCAAAGGCTTAACCTTTGACGCAGGCGGGATTTCTCTCAAACCCGCCGCCGACATGGATGAAATGAAATATGATATGTGCGGTGCGGCATCTGTTTACGGCGTAATGAGCGCATTGGCGCAATTACAGCTGCCGCTAAACGTTATCGGCGTGATGGCGGGCTGCGAAAATCTGCCTGATGGCAATGCTTATCGCCCGGGCGATATTCTCACCACCATGAACGGCTTAACGGTGGAAGTGTTGAACACCGATGCAGAAGGACGTTTAGTGTTGTGCGATACGTTAACTTATGTGGAACGCTTTGATCCGCAAGTCGTTATTGATATTGCTACCTTAACCGGCGCGTGTGTGGTGGCATTAGGTCAACACAACAGCGGCTTGGTTTCCACTCATGATGACATTGCTGCGGCCATTGAAAAAGCGGCGCAACAAAGTGCCGACAAGGCGTGGCGTTTGCCGTTAAGTGAAGAATATCAAGAACAGCTTAAATCTAACTTTGCCGATTTAGCTAACCTTGGCGGACGCTGGGGCGGTACGATCACCGCTGCTGCATTTCTTGCCAATTTCACCAAGAAATACCCATGGGCACACCTAGACATCGCCGGTACCGCGTGGTTACAAGGCGCCAATAAAGGTGCCACCGGCAGACCGGTTTCCTTGCTGGTGCAATTCCTGTTGAATCAAGTGAAA","","","53612","MKYSAQQCAINQPADCLIVGIFEEKILSKSAVEIDNLSGNYLSDLVENGEISGKLGQTALLRHLSNIAAKRVLVVGCGKAGELSERQYKQLIQKSVQALKETQAKSAVSFLTEIQLNQRDLYWNIRFAVETVEQDLYQFTQFKSQKTAEKSTALCEVIFNVDAKDQTTAEQAIQHASAIALGVRFTKDVANCPPNVCTPNYLADKALDLAKHSPLIKTTIINEADMEKLGMGAYLAVSRGSRNEAKLSIMEYRNAPNPNAKPIVLVGKGLTFDAGGISLKPAADMDEMKYDMCGAASVYGVMSALAQLQLPLNVIGVMAGCENLPDGNAYRPGDILTTMNGLTVEVLNTDAEGRLVLCDTLTYVERFDPQVVIDIATLTGACVVALGQHNSGLVSTHDDIAAAIEKAAQQSADKAWRLPLSEEYQEQLKSNFADLANLGGRWGGTITAAAFLANFTKKYPWAHLDIAGTAWLQGANKGATGRPVSLLVQFLLNQVK","1200024","[FUNCTION] Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removalof unsubstituted N-terminal amino acids from various peptides (by similarity). [CATALYTIC ACTIVITY] Release of an N-terminal amino acid, Xaa--Xbb-, in which xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Xbb may be Pro. [COFACTOR] Binds 2 manganese ions per subunit (by similarity).[SUBCELLULAR LOCATION] Cytoplasmic (by similarity). [SIMILARITY] Belongs to peptidase family M","aminopeptidase A/I; cytosol aminopeptidase; leucyl aminopeptidase","Cytoplasm","","
InterPro
IPR000819
Domain
Peptidase M17, leucyl aminopeptidase, C-terminal
PR00481\"[263-280]T\"[285-306]T\"[322-343]T\"[344-364]T\"[372-387]TLAMNOPPTDASE
PF00883\"[183-489]TPeptidase_M17
PS00631\"[348-355]TCYTOSOL_AP
InterPro
IPR008283
Domain
Peptidase M17, leucyl aminopeptidase, N-terminal
PF02789\"[18-146]TPeptidase_M17_N
InterPro
IPR011356
Family
Peptidase M17, leucyl aminopeptidase
PIRSF001116\"[72-496]TCytosol aminopeptidase
PTHR11963:SF3\"[1-493]TLEUCINE AMINOPEPTIDASE
noIPR
unintegrated
unintegrated
G3DSA:3.40.220.10\"[1-161]Tno description
G3DSA:3.40.630.10\"[185-496]Tno description
PTHR11963\"[1-493]TLEUCINE AMINOPEPTIDASE-RELATED


","No hits to the COGs database.","Significant hit (4.6e-107) to 7/7 blocks of the IPB000819 family, which is described as \"Cytosol aminopeptidase\". Interpro entry for IP:IPR000819. IPB000819A 186-195 0.25 IPB000819B 216-254 6.5e-13 IPB000819C 265-280 1.5e-09 IPB000819D 322-364 1e-32 IPB000819E 372-387 2e-11 IPB000819F 409-456 2.5e-21 IPB000819G 457-471 1.3e-09","Residues 122 to 178 match (9e-08) PD:PD589085 which is described as MALATE DEHYDROGENASE MITOCHONDRIAL DEHYDROGENASE ","","","","","Thu Feb 13 17:17:57 2003","","","","","","Fri Jan 7 17:35:30 2005","Tue Jan 7 17:20:16 2003","","Fri Jan 7 17:35:30 2005","Fri Jan 7 17:35:30 2005","Fri Jan 7 17:35:30 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA01778 is paralogously related to AA00723 (1e-47).","Fri Jan 7 17:35:30 2005","","","","","Residues 183 to 489 (E-value = 6.4e-187) place AA01778 in the Peptidase_M17 family which is described as Cytosol aminopeptidase family, catalytic domain (PF00883)","Fri Jan 7 17:35:30 2005","","","","Stirling,C.J., Colloms,S.D., Collins,J.F., Szatmari,G. and Sherratt,D.J. xerB, an Escherichia coli gene required for plasmid ColE1 site-specific recombination, is identical to pepA, encoding aminopeptidase A, a protein with substantial similarity to bovinelens leucine aminopeptidase. EMBO J. 8 (5): 1623-1627 (1989) PubMed: 2670557.Charlier,D., Hassanzadeh,G., Kholti,A., Gigot,D., Pierard,A. and Glansdorff,N. carP, involved in pyrimidine regulation of the Escherichia coli carbamoylphosphate synthetase operon encodes a sequence-specificDNA-binding protein identical to XerB and PepA, also required for resolution of ColEI multimers. J. Mol. Biol. 250 (4): 392-406 (1995) PubMed: 7616564.McCulloch,R., Burke,M.E. and Sherratt,D.J. Peptidase activity of Escherichia coli aminopeptidase A is not required for its role in Xer site-specific recombination. Mol. Microbiol. 12 (2): 241-251 (1994) PubMed: 8057849.","","Thu Feb 13 17:17:57 2003","1","","","" "AA01779","1201234","1200176","1059","ATGCTGTACATTGATGTAAAAAAACAATTAGGCAATTTATCCCTACAGGCGAAGCTTGAAATTCCATCGCAAGGCGTGACCGCACTTTTCGGCTTATCCGGTTCGGGGAAATCTTCTCTGATCAATTTGATAAGCGGGTTAATTAATCCGGATGAGGGCGTAATTGCGTTAAATGATCGTGTGTTATTTGAAGCGGAAGAGGGAATTTGTGTTCCCGCCAATCGGCGCAATATTGGTTATGTTTTTCAGGACGCACGCTTATTTCCGCATTACACGGTGAAAGGCAATTTGCGCTACGGCATGAAAAATACCAGCAAGGATGAATTTGACTACATTGTGGAATTGCTGGGGATCGGGCATTTATTAAAACGTTATCCGATCACTTTATCCGGCGGTGAAAAACAACGTGTGGCAATCGGGCGGGCACTATTAACAGACCCGGAAATTTTATTAATGGACGAACCGCTTTCCGCCCTAGATCTACCACGCAAGCGGGAATTATTGAATTATCTGGAACGATTATCCAAAGAAATTAATATTCCGATTTTGTACGTGACGCACAGCATTGATGAACTTTTGCGCCTGCCGGAACGGGTTGTCTTATTAACCGACGGAAAGGTGGAAGCCTATGATATGTTGGAGAACATTTGGGAAAGCCCGCTGTTCTTACCTTGGAAACAGGAAAACGAACAAAGTGCGGTGCTTTCTCTGCCTGTTTTTATGCATAATCCGTCTTATAAAATGACCGCACTTTCTATCGGCGATCAGAACATTTGGATTAACCAAGTGGCGTCGGAAATGAATGAAAATGTCCGTATTTGCGTTCATAGCTCCGATGTGTCCATCAGTCTGCATAAAGCGGAAAAATCCAGCATTCGAAACATTTTACACGGGCGCATTGTGAAAATTCAGGAACAGGAAAACCGTGTCGATCTCAAACTGGATATTGGCGGAAAGCATATTTGGGCGAGTATCAGCAAATGGTCGTTTCATGATTTGGCATTGCAACCGGGACAACTGGTTTATGCGCAGATTAAAGCCATTTCCGTGCTGTCTGCA","","","39716","MLYIDVKKQLGNLSLQAKLEIPSQGVTALFGLSGSGKSSLINLISGLINPDEGVIALNDRVLFEAEEGICVPANRRNIGYVFQDARLFPHYTVKGNLRYGMKNTSKDEFDYIVELLGIGHLLKRYPITLSGGEKQRVAIGRALLTDPEILLMDEPLSALDLPRKRELLNYLERLSKEINIPILYVTHSIDELLRLPERVVLLTDGKVEAYDMLENIWESPLFLPWKQENEQSAVLSLPVFMHNPSYKMTALSIGDQNIWINQVASEMNENVRICVHSSDVSISLHKAEKSSIRNILHGRIVKIQEQENRVDLKLDIGGKHIWASISKWSFHDLALQPGQLVYAQIKAISVLSA","1200175","[FUNCTION] Iinvolved in the transport of molybdenum into the cell (by similarity). [SUBCELLULAR LOCATION] Inner membrane-associated (Potential).","molybdenum ABC transporter, ATP-binding protein","Cytoplasm, Inner membrane","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[128-171]TQ9CMS0_PASMU_Q9CMS0;
PF00005\"[24-205]TABC_tran
PS50893\"[1-229]TABC_TRANSPORTER_2
PS00211\"[129-143]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[23-205]TAAA
InterPro
IPR005116
Domain
TOBE
PF03459\"[290-352]TTOBE
InterPro
IPR011868
Family
Molybdate ABC transporter, ATP-binding protein
TIGR02142\"[2-351]TmodC_ABC: molybdate ABC transporter, ATP-bi
noIPR
unintegrated
unintegrated
G3DSA:2.40.50.100\"[288-350]Tno description
G3DSA:3.40.50.300\"[9-220]Tno description
PTHR19222\"[21-220]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF49\"[21-220]TMOLYBDENUM ABC TRANSPORTER


","No hits to the COGs database.","Significant hit ( 1.1e-25) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 13-59 4.4e-10 IPB001140B 126-164 4.4e-14 IPB001140C 182-211 2.4e+02","Residues 72 to 142 match (3e-07) PD:PD433312 which is described as MODC ATP-BINDING ","","","","","","","","","","","Wed Jan 8 08:01:12 2003","Wed Jan 8 08:01:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01779 is paralogously related to AA01051 (7e-33), AA01656 (4e-32), AA01867 (1e-31), AA01645 (3e-31), AA02718 (2e-29), AA00415 (2e-29), AA00700 (3e-28), AA01684 (1e-25), AA02353 (3e-24), AA01524 (7e-23), AA01947 (9e-23), AA01616 (6e-22), AA00858 (7e-22), AA02440 (8e-21), AA02324 (2e-20), AA01422 (2e-19), AA02320 (1e-18), AA02899 (2e-18), AA00207 (2e-18), AA01824 (6e-18), AA01568 (8e-18), AA02080 (1e-17), AA00933 (3e-17), AA02606 (4e-17), AA02152 (1e-16), AA02898 (2e-16), AA02140 (2e-16), AA01393 (3e-16), AA00751 (3e-16), AA02550 (1e-15), AA01820 (2e-15), AA01961 (4e-15), AA02805 (9e-15), AA01510 (2e-14), AA02786 (2e-14), AA00799 (2e-14), AA02573 (7e-12), AA02642 (2e-11), AA01509 (2e-11), AA01569 (2e-11), AA01757 (3e-11), AA02225 (6e-11), AA01456 (1e-10), AA02609 (1e-10), AA00061 (4e-10), AA02484 (5e-09), AA02331 (1e-08), AA02146 (3e-08), AA00934 (1e-07), AA01555 (5e-07), AA00591 (1e-05), AA01291 (2e-04) and A02145 (0.001).","","","","","","Residues 290 to 352 (E-value = 5.6e-12) place AA01779 in the TOBE family which is described as TOBE domain (PF03459)","","","","","Maupin-Furlow,J.A., Rosentel,J.K., Lee,J.H., Deppenmeier,U., Gunsalus,R.P. and Shanmugam,K.T. Genetic analysis of the modABCD (molybdate transport)operon of Escherichia coli J. Bacteriol. 177 (17), 4851-4856 (1995) PubMed: 7665460 Walkenhorst,H.M., Hemschemeier,S.K. and Eichenlaub,R. Molecular analysis of the molybdate uptake operon,modABCD, of Escherichia coli and modR, a regulatory gene Microbiol. Res. 150 (4), 347-361 (1995) PubMed: 8564363 Self WT, Grunden AM, Hasona A, Shanmugam KT. Molybdate transport. Res Microbiol. 2001 Apr-May;152(3-4):311-21. Review. PMID: 11421278 Grunden AM, Shanmugam KT. Molybdate transport and regulation in bacteria. Arch Microbiol. 1997 Nov;168(5):345-54. Review. PMID: 9325422 ","","Wed Jan 8 08:01:12 2003","1","","","" "AA01780","1201994","1201224","771","GTGCTACGCTTTGTTTATGGGCTATTTATAAAGGGAATCGGGATTTTGCTTACACAATTTCTGACGTTATTAGGTTTAAGCCAATTAGAAATCGACGCCATTCGGTTGAGCCTGGAAGTGTCTGTCAGTGCGATGATTTGGAGCCTGCCTTTTGCGATTTTTGTGGCGTGGCTGTTAGCGCGTAAAGAATTTTATGGAAAATCCATCGTCAGCGGCATCATCCATTTGCCTTTGGTATTGCCCCCTGTGGTGATTGGTTACCTGTTGTTGGTGGCAATGGGACGCAACGGTTTCATCGGCAAATATTTATACCAATGGTTCGGGCTGACTTTCGGCTTCAGCTGGCGCGGGGCGGTATTAGCCGCTGCCGTGGTGGCATTTCCATTAGTGGTTCGGGCAATTCGTCTTTCGCTGGAAAGTATCGACTTAAAATTGGAACAAGCCGCCAGAACCTTGGGCGCTTCCCCTTGGCGGGTATTTTTTACCATCACCTTGCCCCTATCTTTGCCGGGAATTTTAGCGGGCATCGTATTGGGATTTGCCCGCTCCTTGGGTGAATTCGGCGCAACCATTACTTTCGTTTCCAATATCGCCGGTGAAACACAAACTATTCCTTTAGCAATGTATTCTTTCATTCAAACGCCCGGCGCGGAAGAACAAGCCGCCCGTTTATGTGTTTTTGCTATAATTTTATCCCTGGTTTCCCTGTTGTTATCGGAGTGGCTGGCAAAACGGATGCAGAAAAGATTAGGACAAAGCGATGCTGTACAT","","","28101","VLRFVYGLFIKGIGILLTQFLTLLGLSQLEIDAIRLSLEVSVSAMIWSLPFAIFVAWLLARKEFYGKSIVSGIIHLPLVLPPVVIGYLLLVAMGRNGFIGKYLYQWFGLTFGFSWRGAVLAAAVVAFPLVVRAIRLSLESIDLKLEQAARTLGASPWRVFFTITLPLSLPGILAGIVLGFARSLGEFGATITFVSNIAGETQTIPLAMYSFIQTPGAEEQAARLCVFAIILSLVSLLLSEWLAKRMQKRLGQSDAVH","1201223","[FUNCTION] Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane (by similarity). [SUBCELLULAR LOCATION] Integral membrane protein. Inner membrane (Potential).[SIMILARITY] Belongs to the binding-protein-dependent transport system permease family. CystW subfamily. ","ABC-related molybdenum transport system permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR000515
Family
Binding-protein-dependent transport systems inner membrane component
PF00528\"[34-252]TBPD_transp_1
PS50928\"[34-242]TABC_TM1
InterPro
IPR011867
Family
Molybdate ABC transporter, permease protein
TIGR02141\"[35-245]TmodB_ABC: molybdate ABC transporter, permea
noIPR
unintegrated
unintegrated
signalp\"[1-28]?signal-peptide
tmhmm\"[7-27]?\"[33-53]?\"[74-92]?\"[111-131]?\"[159-181]?\"[221-239]?transmembrane_regions


","BeTs to 20 clades of COG0555COG name: ABC-type sulfate/molybdate transport systems, permease componentsFunctional Class: PThe phylogenetic pattern of COG0555 is aompkz-q-dr-bcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 3.5e-10) to 1/1 blocks of the IPB000515 family, which is described as \"Binding-protein-dependent transport systems inner membrane component\". Interpro entry for IP:IPR000515. IPB000515 147-166 3.6e-10","Residues 55 to 117 match (2e-10) PD:PD390192 which is described as PROTEOME COMPLETE ABC PERMEASE MEMBRANE TRANSPORTER TRANSPORTER PLASMID TRANSMEMBRANE SUGAR ","","","","","","","","","","","Wed Jan 8 08:14:05 2003","Wed Feb 5 15:16:26 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01780 is paralogously related to AA01682 (5e-20), AA01644 (2e-17), AA02720 (3e-17), AA00699 (3e-16), AA01950 (1e-15), AA01649 (6e-14), AA01050 (5e-12), AA01948 (4e-11), AA02719 (2e-09), AA00416 (7e-07), AA01866 (1e-06), AA02352 (4e-05) and AA01650 (5e-04).","","","","","","Residues 34 to 252 (E-value = 1.6e-25) place AA01780 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component (PF00528)","","","","","Maupin-Furlow,J.A., Rosentel,J.K., Lee,J.H., Deppenmeier,U., Gunsalus,R.P. and Shanmugam,K.T. Genetic analysis of the modABCD (molybdate transport) operon of Escherichia coli J. Bacteriol. 177 (17), 4851-4856 (1995) PubMed: 7665460 Walkenhorst,H.M., Hemschemeier,S.K. and Eichenlaub,R. Molecular analysis of the molybdate uptake operon, modABCD, of Escherichia coli and modR, a regulatory gene Microbiol. Res. 150 (4), 347-361 (1995) PubMed: 8564363 Self WT, Grunden AM, Hasona A, Shanmugam KT. Molybdate transport. Res Microbiol. 2001 Apr-May;152(3-4):311-21. Review. PMID: 11421278 Grunden AM, Shanmugam KT. Molybdate transport and regulation in bacteria. Arch Microbiol. 1997 Nov;168(5):345-54. Review. PMID: 9325422 ","","Wed Feb 5 15:16:26 2003","1","","","" "AA01781","1202792","1202031","762","ATGTCTAAATATTCAAAAATTGCCGCAGGTTTAGCCGCCGCTTATTTTGCCTTTTCACTTTCCGCTCAAGCTAAAGTCACTGTTTTTGCCGCTGCGTCCATGACCGATTCCTTGAAGCAGGTCGCCGCCGATTATTACAAAATGAACCCGAAGGAAGAAGTTGTATTTTCTTTCGCCTCCTCTTCCACATTAGCCAAACAAATTGAAGAAGGTGCGCCTGCCGATTTATTTATTTCCGCCAGCGGCAAATGGATGAAATACCTTTCCGATAAAGAATTAACCGTGAAAGAAAGTGAAAAATTATTAGTAGGTAACGAACTGGTACTTATTTCACAAAAAAACAGCAAATTAGAAAATGTCGATATTGCTAAAGGCGAATGGATTAACCAATTAAATAATGCTTATTTATCCGTTGGCGACCCGGCGCACGTGCCTGCCGGTCAATATGCCGAAGAAGCCTTAACCAAATTAAACTTATGGGACAAAGTGAAAGATAAATTAGCCCGTGGCAAAGATGTGCGTGCCGCATTAGCTTTGGTTGAACGTGGTGAGTCTCCGTTGGGTATCGTATATGCAACCGATGCGAAAGTGAGTAAAGAAGTCAAAACGGTCGGTGTCTTCCCACAAGATTCTTATAAACCGGCAAATTATCCGGTTGCCATTTTAAAAGATCACAATAATGCGGAAACGCAAGCCTTCTTAAAATATTTAGAATCGCCTGAAGCGAAAAAAGTCTTTGCGGATTACGGTTTCTCGGTAAAA","","","27721","MSKYSKIAAGLAAAYFAFSLSAQAKVTVFAAASMTDSLKQVAADYYKMNPKEEVVFSFASSSTLAKQIEEGAPADLFISASGKWMKYLSDKELTVKESEKLLVGNELVLISQKNSKLENVDIAKGEWINQLNNAYLSVGDPAHVPAGQYAEEALTKLNLWDKVKDKLARGKDVRAALALVERGESPLGIVYATDAKVSKEVKTVGVFPQDSYKPANYPVAILKDHNNAETQAFLKYLESPEAKKVFADYGFSVK","1202030","From Genbank: [gi:1170988]This protein is involved in the transport of molybdenum into the cell.","molybdenum ABC transporter, periplasmic substrate-binding","Periplasm","","
InterPro
IPR005950
Family
Molybdenum ABC transporter, periplasmic binding protein
TIGR01256\"[31-250]TmodA: molybdate ABC transporter, periplasmi
InterPro
IPR006059
Family
Bacterial extracellular solute-binding protein, family 1
PF01547\"[7-244]TSBP_bac_1
InterPro
IPR011587
Domain
Prokaryotic extracellular metal-binding protein
PD008688\"[173-253]TQ9CMR8_PASMU_Q9CMR8;
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[105-215]Tno description
signalp\"[1-24]?signal-peptide


","BeTs to 13 clades of COG0725COG name: ABC-type molybdate transport system, periplasmic componentFunctional Class: PThe phylogenetic pattern of COG0725 is aompkz-q-dr-bcefgh--uj----Number of proteins in this genome belonging to this COG is","","Residues 177 to 251 match (1e-08) PD:PD038035 which is described as COMPLETE PROTEOME PERIPLASMIC ABC BINDING TRANSPORTER TRANSPORTER SPERMIDINE/PUTRESCINE-BINDING PRECURSOR SPERMIDINE/PUTRESCINE ","","","","","","","","","","","Tue Mar 16 14:17:41 2004","Wed Jan 8 08:18:21 2003","","","","Tue Mar 16 14:06:58 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01781 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Tue Mar 16 14:06:58 2004","","","","","Residues 7 to 244 (E-value = 1.4e-15) place AA01781 in the SBP_bac_1 family which is described as Bacterial extracellular solute-binding protein (PF01547)","Tue Mar 16 14:06:58 2004","","","","Maupin-Furlow JA, Rosentel JK, Lee JH, Deppenmeier U, Gunsalus RP, Shanmugam KT.Genetic analysis of the modABCD (molybdate transport) operon of Escherichia coli.J Bacteriol. 1995 Sep;177(17):4851-6.PMID: 7665460Walkenhorst HM, Hemschemeier SK, Eichenlaub R.Molecular analysis of the molybdate uptake operon, modABCD, of Escherichia coli and modR, a regulatory gene.Microbiol Res. 1995 Nov;150(4):347-61.PMID: 8564363Self WT, Grunden AM, Hasona A, Shanmugam KT.Molybdate transport.Res Microbiol. 152(3-4):311-21.PMID: 11421278Grunden AM, Shanmugam KT.Molybdate transport and regulation in bacteria.Arch Microbiol. 1997 Nov;168(5):345-54.PMID: 9325422Hu Y, Rech S, Gunsalus RP, Rees DC.Crystal structure of the molybdate binding protein ModA.Nat Struct Biol. 1997 Sep;4(9):703-7.PMID: 9302996","","Tue Mar 16 14:17:41 2004","1","","","" "AA01782","1203019","1203795","777","ATGCGAAGTGCCGAAATTTTACTCACCATCAAATTGAAACAACAACTCTTCGCAGATCCGAAGCGGATCCGTTTATTAAAAGAAATTGAAAAATGCGGCTCCATTAACCAAGCGGCAAAAAATGCCAAAGTCAGTTACAAAAGCGCCTGGGATCACCTTGAAGGCATGAATAAAATCAGCCCGAAACCGTTACTGGAACGCAATATCGGCGGCAAAAACGGCGGCGGCACGGCGCTTACCGTTTATGCGCAACGGTTGCTGCAACTTTATGATTTACTTGAACAAACACAAGAAAAGGCCTTTAGAATTTTGAAAGACGAAAAGGTTCCGCTCAACAGTTTGCTTTCCGCTACCGCGCGGTTTTCGCTGCAAAGTAGCGCACGCAATCAGTTTTTCGGCATCGTTCAGGCATTACGTTTTGAAGATGTACATTGTTTTGTGGATATCGAGCTGGAAGGCTTTTCCGAGCCATTAACCGTGTCGATTACAGAAAAAAGTGCGGTGCGTTTAAAACTTGAATTAAATAAGGAAGTTATGTTGATGTTTAAAGCACCTTGGGTAAAAATCCGCGCCAAACAGGCAAGAAATATGCCGAATCAATTCCGTGCAACGGTAAAATCCATTATTGACAAAGGGGAGGCAGGAGAAGCAATTTTAGTCTTAGAAGATTCAAAAATTGAGTTCTGTGCTACACTCACCAAAACTCAACATATTGAGCTTGAGCAACAGGTTTGGATTTCCGTCGATCCGGAGCAAATCATTCTTGCTACCCTTTAT","","","29345","MRSAEILLTIKLKQQLFADPKRIRLLKEIEKCGSINQAAKNAKVSYKSAWDHLEGMNKISPKPLLERNIGGKNGGGTALTVYAQRLLQLYDLLEQTQEKAFRILKDEKVPLNSLLSATARFSLQSSARNQFFGIVQALRFEDVHCFVDIELEGFSEPLTVSITEKSAVRLKLELNKEVMLMFKAPWVKIRAKQARNMPNQFRATVKSIIDKGEAGEAILVLEDSKIEFCATLTKTQHIELEQQVWISVDPEQIILATLY","1203794","From Genbank: [gi:1709071]The modE-Mo complex acts as a repressor of the modABC operon, involved in the transport of molybdate. Upon binding molybdate, the conformation of the protein changes, promoting dimerization of ModE-Mo. The protein dimer is then competent to bind a DNA region, upstream of the modABC operon. Acts also as an enhancer of the expression of genes coding for molybdoenzymes, bothdirectly and indirectly.","molybdenum transport protein; transcriptional regulator","Cytoplasm","","
InterPro
IPR000847
Domain
Bacterial regulatory protein, LysR
PF00126\"[20-84]THTH_1
InterPro
IPR003725
Domain
Molybdenum-binding protein, N-terminal
TIGR00637\"[17-114]TModE_repress: ModE molybdate transport repr
InterPro
IPR004606
Domain
Molybdenum-pterin binding
TIGR00638\"[123-193]TMop: molybdenum-pterin binding domain
InterPro
IPR005116
Domain
TOBE
PF03459\"[125-189]T\"[195-255]TTOBE
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[3-107]Tno description
noIPR
unintegrated
unintegrated
G3DSA:2.40.50.100\"[107-191]Tno description


","BeTs to 6 clades of COG2005COG name: N-terminal domain of molybdenum-binding proteinFunctional Class: RThe phylogenetic pattern of COG2005 is a-m-----------ef-h--uj----Number of proteins in this genome belonging to this COG is","Significant hit ( 7.7e-50) to 2/2 blocks of the IPB003725 family, which is described as \"Molybdenum-binding protein, N-terminal\". Interpro entry for IP:IPR003725. IPB003725A 33-84 4.1e-35 IPB003725B 158-190 1.5e-13","Residues 199 to 258 match (8e-10) PD:PD032882 which is described as PROTEOME COMPLETE MODE REGULATOR ACTIVATOR REGULATION MOLYBDENUM DNA-BINDING TRANSCRIPTION REPEAT ","","","","","","","","","","","Tue Mar 16 14:25:51 2004","Wed Jan 8 08:24:53 2003","","","Tue Mar 16 14:27:58 2004","Tue Mar 16 14:23:42 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01782 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Tue Mar 16 14:23:42 2004","","","","","Residues 195 to 255 (E-value = 1.3e-06) place AA01782 in the TOBE family which is described as TOBE domain (PF03459)","Tue Mar 16 14:23:42 2004","","","","Grunden AM, Shanmugam KT.Molybdate transport and regulation in bacteria.Arch Microbiol. 1997 Nov;168(5):345-54.PMID: 9325422Walkenhorst HM, Hemschemeier SK, Eichenlaub R.Molecular analysis of the molybdate uptake operon, modABCD, of Escherichia coli and modR, a regulatory gene.Microbiol Res. 1995 Nov;150(4):347-61.PMID: 8564363Grunden AM, Ray RM, Rosentel JK, Healy FG, Shanmugam KT.Repression of the Escherichia coli modABCD (molybdate transport) operon by ModE.J Bacteriol. 1996 Feb;178(3):735-44.PMID: 8550508Anderson LA, Palmer T, Price NC, Bornemann S, Boxer DH, Pau RN.Characterisation of the molybdenum-responsive ModE regulatory protein and its binding to the promoter region of the modABCD (molybdenum transport) operon of Escherichia coli.Eur J Biochem. 1997 May;246(1):119-26.PMID: 9210473Hall DR, Gourley DG, Leonard GA, Duke EM, Anderson LA, Boxer DH, Hunter WN.The high-resolution crystal structure of the molybdate-dependent transcriptional regulator (ModE) from Escherichia coli: a novel combination of domain folds.EMBO J. 1999 Mar;18(6):1435-46.PMID: 10075916Self WT, Grunden AM, Hasona A, Shanmugam KT.Molybdate transport.Res Microbiol. 152(3-4):311-21.PMID: 11421278","","Tue Mar 16 14:25:51 2004","1","","","" "AA01784","1203965","1205359","1395","ATGATTACACCACTTTTTACTCCATCACAGAAAAGCAAAATAAACAAGAAAAGTATGATTTTCGTTATTGATGTCATTCTTTTTGTCATTCTTCTTAATGTGCTTCCCTTTGATGAACAAGCCAATCGCGGTTTGGCATTATTGGCGTTTGTCGGCATTTTATGGTTAACCGAGGCCATAAATGTTAGCGTAACCGCCCTTTTTGTACCGATTTTATCCGTAGGACTTGGCTTGGTAAACAGCCGAGAGGCGCTGGTAGCATTTGCCGATCCGACGATTTTTCTGTTCTTTGGCGGTTTTGCATTGGCAACAGCGTTAAATGTACAGAAAATCGATAAAATGATTGCCAATAAAATCATGCATTTGGCAAGAGGCCGTTTATTTATCGCTGTTATGTATATTTTCTTCGCCACCGCCTTTTTATCCATGTGGATGAGTAATACAGCTACCGCCGCCATGATGATCCCGCTTTCCATGAGTATTCTGAGTCAAATGGATCGCCAAAAAGAGCATAATACTTATGTCTTCGTATTGCTCGGTATTGCTTACAGCGCCAGTATCGGCGGCATGGGTACCTTGGTAGGTAGTCCGCCAAACGCTATAGCCGCCTCCCAATTACACCTCAGTTTTGCCGATTGGTTAAAATATGGCTTACCTATGATGTTATTACTGTTTCCAATCATTATCGGCTGGCTTTACATTATTTTCCGCCCACGTTTGAATTTACGTTTTGATGTTCAATTTGAACAAATGAAAATGGATAACAAACGCTGGTTAACCTTAGTGATTTTTGCCCTTGTCGCTTCACTATGGATTTTCAGTAAACAATTGAATTCTGCGCTGACTGTATTACTCGGATTACCGAAAGCTATCGAAAGTATAGACAGCATGATTGCTCTGTGTGCCGCCGTGGTTATTTGTGTTAGCGGTATTGCTACTTGGAAAGAAATTCAATCGAACACCGAATGGGGCGTGCTGTTTTTATTCGGCGGCGGTTTAACCCTGAGTTCTGTCTTGGAAAACTCCGGTGCAAGTAAAATTATGGCAGATGGCATTGTCTATTTAATCAACGGCGGACACACTTATGTTATGGCACTGATTATCGCTGCCTTTATCGTTTGCTTAACCGAATTTACTTCTAACACTGCCAGCGCGGCGCTGCTAGTGCCGATTTTCATCTCTATTGCACACGCACTAAATATGTCACCGCTCGGGTTTGCCATGATTATCGGTTTGGGTGCATCCTGTGCTTTTATGTTGCCGGTAGGTACACCACCGAATGCCATTGTATACGGTACGGGTAACGTAAAACAAAGTGATATGATTCGGGTCGGCAAATATATTGACATCACTTGTATACTTGTCATTGCCACCATCGCGTGTATTTTCTGGATG","","","50633","MITPLFTPSQKSKINKKSMIFVIDVILFVILLNVLPFDEQANRGLALLAFVGILWLTEAINVSVTALFVPILSVGLGLVNSREALVAFADPTIFLFFGGFALATALNVQKIDKMIANKIMHLARGRLFIAVMYIFFATAFLSMWMSNTATAAMMIPLSMSILSQMDRQKEHNTYVFVLLGIAYSASIGGMGTLVGSPPNAIAASQLHLSFADWLKYGLPMMLLLFPIIIGWLYIIFRPRLNLRFDVQFEQMKMDNKRWLTLVIFALVASLWIFSKQLNSALTVLLGLPKAIESIDSMIALCAAVVICVSGIATWKEIQSNTEWGVLFLFGGGLTLSSVLENSGASKIMADGIVYLINGGHTYVMALIIAAFIVCLTEFTSNTASAALLVPIFISIAHALNMSPLGFAMIIGLGASCAFMLPVGTPPNAIVYGTGNVKQSDMIRVGKYIDITCILVIATIACIFWM","1205358","","sodium-dependent transporter","Inner membrane, Cytoplasm","","
InterPro
IPR001898
Family
Sodium/sulphate symporter
PF00939\"[310-465]TNa_sulph_symp
TIGR00785\"[36-464]Tdass: transporter, divalent anion:Na+ sympo
PS01271\"[414-430]TNA_SULFATE
noIPR
unintegrated
unintegrated
PTHR10283\"[38-460]TCATION TRANSPORTER RELATED
PTHR10283:SF37\"[38-460]TSODIUM/DICARBOXYLATE COTRANSPORTER-RELATED
signalp\"[1-59]?signal-peptide
tmhmm\"[19-37]?\"[47-79]?\"[85-107]?\"[122-140]?\"[146-164]?\"[174-194]?\"[216-236]?\"[257-275]?\"[294-314]?\"[324-344]?\"[354-374]?\"[379-397]?\"[403-423]?\"[444-464]?transmembrane_regions


","BeTs to 16 clades of COG0471COG name: Di- and tricarboxylate transportersFunctional Class: PThe phylogenetic pattern of COG0471 is -om-k-yq-d-lbcefghsnu--i--Number of proteins in this genome belonging to this COG is","Significant hit (1.9e-116) to 8/8 blocks of the IPB001898 family, which is described as \"Sodium:sulfate symporter family\". Interpro entry for IP:IPR001898. IPB001898A 55-78 9.4e-08 IPB001898B 94-120 4.3e-11 IPB001898C 138-157 2.1e-16 IPB001898D 177-201 3.9e-17 IPB001898E 208-232 2.6e-10 IPB001898F 250-276 0.00011 IPB001898G 320-349 1.2e-10 IPB001898H 402-450 1e-28 IPB001898B 327-353 0.22 IPB001898C 372-391 0.075 IPB001898G 87-116 0.11 IPB001898H 174-222 0.088","Residues 385 to 464 match (4e-07) PD:PD574152 which is described as TRANSMEMBRANE CHROMOSOME III X K08E5.2 F31F6.6 CG4961 GH13033P B0285.6 R107.1 ","","","","","","","","","","","","Wed Jan 8 08:31:48 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01784 is paralogously related to AA00136 (0.0), AA00941 (9e-23), AA00741 (3e-14), AA00615 (4e-10), AA00143 (2e-05), AA02387 (1e-04) and AA02254 (7e-04).","","","","","","Residues 11 to 465 (E-value = 7.5e-14) place AA01784 in the Na_sulph_symp family which is described as Sodium:sulfate symporter transmembrane region (PF00939)","","","","","","","","1","","","" "AA01787","1206025","1205432","594","ATGGATCGAATAAAAACCAGCCATTTTTTTGCCTGTTTGGATCGCTTGAGATTGATTCAGCGCTGGTCGCTTATGCGTAATATTGAACGGGAAAATCTGGCGGAACATAGCTTACAGGTGGCATTTGTCGGGCATGCCTTAGCCTTAATTAAAAATCGTTTTTACGGTGCACAACTGAATGCAGAGCGCATTGCGGTGATGGCGATGTATCACGACACATCGGAAATTTTTACCGGCGATCTGCCGACACCGATCAAATATTTCAATGAAGAGATTACCCATGCTTACAAACAAATTGAGACCGCTGCCGAGTTGCATTTGATCAGTTTGTTGCCGGAAGAATTGCAGGCAGATTTTTTACCCTATCTGGATAGTCACTATTTTTCGGATGATGAAAAACATATTGTGAAACAGGCAGATTTAATCTGTGCTTATATCAAGGTGAAATTTGAACTGGGAAATGGTAATCAGGAATTTAGATCGGCAAAAGTGCGGTTAGAAAATCTGATGGATCAGTGGCGAAGCCCGGAAATGGATTATTTTTTACAGGTGTTTGTGCCGAGTTTTGGTAAGTCTATTGATGAAATTACCTTG","","","23147","MDRIKTSHFFACLDRLRLIQRWSLMRNIERENLAEHSLQVAFVGHALALIKNRFYGAQLNAERIAVMAMYHDTSEIFTGDLPTPIKYFNEEITHAYKQIETAAELHLISLLPEELQADFLPYLDSHYFSDDEKHIVKQADLICAYIKVKFELGNGNQEFRSAKVRLENLMDQWRSPEMDYFLQVFVPSFGKSIDEITL","1205431","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003607
Domain
Metal-dependent phosphohydrolase, HD region
SM00471\"[29-154]THDc
InterPro
IPR006674
Domain
Metal-dependent phosphohydrolase, HD region, subdomain
PF01966\"[33-145]THD
noIPR
unintegrated
unintegrated
G3DSA:1.10.3210.10\"[5-192]Tno description
PTHR11845\"[9-120]TUNCHARACTERIZED


","BeTs to 10 clades of COG1896COG name: Predicted hydrolases of HD superfamilyFunctional Class: RThe phylogenetic pattern of COG1896 is ao--kzy--d----efgh--u-----Number of proteins in this genome belonging to this COG is","","Residues 22 to 82 match (6e-20) PD:PD009535 which is described as PROTEOME COMPLETE HYDROLASE A SUPERFAMILY BIOSYNTHETIC HD PLASMID OXETANOCIN PAE1004 ","","","","","","","","","","","","Wed Jan 8 08:33:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01787 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 33 to 145 (E-value = 3.9e-10) place AA01787 in the HD family which is described as HD domain (PF01966)","","","","","","","","1","","","" "AA01789","1207062","1206037","1026","ATGTTAAAAAAAATCTTACATTCCGCACTCATCGGTTTGGTTACGGCAGGTGTGATTTTGTTTGTGCTACCGAAAATCACCGGGAAATCCGTGTTACCGGAGCAAGAAATCGCCTCTTATAAAGATGCAGTGCGTATTGCTTCGCCGGCGGTTGTGAACGTTTATAATCAGGCGTTTACTTCTTCGTCCGCGCAATTGCAGGTGAATAACCTCGGTTCGGGCGTGATCATGTCAAAAGACGGTTATATTCTGACGAACAAACACGTTATTCAAAATGCCGATCAAATTGTAGTAGCGTTGCAAAACGGGCATATTTTTGATGCGGCGCTCATTGGTTCCGATTCTTTAACGGATTTGGCAGTATTAAAAATTAAAGCGGATAATTTATCCACGATTCCGCAAAATCTCAGCCGTCCGGTGCATGTGGGAGATGTGGCGCTGGCAATCGGCAATCCGTATAACCTGGGGCAAAGCGTGTCACAGGGGATTATCAGTGCGGTGGGACGTAGCGCGGTGGGTGAGGCGCTCGGGCGACAAAACTTCATTCAAACAGACGCCTCTATTAACCGTGGGAATTCCGGTGGCGCGTTGATTAATTCCGCCGGCGAACTGGTGGGCATCAGCACGTTGAGTATCGGTAAAACCTCCAATGAAATTGCCGAAGGTCTTAATTTTGCCATTCCTATTGACTTGGCAAATGATGTGATGAAAAAAATTATTCGTGACGGACGAGTGATTCGCGGCTATTTCGGCGTGCAAACGGATATTTTGTTTAGCAACGGACAAGGTTCTTCCGAACGCGGGATTTTAATTACCGGCGTCATTGAAAACAGCCCGGCGGCGAAAGCCGGATTACAAGCCGGCGATATTATTTTGAAAATCAATAAGGTAGAGGCCCATTCACCGACAGAAATGATGAAACTGATTGCCGATGTGCGCCCGAATACGAAAGTTGAAGTGGAAATATCCCGCTTAGGTAAAACTTATAAACTTCCGGTAATTATTGAAGAATATACATTTAATCAA","","","36175","MLKKILHSALIGLVTAGVILFVLPKITGKSVLPEQEIASYKDAVRIASPAVVNVYNQAFTSSSAQLQVNNLGSGVIMSKDGYILTNKHVIQNADQIVVALQNGHIFDAALIGSDSLTDLAVLKIKADNLSTIPQNLSRPVHVGDVALAIGNPYNLGQSVSQGIISAVGRSAVGEALGRQNFIQTDASINRGNSGGALINSAGELVGISTLSIGKTSNEIAEGLNFAIPIDLANDVMKKIIRDGRVIRGYFGVQTDILFSNGQGSSERGILITGVIENSPAAKAGLQAGDIILKINKVEAHSPTEMMKLIADVRPNTKVEVEISRLGKTYKLPVIIEEYTFNQ","1206036","","protease DegS precursor; periplasmic serine endoprotease","Periplasm, Outer membrane, Cytoplasm","","
InterPro
IPR001254
Domain
Peptidase S1 and S6, chymotrypsin/Hap
PF00089\"[51-236]TTrypsin
InterPro
IPR001478
Domain
PDZ/DHR/GLGF
PF00595\"[238-323]TPDZ
SM00228\"[248-326]TPDZ
PS50106\"[239-324]TPDZ
InterPro
IPR001940
Family
Peptidase S1C, HrtA/DegP2/Q/S
PR00834\"[81-93]T\"[102-122]T\"[142-166]T\"[178-195]T\"[200-217]T\"[284-296]TPROTEASES2C
InterPro
IPR011783
Family
Peptidase S1C, DegS
TIGR02038\"[2-340]Tprotease_degS: periplasmic serine peptidase
noIPR
unintegrated
unintegrated
G3DSA:2.30.42.10\"[262-334]Tno description
G3DSA:2.40.10.10\"[40-125]T\"[133-252]Tno description
PTHR22939\"[34-338]TSERINE PROTEASE FAMILY S1C HTRA-RELATED
PTHR22939:SF10\"[34-338]TSERINE PROTEASE DO/HTRA-RELATED
signalp\"[1-16]?signal-peptide
tmhmm\"[5-23]?transmembrane_regions


","BeTs to 20 clades of COG0265COG name: Trypsin-like serine proteases, typically periplasmic, contain C-terminal PDZ domainFunctional Class: OThe phylogenetic pattern of COG0265 is -om---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.3e-07) to 2/2 blocks of the IPB000126 family, which is described as \"Serine proteases, V8 family\". Interpro entry for IP:IPR000126. IPB000126A 72-87 11 IPB000126B 183-199 5e-06","Residues 72 to 132 match (4e-09) PD:PD031752 which is described as PROTEASE SERINE HYDROLASE COMPLETE PROTEOME PRECURSOR 3.4.21.- SIGNAL PROBABLE BINDING ","","","","","","","","","","","","Wed Jan 8 08:39:21 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01789 is paralogously related to AA01869 (3e-51).","","","","","","Residues 238 to 323 (E-value = 1e-10) place AA01789 in the PDZ family which is described as PDZ domain (Also known as DHR or GLGF) (PF00595)","","","","","Vogel,R.F., Entian,K.D. and Mecke,D. Cloning and sequence of the mdh structural gene of Escherichia coli coding for malate dehydrogenase Arch. Microbiol. 149 (1), 36-42 (1987) PubMed: 3322223 Bazan,J.F. and Fletterick,R.J. Structural and catalytic models of trypsin-like viral proteases Semin. Virol. 1, 311-322 (1990)Waller,P.R. and Sauer,R.T. Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease J. Bacteriol. 178 (4), 1146-1153 (1996) PubMed: 8576051 Waller,P.R. and Sauer,R.T. Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease. J. Bacteriol. 178 (4): 1146-1153 (1996) [PubMed: 8576051].Bass,S., Gu,Q. and Christen,A. Multicopy suppressors of prc mutant Escherichia coli include two HtrA (DegP) protease homologs (HhoAB), DksA, and a truncated R1pA. J. Bacteriol. 178 (4): 1154-1161 (1996) [PubMed: 8576052].","","Wed Jan 8 08:39:21 2003","1","","","" "AA01790","1208195","1207074","1122","ATGGACGCACAATTTAGCCCGCAAGATGTCGCTTTTATGCAACTCGCCCTGGATTTAGCCAAACAGGGCGAATTTACCACCACACCGAATCCTTCGGTGGGATGCGTGTTGGTAAAAAACGGCAAAATTGTGGGCAAAGGTTTCCATTTTAAAGCGGGCGAACCCCATGCCGAAGTGATGGCATTGCGTGAAGCCGGTGAAAATGCCCGTGGTGCCACGGCGTATGTGACCCTTGAGCCCTGTTCCCATTTCGGACGTACACCGCCTTGCGCCAAAGGGCTGGTGGAAGCCGGCGTAAGTAAGGTGATTGCCGCCATGTGCGATCCGAATCCGCAGGTAGCGGGCAAAGGATTACAGATTTTAGCGGATGCCGGCATTCAAAGTGCGGTAGGTTTATTAGAAGAAAAAGCGGAACAGCTTAACAAAGGTTTCTTAAAACGGATGCGTACGGGCAAGCCTTTCGTGCAGTTAAAATTGGCTATGAGCATTGATGGCAAAACCGCCATGGCGAGCGGCGAAAGCAAATGGATCACCGGCGCACAGGCAAGAATGGATGTGCAACAATATCGTGCCAAAGCTTCGGCGATGTTATCTACCTCACAAACGGTACTGGCGGACGATCCGAGTTTAAATGTGCGTTGGGCTGAATTGCCAAATGAAACACAAGCCCGCTACGTACAGGAAAATTTACGCCAGCCGGTACGCGTTATTTTGGATTCCACTCATAAAGTGCGGTCGGATTTTAAGGTGTTTTTAACGGATGCTCCTGTTTGGCTGGCAGGTGAGGATGACTTTCAACTAACGGGTTTTCCGGCGTCAACGGAATATTTAAAATTAGACCGAAGCCATGGCGAAAGCCGTTTACAGGCACTGATGACAGAATTGGGCAAACGTCAGATCAATACGCTTTGGGTCGAAGCGGGTGCCACCTTAGCCGGCGCGCTAATTGCCGAAAACCTGGTAGATGAATTAATCATCTATATGGCGCCAAAACTGTTAGGCGATCACGCCAAAGATTTATGTCATTTGCCCCATTTAACCCGACTCGCCGACGCGCCTTTATGGCAATTGCAATCTTGTGAACCTACCGGCGACGATCTTAAATTAATTTATATAAGAAAA","","","40752","MDAQFSPQDVAFMQLALDLAKQGEFTTTPNPSVGCVLVKNGKIVGKGFHFKAGEPHAEVMALREAGENARGATAYVTLEPCSHFGRTPPCAKGLVEAGVSKVIAAMCDPNPQVAGKGLQILADAGIQSAVGLLEEKAEQLNKGFLKRMRTGKPFVQLKLAMSIDGKTAMASGESKWITGAQARMDVQQYRAKASAMLSTSQTVLADDPSLNVRWAELPNETQARYVQENLRQPVRVILDSTHKVRSDFKVFLTDAPVWLAGEDDFQLTGFPASTEYLKLDRSHGESRLQALMTELGKRQINTLWVEAGATLAGALIAENLVDELIIYMAPKLLGDHAKDLCHLPHLTRLADAPLWQLQSCEPTGDDLKLIYIRK","1207073","[FUNCTION] Converts 2,5-diamino-6-(ribosylamino)-4(3H)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1H,3H)-pyrimidinedione 5'-phosphate. [CATALYTIC ACTIVITY] 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + h(2)o = 5-amino-6-(5-phosphoribosylamino)uracil + nh(3). [CATALYTIC ACTIVITY] 5-amino-6-(5-phosphoribitylamino)uracil + NADP(+) = 5-amino-6-(5-phosphoribosylamino)uracil + NADPH. [COFACTOR] Zinc (by similarity). [PATHWAY] Riboflavin biosynthesis; second step. [PATHWAY] Riboflavin biosynthesis; third step. [SIMILARITY] In the N-terminal section; belongs to the cytidine and deoxycytidylate deaminases family. [SIMILARITY] in the C-terminal section; belongs to the htp reductase family. ","riboflavin bifunctional biosynthesis protein","Cytoplasm, Periplasm","","
InterPro
IPR002125
Domain
CMP/dCMP deaminase, zinc-binding
PF00383\"[6-106]TdCMP_cyt_deam_1
PS00903\"[56-94]TCYT_DCMP_DEAMINASES
InterPro
IPR002734
Domain
Bacterial bifunctional deaminase-reductase, C-terminal
PF01872\"[153-369]TRibD_C
InterPro
IPR004794
Family
Riboflavin biosynthesis protein RibD
PTHR11079:SF10\"[8-335]TRIBOFLAVIN-SPECIFIC DEAMINASE
TIGR00326\"[13-370]Teubact_ribD: riboflavin biosynthesis protei
InterPro
IPR011549
Domain
Riboflavin-specific deaminase, C-terminal
TIGR00227\"[151-373]TribD_Cterm: riboflavin-specific deaminase C
noIPR
unintegrated
unintegrated
G3DSA:3.40.140.10\"[7-150]Tno description
PTHR11079\"[8-335]TCYTOSINE DEAMINASE


","BeTs to 8 clades of COG1985COG name: Pyrimidine reductase, riboflavin biosynthesisFunctional Class: HThe phylogenetic pattern of COG1985 is aom--zyqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is","Significant hit (3.8e-100) to 7/7 blocks of the IPB002734 family, which is described as \"RibD/ribG C-terminal domain\". Interpro entry for IP:IPR002734. IPB002734A 29-39 4e-06 IPB002734B 56-90 1.3e-33 IPB002734C 114-125 0.019 IPB002734D 157-166 0.00096 IPB002734E 172-213 3.3e-25 IPB002734F 232-241 0.01 IPB002734G 303-335 7.9e-18Significant hit ( 4.8e-05) to 1/1 blocks of the IPB002125 family, which is described as \"Cytidine and deoxycytidylate deaminase zinc-binding region\". Interpro entry for IP:IPR002125. IPB002125 71-81 4.9e-05","Residues 12 to 54 match (1e-14) PD:PD009434 which is described as DEAMINASE COMPLETE PROTEOME REDUCTASE RIBOFLAVIN RIBOFLAVIN-SPECIFIC BIOSYNTHESIS RIBD DIAMINOHYDROXYPHOSPHORIBOSYLAMINOPYRIMIDINE HTP ","","","","","","","","","","","Wed Jan 8 08:46:54 2003","Wed Jan 8 08:46:54 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01790 is paralogously related to AA00198 (4e-08).","","","","","","Residues 153 to 369 (E-value = 7.7e-70) place AA01790 in the RibD_C family which is described as RibD C-terminal domain (PF01872)","","","","","Fuller,T.E. and Mulks,M.H. Characterization of Actinobacillus pleuropneumoniae riboflavin biosynthesis genes J. Bacteriol. 177 (24), 7265-7270 (1995) PubMed: 8522537 Mironov,V.N., Perumov,D.A., Kraev,A.S., Stepanov,A.I. and Skriabin,K.G. Unusual structure of the regulatory region of the riboflavin biosynthesis operon in Bacillus subtilis Mol. Biol. (Mosk.) 24 (1), 256-261 (1990) PubMed: 2112225 Richter,G., Fischer,M., Krieger,C., Eberhardt,S., Luttgen,H., Gerstenschlager,I. and Bacher,A. Biosynthesis of riboflavin: characterization of the bifunctional deaminase-reductase of Escherichia coli and Bacillus subtilis J. Bacteriol. 179 (6), 2022-2028 (1997) PubMed: 9068650 ","","Wed Jan 8 08:46:54 2003","1","","","" "AA01792","1208647","1208198","450","ATGCGTTGTCCTTTTTGTTCAACGGAAGAAACCAAAGTCATTGACAGTCGTTTGGTTTCCGATGGTTTTCAGGTGCGTCGGCGCAGAGAGTGCGGTCAGTGTCACGAGCGTTTTACCACCTTTGAAACGGCGGAATTAATCGTGCCGAAAATTATTAAAAATAACGGTAATCGCGAGCCGTTTAACGAAGACAAATTACGTCGCGGCATTCAGCACGCGCTGGAAAAACGCCCGGTTAGCTCCGACGACGTGGAAAAGGCAATTAGCCGTATTATTCACCAATTACGCGCCACCGGCGAGCGTGAAGTGCCAAGTAAATTGGTGGGTACGCTTGTGATGGACGAGTTAAAAAATCTGGATAAAGTGGCGTATATCCGTTTTGCGTCCGTGTATTTGAGCTTTGATAACATTAATGAATTTAGCCAAGAAATCGAAAACCTCAAGGATCAA","","","17413","MRCPFCSTEETKVIDSRLVSDGFQVRRRRECGQCHERFTTFETAELIVPKIIKNNGNREPFNEDKLRRGIQHALEKRPVSSDDVEKAISRIIHQLRATGEREVPSKLVGTLVMDELKNLDKVAYIRFASVYLSFDNINEFSQEIENLKDQ","1208197","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003796
Family
Ribonucleotide reductase regulator NrdR-like
TIGR00244\"[1-147]TTIGR00244: transcriptional regulator, NrdR
InterPro
IPR005144
Domain
ATP-cone
PF03477\"[49-139]TATP-cone
PS51161\"[49-139]TATP_CONE


","BeTs to 12 clades of COG1327COG name: Predicted transcriptional regulator, consists of a Zn-ribbon and ATP-cone domainsFunctional Class: KThe phylogenetic pattern of COG1327 is --------vdrlbcefghsn-j-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 1e-71) to 2/2 blocks of the IPB003796 family, which is described as \"DUF193\". Interpro entry for IP:IPR003796. IPB003796A 26-80 1.3e-39 IPB003796B 101-149 4e-31 IPB003796A 23-77 0.61","Residues 45 to 141 match (3e-10) PD:PD480941 which is described as PROTEOME COMPLETE NMA0645 NMB1816 ","","","","","","","","","","","","Wed Jan 8 08:49:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01792 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 49 to 139 (E-value = 2e-31) place AA01792 in the ATP-cone family which is described as ATP cone domain (PF03477)","","","","","","","","1","","","" "AA01793","1209921","1208767","1155","ATGAACGAATCGTCGCGTTCCGTTCCTGGATTATTCAAACTATCAATCAAGAAGAAAATAAACAAGAAAATGAATAAGTTGGCATTATATTGTCGAATGGGCTTTGAGCGCGAGCTGGCGGCAGAAATCACCGATAAAGCGGCGGAAAAGGGCGTGTTTGGATTTGCCCGCATGGCGGAAAACAGCGGCTATGTGATATTTGAATGCTATCAGCCCGGCGATGCCGATTTATTGGCGCGTGAGTTGCCTTTTCAACAGCTGATTTTCGCCCGTCAAATGTTGGTGGTGTCCGATTTATTAACGGATTTACCGCAACAGGATCGCATCACGCCGATTGTTCACCAATATCAACAAATTGCCGATACCATTGCGTTGAAAAACAGCAGTGAATTATGGGTGGAAACCGCCGATACCAACGAAGCAAAGGAATTACTCGGATTTTGTCGCAAATTTACCGTGCCGTTGCGTCAAGCGTTGAAAAAGCAAGGCTGGCTGAATGCCAAACCTAATCAAAAGTGCGGTCTGACATTACATCTTTTTTTCTTACGCAATAACGCCTGCTATGTGGGCTATTCCTATAATCACAACCATTCCGCGCATTTGATGGGCATTCAGCGCTTAAAATTTCCCGCCGAGGCGCCAAGTCGTTCTACGCTGAAACTGGAAGAGGCGATTTTAACCTTCATTTCGCGCCACCAAGAACCGGAATTGCTTAATGAGACGATGTATGCCGTGGATCTCGGCGCTTGCCCGGGTGGCTGGACCTATCAATTGGTGAAGCGCGGTTTATTTGTGTATGCGGTGGATCACGGCAAAATGGCGGCAAGTCTGCACGAGACGGGGCGCATTGAACATTGTGCGGAAGACGGGTTTAAATTTCAGCCGCCGAAGCGACGTAAAATCGATTGGCTGGTGTGCGATATGGTGGAGCAACCGAGCCGAATTGCGGAACTGATGACCAAATGGCTGCTCAACGGCTGGTGCCACAGCATGATTTTCAACCTAAAACTGCCGATGAAAAAACGCTATGCCCAAGTACAACAATGCCTGCAACTGATTGCGGATAAATTGTCGCAACAAGGCTTAAAATATCGGTTACAGGCAAAACATTTGTATCATGATCGTGAAGAAATTACCGTTTATCTTCGATTGTTG","","","46869","MNESSRSVPGLFKLSIKKKINKKMNKLALYCRMGFERELAAEITDKAAEKGVFGFARMAENSGYVIFECYQPGDADLLARELPFQQLIFARQMLVVSDLLTDLPQQDRITPIVHQYQQIADTIALKNSSELWVETADTNEAKELLGFCRKFTVPLRQALKKQGWLNAKPNQKCGLTLHLFFLRNNACYVGYSYNHNHSAHLMGIQRLKFPAEAPSRSTLKLEEAILTFISRHQEPELLNETMYAVDLGACPGGWTYQLVKRGLFVYAVDHGKMAASLHETGRIEHCAEDGFKFQPPKRRKIDWLVCDMVEQPSRIAELMTKWLLNGWCHSMIFNLKLPMKKRYAQVQQCLQLIADKLSQQGLKYRLQAKHLYHDREEITVYLRLL","1208766","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR002877
Domain
Ribosomal RNA methyltransferase RrmJ/FtsJ
PF01728\"[213-274]TFtsJ
InterPro
IPR011224
Family
YdgE, putative RNA 2'-O-ribose methyltranserase
PIRSF028774\"[24-385]TUncharacterised conserved protein


","BeTs to 4 clades of COG2933COG name: Predicted SAM-dependent methyltransferaseFunctional Class: RThe phylogenetic pattern of COG2933 is --------------ef-hs-------Number of proteins in this genome belonging to this COG is","","Residues 28 to 381 match (3e-162) PD:PD041763 which is described as PROTEOME COMPLETE METHYLTRANSFERASE HI1195 SAM-DEPENDENT XF0748 STY3120 YGDE PM0568 PA1563 ","","","","","","","","","","","","Wed Jan 8 08:50:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01793 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01794","1210750","1209848","903","ATGTATAAGCGTTTGCCACCGTTAAACTCGCTTAAAGCCTTTGAGGCCGCTGCCAGATTTTTAAGTTTCACCAAAGCGGCGGATGAGCTTTTTGTTACCCAAGCGGCGATTAGCCACCAAATTAAACTGCTGGAAGATTTTTTAGGCGTGGAACTCTTTAAACGAAAAAACCGCGCCCTGGAACTCACGGATTTCGGCAAAGCCTATTATGCCGATATTACGAAAATCCTTTTCCGTTTAGTGGAAGCCACCGATAAACTGCTTGCTTTAAAAACCGATAAACACTTAACCATCAGTGTGCCGCAAACCTTTGGGATTCAATGGTTAGTGCCGCGTTTGAGTGATTTTAATAGGCTACATCCCGATATTGAAGTGCGTTTAAAAGGCGTGGATCAGGATGAGGGTTTACTTAGCCAGGATATTGATATTGCCATTTATTACGGCAAGGGCAATTGGGATAACTTACAGCTGGATCGTCTGGTGGAGGAGGATTTATTGATTCTTGCTTCGCCGAAATTATTGGCGCAAAAACCGATTCATCATCGAGACGATTTAAAACATCATACGCTGCTGCATATTCACGCCCGTGACAATTGGCAACACATGGCGAATTATCTGGAACTGGAAGATTTAAATATTCAGCAAGGTCCGATTTTCAGCCACACGTTTATGGCGTTACAGGCGGCGATTCACGAGCAGGGCATTGTGCTTGCCAATCGAATTTTAGCGCAGCAAGAGCTGGATAACGGCAATTTACAGCCGGTTTTTGACACGAATTTACGCGATCCGAAATCCTTTTATGTCGTCAATCATTTGGATAACAACAAAGATGAACGAATCGTCGCGTTCCGTTCCTGGATTATTCAAACTATCAATCAAGAAGAAAATAAACAAGAAAATGAA","","","34846","MYKRLPPLNSLKAFEAAARFLSFTKAADELFVTQAAISHQIKLLEDFLGVELFKRKNRALELTDFGKAYYADITKILFRLVEATDKLLALKTDKHLTISVPQTFGIQWLVPRLSDFNRLHPDIEVRLKGVDQDEGLLSQDIDIAIYYGKGNWDNLQLDRLVEEDLLILASPKLLAQKPIHHRDDLKHHTLLHIHARDNWQHMANYLELEDLNIQQGPIFSHTFMALQAAIHEQGIVLANRILAQQELDNGNLQPVFDTNLRDPKSFYVVNHLDNNKDERIVAFRSWIIQTINQEENKQENE","1209847","[FUNCTION] Not known, the gcv operon regulated by the E.coli homolog does not exist in h.influenzae, so it probably acts as a transcriptional regulator on some other operon. [SUBCELLULAR LOCATION] Cytoplasmic.[SIMILARITY] Belongs to the lysR family of transcriptional ","glycine cleavage system transcription activator","Cytoplasm","","
InterPro
IPR000847
Domain
Bacterial regulatory protein, LysR
PR00039\"[23-34]T\"[34-44]T\"[44-55]THTHLYSR
PF00126\"[8-67]THTH_1
PS50931\"[6-63]THTH_LYSR
InterPro
IPR005119
Domain
LysR, substrate-binding
PF03466\"[89-292]TLysR_substrate
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[8-92]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[94-200]Tno description


","BeTs to 12 clades of COG0583COG name: Transcriptional regulatorFunctional Class: KThe phylogenetic pattern of COG0583 is a-m----q-drlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.8e-17) to 1/1 blocks of the IPB000847 family, which is described as \"Bacterial regulatory protein, LysR family\". Interpro entry for IP:IPR000847. IPB000847 22-55 1.7e-17Significant hit ( 4.9e-07) to 1/2 blocks of the IPB001583 family, which is described as \"NodD transcription activator carboxyl terminal region\". Interpro entry for IP:IPR001583. IPB001583A 10-60 4.5e-07","Residues 96 to 289 match (1e-08) PD:PD553665 which is described as PROBABLE PROTEOME ACTIVATOR LYSR-FAMILY PLASMID COMPLETE TRANSCRIPTIONAL ","","","","","","","","","","","Wed Jan 8 08:55:10 2003","Wed Jan 8 08:55:10 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01794 is paralogously related to AA00977 (8e-16), AA00940 (3e-14), AA00985 (2e-12), AA02539 (4e-12), AA00371 (2e-05), AA01999 (2e-05) and AA01513 (2e-05).","","","","","","Residues 89 to 292 (E-value = 6.8e-29) place AA01794 in the LysR_substrate family which is described as LysR substrate binding domain (PF03466)","","","","","Everett,M., Walsh,T., Guay,G. and Bennett,P. GcvA, a LysR-type transcriptional regulator protein, activates expression of the cloned Citrobacter freundii ampC beta-lactamase gene in Escherichia coli: cross-talk between DNA-binding proteins Microbiology 141 (Pt 2), 419-430 (1995) PubMed: 7704273 Wilson,R.L. and Stauffer,G.V. DNA sequence and characterization of GcvA, a LysR family regulatory protein for the Escherichia coli glycine cleavage enzyme system Journal of bacteriology. 176 (10), 2862-2868 (1994) PubMed: 8188587 ","","Wed Jan 8 08:55:10 2003","1","","","" "AA01796","1211212","1212228","1017","ATGTCAGACTTACTTGATTGGAAAAATCTCGGCTTCAGTTATATCAAAACGGATTATCGTTTCATCGCCCGCTGGAAAGAGGGCAAATGGAACAACGGTGAATTAAGCACCGACAGCACACTCCATATTCACGAAGGATCTACCGCACTTCACTACGGTCAACAATGTTTTGAAGGCTTAAAAGCTTACCGCTGTAAAGACGGTTCAATTAACCTTTTTCGCCCCGACCAAAATGCCAAACGTATGCAAAATACCTGCGATCGTTTATTAATGCCGCAAGTGCCTACCGAATTATTTATCCGCGCCTGTAAAGAAGTGGTGAAAGCTAATGAACGCTGGGTGGCACCTTACGGTACCGGAGCGACCTTATATTTGCGTCCGTTCGTGATCGGCGTGGGTGAAAACATCGGCGTGCGCCCGGCACCGGAATATATTTTCTGCGTATTCTGCTGCCCGGTCGGTGCTTATTTCAAAGGCGGCATGAAACCGTCCAATTTCCTGGTGACCGATTATGACCGCGCTGCACCGCACGGTACCGGTGGCGTGAAAGTGGGTGGAAACTACGCGGCAAGTTTGTTACCGCATGAACTTGCCGCCGAACGCAAATTCGCCGATGCCATCTATCTTGATCCGAAAACCCATACCAAAATTGAAGAAGTGGGCGCGGCAAACTTTTTCGGTATTACCCGCGATAACAAATTCATCACTCCGCTTTCTCCGTCTATTTTGCCAAGTATCACCAAATACTCGCTACTTTATTTAGCCAAAGAACGCTTAGGTATGGAAACTATTGAAGGCGATGTGTATATCAACGAACTCGGTCAATTTACCGAAGCCGGTGCTTGCGGAACTGCCGCCGTTATCTCCCCAATCGGCGGAATCCAATACGGCGATGATTTCCACGTTTTCTATTCCGAAACCGAAGTGGGTCCAGTCACCAAACGCCTTTACGACGAACTCACCGGCATCCAATTCGGTGACGTGGAAGCGCCGGAAGGTTGGATTGTAAAAGTGAAT","","","37647","MSDLLDWKNLGFSYIKTDYRFIARWKEGKWNNGELSTDSTLHIHEGSTALHYGQQCFEGLKAYRCKDGSINLFRPDQNAKRMQNTCDRLLMPQVPTELFIRACKEVVKANERWVAPYGTGATLYLRPFVIGVGENIGVRPAPEYIFCVFCCPVGAYFKGGMKPSNFLVTDYDRAAPHGTGGVKVGGNYAASLLPHELAAERKFADAIYLDPKTHTKIEEVGAANFFGITRDNKFITPLSPSILPSITKYSLLYLAKERLGMETIEGDVYINELGQFTEAGACGTAAVISPIGGIQYGDDFHVFYSETEVGPVTKRLYDELTGIQFGDVEAPEGWIVKVN","1212227","[FUNCTION] Acts on leucine, isoleucine and valine (By similarity).[CATALYTIC ACTIVITY] L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate.[COFACTOR] Pyridoxal phosphate. [PATHWAY] Valine and isoleucine biosynthesis.","branched-chain amino acid aminotransferase","Cytoplasm","","
InterPro
IPR001544
Family
Aminotransferase, class IV
PD001961\"[203-319]TQ8E507_STRA3_Q8E507;
PTHR11825\"[15-339]TSUBGROUP IIII AMINOTRANSFERASE
PF01063\"[32-321]TAminotran_4
PS00770\"[219-248]?AA_TRANSFER_CLASS_4
InterPro
IPR005786
Family
Branched-chain amino acid aminotransferase II
PIRSF006468\"[1-339]TBranched-chain amino acid aminotransferase, BCAT1 type
PTHR11825:SF2\"[15-339]TBRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE
TIGR01123\"[30-338]TilvE_II: branched-chain amino acid aminotra
noIPR
unintegrated
unintegrated
G3DSA:3.20.10.10\"[187-318]Tno description
G3DSA:3.30.470.10\"[5-177]Tno description


","BeTs to 19 clades of COG0115COG name: Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyaseFunctional Class: E,HThe phylogenetic pattern of COG0115 is aom---yqvdrlbcefghsnujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 4.6e-40) to 6/6 blocks of the IPB001544 family, which is described as \"Aminotransferases class-IV\". Interpro entry for IP:IPR001544. IPB001544A 50-61 2.6e-07 IPB001544B 72-86 5e-06 IPB001544C 124-138 0.00025 IPB001544D 178-188 0.0012 IPB001544E 242-257 1.9e-05 IPB001544F 278-291 8.5e-05 IPB001544E 224-239 0.61","Residues 157 to 216 match (1e-09) PD:PD541388 which is described as ILVE PROTEOME BRANCHED-CHAIN-AMINO-ACID COMPLETE TRANSAMINASE ","","","","","","","","","","","Wed Jan 8 09:00:11 2003","Wed Jan 8 09:00:11 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01796 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 32 to 321 (E-value = 2.5e-125) place AA01796 in the Aminotran_4 family which is described as Aminotransferase class IV (PF01063)","","","","","","","","1","","","" "AA01798","1212210","1212395","186","TTGGATTGTAAAAGTGAATTAATTCCCGGCTACTACAGAACACAAAAGTGCGGCGGAAAAACACGGTATTTTTCTACCGCACTTTTGTGTCAGTTTAAATTGATCATACTAGATAACATACGAATTAAAAATCAATTTAAAATCCTCCTTATGCTTTTGCATTCACAAACCCAACAACTTACTTTA","","","7246","LDCKSELIPGYYRTQKCGGKTRYFSTALLCQFKLIILDNIRIKNQFKILLMLLHSQTQQLTL","1212394","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Jan 8 09:02:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01798 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01799","1212599","1213336","738","ATGTTAAAAACCTTAAGTAAACTTATCTCATCTTCGATTTCTATGGCTTTTTTAGTCGTTTTGGGTTGGTCAGTAGCTTACGGCTATGGCTGGGGACAATCTTATTTTTATGGCTTCCCATGGTGGTATGTAGATGTGGGCACCGGTAATGTAGCACGTAGTTTCGGTTATGTAATTTGGGTAAGTATTATCCTCTTGGCAACTTATTTAGTTGGCTTGTTTGGGTTAAAAAAAGCCAGACCATTCATGACCGATTACTGCATGAATCTGTTGCGGACTTATATTCTGTGTAATGTCTTCTTTATTCCGGTTATTCTTGGTTACATCCTGACAGTTGGAAAAGTTAATTATCTTTTCGCAATCTTCTATATTGGCATTACTTTTATCTTTACTCTTTTGTTTAAAAATTATATTCACAAGCACATCGGTACGATTTCTATCAACACGACTCTCGCGTTTTTATATAAAAATAAAATTTATGTGATGTTGGCTACCTATTGTTATTTTGTAATATGTGCGTTTATCGTCGGATATTCCCGCCCACATTTCAAAACAGTATTTGACTCATTAGAAATTGAAGGCAAAGCCTATTACGTATTAGCAAAATACAGTGACACTTTTATCTTAGCGAAAAGTACTCGTGCTACTAATGACAGTTTTTATCTTTATAAAATGAATATTAATTTTTTATGTCGTGTCAGAGTGGTTAATACACATAATGCTTTAATACAACCTGAC","","","28363","MLKTLSKLISSSISMAFLVVLGWSVAYGYGWGQSYFYGFPWWYVDVGTGNVARSFGYVIWVSIILLATYLVGLFGLKKARPFMTDYCMNLLRTYILCNVFFIPVILGYILTVGKVNYLFAIFYIGITFIFTLLFKNYIHKHIGTISINTTLAFLYKNKIYVMLATYCYFVICAFIVGYSRPHFKTVFDSLEIEGKAYYVLAKYSDTFILAKSTRATNDSFYLYKMNINFLCRVRVVNTHNALIQPD","1213335","This gene has a potential transcription terminator (1687-1714) but no known promoter, it may be transcribed off the pilin subunit gene promoter ","polysacharide biosynthesis protein (Orf14 of cluster)","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-28]?signal-peptide
tmhmm\"[15-35]?\"[54-74]?\"[94-112]?\"[118-138]?\"[159-179]?transmembrane_regions


","No hits to the COGs database.","","Residues 189 to 246 match (4e-13) PD:PD256794 which is described as ORF14 ","","","","","","","","","","","Wed Jan 8 09:06:32 2003","Thu Feb 20 08:00:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01799 is paralogously related to AA02620 (1e-117).","","","","","","","","","","Nakano,Y., Yoshida,Y., Suzuki,N., Yamashita,Y. and Koga,T.A gene cluster for the synthesis of serotype d-specificpolysaccharide antigen in Actinobacillus actinomycetemcomitansBiochim. Biophys. Acta 1493 (1-2), 259-263 (2000)PubMed: 20435309","Fulks,K.A., Marrs,C.F., Stevens,S.P. and Green,M.R. Sequence analysis of the inversion region containing the pilin genes of Moraxella bovis. J. Bacteriol. 172 (1): 310-316 (1990) PubMed: 2403542.Rozsa,F.W. and Marrs,C.F. Interesting sequence differences between the pilin gene inversion regions of Moraxella lacunata ATCC 17956 and Moraxella bovis Epp63. J. Bacteriol. 173 (13): 4000-4006 (1991) PubMed: 2061282.","Thu Feb 20 08:00:44 2003","Thu Feb 20 08:00:44 2003","1","","","" "AA01800","1213351","1213518","168","GTGCATTTTAGCCATTTCTCATATTCTACGTATTCCCAGATAGAGAAAATCCCCGTTCAAGCGGGGATTTTCTCGATAGGGAACGAAAGCAATAAAAACGCAGAAAATATTCACCGCACTTTTTATGCTATGCCCAAGGTCAGCCTATGGATTAATAAACTTCTCACC","","","6441","VHFSHFSYSTYSQIEKIPVQAGIFSIGNESNKNAENIHRTFYAMPKVSLWINKLLT","1213518","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 10:45:17 2004","Thu Feb 26 10:45:17 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01800 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 10:45:17 2004","","","","","","","","","","","","","1","","","" "AA01801","1214430","1213498","933","ATGAAAGTTGCTGTTTTAGGTGCCGCAGGCGGTATCGGTCAAGCATTGGCATTATTACTGAAGTTACAACTGCCGGCAGGTTCCGAATTGTCACTTTATGATATTGCGCCGGTTACTCCGGGTGTTGCGGTGGATGTGAGCCACATTCCTACGGCGGTGAAAATTGAAGGCTTTGGCGGTGAAGATCCGACACCTGCGCTTAAAGGCGCGGATGTGGTGTTAATTTCTGCCGGTGTGGCGCGTAAACCGGGTATGGATCGCTCCGATTTATTCAACATTAATGCAGGTATCGTGCGTAATTTAATCGAAAAAGTGGCAATAACTTGTCCGAAAGCCTGTATCGGTATCATCACCAACCCGGTCAATACCACAGTTGCTATCGCGGCGGAAGTGTTGAAAAAAGCCGGTGTTTATGACAAGCGTAAATTATTCGGCGTGACCACCTTGGATGTGCTTCGTTCCGAAACTTTCGTTTCCGAATTAAAAGGCTTAAATGCTTATCGCACCACCGTGCCTGTCATCGGCGGACACTCCGGTGTGACTATTCTTCCGTTATTATCTCAAGTGCAATACGTTGAATGGAAAGAGGACGAAATTGAACCGTTAACCAAACGCATTCAAAATGCCGGCACCGAAGTAGTAAACGCGAAAGCCGGCGGCGGTTCCGCAACCTTATCCATGGCGCAGGCGGCAGCCCGTTTTGCTAATGCTGTAGTCCGCGGTTTACAAGGTGAAACCGTCGTAGAATGCAGCTATGTGGAAGGCGACGGCAAATACGCCCGCTTCTTCGCACAACCGGTTCGCTTCGGCAAGGAAGGTGTGGAAGAAATCCTACCAATCGGTAAACTCAGCGCCTTGGAACAACAGGCTTTAGAAACCATGTTACCGACATTGCGTGCAGATATTGAATTAGGTGAGAAGTTTATTAATCCA","","","35884","MKVAVLGAAGGIGQALALLLKLQLPAGSELSLYDIAPVTPGVAVDVSHIPTAVKIEGFGGEDPTPALKGADVVLISAGVARKPGMDRSDLFNINAGIVRNLIEKVAITCPKACIGIITNPVNTTVAIAAEVLKKAGVYDKRKLFGVTTLDVLRSETFVSELKGLNAYRTTVPVIGGHSGVTILPLLSQVQYVEWKEDEIEPLTKRIQNAGTEVVNAKAGGGSATLSMAQAAARFANAVVRGLQGETVVECSYVEGDGKYARFFAQPVRFGKEGVEEILPIGKLSALEQQALETMLPTLRADIELGEKFINP","1213497","[CATALYTIC ACTIVITY] (S)-malate + NAD(+) = oxaloacetate + NADH.[SUBUNIT] Homodimer (By similarity).","malate dehydrogenase","Periplasm, Cytoplasm","","
InterPro
IPR001236
Family
Lactate/malate dehydrogenase
G3DSA:3.90.110.10\"[147-311]Tno description
PF00056\"[1-145]TLdh_1_N
PF02866\"[147-309]TLdh_1_C
InterPro
IPR001252
Active_site
Malate dehydrogenase, active site
PS00068\"[146-158]TMDH
InterPro
IPR001557
Family
L-lactate/malate dehydrogenase
PIRSF000102\"[2-309]TL-lactate/malate dehydrogenase
InterPro
IPR010097
Family
Malate dehydrogenase, NAD-dependent, eukaryotes and gamma proteobacteria
PTHR11540:SF1\"[1-311]TMALATE DEHYDROGENASE
TIGR01772\"[2-311]TMDH_euk_gproteo: malate dehydrogenase, NAD-
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[1-146]Tno description
PTHR11540\"[1-311]TMALATE AND LACTATE DEHYDROGENASE
signalp\"[1-30]?signal-peptide


","BeTs to 21 clades of COG0039COG name: Malate/lactate dehydrogenasesFunctional Class: CThe phylogenetic pattern of COG0039 is aomp-zyqvdrlbce-ghs-ujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.3e-18) to 1/1 blocks of the IPB001252 family, which is described as \"Malate dehydrogenase active site\". Interpro entry for IP:IPR001252. IPB001252 69-99 1.3e-18Significant hit ( 1.5e-15) to 5/6 blocks of the IPB001557 family, which is described as \"L-lactate dehydrogenase\". Interpro entry for IP:IPR001557. IPB001557A 3-34 13 IPB001557B 63-112 8.8e-12 IPB001557C 118-160 16 IPB001557E 205-246 1.4e+02 IPB001557F 260-298 2.2e+02","","","","","","","","","","","","Wed Jan 8 09:11:21 2003","Wed Jan 8 09:11:21 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01801 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 147 to 309 (E-value = 3.5e-57) place AA01801 in the Ldh_1_C family which is described as lactate/malate dehydrogenase, alpha/beta C-terminal domain (PF02866)","","","","","McAlister-Henn,L., Blaber,M., Bradshaw,R.A. and Nisco,S.J. Complete nucleotide sequence of the Escherichia coli gene encoding malate dehydrogenase Nucleic Acids Res. 15 (12), 4993 (1987) PubMed: 3299262 Vogel,R.F., Entian,K.D. and Mecke,D. Cloning and sequence of the mdh structural gene of Escherichia coli coding for malate dehydrogenase Arch. Microbiol. 149 (1), 36-42 (1987) PubMed: 3322223 Boyd,E.F., Nelson,K., Wang,F.S., Whittam,T.S. and Selander,R.K. Molecular genetic basis of allelic polymorphism in malate dehydrogenase (mdh) in natural populations of Escherichia coli and Salmonella enterica Proc. Natl. Acad. Sci. U.S.A. 91 (4), 1280-1284 (1994) PubMed: 8108402 Pupo,G.M., Karaolis,D.K., Lan,R. and Reeves,P.R. Evolutionary relationships among pathogenic and nonpathogenic Escherichia coli strains inferred from multilocus enzyme electrophoresis and mdh sequence studies Infect. Immun. 65 (7), 2685-2692 (1997) PubMed: 9199437 Hall,M.D., Levitt,D.G. and Banaszak,L.J. Crystal structure of Escherichia coli malate dehydrogenase. A complex of the apoenzyme and citrate at 1.87 A resolution J. Mol. Biol. 226 (3), 867-882 (1992) PubMed: 1507230 ","","Wed Jan 8 09:11:21 2003","1","","","" "AA01802","1214661","1214572","90","GTGGCTGAATTTTGCATAAAAGCAGTGACTTTAGCAAATAAATATTTAATTAAAACGGAAAAGTGCGGTCATAAAAAATTATGTTTTTTG","","","3395","VAEFCIKAVTLANKYLIKTEKCGHKKLCFL","1214572","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 10:39:01 2004","Thu Feb 26 10:39:01 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01802 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 10:39:01 2004","","","","","","","","","","","","","1","","","" "AA01803","1214686","1215150","465","ATGTTGAATAAAAATCCGGACAATCTGGTCAAAGCATTTAAAACTTTATTACGCGAAGAAAAATACGGTTCACAAACGGAAATTGCCGCCGAGCTTCAAAAACTTGGTTTTCGTAGCGTAAACCAATCGAAAGTATCCCGTATGCTCAGCAAATTCGGCGCCGTGCGCACCCGTAACACGCGTATGGAAATGGTGTATTGCCTACCGAGCGAACTCAGCGTGCCGAATACTCAAACGTCATTAAGAGATTTAGTGCTGGACATTGACCATAACGGCATATTAATCGTCATTCGAACTTCCCCCGGTGCGGCACAGCTGATCGCCCGCCTGCTTGATTCAATCAGTAAAGTGGAGGGCATTTTAGGCAATATTGCGGGCGACGATACGATTTTTGTCACACCAACCAAAAACACCGACATCAATAACTTAATGTTACGCATTCAGGATTTATTCGAAAACGCCTTT","","","17294","MLNKNPDNLVKAFKTLLREEKYGSQTEIAAELQKLGFRSVNQSKVSRMLSKFGAVRTRNTRMEMVYCLPSELSVPNTQTSLRDLVLDIDHNGILIVIRTSPGAAQLIARLLDSISKVEGILGNIAGDDTIFVTPTKNTDINNLMLRIQDLFENAF","1215149","[FUNCTION] Negatively controls the expression of the four operons of arginine biosynthesis in addition to the carab operon. Predominantly interacts with a.t residues in arg boxes (by similarity). [SUBUNIT] Homohexamer (By similarity).[SUBCELLULAR LOCATION] Cytoplasmic (Potential).[SIMILARITY] Belongs to the argR family. ","arginine repressor","Cytoplasm","","
InterPro
IPR001669
Family
Arginine repressor
PD007402\"[88-152]TARGR_SALTY_P37170;
PR01467\"[24-37]T\"[41-56]T\"[89-102]T\"[120-135]TARGREPRESSOR
PF01316\"[4-74]TArg_repressor
PF02863\"[80-150]TArg_repressor_C
TIGR01529\"[7-151]TargR_whole: arginine repressor
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[3-77]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.30.1360.40\"[78-155]Tno description


","BeTs to 8 clades of COG1438COG name: Arginine repressorFunctional Class: EThe phylogenetic pattern of COG1438 is --------vdrlb-e-gh-----i--Number of proteins in this genome belonging to this COG is","Significant hit ( 2.2e-32) to 4/4 blocks of the PR01467 family, which is described as \"Bacterial arginine repressor signature\". Prints database entry for PR:PR01467. PR01467A 24-37 0.025 PR01467B 41-56 1e-09 PR01467C 89-102 3.1e-07 PR01467D 120-135 4.1e-08","Residues 81 to 152 match (2e-18) PD:PD007402 which is described as REPRESSOR ARGININE COMPLETE PROTEOME TRANSCRIPTION REGULATION DNA-BINDING TRANS-ACTING FACTOR DNA ","","","","","","","","","","","Wed Jan 8 09:16:28 2003","Wed Jan 8 09:16:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01803 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 80 to 150 (E-value = 4.5e-31) place AA01803 in the Arg_repressor_C family which is described as Arginine repressor, C-terminal domain (PF02863)","","","","","Kiupakis AK, Reitzer L. ArgR-independent induction and ArgR-dependent superinduction of the astCADBE operon in Escherichia coli. J Bacteriol. 2002 Jun;184(11):2940-50. PMID: 12003934 Dennis C CA, Glykos NM, Parsons MR, Phillips SE. The structure of AhrC, the arginine repressor/activator protein from Bacillus subtilis. Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):421-30. PMID: 11856827 Szwajkajzer D, Dai L, Fukayama JW, Abramczyk B, Fairman R, Carey J. Quantitative analysis of DNA binding by the Escherichia coli arginine repressor. J Mol Biol. 2001 Oct 5;312(5):949-62. PMID: 11580241 Makarova KS, Mironov AA, Gelfand MS. Conservation of the binding site for the arginine repressor in all bacterial lineages. Genome Biol. 2001;2(4):RESEARCH0013. PMID: 11305941 ","","Wed Jan 8 09:16:28 2003","1","","","" "AA01804","1215177","1216061","885","ATGAAAATTCTTATGACAGGTGGCACCGGTTTTATCGGAAGTGCACTAATTCCTTCGTTACTGGCACAACATCATCAAATCACCGCCTTGGCACGCCACCCCGCCAAGGCGCAAAAACAACTTCCCAAAAATATTGAATTGATTAATACATTGGATTATTTTCAGCATTTCAATCAATTTGACGCCATTATTAATTTGGCGGGCGAGCCGATTTTTGCCCGCCGTTGGACGGAAATCCAAAAAGTGCGGTTGGAATCCAGCCGCGTTTCTTTAACGGAAAAACTGGCGCAACTCATTAACCGCAGCGATGATCCGCCGCAATGTTTTATTTCCGGTTCGGCGACGGGGTATTACGGCGATTGCGGCGAACAGATCATTGACGAACATAGCCCACCCGTAGGCAACTTCGCCGCCCGTTTGTGTCGGCGTTGGGAAGCGGCAGCGCTGAAAGCCAATACACGGGTTTGTTTGGTGCGCACGGGCATTGTGCTCGGCACACAAGGTGGCGCGCTGGCGCAAATGCTGCCGTTATATCGTTGCGGATTGGGTGTAAAATTAAGCACAGGCAAGCAATATTGGGGCTGGATCTCGCTGGCGGACATGGTGCGTGGGATTTTATTTTTACTGGAAAATCCCGATTGTCGCGGCGCCTTTAATTTTGTTGCACCGCACGCCGTACGTAATGCCGAATTTAATGCCCTATTAGGCAAAACCCTGCGCCGACCGCACTTTGCAACAGTGCCGGCATTTATCCTGAAACTCATGCTCGGCGAACGCGCCGGTTTGTTGCTGGACAGCCAAAATCTCGTGCCGCAACATTTGTTGGCACAAGGCTTTCAATTTGAGTATCCGGATCTCGGCGAATTTCTTGCGCAAGAAATCCCA","","","32648","MKILMTGGTGFIGSALIPSLLAQHHQITALARHPAKAQKQLPKNIELINTLDYFQHFNQFDAIINLAGEPIFARRWTEIQKVRLESSRVSLTEKLAQLINRSDDPPQCFISGSATGYYGDCGEQIIDEHSPPVGNFAARLCRRWEAAALKANTRVCLVRTGIVLGTQGGALAQMLPLYRCGLGVKLSTGKQYWGWISLADMVRGILFLLENPDCRGAFNFVAPHAVRNAEFNALLGKTLRRPHFATVPAFILKLMLGERAGLLLDSQNLVPQHLLAQGFQFEYPDLGEFLAQEIP","1216060","","sugar nucleotide epimerase; cell division inhibitor","Cytoplasm, Periplasm","","
InterPro
IPR001509
Family
NAD-dependent epimerase/dehydratase
PF01370\"[3-132]TEpimerase
InterPro
IPR010099
Family
Conserved hypothetical protein, YfcH
PTHR11092\"[5-294]TSUGAR NUCLEOTIDE EPIMERASE RELATED
TIGR01777\"[3-290]TyfcH: conserved hypothetical protein TIGR01
InterPro
IPR013549
Domain
Domain of unknown function DUF1731
PF08338\"[247-294]TDUF1731
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[2-241]Tno description
signalp\"[1-22]?signal-peptide


","No hits to the COGs database.","Significant hit ( 3.7e-08) to 1/5 blocks of the IPB001509 family, which is described as \"NAD dependent epimerase/dehydratase family\". Interpro entry for IP:IPR001509. IPB001509A 3-24 3.8e-08","Residues 247 to 286 match (4e-07) PD:PD011289 which is described as PROTEOME COMPLETE INHIBITOR NUCLEOTIDE DIVISION HCDI SUGAR EPIMERASE CELL HI1208 ","","","","","","","","","","","","Wed Jan 8 09:41:11 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01804 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01805","1216255","1216833","579","ATGACACATTATATTTTACTGATCATCGGCACGGCATTAATTAATAACTTCGTGCTGGTGAAATTCCTTGGGCTTTGCCCTTTTATGGGCGTTTCAAAAAAAATCGAGACCGCCATCGGCATGGGCTTGGCAACAACCTTCGTGCTGACGGTGGCGGCGTTGTGTTCTTATTTGATCGATAATTATATTCTCGCGCCTTTAAACGCCACGTTCTTACGTACCCTAGTGTTTATTTTAGTGATCGCCGTGGTGGTGCAATTTACCGAAATGGTCATCAATAAAACCAGCCCGACTCTATATCGTTTATTGGGCATTTTCCTGCCGCTGATTACCACCAACTGTGCGGTGCTTGGCGTGGCGTTATTGAACGTCAATCTTGCTCATAATTTAACGGAATCCGTGGCTTATGGCTTCGGCGCATCCGCTGGTTTCGCTTTGGTTTTAGTCTTATTCGCCGCCTTGCGTGAACGTCTGGTTGCCGCCGATGTGCCCATGCCGTTTCGTGGCGCGTCCATCGCCCTGATTACGGCAGGCTTAATGTCGCTTGCCTTTATGGGCTTCACCGGATTAGTGAAACTA","","","20589","MTHYILLIIGTALINNFVLVKFLGLCPFMGVSKKIETAIGMGLATTFVLTVAALCSYLIDNYILAPLNATFLRTLVFILVIAVVVQFTEMVINKTSPTLYRLLGIFLPLITTNCAVLGVALLNVNLAHNLTESVAYGFGASAGFALVLVLFAALRERLVAADVPMPFRGASIALITAGLMSLAFMGFTGLVKL","1216832","[FUNCTION] May be part of a membrane complex involved in electron transport (By similarity).[SUBUNIT] Composed of at least six subunits; rnfA, rnfB, rnfC, [SUBCELLULAR LOCATION] Integral membrane protein. Inner membrane (By similarity).","electron transport complex protein","Inner membrane, Cytoplasm","","
InterPro
IPR003667
Family
RnfA-Nqr electron transport subunit
PF02508\"[1-192]TRnf-Nqr
InterPro
IPR011293
Family
Electron transport complex, RnfABCDGE type, A subunit
TIGR01943\"[2-191]TrnfA: electron transport complex, RnfABCDGE
noIPR
unintegrated
unintegrated
signalp\"[1-20]?signal-peptide
tmhmm\"[4-24]?\"[39-59]?\"[69-87]?\"[102-124]?\"[134-154]?\"[169-191]?transmembrane_regions


","BeTs to 7 clades of COG2209COG name: Na+-transporting NADH:ubiquinone oxidoreductase subunit 5Functional Class: CThe phylogenetic pattern of COG2209 is --------v-----efgh-n---i--Number of proteins in this genome belonging to this COG is","Significant hit ( 2.8e-76) to 4/4 blocks of the IPB003667 family, which is described as \"RnfA-Nqr electron transport subunit\". Interpro entry for IP:IPR003667. IPB003667A 12-44 4.9e-23 IPB003667B 72-124 3.1e-35 IPB003667C 133-163 1.2e-12 IPB003667D 173-181 0.18","Residues 4 to 191 match (6e-47) PD:PD006282 which is described as SUBUNIT E D NA-TRANSLOCATING NQR COMPLEX ELECTRON NADH-QUINONE REDUCTASE 1.6.5.- ","","","","","","","","","","","Wed Jan 8 09:45:19 2003","Wed Jan 8 09:45:19 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01805 is paralogously related to AA01028 (8e-39), AA01813 (7e-19) and AA01029 (2e-13).","","","","","","Residues 1 to 192 (E-value = 4e-109) place AA01805 in the Rnf-Nqr family which is described as Rnf-Nqr subunit, membrane protein (PF02508)","","","","","Saaf,A., Johansson,M., Wallin,E. and von Heijne,G. Divergent evolution of membrane protein topology: the Escherichia coli RnfA and RnfE homologues. Proc. Natl. Acad. Sci. U.S.A. 96 (15): 8540-8544 (1999) [PubMed: 10411911].","","Wed Jan 8 09:45:19 2003","1","","","" "AA01807","1216836","1217423","588","ATGACTACCTTCCACTACGTACTCATTGCCATAGCTGTGTTGGCGCTGATTTTTGGCGCCATTTTGGGCTTTGCGTCGGTTAAACTGAAGGTGGAAGCCGATCCCATCGTGGAAAAAATTGATGCTATTTTGCCGCAGAGCCAATGCGGGCAATGCGGTTATCCCGGTTGTAAACCTTACGCAGAAGCCATTGCTAACGGTGATGTGATTACCAAATGTATTCCGGGTGGCCGCCCGACAGTGATTAAAATTGCCGAGTTGCTGGGGGTTGATGCGCCGGAAACGGATTTAGCAGAAGATCCCGAACCGAAAGTGGCATTTATTGATGAAAATATGTGTATCGGCTGCACCAAATGTATCCAAGCCTGCCCGGTGGATGCCATTATCGGCACCAACAAATCCATGCACACCATTATTCCCGATTTGTGTACAGGCTGCGAACTTTGCGTTGCTCCCTGCCCGACTAGTTGTATTTCGATGATTAAAGTGGAAAAAAATATTGATAGCTGGGATTGGAAATTCGATCCTAATTTAGTCATTCCGATTATTGACACCACATCGGCCGAAAAGAAAATCATTGTGGGGAAA","","","20920","MTTFHYVLIAIAVLALIFGAILGFASVKLKVEADPIVEKIDAILPQSQCGQCGYPGCKPYAEAIANGDVITKCIPGGRPTVIKIAELLGVDAPETDLAEDPEPKVAFIDENMCIGCTKCIQACPVDAIIGTNKSMHTIIPDLCTGCELCVAPCPTSCISMIKVEKNIDSWDWKFDPNLVIPIIDTTSAEKKIIVGK","1217422","[FUNCTION] May be part of a membrane complex involved in electron transport (By similarity).[COFACTOR] Binds 1 2Fe-2S and 2 4Fe-4S clusters (Potential).[SUBUNIT] Composed of at least six subunits; rnfA, rnfB, rnfC, rnfD, rnfE and rnfG (By similarity). [SUBCELLULAR LOCATION] Cytoplasmic; inner membrane-associated (By similarity).","electron transport complex protein","Cytoplasm, Periplasm, Inner membrane","","
InterPro
IPR001450
Domain
4Fe-4S ferredoxin, iron-sulfur binding
PR00353\"[106-117]T\"[118-129]T4FE4SFRDOXIN
PF00037\"[106-129]T\"[136-159]TFer4
PS00198\"[113-124]T\"[143-154]T4FE4S_FERREDOXIN
InterPro
IPR007202
Domain
Putative Fe-S cluster
PF04060\"[43-76]TFeS
InterPro
IPR010207
Family
Electron transport complex, RnfABCDGE type, B subunit
TIGR01944\"[1-188]TrnfB: electron transport complex, RnfABCDGE
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.20\"[73-181]Tno description
PTHR19248\"[101-128]TATP-BINDING TRANSPORT PROTEIN-RELATED
PTHR19248:SF6\"[101-128]TRNASE L INHIBITOR-RELATED
signalp\"[1-23]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","BeTs to 7 clades of COG2878COG name: Predicted alternative beta subunit of Na+-transporting NADH:ubiquinone oxidoreductaseFunctional Class: CThe phylogenetic pattern of COG2878 is --------v-----efghsn------Number of proteins in this genome belonging to this COG is","Significant hit ( 3.7e-09) to 2/2 blocks of the PR00353 family, which is described as \"4Fe-4S ferredoxin signature\". Prints database entry for PR:PR00353. PR00353A 106-117 0.0022 PR00353B 118-129 0.00068 PR00353A 136-147 0.18 PR00353B 148-159 0.48Significant hit ( 8.4e-08) to 2/3 blocks of the PR00354 family, which is described as \"7Fe ferredoxin signature\". Prints database entry for PR:PR00354. PR00354B 121-131 2 PR00354C 138-155 1.8e-05","Residues 6 to 39 match (1e-08) PD:PD229894 which is described as ELECTRON RNFB INNER PROTEOME COMPLETE MEMBRANE IRON-SULFUR COMPLEX 4FE-4S ","","","","","","","","","","","Wed Jan 8 09:48:55 2003","Wed Jan 8 09:48:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01807 is paralogously related to AA00044 (5e-05) and AA02677 (0.001).","","","","","","Residues 136 to 159 (E-value = 1.2e-05) place AA01807 in the Fer4 family which is described as 4Fe-4S binding domain (PF00037)","","","","","Saaf,A., Johansson,M., Wallin,E. and von Heijne,G. Divergent evolution of membrane protein topology: the Escherichia coli RnfA and RnfE homologues. Proc. Natl. Acad. Sci. U.S.A. 96 (15): 8540-8544 (1999) [PubMed: 10411911].","","Wed Jan 8 09:48:55 2003","1","","","" "AA01808","1217427","1219376","1950","ATGGCTGATGTATTAACCCGTTTCAACAGTGGCAAGCTTTGGGAATTCGATGGCGGCATTCATCCGCCCGACATGAAATCCCAATCCAACCGCGCGCCTATTCGTACCTTGCCGTTGCCCGATAATTTCTACGTTCTTCTGAAACAACACGCCGGCACAGCGGGCAATTTATTGGTAAAATGCGGCGATCATGTTTTGAAAGGTCAACCGCTCACCCAGGGGGACGGTTTGCGTTCGCTGCCGGTTCATGCGCCTACTTCAGGCACGGTCATTGATGTGATGCCTTATGTCACCGCCCATCCTTCCGGTCTACCGGAAACCTGTGTGCATATTAAAGCGGATGGATTAGATCAATGGCGCGAGCAAACCCCGTTGGAGGATTTCCTTAGCCAAACGCCGGAACAGTTAATCGAAAAAATTTATCAGGCGGGCATTGCCGGTCTGGGTGGCGCGGTATTCCCGACCGCGGCAAAAATTCATTCCGCCGAGAAACAGGTGAAATTACTGATTATTAACGGCGCGGAATGTGAACCTTACATTACCTGCGACGATCGCTTAATGCATGATTATGCTGATGAAATTATCGAAGGCGTGCGTATTTTGCGCTACATTTTACGCCCTGAGAAAGTGGTGATCGCCGTTGAAGATAATAAACCAAAAGCGGTGAAATCCTTGGAACGCGCCTTACACGGCGCCAACGATATTGAAATCCGAGTGATTCCGACCAAATACCCTTCCGGCGCGGCAAAACAGTTAATTCAAGTGCTGACCGGCATGGAGGTACCTAGCGGTCAACGCTCCTCCGGTATCGGCGTGCTGATGCAAAACATCGGCACCGCTTTTGCTATTAAACGCGCAGTGATGGATGATGAACCGCTGATTGAGCGCGTCGTCACCCTCACCGGTGATAAAATCGCCGATAAAGGCAACTATTGGGCGCGTTTTGGAACGCCGATTTATCACTTGTTGCGCGAAACGGGCTATCAATACGACGATCGTTTCCCGGTCTTCATGGGCGGTCCGATGATGGGCTTTATTCTGCCCGATTTAAATGCGCCGATGACCAAAGTGACCAACTGCCTGTTGGCGCCGGATCATTTTGAATACGCCCCGCCGGAAGAAGAAAAAAATTGTATTCGCTGTTCTGCCTGTTCCGATGCCTGCCCGGTGAAACTCATGCCGCAGCAATTGTATTGGTTTGCACGCAGCGAAGATCACGAAAAATCGGAAGAATATTCCCTCAAAGATTGTATTGAATGCGGCGTGTGCGCTTATGTTTGCCCAAGTCACATTCCGTTAATTCAATATTTCCGCCGGGAAAAAGCTAAAATCTGGGAAATCAAACACAAAGCCAAATTGGCGGAAGAAGCTAAAATACGTTTTGAACAACGCCAAGCCCGTTTGGAACGGGAAGAACAGGAACGCAAAGATCGCTCACAACGTGCTGCAGCCGCCCGTCGTGAAGAATTGGCGCAACAAAAAGGCGTGGATCCGGTGGCTGCCGCCTTAGCGCGCTTAAAAGCGAAAAAAGCCGAAACGACGGAAGCTACGCAGGCAGAACAGAAAACCATTGTTGACGAAAAAGGTCATATCCTGCCTGACAACAGCGACATCATGGCACAACGCAAAGCCCGTCGTTTAGCCCGTCAGGCGGAAGCGGCACACTCGCCGTCGCAGAAAACAGAAAAAACGCTAGAAAAAACGCTAGAAAAAACCACCGCACTTGAGGATAAAAAATCTACCGTTGCCGCCGCCATTGCCCGTGCGAAAGCCAAGAAAGCGGCGCAGCAAACGGAAGCCGTCGAAGCAAACGAACCTGAAACGGCAAAAAGTGCGGTCAATATTTCCGGTGAAAATGGCGCAGAGAACGATCCGCGCAAAGCCGCTGTTGCCGCCGCTATTGCCCGTGCGAAAGCGAAGAAAGCCCAACGTGAAAACACGCAACAAGAT","","","71992","MADVLTRFNSGKLWEFDGGIHPPDMKSQSNRAPIRTLPLPDNFYVLLKQHAGTAGNLLVKCGDHVLKGQPLTQGDGLRSLPVHAPTSGTVIDVMPYVTAHPSGLPETCVHIKADGLDQWREQTPLEDFLSQTPEQLIEKIYQAGIAGLGGAVFPTAAKIHSAEKQVKLLIINGAECEPYITCDDRLMHDYADEIIEGVRILRYILRPEKVVIAVEDNKPKAVKSLERALHGANDIEIRVIPTKYPSGAAKQLIQVLTGMEVPSGQRSSGIGVLMQNIGTAFAIKRAVMDDEPLIERVVTLTGDKIADKGNYWARFGTPIYHLLRETGYQYDDRFPVFMGGPMMGFILPDLNAPMTKVTNCLLAPDHFEYAPPEEEKNCIRCSACSDACPVKLMPQQLYWFARSEDHEKSEEYSLKDCIECGVCAYVCPSHIPLIQYFRREKAKIWEIKHKAKLAEEAKIRFEQRQARLEREEQERKDRSQRAAAARREELAQQKGVDPVAAALARLKAKKAETTEATQAEQKTIVDEKGHILPDNSDIMAQRKARRLARQAEAAHSPSQKTEKTLEKTLEKTTALEDKKSTVAAAIARAKAKKAAQQTEAVEANEPETAKSAVNISGENGAENDPRKAAVAAAIARAKAKKAQRENTQQD","1219375","[FUNCTION] May be part of a membrane complex involved in electron transport (By similarity).[COFACTOR] Binds 2 4FE-4S clusters (Potential).[SUBUNIT] Composed of at least six subunits; rnfA, rnfB, rnfC, rnfD, rnfE and rnfG (By similarity).[SUBCELLULAR LOCATION] Inner membrane-associated (By similarity). ","electron transport complex protein","Cytoplasm, Inner membrane","","
InterPro
IPR001450
Domain
4Fe-4S ferredoxin, iron-sulfur binding
PF00037\"[371-394]T\"[410-433]TFer4
PS00198\"[378-389]T\"[417-428]T4FE4S_FERREDOXIN
InterPro
IPR010208
Family
Electron transport complex, RnfABCDGE type, C subunit
TIGR01945\"[13-448]TrnfC: electron transport complex, RnfABCDGE
InterPro
IPR011538
Domain
Respiratory-chain NADH dehydrogenase domain, 51 kDa subunit
PF01512\"[118-341]TComplex1_51K
InterPro
IPR012285
Domain
Fumarate reductase, C-terminal
G3DSA:1.10.1060.10\"[343-448]Tno description
noIPR
unintegrated
unintegrated
PD025201\"[57-323]TQ6MF30_PARUW_Q6MF30;
PTHR11780\"[125-232]TNADH-UBIQUINONE OXIDOREDUCTASE FLAVOPROTEIN 1 (NDUFV1)


","No hits to the COGs database.","Significant hit ( 5.4e-50) to 4/5 blocks of the IPB001949 family, which is described as \"Respiratory-chain NADH dehydrogenase 51 Kd subunit\". Interpro entry for IP:IPR001949. IPB001949A 133-162 2.5e-11 IPB001949B 168-205 5.1e-14 IPB001949C 339-391 8.6e-09 IPB001949D 410-450 1.8e-11 IPB001949C 242-294 0.0065","Residues 80 to 356 match (8e-07) PD:PD119979 which is described as PROTEOME COMPLETE BB0072 ","","","","","","","","","","","Wed Jan 8 09:50:49 2003","Wed Jan 8 09:50:49 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01808 is paralogously related to AA02832 (3e-10), AA02347 (3e-07) and AA02693 (2e-04).","","","","","","Residues 118 to 341 (E-value = 1.3e-81) place AA01808 in the Complex1_51K family which is described as Respiratory-chain NADH dehydrogenase 51 Kd subunit (PF01512)","","","","","","","","1","","","" "AA01810","1219390","1220466","1077","ATGTTTAAGATGATAAGTTCACCCCATACCCATTCCGGCAAGCTCACGGCGCGCGTGATGTTTTGGGTGATTTTTGCCATGATTCCGGCAATCGTTTTGCAAGTTCATTATTTCGGCTTTGGTGTGTTGATTCAATCGGCGTTGGCAATTATGTTTGCATTATTGCTGGAATTGGCGGTAACGCGGTTACGCAAAAAAAGGATGTTAAGTTACATTTCCGATTTTAGCGTGATTTTGACCGCACTTATTCTCGCCGTTGCCATCCCACCTTACGCACCTTACTGGGTTATTCTGATTGGTACGTTTTGTGCAGTGATTCTCGGCAAGCACGTTTATGGCGGCTTGGGGCAAAATCCGTTTAATCCTGCCATGGTGGGTTATGTGGTGCTGCTCGTGTCGTTCCCGTTACAAATGACTACTTGGATGCCACCTATCGCATTATTGGCGGAACCGCCGACCTTTCATGATGCGGCATTGTTGATTTTTTCAGGGCTGACCTCCGACGGTTTTAGTCTGCACCAATTAACGGCATCCATTGACGGCATTACACAGGCAACTCCGCTCGACAGCGCACGAACTTTCTATTCAGCCCTTTGTTCCGATTGCAGCGCCGATGTGGCATTTTACGATTTGGTGAAATTACCAATTTTTACGCAAAATGGCTGGGACCTTGCGCAAGGGTGGTGGCAAATTAACGTGGCGTTTCTTATCGGTGGTGTATTCTTAATTCTAAAAAAAATCATTCACTGGCAAATCCCTACAGCCATGTTAGGCAGTTTTGCGTTGTTAGATTTACTGACCGAATTATTCGGCAACGGCGCGCAATTAAGCTTACCGGCGCAGTTAATGAGCGGCGCCATGATGTTCGGCGCATTCTTTATCGCCACCGATCCGGTCACAGCTTCCATCACGCCGCGCGGCAAATTGGTGTTCGGTGCGTTGGTAGGAAGCTTGTTGTATTTAATCCGTTTTTATGGCAACTATCCTGACGGTGTCGCCTTCGCGATTTTACTCAGCAACATTTGCGTGCCGTTAATTGATCACTATACCCGCCCGCGGGTTGCCGGTCATCGGAGG","","","39330","MFKMISSPHTHSGKLTARVMFWVIFAMIPAIVLQVHYFGFGVLIQSALAIMFALLLELAVTRLRKKRMLSYISDFSVILTALILAVAIPPYAPYWVILIGTFCAVILGKHVYGGLGQNPFNPAMVGYVVLLVSFPLQMTTWMPPIALLAEPPTFHDAALLIFSGLTSDGFSLHQLTASIDGITQATPLDSARTFYSALCSDCSADVAFYDLVKLPIFTQNGWDLAQGWWQINVAFLIGGVFLILKKIIHWQIPTAMLGSFALLDLLTELFGNGAQLSLPAQLMSGAMMFGAFFIATDPVTASITPRGKLVFGALVGSLLYLIRFYGNYPDGVAFAILLSNICVPLIDHYTRPRVAGHRR","1220465","[FUNCTION] May be part of a membrane complex involved in electron transport (By similarity). [COFACTOR] Binds 2 4FE-4S clusters (Potential). [SUBUNIT] Composed of at least six subunits; rnfA, rnfB, rnfC, rnfD, rnfE and rnfG (By similarity). [SUBCELLULAR LOCATION] Inner membrane-associated (By similarity). ","electron transport complex protein","Inner membrane, Cytoplasm","","
InterPro
IPR004338
Family
NQR2 and RnfD
PF03116\"[1-358]TNQR2_RnfD_RnfE
InterPro
IPR011303
Family
Electron transport complex, RnfABCDGE type, D subunit
TIGR01946\"[7-357]TrnfD: electron transport complex, RnfABCDGE
noIPR
unintegrated
unintegrated
signalp\"[1-34]?signal-peptide
tmhmm\"[15-33]?\"[37-59]?\"[69-89]?\"[95-115]?\"[125-145]?\"[224-244]?\"[254-274]?\"[280-300]?\"[309-327]?\"[331-349]?transmembrane_regions


","No hits to the COGs database.","","Residues 236 to 348 match (4e-08) PD:PD590584 which is described as B SUBUNIT OXIDOREDUCTASE NQR NA-TRANSLOCATING UBIQUINONE NAD PROBABLE NA-NQR SODIUM ","","","","","","","","","","","Wed Jan 8 09:52:20 2003","Wed Jan 8 09:52:20 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01810 is paralogously related to AA01032 (3e-22).","","","","","","Residues 1 to 358 (E-value = 2e-158) place AA01810 in the NQR2_RnfD_RnfE family which is described as NQR2, RnfD, RnfE family (PF03116)","","","","","","","","1","","","" "AA01811","1220476","1221093","618","ATGCAAACCATTAAAGTCACTTCTAAATCCGCTATATTGTTGGCGTTTGTTGCGTTTTGCTGCACAATAATTTCCGGTGGCATTTACTTTTTAACCAAAGATAAAATCAAGCAGGCAATACAGGCACAGCAACAGGAACTGTTACTACAAGTGATCCCGCAGGATTACTTCAATAATGATCTGACGCAGGCTTGTTATGCACCGCAAGCGGGGACATTACAAGTCGTGGAGATAAGCAAAATATGCACGGCAAAGAAAGACGGCGTGACTACTGCCTATGCCTTTGAAAGCACGGCGCATGATGGCTATTCCGGCGATATTCATATTTTGGTGGGCATGAAACCTGATGGCGAAGTGCTTGGCGTGCGCATTACGGAACACCACGAAACCCCGGGATTAGGCGATAAAATTGAAACCCGCATTTCCAACTGGGTTTTAAGTTTTGATCATCAGGTTATCAGCAACGAAAATGCCGCAGAATGGGCGGTGAAAAAAGACGGCGGTAAATTCGATCAATTCGCCGGTGCCACCATCACGCCCCGCGCTGTGGTTAACCAAGTGAAACGGGCGGCATTGGCTATGCTGGATAATCTGCCGAAAGAGAGAGAAAGTGATGGA","","","22499","MQTIKVTSKSAILLAFVAFCCTIISGGIYFLTKDKIKQAIQAQQQELLLQVIPQDYFNNDLTQACYAPQAGTLQVVEISKICTAKKDGVTTAYAFESTAHDGYSGDIHILVGMKPDGEVLGVRITEHHETPGLGDKIETRISNWVLSFDHQVISNENAAEWAVKKDGGKFDQFAGATITPRAVVNQVKRAALAMLDNLPKERESDG","1221092","[FUNCTION] May be part of a membrane complex involved in electron transport (By similarity). [COFACTOR] Binds 2 4FE-4S clusters (Potential). [SUBUNIT] Composed of at least six subunits; rnfA, rnfB, rnfC, rnfD, rnfE and rnfG (By similarity). [SUBCELLULAR LOCATION] Inner membrane-associated (By similarity).","electron transport complex protein","Periplasm, Inner membrane, Cytoplasm","","
InterPro
IPR007329
Domain
FMN-binding
PF04205\"[102-194]TFMN_bind
InterPro
IPR010209
Family
Electron transport complex, RnfABCDGE type, G subunit
PIRSF006091\"[3-204]TElectron transport complex, protein RnfG
TIGR01947\"[11-196]TrnfG: electron transport complex, RnfABCDGE
noIPR
unintegrated
unintegrated
signalp\"[1-26]?signal-peptide
tmhmm\"[10-30]?transmembrane_regions


","BeTs to 7 clades of COG2869COG name: Na+-transporting NADH:ubiquinone oxidoreductase gamma subunitFunctional Class: CThe phylogenetic pattern of COG2869 is --------v-----efgh-n---i--Number of proteins in this genome belonging to this COG is","","Residues 1 to 69 match (5e-16) PD:PD271081 which is described as ELECTRON RNFG INNER PROTEOME TRANSMEMBRANE COMPLETE MEMBRANE COMPLEX ","","","","","","","","","","","Wed Jan 8 09:53:40 2003","Wed Jan 8 09:53:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01811 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 96 to 194 (E-value = 5.1e-39) place AA01811 in the FMN_bind family which is described as FMN-binding domain (PF04205)","","","","","","","","1","","","" "AA01813","1221089","1221871","783","ATGGATAAATTAGACGAAACACAAGAACTGCAACAAACCGAAGCCAAAAGTGCGGTTGACAAAAAACAACATTTTTTGAACGTTGGTTCTGCCAACGGCCCCGAAGGGGTGAATAAGCGAACAAGTGAGCTTATGAATAATATTTCAAATGAAAAAAGCATTTGGAAAACGATTTTCATTCAGGGCATCTGGACCAACAATTCCACCGTGGTGCAACTGCTTGGGTTGTGTCCGCTGCTGGCGGTGTCCAACTCCGTGACCAACGCCCTCGGGCTGGGTTTAGCCACCATGCTTGTGCTGACGTGTACGAACACGGTAGTTTCTCTTTTCCGTAAGCACATCCCCAATGAAATCCGCATTCCGATTTATGTGATGATCATCGCAACCACGGTAACCGCTGTGCAATTATTGATGAATGCCTATACCTACGCGCTTTATCAATCTCTCGGGATTTTTATTCCGCTCATCGTCACCAACTGTATTGTGATCGGTCGCGCCGAAGCCTTTGCTTCCAAGAACAGCATTTCCCATTCCGCCTTTGACGGTTTTTCCATGGGATTAGGGATGTTATTCAGTTTAGTAGCGCTCGGCGGCATCCGCGAAATCATCGGCAACGGTACTTTATTTGACGGCATCGAAAATTTGCTGGGCGATTGGGCTAAATTCATGCGGATTGAATTTTTCCACAATGACAGTAATCTGTTACTTGCGATTTTGCCTCCCGGCGCATTTATTGGTTTAGCTTTGTTGTTAGCCTTAAAAAATGTAATAGATACAAAAAAG","","","28517","MDKLDETQELQQTEAKSAVDKKQHFLNVGSANGPEGVNKRTSELMNNISNEKSIWKTIFIQGIWTNNSTVVQLLGLCPLLAVSNSVTNALGLGLATMLVLTCTNTVVSLFRKHIPNEIRIPIYVMIIATTVTAVQLLMNAYTYALYQSLGIFIPLIVTNCIVIGRAEAFASKNSISHSAFDGFSMGLGMLFSLVALGGIREIIGNGTLFDGIENLLGDWAKFMRIEFFHNDSNLLLAILPPGAFIGLALLLALKNVIDTKK","1221870","[FUNCTION] May be part of a membrane complex involved in electron transport (By similarity). [COFACTOR] Binds 2 4FE-4S clusters (Potential). [SUBUNIT] Composed of at least six subunits; rnfA, rnfB, rnfC, rnfD, rnfE and rnfG (By similarity). [SUBCELLULAR LOCATION] Inner membrane-associated (By similarity).","electron transport complex protein","Inner membrane, Cytoplasm","","
InterPro
IPR003667
Family
RnfA-Nqr electron transport subunit
PF02508\"[52-252]TRnf-Nqr
InterPro
IPR010968
Family
Electron transport complex, RnfABCDGE type, E subunit
TIGR01948\"[56-260]TrnfE: electron transport complex, RnfABCDGE
noIPR
unintegrated
unintegrated
tmhmm\"[64-84]?\"[90-110]?\"[120-140]?\"[146-164]?\"[179-199]?\"[233-253]?transmembrane_regions


","BeTs to 7 clades of COG1347COG name: Na+-transporting NADH:ubiquinone oxidoreductase subunit 4Functional Class: CThe phylogenetic pattern of COG1347 is --------v-----efgh-n---i--Number of proteins in this genome belonging to this COG is","Significant hit ( 5.8e-71) to 4/4 blocks of the IPB003667 family, which is described as \"RnfA-Nqr electron transport subunit\". Interpro entry for IP:IPR003667. IPB003667A 63-95 7.6e-18 IPB003667B 118-170 9.3e-35 IPB003667C 178-208 5.2e-15 IPB003667D 243-251 23","Residues 204 to 260 match (3e-16) PD:PD036368 which is described as ELECTRON MEMBRANE RNFE COMPLETE PROTEOME INNER TRANSMEMBRANE COMPLEX NITROGEN FIXATION ","","","","","","","","","","","Wed Jan 8 09:56:09 2003","Wed Jan 8 09:56:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01813 is paralogously related to AA01029 (4e-29), AA01805 (1e-18) and AA01028 (3e-18).","","","","","","Residues 52 to 252 (E-value = 9.9e-111) place AA01813 in the Rnf-Nqr family which is described as Rnf-Nqr subunit, membrane protein (PF02508)","","","","","Saaf,A., Johansson,M., Wallin,E. and von Heijne,G. Divergent evolution of membrane protein topology: the Escherichia coli RnfA and RnfE homologues Proc. Natl. Acad. Sci. U.S.A. 96 (15), 8540-8544 (1999) PubMed: 10411911 ","","Wed Jan 8 09:56:09 2003","1","","","" "AA01814","1222021","1222653","633","ATGAATAAAGAAAAAAGAATTGAAATCCTAAAACGCCTACGCGCTGCTAATCCGCACCCAACGACGGAACTGAATTTCAGTTCCCCTTTTGAATTGTTAATTGCGGTGATTCTATCGGCACAAGCCACCGACAAAGGCGTGAACAAGGCGACGGACAAACTGTTTCCCGTCGCCAATACCCCACAAACGATTTTGGCGTTAGGTGTGGATGGTTTGAAGGAGTACATTAAAACCATCGGTTTGTTTAACAGCAAAGCGGAAAATATCATCAAAACCTGCCGTGATTTAATTGAAAAACACAACGGCGACGTGCCGGAAGATCGCGCCGCCTTAGAAGCCCTTGCCGGTGTCGGCAGAAAAACCGCTAATGTGGTGCTAAACACCGCCTTCGGACATCCCACTATCGCTGTGGACACCCACATTTTCCGCGTGTGTAATCGTACCGGCTTTGCACCCGGCAAAGATGTGGTGAAAGTGGAAGAAAAATTGATTAAAGTGGTGCCCGCCGAATTTAAAGTGGATGTGCACCATTGGCTGATTCTGCACGGGCGTTATACCTGCGTGGCGCGCAAACCCCGTTGCGGGGCGTGCATTATTGAAGATTTATGTGAATATAAAGATAAAACGGAATAT","","","25103","MNKEKRIEILKRLRAANPHPTTELNFSSPFELLIAVILSAQATDKGVNKATDKLFPVANTPQTILALGVDGLKEYIKTIGLFNSKAENIIKTCRDLIEKHNGDVPEDRAALEALAGVGRKTANVVLNTAFGHPTIAVDTHIFRVCNRTGFAPGKDVVKVEEKLIKVVPAEFKVDVHHWLILHGRYTCVARKPRCGACIIEDLCEYKDKTEY","1222652","[FUNCTION] Has both an apurinic and/or apyrimidinic endonuclease activity and a DNA N-glycosylase activity. Incises damaged DNA at cytosines, thymines and guanines. Acts on a damaged strand, 5' from the damaged site (by similarity). [CATALYTIC ACTIVITY] The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.[COFACTOR] Binds a 4Fe-4S cluster which is not important for the catalytic activity, but which is probably involved in the proper positioning of the enzyme along the dna strand (by similarity). [SUBUNIT] Monomer (by similarity). [SIMILARITY] Belongs to the nth/mutY family. ","endonuclease III","Cytoplasm, Periplasm","","
InterPro
IPR000445
Domain
Helix-hairpin-helix motif
PF00633\"[99-128]THHH
InterPro
IPR003265
Domain
HhH-GPD
PF00730\"[34-169]THhH-GPD
SM00478\"[38-185]TENDO3c
InterPro
IPR003583
Domain
Helix-hairpin-helix DNA-binding, class 1
SM00278\"[109-128]THhH1
InterPro
IPR003651
Domain
Iron-sulfur cluster loop
SM00525\"[186-206]TFES
InterPro
IPR004035
Domain
Endonuclease III, FCL
PS00764\"[187-203]TENDONUCLEASE_III_1
InterPro
IPR004036
Domain
Endonuclease III, HhH
PS01155\"[102-131]TENDONUCLEASE_III_2
InterPro
IPR005759
Family
Endonuclease III/Nth
TIGR01083\"[3-194]Tnth: endonuclease III
noIPR
unintegrated
unintegrated
G3DSA:1.10.1670.10\"[109-209]Tno description
PTHR10359\"[22-205]TA/G-SPECIFIC ADENINE GLYCOSYLASE/ENDONUCLEASE III


","BeTs to 25 clades of COG0177COG name: Predicted EndoIII-related endonucleaseFunctional Class: LThe phylogenetic pattern of COG0177 is aompkzyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.5e-81) to 5/5 blocks of the IPB001502 family, which is described as \"Endonuclease III\". Interpro entry for IP:IPR001502. IPB001502A 33-54 1.4e-11 IPB001502B 72-86 4.4e-07 IPB001502C 100-131 4.7e-20 IPB001502D 137-163 2.1e-15 IPB001502E 176-203 5.5e-22","Residues 1 to 47 match (3e-10) PD:PD498045 which is described as ENDONUCLEASE PROTEOME III COMPLETE ","","","","","","","","","","","Wed Jan 8 10:01:41 2003","Wed Jan 8 10:01:41 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01814 is paralogously related to AA01044 (3e-10).","","","","","","Residues 34 to 169 (E-value = 4.5e-20) place AA01814 in the HhH-GPD family which is described as HhH-GPD superfamily base excision DNA repair protein (PF00730)","","","","","Asahara,H., Wistort,P.M., Bank,J.F., Bakerian,R.H. and Cunningham,R.P. Purification and characterization of Escherichia coli endonuclease III from the cloned nth gene. Biochemistry 28 (10): 4444-4449 (1989) [PubMed: 2669955].Kuo,C.F., McRee,D.E., Fisher,C.L., O'Handley,S.F., Cunningham,R.P. and Tainer,J.A. Atomic structure of the DNA repair [4Fe-4S] enzyme endonuclease III . Science 258 (5081): 434-440 (1992) [PubMed: 1411536]. Thayer,M.M., Ahern,H., Xing,D., Cunningham,R.P. and Tainer,J.A.Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J. 14 (16): 4108-4120 (1995) [PubMed: 7664751].Cunningham,R.P., Ahern,H., Xing,D., Thayer,M.M. and Tainer,J.A.Structure and function of Escherichia coli endonuclease III Ann. N. Y. Acad. Sci. 726, 215-222 (1994) PubMed: 8092678 ","","Wed Jan 8 10:01:41 2003","1","","","" "AA01815","1222681","1224045","1365","ATGACAACAACGAAACCGGAACGACAAACCTGGTCCAGTCGCTTAACTTATGTGCTTACTGTCGCCGGTGCAACCGTAGGCTTTGGTGCAACATGGCGCTTTCCTTATTTGGTAGGCGAACACGGCGGCGGTGCCTATGTGTTGTTATTCTGTTTAGCCATGATTTTAATCGGGATCCCGATGATCTTAGTGGAAAACGTCATCGGTCGCCGTTTGCGGGTGAACTCTATTGATGCCTTCGGCGACAAAATTCTCGATAAAGGCATTTCCAAATATTGGAAAATCATCGGTTATATGGGCTTGCTCGGCGCCTTCGGTATCATGGCGTATTACATGGTGCTTGGCGGCTGGGTAATCACCTACATCATCAACTTAATCACCGGCACGCTGGATATTTCCACTACTATCACAAAAGAAGTCGCCCAAGATTTCTACGAAGTACACATCAGCAACAGTCCCTTAGAAATCATTATTTACACCGCACTTTTTGCGTTAGTGAATTACATCATTTTGGCAAAAGGCATTATCGGCGGCATTGAACGCGCTGTGAGGTACCTTATGCCGTTGCTCTTTATTTTCTTAATCGGCATGGTGATTCGCAATATCACTTTACCGGGCGCCATGGAAGGGATCACCTTTTACCTAAAACCCGATTTCTCCAAAATCACAGCCGAATTATTTATTTTCGTATTAGGACAGGTTTTCTTCGCGTTAAGTCTTGGTTTTGGTGTATTAATCACCCTTTCCAGTTACCTAAATAAAGAAGAAAATCTTATTCAAACCGCCGTCATCACCGGTTTCACCAACACCATTATTGCAGTGCTGGCGGGATTCATGATTTTCCCTTCGCTATTCACCTTCGGCATTGAACCGAACGCCGGACCAACCTTGGTATTCCAAAGCCTACCGATTGTGTTCTCCCATTTATGGGCGGGTAAATTCTTCGCCATTGTTTTCTTCAGTTTACTGTTGATCGCCGCGCTGACTACTTCCATCACCATTTACGAGGTCATCATCACCGCTTTACAGGAAAAACTCAGAATGCGTCGAAGCAAAGCCATTATTTTGACCCTCGGCGGGATTTTCTTATTAGGCAACGTGCCGGCGATTCTCGGCGATAATGTATGGAAAAACGTCACTTTCTTCGGCAAAAGTATTTTTGATGCCTTTGATTTCGTCAGCGGCAACATTCTGTTTATGCTCACCGCACTGGGTTGCGCTATTTTCGTCGGTTTCGTATTAAAAGAGGAAGCGAAAAAAGAACTCTCCCCGGCCCTGAATTCCACCTTTATCAAGGTTTGGTTTAATTATGTGAAATTTGTCGTTCCGTTTATTATTTTGGTGATTTTTATCAGTAACCTGATT","","","50402","MTTTKPERQTWSSRLTYVLTVAGATVGFGATWRFPYLVGEHGGGAYVLLFCLAMILIGIPMILVENVIGRRLRVNSIDAFGDKILDKGISKYWKIIGYMGLLGAFGIMAYYMVLGGWVITYIINLITGTLDISTTITKEVAQDFYEVHISNSPLEIIIYTALFALVNYIILAKGIIGGIERAVRYLMPLLFIFLIGMVIRNITLPGAMEGITFYLKPDFSKITAELFIFVLGQVFFALSLGFGVLITLSSYLNKEENLIQTAVITGFTNTIIAVLAGFMIFPSLFTFGIEPNAGPTLVFQSLPIVFSHLWAGKFFAIVFFSLLLIAALTTSITIYEVIITALQEKLRMRRSKAIILTLGGIFLLGNVPAILGDNVWKNVTFFGKSIFDAFDFVSGNILFMLTALGCAIFVGFVLKEEAKKELSPALNSTFIKVWFNYVKFVVPFIILVIFISNLI","1224044","","probable sodium-dependent transmembrane transport protein","Inner membrane, Cytoplasm","","
InterPro
IPR000175
Family
Sodium:neurotransmitter symporter
PD000448\"[3-35]TQ9CNP7_PASMU_Q9CNP7;
PR00176\"[16-37]T\"[45-64]T\"[263-283]T\"[435-455]TNANEUSMPORT
PTHR11616\"[7-455]TSODIUM/CHLORIDE DEPENDENT TRANSPORTER
PF00209\"[8-424]TSNF
PS50267\"[7-455]TNA_NEUROTRAN_SYMP_3
PS00610\"[32-46]TNA_NEUROTRAN_SYMP_1
noIPR
unintegrated
unintegrated
PTHR11616:SF11\"[7-455]TSODIUM-DEPENDENT NEUROTRANSMITTER TRANSPORTER
signalp\"[1-29]?signal-peptide
tmhmm\"[15-35]?\"[45-63]?\"[101-121]?\"[156-176]?\"[186-204]?\"[226-248]?\"[263-285]?\"[316-338]?\"[353-373]?\"[392-412]?\"[433-453]?transmembrane_regions


","BeTs to 14 clades of COG0733COG name: Na+-dependent transporters of the SNF familyFunctional Class: RThe phylogenetic pattern of COG0733 is aom-k--q----b---gh-nu--it-Number of proteins in this genome belonging to this COG is","Significant hit ( 4.6e-36) to 5/7 blocks of the IPB000175 family, which is described as \"Sodium:neurotransmitter symporter family\". Interpro entry for IP:IPR000175. IPB000175A 16-65 1.6e-15 IPB000175B 110-144 1.9 IPB000175C 155-206 28 IPB000175D 220-272 1.8e-09 IPB000175E 305-344 8.6e-05","Residues 199 to 236 match (4e-10) PD:PD485661 which is described as TRANSPORTER NEUROTRANSMITTER TRANSMEMBRANE SYMPORT GLYCOPROTEIN CHLORIDE-DEPENDENT SODIUM- SODIUM-DEPENDENT GABA PROTEOME ","","","","","","","","","","","","Wed Jan 8 10:06:58 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01815 is paralogously related to AA00884 (1e-49).","","","","","","Residues 8 to 424 (E-value = 3.4e-14) place AA01815 in the SNF family which is described as Sodium:neurotransmitter symporter family (PF00209)","","","","","","","","1","","","" "AA01816","1224096","1224194","99","TTGTTGGTTGTAGATGTGGCTGACTTTCGGCTGAGTCTCGTTAATGCCGAAAAATATACCGGTCCAATTAAACAAAACGGATTTATCGGTTATTCATAC","","","3673","LLVVDVADFRLSLVNAEKYTGPIKQNGFIGYSY","1224194","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-16]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 10:36:04 2004","Thu Feb 26 10:36:04 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01816 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 10:36:04 2004","","","","","","","","","","","","","1","","","" "AA01817","1224365","1224460","96","TTGATGAATCAGAATAGGCAATACATGAATATTTTCGTTATTAGGGAGATAAAGTGCGGTTATTTTTTTCGGCAAATTTTAACCCTGCTGTTTTTT","","","4043","LMNQNRQYMNIFVIREIKCGYFFRQILTLLFF","1224460","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 10:24:36 2004","Thu Feb 26 10:24:36 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01817 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 10:24:36 2004","","","","","","","","","","","","","1","","","" "AA01818","1225138","1224446","693","ATGGCGTATTTCGGCGACACCCTTTCTCACTCGGCACTCCTCGGTGTAGCATTAGGAATTTTTCTGCAAATCAATCCTTACATTGCTATTTTAGCACTCACCTTGTTGCTTTCCATCGCGCTGGTATGGCTGGAAAATAACACTCAGTTTTCCATCGATACCCTGCTCGGCATTATCGCCCACAGTTGCCTTTCCATCGGCGTGGTTACGGTCGGCTTGCTGAAAAATGTGCGGGTGGATTTAATGTCTTATTTGTTCGGCGATTTACTGGCAATTAACTATCAGGATTTATGGTATATCGGCATTGGCGCAATTATTGTGTTAGCGGCACTATGCTATTTCTGGAAGCCGTTAATTTCCGCGACCATCAGCCCGGAACTGGCGCAAGTGGAAGGCATTAACGTGAAAAAAATGCGTTTTATTCTGATGATCTTAACCGCTTTAACCATCGCCTTAAGCATGAAATTCGTCGGTGCATTGATCATCACTTCACTACTGATTATTCCTGCCGCCACCGCCCGACGCTTCGCCCGCACGCCGGAAACTATGGCCATTATCGCCGTCTTCATCAGTATGATCGCTGTCTCCCTCGGTTTGACCTTATCCGCATACTACGACACCGCCGCCGGTCCTTCCGTGGTTATCTGCTCTACATTCCTGTTTCTTTGTTCTTTATTAAAAAAACAGCAGGGT","","","28324","MAYFGDTLSHSALLGVALGIFLQINPYIAILALTLLLSIALVWLENNTQFSIDTLLGIIAHSCLSIGVVTVGLLKNVRVDLMSYLFGDLLAINYQDLWYIGIGAIIVLAALCYFWKPLISATISPELAQVEGINVKKMRFILMILTALTIALSMKFVGALIITSLLIIPAATARRFARTPETMAIIAVFISMIAVSLGLTLSAYYDTAAGPSVVICSTFLFLCSLLKKQQG","1224445","","high-affinity zinc uptake system membrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR001626
Family
ABC-3
PF00950\"[1-228]TABC-3
noIPR
unintegrated
unintegrated
signalp\"[1-44]?signal-peptide
tmhmm\"[12-46]?\"[52-74]?\"[95-115]?\"[140-169]?\"[184-204]?\"[208-226]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.1e-64) to 5/5 blocks of the IPB001626 family, which is described as \"ABC 3 transport family\". Interpro entry for IP:IPR001626. IPB001626A -15-31 0.068 IPB001626B 38-72 8e-12 IPB001626C 80-97 6.7e-09 IPB001626D 147-192 9.1e-24 IPB001626E 193-225 1.4e-12","Residues 2 to 94 match (2e-11) PD:PD487877 which is described as PROTEOME COMPLETE STY4525 STY1595 ","","","","","","","","","","","Thu May 13 13:38:02 2004","Wed Jan 8 10:10:10 2003","","","Thu May 13 13:38:02 2004","Thu May 13 13:38:02 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01818 is paralogously related to AA02552 (3e-24), AA02551 (3e-23), AA02153 (2e-06) and AA00796 (4e-05).","Thu May 13 13:38:02 2004","","","","","Residues 1 to 228 (E-value = 3.4e-96) place AA01818 in the ABC-3 family which is described as ABC 3 transport family (PF00950)","Thu May 13 13:38:02 2004","","","","Patzer,S.I. and Hantke,K. The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli. Mol. Microbiol. 28 (6): 1199-1210 (1998) PubMed: 9680209.","","Wed Feb 5 15:18:48 2003","1","","","" "AA01820","1226013","1225243","771","ATGCAAATTAGTGCAATCAGACTGCCTTTAGTCGAGTTAAAAAACATCAATGTGAAATTCGGACAACAAGCCGCTTTGCAAAACATTAACCTGACTGTTTACCCCAATTCGATCATCACTATTGTCGGGCCAAACGGTGGCGGCAAATCCACCTTATTGAAAGTGCTGCTAAAACTGCAACAGCCTACTTCCGGCAACGTGATTTACAATAAAAATATTCGTATTGGTTATGTGCCGCAAAAAATCTATCTGGATCCCAATCTGCCGATCACCGTGGAGAAATTTTTATCCCTGAAAAAAGGCATCCGCCCACAGGATATCCGGCAAGCAATGGCACTACTATCTATTAGCCACCTCATCCATAACAGTATGCAAAAGCTGTCCGGCGGCGAAATGCAGCGCGTATTGTTAGCACGTGCTATTTTAAATAAACCAAGTTTATTGGTATTAGATGAGCCCACTCAGGGTGTGGACATCGCCGGACAGGCTGAGCTGTATCAGCTCATTCACCAAACCCGCGAAAACCTGAATTGCGCGATTCTCATGGTGTCGCATGATTTACATATTGTAATGGCAGACACCAACGAAGTGTTGTGCATTAATCAGCATATTTGCTGCGCCGGCACGCCGGAAACCGTCTCCAACGATCCGACCTTTATTCACTTTTTCGGAGATCAATTTTCCAAAAATATTGCTGTTTATACACACCATCACAATCACCGGCACGATATGCACGGTAACATTCACCGTGTGGAACCAAAACAATCTCAA","","","28728","MQISAIRLPLVELKNINVKFGQQAALQNINLTVYPNSIITIVGPNGGGKSTLLKVLLKLQQPTSGNVIYNKNIRIGYVPQKIYLDPNLPITVEKFLSLKKGIRPQDIRQAMALLSISHLIHNSMQKLSGGEMQRVLLARAILNKPSLLVLDEPTQGVDIAGQAELYQLIHQTRENLNCAILMVSHDLHIVMADTNEVLCINQHICCAGTPETVSNDPTFIHFFGDQFSKNIAVYTHHHNHRHDMHGNIHRVEPKQSQ","1225242","[FUNCTION] Involved in the high-affinity zinc uptake transport system (by similarity). [SIMILARITY] Belongs to the ABC transporter family. ","high-affinity zinc uptake system ATP-binding protein","Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[128-169]TQ9HT73_PSEAE_Q9HT73;
PF00005\"[36-203]TABC_tran
PS50893\"[11-226]TABC_TRANSPORTER_2
PS00211\"[127-141]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[35-205]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[11-224]Tno description
PTHR19222\"[11-217]TATP BINDING CASSETE (ABC) TRANSPORTER


","No hits to the COGs database.","Significant hit ( 5.8e-31) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 25-71 2.6e-16 IPB001140B 124-162 6.9e-13 IPB001140C 179-208 1e+02Significant hit ( 7.5e-05) to 1/5 blocks of the IPB001482 family, which is described as \"Bacterial type II secretion system protein E\". Interpro entry for IP:IPR001482. IPB001482B 35-57 7.6e-05","Residues 26 to 70 match (4e-09) PD:PD000005 which is described as ATP-BINDING COMPLETE PROTEOME ABC TRANSPORTER TRANSPORTER PROBABLE TRANSMEMBRANE COMPONENT PLASMID ","","","","","","","","","","","Wed Jan 8 10:19:29 2003","Fri Jan 24 13:38:42 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01820 is paralogously related to AA00700 (8e-25), AA01645 (4e-24), AA02550 (3e-23), AA01656 (1e-22), AA01051 (2e-22), AA02718 (3e-22), AA02353 (3e-22), AA02152 (1e-21), AA01824 (1e-21), AA01616 (1e-19), AA01684 (4e-19), AA02324 (7e-19), AA02140 (2e-18), AA00858 (2e-18), AA00799 (2e-18), AA02573 (3e-18), AA00415 (7e-18), AA02440 (9e-18), AA01456 (1e-17), AA01422 (2e-17), AA02320 (2e-17), AA01510 (1e-16), AA02898 (2e-16), AA02080 (2e-16), AA02484 (4e-16), AA02899 (2e-15), AA01779 (2e-15), AA00933 (2e-15), AA01867 (2e-15), AA02786 (3e-15), AA02225 (4e-15), AA01555 (7e-15), AA02805 (2e-14), AA01568 (2e-14), AA00207 (3e-14), AA01524 (5e-14), AA02609 (8e-14), AA01509 (1e-13), AA01569 (5e-12), AA00751 (1e-11), AA00591 (2e-11), AA02331 (3e-11), AA01757 (7e-11), AA01961 (1e-10), AA00934 (3e-10), AA00061 (6e-10), AA01393 (9e-10), AA02606 (1e-08), AA01947 (5e-08), AA02146 (3e-07), AA02642 (6e-07), AA01291 (7e-07), AA02226 (8e-06) and A02145 (2e-04).","","","","","","Residues 36 to 203 (E-value = 3.8e-45) place AA01820 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Patzer,S.I. and Hantke,K. The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli. Mol. Microbiol. 28 (6): 1199-1210 (1998) [PubMed: 9680209].","","Wed Jan 8 10:19:29 2003","1","","","" "AA01822","1226202","1227731","1530","GTGCAACATATAAAACTGGCAAGAGATCGCCGCAAAAGAAAATCGCGTATTAAAGCGATTGTTTTTTTTATTGCGCTTTTTTCTATTTTTGCCGGTTTTTTTTTGCATTTAAATGATTCTGCCTCCAAAAAAATCGACACTGTCAATAATCCGACTTACTCCTATTTCTCCTCAAAAGGTAACGATTTTGCCAATGGCAGTGATCAATTTCAAGATATTTTATCCGACGATCTTTACCCGGCTTCTGCTTACACTATGTCGTTCGCCAACGAAGTTTCCCATGAATTACGGATTCTGGCAGATACTCTGGGTATCAGCACAATTGATAATAACGCCACCTCTTATGACGATGATGTCGGCAAAGATGATGAAGTGGAAGAAGTCAAAACTCACGACGAATTTGATGATTTGGATAAATTGCCGGACGATGCGAAAAATGCGATCACCAATATTTTAGATGTTGCCGATCAGGCGATTCGGATTAAAGATCAGTTCAGTCACACCGTTGTCAAAGGAGATGCCTTAAAAGACGTGTTGGAGTTGTCCGGTTTGGAAGATGACACCAGTAAACAGCTTATCGCTTCTTATCCGGAATTGAAACATTTACAGGCAGGGCAACAATTTTACTGGATTTTAAATAATGACGGAGAGCTGGAATATTTGAACTGGCTGGTTTCCCAGAAAAAAGAACACATTTATGAACTTCAGACAGATGGCAAATTTAAACGCCAAATTGTGGAGAAAAAAAGTGTTTGGAAACGTGAAGTGTTGCGTGGCGAAATGGAAGGATCTTTCGTCAGCAGCCTGAAGAAACTCGGTTTGGATAATCGTCAGATTTATCAATTATTCTCTGCGTTACAATGGCAGGTCAGCCTGAAACAACTGAAAAAAGGCACGAAGATTTCTATTTTGGTTTCCCGTGAATATCTGGAAGACAAACGGACCGGGCAGGGTAATGTGGAAGCCATTCATATTGTGAGCAGCGGCAAAAGTTATTATGCGATCCAAGCCAGCAACGGTCGTTATTACAACCGCCAGGGGGAAACCTTAGGTAAAGGCTTTGCCCGTTACCCGTTGCAACGTCAGGCGCGCGTTTCATCTCCGTTTAATCCGCGTCGCCGCCATCCGATTACGGGACGCATTGCACCACATAAAGGGGTGGATTTTGCGATGCCGACAGGGACACCGGTTATTGCGCCGGCAGACGGCACGGTAGAGAAAATCGCCTATCAGGCTTACGGTGCCGGTCGTTATGTGGTGCTACGCCACTCCCGTGAATACCAAACCGTGTATATGCACCTCAGCAGACCGCTAGTAAAAGTAGGGCAAACAGTGAAAAAAGGGGAGCGTATCGCGTTGTCCGGCAACACCGGCGGTTCTACCGGCCCGCATTTGCACTACGAATTCCATATTAACGGGCGTCCGGTCAATCCGCTTACCGTTAAACTTCCGGGGGGAAGCAGCGGCATAGGTACGGCGGAACGTAAACAATTCCTTGTTAAAGCCAACGAAGTAGAACGCTTGTTGCGC","","","57495","VQHIKLARDRRKRKSRIKAIVFFIALFSIFAGFFLHLNDSASKKIDTVNNPTYSYFSSKGNDFANGSDQFQDILSDDLYPASAYTMSFANEVSHELRILADTLGISTIDNNATSYDDDVGKDDEVEEVKTHDEFDDLDKLPDDAKNAITNILDVADQAIRIKDQFSHTVVKGDALKDVLELSGLEDDTSKQLIASYPELKHLQAGQQFYWILNNDGELEYLNWLVSQKKEHIYELQTDGKFKRQIVEKKSVWKREVLRGEMEGSFVSSLKKLGLDNRQIYQLFSALQWQVSLKQLKKGTKISILVSREYLEDKRTGQGNVEAIHIVSSGKSYYAIQASNGRYYNRQGETLGKGFARYPLQRQARVSSPFNPRRRHPITGRIAPHKGVDFAMPTGTPVIAPADGTVEKIAYQAYGAGRYVVLRHSREYQTVYMHLSRPLVKVGQTVKKGERIALSGNTGGSTGPHLHYEFHINGRPVNPLTVKLPGGSSGIGTAERKQFLVKANEVERLLR","1227730","","lysostaphin precursor","Outer membrane, Inner membrane, Cytoplasm, Extracellular","","
InterPro
IPR002886
Family
Peptidase M23B
PTHR21666:SF7\"[361-481]TM23/M37 PEPTIDASE FAMILY MEMBER
PF01551\"[382-478]TPeptidase_M23
noIPR
unintegrated
unintegrated
PTHR21666\"[361-481]TPEPTIDASE-RELATED
signalp\"[1-32]?signal-peptide
tmhmm\"[20-38]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 7.4e-34) to 2/2 blocks of the IPB002886 family, which is described as \"Peptidase family M23/M37\". Interpro entry for IP:IPR002886. IPB002886A 384-409 3.5e-12 IPB002886B 418-458 2.7e-20","Residues 354 to 481 match (7e-10) PD:PD488132 which is described as PROTEOME COMPLETE ALR4007 SLL1488 ","","","","","","","","","","","","Wed Jan 8 10:24:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01822 is paralogously related to AA01407 (4e-10) and AA00450 (1e-09).","","","","","","Residues 398 to 481 (E-value = 4.4e-41) place AA01822 in the Peptidase_M37 family which is described as Peptidase family M23/M37 (PF01551)","","","","","","","","1","","","" "AA01823","1227807","1227703","105","GTGCGGTGGTTTTCTCAGGTGTTTTTAAAAACACTTAAAAAACCCACCGCACTTTTTAGAAACGGGTTTGAAATCAGCGCAACAAGCGTTCTACTTCGTTGGCTT","","","4136","VRWFSQVFLKTLKKPTALFRNGFEISATSVLLRWL","1227703","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 10:22:11 2004","Thu Feb 26 10:22:11 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01823 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 10:22:11 2004","","","","","","","","","","","","","1","","","" "AA01824","1228600","1227845","756","GTGATTAAAATCGAAAATATCACCTATAAGATCGGTCATGCCACCATTTTAAATAACATCAATCTCACCATTCCCAATGGCGGGATTACCGCCCTCATCGGCGCTAACGGCGCGGGGAAATCGACCTTGTTGTCTTTAATCGCCCGTCTCAATCCCATTCAGCAGGGAAAGATTTGGTTAAATGAAATGGATATTGCCACCACGCCATCGCGCATCATCGCGCAGAATCTGGCGATTTTAACCCAAGATAACGTGATTCATAGCCGTATTACCGTGCAGGATCTGCTCTTTTTCGGGCGCTACCCGCATCACCAAGGCAGACCGACGGAAGAAGATAAAAACATTATTCAGGCGGCATTAAAACGTTTCGATTTGGATGCACTCGCCTACCGTTTTTTAAGCGAACTTTCCGGCGGGCAACGGCAACGGGCGCTGATTGCCATGACGTTCTGCCAAAAGACCGATCACGTTCTGTTGGATGAACCGCTCAATAATCTGGATATATTCCACGCCCGCGAACTCATGCGCCTGTTACGCCAACTCACCAACGAACTGGCACTCACCACCGTGATGGTAGTCCACGACATCAACATGGCCGCTGCCTATGCGGACATCATCGTTGCCATGAAAAACGGCGAAATTGCCATGATAGGCACCCCGGAAGACATCATCACCAAAGCGAATTTAAAAACGATATTTAATCTGGACGCGGAAGTGCTGGAACATCAAGAAAAGCGTTTAGTGGTGCATCATATG","","","28180","VIKIENITYKIGHATILNNINLTIPNGGITALIGANGAGKSTLLSLIARLNPIQQGKIWLNEMDIATTPSRIIAQNLAILTQDNVIHSRITVQDLLFFGRYPHHQGRPTEEDKNIIQAALKRFDLDALAYRFLSELSGGQRQRALIAMTFCQKTDHVLLDEPLNNLDIFHARELMRLLRQLTNELALTTVMVVHDINMAAAYADIIVAMKNGEIAMIGTPEDIITKANLKTIFNLDAEVLEHQEKRLVVHHM","1227844","","iron(III) ABC transporter, ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[135-178]TQ9JXK8_NEIMB_Q9JXK8;
PF00005\"[27-212]TABC_tran
PS50893\"[2-236]TABC_TRANSPORTER_2
PS00211\"[136-150]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[26-213]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[2-234]Tno description
PTHR19222\"[2-244]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF31\"[2-244]TMETAL ABC TRANSPORTER


","BeTs to 14 clades of COG1120COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, ATPase componentsFunctional Class: P,HThe phylogenetic pattern of COG1120 is aompk---vdrlbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is","Significant hit ( 6.2e-28) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 16-62 4.2e-18 IPB001140B 133-171 2.5e-05 IPB001140C 189-218 0.23","Residues 188 to 237 match (5e-07) PD:PD467099 which is described as ATP-BINDING COMPLETE PROTEOME ABC TRANSPORTER TRANSPORTER VITAMIN IRON SYSTEM ATPASE ","","","","","","","","","","","","Wed Jan 8 10:28:27 2003","","","Tue Mar 16 14:41:28 2004","Tue Mar 16 14:41:28 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01824 is paralogously related to AA00799 (2e-40), AA00700 (6e-30), AA02718 (1e-28), AA01645 (6e-27), AA02550 (7e-26), AA01656 (2e-23), AA02152 (7e-23), AA02324 (1e-21), AA01820 (1e-21), AA01051 (5e-21), AA00858 (9e-21), AA01510 (2e-20), AA02140 (1e-19), AA01867 (8e-19), AA02320 (1e-18), AA00415 (3e-18), AA02440 (4e-18), AA01779 (4e-18), AA01947 (7e-18), AA01393 (7e-18), AA02805 (2e-17), AA01422 (2e-17), AA01684 (5e-17), AA02353 (1e-16), AA01456 (3e-16), AA02080 (4e-16), AA02898 (7e-16), AA01961 (7e-16), AA01524 (7e-16), AA02484 (2e-14), AA01616 (1e-13), AA00933 (1e-13), AA02899 (2e-13), AA01757 (4e-13), AA01509 (5e-13), AA02609 (1e-12), AA00751 (2e-12), AA02573 (3e-12), AA02606 (2e-11), AA02786 (4e-11), AA01555 (5e-11), AA02146 (6e-11), AA01568 (6e-11), AA01569 (3e-10), AA00207 (9e-10), A02145 (3e-09), AA02331 (5e-09), AA00061 (5e-09), AA00934 (2e-08), AA00591 (1e-06), AA02225 (2e-06), AA02226 (6e-06), AA02642 (2e-04) and AA01291 (6e-04).","Tue Mar 16 14:41:28 2004","","","","","Residues 27 to 212 (E-value = 2.3e-49) place AA01824 in the ABC_tran family which is described as ABC transporter (PF00005)","Tue Mar 16 14:41:28 2004","","","","","","","1","","","" "AA01825","1229553","1228615","939","ATGGGAAATAATCGCAGAATGCCCTTCCTTTGCCTGTTGCTCACGTTCGCCTGTGTATTTTTCATGAGTTACAACGCCAACGGCAACTGGGATTTCGTGTTACCGTTCCGTGGAAAAAAACTTTTATTATTGCTTATCATGGCTTACACCATCGGGATTTCCACGCTATTGTTCCAAACCCTGACCAACAACCCAATTCTCACCCCGAGCATTTTGGGCTTCGATTCCTTATATTTATTGGTGCAAAGCATTTTAGTTTTCTCCTTTGGCGGCATCGGCTTCACGCAATTAAATATCGCCGGCAAATTTGCCTTTGAAACCCTGTTAATACTGTTCGGGGCTTTATTATTATTTCGCACCTTAACCAAAAATAACAGCGATTTGGCGCGCATGATTTTGGTAGGGATTATTTTCGGCGTACTGTTCCGCAGTCTGAATAATTTACTGCAACGCATGATCGACCCGAACGAATTTGCCGTGGCGCAAGGCTCTTCCTTCGCCAGTTTTAATACGGTGAATCCAATCTTACTTTGGATCGGCACGGCGATCACACTTATCAGCGCCGTCTGGATTTGGCAGCAACGGTTTAAATTAGACGTGTTATTACTCGGACGTGATCGCGCCATCGGGCTCGGTTTGGAATACCACCAATTTAGCCGAAAACTTTTGATTTGCTGCGCATTTTTGGTCTCCGTTTCCACCGCACTTGTCGGCCCGATTCTGTTTTTAGGCTTATTGGTATGCGCTATCGTCAACGCCATCAGCCCAACCATGCACCACAGTCAACGTATCCCTATGACATTTATGGTATCCGCTATCACCCTTGTAAGCGGGCAAGCCTTATTTGAGCAAGTGATGAAAATGCAGGGCGTGCTCAGTGTGGTCATTGAATTCGTCGGCGGTTTGGTGTTCATCTATTTAATGTTAAGACGGGCAAAA","","","34840","MGNNRRMPFLCLLLTFACVFFMSYNANGNWDFVLPFRGKKLLLLLIMAYTIGISTLLFQTLTNNPILTPSILGFDSLYLLVQSILVFSFGGIGFTQLNIAGKFAFETLLILFGALLLFRTLTKNNSDLARMILVGIIFGVLFRSLNNLLQRMIDPNEFAVAQGSSFASFNTVNPILLWIGTAITLISAVWIWQQRFKLDVLLLGRDRAIGLGLEYHQFSRKLLICCAFLVSVSTALVGPILFLGLLVCAIVNAISPTMHHSQRIPMTFMVSAITLVSGQALFEQVMKMQGVLSVVIEFVGGLVFIYLMLRRAK","1228614","From InterPro: IPR000522Bacterial transport system permease protein.This is a subfamily of bacterial binding-protein-dependent transport systems family, and includes transport system permease proteins involved in the transport across the membrane of several compounds. This entry contains the inner components of this multicomponent transport system.","iron(III) ABC transporter, permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR000522
Family
Bacterial transport system permease protein
PF01032\"[51-247]TFecCD
noIPR
unintegrated
unintegrated
PS51257\"[1-18]TPROKAR_LIPOPROTEIN
signalp\"[1-28]?signal-peptide
tmhmm\"[9-27]?\"[41-61]?\"[76-94]?\"[100-118]?\"[128-146]?\"[174-192]?\"[222-256]?\"[289-309]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 9.8e-23) to 3/3 blocks of the IPB000522 family, which is described as \"FecCD transport family\". Interpro entry for IP:IPR000522. IPB000522A 37-78 2.4e-13 IPB000522B 238-252 0.1 IPB000522C 287-310 0.00024","Residues 127 to 195 match (1e-08) PD:PD583613 which is described as PROTEOME COMPLETE PERMEASE MEMBRANE INNER ABC SYSTEM ANGUIBACTIN FERRIC IRON ","","","","","","","","","","","Tue Mar 16 14:49:35 2004","Wed Jan 8 10:33:40 2003","","","Tue Mar 16 14:50:28 2004","Tue Mar 16 14:48:03 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01825 is paralogously related to AA00798 (7e-15), AA01826 (3e-14), AA00796 (3e-12), AA02153 (8e-11), AA02144 (5e-09) and AA02637 (0.001).","Tue Mar 16 14:48:03 2004","","","","","Residues 3 to 310 (E-value = 1.7e-17) place AA01825 in the FecCD family which is described as FecCD transport family (PF01032)","Tue Mar 16 14:48:03 2004","","","","Richardson PT, Park SF.Enterochelin acquisition in Campylobacter coli: characterization of components of a binding-protein-dependent transport system.Microbiology. 1995 Dec;141 ( Pt 12):3181-91.PMID: 8574410Kster WL, Actis LA, Waldbeser LS, Tolmasky ME, Crosa JH.Molecular characterization of the iron transport system mediated by the pJM1 plasmid in Vibrio anguillarum 775.J Biol Chem. 1991 Dec;266(35):23829-33.PMID: 1748657","","Tue Mar 16 14:49:35 2004","1","","","" "AA01826","1230508","1229546","963","ATGCCGAACATTTTCACCCTGAACCGAATTAATTTTGTCCTTCTCCTTTTACTCACCGTGGGCAGCATTACCGTCGGTGTTGCGGATTTTCATTGGGCACAATTTTTTACCCAACCGGAGCAAATGCAGGTATTGCTTATCAGCCGCTTGCCGAGAACCGCCGCCGTGATTTTAGTAGGCGCCACACTTGGCGTGGCGGGCATGGTGTTGCAAATCGTACTGAAAAACCGCTTTATTGAACCCAGCATGATCGGTGCCAGTCAAAGTGCGGCAGTGGGTGTGTTATTGGTGAGTCTGCTCTTTCCAAGTACGGCGCTCCTTCTCAAAATGTCGATAGCCACGCTGAGCGCACTCATCGGCATGGGAATCTTTATGTTATTGCTCCAACGTCTGCCTCCGCATCAAAGCCTGATGGTGCCGTTGGTGGGGATTGTATTCGGTAACATCATTGAAGCGATCACCACCTTTATTGCTTACGAAACGGACAGCATACAACTGCTTTCTATCTGGTTTGCCGGGGATTTCTCCGCTGTTCTGGCGGGGCGTTACGAACTTCTGTGGCTTACCGCCATTCTTGCTGTCGTGGTTTATATTATGGCGGATCAACTAAGCATCACCGGCTTGGGGCGCAATATCAGCACCGCGTTAGGCATTAATTATCGTCAAATGACGTGGTTTGCCTTAATCGTGGTGGCGATGATTACGGCGGTTGTGGTGGTAACCGTCGGGCAAATTCCTTTTATCGGGCTGGTTGTACCGAACATTATTTCCCGCCTTTCCGGCGATCGCCTGCGACAAAATTTGCCTTCCGTGGTGTTGCTCGGCGCAAATTTGGTGTTAATGTGCGACATTGCGGGACGGGTTATCAATGCGCCTTATGAAGTGCCGATTTCAACGGTGTTCGGCATTGTCGGCACCTTGATTTTCCTCTATTTATTATTTAAGGGGAACGCCCATGGGAAA","","","34649","MPNIFTLNRINFVLLLLLTVGSITVGVADFHWAQFFTQPEQMQVLLISRLPRTAAVILVGATLGVAGMVLQIVLKNRFIEPSMIGASQSAAVGVLLVSLLFPSTALLLKMSIATLSALIGMGIFMLLLQRLPPHQSLMVPLVGIVFGNIIEAITTFIAYETDSIQLLSIWFAGDFSAVLAGRYELLWLTAILAVVVYIMADQLSITGLGRNISTALGINYRQMTWFALIVVAMITAVVVVTVGQIPFIGLVVPNIISRLSGDRLRQNLPSVVLLGANLVLMCDIAGRVINAPYEVPISTVFGIVGTLIFLYLLFKGNAHGK","1229545","[FUNCTION] Part of the binding-protein-dependent transport system for ferric anguibactin. Probably responsible for the translocation of the substrate across the membrane. [SUBCELLULAR LOCATION] Integral membrane protein. inner membrane (potential). [SIMILARITY] Belongs to the binding-protein-dependent transport system permease family. fecCD subfamily. ","iron(III) ABC transporter, permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR000522
Family
Bacterial transport system permease protein
PF01032\"[14-315]TFecCD
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[34-164]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-28]?signal-peptide
tmhmm\"[12-32]?\"[54-74]?\"[84-102]?\"[108-128]?\"[137-159]?\"[185-205]?\"[226-248]?\"[267-285]?\"[295-313]?transmembrane_regions


","BeTs to 18 clades of COG0609COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, permease componentsFunctional Class: P,HThe phylogenetic pattern of COG0609 is aompkz--vd-lbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-31) to 3/3 blocks of the IPB000522 family, which is described as \"FecCD transport family\". Interpro entry for IP:IPR000522. IPB000522A 49-90 4.6e-16 IPB000522B 243-257 8.8e-05 IPB000522C 292-315 1e-07 IPB000522C 107-130 0.37","Residues 208 to 313 match (7e-10) PD:PD001557 which is described as PROTEOME COMPLETE PERMEASE ABC SYSTEM TRANSPORTER IRON MEMBRANE TRANSPORTER TRANSMEMBRANE ","","","","","","","","","","","Wed Jan 8 10:38:07 2003","Wed Jan 8 10:35:53 2003","","","Thu Mar 11 14:08:38 2004","Thu Mar 11 14:08:38 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01826 is paralogously related to AA00796 (2e-30), AA00798 (5e-29), AA02144 (2e-24), AA02153 (9e-24) and AA01825 (3e-14).","Thu Mar 11 14:08:38 2004","","","","","Residues 21 to 315 (E-value = 1.9e-46) place AA01826 in the FecCD family which is described as FecCD transport family (PF01032)","Thu Mar 11 14:08:38 2004","","","","Koster,W.L., Actis,L.A., Waldbeser,L.S., Tolmasky,M.E. and Crosa,J.H. Molecular characterization of the iron transport system mediated by the pJM1 plasmid in Vibrio anguillarum 775. J. Biol. Chem. 266 (35): 23829-23833 (1991) [PubMed: 1748657].","","Wed Jan 8 10:38:07 2003","1","","","" "AA01827","1231467","1230571","897","ATGTTGAAAAAGACATTATTGGCATTAAGCTGTCTCGCGTTGGCGACATCCGCTTTGGCAAAAGAAGTCACGATTCCCACTGCGCGCGGTGAAGTGACGTTGGATGCGCCACCGGCAAAAATTGCGGTGTTTGATACCGGCAGTTTGGACACCCTGCAAGCCTTGGGCATAAAAGTGGATGGCGCGGCAGATGTGAGCAAGGTTCTCCCTTATTTAAAACCGACCTTGGAACAAGCCAAAAATGTCGGGACGATTTTTGAACCGAATCTGGAAGCCTTAAATGAATTAAAACCGGATTTAATTATTGTCGGTACCCGTACGGCGAAAAAATTTGATGATGTGAGTGCCATTGCCAAAACCGTGGATTTGACGGATAACGGCGACAAATTGATTAAAAGCGGTATTCAACGCATTGATAGCTTCGGCAAATTATTTAATAAACAAGCGGAAGCGGATAAATTAAAAGCGGAGCTCGAAACCTTGTTTAAACAAACCAAAGACGCAGTAAAAGGCAAGGGTAACGGTTTAATTATTTTAGTCAACGGCGGCAAGATTTCCGCCTTCGGTAAAGGCTATCGTTTAAGTTTTATTCACGAGGATCTCGGCGTGCCGATGGCAGATCCAAGCATAAACGTCAGCGGTCATGGTCAACCGATCAGTTTTGAATTTATTGAGAAAACCAATCCGGATTGGTTGTTTGTGTTAGATCGCATTTCCGCTATCGGGCAGGAAGGGAAAGGCGCCAAAGAAGTATTGGATAACGAATTAATTCGTCACACCAAAGCCTGGAAAAACGGCAATATCGTGTATTTAAGCAGCGCCTCTTACCTTGCGCCGGGTGGTGCGGAACAATTAAAAATGGATTTGAATAACATCAAAGCCGCCTTTGAGAAAAAA","","","32864","MLKKTLLALSCLALATSALAKEVTIPTARGEVTLDAPPAKIAVFDTGSLDTLQALGIKVDGAADVSKVLPYLKPTLEQAKNVGTIFEPNLEALNELKPDLIIVGTRTAKKFDDVSAIAKTVDLTDNGDKLIKSGIQRIDSFGKLFNKQAEADKLKAELETLFKQTKDAVKGKGNGLIILVNGGKISAFGKGYRLSFIHEDLGVPMADPSINVSGHGQPISFEFIEKTNPDWLFVLDRISAIGQEGKGAKEVLDNELIRHTKAWKNGNIVYLSSASYLAPGGAEQLKMDLNNIKAAFEKK","1230570","","iron(III) ABC transporter, periplasmic binding protein","Periplasm","","
InterPro
IPR002491
Family
Periplasmic binding protein
PF01497\"[38-275]TPeripla_BP_2
PS50983\"[40-299]TFE_B12_PBP
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1980\"[34-123]Tno description
signalp\"[1-20]?signal-peptide


","No hits to the COGs database.","","Residues 161 to 214 match (1e-07) PD:PD487765 which is described as COMPLETE PROTEOME ENTEROBACTIN ABC PROTEIN PERIPLASMIC SOLUTE-BINDING BINDING FERRIC TRANSPORTER ","","","","","","","","","","","Tue Mar 16 14:53:34 2004","Wed Jan 8 10:40:21 2003","","","","Tue Mar 16 14:52:14 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01827 is paralogously related to AA00795 (2e-12) and AA02380 (3e-04).","Tue Mar 16 14:52:14 2004","","","","","Residues 38 to 275 (E-value = 4.6e-46) place AA01827 in the Peripla_BP_2 family which is described as Periplasmic binding protein (PF01497)","Tue Mar 16 14:52:14 2004","","","","Actis LA, Tolmasky ME, Farrell DH, Crosa JH.Genetic and molecular characterization of essential components of the Vibrio anguillarum plasmid-mediated iron-transport system.J Biol Chem. 1988 Feb;263(6):2853-60.PMID: 2830268Kster WL, Actis LA, Waldbeser LS, Tolmasky ME, Crosa JH.Molecular characterization of the iron transport system mediated by the pJM1 plasmid in Vibrio anguillarum 775.J Biol Chem. 1991 Dec;266(35):23829-33.PMID: 1748657","","Tue Mar 16 14:53:34 2004","1","","","" "AA01829","1231722","1231543","180","TTGAATAAAACGTCTTCGATTCATCATAATAAGATCCTTAGTTTTAGGGAAAGACGGCGTTATTGTAAGGCAAATGGGCGGGGCTTTGAAAGGAAAAGTGCGGTCATAAAATTCATCGGATTTTTTGACCGCACTTTAATTCTTTATAACGACAGAAAACAAATCAATTTCCCGCAAAAT","","","7227","LNKTSSIHHNKILSFRERRRYCKANGRGFERKSAVIKFIGFFDRTLILYNDRKQINFPQN","1231542","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Jan 8 10:50:33 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01829 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01830","1231696","1233669","1974","ATGATGAATCGAAGACGTTTTATTCAAATTGGTGCGAGCAGTGTTTTGGCGCTGAGTTGCCATCCGATGGCGTTTGCCAAAAACGGGAATCAGGTGGATTTGCGCATTATCGGCACCACCGATATTCACAGCTTTTTGACGGATTTTGATTATTACAAAGACGCGCCGACGGAGAAATTCGGCTTTACCCGCGCGGCAAGTTTGATCCGCCAAGCCCGTGCGGAAGTGAAAAACAGCGTGCTGGTGGATAACGGCGATTTGATTCAGGGCAACCCGATTGCCGATTATCAGGCGGCAGTAGGCTATAAAGAAGGTGAGCCGAACCCGGCAATCGCCTGTTTGAACGCCTTGCATTATGAGGTAGGCACCTTGGGCAATCATGAATTTAATTATGGTTTGGATTATTTAGCTGACGCCATCAAACAGGCGAATTTCCCCATTGTGAACGCCAATGTGGTGAAAGCGGGAACCGATGATCCTTATTACACGCCCTATGTGATTCAGGAAAAAACGGTGGTGGACAACAACGGCAAATCCCATCCGTTAAAAATCGGTTACATCGGTTTTGTGCCGCAGCAAATTATGGTGTGGGATAAAGCCAATTTAACCGACAGAGTGGAAACCCGCGATATTGTCAAAACCGCACAAAAATATGTGCCGGAAATGAAGCAAAAAGGTGCGGATATTATCGTTGCCTTGGCGCATACCGGGCCATCCGATGAGCCGTATCACGAAGGGGCGGAAAATTCCGCTTTCTATCTCGCCGATGTGCCGCATATTGATGCGGTGATTTTTGGCCATTCCCACCGTTTGTTCCCGAATAAAGAATTTGCCAAATCGCCGAATGCGGACATTGCCAAGGGCACGGTGAAAGGTGTGCCGGAAAGCATGGCGGGCTACTGGGCGAACAATATCAGCGTAGTAGATTTGGTATTGAGCGAACATAATGGCAAATGGATTGTGACCGACGGGAAAGCCGTATTGCGCCCGATTTATGATGTGGAAAACAAAAAGCCGTTAGCGGAAAATGACGCAGAAATGACCGCACTTTTGAAAGAAACGCATGACGCCACCCGTAAATTCGTGGCGCAGCCAATCGGTAAAGCCACCGATAATATGTACAGCTATTTGGCGCTGGTGCAGGATGACCCGACCATTCAAATCGTTAACCAAGCGCAAAAAGCCTATGTGGAAAACGTGGCGCCAAGCGTGCCGGCAATGGCGGGCTTGCCGATTTTAAGTGCGGGCGCGCCGTTTAAAGCGGGCGGTCGGAAAAACGATCCGACGGGGTACACTGAAGTGAACAAAGGCGAATTAACTTTCCGTAATGCGGCGGATTTGTATTTGTATCCGAACACCTTGGTTGTCGTGAAAGTCAATGGCGAGCAATTGAAAGAATGGTTGGAATGCAGTGCGGGAATGTTTAAACAAATTGATCCGGGCAGTGACAAACCGCAACCTTTATTGGATTGGGAAGGCTTTCGCACCTATAATTTCGATGTCATCGATGGCGTCAATTACGAATATGATTTAACCCAACCGCCGCGTTATGACGGCGAATGTAAGCTTATCAATCCGAACGCCCACCGCGTGGTGAATTTGACCTATCAAGGCAAAGCGGTGGATCCGAAAGCGGAATTTTTAATCGCCACCAACAATTATCGTGCTTATGGCGAAAAATTCCCCGGCACCGGCGATAAACACATTGTTTATGCGTCGCCGGATGAAAATCGTCAGGTGTTGGCGGATTACATCAAAGCCACCAGCGAGAAAGAAGGCAGCGTAAACCCAAGTGCCGATAAAAACTGGCGTTTTTTGCCGATCAAAGGCAACGCGAAATTAGATGTACGCGTTGAAACTTCACCAAGTGCGCAGGCAACGCAATTCATCAAGGAAAACGCGCAGTATCCGATGAAACAGGTGGGCACCGATGAAGTAGGATTTGCCGTACATCAAATTGATTTATCGGGCAAA","","","72699","MMNRRRFIQIGASSVLALSCHPMAFAKNGNQVDLRIIGTTDIHSFLTDFDYYKDAPTEKFGFTRAASLIRQARAEVKNSVLVDNGDLIQGNPIADYQAAVGYKEGEPNPAIACLNALHYEVGTLGNHEFNYGLDYLADAIKQANFPIVNANVVKAGTDDPYYTPYVIQEKTVVDNNGKSHPLKIGYIGFVPQQIMVWDKANLTDRVETRDIVKTAQKYVPEMKQKGADIIVALAHTGPSDEPYHEGAENSAFYLADVPHIDAVIFGHSHRLFPNKEFAKSPNADIAKGTVKGVPESMAGYWANNISVVDLVLSEHNGKWIVTDGKAVLRPIYDVENKKPLAENDAEMTALLKETHDATRKFVAQPIGKATDNMYSYLALVQDDPTIQIVNQAQKAYVENVAPSVPAMAGLPILSAGAPFKAGGRKNDPTGYTEVNKGELTFRNAADLYLYPNTLVVVKVNGEQLKEWLECSAGMFKQIDPGSDKPQPLLDWEGFRTYNFDVIDGVNYEYDLTQPPRYDGECKLINPNAHRVVNLTYQGKAVDPKAEFLIATNNYRAYGEKFPGTGDKHIVYASPDENRQVLADYIKATSEKEGSVNPSADKNWRFLPIKGNAKLDVRVETSPSAQATQFIKENAQYPMKQVGTDEVGFAVHQIDLSGK","1233668","[FUNCTION] This bifunctional enzyme catalyzes two consecutive reactions converting 2',3'-cyclic-nucleotide to 3'-nucleotide and then 3'-nucleotide to nucleic acid and phosphate (by similarity).[CATALYTIC ACTIVITY] Nucleoside 2',3'-cyclic phosphate + H(2)O = nucleoside 3'-phosphate. [SUBCELLULAR LOCATION] Periplasmic (by similarity).[SIMILARITY] Belongs to the 5'-nucleotidase family. ","2,3-cyclic-nucleotide 2-phosphodiesterase","Periplasm","","
InterPro
IPR004843
Domain
Metallophosphoesterase
PF00149\"[34-271]TMetallophos
InterPro
IPR006146
Domain
5'-Nucleotidase, N-terminal
PS00786\"[119-130]T5_NUCLEOTIDASE_2
InterPro
IPR006179
Family
5'-Nucleotidase and apyrase
PR01607\"[32-50]T\"[225-242]T\"[253-276]T\"[293-313]T\"[438-461]T\"[540-559]TAPYRASEFAMLY
PTHR11575\"[10-475]T\"[491-638]T5'-NUCLEOTIDASE-RELATED
InterPro
IPR006294
Family
2 ,3 -cyclic-nucleotide 2 -phosphodiesterase
TIGR01390\"[32-657]TCycNucDiestase: 2',3'-cyclic-nucleotide 2'-
InterPro
IPR008334
Domain
5'-Nucleotidase, C-terminal
G3DSA:3.90.780.10\"[417-589]Tno description
PF02872\"[365-566]T5_nucleotid_C
noIPR
unintegrated
unintegrated
G3DSA:3.60.21.10\"[26-364]Tno description
PTHR11575:SF6\"[10-475]T\"[491-638]T2,3-CYCLIC-NUCLEOTIDE 2-PHOSPHODIESTERASE
PS51257\"[1-20]TPROKAR_LIPOPROTEIN
signalp\"[1-26]?signal-peptide


","BeTs to 13 clades of COG0737COG name: 5'-nucleotidase/2',3'-cyclic phosphodiesterase and related esterasesFunctional Class: FThe phylogenetic pattern of COG0737 is aom---yqvd-lbce-gh--uj--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 6.2e-18) to 6/9 blocks of the IPB002224 family, which is described as \"5'-Nucleotidase\". Interpro entry for IP:IPR002224. IPB002224A 32-50 12 IPB002224B 78-86 1.8e+02 IPB002224C 117-136 7.5e-05 IPB002224D 143-152 0.1 IPB002224E 228-237 0.1 IPB002224I 539-562 0.086","Residues 436 to 585 match (7e-09) PD:PD302725 which is described as HYDROLASE COMPLETE PROTEOME 5'-NUCLEOTIDASE PRECURSOR SIGNAL UDP-SUGAR ZINC GLYCOPROTEIN 5'-NT ","","","","","","","","","","","Wed Jan 8 10:55:55 2003","Wed Jan 8 10:55:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01830 is paralogously related to AA00536 (2e-18).","","","","","","Residues 365 to 566 (E-value = 5.8e-73) place AA01830 in the 5_nucleotid_C family which is described as 5'-nucleotidase, C-terminal domain (PF02872)","","","","","Liu,J., Burns,D.M. and Beacham,I.R. Isolation and sequence analysis of the gene (cpdB) encoding periplasmic 2',3'-cyclic phosphodiesterase. J. Bacteriol. 165 (3): 1002-1010 (1986) [PubMed: 3005231].Liu,J. and Beacham,I.R. Transcription and regulation of the cpdB gene in Escherichia coli K12 and Salmonella typhimurium LT2: evidence for modulation of constitutive promoters by cyclic AMP-CRP complex. Mol. Gen. Genet. 222 (1): 161-165 (1990) [PubMed: 2172762].","","Wed Jan 8 10:55:55 2003","1","","","" "AA01832","1234663","1233749","915","ATGAGCATCCGAATTCTTCCCGAAAATGAAATTAAACAGGCGGCAGCCTCTTATGTCACCCCGCCGCTGCTTTTCTCCAATCCGAAAAATTTATATCAGCGCCGCGCCGCGCGTCTAAGAGAATTGGCGCAAGATCACCCGCTCGCCAATTATTTGCTGTTCGCCGCCGCTATCGCAGATGCGCAGCTGGAACTCTTGGAAACCATGCCGATTCCGCAGGATCCGCGTTTACAGGCACTCTCTGCCGAACAATTGGGAAATAAGCCTTTAGACGTTAAAAGCCGGCAACGGGATCCCATTTGGCGCGAATTATTGACCGCACTTTTGGCGAAATTAAAACCTTCCGCCAACGATCAAACGCTCGCCACCATCGAATGGCTGGAAAAAGCGGCAGACAGCGAATTGGAAAATCTTGCCGATAAGGTTTTAGCACAGGAATTTGCGGTGATTTCCAGCGACAAAGCGGTGTTCGTGTGGGCGGCGCTTTCTTTATATTGGTTGCAATTAGTCCAACAGATTCCCTACAACGCCAAACAGGAAAGCACCGAAAACCTGCACATCTGCCCTGTTTGCAGCTCTGCGCCGACCGCCAGCATGATTCATTTCGGCGCGAAGCAAGGCTTGCGTTACCTGCACTGCTCCTTGTGCGAAAGCGAATGGAACATGGTGCGCAACCAATGCACCAACTGCGGACAAAGCAGCGACTTGGATTATTGGTCTTTTGACGAATACCTGGCGGCGATCCGAAGTGAGAGCTGTGGGAACTGCCATAGCTATTTGAAAGCTCTATATCAAGAGAAAGATCCGAAAATGGAAGTCATCGCCGACGATTTGGCGTCCATCTTTCTGGATATGGAAATGGAGAAAAAAGGCTTTATGAAAAGCGGCTTGAACCCGTTTGTGTTCCCGCCGGAA","","","34402","MSIRILPENEIKQAAASYVTPPLLFSNPKNLYQRRAARLRELAQDHPLANYLLFAAAIADAQLELLETMPIPQDPRLQALSAEQLGNKPLDVKSRQRDPIWRELLTALLAKLKPSANDQTLATIEWLEKAADSELENLADKVLAQEFAVISSDKAVFVWAALSLYWLQLVQQIPYNAKQESTENLHICPVCSSAPTASMIHFGAKQGLRYLHCSLCESEWNMVRNQCTNCGQSSDLDYWSFDEYLAAIRSESCGNCHSYLKALYQEKDPKMEVIADDLASIFLDMEMEKKGFMKSGLNPFVFPPE","1233748","[FUNCTION] Soluble protein involved in formation of formate dehydrogenase (by similarity). ","formate dehydrogenase formation protein E","Periplasm, Cytoplasm","","
InterPro
IPR006452
Family
Formate dehydrogenase accessory protein
PIRSF018296\"[1-305]TFormate dehydrogenase accessory protein FdhE
PF04216\"[6-302]TFdhE
TIGR01562\"[2-303]TFdhE: formate dehydrogenase accessory prote


","No hits to the COGs database.","","Residues 104 to 183 match (5e-19) PD:PD391747 which is described as PROTEOME COMPLETE DEHYDROGENASE FDHE FORMATION FORMATE ","","","","","","","","","","","Wed Jan 8 10:59:03 2003","Wed Jan 8 10:59:03 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01832 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 6 to 302 (E-value = 1.1e-166) place AA01832 in the FdhE family which is described as Protein involved in formate dehydrogenase formation (PF04216)","","","","","Schlindwein,C. and Mandrand,M.A. Nucleotide sequence of the fdhE gene involved in respiratory formate dehydrogenase formation in Escherichia coli K-12. Gene 97 (1): 147-148 (1991) [PubMed: 1995428].Stewart V, Lin JT, Berg BL. Genetic evidence that genes fdhD and fdhE do not control synthesis of formate dehydrogenase-N in Escherichia coli K-12. J Bacteriol. 1991 Jul;173(14):4417-23. PMID: 1648557 Bokranz M, Gutmann M, Kortner C, Kojro E, Fahrenholz F, Lauterbach F, Kroger A. Cloning and nucleotide sequence of the structural genes encoding the formate dehydrogenase of Wolinella succinogenes. Arch Microbiol. 1991;156(2):119-28. PMID: 1781728 ","","Wed Jan 8 10:59:03 2003","1","","","" "AA01834","1234992","1234780","213","TTGCTTTGTTGCGAGCTATTAAACGAAACAAAAGTTAAGAAAGTATTAAGTCCAACACTTTTTTATAAAAAAGGAAAAATTATGCGTTATGACCAAATGTCTGCCTTCATTGTGATGGATATTGTACGGGAAGCCGCGAAATGTACCGACGGCAGCTATAAATTCGCCAAACTACGACCTACACCCGCAATATCGAGCATTTGTAGGAAGGCG","","","8046","LLCCELLNETKVKKVLSPTLFYKKGKIMRYDQMSAFIVMDIVREAAKCTDGSYKFAKLRPTPAISSICRKA","1234780","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 10:20:19 2004","Thu Feb 26 10:20:19 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01834 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 10:17:11 2004","","","","","","","","","","","","","1","","","" "AA01835","1235036","1235449","414","ATGAAGAAACGCAGTTTAGCAACAATTTTAGTATTATCAACCATCGCTGCTACCGGCGTGTTTGCACAAGGCGGTTTTCAAGACCCGAATGCGCCGAAAATGGAACACCACAAAAAAGGTGATTTCAAACGTGGCGGTTTTGTGAATACCGATCAAACGGTGAGCAAAGCTTCTGAAGCCGGTTCCTGGCAAGATGATCAATACATCATTTTACAGGGTAACATCGTGAAACAAGTGGGCAAAGATGACTTTATCTTTAAAGATGCCAGCGGCGAAATCCAAGTGGAAATCGAACGCAAAGCCTGGCGCGGACAGGATGTTTCCCCAAGCGATGAAGTGAAACTTTACGGCGAAGTGGATAAATCCTGGAATAAGACCGAAGTGGATATTGAACGCGTAGAAAAAATTGTAAAA","","","16122","MKKRSLATILVLSTIAATGVFAQGGFQDPNAPKMEHHKKGDFKRGGFVNTDQTVSKASEAGSWQDDQYIILQGNIVKQVGKDDFIFKDASGEIQVEIERKAWRGQDVSPSDEVKLYGEVDKSWNKTEVDIERVEKIVK","1235448","","conserved hypothetical protein","Periplasm","","
InterPro
IPR005220
Family
Conserved hypothetical protein 156
G3DSA:2.40.50.200\"[30-138]Tno description
PF04076\"[1-135]TDUF388
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","","Residues 71 to 133 match (9e-12) PD:PD020872 which is described as COMPLETE PROTEOME PERIPLASMIC PLASMID SIGNAL PRECURSOR EXPORTED REGION OUTER YDEI ","","","","","","","","","","","","Fri Jan 31 14:13:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01835 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 135 (E-value = 1.7e-35) place AA01835 in the DUF388 family which is described as Domain unknown function (DUF388) (PF04076)","","","","","","","","1","","","" "AA01837","1235590","1236456","867","ATGCGGATTTTATTAATCGAAGATGATCCTTTAATCGGTAACGGCATTCAAATTGGGTTGACCAAATCCGGTTTCGCCGTGGATTGGTTTACCGACGGCAAAACCGGATTGGAAGCGGCGCAGTCGGCGCCTTATGATGCAGTGGTGCTGGATTTAACCTTGCCGAAAATGGACGGGCTGGATGTGTTGCAGGCATGGCGTAAAAACGGGCAGGATGTGCCGGTGCTGATTCTTACCGCGCGGGATACTCTGGATGAGCGCATTACCGGCTTGCAACGCGGTGCGGACGATTATTTGTGTAAGCCGTTTGCCCTGGCGGAAGTGGTGGCACGTTTGCAGGCACTGATTTGTCGTCGCTACGGACACGCCAAGACAATGACTAAATATTTCGCTTATGACGCGTTAGAACGTGAGTTCACGACACATGAAACACTAGAAGAAGCTAAATCAAAAGCGCAAGATTTTGTTGATCAAACTTTTGAATTCGGCGCTAATGATGGATTTCATACTGACCTTGAAAACGCTATAAAAGAAGGGTGCTTTGGGGTTGTATTAGGCGGGTTTGATTTACCAACCCGACCTCTCACCAAAGAGGAGGAGGATATTTACGGTGATCAGTACACTCACATGGTTGACAATCCAGTGCTTGTTGAATATCCACAAAACAATGGATGGATTAAGTGTTCGGAGCGATTGCCAGACGGCTGGAGTGAAGTTTTATTTGCAATGAAGATACCGGAATCCGAATCCGGGTGGCTAATTAGAACGGGCAGCTACTTTGAAGATGGTATGGGATTTTGCAGTTTTGACGGTGTAGAGTTTGAAGGTGTAACACATTGGAAACCGTTACCAAAACCGCCAACAGAA","","","32392","MRILLIEDDPLIGNGIQIGLTKSGFAVDWFTDGKTGLEAAQSAPYDAVVLDLTLPKMDGLDVLQAWRKNGQDVPVLILTARDTLDERITGLQRGADDYLCKPFALAEVVARLQALICRRYGHAKTMTKYFAYDALEREFTTHETLEEAKSKAQDFVDQTFEFGANDGFHTDLENAIKEGCFGVVLGGFDLPTRPLTKEEEDIYGDQYTHMVDNPVLVEYPQNNGWIKCSERLPDGWSEVLFAMKIPESESGWLIRTGSYFEDGMGFCSFDGVEFEGVTHWKPLPKPPTE","1236455","[FUNCTION] Member of a two-component regulatory system qseB/qseC.[SUBCELLULAR LOCATION] Cytoplasmic (Potential).[PTM] Phosphorylated by qseC (Probable).","transcriptional regulatory protein","Cytoplasm","","
InterPro
IPR001789
Domain
Response regulator receiver
PD000039\"[1-116]TQ9CP46_PASMU_Q9CP46;
PF00072\"[1-113]TResponse_reg
SM00448\"[1-112]TREC
PS50110\"[2-116]TRESPONSE_REGULATORY
InterPro
IPR007539
Domain
Protein of unknown function DUF551
PF04448\"[224-288]TDUF551
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2300\"[1-152]Tno description
PTHR23283\"[2-116]TSENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF47\"[2-116]TSENSORY TRANSDUCTION HISTIDINE KINASE (DHKB)


","No hits to the COGs database.","Significant hit ( 2.6e-29) to 2/4 blocks of the IPB001867 family, which is described as \"Transcriptional regulatory protein, C terminal\". Interpro entry for IP:IPR001867. IPB001867A 46-59 2e-05 IPB001867B 74-118 1.8e-22Significant hit ( 2.7e-13) to 3/3 blocks of the IPB001789 family, which is described as \"Response regulator receiver domain\". Interpro entry for IP:IPR001789. IPB001789A 4-10 5.2 IPB001789B 46-59 0.00061 IPB001789C 94-103 1.3e-05","Residues 1 to 116 match (4e-53) PD:PD000039 which is described as SENSORY TRANSDUCTION PHOSPHORYLATION COMPLETE PROTEOME REGULATOR RESPONSE TRANSCRIPTION DNA-BINDING REGULATION ","","","","","","","","","","","Wed Jan 8 11:04:26 2003","Wed Jan 8 11:04:26 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01837 is paralogously related to AA00997 (1e-17), AA02902 (4e-13), AA00959 (7e-12) and AA00757 (2e-08).","","","","","","Residues 224 to 288 (E-value = 5.9e-10) place AA01837 in the DUF551 family which is described as Protein of unknown function (DUF551) (PF04448)","","","","","Sperandio,V., Torres,A.G. and Kaper,J.B. Quorum sensing Escherichia coli regulators B and C (QseBC): a novel two-component regulatory system involved in the regulation offlagella and motility by quorum sensing in E. coli. Mol. Microbiol. 43 (3): 809-821 (2002) [PubMed: 11929534].Dorrell,N., Spencer,S., Foulonge,V., Guigue-Talet,P., O'Callaghan,D. and Wren,B.W. Identification, cloning and initial characterisation of FeuPQ in Brucella suis: a new sub-family of two-component regulatory systems. FEMS Microbiol. Lett. 162 (1): 143-150 (1998) [PubMed: 9595675]. ","","Wed Jan 8 11:04:33 2003","1","","","" "AA01838","1236536","1237003","468","ATGGAACGAAAAGAAGCAAGAAGAAAGCAATTAATTCAGCTTATACACATTGGGAAAAGTAAGTTACAGATGGATAAAGAGGTTTATCGCCTTTTTCTTGTTAATACAGTGGGCAAAGATAGCTGCACGCAGATGAATTTGATTGAGTTAAACAAGGTTGTGAACGCCATGAAAAAACGCGGTTTTCAGGTTTCCGGCGGGCGTTTTAAAGACGGCAAACGTAAATCGCCACCGAGTTCCGCGCATGTGAGCAGTAATATCGTTAAAAAGATCCGAGCTAAATGGATAGAAATGGCAGACGCAGGCATTATCCGTGACAGAAGCGAAGACGGTTTAAATGCGTTCGTTAAAAATATCGCAAAAAATGAACAGGGCGAGCCGATTCCTTTTGTGAGTTGGCTCAATAATGCGCAGGCGTCGATTGTGTTAGAACGCCTTAAACAATGGCAAAAAAGAACGATTAAGGAG","","","17887","MERKEARRKQLIQLIHIGKSKLQMDKEVYRLFLVNTVGKDSCTQMNLIELNKVVNAMKKRGFQVSGGRFKDGKRKSPPSSAHVSSNIVKKIRAKWIEMADAGIIRDRSEDGLNAFVKNIAKNEQGEPIPFVSWLNNAQASIVLERLKQWQKRTIKE","1237002","","conserved hypothetical protein","Periplasm, Cytoplasm","","
InterPro
IPR009363
Family
Protein of unknown function DUF1018
PF06252\"[7-156]TDUF1018


","No hits to the COGs database.","","Residues 8 to 147 match (1e-17) PD:PD035966 which is described as PROTEOME COMPLETE GP16 FLUMU NMA1867 E16-RELATED ECS4960 NMA1301 E16 PROPHAGE ","","","","","","","","","","","","Wed Jan 8 11:05:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01838 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 156 (E-value = 7.5e-49) place AA01838 in the DUF1018 family which is described as Protein of unknown function (DUF1018) (PF06252)","","","","","","","","1","","","" "AA01839","1237010","1237351","342","ATGAAACCGTCACTAATGGAAATCCGCCGCCATGAACTTCTTGAAGAAATCGAATCGCTGGTGATTGCGCTATGTAAAAATTACAACTTAGGGCAGGACATTTGTGAGCAGATTGGCGCTAACGTTGCCAACTGTTTATGCGAAGAATTTGCCGGGCAGGTCATTGCGTTTCCTAAAGACTACTTCTATAAAATTGCTCAACGTGATCTGGAAATCTATAATAGTTTTAACGGCAGAAATTGGGGTGAGCTTGGGCGTAAATATGACTTAACGGAGAATGCTTTGAGGAAGATTGTTAAACGTATTACCCCTAACTTCACTGTTTCTTTTCCGTTTACGCCG","","","13207","MKPSLMEIRRHELLEEIESLVIALCKNYNLGQDICEQIGANVANCLCEEFAGQVIAFPKDYFYKIAQRDLEIYNSFNGRNWGELGRKYDLTENALRKIVKRITPNFTVSFPFTP","1237350","","conserved hypothetical protein (possible transcriptional regulator)","Cytoplasm","","
InterPro
IPR014875
Domain
Mor transcription activator
PF08765\"[8-107]TMor
noIPR
unintegrated
unintegrated
PD015023\"[50-102]TQ7VLE1_HAEDU_Q7VLE1;


","No hits to the COGs database.","","Residues 50 to 102 match (3e-07) PD:PD015023 which is described as DNA-BINDING PROTEOME COMPLETE C TRANSCRIPTION CYTOPLASMIC FLUMU REGULATION REGULATOR BACTERIOPHAGE ","","","","","","","","","","","","Fri Jan 31 14:16:31 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01839 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01840","1237614","1237228","387","ATGCAAAGCAAACGCCTGAAACGTAGTACGCTTATTTCACGGGGCGACCGCTTTTGCGAGGGGTGGGTTGTCGGCGTGAATCAAAATGTGAAGCAATTTGCAATGACACCGCAAGAAAAACAAAAAATGGCTCACTATAAAACCTCAATGTTTGAGGATGAAAAATGGAGTGACACAAAAGTGCGATCAGCCGGTGACACGAGAGATTACGGTGCATCACAAAGCGCAGGTTACAGACAAGGACAACAAGTTACGCTGAATCACGGCGTAAACGGAAAAGAAACAGTGAAGTTAGGGGTAATACGTTTAACAATCTTCCTCAAAGCATTCTCCGTTAAGTCATATTTACGCCCAAGCTCACCCCAATTTCTGCCGTTAAAACTATTA","","","14658","MQSKRLKRSTLISRGDRFCEGWVVGVNQNVKQFAMTPQEKQKMAHYKTSMFEDEKWSDTKVRSAGDTRDYGASQSAGYRQGQQVTLNHGVNGKETVKLGVIRLTIFLKAFSVKSYLRPSSPQFLPLKLL","1237227","","conserved hypothetical protein","Periplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Jan 8 11:10:46 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01840 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01841","1237654","1237923","270","GTGTTAGACCCGCCATATTTGTGTACGAAACAAGAGAGCTATAAGCAAGCGCATTATTTCGATCTTATCGACTTCCTACGCTTAATTAACATTACACGACCACCGTATATCTTCTTCTCATCGACAAAAAGCGAGTTCGTGCGGTTTATTGAGTATATGTGTGAGGATAAAGTCAATAATTGGCAGGCATTTGATGGTGCACAAAGAATTACGATTAAGACAAACCTCAACTACCAAGGGCAATATGAAGATAATTTGGTTTATAAATTT","","","10878","VLDPPYLCTKQESYKQAHYFDLIDFLRLINITRPPYIFFSSTKSEFVRFIEYMCEDKVNNWQAFDGAQRITIKTNLNYQGQYEDNLVYKF","1237922","","conserved hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","Residues 19 to 75 match (7e-15) PD:PD128473 which is described as PROTEOME COMPLETE NMA1821 NMA1330 HI1523 ","","","","","","","","","","","","Wed Jan 8 11:11:43 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01841 is paralogously related to AA02008 (5e-51).","","","","","","","","","","","","","","1","","","" "AA01842","1238411","1238527","117","GTGAGCAGTAACGCGCTGGAAGTGCATATTTACAACCTGCGCCAAAAGCTCGGCAAACAATTTATTCGCACCGTTCACGGCGTGGGCTATGCACTGGGAAAAAATGATGAAACTGAG","","","4368","VSSNALEVHIYNLRQKLGKQFIRTVHGVGYALGKNDETE","1238527","","conserved hypothetical protein","Cytoplasm","This sequence is similar to gi|15602079, a predicted YgiX from Pasteurella multocida. Also see gi|42631936 and gi|16273595.","
InterPro
IPR001867
Domain
Transcriptional regulatory protein, C-terminal
PD000329\"[1-30]TQ9RBI0_ACIAD_Q9RBI0;
PF00486\"[1-32]TTrans_reg_C
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[1-35]Tno description


","BeTs to 15 clades of COG0745COG name: Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domainFunctional Class: T,KThe phylogenetic pattern of COG0745 is -------qvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.7e-05) to 1/4 blocks of the IPB001867 family, which is described as \"Transcriptional regulatory protein, C terminal\". Interpro entry for IP:IPR001867. IPB001867D 18-32 2e-05","Residues 1 to 32 match (3e-11) PD:PD000329 which is described as DNA-BINDING COMPLETE PROTEOME TRANSCRIPTION REGULATOR SENSORY TRANSDUCTION REGULATION PHOSPHORYLATION RESPONSE ","","","","","","","","","","","","Thu Feb 26 10:14:26 2004","Thu Feb 26 10:14:26 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01842 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 10:14:26 2004","","","","","","","","","","","","","1","","","" "AA01843","1238517","1239890","1374","ATGAAACTGAGTAAGTGGAATAATTACAGCCTGCGTTTTCGTTTGATTGTCACCTTGTCGCTGGTGTCGGTGTGCGTGTGGCTGATTTCCACGGCGGTGGCTTGGTTTCAGGTGCGTAAAGAAGTGAACCAAGTGTTTGACGCACAACAAATTTTATTTGCCCAACGTCTGGCGTCTTCCGATTTACGCACCATTTTAATCGGTCATCAACGTGGCAAACCGTCGCATAAACGCCACGGTTTTAAAAGACCGGATTATGAAGATGACGCCTTAGCTTTTGCGATTTTTGCGCCGGACGGGGATATTTTATTGAGCGACGGCGAAAATGGGGAAAACTTTATTTTTGCGCCGGCGCGTGGCTTCAGTAAATCCCGTCTGCGGGAAGATGATGACGAATGGCGTATTTTCTGGCTTCCGGTGGGAGACGGACCGCTCATGATCGCCGTAGGGCAGGAACAGGAATATCGCGATGACTTAGTAAATGAAATGGTGTTTGGGCAAATGTGGATTTGGTTTGCCGGCTTGCCGTTTTTACTGCTCGCTCTCGGATTGGTGATTCGCAAAGAGTTAAAAAGCCTGAAACAAATCGGTGAACAAGTGGCAAAACGTACGCCTGATGATGCGTCTTTGTTGAAAACGGAAAATATCCCGACGGAAATCCTGCCGCTCATTCAAAGTTTGAATCAGTTTTTTGACCGCACTTCTTCCATGTTATTGCGTGAACGGCGTTTTACCTCCGACGCCGCCCACGAATTACGCAGCCCGCTTGCGGCGTTGCGTATTCAAACGGAAGTGGCGCAAATTGCCGGTGATGACGCCAATATGCGTGAACAGGCGTTGGATAATTTAACCCAAGGTATCGACCGTGCGACGCAATTAATTGAACAATTATTAACCCTTTCCCGTTTGGACAGTTTGCAGGAATTGGATAATTTACAGGAAATTCATTGGGAGCAAATTGTTCCGTCCCTTATCGGCGACCTGTATTTTCATGCGGAAAAACGTGATATTACTCTTGAGTTTGAAGAAATTGCCGTGCCGGCAGTGAAGCTGGGGCAGCCGTTGTTGCTTTCTTTAATGTTGCGCAACCTTATCGACAACGCCATTCGTTATTGCCCGCAAGGTAGCCGCATTAAAGTGCGGTTAGAAAAATCCAAGATTGCGGTGGAAGACAACGGCGGTGGCGTAGACGACGCCGATCTCGCCAAACTCGGACAACGCTTTTATCGCCCGGCGGGACAGAACGAAAAAGGCAGCGGCTTGGGCTTATCCATCGTTCACCGTATCGCCGAATTGCATCACTACAAAGTGCGGTTAAAAAATACCACGGATCTGAATGGCAACCGAATGGGTTTGTTGGCAGAGATTCAGTTG","","","52834","MKLSKWNNYSLRFRLIVTLSLVSVCVWLISTAVAWFQVRKEVNQVFDAQQILFAQRLASSDLRTILIGHQRGKPSHKRHGFKRPDYEDDALAFAIFAPDGDILLSDGENGENFIFAPARGFSKSRLREDDDEWRIFWLPVGDGPLMIAVGQEQEYRDDLVNEMVFGQMWIWFAGLPFLLLALGLVIRKELKSLKQIGEQVAKRTPDDASLLKTENIPTEILPLIQSLNQFFDRTSSMLLRERRFTSDAAHELRSPLAALRIQTEVAQIAGDDANMREQALDNLTQGIDRATQLIEQLLTLSRLDSLQELDNLQEIHWEQIVPSLIGDLYFHAEKRDITLEFEEIAVPAVKLGQPLLLSLMLRNLIDNAIRYCPQGSRIKVRLEKSKIAVEDNGGGVDDADLAKLGQRFYRPAGQNEKGSGLGLSIVHRIAELHHYKVRLKNTTDLNGNRMGLLAEIQL","1239889","[FUNCTION] Member of a two-component regulatory system qseB/qseC. Activates the flagella regulon by activating transcription of flhDC. May activate qseB by phosphorylation (By similarity).[SUBCELLULAR LOCATION] Integral membrane protein. Inner membrane (Probable).","sensor protein; probable two-component system sensor histidine kinase","Inner membrane, Cytoplasm","","
InterPro
IPR003594
Domain
ATP-binding region, ATPase-like
G3DSA:3.30.565.10\"[312-445]Tno description
PF02518\"[352-442]THATPase_c
SM00387\"[352-458]THATPase_c
InterPro
IPR003660
Domain
Histidine kinase, HAMP region
PF00672\"[168-236]THAMP
InterPro
IPR003661
Domain
Histidine kinase A, N-terminal
PF00512\"[240-306]THisKA
SM00388\"[240-306]THisKA
InterPro
IPR004358
Domain
Histidine kinase related protein, C-terminal
PR00344\"[385-399]T\"[417-435]TBCTRLSENSOR
InterPro
IPR005467
Domain
Histidine kinase
PS50109\"[247-458]THIS_KIN
noIPR
unintegrated
unintegrated
G3DSA:1.10.287.240\"[230-302]Tno description
PTHR23283\"[10-458]TSENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF23\"[10-458]TSENSORY TRANSDUCTION HISTIDINE KINASE (BACTERIAL SENSOR PROTEIN)
signalp\"[1-34]?signal-peptide
tmhmm\"[15-35]?\"[168-186]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 2.3e-09) to 3/3 blocks of the IPB003661 family, which is described as \"His Kinase A domain\". Interpro entry for IP:IPR003661. IPB003661A 248-257 0.24 IPB003661B 363-372 0.0006 IPB003661C 389-397 3.7Significant hit ( 1.9e-08) to 2/4 blocks of the PR00344 family, which is described as \"Bacterial sensor protein C-terminal signature\". Prints database entry for PR:PR00344. PR00344A 385-399 0.73 PR00344C 417-435 1e-05","Residues 185 to 301 match (8e-09) PD:PD409745 which is described as KINASE TRANSFERASE PHOSPHORYLATION PROTEOME TCTE SENSORY COMPLETE TRANSDUCTION SYSTEM 2.7.3.- ","","","","","","","","","","","Wed Jan 8 11:19:38 2003","Wed Jan 8 11:19:38 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01843 is paralogously related to AA00995 (7e-17) and AA00757 (9e-10).","","","","","","Residues 352 to 457 (E-value = 1.1e-22) place AA01843 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase (PF02518)","","","","","Sperandio,V., Torres,A.G. and Kaper,J.B. Quorum sensing Escherichia coli regulators B and C (QseBC): a novel two-component regulatory system involved in the regulation offlagella and motility by quorum sensing in E. coli. Mol. Microbiol. 43 (3): 809-821 (2002) [PubMed: 11929534].","","Wed Jan 8 11:19:38 2003","1","","","" "AA01845","1241747","1239981","1767","ATGAAGAAATTCACAACAAAATGCTTACTCAGTAGCCTAGCGCTTTCTATTGCGATTGCCGTAGGCAGCTCGGCTATAGCGAATCCGCAAGCCCCTGCCATGACCGCAACGGAACTGGCAGCAGCCCGTTACGACAGCGCTAACGACATATTTCATCCTGTTTACGCCAAACATGGCATGGTCGCCAGTGAGCAAGGGTTAGCCAGTGAAGTGGGCGCGGCAATTTTACGCCAAGGCGGCAATGCCGTGGACGCCGCAGTTGCCGTGGGATTTGCTCTCGCCGTAGTATTACCGAACGCCGGTAACATCGGTGGCGGCGGTTTTATGGTGCTACATGATGCCAAGAGTGGCGAAAACTACTCCGTGGATTTCCGCGAAACTGCGCCGCTGAAAGCCCATCGTGATATGTATCTGGACAAAGACGGCAATGTCATTGACGGACGCTCCCTTTACACCCACTTCGCCGTCGGTGTGCCGGGCACTGTCGCCGGCATGGAATACGTCCTGAAAAAATGGGGCACCATGTCCCTCGCCCAAGTCGTTGAACCCGCCATTCAATTGGCGGAAAAAGGTTTTACCGTCGGTCCGATGCTCGCCAAAACGTTAAAAGAAGAAAAGGACAATTTGGGCAAATGGACATCATCCAAAGCTATTTTCTTTAAAGATGGAGAACCGTTAAAAGAAGGGGATTTGTTGGTGCAAAAAGATCTGGCGAATTCTTTAAAACTCATCGCTAAACAAGGCGCCAAAGCTTTTTATGAAGGCGACATTGCGAAAAAAATCGTCGCTGAAATGGAAAAGCACCAGGGTTTGATCACCATGGAGGATCTGAAAGGCTATAAAGCCATTGAACGCAAACCTGTTGAAGGCGAATATCGCGGTTTCAAAGTGGTCACCATGCCGCCACCAAGCTCCGGCGGGATTCATTTGGTACAAATTCTGAATATTCTGGAACGCTACCCTCTCGCTGATTATGGTGTAAACAGCGCAAAATCCATTCATTATCTAGCGGAAGCCATGAAACTTGCCTATGCCGACCGCTCCGAATATTTGGGTGATCCGGATTTCGTAAAAATTCCGATGAAAGGTTTAACCTCTAAAAAATATGCTGACCAATTGGCGCAAGGCATTAGCGAAGCGGCAGTAAAACCGGCGGCGGAAATCAAACCGGGACAACCGCAGCCTTATGAGAGCGACCAAACTACCCACTTCTCCGTAATGGATAAAAACGGCAACGCGGTGGCGGTGACTTATACGCTAAACTTCAATTTTGGCAGCGGCATTGTGGCAGCAGGCACCGGCATTTTGTTAAACGACGAAATGGATGACTTCTCCGCCAAACCGGGCGTACCGAACGGCTTCGGCTTAATCGGCGGCGAAGCCAACGCCATCGCCCCACAAAAACGTCCGCTTTCTTCCATGACACCAACTTTAGTCATGAAAGACAACAAACCTTGGTTAGTCACCGGCAGCCCGGGCGGCGCACGCATTATCACCACCGTGCTGCAAAGTATCGTCAACACTGTGGATCATAAAATGAACCCGGCGGAAGCCATCGTCACCCCGCGCGTCCACCATCAGTGGTTGCCTGACGAATTGCGTGTAGAAGAAGGTTTAAGCCCCGACACCTTGGCGATCCTAAAAGCCCAAGGCTACACCATCAAAGAAAAAGCCCCGATGGGACGTGTGCAAATTATCCAAGCCCGCGAAGACGGCTTCTACGGCTACTCCGACCCACGCAATCCGGAAGGGAAAACGGTCGGGTAT","","","63145","MKKFTTKCLLSSLALSIAIAVGSSAIANPQAPAMTATELAAARYDSANDIFHPVYAKHGMVASEQGLASEVGAAILRQGGNAVDAAVAVGFALAVVLPNAGNIGGGGFMVLHDAKSGENYSVDFRETAPLKAHRDMYLDKDGNVIDGRSLYTHFAVGVPGTVAGMEYVLKKWGTMSLAQVVEPAIQLAEKGFTVGPMLAKTLKEEKDNLGKWTSSKAIFFKDGEPLKEGDLLVQKDLANSLKLIAKQGAKAFYEGDIAKKIVAEMEKHQGLITMEDLKGYKAIERKPVEGEYRGFKVVTMPPPSSGGIHLVQILNILERYPLADYGVNSAKSIHYLAEAMKLAYADRSEYLGDPDFVKIPMKGLTSKKYADQLAQGISEAAVKPAAEIKPGQPQPYESDQTTHFSVMDKNGNAVAVTYTLNFNFGSGIVAAGTGILLNDEMDDFSAKPGVPNGFGLIGGEANAIAPQKRPLSSMTPTLVMKDNKPWLVTGSPGGARIITTVLQSIVNTVDHKMNPAEAIVTPRVHHQWLPDELRVEEGLSPDTLAILKAQGYTIKEKAPMGRVQIIQAREDGFYGYSDPRNPEGKTVGY","1239980","[CATALYTIC ACTIVITY] (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl-amino acid. [PATHWAY] ggt plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione. [SUBUNIT] This enzyme consists of two polypeptide chains, which are synthesized in precursor form from a single polypeptide.[SUBCELLULAR LOCATION] Periplasmic. [SIMILARITY] strong, to other ggt enzymes and to gl-7aca acylases","gamma-glutamyltranspeptidase precursor","Periplasm","","
InterPro
IPR000101
Family
Gamma-glutamyltranspeptidase
PR01210\"[81-106]T\"[155-173]T\"[173-192]T\"[271-287]T\"[301-320]T\"[401-419]T\"[425-443]T\"[466-481]T\"[490-507]TGGTRANSPTASE
PTHR11686\"[55-589]TGAMMA GLUTAMYL TRANSPEPTIDASES
PF01019\"[73-583]TG_glu_transpept
TIGR00066\"[59-580]Tg_glut_trans: gamma-glutamyltransferase
PS00462\"[401-425]TG_GLU_TRANSPEPTIDASE
noIPR
unintegrated
unintegrated
signalp\"[1-24]?signal-peptide
tmhmm\"[9-27]?transmembrane_regions


","BeTs to 13 clades of COG0405COG name: Gamma-glutamyltranspeptidaseFunctional Class: EThe phylogenetic pattern of COG0405 is ---p-zy--dr-bcefg-snuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 4.3e-51) to 3/3 blocks of the IPB000101 family, which is described as \"Gamma-glutamyltranspeptidase\". Interpro entry for IP:IPR000101. IPB000101A 397-436 1.3e-19 IPB000101B 454-498 2.9e-21 IPB000101C 504-558 1.6e-07","Residues 487 to 578 match (1e-11) PD:PD587194 which is described as TRANSFERASE GLUTATHIONE GGT SIMILAR GLUTAMYLTRANSFERASE TRANSMEMBRANE EG:23E12.1 GLYCOPROTEIN GAMMA-GLUTAMYLTRANSFERASE SIGNAL-ANCHOR ","","","","","","","","","","","Wed Jan 8 11:24:37 2003","Wed Jan 8 11:24:37 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01845 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 73 to 583 (E-value = 2.8e-263) place AA01845 in the G_glu_transpept family which is described as Gamma-glutamyltranspeptidase (PF01019)","","","","","Suzuki,H., Kumagai,H., Echigo,T. and Tochikura,T. DNA sequence of the Escherichia coli K-12 gamma-glutamyltranspeptidase gene, ggt. J. Bacteriol. 171 (9): 5169-5172 (1989) [PubMed: 2570061]. Hashimoto,W., Suzuki,H., Nohara,S. and Kumagai,H. Escherichia coli gamma-glutamyltranspeptidase mutants deficient in processing to subunits. Biochem. Biophys. Res. Commun. 189 (1): 173-178 (1992) [PubMed: 1360205].","","Wed Jan 8 11:24:37 2003","1","","","" "AA01846","1242225","1241983","243","ATGCTTGAAATTGATTCCGTTGAAATTCTGGGCTATGTGGCAACCTTAATTGTCGCCGCCTCCTTTTTGTTTAAGTCTATCGTGCCGCTTCGCATTGTAAACGGTATCGGCGCGGCGTTATTCGTCGTTTATGCCCTGATTACCCAAACCTACCCGGTGGCGTTACTGAACGCGTTTTTAGTCGTCGTACATATTTACCAGCTATGGCGTTTGAAAACCACCGGCAAAATCACCCGCATCGAA","","","8976","MLEIDSVEILGYVATLIVAASFLFKSIVPLRIVNGIGAALFVVYALITQTYPVALLNAFLVVVHIYQLWRLKTTGKITRIE","1241982","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
PD058023\"[7-68]TYH36_HAEIN_P44300;
signalp\"[1-38]?signal-peptide
tmhmm\"[9-29]?\"[35-69]?transmembrane_regions


","No hits to the COGs database.","","Residues 2 to 72 match (2e-14) PD:PD058023 which is described as COMPLETE PROTEOME TRANSMEMBRANE PM0424 VCA0743 HI1736 ","","","","","","","","","","","","Wed Jan 8 11:35:53 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01846 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01848","1243752","1242418","1335","ATGTCAAATACCATTTTGCAACACTTACCGAAAGGTGAAAAAGTCGGCATCGCCTTTTCCGGTGGCTTAGATACCAGCGCGGCATTGCTTTGGATGCGTCAAAAAGGCGCCATTCCTTGCGCTTACACCGCCAATTTAGGTCAACCGGACGAAGACGACTACAACGCAATCCCGCGTAAAGCGAAAGAATATGGCGCAGAAATGGCGCGTTTAATCGACTGCCGCACCCAATTGGCACAAGAAGGTATTGCTGCCATTCAATGCGGCGCCTTCCACGTTTCCACCGGCGGCGCCACCTATTTCAACACCACTCCGTTAGGTCGTGCGGTCACCGGCACCATGTTGGTATCCGCCATGAAAGAAGACGACGTACATATTTGGGGCGACGGCAGCACCTACAAGGGCAACGATATTGAACGTTTTTACCGCTACGGTTTATTAACCAACCCACAATTAAAAATCTATAAACCTTGGTTGGATCAACAATTTATCGACGAATTGGGTGGCCGTTTTGAAATGTCCAACTTCTTAATCGAAAACGGCTTCGACTACAAAATGTCCGTGGAAAAAGCCTACTCCACCGATTCCAATATGCTCGGCGCCACCCATGAAGCCAAAGACCTGGAATTCTTAAATTCCGGCATTCGTATCGTCAACCCGATCATGGGCGTGCCGTTCTGGCGTGAAGACGTACAAATCAAAGCGGAAGAAGTCACCGTGCGCTTTGAAGAAGGCGTGCCGGTGGCATTAAACGGCCAAACCTTTGATAACATCGTGGAATTATTCCTTGAAGCCAACCGCATCGGCGCTCGCCACGGTTTGGGTATGTCCGACCAAATCGAAAACCGTATCATTGAAGCCAAATCACGCGGCATTTACGAAGCCCCGGGCATGGCGTTATTGCATATCGCCTACGAACGTTTGGTGACCGGTATCCACAACGAAGACACCATCGAACAATACCGCATTAACGGTATCCGTTTAGGGCGTTTGTTATACCAAGGTCGCTGGTTCGATCCGCAAGCGTTAATGTTACGCGAAACCTCCCAACGTTGGGTGGCGCGTGCGGTTACCGGTGAAGTGACGCTAGAATTACGTCGTGGTAACGACTACTCCTTACTCAATACCGAATCGCCGAACTTAACCTATCATCCTGAACGGTTAAGTATGGAAAAAGTGGAAAATGCGCCATTCGATCCGCTCGATCGCATCGGTCAATTAACCATGCGCAATCTGGATATTATTGATACCCGCGATAAATTGGGCATTTATTCCGGCACCGGTTTATTGGCGGTGAACAAAGAATCTGCGTTGCCGCAGTTGTATAAAAAGGCG","","","49962","MSNTILQHLPKGEKVGIAFSGGLDTSAALLWMRQKGAIPCAYTANLGQPDEDDYNAIPRKAKEYGAEMARLIDCRTQLAQEGIAAIQCGAFHVSTGGATYFNTTPLGRAVTGTMLVSAMKEDDVHIWGDGSTYKGNDIERFYRYGLLTNPQLKIYKPWLDQQFIDELGGRFEMSNFLIENGFDYKMSVEKAYSTDSNMLGATHEAKDLEFLNSGIRIVNPIMGVPFWREDVQIKAEEVTVRFEEGVPVALNGQTFDNIVELFLEANRIGARHGLGMSDQIENRIIEAKSRGIYEAPGMALLHIAYERLVTGIHNEDTIEQYRINGIRLGRLLYQGRWFDPQALMLRETSQRWVARAVTGEVTLELRRGNDYSLLNTESPNLTYHPERLSMEKVENAPFDPLDRIGQLTMRNLDIIDTRDKLGIYSGTGLLAVNKESALPQLYKKA","1242417","[CATALYTIC ACTIVITY] ATP + L-citrulline + L-aspartate = AMP + diphosphate + L-argininosuccinate.[PATHWAY] Arginine biosynthesis; penultimate step.[SUBUNIT] Homotetramer (By similarity).","argininosuccinate synthetase","Cytoplasm","","
InterPro
IPR001518
Family
Argininosuccinate synthase
PTHR11587\"[10-422]TARGININOSUCCINATE SYNTHASE
PF00764\"[16-420]TArginosuc_synth
TIGR00032\"[14-422]TargG: argininosuccinate synthase
PS00564\"[18-26]TARGININOSUCCIN_SYN_1
PS00565\"[130-141]TARGININOSUCCIN_SYN_2
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620\"[3-190]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.90.1260.10\"[192-414]Tno description


","No hits to the COGs database.","Significant hit (5.6e-110) to 9/9 blocks of the IPB001518 family, which is described as \"Argininosuccinate synthase\". Interpro entry for IP:IPR001518. IPB001518A 17-28 6.4e-06 IPB001518B 36-48 0.0017 IPB001518C 52-94 2.8e-15 IPB001518D 104-142 6.6e-21 IPB001518E 190-206 7e-07 IPB001518F 235-248 4.3e-05 IPB001518G 266-309 6.8e-31 IPB001518H 331-340 3.8e-05 IPB001518I 357-368 9.9e-05","Residues 14 to 73 match (9e-25) PD:PD003544 which is described as PROTEOME COMPLETE LIGASE ARGININOSUCCINATE SYNTHASE BIOSYNTHESIS ARGININE ATP-BINDING CITRULLINE--ASPARTATE UREA ","","","","","","","","","","","Wed Jan 8 11:40:14 2003","Wed Jan 8 11:40:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01848 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 16 to 420 (E-value = 2.5e-185) place AA01848 in the Arginosuc_synth family which is described as Arginosuccinate synthase (PF00764)","","","","","Van Vliet,F., Crabeel,M., Boyen,A., Tricot,C.,Stalon,V., Falmagne,P., Nakamura,Y., Baumberg,S. and Glansdorff,N. Sequences of the genes encoding argininosuccinate synthetase in Escherichia coli and Saccharomyces cerevisiae: comparison with methanogenic archaebacteria and mammals. Gene 95(1): 99-104,1990. PubMed: 2123815. Lemke,C., Yeung,M. and Howell,P.L. Expression, purification, crystallization and preliminary X-ray analysis of Escherichia coli argininosuccinate synthetase. Acta Crystallogr. D 55: 2028-2030, 1999 ","","Mon Jan 27 14:53:35 2003","1","","","" "AA01850","1244674","1243850","825","ATGAGGTCGGTTGCGATTGTCGGCTTGGGTTGGTTAGGGTTGCCGTTGGCGCGCTATTTAAAGAATCTGGGTTGGGAAGTGAAAGGCACGAAACGCACCCACGACAGTGTGGAGCAAATGCGTTTGTTGCGATTAGAAACTTACCACTTGGAACTCACCCCCGATATTAATGCCGATCCCGACGATTTAAGCGCACTGTTATCCGTTGATGCGCTGATTATCAATATTCCTCCGAGCCAATATTTTTTCGATCTCAAACATTATGTGGTCGGCGTGCAGAATCTGGTGAATGAAGCCTTATTGCACGGAGTTCATCATATTATTTTTATTAGTTCCACCTCCGTTTTCCCTGAGATTTCCGCGCATTTTGACGAATCCATCCAACCGCAGCCCGAAACGGATGTGGGGCGCGCCTTAGTGGAAATTGAAAATAACTTGGCGCAACTACAGAATATTGATTGCGATGTTATTCGTTTTGCCGGTCTTGTGGGGCAAGATCGCCATCCGATTTTTTCCCTCGCCGACAAACAGGATCTCAAGTGCGGTCGTTCGCCGGTGAATTTAGTGCATTTGGATGACTGCGCCCGCGCCATTCAACTATTGCTGGAAACACCCGGTGGCTATCGCCTGTATCATTTGGCAGCGCCCGTGCATCCGCCCCGCGAAGCCTATTACCGCTTGGCAGCGGAAAAACACCATGTAAATCCACCGCACTTTATCAGCGCACCGGAAGATCCACAGCGCATTATTGTGGCGAACAAAATTTGTCGTGAACTGGATTTCGTTTATCAATACCCCGATCCAAATCTGATGTTTTCGGAAGAA","","","31739","MRSVAIVGLGWLGLPLARYLKNLGWEVKGTKRTHDSVEQMRLLRLETYHLELTPDINADPDDLSALLSVDALIINIPPSQYFFDLKHYVVGVQNLVNEALLHGVHHIIFISSTSVFPEISAHFDESIQPQPETDVGRALVEIENNLAQLQNIDCDVIRFAGLVGQDRHPIFSLADKQDLKCGRSPVNLVHLDDCARAIQLLLETPGGYRLYHLAAPVHPPREAYYRLAAEKHHVNPPHFISAPEDPQRIIVANKICRELDFVYQYPDPNLMFSEE","1243849","","conserved hypothetical protein; possible enzyme of sugar metabolism","Cytoplasm","","
InterPro
IPR006115
Domain
6-phosphogluconate dehydrogenase, NAD-binding
PF03446\"[1-39]TNAD_binding_2
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[4-238]Tno description
PTHR10366\"[8-39]T\"[56-205]TNAD DEPENDENT EPIMERASE/DEHYDRATASE
signalp\"[1-17]?signal-peptide


","No hits to the COGs database.","","Residues 4 to 167 match (4e-23) PD:PD125092 which is described as PROTEOME COMPLETE STY2279 ALR0480 DEHYDRATASE PA5343 DR0832 ","","","","","","","","","","","","Wed Jan 8 11:42:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01850 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01851","1245009","1244863","147","ATGAAAAAAACCGTCCTGAGACGGCTGAGAATTTGGTCGCGCAACTATATGCTTTTTAGCCTGTCTTTTCAAGACTGGAAAATAATGCTAACAATTACCGCAAAAAATGCAAACGTTTACGTAAAAAGTGCGGTACAATACGCGCCA","","","5865","MKKTVLRRLRIWSRNYMLFSLSFQDWKIMLTITAKNANVYVKSAVQYAP","1244863","","hypothetical protein","Cytoplasm, Extracellular","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-24]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 09:43:49 2004","Thu Feb 26 09:43:49 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01851 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:43:49 2004","","","","","","","","","","","","","1","","","" "AA01852","1245031","1246611","1581","ATGACACATCCTCAAGAACAAGTGAGCAAACGTCGCACGTTTGCGATTATTTCTCACCCCGATGCGGGTAAAACCACCATTACCGAAAAAGTGTTGCTTTACGGCAACGCCATTCAAAAAGCCGGTTCGGTGAAAGGCAAGGGTTCGGCGCAACACGCCAAATCCGACTGGATGGAAATGGAGAAACAACGCGGGATTTCCATTACCACCTCCGTCATGCAATTCCCATATAACGACTGTTTAGTCAACCTGCTGGATACCCCGGGGCATGAGGATTTCTCTGAAGATACCTACCGCACGTTAACCGCCGTGGACAGCTGTTTGATGGTGATCGACTCGGCAAAAGGGGTGGAGGAGCGCACCATTAAATTAATGGAAGTGACCCGTTTGCGTGATACACCGATTATTACCTTTATGAACAAACTCGACCGCGATATTCGTGACCCGATGGAATTGCTGGACGAAGTAGAAAACGTGCTGAAAATCCATTGCGCGCCTATTACTTGGCCTATCGGCTTTGGCAAATTGTTCAAAGGCGTGTATCACTTATATAAAGACGAAACCTATCTTTACCAAACAGGGCAGGGACATACCATTCAAGAGGTGCGTATTATTAAAGGATTGGATAATCCCGAATTGGATAACGCCGTGGGCGATGATTTGGCGCAACAATTGCGTGATGAACTGGAATTAGTGAAAGGCGCCAGTAACGAATTCGATTTAGACTTATTCCTGAGTGGCGAACTCACGCCGGTGTTTTTCGGGACGGCATTGGGGAATTTCGGCGTAGATCATTTCCTCGACGGTTTAACGGAATGGGCGCCGGCGCCGCAAGCTCGTCAGGCAGACTCGCGTAAAGTCTTCGCCGACGAAGAAAAATTCAGCGGTTTCGTGTTCAAAATTCAAGCCAATATGGATCCGAAACATCGCGACCGCGTGGCGTTCCTGCGCGTGGTGTCCGGTAAATACGAAAAAGGCATGAAACTCAAACATGTACGTATCGGCAAAGATGTGGTGATTTCCGATGCCTTAACCTTTATGGCAGGCGATCGCGCCCACGCGGAAGAAGCCTACGCCGGCGACATTATCGGCTTGCACAACCACGGCACCATTCAAATCGGCGATACTTTCACCCAGGGGGAAGATTTGAAATTCACCGGTATTCCGAATTTCGCACCGGAATTGTTCCGTCGTATTCGTTTGAAAGATCCGCTCAAGCAAAAACAATTGTTAAAAGGCTTGGTGCAACTTTCCGAAGAAGGCGCGGTGCAGGTTTTCCGCCCGTTGCTGAACAACGATTTAATCGTTGGTGCAGTGGGTGTGTTGCAGTTTGATGTGGTGGTGTCCCGTTTGAAATCCGAATACAACGTGGAAGCGATTTACGAAAATGTCAATGTGGCAACCGCCCGTTGGGTTGAATGTCGTGATGCGAAACAATTTGAAGAATTTAAACGCAAAAACGAGCAAAACCTCGCATTAGATGGTGGCGATAATCTCACTTATATCGCCCCGACCATGGTGAATCTGAATCTTGCAAAGGAGCGTTACCCCGACGTCACCTTCTTCAAAACCCGCGAACAT","","","59465","MTHPQEQVSKRRTFAIISHPDAGKTTITEKVLLYGNAIQKAGSVKGKGSAQHAKSDWMEMEKQRGISITTSVMQFPYNDCLVNLLDTPGHEDFSEDTYRTLTAVDSCLMVIDSAKGVEERTIKLMEVTRLRDTPIITFMNKLDRDIRDPMELLDEVENVLKIHCAPITWPIGFGKLFKGVYHLYKDETYLYQTGQGHTIQEVRIIKGLDNPELDNAVGDDLAQQLRDELELVKGASNEFDLDLFLSGELTPVFFGTALGNFGVDHFLDGLTEWAPAPQARQADSRKVFADEEKFSGFVFKIQANMDPKHRDRVAFLRVVSGKYEKGMKLKHVRIGKDVVISDALTFMAGDRAHAEEAYAGDIIGLHNHGTIQIGDTFTQGEDLKFTGIPNFAPELFRRIRLKDPLKQKQLLKGLVQLSEEGAVQVFRPLLNNDLIVGAVGVLQFDVVVSRLKSEYNVEAIYENVNVATARWVECRDAKQFEEFKRKNEQNLALDGGDNLTYIAPTMVNLNLAKERYPDVTFFKTREH","1246610","[FUNCTION] Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP (By similarity).[SUBCELLULAR LOCATION] Cytoplasmic.","peptide chain release factor 3","Cytoplasm","","
InterPro
IPR000795
Domain
Protein synthesis factor, GTP-binding
PR00315\"[13-26]T\"[63-71]T\"[83-93]T\"[135-144]TELONGATNFCT
PF00009\"[9-278]TGTP_EFTU
PS00301\"[56-71]TEFACTOR_GTP
InterPro
IPR004161
Domain
Translation elongation factor EFTu/EF1A, domain 2
PF03144\"[311-378]TGTP_EFTU_D2
InterPro
IPR004548
Family
Peptide chain release factor 3
TIGR00503\"[1-527]TprfC: peptide chain release factor
InterPro
IPR005225
Domain
Small GTP-binding protein domain
TIGR00231\"[9-186]Tsmall_GTP: small GTP-binding protein domain
noIPR
unintegrated
unintegrated
G3DSA:2.40.30.10\"[288-382]Tno description
G3DSA:3.40.50.300\"[10-230]Tno description
PTHR23115\"[4-162]T\"[236-410]TTRANSLATION FACTOR
PTHR23115:SF13\"[4-162]T\"[236-410]TTRANSLATION ELONGATION FACTOR G


","BeTs to 26 clades of COG0480COG name: Translation elongation and release factors (GTPases)Functional Class: JThe phylogenetic pattern of COG0480 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 8.1e-33) to 5/6 blocks of the IPB000640 family, which is described as \"Elongation factor G, C-terminus\". Interpro entry for IP:IPR000640. IPB000640A 11-36 1.8e-05 IPB000640B 55-77 5.5e-08 IPB000640C 82-109 1.7e-09 IPB000640D 116-144 0.0012 IPB000640E 266-277 21Significant hit ( 3.6e-17) to 2/3 blocks of the IPB000795 family, which is described as \"GTP-binding elongation factor\". Interpro entry for IP:IPR000795. IPB000795A 13-28 2e-05 IPB000795B 85-116 4.1e-10Significant hit ( 9.7e-11) to 3/8 blocks of the IPB000178 family, which is described as \"Initiation factor 2\". Interpro entry for IP:IPR000178. IPB000178A 10-48 25 IPB000178B 82-114 0.0016 IPB000178C 115-154 0.00041","Residues 12 to 93 match (9e-08) PD:PD249398 which is described as FACTOR ELONGATION G PROTEOME COMPLETE GTP-BINDING LIKE ","","","","","Wed Feb 19 15:05:14 2003","","","","Wed Feb 19 15:05:14 2003","","Wed Jan 8 12:09:35 2003","Wed Jan 8 12:09:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01852 is paralogously related to AA00564 (8e-39), AA03003 (5e-19), AA02344 (2e-18), AA01922 (7e-09), AA00892 (6e-08), AA00931 (2e-07) and AA00563 (2e-07).","","","","","","Residues 311 to 378 (E-value = 1.1e-10) place AA01852 in the GTP_EFTU_D2 family which is described as Elongation factor Tu domain 2 (PF03144)","","","","","Grentzmann,G., Brechemier-Baey,D., Heurgue-Hamard,V. and Buckingham,R.H. Function of polypeptide chain release factor RF-3 in Escherichia coli. RF-3 action in termination is predominantly at UGA-containing stop signals J. Biol. Chem. 270 (18), 10595-10600 (1995) PubMed: 7737996 Mortensen,K.K., Hansen,H.F., Grentzmann,G., Buckingham,R.H. and Sperling-Petersen,H.U. Osmo-expression and fast two-step purification of Escherichia coli translation termination factor RF-3 Eur. J. Biochem. 234 (3), 732-736 (1995) PubMed: 8575429 Kawazu,Y., Ito,K., Matsumura,K. and Nakamura,Y. Comparative characterization of release factor RF-3 genes of Escherichia coli, Salmonella typhimurium, and Dichelobacter nodosus J. Bacteriol. 177 (19), 5547-5553 (1995) PubMed: 7559341 Mikuni,O., Ito,K., Moffat,J., Matsumura,K., McCaughan,K., Nobukuni,T., Tate,W. and Nakamura,Y. Identification of the prfC gene, which encodes peptide-chain-release factor 3 of Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 91 (13), 5798-5802 (1994) PubMed: 8016068 Grentzmann,G., Brechemier-Baey,D., Heurgue,V., Mora,L. and Buckingham,R.H. Localization and characterization of the gene encoding release factor RF3 in Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 91 (13), 5848-5852 (1994) PubMed: 8016077","","Wed Feb 19 07:23:47 2003","1","","","" "AA01853","1246705","1246598","108","TTGCGATGGCGATCGCAAAAACTCCAAAAAAACAATCGCACTTTGATCAAGAAAACCAAAGTGCGGTCTTATTTTTTAGCGTTTTGCGGCATTAATGTTCGCGGGTTT","","","4353","LRWRSQKLQKNNRTLIKKTKVRSYFLAFCGINVRGF","1246598","","hypothetical protein","Cytoplasm, Extracellular","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 09:42:11 2004","Thu Feb 26 09:42:11 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01853 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:42:11 2004","","","","","","","","","","","","","1","","","" "AA01854","1246802","1247149","348","ATGTGGGCGGTGATTTTAACGGAACGATTTGAAACTTGGTTAAATCAACAGCCGATAAAAACGCAGGAATGTGTTTTGGCAAACTTGGTACGGTTGGAACATTTTGGTCCGAATTTAGCCCGTCCTTATGTAGATAGCGTAGCAGGGTCAATTCATAGCAACATGAAAGAACTACGCGTTCAGCATTCGGGAAGAGCAATTCGACTCTTTTTTGCTTTTGATCCAAAGCGTAGAGCCATTGTTTTATGTGGTGGAGATAAAGGCAATGACAAGCGGTTTTACCGTACGATGATTAGAATTGCAGATCAAGAATTGAATCATTATTTGGCAACCATGGAGCAAACAAAA","","","13701","MWAVILTERFETWLNQQPIKTQECVLANLVRLEHFGPNLARPYVDSVAGSIHSNMKELRVQHSGRAIRLFFAFDPKRRAIVLCGGDKGNDKRFYRTMIRIADQELNHYLATMEQTK","1247148","","conserved hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","Residues 4 to 102 match (3e-30) PD:PD030848 which is described as PROTEOME COMPLETE ALL0604 RV2022C PLASMID RV3182 YPPCP1.09C ORF119 ","","","","","","","","","","","","Wed Jan 8 12:10:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01854 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01855","1247149","1247445","297","ATGAAAACATTACAACAAGTTATTGATGAACGTTCGGTAGAAAGCCGCCAACGTATTCAAACCATGGCGGAAGATTTAATTCTTGAAACCGGTTTGCAACTGTTGCGAGAAGAATTAAATATATCGCAACAACAATTAGCTACGATTTTAGGTGTAACTCAACCTGCAATTAATCAACTGGAACAGCGTGGCAATGAAATTAAGCTTGCAACCCTCAAACGTTACATCGAAGCAATGGGCGGCAAATTACGCCTTAGTGTAGAAATGCCTGATGGACATCAGCGGGTTTTTCAAATT","","","11325","MKTLQQVIDERSVESRQRIQTMAEDLILETGLQLLREELNISQQQLATILGVTQPAINQLEQRGNEIKLATLKRYIEAMGGKLRLSVEMPDGHQRVFQI","1247444","","transcriptional regulator, Cro/CI family","Cytoplasm","","
InterPro
IPR001387
Domain
Helix-turn-helix type 3
PF01381\"[32-86]THTH_3
SM00530\"[31-86]THTH_XRE
PS50943\"[32-86]THTH_CROC1
noIPR
unintegrated
unintegrated
G3DSA:1.10.260.40\"[28-80]Tno description


","BeTs to 7 clades of COG1396COG name: Predicted transcriptional regulatorsFunctional Class: KThe phylogenetic pattern of COG1396 is --m----qvdrlb-efghsn-jx-t-Number of proteins in this genome belonging to this COG is","","Residues 22 to 89 match (3e-14) PD:PD479910 which is described as COMPLETE PROTEOME DNA-BINDING PROTEIN TRANSCRIPTIONAL REGULATOR ALL0603 RV3183 ORF101 PLASMID ","","","","","","","","","","","","Wed Jan 8 12:13:27 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01855 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 32 to 86 (E-value = 8.1e-10) place AA01855 in the HTH_3 family which is described as Helix-turn-helix (PF01381)","","","","","","","","1","","","" "AA01857","1250417","1247487","2931","ATGTCTTTTGTTGCATCATTCAGCGATAAACTTAATTCACTTGCCGAGATGTTAATCCAATCTTTTCCTGAGCAATTCGATTCGGCGTTATTTGCACAAATCCGGCAGCAGAAAGACGATCCTGCAAGCCATATCGGGCAGATTGCCGTGGCAGTGGCGATGTCGGATTTTGTGGTGGAAGTGTGGCAAAAACAACCGCACTTTTTGGCGAAATGCTGGCAAAATCCACCGCACTTTGATGACTGCGATCATTATGCCGAACGGCTGGATGCGGTGTTGCAAAAGGTGCAAACGGAAGAAGAATTTTATCGGTCATTACGTCAGTTTCGCGCCCGTGAAATGGTGAAACTGAGTTTTTGCCAAAGCCTGAATCTTGCCACGGTGGAACAGATTTTTATTCGCTTGTCGCAACTGGCGGAAAGCCTGATTATCGGGGCACGCGATTGGCTTTATGTGCGCGCTTGTGAGGAAATGGGCACGCCGATGGATGCGCAGGGCAACGCACAGCAGCTCTACATTCTCGGTATGGGCAAGCTGGGCGGCTTTGAGCTGAATTTTTCCTCCGACATTGATTTGATTTTTACGTACCCGAGCCAAGGGGAAACCGTGGGCGCACGCCGTAACATAGACAATGCAAAATTCTTCACCCGCTTGGGACAACGCCTGATTAACGCCTTGGATCAATACACCGCAGACGGCTTTGTGTATCGCACTGATATGCGTCTGCGCCCGTTTGGTGACAGCGGTGCGCTGGCGCTCAGTTTTAATGCCATGGAACAATATTATCAGGATCAGGGGCGCGATTGGGAACGTTACGCCATGATCAAAAGGCGGATTTTAGGCGCGCAGACAACGGATCCGAATGTCACCGTGTTGCAAAATTTACTGCGCCCGTTTGTGTATCGTCGCTACATTGATTTCAGTGTGATTCAAGCATTGCGCGACATGAAGCAGAAAATCGAGCGGGAAGTGCGTCGCCGCAACCTCACCGATAACATTAAACTGGGTGCCGGCGGGATTCGTGAAGTAGAATTTATCGTGCAGGTTTTTCAGCTGATCCGCGGTGGGCGTGAAGCCGCGCTGCAACAACCCGAACTGCTGAGTTTATTGCCTGAACTCACCAAGCTTCACTTAATTTCCGACGAACAGGAAACGCAGTTGCGCCATGCCTATTTATTTTTGCGACGTGCGGAAAACGTGCTGCAAGCCATCAAAGATCAGCAAACACAACAACTGCCCGATAATGAATCGGATCGCCAACGTTTAATCTTCGCCTGTGCGGAATTCACCCAATGGAATGCGCAGCGGAAAAGTGTCAATATCCGTTATCCGATTCACGATTGGAGCGGTTTTCTTGACGTGTTGCATGACCATCAACGTAAAGTGCGGTCGGTTTTCCAATCATTAATTGGTGACGAACAGGAAGAAAATACCTCAGAAAACGAATGGGAAGATTTTCTCGAAACGGATTTTGACGAACAGGAATTGCTCGGCATTTTGCAACAAAACGGCGTGCCGGAGACGGAACAGGATGTGGTGTTGGATCGCCTGTTACAATTTCGTAATGAACTGCCCCGTTATGCCATCGGCGTACGTGGGCGGGCGGTGCTCAATCGCTTAATGCCCAATGTGTTGCAACAGGTTTTGTATACGCCTCATTGTCCTATTTTGCTGCCGCGCATTCTAACCATCATCGAAAAAATCCTGACCCGCACCACCTATTTGGAATTGCTGGCGGAAAATCCGCAAGCCCTAACGCAACTTATTGAGCTTTGCGCCCAATCGAAATTTATTGCAGAACAAGTGGCGCGCCACCCGATTTTGCTGGATGAACTGCTCGATCAAAAATCCTTGCGAAATCCACCGCACTTTACCGAGTATGCCTCCGAATTGCAGCAATATTTATTGCGTTTGCCGCAAGGCGACGAAGAACAATTTATCGACGGCTTGCGGCAATTTAAGCACGCCGCCCTGCTTCGTATTGCCGCCGCGGATATTCTCGGCGTACTGCCGGTGATGAAAGTCAGCGACCATCTCACCTATTTGGCGGAAGCAATTATCGGCGCGGTGGTCAATCTGGCATGGCAACAAATTGCCGTTCGCTTCGGCGTACCCGAACATTTGGCGGAAGGACAGAAAAATTTCCTGGTGGTGGGTTACGGCAAATTAGGCGGCATTGAATTGGGCTATAAATCCGATTTGGATTTGGTGTTTTTATACGATCCCGCTACTAATAGCCAAACCGTCGGCGGTAAAAAAGTCATCGACAGCAACCAGTTTTATTTGCGCTTGGCACAAAAAATCGTCAGCATTTTCAGCATGAACACCAGCGCGGGGATTTTATACGACGTCGATATGCGATTGCGTCCGTCGGGCGATGCGGGCTTACTGGGTTGTTCCTTCGCCGCCTTTGAAAACTACCAACTGAACGAAGCCTGGACGTGGGAAAAACAGGCCTTGGTGCGTAGCCGGGCGGTCTTCGGCGAACCGAAACTACGTGAAGAATTTGATGCCATTCGTCGCAAAGTGCTAGCCGCGCCACGGGATCTGGCAAAACTCAAACAGGACGTATGTGAAATGCGCAAAAAAATGTATCAGCATTTGACGCAACAGACGGAAAATCAATTCAACATCAAAACCGACTCGGGCGGCATTACGGACATTGAATTCATCGCGCAATATCTGGTGCTGGCGCATTCACCACAACAACCGGCGCTCACCCGCTGGTCTGACAATGTGCGTATTTTCGACATCATGGTGAAATACGGCGTAATTTCCGAAACAGACGGCGAACGCCTGAAACAATGCTATGTAGATCTGCGAAACCGCACTCACCACCTGAATTTACTGGGCTTGCCTTCCGTGGTCAACGCCTCGGAATTTCACGCCGAACGAGCGTTTGTGCGGGAGATTTGGGCGCGGTTGTTTTAT","","","112460","MSFVASFSDKLNSLAEMLIQSFPEQFDSALFAQIRQQKDDPASHIGQIAVAVAMSDFVVEVWQKQPHFLAKCWQNPPHFDDCDHYAERLDAVLQKVQTEEEFYRSLRQFRAREMVKLSFCQSLNLATVEQIFIRLSQLAESLIIGARDWLYVRACEEMGTPMDAQGNAQQLYILGMGKLGGFELNFSSDIDLIFTYPSQGETVGARRNIDNAKFFTRLGQRLINALDQYTADGFVYRTDMRLRPFGDSGALALSFNAMEQYYQDQGRDWERYAMIKRRILGAQTTDPNVTVLQNLLRPFVYRRYIDFSVIQALRDMKQKIEREVRRRNLTDNIKLGAGGIREVEFIVQVFQLIRGGREAALQQPELLSLLPELTKLHLISDEQETQLRHAYLFLRRAENVLQAIKDQQTQQLPDNESDRQRLIFACAEFTQWNAQRKSVNIRYPIHDWSGFLDVLHDHQRKVRSVFQSLIGDEQEENTSENEWEDFLETDFDEQELLGILQQNGVPETEQDVVLDRLLQFRNELPRYAIGVRGRAVLNRLMPNVLQQVLYTPHCPILLPRILTIIEKILTRTTYLELLAENPQALTQLIELCAQSKFIAEQVARHPILLDELLDQKSLRNPPHFTEYASELQQYLLRLPQGDEEQFIDGLRQFKHAALLRIAAADILGVLPVMKVSDHLTYLAEAIIGAVVNLAWQQIAVRFGVPEHLAEGQKNFLVVGYGKLGGIELGYKSDLDLVFLYDPATNSQTVGGKKVIDSNQFYLRLAQKIVSIFSMNTSAGILYDVDMRLRPSGDAGLLGCSFAAFENYQLNEAWTWEKQALVRSRAVFGEPKLREEFDAIRRKVLAAPRDLAKLKQDVCEMRKKMYQHLTQQTENQFNIKTDSGGITDIEFIAQYLVLAHSPQQPALTRWSDNVRIFDIMVKYGVISETDGERLKQCYVDLRNRTHHLNLLGLPSVVNASEFHAERAFVREIWARLFY","1247486","[FUNCTION] Adenylylation and deadenylylation of glutamine synthetase (by similarity). [CATLYTIC ACTIVITY] ATP + [L-glutamate:ammonia ligase (ADP-forming)] = diphosphate + adenylyl-[L-glutamate:ammonia ligase (ADP-forming)]. ","glutamate-ammonia-ligase adenylyltransferase","Cytoplasm","","
InterPro
IPR005190
Domain
Glutamate-ammonia ligase adenylyltransferase
PF03710\"[45-294]T\"[585-839]TGlnE


","No hits to the COGs database.","","Residues 414 to 464 match (2e-07) PD:PD374076 which is described as PROTEOME COMPLETE GLNE ","","","","","","","","","","","Wed Jan 8 12:18:36 2003","Wed Jan 8 12:18:36 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01857 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 642 to 863 (E-value = 3.5e-129) place AA01857 in the GlnE family which is described as Glutamate-ammonia ligase adenylyltransferase (PF03710)","","","","","van Heeswijk,W.C., Rabenberg,M., Westerhoff,H.V. and Kahn,D. The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli Mol. Microbiol. 9 (3), 443-457 (1993) PubMed: 8412694 ","","Wed Jan 8 12:18:36 2003","1","","","" "AA01858","1250839","1251597","759","ATGTCTGAAGTCATCGCCCATGCCCGCCAAGATTCAAAATGGCATTTTCACCCTCTGCAAAACCACTTGAAAAAAGTAGCAAAACTCGCCAGACGCTTTGCCGGACGTTACGGGGCTTTGTTTGCCGAATATGCAGGGCTTTTGCATGATTTGGGAAAATTTCAAGAGGCTTTTCAGGAATATATCCGTAGGGTTACAGGATTTGAACGGGAAAACGCGCATCTTGAGGATATTGAATCTTCCAAACCCCATAAAATTCCCCATTCGACCGCAGGCGCAAAATATGCAACGCAAAATCTTGATCCTTTCTTAGGGCATTTATTGGCATATTTAATAGCAGGGCATCATGCCGGTTTGGCGGATTGGTATGACAAAGGTAGTTTGAAATACCGTTTGGCACAGGCGGACGATGAATTGGCAGAGTCTTTAGCCGGTTTGGAAAAAAGTGGGCTAGTTGAAGACTTTTTATCCTTATCTGGTGATGCGCTTGAAGAAGACCTTTTAAACGTTTGGGAAAGCGGGATAAATCTTGAAGAACTGCATATTTGGATGCGTTTTCTCTTTTCTTGTTTGGTGGATGCTGATTTTTTAGATACCGAAGCCTTTATGAACGGTTTTGTCGATGCGGATGCGGCGCAACAGGCAGGTTTTCGCCCGAATTTCCCCGATTTAGAAGATATGCACAGCCGTTACGAGAAGCATATGCTTGATCTTGCAGAAAAATCGGATACCCGCAGCCATCTTCGGGTGGATCTGTTT","","","29047","MSEVIAHARQDSKWHFHPLQNHLKKVAKLARRFAGRYGALFAEYAGLLHDLGKFQEAFQEYIRRVTGFERENAHLEDIESSKPHKIPHSTAGAKYATQNLDPFLGHLLAYLIAGHHAGLADWYDKGSLKYRLAQADDELAESLAGLEKSGLVEDFLSLSGDALEEDLLNVWESGINLEELHIWMRFLFSCLVDADFLDTEAFMNGFVDADAAQQAGFRPNFPDLEDMHSRYEKHMLDLAEKSDTRSHLRVDLF","1251596","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003607
Domain
Metal-dependent phosphohydrolase, HD region
SM00471\"[15-209]THDc
InterPro
IPR006674
Domain
Metal-dependent phosphohydrolase, HD region, subdomain
PF01966\"[19-77]THD


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Jan 8 12:20:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01858 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01859","1251858","1251950","93","TTGCTGATTATCTTTTTTTCGTTAAAAAAAGGAAAAATTATGCAATATGGTTTTTGTTGTCCGTTATTTGTAAATAACGGAGGGCGTGATGAG","","","3534","LLIIFFSLKKGKIMQYGFCCPLFVNNGGRDE","1251950","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-15]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 09:40:25 2004","Thu Feb 26 09:40:25 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01859 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:40:25 2004","","","","","","","","","","","","","1","","","" "AA01861","1251946","1252167","222","ATGAGTAAGGTTGCGCAAGCGTTGACCATCTTCGGTTCGGACAGCGGCGGCGGTGCCTGGGTTCAGGCGGATTTGAAGATGTTCCAAATGCACAGGATGTCGTTTGGTTCATCGGTGGCCGCGCAAAATACCTTGAACGTGGTTGATATTTACGCCGTGTCACTCAAAACCATCCAATGTCAGCTGAAAGCCATTGTGACAGATTTTGATATTTCGCACCTT","","","8075","MSKVAQALTIFGSDSGGGAWVQADLKMFQMHRMSFGSSVAAQNTLNVVDIYAVSLKTIQCQLKAIVTDFDISHL","1252166","[FUNCTION] Catalyzes the phosphorylation of hmp-p to hmp-pp (by similarity). [CATALYTIC ACTIVITY] ATP + 4-amino-2-methyl-5-phosphomethylpyrimidine = ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine. [PATHWAY] Thiamine biosynthesis.[SIMILARITY] Belongs to the ThiD family.","phosphomethylpyrimidine kinase","Cytoplasm","","
InterPro
IPR013749
Domain
Phosphomethylpyrimidine kinase type-1
PF08543\"[14-71]TPhos_pyr_kin
noIPR
unintegrated
unintegrated
G3DSA:3.40.1190.20\"[4-74]Tno description
PTHR20858\"[2-71]TPHOSPHOMETHYLPYRIMIDINE KINASE
PTHR20858:SF2\"[2-71]TPHOSPHOMETHYLPYRIMIDINE KINASE


","BeTs to 21 clades of COG0351COG name: Hydroxymethylpyrimidine/phosphomethylpyrimidine kinaseFunctional Class: HThe phylogenetic pattern of COG0351 is aompkzyqvdrlb-efghsnuj--t-Number of proteins in this genome belonging to this COG is","","Residues 14 to 72 match (3e-11) PD:PD003501 which is described as KINASE PROTEOME COMPLETE PHOSPHOMETHYLPYRIMIDINE TRANSFERASE HYDROXYETHYLTHIAZOLE THIAMINE BIOSYNTHESIS PYRIDOXAL HMP-P ","","","","","","","","","","","Wed Jan 8 12:26:10 2003","Wed Jan 8 12:28:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01861 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","",""," Mizote,T., Tsuda,M., Smith,D.D., Nakayama,H. and Nakazawa,T.Cloning and characterization of the thiD/J gene of Escherichia coli encoding a thiamin-synthesizing bifunctional enzyme,hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase. Microbiology 145 (Pt 2): 495-501 (1999) [PubMed: 10075431].","","Wed Jan 8 12:26:10 2003","1","","","" "AA01863","1252151","1252315","165","TTGATATTTCGCACCTTTAAAATCGGTATGCCGGTCGGGCTGGTGGAGACTTCGGTGATGATTGCCAAAAGCGTTAGCGTTAAACAAGCGATCAAAACTGCGAAAAGATTACATCACGGTAGCCATCAGCTATCCGTTAAATACTGGGCACGGACACGGACCGAC","","","6206","LIFRTFKIGMPVGLVETSVMIAKSVSVKQAIKTAKRLHHGSHQLSVKYWARTRTD","1252315","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-17]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 09:37:04 2004","Thu Feb 26 09:37:04 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01863 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:37:04 2004","","","","","","","","","","","","","1","","","" "AA01865","1252368","1253369","1002","ATGAAAAAAACACTTTTATTTTTGACCGCACTTTCTTTAACGGCAGGCACGGTGTTTGCCGATAATCAGAAGGAAAACGTGAACATTTACACTTACGATTCCTTCACTTCCGATTGGGGCGCCGGTCCGAAACTTAAGCAGGCGTTTGAACAAAATTTTCCCCGTTGCGTGGTGAATTATATGCCTTTTGAAAGTGGCGGCACGTTGTTTAATCGCGTACGTTTGGAAGGGCATAAAACCAAAGCGGATATTGTGTTGGGGCTGGATAATTTCGTGTTGGATGAAGCGAAAAAAAGCAAATTGTTTGATGTGAATAAGGTGGATTTGAGCAAACTTTCGCTGCCGAGCCAGTGGGCGGACAACAGCTTCTTGCCTTACGACTTCGGCACTTATGCTTTTGTGTATGATAAAAATAAACTGAAAAATCCGCCGAAAAGCTTGAAAGAATTGGTGGAACGTGAAGATTTACGCGTGATTTATCAAGACCCGCGCACCAGTAGCGTCGGACGCGGTTTATTGGTGTGGATGAATGCCGTTTACCCGGCGGAACAAGTGGCGCAGGCGTGGCAGCAACTTGCGAAACACACGGTGACGGTAGGGAAAGGCTGGTCGGACACTTACGGCGCATTCCTGAAAGGCGAGGCGGATTTAGTGTTAAGTTACAGCACTTCGCCCTTGTATCATCAATTATCTGAAAATAAAGATAATTACGCCGCCACCGAATTTGCCGAAGGCAATTTAACGCAGGTGGAACTGGCGGCACGCATTGCCGATCACAAAAATCAATGCGCCGATCAATTTATGGATTTTCTCATTACGCCGGAAGCGCAGAAGCATATTGTGACGGCTAACGTGATGTTGCCGGTGATTCACGCGCCTGTTGAACCGCACTTTAATGCGTTAAAAGAAAAATTGTTACGGCAATCTTTCCTGAATACCTCCAATGTCACTCCGGAAGCATTACGCAGCTGGATCAGCCAATGGCAAACCACCTTAACGCAA","","","37744","MKKTLLFLTALSLTAGTVFADNQKENVNIYTYDSFTSDWGAGPKLKQAFEQNFPRCVVNYMPFESGGTLFNRVRLEGHKTKADIVLGLDNFVLDEAKKSKLFDVNKVDLSKLSLPSQWADNSFLPYDFGTYAFVYDKNKLKNPPKSLKELVEREDLRVIYQDPRTSSVGRGLLVWMNAVYPAEQVAQAWQQLAKHTVTVGKGWSDTYGAFLKGEADLVLSYSTSPLYHQLSENKDNYAATEFAEGNLTQVELAARIADHKNQCADQFMDFLITPEAQKHIVTANVMLPVIHAPVEPHFNALKEKLLRQSFLNTSNVTPEALRSWISQWQTTLTQ","1253368","[FUNCTION] Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and tpp (by similarity).[SUBCELLULAR LOCATION] Periplasmic. [SIMILARITY] Belongs to the bacterial extracellular solute-binding protein family 1. ","thiamin ABC transporter, periplasmic-binding protein","Periplasm","","
InterPro
IPR005948
Family
Thiamine ABC transporter periplasmic binding protein
TIGR01254\"[24-328]TsfuA: ABC transporter periplasmic binding p
InterPro
IPR005967
Family
Proteobacterial thiamine ABC transporter, periplasmic binding protein
TIGR01276\"[7-334]TthiB: thiamin/thiamin pyrophosphate ABC tra
InterPro
IPR011587
Domain
Prokaryotic extracellular metal-binding protein
PD008688\"[218-278]TQ9V0J0_PYRAB_Q9V0J0;
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[26-299]Tno description
signalp\"[1-20]?signal-peptide


","BeTs to 10 clades of COG1840COG name: ABC-type iron/thiamine transport systems, periplasmic componentFunctional Class: HThe phylogenetic pattern of COG1840 is -o--kz---d-lbcefghsnuj--t-Number of proteins in this genome belonging to this COG is","","Residues 29 to 136 match (1e-07) PD:PD548145 which is described as ABC PROTEOME PROTEIN COMPLETE PERIPLASMIC THIAMINE TRANSPORTER THIAMINE-BINDING ","","","","","","","","","","","Wed Jan 8 12:34:33 2003","Wed Jan 8 12:34:33 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01865 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Webb,E., Claas,K. and Downs,D. thiBPQ encodes an ABC transporter required for transport of thiamine and thiamine pyrophosphate in Salmonella typhimurium J. Biol. Chem. 273 (15), 8946-8950 (1998) PubMed: 9535878 Angerer,A., Gaisser,S. and Braun,V. Nucleotide sequences of the sfuA, sfuB, and sfuC genes of Serratia marcescens suggest a periplasmic-binding-protein-dependent iron transport mechanism J. Bacteriol. 172, 572-578 (1990) PubMed: 2404942 ","","Wed Jan 8 12:34:33 2003","1","","","" "AA01866","1253453","1255006","1554","GTGATGTTGTTGATTTCCTTGCTTTATGGTTTCGCCCTGCGCGCGGTGTTGGCGCAGGGTAGTGAGTTTCAGTGGCAAAGCATCTTTTCCGATGTCTATTTACATCACGTTATCGTCTTTAGTTTCGGGCAAGCATTACTTTCTGCACTGTTATCGCTGTTTTTCGGCATGCTGTTAGCCCGTGCCTTTTATTATGTGGATTTTCCCGGCAAATCATTTTTGCTCAGAATTATGTCGCTGACCTTTGTGCTGCCGGTGTTGGTGGCGATTTTCGGCTTGATCGGTATTTACGGCGCTTCCGGCTGGATTGCGCAAAGTCTCGGCTTGTTCGGCGAAACCTGGCAGGGCAGCATTTACGGCTTATCAGGTATTCTAACCGCCCATCTTTTCTTTAATATTCCGCTTGCTGCTAAGTTATTTTTGCAAAGTCTGAAAGCTATTCCTTACGAACAACGCCAACTGGCTGCGCAGCTGAATATTCGCGGCTGGCGTTTTGTGCGCTTGGTGGAATGGTATTATTTGCGCCGCCAAATTCTGCCGACCTTTAGCCTGATTTTCATGCTTTGTTTCACCAGTTTCACCGTGGTGCTGACCCTCGGCGGCGGGCCGCAATATACCACGCTGGAAACGGCGATTTATCAGGCGATCCTGTTTGAATTCGATTTGCCGAAAGCGGCGCTGTTTGCTTTATTGCAATTCGTATTTTGCCTGCTGTTATTCAGTCTTGGCAGTCTGTTTAGTTCCACCGCACAAACTGCGTTAAGCAGCCCTTATCGCTGGCTTGATAGCCCCAAAAGTGCGGTCAAAATTTTCCACGTTTTTTTGCTGGTGATGTTTCTGTTGTTTATGTTATCGCCGTTGCTAAATATTATGGTGAGCGCGCTGGCGTCGGAAAAATTATTCACGGCGTGGCACAACCCGCAACTGTGGAAAGCCTTGGGCTATTCGTTAACCATTGCGCCGACATCTGCGCTGCTGGCGTTGCTGATGGCGGTGGCGTTATTGCTGTTATCCCGTCGTTTGCAATGGCTGTATTATGTGAAAACCGCGCAATTTATCATCAATGCGGGCATGGTGATTTTGGCAATTCCCATTTTGGTATTGGCGATGGGCTTGTTTTTATTGCTGCGAGAAATTGATTTTAACAACGCTTATTTATTCGCCATTGTGGTCGTCTGTAATGCCTTAAGCGCCATGCCGTTCGTGTTACGTATTCTCACCGAACCCTTTAATAACAATATGTTGTATTACGAACGCCTGTGCAATTCCCTTGGTATTCTCGGCTGGCGGCGTTTTCGGCTGATTGAATGGCATGATCTTCGTGCGCCGCTAAAATATGCTTTCGCCCTAGCATTTGCGCTATCTTTGGGGGATTTCACCGCCATTGCGCTGTTCGGCAATCAGGATTTCACCTCGTTGCCCCATTTGTTATATCAACAATTAGGTAGCTATCGCCACCAAGACGCCGCAGTGACGGCAGGCATTTTACTGTTATTATGCGGGGGGATTTTCGCCTTAATTGAAAATCAAAAGGAACAATATGATTCGCTTAGA","","","61136","VMLLISLLYGFALRAVLAQGSEFQWQSIFSDVYLHHVIVFSFGQALLSALLSLFFGMLLARAFYYVDFPGKSFLLRIMSLTFVLPVLVAIFGLIGIYGASGWIAQSLGLFGETWQGSIYGLSGILTAHLFFNIPLAAKLFLQSLKAIPYEQRQLAAQLNIRGWRFVRLVEWYYLRRQILPTFSLIFMLCFTSFTVVLTLGGGPQYTTLETAIYQAILFEFDLPKAALFALLQFVFCLLLFSLGSLFSSTAQTALSSPYRWLDSPKSAVKIFHVFLLVMFLLFMLSPLLNIMVSALASEKLFTAWHNPQLWKALGYSLTIAPTSALLALLMAVALLLLSRRLQWLYYVKTAQFIINAGMVILAIPILVLAMGLFLLLREIDFNNAYLFAIVVVCNALSAMPFVLRILTEPFNNNMLYYERLCNSLGILGWRRFRLIEWHDLRAPLKYAFALAFALSLGDFTAIALFGNQDFTSLPHLLYQQLGSYRHQDAAVTAGILLLLCGGIFALIENQKEQYDSLR","1255005","[FUNCTION] Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and tpp (by similarity).[SUBCELLULAR LOCATION] Periplasmic. [SIMILARITY] Belongs to the bacterial extracellular solute-binding protein family 1.","thiamin ABC transporter, permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR000515
Family
Binding-protein-dependent transport systems inner membrane component
PF00528\"[34-260]TBPD_transp_1
PS50928\"[38-243]T\"[313-508]TABC_TM1
InterPro
IPR005947
Family
Thiamine ABC transporter, permease protein
TIGR01253\"[1-507]TthiP: thiamine/thiamine pyrophosphate ABC t
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide
tmhmm\"[37-59]?\"[80-100]?\"[116-136]?\"[178-198]?\"[229-249]?\"[270-290]?\"[317-337]?\"[352-374]?\"[384-406]?\"[446-466]?\"[489-507]?transmembrane_regions


","No hits to the COGs database.","","Residues 428 to 493 match (2e-13) PD:PD587848 which is described as PERMEASE PROTEOME COMPLETE SYSTEM THIAMINE TRANSMEMBRANE MEMBRANE INNER THIP ","","","","","","","","","","","Wed Jan 8 12:46:18 2003","Wed Jan 8 12:46:18 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01866 is paralogously related to AA01050 (6e-17), AA01950 (1e-11), AA01644 (3e-10), AA00699 (4e-08), AA01780 (3e-06), AA01650 (1e-05) and AA01948 (4e-05).","","","","","","","","","","","Webb,E., Claas,K. and Downs,D. thiBPQ encodes an ABC transporter required for transport of thiamine and thiamine pyrophosphate in Salmonella typhimurium J. Biol. Chem. 273 (15), 8946-8950 (1998) PubMed: 9535878 ","","Wed Jan 8 12:46:18 2003","1","","","" "AA01867","1254993","1255637","645","ATGATTCGCTTAGATAACGTATTTTTAGCCGACGACGCTTTGCCTATGGAATTTGACTTACAGGTAGCGGCGGGGGAACTTGTTGCCATGGTCGGTCCTAGCGGCGCAGGCAAAAGCACATTACTCAATTTCATCGCGGGCTTTGTGTTGCCAACGCGTGGCGAGATTTGGCTGAACGGCGAAAACCATACCCGCAGCGCCCCTTATGAACGACCGGTGTCCATGTTGTTTCAGGAGAATAACCTGTTTCCTCATTTAACGGTGCAACAAAATCTGGCGTTGGGCTTAAAAACGTCCTTAAAACTGACCGCACTTGAGCAACAACAATTGGCGCAGGTCGCCGATGCCGTGGGATTAGGCGCGTTTTTGTCCCGCCTGCCGAACAGCCTTTCCGGCGGGCAAAAACAACGGGTGGCGCTGGCGCGCTGTTTGTTGCGCGATAAGCCGATTTTGTTACTGGACGAACCTTTCTCCGCCCTCGACCCCGAATTGCGCATGGAAATGTTAAACCTGATCGATGAACTCTGCCGTAGCAAACACTTAACCTTGTTGCTTGTTACCCATCAACCTTCGGAGCTGGCAGGAAAAGTGGATCGCATTCTGCAGGTGGAAAATGGTCGGATAACTCACTCAGAAAAATGCGCC","","","24496","MIRLDNVFLADDALPMEFDLQVAAGELVAMVGPSGAGKSTLLNFIAGFVLPTRGEIWLNGENHTRSAPYERPVSMLFQENNLFPHLTVQQNLALGLKTSLKLTALEQQQLAQVADAVGLGAFLSRLPNSLSGGQKQRVALARCLLRDKPILLLDEPFSALDPELRMEMLNLIDELCRSKHLTLLLVTHQPSELAGKVDRILQVENGRITHSEKCA","1255636","[FUNCTION] Part of the binding-protein-dependent transport systemtbpA-thiPQ for thiamine and tpp (by similarity). [SUBCELLULAR LOCATION] Periplasmic. [SIMILARITY] Belongs to the bacterial extracellular solute-bindingprotein family 1.","thiamine transport ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[130-172]TQ9CNP9_PASMU_Q9CNP9;
PF00005\"[25-206]TABC_tran
PS50893\"[2-215]TABC_TRANSPORTER_2
PS00211\"[130-144]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[24-207]TAAA
InterPro
IPR005968
Family
Thiamine ABC transporter, ATP-binding protein
TIGR01277\"[2-214]TthiQ: thiamine ABC transporter, ATP-binding
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[17-208]Tno description
PTHR19222\"[17-208]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF58\"[17-208]TTHIAMINE ABC TRANSPORTER


","BeTs to 3 clades of COG3840COG name: ABC-type thiamine transport systems, ATPase componentsFunctional Class: HThe phylogenetic pattern of COG3840 is --------------e-gh---j----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-35) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 14-60 2.2e-14 IPB001140B 127-165 1.5e-18 IPB001140C 183-212 8.1","Residues 119 to 215 match (8e-07) PD:PD438915 which is described as ATP-BINDING ABC COMPLETE PROTEOME SUGAR TRANSPORTER ","","","","","","","","","","","Wed Jan 8 12:49:28 2003","Wed Jan 8 12:49:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01867 is paralogously related to AA00700 (9e-35), AA01656 (4e-34), AA01779 (5e-32), AA01051 (5e-32), AA01645 (7e-32), AA02718 (6e-31), AA01684 (2e-29), AA00858 (4e-29), AA01616 (4e-27), AA01524 (7e-27), AA01393 (3e-26), AA00415 (3e-26), AA02440 (4e-26), AA01422 (3e-25), AA02080 (4e-24), AA02324 (9e-24), AA01961 (2e-22), AA02320 (5e-22), AA02353 (1e-21), AA02805 (2e-21), AA01947 (2e-21), AA02899 (2e-20), AA01510 (4e-20), AA02609 (1e-19), AA01824 (7e-19), AA02140 (1e-18), AA01568 (4e-18), AA00933 (6e-18), AA00799 (7e-18), AA01509 (1e-17), AA02606 (3e-17), AA02331 (3e-16), AA02550 (7e-16), AA02898 (1e-15), AA01820 (2e-15), AA02573 (2e-15), AA02786 (3e-15), AA00207 (4e-15), AA02152 (2e-14), AA00061 (2e-14), AA00751 (4e-14), AA01757 (9e-13), AA01456 (2e-11), AA02484 (4e-10), AA00591 (6e-10), AA02225 (1e-09), AA01555 (8e-09), AA02642 (1e-08), A02145 (1e-07), AA02146 (4e-07), AA01569 (3e-06), AA00934 (5e-06) and AA02226 (1e-04).","","","","","","Residues 25 to 206 (E-value = 3.8e-65) place AA01867 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Webb,E., Claas,K. and Downs,D. thiBPQ encodes an ABC transporter required for transport of thiamine and thiamine pyrophosphate in Salmonella typhimurium J. Biol. Chem. 273 (15), 8946-8950 (1998) PubMed: 9535878 ","","Wed Jan 8 12:49:28 2003","1","","","" "AA01868","1255685","1256686","1002","ATGTTAACCAGTACCCTGCAAATTTACTCCATCACCCCGCACCCGAGCGTGGAATATTGGTCGGTGTGCAAAGTAGAAGCGTTGTTTGAAACCCCGTTTTTAGATTTGGTTTACCGCGCGGCGCAAGTGCATCGTCAGAATTTCAATCCACGCGCCATTCAGCTTTCAACCTTAATGTCCATTAAAACCGGCGGCTGTCCTGAGGATTGCGGTTATTGCCCGCAATCGGCGCGTTATCAAACGGGCGTGCAAAATCAGCAATTATTGGACGTGGAAGAAATCGTCGCCAAAGCGAAAATTGCCAAAGCCCGTGGGGCGGGGCGTTTTTGTATGGGCGCGGCGTGGCGCGGACCGAAACCGAAAGACATCGCCAAAGTGACGGAAATTATCAAGGCGGTGAAAGCCCTCGGCATGGAAACCTGTGGCACCTTCGGCTTATTGCAAGACGGCATGGCGGAAGAATTAAAAGACGCAGGCTTGGATTATTACAACCACAATTTAGATACCGCGCCGGAGCATTACAGCGAAGTTATCGGCACACGCCGTTTCGATGATCGTATCAGCACCTTGGGCAAAGTACGCAAAGCGGGCTTGAAAGTATGCTGTGGCGGCATTGTCGGCATGAACGAAACCCGCAAAGAACGGGCGGGGCTTATCGCCAGCCTTGCCAATTTGGATCCGCAACCGGAATCCGTTCCGATTAACCAATTAGTGAAAATTGAAGGCACGCCGCTTGCCGATGCAGAAGAACTGGATTGGACGGAATTTGTCCGCACCATCGCCGTGGCGCGTATCACCATGCCGAACAGCTATGTGCGCTTATCCGCCGGTCGCCAGGGCATGAGCGAAGAAATGCAGGCAATGTGCTTCATGGCAGGCGCTAATTCCATTTTCTACGGCGACAAACTCCTCGTCACCGGCAACCCGGAAGAAGACGGCGACCGTCTGCTGATGGAAAAACTCGATTTAGAACCGGAGACGGAAGAGAATAAGTATTTGCGT","","","39076","MLTSTLQIYSITPHPSVEYWSVCKVEALFETPFLDLVYRAAQVHRQNFNPRAIQLSTLMSIKTGGCPEDCGYCPQSARYQTGVQNQQLLDVEEIVAKAKIAKARGAGRFCMGAAWRGPKPKDIAKVTEIIKAVKALGMETCGTFGLLQDGMAEELKDAGLDYYNHNLDTAPEHYSEVIGTRRFDDRISTLGKVRKAGLKVCCGGIVGMNETRKERAGLIASLANLDPQPESVPINQLVKIEGTPLADAEELDWTEFVRTIAVARITMPNSYVRLSAGRQGMSEEMQAMCFMAGANSIFYGDKLLVTGNPEEDGDRLLMEKLDLEPETEENKYLR","1256685","[CATALYTIC ACTIVITY] Dethiobiotin + sulfur = biotin.[PATHWAY] Biotin biosynthesis; last step.","biotin synthetase","Cytoplasm","","
InterPro
IPR002684
Family
Biotin synthase
PIRSF001619\"[5-333]TBiotin synthetase
TIGR00433\"[28-323]TbioB: biotin synthase
InterPro
IPR006638
Domain
Elongator protein 3/MiaB/NifB
SM00729\"[56-264]TElp3
InterPro
IPR007197
Domain
Radical SAM
PF04055\"[60-222]TRadical_SAM
InterPro
IPR010722
Domain
Biotin and thiamin synthesis associated
PF06968\"[233-325]TBATS
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[17-328]Tno description
noIPR
unintegrated
unintegrated
PTHR22976\"[30-329]TBIOTIN SYNTHASE
PTHR22976:SF1\"[30-329]TBIOTIN SYNTHASE


","BeTs to 17 clades of COG0502COG name: Biotin synthase and related enzymesFunctional Class: HThe phylogenetic pattern of COG0502 is --m---yqv-r-bcefghsnuj-i--Number of proteins in this genome belonging to this COG is","Significant hit (3.3e-106) to 7/7 blocks of the IPB002684 family, which is described as \"Biotin synthase\". Interpro entry for IP:IPR002684. IPB002684A 66-77 1e-09 IPB002684B 98-117 4.4e-14 IPB002684C 136-182 1.6e-30 IPB002684D 185-221 6e-24 IPB002684E 229-245 1.5e-10 IPB002684F 267-278 1.8e-06 IPB002684G 304-314 0.012","Residues 53 to 114 match (6e-13) PD:PD495711 which is described as BIOTIN SYNTHASE PROTEOME COMPLETE TRANSFERASE SYNTHETASE IRON-SULFUR BIOSYNTHESIS PROBABLE BIOB ","","","","","","","","","","","Wed Jan 8 12:52:10 2003","Wed Jan 8 12:52:10 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01868 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 233 to 325 (E-value = 3e-47) place AA01868 in the BATS family which is described as Biotin and Thiamin Synthesis associated domain (PF06968)","","","","","Otsuka,A.J., Buoncristiani,M.R., Howard,P.K., Flamm,J., Johnson,C.,Yamamoto,R., Uchida,K., Cook,C., Ruppert,J. and Matsuzaki,J. The Escherichia coli biotin biosynthetic enzyme sequences predicted from the nucleotide sequence of the bio operon J. Biol. Chem. 263 (36), 19577-19585 (1988) PubMed: 3058702 Ugulava NB, Surerus KK, Jarrett JT. Evidence from Mossbauer spectroscopy for distinct [2Fe-2S](2+) and [4Fe-4S](2+) cluster binding sites in biotin synthase from Escherichia coli. J Am Chem Soc. 2002 Aug 7;124(31):9050-1. PMID: 12148999 Ollagnier-De-Choudens S, Mulliez E, Hewitson KS, Fontecave M. Biotin synthase is a pyridoxal phosphate-dependent cysteine desulfurase. Biochemistry. 2002 Jul 23;41(29):9145-52. PMID: 12119030 Farh L, Hwang SY, Steinrauf L, Chiang HJ, Shiuan D. Structure-function studies of Escherichia coli biotin synthase via a chemical modification and site-directed mutagenesis approach. J Biochem (Tokyo). 2001 Nov;130(5):627-35. PMID: 11686925 ","","Wed Jan 8 12:52:10 2003","1","","","" "AA01869","1258169","1256790","1380","ATGAAAAAACACAATTTTGTATTAACAAGTATCGCGCTCGGATTGAGCCTGTTAAGCACACCTATGTTAAGCCAAGCAGAAATTCCCGCTATTGTTGAAGAACAACAAATGCCAAGTCTGGCACCAATGTTGGAAAAAGTGTTACCTTCCGTTGTTTCCATTTCAGTAGAAGGCAAACAAAAAACTCGCTCCGCACAACAATTTGACGACATTCCCGAGGAATTCAGATTTTTCTTTGGCCCTGATATGTTTGACCGCGATCGTGCGCCGCGTAACTTTAGGGGAATCGGTTCCGGTGCAATCATCAATGCAGAAAAAGGTTACGTTTTAACAAACAACCATGTGATTAAAGATGCAGATAAAATCACCGTTCAGTTACAAGATGGTCGCGAATTTAAAGCCAAAGTCATCGGCGCAGACGAACTGTCCGATGTGGCATTAATTCAAATAGAAAAACCGAAAAATCTGACCGCACTTAAAATCGCCGATTCCGACAAATTACGCGTGGGCGATTTCACCGTGGCAATTGGTAATCCATTTGGTTTAGGTCAAACCGTGACCTCCGGGATTGTTTCGGCGTTAGGGCGCTCCACAGGATCCGACAGTGGAATGTACGAAAACTATATCCAAACTGATGCGGCAGTCAATCGTGGTAACTCAGGTGGTCCATTAATCAATTTGAACGGCGAATTAATCGGCATTAATACCGCCATCATCTCCCCGAGCGGCGGTAATGCGGGTATCGCCTTCGCGATTCCGAGCAACATGGCGAATAACCTGGTTCAACAAATTCTTGAATTCGGTGAGGTGCGTCGCGGCATGTTAGGCATTAAAGGCGGCGAATTAAACGCTGATTTAGCACAGGCTTTCGACATTGAAGCAAAAAAAGGCGCTTTCGTAAGTGAAGTCATTCCGGGTTCTGCCGCAGATAAAGCCGGCTTGAAAGCAGGCGATGTGATTACAGCCATAAACGGACAATCTATTTCCAGTTTCGCCGAAATGCGCGCTAAAATCGCCACGTCCGGTGCAGGCAAAGAAATTGAGTTAACGTATTTACGTGATAGCAAGTCCAACACCACAAAAGTAGTCTTACAATCCGATGACAAAATCCAAACCAGTGCCGGCAATTTGCTCCCTGCACTAGACGGCGCGGAATTAAATAATTACGACGAAAAAGGCCTTAAAGGCGTATCTGTGGGCAAAATAAAAACCGGTTCTTTGGCAGAACAACGTGGTTTAAAAACCGGTGATGTGATTATCGGAATCAATCGCCAGAAAATAGAAAATCTCGGACAACTGCGCAAAGAGTTAGATAAAAAACCGTCTGCCGTTGCCTTGAACATTATTCGTGGCGATAGTAACTTCTATTTACTGGTGCAA","","","48920","MKKHNFVLTSIALGLSLLSTPMLSQAEIPAIVEEQQMPSLAPMLEKVLPSVVSISVEGKQKTRSAQQFDDIPEEFRFFFGPDMFDRDRAPRNFRGIGSGAIINAEKGYVLTNNHVIKDADKITVQLQDGREFKAKVIGADELSDVALIQIEKPKNLTALKIADSDKLRVGDFTVAIGNPFGLGQTVTSGIVSALGRSTGSDSGMYENYIQTDAAVNRGNSGGPLINLNGELIGINTAIISPSGGNAGIAFAIPSNMANNLVQQILEFGEVRRGMLGIKGGELNADLAQAFDIEAKKGAFVSEVIPGSAADKAGLKAGDVITAINGQSISSFAEMRAKIATSGAGKEIELTYLRDSKSNTTKVVLQSDDKIQTSAGNLLPALDGAELNNYDEKGLKGVSVGKIKTGSLAEQRGLKTGDVIIGINRQKIENLGQLRKELDKKPSAVALNIIRGDSNFYLLVQ","1256789","[FUNCTION] Protease with a shared specificity with degP. [SUBCELLULAR LOCATION] Periplasmic (Potential).[SIMILARITY] Seems to be a intermediate form between E.coli htrA (protease do) and hhoA.[SIMILARITY] Belongs to peptidase family s2c. [SIMILARITY] Contains 2 pdz/dhr domains. ","periplasmic serine protease do; hhoA-like precursor; heat shock protein","Periplasm, Cytoplasm","","
InterPro
IPR001254
Domain
Peptidase S1 and S6, chymotrypsin/Hap
PF00089\"[99-261]TTrypsin
InterPro
IPR001478
Domain
PDZ/DHR/GLGF
PF00595\"[263-352]T\"[388-449]TPDZ
SM00228\"[273-355]T\"[380-452]TPDZ
PS50106\"[264-355]T\"[383-452]TPDZ
InterPro
IPR001940
Family
Peptidase S1C, HrtA/DegP2/Q/S
PR00834\"[107-119]T\"[128-148]T\"[169-193]T\"[205-222]T\"[227-244]T\"[313-325]TPROTEASES2C
InterPro
IPR011782
Family
Peptidase S1C, Do
TIGR02037\"[38-459]TdegP_htrA_DO: protease Do
noIPR
unintegrated
unintegrated
G3DSA:2.30.42.10\"[291-363]T\"[390-460]Tno description
G3DSA:2.40.10.10\"[35-160]T\"[160-277]Tno description
PTHR22939\"[43-68]T\"[94-454]TSERINE PROTEASE FAMILY S1C HTRA-RELATED
PTHR22939:SF10\"[43-68]T\"[94-454]TSERINE PROTEASE DO/HTRA-RELATED
signalp\"[1-26]?signal-peptide
tmhmm\"[5-23]?transmembrane_regions


","BeTs to 20 clades of COG0265COG name: Trypsin-like serine proteases, typically periplasmic, contain C-terminal PDZ domainFunctional Class: OThe phylogenetic pattern of COG0265 is -om---yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 2.8e-08) to 2/2 blocks of the IPB000126 family, which is described as \"Serine proteases, V8 family\". Interpro entry for IP:IPR000126. IPB000126A 105-120 48 IPB000126B 210-226 2.3e-07Significant hit ( 8.2e-07) to 2/2 blocks of the IPB001478 family, which is described as \"PDZ domain (also known as DHR or GLGF)\". Interpro entry for IP:IPR001478. IPB001478A 300-310 0.22 IPB001478B 317-326 0.0017","Residues 97 to 236 match (7e-07) PD:PD416343 which is described as COMPLETE PROTEASE PROTEOME PROBABLE PDZ DOMAIN FAMILY SERINE ","","","","","","","","","","","Wed Jan 8 12:58:48 2003","Wed Jan 8 12:58:48 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01869 is paralogously related to AA01789 (5e-51).","","","","","","Residues 369 to 449 (E-value = 7.1e-10) place AA01869 in the PDZ family which is described as PDZ domain (Also known as DHR or GLGF) (PF00595)","","","","","Loosmore,S.M., Yang,Y.P., Oomen,R., Shortreed,J.M., Coleman,D.C. and Klein,M.H. The Haemophilus influenzae HtrA protein is a protective antigen Infect. Immun. 66 (3), 899-906 (1998) PubMed: 9488373 Waller,P.R. and Sauer,R.T. Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease. J. Bacteriol. 178 (4): 1146-1153 (1996) [PubMed: 8576051].","","Wed Jan 8 12:58:48 2003","1","","","" "AA01871","1258770","1258363","408","ATGCAAACCTGGACAGCAGAAATGTGGCAAGCGGCGTTAATCGGTTTAGTGATCGGTTTCATTATCGGCTATTTCTTATTACGCATCACCAAAGAATCCGCCAAAAAACAAGTGAAAACCGAAGCGGAATTACGCGTAGCAAAAGAACAACTGGAAAGCCAAAAACAGCAGCTGGAAAAACATTTTGCCGAAAGTGCCGACTTGTTGAAATCTCTCGCGCAGGATTATCAAAAACTGTATCAACACTTCGCGCAATCCTCTACCCGATTATTACCTGAACTGAACGATAACTCACTGTTTCAACATGATTTATTAGACGACAAAGACAACCCTATGAACTCACAAAATACCGACGACCAACCAAAAGATTATTCGGAAGGATCATCCGGCTTATTCAAAGCGGAAAAA","","","15608","MQTWTAEMWQAALIGLVIGFIIGYFLLRITKESAKKQVKTEAELRVAKEQLESQKQQLEKHFAESADLLKSLAQDYQKLYQHFAQSSTRLLPELNDNSLFQHDLLDDKDNPMNSQNTDDQPKDYSEGSSGLFKAEK","1258362","","conserved hypothetical protein","Periplasm, Extracellular","","
InterPro
IPR009386
Family
Protein of unknown function DUF1043
PF06295\"[11-136]TDUF1043
noIPR
unintegrated
unintegrated
signalp\"[1-19]?signal-peptide
tmhmm\"[9-27]?transmembrane_regions


","BeTs to 4 clades of COG3105COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3105 is --------------efgh--------Number of proteins in this genome belonging to this COG is","","Residues 9 to 133 match (5e-26) PD:PD032506 which is described as PROTEOME COMPLETE VC0567 MEMBRANE PERIPLASMIC HI1628 YHCB PM0688 STY3527 ","","","","","","","","","","","","Wed Jan 8 13:00:03 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01871 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 11 to 136 (E-value = 2.4e-53) place AA01871 in the DUF1043 family which is described as Protein of unknown function (DUF1043) (PF06295)","","","","","","","","1","","","" "AA01872","1260704","1258944","1761","ATGACACAACAAACTTTTATTCCCGGCAAAGATGCCGCCCTTGAGGAAAGTATTGAAAAATTTCAGCAAAAACTGACCGCACTTGGCTTTCATATTGAAGAAGCTTCGTGGTTAAATCCGGTGCCGAACGTGTGGTCGGTGCATATTCGCGACAAAGACTGCCCGCAATGTTTTTCCAACGGTAAAGGCGCCAGCAAAAAAGCGGCGTTAGCATCGGCATTGGGCGAATATTTCGAGCGACTTTCCACCAATTATTTCTGGACGGATTTCTATTTAGGGCAAAGCATTGCCAACAGCGATTTTGTGCATTATCCGAACGAAAAATGGTTCCCCATTGAAGATGAAGCCCTGTTACCACGCGGCATTTTAGACGATCATTTATTTGAACATTTCGATCCGAATCAGGAACTTACGCCTGAACTTTTGGTGGATTTGCAATCAGGCAATTACGAACGCGGCATTGTCGCCGTGCCCTATGTACGCCAATCGGATCAACAGGCGGTGTATATTCCGCAAAATATCATTTCCAATCTGTACGTCTCTAACGGCATGTCCGCCGGTAACAGCCAATTTGAAGCACGCGTGCAAGGTTTATCGGAAGTGTTTGAACGCTATGTAAAAAACAAAATCATCGCCGAATCCATCAGTTTGCCGCTTATTCCGCAAGACGTGATGGCACGTTATCCGTCTATTCAGGCATCCATTGAAAAGCTGGAACAGGAAGGCTTCCCGATTTTGGCGTATGACGCGTCTCTCGGCGGAAAATATCCGGTGATTTGTGTGATTTTACTCAACCCGACCAATGGCACCTGCTTCGCTTCCTTCGGTGCGCACCCGAAATTCCAAGTGGCATTGGAGCGCACCGTTACCGAATTATTGCAAGGTCGCAGCTTAAAAGATTTGGATGTATTCGCGCCGCCGTCTTTCAATAATGACGATGTCGCTGAACACGCCAATCTGGAAACCCACTTTATCGATTCCAGCGGTTTAATCTCTTGGGATTTATTCAAAAACACGCCGGATTACGACTTCGCCGACTGGAATTTCTCCGGTAAAGACACCCACGAAGAATACGACAATCTGATGGCGATTTTTCGTGCGGAAAACAAAGAAGTTTACATTATGGATTACAACCATTTGAGCGTTTATGCCTGCCGTATCATTGTGCCGGGCATGTCCGATATTTATCCTGCCGACGATTTAATTTACGCCAACAGCAACATGGGCATGGACTGGCGCGAAATTCTGTTGGATTTACCGCATTTCCACCATGAAAAAGAAACCTATCAGGAATTGTTGGAAGAACTGGATGAGCAAGGCATTGACGACGCCATCCGCGTACGCGAATTTATCGGCATCGTGGCGCCCAAAGGCAGCGGCTGGACAACATTGCGCATCGGCGAATTAAAATCCATGCTTTACCTCGCCTTGGGCGATCTGGAAATGGCGCTGGATTGGGCAAACTGGGCATACAACATGAACGGCTCCGTATTCACCGCCGAACGTGCCAACTATTACCGTTGTTTAATCAGTAGCCTTGAGTTGTTCATGGATGGCAATCGCGATCCGCAACAATACCGCATGGTGTTCGACAAAATGTACGGCAAAGACGCCGTTGAATTTGCCTGGAACGCCATTCAGGGCGGCAATCCGTTCTACAACCTACCAGCCGGCGACGAAACCCTCGCCACGTTTAGCGAACATCAAAAGCTGCTGGCGGCATACGCCAAATTGCAAAAAGCCAAACGGGAAAATTGGCAA","","","66847","MTQQTFIPGKDAALEESIEKFQQKLTALGFHIEEASWLNPVPNVWSVHIRDKDCPQCFSNGKGASKKAALASALGEYFERLSTNYFWTDFYLGQSIANSDFVHYPNEKWFPIEDEALLPRGILDDHLFEHFDPNQELTPELLVDLQSGNYERGIVAVPYVRQSDQQAVYIPQNIISNLYVSNGMSAGNSQFEARVQGLSEVFERYVKNKIIAESISLPLIPQDVMARYPSIQASIEKLEQEGFPILAYDASLGGKYPVICVILLNPTNGTCFASFGAHPKFQVALERTVTELLQGRSLKDLDVFAPPSFNNDDVAEHANLETHFIDSSGLISWDLFKNTPDYDFADWNFSGKDTHEEYDNLMAIFRAENKEVYIMDYNHLSVYACRIIVPGMSDIYPADDLIYANSNMGMDWREILLDLPHFHHEKETYQELLEELDEQGIDDAIRVREFIGIVAPKGSGWTTLRIGELKSMLYLALGDLEMALDWANWAYNMNGSVFTAERANYYRCLISSLELFMDGNRDPQQYRMVFDKMYGKDAVEFAWNAIQGGNPFYNLPAGDETLATFSEHQKLLAAYAKLQKAKRENWQ","1258943","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003776
Domain
YcaO_like
PF02624\"[22-394]TYcaO
TIGR00702\"[12-406]TTIGR00702: uncharacterized domain


","No hits to the COGs database.","Significant hit ( 2.6e-38) to 3/3 blocks of the IPB003776 family, which is described as \"DUF181\". Interpro entry for IP:IPR003776. IPB003776A 61-79 9.6e-12 IPB003776B 181-199 9.6e-10 IPB003776C 274-296 7.1e-14","Residues 399 to 587 match (3e-77) PD:PD552157 which is described as PROTEOME COMPLETE CYTOPLASMIC YCAO HI1265 PA1926 YPO1385 PM0687 ORF STY0975 ","","","","","","","","","","","","Wed Jan 8 13:01:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01872 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 394 (E-value = 9.9e-236) place AA01872 in the DUF181 family which is described as Uncharacterized ACR, COG1944 (PF02624)","","","","","","","","1","","","" "AA01873","1262000","1260798","1203","ATGGCCGGAATTTATCCGCTTAACGGCAGCCTTCAACATTATGTATGGGGCGGAGAAAATTACATTCCGAATTTATTGCATATCAATAAAACACAGGCACATTATGCCGAATACTGGCTCGGTGCGCATACTTCCGCGCCGTCACAGGTTGTCACCGCGCAAGGTGAAATGCCGCTGAGCAATTTTTTACAAAAAAATCCGACCGCACTTGGTGCGCAAAGTCGTAGTTTATTTGGTGAAAATCTGCCTTATTTACTCAAAATTTTAGATGTTGCCAATCCCCTTTCCATTCAGTTGCATCCGACCAAAAAACAAGCAGAAATCGGCTTTGCACAGGAAAATGCGGCGGGCATTGCGTTAAACGATCCGAAACGAACTTATAAAGATGATAATCACAAACCGGAAATGATGATCGCACTATCCGATTTCTGGCTTTTGCACGGTTTTAAAACCAAAGATAAGATTCTCGATACCCTTCGCCAACGTCCATCATTAGCGAATTTGGCAACAAAACTTGAATCACAAAATGTATCGGATTTTTACGCCGATCTGATGCTGGCGAAACAGGATCAACTGGCACAATGGCTTTTACCGATTATTGACGCGCAACAAAACGCCTTTGAGCAAAATCAGCTCTCTCCGCAGGATCCCGATTATTGGGTGCTTTACACGCTGCACGCCATGAATATTTCCAGAGATAAACTGGATGCAGGCTTGATGTGTTTCTACCTATTCAACATTGTCAATTTACATGTCGGCGAAGGCATTTTTCAGGCGCCAAGGATTCCCCACGCCTATTTACGCGGTCAAAATATTGAATTAATGGCGTGCTCCGACAATGTGATTCGCGGCGGTTTGACACCGAAGCACGTCGATATTGAGCAATTATTGAACGTTATTGACTACCGCGAAGTGATTCCGCAAGTGATCGCACCCGCACCGAAAGACGCCGTTTATTACACCTATTCAACGCCTGCTGAAGATTTTGCATTGAGCAATTTACGCTATGCGAAAAACACTGAATTTTCTGACCGCACTTTAAACGGCACAATTCTGTTTGTGATGGAAGGTGAAATGACACTGGAAGGCGACGGGCAAAAACTCACCTTAAAGCAAGGACAGGCGGCGTTTATTGAAGCGGATACAGAATACCACGTACAGGGCACTCAAGCAGGCTATGCCGTGCTAGCGGGCGTACCCACT","","","46346","MAGIYPLNGSLQHYVWGGENYIPNLLHINKTQAHYAEYWLGAHTSAPSQVVTAQGEMPLSNFLQKNPTALGAQSRSLFGENLPYLLKILDVANPLSIQLHPTKKQAEIGFAQENAAGIALNDPKRTYKDDNHKPEMMIALSDFWLLHGFKTKDKILDTLRQRPSLANLATKLESQNVSDFYADLMLAKQDQLAQWLLPIIDAQQNAFEQNQLSPQDPDYWVLYTLHAMNISRDKLDAGLMCFYLFNIVNLHVGEGIFQAPRIPHAYLRGQNIELMACSDNVIRGGLTPKHVDIEQLLNVIDYREVIPQVIAPAPKDAVYYTYSTPAEDFALSNLRYAKNTEFSDRTLNGTILFVMEGEMTLEGDGQKLTLKQGQAAFIEADTEYHVQGTQAGYAVLAGVPT","1260797","[CATALYTIC ACTIVITY] D-mannose 6-phosphate = D-fructose 6-phosphate.[FUNCTION] This enzyme is involved in the conversion of glucose to GDP-L-fucose, which can be converted to L-fucose, a capsular polysaccharide. [COFACTOR] Zinc (by similarity). [SUBCELLULAR LOCATION] Cytoplasmic (probable). [SIMILARITY] Belongs to the mannose-6-phosphate isomerase family 1. ","mannose-6-phosphate isomerase","Cytoplasm, Periplasm","","
InterPro
IPR001250
Family
Mannose-6-phosphate isomerase, type I
PR00714\"[7-25]T\"[34-49]T\"[82-103]T\"[127-150]T\"[245-264]T\"[264-283]T\"[283-302]TMAN6PISMRASE
PF01238\"[4-366]TPMI_typeI
TIGR00218\"[1-396]TmanA: mannose-6-phosphate isomerase, class
PS00965\"[127-135]TPMI_I_1
InterPro
IPR014710
Domain
RmlC-like jelly roll fold
G3DSA:2.60.120.10\"[4-284]Tno description
noIPR
unintegrated
unintegrated
PD049684\"[355-400]TQ9CMJ5_PASMU_Q9CMJ5;
PTHR10309\"[9-400]TMANNOSE-6-PHOSPHATE ISOMERASE


","No hits to the COGs database.","Significant hit ( 1.7e-52) to 4/4 blocks of the IPB001250 family, which is described as \"Mannose-6-phosphate isomerase type I\". Interpro entry for IP:IPR001250. IPB001250A 7-17 0.042 IPB001250B 82-98 3.2e-08 IPB001250C 124-155 9.4e-16 IPB001250D 244-288 4.8e-22","Residues 109 to 257 match (2e-09) PD:PD127424 which is described as ISOMERASE PROTEOME COMPLETE MANA MANNOSE-6-PHOSPHATE ","","","","","","","","","","","Wed Jan 8 13:04:34 2003","Wed Jan 8 13:04:34 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01873 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 366 (E-value = 1.1e-48) place AA01873 in the PMI_typeI family which is described as Phosphomannose isomerase type I (PF01238)","","","","","Miles,J.S. and Guest,J.R. 1984. Nucleotide sequence and transcriptional start point of the phosphomannose isomerase gene (manA) of Escherichia coli. Gene 32(1-2):41-48. PubMed: 6397402. Collins,L.V. and Hackett,J. 1991. Sequence of the phosphomannose isomerase-encoding gene of Salmonella typhimurium. Gene 103(1):135-136. PubMed: 1879695.Collins,L.V. and Hackett,J. Sequence of the phosphomannose isomerase-encoding gene of Salmonella typhimurium. Gene 103 (1): 135-136 (1991) [PubMed: 1879695].","","Wed Jan 8 13:04:34 2003","1","","","" "AA01874","1262176","1262511","336","ATGGCACAAGGATATTACGAATTAAAATTAGCAAAAGATGGACAATTTATGTTCAATTTAATGGCAACTAACGGACAAATTATTTTAACCAGCGAGCTTTACAAATCGAAAGCCTCCGCGCAAAACGGCATTGCCTCCGTGCAAAAAAACGGAGTGGATGCAAAAAACTTTGAATTTCGTACCACAAAAAATGATCAGCCTTATTTCGTATTAAAAGCGGCAAATCATCAGGAAATCGGTCGCAGCCAATATTATTCTTCGCAAGCTGCTGCACAAAAAGGTGTAGAGTCCGTAATGAACAACGCTTCCAGCGAAGATATTCGGGATCTTACCGTA","","","12408","MAQGYYELKLAKDGQFMFNLMATNGQIILTSELYKSKASAQNGIASVQKNGVDAKNFEFRTTKNDQPYFVLKAANHQEIGRSQYYSSQAAAQKGVESVMNNASSEDIRDLTV","1262510","","conserved hypothetical protein","Extracellular","","
InterPro
IPR010879
Domain
Protein of unknown function DUF1508
PF07411\"[11-59]T\"[62-110]TDUF1508


","No hits to the COGs database.","","Residues 6 to 50 match (4e-09) PD:PD031011 which is described as PROTEOME COMPLETE OPERON 5'REGION CC2965 PLASMID PTX ATU5359 YPO2854 REPEAT ","","","","","","","","","","","","Wed Jan 8 13:05:54 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01874 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 62 to 110 (E-value = 2.3e-23) place AA01874 in the DUF1508 family which is described as Domain of unknown function (DUF1508) (PF07411)","","","","","","","","1","","","" "AA01875","1262703","1263566","864","ATGTTTAAACAACTTCAACAAGTCGGAAAGGCATTTATGTTGCCTATTGCCATTTTGCCCGCTGCCGGTTTGCTGTTAGGGATTGGCGGTGCGTTGTCCAATAAAGCCACTGTGCAGGCGTATCCTTTATTGGATAACCCGGCATTGCAGGGCGTTTTTCAGATTATGTCCGCCGCAGGCTCGGTCGTGTTCGGCAATTTGGCACTTTTGTTGTGTATCGGTTTGGGCATCGGCTTGGCGAAACGGGATAAAGGCGTAGCAGCATTGGCGGCGGTGGTCGGTTATTTGATCATGACAGGCACCATTTCGGCGTTAATTCCGTTGTTTTCGCCGGAAACCAAAAGCATTGATACGGGCGTCATTGGCGCGTTGGTGATGGGCTTGATTACGGTAAAACTGCATAACAAATATCACAACATTCAGTTGCCGCAAATTTTAGGCTTCTTCGGCGGTTCGCGTTTTGTGCCAATTGTGACGGCATTTGCCGCGATTTTTGTGGGAGCGATTTTCTTCTTAATTTGGCCGACCTTCCAAAATTGGTTATTGTCTGCGGGTGAACATATCGCTTCTATGGGCGCAATCGGCACTTTCTTCTACGGTTTCTTAATGCGTTTATGCGGCGCGGTAGGGTTGCACCACAATTTACCCGCTGTTCTGGTACACCGAATTAGGCGGCACGGAAATCGTCAACGGCGAAACCATTATCGGCGCGCAAAAGATTTTCTTCGTCCAATTGGCGGATCCGAACCATCAAGGGCTATTTACCGAAGGTACGCGTTTCTTTGCCGGACGTTTCGACACCATGATGTTCGGCTTGACGGCAGCCTGTTTGGCAATGTATCACTGTGTGCCGAAAGCGCGCCG","","","31954","MFKQLQQVGKAFMLPIAILPAAGLLLGIGGALSNKATVQAYPLLDNPALQGVFQIMSAAGSVVFGNLALLLCIGLGIGLAKRDKGVAALAAVVGYLIMTGTISALIPLFSPETKSIDTGVIGALVMGLITVKLHNKYHNIQLPQILGFFGGSRFVPIVTAFAAIFVGAIFFLIWPTFQNWLLSAGEHIASMGAIGTFFYGFLMRLCGAVGLHHNLPAVLVHRIRRHGNRQRRNHYRRAKDFLRPIGGSEPSRAIYRRYAFLCRTFRHHDVRLDGSLFGNVSLCAESAP","1263565","[FUNCTION] This is a component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. the IICD domains contain the sugar binding site and the transmembrane channel; the iia domain contains the primary phosphorylation site (the donor is phospho-hpr); IIA transfers its phosphoryl group to the IIB domain which finally transfers it to the sugar.[FUNCTION] MalX encodes a phosphotransferase system enzyme II that can recognize glucose and maltose as substrates even though thesesugars may not represent the natural substrates of the system. [CATALYTIC ACTIVITY] Protein N-phosphohistidine + sugar = protein histidine + sugar phosphate.[SUBCELLULAR LOCATION] Integral membrane protein. Inner membrane. ","PTS system, glucose-specific enzyme II, A component","Inner membrane, Cytoplasm","","
InterPro
IPR003352
Domain
Phosphotransferase system, EIIC
PF02378\"[9-267]TPTS_EIIC
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[34-175]Tno description
InterPro
IPR013013
Domain
Phosphotransferase system, EIIC component, type 1
PS51103\"[1-288]TPTS_EIIC_TYPE_1
noIPR
unintegrated
unintegrated
signalp\"[1-23]?signal-peptide
tmhmm\"[12-32]?\"[51-71]?\"[86-106]?\"[116-134]?\"[155-175]?\"[181-201]?transmembrane_regions


","BeTs to 6 clades of COG1263COG name: Phosphotransferase system IIC components, glucose/maltose/N-acetylglucosamine-specificFunctional Class: GThe phylogenetic pattern of COG1263 is -----------lb-efgh---j--twNumber of proteins in this genome belonging to this COG is","","Residues 49 to 213 match (9e-53) PD:PD001764 which is described as COMPONENT PTS SYSTEM PROTEOME COMPLETE PHOSPHOTRANSFERASE IIABC ENZYME TRANSFERASE SYSTEM ","","","","","","","","","","","Wed Jan 8 13:12:44 2003","Wed Jan 8 13:12:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01875 is paralogously related to AA02478 (5e-20) and AA02477 (6e-11).","","","","","","Residues 9 to 247 (E-value = 7.5e-35) place AA01875 in the PTS_EIIC family which is described as Phosphotransferase system, EIIC (PF02378)","","","","","Reidl,J. and Boos,W. The malX malY operon of Escherichia coli encodes a novel enzyme II of the phosphotransferase system recognizing glucose and maltoseand an enzyme abolishing the endogenous induction of the maltosesystem. J. Bacteriol. 173 (15): 4862-4876 (1991) [PubMed: 1856179].Reidl,J., Romisch,K., Ehrmann,M. and Boos,W. MalI, a novel protein involved in regulation of the maltose system of Escherichia coli, is highly homologous to the repressor proteinsGalR, CytR, and LacI. J. Bacteriol. 171 (9): 4888-4899 (1989) [PubMed: 2670898].","","Wed Jan 8 13:12:44 2003","1","","","" "AA01876","1263505","1264191","687","ATGATGTTCGGCTTGACGGCAGCCTGTTTGGCAATGTATCACTGTGTGCCGAAAGCGCGCCGTAACGCCATCGGTGGTTTATTTTTAGGCGCGGCGCTCACCTCTTTCATTACCGGCATTACCGAGCCTATCGAATTCATGTTCTTGTTCGTCGCTCCTTGGTTGTATGTGTTCCACGCCTTTTTAGACGGCGTTTCCTTCTACATCGCCGACATTTTGAACATTTCCATTGGCAACACCTTCTCCGGCGGTTTTATCGACTTCTTGCTGTTCGGTATCTTACAAGGCAACGACAATACCAACTGGCTTAAAGTCATTTGGGTGGGCATCGGCTGGGCGGCGTTGTATTATTTCAGCTTCCGTTTCCTGATTACCAAATTTAACGTCATGACCCCGGGACGTGCAGAAGAGCAGGATGACGCGGTTGAACAACAAACGTCTTCGTTAACGGAAAATGCGCACGAGATCATTAAAGCCCTCGGCAATAGTGAGAATATTGAAAATGTGGACGCGTGCATTACCCGTCTGCGCGTGGCGGTGAAGGACGTTAAATTGGTGGATAAACCGCGTTTGAAAGCCTTGGGTGCCATTGATGTGCTGGAAGTGGGCGGCGGCGTGCAAGCCATTTATGGTGCAAAAGCCGTGTTATATAAGAGCGAAATCAATCAGATTTTAGGCAAAGAAGAT","","","27798","MMFGLTAACLAMYHCVPKARRNAIGGLFLGAALTSFITGITEPIEFMFLFVAPWLYVFHAFLDGVSFYIADILNISIGNTFSGGFIDFLLFGILQGNDNTNWLKVIWVGIGWAALYYFSFRFLITKFNVMTPGRAEEQDDAVEQQTSSLTENAHEIIKALGNSENIENVDACITRLRVAVKDVKLVDKPRLKALGAIDVLEVGGGVQAIYGAKAVLYKSEINQILGKED","1264190","[FUNCTION] This is a component of thephosphoenolpyruvate-dependent sugar phosphotransferase system(PTS), a major carbohydrate active transport system. the IICDdomains contain the sugar binding site and the transmembranechannel; the IIA domain contains the primary phosphorylation site(the donor is phospho-hpr); IIA transfers its phosphoryl group tothe IIB domain which finally transfers it to the sugar. [FUNCTION] MalX encodes a phosphotransferase system enzyme II that can recognize glucose and maltose as substrates even though these sugars may not represent the natural substrates of the system. [CATALYTIC ACTIVITY] Protein N-phosphohistidine + sugar = proteinhistidine + sugar phosphate. [SUBCELLULAR LOCATION] Integral membrane protein. Inner membrane.","PTS system, IIBC components","Inner membrane, Cytoplasm","","
InterPro
IPR001996
Domain
Phosphotransferase system, EIIB
PF00367\"[153-187]TPTS_EIIB
PS51098\"[150-229]TPTS_EIIB_TYPE_1
PS01035\"[165-182]TPTS_EIIB_TYPE_1_CYS
InterPro
IPR003352
Domain
Phosphotransferase system, EIIC
PF02378\"[1-64]TPTS_EIIC
InterPro
IPR011535
Domain
Phosphotransferase system, glucose-like IIB component
TIGR00826\"[125-211]TEIIB_glc: PTS system, glucose-like IIB comp
InterPro
IPR013013
Domain
Phosphotransferase system, EIIC component, type 1
PS51103\"[1-136]TPTS_EIIC_TYPE_1
noIPR
unintegrated
unintegrated
G3DSA:3.30.1360.60\"[138-225]Tno description
signalp\"[1-39]?signal-peptide
tmhmm\"[22-40]?\"[50-70]?\"[72-94]?\"[100-120]?transmembrane_regions


","BeTs to 6 clades of COG1263COG name: Phosphotransferase system IIC components, glucose/maltose/N-acetylglucosamine-specificFunctional Class: GThe phylogenetic pattern of COG1263 is -----------lb-efgh---j--twNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.2e-22) to 2/2 blocks of the IPB001996 family, which is described as \"PTS (phosphotransferase system) EIIB domain\". Interpro entry for IP:IPR001996. IPB001996A 153-187 1.3e-18 IPB001996B 202-214 0.031","Residues 103 to 222 match (2e-08) PD:PD094903 which is described as PROTEOME COMPONENT PTS COMPLETE MALX IIABC SYSTEM GLUCOSE-SPECIFIC MALTOSE ","","","","","","","","","","","Wed Jan 8 13:17:51 2003","Wed Jan 8 13:13:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01876 is paralogously related to AA02478 (3e-40).","","","","","","Residues 153 to 187 (E-value = 3.7e-15) place AA01876 in the PTS_EIIB family which is described as phosphotransferase system, EIIB (PF00367)","","","","","Reidl,J. and Boos,W. The malX malY operon of Escherichia coli encodes a novel enzyme II of the phosphotransferase system recognizing glucose and maltose and an enzyme abolishing the endogenous induction of themaltose system. J. Bacteriol. 173 (15): 4862-4876 (1991) [PubMed: 1856179]. Reidl,J., Romisch,K., Ehrmann,M. and Boos,W. MalI, a novel protein involved in regulation of the maltose system of Escherichia coli, is highly homologous to the repressor proteins GalR, CytR, and LacI. J. Bacteriol. 171 (9): 4888-4899(1989) [PubMed: 2670898].Zagorec,M. and Postma,P.W. Cloning and nucleotide sequence of the ptsG gene of Bacillus subtilis. Mol. Gen.Genet. 234 (2): 325-328 (1992) [PubMed: 1508157].Gonzy-Treboul,G., Zagorec,M., Rain-Guion,M.C. and Steinmetz,M.Phosphoenolpyruvate:sugar phosphotransferase system of Bacillus subtilis: nucleotide sequence of ptsX, ptsH and the 5'-end of ptsIand evidence for a ptsHI operon. Mol. Microbiol. 3 (1): 103-112 (1989) [PubMed: 2497294].Sutrina,S.L., Reddy,P., Saier,M.H. Jr. and Reizer,J. The glucose permease of Bacillus subtilis is a single polypeptide chain that functions to energize the sucrose permease. J. Biol. Chem. 265 (30): 18581-18589 (1990) [PubMed: 2120236].Liao,D.I., Kapadia,G., Reddy,P., Saier,M.H. Jr., Reizer,J. and Herzberg,O. Structure of the IIA domain of the glucose permease of Bacillus subtilis at 2.2-A resolution. Biochemistry 30 (40): 9583-9594 (1991) [PubMed: 1911744].","","Wed Jan 8 13:17:51 2003","1","","","" "AA01877","1264950","1264255","696","ATGTGGCGTGCTAAATATGAAAAATCGCTCACCATGCCAAGCGGCTGGCAGCAGCTTCCCAACGGAAGTGCGTATTGTAACGCATTAAGCGACTATTTTGCGCCTTGGCTTACAAAAATTTGTGGCTACCAAATTCTGAAAATCGGCGGACTCAGCGCGGAAATTACCTGCGATTTGCCGCTGCGCCATCAAATCAGTGTCAATGAAAAAACGCCTCCGAATCTGACCGCACTTTTGGGCGACTATCACTCCGTCGTGCAAAGCAAACTGACCGAATTGCCTTTTATCGAACAACACATCGATGCCTGTATTTTAACCAATACCCTTAATTTTGTGCAGGATCCGCACCAGGTTCTGCGCGAAACCCATCGGGTGCTGGCAGACGACGGTTATTTGTTTCTCAGTCTGTTTAACCCGTTGAGCACTTTTATGTTTAAGACCAGACTGGGGGAATTTCCGTTACGCCATTACTGTGCCTGGCGCGTTGCGGATTGGTTGGAATTATTGAATTTTGAGATTCTGGAACAACAAAATTTGGCGCTGAATGAACGACAAAGCGGCTGGTTTTCGCCGCTTATCGTGATGGTAGCGCAAAAACGTACTTATCCTTTAATCCTCAATCCAAAAAAAGTGCGGTCAAAAATCCCGGCGTTTTTACAACCTGCAGAAGCCTTGAAAGCGGCGGGGGAAAATCCG","","","26517","MWRAKYEKSLTMPSGWQQLPNGSAYCNALSDYFAPWLTKICGYQILKIGGLSAEITCDLPLRHQISVNEKTPPNLTALLGDYHSVVQSKLTELPFIEQHIDACILTNTLNFVQDPHQVLRETHRVLADDGYLFLSLFNPLSTFMFKTRLGEFPLRHYCAWRVADWLELLNFEILEQQNLALNERQSGWFSPLIVMVAQKRTYPLILNPKKVRSKIPAFLQPAEALKAAGENP","1264254","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR013216
Domain
Methyltransferase type 11
PF08241\"[46-134]TMethyltransf_11
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[84-210]Tno description
PTHR10108\"[85-134]TMETHYLTRANSFERASE
PTHR10108:SF32\"[85-134]TMETHYLTRANSFERASE-RELATED


","BeTs to 15 clades of COG0500COG name: SAM-dependent methyltransferasesFunctional Class: Q,RThe phylogenetic pattern of COG0500 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 13 to 65 match (9e-13) PD:PD478496 which is described as PROTEOME COMPLETE METHYLTRANSFERASE STY0283 SAM-DEPENDENT VC2235 YAFS PM0686 TRANSFERASE YPO1080 ","","","","","","","","","","","","Wed Jan 8 13:19:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01877 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01878","1264971","1265669","699","ATGTTAATTCCGATTCCTGCCTTAAATGACAACTATATTTGGCTTTATGCCCGAGAAAATTTACCGCCGTTAATCGTCGATGTACCGGAATGTGAAGCGTTGTTCCGGTTCCTGGATACCCACCAGTTAACGCCGGAAGCGGTGTTGCTGACGCATTTGCACGATGACCATGTCGGTGGCGTGGGCGAATTTAAAACGCGTTATCCCGACGTGCCGATTTACGGCCCCGCCGAATGTGCCGCCAAAGGGGCAACGCACATCATTAATGAGGGCGACATTAACACCGAACATTACCGAATTCAAGTGTTGCCCGCCGCAGGGCATACGGCGCAACATGTGGCGTATTTAACGGACGGGCATTTGTTTTGCGGTGACGCGCTATTTTCCGCCGGTTGCGGACGGGTATTTACCGGCGATTACGCCACCATGTTTGCCGCCATGCAACGTTTTGCCAGCTTGCCTGACGAAACCATCGTCTGTCCGGGTCATGAATATACTTTAAGTAACCTGAAATTCGTGGAAAGCGTTTGGGCAAACAAAAGTGCGGTGGAAAATCAGCGCGTTTTGGTGGAACGGCAACGTGCCGCCAATCAGCCAAGCCTGCCGAGCACCATCGGCTTGGAAAAACAAATTAATCCGTTTTTAACGGCAACGAGTCTGGCGCAATTTACGCAATTACGCCAGGCAAAAGATCATTTT","","","25842","MLIPIPALNDNYIWLYARENLPPLIVDVPECEALFRFLDTHQLTPEAVLLTHLHDDHVGGVGEFKTRYPDVPIYGPAECAAKGATHIINEGDINTEHYRIQVLPAAGHTAQHVAYLTDGHLFCGDALFSAGCGRVFTGDYATMFAAMQRFASLPDETIVCPGHEYTLSNLKFVESVWANKSAVENQRVLVERQRAANQPSLPSTIGLEKQINPFLTATSLAQFTQLRQAKDHF","1265668","[FUNCTION] Tthiolesterase that catalyses the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lacticacid (by similarity). [CATALYTIC ACTIVITY] (S)-(2-hydroxyacyl)glutathione + H(2)O = glutathione + a 2-hydroxy acid anion.[COFACTOR] Binds two zinc ions (by similarity)[SIMILARITY] Belongs to the glyoxalase II family.[PATHWAY] Glyoxal pathway.","hydroxyacylglutathione hydrolase","Cytoplasm","","
InterPro
IPR001279
Domain
Beta-lactamase-like
PF00753\"[10-163]TLactamase_B
noIPR
unintegrated
unintegrated
G3DSA:3.60.15.10\"[1-233]Tno description
PTHR11935\"[82-233]TBETA LACTAMASE DOMAIN
PTHR11935:SF7\"[82-233]THYDROXYACYLGLUTATHIONE HYDROLASE


","No hits to the COGs database.","Significant hit ( 2.5e-07) to 1/6 blocks of the IPB001587 family, which is described as \"Uncharacterized protein family UPF0036\". Interpro entry for IP:IPR001587. IPB001587B 28-76 2.3e-07","","","","","","","","","","","","Wed Jan 8 13:24:22 2003","Wed Jan 8 13:24:22 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01878 is paralogously related to AA02708 (3e-11).","","","","","","Residues 10 to 163 (E-value = 5.4e-26) place AA01878 in the Lactamase_B family which is described as Metallo-beta-lactamase superfamily (PF00753)","","","","","","","","1","","","" "AA01879","1265857","1267158","1302","ATGACGATTTTAGTTCTGGGTATCAATCACAAAACTGCTTCCGTGGCATTGCGGGAAAAGGTGGCGTTTTCCGACGAAAAGCGCACTTTTGCTTTGCGTCACATTCAACAAACGCAGTTGGCGGAAAGTGCGGTGATTTTATCCACCTGTAATCGCACGGAAGTTTATCTGCACAATAAAAGCGTTCCGCCGCAAGAGACGCAAACCTGGATCACACTGGCGGTGCAGTGGTTTGCCGGCATTCATCAACTAGCGTTGGCGGAGCTGCAGCACTGTGTTTATACTCACGAAAATCTTCAGGCGGCGAATCATTTAATGGAAGTGGCGTGCGGTTTGGATTCGCTGATTTTAGGCGAACCGCAGATTTTGGGGCAGGTGAAGCAAGCCTACCACATGAGCGAGCAGCATTATCAACAGGAAGGGCAAACCATTTCCGGCGAACTATCCCGTTTATTCCAAAAAACCTTTGCTACCGCTAAACGGGTGCGCACCGAAACCAACATCGGCGAGAGTGCGGTGTCCGTTGCCTATGCCGCCTGTAGCCTAGCACGTCAGATTTTTGAATCCCTGCGTGACTTGACGATTTTATTAGTGGGCGCAGGTGAAACCATTGAACTGGTGAACCGCCATTTGTTACGTCACGGCGTGAAAAACTTATTTATCGCCAACCGTACATTGGCGCGCGCCGAGGCGTTGGTGGAAAAATTGGATTCGGCGGCGAATATTCAAGTCCTTTCCCTGGAACAGTTACAGCAGGGTTTAAATCAGACGGATATTGTGATCAGTTCCACCGGCAGCCCGAACATTCTGATTAGCCGCGACATGGTTCAGTGGGCGCAAACGGCGCGTGGTTATCGCCCGATGTTGTTGGTGGATATTGCCGTGCCCCGCGATATTGATGAAAGTGCGGTGGATTTGGACAGCGTTTATCATTACACGGTGGATGATTTGCAAAACATCATTCAGCATAATTTGAATCAGCGGGAACAGGCGTCCGAACAGGCAAAAGCAATTATTCGGGCGGAATGTGCCGATTTCTTTGAATGGCTGAAAGTACATCAATTTTCCAATTTGATTCGACGTTATCGCGAAAATGCCGAACACGCCCGGCAGGATTTATTGGAAAAAGCGTTGAGTTCGTTACAACAAGGGGAAAATGCCGAACAGGTGTTGCAGGAATTGAGTTATAAATTAATGAATAAATTAATCCATTCGCCGACCCAGGCTATGCAAACGATGGTAAAAAGCGGCAATGCCGGCGGCTTGCAAACCTTTTCAAAAGCCTTGGGAATGGAAGAAGAA","","","48704","MTILVLGINHKTASVALREKVAFSDEKRTFALRHIQQTQLAESAVILSTCNRTEVYLHNKSVPPQETQTWITLAVQWFAGIHQLALAELQHCVYTHENLQAANHLMEVACGLDSLILGEPQILGQVKQAYHMSEQHYQQEGQTISGELSRLFQKTFATAKRVRTETNIGESAVSVAYAACSLARQIFESLRDLTILLVGAGETIELVNRHLLRHGVKNLFIANRTLARAEALVEKLDSAANIQVLSLEQLQQGLNQTDIVISSTGSPNILISRDMVQWAQTARGYRPMLLVDIAVPRDIDESAVDLDSVYHYTVDDLQNIIQHNLNQREQASEQAKAIIRAECADFFEWLKVHQFSNLIRRYRENAEHARQDLLEKALSSLQQGENAEQVLQELSYKLMNKLIHSPTQAMQTMVKSGNAGGLQTFSKALGMEEE","1267157","[CATALYTIC ACTIVITY] Glutamyl-tRNA(Glu) + NADPH = glutamate-1-semialdehyde + NADP(+) + tRNA(Glu).[PATHWAY] Porphyrin biosynthesis by the C5 pathway; first step.","glutamyl-tRNA reductase","Cytoplasm","","
InterPro
IPR000343
Family
Tetrapyrrole biosynthesis, glutamyl-tRNA reductase
PF00745\"[333-432]TGlutR_dimer
PF05201\"[6-167]TGlutR_N
TIGR01035\"[3-432]ThemA: glutamyl-tRNA reductase
PS00747\"[104-127]TGLUTR
InterPro
IPR006151
Domain
Shikimate/quinate 5-dehydrogenase
PF01488\"[171-320]TShikimate_DH
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[171-327]Tno description


","BeTs to 19 clades of COG0373COG name: Glutamyl-tRNA reductaseFunctional Class: HThe phylogenetic pattern of COG0373 is aomp-z-q-dr-bcefghsnu--i--Number of proteins in this genome belonging to this COG is","Significant hit ( 6e-104) to 9/9 blocks of the IPB000343 family, which is described as \"Glutamyl-tRNA reductase\". Interpro entry for IP:IPR000343. IPB000343A 5-21 5e-08 IPB000343B 47-56 9.8e-06 IPB000343C 104-127 3.9e-19 IPB000343D 151-183 1.2e-20 IPB000343E 195-225 3.8e-14 IPB000343F 258-277 4.3e-08 IPB000343G 287-301 3.9e-08 IPB000343H 312-328 9.3e-07 IPB000343I 397-407 0.2","Residues 358 to 410 match (2e-11) PD:PD489822 which is described as OXIDOREDUCTASE NADP GLUTAMYL-TRNA BIOSYNTHESIS PORPHYRIN GLUTR REDUCTASE 1.2.1.- PROTEOME COMPLETE ","","","","","","","","","","","Wed Jan 8 13:30:06 2003","Wed Jan 8 13:30:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01879 is paralogously related to AA00575 (3e-05).","","","","","","Residues 333 to 434 (E-value = 6.9e-26) place AA01879 in the GlutR_dimer family which is described as Glutamyl-tRNAGlu reductase, dimerisation domain (PF00745)","","","","","Breton,R., Sanfacon,H., Papayannopoulos,I., Biemann,K. and Lapointe,J. Glutamyl-tRNA synthetase of Escherichia coli. Isolation and primary structure of the gltX gene and homology with other aminoacyl-tRNA synthetases J. Biol. Chem. 261 (23), 10610-10617 (1986) PubMed: 3015933 Brun,Y.V., Sanfacon,H., Breton,R. and Lapointe,J. Closely spaced and divergent promoters for an aminoacyl-tRNA synthetase gene and a tRNA operon in Escherichia coli. Transcriptional and post-transcriptional regulation of gltX, valU and alaW J. Mol. Biol. 214 (4), 845-864 (1990) PubMed: 2201777 ","","Wed Jan 8 13:30:06 2003","1","","","" "AA01880","1267223","1268443","1221","ATGCGAGAAAATCCTCAAATCGCGAATGTTGATCTAGTGAAACAAATGAATAGTGCGGTTGTGTATAAATTAATCGATCAGCAGGGTCCCATTTCCCGTATTCAAATTTCTGAAATTAGCCAGCTTGCCCCGGCGAGCGTCACCAAAATTACCCGCCATCTTCTTGCCCGCGGTTTAATTAAAGAAGTGGAACAACAGGAATCCACCGGCGGTCGTAGAGCCACTTCTATTGTGGCGGAATATAAAAATTTTCGTTCTATTTCAATTGGTCTCGGGCGTGAACATTTAACGCTAGCGATCATGGATTTGTCGGCGAAGTTGTTAAAAAAAGAGGTGTTCACGCTGCCGAATCACCAAGTCCCGCAAGAATTCGAGCTGTTTTTATTTCGGCATTTAGCTGAATTTATGCTGACCAATCAAACACGGGGTAGTGAATTTATTGCCATCGGCATTACCGTGCCGGGCTTTGTAGATATGAAAAGCGGTATGATTGAACAGGTGCCGCATTTTGATTTAAGCGAGCCTTGGGACTTGGCAAATCATATTGCCGAACGTTTTCACTTAGCTACCTATATCGGGCATGATGTGCGCAGTCTTGCGCTTGCCGAGCATTATTTCGGCGTGACCAAAGATTGTTACGATTCCTTGCTGTTACGTATTCATCGCGGTGTTGGCGCGGGCATTGTGATTAATCATGAAGTCTTTTTAGGTTACAAAAATAATGTAGGCGAAATCGGGCATATTCAGGTGGATCCGCTGGGTAAGCGTTGTATGTGCGGTAATGTCGGTTGTTTGGAAACTGTTGTGAGCAATTCAGCTATTGAAAACAAAATGTCGGAATTGCTGGAAGACGGTTATCAAAGCAAATGGCTTTCGTTAGAAGCCCATGATATTGAAGCTATTTGCAAAGCCAGTAATAAGCAGGACGCGGTGGCGACAGAACTCATTGAACATGTCGGCGTACAAATCGGGCGGGTATTGGCGATGAGCGTAAATATGTTTAATCCGGAAAAAATCGTGATTTCCGGCGAAATTACGCAAGCGAAGAATGTATTATTCGCGGCAATTCGTCGTACATTGGAAAGCCATGCATTGCCTGCATTTGTACAAAATACGCCATTGGTTACATCGGAATTAAGCAATGAAGATGTAATAGGCGCCTTTGCGTTAATTAAAAGGGCGTTATTTGACGGCAGTTTATTGCGTCGTTTAATTGAAGAA","","","45901","MRENPQIANVDLVKQMNSAVVYKLIDQQGPISRIQISEISQLAPASVTKITRHLLARGLIKEVEQQESTGGRRATSIVAEYKNFRSISIGLGREHLTLAIMDLSAKLLKKEVFTLPNHQVPQEFELFLFRHLAEFMLTNQTRGSEFIAIGITVPGFVDMKSGMIEQVPHFDLSEPWDLANHIAERFHLATYIGHDVRSLALAEHYFGVTKDCYDSLLLRIHRGVGAGIVINHEVFLGYKNNVGEIGHIQVDPLGKRCMCGNVGCLETVVSNSAIENKMSELLEDGYQSKWLSLEAHDIEAICKASNKQDAVATELIEHVGVQIGRVLAMSVNMFNPEKIVISGEITQAKNVLFAAIRRTLESHALPAFVQNTPLVTSELSNEDVIGAFALIKRALFDGSLLRRLIEE","1268442","FUNCTION] Acts as a repressor of the nagebacd operon and acts both as an activator and a repressor for the transcription of the glmSU operon. [INDUCTION] By N-acetyl-glucosamine.[SIMILARITY] Belongs to the rok (nagC/xylR) family. ","N-acetylglucosamine repressor","Cytoplasm","","
InterPro
IPR000600
Family
ROK
PF00480\"[88-274]TROK
PS01125\"[220-247]TROK
InterPro
IPR000835
Family
Bacterial regulatory protein, MarR
PF01047\"[24-61]TMarR
noIPR
unintegrated
unintegrated
G3DSA:3.30.420.160\"[195-399]Tno description
PTHR18964\"[152-397]TROK FAMILY
PTHR18964:SF37\"[152-397]TGLUCOSE KINASE


","BeTs to 14 clades of COG1940COG name: Transcriptional regulatorsFunctional Class: KThe phylogenetic pattern of COG1940 is ao-p-z-qvdrlbce-gh---j--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 6.6e-16) to 5/5 blocks of the IPB000600 family, which is described as \"ROK family\". Interpro entry for IP:IPR000600. IPB000600A 66-73 11 IPB000600B 189-203 0.46 IPB000600C 220-229 0.021 IPB000600D 242-248 0.65 IPB000600E 257-266 0.00045","Residues 9 to 121 match (1e-07) PD:PD487166 which is described as PROTEOME COMPLETE LIN0217 LMO0178 ","","","","","","","","","","","Wed Jan 8 13:37:50 2003","Wed Jan 8 13:37:50 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01880 is paralogously related to AA02232 (1e-25), AA02470 (2e-14) and AA02616 (1e-11).","","","","","","Residues 88 to 274 (E-value = 2e-47) place AA01880 in the ROK family which is described as ROK family (PF00480)","","","","","Plumbridge,J.A. Sequence of the nagBACD operon in Escherichia coli K12 and pattern of transcription within the nag regulon. Mol. Microbiol. 3 (4): 505-515 (1989) [PubMed: 2668691].Peri,K.G., Goldie,H. and Waygood,E.B. Cloning and characterization of the N-acetylglucosamine operon of Escherichia coli. Biochem. Cell Biol. 68 (1): 123-137 (1990) [PubMed: 2190615].Plumbridge,J. Co-ordinated regulation of amino sugar biosynthesis and degradation: the NagC repressor acts as both an activator and arepressor for the transcription of the glmUS operon and requirestwo separated NagC binding sites. EMBO J. 14 (16): 3958-3965 (1995) [PubMed: 7545108].","","Wed Jan 8 13:37:50 2003","1","","","" "AA01881","1269825","1269184","642","ATGAAAATTATTCTATTAGGTGCACCGGGCGCAGGAAAAGGTACACAAGCCCAATTTATTATGAATAAATTTGCTATTCCGCAAATCTCCACCGGCGATATGTTACGTTCCGCGATCAAAGCTGGCACCGAGTTAGGCAAACAAGCTAAAACCCTAATGGATGCCGGTCAATTAGTGCCCGATGATTTAATCATTTCGTTAGTTAAAGAACGTGTTGCCCAACCTGACTGCACAAAAGGTTTCTTACTGGACGGCTTCCCGCGCACCATTCCACAAGCGGACGCACTAAAATCTGCCGGTATCGCCATTGATTATGTGTTGGAATTCGATGTGCCGGATGAAGTGATTGTAGAACGCATGAGCGGTCGCCGCGTACACCAACCGTCCGGTCGTTCTTACCACATCGTTTACAATCCGCCGAAAACAGAAGGCAAAGATGATGTTACAGGTGAAGATTTAATTATTCGTGCCGATGACAAACCGGAAACCGTGTTAGATCGTTTAAAAGTGTATCACACCACCACCAAACCGTTGGTTGACTACTACCAAGCTGAAGCCAAAGCAGGCAATGTGCAATATTTCCGCTTAGACGGTACACAAAAAGTGGAAGCTGTGAGCAAGGAATTAGATAAAATCTTGGCT","","","23470","MKIILLGAPGAGKGTQAQFIMNKFAIPQISTGDMLRSAIKAGTELGKQAKTLMDAGQLVPDDLIISLVKERVAQPDCTKGFLLDGFPRTIPQADALKSAGIAIDYVLEFDVPDEVIVERMSGRRVHQPSGRSYHIVYNPPKTEGKDDVTGEDLIIRADDKPETVLDRLKVYHTTTKPLVDYYQAEAKAGNVQYFRLDGTQKVEAVSKELDKILA","1269183","[FUNCTION] This small ubiquitous enzyme is essential for maintenance and cell growth. [CATALYTIC ACTIVITY] ATP + AMP = ADP + ADP.[SUBUNIT] Monomer (By similarity).[SUBCELLULAR LOCATION] Cytoplasmic (By similarity).","adenylate kinase","Cytoplasm, Periplasm","","
InterPro
IPR000850
Family
Adenylate kinase
PR00094\"[4-17]T\"[32-46]T\"[81-97]T\"[156-171]T\"[173-187]TADENYLTKNASE
PTHR23359\"[1-214]TNUCLEOTIDE KINASE
PF00406\"[5-187]TADK
PS00113\"[81-92]TADENYLATE_KINASE
InterPro
IPR006259
Family
Adenylate kinase, subfamily
TIGR01351\"[2-214]Tadk: adenylate kinases
InterPro
IPR007862
Domain
Adenylate kinase, lid region
PF05191\"[123-158]TADK_lid
InterPro
IPR011769
Domain
Adenylate/cytidine kinase, N-terminal
PD000657\"[1-45]TKAD_PASMU_P57837;
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[1-213]Tno description
PTHR23359:SF22\"[1-214]TADENYLATE KINASE


","BeTs to 22 clades of COG0563COG name: Adenylate kinase and related kinasesFunctional Class: FThe phylogenetic pattern of COG0563 is ao--k-yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.5e-72) to 4/4 blocks of the IPB000850 family, which is described as \"Adenylate kinase\". Interpro entry for IP:IPR000850. IPB000850A 4-36 1.1e-20 IPB000850B 76-90 2.2e-09 IPB000850C 111-141 2.8e-21 IPB000850D 156-182 5.8e-17 IPB000850A 22-54 0.53","Residues 3 to 61 match (5e-07) PD:PD504719 which is described as KINASE PROTEOME ADENYLATE COMPLETE ATP-BINDING ATP-AMP TRANSPHOSPHORYLASE TRANSFERASE ","","","","","","","","","","","Wed Jan 8 13:42:19 2003","Wed Jan 8 13:42:19 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01881 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 123 to 158 (E-value = 2.2e-20) place AA01881 in the ADK_lid family which is described as Adenylate kinase, active site lid (PF05191)","","","","","Maskell,D.J., Szabo,M.J., Butler,P.D., Williams,A.E. and Moxon,E.R. Molecular analysis of a complex locus from Haemophilus influenzae involved in phase-variable lipopolysaccharide biosynthesis Mol. Microbiol. 5 (5), 1013-1022 (1991) PubMed: 1956282 Reinstein,J., Brune,M. and Wittinghofer,A. Mutations in the nucleotide binding loop of adenylate kinase of Escherichia coli Biochemistry 27 (13), 4712-4720 (1988) PubMed: 2844237 Brune,M., Schumann,R. and Wittinghofer,F. Cloning and sequencing of the adenylate kinase gene (adk) of Escherichia coli Nucleic Acids Res. 13 (19), 7139-7151 (1985) PubMed: 2997739 ","","Wed Jan 8 13:42:19 2003","1","","","" "AA01883","1271247","1269961","1287","ATGCCTCAAACTCCCCCTTCCTTAGTCCGACAAATTTTCAGCCGCAATATGCTGATTTGCGTATTTACCGGATTTAGTTCGGGTCTGCCCTTATTCGTTTTATTACAAATGTTGCCCATATGGCTGACGGACAAAGGGCTTTCTATTGAACTTATCGGTGCAGTGACCGGCGTCACTCTGCCCTACGGTTTAAAATTTTTATGGGCGCCCCTGCTGGATCGCTACTTTCCCAGTTTTCTCGGGCGACGACGCAGTTGGTTACTGATCACACAAGTTATTTTGCTTATTTTGCTTTATGCCATTAGCCAATTTGATCCGCGTACGCAGCTGAGCATTGTGGCAAATATCGCCTTCCTTATTGCTTTTTTTTCGGCGACGCAGGACATTGTGCTTGATGCTTACCGTCGTGAAATTTTAAGCGACAGCGAACTGGGGTTAGGCAACACCATTCACATAAATGCTTATCGTGTGGCGGGCTTGATTCCCGGCGGGCTTTCCCTTTATCTCGCCACCCTTTACCCCTGGGAAACGGTTTTTTTATGGACCGCACTTTGTATGCTGTTCGGCTTGTTTATGACCTTGTTTCTCGCCAAAGAACCACAAATTACCATCGTAAACCGCGATCAACCGGCTTATCTTGCCTTTTGGGTTCCGCTCCAAGAATTTTTCCAACGTAAAGGCGTTATACAGGCATTGGGCTTTTTGCTCTTTCTGTTTTTATATAAATTTGGGGATTCCTTCGCCACCACGCTACAAACCAAATTTATTTATGACATAGGATTCAGCAAAGAGGATATTGCCCTAGTTGTCAAAAGCACTTCCCTCTGGGCAAGTATTTCCGCTGGTCTCGCGGGTGGCGTGATTATGATTCGACTCGGCATTAATCGCGCCTTATGGGTCTTCGGTTTCGTACAATTAATCACCATCGGCGGATTCGTTTGGCTTGCCGCTTTTGGGCATTTTGCACAAATTACCTCCACCGAACTCTGGAAACTCGGCATTGTGATTGCTGCCGAATATATCGGCGTCGGCCTAGGCACCGCCGCTTTTGTGGCGTTTATGGCACGGGAAACTAACCCGCTTTACACCGCCACCCAACTCGCCTTATTTACCAGCCTGTCTGCATTGCCAAGCAAAGGGTTCGGAATACTCTCGGGCTATTTGGTCAAAGCCGTCGGTTATTATGACTTTTTCTGGATTTGTTTATTGCTCGCCGTACCGGGTATGCTTTGCCTGTTTTGGGTCGCCCCATGGAACGAAAAAACGGTAGCGGCAAAATCCGACAAT","","","47756","MPQTPPSLVRQIFSRNMLICVFTGFSSGLPLFVLLQMLPIWLTDKGLSIELIGAVTGVTLPYGLKFLWAPLLDRYFPSFLGRRRSWLLITQVILLILLYAISQFDPRTQLSIVANIAFLIAFFSATQDIVLDAYRREILSDSELGLGNTIHINAYRVAGLIPGGLSLYLATLYPWETVFLWTALCMLFGLFMTLFLAKEPQITIVNRDQPAYLAFWVPLQEFFQRKGVIQALGFLLFLFLYKFGDSFATTLQTKFIYDIGFSKEDIALVVKSTSLWASISAGLAGGVIMIRLGINRALWVFGFVQLITIGGFVWLAAFGHFAQITSTELWKLGIVIAAEYIGVGLGTAAFVAFMARETNPLYTATQLALFTSLSALPSKGFGILSGYLVKAVGYYDFFWICLLLAVPGMLCLFWVAPWNEKTVAAKSDN","1269960","","recycling protein; permease","Inner membrane, Cytoplasm","","
InterPro
IPR004752
Family
AmpG-related permease
TIGR00901\"[28-376]T2A0125: AmpG-related permease
InterPro
IPR011701
Family
Major facilitator superfamily MFS_1
PF07690\"[20-390]TMFS_1
noIPR
unintegrated
unintegrated
PTHR12778\"[7-429]TSOLUTE CARRIER FAMILY 33 (ACETYL-COA TRANSPORTER)-RELATED
PTHR12778:SF2\"[7-429]TACETYL-COA TRANSPORTER-RELATED
signalp\"[1-43]?signal-peptide
tmhmm\"[20-40]?\"[46-64]?\"[85-103]?\"[113-131]?\"[152-172]?\"[178-198]?\"[228-248]?\"[273-293]?\"[298-318]?\"[332-352]?\"[367-387]?\"[397-417]?transmembrane_regions


","BeTs to 11 clades of COG0477COG name: Permeases of the major facilitator superfamilyFunctional Class: G,E,P,RThe phylogenetic pattern of COG0477 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 344 to 414 match (1e-23) PD:PD333205 which is described as COMPLETE PROTEOME AMPG MEMBRANE TRANSMEMBRANE PROTEIN INNER TRANSDUCER SIGNAL BETA-LACTAMASE ","","","","","","","","","","","","Tue Feb 4 16:13:42 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01883 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Lindquist,S., Weston-Hafer,K., Schmidt,H., Pul,C., Korfmann,G., Erickson,J., Sanders,C., Martin,H.H. and Normark,S. AmpG, a signal transducer in chromosomal beta-lactamase induction Mol. Microbiol. 9 (4), 703-715 (1993) PubMed: 8231804Cheng Q, Park JT.Substrate specificity of the AmpG permease required for recycling of cell wall anhydro-muropeptides.J Bacteriol. 2002 Dec;184(23):6434-6.PMID: 12426329 Uehara T, Park JT.Role of the murein precursor UDP-N-acetylmuramyl-L-Ala-gamma-D-Glu-meso-diaminopimelic acid-D-Ala-D-Ala in repression ofbeta-lactamase induction in cell division mutants.J Bacteriol. 2002 Aug;184(15):4233-9.PMID: 12107141 ","","Tue Feb 4 16:13:10 2003","1","","","" "AA01885","1271595","1271257","339","ATGCACGAATTATCGTTGTGTCAAAACATCATTGAAATTGTTGAGCAACAATGCCAACAACACAACGTCAACAAAGTCACTGACCTCTGGCTTGAGGTCGGTGCCCTTTCCTGTATTGAACCTGGCGCCTTGGAATTTGGCTTTGAAATGGCATCCAAAGGCACGCCTGCCGAAAATTGCAAGCTCCACTTAATCCCGATTCCCGCCAAAGCCTGGTGTTGGGATTGCAAAACATTCGTTGAAATTCAAGCCAATAACAGCACTTGCCCGAATTGCGGCAGCGTGCATTTGCAACGCCAAAGTGGTGATGAATTACGAATTAAAGAAATTTCCGTTGAA","","","12621","MHELSLCQNIIEIVEQQCQQHNVNKVTDLWLEVGALSCIEPGALEFGFEMASKGTPAENCKLHLIPIPAKAWCWDCKTFVEIQANNSTCPNCGSVHLQRQSGDELRIKEISVE","1271256","[FUNCTION] Probably plays a role in an hydrogenase nickel cofactor insertion step. ","hydrogenase nickel incorporation protein","Cytoplasm","","
InterPro
IPR000688
Family
Hydrogenase expression/synthesis, HypA
PD003620\"[1-64]THYBF_SALTY_Q8XEP6;
PIRSF004761\"[1-113]T[NiFe]-hydrogenase maturation factor, HypA/HybF type
PF01155\"[1-113]THypA
TIGR00100\"[1-113]ThypA: hydrogenase nickel insertion protein


","BeTs to 9 clades of COG0375COG name: Zn finger protein HypA/HybF (possibly regulating hydrogenase expression)Functional Class: RThe phylogenetic pattern of COG0375 is a-m-k--q-d---ce-----u-----Number of proteins in this genome belonging to this COG is","Significant hit ( 2e-37) to 2/2 blocks of the IPB000688 family, which is described as \"Hydrogenase expression/synthesis, HypA family\". Interpro entry for IP:IPR000688. IPB000688A 25-71 8.9e-21 IPB000688B 72-112 2.1e-15","Residues 1 to 111 match (1e-10) PD:PD525173 which is described as HYPA2 ","","","","","","","","","","","Wed Jan 8 15:37:52 2003","Wed Jan 8 15:37:52 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01885 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 113 (E-value = 1.1e-50) place AA01885 in the HypA family which is described as Hydrogenase expression/synthesis hypA family (PF01155)","","","","","Lutz,S., Jacobi,A., Schlensog,V., Bohm,R., Sawers,G. and Bock,A.Molecular characterization of an operon (hyp) necessary for the activity of the three hydrogenase isoenzymes in Escherichia coli. Mol. Microbiol. 5 (1): 123-135 (1991) PubMed: 1849603.","","Fri Jan 31 15:52:49 2003","1","","","" "AA01886","1272617","1271604","1014","ATGACCATTTTAGTCACCGGCGGTGCCGGTTATATCGGTTCGCACACTGTCGTGGAATTATTAAATGCAGGCAAAGAGGTAGTGGTTTTAGACAATCTTTGCAACGCCTCACCAAAGTCCTTAGAACGCGTTGAACAAATCACCGGTAAGAAAGTGAAATTCTATCTGGGAGATGTATTGGATCGCACATTATTACAGCAAATCTTCGCCGAAAATAAGATTGACTCGGTGATTCACTTTGCCGGGTTAAAAGCCGTGGGAGAAAGCGTACAAAAACCGGCGGAATATTATTTGAATAACATCACCGGTTCCTTGGTATTGGTACAGGAAATGAAAAAAGCCGGTGTGTGGAATTTCGTATTCAGCTCCTCTGCTACGGTTTACGGCGATCCAAAAGTAATCCCGATTACCGAAGATTGCGAAGTAGGCGGCACCACCAATCCATACGGCACTTCCAAATACATGGTGGAACAAATCCTGCACGATATTGCCAAGGCAGAACCGAAATTCAGCATGACGATTTTACGCTACTTCAACCCGGTAGGTGCGCACGCCAGCAGTTTAATGGGGGAAGATCCGAACGGGATCCCGAACAATTTGTTACCTTACATCAGTCAAGTCGCCATCGGCAAGCTACCGCAGCTTTCCGTGTTCGGTAGCGACTATGATACGCACGACGGCACCGGGGTGCGCGATTATATCCACGTGGTGGATTTGGCTATCGGTCACGTTAAAGCCTTGGCACGCCATCAAGATGATGCCGGATTGCATATTTATAACTTGGGAACCGGTGTGGGCTATTCCGTGCTGGATATGGTGAAAGCCTTTGAGCAGGCAAATGACATTCGGATCCCATATAAATTGGTGGATCGCCGTCCCGGCGATATTGCCACTTGCTATTCCGATCCAAGCCTTGCTGCCAAAGAATTAAACTGGAAAGCGGAACGCGGCTTGGCAGAAATGATGAAAGACACGTGGAACTGGCAAAAAAATAACCCGAAAGGTTATCGGGAT","","","37142","MTILVTGGAGYIGSHTVVELLNAGKEVVVLDNLCNASPKSLERVEQITGKKVKFYLGDVLDRTLLQQIFAENKIDSVIHFAGLKAVGESVQKPAEYYLNNITGSLVLVQEMKKAGVWNFVFSSSATVYGDPKVIPITEDCEVGGTTNPYGTSKYMVEQILHDIAKAEPKFSMTILRYFNPVGAHASSLMGEDPNGIPNNLLPYISQVAIGKLPQLSVFGSDYDTHDGTGVRDYIHVVDLAIGHVKALARHQDDAGLHIYNLGTGVGYSVLDMVKAFEQANDIRIPYKLVDRRPGDIATCYSDPSLAAKELNWKAERGLAEMMKDTWNWQKNNPKGYRD","1271603","[CATALYTIC ACTIVITY] UDP-glucose = UDP-galactose.[COFACTOR] NAD.[PATHWAY] Galactose metabolism; third step.[SUBUNIT] Homodimer (By similarity).See Nakano et al., 1998.","UDP-glucose-4-epimerase","Cytoplasm","","
InterPro
IPR001509
Family
NAD-dependent epimerase/dehydratase
PF01370\"[3-262]TEpimerase
InterPro
IPR005886
Family
UDP-glucose 4-epimerase
PTHR10366:SF39\"[5-337]TUDP-GLUCOSE 4-EPIMERASE
TIGR01179\"[2-336]TgalE: UDP-glucose 4-epimerase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[2-203]Tno description
PTHR10366\"[5-337]TNAD DEPENDENT EPIMERASE/DEHYDRATASE


","BeTs to 14 clades of COG1087COG name: UDP-glucose 4-epimeraseFunctional Class: MThe phylogenetic pattern of COG1087 is --m---yq-d-lbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.9e-40) to 5/5 blocks of the IPB001509 family, which is described as \"NAD dependent epimerase/dehydratase family\". Interpro entry for IP:IPR001509. IPB001509A 3-24 2.9e-14 IPB001509B 75-109 3.6e-16 IPB001509C 197-203 11 IPB001509D 231-238 0.02 IPB001509E 303-313 0.36Significant hit ( 4.8e-08) to 3/4 blocks of the IPB002225 family, which is described as \"3-Beta hydroxysteroid dehydrogenase/isomerase family\". Interpro entry for IP:IPR002225. IPB002225A 0-30 3.2e-05 IPB002225B 123-177 73 IPB002225C 227-269 4.5","Residues 1 to 182 match (1e-07) PD:PD564644 which is described as UDP-GLUCOSE-4-EPIMERASE ","","","","","","","","","","","Tue Feb 11 15:04:46 2003","Wed Jan 8 15:41:46 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01886 is paralogously related to AA02647 (1e-18) and AA00539 (4e-11).","","","","","","Residues 3 to 333 (E-value = 2.8e-184) place AA01886 in the Epimerase family which is described as NAD dependent epimerase/dehydratase family (PF01370)","","","","Nakano,Y., Yoshida,Y., Yamashita,Y. and Koga,T.A gene cluster for 6-deoxy-L-talan synthesis in ActinobacillusactinomycetemcomitansBiochim. Biophys. Acta 1442 (2-3), 409-414 (1998)PubMed: 99023768","Bauer,A.J., Rayment,I., Frey,P.A. and Holden,H.M. The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determined at 2.5 A resolution Proteins 12 (4), 372-381 (1992) PubMed: 1579570 Thoden,J.B., Frey,P.A. and Holden,H.M. Crystal structures of the oxidized and reduced forms of UDP-galactose 4-epimerase isolated from Escherichia coliBiochemistry 35 (8), 2557-2566 (1996) PubMed: 8611559 Thoden,J.B., Frey,P.A. and Holden,H.M. High-resolution X-ray structure of UDP-galactose 4-epimerase complexed with UDP-phenol Protein Sci. 5 (11), 2149-2161 (1996) PubMed: 8931134 Thoden,J.B., Hegeman,A.D., Wesenberg,G., Chapeau,M.C., Frey,P.A. and Holden,H.M. Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli Biochemistry 36 (21), 6294-6304 (1997) PubMed: 9174344 Thoden,J.B., Gulick,A.M. and Holden,H.M. Molecular structures of the S124A, S124T, and S124V site-directed mutants of UDP-galactose 4-epimerase from Escherichia coli Biochemistry 36 (35), 10685-10695 (1997) Thoden,J.B. and Holden,H.M. Dramatic differences in the binding of UDP-galactose and UDP-glucose to UDP-galactose 4-epimerase from Escherichia coli Biochemistry 37 (33), 11469-11477 (1998) PubMed: 9708982 Boels IC, Ramos A, Kleerebezem M, de Vos WM. Functional analysis of the Lactococcus lactis galU and galE genes and their impact on sugar nucleotide and exopolysaccharide biosynthesis. Appl Environ Microbiol. 2001 Jul;67(7):3033-40. PMID: 11425718 Mollerach M, Garcia E. The galU gene of Streptococcus pneumoniae that codes for a UDP-glucose pyrophosphorylase is highly polymorphic and suitable for molecular typing and phylogenetic studies. Gene. 2000 Dec 30;260(1-2):77-86. PMID: 11137293 Nesper J, Lauriano CM, Klose KE, Kapfhammer D, Kraiss A,Reidl J. Characterization of Vibrio cholerae O1 El tor galU and galE mutants: influence on lipopolysaccharide structure, colonization, and biofilm formation. Infect Immun. 2001 Jan;69(1):435-45. PMID: 11119535 ","Tue Feb 11 15:04:46 2003","Tue Feb 11 15:04:46 2003","1","","","" "AA01887","1272811","1273194","384","ATGAATTGGTATTTACATGTATTAAAAAATTATGCCACCTTTAGTGGCAGAGCCAGACGTAAAGAATATTGGATGTTTGTGTTGTTCAATTTGATTGCTACTTTCGTATGTATGTTGATTGATGCCGTTATTCAAATGCCTATTTTTCAATTTGTTTACGGTGTTGGTGTTATTATCCCTTATATTGCGGTAACAGTGCGTCGCTTGCACGATACGGATCGTAGCGGATGGTGGATTTTAATTTCTTTTATTCCGCTTATTGGTTCTATCGTTCTGCTCGTCTTTATGTGTTTTGACAGCCAACCGGGTACAAATCGTTTTGGTGACAATCCTAAGGAAAGCACCGTTTCCAACGAGGTTTCAGAAAAAAGCCGTCTTATCAGT","","","14816","MNWYLHVLKNYATFSGRARRKEYWMFVLFNLIATFVCMLIDAVIQMPIFQFVYGVGVIIPYIAVTVRRLHDTDRSGWWILISFIPLIGSIVLLVFMCFDSQPGTNRFGDNPKESTVSNEVSEKSRLIS","1273193","","conserved hypothetical protein (possible cytochrome","Inner membrane, Cytoplasm","","
InterPro
IPR008523
Family
Protein of unknown function DUF805
PF05656\"[10-113]TDUF805
noIPR
unintegrated
unintegrated
signalp\"[1-45]?signal-peptide
tmhmm\"[24-44]?\"[48-66]?\"[76-98]?transmembrane_regions


","BeTs to 3 clades of COG3152COG name: Uncharacterized membrane proteinFunctional Class: SThe phylogenetic pattern of COG3152 is --------------efg----j----Number of proteins in this genome belonging to this COG is","","Residues 9 to 97 match (1e-18) PD:PD031314 which is described as COMPLETE PROTEOME MEMBRANE INNER TRANSMEMBRANE LAAM LIN0679 CC2178 PA0563 SMC01089 ","","","","","","","","","","","","Fri Jan 31 15:34:04 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01887 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 10 to 113 (E-value = 4.2e-50) place AA01887 in the DUF805 family which is described as Protein of unknown function (DUF805) (PF05656)","","","","","","","","1","","","" "AA01888","1273197","1273346","150","ATGCTAATAGGGTTAATCGAAAAGTTAGCCCTTTTATGTGGTAGTTTGCGCAAACGTTTACTTCTCCAATTTTTTCGGGAAAATGTCGCCCTTATTTTTTCTTCTATCATCAAAGGTAATTTTCAATGTCATCTTTTCAATCAGCTGCTT","","","5759","MLIGLIEKLALLCGSLRKRLLLQFFRENVALIFSSIIKGNFQCHLFNQLL","1273346","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-34]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 09:35:19 2004","Thu Feb 26 09:35:19 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01888 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:35:19 2004","","","","","","","","","","","","","1","","","" "AA01889","1273322","1274650","1329","ATGTCATCTTTTCAATCAGCTGCTTTAGAACAACGCTTTGAGTTGATTAAACGCGGTTCCACCGTGCGTAAAGAAATCATCGCCGGTTTAACCACGTTCTTGGCCATGGTGTATTCCGTTATCGTGGTGCCGAATATGTTAAGTACGGCGGGTTTCCCGGCGGAATCGGTTTTTATCGCCACCTGTTTGGTTGCCGGTCTCGGCTCCATTTTAATTGGCTTTTGGGCAAACGCGCCTATGGCGATCGGTTGTGCGATTTCCCTTACCGCATTTACCGCCTTCAGTTTGGTTATCGGGCAAAAAGTCAGCATTCCCGTGGCGTTAGGTGCGGTCTTCTTAATGGGCGTTTTCTTTACGTTGATTTCCGCCACCGGCATTCGTGCTTGGATTTTACGCAATTTGCCGGTAGGCATTGCCCACGGCGCCGGCATCGGTATCGGTTTGTTCCTGCTGTTAATCGCGGCGAATGGCGTCGGTTTAGTGGTCGGCAATCAAGCCGGCTTGCCGGTGAAACTCGGTGAATTTACCTCCTTTCCAGTGATGATGTCCTTAATCGGTTTGGCATTAATAGTGGGTTTGGAAAAAAAACAGGTGAAAGGCGGTATTTTATGGGTAATTATCGCCATTACCATCATCGGTTTAATTTTTGACCCGAACGTAACTTTCAACGGTCAAATGTTCAAAATGCCAAGTTTCGGCGATGAATCCCTGTTCTTGAAATTAGATGTGCTTGGTGCATTGCAACCGGCGATTTTACCGGTGGTGTTCGCCCTTGTGATGACGGCGGTATTCGATGCTACAGGCACCATTCGCGCTGTTGCCGGACAAGCGAATTTATTGGACAAAGACGGTCAAATCATCAATGGCGGTAAAGCCTTAACCTCCGATTCCGTGAGCAGTTTATTCTCTGGTATTTTCGGCACAGCGCCGGCAGCGGTTTACATTGAATCCGCCGCAGGCACCGCAGCGGGCGGCAAAACCGGTGTCACCGCTATTGTGGTCGGCGTGTTGTTCCTATTAATGCTGTTCTTCCAACCGCTTGCTTTCTTAGTGCCGAATTACGCCACTGCGCCGGCATTAATGTATGTGGGGTTATTAATGTTGAGCAACGTGAGCAAATTAGATTTTGACGATTTCGTCGGCGCCATGAGCGGCTTGATTTGTGCGGTATTCATCGTGTTAACCGCCAACATCGTTACTGGTATTATGCTCGGCTTCGCGGCATTGGTTATCGGACGTGTAGTGAGCGGTGATTTAAAACGCTTAAATATTGGCACGGTGGTGATTGCTACGGTCTTGGTGGCGTTTTACGCTTGCGGTTGGGCGATT","","","45874","MSSFQSAALEQRFELIKRGSTVRKEIIAGLTTFLAMVYSVIVVPNMLSTAGFPAESVFIATCLVAGLGSILIGFWANAPMAIGCAISLTAFTAFSLVIGQKVSIPVALGAVFLMGVFFTLISATGIRAWILRNLPVGIAHGAGIGIGLFLLLIAANGVGLVVGNQAGLPVKLGEFTSFPVMMSLIGLALIVGLEKKQVKGGILWVIIAITIIGLIFDPNVTFNGQMFKMPSFGDESLFLKLDVLGALQPAILPVVFALVMTAVFDATGTIRAVAGQANLLDKDGQIINGGKALTSDSVSSLFSGIFGTAPAAVYIESAAGTAAGGKTGVTAIVVGVLFLLMLFFQPLAFLVPNYATAPALMYVGLLMLSNVSKLDFDDFVGAMSGLICAVFIVLTANIVTGIMLGFAALVIGRVVSGDLKRLNIGTVVIATVLVAFYACGWAI","1274649","","conserved hypothetical protein (possible permease)","Inner membrane, Cytoplasm","","
InterPro
IPR006043
Family
Xanthine/uracil/vitamin C permease
PTHR11119\"[9-437]TXANTHINE-URACIL / VITAMIN C PERMEASE FAMILY MEMBER
PF00860\"[23-404]TXan_ur_permease
noIPR
unintegrated
unintegrated
PTHR11119:SF9\"[9-437]TXANTHINE-URACIL / VITAMIN C PERMEASE FAMILY MEMBER
tmhmm\"[26-46]?\"[56-76]?\"[85-105]?\"[111-131]?\"[136-156]?\"[175-193]?\"[202-222]?\"[244-264]?\"[324-344]?\"[350-368]?\"[389-411]?\"[421-441]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 4.2e-20) to 2/2 blocks of the IPB000444 family, which is described as \"Xanthine/uracil permeases family\". Interpro entry for IP:IPR000444. IPB000444A 295-324 2.1e-06 IPB000444B 379-422 3.9e-12","Residues 303 to 430 match (8e-33) PD:PD005952 which is described as PROTEOME COMPLETE XANTHINE/URACIL MEMBRANE FAMILY PLASMID PERMEASE TRANSPORTER TRANSMEMBRANE INTEGRAL ","","","","","","","","","","","","Wed Feb 5 15:11:39 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01889 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 128 to 415 (E-value = 9.7e-06) place AA01889 in the Sulfate_transp family which is described as Sulfate transporter family (PF00916)","","","","","","","","1","","","" "AA01890","1276027","1274684","1344","ATGTTATCCGCTATGCTTCTCGAACAATTCTCACAGCAGTTACAACGGCACGCACCAAATCAAACGCAATTTCTCATTGGATTTAGCGGTGGCTTGGACTCTACCGCCCTTCTCACCTTATTTGCCAAACACCGGGAAAATCGACCGCACTTTCAGTTGCGCGCTATTCACATTCACCATGGCTTAAGCCCTAATGCCGATGCCTGGACGGCACATTGCCAACAAATTTGCCGACAATTGAATATTCCGTTGCTGATTCAGCCGGTTAAAGTGCGTTTGCAAAACGGCATTGAAGCCGGTGCCCGTGAGGCACGTTATGAAGCCATCGCACAACATATTTTGCCCGAAGAATGGCTAGCCACGGCGCACCATCAGCAAGATCAAACGGAAACTTTTTTTCTTGCGCTCAAACGCGGTAGCGGTTTGCAGGGGTTAGGTGCAATGCAAGCTAACAGCATCGTTTACGGCGTACCGATTTTTCGCCCGCTATTGAATTTTAGCCGTCAGCAACTGATGGCATTCGTGCAACAGCAACAGCTGACTTGGGTTGAAGACGAAAGTAACGAAGACAATCAATACGACCGCAATTTTCTGCGCAATGTGGTGTTGCCTGAATTTCGCCAACGCTGGGCGCATTTTGATTCCGCGGTGCAACGTTCGGCACAACATTGTTATGAGCAACAACAACTGCTCAATGAACTGCTGGCGGAGGAATACCAAAAAAACGTCGTGGAAAATGACCGCACTTTCAAGGTGCACGACTTCGCCACCTATTCTCCGGCGAAACAACGGGCGTTGCTGCGTTTATGGTTGCAGGAACAGGGTGTGATGATGCCCTCATTGGCACAACTGGAGCAGCTCATTTCCGATGTCATTTTCGCCAAAAGCGATGCGCAGCCGCAGTTTCGTTTGGAGGATAAGATCCTTCGCCGTTATCAAAACCGATTGTTTCTCACGCCGGTATTTACGGATATTTCGCCAGTCTGTTTGGAAGCCCAATTTGACGATCCCATGAATTTGCTGGACAACTTGGGCACGTTAAGCCTGAAAAAAACACTGGAAAAAATGACCGCACTTTGGCGCGATGAAAATGGGCAGGAATATAAAGAAACCCTCGGTTTACCGTTAGCGGGAACGAAAGTTTGGATCCGTTTCGGTTATTCGGGCAAAGTTAAATTAACACAACAAGGCGTGAATCAGGACATAAAAAAAGTATGGCAAGGTTTGAACGTGCCACCTTGGCAGCGGCAACGGATTCCGCTGATTTTCTACGGCGATGCGCTACAAAGTGCGGTGGGTTTTTTCCGCGTTTTTCAACATGAATCCAAACAAAAAAGCGCATAT","","","51825","MLSAMLLEQFSQQLQRHAPNQTQFLIGFSGGLDSTALLTLFAKHRENRPHFQLRAIHIHHGLSPNADAWTAHCQQICRQLNIPLLIQPVKVRLQNGIEAGAREARYEAIAQHILPEEWLATAHHQQDQTETFFLALKRGSGLQGLGAMQANSIVYGVPIFRPLLNFSRQQLMAFVQQQQLTWVEDESNEDNQYDRNFLRNVVLPEFRQRWAHFDSAVQRSAQHCYEQQQLLNELLAEEYQKNVVENDRTFKVHDFATYSPAKQRALLRLWLQEQGVMMPSLAQLEQLISDVIFAKSDAQPQFRLEDKILRRYQNRLFLTPVFTDISPVCLEAQFDDPMNLLDNLGTLSLKKTLEKMTALWRDENGQEYKETLGLPLAGTKVWIRFGYSGKVKLTQQGVNQDIKKVWQGLNVPPWQRQRIPLIFYGDALQSAVGFFRVFQHESKQKSAY","1274683","","cell-cycle protein","Cytoplasm, Periplasm","","
InterPro
IPR011063
Domain
PP-loop
PF01171\"[23-201]TATP_bind_3
InterPro
IPR012094
Family
Cell cycle control PP-loop ATPase MesJ/YaeO
PIRSF006290\"[7-443]TCell cycle control PP-loop ATPase MesJ/YaeO
PTHR11807:SF2\"[31-434]TCELL CYCLE PROTEIN MESJ
InterPro
IPR012795
Domain
tRNA(Ile)-lysidine synthetase, N-terminal
TIGR02432\"[23-204]Tlysidine_TilS_N: tRNA(Ile)-lysidine synthet
InterPro
IPR012796
Domain
tRNA(Ile)-lysidine synthetase, C-terminal
TIGR02433\"[381-426]Tlysidine_TilS_C: tRNA(Ile)-lysidine synthet
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620\"[9-184]Tno description
InterPro
IPR015262
Domain
Protein of unkown function DUF1946, PP-loop ATpase
PF09179\"[235-439]TDUF1946
noIPR
unintegrated
unintegrated
G3DSA:2.60.280.10\"[330-435]Tno description
G3DSA:3.90.1040.10\"[236-321]Tno description
PTHR11807\"[31-434]TATPASES OF THE PP SUPERFAMILY-RELATED


","BeTs to 22 clades of COG0037COG name: Predicted ATPase of the PP-loop superfamily implicated in cell cycle controlFunctional Class: DThe phylogenetic pattern of COG0037 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.9e-05) to 3/6 blocks of the IPB000541 family, which is described as \"Uncharacterized protein family UPF0021\". Interpro entry for IP:IPR000541. IPB000541B 22-40 0.081 IPB000541C 50-91 0.81 IPB000541D 103-141 1.7e+02","Residues 24 to 91 match (4e-24) PD:PD034779 which is described as PROTEOME COMPLETE CELL CYCLE MESJ CHLOROPLAST VEG136 YDAO HOMOLOG YCF62 ","","","","","","","","","","","","Wed Jan 8 15:49:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01890 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 23 to 223 (E-value = 4e-92) place AA01890 in the ATP_bind_3 family which is described as PP-loop family (PF01171)","","","","","Pichoff,S., Alibaud,L., Guedant,A., Castanie,M.P. and Bouche,J.P. An Escherichia coli gene (yaeO) suppresses temperature-sensitive mutations in essential genes by modulating Rho-dependent transcription termination. Mol. Microbiol. 29 (3): 859-869 (1998) [PubMed: 9723924].","","Wed Jan 8 15:49:16 2003","1","","","" "AA01891","1276844","1276062","783","ATGCAATTACTCGGTATTGATGTTTGGGCATTAAATACCGTGCAATTTTCCAATCACACCCAATATGGCAAATGGACGGGCATTATCATTCCCAAAGAACAAATCGGCGAAATCGTGCGTGGCATTGAAGAGATTCAAGCGTTGCACAAATGTGATGCCGTGGTCTCCGGCTACTTAGGTTCCGCCGAGCAAATCGATGAAATCGTCAACGCCGTTCATAAAATCAAAGCCATCAATCCAAACGCCTTATATTTATGCGATCCTGTGATGGGCCATCCTGACAAAGGCTGTATCGTTGCCGATGGTGTGCGTGAAGGGTTGATTAATATTGTATCGGAAGCGGATATTATTACACCGAATCTGGTGGAACTGCGTGAATTAAGCGGTTTACCGGTAGAAAATTTTGAACAGGCATTGGCTGCCGTGAAAGCCATTTTGGCAAAAGGGCCGAAAAAAGTATTGGTGAAACATTTAAGCAAAGTGGGCAAAAACGCCAATCAATTTGAAATGTTGCTTGCTACCGAACAGGGCATTTGGCATTTATCCCGTCCATTACATCCGTTCGACCACGAACCCGTTGGCGTGGGTGATTTAACCGCCGGCTTATTCTTAGCCAATTTACTCAACGGCAAATCCGATGTGGAGGCTTTTGAACACATGGCAAACGCAGTCAACGATGTGATGCAAACCACCCTGGAACGTGGCGAATACGAATTACAAATCATCGCCGCCCGCGATCTTATCATCAACCCGCGCAGCCAATATAAAGCACAAAAAATCGCT","","","31184","MQLLGIDVWALNTVQFSNHTQYGKWTGIIIPKEQIGEIVRGIEEIQALHKCDAVVSGYLGSAEQIDEIVNAVHKIKAINPNALYLCDPVMGHPDKGCIVADGVREGLINIVSEADIITPNLVELRELSGLPVENFEQALAAVKAILAKGPKKVLVKHLSKVGKNANQFEMLLATEQGIWHLSRPLHPFDHEPVGVGDLTAGLFLANLLNGKSDVEAFEHMANAVNDVMQTTLERGEYELQIIAARDLIINPRSQYKAQKIA","1276061","[FUNCTION] Phosphorylate B6 vitamers; functions in a salvage pathway. Uses pyridoxamine, but not pyridoxal and pyridoxine as a substrate (by similarity). [CATALYTIC ACTIVITY] ATP + pyridoxal = ADP + pyridoxal 5'-phosphate.","pyridoxine kinase","Cytoplasm","","
InterPro
IPR004625
Family
Pyridoxal kinase
TIGR00687\"[1-261]Tpyridox_kin: pyridoxal kinase
InterPro
IPR011611
Domain
PfkB
PF00294\"[109-157]TPfkB
noIPR
unintegrated
unintegrated
G3DSA:3.40.1190.20\"[1-259]Tno description
PTHR10534\"[1-260]TPYRIDOXINE KINASE


","No hits to the COGs database.","","Residues 68 to 205 match (2e-07) PD:PD022379 which is described as KINASE TRANSFERASE PYRIDOXINE PYRIDOXAL COMPLETE PROTEOME B6 PYRIDOXAMINE VITAMIN SPF1-VMA3 ","","","","","","","","","","","Wed Jan 8 15:53:48 2003","Wed Jan 8 15:53:48 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01891 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Yang,Y., Tsui,H.C., Man,T.K. and Winkler,M.E. Identification and function of the pdxY gene, which encodes a novel pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate biosynthesis in Escherichia coli K-12. J. Bacteriol. 180 (7): 1814-1821 (1998) [PubMed: 9537380].","","Wed Jan 8 15:53:48 2003","1","","","" "AA01892","1276956","1276828","129","TTGCTGTATTTAAAAAGGATTTTAAAAGGAGAAAATAACAATGAAAAATGTACTTTCAATTCAGTCTCATGTAGTTTATGGCTACGCCGGCAACAAGTCGGCAACCTTCCCGATGCAATTACTCGGTAT","","","5038","LLYLKRILKGENNNEKCTFNSVSCSLWLRRQQVGNLPDAITRY","1276828","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 09:33:50 2004","Thu Feb 26 09:33:50 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01892 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:33:50 2004","","","","","","","","","","","","","1","","","" "AA01893","1277932","1276982","951","ATGAGTCAAGAATACTTAGATTTTGAATTACCTATTGCCGAACTTGAAGCGAAAATCGAATCATTACGCTCCGTCTTGGATCAGGATAACGACATTAATCTTGATGATGAAATTGCCCGTTTACAGAAAAAAAGCATGGAACTCACCGAAAAAACCTTTGCAAATTTAGATGCGTGGCAAGTGTCCAAAATGTCCCGTCACCCGAATCGTCCTTACACTCTTGACTATATCGAACATATTTTCACCGATTTTGACGAACTTGCCGGCGATCGTGCTTTTGCCGATGATAAAGCCATTATCGGTGGTTTAGCCCGTTTAGACGGCAGACCGGTGATGGTTATCGGTCACCAAAAAGGTCGCACGGTAAAAGAAAAAGTAAAACGCAACTTCGGTATGCCGGCACCGGAAGGCTATCGCAAAGCATTACGCCTCATGCAAATGGCGGAACGTTTCAAACTTCCAATCATTACTTTCATCGACACCCCAGGGGCTTATCCTGGCGTAGGTGCGGAAGAACGCGGACAATCGGAAGCTATCGCCCGCAACTTACGTGAAATGTCCACCTTAAAAGTACCTGTCATTTGTACCGTTATCGGTGAAGGCGGTTCTGGCGGCGCGTTGGCCATCGGTGTCGGTGATAAAGTGAATATGCTGCAATATTCCACCTATTCCGTTATTTCGCCGGAAGGTTGCGCTTCTATCTTATGGAAAAGCGCCGACAAAGCCTCTACCGCATCGGAAGTCATGGGCTTAACCGCAAAGCGTTTAAAAGAACTCGGTTTGATTGACAACATCGTATCTGAGCCGCTTGGTGGCGCCCATCGTAATTATGAAAAAATAGCGCAAAACCTGAAAAAACGGCTCTTGTCCGACTTAGCGGATTTAGACGTATTAGATGCAGAACAGTTATTGGAGCGTCGTTATCAGCGCTTAATGAGTTACGGCTATGTT","","","36668","MSQEYLDFELPIAELEAKIESLRSVLDQDNDINLDDEIARLQKKSMELTEKTFANLDAWQVSKMSRHPNRPYTLDYIEHIFTDFDELAGDRAFADDKAIIGGLARLDGRPVMVIGHQKGRTVKEKVKRNFGMPAPEGYRKALRLMQMAERFKLPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKASTASEVMGLTAKRLKELGLIDNIVSEPLGGAHRNYEKIAQNLKKRLLSDLADLDVLDAEQLLERRYQRLMSYGYV","1276981","[FUNCTION] This protein is a component of the acetyl coenzyme a carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. [CATALYTIC ACTIVITY] Carboxybiotin carboxyl carrier protein + acetyl-CoA = biotin carboxyl carrier protein + malonyl-CoA.[PATHWAY] Long-chain fatty acid biosynthesis; first step.[SUBUNIT] Aetyl-coa carboxylase is an heterohexamer of biotin carboxyl carrier protein, biotin carboxylase and the two subunits of carboxyl transferase in a 2:2 complex. ","acetyl-coenzyme-A carboxylase subunit A","Cytoplasm","","
InterPro
IPR001095
Family
Acetyl-CoA carboxylase, alpha subunit
PR01069\"[89-100]T\"[114-132]T\"[135-151]T\"[154-167]T\"[170-183]T\"[198-207]TACCCTRFRASEA
PTHR22855:SF3\"[54-315]TACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE ALPHA
PF03255\"[4-149]TACCA
TIGR00513\"[1-317]TaccA: acetyl-CoA carboxylase, carboxyl tran
InterPro
IPR011763
Domain
Acetyl-coenzyme A carboxyltransferase, C-terminal
PS50989\"[1-304]TCOA_CT_CTER
noIPR
unintegrated
unintegrated
G3DSA:3.90.226.10\"[74-266]Tno description
PTHR22855\"[54-315]TACETYL, PROPIONYL, PYRUVATE, AND GLUTACONYL CARBOXYLASE-RELATED


","BeTs to 19 clades of COG0825COG name: Acetyl-CoA carboxylase alpha subunitFunctional Class: IThe phylogenetic pattern of COG0825 is ao--k-yqvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 6.4e-68) to 6/6 blocks of the PR01069 family, which is described as \"Acetyl-CoA carboxylase carboxyl transferase alpha subunit signature\". Prints database entry for PR:PR01069. PR01069A 89-100 2.6e-06 PR01069B 114-132 4.2e-13 PR01069C 135-151 2.9e-13 PR01069D 154-167 6.7e-12 PR01069E 170-183 4.5e-10 PR01069F 198-207 1e-05","Residues 6 to 59 match (2e-18) PD:PD337833 which is described as TRANSFERASE ALPHA SUBUNIT CARBOXYL PROTEOME COMPLETE LIGASE CARBOXYLASE ACETYL-COENZYME A ","","","","","","","","","","","Wed Jan 8 15:58:02 2003","Wed Jan 8 15:58:02 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01893 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 149 (E-value = 1e-98) place AA01893 in the ACCA family which is described as Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit (PF03255)","","","","","Best EA, Knauf VC. Organization and nucleotide sequences of the genes encoding the biotin carboxyl carrier protein and biotin carboxylase protein of Pseudomonas aeruginosa acetyl coenzyme A carboxylase. J Bacteriol. 1993 Nov;175(21):6881-9. PMID: 7693652 Li SJ, Cronan JE Jr. Growth rate regulation of Escherichia coli acetyl coenzyme A carboxylase, which catalyzes the first committed step of lipid biosynthesis. J Bacteriol. 1993 Jan;175(2):332-40. PMID: 7678242Kikuchi,Y., Kojima,H., Tanaka,T., Takatsuka,Y. and Kamio,Y. Characterization of a second lysine decarboxylase isolated from Escherichia coli. J. Bacteriol. 179 (14): 4486-4492 (1997) [PubMed: 9226257].","","Wed Jan 8 15:58:02 2003","1","","","" "AA01894","1279107","1279517","411","ATGAATTTAAAGAGTAAAGTAGCTGGGCTAGCAATGATGTTTGTTGTATCAAGTAGTTTTGCTACAACATACCAGTTGAGTACGCATATTTTAGACATTAATAAAGGAGTGCCTGCACCGAATGTTGGAATTGAGTTGTATAAATTCAATGAAAAAACTGAGGATTGGGTGCAGGTGGCAAAAACTGTCACAGATGGAAATGGTAGAGTTAAAGGATTATTGCCGCTTCAGGACGGAAAAGATAATAAAGGTATCTATAAACTAAAGTTTCAGGTAAAGCAATATCTCGAACAATTATATACGAAGAGTTTTTACCCATTTATTGAAGTACCTTTCGAATTAAAGGATAATGCGCATTATCATGTGCCGATTACACTGTCTCCTTATGGTTACTCTACATATAGAGGTAGC","","","15505","MNLKSKVAGLAMMFVVSSSFATTYQLSTHILDINKGVPAPNVGIELYKFNEKTEDWVQVAKTVTDGNGRVKGLLPLQDGKDNKGIYKLKFQVKQYLEQLYTKSFYPFIEVPFELKDNAHYHVPITLSPYGYSTYRGS","1279517","","conserved hypothetical protein (possible transthyretin-like periplasmic protein)","Periplasm","This sequence is similar to gi|15792064, a predicted transthyretin-like periplasmic protein from Campylobacter jejuni.","
InterPro
IPR000895
Family
Transthyretin
PD003457\"[84-137]TQ9PPJ2_CAMJE_Q9PPJ2;
PR00189\"[25-45]T\"[115-137]TTRNSTHYRETIN
G3DSA:2.60.40.180\"[24-133]Tno description
PF00576\"[24-136]TTransthyretin
SM00095\"[21-136]TTR_THY
PS00768\"[29-44]TTRANSTHYRETIN_1
PS00769\"[120-132]TTRANSTHYRETIN_2
noIPR
unintegrated
unintegrated
PTHR10395\"[21-137]TURICASE AND TRANSTHYRETIN-RELATED
signalp\"[1-21]?signal-peptide
tmhmm\"[7-27]?transmembrane_regions


","BeTs to 5 clades of COG2351COG name: Transthyretin-like proteinFunctional Class: RThe phylogenetic pattern of COG2351 is ---------d--b-ef----uj----Number of proteins in this genome belonging to this COG is","Significant hit ( 6e-12) to 2/3 blocks of the IPB000895 family, which is described as \"Transthyretin precursor\". Interpro entry for IP:IPR000895. IPB000895B 22-61 6.9e-06 IPB000895C 70-121 0.0002","Residues 25 to 137 match (3e-16) PD:PD231643 which is described as COMPLETE PROTEOME TRANSTHYRETIN-LIKE PLASMID MLR5133 5 BMEI1429 CLONE:MCK7 P1 DR1161 ","","","","","","","","","","","","Thu Feb 26 09:31:41 2004","Thu Feb 26 09:31:41 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01894 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:31:41 2004","","","","","Residues 24 to 136 (E-value = 1.2e-46) place AA01894 in the Transthyretin family which is described as Transthyretin precursor (formerly prealbumin) (PF00576)","","","","","","","","1","","","" "AA01895","1279714","1280661","948","ATGAAATCACGTGACATTATGTATTTGTCAGGGCTTTTAGAAAATGATTGTAAGAATATTCCGACATTTTCTAGACCTCTAGATGAAAGTGAGCGTATTATCTATAAAGGTTTCTTTCCAAACCTTAACTTATCCACGGCTAAAGCTACTAGCATTAGTACTGAATGTTATAATTGTGTTGCTTGGACTCTGGGTATAACTGATGACTGGTTGTGGCCTGAATTTCACGCATATACGACGGATAAAGATACAACGCTTGAAGATTTTGATAAGTTTTACGAAAAAATGGGATTTGTTCGGGCAGCTAGCGACAAAGAAGCGCATATTACCGCCTGGGGAAATACTACACCTGAAGGTAAATTATATATGACACATGCTTCTGTAACTTATCCAGATTATCAAGGACAATGGGAATCAAAATTGGGTAAGTTTATTAGAATGAAGCATGATCCAAATGATTTACAAGGTAATAGTTACGGTAGGCGCGTTGCTTATTATAAGAAAAGCACTACTCAAGATTTATTACAAACAAGGCTACGCTTAATAAAAGAAAGACGTCCTGTTACCTATGACGAGGCTATAAAGCTTAATAGAAAGTTAGTAATGTTACCTAAGGCGCTTATTGATAGCTTTGATAATAAGTATGAGTTTTGGAAAGAAACTTGGGATGATTCGTCTGATGTATTGGCTACGTTCAGTTCAAATCCTACAACTTTTAAATTATCTAACGAATATCAAGAATTAGTTAAACTGGGTAAAAACAGTGATATCTTACCACTCATTGTTTTGAGGCTTCTGTTTTTTAAAAATGATTTCTTTGCGTTACAGCTTTATGATGAATTACAAGCAAATAAAAGTTTGGTTGTTGAATATGATGATAATTTTCACCTGTTAGAAGGGGAAAAAGGGCGAGCTCACTTGACAGTTAAAAAATATATCTCTTCGCTT","","","36839","MKSRDIMYLSGLLENDCKNIPTFSRPLDESERIIYKGFFPNLNLSTAKATSISTECYNCVAWTLGITDDWLWPEFHAYTTDKDTTLEDFDKFYEKMGFVRAASDKEAHITAWGNTTPEGKLYMTHASVTYPDYQGQWESKLGKFIRMKHDPNDLQGNSYGRRVAYYKKSTTQDLLQTRLRLIKERRPVTYDEAIKLNRKLVMLPKALIDSFDNKYEFWKETWDDSSDVLATFSSNPTTFKLSNEYQELVKLGKNSDILPLIVLRLLFFKNDFFALQLYDELQANKSLVVEYDDNFHLLEGEKGRAHLTVKKYISSL","1280660","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Jan 9 09:49:56 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01895 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01896","1281101","1281223","123","ATGAATAAAAATGATATTGTTTATTCTCTACCGTCATTTTTACCGTCACCAGAAGAAAATGCCATCAAGAACGTTCAGCAAGCCAAGTATCAATATCAGATTTTCTCCACGCTACACGGCCCA","","","4694","MNKNDIVYSLPSFLPSPEENAIKNVQQAKYQYQIFSTLHGP","1281223","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 09:29:24 2004","Thu Feb 26 09:28:00 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01896 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:28:00 2004","","","","","","","","","","","","","1","","","" "AA01897","1281344","1281168","177","ATGGAACAACAACCAGCGCTACTAAGTAAAGCAAAGGTGATTGAAGTCACCAGCTTGAGCGACACAACAATTTGGCGTATGATTAAACAAGGTAAATTCCCCAAAAGTGTTAAAGCGTCTATGGGCCGTGTAGCGTGGAGAAAATCTGATATTGATACTTGGCTTGCTGAACGTTCT","","","6719","MEQQPALLSKAKVIEVTSLSDTTIWRMIKQGKFPKSVKASMGRVAWRKSDIDTWLAERS","1281168","","conserved hypothetical protein","Cytoplasm, Periplasm","This sequence is similar to gi|17546616, a predicted hypothetical protein from Ralstonia solanacearum.","
InterPro
IPR010260
Family
Prophage CP4-57 regulatory
PF05930\"[5-55]TPhage_AlpA


","BeTs to 3 clades of COG3311COG name: Predicted transcriptional regulatorFunctional Class: KThe phylogenetic pattern of COG3311 is --------------e-g-s-------Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Thu Feb 26 09:10:09 2004","Thu Feb 26 09:12:23 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01897 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:12:23 2004","","","","","Residues 5 to 55 (E-value = 1.7e-13) place AA01897 in the Phage_AlpA family which is described as Prophage CP4-57 regulatory protein (AlpA) (PF05930)","","","","","","","","1","","","" "AA01899","1281704","1281393","312","ATGTTAAAATATTTTATATCTTGGTTATGTTCTTTTATCTATCCACTTAACGGTGTATATCTTGAGCTATGCACTAGCCTTTCTAGGCATGCAGAGGAATGGGATTTTGATGGTTATTACCTTCAGCATAAATCAAAAGAATTAACAATTCGTGGGTTCCAACATTTCTGCGAAATGGAAATATCAATTAAAAATGGTCCAAGCACAAAAATACCTCTTAAATACAAATGGCGATTGTATAAAGTGATAAATGATTTCATTGAGCAGAAATCAGGCGACAAGATCCGCGAAATATTAAATCGCGATATTGGT","","","12473","MLKYFISWLCSFIYPLNGVYLELCTSLSRHAEEWDFDGYYLQHKSKELTIRGFQHFCEMEISIKNGPSTKIPLKYKWRLYKVINDFIEQKSGDKIREILNRDIG","1281393","","conserved hypothetical protein","Cytoplasm, Periplasm","This sequence matches to gi|31544000, a predicted hypothetical protein from Bacteriophage Aaphi23.","
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 09:06:49 2004","Thu Feb 26 09:06:49 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01899 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:06:49 2004","","","","","","","","","","","","","1","","","" "AA01900","1282373","1282642","270","TTGCAAACTATCGCTTGGGCGTGCTTCGCATTCCGACGCAACAACAACCTGCTGCACGAGCTTTACAGCCCGCTTGCTGCCATCGGTTCAAAATTCGCCGTCGAAGCAAGAGATAATGCTGTTGAATATCGCAACACACTACGCCGCTTCAACGAAGTCGTGAAACGTATCACCGTCGACATTGAAGCAGATCCAGAAACAAACTGGCGAGTATTGAAGCATATCCGCAGCTTTAACGAAAAAATCTTCGGCAAAGTCGAAACCACCATC","","","10520","LQTIAWACFAFRRNNNLLHELYSPLAAIGSKFAVEARDNAVEYRNTLRRFNEVVKRITVDIEADPETNWRVLKHIRSFNEKIFGKVETTI","1282641","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Jan 9 09:50:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01900 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01901","1282733","1282930","198","ATGAAACAAATTATTACAACCGCACTTATCGCAATTATCACCGGCGTGATGATGTTATACGCCGTTGCATTAATCACTCTACCCGCTCACGCAGATAACACAACAGATTATTGCGATAACGGTATGAGTCAGCAAATCTCCACCGAATGGGAGGCTAAGGCCAAAGCCGAATGGATATTCCAGCGTTTCTTTATGGGT","","","7398","MKQIITTALIAIITGVMMLYAVALITLPAHADNTTDYCDNGMSQQISTEWEAKAKAEWIFQRFFMG","1282929","","hypothetical protein","Cytoplasm, Outer membrane","","
noIPR
unintegrated
unintegrated
signalp\"[1-31]?signal-peptide
tmhmm\"[9-29]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 5 14:59:02 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01901 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01902","1283676","1283137","540","ATGACTACATTAACTTTTCAAAGCACAACTCTTTCGGCTATTCATCAAAACAATCAAATTTGGCTAACGGTTACAGAGATTGGAAAAGCATTAGGCTATTCAGATCCTTTTAAGTCGGTCAAAAATATCTACGACCGCCACGCCGACGAATTCACCCCACAAATGACCGCACTTATTGATATGCGGACAAATGGCGGAATCCAAAAAGTGCGCATCTTCTCCTTGCGCGGCGCACACCTCATCGGCATGTTAAGCCACACCAAAGTAGCCAAAGACTTCCGCCGCTGGGTGCTGGATATTTTAGACCGCGAAGCCCAACAGCCGAAACAACTTGCCCTGCCGCAACCGGAGAAGACATATACCGTCCCACTAACGGAATACCGTAATTGCCATTTAAAAACGCGTGTTTTTCTTGTTCATTCAACATCTTATTGTCCTTTTTTGAGTAATAAAAAGGCCCTCACGTGGAGGGCTTGGGGTTGGTTAGGGTTGTTTATTTCTTTGGCTTGTATTTGTCTAGATAAGATACATCGGCGGGAG","","","20805","MTTLTFQSTTLSAIHQNNQIWLTVTEIGKALGYSDPFKSVKNIYDRHADEFTPQMTALIDMRTNGGIQKVRIFSLRGAHLIGMLSHTKVAKDFRRWVLDILDREAQQPKQLALPQPEKTYTVPLTEYRNCHLKTRVFLVHSTSYCPFLSNKKALTWRAWGWLGLFISLACICLDKIHRRE","1283136","","conserved hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
tmhmm\"[153-173]?transmembrane_regions


","No hits to the COGs database.","","Residues 2 to 103 match (2e-20) PD:PD339680 which is described as PROTEOME COMPLETE PHAGE-RELATED PHAGE P43 ","","","","","","","","","","","","Thu Jan 9 09:52:18 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01902 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01903","1284275","1284123","153","GTGGCAAAAGTTGCAATTTTGGCTATTCCTGTTATTCTTTATGGCAAAGATCCAATCCTCATAAAATTGCTAAACAGCATTCTGCTTTGCTTGGGGATTTATGGTGGTCTGTTCGCAGGTCGCAAATTCAGAAAAATGAAAGAGGAGGTGCAA","","","5610","VAKVAILAIPVILYGKDPILIKLLNSILLCLGIYGGLFAGRKFRKMKEEVQ","1284123","","hypothetical protein","Cytoplasm, Periplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-39]?signal-peptide
tmhmm\"[19-39]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 09:04:47 2004","Thu Feb 26 09:04:47 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01903 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:04:47 2004","","","","","","","","","","","","","1","","","" "AA01904","1284588","1285109","522","ATGGAAGAGTACGCCAAGTTGCTTAACGCCATACTTACCAAGGTAGTTTTTAATCGCATGACCATGTTCTTCGTTTTCTTGTTTGTTGGCTTTACGTTCATTCCTACCGAATTAACGTTGTATCTCAACGCCAAAACCCCGGCATTCTTTCCTGATTGGTTTACGCTTGCCAATTTCGGATCGTTAGTTTTCGGCTTTGTTGCAACTATGATTTGGATTCTTGGCAGTAATGCGGTTAAATCGCTCATCAACAAAATCCGATGCTTAATTAAGACAAATTCCGAGCAAGCAAAATTGCTTGAGTTGTTACCTACTCTTTCCGGCACAGAAAAAGAAATGCTTGCACTTTCTTGCTTAGGTGAACAAATTTGGCGAGACGATTTCAAAACCAAAATTGCCATTGAAAAACTGCTAGAGCTAAAGCTCATTTCCTATGGTTGGGTATCTAATCGATATGAAGTTAATCCGCTTATTCGTCCAAGTTTAATTTCTGAACTGGATAAGCTAGCCAATACCCATCAA","","","19923","MEEYAKLLNAILTKVVFNRMTMFFVFLFVGFTFIPTELTLYLNAKTPAFFPDWFTLANFGSLVFGFVATMIWILGSNAVKSLINKIRCLIKTNSEQAKLLELLPTLSGTEKEMLALSCLGEQIWRDDFKTKIAIEKLLELKLISYGWVSNRYEVNPLIRPSLISELDKLANTHQ","1285108","","hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-32]?signal-peptide
tmhmm\"[15-35]?\"[54-74]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Jan 9 09:53:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01904 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01905","1286351","1285446","906","ATGGAAAATAGTAATTTACCTACGGGGCCTAGACAGGGTGTTCTTGATATTTCTATCGATAAAGAAGCAGAAATAAATGGAATTGGCATGGGGGTATTAGGAAATGGCATTCCTTACTTGACACAAACAGGATTAGCTAAAGTATGTGATATTTCTCGTATTACATTACAAGAATTATCTTCAGAGTGGACTTCTTCCATACAAAGTGGCCTATTTACCACAAATAGAATGACTTTTTTAAGTTCGTACCTGTTTAATCGCGGGTTTAGCGATGAATCATTATATATTCAAGTAGAGAAAAATGGGGCGATACATTATGCATATCCTGATATTGTTTGTATGGCGATATTGGAGTTTTATGCATTTGAATCGTCAAAGTCAGACAAAACTGTAGCGCAGCGCTCATATAGAGAGCTAGCTTCACTTGGCTTAAAAGAGTACATTTATCGGTCCACCGGATATAAACCAGATGATCCTTGGCGACATTATCATAATAGAGTTTCTTTATTAAAAAATATGGGAACTGTGCCAGATGGATGCTTCATCGTTTTTAATGAGATTGCAGGGATGATGGTCGATCTCATTAATGCGGGACTCGTTGTAAATCAACATACAGTTCCAGATATTAGTGTAGGATTAGGATGGGCTAAGTACTGGAAAGAAAATAAACTCGCTAACCAATATGGCGACCTAAAAAAATGTTCACATTTTTATCCTGAAGAATTTTTGCAATCAGGTTCAAATCCACAACAAATTAATGCATATCCTGACTCTAGCTTAGGTGAATTTAGGAAATGGTTTAAAAATATCTACTTAAAAGAGAAGTTTCCTAGTTATATTCTAAAGAAAACAATGTTATTACCTCGCGGAAAGGAAACTGCCACTAAACTAATTGAGGTGCTTCAA","","","34753","MENSNLPTGPRQGVLDISIDKEAEINGIGMGVLGNGIPYLTQTGLAKVCDISRITLQELSSEWTSSIQSGLFTTNRMTFLSSYLFNRGFSDESLYIQVEKNGAIHYAYPDIVCMAILEFYAFESSKSDKTVAQRSYRELASLGLKEYIYRSTGYKPDDPWRHYHNRVSLLKNMGTVPDGCFIVFNEIAGMMVDLINAGLVVNQHTVPDISVGLGWAKYWKENKLANQYGDLKKCSHFYPEEFLQSGSNPQQINAYPDSSLGEFRKWFKNIYLKEKFPSYILKKTMLLPRGKETATKLIEVLQ","1285445","","hypothetical protein","Outer membrane, Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Jan 9 09:55:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01905 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01906","1287107","1286445","663","ATGATCAGCGAAGAAAAAATTAAACAAGACTTTGCCGAGCGACTTGATATAGCTTGCAAAAGAAAGAATTTGCCGGAAAAAGGCAGAGGTAAGATCATTGCCGACATATTGAAGATAACACCCAAAGCGGTCAGTAAATGGTTTAATGCAGAAACCTTGCCAACACCGGCGAATATTTATGTTTTGTCTGACTTCTTAGGGATTACAAAAGAGTGGTTGAGTTATGGTGACAAAAACGCCTCAATAGAACAGATTGAGAAGCAAATAGCTTACCCGCTATTAAGCCCGATTCAGGCAGGATTATGGACTGGCATTAGCTCACTTGAGGGGTTCGACGGTTATGAGATGATCCCAAGCACCGTTGTGGCCTCCGAAGATTCGTTTTATCTGCGAATTAACGGGGATTCAATGAAACCAAGGTTTAATCACGGCGATTTAGTATTGATAGATCCGAATATAACCCCAACACCGGGGAAGTTCGTCGCGGCAATAAACGGCAATGATGAAGCTACATTTAAACAGTACAAAGAACTTGGCGTAATCGCGGAAAATGGAATGCCTCACTTTGAATTAGTTCCGTTGAATCCGATGTACCCTACATTAAGCTCCCTTAATCAAGAGATCCGAATCATAGGCGTGGCGAGGGAGAGGATTGAAGCATTA","","","24641","MISEEKIKQDFAERLDIACKRKNLPEKGRGKIIADILKITPKAVSKWFNAETLPTPANIYVLSDFLGITKEWLSYGDKNASIEQIEKQIAYPLLSPIQAGLWTGISSLEGFDGYEMIPSTVVASEDSFYLRINGDSMKPRFNHGDLVLIDPNITPTPGKFVAAINGNDEATFKQYKELGVIAENGMPHFELVPLNPMYPTLSSLNQEIRIIGVARERIEAL","1286444","[FUNCTION] This protein allows the phage to reside inactively in the chromosome of its host bacterium. This lysogenic state is maintained by binding of regulatory protein c2 to the or and ol operators, preventing transcription of proteins necessary for lytic development. [MISCELLANEOUS] Bacteriophages P22 and P21 are closely related lambdoid phages; however, their host ranges differ. E.coli is the host of bacteriophage P21 and Salmonella is the host of bacteriophage P22.[SIMILARITY] Belongs to the lambdoid repressor CI/C2 family. ","repressor protein CI","Cytoplasm","","
InterPro
IPR001387
Domain
Helix-turn-helix type 3
PF01381\"[33-73]THTH_3
SM00530\"[14-73]THTH_XRE
InterPro
IPR006198
Domain
Peptidase S24, S26A and S26B
PF00717\"[131-192]TPeptidase_S24
InterPro
IPR011056
Domain
Peptidase S24 and S26, C-terminal region
G3DSA:2.10.109.10\"[123-214]Tno description
noIPR
unintegrated
unintegrated
G3DSA:1.10.260.40\"[6-85]Tno description


","BeTs to 3 clades of COG2932COG name: Predicted transcriptional regulatorFunctional Class: KThe phylogenetic pattern of COG2932 is -----------l--ef-hsn-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 8.8e-05) to 2/3 blocks of the PR00726 family, which is described as \"Repressor LexA serine protease (S24) family signature\". Prints database entry for PR:PR00726. PR00726A 128-138 0.0016 PR00726C 167-179 32","Residues 123 to 212 match (4e-09) PD:PD001529 which is described as REPRESSOR COMPLETE PROTEOME DNA LEXA HYDROLASE SOS TRANSCRIPTION REGULATION CLEAVAGE ","","","","","","","","","","","Thu Jan 9 10:00:09 2003","Thu Jan 9 10:00:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01906 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 90 to 195 (E-value = 2.1e-11) place AA01906 in the Peptidase_S24 family which is described as Peptidase family S24 (PF00717)","","","","","Sauer,R.T., Pan,J., Hopper,P., Hehir,K., Brown,J. and Poteete,A.R.Primary structure of the phage P22 repressor and its gene c2 . Biochemistry 20 (12): 3591-3598 (1981) [PubMed: 7260059]. Poteete,A.R., Ptashne,M., Ballivet,M. and Eisen,H. Operator sequences of bacteriophages P22 and 21 . J. Mol. Biol. 137 (1): 81-91 (1980) [PubMed: 6445008]. Sevilla-Sierra,P., Otting,G. and Wuthrich,K. Determination of the nuclear magnetic resonance structure of the DNA-binding domain of the P22 c2 repressor (1 to 76) in solutionand comparison with the DNA-binding domain of the 434 repressor. J. Mol. Biol. 235 (3): 1003-1020 (1994) [PubMed: 8289306].","","Thu Jan 9 10:00:09 2003","1","","","" "AA01908","1287208","1287444","237","ATGGAAAGTTTAAAAAACATTATTGACTCTTTGGGAGCGGCTAAAGTGGCGAATTTGTGCGGTATTTCCGTTCGTGCTGTTTATAAATGGCGCACATCAAATTCCTTGCCAAGAACTGAATATACAGGCGAGACAAAATATTCAGAAATTCTATCTCAAGCCTTAGAAAACACTGTTTCACCAGAAGAGATTAGAAACTTTAGCAACCCCATTAAGTCATGTTATGCGCTTAATGCG","","","8740","MESLKNIIDSLGAAKVANLCGISVRAVYKWRTSNSLPRTEYTGETKYSEILSQALENTVSPEEIRNFSNPIKSCYALNA","1287444","","conserved hypothetical protein","Periplasm, Cytoplasm","This sequence is similar to gi32030721, a predicted hypothetical protein from Haemophilus somnus 2336. Also see gi15801808 from Escherichia coli O157:H7 EDL933.","
noIPR
unintegrated
unintegrated
PD057771\"[2-64]TQ8X8R6_ECO57_Q8X8R6;


","No hits to the COGs database.","","Residues 2 to 64 match (2e-10) PD:PD057771 which is described as CRO REGULATORY PROTEOME COMPLETE BP-933W REGULATION DNA-BINDING BACTERIOPHAGE TRANSCRIPTION CP-933R ","","","","","","","","","","","","Thu Feb 26 09:03:24 2004","Thu Feb 26 09:03:24 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01908 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:02:50 2004","","","","","","","","","","","","","1","","","" "AA01909","1287474","1287806","333","ATGGCACGCAATGAATTAAGTAAAGACGCAATGAAAATTGCAGATTTGATTTACAAGAAAGCGTCTGAAAAGACGAACAAGGAGATAGCTGAAAAGATTGGGATTGACCCAAGCAACCTTGGCAGATTCCAAACTAACTATCTCGAAATGGTGTGCGCTTATCTCGATGAAATCGGGTTAAGCGTACACGTATATTCGGTGTTGATAGGTAAAATTGGCTTAGCGTTGTTTTATCAGTTTAACAAATCAAAATGCGAAAACTTTATTTCGCAAATTGCTCAATTCTCATTCGCAAATTGCTCGATTCGCAACAGTAAATGGATTCATTTTTCC","","","13734","MARNELSKDAMKIADLIYKKASEKTNKEIAEKIGIDPSNLGRFQTNYLEMVCAYLDEIGLSVHVYSVLIGKIGLALFYQFNKSKCENFISQIAQFSFANCSIRNSKWIHFS","1287805","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Jan 9 10:11:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01909 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01911","1287931","1288344","414","ATGGAAGTTACAGGGTTGAGTAAAAAGTCTGTGATCACCGCTTGCGAGAGCCTTGTTCAAATGGGTCTGCTTGAGCGTTCCGGTGGAGAAAGAAAATTAAATACTTACTCTGTTAAAGCCTTTGATTTTTCCGAATCTGGTGAAAAAAGTACACCAAATGAAACTGGTGAAAAAATTACACCAACTGGTGAAAATTTTTCCGAATCTGGTGAAAAAAGTACACCAGATCTGGTGAAAAAATTACACCCACAAAATAACAATAAAAACACTATACAAAATAACAATAAAAAAAATACCAAAAAAAGCGAACATGAAATTTTGGCAGATTTCGGGGTTGTTGGACAGCTTGCTGATGATTTCATCACTCACCGCAAATCATGCAAGGCACCAATCACAGAAACCGCAATGAATGGT","","","15074","MEVTGLSKKSVITACESLVQMGLLERSGGERKLNTYSVKAFDFSESGEKSTPNETGEKITPTGENFSESGEKSTPDLVKKLHPQNNNKNTIQNNNKKNTKKSEHEILADFGVVGQLADDFITHRKSCKAPITETAMNG","1288343","","hypothetical protein","Periplasm, Cytoplasm, Extracellular","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Jan 9 10:12:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01911 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01913","1290231","1288675","1557","ATGACCAACATCCATAACCATAAAATCCTCATCCTCGACTTCGGTTCCCAATATACCCAACTCATCGCCCGCCGTGTGCGTGAAATCGGGGTGTATTGTGAGCTTTGGGCGTGGGATGTGACCGAACAACAAATCCGTGATTTCAACCCAACGGGGATTATTCTTTCCGGTGGTCCGGAAAGCACCACGGAAGAAAACAGCCCGCGCGCACCGGAATATGTCTTTCATGCCGGCGTGCCGGTATTAGGCATTTGCTACGGTATGCAAACCATGGCAATGCAGCTTGGCGGCTTAACGGAAACCTCTGATCACCGCGAGTTCGGTTATGCCTCCGTTTTAATAGAAAATCCGACCGCACTTTTTGCCCATTTAAATGACGGCGACAGCAAATTAGATGTGTGGATGAGCCACGGCGATAAAGTTACCCGCCTGCCGAAGGACTTCCAAATCACCGGCACCACGCCGACCTGCCCGATTGCCGCCATGTCTGATGAAAATCGCCGTTTCTACGGCGTGCAATTCCACCCTGAAGTAACCCACACCAAAAAAGGCTTGGAATTATTAACCAATTTCGTAGTAAACATTTGCGGTTGCGAAACCAAATGGACGGCAGAAAACATCATTGAAGATGCCGTGGCGCGCATTAAAGCGCAAGTAGGTGATGACGAAGTGATTTTAGGCTTATCCGGCGGCGTGGATTCTTCCGTGGTGGCGCTGTTATTACATCGCGCTATCGGCAAAAACTTACATTGCGTGTTCGTGGATAACGGTTTATTGCGTTTAAACGAAGGCGTTCAGGTGATGGAAATGTTCGGCGATAAATTCGGTTTGAACATTACCCGTGTTGATGCAGAAAGCCGTTTCTTGAGCGAGTTGGCGGGCGTTTCCGACCCTGAGGCAAAACGTAAAATTATCGGCAAAGTGTTTGTGGATGTGTTCGACGACGAATCGAAAAAACTCACCAACGTAAAATGGCTCGCGCAAGGCACCATTTATCCTGACGTGATCGAATCCGCCGCCGGCAAAACCGGCAAAGCCCATGTGATCAAATCCCACCATAACGTAGGCGGCTTGCCGGATTACATGAAATTAGGCTTAGTTGAGCCGTTACGCGAACTATTCAAAGACGAAGTGCGCAAAATCGGCTTGGCATTAGGCTTACCGGCAGAAATGATCAACCGTCATCCGTTTCCCGGCCCGGGTTTAGGGGTGCGCGTACTCGGCGAAGTGAAAAAAGAATACTGCGATTTATTACGTCGCGCCGATGCAATTTTTATCGAAGAATTGCATAACAACGGTTGGTATGCGAAAACCAGCCAAGCCTTCAGCGTATTCCTGCCGGTGAAATCGGTAGGTGTGATGGGCGACGGGCGTAAATATGACTGGGTTATCTCCCTGCGCGCCGTAGAAACGATCGATTTTATGACCGCACATTGGGCACACCTGCCTTATGATTTGCTCGGCAGAATTTCCAATCGCATTATCAATGAAGTAAACGGCATTTCCCGTGTGGTATATGACATCAGCGGAAAACCACCAGCAACGATTGAGTGGGAA","","","57674","MTNIHNHKILILDFGSQYTQLIARRVREIGVYCELWAWDVTEQQIRDFNPTGIILSGGPESTTEENSPRAPEYVFHAGVPVLGICYGMQTMAMQLGGLTETSDHREFGYASVLIENPTALFAHLNDGDSKLDVWMSHGDKVTRLPKDFQITGTTPTCPIAAMSDENRRFYGVQFHPEVTHTKKGLELLTNFVVNICGCETKWTAENIIEDAVARIKAQVGDDEVILGLSGGVDSSVVALLLHRAIGKNLHCVFVDNGLLRLNEGVQVMEMFGDKFGLNITRVDAESRFLSELAGVSDPEAKRKIIGKVFVDVFDDESKKLTNVKWLAQGTIYPDVIESAAGKTGKAHVIKSHHNVGGLPDYMKLGLVEPLRELFKDEVRKIGLALGLPAEMINRHPFPGPGLGVRVLGEVKKEYCDLLRRADAIFIEELHNNGWYAKTSQAFSVFLPVKSVGVMGDGRKYDWVISLRAVETIDFMTAHWAHLPYDLLGRISNRIINEVNGISRVVYDISGKPPATIEWE","1288674","[CATALYTIC ACTIVITY] ATP + xanthosine 5'-phosphate + L-glutamine + H(2)O = AMP + diphosphate + GMP + L-glutamate.[PATHWAY] GMP biosynthesis.[SUBUNIT] Homodimer (By similarity).","GMP synthase","Cytoplasm","","
InterPro
IPR000991
Domain
Glutamine amidotransferase class-I
PF00117\"[10-195]TGATase
InterPro
IPR001317
Domain
Carbamoyl-phosphate synthase, GATase region
PR00099\"[9-23]T\"[50-64]T\"[80-96]TCPSGATASE
InterPro
IPR001674
Domain
GMP synthase, C-terminal
PF00958\"[426-518]TGMP_synt_C
TIGR00884\"[206-519]TguaA_Cterm: GMP synthase, C-terminal domain
InterPro
IPR004506
Family
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase
PF03054\"[222-244]TtRNA_Me_trans
InterPro
IPR004739
Domain
GMP synthase, N-terminal
TIGR00888\"[9-199]TguaA_Nterm: GMP synthase, N-terminal domain
InterPro
IPR006220
Domain
Anthranilate synthase component II/delta crystallin
PR00097\"[53-62]T\"[80-91]T\"[171-184]TANTSNTHASEII
InterPro
IPR011702
Domain
Glutamine amidotransferase superfamily
PR00096\"[53-62]T\"[80-91]T\"[171-184]TGATASE
InterPro
IPR012998
Active_site
Glutamine amidotransferase, class I, active site
PS00442\"[80-91]TGATASE_TYPE_I
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620\"[201-394]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.30.300.10\"[411-519]Tno description
G3DSA:3.40.50.880\"[3-200]Tno description
PTHR11922\"[8-519]TGMP SYNTHASE-RELATED
PTHR11922:SF2\"[8-519]TGMP SYNTHASE


","No hits to the COGs database.","Significant hit (5.6e-247) to 10/10 blocks of the IPB001674 family, which is described as \"GMP synthase C terminal domain\". Interpro entry for IP:IPR001674. IPB001674A 9-35 3.6e-26 IPB001674B 80-89 2.4e-07 IPB001674C 133-145 5.7e-10 IPB001674D 170-191 6.5e-15 IPB001674E 223-263 2.4e-33 IPB001674F 282-314 1.2e-21 IPB001674G 325-338 1.7e-11 IPB001674H 354-408 6.9e-46 IPB001674I 440-479 4.3e-33 IPB001674J 483-519 1.3e-32Significant hit ( 2.5e-13) to 2/2 blocks of the IPB000991 family, which is described as \"Glutamine amidotransferase class-I\". Interpro entry for IP:IPR000991. IPB000991A 80-89 3.6e-05 IPB000991B 169-179 2e-06Significant hit ( 1.8e-09) to 1/4 blocks of the IPB003694 family, which is described as \"NAD+ synthase\". Interpro entry for IP:IPR003694. IPB003694A 225-244 1.8e-09","Residues 53 to 112 match (9e-08) PD:PD349562 which is described as PROTEOME COMPLETE GLUTAMINE TRANSFERASE GMP AMIDOTRANSFERASE SYNTHASE SYNTHETASE LIGASE BIOSYNTHESIS ","","","","","","","","","","","Tue Dec 2 10:29:31 2003","Thu Jan 9 10:17:30 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01913 is paralogously related to AA01611 (3e-05) and AA02175 (6e-04).","","","","","","Residues 399 to 518 (E-value = 8.9e-71) place AA01913 in the GMP_synt_C family which is described as GMP synthase C terminal domain (PF00958)","","","","","Grimaldi C, Dutertre M, Simonet JM. Genetic organization and polymorphism of the guaA gene encoding the GMP synthetase in Lactobacillus rhamnosus. Curr Microbiol. 2000 Apr;40(4):245-9. PMID: 10688693 Tiedeman,A.A., Smith,J.M. and Zalkin,H. Nucleotide sequence of the guaA gene encoding GMP synthetase of Escherichia coli K12. J. Biol. Chem. 260 (15): 8676-8679 (1985) [PubMed: 3894345].Zalkin,H., Argos,P., Narayana,S.V., Tiedeman,A.A. and Smith,J.M. Identification of a trpG-related glutamine amide transfer domain in Escherichia coli GMP synthetase. J. Biol. Chem. 260 (6): 3350-3354 (1985) [PubMed: 2982857].Tesmer,J.J., Klem,T.J., Deras,M.L., Davisson,V.J. and Smith,J.L. The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. Nat. Struct. Biol. 3 (1): 74-86 (1996) [PubMed: 8548458].","","Thu Jan 9 10:17:30 2003","1","","","" "AA01914","1290529","1290266","264","ATGGATTACGTTTTATCAAAAGAATATAAACGGGACTTAAAAAAACTTCCGGTCGAAATTCAATCCGGTCCGGAATATGCAGAGGTTTTATATTGCCTGTTCAATCAAAAATCCCTACCCGAACGATATAAAGATCATGCTTTGCAAGGAAATTGGCAGGGATTTCGAGATTGCCACATCAAAAATGATCTCATTTTAATTTACAAAATAGAAGCAGACACCCTCTATTTTGCAAGGCTAAATTCTCACTCGGAAGTGTTTAAA","","","10499","MDYVLSKEYKRDLKKLPVEIQSGPEYAEVLYCLFNQKSLPERYKDHALQGNWQGFRDCHIKNDLILIYKIEADTLYFARLNSHSEVFK","1290265","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR004386
Family
Conserved hypothetical protein 53
TIGR00053\"[1-88]TTIGR00053: conserved hypothetical protein T
InterPro
IPR007712
Family
Plasmid stabilization system
PF05016\"[3-87]TPlasmid_stabil
InterPro
IPR012753
Family
Addiction module toxin, RelE/StbE
TIGR02385\"[4-87]TRelE_StbE: addiction module toxin, RelE/Stb


","BeTs to 5 clades of COG3041COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3041 is --------------e-ghs-u-----Number of proteins in this genome belonging to this COG is","","Residues 4 to 55 match (5e-07) PD:PD053185 which is described as ORF62 ","","","","","","","","","","","","Thu Jan 9 10:18:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01914 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 87 (E-value = 7.8e-33) place AA01914 in the DUF332 family which is described as Domain of unknown function (DUF332) (PF03890)","","","","","","","","1","","","" "AA01915","1290813","1290544","270","ATGTTAGATAGCGCAGTGAATTTCCGTACTCAAGCCGACATCAAAGAGCAAGCGTTTAACGTCATTAAAAGCTATGGCTTAACGCCCGCTCAGGTGTTAAATATGTTTTTGACCCAAATTGCCAAAACCAACACAATTCCGCTCAGTTTGGATTATCAGCCGAATACAAAAACAGCTAATGCAATCAATGAATTAATGAGCGGAAAAGGGGAAAGATTTAGCGTAGATTCCTTTGATGAATTTCAACAAAAAATTCGTGATTTAAGCAAA","","","10131","MLDSAVNFRTQADIKEQAFNVIKSYGLTPAQVLNMFLTQIAKTNTIPLSLDYQPNTKTANAINELMSGKGERFSVDSFDEFQQKIRDLSK","1290543","","possible negative regulator of translation","Periplasm","","
InterPro
IPR007337
Family
RelB antitoxin
PF04221\"[3-82]TRelB
TIGR02384\"[1-88]TRelB_DinJ: addiction module antitoxin, RelB


","No hits to the COGs database.","","Residues 1 to 66 match (4e-08) PD:PD220735 which is described as NEGATIVE TRANSLATION REGULATOR ","","","","","","","","","","","","Thu Jan 9 10:21:32 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01915 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 82 (E-value = 6e-17) place AA01915 in the RelB family which is described as RelB antitoxin (PF04221)","","","","","Morton,D.J., Whitby,P.W., Jin,H., Ren,Z. and Stull,T.L.Effect of multiple mutations in the hemoglobin- andhemoglobin-haptoglobin-binding proteins, HgpA, HgpB, and HgpC, ofHaemophilus influenzae type bInfect. Immun. 67 (6), 2729-2739 (1999)PubMed: 10338475","","Tue Feb 4 17:07:45 2003","1","","","" "AA01917","1291056","1290856","201","GTGCGGTGGTTTTTCCCGATGTTTTTCTACACTAAAAAAACACCCGTGAAATCCACCGCACTTTTGTTTGCCAAAACACCGCAATCGTTTACGTTATTCAAGGGAAGTGGTAGAATGCGCCACCGTTTTACAAGAGAGACAAAAAATCATAAGCAAGTGCGGTTAAAATTCGCGCTATTTTGTATTGCATTGCAATACGAT","","","10205","VRWFFPMFFYTKKTPVKSTALLFAKTPQSFTLFKGSGRMRHRFTRETKNHKQVRLKFALFCIALQYD","1290855","","hypothetical protein","Periplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-19]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Jan 9 10:25:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01917 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01918","1292420","1291071","1350","ATGGATTTAATTATCGGTTTAATCGCCATTGTCGCCGTCGCCTACTACATCGTAAAAGGCTATTCGGCGACAGGCGTATTAATGTTCGGCGGCTTGGCGCTGTTATTGATTTCCGTGTTATTGGGGCATTCCATTTTGCCGGAAAACGTCAAAAGCACCGGCTCCGCCTATTTTGATATTCTGGAATATGTGAAACATTTACTGTCAAATCGCGCCGGCGGCTTGGGTTTAATGATCATGATTTTATGCGGCTTCTCCGCCTACATGACCCATTTGGGCGCCAACGACGTGGTGGTCAAACTGGTTTCCAAACCCTTAAAAAATATTCGTTCGCCATATATTTTAATGGTGTTCGCCTATTTTCTAGCGTGCCTGATGTCCTTTGCGGTCGCCTCTGCCACAGGTTTAGGCGTATTGTTAATGGCGACCCTGTTCCCCGTCATGGTCAATGTCGGCATCTCTCGAGGTGCGGCGGCAGCCATTTGTGCCTCACCGATTTCCATTATTTTGTCACCGACCTCCGGTGATGTGGTGTTATCCGCCGAAATCTCCCAAATCCCATTAAGCGAATTTGCTTTCGGCACCAGCCTGCCGGTTTCCCTTTTCGCCATTTGCGGCATCGCCGTCGCCCATTTTTTCTGGCAACGTTATTTGGATCGCAAAGAAGGCATTAAAATCGAACGGGTTGACGCGTCCGAAATCAAAACCATCGCGCCGAATTTCTACGCGATTCTACCGCTTTTACCCATCATCGGCGTGTTACTTTTCGATGGTAAATTCGGGTTACCGAAACTGCACATCGTGACCATCATTATTCTGTGTTTTATCATTACCGCTGTGATTGATTTCGCCCGCAACTTCAGCGCGAAGAAAACCTTTGATAACTTGGTGGTCGCCTATCGCGGCATGGCGGACGCCTTTGCCGGCGTGGTGATGCTATTGGTCGCCGCAGGCGTATTCGCACAAAGTTTAAGCACTATTGGTTTTATCACCAATCTCATTGATTCCGCCCAATCTTTCGGTGGCAGCAGCTTAACTATGATGTTAGTACTCGCCGTCATCACCATTTTAGCCACCATGGCGACCGGCTCCAGCAACGCGGCATTCTACGCTTTCGCCGAACTGATCCCGAAACTGGCGGCGCAAATGGGCGCCAATCCGGCTTATTTAACTATTCCGATGTTACAAGCCTCCAACTTAGGTCGCGGCTTATCACCGGTGTCTGGCGTAGTGGTCGCGGTGTCCGGCATGGCGAAAATCTCTCCGTTTGAAATCGTAAAACGAATGTCCGTGCCGATGGCGGTGGGTTTCATTTGTGTGGTTATCGCCACAGAGTTATTCATTCCCGCC","","","47482","MDLIIGLIAIVAVAYYIVKGYSATGVLMFGGLALLLISVLLGHSILPENVKSTGSAYFDILEYVKHLLSNRAGGLGLMIMILCGFSAYMTHLGANDVVVKLVSKPLKNIRSPYILMVFAYFLACLMSFAVASATGLGVLLMATLFPVMVNVGISRGAAAAICASPISIILSPTSGDVVLSAEISQIPLSEFAFGTSLPVSLFAICGIAVAHFFWQRYLDRKEGIKIERVDASEIKTIAPNFYAILPLLPIIGVLLFDGKFGLPKLHIVTIIILCFIITAVIDFARNFSAKKTFDNLVVAYRGMADAFAGVVMLLVAAGVFAQSLSTIGFITNLIDSAQSFGGSSLTMMLVLAVITILATMATGSSNAAFYAFAELIPKLAAQMGANPAYLTIPMLQASNLGRGLSPVSGVVVAVSGMAKISPFEIVKRMSVPMAVGFICVVIATELFIPA","1291070","[FUNCTION] Responsible for the transport of c4-dicarboxylates during anaerobic growth.[SUBCELLULAR LOCATION] Integral membrane protein. inner membrane (potential). [SIMILARITY] Belongs to the dcuC / dcuD (tc 2.a.61) family of transporters. ","anaerobic C4-dicarboxylate transporter","Inner membrane, Cytoplasm","","
InterPro
IPR004669
Family
C4-dicarboxylate anaerobic carrier
PF03606\"[1-449]TDcuC
TIGR00771\"[54-438]TDcuC: transporter, anaerobic C4-dicarboxyla
noIPR
unintegrated
unintegrated
signalp\"[1-42]?signal-peptide
tmhmm\"[2-21]?\"[27-47]?\"[68-88]?\"[117-139]?\"[149-169]?\"[195-215]?\"[236-256]?\"[262-284]?\"[305-334]?\"[340-362]?\"[429-449]?transmembrane_regions


","No hits to the COGs database.","","Residues 214 to 291 match (7e-11) PD:PD457462 which is described as COMPLETE PROTEOME DCUC ANAEROBIC C4-DICARBOXYLATE TRANSPORTER TRANSMEMBRANE INNER MEMBRANE CARRIER ","","","","","","","","","","","Thu Jan 9 10:32:39 2003","Thu Jan 9 10:32:39 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01918 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 449 (E-value = 2.4e-174) place AA01918 in the DcuC family which is described as C4-dicarboxylate anaerobic carrier (PF03606)","","","","","Zientz,E., Six,S. and Unden,G. Identification of a third secondary carrier (DcuC) for anaerobic C4-dicarboxylate transport in Escherichia coli: roles of the threeDcu carriers in uptake and exchange. J. Bacteriol. 178 (24): 7241-7247 (1996) [PubMed: 8955408].Zientz,E., Janausch,I.G., Six,S. and Unden,G. Functioning of DcuC as the C4-dicarboxylate carrier during glucose fermentation by Escherichia coli. J. Bacteriol. 181 (12): 3716-3720 (1999) [PubMed: 10368146].Six,S., Andrews,S.C., Roberts,R.E., Unden,G. and Guest,J.R. Construction and properties of Escherichia coli mutants defective in two genes encoding homologous membrane proteins with putative roles in anaerobic C4-dicarboxylic acid transport Biochem. Soc. Trans. 21 (4), 342S (1993) PubMed: 8131924 ","","Thu Jan 9 10:32:39 2003","1","","","" "AA01919","1292859","1293311","453","TTGGCAACTTTGGAACAAAAATTACAGGATTTATTACAAGGCTCGGTGGAAGATTTCGGTTGTCAGCTTTGGGGCATTGAATGCCAGCGTGTCGGTCGTTATTTAACCGTGCGTTTGTTTATTGATAAAGAAGGCGGTGTGACGGTGGAAGATTGCGCCGATGTGAGCCGTCAGGTGAGTGCAGTGTTAGATGTGGAAGATCCTATTGCGGATAAATATAACCTTGAGGTTTCCTCACCGGGGTTGGATCGCCCGTTGTTTACCTTGGCGCAATATGCCCGTTATGTTGGGCAGGAAATCTTGGTGCATTTGCGCATTCCGGTGGCGGATCGTCGTAAATGGCAAGGGGAATTGGCGAAAATTGAAAATGATATGATTACGCTGATTGTGGATAAACAGGAACAGATTTTAGCGTTCGGTAATATTCAAAAAGCTAGCGTTGTCGCGAAATTT","","","17573","LATLEQKLQDLLQGSVEDFGCQLWGIECQRVGRYLTVRLFIDKEGGVTVEDCADVSRQVSAVLDVEDPIADKYNLEVSSPGLDRPLFTLAQYARYVGQEILVHLRIPVADRRKWQGELAKIENDMITLIVDKQEQILAFGNIQKASVVAKF","1293310","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003728
Family
Protein of unknown function DUF150
PF02576\"[11-147]TDUF150
noIPR
unintegrated
unintegrated
G3DSA:3.30.300.70\"[3-80]Tno description


","BeTs to 16 clades of COG0779COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG0779 is -------qvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 6.8e-34) to 1/1 blocks of the IPB003728 family, which is described as \"DUF150\". Interpro entry for IP:IPR003728. IPB003728 47-100 5.9e-34","Residues 112 to 151 match (6e-11) PD:PD200410 which is described as PROTEOME COMPLETE CYTOPLASMIC VC0641 YPO3498 YHBC STY3469 ORF PM0761 ","","","","","","","","","","","","Thu Jan 9 10:33:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01919 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 11 to 147 (E-value = 2.5e-63) place AA01919 in the DUF150 family which is described as Uncharacterised BCR, YhbC family COG0779 (PF02576)","","","","","","","","1","","","" "AA01920","1293338","1294831","1494","ATGAGTAAAGAAATTTTATTAGCGGCAGAAGCCGTATCCAATGAAAAATTATTGCCACGCGAGAAAATTTTTGAAGCGTTGGAAAGTGCAATCGCCCTCTCAACCAAGAAAAAATACGAATATGACGTAGATGTTCGCGTCGCCATTAATCCAAAAACCGGCGAATTCGACACCTTCCGTCGTTGGGTTGTGGTGGAAGAAGTGAATAATCCGACTAAAGAAATCACGTTGGAAGCAGCACGTTTTGAAGATCCTGACGCGCAAGTGGGTGATTATGTGGAAGATCAAATTGAGTCCATCGCCTTTGACCGTATTACTATGCAAACCGCCCGTCAGGTTATCAGTACCAAAATTCGTGAAGCGGAACGCAGCAAAATCGTTGATCAATTCCGCTCCAAAGAAGGTCAAATTATTACTGCTACCGTGAAGAAAAGTAACCGCGACAGCGTTATTTTAGATGTGAACGGTGAAGACGGTAACAAAGCGGAAGCAGTCATGTTACGCGAAGATATGTTACCGCGTGAGAATTTCCGTCCGGGCGACCGTGTGCGCGGTGTGTTATATAAAGTCAGTCCGGAAAATAAAGGCACTCAATTGTTCGTGAGCCGCGCCAAACCGGAAATGTTGATTGAATTATTCCGTTTGGAGGTGCCTGAAATCGGTGAAGAATTAATCGAAATCAGAAGTGCCGCCCGTGATCCGGGATCCCGTGCGAAAATTGCGGTGAAAAGCAATGATAAACGTATTGATCCGGTGGGCGCTTGCGTAGGTATGCGTGGTGCGCGCGTTCAGGCAATTACCAATGAATTGGGCGGTGAGCGCGTTGATATCGTACTTTGGGACGACAATCCGGCACAATTTGTGATTAACGCCATGGCGCCGGCAGATGTGAGTTCCATTGTGGTGGATGAAGATAAACATGCCATGGATATTGCCGTCGAAGAAGTAAATCTGGCGCAAGCCATCGGTCGTAACGGGCAAAACGTGCGTTTGGCGACCCAATTAACCGGTTGGGTGTTGAACGTGATGACCACACAGGAACTCAATGCGAAACACCAAGCGGAAGATGACAAAGTGTTGAACTTGTTCATTGATACATTAGAAATTGATGAAGAATTCGCCCAATTATTAATTGATGAAGGTTTCTCTACGTTAGAAGAATTGGCTTATGTTTCCGTCAGCGAATTGACTGCCATTGACGGTTTGGAAGACGAAGATTTGGTCGAAGAATTGCAAACCCGTGCGAAAAACGCCATTACGGCACAAGCCTTGGCGGAAGAAGAAGCTTTGAAACAAGCGAAAATTGAAGATCGTTTACTCAATCTTGAAGGCATGAATCGACATATCGCATTTAAATTGTCGGAAAAACAAATCACTACGCTGGAAGAACTTGCAGAGCAAGGCGTTGATGATTTAGCAGATATTGAAGAACTCGGTGCCGAACAAGCTGCTGATTTAATCATGGCAGCCAGAAATATTTGTTGGTTCACTGAG","","","55657","MSKEILLAAEAVSNEKLLPREKIFEALESAIALSTKKKYEYDVDVRVAINPKTGEFDTFRRWVVVEEVNNPTKEITLEAARFEDPDAQVGDYVEDQIESIAFDRITMQTARQVISTKIREAERSKIVDQFRSKEGQIITATVKKSNRDSVILDVNGEDGNKAEAVMLREDMLPRENFRPGDRVRGVLYKVSPENKGTQLFVSRAKPEMLIELFRLEVPEIGEELIEIRSAARDPGSRAKIAVKSNDKRIDPVGACVGMRGARVQAITNELGGERVDIVLWDDNPAQFVINAMAPADVSSIVVDEDKHAMDIAVEEVNLAQAIGRNGQNVRLATQLTGWVLNVMTTQELNAKHQAEDDKVLNLFIDTLEIDEEFAQLLIDEGFSTLEELAYVSVSELTAIDGLEDEDLVEELQTRAKNAITAQALAEEEALKQAKIEDRLLNLEGMNRHIAFKLSEKQITTLEELAEQGVDDLADIEELGAEQAADLIMAARNICWFTE","1294830","[FUNCTION] Participates in both the termination and antitermination of transcription. Interacts with RNA polymeraseand binds RNA (by similarity). NusA binds directly to the core enzyme of the DNA-dependent RNA polymerase. NusA also interacts with lambda N protein, RNA, RHO factor, and perhaps NusB. Binds RNA. ","N utilization substance protein A","Cytoplasm","","
InterPro
IPR003029
Domain
RNA binding S1
PF00575\"[131-202]TS1
SM00316\"[133-204]TS1
PS50126\"[135-204]TS1
InterPro
IPR004087
Domain
KH
SM00322\"[234-297]T\"[305-381]TKH
InterPro
IPR004088
Domain
KH, type 1
PS50084\"[306-378]TKH_TYPE_1
InterPro
IPR009019
Domain
KH, prokaryotic type
G3DSA:3.30.300.20\"[218-296]T\"[296-348]Tno description
InterPro
IPR010213
Domain
Transcription termination factor NusA
TIGR01953\"[4-347]TNusA: transcription termination factor NusA
InterPro
IPR010214
Repeat
Transcription termination factor NusA, C-terminal duplication
TIGR01954\"[369-419]T\"[445-494]TnusA_Cterm_rpt: transcription termination f
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[155-217]Tno description
InterPro
IPR013735
Domain
NusA N-terminal
PF08529\"[4-125]TNusA_N
noIPR
unintegrated
unintegrated
G3DSA:1.10.150.20\"[356-426]T\"[437-496]Tno description
G3DSA:3.30.1480.10\"[1-134]Tno description
PTHR22648\"[1-437]TTRANSCRIPTION TERMINATION FACTOR NUSA


","BeTs to 23 clades of COG0195COG name: Transcription elongation factorFunctional Class: KThe phylogenetic pattern of COG0195 is aompkz-qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 126 to 235 match (1e-40) PD:PD004993 which is described as COMPLETE PROTEOME SUBSTANCE A N UTILIZATION TRANSCRIPTION TERMINATION RNA-BINDING HOMOLOG ","","","","","","","","","","","Thu Jan 9 10:39:15 2003","Thu Jan 9 10:39:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01920 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Secondary Laboratory Evidence:Yakhnin AV, Babitzke P. NusA-stimulated RNA polymerase pausing and termination participates in the Bacillus subtilis trp operon attenuation mechanism in vitro. Proc Natl Acad Sci U S A. 2002 Aug 20;99(17):11067-72. PMID: 12161562 Zhou Y, Mah TF, Greenblatt J, Friedman DI. Evidence that the KH RNA-binding domains influence the action of the E. coli NusA protein. J Mol Biol. 2002 May 17;318(5):1175-88. PMID: 12083510Ishii,S., Ihara,M., Maekawa,T., Nakamura,Y., Uchida,H. and Imamoto,F. The nucleotide sequence of the cloned nusA gene and its flanking region of Escherichia coli. Nucleic Acids Res. 12 (7): 3333-3342 (1984) PubMed: 6326058.Saito,M., Tsugawa,A., Egawa,K. and Nakamura,Y. Revised sequence of the nusA gene of Escherichia coli and identification of nusA11 (ts) and nusA1 mutations which cause changes in a hydrophobic amino acid cluster. Mol. Gen. Genet. 205 (2): 380-382 (1986) PubMed: 3027511.Ito,K., Egawa,K. and Nakamura,Y. Genetic interaction between the beta' subunit of RNA polymerase and the arginine-rich domain of Escherichia coli nusA protein. J. Bacteriol. 173 (4): 1492-1501 (1991) PubMed: 1847365.","","Wed Feb 5 14:17:43 2003","1","","","" "AA01922","1294850","1297339","2490","ATGATAGAAGAATTAAAAGGCGCGCCGAAGAAACTGAGTTTGCAGCGTAGAACGAAAACCATTGTTAGTGGTACCAGCGCTTCCGGCAAGAGTAAAGAAGTGCAGGTGGAAGTGCGTAAAAAGCGCACTATTCCGACAGAAGCCGCACAAAAAGCCGAAGAAGCGGCAAAATTGAAAGCCAGACAAGAAGCCGAGCAAAAAGCGGTAGAAGAAAAAGTGCAAAGAGAGAAGGCGGTGAAAGAAAAAGAAGCCGCTGAAAAAGCAAAACAGGCACAGGCCACTAAGGCACAAAGTGCGGTCAATAATCAAGTTAAATCTGTGGATCCGGAAAAAGAGAAACGCAAAGCGGAAGAAGCGGAATTACGTCGTAAAGCGGATGAGTTAGCCCGCCAAAAAGCGGAAGAACAAGCGCGTAAAGCAGCAGAAGAAGCGAAGCGTTACGCGGAACTTTCCGATGATAATCAGCACAACAGCAATACGGAAGATTACTCCGATTACAATTTAACCTCCAGTTATGCCCTGGAAGCGGAAGATGAAGAAGAGCGCCGCAATGAAGGTCGTGGTCGCGGCAAAAATAAAGTGACCAAAGCCAAAAAAGGCGGACGTGATGATGACAGCAACAAAAATGAACGCGAGTCTAACCGTCGTAATCAAAAAGATGTGAAGGGCGGCAAAGGCAAACAAGCGAAAAAAGGCAGTGCACTACAACAAGCCTTTACCAAGCCGGCGCAGGCGGTGAACCGTGATGTGGTGATCGGCGAAACCATTACTGTTGCCGAACTTGCCAATAAAATGGCGGTAAAAGCCACTGAAGTGATTAAAACCATGATGAAAATGGGCGCCATGGCGACTATCAACCAAGTGATCGACCAAGAAACCGCACAATTGGTGGCGGAAGAAATGGGTCACAAAGTGATCGTGCGTAAAGAAAACGAGTTGGAAGAAGCGGTCATGAGCGATCGTGATGTGGACGCCGAATTGGTCACCCGCGCACCGGTGGTGACTATCATGGGGCACGTTGACCATGGTAAAACCTCCTTACTTGACTATATTCGTAAAGCCAAAGTGGCGGCAGGCGAAGCAGGCGGGATCACGCAACATATCGGTGCGTACCATGTGGAAACCGACGACGGCAAAATGATCACTTTCTTAGATACGCCAGGACATGCGGCGTTTACTTCCATGCGTGCGCGTGGTGCGAAAGCGACGGACATCGTGGTGCTTGTGGTTGCCGCCGATGACGGCGTGATGCCGCAAACTATCGAAGCGATCCAACACGCCAAAGCGGCGGGTGTGCCGATTGTCGTTGCAGTAAACAAAATTGATAAACCGGAAGCCAATCCGGAACACGTCGAGCAAGAATTATTGCAATATGACGTTATCGCCGAAAAATTCGGTGGTGACGTGCAATTCGTGTATGTTTCCGCGAAAAAAGGGACCGGTGTTGACGAATTGCTTGAAGCCATCTTGTTGCAATCTGAAGTGCTTGAATTAACCGCCGTGAAAAACGGCATGGCGACAGGCGTGGTAATTGAATCCTACTTAGATAAAGGTCGCGGCCCGGTAGCTACCATCTTAGTTCAATCCGGTACTTTAACCAAAGGCGACATTTTGCTTTGTGGTTTCGAATACGGACGTGTGCGTGCAATGCGCGATGAAAACGGCAAAGAGATCGACGAAGCCGGTCCGGCAATTCCGGTGGAAGTGTTAGGGCTTTCCGGCGTACCGGCGGCAGGTGATGAAGCTACCGTAGTGCGTGATGAGAAAAAAGCGCGTGAAGTGGCGTTATACCGTCAAGGTAAATTCCGCGAAGTGAAACTTGCCCGTCAACAAAAAGCCAAACTGGAAAATATGTTCAGCAACATGGCGGAAGGCGATGTGGCGGAATTAAACGTCATTGTGAAAGCGGACGTACAAGGTTCCGTGGAAGCTATCGTTCAATCTTTAATGGAGCTTTCAACGGACGAAGTGAAAGTGAAAGTGGTTGGCTCCGGTGTAGGTGGTATCACTGAAACCGATGCAACGTTAGCCGCAGCTTCTAACGCCATCATTGTCGGCTTTAACGTACGTGCAGACGGCTCCGCCCGCCGCATTATCGAAAGCGAAAATATCGATTTACGTTACTATTCCATCATTTATGAATTGCTCAACGAAATCAAAGCGGCAATGAGCGGCATGCTTCAACCTGAATTCAAACAAGAAATCATCGGTCTGGCAGAAGTGCGCGATGTGTTCCGTCATCCGAAATTCGGTGCGATCGCCGGCTGTATGGTGACCGAAGGTGTCGTGAAACGTAACAACCCAATCCGCGTATTGCGCGACAATGTGGTGATTTTTGAAGGCGAACTGGAATCCCTCCGCCGCTTCAAAGACGACGTTTCCGAAGTGCGTAACGGCATGGAATGCGGTATCGGCGTGAAGAACTACAACGATGTGAAAGTCGGCGACCAGATTGAAGTGTTTGAAGTGGTTGAGGTTAAACGTTCGATC","","","90712","MIEELKGAPKKLSLQRRTKTIVSGTSASGKSKEVQVEVRKKRTIPTEAAQKAEEAAKLKARQEAEQKAVEEKVQREKAVKEKEAAEKAKQAQATKAQSAVNNQVKSVDPEKEKRKAEEAELRRKADELARQKAEEQARKAAEEAKRYAELSDDNQHNSNTEDYSDYNLTSSYALEAEDEEERRNEGRGRGKNKVTKAKKGGRDDDSNKNERESNRRNQKDVKGGKGKQAKKGSALQQAFTKPAQAVNRDVVIGETITVAELANKMAVKATEVIKTMMKMGAMATINQVIDQETAQLVAEEMGHKVIVRKENELEEAVMSDRDVDAELVTRAPVVTIMGHVDHGKTSLLDYIRKAKVAAGEAGGITQHIGAYHVETDDGKMITFLDTPGHAAFTSMRARGAKATDIVVLVVAADDGVMPQTIEAIQHAKAAGVPIVVAVNKIDKPEANPEHVEQELLQYDVIAEKFGGDVQFVYVSAKKGTGVDELLEAILLQSEVLELTAVKNGMATGVVIESYLDKGRGPVATILVQSGTLTKGDILLCGFEYGRVRAMRDENGKEIDEAGPAIPVEVLGLSGVPAAGDEATVVRDEKKAREVALYRQGKFREVKLARQQKAKLENMFSNMAEGDVAELNVIVKADVQGSVEAIVQSLMELSTDEVKVKVVGSGVGGITETDATLAAASNAIIVGFNVRADGSARRIIESENIDLRYYSIIYELLNEIKAAMSGMLQPEFKQEIIGLAEVRDVFRHPKFGAIAGCMVTEGVVKRNNPIRVLRDNVVIFEGELESLRRFKDDVSEVRNGMECGIGVKNYNDVKVGDQIEVFEVVEVKRSI","1297338","[FUNCTION] IF-2,one of the essential components for the initiation of protein synthesis in vitro, protects formylmethionyl-trna from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. It is also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex (bysimilarity).[SUBCELLULAR LOCATION] Cytoplasmic.","translation initiation factor IF2","Cytoplasm","","
InterPro
IPR000178
Family
Initiation factor 2
PD186100\"[453-557]TIF2_HAEIN_P44323;
TIGR00487\"[245-830]TIF-2: translation initiation factor IF-2
PS01176\"[781-803]TIF2
InterPro
IPR000795
Domain
Protein synthesis factor, GTP-binding
PF00009\"[329-497]TGTP_EFTU
InterPro
IPR004161
Domain
Translation elongation factor EFTu/EF1A, domain 2
PF03144\"[520-583]T\"[751-819]TGTP_EFTU_D2
InterPro
IPR005225
Domain
Small GTP-binding protein domain
TIGR00231\"[329-491]Tsmall_GTP: small GTP-binding protein domain
InterPro
IPR006847
Domain
Translation initiation factor IF-2, N-terminal
PF04760\"[253-304]TIF2_N
InterPro
IPR013575
Domain
Initiation factor 2 associated region, bacterial
PF08364\"[8-48]TIF2_assoc
InterPro
IPR015760
Domain
Translation initiation factor 2 related
PTHR23115:SF41\"[30-192]T\"[211-593]T\"[612-634]TTRANSLATION INITIATION FACTOR IF-2
noIPR
unintegrated
unintegrated
G3DSA:2.40.30.10\"[731-829]Tno description
G3DSA:3.40.50.10050\"[630-709]Tno description
G3DSA:3.40.50.300\"[327-502]Tno description
PTHR23115\"[30-192]T\"[211-593]T\"[612-634]TTRANSLATION FACTOR


","BeTs to 26 clades of COG0532COG name: Translation initiation factor 2 (GTPase)Functional Class: JThe phylogenetic pattern of COG0532 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 7e-255) to 8/8 blocks of the IPB000178 family, which is described as \"Initiation factor 2\". Interpro entry for IP:IPR000178. IPB000178A 330-368 4.2e-38 IPB000178B 381-413 3.2e-30 IPB000178C 414-453 2.7e-35 IPB000178D 454-495 1.1e-25 IPB000178E 520-572 1.4e-34 IPB000178F 628-669 2e-27 IPB000178G 704-745 3.5e-24 IPB000178H 777-821 6.1e-32Significant hit ( 7.8e-30) to 3/3 blocks of the IPB000795 family, which is described as \"GTP-binding elongation factor\". Interpro entry for IP:IPR000795. IPB000795A 333-348 9e-07 IPB000795B 384-415 3.1e-13 IPB000795C 419-443 1.1e-06Significant hit ( 2e-20) to 3/6 blocks of the IPB000640 family, which is described as \"Elongation factor G, C-terminus\". Interpro entry for IP:IPR000640. IPB000640A 331-356 0.0058 IPB000640C 381-408 1.5e-06 IPB000640D 415-443 1.6e-07","Residues 593 to 621 match (8e-08) PD:PD491962 which is described as INITIATION FACTOR TRANSLATION GTP-BINDING IF-2 BIOSYNTHESIS PROTEOME COMPLETE ALTERNATIVE IF2-2 ","","","","","","","","","","","Thu Jan 9 10:45:51 2003","Thu Jan 9 10:45:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01922 is paralogously related to AA03003 (5e-19), AA00892 (2e-14), AA02344 (3e-14), AA00931 (1e-13), AA00563 (1e-13), AA02832 (1e-11), AA02347 (5e-11), AA01852 (1e-08), AA00564 (2e-06), AA03008 (7e-05) and AA00450 (4e-04).","","","","","","Residues 751 to 819 (E-value = 9.8e-10) place AA01922 in the GTP_EFTU_D2 family which is described as Elongation factor Tu domain 2 (PF03144)","","","","","Hedegaard,J., Okkels,H., Bruun,B., Kilian,M., Mortensen,K.K. and Norskov-Lauritsen,N.Phylogeny of the genus Haemophilus as determined by comparison of partial infB sequences Microbiology 147 (Pt 9), 2599-2609 (2001) PubMed: 11535800 Nyengaard,N.R., Mortensen,K.K., Lassen,S.F., Hershey,J.W. and Sperling-Petersen,H.U. Tandem translation of E. coli initiation factor IF2 beta: purification and characterization in vitro of two active forms Biochemical and biophysical research communications. 181 (3), 1572-1579 (1991) PubMed: 1764105 Sacerdot,C., Dessen,P., Hershey,J.W., Plumbridge,J.A. and Grunberg-Manago,M. Sequence of the initiation factor IF2 gene: unusual protein features and homologies with elongation factors. Proc. Natl. Acad. Sci. U.S.A. 81 (24): 7787-7791 (1984) [PubMed: 6096856].Ishii,S., Ihara,M., Maekawa,T., Nakamura,Y., Uchida,H. and Imamoto,F. The nucleotide sequence of the cloned nusA gene and its flanking region of Escherichia coli. Nucleic Acids Res. 12 (7): 3333-3342 (1984) [PubMed: 6326058].Sands,J.F., Regnier,P., Cummings,H.S., Grunberg-Manago,M. and Hershey,J.W. The existence of two genes between infB and rpsO in the Escherichia coli genome: DNA sequencing and S1 nuclease mapping. Nucleic Acids Res. 16 (22): 10803-10816 (1988) [PubMed: 2849753].Laalami,S., Sacerdot,C., Vachon,G., Mortensen,K., Sperling-Petersen,H.U., Cenatiempo,Y.and Grunberg-Manago,M. Structural and functional domains of E coli initiation factor IF2. Biochimie 73 (12): 1557-1566 (1991) [PubMed: 1805969].","","Thu Jan 9 10:45:51 2003","1","","","" "AA01923","1297627","1299996","2370","TTGGCGAGCAATGCCGAGCAAGAAACGGCAGTTTATAACCATCTTTTCACTTTCTTTTCCCGCTATTACGACAACGGCGATTTTATCAGCCAACGCCGTTATAAAAACGACACTTACGCTTATCTTGAACTCTTTTCGCTTATGCCAACAGAAAAAGAGAAAGAACGCACCTTATTGAAAAAGTATTTGCAGGATTACACCGCAAAAAATACGGCTGATTATTTTATTCATAAAAACTTGGGTAAATTTCTAAATCAAGAACTGGATTTTTATATTAAAAATGAAGTGATGAATTTAGATAATATTCAAGCGGAAACCGCTTTTTCTGAAATTGAACAAAATTTACAGCAAATTAAAATTTTAAAAACCGTTGCCCAAGAAATTATTGCGTTTTTGGCACAATTAGAAGATTTCCAAAAGAAATTATGGCTGAAAAAGAAATTTGTGGCAGGCACGCATTATTTAATTACGCTTGATCATTTATCTGATGAATTGATTGAAACCGCGTTAGCGAATCCTGCACAGCTAGAACAATGGCAAGCTTTGTTTAACGTGAATGCAAGCGGTTTAAATGCGGAAAAACTTTGCGAAAATTACCCGCACTTGGTGGTGGATACGTCGCTTTTTGAGCCAAGTTTTCAGGCAGATATATTAAAAAACATTGAAGATCTAGATGAACAAACTAATGGCTTATTAATTCATTCCGATAATTTCCAAGCATTAAATTTATTGCAGGCAAGATATAAAGAACAGGTGAAATGTATTTATATTGATCCGCCGTATAATACAGAAAAAGATAGAATTGATGGAAAATTTGTCTATAAAGATGGCTATCCTCATTCTACATGGGCATCTTTTTTATATAATTTATCAAAAGCCTCCAAGAGCATTTTGAATAAAGATGCAATTTTTTTATCAAGTATTGATGATAATGAGATTATCAATCTGAAAAATATTTTAGATTATACTCTAGGTAAAGATAACTTTATTGATATTTTTTCTTGGCAAAAGACAACCACACCACCTAATTTATCTAAACAAACAAAACAATCTTGCGAATACATTTTAGCTTATCAAAGTGAGAATAGAATATCTCTTACTGGTATTAGAAAAAATAGTAAGAGTTCAAATGGTTTAATGAATCAGACAAACAATATAGGGGTTCTTAAATTTCCTTCAGATATTATTACTACAAAATTACCAGATGGGATTTATAAGGCTGGTATGTACGGCACATCAAGTTATAAAATTGAATTATTAGAAGATACCGAAGTTAAAAATAATAAGTTTATTAAACCTATTGTGTTAAAAGGAAAATTTAAATGGAGCCAAAAATATTTGGATGATTCAATCAAGAGTGGAGTAAAGGTTATTATTCAAACCAAAGCATTTTCCCCATCTTATGAAAAAGAAGAATATGAGCCAGATAAGCCTTGGAATATCATTAATTTAAATTTTAATGTTGGCACTAATGAAAATGCTAGTGCAGAATTAGATCATATGTTTTATCAGAATTTTTCTGATAAGCGTTATCCCAAACCAGTTTCTTTAATGAAATATATTTTGAATTTTAATTTAAATGTAGAAAGTCTTATTCTTGACTACTTCGCAGGTAGCGGCACAACCGCCCACGCTGTAATTAACCTCAACCTTGAAGATAACGGCAATCGCAAATATATCCTTGTGGAACAAGGGGAGTATTTCGATACGGTGTTAAAACCTCGCGTACAAAAAGTGATTTTTAGCGAAAAATGGAAAGAGGGGAAGCCAGAAGCGGGGGAAAATGGTTTGAATGGCGTATCGCAAATTGTGAAAGTGTTGAAGTTGGAAAGCTATGAAGATACCTTGAACAATCTTGAATTACGCAAGCCAACTTATACCTTTGATTTTGATGAACAGGTGCGAAATGACTACTTGTTGCACTATATGCTTGATGTGGAAAGTCGCGGTTCGTTGCTTTCGACGGAGCATTTTGCCAAACCGTTCGATTACGAATTAAATATTGCCACCAGCTCGGCAGGGGCGTATCAGCCACAAAAAATTGATTTAGTGGAAACCTTTAACTATTTGATTGGGTTGCGGGTGAATACGGTAGATGATCGCCGTGAGCGTGGCATGGTGTCGGTGGAGGGTACGCTTCCAAGCGGTGAAAAAACCTTAATTATTTGGCGAGATGTGGAACGCATGGATTATGAGGCGTTAAACCGTTATTTAGATAGCCGCGATATTAACCCGCAAGATAGCGAATATGATGTGGTGTATATCAACGGCGATCATAATATCCCGACGGTGTTTGCCGACAGTGATGATGTCGTGAAAACGCTGAAAGTGCGGTCGATTGAAGGGGAGTTTTTGGAGCGAATGTTTTCG","","","91305","LASNAEQETAVYNHLFTFFSRYYDNGDFISQRRYKNDTYAYLELFSLMPTEKEKERTLLKKYLQDYTAKNTADYFIHKNLGKFLNQELDFYIKNEVMNLDNIQAETAFSEIEQNLQQIKILKTVAQEIIAFLAQLEDFQKKLWLKKKFVAGTHYLITLDHLSDELIETALANPAQLEQWQALFNVNASGLNAEKLCENYPHLVVDTSLFEPSFQADILKNIEDLDEQTNGLLIHSDNFQALNLLQARYKEQVKCIYIDPPYNTEKDRIDGKFVYKDGYPHSTWASFLYNLSKASKSILNKDAIFLSSIDDNEIINLKNILDYTLGKDNFIDIFSWQKTTTPPNLSKQTKQSCEYILAYQSENRISLTGIRKNSKSSNGLMNQTNNIGVLKFPSDIITTKLPDGIYKAGMYGTSSYKIELLEDTEVKNNKFIKPIVLKGKFKWSQKYLDDSIKSGVKVIIQTKAFSPSYEKEEYEPDKPWNIINLNFNVGTNENASAELDHMFYQNFSDKRYPKPVSLMKYILNFNLNVESLILDYFAGSGTTAHAVINLNLEDNGNRKYILVEQGEYFDTVLKPRVQKVIFSEKWKEGKPEAGENGLNGVSQIVKVLKLESYEDTLNNLELRKPTYTFDFDEQVRNDYLLHYMLDVESRGSLLSTEHFAKPFDYELNIATSSAGAYQPQKIDLVETFNYLIGLRVNTVDDRRERGMVSVEGTLPSGEKTLIIWRDVERMDYEALNRYLDSRDINPQDSEYDVVYINGDHNIPTVFADSDDVVKTLKVRSIEGEFLERMFS","1299995","[FUNCTION] Binds the system-specific DNA recognition site 5'-cagcac-3'. necessary for both restriction and methylation (of one of the two a's). [CATALYTIC ACTIVITY] S-adenosyl-L-methionine + DNA adenine =S-adenosyl-L-homocysteine + DNA 6-methylaminopurine. [SUBUNIT] Contains two different subunits: res and mod. Mod is a homotetramer. [SIMILARITY] With other type III mod proteins. ","type III restriction-modification system methylation subunit","Outer membrane, Cytoplasm","","
InterPro
IPR001091
Family
Site-specific DNA-methyltransferase (cytosine-N4-specific)
PR00508\"[251-265]T\"[528-546]T\"[557-577]TS21N4MTFRASE
InterPro
IPR002052
Domain
N-6 Adenine-specific DNA methylase
PS00092\"[255-261]?N6_MTASE
InterPro
IPR002295
Family
N6 adenine-specific DNA methyltransferase, D21 class
PR00506\"[252-264]T\"[532-546]TD21N6MTFRASE
InterPro
IPR002941
Domain
DNA methylase N-4/N-6
PF01555\"[252-573]TN6_N4_Mtase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[230-579]Tno description


","BeTs to 7 clades of COG2189COG name: Adenine specific DNA methylase ModFunctional Class: LThe phylogenetic pattern of COG2189 is a--p-------------hsnuj---wNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.5e-14) to 3/4 blocks of the PR00506 family, which is described as \"D21 class N6 adenine-specific DNA methyltransferase signature\". Prints database entry for PR:PR00506. PR00506A 252-264 0.00015 PR00506C 509-531 15 PR00506D 532-546 1.4e-06Significant hit ( 1.6e-09) to 2/2 blocks of the IPB001091 family, which is described as \"N-4 DNA methylase (N4-MTase)\". Interpro entry for IP:IPR001091. IPB001091A 249-261 0.0058 IPB001091B 532-542 9.9e-05","Residues 307 to 359 match (1e-07) PD:PD096111 which is described as METHYLTRANSFERASE COMPLETE PROTEOME TYPE III TRANSFERASE SYSTEM RESTRICTION-MODIFICATION ENZYME MOD ","","","","","","","","","","","Tue Jan 28 15:53:13 2003","Thu Jan 9 11:00:53 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01923 is paralogously related to AA00029 (9e-66) and AA02031 (1e-07).","","","","","","Residues 245 to 576 (E-value = 3.6e-09) place AA01923 in the N6_N4_Mtase family which is described as DNA methylase (PF01555)","","","","","Humbelin,M., Suri,B., Rao,D.N., Hornby,D.P., Eberle,H., Pripfl,T., Kenel,S. and Bickle,T.A. Type III DNA restriction and modification systems EcoP1 and EcoP15. Nucleotide sequence of the EcoP1 operon, the EcoP15 mod gene andsome EcoP1 mod mutants. J. Mol. Biol. 200 (1): 23-29 (1988) PubMed: 2837577.","","Tue Jan 28 15:53:13 2003","1","","","" "AA01925","1300101","1301060","960","ATGTCACGCACATTTCATCAAGATTTAATTTTAAACCAATGGGTTTTGTCGTTATTTAATCAAACGGATTTAAAAGCCTTTAAAGCACGCCTTGGCGATAACGAAGGGATTTATGCCGATGGGCAAACGGAATTTTTTCATGCGTTAACTTGGCAATTATTTGATACGGATAAAATTTCATTAACTGATTTACGCCGTTACGATTTAAATATCGTGAAACATTGGCAACAAATTACCGAACAACGCAATAAAAAAGAAGGGCATATTTTACATTTAAAATATTTCCAATATCTCTCGTTATTATTTTCTGAAATTTATTTAGATTATTATTTTAACCGCCGTGAGCAATTATTGCGGGAATTAAATACTCAATTAAAGGCACATTTAGATGAAGATGCCAATGCACCCGAATTTCAACCTTATACGGAAGCCGATTTAAACAAAATCGCCTTTTGGAATGCCACGGGCAGCGGTAAAACTTTGTTAATGCATGTGAACATTTTGCAATATTTGCACTATTGCAAAAAGCCGCAGGAGCTCACGGTGTTTGTCATTACGCCGAATGAGGGGCTTTCTAAACAGCATTTAAATGAATTTATTGATTCCAATTTCCATGCCACGACTTTTGATCGCAATAAGGGCGTGCAATCGAGCGGCTTGTTTAACGATATTCAAATTATCGAAATCAGCAAACTTGCCGATAAACAAGGCGAAACAACGGTTGCGGTAGAAAGTTTTGCTTCTATGAATAAGCTGGTGTTGGTGGACGAAGGGCATCGTGGTGCATCAGGCAATGAATGGTTAGCACGCCGTCAGCAAATGATTGGCGATGGCTTTGCTTTTGAATATTCCGCCACTTTTGGGCAAGCGGCGAAAGATCGCAAAACGGCTACCGATATGGAATTTGAACTACAAAAGAGAATCGGTAAATTGCAAGGCATCACCAAAAAAAGCGGAAGT","","","38487","MSRTFHQDLILNQWVLSLFNQTDLKAFKARLGDNEGIYADGQTEFFHALTWQLFDTDKISLTDLRRYDLNIVKHWQQITEQRNKKEGHILHLKYFQYLSLLFSEIYLDYYFNRREQLLRELNTQLKAHLDEDANAPEFQPYTEADLNKIAFWNATGSGKTLLMHVNILQYLHYCKKPQELTVFVITPNEGLSKQHLNEFIDSNFHATTFDRNKGVQSSGLFNDIQIIEISKLADKQGETTVAVESFASMNKLVLVDEGHRGASGNEWLARRQQMIGDGFAFEYSATFGQAAKDRKTATDMEFELQKRIGKLQGITKKSGS","1301059","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR006935
Family
Type III restriction enzyme, res subunit
PF04851\"[135-289]TResIII


","No hits to the COGs database.","","Residues 7 to 120 match (9e-08) PD:PD147799 which is described as PROTEOME COMPLETE AF1406 ","","","","","","","","","","","","Thu Jan 9 11:02:20 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01925 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01927","1301068","1302051","984","TTGCCGTTAAGCTATGCCGATAAGCAAGAAGCTCGCCAAAAATCAGTATTTGAAACTTATGCAAAATGCGTCTTGTTTGATTATTCCTACAAATTTTTCTATGCCGATGGCTACGGTAAAGAGAGTTTGATTTTGAATATGAAAGCGGAGGATTACGACAATGCGGAAAATCTGCAAAAGTATTTTATTGCCTGTTTGTTGTCGTTTTACCAGCAGCAATATCTCTTTGCAAAAAATCAGTCAAAATTGACCGCTTATAACCTTGCAAAGCCACTTTGGATTTTTGTGGGGAATAAGGTGAATACGGACGATAGCGATATTTTGGAAGTGGTTTCATTATTGGCGTTCTTTTTAGCCGCCGAATATCGCAGCCAAGTGCTGACTTGGCTTGAGGAGTTTGTGGAAGATAAAACCGCGTTGCTAGATAACAAAGGCAATGCGATTTTTAAACATCGCTTTCATTATTTGCGTGATTGGCAAGGCAATATGGAAGGGCTATATGCCGATATTCTGCGGAAATTGTTTAATGCTGAAAGTGCTCAAAAACTTCAGCTCAATCAAATTAAAAAAGCCAGTGGCGAAATTGCCTTAAGCGTGGGGAACCATCAGCCTTTTGGGGTGATTAACGTGGGTGACAGTGCCTCTTTGATAAAAGAAGCGGATAAATATCCGAATTTGTTATTTGCCACCGATGAATTTACGCCAAGTTTGTTTAATGACATCAATCAAAAAGAGAGCACGGTTAATTTGCTTATCGGTTCGCGTAAATTTACGGAAGGTTGGTCGAGCTGGCGAGTTTCCACCATGGGCTTGCTCAACATGGGGAAAGGCGAAGGATCGCAAATTATTCAGCTTTTCGGGCGTGGCGTGCGTTTAAAAGGGGAGAATTTCTCACTAAAAAGAACGGTAACCGCTTATCGCAATCGCTTTTTGATGCGAAAGTCGATCTCAACCCGCATCAGATTGATGCGGCATTATTCGCCT","","","43246","LPLSYADKQEARQKSVFETYAKCVLFDYSYKFFYADGYGKESLILNMKAEDYDNAENLQKYFIACLLSFYQQQYLFAKNQSKLTAYNLAKPLWIFVGNKVNTDDSDILEVVSLLAFFLAAEYRSQVLTWLEEFVEDKTALLDNKGNAIFKHRFHYLRDWQGNMEGLYADILRKLFNAESAQKLQLNQIKKASGEIALSVGNHQPFGVINVGDSASLIKEADKYPNLLFATDEFTPSLFNDINQKESTVNLLIGSRKFTEGWSSWRVSTMGLLNMGKGEGSQIIQLFGRGVRLKGENFSLKRTVTAYRNRFLMRKSISTRIRLMRHYSP","1302050","","conserved hypothetical protein","Outer membrane, Cytoplasm","","No hits reported.","No hits to the COGs database.","","Residues 12 to 293 match (3e-53) PD:PD044001 which is described as PROTEOME COMPLETE R III TYPE AF1406 RESTRICTION ENZYME ","","","","","","","","","","","","Thu Jan 9 11:44:41 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01927 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01928","1302126","1304747","2622","GTGTTGTGTCAAATGTGGGCGGAGCGTAAGCGAAAACTGCTGATCGTTTGCCCTGCGATTTTACGCAAGCAATGGGCAAATGAGCTGGCGGAGAAATTTAACTTGCCAACGTTGGTGGTCGATAAAGCAGTGGTAATGGCGGAAATGCGGCAAAAGAGCGGTTCAAAATTGCTGAATTTTTGCAAAAACCACCTTGAGCAGCAAGTAATGATTGTTTCGCACCAATATGCCACAAAAGAGATGGCGACGTTCAAGCAATTTGATTGGGATTTAGTGGTGATTGATGAAGCCCATAAAATGCGAAACGCCTACAAAACCGATAATAAAATGGGTAAAGCAATGCGCCAGGCATTTGGCGGTAAGCGAAAATTGTTGCTGACGGCAACGCCACTGCAAAATTCATTGATGGAGCTTTATGGCTTATCGACATTATTAGACGAGCATTTATTTGGGGATAAAAAATTCTTTCAAAAAGAGTTTGTGCGAAAAGGGAATTTAAGCGAACTGAAAAGCCGTATGGCGAAATTCATTAAACGCACGTTACGAAAAAATGTGCTGGAATATGTGCGTTATACCGAGCGGAAAACCATCACGCAAGAATTTATGCCAAGCGATGCCGAACAACAACTTTATGAGGCGATTTCTGATTTTCTGCATAAAGAGACGATTTACGCTTTGCCGAAACAGCACAAACATTTAACGGCATTGATTTTACGCAAATTATTGGCTTCCAGCCCGAAGGCAGTACTTGGCACGTTGCGTGCGATTTTAGACCGCTTGTTATCGTTGAAAAATACAGGCGTGCTTTCTTCTGAACTTGCCGTCGTTGATGAATTGTTAGCCGATGAAGGCGTAAGCGATGCGGATTTAGAAGCTGATGAGGAAACGCCAGAAACTGAAGGTACGTTAAACCTGAATGTTTTAGACAAAGAGATTCGTGAAATTGAAGGCTTTATTCGCTTAGCAGAAAGTTTAGTCGGCGATAGTAAACTCAATTCATTATTAAAAGCCTTGCAAACAGGCTTTGGCGAAATAGCAAAACTGGGGGCGACACAAAAGGCGATTATTTTTACGGAATCGGTTCGTACACAACATTATTTGTATGATTTCTTGCTTCAAAATGGCTACGCCGATCAGGTGGTGATGTTTAGTGGGACAAATAATGATGCTCAATCGACCCAAATTTACCATGATTGGTTAGCATGCAATGCTGGTACGGAAAAAGTCACGGGATCGGTCGATGTGGATAAACGTTCTGCCTTAATTGAGCATTTCCGCAAAAATGCACAGATTATGATTGCCACTGAGGCTGCGAGCGAAGGGGTGAACTTACAATTTTGCTCATTGCTGATTAACTATGATTTACCTTGGAATCCACAGCGAGTAGAACAGCGGATTGGTCGTTGTCATCGTTATGGGCAGAAATTTGACGTAGTTGTGGTGAATTTCTTGAATAAACGCAATCTTGCCGATCAACGCGTGTTAGAGTTACTTACCGAGAAATTTAAACTTTTCCAAGGTGTGTTAGGGGCTTCTGATGAAGTGCTGGGGCAGATTGAATCGGGCGTAGATATTGAAAATCAAATAGCCAACATTTATGCCACTTGTCGAACAGAGAAAGAAATTCAGCATGCCTTTGATGAGTTACAAGCGAAATTTGCCGATAAAATTAGCGACCGCATAAAAGAAACGCAAGAAGCCTTAGTGGAGCGTTTTGATCAGGCGGTTTTAGATCGTCTAAAAGTGATGGCGCGTGAGCGTTTGAGTGCGATGGAACAATGGTTCTGGGGTGTGACGCAATTTGCCTTGGCAGAGAAAGCGGTGTTTAACCATTCGGATTGGTATTTCTTATTGAAAGATTCGCCGGTGGGAGGTGTGTCGATAGGGCGTTATTTGTTACCGAAGAAAACACGATCTCAACAGATTGAAGGGCTGGAATATCGTTTAAATCAGCCTTTAGGGCAATATTGTGTTAATGAGGCATTAAATACCCAAACGCCAAATGCAACATTAGTATTTGACTACACACATTATCCTGAAAAAATCAGTTTATTGGAACAATATAAAGGGCAATCGGGCTGGTTAAAATTGGATAAAATTTGCGTAACATCACCTGTGGAAAAACAAGATGTGTTGGTGTTTAGCGTTTGCGATCAACAAGGGAATGCGATTAGCGATGAAGAATTTACGCAAAAGCTCTTTTCATTACCCGCACAAGTGCGAACGTTAGCAGAAAATCAACCGCTTGGTTTTGATGCTTTGATTTATCAACAGATTGAGCAAGCTAAACAGCAGATTCAGTTAGAAAATAATGTCTTGTTGAAAACGGAAATGTTGCGTATTCAAACTTGGGCAGAAGATCAAATGCAGGCTGCGGAAGATTTAATTAGCGAAATTAAAGAAGATATTCGGGCAAAAGAACGTGAAGCGGTCACGGAAAATGACTTGGCACGTCAGATTGATTTGCAAGAATCAGTTTCAAAATTACGCAAACAACTTCGTAAAGCACGCAACGAGATTGATGATGTGCAAGATGAAATTCAAGAAGAGGAATCTAGATTACTTAAGGCATTGAAGGCAAAAGTACAGCAAACCATGGATAATCAATCGGTGTTTTTGATT","","","110412","VLCQMWAERKRKLLIVCPAILRKQWANELAEKFNLPTLVVDKAVVMAEMRQKSGSKLLNFCKNHLEQQVMIVSHQYATKEMATFKQFDWDLVVIDEAHKMRNAYKTDNKMGKAMRQAFGGKRKLLLTATPLQNSLMELYGLSTLLDEHLFGDKKFFQKEFVRKGNLSELKSRMAKFIKRTLRKNVLEYVRYTERKTITQEFMPSDAEQQLYEAISDFLHKETIYALPKQHKHLTALILRKLLASSPKAVLGTLRAILDRLLSLKNTGVLSSELAVVDELLADEGVSDADLEADEETPETEGTLNLNVLDKEIREIEGFIRLAESLVGDSKLNSLLKALQTGFGEIAKLGATQKAIIFTESVRTQHYLYDFLLQNGYADQVVMFSGTNNDAQSTQIYHDWLACNAGTEKVTGSVDVDKRSALIEHFRKNAQIMIATEAASEGVNLQFCSLLINYDLPWNPQRVEQRIGRCHRYGQKFDVVVVNFLNKRNLADQRVLELLTEKFKLFQGVLGASDEVLGQIESGVDIENQIANIYATCRTEKEIQHAFDELQAKFADKISDRIKETQEALVERFDQAVLDRLKVMARERLSAMEQWFWGVTQFALAEKAVFNHSDWYFLLKDSPVGGVSIGRYLLPKKTRSQQIEGLEYRLNQPLGQYCVNEALNTQTPNATLVFDYTHYPEKISLLEQYKGQSGWLKLDKICVTSPVEKQDVLVFSVCDQQGNAISDEEFTQKLFSLPAQVRTLAENQPLGFDALIYQQIEQAKQQIQLENNVLLKTEMLRIQTWAEDQMQAAEDLISEIKEDIRAKEREAVTENDLARQIDLQESVSKLRKQLRKARNEIDDVQDEIQEEESRLLKALKAKVQQTMDNQSVFLI","1304746","[SIMILARITY] Belongs to the Snf2/Rad54 helicase family.","ATP-dependent RNA helicase","Cytoplasm, Periplasm","","
InterPro
IPR000330
Domain
SNF2-related
PF00176\"[12-239]TSNF2_N
InterPro
IPR001650
Domain
Helicase, C-terminal
PF00271\"[398-473]THelicase_C
SM00490\"[393-473]THELICc
PS51194\"[330-523]THELICASE_CTER
InterPro
IPR014021
Domain
Helicase superfamily 1 and 2 ATP-binding
PS51192\"[1-148]THELICASE_ATP_BIND_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[352-519]Tno description
PTHR10799\"[4-250]T\"[306-371]T\"[400-573]TATP-DEPENDENT HELICASE SMARCA (SWI/SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN A)-RELATED
PTHR10799:SF40\"[4-250]T\"[306-371]T\"[400-573]TATP-DEPENDENT HELICASE


","BeTs to 16 clades of COG0553COG name: Superfamily II DNA/RNA helicases, SNF2 familyFunctional Class: K,LThe phylogenetic pattern of COG0553 is ao-pkzy-vdrlbcefghs----i-wNumber of proteins in this genome belonging to this COG is","Significant hit ( 9.4e-33) to 4/7 blocks of the IPB000330 family, which is described as \"SNF2 related domain\". Interpro entry for IP:IPR000330. IPB000330C 12-25 0.04 IPB000330D 123-147 1.6e-05 IPB000330F 406-426 0.032 IPB000330G 431-482 5.3e-18Significant hit ( 2.4e-05) to 1/5 blocks of the IPB000629 family, which is described as \"ATP-dependent helicase, DEAD-box\". Interpro entry for IP:IPR000629. IPB000629E 435-476 2.3e-05","Residues 318 to 384 match (1e-20) PD:PD035659 which is described as ALPHA SUBUNIT TRANSHYDROGENASE COMPLETE NUCLEOTIDE PROTEOME NADP PYRIDINE OXIDOREDUCTASE TRANSHYDROGENASE ","","","","","","","","","","","Thu Jan 9 11:51:33 2003","Thu Jan 9 11:51:33 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01928 is paralogously related to AA02544 (1e-18), AA00263 (6e-07), AA00148 (1e-05) and AA00506 (0.001).","","","","","","Residues 398 to 473 (E-value = 4.4e-20) place AA01928 in the Helicase_C family which is described as Helicase conserved C-terminal domain (PF00271)","","","","","","","","1","","","" "AA01930","1304852","1305235","384","ATGGCTCGAGAATTCAAACGTAGCGACCGTGTCGCACAAGAAATCCAAAAAGAAATCGCGGTGATTTTACAACGCGAAGTGAAAGATCCCCGAATCGGCATGGTGACGGTGTCCGATGTGGACGTTTCCAGTGATTTGGCGTATGCCAAAGTGTTCGTCACGTTCTTGTTTGATCATGATGAACAAGCGATCGCACAAGGCATGAAAGGCTTGGAAAAAGCCGCGCCTTATATTCGCACGCTACTTGGTAAAGCCATGCGCTTGCGGATCGTGCCGGAAATTCGTTTTATTTACGATCAATACTTAGTGGAAGGTATGCGTATGTCGAATTTAGTCACTAATGTGGTGCGCGAAGATCAGAAAAAACACCATGAGGACAATGAA","","","15068","MAREFKRSDRVAQEIQKEIAVILQREVKDPRIGMVTVSDVDVSSDLAYAKVFVTFLFDHDEQAIAQGMKGLEKAAPYIRTLLGKAMRLRIVPEIRFIYDQYLVEGMRMSNLVTNVVREDQKKHHEDNE","1305234","[FUNCTION] Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Essential for efficient processing of 16S rRNA. May interact with the 5'terminal helix region of 16S rRNA (by similarity).[SUBCELLULAR LOCATION] Cytoplasmic (Potential).","ribosome-binding factor A","Cytoplasm","","
InterPro
IPR000238
Family
Ribosome-binding factor A
PD007327\"[9-99]TRBFA_HAEIN_P45141;
PF02033\"[7-112]TRBFA
TIGR00082\"[1-118]TrbfA: ribosome-binding factor A
PS01319\"[78-99]TRBFA
InterPro
IPR009019
Domain
KH, prokaryotic type
G3DSA:3.30.300.20\"[1-106]Tno description


","No hits to the COGs database.","Significant hit ( 2e-43) to 3/3 blocks of the IPB000238 family, which is described as \"Ribosome-binding factor A\". Interpro entry for IP:IPR000238. IPB000238A 7-30 1.3e-14 IPB000238B 36-50 1.7e-05 IPB000238C 70-112 1.8e-20","Residues 6 to 111 match (1e-39) PD:PD007327 which is described as FACTOR A RRNA PROCESSING PROTEOME COMPLETE RIBOSOME-BINDING BINDING RIBOSOME PROBABLE ","","","","","","","","","","","Thu Jan 9 11:55:58 2003","Thu Jan 9 11:55:58 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01930 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 112 (E-value = 6.6e-63) place AA01930 in the RBFA family which is described as Ribosome-binding factor A (PF02033)","","","","","Bylund,G.O., Wipemo,L.C., Lundberg,L.A. and Wikstrom,P.M. RimM and RbfA are essential for efficient processing of 16S rRNA in Escherichia coli J. Bacteriol. 180 (1), 73-82 (1998) PubMed: 9422595Sands,J.F., Regnier,P., Cummings,H.S., Grunberg-Manago,M. and Hershey,J.W. The existence of two genes between infB and rpsO in the Escherichia coli genome: DNA sequencing and S1 nuclease mapping. Nucleic Acids Res. 16 (22): 10803-10816 (1988) [PubMed: 2849753].Dammel,C.S. and Noller,H.F. Suppression of a cold-sensitive mutation in 16S rRNA by overexpression of a novel ribosome-binding factor, RbfA. Genes Dev. 9 (5): 626-637 (1995) [PubMed: 7535280].","","Thu Jan 9 11:55:58 2003","1","","","" "AA01932","1305238","1306152","915","ATGTCCAAACCGCGTAAACGTGGGCGTGATATTCACGGCGTATTTTTGCTGGATAAACCGCAAGGAATGTCTTCCAACGACATCATGCAAAAAGTGAAACGCATTTTTCAGGCGAACAAAGCCGGGCATACGGGCGCATTGGATCCGTTAGCCACGGGAATGTTGCCTATCTGCTTGGGCGAAGCTACCAAGTTTTCCCAGTTTTTGTTGGACGCCGATAAACGTTATTTGGTGACGGCAAAGTTGGGCGAGCGCACCGATACCTCCGATGCGGAAGGGCAGGTGGTGGAAACCCGCCCGATTAACGTAAAAACACCTGAAATTTTGACCACACTTGAGGCTTTTCGTGGCGATATTTTGCAAGTACCGACCATGTTTTCCGCCTTGAAGCATAACGGCAAGCCCCTTTATGAATATGCCCGTGCCGGTATTACGGTGGAACGGGAAGCGCGCCCCATTACGATCTTTGAATTGAACTTTATTGAATACCACGCGCCGTATTTAACCCTCGAAGTGCACTGTTCCAAAGGCACTTACATTCGTACCTTGGTGGATGATTTAGGCGAAGTCCTTGGCTGTGGCGCGCACGTCACCATGCTACGTCGCACGGCAGTGGCGGATTACCCGACGGAAAAAATGATGAGTTGGGACGACTTACAAGCCTTGGCGGAACAACAAGATTTAGCGGTGTTGGATGCACTTTTGTTACCGATGGATACCGCCGTAGCGAAACTCTCGGCGTTAATCTTGGATGAAAGCCAAACCCAAGGTATCGGATTCGGTCAACGCATAAAATTCAATAACCCGTCAAAACGACAAGGTCAAGTGCGGTTATTTTCCCATGAGAATCGCTTTCTCGGCGTTGCGGTGATTGATGAGAATAATGTGATTCGACCACAGCGATTGGTGGTGTAT","","","34058","MSKPRKRGRDIHGVFLLDKPQGMSSNDIMQKVKRIFQANKAGHTGALDPLATGMLPICLGEATKFSQFLLDADKRYLVTAKLGERTDTSDAEGQVVETRPINVKTPEILTTLEAFRGDILQVPTMFSALKHNGKPLYEYARAGITVEREARPITIFELNFIEYHAPYLTLEVHCSKGTYIRTLVDDLGEVLGCGAHVTMLRRTAVADYPTEKMMSWDDLQALAEQQDLAVLDALLLPMDTAVAKLSALILDESQTQGIGFGQRIKFNNPSKRQGQVRLFSHENRFLGVAVIDENNVIRPQRLVVY","1306151","[FUNCTION] Formation of pseudouridine at position 55 in the psi GC loop of transfer RNAs (by similarity).[CATALYTIC ACTIVITY] Uracil + D-ribose 5-phosphate = pseudouridine 5'-phosphate + H(2)O.[SIMILARITY] Belongs to the truB family of pseudouridine synthases","tRNA pseudouridine synthase B","Cytoplasm","","
InterPro
IPR002501
Domain
tRNA pseudouridine synthase B, N-terminal-2
PF01509\"[33-180]TTruB_N
InterPro
IPR004510
Family
tRNA pseudouridine synthase B
PIRSF004489\"[11-302]TtRNA pseudouridine synthase B
InterPro
IPR007449
Domain
ZipA, C-terminal FtsZ-binding region
SM00771\"[164-250]Tno description
InterPro
IPR014780
Domain
tRNA pseudouridine synthase B, N-terminal
TIGR00431\"[11-219]TTruB: tRNA pseudouridine synthase B
InterPro
IPR015240
Domain
tRNA pseudouridine synthase B, C-terminal
PF09157\"[246-303]TTruB-C_2
noIPR
unintegrated
unintegrated
PTHR13767\"[104-304]TTRNA-PSEUDOURIDINE SYNTHASE


","BeTs to 25 clades of COG0130COG name: Pseudouridine synthaseFunctional Class: JThe phylogenetic pattern of COG0130 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-66) to 3/3 blocks of the IPB002501 family, which is described as \"Pseudouridylate synthase, TruB family, N-terminus\". Interpro entry for IP:IPR002501. IPB002501A 22-76 4e-35 IPB002501B 133-148 1e-05 IPB002501C 174-206 2.5e-23 IPB002501B 121-136 0.21","Residues 16 to 64 match (2e-21) PD:PD006841 which is described as SYNTHASE TRNA PSEUDOURIDINE COMPLETE PROTEOME B LYASE PSEUDOURIDYLATE PSI55 PROCESSING ","","","","","","","","","","","Thu Jan 9 12:02:01 2003","Thu Jan 9 12:02:01 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01932 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 30 to 180 (E-value = 9.3e-87) place AA01932 in the TruB_N family which is described as TruB family pseudouridylate synthase (N terminal domain) (PF01509)","","","","","Nurse,K., Wrzesinski,J., Bakin,A., Lane,B.G. and Ofengand,J.Purification, cloning, and properties of the tRNA psi 55 synthase from Escherichia coli RNA 1 (1), 102-112 (1995) PubMed: 7489483 Sands,J.F., Regnier,P., Cummings,H.S., Grunberg-Manago,M. and Hershey,J.W. The existence of two genes between infB and rpsO in the Escherichia coli genome: DNA sequencing and S1 nuclease mapping. Nucleic Acids Res. 16 (22): 10803-10816 (1988) [PubMed: 2849753].Nurse,K., Wrzesinski,J., Bakin,A., Lane,B.G. and Ofengand,J. Purification, cloning, and properties of the tRNA psi 55 synthase from Escherichia coli. RNA 1 (1): 102-112 (1995) [PubMed: 7489483].","","Thu Jan 9 12:02:01 2003","1","","","" "AA01933","1306349","1306200","150","GTGGAAATGTTATTTGATCGTTATGTGGCGGAAATTGTCCTGAATGACGGCGAAAATGATGACTTCTCGCTTTTTTGCAGATTGGAAAATTGGCTTACAAGTGAAAGGGAATTAGAACTGCAGATTAGCTATTCAGCAGCAATTCAATAT","","","5932","VEMLFDRYVAEIVLNDGENDDFSLFCRLENWLTSERELELQISYSAAIQY","1306200","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 09:00:32 2004","Thu Feb 26 09:00:32 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01933 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 09:00:32 2004","","","","","","","","","","","","","1","","","" "AA01934","1307053","1306445","609","ATGCGTTTTTTAACTACATTTTTAAATAGTATGCCTAAAATCGTTCTTATCAGACATGTAACACCGTTAGTTGATGGAAGTAAATGTAACGCCACTGTTGCTCAAAATCGTTTGGTCGAATATAACGAAACCGAACGCTTGGCATTAGATGAAATAAATTCCTTCAAACAAAGTACTGCATATCAAGAGATGTTAACAATTCCCAAAATATTTGTTTCTCCTATGATAAGAGCACAAAAAACAGCAAACGCTTTATTCCCAAGTAATGAATTAATTACATTGGAGGATCTAAAAGAGTTTGATCTTAAAATAACAAATATGCCTAAAATAAAACTAACGCTTAATTCATGGTTTATTCTTTCCAGAATCTTATGGCTACTGGGACTAAACAAAACACAAAAAAATATTGGTGAAGAAAAAAAGCGCGTTAAGAAATTAATGCCAACCTTACTAAAACAAGATTGCTGTATTGTCAGCCACGGTTTTATCCAACATGAAATAAAAAACTATTTGAAAAAGAATGAGTTTGTAAAATTATTTCATCAAAAAAATGGGTGTTTTTCTGTAGAGATTTTCCAAAATGCTACATTCAAGCAGAATATAAATCTA","","","23592","MRFLTTFLNSMPKIVLIRHVTPLVDGSKCNATVAQNRLVEYNETERLALDEINSFKQSTAYQEMLTIPKIFVSPMIRAQKTANALFPSNELITLEDLKEFDLKITNMPKIKLTLNSWFILSRILWLLGLNKTQKNIGEEKKRVKKLMPTLLKQDCCIVSHGFIQHEIKNYLKKNEFVKLFHQKNGCFSVEIFQNATFKQNINL","1306444","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR013078
Domain
Phosphoglycerate mutase
PF00300\"[13-167]TPGAM
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1240\"[13-181]Tno description
signalp\"[1-26]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Fri Jan 31 14:30:11 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01934 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA01936","1308367","1307183","1185","ATGACTGATATGAATACCGTTCTCGCAGAACTAAAGCGCGGTGTAGATGAAATTCTTTCCGAACAGGATTTAATTGAAAAAATTAAAGAAAATCGCCCACTGCGCGTGAAACTCGGTGCAGACCCAACCGCACCGGACATTCATTTAGGTCACACGGTCGTACTGAAAAAATTACGTCAATTCCAAAATTTCGGTCATGAAGTGATCTTCCTCATCGGCGACTTCACCGGCATGGTGGGCGACCCGTCCGGTAAAAACACCACCCGCCCGCCACTCAGCCGCGAAGACGTGTTGCGCAACGCAGAAACCTACAAACAGCAGATCTTCAAAATTCTTGATCCGCAAAAAACCCGCATCGTGTTTAACTCCGACTGGCTTGGTAAACTCGGCACCGAAGGCATGATTCGCCTGGCAAGCAATTACACCGTTGCCCGTATGCTGGAACGTGATGATTTCAAAAAACGCTTTTCAAATAACCAACCGATAGCTATTCACGAATTCATTTATCCGCTTCTGCAAGGGCAGGATTCCGTTGCCTTAGAAGCCGACGTTGAACTTGGCGGGACCGACCAAAAATTCAATTTATTGGTGGGTCGTGAGTTACAAAAATCCGCCGGTCAAAAACCACAAGTGGCAATTACCCTGCCGCTGTTGGTGGGCTTGGACGGCGAGAAAAAAATGTCCAAATCCCTTGGCAATTACATCGGCGTAACGGACGCACCGAGCGAAATGTTCGGTAAAATCATGTCCATTTCCGATGATCTAATGTGGGATTGGTATAACCTGCTTTCCTTCCGCCCGTTAACGGAAATCATCCAACTGAAAGAGGACGTGGCGAACGGTAAAAACCCACGTGATGTGAAAATTCTGCTGGCAAAAGAAATCATCGCCCGCTTCCACAGCGAAGCCGATGCCGACGCGGCGGAACAAGAATTTATCAACCGCTTCCAAAAAGGCGCCATGCCGGATGACATGCCGGAATTCACCTTTGAAGGTGAAATCGGACTTGCCAACTTGTTAAAAGACGCCGGCTTAGTCGCCTCCACCTCCGAAGCCAACCGCATGGTACAACAAGGCGGCGTGAAAATTGACGGCGAAAAAGTGGACGACGCTAAGCTGATCATCACCACCTCCACCGCCGTTTACCAAGTGGGCAAACGCAAGTTCGCCAAGGTAACGGTGAAA","","","44111","MTDMNTVLAELKRGVDEILSEQDLIEKIKENRPLRVKLGADPTAPDIHLGHTVVLKKLRQFQNFGHEVIFLIGDFTGMVGDPSGKNTTRPPLSREDVLRNAETYKQQIFKILDPQKTRIVFNSDWLGKLGTEGMIRLASNYTVARMLERDDFKKRFSNNQPIAIHEFIYPLLQGQDSVALEADVELGGTDQKFNLLVGRELQKSAGQKPQVAITLPLLVGLDGEKKMSKSLGNYIGVTDAPSEMFGKIMSISDDLMWDWYNLLSFRPLTEIIQLKEDVANGKNPRDVKILLAKEIIARFHSEADADAAEQEFINRFQKGAMPDDMPEFTFEGEIGLANLLKDAGLVASTSEANRMVQQGGVKIDGEKVDDAKLIITTSTAVYQVGKRKFAKVTVK","1307182","[CATALYTIC ACTIVITY] ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr).[SUBUNIT] Homodimer (By similarity).[SUBCELLULAR LOCATION] Cytoplasmic.","tyrosyl-tRNA synthetase","Cytoplasm","","
InterPro
IPR001412
Family
Aminoacyl-tRNA synthetase, class I
PS00178\"[42-52]TAA_TRNA_LIGASE_I
InterPro
IPR002305
Domain
Aminoacyl-tRNA synthetase, class Ib
PF00579\"[29-317]TtRNA-synt_1b
InterPro
IPR002307
Family
Tyrosyl-tRNA synthetase, class Ib
PR01040\"[46-68]T\"[161-176]T\"[178-200]T\"[211-223]TTRNASYNTHTYR
PTHR11766\"[3-395]TTYROSYL-TRNA SYNTHETASE
TIGR00234\"[1-395]TtyrS: tyrosyl-tRNA synthetase
InterPro
IPR002942
Domain
RNA-binding S4
PF01479\"[334-381]TS4
SM00363\"[334-395]TS4
PS50889\"[334-394]TS4
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620\"[12-217]Tno description
noIPR
unintegrated
unintegrated
G3DSA:1.10.240.10\"[218-339]Tno description


","BeTs to 25 clades of COG0162COG name: Tyrosyl-tRNA synthetaseFunctional Class: JThe phylogenetic pattern of COG0162 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 6.8e-06) to 2/2 blocks of the IPB001412 family, which is described as \"Aminoacyl-transfer RNA synthetases class-I\". Interpro entry for IP:IPR001412. IPB001412A 41-51 7.5 IPB001412B 223-233 0.00045","Residues 162 to 302 match (1e-07) PD:PD131906 which is described as SYNTHETASE LIGASE TYROSYL-TRNA AMINOACYL-TRNA COMPLETE PROTEOME TYRRS TYROSINE--TRNA BIOSYNTHESIS ATP-BINDING ","","","","","Wed Feb 19 07:11:32 2003","","","","","","Thu Jan 9 12:07:06 2003","Thu Jan 9 12:07:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01936 is paralogously related to AA00473 (3e-04).","","","","","","Residues 334 to 381 (E-value = 1e-08) place AA01936 in the S4 family which is described as S4 domain (PF01479)","","","","","Barker,D.G., Bruton,C.J. and Winter,G. The tyrosyl-tRNA synthetase from Escherichia coli. Complete nucleotide sequence of the structural gene. FEBS Lett. 150 (2): 419-423 (1982) [PubMed: 6761148].Lam,H.M. and Winkler,M.E. Characterization of the complex pdxH-tyrS operon of Escherichia coli K-12 and pleiotropic phenotypes caused by pdxH insertion mutations. J. Bacteriol. 174 (19): 6033-6045 (1992) [PubMed: 1356963].","","Thu Jan 9 12:07:06 2003","1","","","" "AA01937","1309394","1308618","777","GTGCTAAAAACACTTAAAAAATCAACCGCACTTTATTGTTCAAAGGTCAACACTATGCAATTACCATCTCTCCAATCCGCAACCTTAATTCGTCGTTACAAACGTTTTCTCGCGGATGTACAACTACCGAGCGGTGACATCACTACCTTGCACTGCGCTAATACCGGTGCCATGATCGGTTGCGGTTCGCAAGGCGACACCCTGTGGTATTCCACCTCCGACAGCGCCACGCGCAAATACCCGAGCTCCTGGGAACTGACCCAATTGGCAAACGGCCACTTAGTTTGTATCAATACCCATCGATCCAATCAACTCACCTTTGATGCATTACAAAAAAAGCAAATTATTGAACTTGCCATGTATGACAAAATCTACCCCGAAGTGAAATACGGCGAAGAGAACAGTCGTATTGATTTCTTACTGAAAGGCAAAGATCTGCCTGATTGCTATGTAGAAGTGAAATCCATCACTTATGTAGATAACGACAAAAAACTCGGTATGTTTCCCGACGCGGTGACCACGCGCGGTCAAAAACATTTACGTGAATTGATCAGCATGAAAAAACAAGGACATCGTGCAGTGATTTTCTTCTGTGGGCTACATGATGGTTTTGATCATTTCCAAATCGCCAAACACATTGATGCCAGATATGACGAATTACTTCATCAGGCGCTGAAAGAAGGTGTGGAAGCCTATGCTTATGCCGCTGAGTTTGAAAAAACACAAGGCATTCCCACCGCACTTAATTTAACTAAAGTGGCACCGTTTAAAGCGGGT","","","29146","VLKTLKKSTALYCSKVNTMQLPSLQSATLIRRYKRFLADVQLPSGDITTLHCANTGAMIGCGSQGDTLWYSTSDSATRKYPSSWELTQLANGHLVCINTHRSNQLTFDALQKKQIIELAMYDKIYPEVKYGEENSRIDFLLKGKDLPDCYVEVKSITYVDNDKKLGMFPDAVTTRGQKHLRELISMKKQGHRAVIFFCGLHDGFDHFQIAKHIDARYDELLHQALKEGVEAYAYAAEFEKTQGIPTALNLTKVAPFKAG","1308617","[FUNCTION] Probable regulatory factor involved in maltose metabolism. ","sugar fermentation stimulation protein","Cytoplasm","","
InterPro
IPR000276
Family
Rhodopsin-like GPCR superfamily
PS00237\"[89-105]?G_PROTEIN_RECEP_F1_1
InterPro
IPR005224
Family
Sugar fermentation stimulation protein
PD011325\"[19-230]TSFSA_HAEIN_P46457;
PF03749\"[30-249]TSfsA
TIGR00230\"[15-254]TsfsA: sugar fermentation stimulation protei


","BeTs to 12 clades of COG1489COG name: Sugar fermentation stimulation protein (uncharacterized)Functional Class: GThe phylogenetic pattern of COG1489 is a-mp-z-qv---bcefgh---j----Number of proteins in this genome belonging to this COG is","","Residues 19 to 230 match (1e-94) PD:PD011325 which is described as STIMULATION SUGAR COMPLETE PROTEOME FERMENTATION HOMOLOG A CONJECTURAL REGULATOR DNA-BINDING ","","","","","","","","","","","Thu Jan 9 12:14:43 2003","Thu Jan 9 12:14:43 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01937 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 30 to 249 (E-value = 1.4e-107) place AA01937 in the SfsA family which is described as Sugar fermentation stimulation protein (PF03749)","","","",""," Kawamukai,M., Utsumi,R., Takeda,K., Higashi,A., Matsuda,H., Choi,Y.L. and Komano,T. Nucleotide sequence and characterization of the sfs1 gene: sfs1 is involved in CRP*-dependent malgene expression in Escherichia coli. J. Bacteriol. 173 (8): 2644-2648 (1991) [PubMed: 2013578].2. Fujita,N., Mori,H., Yura,T. and Ishihama,A. Systematic sequencing of the Escherichia coligenome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region. Nucleic Acids Res. 22 (9):1637-1639 (1994) [PubMed: 8202364].3. Kang,P.J. and Craig,E.A. Identification and characterization of a new Escherichia coli gene that is adosage-dependent suppressor of a dnaK deletion mutation. J. Bacteriol. 172 (4): 2055-2064 (1990)[PubMed: 2180916].","","Thu Jan 9 12:14:43 2003","1","","","" "AA01938","1309633","1311165","1533","ATGTTAATTGGTGTACCTAGAGAACTACTTGATAATGAAAGTCGCGTGGCGGCAACGCCGAAGACGGTTCAGCAAATTTTGAAGCTTGGCTTTGAGGTGATTGTTGAACATGATGCGGGTTTTAAAGCAAGCTTTGAGGATCAGGCATTTGCGGCAGCCGGCGCGAAAATCGGCGATACTGCGCAGGTTTGGAACGCGGACATAATTTTTAAAGTTAACGCGCCGACCGACGATGAAATTACCTTAATGAAGGAAGGTGCGACTTTGGTCAGCTTTATTTGGCCTGCGCAAAATCCGCCATTAATGGAAAAACTCTCCGCGAAAAAGATCAATGTGTTGGCCATGGATGCCGTGCCGCGTATTTCACGGGCACAAGCGCTTGATGCGTTAAGCTCCATGGCGAATATTGCGGGTTACCGTGCGGTAGTGGAAGCCGCTCATGAATTCGGCAGCTTCTTCACCGGACAAATTACTGCTGCAGGTAAAGTACCGCCAGCGAAAGTGTTGGTGATTGGTGCGGGCGTTGCGGGTCTTGCGGCGATTGGTGCGGCAAACAGCCTCGGCGCCATTGTGCGTGCTTTTGACTCCCGTCCGGAAGTGAAAGAACAGGTTGAAAGTATGGGTGCCAGCTTCCTTGAAATTGATTTCAAAGAAGAAGGCGGCAGCGGCGACGGTTATGCGAAAGTGATGTCCGATGAGTTCAATCGTCGCGCGTTAGAACTTTACGCCGAACAAGCGAAAGAAGTGGATATTATTATTACCACCGCGTTAATTCCGGGCAAACCGGCGCCACGCTTGATCACCAAAGAAATGGTGGCATCCATGAAACCGGGTAGCGTAATCGTGGATTTGGCAGCAGCCACCGGCGGTAACTGTGAACTCAGCAAAGCAGGCAAAGTGGTGGTTACCGACAACCAAGTGAAAATCATCGGTTACACTGATTTGCCAAGCCGTTTACCAACCCAATCTTCACAGCTTTACGGCACCAACCTTGTTAATTTATTGAAATTACTTTGTAAAAACAAAGACGGTCAAATTGACATCAATTTTGATGATGTAGTATTGCGTGGCGTGACTGTGATTCGTGACGGTGAAATTACTTGGCCGGCACCACCGATTCAGGTTTCCGCTCAGCCGCAGCAAGCAAAAGCGGCAACAAGTGCGGTCAAAAAAGAAGATGAAAAACCGGTAGATCCGCGTAAGAAATACGGCATTATGGCAGGAGTCGGTATTCTTTTTCTGTGGCTCACATCTGTTGCACCGGCCGCGTTTTTATCACATTTAACCGTTTTCGTATTGGCTTGTGTCGTGGGTTATTATGTGGTCTGGAACGTCAGCCATGCGTTACATACGCCGTTAATGGCAGTCACCAACGCCATTTCGGGGATTATTATTGTGGGAGCGTTATTGCAAATTTCACAAGGTAATCTTTTTATCAGCATGTTGGCGTTTATTGCGATTTTAGTGGCAAGCATCAACATTTTCGGTGGCTTCCGTGTCACCCAACGTATGCTTTCTATGTTTAGAAAAGGC","","","56195","MLIGVPRELLDNESRVAATPKTVQQILKLGFEVIVEHDAGFKASFEDQAFAAAGAKIGDTAQVWNADIIFKVNAPTDDEITLMKEGATLVSFIWPAQNPPLMEKLSAKKINVLAMDAVPRISRAQALDALSSMANIAGYRAVVEAAHEFGSFFTGQITAAGKVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVESMGASFLEIDFKEEGGSGDGYAKVMSDEFNRRALELYAEQAKEVDIIITTALIPGKPAPRLITKEMVASMKPGSVIVDLAAATGGNCELSKAGKVVVTDNQVKIIGYTDLPSRLPTQSSQLYGTNLVNLLKLLCKNKDGQIDINFDDVVLRGVTVIRDGEITWPAPPIQVSAQPQQAKAATSAVKKEDEKPVDPRKKYGIMAGVGILFLWLTSVAPAAFLSHLTVFVLACVVGYYVVWNVSHALHTPLMAVTNAISGIIIVGALLQISQGNLFISMLAFIAILVASINIFGGFRVTQRMLSMFRKG","1311164","[FUNCTION] The transhydrogenation between nadh and nadp is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane (by similarity). [CATALYTIC ACTIVITY] NADPH + NAD(+) = NADP(+) + NADH.[SUBUNIT] Heterodimer of an alpha and a beta chain (by similarity). [SUBCELLULAR LOCATION] Integral membrane protein. Inner membrane (By similarity).","NAD(P) transhydrogenase subunit alpha","Inner membrane, Cytoplasm","","
InterPro
IPR004571
Family
NAD(P) transhydrogenase, alpha subunit
TIGR00561\"[2-511]TpntA: NAD(P) transhydrogenase, alpha subuni
InterPro
IPR007698
Domain
Alanine dehydrogenase/PNT, C-terminal
PF01262\"[146-317]TAlaDh_PNT_C
InterPro
IPR007886
Domain
Alanine dehydrogenase/PNT, N-terminal
PF05222\"[4-137]TAlaDh_PNT_N
InterPro
IPR008142
Domain
Alanine dehydrogenase/PNT, N-terminal subdomain
PS00836\"[4-30]TALADH_PNT_1
InterPro
IPR008143
Domain
Alanine dehydrogenase/PNT, C-terminal subdomain
PS00837\"[170-195]TALADH_PNT_2
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[137-318]Tno description
PTHR10160\"[1-510]TNADP TRANSHYDROGENASE
PTHR10160:SF2\"[1-510]TNADP TRANSHYDROGENASE
tmhmm\"[423-443]?\"[453-473]?\"[477-497]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.4e-92) to 3/3 blocks of the IPB004002 family, which is described as \"Alanine dehydrogenase and pyridine nucleotide transhydrogenase\". Interpro entry for IP:IPR004002. IPB004002A 1-40 5.4e-24 IPB004002B 157-209 3e-37 IPB004002C 258-293 4e-29Significant hit ( 2.1e-05) to 1/5 blocks of the PR00368 family, which is described as \"FAD-dependent pyridine nucleotide reductase signature\". Prints database entry for PR:PR00368. PR00368A 167-189 2.1e-05 PR00368C 167-192 0.00039","","","","","","","","","","","","Thu Jan 9 12:19:07 2003","Thu Jan 9 12:19:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01938 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 144 to 350 (E-value = 1.3e-109) place AA01938 in the AlaDh_PNT_C family which is described as Alanine dehydrogenase/PNT, C-terminal domain (PF01262)","","","","","Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D. Nucleotide sequence of the pntA and pntB genes encoding the pyridine nucleotide transhydrogenase of Escherichia coli. Eur. J. Biochem. 158 (3): 647-653 (1986) [PubMed: 3525165].Ahmad,S., Glavas,N.A. and Bragg,P.D. A mutation at Gly314 of the beta subunit of the Escherichia coli pyridine nucleotide transhydrogenase abolishes activity and affects the NADP(H)-induced conformational change. Eur. J. Biochem. 207 (2): 733-739 (1992) [PubMed: 1633824].Anderlund M, Nissen TL, Nielsen J, Villadsen J, Rydstrom J,Hahn-Hagerdal B, Kielland-Brandt MC. Expression of the Escherichia coli pntA and pntB genes, encoding nicotinamide nucleotide transhydrogenase, in Saccharomyces cerevisiae and its effect on product formation during anaerobic glucose fermentation. Appl Environ Microbiol. 1999 Jun;65(6):2333-40. PMID: 10347010 ","","Thu Jan 9 12:19:45 2003","1","","","" "AA01939","1311179","1312600","1422","ATGTCAGAAGGTTTAGTACAAGCTGCATATATTGTGGCAGCGTTGCTCTTTATCATGAGCTTAGCCGGTCTTTCCAAACATGAAACCGCCAAAGCAGGTTGCTGGTACGGTATTATCGGCATGGGCATTGCGCTCATCGCTACCATTTTCGGACCAAAATCCGAAGGCACCTTGTGGATCATTATCGCGATGGTAATCGGCGGTGTTATCGGTATTCAACGTGCATTAAAAGTGGAAATGACCGAAATGCCGGAATTGGTTGCGATCTTACACAGCTTCGTCGGTTTGGCCGCTGTATTGGTTGGCTATAACAGCTACGGTTTGCATGATATCCCAACCATGCCGAATGGCTTAAACGATGTAGAACAAGCTAAATTTTTGGCTGAGCAAGCCGCCCTTACGAGCGTTCATAATGTGGAAGTGTTCCTAGGTATCTTCATCGGTGCGGTAACCTTCACCGGTTCTGTAGTGGCATTCGGCAAATTAAGTGGAAAAATCAATTCCAAAGCCTTAATGTTGCCGCATCGCCATAAATTAAATTTAGCGGCGCTTGTGGTTTCCGCTTTATTGATGGCGGCGTTTCTGAACAATCCGGACAACATCTTTCCGTTGTTAGTCATGACCGTTATTGCCCTTGCTTTCGGCTGGCACTTGGTGGCATCCATTGGCGGTGCGGATATGCCGGTGGTGGTTTCCATGTTGAACTCCTATTCCGGTTGGGCGGCTGCAGCGGCAGGTTTCATGCTGAGCAATGACCTGTTGATCGTCACCGGTGCACTCGTGGGTTCTTCCGGTGCGATCCTTTCCTACATCATGTGTAAAGCCATGAACCGCTCCTTCATCAGCGTTATTGCCGGCGGTTTTGGGAATGACGTACAGGTTTCTTCCGATACGGAACAAGGTGAACACCGTGAAACCAGCGCAGAAGAAGTGGCGGAATTATTGAAAAATTCCGGCTCTGTGATTATCACTCCGGGATACGGCATGGCAGTTGCACAAGCCCAATATCCGGTAGCGGAAATTACGCAAAAATTACGTGAACGTGGTATCAACGTGCGTTTCGGTATCCACCCGGTTGCCGGACGTTTGCCTGGCCACATGAACGTATTATTGGCGGAAGCGAAAGTGCCTTACGATATCGTATTGGAAATGGATGAAATCAACGATGATTTCGCCGATACCGATACTGTCTTAGTTATTGGCGCCAATGACACCGTCAACCCGGCGGCAATGGACGATCCACACAGCCCAATCGCCGGCATGCCGGTGTTAGAAGTCTGGAAAGCCGCTAACGTAGTAGTATTCAAACGTTCCATGAATACCGGTTACGCGGGCGTACAAAATCCTCTCTTCTTCAAAGAAAACACGCAAATGCTGTTTGGTGATGCCAAAGAGCGTGTGGATGACATTTTAAAAGCGTTG","","","52441","MSEGLVQAAYIVAALLFIMSLAGLSKHETAKAGCWYGIIGMGIALIATIFGPKSEGTLWIIIAMVIGGVIGIQRALKVEMTEMPELVAILHSFVGLAAVLVGYNSYGLHDIPTMPNGLNDVEQAKFLAEQAALTSVHNVEVFLGIFIGAVTFTGSVVAFGKLSGKINSKALMLPHRHKLNLAALVVSALLMAAFLNNPDNIFPLLVMTVIALAFGWHLVASIGGADMPVVVSMLNSYSGWAAAAAGFMLSNDLLIVTGALVGSSGAILSYIMCKAMNRSFISVIAGGFGNDVQVSSDTEQGEHRETSAEEVAELLKNSGSVIITPGYGMAVAQAQYPVAEITQKLRERGINVRFGIHPVAGRLPGHMNVLLAEAKVPYDIVLEMDEINDDFADTDTVLVIGANDTVNPAAMDDPHSPIAGMPVLEVWKAANVVVFKRSMNTGYAGVQNPLFFKENTQMLFGDAKERVDDILKAL","1312599","[FUNCTION] The transhydrogenation between NADH and NADP iscoupled to respiration and ATP hydrolysis and functions asa proton pump across the membrane (by similarity). [CATALYTIC ACTIVITY] NADPH + NAD(+) = NADP(+) + NADH. [SUBUNIT] Heterodimer of an alpha and a beta chain (bysimilarity). [SUBCELLULAR LOCATION] Integral membrane protein. Innermembrane (By similarity).","NAD(P) transhydrogenase subunit beta","Inner membrane, Cytoplasm","","
InterPro
IPR004003
Family
NAD(P) transhydrogenase, beta subunit
PF02233\"[4-474]TPNTB
InterPro
IPR012136
Family
NADP transhydrogenase, beta subunit
PIRSF000204\"[1-474]TNAD(P) transhydrogenase, beta subunit
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1220\"[297-474]Tno description
PTHR10160\"[1-474]TNADP TRANSHYDROGENASE
signalp\"[1-23]?signal-peptide
tmhmm\"[4-24]?\"[34-52]?\"[58-76]?\"[86-106]?\"[141-159]?\"[179-194]?\"[200-220]?\"[229-247]?\"[253-273]?transmembrane_regions


","BeTs to 8 clades of COG1282COG name: NAD/NADP transhydrogenase beta subunitFunctional Class: CThe phylogenetic pattern of COG1282 is ----------r--cefgh-n-jx---Number of proteins in this genome belonging to this COG is","","Residues 73 to 103 match (1e-07) PD:PD349602 which is described as BETA TRANSHYDROGENASE SUBUNIT NADP COMPLETE PROTEOME NUCLEOTIDE OXIDOREDUCTASE PYRIDINE TRANSMEMBRANE ","","","","","","","","","","","Thu Jan 9 12:24:40 2003","Thu Jan 9 12:24:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01939 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Anderlund M, Nissen TL, Nielsen J, Villadsen J, Rydstrom J, Hahn-Hagerdal B, Kielland-Brandt MC. Expression of the Escherichia coli pntA and pntB genes, encoding nicotinamide nucleotide transhydrogenase, in Saccharomyces cerevisiae and its effect on product formation during anaerobic glucose fermentation. Appl Environ Microbiol. 1999 Jun;65(6):2333-40. PMID: 10347010 Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D. Nucleotide sequence of the pntA and pntB genes encoding the pyridine nucleotide transhydrogenase of Escherichia coli. Eur. J. Biochem. 158 (3): 647-653 (1986) [PubMed: 3525165].Ahmad,S., Glavas,N.A. and Bragg,P.D. A mutation at Gly314 of the beta subunit of the Escherichia coli pyridine nucleotide transhydrogenase abolishes activity and affectsthe NADP(H)-induced conformational change. Eur. J. Biochem. 207 (2): 733-739 (1992) [PubMed: 1633824].","","Thu Jan 9 12:24:40 2003","1","","","" "AA01941","1312620","1312769","150","ATGAAGATAAAAAGTGCGGTGATTTTTCACCGCACTTTTTTATTCGGCTATGAAAATAAAATTTTGCGATCACCATTCCAAATCCGGCTTATACAGTATAGTTTTCATGTTTTTTATGTGTATATTTATCCAGTGAATAATTGGAGTGAA","","","6188","MKIKSAVIFHRTFLFGYENKILRSPFQIRLIQYSFHVFYVYIYPVNNWSE","1312769","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 08:50:48 2004","Thu Feb 26 08:50:48 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01941 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 08:50:48 2004","","","","","","","","","","","","","1","","","" "AA01942","1312861","1313013","153","GTGGTTGGCATCTTAACAGACAGCCCAACCCCGAAGAAATATTGGAGCGTCTTGAAAACCCGTAATAAACTAACGGACTATTGGAAAGAATCGGATATTGAAAAAACGCCTAAAGAATTTGCCTTGTTAACCAATAATCTTTTTCAGGTTGGC","","","5896","VVGILTDSPTPKKYWSVLKTRNKLTDYWKESDIEKTPKEFALLTNNLFQVG","1313013","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 08:47:47 2004","Thu Feb 26 08:47:47 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01942 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 08:47:47 2004","","","","","","","","","","","","","1","","","" "AA01943","1313148","1312990","159","ATGAGCATAACAACACAAGAAACCTATCGTAAGGAAGGCTATTTGCCGCAAAAAGTGACACTTTCAGAAGAAGTTGTATTTTTCACTAAAATTGACAATGGCGAAATTAAAGTAAAATCCAATGATGAGGTCTTAGCCAACCTGAAAAAGATTATTGGT","","","6029","MSITTQETYRKEGYLPQKVTLSEEVVFFTKIDNGEIKVKSNDEVLANLKKIIG","1312990","","conserved hypothetical protein","Cytoplasm","This sequence is similar to gi|10954430, an unknown from Actinobacillus actinomycetemcomitans.","No hits reported.","No hits to the COGs database.","","Residues 1 to 53 match (1e-13) PD:PD253686 which is described as PLASMID ","","","","","","","","","","","","Thu Feb 26 08:45:41 2004","Thu Feb 26 08:45:41 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA01943 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 08:45:41 2004","","","","","","","","","","","","","1","","","" "AA01944","1313616","1314461","846","ATGAATATCTTAGACGAACTAAAGAAAGTATTGGATTCAAAGCGTCCGCTTGACCTCATTACAGCAAAATCCTTACAAGATGATTTTATGCTACGTTATAACCAAGCTTCCAATGCTATTGAAGGTAATCAGCTCACCTTAATGGAAACCCGGGTATTATTGGAAAGCGGGATTACGGCCAAGGGGAAACCGTTTAGAGATCACCTGGATATAATCAACCACCGGGAGGCTATTAATTACCTATTGGATATAGTCAAAATACAGGAATCTTTATCAGAACGACATATCAAAAAATTTAATGCATTATTACTGAAAGGTTCTGAAAAAGAAATCTATGCTGGAAAATACCGCACTGTACCGGTAGCCATTCAGGGTGCTGAGCATATTCCACCACAGCCTTATTTATTACAAAGTGCGATGGAAAATCTGATTATAAAAAATCAACAGGCAAAAGATAACGGACAACCAGATATAGACCGAATTGCCGAATTACACGCAGATTTTGTAAAAATTCATCCGTTTGTTGATGGCAACGGACGCACCGGTAGATTAATTATGAATCTCGAACTGATGAGCGTAGGATACAGTATCGCCATTATTGAGCTGACAGACAGGGAAGCTTATTACAACGCATTAGCGAAAGCCGATAATGGGAATTACCAGGCTATCACCAGATTAGTAAAAGAAACGGTGCAACGTTCAATAGAACGTGAATTACAGATAGTTTATCCACAGTGGCAAAAGGATTATCCTAAACTTGCCTACCAGCTAGCTAAACAAAAGGAGGTTAGCGAAAAAAAGCATGAACTTACTCTTGTTAAAGAGCAGGAAAAATTATATAAAATT","","","32425","MNILDELKKVLDSKRPLDLITAKSLQDDFMLRYNQASNAIEGNQLTLMETRVLLESGITAKGKPFRDHLDIINHREAINYLLDIVKIQESLSERHIKKFNALLLKGSEKEIYAGKYRTVPVAIQGAEHIPPQPYLLQSAMENLIIKNQQAKDNGQPDIDRIAELHADFVKIHPFVDGNGRTGRLIMNLELMSVGYSIAIIELTDREAYYNALAKADNGNYQAITRLVKETVQRSIERELQIVYPQWQKDYPKLAYQLAKQKEVSEKKHELTLVKEQEKLYKI","1314460","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003812
Family
Filamentation induced by cAMP protein Fic
PF02661\"[96-218]TFic
noIPR
unintegrated
unintegrated
PTHR13504\"[8-243]TFAMILY NOT NAMED
PTHR13504:SF9\"[8-243]Tgb def: Huntingtin interacting protein E-like protein


","BeTs to 5 clades of COG3177COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3177 is -o-----q------ef-h-nuj----Number of proteins in this genome belonging to this COG is","","Residues 37 to 84 match (8e-09) PD:PD483463 which is described as PROTEOME COMPLETE MLR2757 ALR0501 ","","","","","Sun Aug 24 13:51:11 2003","","","","","","","Thu Jan 9 12:58:13 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01944 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 96 to 218 (E-value = 9.3e-31) place AA01944 in the Fic family which is described as Fic protein family (PF02661)","","","","","","","","1","","","" "AA01945","1315006","1316082","1077","ATGACAAATCAAGCTGTGCACGGTGTGCAAGACGAAATCACTGTGGATAATATTCGATTGACGCAATACAGCCATGGAGCAGGGTGTGGTTGTAAAATCTCGCCTAAGGTATTAGAGAGTATTCTGCATTCAAAAATGGAAAAATTTGTTGACCCGAATTTATTGGTGGGTAACGAAACCAAAGATGATGCGGCAGTATATGATATTGGTAATGGTATCGGGATCATCAGCACAACAGATTTTTTCATGCCAATTGTCGATGATCCTTTCGATTTTGGGCGTATTGCGGCAACTAACGCAATTAGTGACATTTTCGCTATGGGTGGTAAGCCGATAATGGCGATTGCGGTGTTAGGATTTCCGATTACTAAATTACCCGCCGAGGTTGCCCAACGCATTGTTGACGGCGGTCGTTTCGCTTGTCAGGAAGCGGGCATTGCCCTAGCCGGCGGACATTCCATTGATTCGCCCGAACCGATTTTCGGCTTGGCGGTGACCGGCATTATTGATACGGAAAAAGTCAAACGAAACGCCTCCGCAGAAGCCGGTTGCAACCTGTATTTAACCAAACCTCTGGGCATCGGCGTTTTAACTACGGCGGAAAAACAGGGCAAATTAAAACCGGAACACAAAGGGTTGGCAACTAAATGGATGTGCCAAATGAATCTGGTGGGAAGCCAATTTTCGAATATTGACGGCGTGACCGCCATGACCGACGTAACCGGTTTCGGTTTGTTAGGGCATTTAACGGAAATTTGCGAAGGTTCCGATCTGAATGCCGAAGTGGATTTCGCCAACATTAAAACCTTAGACGGCGTGTACGATTACATCGCGCAAGGTTGCATCCCGGGCGGTACCAATCGTAACTTCGACAGCTACGGACACAAAATTGCCCCGATTACCGATCTGCAAAAAGCCGTATTGTGTGACCCGCAAACCTCCGGCGGTTTGCTCATTGCCGTTAAACCGGAAGCGGAAAGCGAGGTCTTTGCCGTTGCACAGAAAGCCGGTGTGGCGCTTTATCCTGTCGGCAGATTAATTGAAAGACAGGGAATGCCAGAATTTATTGTAGTGAAA","","","39251","MTNQAVHGVQDEITVDNIRLTQYSHGAGCGCKISPKVLESILHSKMEKFVDPNLLVGNETKDDAAVYDIGNGIGIISTTDFFMPIVDDPFDFGRIAATNAISDIFAMGGKPIMAIAVLGFPITKLPAEVAQRIVDGGRFACQEAGIALAGGHSIDSPEPIFGLAVTGIIDTEKVKRNASAEAGCNLYLTKPLGIGVLTTAEKQGKLKPEHKGLATKWMCQMNLVGSQFSNIDGVTAMTDVTGFGLLGHLTEICEGSDLNAEVDFANIKTLDGVYDYIAQGCIPGGTNRNFDSYGHKIAPITDLQKAVLCDPQTSGGLLIAVKPEAESEVFAVAQKAGVALYPVGRLIERQGMPEFIVVK","1316081","[FUNCTION] Ssynthesizes selenophosphate from selenide and ATP.[CATALYTIC ACTIVITY] ATP + selenide + H(2)O = AMP + selenophosphate + phosphate. [COFACTOR] Requires magnesium. [SUBUNIT] Monomer (potential).","selenophosphate synthase","Cytoplasm","","
InterPro
IPR000728
Domain
AIR synthase related protein
PF00586\"[25-170]TAIRS
InterPro
IPR004536
Family
Selenide water dikinase
PIRSF036407\"[1-357]TSelenophosphate synthetase
TIGR00476\"[13-347]TselD: selenide, water dikinase
InterPro
IPR010918
Domain
AIR synthase related protein, C-terminal
PF02769\"[181-357]TAIRS_C
noIPR
unintegrated
unintegrated
G3DSA:3.30.1330.10\"[59-173]Tno description
PTHR10256\"[3-329]TSELENOPHOSPHATE SYNTHASE


","BeTs to 6 clades of COG0709COG name: Selenophosphate synthaseFunctional Class: EThe phylogenetic pattern of COG0709 is --m----q------ef-h--u-----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-05) to 2/2 blocks of the IPB000728 family, which is described as \"AIR synthase related protein\". Interpro entry for IP:IPR000728. IPB000728A 91-108 0.00035 IPB000728B 316-324 21","Residues 16 to 61 match (2e-17) PD:PD403944 which is described as COMPLETE PROTEOME SELENOPHOSPHATE TRANSFERASE SELENIUM DIKINASE SYNTHETASE DONOR MAGNESIUM ATP-BINDING ","","","","","","","","","","","Thu Jan 9 13:05:16 2003","Thu Jan 9 13:05:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01945 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 181 to 357 (E-value = 2e-18) place AA01945 in the AIRS_C family which is described as AIR synthase related protein, C-terminal domain (PF02769)","","","","","Secondary Laboratory Evidence:Leinfelder,W., Forchhammer,K., Veprek,B., Zehelein,E. and Bock,A. In vitro synthesis of selenocysteinyl-tRNA(UCA) from seryl-tRNA(UCA): involvement and characterization of the selD gene product Proc. Natl. Acad. Sci. U.S.A. 87 (2), 543-547 (1990) PubMed: 2405383 Kim,I.Y., Veres,Z. and Stadtman,T.C. Escherichia coli mutant SELD enzymes. The cysteine 17 residue is essential for selenophosphate formation from ATP and selenide J. Biol. Chem. 267 (27), 19650-19654 (1992) PubMed: 1527085 Kim,I.Y., Veres,Z. and Stadtman,T.C. Biochemical analysis of Escherichia coli selenophosphate synthetase mutants. Lysine 20 is essential for catalytic activity and cysteine 17/19 for 8-azido-ATP derivatization J. Biol. Chem. 268 (36), 27020-27025 (1993) PubMed: 8262938 ","","Thu Jan 9 13:05:16 2003","1","","","" "AA01947","1316530","1317390","861","GTGCCGCCGGAAAAACGCAATACCGCCATGTGTTTCCAATCTTATGCACTCTTTCCCCACCTCAACGTCTCCCATAATATCTGCTACGGTTTAAAGCAACGTAAAATTGATATTGAAGAACAAAAACAACGGCTGAATTTGGCGTTAAAACAAATGGATTTGGATTTTCATAAATTGAAATTGCCAAGCGAATTGTCCGGTGGTCAGCAGCAGCGGGTCGCCTTGGCGCGCGCAATGGTCACCCGCCCGGATGTGATTTTGTTTGACGAGCCGTTATCCAATCTGGATGCCAAATTACGCGAAAGCGTGCGTTTTGAAATTAAGCAACTTTCCAAACAATACCATCTCACCAGTATTTATGTGACTCATGATCAGGCGGAAGCCTTGACTATGTCCGATAAAATCATCGTGTTAAATAAAGGCGCCATTGAGCAAATCGGTTCGCCGCAGGAAATTTATCATCAGCCGAAAAATCGTTTTGTCGCCGATTTCATCGGTATTGCCAACATTGCCGAGGCGCGGGTCGAATCCATCGATGAAAATCTGTATTCCGCCAAATCGATTTTCGGCGATTTCACGGTCTTTTCTGCAAAACCGCCTGAATCCGAACACATTTATATTTGTTTCCGTCCGGAAGATATTGAATTGTTGCCGGATACGCATAAGCAGGCAGAAAATCAGATTACCATAGATATTACAAACACCGCATTTATGGGCAATATCACAGAAGTGCAGGGCATGGTGCAACGGGACGGCGAAGAGAAAAAATTACGTTTGCAATTAACGAAATGCCCGAATTTGAGCGATACGCTGACGTTTACGGTTCCTCGTAATGCCATTAAATTCTTGGAGTCGGTAAAA","","","36139","VPPEKRNTAMCFQSYALFPHLNVSHNICYGLKQRKIDIEEQKQRLNLALKQMDLDFHKLKLPSELSGGQQQRVALARAMVTRPDVILFDEPLSNLDAKLRESVRFEIKQLSKQYHLTSIYVTHDQAEALTMSDKIIVLNKGAIEQIGSPQEIYHQPKNRFVADFIGIANIAEARVESIDENLYSAKSIFGDFTVFSAKPPESEHIYICFRPEDIELLPDTHKQAENQITIDITNTAFMGNITEVQGMVQRDGEEKKLRLQLTKCPNLSDTLTFTVPRNAIKFLESVK","1317389","","iron(III)-transport ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[64-107]TQ7WKN4_BORBR_Q7WKN4;
PF00005\"[5-141]TABC_tran
PS50893\"[1-165]TABC_TRANSPORTER_2
PS00211\"[65-79]TABC_TRANSPORTER_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[5-168]Tno description
PTHR19222\"[1-176]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF43\"[1-176]TSPERMIDINE/PUTRESCINE ABC TRANSPORTER


","BeTs to 6 clades of COG3839COG name: ABC-type sugar transport systems, ATPase componentsFunctional Class: NThe phylogenetic pattern of COG3839 is -o-pkz-qvdrlbcefghs--j--twNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.8e-16) to 2/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140B 62-100 1.6e-13 IPB001140C 118-147 0.39","Residues 108 to 156 match (5e-07) PD:PD000174 which is described as ATP-BINDING COMPLETE PROTEOME ABC TRANSPORTER TRANSPORTER CASSETTE SYSTEM BINDING OLIGOPEPTIDE ","","","","","","","","","","","","Thu Jan 9 13:19:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01947 is paralogously related to AA02718 (2e-49), AA01656 (3e-48), AA01645 (1e-47), AA00700 (5e-47), AA01051 (2e-34), AA02353 (6e-24), AA01779 (7e-23), AA01524 (3e-22), AA00415 (3e-21), AA01867 (4e-21), AA00858 (2e-20), AA02899 (3e-18), AA01824 (8e-18), AA02324 (1e-15), AA01684 (2e-15), AA01616 (5e-15), AA02080 (6e-14), AA01422 (3e-13), AA02440 (5e-13), AA02898 (1e-12), AA01568 (1e-12), AA02786 (1e-12), AA02320 (7e-12), AA02606 (2e-11), AA01509 (2e-11), AA02140 (3e-11), AA00933 (3e-11), AA00207 (6e-11), AA00799 (1e-10), AA02805 (1e-10), AA02550 (2e-10), AA01456 (3e-10), AA01393 (3e-10), AA02573 (8e-10), AA02225 (5e-09), AA02484 (7e-09), AA01961 (9e-09), AA00934 (9e-09), AA00751 (9e-09), AA02331 (4e-08), AA01820 (6e-08), AA02146 (1e-07), AA02152 (2e-07), AA02642 (4e-06), AA01510 (6e-06), AA01757 (7e-06), AA02609 (1e-05), AA01569 (1e-05) and AA01555 (2e-05).","","","","","","Residues 1 to 141 (E-value = 1.3e-21) place AA01947 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Furuchi,T., Kashiwagi,K., Kobayashi,H. and Igarashi,K. Characteristics of the gene for a spermidine and putrescine transport system that maps at 15 min on the Escherichia coli chromosome J. Biol. Chem. 266 (31), 20928-20933 (1991) PubMed: 1939142 Kashiwagi K, Innami A, Zenda R, Tomitori H, Igarashi K. The ATPase activity and the functional domain of PotA, a component of the sermidine-preferential uptake system in Escherichia coli. J Biol Chem. 2002 Jul 5;277(27):24212-9. PMID: 11976340 ","","Thu Jan 9 13:19:35 2003","1","","","" "AA01948","1317390","1318256","867","ATGAAAAATCTCAAAAATGATTTAAAAGCCTGGCTGCTGCTATGCAGTGGTTTGGGAACGATCCTGTTTTTAATGGGGTCCACGTTCTATATTGTTGTGTCGCAGAGCCTTGGTTTATACAGCATGGCGGGCGAGGAAAGCCGATTTAGTCTGGAATATTGGCAAACCGTGTTGAATAGCCCGGTGTTTCAAAAGTCCTATCTTTATTCCGTGAAAGTGTCATTGCTGGGGGCGATTTTCTCTATTATCGTGGCTTACCCCATTGCCATGTGGCTGCGTAAAAAACTGCCGGCAAAAGTCACTATTATCACCATCTTACGTGCACCGATGCTGGTGCCGGGATTGGTCGCCGCCTTCCTGTTTGTCAACATGATTTCCTATCACGGCATTTTAAATGAAGTCTTTGTTTATTTAGGCATCTGGGATGAGCCGAAAACCCTGCAAAACGATGAATTCGGCTGGGGCGTGGTGATTTTGCAAATGTGGAAAAATATTCCTTTTGCCTTAATCTTAATCGGCGGCGCGGTAAATTCGTTAAAAACCGATTTACTGGATGCAGCGGCAAATTTAGGTTCGACACCATGGCAACGGTTTCATTATGTGATTTTCCCGCTGACACTCGGTGCCGTGCAGGTTTCCTTTATTTTGATTTTCATCGGCGCGCTGGGCGATTTTGCCTTTTACAGTATTGCCGGTCCGCGTAGCACCTATTCTTTGGCGCGTTTAATGCAAATGTCCGCTTATGAATTTGAAGAATGGAACCAAAGTGCGGTGATGGCGTTAACGATCATGCTGACTTCCGCCTTTTTCACGATTCTGGTGTCGTTGCTGATTAAGCCATTGGCGGTGAAATGGGGAGAAGTCAAA","","","32300","MKNLKNDLKAWLLLCSGLGTILFLMGSTFYIVVSQSLGLYSMAGEESRFSLEYWQTVLNSPVFQKSYLYSVKVSLLGAIFSIIVAYPIAMWLRKKLPAKVTIITILRAPMLVPGLVAAFLFVNMISYHGILNEVFVYLGIWDEPKTLQNDEFGWGVVILQMWKNIPFALILIGGAVNSLKTDLLDAAANLGSTPWQRFHYVIFPLTLGAVQVSFILIFIGALGDFAFYSIAGPRSTYSLARLMQMSAYEFEEWNQSAVMALTIMLTSAFFTILVSLLIKPLAVKWGEVK","1318255","","ABC transporter permease, membrane spanning protein","Inner membrane, Cytoplasm","","
InterPro
IPR000515
Family
Binding-protein-dependent transport systems inner membrane component
PF00528\"[67-283]TBPD_transp_1
PS50928\"[67-274]TABC_TM1
noIPR
unintegrated
unintegrated
signalp\"[1-34]?signal-peptide
tmhmm\"[10-32]?\"[68-90]?\"[111-131]?\"[159-179]?\"[200-222]?\"[258-278]?transmembrane_regions


","BeTs to 11 clades of COG1176COG name: ABC-type spermidine/putrescine transport system, permease component IFunctional Class: EThe phylogenetic pattern of COG1176 is ao---z--vd-l--efgh-nuj--twNumber of proteins in this genome belonging to this COG is","","Residues 186 to 278 match (3e-22) PD:PD015756 which is described as COMPLETE PROTEOME PERMEASE ABC TRANSPORTER TRANSMEMBRANE SYSTEM MEMBRANE TRANSPORTER INNER ","","","","","","","","","","","","Thu Jan 9 13:21:36 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01948 is paralogously related to AA02719 (5e-17), AA01950 (3e-11), AA01780 (4e-11), AA01650 (1e-10), AA01644 (2e-10), AA00699 (3e-08), AA01649 (2e-07), AA02720 (5e-07), AA01050 (1e-06), AA01682 (6e-06) and AA01866 (2e-05).","","","","","","Residues 67 to 283 (E-value = 4.5e-09) place AA01948 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component (PF00528)","","","","","","","","1","","","" "AA01950","1318256","1319104","849","ATGAATAGCAGCGCACAAATCACGACAAAAAACAGTCGATTAATCGCCCGCATTTCCCTCATCTTTTTTATCCTCGCGAATTTTATCTGGCTGTTTCTGCCGTTTTTGATGGCGGGCTTATGGTCGTTGGTGGATCCGTCAAAGCCTTGGAGCTATCCCGACATTTTCCCGCAATCATTGTCTTTTGAACGTTGGAAAATCGTGTGGGAAACCACCTCGTTATCGGAGGCAATGTTCAATAGTTATACTATTGCGCCGACGGTTTCGTTGATTACCATTTTGCTCTCATTGCCCACCGCCTATGCCTTCGGGCGCATGGAATTTCGCGGAAAAAAACTGGCTGAGTTGTTGACGTTAATTCCATTGGTGATTCCGGGCATGATCATCGCGTTGTTCTTCAGCCGTATGTTATTGGATTTGAAAATTAATAATCCGTTTATCGGGATTGTTATCGGGCACGTCGTATTAACGCTGCCTTACGCCATTCGGATTTTATCGGCGGGATTTTCTTCCGTGCCTCAGGATTTAATTGAAGCGAGTCGCGACCTTGGCGCGTCTAAATTGACCGTGTTTAAGGACGTTTATCTGCCGATGCTCAAACCCAGTTTTCTGGCGTCCATTATTTTTTGTTTAGTGAAAAGTATTGAAGAATTTGCCATTTCATTTGTGATCGGTTCCCCGGATTTCATCACCGTGCCGACCATTTTATATTCTTTCCTAGGCTATTCCTTCATTCGCCCGAATGCCGCCGTGGTATCCATTATTCTCTTGGTGCCGAACATTATTTTAATGATGATTATCGAAAAACTGCTCAAAGGTAATTATCTCTCTCAGTCCACAGGAAAAGCA","","","32149","MNSSAQITTKNSRLIARISLIFFILANFIWLFLPFLMAGLWSLVDPSKPWSYPDIFPQSLSFERWKIVWETTSLSEAMFNSYTIAPTVSLITILLSLPTAYAFGRMEFRGKKLAELLTLIPLVIPGMIIALFFSRMLLDLKINNPFIGIVIGHVVLTLPYAIRILSAGFSSVPQDLIEASRDLGASKLTVFKDVYLPMLKPSFLASIIFCLVKSIEEFAISFVIGSPDFITVPTILYSFLGYSFIRPNAAVVSIILLVPNIILMMIIEKLLKGNYLSQSTGKA","1319103","","ABC transporter, membrane spanning protein","Inner membrane, Cytoplasm","","
InterPro
IPR000515
Family
Binding-protein-dependent transport systems inner membrane component
PF00528\"[78-277]TBPD_transp_1
PS50928\"[78-267]TABC_TM1
noIPR
unintegrated
unintegrated
signalp\"[1-38]?signal-peptide
tmhmm\"[21-43]?\"[82-102]?\"[117-135]?\"[141-161]?\"[194-212]?\"[218-238]?\"[247-267]?transmembrane_regions


","No hits to the COGs database.","","Residues 93 to 167 match (3e-20) PD:PD390192 which is described as PROTEOME COMPLETE ABC PERMEASE MEMBRANE TRANSPORTER TRANSPORTER PLASMID TRANSMEMBRANE SUGAR ","","","","","","","","","","","","Thu Jan 9 13:22:39 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01950 is paralogously related to AA02720 (8e-18), AA01780 (1e-15), AA00699 (2e-14), AA02719 (8e-13), AA01644 (4e-12), AA01866 (5e-12), AA01948 (3e-11), AA01050 (4e-11), AA01649 (6e-10), AA00416 (3e-08), AA01650 (7e-06) and AA01682 (3e-05).","","","","","","Residues 78 to 277 (E-value = 2.2e-16) place AA01950 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component (PF00528)","","","","","","","","1","","","" "AA01952","1319127","1320215","1089","ATGCAAAAAAATATTCGTAAACTTGTTTCTATCGGCTTAACCGCCGCGGCATTCGCCGTGACCAATTTTGCGCTGGCTGCAACGGATTTAAGCGGTAAATCCTGGAGTGAAATTGAAGCGCTGGCGAAGAAAGAAGGCAAAGTAACGGTGAGCGTATGGTATTTGCAGCCGCAGTTCCGTAATTTCGTGAAAGAATTTGAAAGCCAATACGGCATTAAAGTCAAAGTGCCGGAAGGCACCATGGACGGCAATATCAATAAACTGATTGCCGAGAAAAACCTGGAAACCGGCAAAATGGACGTGGTGGTGCTCAACGCGGATCGCTTGAGTAACGTAGCGAAAAACGACACTCTCACCAAGCTGAATCAGTTACCGAATTTCGATAAATTAAATCATCACTTGCAAGGCGTGGAACTGGGTGATGTGGCGGTCGGTTATTGGGGTAACCAAACCGGCTTGGCTTACGATCCGCTGCGTATCAAAGAAGAGGAATTGCCGCAATCCTGGCAGGATATGGAAAATTATATTGATAAACATCCGAAAAAATTCGGCTATTCCGACCCGAACGGCGGCAGTTCAGGTAACGCCTTTATTCAACGGGCTTTAGTTTATATTAACGGCGACTACGATTATCGCACCGACAAAATTGATGAAGCGCAAATTGCCAGCTGGAAGAAAACCTGGGATTGGTTCAGCAGCAAAAAAGATTCGCTGATTCGCACCGCCTCCAATGCAGACAGCTTAACCCGCCTAAATGACGGCGAATTGGTGATTGTCTCCGCCTGGCAGGATCACTTGTTCAGCTTGCAAAAACAAGGCGCAATCACCGACCGCTTAAAATTCTACATTCCGAAATTCGGCATGCCGGGCGGCGGTAATGTGATGACGGTGGCGAAAAATACACCGAACCCTGCGGTATCTTTAGTGTTTGTCCACTGGATTACTTCCCCAGAAGTGCAACAAAAATTAAGCCAAGAATTTGGGGTTCGTCCGTTAGATAGTCAATCCGGCTTAAAAGACACCATTTTCTTCTCCGCCCCATGGCGCAAAGCTGAAATGGAATCTTTCACCAAAGAAGTGATTTCACGT","","","40769","MQKNIRKLVSIGLTAAAFAVTNFALAATDLSGKSWSEIEALAKKEGKVTVSVWYLQPQFRNFVKEFESQYGIKVKVPEGTMDGNINKLIAEKNLETGKMDVVVLNADRLSNVAKNDTLTKLNQLPNFDKLNHHLQGVELGDVAVGYWGNQTGLAYDPLRIKEEELPQSWQDMENYIDKHPKKFGYSDPNGGSSGNAFIQRALVYINGDYDYRTDKIDEAQIASWKKTWDWFSSKKDSLIRTASNADSLTRLNDGELVIVSAWQDHLFSLQKQGAITDRLKFYIPKFGMPGGGNVMTVAKNTPNPAVSLVFVHWITSPEVQQKLSQEFGVRPLDSQSGLKDTIFFSAPWRKAEMESFTKEVISR","1320214","","ABC transporter, substrate binding protein","Periplasm","","
InterPro
IPR006059
Family
Bacterial extracellular solute-binding protein, family 1
PF01547\"[7-321]TSBP_bac_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[43-332]Tno description
signalp\"[1-19]?signal-peptide
tmhmm\"[9-27]?transmembrane_regions


","No hits to the COGs database.","","Residues 170 to 320 match (2e-09) PD:PD557762 which is described as ABC PROTEOME COMPLETE BINDING SUBSTRATE TRANSPORTER ","","","","","","","","","","","","Thu Jan 9 13:26:39 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01952 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 321 (E-value = 1.3e-08) place AA01952 in the SBP_bac_1 family which is described as Bacterial extracellular solute-binding protein (PF01547)","","","","","","","","1","","","" "AA01953","1320409","1320272","138","GTGCAACAGCTACACAATAGTGAAAAACACGTGGGAAAATTATTCACAAACTCGATCTCTCGTTTGTTCACCCCTAACGGGGCCGTTGGCAAAGCCAACGTTAAAAAAACGTCGTTTTTTGTGACCGCACTTTTTGGA","","","5002","VQQLHNSEKHVGKLFTNSISRLFTPNGAVGKANVKKTSFFVTALFG","1320272","","hypothetical protein","Cytoplasm, Extracellular","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 08:43:10 2004","Thu Feb 26 08:43:10 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA02219.AA01953 is paralogously related to AA02219 (3e-12), AA02106 (1e-04) and AA00052 (1e-04).","Thu Feb 26 08:43:10 2004","","","","","","","","","","","","","1","","","" "AA01954","1322374","1320608","1767","ATGTATGACGATAAAAGCACGGTGATTTATGTGGGCAAGGCGAAAGATCTGAAAAAACGCTTATCCAGTTATTTTCGCAAGCAGTTAAGCAGCAAAAAAACGGAAGCATTGGTGGCGTCGATTCAGCATATCGAAACCACCATTACCACATCGGAAACCGAAGCCCTGCTCCTAGAGCACAATTACATCAAAACCTACCAGCCGCGCTATAACGTGCTGTTGCGCGATGATAAATCTTATCCGTACATTTTATTAACCAAAGAAACCCACCCGCGTATTACCGCTTATCGCGGTTCGAAAAAAATCCAAGGGGAATATTTCGGTCCTTATCCGAATGCCGGTGCAGTGCGCGAAACCCTGTCTTTATTACAAAAACTGTTCCCCATTCGGCAGTGTGAAAACTCCGTGTATAACAACCGTTCGCGCCCCTGTTTGCAGTATCAAATCGGGCGTTGTCTGGCGCCTTGCGTAAAGGGCTATGTGACCGATGAAGCCTATGCGCAGCAGGTCAATTTCGCCCGCTTGTTTTTACAAGGAAAAGATCAACAGGTGCTGGATCATTTGGTGAAGCAAATGGAACAGGCAAGTCAGCAACTGAATTTTGAAGAAGCGGCACGCGTTCGTGATCAAATTCAGGCAGTGCGGGCAGTAATTGAAAAACAATTTGTCGCCAACGATCGCCATGACGACATTGATATTATCGCCATCACCTATCAACTCGGCGTGGCCTGCGTGCAGGTTTTGTTTATTCGTCAAGGTAAGATTTTGGGCAATCGCAGCTATTTTCCGAAAGTCCCGAGCAATACCAATCTGGCAGAACTCACGGAAACCTTTGTGGGGCAATTTTATTTGCAGGCGCACCAAGGCAGAACCATTCCGAACACCATTATCGTGGATCAAAAACTGGACGAAAAAGTCGATTTGGAAACTTTACTCAGCGACCAAGCGGGACGCAAAGTCAGCATTCAGGATCATGCCAAAGGCGATAAAAGCAAATATTTGCAACTGGCACAAATGAACGCCAAAGCGGCGTTAGTCACCAAATTAAAACAATCCACATTACAGCACGATCGCTACGTCGCACTGCAGGAATTACTCGGCATCGCTGCCATCAAACGCATGGAATGTTTCGACATCAGCCACACCATGGGCGAACAAACCACCGCCTCCTGCGTGGTTTTCAACCAAGACGGACCGCTGAAATCCGATTACCGCCGTTTCAACATCAGCGGCATCACCAAAGGCGACGATTACGCCGCCATGGAACAAGCCCTGTTAAAACGCTACGACAAAGATCTGGAAGACGACAAAATTCCCGACATTATTTTTATCGACGGCGGCAAGGGACAACTCAACCGCGCGTTGCAGGTGTTCGAAAACCTTAATGTAAAATGGAACAAAAACCAACCGCACTTAATCGGTGTTGCCAAAGGCGTGGATCGTCGTGCCGGTTTGGAAACCTTGATTTTGAGCAAATGGGACAAAGAATTGCATTTACCGGCGGACAGCCTTGCGCTTCACTTGATCCAGCATATCCGCGACGAAAGCCACAATCACGCCATTAGCGGACACCGCAAAAAACGCCAACAACATTTCACCCAAAGTGGCTTGGAAAGCATTGAAGGCGTCGGCGCCAAACGCCGCCAAGCCCTGCTCAAATACCTCGGCGGCTTGCAAGGCGTCAAAAATGCCACCCTCGACGAAATCGCCTCCGTCCCCGGCATATCAAAAGCCCTGGCAGAAAAGATTTTTGAGACCTTGCAGCAT","","","69074","MYDDKSTVIYVGKAKDLKKRLSSYFRKQLSSKKTEALVASIQHIETTITTSETEALLLEHNYIKTYQPRYNVLLRDDKSYPYILLTKETHPRITAYRGSKKIQGEYFGPYPNAGAVRETLSLLQKLFPIRQCENSVYNNRSRPCLQYQIGRCLAPCVKGYVTDEAYAQQVNFARLFLQGKDQQVLDHLVKQMEQASQQLNFEEAARVRDQIQAVRAVIEKQFVANDRHDDIDIIAITYQLGVACVQVLFIRQGKILGNRSYFPKVPSNTNLAELTETFVGQFYLQAHQGRTIPNTIIVDQKLDEKVDLETLLSDQAGRKVSIQDHAKGDKSKYLQLAQMNAKAALVTKLKQSTLQHDRYVALQELLGIAAIKRMECFDISHTMGEQTTASCVVFNQDGPLKSDYRRFNISGITKGDDYAAMEQALLKRYDKDLEDDKIPDIIFIDGGKGQLNRALQVFENLNVKWNKNQPHLIGVAKGVDRRAGLETLILSKWDKELHLPADSLALHLIQHIRDESHNHAISGHRKKRQQHFTQSGLESIEGVGAKRRQALLKYLGGLQGVKNATLDEIASVPGISKALAEKIFETLQH","1320607","[FUNCTION] The ABC excision nuclease is a DNA repair enzyme that catalyzes the excision reaction of UV-damaged nucleotide segments producing oligomers having the modified base(s). Attaches to theuvrA-uvrB complex, displacing uvrA, and the damaged DNA strand is nicked on both sides of the damaged site.[SUBUNIT] Consists of three subunits; uvrA, uvrB and uvrC. [SUBCELLULAR LOCATION] Cytoplasmic.","excinuclease ABC, subunit C","Cytoplasm, Outer membrane","","
InterPro
IPR000305
Domain
Excinuclease ABC, C subunit, N-terminal
PF01541\"[1-77]TGIY-YIG
SM00465\"[1-76]TGIYc
PS50164\"[1-72]TUVRC_1
InterPro
IPR000445
Domain
Helix-hairpin-helix motif
PF00633\"[557-586]THHH
InterPro
IPR001162
Domain
Excinuclease ABC, C subunit, C-terminal
PD005870\"[361-535]TUVRC_HAEIN_P44489;
PF08459\"[362-521]TUvrC_HhH_N
PS50165\"[233-458]TUVRC_2
InterPro
IPR001943
Domain
UvrB/UvrC protein
PF02151\"[182-217]TUVR
PS50151\"[182-217]TUVR
InterPro
IPR003583
Domain
Helix-hairpin-helix DNA-binding, class 1
SM00278\"[535-554]T\"[567-586]THhH1
InterPro
IPR004791
Family
Excinuclease ABC, C subunit
TIGR00194\"[1-568]TuvrC: excinuclease ABC, C subunit
noIPR
unintegrated
unintegrated
G3DSA:1.10.150.20\"[534-589]Tno description
G3DSA:4.10.860.10\"[160-222]Tno description


","BeTs to 20 clades of COG0322COG name: Nuclease subunit of the excinuclease complexFunctional Class: LThe phylogenetic pattern of COG0322 is -om----qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.3e-14) to 2/3 blocks of the IPB001943 family, which is described as \"UvrB/uvrC motif\". Interpro entry for IP:IPR001943. IPB001943B 72-81 0.05 IPB001943C 188-215 6.9e-11Significant hit ( 2.8e-10) to 2/2 blocks of the IPB000305 family, which is described as \"UvrC homology region 1\". Interpro entry for IP:IPR000305. IPB000305A -3-24 0.02 IPB000305B 59-71 4.8e-06","Residues 284 to 371 match (3e-08) PD:PD546127 which is described as C PROTEOME SUBUNIT ABC COMPLETE EXCINUCLEASE ","","","","","","","","","","","Thu Jan 9 13:32:51 2003","Thu Jan 9 13:32:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01954 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 557 to 586 (E-value = 1.9e-06) place AA01954 in the HHH family which is described as Helix-hairpin-helix motif (PF00633)","","","","","Moolenaar GF, van Sluis CA, Backendorf C, van de Putte P.Regulation of the Escherichia coli excision repair gene uvrC. Overlap between the uvrC structural gene and the region coding for a 24 kD protein. Nucleic Acids Res 1987 May 26;15(10):4273-89. PubMed: 3295776. Sharma,S., Stark,T.F., Beattie,W.G. and Moses,R.E. Multiple control elements for the uvrC gene unit of Escherichia coli Nucleic Acids Res. 14 (5), 2301-2318 (1986) PubMed: 3515318 Sancar,G.B., Sancar,A. and Rupp,W.D. Sequences of the E. coli uvrC gene and protein . Nucleic Acids Res. 12 (11): 4593-4608 (1984) PubMed: 6330676.Gopalakrishnan,A.S., Chen,Y.C., Temkin,M. and Dowhan,W. Structure and expression of the gene locus encoding the phosphatidylglycerophosphate synthase of Escherichia coli. J. Biol. Chem. 261 (3): 1329-1338 (1986) PubMed: 3003065.","","Tue Jan 28 15:55:44 2003","1","","","" "AA01956","1323346","1322576","771","ATGACACAATTCACCGTGATCATTCCCGCCCGTTACGCCTCCAGCCGCTTACTGGGCAAACCCTTAGCCGATATTGCCGGCAAGCCGATGATTCAACACGTTTTTGAACAAGCCAAACAATCCGGTGCCAACCGCGTCATTATCGCCACCGATAACGAATTGGTGGCAACCGCCGCAAGAAATTTCGGGGCGGAAGTGTGCATGACTGCCAAAAACCACAATTCCGGCACGGAACGCCTGGCGGAAGTGGTGGAAAAACTGGTGCTGCCCGACGATGAAATTATCGTCAACATTCAAGGCGACGAACCGCTCATTCCGCCCGTTATCGTGAAACAAGTGGCGGAAAACCTGGCAAAATACCCTGTGAACATGGCAAGCCTTGCGGTAAAAATTGATGACGCGAAAGAATTGTTTAATCCCAACGTGGTAAAAGTGCTGACCGACAAAAACGGCTATGTGCTTTATTTCTCCCGCGCCGTGATTCCCTGGGATCGCGATCAATTCGCACAAACGGACGATACGGCAAAGTTACGGCTGAATACCGAATATTTACGTCACATCGGCATTTACGCTTACCGTGCCGGATTCATTAAACAATACGTACAGTGGCAGCCGACTGCGCTGGAACACATCGAAAAACTGGAACAATTACGCGTGCTTTGGCATGGCGAAAAAATCCATGTAGAACTCGCTAAAGAAGTGCCTGCCGTGGGTGTGGATACCCCCGAAGATCTGGAAAAAGTGCGGTCGATTTTATCGGAGAAATGCCGT","","","28868","MTQFTVIIPARYASSRLLGKPLADIAGKPMIQHVFEQAKQSGANRVIIATDNELVATAARNFGAEVCMTAKNHNSGTERLAEVVEKLVLPDDEIIVNIQGDEPLIPPVIVKQVAENLAKYPVNMASLAVKIDDAKELFNPNVVKVLTDKNGYVLYFSRAVIPWDRDQFAQTDDTAKLRLNTEYLRHIGIYAYRAGFIKQYVQWQPTALEHIEKLEQLRVLWHGEKIHVELAKEVPAVGVDTPEDLEKVRSILSEKCR","1322575","[FUNCTION] Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in gram-negative bacteria (by similarity). [CATALYTIC ACTIVITY] CTP + 3-deoxy-D-manno-octulosonate = diphosphate + CMP-3-deoxy-D-manno-octulosonate. [PATHWAY] Liposaccharide biosynthesis. [SUBCELLULAR LOCATION] Cytoplasmic (Potential).","3-deoxy-manno-octulosonate cytidylyltransferase","Cytoplasm","","
InterPro
IPR003329
Family
Acylneuraminate cytidylyltransferase
PF02348\"[5-226]TCTP_transf_3
InterPro
IPR004528
Family
3-deoxy-D-manno-octulosonate cytidylyltransferase
TIGR00466\"[2-246]TkdsB: 3-deoxy-D-manno-octulosonate cytidyly
noIPR
unintegrated
unintegrated
G3DSA:3.90.550.10\"[4-252]Tno description
PTHR21485\"[9-255]TCMP-N-ACETYLNEURAMINIC ACID SYNTHASE
PTHR21485:SF4\"[9-255]TCMP-2-KETO-3-DEOCTULOSONATE (CMP-KDO) CYTIDYLTRANSFERASE


","BeTs to 11 clades of COG1212COG name: CMP-2-keto-3-deoxyoctulosonic acid synthetaseFunctional Class: MThe phylogenetic pattern of COG1212 is -------q------efghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 3.2e-22) to 3/3 blocks of the IPB003329 family, which is described as \"Cytidylyltransferase (CMP-NeuAc synthetase)\". Interpro entry for IP:IPR003329. IPB003329A 7-24 5.4e-09 IPB003329B 46-63 0.00036 IPB003329C 212-226 1.1e-05","","","","","","","","","","","","Thu Jan 9 13:37:45 2003","Thu Jan 9 13:37:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01956 is paralogously related to AA01539 (4e-07).","","","","","","Residues 5 to 226 (E-value = 1.7e-86) place AA01956 in the CTP_transf_3 family which is described as Cytidylyltransferase (PF02348)","","","","","Goldman,R.C., Bolling,T.J., Kohlbrenner,W.E., Kim,Y. and Fox,J.L. Primary structure of CTP:CMP-3-deoxy-D-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase) from Escherichia coli. J. Biol. Chem. 261 (34): 15831-15835 (1986) [PubMed: ].Pazzani,C., Rosenow,C., Boulnois,G.J., Bronner,D., Jann,K. and Roberts,I.S. Molecular analysis of region 1 of the Escherichia coli K5 antigen gene cluster: a region encoding proteins involved in cell surface expression of capsular polysaccharide J. Bacteriol. 175 (18), 5978-5983 (1993) PubMed: 8397187 Jelakovic,S., Jann,K. and Schulz,G.E. The three-dimensional structure of capsule-specific CMP: 2-keto-3-deoxy-manno-octonic acid synthetase from Escherichia coli FEBS Lett. 391 (1-2), 157-161 (1996) PubMed: 8706906 ","","Thu Jan 9 13:37:45 2003","1","","","" "AA01957","1323527","1323351","177","ATGAATGGAAAATTATTAGAAATCATGGCATGCCCAAGCTGTCACGGACGTTTGGAATACGATGAACAACATCAACGTTTAATCTGTCGTTTTGAAAAAATCGCTTACCCGATTAAGAACGGCATTCCCGTATTACCGGCGGAACAGGCGCAGCCGTTAAATCAAGAACAGGATAAT","","","6775","MNGKLLEIMACPSCHGRLEYDEQHQRLICRFEKIAYPIKNGIPVLPAEQAQPLNQEQDN","1323351","","conserved hypothetical protein","Cytoplasm","This sequence is similar to gi|15602724, a predicted unknown from Pasteurella multocida. Also see gi|23467747 from Haemophilus somnus 129PT.","
InterPro
IPR005651
Family
Protein of unknown function DUF343
PF03966\"[2-41]TTrm112p


","No hits to the COGs database.","","Residues 5 to 51 match (8e-09) PD:PD052742 which is described as COMPLETE PROTEOME INNER RSC2531 YPO1399 MEMBRANE PA2980 CC0108 STY0989 ","","","","","","","","","","","","Thu Feb 26 08:40:46 2004","Thu Feb 26 08:40:46 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01957 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 08:40:46 2004","","","","","Residues 2 to 52 (E-value = 4.3e-14) place AA01957 in the DUF343 family which is described as Protein of unknown function (DUF343) (PF03966)","","","","","","","","1","","","" "AA01959","1324523","1323552","972","ATGCAGTTTTGGTATTCCCGCTCGTGGATCACATGGCTACTCTGCCCTTTCTCCTTGTTATTTTGGCTAATTACCGCCATTCGTCGCGCGCTCTTTCGTTTTAACTTGCTAAAATCCTATCGTGCGCCGGTTCCTGTGGTAGTCGTCGGCAATCTTTCCGTCGGCGGTAACGGCAAAACACCGGCAGTGATTTGGTTGGTACAGGAACTCAGCAAGCGCGGTTTAAAAGTCGGCGTGATTTCACGGGGCTACGGCAGCCAAGCCAAACATTATCCTTTGTTGGTTACGCCGCCCAGCGATCCTGTAGAAGCCGGCGATGAGCCCGTGTTGATCGCCACCCGTACCCAAGCGCCCGTTTGTATCTCACCCAACCGACAACAAGCCGTTGAATGCCTGTTAGAACACGCCCAATGCGATGTCATTATCAGCGATGACGGCTTGCAACATTATAAATTACAACGTGATATCGAAGTCGTCATCATGGACGCACAACGTGGTCTGGGTAACGGTTTCTTATTGCCTGCCGGACCGTTGCGCGAGTTGCCAAGCCGTTTAAAATCTGTCGATTTCGTCGTTACTAATGGCGCGGAAAACCAATACAGCGACGCGGTGATGACATTGCAACCACAGTATGCCGTCAATTTAGTCAACAAAGCACAGTACCCGTTAAAAGAATTCTCACAGGCAACCGCCATTGCCGGCATTGGCAATCCGCCGCGTTTTTTTGCCATGTTGCAACAACAGGGCATTATCTTAAGCGACATCAAAGCATTTCAAGATCACCAACGTTTCAGCGCGGATTTATTCAACCAATTCGATAAAAACCAACCGCTCCTGATGACGGAAAAAGATGCGGTAAAATGTCTTGCATTTGCACAGGAAAACTGGTGGTATGTGCCGGTGACGGCAGAAATTCACGGCGAAAAAGCCCGGCAATTGATTCAAAAGATCGTGCAAAAGTGCGGTGAAAAA","","","36338","MQFWYSRSWITWLLCPFSLLFWLITAIRRALFRFNLLKSYRAPVPVVVVGNLSVGGNGKTPAVIWLVQELSKRGLKVGVISRGYGSQAKHYPLLVTPPSDPVEAGDEPVLIATRTQAPVCISPNRQQAVECLLEHAQCDVIISDDGLQHYKLQRDIEVVIMDAQRGLGNGFLLPAGPLRELPSRLKSVDFVVTNGAENQYSDAVMTLQPQYAVNLVNKAQYPLKEFSQATAIAGIGNPPRFFAMLQQQGIILSDIKAFQDHQRFSADLFNQFDKNQPLLMTEKDAVKCLAFAQENWWYVPVTAEIHGEKARQLIQKIVQKCGEK","1323551","From InterPro: IPR003758Tetraacyldisaccharide-1-P 4'-kinase.Tetraacyldisaccharide 4'-kinase phosphorylates the 4'-position of a tetraacyldisaccharide 1-phosphate precursor (DS-1-P) of lipid A, but the enzyme has not yet been purified because of instability. This enzyme is involved in the synthesis of lipid A portion of the bacterial lipopolysaccharide layer (LPS).","tetraacyldisaccharide 4'-kinase","Cytoplasm, Inner membrane","Its nearest neighbor in the NR database is gi:16272033 from Haemophilus influenzae Rd KW20.","
InterPro
IPR003758
Family
Tetraacyldisaccharide-1-P 4'-kinase
PF02606\"[12-305]TLpxK
TIGR00682\"[17-323]TlpxK: tetraacyldisaccharide 4'-kinase
noIPR
unintegrated
unintegrated
signalp\"[1-30]?signal-peptide
tmhmm\"[9-27]?transmembrane_regions


","BeTs to 10 clades of COG1663COG name: Lipid A biosynthesis protein LpxK, tetraacyldisaccharide-1-P 4'-kinaseFunctional Class: NThe phylogenetic pattern of COG1663 is -------q------efghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit (1.4e-100) to 6/6 blocks of the IPB003758 family, which is described as \"Tetraacyldisaccharide-1-P 4'-kinase\". Interpro entry for IP:IPR003758. IPB003758A 20-56 4.6e-16 IPB003758B 68-112 1.6e-17 IPB003758C 117-154 1.8e-16 IPB003758D 158-196 7.8e-24 IPB003758E 230-242 6.3e-05 IPB003758F 280-301 4.2e-15 IPB003758A 22-58 0.02 IPB003758C 116-153 0.01","Residues 207 to 317 match (2e-07) PD:PD566385 which is described as LIPID A 4'-KINASE KINASE COMPLETE ATP-BINDING SYNTHESIS PROTEOME TRANSFERASE TETRAACYLDISACCHARIDE ","","","","","","","","","","","Wed Mar 16 11:03:36 2005","Wed Mar 16 11:03:36 2005","Wed Mar 16 11:03:36 2005","Wed Mar 16 11:03:36 2005","Wed Mar 16 11:03:36 2005","Wed Mar 16 11:03:36 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA01959 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Mar 16 11:03:36 2005","","","","","Residues 2 to 319 (E-value = 3.1e-132) place AA01959 in the LpxK family which is described as Tetraacyldisaccharide-1-P 4'-kinase (PF02606)","Wed Mar 16 11:03:36 2005","","","","Hashimoto M, Asai Y, Tamai R, Jinno T, Umatani K, Ogawa T.Chemical structure and immunobiological activity of lipid A from Prevotella intermedia ATCC 25611 lipopolysaccharide.FEBS Lett. 2003 May;543(1-3):98-102.PMID: 12753913Garrett TA, Que NL, Raetz CR.Accumulation of a lipid A precursor lacking the 4'-phosphate following inactivation of the Escherichia coli lpxK gene.J Biol Chem. 1998 May;273(20):12457-65.PMID: 9575203Garrett TA, Kadrmas JL, Raetz CR.Identification of the gene encoding the Escherichia coli lipid A 4'-kinase. Facile phosphorylation of endotoxin analogs with recombinant LpxK.J Biol Chem. 1997 Aug;272(35):21855-64.PMID: 9268317Reddi K, Poole S, Nair S, Meghji S, Henderson B, Wilson M.Lipid A-associated proteins from periodontopathogenic bacteria induce interleukin-6 production by human gingival fibroblasts and monocytes.FEMS Immunol Med Microbiol. 1995 Apr;11(2):137-44.PMID: 7640674","","Wed Mar 16 11:03:36 2005","1","","","" "AA01961","1326290","1324545","1746","ATGCAAGATCAAGACCTTTCCACCATGCAAACCTTCAAACGTTTATGGCCGATGATTAGCCCGTATAAAGCAGGTTTGATCGTTTCCGGTGTTGCGTTAGTATTAAACGCGTTAACCGATTCCGGCTTAATTTTCTTACTGAAACCCTTATTGGATGATGGTTTTGGCAAAGCTGACGCTTCTTTTTTAAAACAAATGTCGGTATTTGTGGTGCTGCTGATTCTCTTTCGCGGCATTTCCAGCTTTATTTCCAATTACTGTCTGGCATGGGTCTCCGGCAAAGTAGTGATGACCATGCGCCGCCGTTTGTTTAAACACTTAATGTTCATGCCGGTGAGTTTTTTCGACAGCAACTCTTCCGGTCGCTTACTTTCCCGCATTACTTACGATTCCGAAATGATCGCCAGCGCCTCCTCCGGTTCCCTCATTACCATCGTACGTGAAGGCGCATATTTGCTTTCCTTGCTCAGTATCATGCTTTACACCAGCTGGCAGCTTTCCTTGGTTTTATTTGTTATCGGACCGATTATCGGTATTTTAATTCGTATAGTTTCCAAGAAATTCCGTGAGCTAAGTCGCAATATGCAAAATTCTATGGGAGAACTGACCTCGACTACGGAACAAATGTTAAAAGGACATAAAGTAGTGCTTTCTTTCGGTGGGCAATTCATTGAAGAAGAACGCTTTAACCGTGTAAGTAACGATATGCGCCGTAAGGGTATGAAAATGACCGCCGCCGATGCCATTGCCGATCCTGTGGTACAGATTATCGCCTCTTTCGCCCTGGCTGCCGTACTTTATCTAGCCACTTTCCCCTCCATTATGGATCAGAACTTAAGTGCGGGTACATTTACCGTCGTTTTCTCCTCCATGCTTGCTTTAATGCGCCCGCTAAAATCCTTAACTAACGTGAATGCGCAATTCCAACGCGGCATGGCGGCGTGCCAAACCCTGTTCGGCATTTTGGATATGGACACAGAAAAAGACACCGGCACGTATAAAGCAGACAAGGTAAAAGGCGACGTTGAATTCAAAAATGTGACATTCAGCTACCAAGGGAAAGATGAACCCGCTTTAGACAATATTTCTTTCAAGATTCCGCACGGCAAAACCGTGGCATTGGTCGGGCGTTCAGGCTCCGGTAAATCTACTATCGCCAACTTAGTCACCCGTTTTTATGATATAAACCAAGGGGAAATTACGCTGGACGGCGTAAATATTCAGGATTATCGCCTGTCCGATTTACGCGAAAACTGCGCGGTGGTCTCCCAACAAGTGCATTTATTTAATGACACGATCGCCAACAACATTGCTTATGCGGCGAAAGACAAATACAGTCGTGAAGAAATCATCAAAGCGGCAAAAGCGGCGCACGCCATGGAATTTATCGAGCATTTGGAAAACGGTCTGGATACGGTTATCGGCGAAAACGGCGCCAGCTTATCCGGCGGTCAACGCCAGCGTTTAGCCATCGCCCGCGCCTTGTTGCGTAACTCGCCGGTATTGATTTTAGATGAAGCCACCTCGGCATTGGATACGGAATCCGAACGCGCAATTCAAGCGGCATTGGAAGAAATCCAAAAAGATCGCACGGTTTTGGTGATTGCCCATCGTTTATCCACCATCGAAAAAGCCGATGAAATTTTAGTCATCGAACACGGACAAATTAAAGAACGCGGCAACCACAAAACATTGTTGGAGCAAGGTGGTGCTTATAAACAATTGCACAGCATGCAATTCAGTCAA","","","64434","MQDQDLSTMQTFKRLWPMISPYKAGLIVSGVALVLNALTDSGLIFLLKPLLDDGFGKADASFLKQMSVFVVLLILFRGISSFISNYCLAWVSGKVVMTMRRRLFKHLMFMPVSFFDSNSSGRLLSRITYDSEMIASASSGSLITIVREGAYLLSLLSIMLYTSWQLSLVLFVIGPIIGILIRIVSKKFRELSRNMQNSMGELTSTTEQMLKGHKVVLSFGGQFIEEERFNRVSNDMRRKGMKMTAADAIADPVVQIIASFALAAVLYLATFPSIMDQNLSAGTFTVVFSSMLALMRPLKSLTNVNAQFQRGMAACQTLFGILDMDTEKDTGTYKADKVKGDVEFKNVTFSYQGKDEPALDNISFKIPHGKTVALVGRSGSGKSTIANLVTRFYDINQGEITLDGVNIQDYRLSDLRENCAVVSQQVHLFNDTIANNIAYAAKDKYSREEIIKAAKAAHAMEFIEHLENGLDTVIGENGASLSGGQRQRLAIARALLRNSPVLILDEATSALDTESERAIQAALEEIQKDRTVLVIAHRLSTIEKADEILVIEHGQIKERGNHKTLLEQGGAYKQLHSMQFSQ","1324544","From Genbank: [gi:1171029] This protein is involved in lipid A export and possibly also inglycerophospholipid export and for biogenesis of the outermembrane. Transmembrane domains (TMD) form a pore in the innermembrane and the ATP-binding domain (NBD) is responsible for energy generation.In msbA the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.","lipid A export ATP-binding/permease protein msbA","Inner membrane, Cytoplasm","","
InterPro
IPR001140
Domain
ABC transporter, transmembrane region
PF00664\"[22-298]TABC_membrane
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[481-523]TMSBA_HAEIN_P44407;
PF00005\"[369-554]TABC_tran
PS50893\"[342-578]TABC_TRANSPORTER_2
PS00211\"[481-495]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[368-555]TAAA
InterPro
IPR011527
Domain
ABC transporter, transmembrane region, type 1
PS50929\"[27-310]TABC_TM1F
InterPro
IPR011917
Family
Lipid A export ATP-binding/permease protein MsbA
TIGR02203\"[11-582]TMsbA_lipidA: lipid A export permease/ATP-bi
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[323-576]Tno description
PTHR19242\"[1-582]TATP-BINDING CASSETTE TRANSPORTER
PTHR19242:SF91\"[1-582]TLIPID A EXPORT ATP-BINDING/PERMEASE PROTEIN MSBA
signalp\"[1-81]?signal-peptide
tmhmm\"[25-47]?\"[68-88]?\"[164-184]?\"[248-270]?transmembrane_regions


","BeTs to 20 clades of COG1132COG name: ABC-type multidrug/protein/lipid transport system, ATPase componentFunctional Class: QThe phylogenetic pattern of COG1132 is -o--k-yqvdrlbcefghsnujxi-wNumber of proteins in this genome belonging to this COG is","Significant hit ( 5.7e-76) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 358-404 1.2e-26 IPB001140B 478-516 3e-29 IPB001140C 531-560 1.1e-17 IPB001140B 471-509 0.26","Residues 524 to 560 match (6e-08) PD:PD375591 which is described as ATP-BINDING ABC COMPLETE PROTEOME TRANSPORTER TRANSMEMBRANE MULTIDRUG RESISTANCE P-GLYCOPROTEIN GLYCOPROTEIN ","","","","","","","","","","","Thu May 13 15:01:32 2004","Thu May 13 15:01:32 2004","","","Thu May 13 15:01:32 2004","Thu May 13 15:01:32 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA01961 is paralogously related to AA02805 (5e-71), AA01393 (4e-56), AA01510 (1e-55), AA02609 (2e-48), AA01509 (4e-46), AA02606 (1e-41), AA02331 (4e-37), AA00415 (1e-25), AA01867 (6e-22), AA02440 (8e-22), AA00700 (8e-21), AA02718 (9e-20), AA02080 (2e-19), AA01616 (3e-19), AA00858 (8e-19), AA02353 (1e-18), AA01645 (1e-18), AA01684 (2e-18), AA01422 (4e-18), AA01524 (2e-16), AA02899 (1e-15), AA01824 (2e-15), AA02140 (3e-15), AA01656 (4e-15), AA01779 (7e-15), AA02786 (1e-14), AA00207 (1e-14), AA00799 (6e-14), AA02550 (1e-13), AA01051 (2e-13), AA02152 (3e-13), AA01456 (3e-13), AA02898 (6e-13), AA02320 (6e-13), AA01568 (1e-12), AA00751 (2e-12), AA02573 (3e-12), AA01757 (4e-12), AA02484 (1e-11), AA02324 (1e-11), AA00591 (1e-11), AA00933 (2e-11), AA01820 (3e-10), AA01555 (1e-09), AA02642 (1e-08), AA01947 (2e-08), AA02225 (2e-07), AA01569 (3e-07), AA01291 (4e-05), AA00061 (8e-05) and A02145 (2e-04).","Thu May 13 15:01:32 2004","","","","","Residues 369 to 554 (E-value = 1.3e-67) place AA01961 in the ABC_tran family which is described as ABC transporter (PF00005)","Thu May 13 15:01:32 2004","","","","Karow,M. and Georgopoulos,C. The essential Escherichia coli msbA gene, a multicopy suppressor of null mutations in the htrB gene, is related to the universally conserved family of ATP-dependent translocators. Mol. Microbiol. 7 (1): 69-79 (1993) PubMed: 8094880.Zhou,Z., White,K.A., Polissi,A., Georgopoulos,C. and Raetz,C.R. Function of Escherichia coli MsbA, an essential ABC family transporter, in lipid A and phospholipid biosynthesis. J. Biol. Chem. 273 (20): 12466-12475 (1998) PubMed: 9575204.Chang,G. and Roth,C.B. Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters. Science 293 (5536): 1793-1800 (2001) PubMed: 11546864].","","Wed Feb 5 14:58:06 2003","1","","","" "AA01962","1328766","1326340","2427","GTGAGCGTTTCGTTGGATAAGTTGGCTATAGCCCTGATTTTTAGCGGTTTAACATTATTGTTTTTGCCCGATCGCTTTTTATTATCGTGGCAAACGGCGTGCTATTTACTCCTCTTATTATGTCCACTCATGTTGCTTGCTTATGCCCTGCGACAGGACAAAATCAAGCAAATAGTAATGTGGCTACTGATCTTGATGATTCAGTCCGCTTACGTCCACCAATCGGCAATTTCCATACTGACCCAGGCGGATAATCTTGCCAATCTGCCGAAAACCGTTCACCGCGAATTTACCGTCAAGGAAATTCTGCATCAGCAGCATTATCAAACCCTGGTTATTCGCGCCAAACTCGCCGAAAATCTTCCCGAACAACGTATTTACGCGCAATGGAAACTCAAGCAACCAGTCAACCCCGGCGAACGTTACGCAGGCAATTTACGCTTGCGAGCGCTTTCTTCCCGCCTGAATTTTGACGGTTTTGACCGCCAGCCATGGTATTTCGGCAAGCACATCACCGCTTGGGCAGAGATTAAAAGTGCGGTCAAATTGGAAAACGTTTTTTCGTTACGCCAAACCGCTCTCAATCAAGCCTTACAACAAACGGAGAATTTACCCCGACAAGGCTTGTTGCTGGCACTCGGTTTTGGCGAACGTTTCCGCTTAGACCAAAAAACTTGGCAAATTTATCAAAAAACAAATACGGCGCATTTAATTGCCATTTCAGGGCTGCATATCGGACTGGCGATGATGCTGGGTTTTACCTTGGCGCGTCTACTGCAATTTGCCTTGCCGACGCGTTACATCAGCCCGACATTTCCGATTCTGTGCGGATTCATTTTTGCGTTGTTATACAGCCAACTGGCGGGGCTTGCTATTCCGACTTTACGCGCTATGATTGCGTTAGCCATGCTCTACGCGATTCAGTATTGGCGACGATATTGGACGGTATGGCAATTCTTGTTAAGAGTGGTTGCCTTGCTGATTTTTATCGATCCGCTCATGTTACTTTCCACCAGCTTTTGGTTGTCGGTGGGCGCAGTGACCTGTCTGATTGTTTGGTATCAGTATTTTCCGTTGTCTCTATTGCAATGGCGCGGCCATTCCCTTGCCAATTCGCCGTGGCGGAAAGTGCGGTATGTTTTCGGCTTGTTTCATTTGCAATTCGGTCTGCTCTGGCTGTTCACGCCCATTCAGCTGTTATTTTTTAACGGCATTTCGTTAAATAGTTTTATCGCCAATGTCATCGCAGTGCCGCCTTATAGCTTCGTTTTGGTCCCGTTGATGTTATTTGCCGTAGTCACCCAAGGTGCGTGGCATTCGTGGCAGCTCGCCAACGATTTGGCGGAAAAAATCACCGCACTTTTGACGCCCTGGCAGGATGACTGGTTGGCAATTTCCATTCCGCACAGTTTATGGATAACCCTATGTTTAACCTTTCTTTTTTTAGTGGCGCTCTATGTTATTTATAAACCGCCCAAACCGATAACATCCACTTTAGCATTGTCAAGGCAGCACCGCTTTAAAGGATTTCATTTTAATCCGGAACGCGCCTTAAGTTTACCGTTACGAAAAAGCGCTTATTGCGTGGGCGGTGGGCTGATTGCCCTGTGTTGCCTGACGTTAATTTCTCAGTCTATTTCACGTCCGAACTGGCAATTGGAAACCTTGGACGTGGGGCAAGGGTTGGCAACTTTAATCGTGAAAGACGGCAAAGGCGTGCTTTACGATACCGGCCCGAGTTGGAAGGGCGGCAGTATGGCACAATTGGAAATTCTGCCTTATTTACAACGGCAAGGCATTGATTTGGAATGGCTGATATTAAGCCATGACGACAACGATCACGCAGGTGGTGCCAAAGATATTTTAGCAATGTATCCCCATATTCAACTGACCACCGCTTCACAAAAGCGATATGGTTCCCAAAACACCGAAAAAAATGACCGCACTTTTTGTCAAGCCGGTAAACAATGGCATTGGCAGGGGTTGCATTTTACCGTGCTATCACCGGAGAATATCGTGCCCCGTGCGGAAAATCGGGATTCCTGCACACTTTTATTAACCGATGGCACGCACCATATTTTGCTGACGGGCGACGCGGATCTTAGCGTGGAATATAAGATCCTACCGAAACTTGGCAAAATCCATGTGTTACAAGTAGGGCATCACGGTAGCAAAACCTCGACGGGGCAGGCATTAGTGCAACATATTCAACCGGACATTGCGCTGATTTCCAGCGGACGCTGGAACCCATGGCATTTTCCCCATAAAGACGTGGTGGCGCGCCTGCAACAACAAGGATCACAAATTTATAATACGGCGCATAGCGGGCAAATCAGTCTATTGTTCTACAATGAAGAGATCAAAATTCAGACCGCGCGCGCTGAATTTTCGCCTTGGTATCGCAGATTGATTGGCTTGAGCACGAAA","","","92127","VSVSLDKLAIALIFSGLTLLFLPDRFLLSWQTACYLLLLLCPLMLLAYALRQDKIKQIVMWLLILMIQSAYVHQSAISILTQADNLANLPKTVHREFTVKEILHQQHYQTLVIRAKLAENLPEQRIYAQWKLKQPVNPGERYAGNLRLRALSSRLNFDGFDRQPWYFGKHITAWAEIKSAVKLENVFSLRQTALNQALQQTENLPRQGLLLALGFGERFRLDQKTWQIYQKTNTAHLIAISGLHIGLAMMLGFTLARLLQFALPTRYISPTFPILCGFIFALLYSQLAGLAIPTLRAMIALAMLYAIQYWRRYWTVWQFLLRVVALLIFIDPLMLLSTSFWLSVGAVTCLIVWYQYFPLSLLQWRGHSLANSPWRKVRYVFGLFHLQFGLLWLFTPIQLLFFNGISLNSFIANVIAVPPYSFVLVPLMLFAVVTQGAWHSWQLANDLAEKITALLTPWQDDWLAISIPHSLWITLCLTFLFLVALYVIYKPPKPITSTLALSRQHRFKGFHFNPERALSLPLRKSAYCVGGGLIALCCLTLISQSISRPNWQLETLDVGQGLATLIVKDGKGVLYDTGPSWKGGSMAQLEILPYLQRQGIDLEWLILSHDDNDHAGGAKDILAMYPHIQLTTASQKRYGSQNTEKNDRTFCQAGKQWHWQGLHFTVLSPENIVPRAENRDSCTLLLTDGTHHILLTGDADLSVEYKILPKLGKIHVLQVGHHGSKTSTGQALVQHIQPDIALISSGRWNPWHFPHKDVVARLQQQGSQIYNTAHSGQISLLFYNEEIKIQTARAEFSPWYRRLIGLSTK","1326339","[FUNCTION] Might contribute to transformation as a member of a membrane bound pore complex at the base of the transformasome. It could directly interact with transforming DNA during translocation indirectly by participating in the assembly of the pore. [SUBCELLULAR LOCATION] I","recombination protein rec2","Inner membrane, Cytoplasm","","
InterPro
IPR001279
Domain
Beta-lactamase-like
PF00753\"[560-747]TLactamase_B
InterPro
IPR004477
Domain
ComEC/Rec2-related protein
PF03772\"[213-487]TCompetence
TIGR00360\"[234-427]TComEC_N-term: ComEC/Rec2-related protein
InterPro
IPR004797
Family
DNA internalization-related competence protein ComEC/Rec2
TIGR00361\"[77-776]TComEC_Rec2: DNA internalization-related com
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[188-331]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.60.15.10\"[563-626]Tno description
signalp\"[1-47]?signal-peptide
tmhmm\"[5-23]?\"[29-49]?\"[59-79]?\"[236-256]?\"[266-284]?\"[290-310]?\"[320-340]?\"[346-364]?\"[374-394]?\"[400-418]?\"[423-441]?\"[469-489]?\"[526-546]?transmembrane_regions


","BeTs to 9 clades of COG0658COG name: Predicted multitransmembrane, metal-binding proteinFunctional Class: RThe phylogenetic pattern of COG0658 is -------qvdrlbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is","","Residues 71 to 144 match (2e-07) PD:PD128129 which is described as PROTEOME COMPLETE INNER TRANSMEMBRANE RECOMBINATION MEMBRANE REC2 ","","","","","","","","","","","Thu Jan 9 14:01:31 2003","Thu Jan 9 14:01:31 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01962 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 560 to 747 (E-value = 1.9e-14) place AA01962 in the Lactamase_B family which is described as Metallo-beta-lactamase superfamily (PF00753)","","","","","Clifton,S.W., McCarthy,D. and Roe,B.A. Sequence of the rec-2 locus of Haemophilus influenzae: homologies to comE-ORF3 of Bacillus subtilis and msbA of Escherichia coli. Gene 146 (1): 95-100 (1994) [PubMed: 8063112].Karow,M. and Georgopoulos,C. The essential Escherichia coli msbA gene, a multicopy suppressor of null mutations in the htrB gene, is related to the universally conserved family of ATP-dependent translocators. Mol. Microbiol. 7 (1): 69-79 (1993) [PubMed: 8094880].","","Thu Jan 9 14:01:31 2003","1","","","" "AA01963","1329064","1329498","435","ATGAGTAAAGCGTCTTTGAGTTTATTAGCTTTAGCCGGCGTTGAGCCGTACAAAGAAAAGAAAGGCGAAGAATACATGAATGAGCACCAAGTGCTGCATTTCAAGAAGATCCTTCAAGCCTGGCATGATCAAATTAGAGATGAAGCTTCTCGAACCGTAGCTCATATGCAGGACGAAGCGTCTAATTTCCCGGATCCATCCGACCGCGCCACACAGGAAGAAGAATTTAGCCTGGAGTTGCGTACCCGTGATCGTGAACGCAAATTAATGAAGAAAATCGAAAGCACCTTGAAAAAATTGGATACGGACGATTTCGGTTATTGCGAATCCTGTGGCGTAGAAATCGGTATTAAACGTTTAGAAGCGCGCCCAACCGCCGATCTTTGTATCGATTGCAAAACCCTGGCGGAAATTCGCGAAAAACAAATGGTGGGT","","","16703","MSKASLSLLALAGVEPYKEKKGEEYMNEHQVLHFKKILQAWHDQIRDEASRTVAHMQDEASNFPDPSDRATQEEEFSLELRTRDRERKLMKKIESTLKKLDTDDFGYCESCGVEIGIKRLEARPTADLCIDCKTLAEIREKQMVG","1329497","[FUNCTION] Dosage-dependent suppressor of a dnaK deletion mutation. It suppressed not only the temperature-sensitive growth but also the filamentous phenotype of the dnaK deletion strain, but the defect of lambda growth is not suppressed. ","dnaK suppressor protein","Cytoplasm","","
InterPro
IPR000962
Domain
Zinc finger, DksA/TraR C4-type
PR00618\"[108-119]T\"[120-132]TDKSAZNFINGER
PF01258\"[70-140]Tzf-dskA_traR
PS51128\"[65-145]TZF_DKSA_2
PS01102\"[108-132]TZF_DKSA_1
InterPro
IPR012784
Family
RNA polymerase-binding, DksA
TIGR02420\"[26-135]TdksA: RNA polymerase-binding protein DksA


","BeTs to 12 clades of COG1734COG name: DnaK suppressor proteinFunctional Class: TThe phylogenetic pattern of COG1734 is -------q----b-efghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 7.8e-18) to 1/1 blocks of the IPB000962 family, which is described as \"Prokaryotic dksA/traR C4-type zinc finger\". Interpro entry for IP:IPR000962. IPB000962 108-133 7.8e-18","Residues 83 to 139 match (4e-21) PD:PD189216 which is described as PROTEOME COMPLETE DNAK SUPPRESSOR ZINC-FINGER HOMOLOG DKSA PLASMID STRESS DNA-BINDING ","","","","","","","","","","","Thu Jan 9 14:06:17 2003","Thu Jan 9 14:06:17 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01963 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 70 to 140 (E-value = 1.3e-33) place AA01963 in the zf-dskA_traR family which is described as Prokaryotic dksA/traR C4-type zinc finger (PF01258)","","","","","Kang,P.J. and Craig,E.A. Identification and characterization of a new Escherichia coli gene that is a dosage-dependent suppressor of a dnaK deletion mutation J. Bacteriol. 172 (4), 2055-2064 (1990) PubMed: 2180916 Kang,P.J. and Craig,E.A. Identification and characterization of a new Escherichia coli gene that is a dosage-dependent suppressor of a dnaK deletion mutation. J. Bacteriol. 172 (4): 2055-2064 (1990) [PubMed: 2180916].Kawamukai,M., Utsumi,R., Takeda,K., Higashi,A., Matsuda,H., Choi,Y.L. and Komano,T. Nucleotide sequence and characterization of the sfs1 gene: sfs1 is involved in CRP*-dependent mal gene expression in Escherichia coli. J. Bacteriol. 173 (8): 2644-2648 (1991) [PubMed: 2013578].","","Thu Jan 9 14:06:17 2003","1","","","" "AA01965","1329618","1331081","1464","TTGAGCAAGAAAACGAAGAACAAAACCTCCGCTCAAAATGAAGTTAAAGTCTCGCCTAAAAAACAATCCGTTATTGAATCTGAACCTGTAAAAAACAAGGTTCAAGGTTCCTCCCGCAACAAAAAAAACACGCATAAAAAAGAATTCAAACACAGTATTAAAGCCTCAATGCACGGCATTACGCCGCGCATGATCAATCGCCATGCGTTGACCGTGGTGGAAAAATTACAACGCCAAGGCTATGAAGCCTATGTGGTCGGCGGCTGTTTGCGCGATTTATTGTTAGGCAAAAAACCAAAAGATTTTGATGTGGCGACCAATGCCCGCCCGGAACAGATTCAGGCGGTTTTTCAGCGTCAATGCCGTTTGGTGGGACGACGTTTCCGCCTGGCACACGTGATGTTCGGACGTGAAATTATTGAAGTCGCCACTTTCCGCGCCGGTCACATGGAACATCATAATGAAAAACTCGCTAAACAAAGCGAAGAAGGGATGTTACTGCGCGACAACGTATATGGCACTCTGGAGCAGGATGCGGAACGCCGCGATTTTAGTGTGAACGCGCTATATTACAATCCGCAGGACAACACCCTGAAAGACTATTTCAACGGTATTGAAGATTTAAAAAACGGCAAATTGCGTTTAATCGGTGATCCGGTGACCCGTTATCAGGAAGATCCGGTGCGGATGTTACGCTCCATTCGTTTTATGGCGAAGCTGGAAATGTTTTTGGATAAACCGAGCGAAGCGCCTATTAAAGAATTGTCACATTTATTAAAAAATATTCCGTCGGCACGCTTATTTGAAGAAAGCCTGAAATTGTTACAGGGCGGAAACGGCGTGAAAACCTATCGCTTATTGCGTCAATACGGCTTGTTTGAACAACTGTTTCCGCTACTACAAAATTACTTCACGGAGCGTGAAGACAGCATGGCGGAGAAAATGATTCTGCGTGCGCTAACCTCCACCGATGAACGTGTTGCCGATAAATTGCCGATTAATCCGGCGTTTTTATTTGCTGCATTTTTTTGGTATCCGTTACGTGAACGGGTGGAAATGCTAAAAAATGAAGGCGGTTTGAATAATTACGATGCCTATGCGTTGGCGTCTAATGATTTGTTGGATGTGTTGTGCAATGCCTTAGCCATTCCGCGCCGTCATACCGCAGTGATTCGCGACATTTGGTCGTTGCAGCTGCAATTTTTAAAACGTACCCCAAAATCCGTGCAACGTGTTATGGAGCAATCGAAATTCCGCGCAGGGTTTGATTTATTGGTGATGCGTGCGGAAATTGAGGGCGGGGAAGCTGTGGAATTATCCGCGTGGTGGCACGAATACCAATTCAGCAACGATAGCCAACGGCAGGATCTGGTTAAAGAATTACCAAGCCAGCCGAAAAAACGCAAATATCATTGTCGTAAACGTAGCTCCGCTACGAAAAACACGAATAAGGCTGCCCATGAA","","","56533","LSKKTKNKTSAQNEVKVSPKKQSVIESEPVKNKVQGSSRNKKNTHKKEFKHSIKASMHGITPRMINRHALTVVEKLQRQGYEAYVVGGCLRDLLLGKKPKDFDVATNARPEQIQAVFQRQCRLVGRRFRLAHVMFGREIIEVATFRAGHMEHHNEKLAKQSEEGMLLRDNVYGTLEQDAERRDFSVNALYYNPQDNTLKDYFNGIEDLKNGKLRLIGDPVTRYQEDPVRMLRSIRFMAKLEMFLDKPSEAPIKELSHLLKNIPSARLFEESLKLLQGGNGVKTYRLLRQYGLFEQLFPLLQNYFTEREDSMAEKMILRALTSTDERVADKLPINPAFLFAAFFWYPLRERVEMLKNEGGLNNYDAYALASNDLLDVLCNALAIPRRHTAVIRDIWSLQLQFLKRTPKSVQRVMEQSKFRAGFDLLVMRAEIEGGEAVELSAWWHEYQFSNDSQRQDLVKELPSQPKKRKYHCRKRSSATKNTNKAAHE","1331080","","poly(A) polymerase","Cytoplasm","","
InterPro
IPR002646
Domain
Polynucleotide adenylyltransferase region
PF01743\"[83-214]TPolyA_pol
InterPro
IPR010206
Family
Poly(A) polymerase, PcnB
TIGR01942\"[53-485]TpcnB: poly(A) polymerase
InterPro
IPR012222
Family
Poly-A polymerase/tRNA nucleotidyltransferase
PIRSF000814\"[14-479]TPoly(A) polymerase/tRNA nucleotidyltransferase
noIPR
unintegrated
unintegrated
G3DSA:1.10.3090.10\"[212-299]Tno description
G3DSA:3.30.460.10\"[52-211]Tno description
PTHR13734\"[98-318]TTRNA-NUCLEOTIDYLTRANSFERASE/POLY(A) POLYMERASE FAMILY MEMBER
PTHR13734:SF5\"[98-318]TPOLY(A) POLYMERASE


","BeTs to 18 clades of COG0617COG name: tRNA nucleotidyltransferase/poly(A) polymeraseFunctional Class: JThe phylogenetic pattern of COG0617 is ------yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 7.3e-42) to 4/4 blocks of the IPB002646 family, which is described as \"Poly A polymerase family\". Interpro entry for IP:IPR002646. IPB002646A 84-103 2.5e-12 IPB002646B 174-189 9.6e-08 IPB002646C 214-240 2e-15 IPB002646D 262-275 0.097","Residues 86 to 145 match (5e-11) PD:PD479582 which is described as AT5G23690/MQM1_4 ","","","","","","","","","","","","Thu Jan 9 14:10:46 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01965 is paralogously related to AA02742 (5e-14).","","","","","","Residues 142 to 306 (E-value = 3.2e-76) place AA01965 in the PolyA_pol family which is described as Poly A polymerase family (PF01743)","","","","","Liu,J.D. and Parkinson,J.S. Genetics and sequence analysis of the pcnB locus, an Escherichia coli gene involved in plasmid copy number control. J. Bacteriol. 171 (3): 1254-1261 (1989) [PubMed: 2537812].Cao,G.J. and Sarkar,N. Identification of the gene for an Escherichia coli poly(A) polymerase. Proc. Natl. Acad. Sci. U.S.A. 89 (21): 10380-10384 (1992) [PubMed: 1438224].Masters,M., March,J.B., Oliver,I.R. and Collins,J.F. A possible role for the pcnB gene product of Escherichia coli in modulating RNA: RNA interactions. Mol. Gen. Genet. 220 (2): 341-344 (1990) [PubMed: 1691435].Mohanty BK, Kushner SR. Residual polyadenylation in poly(A) polymerase I (pcnB) mutants of Escherichia coli does not result from the activity encoded by the f310 gene. Mol Microbiol. 1999 Dec;34(5):1109-19. PMID: 10594834 ","","Thu Jan 9 14:10:46 2003","1","","","" "AA01966","1331077","1331574","498","ATGAATAAGGTGTATGTCGCTTTAGGCAGTAATTTAGCGGATCCGCAAGCACAACTGGTCGCCGCATTACGGGCGATGAATCAATTGCCTGGCAGCCGTCTGATTAGCGTCAGTTCTTTTTATCAAAGCAAACCTCTCGGTCCGCAAGATCAGCCTGATTATGTCAACGCCGTCGCTTGCCTGGAAACGGCGCTTTCTCCCTTCGCATTGCTTGATGAATTACAACGTATTGAACAGGAACAAGGGCGTGTCCGTCTTCGTCGTTGGGGTGAGCGCACATTAGATCTGGATATTTTGCTTTACGCCGATCAAACCATTCAGTCGGAACGTCTGACTGTTCCCCATTATGATATGCACAATCGTGAATTTGTAATTATCCCGTTGGCGGAAATCGCACCTTCGTTTTCCTTGCCGAACGGGCAATCCATCAGGGAGTTAATGCAAAATTTTACCCATCATAAAATGGTGATTGTGAAAGAGAAGGGCGAGGTTGTGTTT","","","18801","MNKVYVALGSNLADPQAQLVAALRAMNQLPGSRLISVSSFYQSKPLGPQDQPDYVNAVACLETALSPFALLDELQRIEQEQGRVRLRRWGERTLDLDILLYADQTIQSERLTVPHYDMHNREFVIIPLAEIAPSFSLPNGQSIRELMQNFTHHKMVIVKEKGEVVF","1331573","[SIMILARITY] Belongs to the HppK family.","2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase","Cytoplasm","","
InterPro
IPR000550
Domain
7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase, HPPK
PF01288\"[5-132]THPPK
TIGR01498\"[4-133]TfolK: 2-amino-4-hydroxy-6-hydroxymethyldihy
PS00794\"[88-99]THPPK
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.560\"[2-158]Tno description
PTHR20941\"[40-146]TFOLATE SYNTHESIS PROTEINS
PTHR20941:SF2\"[40-146]T2-AMINO-4-HYDROXY-6-HYDROXYMETHYLDIHYDROPTERIDINE PYROPHOSPHOKINASE


","No hits to the COGs database.","Significant hit ( 2.3e-44) to 4/4 blocks of the IPB000550 family, which is described as \"7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase\". Interpro entry for IP:IPR000550. IPB000550A 4-18 1.8e-06 IPB000550B 51-74 6.8e-10 IPB000550C 78-101 6.3e-14 IPB000550D 111-128 1.8e-09","Residues 1 to 156 match (2e-56) PD:PD003866 which is described as PYROPHOSPHOKINASE COMPLETE PROTEOME FOLATE 2-AMINO-4-HYDROXY-6-HYDROXYMETHYLDIHYDROPTERIDINE TRANSFERASE HPPK SYNTHESIS PPPK 78-DIHYDRO-6-HYDROXYMETHYLPTERIN-PYROPHOSPHOKINASE ","","","","","","","","","","","Thu Jan 9 14:15:58 2003","Wed Jan 22 17:12:25 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01966 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 132 (E-value = 2.1e-69) place AA01966 in the HPPK family which is described as 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK) (PF01288)","","","","","Talarico,T.L., Dev,I.K., Dallas,W.S., Ferone,R. and Ray,P.H. Purification and partial characterization of 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase and 7,8-dihydropteroate synthase from Escherichia coli MC4100 Journal of bacteriology. 173 (21), 7029-7032 (1991) PubMed: 1657875 Talarico,T.L., Ray,P.H., Dev,I.K., Merrill,B.M. and Dallas,W.S. Cloning, sequence analysis, and overexpression of Escherichia coli folK, the gene coding for 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase. J. Bacteriol. 174 (18): 5971-5977 (1992)[PubMed: 1325970].Liu,J.D. and Parkinson,J.S. Genetics and sequence analysis of the pcnB locus, an Escherichia coli gene involved in plasmid copy number control. J. Bacteriol. 171 (3): 1254-1261 (1989) [PubMed: 2537812].","","Thu Jan 9 14:15:58 2003","1","","","" "AA01967","1331794","1331651","144","TTGCTTGACGACACGGAAAAACATGACATCAGCGTGGGTCAAGTGTTGAATTTTGGCGGCAAGCATTTTATTCAAGGGGAAGCGATGGAAGATACGGTGATTTTAGTCACCTTAGTCGGCGAACATCACGAACATAAGCACAAG","","","5385","LLDDTEKHDISVGQVLNFGGKHFIQGEAMEDTVILVTLVGEHHEHKHK","1331651","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 08:37:51 2004","Thu Feb 26 08:37:51 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01967 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 08:37:51 2004","","","","","","","","","","","","","1","","","" "AA01968","1332009","1331878","132","ATGAAAAAATTCATGCTGGGCATGGCATTAGGTCTCGGTATCACACTTAACGCCAATGCGGACATCGGTACGGTAAAAGAAGGCTCCGGCAAAATTTTGCAAGGCGATCAGTTTACCGTGGTAAAAAAGTAT","","","4670","MKKFMLGMALGLGITLNANADIGTVKEGSGKILQGDQFTVVKKY","1331878","","hypothetical protein","Periplasm, Cytoplasm, Extracellular","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-20]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 08:36:14 2004","Thu Feb 26 08:36:14 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01968 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 08:36:14 2004","","","","","","","","","","","","","1","","","" "AA01969","1332225","1332109","117","GTGGAAAATAGTACCATTACGATTCCGTATATTTTAAAGATCGCCCGGAGTTGCTGCACCCGACCTGTCAATAAATGTAAAACGCGGAAAAAAACGACCGCACTTTATATTAAAATA","","","4451","VENSTITIPYILKIARSCCTRPVNKCKTRKKTTALYIKI","1332109","","hypothetical protein","Cytoplasm, Extracellular","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 08:34:32 2004","Thu Feb 26 08:34:32 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01969 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 08:34:32 2004","","","","","","","","","","","","","1","","","" "AA01972","1334491","1332359","2133","ATGTCCCGTACTATTATTCTCATTCCGATTAGCACCGGCGTAGGTTTAACCAGTGTAAGCCTCGGTTTAATCAATGCCCTTGAACAAAAAGGCGCCAAAGTCGGCTTTATGAAACCAATTTCCCAACCGAACACCGGTGAGGATGTTATCGACCGCACCACCTCCATCGTGCGTACCAGCACCGCTTTAGAAACTGCCGAACCGTTTATGTTAAGCGTGGCGGAATCCTTAATCGGTCAAAATCAATCCGATGTGTTATTAGAAAAAATTGTTGAGAATCACCAAAAGCTGGCGAAAAACAACGAAATCGTGATCGTGGAAGGCTTGATTCCAACCCGTAAACATACCTTTGCCAACAGCATTAACTACGAAATAGCCCAAGCTCTTGATGCAGAAATCGTATTGGTCGCCGCCCCATCAACGGAAACTCCGACACAATTAAAAGAGCGCGTCGAAGCGGCTGCTTCATTATTCGGCGGTAAAAGCAATAAGAATCTCCTTGGTGTGATCGTCAACAAATTCAACGCACCGGTTGACGAATCCGGCAGAACACGCCCTGATTTAAGCGAAATTTTCGATTCCTTCCAACACAGTCACAACAGCGAGTCCGAACTTATCAGACTTTTCGCCCAAAGCACGATTAAACTATTAGCCTGCATTCCTTGGTCCGCCGATCTGATCGCCACCCGCGCTATTGATTTAATCAAGCATTTAGGCGCAGCGATTATGAATGAAGGCGATGTTAATCGTCGGATTCGCGGCATTACCTTCTGCGCCAGAAGTCTGCCGAACATGGTGGAACATTTCCGCGCAGGCAGCTTATTAGTGGTTTCCGCAGACCGGCCTGATGTCATCGTTGCGGCGGCGCTTGCCGTGTCTAATGACATTGAAATCGGCGGTTTACTATTAACCGGCGGTTACAAATTAGATCCGCAAATCAAAAAGCTTTGCCAACACGTGTTTGAAAGCAAAAAATTGCCGGTATTCCGCATTGAGGGTAACACCTGGCAAACCGCATTAAGCCTGCAAAGTTTCAACCTTGAAGTGCCGGTTGATGATAAAGAACGTATCGAAAACATCAAACGTTACACCGGTGAAAAATTAGATACGGCGTTTGTCAACGGATTAGTGGAAGCCTCGAGCCGTTTACGTCGCTTATCCCCGCCGGCATTCCGTTTCCAATTAACCGAATTAGCCCGCGCCGCCCAAAAACGCATCGTCTTACCGGAAGGCGACGAACCGCGCACCATTAAAGCGGCGATTTTATGTGCCGAACGCGGTATCGCAGAATGTGTGCTGTTAGCCAAACCGGAAGACGTACAACGCGTGGCGGAATCCCAAGGCGTTAAGTTGGTAAACGGCATTACCGTTATCGACCCGGCGAGCGTGCGTGAAAACTATGTGGCACGTTTGGTTGAGCTACGCAAAGCCAAAGGCATGACCGAAACCATGGCGCGTGAACAATTGGAAGACAATGTTGTGCTCGGTACCATGATGTTGGAAGCCAACCAAGTAGACGGTTTGGTATCCGGCGCCGTACACACCACCGCCAACACCATTCGCCCGCCAATGCAAATCATCAAAACCGCACCGGGCAGCTCCATTATTTCTTCCATCTTCTTCATGTTGCTACCGGATCAAGTATTGGTCTATGGCGATTGCGCAGTGAACCCGGATCCGACGGCAGAACAATTGGCGGAAATCGCCATTCAATCTGCCGAATCGGCAAAATCCTTCGGTATAGATCCGAAAGTGGCAATGATTTCCTACTCCACCGGTACATCAGGCAGCGGTGCTGACGTAGAAAAAGTGAAAGAAGCCACCCGCATTGCGAAGGAAAAACGCCCTGATTTACTCATCGACGGTCCGTTACAATATGACGCTGCGGTGATGGAAGACGTGGCTCGCTCTAAAGCGCCTAACTCACCGGTTGCCGGTCAAGCCACCGTCTTCATCTTCCCGGATTTGAATACCGGTAACACCACCTACAAAGCGGTTCAACGTTCCGCCGACCTCGTTTCCATCGGTCCGATGCTACAGGGTATGCGCAAACCGGTGAACGATTTATCCCGTGGCGCGCTAGTTGACGACATTGTGTACACCATTGCCTTAACCGCAATCCAAGCGACACAA","","","76935","MSRTIILIPISTGVGLTSVSLGLINALEQKGAKVGFMKPISQPNTGEDVIDRTTSIVRTSTALETAEPFMLSVAESLIGQNQSDVLLEKIVENHQKLAKNNEIVIVEGLIPTRKHTFANSINYEIAQALDAEIVLVAAPSTETPTQLKERVEAAASLFGGKSNKNLLGVIVNKFNAPVDESGRTRPDLSEIFDSFQHSHNSESELIRLFAQSTIKLLACIPWSADLIATRAIDLIKHLGAAIMNEGDVNRRIRGITFCARSLPNMVEHFRAGSLLVVSADRPDVIVAAALAVSNDIEIGGLLLTGGYKLDPQIKKLCQHVFESKKLPVFRIEGNTWQTALSLQSFNLEVPVDDKERIENIKRYTGEKLDTAFVNGLVEASSRLRRLSPPAFRFQLTELARAAQKRIVLPEGDEPRTIKAAILCAERGIAECVLLAKPEDVQRVAESQGVKLVNGITVIDPASVRENYVARLVELRKAKGMTETMAREQLEDNVVLGTMMLEANQVDGLVSGAVHTTANTIRPPMQIIKTAPGSSIISSIFFMLLPDQVLVYGDCAVNPDPTAEQLAEIAIQSAESAKSFGIDPKVAMISYSTGTSGSGADVEKVKEATRIAKEKRPDLLIDGPLQYDAAVMEDVARSKAPNSPVAGQATVFIFPDLNTGNTTYKAVQRSADLVSIGPMLQGMRKPVNDLSRGALVDDIVYTIALTAIQATQ","1332358","[CATALYTIC ACTIVITY] Acetyl-CoA + phosphate = CoA + acetyl phosphate. [PATHWAY] Last of two steps in the conversion of acetate toacetyl-CoA. [SUBCELLULAR LOCATION] Cytoplasmic (Potential).","phosphotransacetylase","Cytoplasm, Inner membrane","","
InterPro
IPR002505
Domain
Phosphate acetyl/butaryl transferase
PF01515\"[390-706]TPTA_PTB
InterPro
IPR004614
Domain
Phosphate acetyltransferase
TIGR00651\"[406-706]Tpta: phosphate acetyltransferase
InterPro
IPR010766
Domain
DRTGG
PF07085\"[233-345]TDRTGG
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[2-241]Tno description
PTHR23406\"[458-711]TMALIC ENZYME-RELATED
PTHR23406:SF3\"[458-711]TPHOSPHATE ACETYLTRANSFERASE
signalp\"[1-26]?signal-peptide
tmhmm\"[5-27]?transmembrane_regions


","BeTs to 15 clades of COG0280COG name: PhosphotransacetylaseFunctional Class: CThe phylogenetic pattern of COG0280 is -o------vdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is","Significant hit (2.8e-105) to 5/5 blocks of the IPB002505 family, which is described as \"Phosphate acetyl/butaryl transferase\". Interpro entry for IP:IPR002505. IPB002505A 508-542 1.1e-21 IPB002505B 551-573 3.9e-18 IPB002505C 583-592 3.9e-05 IPB002505D 616-659 1.7e-31 IPB002505E 676-708 8.6e-24","Residues 15 to 399 match (7e-07) PD:PD416269 which is described as TRANSFERASE PHOSPHATE PHOSPHOTRANSACETYLASE PROTEOME COMPLETE ACETYLTRANSFERASE ACYLTRANSFERASE ","","","","","","","","","","","Thu Jan 9 14:32:40 2003","Thu Jan 9 14:32:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01972 is paralogously related to AA00066 (1e-36).","","","","","","Residues 390 to 706 (E-value = 6.4e-180) place AA01972 in the PTA_PTB family which is described as Phosphate acetyl/butaryl transferase (PF01515)","","","","","Matsuyama,A., Yamamoto-Otake,H., Hewitt,J., MacGillivray,R.T. and Nakano,E. Nucleotide sequence of the phosphotransacetylase gene of Escherichia coli strain K12 Biochim. Biophys. Acta 1219 (2), 559-562 (1994) PubMed: 7918659 Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S. Identification and characterization of the ackA (acetate kinase A)-pta (phosphotransacetylase) operon and complementation analysisof acetate utilization by an ackA-pta deletion mutant ofEscherichia coli. J. Biochem. 116 (4): 916-922 (1994) [PubMed: 7883769].Matsuyama,A., Yamamoto,H. and Nakano,E. Cloning, expression, and nucleotide sequence of the Escherichia coli K-12 ackA gene. J. Bacteriol. 171 (1): 577-580 (1989) [PubMed: 2536666].","","Thu Jan 9 14:32:40 2003","1","","","" "AA01973","1335793","1334564","1230","TTGTTTAACTCAAACCAGTATAGGTCGTTTATGTCTGAAAAATTAGTCCTAATTCTCAATTGTGGTAGTTCCTCATTAAAATTCTCAATTCTTAATCCTGCAACAGGCGAAGAAAAATTATCCGGCTTAGCCGAAGCGTTTTATTTACCTGAAGCCCGTATTAAATGGAAATTGCACGGTGAAAAAGGGCAGGCAGATTTAGGTGCCGGTGCCGCTCACGCCGAAGCATTAAATTTCATTGTTAATAACATTTTCTCTCTTGATCCTGAATTACAAAAAGGCGTTGTAGCCATCGGTCATCGTATCGTACACGGCGGCGAAAAATTCACTTCTTCCGTTATTGTGACCGATGAAGTGGTCAAAGGCATTGAAGAAGCAATTCAATTCGCACCGCTGCACAACCCGGCACATTTAATCGGGATCAGAGAGGCTTTCAAATTATTCCCGCACCTGAAAGATAAAAATGTCGTGGTGTTCGATACCGCCTTCCATCAAACCATGCCGGAAGAAGCATTCCTATACGCATTACCATACTCTTTATACCGTGAACATGGCGTTCGTCGCTATGGCGCGCATGGTACCAGCCACTATTATGTCAGCCGTGAAGCAGCAAAACGGTTAGGTGTGCCGGAAGATAAAATCAACGTGATCACTTGTCATTTAGGTAACGGCGGTTCCGTATCGGCAATCCGTCACGGCAAATGTATCGACACCTCAATGGGTTTAACGCCATTGGAAGGTTTAGTGATGGGTACCCGTTCCGGCGACATCGACCCTGCTATTATTTTCTATATGCACGATACTTTGGGTATGTCCGTGAAAGAAATTAACGGTACGTTAACTAAGAAATCCGGTTTATTAGGCTTAACGGAAGTGACCAGTGACTGTCGTTATGCAGAAGATAATTATGAGAAAGAAATCCCGGCAAAACGCGCATTAGGTGTCTATTGCTATCGTTTAGCCAAATACATCGGTTCTTATATGGCGGTAATCGGTGAACGTCTGGATGCTATCGTGTTTACCGGCGGTATCGGTGAAAACTCCGCCCATGTGCGTGAAATCACCTTGGATCACTTAAAATTATTCGGTTACAAACTGGATCAAGAGAAAAATCTTGCCGCCCGTTTCGGTAAAGAAGGTATCATCACGGCCGATAACACTCCTATCGCTATAGTAATTCCAACCAACGAAGAGCTCGTTATCGCACAAGATACTGCACGTCTTTGTATT","","","45012","LFNSNQYRSFMSEKLVLILNCGSSSLKFSILNPATGEEKLSGLAEAFYLPEARIKWKLHGEKGQADLGAGAAHAEALNFIVNNIFSLDPELQKGVVAIGHRIVHGGEKFTSSVIVTDEVVKGIEEAIQFAPLHNPAHLIGIREAFKLFPHLKDKNVVVFDTAFHQTMPEEAFLYALPYSLYREHGVRRYGAHGTSHYYVSREAAKRLGVPEDKINVITCHLGNGGSVSAIRHGKCIDTSMGLTPLEGLVMGTRSGDIDPAIIFYMHDTLGMSVKEINGTLTKKSGLLGLTEVTSDCRYAEDNYEKEIPAKRALGVYCYRLAKYIGSYMAVIGERLDAIVFTGGIGENSAHVREITLDHLKLFGYKLDQEKNLAARFGKEGIITADNTPIAIVIPTNEELVIAQDTARLCI","1334563","[FUNCTION] Involved in the activation of acetate to acetyl CoA and the secretion of acetate. During anaerobic growth of the organism, this enzyme is also involved in the synthesis of most of the ATP formed catabolically. [CATALYTIC ACTIVITY] ATP + acetate = ADP + acetyl phosphate.[PATHWAY] Conversion of acetate to acetyl-CoA; first step.[SUBUNIT] Homodimer.[SUBCELLULAR LOCATION] Cytoplasmic.","acetate kinase","Cytoplasm","","
InterPro
IPR000890
Family
Acetate and butyrate kinase
PR00471\"[16-27]T\"[186-199]T\"[216-237]T\"[312-325]T\"[335-351]T\"[390-402]TACETATEKNASE
PTHR21060\"[16-410]TFAMILY NOT NAMED
PF00871\"[15-403]TAcetate_kinase
PS01075\"[16-27]TACETATE_KINASE_1
PS01076\"[216-233]TACETATE_KINASE_2
InterPro
IPR004372
Family
Acetate kinase
PIRSF000722\"[14-408]TAcetate/propionate kinase
PTHR21060:SF11\"[16-410]TSUBFAMILY NOT NAMED
TIGR00016\"[11-410]TackA: acetate kinase
noIPR
unintegrated
unintegrated
G3DSA:3.30.420.40\"[14-196]Tno description


","BeTs to 15 clades of COG0282COG name: Acetate kinaseFunctional Class: CThe phylogenetic pattern of COG0282 is --------vdrlbcefgh-nujx-twNumber of proteins in this genome belonging to this COG is","Significant hit ( 4e-112) to 9/9 blocks of the IPB000890 family, which is described as \"Acetate and butyrate kinase\". Interpro entry for IP:IPR000890. IPB000890A 16-27 1.3e-06 IPB000890B 97-107 3.8e-07 IPB000890C 129-141 4e-08 IPB000890D 156-177 5.9e-18 IPB000890E 186-199 5.5e-10 IPB000890F 219-257 4.5e-32 IPB000890G 280-291 0.00032 IPB000890H 336-347 8.9e-09 IPB000890I 393-402 1.4e-05","Residues 366 to 408 match (2e-13) PD:PD135366 which is described as KINASE ACETATE COMPLETE PROTEOME TRANSFERASE ACETOKINASE ACKA ACKA2 PLASMID ACKB ","","","","","","","","","","","Thu Jan 9 14:36:14 2003","Thu Jan 9 14:36:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01973 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 15 to 403 (E-value = 6.1e-235) place AA01973 in the Acetate_kinase family which is described as Acetokinase family (PF00871)","","","","","Kakuda,H., Hosono,K., Shiroishi,K. and Ichihara,S. Identification and characterization of the ackA (acetate kinase A)-pta (phosphotransacetylase) operon and complementation analysis of acetate utilization by an ackA-pta deletion mutant of Escherichia coli J. Biochem. 116 (4), 916-922 (1994) PubMed: 7883769 Kirkpatrick C, Maurer LM, Oyelakin NE, Yoncheva YN, Maurer R, Slonczewski JL. Acetate and formate stress: opposite responses in the proteome of Escherichia coli. J Bacteriol. 2001 Nov;183(21):6466-77. PMID: 11591692 Moir-Blais TR, Grundy FJ, Henkin TM. Transcriptional activation of the Bacillus subtilis ackA promoter requires sequences upstream of the CcpA binding site. J Bacteriol. 2001 Apr;183(7):2389-93. PMID: 11244084 ","","Thu Jan 9 14:36:14 2003","1","","","" "AA01974","1336031","1336471","441","ATGAGCTTTTTCAGCACTCTAAAAAGCGGTCAGCAATATTTGAAAACCTGGCCGTTAGAACCTAAACTCGGTGCGATTTTTCCGGAAAATCGTGTCATCAAAACCACATTATTTGCCCAAAAATTCATGCCGTTCTTGGCAGTGTTTTCTATTGTATGGCAACAATTTTATGCGCAAAGTGACGGGATTGCATTGGCGGTAGCGGTTCTGACAGCGTTATTTACGTTATTTTTACCTATGCAAGGCATTTACTGGTTGGGTAAGCGCGCCAAAACACCGTTACCACCAAAAAGTGCGGTCGGTTTTCAGCGCGTTTATGAGGCACTGAAAGAAAAACAGATGGCGTTGCCGATATGTCCCGAAAAGCCGACTTACTTTGATTTAGCGGTGTTGTTAAGACAGGCGCAACAAAAATTAGGACGGGATTTCTGGCAGGATCTT","","","16838","MSFFSTLKSGQQYLKTWPLEPKLGAIFPENRVIKTTLFAQKFMPFLAVFSIVWQQFYAQSDGIALAVAVLTALFTLFLPMQGIYWLGKRAKTPLPPKSAVGFQRVYEALKEKQMALPICPEKPTYFDLAVLLRQAQQKLGRDFWQDL","1336470","","conserved hypothetical protein","Periplasm, Inner membrane","","
InterPro
IPR007334
Family
Protein of unknown function DUF412
PF04217\"[1-147]TDUF412
noIPR
unintegrated
unintegrated
PD033645\"[1-147]TY703_PASMU_Q9CMV2;
tmhmm\"[37-57]?\"[63-83]?transmembrane_regions


","No hits to the COGs database.","","Residues 3 to 97 match (2e-24) PD:PD033645 which is described as COMPLETE PROTEOME TRANSMEMBRANE VC1099 CYTOPLASMIC YPO2564 HI1205 STY2566 YFBV ECS3179 ","","","","","","","","","","","","Thu Jan 9 14:38:21 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01974 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 147 (E-value = 3.3e-80) place AA01974 in the DUF412 family which is described as Protein of unknown function, DUF412 (PF04217)","","","","","","","","1","","","" "AA01976","1336653","1337192","540","ATGATTGATTACATTATTATCGGCATTATTGTTTTTTCCATTATTGTCAGTTTATTACGCGGTTTTGTCCGCGAAGTCATGTCACTAGCCAGCTGGATCGTGGCATTTTTAATTGCAAGCAATTTTTATATGTATCTTGCCGGACTCTTAACATCAATTGAGTCCGTTTATATTCGTAACGGCACGGCTATCGGTATTTTATTTATCGCTTCACTCATTGTCGGCGCCATTGTCAATTATGTCTTAGGGCAACTGGTAGATCGTACCGGGTTAAGCGGCACGGATCGTGTGCTCGGCGCCTGTTTCGGCTTATTACGCGGGGTTTTGATTGTTGCCGCTATGTTGTTTTTCTTAGATACATTTACCAGTTCAAATCAAACCGATTGGTGGAAAGAATCCAAATTAATACCGCACTTTCGTTTCGTGGTGGATTGGTTCTTCCAACAATTACAAGCCAATTCCGGTTTTTTAAATTCAACCCTGAACTTGGAGCAGATTGCCAATCCGGCAACAAATGCGGTTCCGGTTTCAACTACAAAC","","","19853","MIDYIIIGIIVFSIIVSLLRGFVREVMSLASWIVAFLIASNFYMYLAGLLTSIESVYIRNGTAIGILFIASLIVGAIVNYVLGQLVDRTGLSGTDRVLGACFGLLRGVLIVAAMLFFLDTFTSSNQTDWWKESKLIPHFRFVVDWFFQQLQANSGFLNSTLNLEQIANPATNAVPVSTTN","1337191","","colicin V production protein","Inner membrane, Cytoplasm","","
InterPro
IPR003825
Family
Colicin V production protein
PF02674\"[1-152]TColicin_V
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide
tmhmm\"[5-23]?\"[29-49]?\"[64-84]?\"[98-118]?transmembrane_regions


","BeTs to 10 clades of COG1286COG name: Uncharacterized membrane protein, required for colicin V productionFunctional Class: RThe phylogenetic pattern of COG1286 is ------------b-efghsnuj--t-Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Thu Jan 9 14:41:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01976 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 152 (E-value = 9.9e-58) place AA01976 in the Colicin_V family which is described as Colicin V production protein (PF02674)","","","","","Nonet,M.L., Marvel,C.C. and Tolan,D.R. The hisT-purF region of the Escherichia coli K-12 chromosome. Identification of additional genes of the hisT and purF operons. J. Biol. Chem. 262(25): 12209-12217.1987. PubMed: 3040734. Makaroff,C.A. and Zalkin,H. Regulation of Escherichia coli purF. Analysis of the control region of a pur regulon gene. J. Biol. Chem. 260(18): 10378-10387.1985. PubMed: 2991286. Fath,M.J., Mahanty,H.K. and Kolter,R. Characterization of a purF operon mutation which affects colicin V production. J. Bacteriol. 171(6): 3158-3161.1989. PubMed: 2542219.","","Thu Jan 9 14:41:24 2003","1","","","" "AA01978","1337317","1337195","123","ATGAAAAGTGCGGTGGGTTTTAAAAACATTTTTAAAACCCACCGCACTTTAAACACCTACCCCCGCCAACGTTCAAATAAATCCCGTTCCAAGGGGTATTCATCTGATCCCAACCAAATAGAC","","","4742","MKSAVGFKNIFKTHRTLNTYPRQRSNKSRSKGYSSDPNQID","1337195","","hypothetical protein","Cytoplasm, Extracellular","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 08:32:59 2004","Thu Feb 26 08:32:59 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01978 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 08:32:59 2004","","","","","","","","","","","","","1","","","" "AA01981","1339414","1337342","2073","ATGTCTATTAAAGAAAAACGCTTCGACCAAGCGGGTATCATGCCCTACTTTTTTGACGAACGCGGGCAGAAAATTCGTGCGCCGCTCGCCATCAAAAAAGCCTTGCTTTCCACTTTTGAAGGTCATATAAACAGCCGTACTCACCCGCTACCGCCGGTGAAAATTCTCCGCCAAAATCAACCGCACTTTTTATCGTTAAATGTTTCCGATGCCAGCCGTTCATGGCAAGGCAAATGGCAGCTTCACCTGGAAGACAATGCCGGCATCCTTGAAGGCAAAGTGAAAAAAAATAGCATAACCCTGCCACGCGATTTACCGTTGGGTTATCACGATCTGGTGTTGCACGGTGGAAAAGAAGAAGTACATTGCCGCCTTATCGTTGCGCCGCAGCGTTGTTATGAACCGGAAGCATTCGCCGAACAGAAAAAACTCTGGGGCAGTTTTATTCAGCTTTATACCCTGAAATCCGAGCGCAACTGGGGCGTGGGCGATTTCGGTGATTTGCAAGAATTTATTCGCGGGCTTGCGCCGTATCAGGCAGATTTTTTAGGCTTAAACCCGATTCATGCCCTCTTTCCGGGCAATCCCGATGGTGCCAGCCCGTATAGCCCGTCATCGCGCAAATGGCTGAACATCATTTACATCAACATAGATCAACTGCCGGAATTTCAACAAAGCGCAGAGGCGCAACGCTGGTTTAATTCGGCGGAAGTACAGGAAAAATTGAACGCCTTACGCGCCGCCGAATGGATTGATTACGCCGAGGTGATGGCGTTGAAATTGAAGGGGCTGCATTTTGCCTTTGCCGAATTTAAAGAAAATCCGACCGCACTTTCCCAACAAGCTTTTGCCGATTTCGTGCGCAACGGTGGCGAAAGTTTACAGGTGCAAGCCACTTTTGATGCGCTGCACGCCCATTTAAGCGCCCGATATCGCGAGCAATGGGGTTGGGATTTCTGGGCGCCGGAATTCCAAGATTATCATTCCGAGGTCGTCGCGCAATTCCGCCGTCAATATGGTGAGGAAATCGAATTTTATGCCTGGTTGCAATTCTGCGCCGACCAACAACTTGCCGAATGCGATGCCTTATGTAAAGCGCAACAAATGACCATCGGCATGTACCGCGACTTGGCGGTAGGCGTCACCGGCAGCGGTTCGGAAACCTGGAGCGATAAGGAATTGTACTGTCTGCGGGCGTCCGTGGGTGCGCCGCCGGATGTGTTAGGTCCGCAAGGACAAAACTGGGGCTTAACGCCGATGAACCCGCACATTCTGAAACAACGCGCTTATCAGCCGTTTATCGACTTGGTGCGCGCCAATATGAATCATTGCGGTGCATTGCGTATCGATCACATTATGTCGTTATTGCGTTTATGGTGGATCCCGAAAGGCGACAGCCCGGTCAACGGCGCCTATGTGCGTTATCCGGTCGATGATTTAATCGCCATTCTCGCCCTTGAAAGCCAACGTCGTCGCTGCGTGATTATCGGCGAAGATTTAGGCACCGTGCCGAAAGAAATCGTCAGCAAACTCAAAAATGCCGGCATTTTGTCTTACAAAATCTTCTATTTTGAATTTGATAAACAAGGACAAAGTCGTGACCTGCGGGACTATCCGTACCAAGCGATGACCACCCTAAGCACCCACGATCTGCCGACCATTAACGGTTATTGGCGCGGTTATGATTTTGAATTGGGGCAAAAATACGGTGTGTATCCGAACCCGCAAATTCTGGAAATCCTGAAAAAAGATCGCGTAAAAGCAAAAGCGGGCATTCTGCAACGCTTAAAAGAGCATGATATTGACGTGGACGCCGGCATCGACGAAACCTTGTCTTCCGATGTGAACAAAAAATTCGTCCATCAGCTACAATCTTACGTCGCCGAGGTCAACAGCGCCCTGTTCGGCTTCCAACCGGAAGACTGGCTGGGTATGACCGAACCGGTCAACATCCCGGGCACCAGTATGCAATACGCCAACTGGCGCCGCCGTTTAACGCAAAACACCGACGCAATTTTTGCCGATCAAGACATTCAGAAATTGCTGAAAGAAGTGAACGCTAAACGTAAAGGG","","","79002","MSIKEKRFDQAGIMPYFFDERGQKIRAPLAIKKALLSTFEGHINSRTHPLPPVKILRQNQPHFLSLNVSDASRSWQGKWQLHLEDNAGILEGKVKKNSITLPRDLPLGYHDLVLHGGKEEVHCRLIVAPQRCYEPEAFAEQKKLWGSFIQLYTLKSERNWGVGDFGDLQEFIRGLAPYQADFLGLNPIHALFPGNPDGASPYSPSSRKWLNIIYINIDQLPEFQQSAEAQRWFNSAEVQEKLNALRAAEWIDYAEVMALKLKGLHFAFAEFKENPTALSQQAFADFVRNGGESLQVQATFDALHAHLSARYREQWGWDFWAPEFQDYHSEVVAQFRRQYGEEIEFYAWLQFCADQQLAECDALCKAQQMTIGMYRDLAVGVTGSGSETWSDKELYCLRASVGAPPDVLGPQGQNWGLTPMNPHILKQRAYQPFIDLVRANMNHCGALRIDHIMSLLRLWWIPKGDSPVNGAYVRYPVDDLIAILALESQRRRCVIIGEDLGTVPKEIVSKLKNAGILSYKIFYFEFDKQGQSRDLRDYPYQAMTTLSTHDLPTINGYWRGYDFELGQKYGVYPNPQILEILKKDRVKAKAGILQRLKEHDIDVDAGIDETLSSDVNKKFVHQLQSYVAEVNSALFGFQPEDWLGMTEPVNIPGTSMQYANWRRRLTQNTDAIFADQDIQKLLKEVNAKRKG","1337341","","4-alpha-glucanotransferase","Cytoplasm","","
InterPro
IPR003385
Family
Glycoside hydrolase, family 77
PF02446\"[149-686]TGlyco_hydro_77
TIGR00217\"[101-687]TmalQ: 4-alpha-glucanotransferase
InterPro
IPR013781
Domain
Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80\"[139-688]Tno description


","No hits to the COGs database.","Significant hit ( 1.7e-67) to 6/6 blocks of the IPB003385 family, which is described as \"4-alpha-glucanotransferase\". Interpro entry for IP:IPR003385. IPB003385A 154-167 0.0002 IPB003385B 200-222 3.6e-10 IPB003385C 345-380 2.1e-08 IPB003385D 402-431 6.3e-15 IPB003385E 432-464 1.4e-18 IPB003385F 650-662 0.0016 IPB003385C 339-374 0.37","Residues 11 to 140 match (2e-10) PD:PD580875 which is described as TRANSFERASE 4-ALPHA-GLUCANOTRANSFERASE COMPLETE PROTEOME GLYCOSYLTRANSFERASE AMYLOMALTASE DISPROPORTIONATING CARBOHYDRATE ENZYME METABOLISM ","","","","","","","","","","","","Thu Jan 9 14:44:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01981 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 149 to 686 (E-value = 4.4e-159) place AA01981 in the 4a_glucanotrans family which is described as 4-alpha-glucanotransferase (PF02446)","","","","","Pugsley,A.P. and Dubreuil,C. Molecular characterization of malQ, the structural gene for the Escherichia coli enzyme amylomaltase. Mol. Microbiol. 2 (4): 473-479 (1988) [PubMed: 2845225].","","Thu Jan 9 14:44:28 2003","1","","","" "AA01982","1341914","1339527","2388","ATGCCTAAACAACGAACCTATGACAACGCATTTGATGCGATTGTCAAAAAATATTGCCGTTATTTTGATGTGCAATCAGCCAAACAATTCGCCCTCGACCAATGGTATCGCGTGATTGCCGAAGGCACTCTCGAACTGGCTTATGGCAAACCTGCAGCGAAAAAAAGCGGTCGCCATGTGAATTATCTTTCCATGGAATTTTTAATCGGTCGAATCACCGGCAATAATTTGATGAATCTCGGTTACTACGACGACATTAAAGCCTATTTGGCAAAATACGATGTGGAACTGGTAGATGTGTTGGAACAGGAGCGGGATCCCGCATTAGGTAACGGCGGTTTAGGTCGTTTGGCGGCGTGCTTTTTGGATTCCATGGCGGAGCTCGGACAAAACGCCACCGGCTACGGCTTGCATTACCAATACGGTTTATTTAAACAATCTTTTGAAGACGGTATGCAAAAAGAAAACGCTGATCTGTGGTCGCGCAACAGCTACCCATGGCACCGTTATAACCCGTCCAAAACGCAAAATATCGGCTTCGGCGGTAAAATCACGCCGATTAAAGGCGACAAATACGCTTGGGAGCCGAAACTCATCATTCAAGGCAAAGCCTTTGATTTGCCGATTGTCGGCTATAAGAATGATGTCCTCCAACCGCTGCGTTTATGGCAGGCGGACAGCGAACAATCATTCGATTTGGCGTTGTTCAACGACAGTAAATTCCTTAACGCGGATAAAACGATCGTCAATGCCACCGCACTTACTCAAGTGCTCTACCCGAACGACAACCACAAAGCGGGACAAAAATTGCGCTTAATGCAGCAATATTTCCACTGCGCCTGTTCCGTCGCCGATATTCTGGCGCGCCATTTTGCCGAAGGTCATGCGTTGAAAGACTTCGCCAAATATCAAGTGATTCAACTGAACGACACCCACCCGACCCTTGCCATTCCGGAATTAATGCGCGTGTTGTTGGATGAGCATGATCTCAGCTGGGACGACGCCTGGAAAATCTGTTCCCACACCTTTGCTTACACCAACCACACCTTATTGCCGGAGGCCCTGGAACAATGGGATCAACGTTTATTCAAACAATTACTGCCGCGCCATTTCCAAATTGTGGAAAAAATCAATAACCTCTTCCACGAAAAAGTGCGGTCGAAATTCGGTGCGGATCCGAAAGTGTGGGAAAAATTGGCGATTCTGTTCGACTACCGCGTGCGTATGGCGAATCTGTGCGTAGTGACCTGTTTCAAAGTCAACGGCGTAGCGCAAATTCACTCGGATTTGGTGGTCAGTGATTTGTTCCCGGAATACCACAAACTGTTCCCGACCAAATTCTGCAACGTCACCAACGGCATTACACCGCGTCGCTGGATCCAACAAGCCAACCCGAAATTAAGCGCGCTGTTGGATAAAACCCTGAAAAAAGACTGGGCGAAAGATCTGGAGTTGCTCAAAGGCGTGGAAAAATTTGTGGACGATGCGGCGTTCCGTGAAGAATATCGCGCCATTAAACATCACAATAAAGTGGTGTTAGCCGATGAAATTCAACGCACTTTAGGCTTCACCGTGAATACCGATGCGATTTTCGATATTCAAATTAAGCGTTTCCACGAATATAAACGCCAGCATCTGAATCTGTTAAACATTATCGCTACATACCAATCGCTGAAAGCCAATCCGAATCAGGATTACACCCCGCGCGTGTTCGTGTTTGCCGGTAAAGCGGCGCCGGGCTATTATCTGGCGAAAAATATTATTCACGCCATTAACAATGTGGCGGAGGTCATCAATAACGACAAAGCCATGAAAGATCGCCTGCAAGTGGCGTTCCTGCCGGATTATCGCGTCAGCCTGGCGGAAAAAATCATTCCGGCGGCGGACGTGTCCGAGCAGATTTCCATGGCGGGTAAAGAAGCCTCCGGCACCGGCAACATGAAGCTGGCGCTCAACGGCGCATTGACCTTAGGCACATTGGACGGCGCGAATGTGGAAATCGCCGAAATGGTGGGTGAAGAAAACGTGTTTATTTTCGGCCACACCGTAGAAAGCGTGCGCGAGTTATTAGCGAAAGGCTACAAACCGCGCGATTACTACAAACGCAATCCGGTGTTAAAAAGCGCTATGGATTTCTTAACCAAAGGCAAAGTCTGCCATGGCGACAAACAGATGTTTAAACTGATGCTGGACAGCCTGTTGAAGCATGACCCGTTCCTTGTACTTGCGGATTTCGACAGCTATGTCAACGCGCAACAAAAAATCGGCGAAGCCTATTTGGATCAGGATACCTGGTTACGCAGCGCCATTTTAAATACCGCACGTTTAGGCATGTTCAGCTCCGATCGTTCCATCCGCGATTATCAACAACGAATCTGGCTGAAAAAA","","","91111","MPKQRTYDNAFDAIVKKYCRYFDVQSAKQFALDQWYRVIAEGTLELAYGKPAAKKSGRHVNYLSMEFLIGRITGNNLMNLGYYDDIKAYLAKYDVELVDVLEQERDPALGNGGLGRLAACFLDSMAELGQNATGYGLHYQYGLFKQSFEDGMQKENADLWSRNSYPWHRYNPSKTQNIGFGGKITPIKGDKYAWEPKLIIQGKAFDLPIVGYKNDVLQPLRLWQADSEQSFDLALFNDSKFLNADKTIVNATALTQVLYPNDNHKAGQKLRLMQQYFHCACSVADILARHFAEGHALKDFAKYQVIQLNDTHPTLAIPELMRVLLDEHDLSWDDAWKICSHTFAYTNHTLLPEALEQWDQRLFKQLLPRHFQIVEKINNLFHEKVRSKFGADPKVWEKLAILFDYRVRMANLCVVTCFKVNGVAQIHSDLVVSDLFPEYHKLFPTKFCNVTNGITPRRWIQQANPKLSALLDKTLKKDWAKDLELLKGVEKFVDDAAFREEYRAIKHHNKVVLADEIQRTLGFTVNTDAIFDIQIKRFHEYKRQHLNLLNIIATYQSLKANPNQDYTPRVFVFAGKAAPGYYLAKNIIHAINNVAEVINNDKAMKDRLQVAFLPDYRVSLAEKIIPAADVSEQISMAGKEASGTGNMKLALNGALTLGTLDGANVEIAEMVGEENVFIFGHTVESVRELLAKGYKPRDYYKRNPVLKSAMDFLTKGKVCHGDKQMFKLMLDSLLKHDPFLVLADFDSYVNAQQKIGEAYLDQDTWLRSAILNTARLGMFSSDRSIRDYQQRIWLKK","1339526","[FUNCTION] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. [CATALYTIC ACTIVITY] {(1,4)-alpha-D-glucosyl}(N) + phosphate = {(1,4)-alpha-D-glucosyl}(N-1) + alpha-D-glucose 1-phosphate.[COFACTOR] Pyridoxal phosphate.[SUBUNIT] Homodimer.","maltodextrin phosphorylase","Cytoplasm","","
InterPro
IPR000811
Family
Glycosyl transferase, family 35
PIRSF000460\"[25-796]TGlucan phosphorylase
PTHR11468\"[54-793]TGLYCOGEN PHOSPHORYLASE
PF00343\"[90-796]TPhosphorylase
PS00102\"[640-652]TPHOSPHORYLASE
InterPro
IPR011833
Family
Glycogen/starch/alpha-glucan phosphorylase
TIGR02093\"[6-794]TP_ylase: glycogen/starch/alpha-glucan phosp
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2000\"[9-483]Tno description


","BeTs to 13 clades of COG0058COG name: Glucan phosphorylaseFunctional Class: GThe phylogenetic pattern of COG0058 is --m-k-yq-drlbcefgh---j-i--Number of proteins in this genome belonging to this COG is","Significant hit (4.4e-267) to 10/10 blocks of the IPB000811 family, which is described as \"Glycosyltransferase family 35\". Interpro entry for IP:IPR000811. IPB000811A 58-100 1.5e-16 IPB000811B 104-143 6.7e-30 IPB000811C 194-226 1.9e-11 IPB000811D 251-290 2.1e-22 IPB000811E 332-378 9.7e-32 IPB000811F 407-459 1.8e-36 IPB000811G 525-559 8.5e-21 IPB000811H 568-611 6.7e-25 IPB000811I 625-679 3.9e-46 IPB000811J 759-796 1.4e-16","Residues 404 to 502 match (2e-34) PD:PD002287 which is described as PHOSPHORYLASE GLYCOGEN METABOLISM GLYCOSYLTRANSFERASE TRANSFERASE PYRIDOXAL CARBOHYDRATE PHOSPHATE PROTEOME COMPLETE ","","","","","","","","","","","Thu Jan 9 14:50:21 2003","Thu Jan 9 14:50:21 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01982 is paralogously related to AA02094 (0.0).","","","","","","","","","","","Debarbouille,M., Cossart,P. and Raibaud,O. A DNA sequence containing the control sites for gene malT and for the malPQ operon. Mol. Gen. Genet. 185 (1): 88-92 (1982) PubMed: 6283313.Raibaud,O., Debarbouille,M. and Cossart,P. Clonage de la region malA de Escherichia coli K12: Sequence des nucleotides des regions regulatrices et des promoteurs,identification et purification de la proteine activatrice MalT. Ann. Inst. Pasteur Microbiol. 133, 59-63 (1982) Palm,D., Goerl,R. and Burger,K.J. Evolution of catalytic and regulatory sites in phosphorylases . Nature 313 (6002): 500-502 (1985) PubMed: 3155826.Palm,D., Goerl,R., Weidinger,G., Zeier,R., Fischer,B. and Schinzel,R. E. coli maltodextrin phosphorylase: primary structure and deletion mapping of the C-terminal site. Z. Naturforsch., C, J. Biosci. 42 (4): 394-400 (1987) PubMed: 3037809.Pugsley,A.P. and Dubreuil,C. Molecular characterization of malQ, the structural gene for the Escherichia coli enzyme amylomaltase. Mol. Microbiol. 2 (4): 473-479 (1988) PubMed: 2845225].","","Mon Feb 17 15:15:59 2003","1","","","" "AA01983","1342087","1344798","2712","ATGTTAATTCCATCAAAGTTAATTTGTTCTTATCGCCTGCAAAACAGTATTCAACGGGATCGTTTAACCCGCTTGCTGGACAAGGCGCATCTTTATCCGCTGGTGCTGATTCATGCGCCGGCAGGCTATGGCAAAACCACCTTAATTTCCCAATGGGTCGCCGGGCAGAAAAATGTCGGTTGGTATTCTTTAGATGAAAGCGATAATGAGGCGGAACGTTTCGCCACCTATTTCAGCGCGGCGTTGTATCGTGCTATCGGCGCGAAATCACCGATGGTTGAAGAAGGGTTTAATCAGGCGAATTTACTTTCTTCGTTAAATCAGTTGCTGATGAAGGTCTTGGATTTCAAGGAACATTTCTATTTGATTATCGATGACTACCACTTGATCGATAATGACGAAATTCATGACGCATTAAAGTATTGGATTCGCCATCAGCCGGAAAACATGACGCTGATTCTCATTTCCCGCGCCGTACCGCCGTTTGGCATTGCCGGCTTGCGGGTGCAGGAACAATTGCTGGAAATTGATATGCATCAGCTTTCTTTTAATCATCAGGAATCCCTCGCCTTTTTCCAATCCCGTTTAGGAAATGGACTGCCGGAACAGGAAATCATTGCGTTATGTAACGAAGTGGAAGGCTGGCCGACCGCACTTCAGCTGATTAGCTTATCCGCCAAACAGGCAATGGATAAATCCGGTGGCGTGTTGCCGTTGCAGGAAATGGAAAAACGGCTGGCAAAATTAAATAATTTCCACATTAACGAATATCTAAGCGATGAAGTGCTGAATCATGTGGATAACGAGACCCGCACCTTCGTGTTGCAATGTTCCATTTTGCGTTCCATGAATGAGAATCTGGTAAAAGAAGTCACAGGTTTGACCAATAGCCGCCGCAAACTGGAAGAATTGGAAAAGCAGGGTCTGTTTATTCAGCAAATGGATTCTGACGACAACTGGTGGCGTTTCCACCCGCTGTTTGCCTCTTTCTTGGCGCATTGTTGCGAACTGGAATTAACGGAACAACTGGAAGAATTGCACCGCCGCGCCGCCCAAGCCTGGTTAAAACTGGGCTATTTTACCGAAGCGCTTTATCACGCCATGCAGTTAAGCGATGTGTCCACATTATTGGTGATTTTACAACAGCACGCCTGGTATTTGTTTCATCAAGGTGAATTAAAGTTACTGGAAGAAAGTTTGAATCGCGTTGATTATGCAGTATTGATTCAACACCCGAATTTGGTATTACTGAAGGCGTGGTTGGTACAAAGTCAACACCGTCATGTAGAAGTGTCCGGTATTTTTGCTCATTTTCAGGATGCCTTGGCTGAACATAACGTACAAATGAGCAAAGAAAATCAGGCAGAATTTGACGTGCTGAAAGCACAGGTGGCGATTAACAGCGGAGATGAGAATACTGCCTTCTCTTTGGCTTCTAAAGCGCTAGCCGATTTATCAGAGAATTATTATTATGCACGTATTGTGGCAACTTCCATTATCGGCGAAGCTTACCATTGTTACGGCAACCTTAACGAAGCGTTAATTATGTTGCAAGGTGCGGAAAAAATGGCACGTCAACATCACGCTTATCACAATATTTTGTGGTCGCTGTTGCAACAATCGGAAATTCTCATGGCGCAAGGTTTCCTGCAAGCTGCTTACGATATGCTGGACAAAGCCGGTTTATTCGTGAAAGAAAATCATCTGCAAAAAGTGCCGATGTACGAGTTTTTACTCCGACTGAAAGGGCGTATTCTGTGGGAGTGGTACAATCTGGATAAAGCGGAAGCCATGGCAAATGCGGGTATCGCCGTGCTGAATGAACCGAAAGATAAATTACAGTGCATTGCTTTGTTGAGCAAAATTTCCCTAGTGCGCGGCGACTTGGACAATGCCACCCGTTTATTGCGGGAAGCGGAGCAGTTGCAAAATGCCTATAACCATCATCATGACTGGCTGGCAAATGTGGATCAGGTGAAATTATTTTTATGGCAAATGACTAATGACGAAGAAGCAGCACACAATTGGCTGATTCAAAATCAGCCGCCGGCAACTGATCGTAATCATTTTACTCAGGTTCAATGGCGCAATATCGTGCGTGCGCAAATGTTGGTGGGGCAGTTTGAAGAAGCCAAACAGATTCTGGATAAACTCATCGCCACGGCGGAAGAATATCATCTCACCAGCGATTTAAACCGTGCCTTGATATTGCGTAACCGTTGGTATTTCCTGCAGAACGAAAAACATTTAGCGCAAAAGGATTTAATCGAGGCGTTGCGTTTGGCGCGTCAAACCAATTTCATCAGCGCCTTTGTGATTGAAGGGGAGATGATGGCGCAACAAATTCGCCATTTGCTGCAATTAAACGTATTGGACGAACTTGCTTTGCATAAAGCGCAATTTATTTTGCGAAACATTAATCAATATTACCGTCATAAATTCGCTCATTTCGATGAACAGTTCGTCGCCAAGCTGCTTGCCAATCCGCAAGTGCCCGAGTTGCTCAAAATCAGCCCGCTCACGCAACGGGAGTGGCAGGTACTGGGGCTGATTTATTCCGGTTACAGCAATGAACAAATCTCCGATGAACTGCAAGTGGCAACCACCACTATCAAAACCCACATCCGTAATCTCTACCAAAAAATCGGCGTGGCAAACCGTAGTGAAGCCATTTCTTATACGAAAGATTTGTTGAAGCTGATGGGGTATATA","","","104563","MLIPSKLICSYRLQNSIQRDRLTRLLDKAHLYPLVLIHAPAGYGKTTLISQWVAGQKNVGWYSLDESDNEAERFATYFSAALYRAIGAKSPMVEEGFNQANLLSSLNQLLMKVLDFKEHFYLIIDDYHLIDNDEIHDALKYWIRHQPENMTLILISRAVPPFGIAGLRVQEQLLEIDMHQLSFNHQESLAFFQSRLGNGLPEQEIIALCNEVEGWPTALQLISLSAKQAMDKSGGVLPLQEMEKRLAKLNNFHINEYLSDEVLNHVDNETRTFVLQCSILRSMNENLVKEVTGLTNSRRKLEELEKQGLFIQQMDSDDNWWRFHPLFASFLAHCCELELTEQLEELHRRAAQAWLKLGYFTEALYHAMQLSDVSTLLVILQQHAWYLFHQGELKLLEESLNRVDYAVLIQHPNLVLLKAWLVQSQHRHVEVSGIFAHFQDALAEHNVQMSKENQAEFDVLKAQVAINSGDENTAFSLASKALADLSENYYYARIVATSIIGEAYHCYGNLNEALIMLQGAEKMARQHHAYHNILWSLLQQSEILMAQGFLQAAYDMLDKAGLFVKENHLQKVPMYEFLLRLKGRILWEWYNLDKAEAMANAGIAVLNEPKDKLQCIALLSKISLVRGDLDNATRLLREAEQLQNAYNHHHDWLANVDQVKLFLWQMTNDEEAAHNWLIQNQPPATDRNHFTQVQWRNIVRAQMLVGQFEEAKQILDKLIATAEEYHLTSDLNRALILRNRWYFLQNEKHLAQKDLIEALRLARQTNFISAFVIEGEMMAQQIRHLLQLNVLDELALHKAQFILRNINQYYRHKFAHFDEQFVAKLLANPQVPELLKISPLTQREWQVLGLIYSGYSNEQISDELQVATTTIKTHIRNLYQKIGVANRSEAISYTKDLLKLMGYI","1344797","[FUNCTION] MalT is the positive regulator of the E.coli maltose regulon. It binds and recognizes a DNA motif (called themalt box): 5'-gga[tg]ga-3'. It also binds maltotriose and ATP. ","maltose regulon positive regulatory protein","Cytoplasm, Inner membrane","","
InterPro
IPR000792
Domain
Bacterial regulatory protein, LuxR
PD000307\"[839-897]TMALT_PHOLL_Q7N976;
PR00038\"[840-854]T\"[854-870]T\"[870-882]THTHLUXR
PF00196\"[837-894]TGerE
SM00421\"[837-894]THTH_LUXR
PS50043\"[833-898]THTH_LUXR_2
PS00622\"[854-881]THTH_LUXR_1
InterPro
IPR001531
Family
Phospholipase C zinc-binding, prokaryotic
SM00770\"[368-564]Tno description
InterPro
IPR011990
Domain
Tetratricopeptide-like helical
G3DSA:1.25.40.10\"[442-812]Tno description
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[813-900]Tno description


","BeTs to 4 clades of COG2909COG name: ATP-dependent transcriptional regulatorFunctional Class: KThe phylogenetic pattern of COG2909 is ----------r---efg---------Number of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-19) to 1/1 blocks of the IPB000792 family, which is described as \"Bacterial regulatory protein, LuxR family\". Interpro entry for IP:IPR000792. IPB000792 840-886 1.1e-19","Residues 36 to 560 match (4e-07) PD:PD480557 which is described as REGULATION TRANSCRIPTION DNA-BINDING REGULATOR REGULATORY ALK PLASMID ATP-BINDING ALKB1GHJ ALKS ","","","","","","","","","","","Wed Feb 5 13:18:12 2003","Thu Jan 9 15:15:32 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01983 is paralogously related to AA00959 (5e-07).","","","","","","Residues 837 to 894 (E-value = 2.8e-23) place AA01983 in the GerE family which is described as Bacterial regulatory proteins, luxR family (PF00196)","","","","","Cole,S.T. and Raibaud,O. The nucleotide sequence of the malT gene encoding the positive regulator of the Escherichia coli maltose regulon. Gene 42 (2): 201-208 (1986) PubMed: 3015733.Debarbouille,M., Cossart,P. and Raibaud,O. A DNA sequence containing the control sites for gene malT and for the malPQ operon. Mol. Gen. Genet. 185 (1): 88-92 (1982) PubMed: 6283313. Richet,E. and Raibaud,O. MalT, the regulatory protein of the Escherichia coli maltose system, is an ATP-dependent transcriptional activator. EMBO J. 8 (3): 981-987 (1989) PubMed: 2524384.","","Wed Jan 29 13:55:21 2003","1","","","" "AA01984","1345814","1344957","858","ATGCAAAGCGAGCTGATTTCTTATAAAAAAATGCCTGTTTGGACTAAACACACATTGCCCAAAATGTTTCGGGAAAAACACAACACCAAAACCGGCACTTGGGGAAAAATCACTGTCTTAAAAGGAAAATTAAAATTTTATGTACTGACCGAAGACGGCGATTTGCTCAGCGAGCATATTTTCACCCCACAAGATGAAACGCCTTTTGTGGAACCGCAACTTTGGCACCGTGTAGAAGCACTATCAGACGATTTAGAATGTTTCCTTGAATTCTATTGTACAAAAGAAGACTATTTCAGCAAAAAATACAACATGACTGCCACCCACGGCGATGTGGTGGATGCTGCCAAAATCATCAAACCGTGCAAGGTGTTGGATTTAGGCTGCGGACAAGGACGTAATTCCCTTTATTTAAGTTTGCTCGGTTATGATGTGACCTCTTGGGATCACAATGAAAGCAGTCTCATGTTTTTAAATGAGATCAAAGAAAAAGAAAATCTGAATATTCAGACCGCACTTTACAACATCAACGATGCCAATATTCAAGAAAACTATGATTTCATCGTTTCCACGGTGGTCTTCATGTTCCTGGATCGCGACCGCATGCCGGTAATTATCGAAAATATACAAGACCGCACCAACCCGAATGGTTATAATTTAATCGTTGCCGCCATGTCTACAGCGGAAGTCCCTTGTCCACTGCCGTTTTCTTTCACCTTCGCCGAAGAAGAATTAAAACAATACTACAAAGACTGGGAATTTCTTGAGTACAACGAAGACATGGGCGAATTGCACAAAACCGATGAAAACGGCAATCGAATTAAAATGAAATTTGTGACAATGTTGGCAAGAAAGAAA","","","34049","MQSELISYKKMPVWTKHTLPKMFREKHNTKTGTWGKITVLKGKLKFYVLTEDGDLLSEHIFTPQDETPFVEPQLWHRVEALSDDLECFLEFYCTKEDYFSKKYNMTATHGDVVDAAKIIKPCKVLDLGCGQGRNSLYLSLLGYDVTSWDHNESSLMFLNEIKEKENLNIQTALYNINDANIQENYDFIVSTVVFMFLDRDRMPVIIENIQDRTNPNGYNLIVAAMSTAEVPCPLPFSFTFAEEELKQYYKDWEFLEYNEDMGELHKTDENGNRIKMKFVTMLARKK","1344956","","tellurite resistance protein; hemagglutinin homolog","Cytoplasm","","
InterPro
IPR004537
Family
Tellurite resistance methyltransferase, TehB-1
PF03848\"[91-282]TTehB
TIGR00477\"[49-285]TtehB: tellurite resistance protein TehB
InterPro
IPR015392
Domain
Protein of unknown function DUF1971
PF09313\"[9-90]TDUF1971
noIPR
unintegrated
unintegrated
PD331793\"[1-96]TTEHB_HAEIN_P45134;
G3DSA:3.40.50.150\"[112-221]Tno description
PTHR10108\"[111-231]TMETHYLTRANSFERASE


","BeTs to 14 clades of COG0500COG name: SAM-dependent methyltransferasesFunctional Class: Q,RThe phylogenetic pattern of COG0500 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 218 to 286 match (1e-29) PD:PD186997 which is described as RESISTANCE PROTEOME COMPLETE TELLURITE TEHB HEMAGGLUTININ ANTIBIOTIC TELLURIUM DNA-BINDING CONSERVED ","","","","","","","","","","","","Thu Jan 9 15:25:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01984 is paralogously related to AA02263 (2e-07).","","","","","","Residues 91 to 282 (E-value = 9.6e-155) place AA01984 in the TehB family which is described as Tellurite resistance protein TehB (PF03848)","","","","","Rao,V.K., Whitlock,J.A. and Proguske-Fox,A. Cloning, characterization and sequencing of two haemagglutinin genes from Eikenella corrodens. J. Gen. Microbiol. 139 (Pt 3): 639-650 (1993) [PubMed: 8473870].","","Thu Jan 9 15:25:29 2003","1","","","" "AA01985","1346207","1348861","2655","ATGTCAGAATTGTTAAAAAATGACGTAGATCCGATCGAAACTAACGATTGGTTGGCAGCAATTGATTCGTTAATTCGTGAAGAAGGTGTTGAGCGTGCGCAGTTCATTATTGATCAAGTGATGCAGCAAGCTCGTATTGGCGGCGTTTCTTTGCCGACAGGGATTACTACAGATTACGTGAATACGATCCCGGTTTCTGAACAGCCCGAGTATCCGGGAAATTTAGACATTGAGCGTCGTATTCGTTCTTATGTCCGCTGGAATGCTGTGATGATGGTGTTGCGCGGTCAGAAAAAAGACCTTGATTTAGGCGGTCACTTATCTACTTTCCAATCTGCTGCAACGGTTTATGAAGTTTGTTTTAATCATTTCTTCAAAGCCGCAACCGAGAAAAATGGCGGCGATTTGGTCTTCTTCCAAGGTCACGCTGCACCAGGTATGTATGCGCGCGCATTCCTAGAAGGTCGTTTGACCGAAGACCAATTAGACAATTTCCGTCAAGAAGTGCACGGCAAAGGTTTGTCTTCTTATCCGCATCCGAAATTAATGCCTGATTTTTGGCAATTCTCAACAGTATCTATGGGTTTAGGTCCGGTCAATGCGATTTATCAAGCCCGTTTCTTAAAATACTTGGAAAATCGCGGTTTGAAAGATACGGCTGATCAAAAAGTGTATGCTTTCCTGGGCGATGGCGAAATGGATGAAATTGAATCTAAAGGTGCATTGACATTTGCCGCCCGTGAACATTTGGATAACTTAATTTTTGTGATTTCCTGTAACTTACAACGCTTAGACGGACCGGTAAACGGTAACGGTAAAATCGTTCAAGAATTAGAAGGTTTATTCGTCGGCGCAGGTTGGGAAGTGATTAAAGTCATGTGGGGTAGCGGTTGGGATAAATTATTCGCCAAAGACACCACAGGCAAATTAACCCAATTAATGATGGAAGTGGTTGACGGGGACTACCTGACTTTCAAATCAAAAGATGGTGCCTATGTGCGCGAGCATTTCTTCGGTCGTTACCCTGAAACTGCCGCTTTAGTTGCCGACATGACAGATGATGAAATCTGGGCGTTAAGACGCGGTGGTCATGATTCGAAGAAAGTTTTTGCCGCATTCAAGAAAGCGCAAACAGCGGGCAAACCGGTGGTGATTTTAGTGCATTCCGTGAAAGGGTATAAAATTTCCGAAGCAGAAAGTAAAAACACTGCGCACCAATCCAAAAAAATGTCTATGGATAGCCTTAAAGCCTACCGTGATTACTTCCATATTCCGGTGAAAGACGAAGATTTGGAAAAACTGCCTTACATGACCTTCCCTGAAGGTTCGGACGAGTACAATTACTTGCACCAACATCGTAAAGCATTACAAGGATATTTACCGGCGCGTCAACCGAAATTTGACGTTGAATTTAAGGTGCCTGAGCTTAGCGAATTCGCACCGTTGTTAGGCGCACAACCACGTCCGATTTCAACTACAATGGCATTCGTCCGTTTCCTAAATACCTTATTGAAAGACAAAAATATCGGTAAAAACATTGTTCCGATCGTTGCGGATGAAGCCCGTACTTTTGGTATGGAAGGCTTGTTCCGTCAAGTGGGTATTTATAACCCGCACGGTCAAAACTATGTTCCTTCAGACCGCGACCTCGTGGCGTACTATCGTGAAGCGAAAGACGGTCAGGTATTGCAAGAAGGTATCAACGAATTAGGCGCGACATCTTCCTGGTTGGCTGCGGCAACCTCTTATTCCATCAGTAATGTGCCGATGATTCCGTTCTTTATTTATTACTCTATGTTCGGCTTCCAACGTGTGGGCGACTTATTGTGGGCAGCGGGCGACCAATTGGCGCGCGGCTTCATGATCGGCGGTACATCAGGTCGTACGACATTAAACGGTGAAGGTTTACAACACGAAGATGGTCACAGCCATATTCAATCCTTAATCATTCCGAACTGCGTGTCTTATGATCCGGCATTCGCTTATGAAGTGGCGGTAATAATGCAGGATGGTATCCACCGTATGTACGGCGAAAAACAAGAAGATGTGTTCTATTACATCACCACCTTAAACGAAATTTATGACCAACCGGCAATGCCTGCCGGTGCGGAAGACGGTATCCGTAAAGGTCTGTATAAATTTGAAAGCGTTGAGGGCAAAGGTAAAGGCGCCGTACAATTATTAGGTTCCGGCGCGATTTTACGTCATGTTCGCGAAGCGGCTCAAATCTTAGCGAAAGATTACGGCGTCAGTTCTGATGTTTATAGCGCGCCGTCTTTCACTGAAGCGGCTCGCGAAGGTGCCGACGCGGTACGTTGGAATATGTTACACCCAACCGAAACGCCACGTGTGCCATACGTTGCGCAAGTGATGAACGACAAACCGGCAGTGGCGGCAACGGATTACATGAAGCTGTTTGCCGAGCAAATTCGTGCCTATGTGCCGTCTAAACACTACCATGTGTTAGGTACCGACGGTTTCGGTCGTTCCGATAGCCGTGAAAACTTACGCGATCACTTTGAAGTCGATGCGCACCACGTCGTTGTTGCGGCATTAAACGTGTTGGTGCAAGAAGGCTCGGTTGATAAGAAAGTTGTTGCCGAAGCAATCGCTAAATACGGTATCGATCCTGAAAGATTGAACCCGCTATACGCA","","","98922","MSELLKNDVDPIETNDWLAAIDSLIREEGVERAQFIIDQVMQQARIGGVSLPTGITTDYVNTIPVSEQPEYPGNLDIERRIRSYVRWNAVMMVLRGQKKDLDLGGHLSTFQSAATVYEVCFNHFFKAATEKNGGDLVFFQGHAAPGMYARAFLEGRLTEDQLDNFRQEVHGKGLSSYPHPKLMPDFWQFSTVSMGLGPVNAIYQARFLKYLENRGLKDTADQKVYAFLGDGEMDEIESKGALTFAAREHLDNLIFVISCNLQRLDGPVNGNGKIVQELEGLFVGAGWEVIKVMWGSGWDKLFAKDTTGKLTQLMMEVVDGDYLTFKSKDGAYVREHFFGRYPETAALVADMTDDEIWALRRGGHDSKKVFAAFKKAQTAGKPVVILVHSVKGYKISEAESKNTAHQSKKMSMDSLKAYRDYFHIPVKDEDLEKLPYMTFPEGSDEYNYLHQHRKALQGYLPARQPKFDVEFKVPELSEFAPLLGAQPRPISTTMAFVRFLNTLLKDKNIGKNIVPIVADEARTFGMEGLFRQVGIYNPHGQNYVPSDRDLVAYYREAKDGQVLQEGINELGATSSWLAAATSYSISNVPMIPFFIYYSMFGFQRVGDLLWAAGDQLARGFMIGGTSGRTTLNGEGLQHEDGHSHIQSLIIPNCVSYDPAFAYEVAVIMQDGIHRMYGEKQEDVFYYITTLNEIYDQPAMPAGAEDGIRKGLYKFESVEGKGKGAVQLLGSGAILRHVREAAQILAKDYGVSSDVYSAPSFTEAAREGADAVRWNMLHPTETPRVPYVAQVMNDKPAVAATDYMKLFAEQIRAYVPSKHYHVLGTDGFGRSDSRENLRDHFEVDAHHVVVAALNVLVQEGSVDKKVVAEAIAKYGIDPERLNPLYA","1348860","[FUNCTION] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).[CATALYTIC ACTIVITY] Pyruvate + lipoamide = S-acetyldihydrolipoamide + CO(2).[COFACTOR] Thiamine pyrophosphate and magnesium ions.[SUBUNIT] Homodimer.","pyruvate dehydrogenase, E1 component","Cytoplasm","","
InterPro
IPR004660
Family
2-oxo-acid dehydrogenase E1 component homodimeric type
PIRSF000156\"[2-885]TPyruvate dehydrogenase, E1 component
TIGR00759\"[4-885]TaceE: 2-oxo-acid dehydrogenase E1 component
InterPro
IPR009014
Domain
Transketolase, C-terminal-like
G3DSA:3.40.50.920\"[709-885]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.970\"[71-468]Tno description
PTHR11624\"[112-292]TDEHYDROGENASE RELATED
PTHR11624:SF2\"[112-292]TTRANSKETOLASE


","BeTs to 8 clades of COG2609COG name: Pyruvate dehydrogenase, decarboxylase componentFunctional Class: CThe phylogenetic pattern of COG2609 is ---------dr---efghsn-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 3.2e-15) to 3/3 blocks of the IPB000360 family, which is described as \"Transketolase\". Interpro entry for IP:IPR000360. IPB000360A 105-116 1.1 IPB000360B 578-617 0.0048 IPB000360C 631-660 6.3e-08","Residues 293 to 338 match (6e-19) PD:PD009824 which is described as PYRUVATE DEHYDROGENASE COMPONENT E1 OXIDOREDUCTASE PYROPHOSPHATE GLYCOLYSIS PROTEOME COMPLETE THIAMINE ","","","","","","","","","","","Thu Jan 9 15:30:21 2003","Thu Jan 9 15:30:21 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01985 is paralogously related to AA01563 (8e-07).","","","","","","Residues 77 to 357 (E-value = 1.5e-06) place AA01985 in the Transketolase_N family which is described as Transketolase, thiamine diphosphate binding domain (PF00456)","","","","","Stephens,P.E., Darlison,M.G., Lewis,H.M. and Guest,J.R. The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the pyruvate dehydrogenase component. Eur. J. Biochem. 133 (1): 155-162 (1983) [PubMed: 6343085].Arjunan,P., Nemeria,N., Brunskill,A., Chandrasekhar,K., Sax,M., Yan,Y., Jordan,F., Guest,J.R. and Furey,W. Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution. Biochemistry 41 (16): 5213-5221 (2002) [PubMed: 11955070].","","Thu Jan 9 15:30:21 2003","1","","","" "AA01986","1348893","1350560","1668","GTGCTCGGCATGAAAAGTGCGGTCGGTTTTAAAAACATTTTTAAAGGTAAAAAAGAAATGGCTAAACAAATTCAAATCCCGGATATCGGTAGTGATGAAGTTACCGTAACCGAAGTGATGGTAAACGTTGGAGATAGCATCACTGCGGATCAATCCATTATTAATGTTGAAGGTGACAAGGCTTCTATGGAAGTGCCGGCACCGGAAGCGGGCGTGGTAAAAGAAATTTTAGTAAAAGTGGGCGACAAAGTGACTACCGGCACGCCGATGTTGGTGTTAGATAGTGCCGATGCCGCACCGGCTCAAGCGCCTCAAGCTGAGGCACCTGCACCGCAAGCCGCGCCTGCCGCCGCACAAGTGGTGGATGTTAATGTACCTGACATCGGCGGTGACGAAGTGAACGTGACCGATGTGATGGTGAACGTGGGTGATCGTGTTGAAGTGGATCAATCCATTATTAATGTTGAAGGTGATAAGGCTTCTATGGAAGTACCGGCACCGGTGGCGGGTATCGTTAAAGAAATTATTATCAAAGCCGGCGATAAAGTGTCCACAGGTACGTTAATCATGCGTTTTGAAACGGCGGGCAGTGCGCCTGCAGCTGCTCCGGTAGCTTCTTCGCCTGCTGCAGCGCCGGCACCGACTGAGCAAGCAGTACCACAAGCTGTACCTGCACCGACAGCACAGGCTTCCGCGCCGGCAGCCGCATCTTCTTCCCAAGCGGATGTTGAAAGTGCGAAAAGCTATGCGCACGCCACACCGGTGATTCGTCGTTTAGCGCGCGAATTCGGTGTGAACCTGGATAAAGTAAAAGGCACAGGTCGTAAGGGTCGTATTTTAAAAGAAGATATTCAAGCCTATGTGAAAGCCGCCGTGAAAGCTTTGGAAAGCGGTGCTGCGGCAACAGGCGCGGCGAATGGTGCCGGTTTAGGCTTGTTACCGTGGCCGAAAGTGGATTTCAGAAAATTCGGCGAAATCGAAGAAGTGGAATTAAGTCGTATCAACAAGATTTCGGGTGCGAATTTACATCGTAACTGGGTCATGATTCCGCATGTTACCCATTTCGATAAAGCGGACATCACCGAGTTGGAAGCATTCCGTAAAGAGCAAAACGCCTTGTCTGAAAAACAAAAACTGGGCGTGAAAATCACCCCTGTGGTCTTCATTATGAAAGCCGTTGCCAAAGCGTTGGAAGCCTTCCCGCGTTTCAACAGCTCCATTACCGAAGATGTCCAACGTTTGATCCTGAAAAAATACATCAATGTGGGCGTGGCGGTAGATACGCCGAACGGTTTAGTTGTACCGGTCTTTAAAGATGTCAACAAAAAAGGCATTATCGAGCTTTCCCGTGAATTGATGGAAGTGTCCAAAAAAGCCCGTGACGGTAAATTAACCGCAGCGGATATGCAAGGCGGTTGTTTCACCATTTCCAGCCTTGGCGGCATTGGTACAACACATTTTGCACCAATCGTGAATGCACCTGAAGTGGCGATTTTGGGTGTCTCCAAATCCGCTATGGAACCGGTTTGGAACGGTAAAGAATTTGTGCCGCGCTTGATTCTGCCGATTTCCTTATCCTTCGACCACCGTGTTATTGACGGTGCGGACGGTGCACGCTTCATCAGCTACATCGGTTCCGTATTAGCCGACTTACGTCGTTTAATTATG","","","58446","VLGMKSAVGFKNIFKGKKEMAKQIQIPDIGSDEVTVTEVMVNVGDSITADQSIINVEGDKASMEVPAPEAGVVKEILVKVGDKVTTGTPMLVLDSADAAPAQAPQAEAPAPQAAPAAAQVVDVNVPDIGGDEVNVTDVMVNVGDRVEVDQSIINVEGDKASMEVPAPVAGIVKEIIIKAGDKVSTGTLIMRFETAGSAPAAAPVASSPAAAPAPTEQAVPQAVPAPTAQASAPAAASSSQADVESAKSYAHATPVIRRLAREFGVNLDKVKGTGRKGRILKEDIQAYVKAAVKALESGAAATGAANGAGLGLLPWPKVDFRKFGEIEEVELSRINKISGANLHRNWVMIPHVTHFDKADITELEAFRKEQNALSEKQKLGVKITPVVFIMKAVAKALEAFPRFNSSITEDVQRLILKKYINVGVAVDTPNGLVVPVFKDVNKKGIIELSRELMEVSKKARDGKLTAADMQGGCFTISSLGGIGTTHFAPIVNAPEVAILGVSKSAMEPVWNGKEFVPRLILPISLSFDHRVIDGADGARFISYIGSVLADLRRLIM","1350559","[FUNCTION] The pyruvate dehydrogenase complex catalyzes theoverall conversion of pyruvate to acetyl-CoA and CO(2). Itcontains multiple copies of three enzymatic components:pyruvate dehydrogenase (E1), dihydrolipoamideacetyltransferase (E2) and lipoamide dehydrogenase (E3). [CATALYTIC ACTIVITY] Pyruvate + lipoamide =S-acetyldihydrolipoamide + CO(2). [SUBUNIT] Homodimer.","pyruvate dehydrogenase complex E2","Cytoplasm","","
InterPro
IPR000089
Domain
Biotin/lipoyl attachment
PF00364\"[22-93]T\"[121-192]TBiotin_lipoyl
PS50968\"[22-93]T\"[121-192]TBIOTINYL_LIPOYL
InterPro
IPR001078
Domain
Catalytic domain of components of various dehydrogenase complexes
PD001115\"[476-548]TQ8ZRT1_SALTY_Q8ZRT1;
PF00198\"[323-556]T2-oxoacid_dh
InterPro
IPR003016
Binding_site
2-oxo acid dehydrogenase, lipoyl-binding site
PS00189\"[44-73]T\"[143-172]TLIPOYL
InterPro
IPR004167
Domain
E3 binding
PF02817\"[252-288]TE3_binding
InterPro
IPR006256
Family
Dihydrolipoamide acetyltransferase
TIGR01348\"[22-556]TPDHac_trf_long: pyruvate dehydrogenase comp
noIPR
unintegrated
unintegrated
G3DSA:2.40.50.100\"[20-99]T\"[119-198]Tno description
G3DSA:3.30.559.10\"[312-556]Tno description
G3DSA:4.10.320.10\"[241-291]Tno description
PTHR23151\"[40-47]T\"[120-529]TDIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED
PTHR23151:SF19\"[40-47]T\"[120-529]TDIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX, E2


","BeTs to 17 clades of COG0508COG name: Dihydrolipoamide acyltransferasesFunctional Class: CThe phylogenetic pattern of COG0508 is -o-p-zy--drlbcefghsn-jxi-wNumber of proteins in this genome belonging to this COG is","Significant hit ( 6.6e-89) to 5/5 blocks of the IPB001078 family, which is described as \"2-Oxo acid dehydrogenase acyltransferase catalytic domain\". Interpro entry for IP:IPR001078. IPB001078A 138-170 1e-13 IPB001078B 254-284 5.7e-17 IPB001078C 382-403 1.6e-07 IPB001078D 459-501 1e-27 IPB001078E 520-556 1.1e-17Significant hit ( 1.8e-16) to 1/1 blocks of the IPB003016 family, which is described as \"2-oxo acid dehydrogenases acyltransferase component lipoyl binding site\". Interpro entry for IP:IPR003016. IPB003016 42-76 1.7e-16 IPB003016 141-175 2.2e-16Significant hit ( 5.6e-13) to 2/2 blocks of the IPB000089 family, which is described as \"Biotin / Lipoyl attachment\". Interpro entry for IP:IPR000089. IPB000089A 421-440 4.3e-07 IPB000089B 475-494 0.00037Significant hit ( 1.8e-07) to 2/3 blocks of the IPB002215 family, which is described as \"HlyD family secretion protein\". Interpro entry for IP:IPR002215. IPB002215A 59-95 1.7e-06 IPB002215B 163-197 41Significant hit ( 6.8e-05) to 1/8 blocks of the IPB001882 family, which is described as \"Biotin-requiring enzymes attachment site.\". Interpro entry for IP:IPR001882. IPB001882H 31-76 6.6e-05 IPB001882H 130-175 0.0003","Residues 314 to 340 match (2e-07) PD:PD073029 which is described as PYRUVATE COMPLETE PROTEOME COMPONENT DEHYDROGENASE DIHYDROLIPOAMIDE ACETYLTRANSFERASE LIPOYL TRANSFERASE ACYLTRANSFERASE ","","","","","","","","","","","Thu Jan 9 15:50:01 2003","Thu Jan 9 15:50:01 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01986 is paralogously related to AA02704 (1e-46), AA00183 (5e-07), AA02195 (6e-06) and AA01340 (5e-04).","","","","","","Residues 323 to 556 (E-value = 4e-116) place AA01986 in the 2-oxoacid_dh family which is described as 2-oxoacid dehydrogenases acyltransferase (catalytic domain) (PF00198)","","","","","Stephens,P.E., Darlison,M.G., Lewis,H.M. and Guest,J.R. The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component. Eur. J. Biochem. 133 (3): 481-489 (1983) [PubMed: 6345153].Hale,G. and Perham,R.N. Amino acid sequence around lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. Biochem. J. 187 (3): 905-908 (1980)[PubMed: 6821375].Russell,G.C. and Guest,J.R. Overexpression of restructured pyruvate dehydrogenase complexes and site-directed mutagenesis of a potential active-site histidine residue. Biochem. J. 269 (2): 443-450(1990) [PubMed: 2201286].Ali,S.T. and Guest,J.R. Isolation and characterization of lipoylated and unlipoylated domains of the E2p subunit of the pyruvate dehydrogenase complex of Escherichia coli. Biochem. J. 271 (1): 139-145(1990) [PubMed: 2121129].Rae,J.L., Cutfield,J.F. and Lamont,I.L. Sequences and expression of pyruvate dehydrogenase genes from Pseudomonas aeruginosa. J. Bacteriol. 179(11): 3561-3571, 1997. PubMed: 9171401. Hein,S. and Steinbuchel,A. Biochemical and molecular characterization of the Alcaligenes eutrophus pyruvate dehydrogenase complex and identification of a new type of dihydrolipoamide dehydrogenase. J. Bacteriol. 176(14): 4394-4408, 1994. PubMed: 8021225. Westphal,A.H. and de Kok,A. 1990. The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 2. Molecular cloning and sequence analysis of the gene encoding the succinyltransferase component. Eur. J. Biochem. 187(1): 235-239. PubMed: 2404760. Carlsson,P. and Hederstedt,L. 1989. Geneticcharacterization of Bacillus subtilis odhA and odhB, encoding 2-oxoglutarate dehydrogenase and dihydrolipoamide transsuccinylase, respectively. J. Bacteriol. 171(7): 3667-3672. PubMed: 2500417. ","","Thu Jan 9 15:50:01 2003","1","","","" "AA01987","1350680","1350555","126","TTGGGTTTTAATTTCTTTACTCATTTTTACCTCGTAAAAACGTTGAAATTTCTGACCGCACTTTTCGGCGATCAGTGTCAATGTAACAACGCCCCTCAATGCGAGAGGCGTAGCAAATTACATAAT","","","4934","LGFNFFTHFYLVKTLKFLTALFGDQCQCNNAPQCERRSKLHN","1350555","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-23]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 08:31:10 2004","Thu Feb 26 08:31:10 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01987 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 08:31:10 2004","","","","","","","","","","","","","1","","","" "AA01988","1350657","1352078","1422","ATGAGTAAAGAAATTAAAACCCAAGTGGTTGTACTTGGTGCAGGCCCTGCCGGTTATTCCGCCGCCTTCCGTTGTGCCGACTTAGGCTTAGAAACCGTCATTGTAGAACGTTATTCCACCCTTGGCGGTGTGTGCTTAAACGTCGGTTGTATTCCGTCTAAAGCCTTATTGCACGTTGCGAAAATTATTGAAGAAGCGAGACACGTTGAACATCACGGTGTGGTATTTGCCGAGCCAACAATCGATTTAGACAAAATCCGTGCCGGTAAAGAAGGCGTGGTTTCCCGCTTAACCGGCGGTTTGGCGAACATGGCGAAAATGCGTAAAGTGCAAGTGGTGCAAGGCGAAGCCAAATTTGCCGATTTCCACACTTTAGCGGTGACCGACAAAGACGGTAACGTCACCAGCGTGAAATTCGACAACGCCATTATTGCGGCGGGTTCACGTCCGATTGAACTTCCATTCATCCCTCATCACGATCCGCGTGTTTGGGATTCCACCGATGCCCTTGCTTTGCGTGAAGTGCCGAATGATTTGTTAATCATGGGTGGCGGTATCATCGGTTTGGAAATGGGTACTGTATATGAAGCCTTGGGTTCAAAAGTTGACGTGGTAGAAATGTTCGACCAGGTAATTCCGGCGGCGGACAAAGACATCGTCAAAATCTTCACCAAACGTATCGAGAAAAAATTCAACTTAATGCTTGAAACCAAAGTGACTGCAGTAGAAGCCAAACAAGACGGTATTTACGTTTCTATGGAAGGCAAAGCGGGCAACATCACTAACCGTTATGATGCAGTGTTGGTGGCGATTGGTCGTACCCCGAACGGCAAATTAATCGATGCGGAAAAAGCCGGCGTAAACGTTGATGAACGCGGTTTTATCCGTACTGACAAACAAATGCGTACCAACGTTTCCCACATTTTTGCTATCGGTGACATCGTAGGTCAACCGATGTTGGCACATAAAGGGGTACACGAAGGTCACGTTGCCGCCGAAGTGATTGCGGGTAAAAAACACTATTTCGACCCGAAAGTGATCCCGTCAATCGCTTACACCGAGCCGGAAGTAGCGTGGGTAGGTAAAACCGAGAAAGAATGTAAAGCCGAAGGCGTAAACTACGAAATCGCAAACTTCCCATGGGCAGCTTCCGGTCGTGCAATCGCTTCCGACTGCGCCGACGGTATGACCAAACTGATTTTCGATAAAGACACGCATCGCGTACTTGGCGGCGCCATCGTCGGCACCAATGCCGGTGAATTGTTAGGCGAAATTGGTCTTGCCATCGAAATGGGTTGTGACGCGGAAGACATCGCATTGACTATCCACGCCCACCCGACTTTACACGAATCTGTCGGTCTTGCGGCCGAAGTGTTTGAGGGGTCGGTCACCGACTTACCTAATCCAAAAGCGAAGAAAAAA","","","53738","MSKEIKTQVVVLGAGPAGYSAAFRCADLGLETVIVERYSTLGGVCLNVGCIPSKALLHVAKIIEEARHVEHHGVVFAEPTIDLDKIRAGKEGVVSRLTGGLANMAKMRKVQVVQGEAKFADFHTLAVTDKDGNVTSVKFDNAIIAAGSRPIELPFIPHHDPRVWDSTDALALREVPNDLLIMGGGIIGLEMGTVYEALGSKVDVVEMFDQVIPAADKDIVKIFTKRIEKKFNLMLETKVTAVEAKQDGIYVSMEGKAGNITNRYDAVLVAIGRTPNGKLIDAEKAGVNVDERGFIRTDKQMRTNVSHIFAIGDIVGQPMLAHKGVHEGHVAAEVIAGKKHYFDPKVIPSIAYTEPEVAWVGKTEKECKAEGVNYEIANFPWAASGRAIASDCADGMTKLIFDKDTHRVLGGAIVGTNAGELLGEIGLAIEMGCDAEDIALTIHAHPTLHESVGLAAEVFEGSVTDLPNPKAKKK","1352077","[FUNCTION] Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. [CATALYTIC ACTIVITY] Dihydrolipoamide + NAD(+) = lipoamide + NADH.[COFACTOR] FAD.[SUBUNIT] Homodimer.[SUBCELLULAR LOCATION] Cytoplasmic.","dihydrolipoamide dehydrogenase; lipoamide dehydrogenase","Cytoplasm, Periplasm","","
InterPro
IPR000815
Family
Mercuric reductase
PR00945\"[18-36]T\"[54-73]T\"[178-195]T\"[198-213]T\"[444-463]THGRDTASE
InterPro
IPR001100
Family
Pyridine nucleotide-disulphide oxidoreductase, class I
PR00411\"[8-30]T\"[41-56]T\"[142-151]T\"[178-203]T\"[265-279]T\"[308-315]T\"[343-364]T\"[408-423]T\"[430-450]TPNDRDTASEI
InterPro
IPR001327
Domain
Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PD000139\"[147-211]TQ9CMD7_PASMU_Q9CMD7;
PF00070\"[178-272]TPyr_redox
InterPro
IPR004099
Domain
Pyridine nucleotide-disulphide oxidoreductase dimerisation region
G3DSA:3.30.390.30\"[346-471]Tno description
PF02852\"[347-456]TPyr_redox_dim
InterPro
IPR006258
Family
Dihydrolipoamide dehydrogenase
TIGR01350\"[6-466]Tlipoamide_DH: dihydrolipoamide dehydrogenas
InterPro
IPR012999
Active_site
Pyridine nucleotide-disulphide oxidoreductase, class I, active site
PS00076\"[42-52]TPYRIDINE_REDOX_1
InterPro
IPR013027
Domain
FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PR00368\"[8-30]T\"[142-151]T\"[178-203]T\"[265-279]T\"[308-315]TFADPNR
PF07992\"[8-319]TPyr_redox_2
noIPR
unintegrated
unintegrated
G3DSA:3.50.50.60\"[4-339]Tno description
PTHR22912\"[10-463]TDISULFIDE OXIDOREDUCTASE
PTHR22912:SF20\"[10-463]TDIHYDROLIPOAMIDE DEHYDROGENASE-RELATED


","BeTs to 20 clades of COG1249COG name: Dihydrolipoamide dehydrogenase/glutathione oxidoreductase and related enzymesFunctional Class: CThe phylogenetic pattern of COG1249 is aomp-zyqvdrlbcefghsn-jxi-wNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-33) to 5/5 blocks of the PR00368 family, which is described as \"FAD-dependent pyridine nucleotide reductase signature\". Prints database entry for PR:PR00368. PR00368A 8-30 4.6e-10 PR00368B 142-151 0.65 PR00368C 178-203 8.8e-09 PR00368D 265-279 1.7e-05 PR00368E 308-315 0.12Significant hit ( 2.5e-14) to 3/5 blocks of the IPB000103 family, which is described as \"Pyridine nucleotide-disulphide oxidoreductase class-II\". Interpro entry for IP:IPR000103. IPB000103A 8-28 3.6e-05 IPB000103D 266-277 0.17 IPB000103E 303-340 0.00048Significant hit ( 2.3e-10) to 1/1 blocks of the IPB001100 family, which is described as \"Pyridine nucleotide-disulphide oxidoreductase, class I\". Interpro entry for IP:IPR001100. IPB001100 42-56 2.4e-10Significant hit ( 2.3e-08) to 1/5 blocks of the IPB000171 family, which is described as \"Bacterial-type phytoene dehydrogenase\". Interpro entry for IP:IPR000171. IPB000171A 10-40 2.3e-08 IPB000171A 180-210 0.16","Residues 82 to 132 match (7e-07) PD:PD459598 which is described as DEHYDROGENASE OXIDOREDUCTASE DIHYDROLIPOAMIDE FAD FLAVOPROTEIN COMPLETE PROTEOME CENTER REDOX-ACTIVE E3 ","","","","","","","","","","","Fri Jan 10 10:13:59 2003","Fri Jan 10 10:13:59 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01988 is paralogously related to AA01306 (5e-43) and AA02604 (1e-04).","","","","","","Residues 347 to 456 (E-value = 1.2e-50) place AA01988 in the Pyr_redox_dim family which is described as Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain (PF02852)","","","","","Stephens,P.E., Lewis,H.M., Darlison,M.G. and Guest,J.R. Nucleotide sequence of the lipoamide dehydrogenase gene of Escherichia coli K12. Eur. J. Biochem. 135(3): 519-527, 1983. PubMed: 6352260. Cunningham L, Georgellis D, Green J, Guest JR. Co-regulation of lipoamide dehydrogenase and 2-oxoglutarate dehydrogenase synthesis in Escherichia coli: characterisation of an ArcA binding site in the lpd promoter. FEMS Microbiol Lett. 1998 Dec 15;169(2):403-8. PMID: 9868788 Guillen G, Alvarez A, Silva R, Morera V, Gonzalez S,Musacchio A, Besada V, Coizeau E, Caballero E, Nazabal C,Carmenate T, Gonzalez LJ, Estrada R, Tambara Y, Padron G,Herrera L. Expression in Escherichia coli of the lpdA gene, proteinsequence analysis and immunological characterization of theP64k protein from Neisseria meningitidis. Biotechnol Appl Biochem. 1998 Jun;27 ( Pt 3):189-96. PMID: 9664678 Steiert,P.S., Stauffer,L.T. and Stauffer,G.V. The lpd gene product functions as the L protein in the Escherichia coli glycine cleavage enzyme system. J. Bacteriol. 172 (10): 6142-6144 (1990) PubMed: 2211531.","","Wed Jan 29 13:19:32 2003","1","","","" "AA01989","1352179","1352301","123","GTGCGGTCGGAATTGAGTGAAAAATCTGCAGTTTGTTTGCTGCGATTGGCAATGGTCAGCTGTGATGGGTTAATGGGTGATTTATCTCAATACTTGGGTTTACCACGTGGGGCAACGTTTGAT","","","4385","VRSELSEKSAVCLLRLAMVSCDGLMGDLSQYLGLPRGATFD","1352301","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 08:29:48 2004","Thu Feb 26 08:29:48 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01989 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 08:29:48 2004","","","","","","","","","","","","","1","","","" "AA01991","1353063","1352512","552","ATGGACGCATTACAATTACTCACCGAACGCAGTTCGGAAAAAAAACTCAACGCCCCCGCCCCGACGCCTCAACAATTGGATCTGATCTTTCAGGCAGCATTACGCGCGCCGGATCACGGCAAACTGCAACCTTATCGTTTTATCGTCATTGAACAAGCCAAAATGAATAACTTCAGCGAGTTACTAAAAGATGCCGTGCAGGAATTCGACCTTGGCGAAGAACGCTTGAAAAAAGCGGAAAATCTGGCTACCCGAGCACCAATGATTATCGGCGTGGTGGCGAAATTGGATCCGAGCATTAAAAAAGTGCCGAAATGGGAGCAGTTACTCTGCGCAGGTTGCGCCACTTACGCCATTCAACTGGCCTCCAACGCCTTAGGCTTTAAAAATGTTTGGATCAGCGGTCCGTGGCTGGACGGTGCCGCATTGCGTGAAGCTTTCCACTGTTCGGCACAGGACAAAATTATCGGTTTCGTCATGATCGGTTCCGCCGAAGAAAAAACGGAACGGGAGAAAAAAGCCGTTAATTGCAGTGAGTTGGTCAGTTATTTC","","","20433","MDALQLLTERSSEKKLNAPAPTPQQLDLIFQAALRAPDHGKLQPYRFIVIEQAKMNNFSELLKDAVQEFDLGEERLKKAENLATRAPMIIGVVAKLDPSIKKVPKWEQLLCAGCATYAIQLASNALGFKNVWISGPWLDGAALREAFHCSAQDKIIGFVMIGSAEEKTEREKKAVNCSELVSYF","1352511","","conserved hypothetical protein (possible nitroreductase)","Cytoplasm, Periplasm","","
InterPro
IPR000415
Family
Nitroreductase
PF00881\"[7-163]TNitroreductase
noIPR
unintegrated
unintegrated
G3DSA:3.40.109.10\"[1-183]Tno description
PIRSF000232\"[1-184]TNADH dehydrogenase/NAD(P)H nitroreductase


","BeTs to 14 clades of COG0778COG name: NitroreductaseFunctional Class: CThe phylogenetic pattern of COG0778 is aompkz-qvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 8.6e-08) to 2/2 blocks of the IPB000415 family, which is described as \"Nitroreductase family\". Interpro entry for IP:IPR000415. IPB000415A 37-49 0.0015 IPB000415B 118-136 0.025","Residues 113 to 171 match (2e-07) PD:PD523563 which is described as PROTEOME COMPLETE VC1048 ","","","","","","","","","","","","Fri Jan 31 15:35:58 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01991 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 163 (E-value = 2.1e-35) place AA01991 in the Nitroreductase family which is described as Nitroreductase family (PF00881)","","","","","","","","1","","","" "AA01992","1353169","1355064","1896","TTGATTTCCCGAGGTTATATGAAAGTTATTTTTTCGATTATTAAATTTGCCTGGCGCACATTAAATTTTATTCGTGATTTGGTCATGAATATTGTGTTTCTGGTTTTCGTTTTATTATTGCTGACTGCGCTGCCTTTCGTGGTTGGGCTGGATAAACAAACTGTGGCGTTAAAAGGCGATCAGGGGGCGTTGTATTTAAACCTGGATGGCTATTTGGCGGACAATCGCGATAATCAAGGTGGCGTAAAAACGCTTTTAAAAGAACTGGATAATCAACATATTCCACAACAATATTCCACTTTTGATGTAGTTTACGCTATTGATTCGGCCGCACTGGACGACAAGGTTCGCGGTTTGGTGCTGGATTTGAATTATTTTCAAGGTGGCGATTTACCTTCATTGGAATTTGTGGGTGCTTCCATTGAAAACTTCAAGAAAAACGGCAAGCAGGTTATTGCGTATTCCGATAATTACAATCGGGCGCAATATTTTTTGGCCAGCTATGCCGATGAAGTTTATATGAATCCGGTAGGAACGGTATCTATTGATGGCTTGGTGCAGGAAAATCTGTATTACAAAGATCTGCTGGATAGCTTGGAGGTGAACCCGCACGTTTTCCGCGTAGGCACTTACAAATCCGCCGTCGAACCGTTTTTGCGCAACGATATGTCCGACGAAGCCAAAACCAATTTGCGTCGTTGGTTGGGTATCATGTGGAACAATTATAAACAGCGTGTGGCGGAGAATCGTAACATCAAAGAAGAGGCTGTTGCACCGAATGCGCACACCTATTTAACCGAATTAAAAGCCTTGCAAGGCGACATGACGGCTTATGTGAAACAACGTAAGTTGATTAACGGCGTATTGGACCGCTTTAATTTAGATAAAAAACTGACCGCACTTTTCGGTGATAATGAAGATAAGCAACCGAAAATGGTAGATTACGACACTTACCTGGCTTCTTTGCCGGATCGTATGTCGGGCGACACCAAGAATAAAATTGCTGTAGTGAACGTGGAAGGGGCGATCATTGATGGCGAAACCGATGAAGAAAACGTTGGTGGCGACACTATCGCAAACTTGTTACGCAAGGCTTATGATGATAAGGACGTGAAAGCTGTCGTTCTGCGCGTTAACAGCCCGGGCGGTAGTGCTTTTGCATCGGAAATCATTCGTCAGGAGCTCAGTCACTTACAACAAGCAGGCAAACCGGTGGTGGTTTCCATGGGTGGCATGGCGGCTTCCGGCGGGTATTGGATTTCTTCCACCGCTGATTATATTGTGGCGGATAAAAACACCATCACCGGTTCTATCGGGATTTTTGCCGTATTACCGACATTCGAGAAAACCATCAAGAAAATCGGTGTGTCCGCCGACGGGGTGAAAACCTCCGATTTAGCACTGGGATCCGCGTTCTCGCCGTTATCTTCCGAATTAAATGATGTATTACAGCTAGAAATTGAACATGGCTACGACGAATTCCTGACTAAAGTCAGTCAAGGTCGTCACTTAAGCAAAGCGCAAGTGGATAAAATCGCCCAAGGTCAGGTTTGGCTGGGTTCCGAAGCGATTGAACATAAATTGGTGGATGAGCTGGGCGATTTGAATACTGCTTTAGGCAAAGCCATGGAATTGGTGAACGAAAAACTGGACGAAAATAGCAAAATTCAGGAAGAAGGTTTTTCCGTAGAATGGCTGGATGACGACAGCGGTTCGTTCTTCAAAAAATTCATGCGTGATTTCAAAGGCGATAGTAAAGCATGGGTAACGGGGTTGGTGACTGAAGCCGTCGGTTTACCGAAAGAATTTACGCAGGTGAAACAACTTGGTTTGTTGAACACCTTTAACGATCCGAAAGGGCAGTATTTATATTGCTTAACCTGCGGCAAAGTGCAA","","","70179","LISRGYMKVIFSIIKFAWRTLNFIRDLVMNIVFLVFVLLLLTALPFVVGLDKQTVALKGDQGALYLNLDGYLADNRDNQGGVKTLLKELDNQHIPQQYSTFDVVYAIDSAALDDKVRGLVLDLNYFQGGDLPSLEFVGASIENFKKNGKQVIAYSDNYNRAQYFLASYADEVYMNPVGTVSIDGLVQENLYYKDLLDSLEVNPHVFRVGTYKSAVEPFLRNDMSDEAKTNLRRWLGIMWNNYKQRVAENRNIKEEAVAPNAHTYLTELKALQGDMTAYVKQRKLINGVLDRFNLDKKLTALFGDNEDKQPKMVDYDTYLASLPDRMSGDTKNKIAVVNVEGAIIDGETDEENVGGDTIANLLRKAYDDKDVKAVVLRVNSPGGSAFASEIIRQELSHLQQAGKPVVVSMGGMAASGGYWISSTADYIVADKNTITGSIGIFAVLPTFEKTIKKIGVSADGVKTSDLALGSAFSPLSSELNDVLQLEIEHGYDEFLTKVSQGRHLSKAQVDKIAQGQVWLGSEAIEHKLVDELGDLNTALGKAMELVNEKLDENSKIQEEGFSVEWLDDDSGSFFKKFMRDFKGDSKAWVTGLVTEAVGLPKEFTQVKQLGLLNTFNDPKGQYLYCLTCGKVQ","1355063","[FUNCTION] Digestion of the cleaved signal peptides. this activity is necessary to maintain proper secretion of mature proteins across the membrane. ","protease IV; signal peptide peptidase; Endopeptidase IV","Outer membrane, Periplasm, Inner membrane, Cytoplasm","","
InterPro
IPR002142
Domain
Peptidase S49
PD002897\"[163-218]T\"[403-484]TSPPA_HAEIN_P45243;
PF01343\"[143-299]T\"[397-549]TPeptidase_S49
InterPro
IPR004634
Family
Peptidase S49, protease IV
PIRSF001217\"[10-632]TProtease IV with duplicated peptidase family U7 domain
TIGR00705\"[18-623]TSppA_67K: signal peptide peptidase SppA,
InterPro
IPR004635
Domain
Peptidase S49, SppA
TIGR00706\"[333-547]TSppA_dom: signal peptide peptidase SppA,
noIPR
unintegrated
unintegrated
G3DSA:3.90.226.10\"[307-532]Tno description
signalp\"[1-49]?signal-peptide
tmhmm\"[27-47]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 4.4e-48) to 3/3 blocks of the IPB002142 family, which is described as \"Peptidase family U7\". Interpro entry for IP:IPR002142. IPB002142A 374-383 9.7e-05 IPB002142B 407-456 8.5e-30 IPB002142C 513-539 8.9e-11","Residues 586 to 631 match (3e-09) PD:PD108865 which is described as COMPLETE PROTEASE PROTEOME IV INNER 3.4.21.- TRANSMEMBRANE MEMBRANE PEPTIDASE PEPTIDE ","","","","","","","","","","","Fri Jan 10 10:30:04 2003","Fri Jan 10 10:30:04 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01992 is paralogously related to AA02026 (1e-16).","","","","","","Residues 397 to 549 (E-value = 5.5e-64) place AA01992 in the Peptidase_S49 family which is described as Peptidase family S49 (PF01343)","","","","","Ichihara,S., Suzuki,T., Suzuki,M. and Mizushima,S. Molecular cloning and sequencing of the sppA gene and characterization of the encoded protease IV, a signal peptide peptidase, of Escherichia coli. J. Biol. Chem. 261(20): 9405-9411. 1986 PubMed: 3522590. Guttman,D.S. and Dykhuizen,D.E. Clonal divergence in Escherichia coli as a result of recombination, not mutation. Science 266 (5189): 1380-1383 (1994) [PubMed: 7973728]. ;","","Fri Jan 10 10:30:04 2003","1","","","" "AA01994","1355099","1355311","213","ATGGGATACATGGAACGCTTGGCGGAATTAAGAGAGCAGATTGATTCATTGGATCATGAACTGTTGCAACTGCTGGCGAAACGGCAACAGGTGGTGCACAAAGTGGGGGAAGTGAAACAGCAACACGGGTTGCCCATTATGCACCACAGCGTGAGGCGGAAATGTTGCAACGCAAGCGTGAGGCCGCCGAGCAAATGGGGTTATCTCCTAATC","","","8283","MGYMERLAELREQIDSLDHELLQLLAKRQQVVHKVGEVKQQHGLPIMHHSVRRKCCNASVRPPSKWGYLLI","1355310","[CATALYTIC ACTIVITY] Chorismate = prephenate.[CATALYTIC ACTIVITY] Prephenate + NAD(+) = 4-hydroxyphenylpyruvate + CO(2) + NADH.[PATHWAY] Tyrosine biosynthesis.[SUBCELLULAR LOCATION] Cytoplasmic.","chorismate mutase; prephenate dehydrogenase","Cytoplasm","","
InterPro
IPR002701
Domain
Chorismate mutase
PF01817\"[11-63]TCM_2
PS51168\"[1-71]TCHORISMATE_MUT_2
noIPR
unintegrated
unintegrated
G3DSA:1.20.59.10\"[7-58]Tno description


","BeTs to 15 clades of COG1605COG name: Chorismate mutaseFunctional Class: EThe phylogenetic pattern of COG1605 is aomp-zyqvdrlb-efghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 9.7e-15) to 1/1 blocks of the IPB002701 family, which is described as \"Chorismate mutase\". Interpro entry for IP:IPR002701. IPB002701 7-39 9.1e-15","Residues 4 to 46 match (2e-07) PD:PD005194 which is described as COMPLETE PROTEOME CHORISMATE MUTASE ISOMERASE PREPHENATE DEHYDRATASE BIOSYNTHESIS DEHYDROGENASE INCLUDES: ","","","","","","","","","","","Fri Jan 10 10:35:27 2003","Fri Jan 10 10:35:27 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01994 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Hudson,G.S. and Davidson,B.E. Nucleotide sequence and transcription of the phenylalanine and tyrosine operons of Escherichia coli K12. J. Mol. Biol. 180 (4): 1023-1051 (1984) [PubMed: 6396419].","","Fri Jan 10 10:35:27 2003","1","","","" "AA01995","1355260","1355454","195","ATGTTGCAACGCAAGCGTGAGGCCGCCGAGCAAATGGGGTTATCTCCTAATCTGATTGAAGATGTGCTACGCCGCATTATGCGTGAATCCTATGTCAGCGAAAATCAATTCGGCTTTAAAACCGTAATCCGCAAATTCGGAAAATCGTTATCGTGGGCGGACGAGGCAAACTCGGCAGCTTATTCTGTCGTTATT","","","7449","MLQRKREAAEQMGLSPNLIEDVLRRIMRESYVSENQFGFKTVIRKFGKSLSWADEANSAAYSVVI","1355454","","conserved hypothetical protein (possible chorismate mutase)","Cytoplasm, Periplasm","This sequence is similar to gi|23467761, a predicted chorismate mutase from Haemophilus somnus 129PT. Also see gi|15602529, a predicted TyrA from Pasteurella multocida.","
InterPro
IPR002701
Domain
Chorismate mutase
PF01817\"[1-37]TCM_2


","BeTs to 3 clades of COG1605COG name: Chorismate mutaseFunctional Class: EThe phylogenetic pattern of COG1605 is aomp-zyqvdrlb-efghsnuj----Number of proteins in this genome belonging to this COG is","","Residues 5 to 42 match (5e-08) PD:PD550279 which is described as PROTEOME DEHYDROGENASE COMPLETE CHORISMATE ISOMERASE PREPHENATE MUTASE T-PROTEIN OXIDOREDUCTASE MULTIFUNCTIONAL ","","","","","","","","","","","","Thu Feb 26 08:27:55 2004","Thu Feb 26 08:27:55 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA01995 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 08:27:55 2004","","","","","","","","","","","","","1","","","" "AA01996","1355454","1356227","774","TTGAAGGGTTCCGGCTATCAGGTGAAATGTCTGGAGCGGGACGATTGGGCGCGCGCCGACCAAATTTTGCAGCATGCCGATGTGGTAATTGTGTCTGTGCCCATTGCCAACACGTTGGCGGTGATCGAACGGCTCAAACCTTATTTGACGGAAAATATGCTGCTGGCGGATTTCACTTCCGTGAAACGCACGCCTTTAGAGAAAATGCTGGAAGTGCACAAAGGTGCGGTGGTCGGTTTACACCCCATGTTCGGACCTGATGTGGCAAGTATGGCGAAGCAGGTCGTGGTGTGCTGCGACGGACGTTTTAGCGAGCGTTACCAATGGTTGTTGCAACAAATCCAAATCTGGGGCGCGAAAATTTATCAGGTTGATGCCACCGAACATGATCATCACATGACTTATATTCAGGCGTTGCGCCATTTTTCCACCTTTGTTTATGGCTTGTATTTGTCACAACAGCCGGTGGATTTGGAAAAATTACTGGCGCTTTCTTCGCCGATTTATCGTCTGGAACTTGCCATGGTCGGGCGTTTATTTGCGCAAGATGCGGCATTGTATGCGGACATTATCGCCCACAAGCCGGAAAACCTGGCGGTTATCGAGCATTTCAAAGACAGCTACGAAACGGGTCTCGCCTTTTTCAAACACCATGATCGGCAAGGCTTTATTGAACAATTTAATCAGATTCGTGACTGGTTCGGTGGTTATTCCGAGCAATTTTTGCAGGAAAGCCGCCAGTTACTTCAGCAAGCCAATGACTCTCGAAATGTT","","","31151","LKGSGYQVKCLERDDWARADQILQHADVVIVSVPIANTLAVIERLKPYLTENMLLADFTSVKRTPLEKMLEVHKGAVVGLHPMFGPDVASMAKQVVVCCDGRFSERYQWLLQQIQIWGAKIYQVDATEHDHHMTYIQALRHFSTFVYGLYLSQQPVDLEKLLALSSPIYRLELAMVGRLFAQDAALYADIIAHKPENLAVIEHFKDSYETGLAFFKHHDRQGFIEQFNQIRDWFGGYSEQFLQESRQLLQQANDSRNV","1356226","CATALYTIC ACTIVITY] Chorismate = prephenate.[CATALYTIC ACTIVITY] Prephenate + NAD(+) = 4-hydroxyphenylpyruvate + CO(2) + NADH.[PATHWAY] Tyrosine biosynthesis.[SUBCELLULAR LOCATION] Cytoplasmic.","prephenate dehydrogenase","Cytoplasm","","
InterPro
IPR003099
Domain
Prephenate dehydrogenase
PF02153\"[1-234]TPDH
PS51176\"[1-245]TPDH_ADH


","BeTs to 15 clades of COG0287COG name: Prephenate dehydrogenaseFunctional Class: EThe phylogenetic pattern of COG0287 is aomp-zyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is","","Residues 4 to 51 match (2e-10) PD:PD584530 which is described as PROTEOME COMPLETE CHORISMATE T-PROTEIN ISOMERASE DEHYDROGENASE MULTIFUNCTIONAL PDH CM PREPHENATE ","","","","","","","","","","","Fri Jan 10 10:40:42 2003","Fri Jan 10 10:40:42 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01996 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 234 (E-value = 2.4e-12) place AA01996 in the PDH family which is described as Prephenate dehydrogenase (PF02153)","","","","","Fischer,R.S., Zhao,G. and Jensen,R.A. Cloning, sequencing, and expression of the P-protein gene (pheA) of Pseudomonas stutzeri in Escherichia coli: implications for evolutionary relationships in phenylalanine biosynthesis J. Gen. Microbiol. 137 (Pt 6), 1293-1301 (1991) PubMed: 1919506 Hudson,G.S. and Davidson,B.E. Nucleotide sequence and transcription of the phenylalanine and tyrosine operons of Escherichia coli K12 J. Mol. Biol. 180 (4), 1023-1051 (1984) PubMed: 6396419 ","","Fri Jan 10 10:40:42 2003","1","","","" "AA01997","1356304","1356924","621","ATGAGTCAATTTTTTTATATTCATCCGGAAAACCCGCAAGTTCGCCTGATTAATCAAGCGGTCGAAATTTTGCGCAACGGCGGGGTGGTTGTGTATCCTACCGATTCCGGCTACGCCTTGGGGTGCATGATTGGCGATAAGCACGCAATGGACAGAATCGTGCACATTCGTCAATTACCCGAGGGACACAATTTTACGTTGGTGTGCAGCGATTTGTCGGAATTATCCACCTATTCTTTGGTAACTAATTCCGCTTACCGTTTGATTAAAAATAACACGCCGGGGCGTTACACATTTATTTTAACGGCAACCAAAGAATTGCCGCGTCGCTTAATGACGTCCAAGCGCAAAACCATCGGCATTCGCGTGCCGGATAACCAAATTGCGTTGGATTTACTAAAAGCCCTTGGTGAACCGATTTTATCCTGCTCGTTGATGCTACCGAATGAAGAACATTTGACGCAATCGGATCCGGAAGAGATCCGTGATCGTTTGGAACATCAGGTGGATTTAATTATTCACGGCGGTTATTTGGGACAAGAACCGACAACGGTGGTGGATTTAACCGGAGACACGCCGGTGATCTTGCGTGAAGGCAGCGGCGCGGTTACGCCATTTATT","","","23092","MSQFFYIHPENPQVRLINQAVEILRNGGVVVYPTDSGYALGCMIGDKHAMDRIVHIRQLPEGHNFTLVCSDLSELSTYSLVTNSAYRLIKNNTPGRYTFILTATKELPRRLMTSKRKTIGIRVPDNQIALDLLKALGEPILSCSLMLPNEEHLTQSDPEEIRDRLEHQVDLIIHGGYLGQEPTTVVDLTGDTPVILREGSGAVTPFI","1356923","","probable translation factor","Cytoplasm","","
InterPro
IPR004388
Domain
Sua5/YciO/YrdC/YwlC
TIGR00057\"[7-207]TTIGR00057: Sua5/YciO/YrdC/YwlC family prote
InterPro
IPR006070
Domain
SUA5/yciO/yrdC, N-terminal
PF01300\"[22-199]TSua5_yciO_yrdC
PS51163\"[14-201]TYRDC
InterPro
IPR012200
Family
RNA-binding protein, YrdC
PIRSF004931\"[8-207]TRNA-binding protein, YrdC type
noIPR
unintegrated
unintegrated
G3DSA:3.90.870.10\"[1-207]Tno description
PTHR17490\"[27-201]TSUA5


","BeTs to 23 clades of COG0009COG name: Putative translation factor (SUA5)Functional Class: JThe phylogenetic pattern of COG0009 is aompkzyqvdrlbcefghsn-jxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.6e-23) to 2/2 blocks of the IPB000666 family, which is described as \"SUA5/yciO/yrdC family\". Interpro entry for IP:IPR000666. IPB000666A 29-57 1.4e-12 IPB000666B 182-199 3.3e-09","Residues 18 to 157 match (6e-51) PD:PD034569 which is described as COMPLETE PROTEOME PRODUCTION V COLICIN TRANSMEMBRANE MEMBRANE HOMOLOG FOR DEDE ","","","","","Wed Feb 19 07:24:57 2003","","","","","","","Fri Jan 10 10:45:04 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01997 is paralogously related to AA00576 (2e-04).","","","","","","Residues 22 to 199 (E-value = 2.9e-75) place AA01997 in the Sua5_yciO_yrdC family which is described as yrdC domain (PF01300)","","","","","Gubanov,V.V., Lebedev,Iu.B., Monastyrskaia,G.S., Rubtsov,P.M. and Skriabin,K.G. Primary structure of the E. coli DNA region preceding the tryptophan operon genes. Bioorg. Khim. 10 (3): 415-417 (1984) PubMed: 6385993.","","Fri Jan 31 13:44:27 2003","1","","","" "AA01998","1356982","1357947","966","ATGAAACCCACAACAAAACGCACTCAAAATCGACCGCACTTTTCGTCGAACAAAGATAAAAATGCGACGGCGAAGCCGCGTCCGATCAGCAGCGCAAGCAAAACCTCCGCGGCAGAAGGCGAAAAATTACAAAAAGTGTTAGCCCGTGCAGGACAAGGTTCGCGCCGTGAAATCGAAGCTATTATTGCGGAAAACCGGGTCAGTGTGGATGGTAAAATTGCCACTTTAGGCGATCGGATTAATGTGTATGCCGGCGTGAAAGTGCGTATCGACGGACATCTGATTAATTTAACCCAAGCGCAGAAGGAAGTGTGCCGTGTGTTGATGTATTACAAAGCGGAGGGTGAGCTATGCACCCGCCACGATCCGGAAGGGCGCGCCACCGTCTTTGATCGTCTGCCGCGTTTAACCGGCGCCCGCTGGATTGCCGTAGGGCGTTTGGATATTAATACCTCAGGTTTATTGTTATTTACGACAGATGGCGAATTAGCCAACCGCTTAATGCACCCGAGCCGTGAAGTGGAGCGCGAATATTCCGTGCGTGTGTTCGGGCAAGTGGATGATGCCATGTTGAACCGTTTGAAAAAAGGCGTGCAACTGGAAGACGGTCCGGCAAATTTCAAAGAAATTAAAGTCGTTGGCGGCGTAGGCATGAACCAATGGTTTGACGTGACCTTAATGGAAGGGCGCAACCGTGAAGTGCGTCGTTTATGGGAATCGCAAGGCATTCAGGTCAGTCGTTTGATTCGCATTCGTTACGGCAACATTAAACTGATGAAAACTTTGCCGCGCGGTGGCTGGCAGGAAATGGAACTGGCGGATGTGAATTATTTGCGTGAACTTGTCGGTTTGCCGCCGGAAACGGAAACCAAATTGGGTGCCAATAAAACCCGTCATAAACCGAAATTCAGTCAAATCCGTAAAGCAGTAAAACGTTACTCAGAATTAAATAAACGTTATAAAAAA","","","36566","MKPTTKRTQNRPHFSSNKDKNATAKPRPISSASKTSAAEGEKLQKVLARAGQGSRREIEAIIAENRVSVDGKIATLGDRINVYAGVKVRIDGHLINLTQAQKEVCRVLMYYKAEGELCTRHDPEGRATVFDRLPRLTGARWIAVGRLDINTSGLLLFTTDGELANRLMHPSREVEREYSVRVFGQVDDAMLNRLKKGVQLEDGPANFKEIKVVGGVGMNQWFDVTLMEGRNREVRRLWESQGIQVSRLIRIRYGNIKLMKTLPRGGWQEMELADVNYLRELVGLPPETETKLGANKTRHKPKFSQIRKAVKRYSELNKRYKK","1357946","","16S rRNA pseudouridine synthase","Cytoplasm","","
InterPro
IPR000748
Domain
Pseudouridine synthase, Rsu
TIGR00093\"[111-272]TTIGR00093: conserved hypothetical protein
PS01149\"[145-159]TPSI_RSU
InterPro
IPR002942
Domain
RNA-binding S4
PF01479\"[41-88]TS4
SM00363\"[41-112]TS4
PS50889\"[41-113]TS4
InterPro
IPR006145
Domain
Pseudouridine synthase
PF00849\"[106-240]TPseudoU_synth_2
noIPR
unintegrated
unintegrated
PTHR21600\"[45-318]TRIBOSOMAL LARGE SUBUNIT PSEUDOURIDINE SYNTHASE B
PTHR21600:SF2\"[45-318]TRIBOSOMAL LARGE SUBUNIT PSEUDOURIDINE SYNTHASE B


","BeTs to 17 clades of COG1187COG name: 16S rRNA uridine-516 pseudouridylate synthase and related pseudouridylate synthasesFunctional Class: JThe phylogenetic pattern of COG1187 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 1e-71) to 4/4 blocks of the IPB000748 family, which is described as \"Pseudouridine synthase, Rsu family\". Interpro entry for IP:IPR000748. IPB000748A 42-67 1.3e-12 IPB000748B 111-126 2.4e-06 IPB000748C 144-176 1.4e-25 IPB000748D 224-258 3.5e-23Significant hit ( 8.7e-10) to 2/4 blocks of the IPB000613 family, which is described as \"Pseudouridine synthase\". Interpro entry for IP:IPR000613. IPB000613B 144-183 1.1e-08 IPB000613C 228-252 27","Residues 40 to 82 match (1e-09) PD:PD004022 which is described as COMPLETE PROTEOME SYNTHASE PSEUDOURIDINE RIBOSOMAL SUBUNIT LARGE LYASE PSEUDOURIDYLATE D ","","","","","","","","","","","","Wed Jan 29 15:15:37 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01998 is paralogously related to AA00064 (4e-18) and AA00885 (5e-04).","","","","","","Residues 106 to 240 (E-value = 2e-09) place AA01998 in the PseudoU_synth_2 family which is described as RNA pseudouridylate synthase (PF00849)","","","","","Sivaraman J, Sauve V, Larocque R, Stura EA, Schrag JD, Cygler M, Matte A.Structure of the 16S rRNA pseudouridine synthase RsuA bound to uracil and UMP.Nat Struct Biol. 2002 May;9(5):353-8.PMID: 11953756 Del Campo M, Kaya Y, Ofengand J.Identification and site of action of the remaining four putative pseudouridine synthases in Escherichia coli.RNA. 2001 Nov;7(11):1603-15.PMID: 11720289","","Wed Jan 29 15:15:37 2003","1","","","" "AA01999","1357981","1358949","969","ATGAAATTTCAGCAACTTCGTTACGTGGTTGAGATTGTGAACCAAAATTATAATGTCACGGAAGCTGCACATGCGTTATACACCTCCCAACCGGGAATTAGTAAACAGGTTCGTTTATTGGAAAATGAGCTTGGTTTGGAAATTTTTGATCGTCACGGTAAACATATTAAAGGGCTTACGCCCGCCGGTAAAAAAATCGTGGGTATTTCCCGGGAATTAATGGTGAAAATGCAAGCGATTCGTTCCGTGTCCGACGAATATACTAAACCGGATCACGGTGTGTTGCGCATTGCCACCACAAACACCCAGGCACGTTATATGTTGCCTCATGTGGTAGAACGTTTTGCCAAACGTTATCCTGATGTGAGTTTACACATTCATCAGGGTTCTCCAATGCAGATTTATGATGTGCTATTGTCCGGTGAAGTGGACTTGGCAATTACCACGGAAGCTCAATATTTATTTGATGGCGTGGTGTTGCTGCCATGTTATATGTGGAATCGCTCGGTCATTGTGAAGTCAGATCATCCGTTAGCCAAATGTGAGCTACTGACTATCGAAGAATTAGGCAAATATCCTTTAATTACTTATACTTTCGGCTTTACCGGCGTTTCCGATTTGGATTATGCCTTTAATGGTGCCGGTATCCTGCCGAATATTGTATTTACCGCTACCGATGCGGATGTTATCAAAACCTATGTCCGTTTAGGCTTAGGTGTGGGCATTATGGCGTCCATGGCGCATACGCCGGCGGATGTTGATTTGGTGGCACTTAAAGCGGATCATTTATTCCGCGCCAGCATGACGCAAATCGCCTTTAAACACGGCGCTTTCCTGCGTAATTATATGTATGATTTTATCAACTATTTTTCACCGCACTTAACCCGTGAAAACGTGGAACGGGCAGAGCGTATGCACGACAATAATGCGGTGAAAAGATTATTTGATGACGTCAGATTGCAAACTTTG","","","36584","MKFQQLRYVVEIVNQNYNVTEAAHALYTSQPGISKQVRLLENELGLEIFDRHGKHIKGLTPAGKKIVGISRELMVKMQAIRSVSDEYTKPDHGVLRIATTNTQARYMLPHVVERFAKRYPDVSLHIHQGSPMQIYDVLLSGEVDLAITTEAQYLFDGVVLLPCYMWNRSVIVKSDHPLAKCELLTIEELGKYPLITYTFGFTGVSDLDYAFNGAGILPNIVFTATDADVIKTYVRLGLGVGIMASMAHTPADVDLVALKADHLFRASMTQIAFKHGAFLRNYMYDFINYFSPHLTRENVERAERMHDNNAVKRLFDDVRLQTL","1358948","[FUNCTION] This protein is a positive regulator of gene expression for the cysteine regulon. The inducer for cysB is N-acetylserine (by similarity). ","cys regulon transcriptional activator; cysteine synthase","Cytoplasm","","
InterPro
IPR000847
Domain
Bacterial regulatory protein, LysR
PR00039\"[19-30]T\"[30-40]T\"[40-51]THTHLYSR
PF00126\"[3-64]THTH_1
PS50931\"[1-59]THTH_LYSR
InterPro
IPR005119
Domain
LysR, substrate-binding
PF03466\"[88-295]TLysR_substrate
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[88-323]Tno description


","BeTs to 13 clades of COG0583COG name: Transcriptional regulatorFunctional Class: KThe phylogenetic pattern of COG0583 is a-m----q-drlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 2.2e-12) to 1/1 blocks of the IPB000847 family, which is described as \"Bacterial regulatory protein, LysR family\". Interpro entry for IP:IPR000847. IPB000847 18-51 2.2e-12Significant hit ( 3.2e-05) to 1/2 blocks of the IPB001583 family, which is described as \"NodD transcription activator carboxyl terminal region\". Interpro entry for IP:IPR001583. IPB001583A 6-56 3e-05","Residues 95 to 243 match (4e-07) PD:PD488793 which is described as TRANSCRIPTIONAL REGULATOR PROTEOME LYSR COMPLETE FAMILY ","","","","","","","","","","","Fri Jan 10 10:59:28 2003","Fri Jan 24 13:39:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA01999 is paralogously related to AA01513 (2e-17), AA02539 (5e-16), AA00371 (2e-13), AA00940 (5e-12), AA01794 (2e-05) and AA00977 (6e-05).","","","","","","Residues 88 to 295 (E-value = 5.9e-40) place AA01999 in the LysR_substrate family which is described as LysR substrate binding domain (PF03466)","","","","","Ostrowski,J., Jagura-Burdzy,G. and Kredich,N.M. DNA sequences of the cysB regions of Salmonella typhimurium and Escherichia coli. J. Biol. Chem. 262 (13): 5999-6005 (1987) [PubMed: 3032952].Tei,H., Watanabe,K., Murata,K. and Kimura,A. Analysis of the Escherichia coli K-12 cysB gene and its product using the method of gene fusion. Biochem. Biophys. Res. Commun. 167 (3): 962-969 (1990) [PubMed: 2182030].Prodromou,C., Artymiuk,P.J. and Guest,J.R. The aconitase of Escherichia coli. Nucleotide sequence of the aconitase gene and amino acid sequence similarity with mitochondrial aconitases, the iron-responsive-element-binding protein and isopropylmalate isomerases. Eur. J. Biochem. 204 (2): 599-609 (1992) [PubMed: 1541275].Parry J, Clark DP. Identification of a CysB-regulated gene involved in glutathione transport in Escherichia coli. FEMS Microbiol Lett. 2002 Mar 19;209(1):81-5. PMID: 12007658 van der Ploeg JR, Eichhorn E, Leisinger T. Sulfonate-sulfur metabolism and its regulation in Escherichia coli. Arch Microbiol. 2001 Jul;176(1-2):1-8. Review. PMID: 11479697","","Fri Jan 10 10:59:28 2003","1","","","" "AA02000","1359037","1359861","825","ATGTCAAATTTACAACAACTTATTGAAAACGCTTTTGAAAAACGCACTGAAATTACACCAAAAACCATTGACGTACAAACCCGTGCGGCGGTTGAAGAGGTGATTGAAGGCTTGGACAGCGGCAAGTATCGTGTTGCCGAAAAAATCGACGGCGAATGGGTGACTCACCAATGGTTGAAAAAAGCGGCCTTGTTATCTTTCCGTATTAACGACAATCAACTTGTTGACGGTGCAGAAACCAAATACTACGACAAAGTCCCATTGAAATTTGCCGATTACACCGAAGAACGTTTCCAACAAGAAGGCTTCCGTGTAGTGCCGTCTGCTACCGTACGTAAAGGCGCATATATTGCTAAAAACTGCGTGTTAATGCCGTCTTATGTGAATATCGGCGCTCACGTGGGCGAAGGCACCATGGTAGATACTTGGGCAACCGTAGGTTCCTGTGCGCAAATCGGTAAAAACGTGCACTTATCCGGCGGCGTGGGTATCGGCGGTGTGTTAGAACCGTTACAAGCCAACCCGACTATTATCGGCGATAACTGTTTCATTGGTGCCCGTTCCGAAGTGGTAGAAGGCGTTATCGTGGAAGACGGCTGCGTGATTTCCATGGGCGTATTCATTGGCCAATCCACCAAAATCTACGATCGTGAAACCGGCGAAGTGTATTATGGCCGCGTACCGGCAGGTTCCGTGGTGGTTTCGGGCAGCCTTCCGAGCAAAGATGGCAGATACAGCCTCTACTGCGCGGTTATCGTGAAAAAAGTAGATGCGAAAACCTTAGGCAAAGTGGGTATCAACGAGTTATTACGTTCTATTGAAGAA","","","29930","MSNLQQLIENAFEKRTEITPKTIDVQTRAAVEEVIEGLDSGKYRVAEKIDGEWVTHQWLKKAALLSFRINDNQLVDGAETKYYDKVPLKFADYTEERFQQEGFRVVPSATVRKGAYIAKNCVLMPSYVNIGAHVGEGTMVDTWATVGSCAQIGKNVHLSGGVGIGGVLEPLQANPTIIGDNCFIGARSEVVEGVIVEDGCVISMGVFIGQSTKIYDRETGEVYYGRVPAGSVVVSGSLPSKDGRYSLYCAVIVKKVDAKTLGKVGINELLRSIEE","1359860","","2,3,4,5-tetrahydropyridine-2-carboxylate","Cytoplasm","","
InterPro
IPR001451
Repeat
Bacterial transferase hexapeptide repeat
PF00132\"[108-125]T\"[131-148]T\"[149-166]T\"[175-192]T\"[193-210]THexapep
PS00101\"[134-162]THEXAPEP_TRANSFERASES
InterPro
IPR005664
Family
2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase
TIGR00965\"[3-273]TdapD: 2,3,4,5-tetrahydropyridine-2,6-dicarb
noIPR
unintegrated
unintegrated
G3DSA:1.10.166.10\"[1-70]Tno description
G3DSA:2.160.10.10\"[87-256]Tno description


","BeTs to 12 clades of COG2171COG name: Tetrahydrodipicolinate N-succinyltransferaseFunctional Class: EThe phylogenetic pattern of COG2171 is --------v-rlb-efghsnujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 2.2e-08) to 1/1 blocks of the IPB001451 family, which is described as \"Bacterial transferase hexapeptide repeat\". Interpro entry for IP:IPR001451. IPB001451 178-213 2.2e-08 IPB001451 140-175 1.1e-07 IPB001451 184-219 0.016 IPB001451 134-169 0.02 IPB001451 122-157 0.042 IPB001451 172-207 0.051 IPB001451 128-163 0.35","Residues 128 to 210 match (1e-13) PD:PD013088 which is described as TRANSFERASE COMPLETE PROTEOME ACETYLTRANSFERASE ACYLTRANSFERASE SERINE REPEAT BIOSYNTHESIS A 2.3.1.- ","","","","","","","","","","","Fri May 20 15:01:55 2005","Fri Jan 10 11:03:04 2003","","Fri May 20 15:01:55 2005","Fri May 20 15:01:55 2005","Fri May 20 15:01:55 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA02000 is paralogously related to AA01539 (2e-09), AA00612 (2e-05) and AA00610 (9e-04).","Fri May 20 15:01:55 2005","","","","","","","","","","Richaud,C., Richaud,F., Martin,C., Haziza,C. and Patte,J.C.Regulation of expression and nucleotide sequence of the Escherichia coli dapD gene J. Biol. Chem. 259 (23), 14824-14828 (1984) PubMed: 6094577 ","","Fri Jan 10 11:03:04 2003","1","","","" "AA02001","1360299","1359982","318","ATGACAGAATTAACCCGGCTTGATCCTGATAAAGCCATCGACATTGCCTACGATATTTTTCTTGAAATGGCACCGGAAAACTTAGACCCGGCAGATATTATGCTGTTCAACCTCCAGTTTGAAGAACACGGCGCAGTAGAATTTGTGGAAACCGCTGACAACTGGGAAGAACAAATCGGCATACTTATCGACCCGCAAGAATACGCAGAAGTCTGGATCGGGCTGGTAAACAAACAAGATGAAATGGACAACATCTTCGCTAAATTCCTCATTTCCCACCGCGAAGACGATCGGCAATATCATATTATTTGGAAGGCG","","","12483","MTELTRLDPDKAIDIAYDIFLEMAPENLDPADIMLFNLQFEEHGAVEFVETADNWEEQIGILIDPQEYAEVWIGLVNKQDEMDNIFAKFLISHREDDRQYHIIWKA","1359981","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR007376
Family
Protein of unknown function DUF440
PD020447\"[6-105]TYE50_HAEIN_P44199;
PIRSF004916\"[1-106]TUncharacterised conserved protein
PF04269\"[1-106]TDUF440


","BeTs to 3 clades of COG3099COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3099 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 2 to 105 match (4e-39) PD:PD020447 which is described as PROTEOME COMPLETE CYTOPLASMIC Z2024 YCIU VC1208 HI1450 YPO2187 STY1311 PM0536 ","","","","","","","","","","","","Fri Jan 10 11:03:56 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02001 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 106 (E-value = 7.8e-76) place AA02001 in the DUF440 family which is described as Protein of unknown function, DUF440 (PF04269)","","","","","","","","1","","","" "AA02002","1360467","1360336","132","TTGTCACCAATCGGTCCATTGCCGGCAATGATTTTTAGTAAAGCGATAGAAGGTTATCGGAACGAAGGCCCCAAAAGTGCGGTTGGAAAAAACATCATTTTTTTCGACCGCACTTCTTACTGGCTTATGTTA","","","4912","LSPIGPLPAMIFSKAIEGYRNEGPKSAVGKNIIFFDRTSYWLML","1360336","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 08:24:39 2004","Thu Feb 26 08:24:39 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02002 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 08:24:39 2004","","","","","","","","","","","","","1","","","" "AA02003","1361768","1360773","996","ATGGCTACCATCAAAGATGTCGCAAAAATGGCAGGCGTATCGACCACCACAGTATCCCACGTTATCAATAAAACCCGTTTTGTTGCCGCTGAAACCAAACAACAGGTTTTGCAAGCAATAAAAGATCTGAATTATTCACCCAGTGCGGTGGCGCGCAGTTTAAAAGTCAACACTACCAAATCCATCGGCATGATCGTCACCACCAGCGAAGCCCCTTATTTCGCCGAAATCATTCATGCGGTGGAAGAACATTGCTATCGCCAAGGCTATTCTCTGTTTTTATGTAATACGCAAAATAATGCGGAAAAGATCAAAAATCACTTGGAAATGCTGGCAAAAAAACGTGTTGATGGAATTTTGGTGATGTGTTCCGAATATTTGCAGGATCCGCAGGATTTACTTACGGTATTTTCTTCTATTCCAATGGTGGTGATGGATTGGGGCCCGAATGCCCATACGAATATTATTCAGGATAACAGTTTCGACGGCGGCTATCTGGCGACTAAACATCTGATTGAAAACGGACATAAAAATATCGGTATTATCGCCGGTGAACTGAACAAAACCACAGCGAAAACCCGCTATGAAGGCTTCGTACACGCCATGCAGGAAGCCGGGCTGGCAATTAACCCGAACTGGGTCATGGAAGGTTTTTTTGAACCGGAAGACGGCTATGAATGTATGAACAAAATTCTGCGTCAAGAAACCCTACCCACCGCCGTATTCTGTTGCAACGACGTTATGGCGTTAGGGGCAATTTCTGCTATCGGCGAAAAAGGCTTATGTGTGCCGGACGACATTTCCATTATCGGCTACGACAATATTCACGCCTCCCGTTTTTATTCGCCGCCGTTGACCACCATTCACCAATCCAAATCCCGTTTGGGGGTACAGGCGGTAAATTTGTTGTTTGAACGCATTAATCACAAATCCGATCAACGAAAAACTATTGAAATTCACCCTGAATTAGTAATGCGTAAATCGGTAAAAAAACTT","","","36947","MATIKDVAKMAGVSTTTVSHVINKTRFVAAETKQQVLQAIKDLNYSPSAVARSLKVNTTKSIGMIVTTSEAPYFAEIIHAVEEHCYRQGYSLFLCNTQNNAEKIKNHLEMLAKKRVDGILVMCSEYLQDPQDLLTVFSSIPMVVMDWGPNAHTNIIQDNSFDGGYLATKHLIENGHKNIGIIAGELNKTTAKTRYEGFVHAMQEAGLAINPNWVMEGFFEPEDGYECMNKILRQETLPTAVFCCNDVMALGAISAIGEKGLCVPDDISIIGYDNIHASRFYSPPLTTIHQSKSRLGVQAVNLLFERINHKSDQRKTIEIHPELVMRKSVKKL","1360772","[FUNCTION] Repressor that binds to the purF operator and coregulates other genes for de novo purine nucleotide synthesis. binds hypoxanthine and guanine as inducers (by similarity). ","purine nucleotide synthesis repressor protein","Cytoplasm","","
InterPro
IPR000843
Domain
Bacterial regulatory protein, LacI
PR00036\"[3-13]T\"[13-23]THTHLACI
PF00356\"[2-27]TLacI
SM00354\"[1-71]THTH_LACI
PS50932\"[2-56]THTH_LACI_2
PS00356\"[4-22]THTH_LACI_1
InterPro
IPR001761
Domain
Periplasmic binding protein/LacI transcriptional regulator
PF00532\"[59-327]TPeripla_BP_1
noIPR
unintegrated
unintegrated
G3DSA:1.10.260.40\"[2-59]Tno description
G3DSA:3.40.50.2300\"[160-307]Tno description


","BeTs to 9 clades of COG1609COG name: Transcriptional regulatorsFunctional Class: KThe phylogenetic pattern of COG1609 is --------vdrlb-efghs--j----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.8e-31) to 2/2 blocks of the IPB000843 family, which is described as \"Bacterial regulatory protein, LacI family\". Interpro entry for IP:IPR000843. IPB000843A 3-23 1.1e-13 IPB000843B 28-66 2.2e-16","Residues 59 to 121 match (3e-08) PD:PD570461 which is described as COMPLETE PROTEOME TRANSCRIPTION DNA-BINDING REGULATION REGULATOR TRANSCRIPTIONAL DEGRADATION B CONTROL ","","","","","","","","","","","Fri Jan 10 11:10:07 2003","Fri Jan 10 11:10:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02003 is paralogously related to AA00749 (9e-30), AA02673 (2e-25), AA02006 (3e-23), AA00932 (2e-10), AA00209 (3e-10) and AA01462 (3e-04).","","","","","","Residues 59 to 332 (E-value = 1.1e-24) place AA02003 in the Peripla_BP_1 family which is described as Periplasmic binding proteins and sugar binding domain of the LacI family (PF00532)","","","","","Meng,L.M., Kilstrup,M. and Nygaard,P. Autoregulation of PurR repressor synthesis and involvement of purR in the regulation of purB, purC, purL, purMN and guaBA expression in Escherichia coli. Eur. J. Biochem. 187(2): 373-379, 1990. PubMed: 2404765. Mauzy,C.A. and Hermodson,M.A. Structural and functional analyses of the repressor, RbsR, of the ribose operon of Escherichia coli Protein Sci. 1 (7), 831-842 (1992) PubMed: 1304369 Rolfes,R.J. and Zalkin,H. Escherichia coli gene purR encoding a repressor protein for purine nucleotide synthesis. Cloning, nucleotide sequence, and interactionwith the purF operator. J. Biol. Chem. 263 (36): 19653-19661 (1988) [PubMed: 3058704].Schumacher,M.A., Choi,K.Y., Lu,F., Zalkin,H. and Brennan,R.G. Mechanism of corepressor-mediated specific DNA binding by the purine repressor. Cell 83 (1): 147-155 (1995) [PubMed: 7553867].Schumacher,M.A., Choi,K.Y., Zalkin,H. and Brennan,R.G. Crystal structure of LacI member, PurR, bound to DNA: minor groove binding by alpha helices. Science 266 (5186): 763-770 (1994) [PubMed: 7973627].","","Fri Jan 10 11:11:42 2003","1","","","" "AA02004","1363177","1362077","1101","ATGACAATAAAAAAAACCACTATTTTTACCCATCAACCTTTACACCTCGTTTTAGGCGGTCAACTTCAACAAATTGACGTGGCTTATCAAACCTATGGTGAATTGAATGCGGATAAAAGCAATGCGGTGTTAATCTGCCACGCGCTTACCGGCGACGCCGAACCTTATTTTGATAAAAGCACAAACCAAGAAGGCTGGTGGCAAAATTTTATGGGCGATGGCTTAGCATTGGACACTTCCCGCTATTTTTTTATTTGTTCCAACGTACTTGGCGGCTGCAAAGGCACGACCGGTCCGTCCTCAATTAATCCGCAAACCAATCGCCCTTACGGCAGCCAATTTCCCGCGGTTATCGTGCAAGACATCATCAAAGTGCAAAAAGCGCTGCTGGATTTTCTTGAAATTCCGCATTTACACGCCATTATCGGCGGTTCCTTTGGCGGTATGCAGGCAACCCAATGGGCGATTGATTATCCCGATTTCGTCTCCAATGTGGTTAATCTATGCTCTTCCCTTTCCTTGAGCGCGGAAGCCATCGGTTTTAATCACGTCATGCGCCAAGCGGTGATGAACGATCCAAATTTCAATAATGGCGATTATTATGACGGCGAGCGCCCGGACAAAGGTTTAGCCATCGCCCGTATGCTCGGTATGCTCACGTATCGCACCGATGTCCAACTCAGCAAAGCCTTCGGACGCGCCACCAAAGCGGAAGGTCATTTGCAGGGCGACTATTTTCAAGTGGAATCCTATTTAAGCTATCAAGGACAAAAATTTCTGGCGCGCTTCGATGCCAACAGTTATTTGCATTTATTACGCGCGTTGGATTTATACGATTCGAGCATCGGCTATGCCGATTTAAAAACCGCTCTTTCTCGAATCAAAGCCCGTTATACACTGGTCTCGGTGGATAACGATCAGCTGTTCAAACTGCCGGAATTACGCAAAAGTAAACAATTACTGGAGCAATACGGCGTCAATTTGAATTATTACGAATTCAACTCCGATTACGGACATGATGCGTTTTTAGTGGACTATGCGTTTTTTGAAAATAAAATCCGTAACGGACTGGCGGGAGGCAATCAAGATTTAACAAAAAAG","","","41075","MTIKKTTIFTHQPLHLVLGGQLQQIDVAYQTYGELNADKSNAVLICHALTGDAEPYFDKSTNQEGWWQNFMGDGLALDTSRYFFICSNVLGGCKGTTGPSSINPQTNRPYGSQFPAVIVQDIIKVQKALLDFLEIPHLHAIIGGSFGGMQATQWAIDYPDFVSNVVNLCSSLSLSAEAIGFNHVMRQAVMNDPNFNNGDYYDGERPDKGLAIARMLGMLTYRTDVQLSKAFGRATKAEGHLQGDYFQVESYLSYQGQKFLARFDANSYLHLLRALDLYDSSIGYADLKTALSRIKARYTLVSVDNDQLFKLPELRKSKQLLEQYGVNLNYYEFNSDYGHDAFLVDYAFFENKIRNGLAGGNQDLTKK","1362076","","homoserine O-acetyltransferase","Extracellular, Cytoplasm","","
InterPro
IPR000073
Domain
Alpha/beta hydrolase fold-1
PF00561\"[83-355]TAbhydrolase_1
InterPro
IPR006296
Family
Homoserine O-acetyltransferase
TIGR01392\"[10-358]ThomoserO_Ac_trn: homoserine O-acetyltransfe
InterPro
IPR008220
Family
Homoserine acetyltransferase
PIRSF000443\"[1-365]THomoserine acetyltransferase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1820\"[106-348]Tno description


","BeTs to 10 clades of COG2021COG name: Homoserine acetyltransferaseFunctional Class: EThe phylogenetic pattern of COG2021 is -om---y--dr----f-hsn-j----Number of proteins in this genome belonging to this COG is","","Residues 179 to 233 match (2e-09) PD:PD486191 which is described as HOMOSERINE ACYLTRANSFERASE TRANSFERASE PROTEOME HTA O- O-ACETYLTRANSFERASE COMPLETE TRANS-ACETYLASE HOMOSERINE-ORTHO-ACYLTRANSFERASE ","","","","","","","","","","","Mon May 23 08:47:59 2005","Mon May 23 08:51:26 2005","","Mon May 23 08:47:59 2005","","Mon May 23 08:47:59 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA02004 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon May 23 08:47:59 2005","","","","","Residues 83 to 355 (E-value = 1.1e-22) place AA02004 in the Abhydrolase_1 family which is described as alpha/beta hydrolase fold (PF00561)","Mon May 23 08:47:59 2005","","","","","","","1","","","" "AA02005","1363283","1364080","798","TTGAAGTCTATAAATAAAGAGATTGGACTTGAATTCTGTGTTTTTTTTCTTTATGTTGAGCACCAGTATTTTTTGACAATAATGCTAATGAAATTGAATTTAAAAGAAAAGTTACAAGCTTATTTAACTGCGACGCAAATTAAACGGATTGGCCGTTATTTTGCCTTGTTTTTTGCGGGTTTTGCTTTGTTATTGATCGTTGTGGATCAAATTATTGGTTATTATGTGCGCAAAGATATTTATTATGACATCGACAAAGTGCCGAACCGCCCGTATGGTTTAGTGCTTGGTACCTCAAAATATTTCTCCAATAACACACTAAATCTGTTCTATTATAATCGTTTACTTGCTGCGCAACGTTTATTTGAAGCAAGAAAAGTGGACTATCTGTTGTTAAGCGGTGATAACCGCACATTGCAATACAACGAACCGCGTACCATGTTGCAGGATTTGAAGAAAATGGGTGTGCCGCAAGAGTTTATTTATCTGGATTTTGCGGGCTTTCGCACATTGGATTCGGTGATTCGTGCCGATCAGGTATTTAAAGCCCATTCCCTGACGATTATTTCGCAGAAATTTCATTGTGAACGCGCTTTATTCATCGCTAAATTCCACAATATTGACGCCATTTGTTTTGCGGCGGATTATCCGCAGGTGTATTCTTTCGTGCGTGTACGGGAATTTTTTGCCCGTTTGCAGGCTGTGTGGGATTTATTGGTAGAAAGGGAACCGCACTTTTTGGGGGCGCCGGAACCTTTGCCCCCGCCGGTGACGATTCCCGATGTTAACAGTGATATT","","","31135","LKSINKEIGLEFCVFFLYVEHQYFLTIMLMKLNLKEKLQAYLTATQIKRIGRYFALFFAGFALLLIVVDQIIGYYVRKDIYYDIDKVPNRPYGLVLGTSKYFSNNTLNLFYYNRLLAAQRLFEARKVDYLLLSGDNRTLQYNEPRTMLQDLKKMGVPQEFIYLDFAGFRTLDSVIRADQVFKAHSLTIISQKFHCERALFIAKFHNIDAICFAADYPQVYSFVRVREFFARLQAVWDLLVEREPHFLGAPEPLPPPVTIPDVNSDI","1364079","[FUNCTION] Participates in the barrier function of the cell envelope (by similarity). ","vancomycin sensitivity; SanA protein","Inner membrane, Cytoplasm","","
InterPro
IPR003848
Domain
Protein of unknown function DUF218
PF02698\"[89-231]TDUF218
noIPR
unintegrated
unintegrated
tmhmm\"[14-34]?\"[55-75]?transmembrane_regions


","BeTs to 4 clades of COG2949COG name: Uncharacterized membrane proteinFunctional Class: SThe phylogenetic pattern of COG2949 is ---------d----e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 80 to 218 match (9e-59) PD:PD006234 which is described as COMPLETE PROTEOME MEMBRANE SANA TRANSMEMBRANE PLASMID INTEGRAL INNER VANCOMYCIN SENSITIVITY ","","","","","","","","","","","Fri Jan 10 11:22:30 2003","Fri Jan 10 11:22:30 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02005 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Rida,S., Caillet,J. and Alix,J.H. 1996. Amplification of a novel gene, sanA, abolishes a vancomycin-sensitive defect in Escherichia coli. J. Bacteriol. 178(1): 94-102. PubMed: 8550448.","","Fri Jan 10 11:22:30 2003","1","","","" "AA02006","1365053","1364070","984","GTGAAATTAGATGAAATAGCCAAGCTTGCGGGCGTTTCCTGCACCACGGTGAGCTACGTTGTGAACGGAAAAGCCAAACAGTATCGTGTAAGCGATAGCACTATCGAAAAAGTCCAAGCCTTGATTAAACAGTATGACTTTAAACCTAACGCCATGGCGGCAAGCCTGCGCGTGGGGAAAAGTAAAACCATCGGTTTAGTGATTCCCGATTTTGAAAATATCAGTTATGCGAAAATCGCCAATAATCTGGAAAATCGTTTACGGGAAAAAGGCTATCAACTACTCATCGCCTGTTCTAACGACAAAGTGGAAAATGAGCAAGATTGCGTGAAACATTTATTACAACGTCAGGTTGATGCATTGTTGGTTTCCTCAGCACTGCCACCGAACACAGATTTTTACCAAAACGCCAGCGTGCCGATTATCGGTTTTGATCGCCGTATTAGCTCCCCGAAAGTGGTGAATGCCCTGACCGACGATGAAGGCGATGCATATCGTTTAACGAAGGAATTGTTGAAAATCCCTCATCAAAAAAGAATTTTGTTCTTCGGTGCGTTACCGGATTTGCCGACAAGCCGGGAACGGGAAGAAGGATTTCGCTCGGCATTAAGGTATCGGAAGGCTTCCGCCAAATATCTTTACGGCGATATGTTCCGTAAAAACGAAGCGGCGCAATGTTTTGCCCAATGGTTAGAAAATAATCCGTTACCAACGGCAATTTTCACCACGTCTTTTACCTTGTTGGAAGGAGTGTTATTGGTCTTGTTGCAAAAACTGGGACAGGTGCCGAAAGACTTAGTGGTTGCCACCTTCGGGCATGTTGAGATGTTAGAGCTACTGGAAAACAGAGTACTGTGCAGCGTGCAGGATTATGACAAAGTGTCGCAATCTTTGCTGACATTGACCTTTGATGCCATGTCGAAGAAACACAAAAACAGCGTCAATACAACGCCGTTAACCCGCAGTATTATTAAATATCACTGT","","","36896","VKLDEIAKLAGVSCTTVSYVVNGKAKQYRVSDSTIEKVQALIKQYDFKPNAMAASLRVGKSKTIGLVIPDFENISYAKIANNLENRLREKGYQLLIACSNDKVENEQDCVKHLLQRQVDALLVSSALPPNTDFYQNASVPIIGFDRRISSPKVVNALTDDEGDAYRLTKELLKIPHQKRILFFGALPDLPTSREREEGFRSALRYRKASAKYLYGDMFRKNEAAQCFAQWLENNPLPTAIFTTSFTLLEGVLLVLLQKLGQVPKDLVVATFGHVEMLELLENRVLCSVQDYDKVSQSLLTLTFDAMSKKHKNSVNTTPLTRSIIKYHC","1364069","[FUNCTION] Represses some operons but activates others. It is implicated in the regulation of a large number of operons encoding enzymes which comprise central pathways of carbon metabolism. Binds D-fructose as an inducer. ","PEP--fructosephosphotransferase system repressor, DeoR family","Cytoplasm","","
InterPro
IPR000843
Domain
Bacterial regulatory protein, LacI
PF00356\"[1-26]TLacI
SM00354\"[1-73]THTH_LACI
PS50932\"[1-58]THTH_LACI_2
PS00356\"[3-21]THTH_LACI_1
InterPro
IPR001761
Domain
Periplasmic binding protein/LacI transcriptional regulator
PF00532\"[61-327]TPeripla_BP_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2300\"[55-184]Tno description


","BeTs to 8 clades of COG1609COG name: Transcriptional regulatorsFunctional Class: KThe phylogenetic pattern of COG1609 is --------vdrlb-efghs--j----Number of proteins in this genome belonging to this COG is","Significant hit ( 3.1e-24) to 2/2 blocks of the IPB000843 family, which is described as \"Bacterial regulatory protein, LacI family\". Interpro entry for IP:IPR000843. IPB000843A 2-22 2e-08 IPB000843B 30-68 2.6e-14","Residues 125 to 213 match (1e-15) PD:PD583544 which is described as REPRESSOR COMPLETE PROTEOME TRANSCRIPTION REGULATION FRUCTOSE DNA-BINDING ACTIVATOR CATABOLITE REPRESSOR/ACTIVATOR ","","","","","","","","","","","Fri Jan 10 11:28:29 2003","Fri Jan 10 11:28:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02006 is paralogously related to AA02003 (3e-23), AA02673 (2e-11), AA00749 (9e-11) and AA00209 (7e-08).","","","","","","Residues 1 to 26 (E-value = 6.4e-09) place AA02006 in the LacI family which is described as Bacterial regulatory proteins, lacI family (PF00356)","","","","","Jahreis,K., Postma,P.W. and Lengeler,J.W. Nucleotide sequence of the ilvH-fruR gene region of Escherichia coli K12 and Salmonella typhimurium LT2. Mol. Gen. Genet. 226 (1-2): 332-336 (1991) PubMed: 1851954.Vartak,N.B., Reizer,J., Reizer,A., Gripp,J.T., Groisman,E.A., Wu,L.F., Tomich,J.M. and Saier,M.H. Jr. Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding protein. Res. Microbiol. 142 (9): 951-963 (1991) PubMed: 1805309.El Hanafi,D. and Bossi,L. Activation and silencing of leu-500 promoter by transcription-induced DNA supercoiling in the Salmonella chromosome. Mol. Microbiol. 37 (3): 583-594 (2000) [PubMed: 10931352].","","Wed Feb 5 13:22:36 2003","1","","","" "AA02007","1365888","1366142","255","TTGTTACAAAAAGAAGTTTGTTTATTACAGAGAAATTCCTTTTTAGTCGGTTTAACTTCGGGTATTTTAAGAAAAAATCTCTGTAATTTTTACAGAATCAAAATTGATAACGCTACGCCAATTTTGCACACCGAATTTTTAAATATTAGATTTGTTGAAGACGGACGCAAAGATAGCGTAGTAAAATTTGTCTCTACCCTTGCACCATCCACTCCGCCGTTTTATTGCTTATTATCTGAATTGAATGAAGAAGAA","","","9743","LLQKEVCLLQRNSFLVGLTSGILRKNLCNFYRIKIDNATPILHTEFLNIRFVEDGRKDSVVKFVSTLAPSTPPFYCLLSELNEEE","1366141","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Fri Jan 10 11:29:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02007 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02008","1366534","1366184","351","TTGGATGGTATAGAGATTACCAATGAATCATTCCACACGTTACTTCCGCGTTTTATCAATGACGAAAGGGCGGTATTTGTGTTAGACCCGCCATATTTGTGTACGAAACAAGAGAGCTATAAGCAAGCGCATTATTTCGATCTTATCGACTTCCTACGCTTAATTAACATTACACGACCACCGTATATCTTCTTCTCATCGACAAAAAGCGAGTTCGTGCGGTTTATTGAGTATATGTGTGAAGATAAAGTCAATAACTGGCAGGCATTTGATGGCGCCCAAAGAATTACGATTAAGACAAACCTCAACTATCAAGGGCAATATGAAGATAATTTAGTGTATAATTTTATA","","","14007","LDGIEITNESFHTLLPRFINDERAVFVLDPPYLCTKQESYKQAHYFDLIDFLRLINITRPPYIFFSSTKSEFVRFIEYMCEDKVNNWQAFDGAQRITIKTNLNYQGQYEDNLVYNFI","1366183","","conserved hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","Residues 1 to 40 match (2e-10) PD:PD358937 which is described as PROTEOME COMPLETE NMA1821 HI1523 ","","","","","","","","","","","","Fri Jan 10 11:30:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02008 is paralogously related to AA01841 (9e-51).","","","","","","","","","","","","","","1","","","" "AA02010","1367799","1367320","480","ATGAAAAAATTTATCGCATTAATTCTGATGGCAGTTAGCTTGAACAGCTTCGCAGAAGGAGAAAATTCATTGAAAGATGTGCAGTTTAAAGATCTTAACAACGCCACGGTTACACTGGATCAGGTAACCAGCAAAGGCAAACCGGTTTATGTCAAAATGTGGGCATCTTGGTGTCCGATCTGCTTGGCCGGATTAGCGGAAATCAACGAATTAAGTGGAGAGCCGAACAAAAACTTCGATGTAATTACCATAGTTTCACCGGGCAAAAAAGGGGAAAAAGAAACGCAAGATTTCATCGACTGGTACAAAGGATTAGATTATAAAAATATCATTGTATTATTAGATGAAAATGGCGAAACCCTCAAACGTGCCAAAGTGCGTGGCTACCCTTCCAGCGTATTGCTTGATACGGATTTGAATATCCAAAAAACCGTACCGGGACATTTAGGCACGGCGCAAATTAAACAGCTGGCAGGAAAT","","","17902","MKKFIALILMAVSLNSFAEGENSLKDVQFKDLNNATVTLDQVTSKGKPVYVKMWASWCPICLAGLAEINELSGEPNKNFDVITIVSPGKKGEKETQDFIDWYKGLDYKNIIVLLDENGETLKRAKVRGYPSSVLLDTDLNIQKTVPGHLGTAQIKQLAGN","1367319","[FUNCTION] Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxidein proteins to methionine (by similarity). [CATALYTIC ACTIVITY] protein l-methionine + oxidized thioredoxin = protein l-methionine s-oxide + reduced thioredoxin.[DOMAIN] Possesses 2 methionine sulfoxide reductase domains (a/msrA and B/msrB) and 1 N-terminal thioredoxin domain. the domain B exhibits a thioredoxin dependent methionine sulfoxide reductase activity; the cys-495 is probably involved in the reduction of metSO and in formation of the sulfenic acidderivative. Tthe regeneration of cys-495 is probably done via formation of a disulfide bond with cys-440 followed by its reduction by thioredoxin.","peptide methionine sulfoxide reductase; cytochrome C-TYPE biogenesis protein; transcriptional regulator","Periplasm","","
InterPro
IPR006662
Domain
Thioredoxin-related
PR00421\"[49-57]T\"[57-66]T\"[125-136]TTHIOREDOXIN
InterPro
IPR011594
Domain
Thioredoxin-like
PD003679\"[67-157]TQ8RGU0_FUSNN_Q8RGU0;
InterPro
IPR012335
Domain
Thioredoxin fold
G3DSA:3.40.30.10\"[21-155]Tno description
InterPro
IPR013740
Domain
Redoxin
PF08534\"[19-157]TRedoxin
noIPR
unintegrated
unintegrated
signalp\"[1-20]?signal-peptide


","No hits to the COGs database.","","Residues 26 to 79 match (4e-17) PD:PD585994 which is described as COMPLETE PROTEOME HI1453 THIOREDOXIN FAMILY SPY1558 SIGNAL PRECURSOR ","","","","","","","","","","","Fri Jan 10 11:38:23 2003","Fri Jan 10 11:38:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02010 is paralogously related to AA00054 (3e-06).","","","","","","","","","","","","","","1","","","" "AA02011","1368455","1367817","639","ATGTTTGATCAACAATTATTAATCGGCACCGTATTCTTAGCGGGTTTAGCCTCCTTTTTGTCGCCTTGCATTTTCCCCATTATCCCGATTTATTTCGGCATCTTGGCGAAAGGCGGTAGAAAAATTATGAACACCTTTTTGTTCATTGCAGGTTTATCTTTAACCTTCGTCAGCCTAGGCTTCAGCTTCGGATTTTTAGGCAATTTATTCTTTAACGATAACGTGCGCATTATTGCCGGCATTATCGTGATTATTCTGGGAATCCATCAATTAGGTATTATCAAATTGAATTTCCTGGAAAGAACCAAAGTAGTTGAAGTAAAAACTGAAGGCAAAAGTGCCTCTTTTGAAGCCTTTTTCCTAGGGCTTACCTTCAGCCTTGGCTGGACACCTTGTATTGGACCGATTTTAGCATCTGTTCTGGCGTTGTCCGGCGATGAAGGTTCCGCTCTATACGGTGCTTCTATGATGTTGGTTTATGTATTAGGTTTGGCAACGCCGTTTGTACTCTTCTCTTTATTCTCACAAGAGTTACTAAAACGCACCAAAGCACTAAACAAACACTTAGACAAATTTAAAATTATCGGTGGTTTACTCATTATCGTCATGGGGATTCTACTCATCACTAATAAATTACAA","","","23145","MFDQQLLIGTVFLAGLASFLSPCIFPIIPIYFGILAKGGRKIMNTFLFIAGLSLTFVSLGFSFGFLGNLFFNDNVRIIAGIIVIILGIHQLGIIKLNFLERTKVVEVKTEGKSASFEAFFLGLTFSLGWTPCIGPILASVLALSGDEGSALYGASMMLVYVLGLATPFVLFSLFSQELLKRTKALNKHLDKFKIIGGLLIIVMGILLITNKLQ","1367816","","cytochrome C-type biogenesis protein","Inner membrane, Cytoplasm","","
InterPro
IPR003834
Domain
Cytochrome c biogenesis protein, transmembrane region
PF02683\"[11-209]TDsbD
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide
tmhmm\"[10-30]?\"[45-65]?\"[75-93]?\"[119-141]?\"[151-171]?\"[192-210]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 8.6e-10) to 2/2 blocks of the IPB003834 family, which is described as \"Cytochrome c biogenesis protein transmembrane region\". Interpro entry for IP:IPR003834. IPB003834A 12-26 3.3e-08 IPB003834B 58-67 9.9","Residues 12 to 193 match (3e-49) PD:PD003510 which is described as PROTEOME COMPLETE CYTOCHROME BIOGENESIS C-TYPE INTERCHANGE MEMBRANE TRANSMEMBRANE REDOX-ACTIVE THIOL:DISULFIDE ","","","","","","","","","","","","Fri Jan 10 12:49:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02011 is paralogously related to AA02907 (2e-13).","","","","","","Residues 11 to 209 (E-value = 3.5e-85) place AA02011 in the DsbD family which is described as Cytochrome C biogenesis protein transmembrane region (PF02683)","","","","","","","","1","","","" "AA02012","1369529","1368462","1068","ATGAAAAAATCAAAATTAGTTGTGGCGTTAGCCGCAATTTTATCTTGTGCAGCAATCCCGACAACCGTTATGGCAGAAAGTAACGTTCAACAAACTATGGAGAAAAGCAATATGTCCGAAGCTAAAAAAGATCTTCACGAAATTTATTTGGCTGGTGGCTGCTTCTGGGGCATAGAGGCTTATATGGAGCGCATTTACGGCGTGGAAGATGCGATTTCAGGATACGCTAATGGTAAAAGTGACAAAACCAATTACCAAAAGATCGGCATTACCGATCATGCAGAAACGGTCAAAGTAACTTATGACCGCAATAAAGTTTCCTTGGATAAATTGTTAAAATACTATTTCCAAGTTATTGATCCGACCAGCGTGAACAAACAAGGTAATGATCGCGGTAGACAATATCGTACCGGTATTTATTATCAAGATACTGCTGATAAGTCTATAATTGAAAAAGAAATTACTGCTTTGCAAGGAAAGTATAAAAATAAAATTCAGATTGAAGTGGAACCGCTACATAACTATATCGTAGCAGAAGAATACCATCAGGATTATTTGAAGAAAAACCCAAACGGCTATTGCCATATTGATTTGGAACAGGCCAATTATGTTATTATTGACGAAAAAGATTATCCGAAACCGAGCGATGCGGAACTGAAAGCTAAATTGACCCCGCTGCAATATAGCGTCACGCAAAACAAAAATACCGAGCATTCTTTCAGCAACGAATACTGGGATAACTTTAAACCGGGTATTTATGTGGATGTCACCACCGGTGAACCACTTTTCTCTTCTAAAGATAAATTTGAATCCGGTTGTGGCTGGCCAAGTTTCACCAAACCGATTACAAAAGAGGTCGTCACCTATCAGGACGATCACAGTTTCAACATGCTCAGAACGGAAGTAATAAGCCGCAGTGGTAAAGCTCATTTAGGACATGTTTTTGATGACGGTCCAAAAGACAAAGGCGGTTTGCGCTATTGCATTAATAGTGCCGCAGTTAAATTTATTCCGTTAGAAGACATGGTAAAAGAAAACTATGGTTATCTAACCAATGCTGTAAAGGAG","","","41383","MKKSKLVVALAAILSCAAIPTTVMAESNVQQTMEKSNMSEAKKDLHEIYLAGGCFWGIEAYMERIYGVEDAISGYANGKSDKTNYQKIGITDHAETVKVTYDRNKVSLDKLLKYYFQVIDPTSVNKQGNDRGRQYRTGIYYQDTADKSIIEKEITALQGKYKNKIQIEVEPLHNYIVAEEYHQDYLKKNPNGYCHIDLEQANYVIIDEKDYPKPSDAELKAKLTPLQYSVTQNKNTEHSFSNEYWDNFKPGIYVDVTTGEPLFSSKDKFESGCGWPSFTKPITKEVVTYQDDHSFNMLRTEVISRSGKAHLGHVFDDGPKDKGGLRYCINSAAVKFIPLEDMVKENYGYLTNAVKE","1368461","[FUNCTION] Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).[CATALYTIC ACTIVITY] Protein L-methionine + oxidized thioredoxin = protein L-methionine S-oxide + reduced thioredoxin.","peptide methionine sulfoxide reductase","Periplasm, Extracellular","","
InterPro
IPR002569
Domain
Methionine sulfoxide reductase A
PD003489\"[67-194]TPMSR
G3DSA:3.30.1060.10\"[3-195]TMsrA
PF01625\"[46-199]TPMSR
TIGR00401\"[46-194]TmsrA
SSF55068\"[9-194]TMsrA
InterPro
IPR002579
Domain
Methionine sulfoxide reductase B
PD004057\"[216-354]TDUF25
PF01641\"[216-339]TSelR
TIGR00357\"[213-347]TMsrB
InterPro
IPR011057
Domain
Mss4-like
SSF51316\"[211-354]TMss4_like
noIPR
unintegrated
unintegrated
G3DSA:2.170.150.20\"[204-355]TG3DSA:2.170.150.20
PTHR10173\"[47-128]T\"[220-338]TPTHR10173
PS51257\"[1-16]FPROKAR_LIPOPROTEIN


","BeTs to 10 clades of COG0225COG name: Peptide methionine sulfoxide reductaseFunctional Class: OThe phylogenetic pattern of COG0225 is -om---y--drlbcefghsnuj--twNumber of proteins in this genome belonging to this COG is","Significant hit ( 8.4e-47) to 3/3 blocks of the IPB002569 family, which is described as \"Peptide methionine sulfoxide reductase\". Interpro entry for IP:IPR002569. IPB002569A 50-59 8e-05 IPB002569B 107-140 9.3e-21 IPB002569C 165-194 2.1e-18Significant hit ( 3.1e-40) to 5/5 blocks of the IPB002579 family, which is described as \"Domain of unknown function DUF25\". Interpro entry for IP:IPR002579. IPB002579A 212-220 43 IPB002579B 236-244 0.27 IPB002579C 251-278 7.4e-22 IPB002579D 304-315 5.7e-05 IPB002579E 326-336 1.9e-06","","","","","","","","","","","","Fri Jan 10 12:54:09 2003","Fri Jan 24 13:41:26 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02012 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 216 to 339 (E-value = 1.1e-84) place AA02012 in the SelR family which is described as SelR domain (PF01641)","","","","","Etienne F, Spector D, Brot N, Weissbach H.A methionine sulfoxide reductase in Escherichia coli that reduces the R enantiomer of methionine sulfoxide.Biochem Biophys Res Commun. 2003 Jan 10;300(2):378-82.PMID: 12504094Bar-Noy S, Moskovitz J.Mouse methionine sulfoxide reductase B: effect of selenocysteine incorporation on its activity and expression of theseleno-containing enzyme in bacterial and mammalian cells.Biochem Biophys Res Commun. 2002 Oct 4;297(4):956-61.PMID: 12359247Kauffmann B, Favier F, Olry A, Boschi-Muller S, Carpentier P, Branlant G, Aubry A.Crystallization and preliminary X-ray diffraction studies of the peptide methionine sulfoxide reductase B domain of Neisseriameningitidis PILB.Acta Crystallogr D Biol Crystallogr. 2002 Sep;58(Pt 9):1467-9.PMID: 12198304","","Fri Jan 31 15:57:39 2003","1","","","" "AA02013","1369745","1370434","690","ATGAAAAAAATAGAACAACTTTTTGCCAATAATTACCGCTGGGCAACTCGTATGAAAGAGGAAAATTCCACCTATTTTCAGGAATTGGCGGAGCACCAGCAGCCCCATTATTTGTGGATCGGTTGTTCGGACAGTCGTGTGCCTGCGGAGAAATTAACCAACCTGGAACCGGGAGAATTATTTGTGCATCGTAATGTTGCAAATCAGGTGATTCACACCGATTTAAACTGCCTTTCCGTAGTGCAATATGCGGTGGATGTGTTGAATATTGAGCATATTATCATCTGCGGACATACGAATTGCGGCGGTATTCATGCGGCAACGAACGATCAGGATTTAGGGTTGATAAATAACTGGTTGTTACATATTCGCGATATTTGGTTTAAGCACAGTCACTTGCTTGGTAATCTTTCCCCGGAGCGCCGTGCCGATATGCTGACAAAATTAAACGTTGCGGAACAGGTATATAACCTGGGACGTTCGTCTATTGTGAAAAATGCCTGGAAGAATGGGAAAAAATTGTCGTTGCACGGTTGGGTATATGATGTAAAAGACGGCTTTTTAATCGACCAGGGCGTGATGGCGACCAGTCGTGAAAGCCTGGAAATTTCTTATCGCAATGCTATTTCCCGTTTGTTGAAATTAAATGAAGAAGAAATGTTGAAAAAGGCGCACGAGCTGGATGCGGAA","","","26470","MKKIEQLFANNYRWATRMKEENSTYFQELAEHQQPHYLWIGCSDSRVPAEKLTNLEPGELFVHRNVANQVIHTDLNCLSVVQYAVDVLNIEHIIICGHTNCGGIHAATNDQDLGLINNWLLHIRDIWFKHSHLLGNLSPERRADMLTKLNVAEQVYNLGRSSIVKNAWKNGKKLSLHGWVYDVKDGFLIDQGVMATSRESLEISYRNAISRLLKLNEEEMLKKAHELDAE","1370433","[FUNCTION] Reversible hydratation of carbon dioxide. Carbon dioxide formed in the bicarbonate-dependent decomposition of cyanate by cyanase (cynS) diffuses out of the cell faster than it would be hydrated to bicarbonate, so the apparent function of this enzyme is to catalyze the hydration of carbon dioxide and thus prevent depletion of cellular bicarbonate. ","carbonic anhydrase","Cytoplasm","","
InterPro
IPR001765
Domain
Carbonic anhydrase, prokaryotic and plant
G3DSA:3.40.1050.10\"[1-220]Tno description
PF00484\"[30-192]TPro_CA
PS00704\"[42-49]TPROK_CO2_ANHYDRASE_1
PS00705\"[82-102]TPROK_CO2_ANHYDRASE_2
noIPR
unintegrated
unintegrated
PTHR11002\"[7-218]TCARBONIC ANHYDRASE
PTHR11002:SF1\"[7-218]TCARBONIC ANHYDRASE


","BeTs to 14 clades of COG0288COG name: Carbonic anhydraseFunctional Class: PThe phylogenetic pattern of COG0288 is -om---y--drlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 1e-63) to 4/4 blocks of the IPB001765 family, which is described as \"Prokaryotic-type carbonic anhydrase\". Interpro entry for IP:IPR001765. IPB001765A 28-71 4.6e-30 IPB001765B 76-100 6e-15 IPB001765C 115-127 0.0049 IPB001765D 156-191 1.5e-11","Residues 7 to 155 match (3e-07) PD:PD430502 which is described as PROTEOME COMPLETE CARBONIC ANHYDRASE ","","","","","","","","","","","Fri Jan 10 12:59:17 2003","Tue Jan 28 14:52:18 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02013 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 30 to 192 (E-value = 1.7e-75) place AA02013 in the Pro_CA family which is described as Carbonic anhydrase (PF00484)","","","","","Guilloton,M.B., Korte,J.J., Lamblin,A.F., Fuchs,J.A. and Anderson,P.M. Carbonic anhydrase in Escherichia coli. A product of the cyn operon . J. Biol. Chem. 267 (6): 3731-3734 (1992) PubMed: 1740425.Sung,Y.C. and Fuchs,J.A. Characterization of the cyn operon in Escherichia coli K12 . J. Biol. Chem. 263 (29): 14769-14775 (1988) PubMed: 3049588.","","Tue Jan 28 14:52:18 2003","1","","","" "AA02014","1371037","1370546","492","TTGCCGGAAGCAACCAAAGTGGCAACCGACCCAAAAACCTTCGGTACACAAATTGATGACGAAACCCTTGAAACCCGCGTGGATTCGGCAATCAGAAAAGACCAACAACTTAAATCCGAAGCGCGTATCAGCGTCACCTCTTACAGCGGTCGTGTGTTATTGACCGGTCAGGTTCCAAACGAAAGTTTGCGCGAAGTCGCCACCAGTTTGGCGAAAGGCGTACCAAACGTCAATGATGTGTACAACGAAGTGCGCGTCGGCCCCAAAGTGAATTTCGCTCAAATCAGCAAAGACAGTTGGATCACCAGCCAAATCAAATCCAAGATGTTGATTGATTCCAAAGTAAAAACCAGCGACATCAAAGTCGTCACCGAAAATAACGAAGTATTCCTGATGGGTAACGTTACTCAGGATCAAGCCAACGCCGCCGCAAAAATCGCGCGTAACGTGGCGGGGGTAGCGAAAGTGATTAAGGTGTTCAATTATTTAAAC","","","18857","LPEATKVATDPKTFGTQIDDETLETRVDSAIRKDQQLKSEARISVTSYSGRVLLTGQVPNESLREVATSLAKGVPNVNDVYNEVRVGPKVNFAQISKDSWITSQIKSKMLIDSKVKTSDIKVVTENNEVFLMGNVTQDQANAAAKIARNVAGVAKVIKVFNYLN","1370545","","probable hemolysin","Periplasm, Cytoplasm","","
InterPro
IPR007055
Domain
Transport-associated
PF04972\"[24-88]T\"[102-161]TBON
PS50914\"[19-88]T\"[97-164]TBON
InterPro
IPR014004
Domain
Transport-associated and nodulation region, bacteria
SM00749\"[24-87]T\"[102-163]TBON


","BeTs to 6 clades of COG2823COG name: Predicted periplasmic or secreted lipoproteinFunctional Class: RThe phylogenetic pattern of COG2823 is --------------efgh-n--x---Number of proteins in this genome belonging to this COG is","","Residues 4 to 162 match (5e-47) PD:PD337487 which is described as PROTEOME COMPLETE SIGNAL LIPOPROTEIN PERIPLASMIC PRECURSOR HEMOLYSIN YRAP PA4426 RSC3264 ","","","","","","","","","","","","Fri Jan 10 13:29:13 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02014 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 102 to 161 (E-value = 2e-14) place AA02014 in the BON family which is described as Putative phospholipid-binding domain (PF04972)","","","","","Madrid C, Nieto JM, Paytubi S, Falconi M, Gualerzi CO, Juarez A. Temperature- and H-NS-dependent regulation of a plasmid-encoded virulence operon expressing Escherichia coli hemolysin. J Bacteriol. 2002 Sep;184(18):5058-66. PMID: 12193622 Ito,H., Uchida,I., Sekizaki,T. and Terakado,N. A cryptic DNA sequence, isolated from Actinobacillus pleuropneumoniae, confers a hemolytic activity upon Escherichia coli K12 strains. J. Vet. Med. Sci. 55 (1): 173-175 (1993) [PubMed: 8461417].","","Fri Jan 10 13:29:13 2003","1","","","" "AA02015","1371780","1371199","582","ATGCAAAACAAACTCAATGATTTATATGAGGAAAATATTAAAACTCATATTTATTCAAAAAGCCTGCTCAGCGCACAAATCGTCGAAGCGACGCAACACCTGATTGCCTGCCTGTTGCGTGGTAATAAAGTCATTGTCTGCGGTGACGGTCGTTCTTACATTAATGCGCAATGTCTGGTGGCGAATTTGCTTAACCGTTATGATCTAAAACGTCCGAGTTTTCCTTCCGTGTTATTGAGCCTGGATAGTGCGGTCGGTTCCACTTTCGTTTCCGACAATACGCTGGAAAAACTGTATCAACACCAATTCAGCGCCATCGCGCGGTCCGGCGATATTTTGGTGGCATTCGCACCTTTAGGAAATGAAAAAAATGTGCTCAATACAATTACACATGCCGTGAACAAAGAGATTAATGTGATTGTCTTAACGGGTAACAGTAACGATCATATTCAGGGAATTTTGACAGACAAAGATTTACAAATCGCCGTGCCGAGCAGTAAGGAAAGTCGCATACTGGAGAACCATTTATTCATTATTAACAGTATGTGTGAACTCATTGATTTTCAATTATTTTCACATTCG","","","21537","MQNKLNDLYEENIKTHIYSKSLLSAQIVEATQHLIACLLRGNKVIVCGDGRSYINAQCLVANLLNRYDLKRPSFPSVLLSLDSAVGSTFVSDNTLEKLYQHQFSAIARSGDILVAFAPLGNEKNVLNTITHAVNKEINVIVLTGNSNDHIQGILTDKDLQIAVPSSKESRILENHLFIINSMCELIDFQLFSHS","1371198","","phosphoheptose isomerase","Cytoplasm","","
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.10490\"[4-190]Tno description


","No hits to the COGs database.","","Residues 35 to 166 match (6e-14) PD:PD000868 which is described as COMPLETE PROTEOME ISOMERASE TRANSCRIPTIONAL REGULATOR TRANSCRIPTION PHOSPHOHEPTOSE FAMILY DOMAIN ATP-BINDING ","","","","","","","","","","","","Mon Jan 27 15:23:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02015 is paralogously related to AA00860 (1e-17).","","","","","","","","","","","","","","1","","","" "AA02017","1372152","1371796","357","ATGTTATCACCAAAACGTCAACAAGGGGCGAGATTTGAACAAAAAGCTCGCCTCTTTTTAGAATCTAAAGGCATGAAATTTCTCGCCGCCAACCAAAATTTCAAGTGCGGCGAACTGGATTTAATTATGTTGGAACAAAATACCATCGTATTTGTGGAAGTGCGCCAACGTAAAAATGATCATTTTGGCTCTGCCGTGGAAAGCGTAGATTGGCAAAAGCAACAACGCTGGCTGAATGCGGCAGCACTTTGGCTGGCACAACGGGAACAAAGTTTAGAAGACACCGATTGCCGTTTCGATTTGGTCGCGTTTGGTAAAACCGATCAAGACATTCAATGGATCTCCAACTTTCTTGAT","","","14265","MLSPKRQQGARFEQKARLFLESKGMKFLAANQNFKCGELDLIMLEQNTIVFVEVRQRKNDHFGSAVESVDWQKQQRWLNAAALWLAQREQSLEDTDCRFDLVAFGKTDQDIQWISNFLD","1371795","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003509
Family
Protein of unknown function UPF0102
PF02021\"[11-105]TUPF0102
TIGR00252\"[1-119]TTIGR00252: conserved hypothetical protein T


","BeTs to 14 clades of COG0792COG name: Predicted endonuclease distantly related to archaeal Holliday junction resolvaseFunctional Class: LThe phylogenetic pattern of COG0792 is -------qvdr--cefghsnuj--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 5.3e-30) to 2/2 blocks of the IPB003509 family, which is described as \"Uncharacterised protein family UPF0102\". Interpro entry for IP:IPR003509. IPB003509A 13-55 2e-21 IPB003509B 69-86 3.6e-07","Residues 5 to 88 match (2e-14) PD:PD463292 which is described as PROTEOME COMPLETE YRAN ENDONUCLEASE TP0913 ML1607 RV2898C SCO5602 ORF ","","","","","","","","","","","","Fri Jan 10 13:34:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02017 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 11 to 105 (E-value = 2.5e-42) place AA02017 in the UPF0102 family which is described as Uncharacterised protein family UPF0102 (PF02021)","","","","","","","","1","","","" "AA02018","1373880","1372165","1716","ATGCCTATTCTATTACAACGCATTAATTTAAAAAATCGATTAATGCCCTTTTTATTTACGCTCTTTTTAGCCGGTTGTACGACGAATTTCTTCGGCAGCAGCTTCACCGGCGAGCTAAAAAAAGATGCGAATGCGAGCTCCGAATTTTACATGAACAAAATCGGACAAACACAAGATATTGAAGATCAGCAAACCTATAAACTTTTAGCTGCACGCGTTTTAGTTACCGAAAATAAAGTGGCGCAAGCGCAATCTTTATTAAATGAATTGACCGAGTTAAATCCGGAACAATTATTGGATAAAACGTTGATTGATGCCGATATTGCGGCAGTGAAAGGTCAAAATAACGAAGCGGAAAACTTACTCAAAGGCATTGATTTAACCCAATTAAGCTCCTCTCAGGTCGGGCGTTATTACGCAGTGAAAGCCCGTGTTGCAGAAAACCAAAATGCCATTATTGATGCGGTGAAAGCGCGCATTGAAATGGATCATGTGTTGAGCGACATACAAAGAAAACAGGAAAATAATGACCGCACTTGGGCGTTATTACGTCGTACTAATCGTGGTTTAATCCACAATACGTCCGATGAAGGCAATTTGGCGTTAGCCGGTTGGTTGGCACTAGCCCGCGCCTATAACGATAACTTAAATCAAGCGACTCAATTAAGTCAGGCATTACAAAGCTGGAAGTCATCCTATCCGAACCACTCCGCCGCCTATTTATTCCCAACCGAGTTACAAGGTTTATTTAACTTCCAACAAACTGCCCTTTCACAAATCGGTTTGCTTTTACCGTTAAGCGGTAACGGTCAGGTTTTGGGCAATACCATCAAATCCGGTTTTGATGCGGCAAAAGGCGAAGATACCACCATTCAGGTGCAGGTGTACGACACCGTAGCCACCCCGATGAACGAAATCATCGAACAAGCCAGACAAGCAGGCGTACGCGCCCTTATCGGTCCGTTATTGAAACAAAACGTAGATGTTATTTTGAACAATCCGTCCGCTATTCAGGGTTTAGATGTGCTTGCATTGAATTCTACCCCGAATGCCCGCGCTATCGGTCAGGTTTGTTACTATGGTTTATCGCCTGAAGACGAAGCGGAATCCGCCGCCAACAAAATGTGGCGTGACGGCATTCGCGAACCGATGGTCGCGGTGCCGCAAAATGATTTAGGACAACGCACCGCAACCGCATTTAATGTGCGTTGGCAACAATTAGCCGGCACCGATGCAAATATCAAATATTACAACCAAGCCGGTGATGTCGGCGTTGCGCTCCAAGGACAAAGCGTACAAGGGCTTTATATCGTTGCGAAAAGTGAAGAATTATCCGACTTGAAAAGCGTGATTGATAACAGCGGCAACAACATTAAATTGTACGCCAGCTCACGCAGCAACTCTTCCAATAACGGTCCGGAATACCGTTTATTGATGAACGGACTGCAATTCAGCGATATTCCATTCTTTAAAGATACGGATTCCGCGCAATATCAAAAAGTGGCGACCGAAACCAATAACGATTATTCCTTAATGCGTTTATATGCGATGGGTGCTGATTCCTGGTTATTAATCAACCACTTCAATGAACTTCGCCAAGTGCCGGGCTATAACATTGACGGTTTAACCGGTAAATTAAGCGCCGGTCCGAATTGCAATATCGAACGTGATATGACCTGGTTCCAATACCAAAACGGCGGTATTCAGGTATTGAAT","","","63190","MPILLQRINLKNRLMPFLFTLFLAGCTTNFFGSSFTGELKKDANASSEFYMNKIGQTQDIEDQQTYKLLAARVLVTENKVAQAQSLLNELTELNPEQLLDKTLIDADIAAVKGQNNEAENLLKGIDLTQLSSSQVGRYYAVKARVAENQNAIIDAVKARIEMDHVLSDIQRKQENNDRTWALLRRTNRGLIHNTSDEGNLALAGWLALARAYNDNLNQATQLSQALQSWKSSYPNHSAAYLFPTELQGLFNFQQTALSQIGLLLPLSGNGQVLGNTIKSGFDAAKGEDTTIQVQVYDTVATPMNEIIEQARQAGVRALIGPLLKQNVDVILNNPSAIQGLDVLALNSTPNARAIGQVCYYGLSPEDEAESAANKMWRDGIREPMVAVPQNDLGQRTATAFNVRWQQLAGTDANIKYYNQAGDVGVALQGQSVQGLYIVAKSEELSDLKSVIDNSGNNIKLYASSRSNSSNNGPEYRLLMNGLQFSDIPFFKDTDSAQYQKVATETNNDYSLMRLYAMGADSWLLINHFNELRQVPGYNIDGLTGKLSAGPNCNIERDMTWFQYQNGGIQVLN","1372164","","LppC precursor; possible acid phosphatase","Outer membrane, Periplasm","","
InterPro
IPR007443
Family
LppC putative lipoprotein
PF04348\"[40-566]TLppC
noIPR
unintegrated
unintegrated
PS51257\"[1-26]TPROKAR_LIPOPROTEIN
signalp\"[1-28]?signal-peptide
tmhmm\"[15-35]?transmembrane_regions


","No hits to the COGs database.","","Residues 533 to 572 match (6e-14) PD:PD144668 which is described as COMPLETE LPPC PROTEOME HI1655 SIGNAL PRECURSOR ","","","","","","","","","","","","Fri Jan 10 13:36:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02018 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 40 to 566 (E-value = 2.8e-295) place AA02018 in the LppC family which is described as LppC putative lipoprotein (PF04348)","","","","","","","","1","","","" "AA02019","1373985","1373899","87","ATGTATAAAATTCCTTTTGAATTGCTCATTTCGTGCTTCTTTTATTTGCTTTTAGTTGGTGAGATAAGTAAGATCGCTCCGATTATT","","","3357","MYKIPFELLISCFFYLLLVGEISKIAPII","1373899","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-20]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 08:23:03 2004","Thu Feb 26 08:23:03 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02019 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 08:23:03 2004","","","","","","","","","","","","","1","","","" "AA02020","1374008","1374802","795","TTGCAGGACATCACCCAACGGGCGTTAGACACCTTCCAAAAGGTGGATTTAATTGCGGCGGAAGACACCCGTCACAGCGGATTATTATTAAGCCATTATGGCATTAAAAGGCCATTTTTTGCCTTACATGATCATAACGAACAACAAAAAGCGGGTGCCCTGGTGGAAAAGTTGTCACAAGGCATCAACATCGCGTTAATTTCCGACGCGGGGACACCGCTTATCAGCGATCCTGGATTTCACTTAGTGCGTCAATGTCGTCAGGCGGACATTCAGGTTGTGCCGCTGCCCGGCGCTTGCGCGGCAATTACCGCTTTGTGCGCTTCCGGCATTGCTTCCGATCGTTTTTGCTTTGAAGGTTTTTTACCGGCGAAAAGTAAAGCCCGTTTGGACAAACTGAAAAACGTCGCCGAAGAAGACCGCACTTTAATCTTCTACGAATCCACCCACCGCATTTTAGACAGCCTTACGGATATGCAAACGGTGTTCGGTGGCGAGCGTTATGTGGTTTTAGCGCGCGAAATTACCAAAACCTGGGAAACCATTCATGGCGATCATTTGGCGGATTTGCTGGCTTGGCTGCAAGAAGAACCCAATCGTACCAAAGGCGAAATGGTGGTAATTGTCGAAGGCAAAACTAAAGAAGAAAACGCCGAAGAAATCTCACCGCAAGCCATCAAAGCCCTTGAACTCATCAGTCGCGAATTGCCGTTAAAAAAAGCTGCCGCCATTGTGGCGGAGCTTTACGGCTATAAGAAAAATCAGTTGTATCAGTTCGGATTGGAGTTTTTGAGT","","","31259","LQDITQRALDTFQKVDLIAAEDTRHSGLLLSHYGIKRPFFALHDHNEQQKAGALVEKLSQGINIALISDAGTPLISDPGFHLVRQCRQADIQVVPLPGACAAITALCASGIASDRFCFEGFLPAKSKARLDKLKNVAEEDRTLIFYESTHRILDSLTDMQTVFGGERYVVLAREITKTWETIHGDHLADLLAWLQEEPNRTKGEMVVIVEGKTKEENAEEISPQAIKALELISRELPLKKAAAIVAELYGYKKNQLYQFGLEFLS","1374801","","conserved hypothetical protein (possible tetrapyrrole methylase family protein)","Cytoplasm","","
InterPro
IPR000878
Domain
Tetrapyrrole methylase
PF00590\"[1-191]TTP_methylase
InterPro
IPR008189
Family
Protein of unknown function UPF0011
PIRSF005917\"[1-264]TPredicted methyltransferase, YraL type
TIGR00096\"[1-262]TTIGR00096: conserved hypothetical protein T
PS01296\"[68-79]TUPF0011
InterPro
IPR014777
Domain
Tetrapyrrole methylase, subdomain 1
G3DSA:3.40.1010.10\"[4-99]Tno description
noIPR
unintegrated
unintegrated
PTHR21091\"[31-236]TMETHYLTETRAHYDROFOLATE:HOMOCYSTEINE METHYLTRANSFERASE RELATED
PTHR21091:SF18\"[31-236]TS-ADENOSYLMETHIONINE-DEPENDENT METHYTRANSFERASE


","BeTs to 18 clades of COG0313COG name: Predicted methyltransferasesFunctional Class: RThe phylogenetic pattern of COG0313 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.7e-57) to 5/5 blocks of the IPB000578 family, which is described as \"Uncharacterized protein family UPF0011\". Interpro entry for IP:IPR000578. IPB000578A -9-30 0.0007 IPB000578B 64-83 3.2e-14 IPB000578C 96-125 3.7e-22 IPB000578D 142-152 3.5e-05 IPB000578E 169-182 4.6e-06","Residues 219 to 261 match (4e-13) PD:PD037760 which is described as COMPLETE PROTEOME METHYLTRANSFERASE YRAL VC0582 METHYLASE HI1654 TETRAPYRROLE PM0645 STY3446 ","","","","","","","","","","","","Fri Jan 31 15:36:43 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02020 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 191 (E-value = 5.5e-36) place AA02020 in the TP_methylase family which is described as Tetrapyrrole (Corrin/Porphyrin) Methylases (PF00590)","","","","","","","","1","","","" "AA02021","1375075","1376661","1587","ATGCAAAGAAATATTGAACTTGAGAAAGTAACGAGTACGGATAAATGGGATTTTATTGTCATCGGTGGTGGCGCCAGCGGTTTAGGGATTGCTTTAGATGCCGCATCTCGTGGCTATAAAACCTTGTTGTTGGAAGGTTATGACTTTGCAAAAGGGACTTCAAGCCGTAGTACCAAATTAGTTCACGGCGGCGTGCGTTATTTGGCGGCCGGCGATGTGGCGTTAGTGAAAGAGGCGTTGCGTGAACGTGGTCGTTTAGCAAAAAACGCGTCCCACCTGTTCAAAAATCAGAATTTTATTATTCCTAACTATAATTTTATCGACAGCGTGAAATACCGTGTCGGGTTGGGGTTGTATGATTATTTGTCCGGCGATTTAAGTTTGGGTAAAACCATCGCGATTAATAAAGACACCACGATGCAGCGTTTACCAACCTTAAACGGAACGGACTTGAAAAACGGCGTGGTATATAAAGACGGTCAGTTTGACGATTCCCGCTTGGCGATAAATATCGCGCAAACCGTGGTTGAACAAGGCGGTACCGTGCTTAATTATGCGAAAGTGACTGAGTTGTTAAAGGACGGGCAAGGTAAAATCAACGGCGTTAAATTTACCGATGAATTAAACGGCGAACAATATAGCGTGCATGGTACGGCAGTGATTAACGCCACCGGTGTATTCATGAATGAGGTGTTATCCATGGATCACGGTACCGATAAAAAATTCGTGGTGCCAAGCCAAGGGGTGCATTTGGTGTTGGATAAATCCTTCTTACCGAGCGATGACGCGTTAATGATTCCGAAAACTTCCGACGGTCGTGTTTTATTCGCGGTGCCATGGCATGAAAGATTGGTAGTAGGAACAACGGATACGCTGGTGAAAGAACCGTCTTACGAACCTGTTGCGTTGGAACAGGAAATTCAATTTATTTTGGATACGGCAGGTCAATACCTCACCAAGAAACCGACCCGTGATGATGTGTTGAGTATTTTTGCCGGTTTACGTCCGTTAGCGGCGCCGGAAAAAGCCGGTCAAAGCACGAAAGAAGTGTCCCGTAGCCACAAAGTTGTGGTCAGCGATAGCGGTTTGGTTACTATTACCGGCGGTAAATGGACGACCTATCGTCAAATGTCGGAAGATACGGTGGATGAAGCTTTGAAAGTGCATCCGCAATTAGCGAAAAAAGCCTGTGTCACCACGAAGTTAGCGATTCACGGTAAAATTCCGGCGGAACAGGTAGATTTGAAAAATCACTTATACATTTACGGTGCCGACATCCCGGCAATTAAAGCCTTGGAAGCGGAAAATCCGGCAATGACAGAAAAAATTCATCCGCGTCATCCGAATACCATTGCCGAAGTGGTTTGGGCGGCACGTCAGGAAATGGCGCAATCTGTGGAAGATGTCCTTGCCCGCCGTGTGCGTTTGTTGTTCCTTGATGCCCGTGCGGCGATGGACAGTGCTGCGAAAGTGGCAAATATTCTGGCGAAAGAATTAGGCAAAGATGCGCAATGGGAAAAAGAACAAACAGAAAAATTCTTAAACATTGCGAAACACTGTTTGCTTGTGGATTATATGCTGCAAGTC","","","60712","MQRNIELEKVTSTDKWDFIVIGGGASGLGIALDAASRGYKTLLLEGYDFAKGTSSRSTKLVHGGVRYLAAGDVALVKEALRERGRLAKNASHLFKNQNFIIPNYNFIDSVKYRVGLGLYDYLSGDLSLGKTIAINKDTTMQRLPTLNGTDLKNGVVYKDGQFDDSRLAINIAQTVVEQGGTVLNYAKVTELLKDGQGKINGVKFTDELNGEQYSVHGTAVINATGVFMNEVLSMDHGTDKKFVVPSQGVHLVLDKSFLPSDDALMIPKTSDGRVLFAVPWHERLVVGTTDTLVKEPSYEPVALEQEIQFILDTAGQYLTKKPTRDDVLSIFAGLRPLAAPEKAGQSTKEVSRSHKVVVSDSGLVTITGGKWTTYRQMSEDTVDEALKVHPQLAKKACVTTKLAIHGKIPAEQVDLKNHLYIYGADIPAIKALEAENPAMTEKIHPRHPNTIAEVVWAARQEMAQSVEDVLARRVRLLFLDARAAMDSAAKVANILAKELGKDAQWEKEQTEKFLNIAKHCLLVDYMLQV","1376660","","anaerobic glycerol-3-phosphate dehydrogenase","Cytoplasm, Inner membrane","","
InterPro
IPR000447
Family
FAD-dependent glycerol-3-phosphate dehydrogenase
PR01001\"[16-28]T\"[29-39]T\"[45-57]T\"[90-102]T\"[331-337]T\"[363-375]TFADG3PDH
InterPro
IPR001100
Family
Pyridine nucleotide-disulphide oxidoreductase, class I
PR00411\"[17-39]T\"[374-394]TPNDRDTASEI
InterPro
IPR006076
Family
FAD dependent oxidoreductase
PF01266\"[17-375]TDAO
noIPR
unintegrated
unintegrated
G3DSA:3.50.50.60\"[15-225]Tno description
PTHR11985\"[3-515]TGLYCEROL-3-PHOSPHATE DEHYDROGENASE


","No hits to the COGs database.","Significant hit ( 4.9e-87) to 6/6 blocks of the IPB000447 family, which is described as \"FAD-dependent glycerol-3-phosphate dehydrogenase\". Interpro entry for IP:IPR000447. IPB000447A 16-68 2.8e-35 IPB000447B 75-102 1.7e-06 IPB000447C 209-231 0.0001 IPB000447D 267-289 3e-09 IPB000447E 326-337 0.00051 IPB000447F 347-383 2.8e-20Significant hit ( 3.1e-07) to 1/5 blocks of the IPB000171 family, which is described as \"Bacterial-type phytoene dehydrogenase\". Interpro entry for IP:IPR000171. IPB000171A 19-49 3.1e-07Significant hit ( 2.7e-05) to 1/6 blocks of the IPB002135 family, which is described as \"3-hydroxyacyl-CoA dehydrogenase\". Interpro entry for IP:IPR002135. IPB002135A 20-45 2.7e-05","Residues 422 to 490 match (1e-07) PD:PD589400 which is described as DEHYDROGENASE GLYCEROL-3-PHOSPHATE GLYCEROL PHOSPHATE PROTEOME COMPLETE FLAVOPROTEIN FAD OXIDOREDUCTASE METABOLISM ","","","","","","","","","","","","Fri Jan 10 13:58:37 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02021 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 16 to 382 (E-value = 1.3e-82) place AA02021 in the DAO family which is described as FAD dependent oxidoreductase (PF01266)","","","","","Iuchi S, Cole ST, Lin EC. Multiple regulatory elements for the glpA operon encoding anaerobic glycerol-3-phosphate dehydrogenase and the glpD operon encoding aerobic glycerol-3-phosphate dehydrogenase in Escherichia coli: further characterization of respiratory control. J Bacteriol. 1990 Jan;172(1):179-84. PMID: 2403539 Cole ST, Eiglmeier K, Ahmed S, Honore N, Elmes L, Anderson WF, Weiner JH. Nucleotide sequence and gene-polypeptide relationships of the glpABC operon encoding the anaerobic sn-glycerol-3-phosphate dehydrogenase of Escherichia coli K-12. J Bacteriol. 1988 Jun;170(6):2448-56. PMID: 3286606 Ehrmann M, Boos W, Ormseth E, Schweizer H, Larson TJ. Divergent transcription of the sn-glycerol-3-phosphate active transport (glpT) and anaerobic sn-glycerol-3-phosphate dehydrogenase (glpA glpC glpB) genes of Escherichia coli K-12. J Bacteriol. 1987 Feb;169(2):526-32. PMID: 3027032 Schryvers A, Weiner JH. The anaerobic sn-glycerol-3-phosphate dehydrogenase: cloning and expression of the glpA gene of Escherichia coli and identification of the glpA products. Can J Biochem. 1982 Mar;60(3):224-31. PMID: 6282417","","Fri Jan 10 13:58:37 2003","1","","","" "AA02022","1376814","1376722","93","TTGCAAAATTTAATTAACAATATTTTAACACCAATTTATTATTTTTGCTTAGGGTTGATTTGTAAAAAAGGAAAATACTTCGTTACCGTTATG","","","3607","LQNLINNILTPIYYFCLGLICKKGKYFVTVM","1376722","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 08:21:33 2004","Thu Feb 26 08:21:33 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02022 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 08:21:33 2004","","","","","","","","","","","","","1","","","" "AA02023","1376841","1378175","1335","ATGAAAAACATCGTTATTGTCGGTGGTGGCGCCGGCGGGTTAGAACTTGCCACCCACTTAGGCAACAAACTTGGACGCAAAAAACGCGCTAATGTCACTTTAATTGATCGCAACCAAACCCATTTATGGAAACCGTTATTGCATGAATTGGCAACAGGCGCATTAGATGACGGCGTAGAAGCTTTGAGTTATCGTGCCCATGCCTGCAATCATCATTTCAATTTTGAGCAAGGCTCCATGGTTGGCTTAAATCGTCAGCATAAATATGTAGAACTTGCCCCGGTTTACGGTGAAGACGGCGATATGATCGTGGTTTCCCGTCGCATTCCTTATGATTATTTAGTCATTGCCATCGGCAGTAAATCCAACGATTTCAATACTAAAGGTGTGGCAGAAAACTGTATTTTCTTAGATAACCCGTCACAAGCCATGCGCTTCCAACACAAAATGTTGGAGCTGTTCCTTAAATTCCGTGAAAATCAAGCCCTGGACGATATTGGTGAGGAAGAGAGTAAACAACAATTAGTAGAAGACGGGCATATTAATATTGCCATTGTTGGCGCGGGTGCAACGGGCGTGGAGCTTTCCGCCGAACTTTATAATGCGGCAGAGCATTTGTCTTCTTATGGATACGGTCAAATTGACAGTAGCCGTTTAAAAGTCACCTTGGTAGAAGCCGGTCCGCGTATTCTGCCAGCCTTGCCGGAGCGTATTTCTAATGATGCCACGGAAGAATTACGTAAACTCGGCGTGGATGTAAAGACTAATACGATGATTGTTGAAGCTAAGAAAAAACAATTGGTGACAAAAGATGGTCAGTTAATTCCTGCAGATTTAATCGTGTGGTCGGCAGGCATTCGCACGTCAGCTATTACAAAAAATTTCGATGGTTTGGAAATTAACCGCATCAATCAACTCGTTGTGAAGAAGACATTACAAACTACAAACGATAGTACGATTTTTGCTATGGGGGACTGTTGTTTATTGATGCAAGACGATGGAAAACCGGTTCCGCCTAAGGCGCAGGCAGCCCATCAAATGGCAAGTTTATGTGCGAAAAATATGGTTGCTTTATTTGATAATAAGCCGTTAAAAGACTTTGAATATAATGATAAAGGATCGTTGGTTTCCTTATCGGAATTCACCGCTTTTGGTGCCTTAAGCGGTAAAATCACGGGTGGTTCTTCGATGACCATTGAAGGGAAAATCGCGCAATGGGTATATGTTTCGCTTTATCGTATGCACCAGGCGGCGCTACACGGTTGTTTTAAAACCGGTTTGATTATTGTGGTAGGGCATTTGAATCGTTTCCTACGCCCATCATTAAAGTTGCAT","","","48870","MKNIVIVGGGAGGLELATHLGNKLGRKKRANVTLIDRNQTHLWKPLLHELATGALDDGVEALSYRAHACNHHFNFEQGSMVGLNRQHKYVELAPVYGEDGDMIVVSRRIPYDYLVIAIGSKSNDFNTKGVAENCIFLDNPSQAMRFQHKMLELFLKFRENQALDDIGEEESKQQLVEDGHINIAIVGAGATGVELSAELYNAAEHLSSYGYGQIDSSRLKVTLVEAGPRILPALPERISNDATEELRKLGVDVKTNTMIVEAKKKQLVTKDGQLIPADLIVWSAGIRTSAITKNFDGLEINRINQLVVKKTLQTTNDSTIFAMGDCCLLMQDDGKPVPPKAQAAHQMASLCAKNMVALFDNKPLKDFEYNDKGSLVSLSEFTAFGALSGKITGGSSMTIEGKIAQWVYVSLYRMHQAALHGCFKTGLIIVVGHLNRFLRPSLKLH","1378174","[FUNCTION] Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. does not couple the redox reaction to proton translocation (by similarity). [CATALYTIC ACTIVITY] NADH + acceptor = NAD(+) + reduced acceptor.[COFACTOR] FAD;","NADH dehydrogenase","Cytoplasm, Periplasm","","
InterPro
IPR001100
Family
Pyridine nucleotide-disulphide oxidoreductase, class I
PR00411\"[3-25]T\"[182-207]T\"[320-327]TPNDRDTASEI
InterPro
IPR001327
Domain
Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PF00070\"[182-285]TPyr_redox
InterPro
IPR013027
Domain
FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PR00368\"[3-25]T\"[182-207]T\"[320-327]TFADPNR
PF07992\"[3-330]TPyr_redox_2
noIPR
unintegrated
unintegrated
G3DSA:3.50.50.60\"[2-130]T\"[182-355]Tno description
PTHR22915\"[1-394]TNADH DEHYDROGENASE-RELATED
PTHR22915:SF4\"[1-394]TNADH DEHYDROGENASE-RELATED


","BeTs to 10 clades of COG1252COG name: NADH dehydrogenase, FAD-containing subunitFunctional Class: CThe phylogenetic pattern of COG1252 is -o----y--drlbcefgh---j----Number of proteins in this genome belonging to this COG is","Significant hit ( 9.1e-10) to 4/5 blocks of the PR00368 family, which is described as \"FAD-dependent pyridine nucleotide reductase signature\". Prints database entry for PR:PR00368. PR00368A 3-25 0.16 PR00368B 114-123 76 PR00368C 182-207 0.022 PR00368E 320-327 0.57","Residues 4 to 55 match (2e-08) PD:PD445179 which is described as OXIDOREDUCTASE FAD FLAVOPROTEIN COMPLETE PROTEOME NADH DEHYDROGENASE REDOX-ACTIVE CENTER YUMB ","","","","","","","","","","","Fri Jan 10 14:02:12 2003","Fri Jan 10 14:02:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02023 is paralogously related to AA01306 (3e-05).","","","","","","Residues 3 to 334 (E-value = 3.9e-44) place AA02023 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase (PF00070)","","","","","Young,I.G., Rogers,B.L., Campbell,H.D., Jaworowski,A. and Shaw,D.C. Nucleotide sequence coding for the respiratory NADH dehydrogenase of Escherichia coli. UUG initiation codon. Eur. J. Biochem. 116(1): 165-170, 1981. PubMed: 6265208. David P, Baumann M, Wikstrom M, Finel M. Interaction of purified NDH-1 from Escherichia coli with ubiquinone analogues. Biochim Biophys Acta. 2002 Feb 15;1553(3):268-78. PMID: 11997136 Lee AS, Teo AS, Wong SY. Novel mutations in ndh in isoniazid-resistant Mycobacterium tuberculosis isolates. Antimicrob Agents Chemother. 2001 Jul;45(7):2157-9. PMID: 11408244 Green J, Anjum MF, Guest JR. Regulation of the ndh gene of Escherichia coli by integration host factor and a novel regulator, Arr. Microbiology. 1997 Sep;143 ( Pt 9):2865-75. PMID: 9308170 ","","Fri Jan 10 14:02:12 2003","1","","","" "AA02024","1378799","1378284","516","TTGGAAAGCAAGCTTACAGGCAAAAATATCGCCGTGCGCGATCTTGCAGTAAATCAACTTCCCCACTTTGGTGCCACTGCCACAACCGCCCTACGCGGTCAACCGACGACAGCGGAAGAAAACGCATTATTGGCGTTATCTGATGAATTAGTCGCCGAAATTAAAAACGCAAACACCATTATCATCAATGCACCGATGTATAATTTTAATATCCCTACCCAATTAAAAAGCTATTTTGATTTCATTGCACGCCCTCGCGTAACATTTCAATATACGGAGGAAGGCCCTGAAGGATTATTAACAGGCAAAAAAGCCGTGGTATTAGCTGTATTCGGCGGGTTCCACCAAAATCAATCTTCCGATATCGTCACGGCATACTTAAAAATGATTTTAGGTTTCGTGGGTATTACCGATGTGCAATTCGTGTATGCAGAAGGCATTGGTTTTGGTCCTGAAGCGGTTGAAAAAGCACAAGCGCAAGCGAAAGCAGAAATAGATAAAATTGTGGCCGCACTT","","","21153","LESKLTGKNIAVRDLAVNQLPHFGATATTALRGQPTTAEENALLALSDELVAEIKNANTIIINAPMYNFNIPTQLKSYFDFIARPRVTFQYTEEGPEGLLTGKKAVVLAVFGGFHQNQSSDIVTAYLKMILGFVGITDVQFVYAEGIGFGPEAVEKAQAQAKAEIDKIVAAL","1378283","[FUNCTION] Converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine prosthetic group from ACP (By similarity).[CATALYTIC ACTIVITY] Holo-[acyl-carrier protein] + H(2)O = 4'-phosphopantetheine + apo-[acyl-carrier protein].","acyl carrier protein phosphodiesterase","Cytoplasm","","
InterPro
IPR003680
Family
Flavodoxin-like fold
PF02525\"[7-170]TFlavodoxin_2
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.360\"[7-171]Tno description


","No hits to the COGs database.","","Residues 39 to 116 match (3e-10) PD:PD580028 which is described as COMPLETE PROTEOME PHOSPHODIESTERASE CARRIER ACYL ACYL-CARRIER ACYL-CARRIER-PROTEIN PROBABLE LIN0620 ","","","","","","","","","","","Fri Jan 10 14:07:10 2003","Fri Jan 10 14:07:10 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02024 is paralogously related to AA02589 (0.001).","","","","","","Residues 2 to 170 (E-value = 1.3e-20) place AA02024 in the Flavodoxin_2 family which is described as Flavodoxin-like fold (PF02525)","","","","","Chandler,M.S. and Smith,R.A. Characterization of the Haemophilus influenzae topA locus: DNA topoisomerase I is required for genetic competence. Gene 169 (1): 25-31 (1996) [PubMed: 8635745].Moriya,H., Kasai,H. and Isono,K. Cloning and characterization of the hrpA gene in the terC region of Escherichia coli that is highly similar to the DEAH family RNA helicase genes of Saccharomyces cerevisiae. Nucleic Acids Res. 23 (4): 595-598 (1995) [PubMed: 7899078].Fischl,A.S. and Kennedy,E.P. Isolation and properties of acyl carrier protein phosphodiesterase of Escherichia coli. J. Bacteriol. 172 (9): 5445-5449 (1990) [PubMed: 2168383].","","Fri Jan 10 14:07:10 2003","1","","","" "AA02025","1378911","1378807","105","ATGACCGCACTTTTCACTCATTCATTTAGGAAGGAACAAAATGAACAACGTTCTTGTATTAAAATCCAGTATTCTGGCAGACAGTTCACAAACCAATCAATTATC","","","4174","MTALFTHSFRKEQNEQRSCIKIQYSGRQFTNQSII","1378807","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Thu Feb 26 08:19:11 2004","Thu Feb 26 08:19:11 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02025 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 08:19:11 2004","","","","","","","","","","","","","1","","","" "AA02026","1379064","1380119","1056","ATGTGTTCGGAAATTTTTATTGGTTATGGTGTATTTCTTTTGGAAGTTATCACGCTATTACTTGTGATCGCCGCCGTGGTCGCGATGATTATTGCAATTAAACAGAAAAAAGCGCATTTGCACGGTGAATTGGTGATTACCGATTTATCCAAGGAATTTGAGGAAAATGGTAAAAAATTAAGCGATTTTCATCTCACCGAAGACGAATTAAAAGCGGCGGAAAAAGCCGAGAAAAAAGCGGAAAAAGCGAAAGCAAAAGCATTAAAAGCGCAACGTAAAAAAGGCGAAAATCCGGCAGAAGAACGTAAGCCAACTCTTTATGTTTTACATTTTAAAGGGGATATTTCTGCTTCGGAAACAGCAGCGTTAAGAGAGGAAATCAGCGCTATTATTCAAGTTGCCAAACCCACTGATGAAGTTTTGGTATGTTTGGAAAGCCCGGGCGGTGTTGTACATGGCTATGGGCTCGCTGCCTCTCAATTAATGCGTTTGAAACAACGCAACATTAGATTAACCGTTGCCGTGGATAAAGTAGCAGCAAGCGGTGGTTATATGATGGCCTGTGTTGCCGATAAAATTGTATCCGCACCGTTTGCTATTATCGGTTCTATCGGTGTGGTAGCGCAGATTCCAAATGTTCATCGCCTACTAAAAAAACATGATGTGGATGTGGACGTGATGACGGCAGGCGAATATAAACGCACTATGACGATTTTTGGTGAAAATACCGAAAAAGGAAAGCAAAAATTCCAACAGGAATTAGAAGAAACTCATCAGTTATTCAAGCAATTTGTCGCACAGAATCGACCGCACTTGGATCTGGATAAAGTAGCAACAGGGGAACATTGGTTAGGTCAGCAGGCATTAAATTTAAATTTAGTGGATGAGATTATGACCAGCGATGATTTGCTATTACAGGCGATGAAAGAGAAATCGGTTATCGGCGTAAAATATGCGGTGAAGAAATCGTTATTACAAAAAGTCGGTAAACAGGCGGAAGAAAGTGCCGATAATATTGCTTTACGTTGGCTTAAGAAAAATGAAAGAACATTGATA","","","38962","MCSEIFIGYGVFLLEVITLLLVIAAVVAMIIAIKQKKAHLHGELVITDLSKEFEENGKKLSDFHLTEDELKAAEKAEKKAEKAKAKALKAQRKKGENPAEERKPTLYVLHFKGDISASETAALREEISAIIQVAKPTDEVLVCLESPGGVVHGYGLAASQLMRLKQRNIRLTVAVDKVAASGGYMMACVADKIVSAPFAIIGSIGVVAQIPNVHRLLKKHDVDVDVMTAGEYKRTMTIFGENTEKGKQKFQQELEETHQLFKQFVAQNRPHLDLDKVATGEHWLGQQALNLNLVDEIMTSDDLLLQAMKEKSVIGVKYAVKKSLLQKVGKQAEESADNIALRWLKKNERTLI","1380118","[FUNCTION] Multicopy suppressor of the htrA (degP) null phenotype. It is possibly a protease, not essential for bacterial viability. ","probable serine proteinase","Cytoplasm","","
InterPro
IPR002142
Domain
Peptidase S49
PD002897\"[163-254]TSOHB_HAEIN_P45315;
PF01343\"[163-314]TPeptidase_S49
InterPro
IPR013703
Domain
Peptidase S49, N-terminal proteobacteria
PF08496\"[3-161]TPeptidase_S49_N
InterPro
IPR014437
Family
Protease IV-related
PIRSF006227\"[60-345]TProtease IV-related protein, single domain form
noIPR
unintegrated
unintegrated
signalp\"[1-28]?signal-peptide
tmhmm\"[10-32]?transmembrane_regions


","BeTs to 24 clades of COG0616COG name: Periplasmic serine proteases (ClpP class)Functional Class: N,OThe phylogenetic pattern of COG0616 is aompkz-qvdr-bcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 3.3e-50) to 3/3 blocks of the IPB002142 family, which is described as \"Peptidase family U7\". Interpro entry for IP:IPR002142. IPB002142A 140-149 0.19 IPB002142B 173-222 1.2e-32 IPB002142C 278-304 2.2e-13","Residues 299 to 352 match (2e-11) PD:PD439229 which is described as PROTEOME COMPLETE SOHB ","","","","","","","","","","","Fri Jan 10 14:10:48 2003","Fri Jan 10 14:10:48 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02026 is paralogously related to AA01992 (5e-17).","","","","","","Residues 163 to 314 (E-value = 1.4e-67) place AA02026 in the Peptidase_S49 family which is described as Peptidase family S49 (PF01343)","","","","","Baird,L., Lipinska,B., Raina,S. and Georgopoulos,C. Identification of the Escherichia coli sohB gene, a multicopy suppressor of the HtrA (DegP) null phenotype J. Bacteriol. 173 (18), 5763-5770 (1991) PubMed: 1885549 ","","Fri Jan 10 14:10:48 2003","1","","","" "AA02027","1380234","1381133","900","TTGCTTTTTGAGCCTTCTTTTTATTATATCTATGGTTCCTTTGGATTGTTCTACTCACCTAAAAATAAGGTAAAACAGATGAAATTATCACATTTCTTATTATCTGCAATCGCAGCGGCAACTCTTGTTGCTTGTGGTAACTTAAGTAAAGTATCTAAAGAAGGTACTCCTGCCGAAGGTTCTGAATTAGTATGGCCTCAAATTGAAAAATCTACATTTAATCATAACGGTAGCCAATTCGGTTCCTGGCCGAACTGGGACAATGTTCGTATGATTGAAAAAGGCATGAATAAAGATCAGCTTTATAACTTGATTGGTCGTCCGCACTTCGCTGAAGGTTTATTCGGTATTCGCGAATGGGACTATGTGTTTAACTATCGTGAAAACGGCGAGCACAAAGTGTGCCAATATAAAATCTTATTCAATTCCAACATGAACGCACAAAACTTTTATTGGTATCCGAATGGCTGTAACGGTAACTCTTCTTATTCTTTAACCGCCGATTTCTTATTTGATTTCGATAAAGATACGTTAACGGTGAAAGGCAGAGAAGTGGTTGATAAAGTGGCGGCACAATTAAAAGAATCCAAAGCGCAGGAAGTGAAAGCTGCCGGTTATACCGACCGTTTAGGTTCCAAAGTGTATAACATGGATCTTTCCCAGCGTCGTGCAGATCGTGTTAAAAACCGTTTAATTGAACAAGGTATTGATGTTCAAATTAATGCAGTTGGTTACGGTGAAGCTCACCAAGTTCAAGCCTGTAACAATGTTAAATCCAGCCAATTAATCAGCTGCTTGCGTCCAAACCGTCGTGTTGAAATTTCCTCTTCCGGTATCACACCAAAAGATGAAAGTAAACAAGTTGGCGGCGAAATAGGACCAACTCCGTTATATCAAAAA","","","33895","LLFEPSFYYIYGSFGLFYSPKNKVKQMKLSHFLLSAIAAATLVACGNLSKVSKEGTPAEGSELVWPQIEKSTFNHNGSQFGSWPNWDNVRMIEKGMNKDQLYNLIGRPHFAEGLFGIREWDYVFNYRENGEHKVCQYKILFNSNMNAQNFYWYPNGCNGNSSYSLTADFLFDFDKDTLTVKGREVVDKVAAQLKESKAQEVKAAGYTDRLGSKVYNMDLSQRRADRVKNRLIEQGIDVQINAVGYGEAHQVQACNNVKSSQLISCLRPNRRVEISSSGITPKDESKQVGGEIGPTPLYQK","1381132","Related to ompA protein.","lipoprotein; hemagglutinin antigen","Outer membrane, Extracellular","","
InterPro
IPR006664
Domain
Bacterial outer membrane protein
PR01021\"[171-193]T\"[201-216]T\"[216-232]TOMPADOMAIN
InterPro
IPR006665
Domain
OmpA/MotB
PD000930\"[181-228]TO85277_PASHA_O85277;
PF00691\"[170-262]TOmpA
PS51123\"[158-280]TOMPA_2
InterPro
IPR007450
Domain
SmpA/OmlA
PF04355\"[45-151]TSmpA_OmlA
noIPR
unintegrated
unintegrated
G3DSA:3.30.1330.60\"[163-275]Tno description
signalp\"[1-39]?signal-peptide
tmhmm\"[29-49]?transmembrane_regions


","BeTs to 11 clades of COG2885COG name: Outer membrane protein and related peptidoglycan-associated (lipo)proteinsFunctional Class: MThe phylogenetic pattern of COG2885 is -------q--r---efghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 1e-23) to 3/4 blocks of the IPB001145 family, which is described as \"Bacterial outer membrane protein\". Interpro entry for IP:IPR001145. IPB001145B 167-194 2.2e-07 IPB001145C 201-247 8.8e-11 IPB001145D 265-276 0.028","Residues 160 to 278 match (8e-34) PD:PD000930 which is described as MEMBRANE OUTER COMPLETE PROTEOME LIPOPROTEIN PRECURSOR SIGNAL PORIN TRANSMEMBRANE A ","","","","","","","","","","","Tue Jan 28 13:19:33 2003","Fri Jan 10 14:15:25 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02027 is paralogously related to AA02479 (2e-20), AA02458 (6e-19) and AA02829 (2e-08).","","","","","","Residues 170 to 262 (E-value = 8.2e-20) place AA02027 in the OmpA family which is described as OmpA family (PF00691)","","","","","Nardini,P.M., Mellors,A. and Lo,R.Y. Characterization of a fourth lipoprotein from Pasteurella haemolytica A1 and its homology to the OmpA family of outermembrane proteins. FEMS Microbiol. Lett. 165 (1): 71-77 (1998) PubMed: 9711841.Hobb,R.I., Tseng,H.J., Downes,J.E., Terry,T.D., Blackall,P.J., Takagi,M. and Jennings,M.P. Molecular analysis of a haemagglutinin of Haemophilus paragallinarum. Microbiology 148 (Pt 7): 2171-2179 (2002) ","","Tue Jan 28 13:19:33 2003","1","","","" "AA02028","1382070","1381198","873","ATGTGGAAATCGATTTCTCAAGTTTTAGCTGATCAATTCGGGGCGTATTATTCCATCAAAAATAAAACCAAAATTCATACGGGCGAAATGCATGAATCTTGGCTCATTAATGACGGCATTCAACCCGTCTTCGTAAAACTGAATGAAAAGTCCTACCGTTCCATGTTCCGCGCCGAAGCGGATCAATTGATCCTTTTAGGCAAAACCAACACCGTACGCGTGCCTGAAGTGTATGGTGTGGGATGCTCACAAAATCATAGTTTTTTGTTATTGGAAGGCTTAAATATGCAACCGAATACGCCGCAAAATATGGCGGAATTCGGTGAGCAACTCGCCCGTTTGCACCAATATCACGGCTCAGAAAACTACGGTTTGTCTTTTGATACTTGGCTTGGTCCGCAATATCAACCGAACGAATGGAGCAACCACTGGGCGAAGTTTTTCAGCGAACAGCGGATTGGCTGGCAATTACAGCTTTGCGCGGAAAAACAACTGCATTTCGGTGATACGGAAACCATCATCAAAGCCGTGGCAACGCTGTTGGCAAAACATCAGCCGCAGCCGTCTTTGCTACATGGTAATTTGTGGATTGAAAATTGTGCCAATATTGACGGACATACGGTTACTTATGATCCGGCGTGTTATTGGGGGGATCGGGAATGCGATTTGGCGTTTACCGAATTATTTGAACCGTTCCCGCGTGAATTCTATGAAAATTATGACCGCACTTTTCCGTTAGAAGAAGGCTATCAGGATCGAAAAATCGTGTATCAGCTTTATCATTTGCTTAACTTCAGCAGCCGCTTCCACGGCAATTATGTGGCACTTGCCAATAAATGGGTGCATGATGTGTTGCAACGCTATGAAAATCTA","","","34042","MWKSISQVLADQFGAYYSIKNKTKIHTGEMHESWLINDGIQPVFVKLNEKSYRSMFRAEADQLILLGKTNTVRVPEVYGVGCSQNHSFLLLEGLNMQPNTPQNMAEFGEQLARLHQYHGSENYGLSFDTWLGPQYQPNEWSNHWAKFFSEQRIGWQLQLCAEKQLHFGDTETIIKAVATLLAKHQPQPSLLHGNLWIENCANIDGHTVTYDPACYWGDRECDLAFTELFEPFPREFYENYDRTFPLEEGYQDRKIVYQLYHLLNFSSRFHGNYVALANKWVHDVLQRYENL","1381197","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR005581
Family
Fructosamine kinase
PF03881\"[1-287]TFructosamin_kin


","BeTs to 3 clades of COG3001COG name: Fructosamine-3-kinaseFunctional Class: GThe phylogenetic pattern of COG3001 is -------------ce-gh--------Number of proteins in this genome belonging to this COG is","","Residues 1 to 285 match (2e-122) PD:PD040103 which is described as COMPLETE KINASE TRANSFERASE PROTEOME FRUCTOSAMINE-3-KINASE ACETYLATION 2.7.1.- YNIA FLJ12171/DKFZP564D202 KINASE-LIKE ","","","","","","","","","","","","Fri Jan 10 14:16:19 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02028 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 287 (E-value = 9.2e-183) place AA02028 in the Fructosamin_kin family which is described as Fructosamine kinase (PF03881)","","","","","","","","1","","","" "AA02029","1382275","1382090","186","GTGACTTGTTTCATTTCATTTAAAAAACGCTTAAAAAAACCACCGCACTTTTATCATCCTTACAAGCGGACAAACCAAGTGCGGCGCGCAATTTTAGCATATTTTACAATGACAACCAAATGTCTAAATTTTGACTTGAGTCACAGTAATTTTTTCTCAATCTTTTACACTATAAACATGATTAAC","","","7524","VTCFISFKKRLKKPPHFYHPYKRTNQVRRAILAYFTMTTKCLNFDLSHSNFFSIFYTINMIN","1382089","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Fri Jan 10 14:17:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02029 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02030","1382311","1384239","1929","ATGCCGATTATTACTTTACCTGACGGTTCACAACGTCAATTTGATAAACCCGTTACCGTATTAGAAGTTGCTCAAGATATTGGCGTAGGACTTGCAAAAGCGACCATTGCCGGTCGTGTCAACGGCGAACGCAAAGATGCCTGCGACCTGATTACCGAAGACAGCCGTGTTGCAATTATTACTGCCAAAGAGGAAGACGGTCTGGAAATTATCCGTCACTCTACCGCACACTTGCTTGGTCACGCCATTAAACAATTATTTCCAAACGTCAAAATGGCCATCGGGCCTACCATCGACAACGGTTTCTATTATGACGTGGACTTAGACCGCTCTTTAACCCAAGAGGATTTAGACGCCCTTGAAAAACGGATGTTGGAGTTGGCAAAAACCAATTATGACGTCATCAAAACGCCGGTGAGTTGGCAAGAAGCAAGGGATACTTTTGGGAAACGCGGCGAACCTTACAAAATGGCGATCTTAGATGAAAACATTGAACGCACCGCAACGCCTGCACTTTATCATCACCAAGAATATATCGATATGTGCCGTGGTCCTCATGTGCCGAATATGCGTTTCTGTCATCATTTCAAATTGCAAAAAATTGCCGGCGCATACTGGCGTGGGGACAGCAAAAATAAAATGCTGCAACGGATTTACGGTACCGCCTGGGCGGATAAAAAACAACTTGAAGCCTATTTGCATCGTCTGGAAGAAGCGGCAAAACGGGATCATCGTAAAATCGGTAAAGCATTGGATTTATATCACATGCAGGAAGAAGCGCCGGGTATGGTGTTCTGGCACAATGACGGCTGGACGATTTTCCGTGAACTGGAAACTTTCGTGCGCACTAAATTGAAACAATATGACTATCAGGAAGTGAAAGGTCCGTTCATGATGGATCGCGTGTTGTGGGAAAAAACCGGTCACTGGCAAAACTACGGCGATTTGATGTTCACCACCTTTTCTGAAAACCGCGAATATGCCATCAAACCGATGAACTGCCCGGGACACGTTCAGATCTTCAATCAAGGTTTAAAATCTTATCGCGATTTACCGCTACGTATGGCGGAATTCGGTTCCTGCCACCGTAACGAACCGTCCGGTTCATTGCACGGTTTAATGCGCGTGCGCGGTTTTACTCAAGATGACGCTCACATTTTCTGTATGCCGGATCAAGTGGAAAGCGAAGTGACTTCCTGCATTAAAATGGTGTATGACATTTACAGCACCTTCGGTTTCGAAAACATCAAAGTGAAACTTTCCACCCGCCCGGAAAAACGCATCGGGTCCGATGAGATGTGGGATAAAGCGGAGGCGGACTTAGCGAAAGCGTTGGAACATAACGGCTTGTCTTACGAAATTCAGGAAGGCGAGGGCGCATTCTACGGTCCTAAACTGGAATTTGCTTTAACCGATAGCTTAGATCGCGAATGGCAGTGCGGCACGATTCAGTTAGACTTCTTCCTGCCGGAACGTTTAAATGCCTCTTATGTGGGAGAAGATAACGAACGTAAAGTGCCTGTTATGATTCACCGTGCAATTTTGGGCTCCATTGAACGTTTCATCGGCATTATCACCGAAGAATACGCCGGTTTCTTCCCGGCTTGGTTGGCGCCGACCCAAGTGGTCGTGATGAACATTACCGACTCTCAATCGGAATATGTGCAAAAAGTCGCGAAACAGCTTTCCGATGCGGGCTTGCGCGTGAAAACCGATTTGCGTAACGAAAAAGTCGGTTTCAAAATCCGCGAACACACCTTGCGTCGCGTGCCTTACATGCTGGTCTGCGGCGACAAAGAAATCGAAGCCGGCAAAGTGGCAGTACGCACCCGTAAAGGTCAAGATCTCGGCACCTTCACCGTGGAAGAATTTTTAGACATTCTGAAAAAACAAGTGAGAAATCGCGAATTGAAATTATTGGGTGAGGCG","","","74781","MPIITLPDGSQRQFDKPVTVLEVAQDIGVGLAKATIAGRVNGERKDACDLITEDSRVAIITAKEEDGLEIIRHSTAHLLGHAIKQLFPNVKMAIGPTIDNGFYYDVDLDRSLTQEDLDALEKRMLELAKTNYDVIKTPVSWQEARDTFGKRGEPYKMAILDENIERTATPALYHHQEYIDMCRGPHVPNMRFCHHFKLQKIAGAYWRGDSKNKMLQRIYGTAWADKKQLEAYLHRLEEAAKRDHRKIGKALDLYHMQEEAPGMVFWHNDGWTIFRELETFVRTKLKQYDYQEVKGPFMMDRVLWEKTGHWQNYGDLMFTTFSENREYAIKPMNCPGHVQIFNQGLKSYRDLPLRMAEFGSCHRNEPSGSLHGLMRVRGFTQDDAHIFCMPDQVESEVTSCIKMVYDIYSTFGFENIKVKLSTRPEKRIGSDEMWDKAEADLAKALEHNGLSYEIQEGEGAFYGPKLEFALTDSLDREWQCGTIQLDFFLPERLNASYVGEDNERKVPVMIHRAILGSIERFIGIITEEYAGFFPAWLAPTQVVVMNITDSQSEYVQKVAKQLSDAGLRVKTDLRNEKVGFKIREHTLRRVPYMLVCGDKEIEAGKVAVRTRKGQDLGTFTVEEFLDILKKQVRNRELKLLGEA","1384238","[FUNCTION] ThrS is also a translational repressor protein, it controls the translation of its own gene by binding to its mRNA. [CATALYTIC ACTIVITY] ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr).[COFACTOR] Binds 1 zinc ion per subunit.[SUBUNIT] Homodimer.[SUBCELLULAR LOCATION] Cytoplasmic.","threonyl-tRNA synthetase","Cytoplasm","","
InterPro
IPR002314
Domain
tRNA synthetase, class II (G, H, P and S)
PF00587\"[273-438]TtRNA-synt_2b
InterPro
IPR002320
Family
Threonyl-tRNA synthetase, class IIa
PR01047\"[329-357]T\"[362-385]T\"[464-492]T\"[507-520]T\"[534-546]TTRNASYNTHTHR
TIGR00418\"[72-632]TthrS: threonyl-tRNA synthetase
InterPro
IPR004095
Domain
TGS
PF02824\"[2-61]TTGS
InterPro
IPR004154
Domain
Anticodon-binding
G3DSA:3.40.50.800\"[531-642]Tno description
PF03129\"[541-631]THGTP_anticodon
InterPro
IPR006195
Domain
Aminoacyl-transfer RNA synthetase, class II
PS50862\"[243-534]TAA_TRNA_LIGASE_II
InterPro
IPR012675
Domain
Beta-grasp fold, ferredoxin-type
G3DSA:3.10.20.30\"[1-64]Tno description
InterPro
IPR012947
Domain
Threonyl/alanyl tRNA synthetase, SAD
PF07973\"[170-219]TtRNA_SAD
noIPR
unintegrated
unintegrated
G3DSA:3.30.930.10\"[242-530]Tno description
G3DSA:3.30.980.10\"[65-233]Tno description
PTHR11451\"[177-643]TTRNA SYNTHETASE-RELATED
PTHR11451:SF5\"[177-643]TTHREONYL-TRNA SYNTHETASE


","BeTs to 26 clades of COG0441COG name: Threonyl-tRNA synthetaseFunctional Class: JThe phylogenetic pattern of COG0441 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 416 to 455 match (4e-07) PD:PD581084 which is described as SYNTHETASE LIGASE THREONYL-TRNA AMINOACYL-TRNA PROTEOME BIOSYNTHESIS COMPLETE ATP-BINDING METAL-BINDING ZINC ","","","","","","","","","","","Fri Jan 10 14:31:01 2003","Fri Jan 10 14:31:01 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02030 is paralogously related to AA00896 (5e-11).","","","","","","Residues 541 to 631 (E-value = 4.9e-33) place AA02030 in the HGTP_anticodon family which is described as Anticodon binding domain (PF03129)","","","","","Mayaux,J.F., Fayat,G., Fromant,M., Springer,M., Grunberg-Manago,M. and Blanquet,S. Structural and transcriptional evidence for related thrS and infC expression Proc. Natl. Acad. Sci. U.S.A. 80 (20), 6152-6156 (1983) PubMed: 6353409 Springer,M., Graffe,M., Butler,J.S. and Grunberg-Manago,M. Genetic definition of the translational operator of the threonine-tRNA ligase gene in Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 83 (12), 4384-4388 (1986) PubMed: 3086882 Sankaranarayanan,R., Dock-Bregeon,A.C., Romby,P., Caillet,J., Springer,M., Rees,B., Ehresmann,C., Ehresmann,B. and Moras,D. The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site Cell 97 (3), 371-381 (1999) PubMed: 10319817 Sankaranarayanan,R., Dock-Bregeon,A.C., Rees,B., Bovee,M., Caillet,J., Romby,P., Francklyn,C.S. and Moras,D. Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase Nat. Struct. Biol. 7 (6), 461-465 (2000) PubMed: 10881191 ","","Fri Jan 10 14:31:01 2003","1","","","" "AA02031","1384478","1385215","738","ATGATCTCCGAAGAACTTTTCTCTCGTGACGGCGTTTCCGCTAACTCTGCACAACTTACCCAACTTAAAGCTCTTTTCCCGAATTGTTTCGATGTAAGCGGTCAATTTTTATTAGAAAAATTCCAATCTGAAATTGCAGAACAAGCCGACATCAGCCGTGAATTTTACGAAATGAACTGGTTGGGTAAATCCTATGCCAAATTGCTGCGTAATCTTCCGCCTGAAACTTTACTTTGCGAAGACAAAAACCACAACGCTAAACCTGAAAATGCCAACAGCCAAAATCTGTTAATCCAAGGGGATAATTTGGACGTGTTAAAGCACCTAAAAAATGCTTATACAAACAAAGTGAAGATGATTTATATCGATCCGCCGTATAACACAGGTTCAGATGGCTTTGTCTATCAAGACGACTGCAAATTCACGCCCGAACAGTTAACCGTGTTTACTAAAATCCCGAAAAATTCTATCAAAATCCCCGTGGCAGGAGGCGGGACTTATTCCCCTGATTTTGCCTATATCGTCAAAACCAAAACAGGCGAGATTTTGAATTTTGTGATTGAAGCAAAAGGCGTGGATGGTTCGGATAACTTACGAAAAGGCGAAGAACGCAAAATCAAACACGCCGAACGTTTATTTGCCCAAATCTCAAAAGAGGTGAAAGTCGTGTTTAAAACTCAGTTTGAGGGGGACAGGGTGGCTGAGTTGATTATGAAAACGATAACCTCTTTATCCGGG","","","27672","MISEELFSRDGVSANSAQLTQLKALFPNCFDVSGQFLLEKFQSEIAEQADISREFYEMNWLGKSYAKLLRNLPPETLLCEDKNHNAKPENANSQNLLIQGDNLDVLKHLKNAYTNKVKMIYIDPPYNTGSDGFVYQDDCKFTPEQLTVFTKIPKNSIKIPVAGGGTYSPDFAYIVKTKTGEILNFVIEAKGVDGSDNLRKGEERKIKHAERLFAQISKEVKVVFKTQFEGDRVAELIMKTITSLSG","1385214","[FUNCTION] Binds the system-specific DNA recognition site 5'-cagcac-3'. necessary for both restriction and methylation (of one of the two a's). [CATALYTIC ACTIVITY] S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine. [SUBUNIT] Contains two different subunits: res and mod. Modis a homotetramer. [SIMILARITY] With other type III mod proteins.","type III site-specific deoxyribonuclease","Cytoplasm","","
InterPro
IPR002052
Domain
N-6 Adenine-specific DNA methylase
PS00092\"[120-126]?N6_MTASE
InterPro
IPR002941
Domain
DNA methylase N-4/N-6
PF01555\"[117-145]TN6_N4_Mtase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[91-138]Tno description


","BeTs to 5 clades of COG2189COG name: Adenine specific DNA methylase ModFunctional Class: LThe phylogenetic pattern of COG2189 is a--p-------------hsnuj---wNumber of proteins in this genome belonging to this COG is","Significant hit ( 3e-06) to 1/4 blocks of the PR00506 family, which is described as \"D21 class N6 adenine-specific DNA methyltransferase signature\". Prints database entry for PR:PR00506. PR00506A 117-129 3.1e-06","Residues 116 to 158 match (1e-09) PD:PD485570 which is described as METHYLTRANSFERASE SYSTEM TRANSFERASE ENZYME ECOPI DNA-BINDING MOD III TYPE RESTRICTION-MODIFICATION ","","","","","","","","","","","Tue Jan 28 15:56:39 2003","Fri Jan 10 14:34:42 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02031 is paralogously related to AA00029 (1e-12) and AA01923 (3e-08).","","","","","","","","","","","Humbelin,M., Suri,B., Rao,D.N., Hornby,D.P., Eberle,H.,Pripfl,T., Kenel,S. and Bickle,T.A. Type III DNA restriction and modification systems EcoP1 and EcoP15. Nucleotide sequence of the EcoP1 operon, the EcoP15 mod gene andsome EcoP1 mod mutants. J. Mol. Biol. 200 (1): 23-29 (1988) PubMed: 2837577.","","Tue Jan 28 15:56:39 2003","1","","","" "AA02032","1385220","1385354","135","TTGGAGGGATTTACCACTATTTTTTCCATCAAACCGCCGCCGACATGCAACAAATGTGCCGACAAATTCGCGGCGGCAGAACCGTTTAAAAAACGCATCAAAAATCAACCGCACTTTAAAACGCGTTTTCCATCA","","","5121","LEGFTTIFSIKPPPTCNKCADKFAAAEPFKKRIKNQPHFKTRFPS","1385354","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 17:03:38 2004","Wed Feb 25 17:03:38 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02032 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 17:03:38 2004","","","","","","","","","","","","","1","","","" "AA02034","1386114","1385338","777","ATGAACACATCCGTAAAAGAATATACTTTCACCGAACAAAAAGTCCGTTGGGTGAAAAAACATACGCCGAAACTCCTCTCTTTCAGCATCACCCGACCTGCCGATTTTGATTTTATTGCCGGTCAATTTGCCAAATTAGGTTTTATGAATGGAGATAATTACGTTTCCCGCGCCTATTCCATGATCTCTTCCGAAACGGCGGAATATTTGGATTTTTACGCCATTTTAATCGAAGGCGGCATCATGTCCGCCTACTTTAAGCAAATGCAGGCGGGCGATACGTTACTACTTGAGAAAAAGCCCGTCGGCTTTTTTACCGTCAACCGAATTCCACAGGGTAAGGAATTAATTTTGCTTGCCACCGGTTCAGGCATTGCACCTTTTTTATCCATGCTGCAAAGCGAAGAATTCTGGCAAAAAACGGACAAAATTGTGCTGGTGCATTCCGTGTCTTATGCCGACGATTTAGTTTTTGAGCAATACTTGGCTGATTTAAAAGGTCATTCCCTTATCGGCCAATATGCCGATAAACTAATTTATCAACCGGTCATTACCCGAGAAAAAGTCAACAGCACATTACATCAACGCATTCCCCAATTGCTGGAAAACGGCGAATTAGAACACGCCTTAAATATCCGTTTTAGCAAAACCGATACGCGTTTTCTGATTTGCGGCAATCCGAATATGGTAAAAGCAAGCTATGAGCATTTAAAAGCCAAAGGATACGCCCTTCATCGCGTACATAAAAACGGCGAGATTATGATGGAAAACGCGTTT","","","29525","MNTSVKEYTFTEQKVRWVKKHTPKLLSFSITRPADFDFIAGQFAKLGFMNGDNYVSRAYSMISSETAEYLDFYAILIEGGIMSAYFKQMQAGDTLLLEKKPVGFFTVNRIPQGKELILLATGSGIAPFLSMLQSEEFWQKTDKIVLVHSVSYADDLVFEQYLADLKGHSLIGQYADKLIYQPVITREKVNSTLHQRIPQLLENGELEHALNIRFSKTDTRFLICGNPNMVKASYEHLKAKGYALHRVHKNGEIMMENAF","1385337","[FUNCTION] Transports electrons between flavodoxin or ferredoxin and nadph (by similarity). ","ferredoxin NADP+ reductase","Cytoplasm","","
InterPro
IPR001221
Domain
Phenol hydroxylase reductase
PR00410\"[38-50]T\"[117-136]T\"[220-228]TPHEHYDRXLASE
InterPro
IPR001433
Domain
Oxidoreductase FAD/NAD(P)-binding
PF00175\"[117-235]TNAD_binding_1
InterPro
IPR001709
Domain
Flavoprotein pyridine nucleotide cytochrome reductase
PR00371\"[57-64]T\"[117-136]T\"[220-228]TFPNCR
InterPro
IPR008333
Domain
Oxidoreductase FAD-binding region
PF00970\"[12-106]TFAD_binding_6
noIPR
unintegrated
unintegrated
G3DSA:2.40.30.10\"[7-103]Tno description
G3DSA:3.40.50.80\"[104-259]Tno description
PTHR19384\"[77-166]TFLAVODOXIN-RELATED
PTHR19384:SF15\"[77-166]TFERREDOXIN REDUCTASE


","No hits to the COGs database.","Significant hit ( 1.1e-09) to 3/8 blocks of the PR00371 family, which is described as \"Flavoprotein pyridine nucleotide cytochrome reductase signature\". Prints database entry for PR:PR00371. PR00371B 57-64 1.4 PR00371D 117-136 1.3e-05 PR00371H 220-228 15Significant hit ( 4.9e-09) to 3/6 blocks of the PR00410 family, which is described as \"Phenol hydroxylase reductase family signature\". Prints database entry for PR:PR00410. PR00410A 38-50 3.2 PR00410B 57-64 31 PR00410D 117-136 1.2e-05Significant hit ( 1.2e-06) to 2/2 blocks of the IPB001433 family, which is described as \"Oxidoreductase FAD and NAD(P)-binding domain\". Interpro entry for IP:IPR001433. IPB001433A 118-127 0.016 IPB001433B 220-231 0.035","Residues 15 to 111 match (8e-09) PD:PD484283 which is described as REDUCTASE FNR NADP FLAVODOXIN FLDR FLXR FLAVOPROTEIN FERREDOXIN--NADP FAD OXIDOREDUCTASE ","","","","","","","","","","","Fri Jan 10 14:43:09 2003","Fri Jan 10 14:43:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02034 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 113 to 236 (E-value = 6.4e-08) place AA02034 in the NAD_binding_1 family which is described as Oxidoreductase NAD-binding domain (PF00175)","","","","","Bianchi,V., Reichard,P., Eliasson,R., Pontis,E., Krook,M., Jornvall,H. and Haggard-Ljungquist,E. Escherichia coli ferredoxin NADP+ reductase: activation of E. coli anaerobic ribonucleotide reduction, cloning of the gene (fpr), and overexpression of the protein. J. Bacteriol. 175 (6): 1590-1595 (1993) [PubMed: 8449868].Truniger,V., Boos,W. and Sweet,G. Molecular analysis of the glpFKX regions of Escherichia coli and Shigella flexneri. J. Bacteriol. 174 (21): 6981-6991 (1992) [PubMed: 1400248].Morimyo,M. Isolation and characterization of methyl viologen-sensitive mutants of Escherichia coli K-12. J. Bacteriol. 170 (5): 2136-2142 (1988) [PubMed: 2834327].Jenkins,C.M. and Waterman,M.R. Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities. J. Biol. Chem. 269 (44): 27401-27408 (1994) [PubMed: 7961651].Ingelman,M., Bianchi,V. and Eklund,H. The three-dimensional structure of flavodoxin reductase from Escherichia coli at 1.7 A resolution. J. Mol. Biol. 268 (1): 147-157 (1997) [PubMed: 9149148].","","Fri Jan 10 14:43:09 2003","1","","","" "AA02035","1386489","1386965","477","GTGAAAGAAGTCCGCTTGATTGACCAGGACGGTGAGCAAGTTGGGATTGTTCCGATTCAACAGGCATTGGAGATGGCGGAAAACGCCGCTTTAGATCTTGTGGAAATTAGCCCGAATGCGGAACCTCCGGTATGTCGCATTATGAACTACGGTAAATTCCTTTACGAGAAAAGCAAAACGGCCAAAGAGCAGAAGAAAAAGCAGAAAGTTGTGCAGGTGAAAGAAATTAAATTCCGTCCCGGCACAGACGAAGGCGACTACCAGGTAAAACTACGCAGCCTGGTTCGCTTTTTGGAAGATGGGGATAAAGCCAAAGTCACCGTTCGTTTCCGCGGACGTGAAATGGCTCACCAAGATATCGGTTTGGACGTGTTAGAGCGTGTTAAAAATGATTTAGCCGAAATTGCCGTGGTGGAATCTGCACCGGGTAAATTGGAAGGTCGCCAAGCCATTATGGTGCTTGCTCCGAAAAAGAAA","","","17897","VKEVRLIDQDGEQVGIVPIQQALEMAENAALDLVEISPNAEPPVCRIMNYGKFLYEKSKTAKEQKKKQKVVQVKEIKFRPGTDEGDYQVKLRSLVRFLEDGDKAKVTVRFRGREMAHQDIGLDVLERVKNDLAEIAVVESAPGKLEGRQAIMVLAPKKK","1386964","[FUNCTION] IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70s ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins. ","translation initiation factor IF-3","Cytoplasm","","
InterPro
IPR001288
Family
Initiation factor 3
PD002880\"[78-159]TIF3_HAEIN_P43814;
G3DSA:3.10.20.80\"[1-66]Tno description
G3DSA:3.30.110.10\"[67-157]Tno description
PTHR10938\"[10-158]TTRANSLATION INITIATION FACTOR IF-3
PF00707\"[70-158]TIF3_C
PF05198\"[1-65]TIF3_N
TIGR00168\"[1-159]TinfC: translation initiation factor IF-3
PS00938\"[46-59]TIF3


","BeTs to 18 clades of COG0290COG name: Translation initiation factor IF3Functional Class: JThe phylogenetic pattern of COG0290 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 3e-89) to 4/4 blocks of the IPB001288 family, which is described as \"Initiation factor 3\". Interpro entry for IP:IPR001288. IPB001288A -5-17 0.5 IPB001288B 26-74 1e-38 IPB001288C 77-128 2e-38 IPB001288D 144-157 2.1e-07","Residues 2 to 55 match (5e-10) PD:PD555151 which is described as INITIATION FACTOR PROTEOME BIOSYNTHESIS IF-3 TRANSLATION COMPLETE FACTOR TRANSCRIPTION ","","","","","","","","","","","Fri Jan 10 15:00:06 2003","Fri Jan 10 15:00:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02035 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 70 to 158 (E-value = 1.1e-56) place AA02035 in the IF3_C family which is described as Translation initiation factor IF-3, C-terminal domain (PF00707)","","","","","Butler,J.S., Springer,M. and Grunberg-Manago,M. AUU-to-AUG mutation in the initiator codon of the translation initiation factor IF3 abolishes translational autocontrol of itsown gene (infC) in vivo. Proc. Natl. Acad. Sci. U.S.A. 84 (12): 4022-4025 (1987) [PubMed: 2954162].Spurio,R., Paci,M., Pawlik,R.T., La Teana,A., DiGiacco,B.V., Pon,C.L. and Gualerzi,C.O. Site-directed mutagenesis and NMR spectroscopic approaches to the elucidation of the structure-function relationships in translation initiation factors IF1 and IF3. Biochimie 73 (7-8): 1001-1006 (1991) [PubMed: 1742345].Garcia,C., Fortier,P.L., Blanquet,S., Lallemand,J.Y. and Dardel,F. 1H and 15N resonance assignments and structure of the N-terminal domain of Escherichia coli initiation factor 3. Eur. J. Biochem. 228 (2): 395-402 (1995) [PubMed: 7705354].Moreau,M., de Cock,E., Fortier,P.L., Garcia,C., Albaret,C., Blanquet,S., Lallemand,J.Y. and Dardel,F. Heteronuclear NMR studies of E. coli translation initiation factor IF3. Evidence that the inter-domain region is disordered insolution. J. Mol. Biol. 266 (1): 15-22 (1997) [PubMed: 9054966].Hua,Y. and Raleigh,D.P. On the global architecture of initiation factor IF3: a comparative study of the linker regions from the Escherichia coli protein andthe Bacillus stearothermophilus protein. J. Mol. Biol. 278 (4): 871-878 (1998) [PubMed: 9614948].Brauer,D. and Wittmann-Liebold,B. The primary structure of the initiation factor IF-3 from Escherichia coli. FEBS Lett. 79 (2): 269-275 (1977) [PubMed: 330233].Sacerdot,C., Fayat,G., Dessen,P., Springer,M., Plumbridge,J.A., Grunberg-Manago,M. and Blanquet,S. Sequence of a 1.26-kb DNA fragment containing the structural gene for E.coli initiation factor IF3: presence of an AUU initiatorcodon. EMBO J. 1 (3): 311-315 (1982) [PubMed: 6325158]. ","","Fri Jan 10 15:00:06 2003","1","","","" "AA02037","1387112","1386972","141","GTGCAAATTGCACTGTCTTCAGCGGTTTGCCTTGTACTCACTTTAAATCTAAAAGGCTCTATCACAAATAATCAGGCGAATAAAAGTGCGGTTGAAAAAACACTTGGAATTTTCACCGCACTTTTGTTACTTGAAATGCAC","","","4964","VQIALSSAVCLVLTLNLKGSITNNQANKSAVEKTLGIFTALLLLEMH","1386972","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 17:01:50 2004","Wed Feb 25 17:01:50 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02037 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 17:01:50 2004","","","","","","","","","","","","","1","","","" "AA02038","1387192","1387386","195","ATGCCTAAAATTAAAACAGCACGCGGTGCTGCTAAGCGTTTCAAAAAAACTGCTTCCGGTGGTTTCAAGCGTAAACAATCTCACTTACGTCATATTTTGACTAAGAAAACAACAAAACGTAAACGTCACCTACGCCATAAATCTATGGTTGCTAAGTCCGACTTAGTATTAGTAGTCGCGTGCTTGCCATACGCA","","","7394","MPKIKTARGAAKRFKKTASGGFKRKQSHLRHILTKKTTKRKRHLRHKSMVAKSDLVLVVACLPYA","1387385","","50S ribosomal protein L35","Periplasm, Cytoplasm","","
InterPro
IPR001706
Family
Ribosomal protein L35
PD003417\"[4-54]TRL35_HAEIN_P45519;
PR00064\"[3-20]T\"[21-35]T\"[36-54]TRIBOSOMALL35
PF01632\"[4-62]TRibosomal_L35p
TIGR00001\"[2-64]TrpmI_bact: ribosomal protein L35
PS00936\"[5-31]TRIBOSOMAL_L35


","BeTs to 16 clades of COG0291COG name: Ribosomal protein L35Functional Class: JThe phylogenetic pattern of COG0291 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 8.9e-24) to 1/1 blocks of the IPB001706 family, which is described as \"Ribosomal protein L35\". Interpro entry for IP:IPR001706. IPB001706 2-40 7.8e-24","","","","","","","","","","","","","Wed Jan 29 15:31:02 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02038 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 62 (E-value = 4e-30) place AA02038 in the Ribosomal_L35p family which is described as Ribosomal protein L35 (PF01632)","","","","","Kashiwagi,K. and Igarashi,K. Nonspecific inhibition of Escherichia coli ornithine decarboxylase by various ribosomal proteins: detection of a new ribosomal protein possessing strong antizyme activity. Biochim. Biophys. Acta 911 (2): 180-190 (1987) PubMed: 3542048.Wada,A. and Sako,T. Primary structures of and genes for new ribosomal proteins A and B in Escherichia coli. J. Biochem. 101 (3): 817-820 (1987) PubMed: 3298224.Arnold,R.J. and Reilly,J.P. Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry. Anal. Biochem. 269 (1): 105-112 (1999) PubMed: 10094780Guillier M, Allemand F, Raibaud S, Dardel F, Springer M, Chiaruttini C.Translational feedback regulation of the gene for L35 in Escherichia coli requires binding of ribosomal protein L20 to two sites in its leader mRNA: a possible case of ribosomal RNA-messenger RNA molecular mimicry.RNA. 2002 Jul;8(7):878-89.PMID: 12166643.","","Wed Jan 29 15:29:42 2003","1","","","" "AA02039","1387443","1387793","351","ATGGCTCGTGTAAAACGTGGTGTTATTGCAAGAGCACGCCATAAGAAAATTCTTAAGGCTGCTAAAGGTTATTATGGTGCACGTTCACGCGTGTATCGCGTTGCTTTCCAAGCGGTGATCAAAGCCGGTCAATATGCATATCGTGACCGTCGTCAACGTAAACGTCAATTCCGTCAATTATGGATTGCGCGTATTAACGCAGCGGCTCGTCAAAACGGTTTGTCTTACAGCAAATTCATCAATGGCTTGAAAAAAGCCTCTGTTGAAATCGACCGTAAGATCCTTGCTGATATCGCCGTATTCGACAAAGTGGCTTTCGCTGCATTAGTTGAAAAAGCAAAATCTGCACTT","","","13338","MARVKRGVIARARHKKILKAAKGYYGARSRVYRVAFQAVIKAGQYAYRDRRQRKRQFRQLWIARINAAARQNGLSYSKFINGLKKASVEIDRKILADIAVFDKVAFAALVEKAKSAL","1387792","[FUNCTION] This protein binds directly to 23S ribosomal RNA and is necessary to the in vitro assembly process of the 50S ribosomal subunit; it is not involved in the protein synthesizing functions of that subunit (by similarity). ","50S ribosomal protein L20","Cytoplasm, Extracellular","","
InterPro
IPR005812
Family
Ribosomal protein L20, bacterial and organelle form
PR00062\"[12-41]T\"[42-71]T\"[75-101]TRIBOSOMALL20
TIGR01032\"[1-114]TrplT_bact: ribosomal protein L20
PS00937\"[54-70]TRIBOSOMAL_L20
InterPro
IPR005813
Family
Ribosomal protein L20
PD002389\"[3-69]TRL20_HAEDU_Q7VKS2;
PTHR10986\"[1-117]T50S RIBOSOMAL PROTEIN L20
PF00453\"[2-109]TRibosomal_L20


","No hits to the COGs database.","Significant hit ( 9.1e-39) to 1/1 blocks of the IPB001081 family, which is described as \"Ribosomal protein L20\". Interpro entry for IP:IPR001081. IPB001081 32-77 8e-39","Residues 70 to 114 match (2e-09) PD:PD589691 which is described as RIBOSOMAL L20 50S RRNA-BINDING PROTEOME COMPLETE CHLOROPLAST B1060H01.9 ","","","","","","","","","","","Fri Jan 10 15:10:12 2003","Fri Jan 10 15:10:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02039 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 109 (E-value = 7.2e-69) place AA02039 in the Ribosomal_L20 family which is described as Ribosomal protein L20 (PF00453)","","","","","Fayat,G., Mayaux,J.F., Sacerdot,C., Fromant,M., Springer,M., Grunberg-Manago,M. and Blanquet,S. Escherichia coli phenylalanyl-tRNA synthetase operon region. Evidence for an attenuation mechanism. Identification of the gene for the ribosomal protein L20 J. Mol. Biol. 171 (3), 239-261 (1983) PubMed: 6317865 Springer,M., Mayaux,J.F., Fayat,G., Plumbridge,J.A., Graffe,M., Blanquet,S. and Grunberg-Manago,M. Attenuation control of the Escherichia coli phenylalanyl-tRNA synthetase operon J. Mol. Biol. 181 (4), 467-478 (1985) PubMed: 3158742 Arnold,R.J. and Reilly,J.P. Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry Anal. Biochem. 269 (1), 105-112 (1999) PubMed: 10094780 ","","Fri Jan 10 15:10:12 2003","1","","","" "AA02040","1388276","1388494","219","ATGCTTCTAAAAATTCCGCCGAAATTATCGGTATCAAGTTTTATAAGGTATTTAAAGGGAAAATCATCGTTAATGATTTTTGAAAGGCATGCGAACCTAAAATACAACTATGGTAACCGATATTTTTGGTCGAAAGGCTATTATGTAAGCACGGTAGGGCTAAATACAAAGGCTGTGGAGGAGTATATAAGGAATCAGGAAAAAGGAGGATATTTATAC","","","8607","MLLKIPPKLSVSSFIRYLKGKSSLMIFERHANLKYNYGNRYFWSKGYYVSTVGLNTKAVEEYIRNQEKGGYLY","1388494","","hypothetical protein (possible transposase fragment)","Periplasm, Extracellular","This sequence is similar to gi12584558, a predicted transposase from Clostridium thermocellum. Also see gi|20147458 from Clostridium perfringens.","
InterPro
IPR002686
Family
Transposase IS200-like
PF01797\"[1-59]TTransposase_17


","BeTs to 7 clades of COG1943COG name: Predicted transposaseFunctional Class: LThe phylogenetic pattern of COG1943 is -o-p----vd--b-efgh-nuj----Number of proteins in this genome belonging to this COG is","","Residues 2 to 59 match (5e-17) PD:PD588153 which is described as TRANSPOSASE PROTEOME COMPLETE IS200 INSERTION SEQUENCE ELEMENT FOR FROM PLASMID ","","","","","","","","","","","","Wed Feb 25 16:59:35 2004","Wed Feb 25 17:00:11 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA0823 and AA0232. AA02040 is paralogously related to AA01244 (3e-30), AA00357 (3e-30) and AA01226 (8e-25).","Wed Feb 25 16:59:35 2004","","","","","Residues 1 to 59 (E-value = 4.6e-14) place AA02040 in the Transposase_17 family which is described as Transposase IS200 like (PF01797)","","","","","","","","1","","","" "AA02041","1389299","1389183","117","ATGAAAGTTGTGATCAATATCACAAAACATTACAAATCGTATTTTCTAAAATTAATAGGCGATGCTTTGCCGGGATTCGAGAGAGAAAAAAGTGCGGTCAAAAATTTTAGTATTTTT","","","4516","MKVVINITKHYKSYFLKLIGDALPGFEREKSAVKNFSIF","1389183","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 16:35:08 2004","Wed Feb 25 16:35:08 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02041 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 16:35:08 2004","","","","","","","","","","","","","1","","","" "AA02042","1389390","1390337","948","ATGACAATATTAAAACAAAAACGGTTGGAAAAATTATACGGTAAAGAGCGAATTTTTCGCGCTTTAGCAATTGATCAGCGCGGCGCGTTAAAGCGGATGCTGGGTGAAGAGGTAACGGATGAGCAGCTTCAGATTTTTAAAAGGTTAGTGTCCGAGAACTTGACGACACGGGCTTCAGCCATTTTGTTGGATCTGGAATTTGGCTGGCAGGCAGCGGGATTAAAAGAGCAGCATTGCGGTTTAATTATGGCTTACGAAAAAACCGGCTATGACAAAACCAAAATCGGACGTTTTCCCGATTTGATTGACGGCGTATCGGTTAAGGGGTTGAAAGAGAAAGGCGCAGATGCGGTGAAATTGCTGTTGTACTTTGATGTAGATGAGGGTGACGCGATTAATCGGGTGAAAACCGCTTTTGTAGAACGCGTCGGTTCCGAATGTATCGCAGAGGAAATGCCGTTCTTTTTGGAGATTTTGACGTATGACTCTAATGTTTCGTATAAGAAAGAATTCGCAAAAATGAAACCTGGAAAAGTGATTGAAGCGATGAAAGTGTTTTCGAATAAACGTTTTGCGGTGGATGTCTTAAAAGTGGAAGTTCCGGTAGATATGAATTATGTGCAAGGATTTACAAATGGTGAGGACTATGTCTATACGCAAAAAAGCGCACAGGCATTTTTTAAAGAGCAAAGCGATTGCAGTGATATTCCGTTTATCTTCCTAAGCGCAGGTGTTTCGCCGAAATTGTTTCAAGACACGCTTGAATTTGCCAAATCGGCTGGTTCTACCTTTAATGGCGTATTGTGCGGACGCGCTACCTGGGCGGGCAGTGCCGAGGCATTTAAAACTCAAGGCGTGGCACAAGCGGCTGAATGGTTACGTATACAAGGTGTAAAAAATATCAATGAACTCAATGAGGTATTAATGAAATCCGCAACACCGGTTAAG","","","35361","MTILKQKRLEKLYGKERIFRALAIDQRGALKRMLGEEVTDEQLQIFKRLVSENLTTRASAILLDLEFGWQAAGLKEQHCGLIMAYEKTGYDKTKIGRFPDLIDGVSVKGLKEKGADAVKLLLYFDVDEGDAINRVKTAFVERVGSECIAEEMPFFLEILTYDSNVSYKKEFAKMKPGKVIEAMKVFSNKRFAVDVLKVEVPVDMNYVQGFTNGEDYVYTQKSAQAFFKEQSDCSDIPFIFLSAGVSPKLFQDTLEFAKSAGSTFNGVLCGRATWAGSAEAFKTQGVAQAAEWLRIQGVKNINELNEVLMKSATPVK","1390337","[CATALYTIC ACTIVITY] D-tagatose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.[PATHWAY] Tagatose 6-phosphate pathway of lactose catabolism.","tagatose 1,6-diphosphate aldolase","Cytoplasm","","
InterPro
IPR002915
Family
Deoxyribose-phosphate aldolase/phospho-2-dehydro-3-deoxyheptonate aldolase
PF01791\"[19-276]TDeoC
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[2-315]Tno description


","No hits to the COGs database.","","Residues 9 to 277 match (4e-80) PD:PD017729 which is described as ALDOLASE COMPLETE PROTEOME TAGATOSE 16-DIPHOSPHATE TAGATOSE-BISPHOSPHATE LACTOSE LYASE METABOLISM YIHT ","","","","","","","","","","","Fri Jan 10 15:15:00 2003","Fri Jan 10 15:15:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02042 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 316 (E-value = 1.2e-130) place AA02042 in the LacD family which is described as Tagatose 1,6-diphosphate aldolase, (LacD) (PF04274)","","","","","de Vos,W.M., Boerrigter,I., van Rooyen,R.J., Reiche,B. and Hengstenberg,W. Characterization of the lactose-specific enzymes of the phosphotransferase system in Lactococcus lactis. J. Biol. Chem. 265 (36): 22554-22560 (1990) [PubMed: 2125052]. van Rooijen,R.J., van Schalkwijk,S. and de Vos,W.M. Molecular cloning, characterization, and nucleotide sequence of the tagatose 6-phosphate pathway gene cluster of the lactose operon of Lactococcus lactis. J. Biol. Chem. 266 (11): 7176-7181 (1991) [PubMed: 1901863].Rosey,E.L. and Stewart,G.C. The nucleotide sequence of the lacC and lacD genes of Staphylococcus aureus. Nucleic Acids Res. 17 (10): 3980 (1989) [PubMed: 2543958]. Rosey,E.L., Oskouian,B. and Stewart,G.C. Lactose metabolism by Staphylococcus aureus: characterization of lacABCD, the structural genes of the tagatose 6-phosphate pathway. J. Bacteriol. 173 (19): 5992-5998 (1991) [PubMed: 1655695].","","Fri Jan 10 15:15:00 2003","1","","","" "AA02043","1390358","1391647","1290","ATGCAAGAATTAGTGAAAAAACATAAAGCAGGGCAACAAGTGGGAATTTGCTCGGTTTGTTCGGCGCATCCGCCGGTGGTTGAAGCAGCGTTGCGGTTTGATTTGGAGACGGATAATGATGTATTAATTGAAGCGACGTCTAATCAAGTGAATCAATTCGGCGGTTATACCGGTATGAAACCGACAGATTTTAAAGCTTTCGTTTATCAGATAGCGGAAAAAGTGAATTTTCCGAAAGAGCGCATTATTTTAAGTGGCGATCATCTGGGACCGAATTGTTGGCAAAATGAAGCGGCTGAAATGGCGATGGAAAAAGCCAAAGCGTTGGTGATTGATTATGCGAAAGCGGGTTTTACTAAAATTCATTTGGATGCTTCAATGTCTTGTGCTGATGATCCGGTGCCCCTTCCTCCGACTGTAATCGCCGAATGCGCGGCAGAGTTATGCGCCGCCGTTGAAAGCGTGTTAAGCGAAGAGCAAAAAGCCAAAATCAGCTATATCATCGGCACCGAAGTACCTGTGCCGGGTGGTGAGGCGCATACCATTCAATGTGTCGACGTTACCACAGTGGCAAGCACCAACGAAACTATTGAGACCCATCGCAAGGCATTTGCGAGACGTAATCTGGACGATGCCTTCCGACGCGTGGCGGGGCTGGTCGTGCAGCCGGGTGTAGAATTTAATCATTCTAATGTCATTTTATATAAACCGGAATTGGCACAAGAACTGTCGAAATTCATTGAAACCACACCTTATGTTTTTGAAGCCCATTCTACCGATTATCAGACAAAATATGCTTATCGTAGTTTGGTGAAAGATCACTTTGCCATTCTTAAAGCCGGACCGGCGTTAACCTTTGCGTTACGGGAAGCACTCTTCGCCTTGGCAAAAATTGAAGATGAATTGATCCCGCCGGAGCGTAAAAGCCATTTATTAGACGTAATCGACCAGATCATGCAGGATGAACCGAAATATTGGAGCAAATATTACTCACCACAACATTCCAAAGCCATGATTGATTTGCATTTCAGTCTGTCGGATCGTATTCGTTACTACTGGCCGAACGAGCGCATTAACAGTACGGTGGAAAAACTGATTGCCAACCTGTCCGCTGAAAATATCCCGTTGGGCCTGCTCAGCCAGTATTTGCCGGATCAATATCGCAAAGTGTTGTTGGAAAAAATACCGGCAAAACCGACCGCACTTATTCTGGATAAGATTCAGCAGGTGCTGAGCGATTATGCATTTGGTTGCAACGAGGAGAACGCTGATGAAAACCGACATTTTAAT","","","48193","MQELVKKHKAGQQVGICSVCSAHPPVVEAALRFDLETDNDVLIEATSNQVNQFGGYTGMKPTDFKAFVYQIAEKVNFPKERIILSGDHLGPNCWQNEAAEMAMEKAKALVIDYAKAGFTKIHLDASMSCADDPVPLPPTVIAECAAELCAAVESVLSEEQKAKISYIIGTEVPVPGGEAHTIQCVDVTTVASTNETIETHRKAFARRNLDDAFRRVAGLVVQPGVEFNHSNVILYKPELAQELSKFIETTPYVFEAHSTDYQTKYAYRSLVKDHFAILKAGPALTFALREALFALAKIEDELIPPERKSHLLDVIDQIMQDEPKYWSKYYSPQHSKAMIDLHFSLSDRIRYYWPNERINSTVEKLIANLSAENIPLGLLSQYLPDQYRKVLLEKIPAKPTALILDKIQQVLSDYAFGCNEENADENRHFN","1391647","","tagatose 6-phosphate kinase","Cytoplasm","","
InterPro
IPR012062
Family
D-tagatose-bisphosphate aldolase, class II, non-catalytic subunit AgaZ
PIRSF009264\"[1-424]TD-tagatose-bisphosphate aldolase class II accessory protein Z
PF08013\"[1-420]TTagatose_6_P_K
TIGR02810\"[2-419]TagaZ_gatZ: D-tagatose-bisphosphate aldolase


","No hits to the COGs database.","","Residues 1 to 417 match (3e-149) PD:PD025113 which is described as KINASE COMPLETE TAGATOSE PROTEOME 6-PHOSPHATE TRANSFERASE GATZ AGAZ PLASMID 2.7.1.- ","","","","","","","","","","","","Fri Jan 10 15:23:26 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02043 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Nobelmann,B. and Lengeler,J.W. Sequence of the gat operon for galactitol utilization from a wild-type strain EC3132 of Escherichia coli. Biochim. Biophys. Acta 1262 (1): 69-72 (1995) [PubMed: 7772602].","","Fri Jan 10 15:23:26 2003","1","","","" "AA02044","1391628","1392074","447","ATGAAAACCGACATTTTAATTAAAACGGGTGTGGATTTTGCCGATTATGAAGCGGTGTTTCATCATTTGGCGGACAGATTTATCGCCGAAGGATTCGCCAAAGCATCGTACCGCGAGGCGATTTTTGCACGGGAAAAAGATTTTCCCACCGGCATTGCCTTAGAATATCACGCCGTCGCCATTCCCCATAGTGACGCCGAACACGCGCTGAAATCGGCGATTTATTTTATTCGTCCGAATAAACCGGTGAAGTTTAATCGTCCTGATGAAGACAGTCAGGTAGATGCAGAATTGATTATCGCGTTAGTGGTAACCGATCCGCAGGATCAACTGGTGGTGCTACATAAATTATTCGGAAAATTGCAGGACAATGCCTTTGTGGAGCAGCTTCTTATGGCTGAGGAAAGCGCGTTGTCCGACCTACTTGAACAACATTTAAGTTTTAAC","","","17990","MKTDILIKTGVDFADYEAVFHHLADRFIAEGFAKASYREAIFAREKDFPTGIALEYHAVAIPHSDAEHALKSAIYFIRPNKPVKFNRPDEDSQVDAELIIALVVTDPQDQLVVLHKLFGKLQDNAFVEQLLMAEESALSDLLEQHLSFN","1392074","[FUNCTION] This is a component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. The IICD domains contain the sugar binding site and the transmembrane channel; the IIA domain contains the primary phosphorylation site (the donor is phospho-hpr); IIA transfers its phosphoryl group to the IIB domain which finally transfers it to the sugar. ","phosphotransferase system enzyme II, galactitol specific, protein A","Cytoplasm, Inner membrane","","
InterPro
IPR002178
Domain
Phosphotransferase system, phosphoenolpyruvate-dependent sugar EIIA 2
PD001689\"[6-134]TQ8RD66_THETN_Q8RD66;
G3DSA:3.40.930.10\"[7-137]Tno description
PF00359\"[1-145]TPTS_EIIA_2
PS51094\"[1-145]TPTS_EIIA_TYPE_2


","BeTs to 4 clades of COG1762COG name: Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type)Functional Class: G,TThe phylogenetic pattern of COG1762 is ---------d-lb-efgh-n-j-itwNumber of proteins in this genome belonging to this COG is","","Residues 73 to 146 match (8e-11) PD:PD028535 which is described as COMPONENT IIA PHOSPHOTRANSFERASE GALACTITOL-SPECIFIC SYSTEM SYSTEM TRANSFERASE PTS ENZYME SUGAR ","","","","","","","","","","","Fri Jan 10 15:37:50 2003","Fri Jan 10 15:28:01 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02044 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 145 (E-value = 5.9e-07) place AA02044 in the PTS_EIIA_2 family which is described as Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2 (PF00359)","","","",""," Nobelmann,B. and Lengeler,J.W. Sequence of the gat operon for galactitol utilization from a wild-type strain EC3132 of Escherichia coli. Biochim. Biophys. Acta 1262 (1): 69-72 (1995) PubMed: 7772602.","","Wed Jan 29 14:57:13 2003","1","","","" "AA02045","1392096","1392377","282","ATGAAAAAGAAAGTGATTGTAGCCTGTGGAGGCGCGGTCGCCACTTCAACCTTAGCAGCGGAAGAAATCAAAGAATTATGTGAAGAAAACCATATTCCGCTGGAACTGGTACAATGCCGAATCAATGAAATCGACAGTTATATTCAAGATGTGGATTTGATTTGCACCACCTCGAAAATTACCCAAACCTACGGTGATATTCCGATTATACACGGCATGCCTTTTGTTTCCGGTGTCGGAATTGAACAGCTTAAAAAGAAAATCTTAACAATTTTAAGAGGA","","","10281","MKKKVIVACGGAVATSTLAAEEIKELCEENHIPLELVQCRINEIDSYIQDVDLICTTSKITQTYGDIPIIHGMPFVSGVGIEQLKKKILTILRG","1392377","[FUNCTION] This is a component of the phosphoenolpyruvate-dependent sugar phosphotransferasesystem (PTS), a major carbohydrate active transport system. The IICD domains contain the sugar binding site and the transmembrane channel; the IIA domain contains the primary phosphorylation site (the donor is phospho-hpr); IIA transfers its phosphoryl group to the IIB domain which finally transfers it to the sugar. ","PTS system, galactitol-specific IIB component","Periplasm, Cytoplasm","","
InterPro
IPR003501
Domain
Phosphotransferase system, lactose/cellobiose-specific IIB subunit
PF02302\"[4-93]TPTS_IIB
InterPro
IPR013011
Domain
Phosphotransferase system, EIIB component, type 2
PS51099\"[3-94]TPTS_EIIB_TYPE_2
noIPR
unintegrated
unintegrated
signalp\"[1-20]?signal-peptide


","No hits to the COGs database.","","Residues 3 to 93 match (4e-31) PD:PD065163 which is described as COMPLETE PROTEOME COMPONENT ENZYME PHOSPHOTRANSFERASE TRANSFERASE IIB PTS SYSTEM GALACTITOL-SPECIFIC ","","","","","","","","","","","Fri Jan 10 15:31:18 2003","Fri Jan 10 15:31:18 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02045 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 93 (E-value = 5.4e-16) place AA02045 in the PTS_IIB family which is described as PTS system, Lactose/Cellobiose specific IIB subunit (PF02302)","","","","","Nobelmann,B. and Lengeler,J.W. Sequence of the gat operon for galactitol utilization froma wild-type strain EC3132 of Escherichia coli. Biochim. Biophys. Acta 1262 (1): 69-72 (1995) PubMed: 7772602.","","Wed Jan 29 14:58:30 2003","1","","","" "AA02046","1392386","1393747","1362","ATGTTTACGCAAATCATGCAGTACATTTTGGATCTCGGGCCGTCGGTCATGCTGCCGATTGTGATTATTATTCTTTCGTTGTTGCTCGGCATGAAAGCCGGCGATTCCTTTAAGGCCGGATTACAAATCGGTATTGGCTTTGTAGGGATCGGGCTGGTTATCGGCTTAATGCTGGATTCTATCGGACCGGCAGCAAAAGCGATGGCGCAGGCATTTGATATTAATTTGAATGTGGTGGATATCGGCTGGCCGGGCGCCGCACCGATTACTTGGGCATCGCAAATTGCGTTAATCGCTATTCCTATCACAATCGCGGTGAATATCGTCATGTTGCTGTTGAAACTGACCCGCGTGGTGAACGTAGATATTTGGAATATCTGGCATATGACCTTCACCGGCGCCATTGTGCATATCGCCACCGGTTCTTATTGGCTGGGTATTCTCGGGGTTGTGATTCACGCTGCGTTTGTTTACAAACTGGGAGATTGGTTTAGTCGCGATACGAAAAATTTCTTTGAACTGGACGGCATTGCCATTCCGCACGGCACATCGGCATATTTGGGGCCGATCGCAGTATTGACCGACACCATCATCGAAAAAATCCCGGGCTTGAATAAAGTGCATTTCTCCGCCGATGATTTGCAAAAACGCTTCGGACCGTTCGGCGAGCCGGTCACCGTCGGTTTTGTCATGGGGATTATTATCGGTATTTTGGCGGGCTATCCGTTAAAAGACATTTTGCAGTTAGCGGTAAAAACCGCTGCAGTGATGTTGTTAATGCCACGCGTCATTAAACCAATCATGGACGGTTTAACACCCATTGCCAAGCAAGCACGTAAAAAATTACAGGCGCGTTTCGGCGGCGAAGAATTTCTTATCGGCTTGGATCCGGCGCTCTTGCTTGGACACACCTCAGTGGTGTCCGCCAGTTTGATTTTTATTCCGCTGACTATTTTGGTTGCCGTTATCTTACCGGGAAATCAGGTGCTGCCTTTCGGCGATTTGGCCACTATCGGTTTCTTTGTCGCCATGGCGGTCGCGGTGCATCAGGGCAATTTATTCAGAACGCTGATTTCGGGTGTGATCATCATGTCCATCACTCTTCGGATTGCGACCCAAACCATTGCATTGAATACCCAATTAGCCGCCAATGCAGGCACATTGAAAGCGGGTGAACAGGTGGCGTCGATGGATCAGGGCGGTTCGCCGATCACCTATTTACTTGTACAACTCTGTACTGTTGAAAATCTTATCGGATTGTTGGTTATCGGCTGTATCTATGCGCTGGGCGTGTTTTTAACTTGGCGTCGCGCAAAAGGGTTTGAAAAGGCGGAGCGAGTAGTTGAAAGTGCGGTTAAAAAT","","","48513","MFTQIMQYILDLGPSVMLPIVIIILSLLLGMKAGDSFKAGLQIGIGFVGIGLVIGLMLDSIGPAAKAMAQAFDINLNVVDIGWPGAAPITWASQIALIAIPITIAVNIVMLLLKLTRVVNVDIWNIWHMTFTGAIVHIATGSYWLGILGVVIHAAFVYKLGDWFSRDTKNFFELDGIAIPHGTSAYLGPIAVLTDTIIEKIPGLNKVHFSADDLQKRFGPFGEPVTVGFVMGIIIGILAGYPLKDILQLAVKTAAVMLLMPRVIKPIMDGLTPIAKQARKKLQARFGGEEFLIGLDPALLLGHTSVVSASLIFIPLTILVAVILPGNQVLPFGDLATIGFFVAMAVAVHQGNLFRTLISGVIIMSITLRIATQTIALNTQLAANAGTLKAGEQVASMDQGGSPITYLLVQLCTVENLIGLLVIGCIYALGVFLTWRRAKGFEKAERVVESAVKN","1393747","[FUNCTION] This is a component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. The IICD domains contain the sugar binding site and the transmembrane channel; the IIA domain contains the primary phosphorylation site (the donor is phospho-hpr); IIA transfers its phosphoryl group to the IIB domain which finally transfers it to the sugar. ","PTS system galactitol-specific enzyme IIC","Inner membrane, Cytoplasm","","
InterPro
IPR004703
Family
Phosphotransferase system, galactitol-specific IIC component
PF03611\"[108-412]TEIIC-GAT
InterPro
IPR013014
Domain
Phosphotransferase system, EIIC component, type 2
PS51104\"[6-435]TPTS_EIIC_TYPE_2
InterPro
IPR013853
Family
Phosphotransferase system, galactitol-specific 2C component
TIGR00827\"[9-413]TEIIC-GAT: PTS system, galactitol-specific I
noIPR
unintegrated
unintegrated
signalp\"[1-34]?signal-peptide
tmhmm\"[10-30]?\"[36-58]?\"[67-87]?\"[93-113]?\"[134-156]?\"[225-243]?\"[304-324]?\"[330-348]?\"[357-377]?\"[417-435]?transmembrane_regions


","No hits to the COGs database.","","Residues 5 to 83 match (5e-09) PD:PD331629 which is described as COMPLETE PROTEOME IIC COMPONENT ENZYME PTS SYSTEM GALACTITOL-SPECIFIC PHOSPHOTRANSFERASE SYSTEM ","","","","","","","","","","","Fri Jan 10 15:33:09 2003","Fri Jan 10 15:33:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02046 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 108 to 412 (E-value = 3.6e-178) place AA02046 in the EIIC-GAT family which is described as PTS system Galactitol-specific IIC component (PF03611)","","","","","Nobelmann,B. and Lengeler,J.W. Sequence of the gat operon for galactitol utilization froma wild-type strain EC3132 of Escherichia coli. Biochim.Biophys. Acta 1262 (1): 69-72 (1995) PubMed: 7772602.","","Wed Jan 29 14:59:29 2003","1","","","" "AA02047","1393773","1394813","1041","ATGAAAGCGGTTGTTGTTGAAGAAAACAGAAAATTGGTGCTGGCGGACATTGCGATGCCGAAAATCGAAGATGGGGAAGACGTGCTGGTAAAAGTACTGTATTCGGGGGTATGCGGTTCCGATATTCCGCGCATATTTCACCATGGCACGCATTTTTACCCCATCGTACTAGGGCACGAATTTTGTGGTACGGTAGTGGAAATAGGGAAAAGCGTGACGGAATTCCGCAAAGGGGATTTGGTAGTTTGCGCACCATTACAGCCTTGTTTTGATTGCGAAGAATGTCACAAAGGATATTATTCATTATGTAAAAACTACAATTTCATCGGTTCCCGTCGCTTCGGCGCCAATGCGGAATATATTTGCGTCAACAAGAAAAATTTGGTGAAAGTATCACCAGATTCCAACCCTTTGCATGATGCTTTTATCGAACCTATTACGGTGGGTCTGCACGCCATTAATCTGGCGCAGGGGTGTAGCGATAAAAATGTGATTGTGGTAGGAGCCGGTACTATTGGCTTGCTTGCCGCCCAGTGTGCCGAAGCGCTGGGTGCCAAAAGTGTAACCGTCATCGATATTAACGATGAAAAATTGATGTTGGCGAAAGCGTTGGGTGCTACGCAAACCTTCAATTCCCGTGAATTAGCCGCAGAAGAAATTGAAAAAAGATTACTTGACAGCCGTTTTGACCAACTCGTATTGGAAACCGCCGGCGTTCCGCAATCAGTTGAATTAGCAATAAAAATTGCAGGTCCGCGTGCGCAAGTGGCATTGATCGGCACCCTACATAATGATTTAACCCTGAATCAGAAAGTGTTCGGTTTGATTTTGCGCAAAGAATTGAGCATTCTCGGTTCTTGGATGAATTATTCCGCGCCGTGGCCGGGTGGTGAATGGACGAAGGCAATCGAATTGGTTAAACAAGGTAAAATTCAATTCGACAAGCTGATTGCGTCGGTAAATTTCATTGAAGATTATATTACCGAAGTTAAAAAGCTTGACGGCACACCGATGAATGGAAAAATAGTCTTAAAATTTCAG","","","37987","MKAVVVEENRKLVLADIAMPKIEDGEDVLVKVLYSGVCGSDIPRIFHHGTHFYPIVLGHEFCGTVVEIGKSVTEFRKGDLVVCAPLQPCFDCEECHKGYYSLCKNYNFIGSRRFGANAEYICVNKKNLVKVSPDSNPLHDAFIEPITVGLHAINLAQGCSDKNVIVVGAGTIGLLAAQCAEALGAKSVTVIDINDEKLMLAKALGATQTFNSRELAAEEIEKRLLDSRFDQLVLETAGVPQSVELAIKIAGPRAQVALIGTLHNDLTLNQKVFGLILRKELSILGSWMNYSAPWPGGEWTKAIELVKQGKIQFDKLIASVNFIEDYITEVKKLDGTPMNGKIVLKFQ","1394813","[FUNCTION] This is a component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. The IICD domains contain the sugar binding site and the transmembrane channel; the IIA domain contains the primary phosphorylation site (the donor is phospho-hpr); IIA transfers its phosphoryl group to the IIB domain which finally transfers it to the sugar. ","galactitol-1-phosphate 5-dehydrogenase","Cytoplasm","","
InterPro
IPR002085
Family
Alcohol dehydrogenase superfamily, zinc-containing
PTHR11695\"[11-85]T\"[113-346]TALCOHOL DEHYDROGENASE RELATED
InterPro
IPR002328
Domain
Alcohol dehydrogenase, zinc-containing
PS00059\"[58-72]TADH_ZINC
InterPro
IPR011597
Domain
GroES-related
PD040557\"[162-329]TQ8KCJ7_CHLTE_Q8KCJ7;
InterPro
IPR013149
Domain
Alcohol dehydrogenase, zinc-binding
PF00107\"[160-308]TADH_zinc_N
InterPro
IPR013154
Domain
Alcohol dehydrogenase GroES-like
PF08240\"[25-131]TADH_N
noIPR
unintegrated
unintegrated
G3DSA:3.90.180.10\"[1-180]Tno description
PTHR11695:SF38\"[11-85]T\"[113-346]TZINC-TYPE ALCOHOL DEHYDROGENASE-RELATED


","No hits to the COGs database.","Significant hit ( 1.5e-26) to 4/4 blocks of the IPB002328 family, which is described as \"Zinc-containing alcohol dehydrogenase\". Interpro entry for IP:IPR002328. IPB002328A 12-43 1.7e-05 IPB002328B 54-79 2.3e-12 IPB002328C 89-103 0.0006 IPB002328D 128-175 11Significant hit ( 6e-09) to 1/1 blocks of the IPB002364 family, which is described as \"Quinone oxidoreductase/zeta-crystallin\". Interpro entry for IP:IPR002364. IPB002364 54-81 5.9e-09","Residues 261 to 345 match (1e-22) PD:PD582269 which is described as PROTEOME COMPLETE GALACTITOL-1-PHOSPHATE DEHYDROGENASE OXIDOREDUCTASE 1.1.1.- GALACTITOL GATD ZINC 5-DEHYDROGENASE ","","","","","","","","","","","Fri Jan 10 15:38:10 2003","Thu Jan 16 14:46:41 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02047 is paralogously related to AA01114 (1e-21) and AA00810 (3e-16).","","","","","","Residues 7 to 346 (E-value = 1.6e-75) place AA02047 in the ADH_zinc_N family which is described as Zinc-binding dehydrogenase (PF00107)","","","","","Nobelmann,B. and Lengeler,J.W. Sequence of the gat operon for galactitol utilization from a wild-type strain EC3132 of Escherichia coli. Biochim. Biophys. Acta 1262 (1): 69-72 (1995) [PubMed: 7772602].","","Thu Jan 16 15:03:09 2003","1","","","" "AA02048","1394884","1395639","756","ATGAATGCTTTTGATCGACGAAATCTGATTATCGACTTATTAAAAGAAAACGGTAGCGTATTAGTCAGCGATCTTGCCAAACGCTTTAATGTATCGGAAGTTTCCATTCGTACCGATTTGCGTTTGTTGGAAGCGCAAAATTTACTGACCCGTTTTCACGGCGGTGCGGGATTACTGCAATCACAGGATAACGAAACCTTTCTGGATGACCGCTATTTATTATCGCCTGATCCGAAAATCCGTATCGCCAAAGCAGCGGCCGGACTCATTAAAGAAGGGGATACAATTATTCTGGACAGTGGTAGCACGACGATGATGATTGCCAATGAGTTATTGAAAATTAAGAATATCACCGTTATCACCAACAACCTTCCCGCCGCTTTTGTGTTGTCCGATTCCGTAGATATTACATTGGTGATTTGCGGCGGTTATGTGCGTCACAAAACCCGCTCCATGCACGGCACTATTGCGGAACACACACTTAACGGCATTCGTGCGGATATTATGTTCGTCGGGGCGGATGGCATTGATCCGATTAATGGACTTACCACTTTTAACGAAGGCTATCACATCAGCTCCATCATGGCGAAAGCATCGTCAAAAGTGGTATGTGTTGCCGATTCGACGAAATTCAATCGTAACGGTTTTAATCAGGTGTTACCAATGAGTGTAGTAAATTTAATTATTACCGACAGCAATATTACGGAAAAAAATAAAGCGGAATTGGCGGGGTTAAATATGCCGTTGCAGGTGGTT","","","27441","MNAFDRRNLIIDLLKENGSVLVSDLAKRFNVSEVSIRTDLRLLEAQNLLTRFHGGAGLLQSQDNETFLDDRYLLSPDPKIRIAKAAAGLIKEGDTIILDSGSTTMMIANELLKIKNITVITNNLPAAFVLSDSVDITLVICGGYVRHKTRSMHGTIAEHTLNGIRADIMFVGADGIDPINGLTTFNEGYHISSIMAKASSKVVCVADSTKFNRNGFNQVLPMSVVNLIITDSNITEKNKAELAGLNMPLQVV","1395639","[FUNCTION] Repressor of the gat operon for galacticol transport and metabolism. ","galactitol utilization operon repressor","Cytoplasm","","
InterPro
IPR001034
Domain
Bacterial regulatory protein, DeoR N-terminal
PR00037\"[24-38]T\"[38-56]THTHLACR
PF08220\"[6-62]THTH_DeoR
SM00420\"[6-58]THTH_DEOR
PS51000\"[3-58]THTH_DEOR_2
InterPro
IPR001969
Active_site
Peptidase aspartic, active site
PS00141\"[96-107]?ASP_PROTEASE
InterPro
IPR014036
Domain
Bacterial regulatory protein, DeoR
PF00455\"[76-231]TDeoR


","BeTs to 9 clades of COG1349COG name: Transcriptional regulators of sugar metabolismFunctional Class: K,GThe phylogenetic pattern of COG1349 is -------qvd-lb-efgh-n-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 9.3e-42) to 5/5 blocks of the IPB001034 family, which is described as \"Bacterial regulatory protein, DeoR family\". Interpro entry for IP:IPR001034. IPB001034A 20-55 5.9e-14 IPB001034B 79-103 2.6e-14 IPB001034C 120-130 0.04 IPB001034D 142-154 0.0039 IPB001034E 203-213 0.099Significant hit ( 2e-05) to 1/1 blocks of the IPB000524 family, which is described as \"Bacterial regulatory proteins, GntR family\". Interpro entry for IP:IPR000524. IPB000524 19-59 1.9e-05","Residues 36 to 108 match (2e-07) PD:PD002333 which is described as PROTEOME COMPLETE TRANSCRIPTIONAL TRANSCRIPTION DNA-BINDING REGULATION REGULATOR REPRESSOR DEOR FAMILY ","","","","","","","","","","","Fri Jan 10 15:41:40 2003","Fri Jan 10 15:41:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02048 is paralogously related to AA00973 (2e-35), AA00308 (2e-27), AA01698 (3e-20), AA01546 (4e-13) and AA00585 (6e-12).","","","","","","Residues 6 to 231 (E-value = 1.3e-74) place AA02048 in the DeoR family which is described as Bacterial regulatory proteins, deoR family (PF00455)","","","","","Nobelmann,B. and Lengeler,J.W. Sequence of the gat operon for galactitol utilizationfrom a wild-type strain EC3132 of Escherichia coli.Biochim. Biophys. Acta 1262 (1): 69-72 (1995) [PubMed: 7772602].Komoda,Y., Enomoto,M. and Tominaga,A. Large inversion in Escherichia coli K-12 1485IN between inversely oriented IS3 elements near lac and cdd. Genetics 129 (3): 639-645 (1991) [PubMed: 1661252].","","Fri Jan 10 15:41:40 2003","1","","","" "AA02049","1395666","1395755","90","TTGAAGAGGATTTATAAAAACATCGTTTTTTGTGACCGCACTTTTGAGAACAAGAAACCGTTCCAACATCGGAACGGTTTTTTATGCGGC","","","3655","LKRIYKNIVFCDRTFENKKPFQHRNGFLCG","1395755","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 16:33:28 2004","Wed Feb 25 16:33:28 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02049 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 16:33:28 2004","","","","","","","","","","","","","1","","","" "AA02050","1397612","1395765","1848","ATGCAAAATTATCCCCTTTTATCATTAATTAATTCGCCTGAAGATTTGCGTTTGTTGAACAAAGAGCAACTTCCTCAAGTGTGTCAGGAATTGCGTGAATATCTGTTGGAATCGGTTAGTCAAAGCAGCGGGCATTTAGCCTCAGGCTTAGGCACGGTGGAACTTACCGTTGCCTTGCATTATGTATTTAAAACCCCTTTCGATCAGCTAATTTGGGATGTAGGACATCAGGCATATCCCCATAAAATTCTGACCGGTCGCCGCGACCAAATGCCGACCATCCGCCAAAAAGGCGGACTACATCCTTTCCCGTGGCGCGGTGAAAGTGAATTCGATGTATTAAGTGTGGGACACTCCTCTACTTCTATCAGTGCCGGATTAGGAATTGCCATTGCCGCCGAGCGTGAAAATGCAGGACGCAAAACTGTTTGTGTCATCGGCGACGGTGCGATTACCGCAGGCATGGCATTTGAAGCGCTGAACCATGCCGGTTCATTGCATACGGATATGCTGGTGATTCTCAATGACAACGAAATGTCCATTTCTGAAAATGTAGGTGCGCTGAATAACCATTTAGCGCGTTTGCTGTCCGGTTCCTTCTATTCCAGCCTTCGCGAAGGCGGCAAAAAAATCCTTTCCGGTGTGCCGCCCATTAAAGAATTTGTGAAAAAAACCGAAGAACACGTCAAAGGTTTTGTCTCACCAGGCAGTACTATGTTTGAAGAACTCGGGTTTAACTACATCGGACCAATTGATGGACACAACGTGGAAGAACTGATTAGCACCTTGCAAAATATGAGCTCACTCAAAGGTCCGCAATTTTTACATATCGTCACTAAAAAAGGCAAAGGCTACACACCGGCGGAAAAAGACCCTATCGGCTTCCACGGGGTACCGAAATTTAACCATTTAAGTGGTGAATTGCCGAAATCCAACGCCACCCCGACCTATTCTAAAATTTTCGGTGATTGGCTATGTGAAATAGCGGAACAGGATCCGAAACTCATTGGCATTACCCCGGCAATGCGCGAAGGTTCCGGCATGGTGGAATTTTCTCAACGCTTTCCGCAACAATATTTTGATGTTGCCATCGCCGAACAACACGCCGTGACTTTTGCCGCCGGTTTGGCAATCGGCGGGTATAAACCGGTGGTCGCCATCTATTCCACATTCCTGCAACGGGCTTACGACCAGTTAATTCATGATGTGGCGATTCAGAATCTCCCCGTCTTATTTGCCATTGACCGCGCCGGCATTGTCGGTGCCGACGGACAAACCCACCAAGGGGCTTTCGATATCAGTTTCATGCGCTGCATTCCGAATCTCGTGATCATGACACCAAGCGATGAAAATGAATGCCGTCAAATGCTTTACACCGGCTATCATTGCGGCAAGCCCGCCGCCGTGCGTTATCCTCGCGGCAATGCGGTTGGTGTTGAATTGGAACCGTTGCAACCATTGGAATTGGGAAAATCCAAACTGATTCGCGAAGGCAAAAAAATCGCCATTTTAAATTTCGGTACGCTATTACCAAACGCTCTGCAAGTGGCGGAAAAACTCAATGCCACAGTTATCGATATGCGTTTCGTTAAACCGCTGGATGCTGCTCGTATTAATGCGGTCGCTAAACATGAACTTATCGTTACATTGGAAGAAAATGCTCTTCAAGGGGGCGCAGGCAGCGCGGTAGCCGAAGTGTTGAATCATCAACAACATCAGGTAAAATTGCTGCAATTAGGCTTACCGGATTTCTTTATCCCGCAAGGCACCCAATCGGAAATGCTCACCGAACTTAAGTTGGATGCTGCAGGGATTGAATGGCAGATTTTGAATTATTTAGGTGAGAAG","","","67380","MQNYPLLSLINSPEDLRLLNKEQLPQVCQELREYLLESVSQSSGHLASGLGTVELTVALHYVFKTPFDQLIWDVGHQAYPHKILTGRRDQMPTIRQKGGLHPFPWRGESEFDVLSVGHSSTSISAGLGIAIAAERENAGRKTVCVIGDGAITAGMAFEALNHAGSLHTDMLVILNDNEMSISENVGALNNHLARLLSGSFYSSLREGGKKILSGVPPIKEFVKKTEEHVKGFVSPGSTMFEELGFNYIGPIDGHNVEELISTLQNMSSLKGPQFLHIVTKKGKGYTPAEKDPIGFHGVPKFNHLSGELPKSNATPTYSKIFGDWLCEIAEQDPKLIGITPAMREGSGMVEFSQRFPQQYFDVAIAEQHAVTFAAGLAIGGYKPVVAIYSTFLQRAYDQLIHDVAIQNLPVLFAIDRAGIVGADGQTHQGAFDISFMRCIPNLVIMTPSDENECRQMLYTGYHCGKPAAVRYPRGNAVGVELEPLQPLELGKSKLIREGKKIAILNFGTLLPNALQVAEKLNATVIDMRFVKPLDAARINAVAKHELIVTLEENALQGGAGSAVAEVLNHQQHQVKLLQLGLPDFFIPQGTQSEMLTELKLDAAGIEWQILNYLGEK","1395765","[FUNCTION] Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP) (By similarity).","1-deoxy-D-xylulose 5-phosphate synthase","Cytoplasm, Inner membrane","","
InterPro
IPR005474
Domain
Transketolase, N-terminal
PS00801\"[32-51]TTRANSKETOLASE_1
InterPro
IPR005475
Domain
Transketolase, central region
PF02779\"[313-479]TTransket_pyr
PS00802\"[421-437]TTRANSKETOLASE_2
InterPro
IPR005476
Domain
Transketolase, C-terminal
PF02780\"[490-605]TTransketolase_C
InterPro
IPR005477
Family
Deoxyxylulose-5-phosphate synthase
PIRSF005462\"[4-615]TDeoxyxylulose-5-phosphate synthase
TIGR00204\"[7-614]Tdxs: 1-deoxy-D-xylulose-5-phosphate synthas
InterPro
IPR009014
Domain
Transketolase, C-terminal-like
G3DSA:3.40.50.920\"[489-615]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.970\"[121-185]T\"[302-488]Tno description
PTHR11624\"[343-616]TDEHYDROGENASE RELATED
PTHR11624:SF20\"[343-616]T1-DEOXYXYLULOSE-5-PHOSPHATE SYNTHASE


","BeTs to 16 clades of COG1154COG name: Deoxyxylulose-5-phosphate synthaseFunctional Class: H,IThe phylogenetic pattern of COG1154 is -------qvdrlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is","Significant hit ( 3.7e-39) to 3/3 blocks of the IPB000360 family, which is described as \"Transketolase\". Interpro entry for IP:IPR000360. IPB000360A 44-55 0.077 IPB000360B 369-408 3.7e-17 IPB000360C 420-449 3.1e-17Significant hit ( 2.5e-05) to 1/6 blocks of the IPB001017 family, which is described as \"Dehydrogenase, E1 component\". Interpro entry for IP:IPR001017. IPB001017D 145-183 2.5e-05","Residues 487 to 612 match (8e-07) PD:PD432802 which is described as SYNTHASE THIAMINE BIOSYNTHESIS DXPS PYROPHOSPHATE ISOPRENE PROTEOME 1- COMPLETE 5-PHOSPHATE ","","","","","","","","","","","Fri Jan 10 15:55:43 2003","Fri Jan 10 15:55:43 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02050 is paralogously related to AA02563 (5e-24), AA01563 (4e-06) and AA02564 (0.001).","","","","","","Residues 490 to 605 (E-value = 4.6e-35) place AA02050 in the Transketolase_C family which is described as Transketolase, C-terminal domain (PF02780)","","","","","Lois,L.M., Campos,N., Putra,S.R., Danielsen,K., Rohmer,M. and Boronat,A. Cloning and characterization of a gene from Escherichia coli encoding a transketolase-like enzyme that catalyzes the synthesisof D-1-deoxyxylulose 5-phosphate, a common precursor for isoprenoid, thiamin, and pyridoxol biosynthesis. Proc. Natl. Acad. Sci. U.S.A. 95 (5): 2105-2110 (1998) [PubMed: 9482846].Sprenger,G.A., Schorken,U., Wiegert,T., Grolle,S., de Graaf,A.A., Taylor,S.V., Begley,T.P., Bringer-Meyer,S. and Sahm,H.Identification of a thiamin-dependent synthase in Escherichia coli required for the formation of the 1-deoxy-D-xylulose 5-phosphateprecursor to isoprenoids, thiamin, and pyridoxol. Proc. Natl. Acad. Sci. U.S.A. 94 (24): 12857-12862 (1997) [PubMed: 9371765].Kuzuyama,T., Takagi,M., Takahashi,S. and Seto,H. Cloning and characterization of 1-deoxy-D-xylulose 5-phosphate synthase from Streptomyces sp. Strain CL190, which uses both themevalonate and nonmevalonate pathways for isopentenyl diphosphatebiosynthesis. J. Bacteriol. 182 (4): 891-897 (2000) [PubMed: 10648511].","","Fri Jan 10 15:55:43 2003","1","","","" "AA02051","1398587","1397700","888","ATGTATCATTTTTCGCAAGATTTACAGCACGTTCAGCAACGGATTAATCAATTTTTAGCCAAGCAATTTGCGCACATTGACAGCGCCCCCGCGCCACTGGCTGAAGCCATGAAATACGGATTGCTATTGGGTGGCAAACGCATTCGTCCTTTTTTGGTGTACGCCACCGGCAAAATGCTAGGCGCTGACATGGCGCACCTGGATTACGCCGCCGCCGCTATTGAAGCCATTCACGCTTACTCGTTAATTCACGATGATTTGCCCGCTATGGACGACGATGAATTGCGTCGCGGACACCAAACCTGCCACATTGCATTTGATGAAGCCACCGCTATTTTAGCTGGCGATGCGCTGCAGACATTGGCTTTTGAGATCTTAACGGATATTCCTCATTTATCGGCAGAACAAAAACTGATGTTAATTAAAACGTTAAGTGCGGCAGCAGGCGTAAAAGGGATGTGTTTGGGGCAAAGTCTGGATTTAATTTCAGAACAAAAAATCATCAGCTTACAAAAACTGGAACAGATTCATTTAAACAAAACCGGCGCATTACTGACCGCTGCCTTAAAAATGGGCTTTATTTGCTCACCGCACTTTGCCGATGCAGCGTTAGCGCAACAATTGGAACGCTATGCTACGGCCATCGGTTTAGCCTTCCAAGTGCAGGATGATATTTTAGACATCGAGGGCGACAGTGCGACCCTCGGCAAAACCACCGGTTCCGATTTAACCGCGGACAAAAGCACTTACCCGAAATTATTGGGGCTTGAAGGCGCCAAACAAAAAGCACTGGAACTATACGAAAGAGCATTAACCGAGCTAAAAAATTTACCTTTTAATACCACCGCACTTTATGCGTTGGCGGAATTTATCGTTAAACGAAAAAGC","","","37386","MYHFSQDLQHVQQRINQFLAKQFAHIDSAPAPLAEAMKYGLLLGGKRIRPFLVYATGKMLGADMAHLDYAAAAIEAIHAYSLIHDDLPAMDDDELRRGHQTCHIAFDEATAILAGDALQTLAFEILTDIPHLSAEQKLMLIKTLSAAAGVKGMCLGQSLDLISEQKIISLQKLEQIHLNKTGALLTAALKMGFICSPHFADAALAQQLERYATAIGLAFQVQDDILDIEGDSATLGKTTGSDLTADKSTYPKLLGLEGAKQKALELYERALTELKNLPFNTTALYALAEFIVKRKS","1397700","","geranylgeranyl pyrophosphate synthase; farnesyl-diphosphate synthase","Cytoplasm","","
InterPro
IPR000092
Family
Polyprenyl synthetase
PTHR12001\"[1-296]TGERANYLGERANYL PYROPHOSPHATE SYNTHASE
PF00348\"[33-292]Tpolyprenyl_synt
PS00444\"[215-227]TPOLYPRENYL_SYNTHET_2
PS00723\"[82-98]TPOLYPRENYL_SYNTHET_1
noIPR
unintegrated
unintegrated
G3DSA:1.10.600.10\"[2-292]Tno description
PTHR12001:SF8\"[1-296]TGERANYL GERANYL PYROPHOSPHATE SYNTHASE


","BeTs to 25 clades of COG0142COG name: Geranylgeranyl pyrophosphate synthaseFunctional Class: HThe phylogenetic pattern of COG0142 is aompkzyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 3.9e-37) to 5/5 blocks of the IPB000092 family, which is described as \"Polyprenyl synthetase\". Interpro entry for IP:IPR000092. IPB000092A 44-53 0.00085 IPB000092B 74-85 1.2e-05 IPB000092C 88-103 1.7e-06 IPB000092D 156-161 24 IPB000092E 215-237 3.8e-15","Residues 11 to 268 match (6e-93) PD:PD000572 which is described as SYNTHASE TRANSFERASE COMPLETE PROTEOME SYNTHETASE PYROPHOSPHATE DIPHOSPHATE GERANYLGERANYL FARNESYL GERANYLTRANSTRANSFERASE ","","","","","","","","","","","","Fri Jan 10 15:57:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02051 is paralogously related to AA02879 (1e-24).","","","","","","Residues 33 to 292 (E-value = 1.3e-110) place AA02051 in the polyprenyl_synt family which is described as Polyprenyl synthetase (PF00348)","","","","","Fujisaki,S., Hara,H., Nishimura,Y., Horiuchi,K. and Nishino,T.Cloning and nucleotide sequence of the ispA gene responsible for farnesyl diphosphate synthase activity in Escherichia coli. J. Biochem. 108(6): 995-1000, 1990. PubMed: 2089044.","","Fri Jan 10 15:57:35 2003","1","","","" "AA02052","1398969","1398601","369","GTGCGGTACTTTTTTGCGGCGTTTTTCACCGGCATTTTTCAGCGGAAATACCTCAAATTCGCCCTAACAAAATCACTAAAAATCAAGTACAATACGCCAATTCTATTTTGCGCAAAGGACAATATCATGGCACGTAAGCCGGCTGAAAAAAACGAACCTGATTTTGAAAATACGCTAAAACAGTTGGAGGAAATCGTTTCCCGTTTGGAAAATAACGAACTTTCCCTTGAAGACGCTTTAAAAGATTTTGAACAAGGGATCAAATTGGCTCAATTGGGTCAGGAACGTTTACAACAAGCGGAACAACGCATCCAAATTTTGTTGCAAAAAAGCGAAAGCGCAAAACTCAGCGATTATCAACCGGAAGAA","","","14405","VRYFFAAFFTGIFQRKYLKFALTKSLKIKYNTPILFCAKDNIMARKPAEKNEPDFENTLKQLEEIVSRLENNELSLEDALKDFEQGIKLAQLGQERLQQAEQRIQILLQKSESAKLSDYQPEE","1398601","[FUNCTION] Bidirectionally degrades single-stranded dna into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides (by similarity). ","probable exodeoxyribonuclease VII small subunit","Cytoplasm, Periplasm","","
InterPro
IPR003761
Family
Exonuclease VII, small subunit
PD028235\"[54-105]TEX7S_PASMU_Q9CNA0;
PF02609\"[53-115]TExonuc_VII_S
TIGR01280\"[51-119]TxseB: exodeoxyribonuclease VII, small subun


","BeTs to 12 clades of COG1722COG name: Exonuclease VII small subunitFunctional Class: LThe phylogenetic pattern of COG1722 is --------vdrlb-efghsnujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 6.5e-29) to 1/1 blocks of the IPB003761 family, which is described as \"Exonuclease VII, small subunit\". Interpro entry for IP:IPR003761. IPB003761 54-107 5.5e-29","Residues 52 to 119 match (3e-17) PD:PD028235 which is described as SMALL SUBUNIT VII EXONUCLEASE EXODEOXYRIBONUCLEASE NUCLEASE HYDROLASE PROTEOME COMPLETE PROBABLE ","","","","","","","","","","","Fri Jan 10 16:02:15 2003","Fri Jan 10 16:02:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02052 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 53 to 115 (E-value = 8.7e-25) place AA02052 in the Exonuc_VII_S family which is described as Exonuclease VII small subunit (PF02609)","","","","","Fujisaki,S., Hara,H., Nishimura,Y., Horiuchi,K. and Nishino,T. Cloning and nucleotide sequence of the ispA gene responsible for farnesyl diphosphate synthase activity in Escherichia coli. J. Biochem. 108 (6): 995-1000 (1990) [PubMed: 2089044].Vales,L.D., Rabin,B.A. and Chase,J.W. Subunit structure of Escherichia coli exonuclease VII . J. Biol. Chem. 257 (15): 8799-8805 (1982) [PubMed: 6284744].","","Fri Jan 10 16:02:15 2003","1","","","" "AA02053","1399068","1399961","894","ATGAGCTGGATTGATAGAATTTTTAGTAAAAATACATCTTCTTCCTCACGCAAAGCCAATGTGCCGGAAGGCGTTTGGACAAAATGTACCTCATGCGAACAAGTATTATATCGCGAGGAATTAAAACGCCATTTGGAAGTGTGTCCGAAGTGTGGTCACCACATGCGTATTGATGCCCGTGTTCGTTTATTGACCTTATTGGATCAAGACAGTGCGCAAGAATTGGCGGCGGATTTAGAACCGAAAGACATTTTAAAATTCAAAGATTTGAAAAAATATAAAGATCGTATTACCGCCGCACAAAAAGACACCAGTGAAAAAGACGCGTTAATTGCCTTTTACGGCACCTTATACAATATGCCGCTTGTGGCTGCTGCATCTAACTTTAGCTTTATGGGCGGTTCTATGGGTTCCGTGGTGGGGGCGAAATTCGTGAAAGCAGCGGAAAAAGCCATGGAAGAAAATTGCCCGTTCGTGTGTTTTTCCGCCAGTGGTGGCGCACGTATGCAGGAAGCTTTATTCTCCTTAATGCAAATGGCGAAAACCAGTGCGGTATTGGCGCAAATGCGTGAAAAAGGCGTGCCGTTCATTTCCGTGTTGACCGATCCGACGTTAGGCGGTGTGTCCGCCAGTTTCGCTATGTTGGGCGACATTAATATTGCCGAACCGAAAGCGTTAATCGGCTTCGCCGGGCCGCGCGTCATTGAACAAACCGTGCGTGAAAAACTGCCGGAAGGATTCCAACGCAGTGAATTTTTATTGGAAAAGGGCGCCATCGACATGATCGTAAAACGTGCCGATATGCGTAATACTTTGGCGAGTTTATTGAGCAAACTCATGAACAAACCTTCACCTTTCGTAGAAAGCGAATTGGTTATTGAAGAAACCGCCGCA","","","32821","MSWIDRIFSKNTSSSSRKANVPEGVWTKCTSCEQVLYREELKRHLEVCPKCGHHMRIDARVRLLTLLDQDSAQELAADLEPKDILKFKDLKKYKDRITAAQKDTSEKDALIAFYGTLYNMPLVAAASNFSFMGGSMGSVVGAKFVKAAEKAMEENCPFVCFSASGGARMQEALFSLMQMAKTSAVLAQMREKGVPFISVLTDPTLGGVSASFAMLGDINIAEPKALIGFAGPRVIEQTVREKLPEGFQRSEFLLEKGAIDMIVKRADMRNTLASLLSKLMNKPSPFVESELVIEETAA","1399961","[FUNCTION] This protein is a component of the acetyl coenzyme a carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA (by similarity). ","acetyl-CoA carboxylase carboxyltransferase, beta","Cytoplasm, Periplasm","","
InterPro
IPR000022
Domain
Carboxyl transferase
PF01039\"[123-236]TCarboxyl_trans
InterPro
IPR000438
Family
Acetyl-CoA carboxylase carboxyl transferase, beta subunit
PR01070\"[129-143]T\"[163-181]T\"[200-217]T\"[229-240]T\"[251-260]TACCCTRFRASEB
TIGR00515\"[1-285]TaccD: acetyl-CoA carboxylase, carboxyl tran
InterPro
IPR011762
Domain
Acetyl-coenzyme A carboxyltransferase, N-terminal
PS50980\"[31-258]TCOA_CT_NTER
noIPR
unintegrated
unintegrated
G3DSA:3.90.226.10\"[14-286]Tno description
PTHR22855\"[55-276]TACETYL, PROPIONYL, PYRUVATE, AND GLUTACONYL CARBOXYLASE-RELATED
PTHR22855:SF4\"[55-276]TACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE-RELATED


","BeTs to 19 clades of COG0777COG name: Acetyl-CoA carboxylase beta subunitFunctional Class: IThe phylogenetic pattern of COG0777 is ao--k-yqvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.7e-55) to 5/5 blocks of the PR01070 family, which is described as \"Acetyl-CoA carboxylase carboxyl transferase beta subunit signature\". Prints database entry for PR:PR01070. PR01070A 129-143 5.6e-11 PR01070B 163-181 2e-15 PR01070C 200-217 5.3e-13 PR01070D 229-240 1.9e-07 PR01070E 251-260 0.016","Residues 186 to 262 match (5e-08) PD:PD312146 which is described as CARBOXYLASE PYRUVATE CARBOXYLASE/PYRUVATE ACETYL-COA FUSION ","","","","","","","","","","","Fri Jan 10 16:06:01 2003","Fri Jan 10 16:06:01 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02053 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Li,S.J. and Cronan,J.E. Jr. Growth rate regulation of Escherichia coli acetyl coenzyme A carboxylase, which catalyzes the first committed step of lipid biosynthesis J. Bacteriol. 175 (2), 332-340 (1993) PubMed: 7678242 Bognar,A.L., Osborne,C. and Shane,B. Primary structure of the Escherichia coli folC gene and its folylpolyglutamate synthetase-dihydrofolate synthetase product andregulation of expression by an upstream gene. J. Biol. Chem. 262 (25): 12337-12343 (1987) [PubMed: 3040739].Nonet,M.L., Marvel,C.C. and Tolan,D.R. The hisT-purF region of the Escherichia coli K-12 chromosome. Identification of additional genes of the hisT and purF operons. J. Biol. Chem. 262 (25): 12209-12217 (1987) [PubMed: 3040734].Li,S.J. and Cronan,J.E. Jr. Growth rate regulation of Escherichia coli acetyl coenzyme A carboxylase, which catalyzes the first committed step of lipidbiosynthesis. J. Bacteriol. 175 (2): 332-340 (1993) [PubMed: 7678242].Nagano,Y., Matsuno,R. and Sasaki,Y. An essential gene of Escherichia coli that has sequence similarity to a chloroplast gene of unknown function. Mol. Gen. Genet. 228 (1-2): 62-64 (1991) [PubMed: 1886618].Li,S.J., Rock,C.O. and Cronan,J.E. Jr. The dedB (usg) open reading frame of Escherichia coli encodes a subunit of acetyl-coenzyme A carboxylase. J. Bacteriol. 174 (17): 5755-5757 (1992) [PubMed: 1355086].","","Fri Jan 10 16:06:01 2003","1","","","" "AA02056","1399987","1401330","1344","ATGCAAACAGAATTAAAAGCCACTTCGCCACTCAACGAGTGGCTTTCTTATTTGGAAAACAGTCATTTTAAAGCTATCGATTTAGGGCTGGAACGGGTGAAATCCGTCGCTCAGGCACTGGATTTATTAACGCCGGCACCTTTTGTGATTACGGTGGGCGGCACCAACGGCAAAGGCACCACCTGTCGTTTACTGGAAACGATTTTACTGAGCGCCGGTTACCGCGTGGGCGTGTATTCTTCACCGCATTTGTTACGTTATAACGAACGCGTGCGTATTCAGAATCAGGAGCTGGAAGATATGCTGCATACGGCTTCCTTCGCTTATATTGAGCAGCACAAAACCCAATCCTTAACGTATTTTGAATTCAGCACCTTGTCGGCGTTGCATTTATTTAAACAGGCAAATTTGGATGTGGTGATTTTGGAAGTAGGGCTGGGCGGTCGGCTGGATGCCACCAATATTGTGGATAACCACATGGCGGTGATTACCAGCATCGATATTGATCACACGGATTTTCTCGGTTCCACCCGTGAACAAATCGGCTTTGAAAAAGCGGGGATTTTCCGCGCTCATAAACCGGTGATTATCGGCGAGCCGAACATTCCGCAAACCATGCTGAATCACGCGAATACGCTTGGTAGCCAATTGTTTTGTCGCCATCTTGATTGGACGTTTAACCAACAAGAACAACATTGGACATGGCAAACCGTGCAACCGGAACAAAAAGTGCGGTGGGATTTTTTAGCGGATTTACCGCTTTGCCAAATTCCGTTAGCCAATGCGGCAACGGCGATCGCGGCGGTGCAAAAACTGCCTTTTGACATTTCTCTTGAAACCGTTAAAAAATCCTTAGCTGAGGTGGAACTCACCGGGCGTTTTCAAACCATCAAACCGGCACAGTTAACCCATTTGGCGCAGAAATTGCAGCGTGAAGTGACAACGTTACCGCGTATCATTATTGACGTGGGGCATAACCCGCACGCGGCGCGTTATTTAGCGGAAAAACTGACCGCACTTAAGGCACAATCTCATGGCAAACTTATTGCCGTTTGCGGCATTTTGAAAGATAAAGACGCGGTGGGGGTGTTGACGCCGTTGCTGTCCTTAATAGATGAATGGCGTTGCGTGACATTGGATGGTTATCGCGGTCAACGCGGGGCGGATTTATTTGTGACGTTGCAACAGGTTGCCGCTCAACATCGCTTAAATGTTAAAGGCGGTTATGCCGATTCTGTTGCAGAAGGCGTAAAAAGTGCGGTAGAAATTTCCGATGAAAATGATACCATACTGGTGTTTGGTTCATTTCATACGGTGGGTGAGTTTTTAACCTTTAGCCAAGCC","","","51403","MQTELKATSPLNEWLSYLENSHFKAIDLGLERVKSVAQALDLLTPAPFVITVGGTNGKGTTCRLLETILLSAGYRVGVYSSPHLLRYNERVRIQNQELEDMLHTASFAYIEQHKTQSLTYFEFSTLSALHLFKQANLDVVILEVGLGGRLDATNIVDNHMAVITSIDIDHTDFLGSTREQIGFEKAGIFRAHKPVIIGEPNIPQTMLNHANTLGSQLFCRHLDWTFNQQEQHWTWQTVQPEQKVRWDFLADLPLCQIPLANAATAIAAVQKLPFDISLETVKKSLAEVELTGRFQTIKPAQLTHLAQKLQREVTTLPRIIIDVGHNPHAARYLAEKLTALKAQSHGKLIAVCGILKDKDAVGVLTPLLSLIDEWRCVTLDGYRGQRGADLFVTLQQVAAQHRLNVKGGYADSVAEGVKSAVEISDENDTILVFGSFHTVGEFLTFSQA","1401330","[FUNCTION] Conversion of folates to polyglutamate derivatives (by similarity). ","tetrahydrofolylpolyglutamate synthase (FPGS)","Cytoplasm","","
InterPro
IPR001645
Family
Folylpolyglutamate synthetase
TIGR01499\"[30-446]TfolC: FolC bifunctional protein
PS01011\"[50-73]TFOLYLPOLYGLU_SYNT_1
PS01012\"[141-156]TFOLYLPOLYGLU_SYNT_2
InterPro
IPR013221
Domain
Mur ligase, middle region
PF08245\"[50-269]TMur_ligase_M
noIPR
unintegrated
unintegrated
G3DSA:3.40.1190.10\"[11-291]Tno description
G3DSA:3.90.190.20\"[292-445]Tno description
PTHR11136\"[36-443]TFOLYLPOLYGLUTAMATE SYNTHASE-RELATED


","BeTs to 19 clades of COG0285COG name: Folylpolyglutamate synthaseFunctional Class: HThe phylogenetic pattern of COG0285 is -o-p--yqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 2.2e-80) to 5/5 blocks of the IPB001645 family, which is described as \"Folylpolyglutamate synthetase\". Interpro entry for IP:IPR001645. IPB001645A 49-73 5.9e-14 IPB001645B 76-96 2.5e-11 IPB001645C 121-156 9.5e-24 IPB001645D 161-194 2.6e-19 IPB001645E 430-443 1.4e-06","Residues 131 to 285 match (4e-12) PD:PD212530 which is described as LIGASE COMPLETE PROTEOME SYNTHETASE CELL PEPTIDOGLYCAN SYNTHESIS ENZYME DIVISION WALL ","","","","","","","","","","","Fri Jan 10 16:08:48 2003","Tue Feb 4 17:05:17 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02056 is paralogously related to AA00841 (9e-04).","","","","","","Residues 1 to 278 (E-value = 2.7e-07) place AA02056 in the Mur_ligase family which is described as Mur ligase family, catalytic domain (PF01225)","","","","","Sheng Y, Cross JA, Shen Y, Smith CA, Bognar AL. Mutation of an essential glutamate residue in folylpolyglutamate synthetase and activation of the enzyme by pteroate binding. Arch Biochem Biophys. 2002 Jun 1;402(1):94-103. PMID: 12051687 Murata T, Bognar AL, Hayashi T, Ohnishi M, Nakayama K, Terawaki Y. Molecular analysis of the folC gene of Pseudomonas aeruginosa. Microbiol Immunol. 2000;44(11):879-86. PMID: 11145267 Bogner,A.L., Osborne,C. and Shane,B. Primary structure of the Escherichia coli folC gene and its folylpolyglutamate synthetase-dihydrofolate synthetase product and regulation of expression by an upstream gene J. Biol. Chem. 262, 12334-12343 (1987)PMID: 3040739Keshavjee K, Pyne C, Bognar AL.Characterization of a mutation affecting the function of Escherichia coli folylpolyglutamate synthetase-dihydrofolate synthetase andfurther mutations produced in vitro at the same locus.J Biol Chem. 1991 Oct 25;266(30):19925-9.PMID: 1939056 Kimlova LJ, Pyne C, Keshavjee K, Huy J, Beebakhee G, Bognar AL.Mutagenesis of the folC gene encoding folylpolyglutamate synthetase-dihydrofolate synthetase in Escherichia coli.Arch Biochem Biophys. 1991 Jan;284(1):9-16.PMID: 1989505","","Tue Feb 4 17:05:17 2003","1","","","" "AA02057","1402031","1401393","639","ATGAACAAAAATCTGACTTTTTATTTAATCCGCCACGGTCGTACCCTTTGGAACGAACAGGGTTTATTGCAAGGCTTCGGCAATTCCGCATTAACGGAAAGCGGCGTCAAAGGCGCACAGCTTACCGGCATGGCATTAAAAGACACACCTTTCGTAGCGGCTTATACCAGCTGCCTACAACGCACTATCGACACGGCGCAACATATCTTGGGCGAGCGAAATGTGCCGCTATTTCAACATTATGGTTTAAATGAACAATATTTCGGCACCTGGGAAGGCTTGCCCGTTGACGAACTACGCCATTTGGAAGAATTCCAACAAATGCGCAGCGACGCGGCAAATTACAAAGCGCAAAGCAATAACGGCGAGACCTTTGAGCAATTAGCCGAACGGGCAATGAAAGCCATACAGGATATTATTCAGGTGCATGATCAGGGAAATATTCTGATTATTTCCCACGGGCACACGCTCCGCTTGCTTTTATCTCTTTTCAACGGGGTAACCTGGCAGGAACACCGTAACGAGGGCAAAAGCCAGACCTTGCTGAATACCTCGATTAATATCGTGCGTTACCGACAAACCAACGCCGACGACGGTAAGTTTACCCTTGAAGTGATCAATGAAACGGGACATTTAAGT","","","24129","MNKNLTFYLIRHGRTLWNEQGLLQGFGNSALTESGVKGAQLTGMALKDTPFVAAYTSCLQRTIDTAQHILGERNVPLFQHYGLNEQYFGTWEGLPVDELRHLEEFQQMRSDAANYKAQSNNGETFEQLAERAMKAIQDIIQVHDQGNILIISHGHTLRLLLSLFNGVTWQEHRNEGKSQTLLNTSINIVRYRQTNADDGKFTLEVINETGHLS","1401393","","phosphoglycerate mutase","Cytoplasm","","
InterPro
IPR013078
Domain
Phosphoglycerate mutase
PF00300\"[6-160]TPGAM
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1240\"[6-212]Tno description
PIRSF001490\"[5-211]TCofactor-dependent phosphoglycerate mutase
PTHR23029\"[5-212]TPHOSPHOGLYCERATE MUTASE


","BeTs to 12 clades of COG0406COG name: Fructose-2,6-bisphosphataseFunctional Class: GThe phylogenetic pattern of COG0406 is ---p--yqvdrlbcefghs--j----Number of proteins in this genome belonging to this COG is","Significant hit ( 9.6e-24) to 4/4 blocks of the IPB001345 family, which is described as \"Phosphoglycerate mutase family\". Interpro entry for IP:IPR001345. IPB001345A 7-36 6.1e-08 IPB001345B 54-66 0.001 IPB001345C 75-106 6.6e-05 IPB001345D 120-138 0.06","Residues 8 to 164 match (2e-43) PD:PD002638 which is described as PROTEOME COMPLETE PHOSPHOGLYCERATE MUTASE PGAM ISOMERASE KINASE GLYCOLYSIS BPG-DEPENDENT PHOSPHOGLYCEROMUTASE ","","","","","","","","","","","","Fri Jan 10 16:14:01 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02057 is paralogously related to AA00942 (1e-11) and AA00453 (6e-10).","","","","","","Residues 5 to 200 (E-value = 8.7e-30) place AA02057 in the PGAM family which is described as Phosphoglycerate mutase family (PF00300)","","","","","Rigden DJ, Littlejohn JE, Henderson K, Jedrzejas MJ.Structures of Phosphate and Trivanadate Complexes of Bacillus stearothermophilus Phosphatase PhoE: Structural and FunctionalAnalysis in the Cofactor-dependent Phosphoglycerate Mutase Superfamily.J Mol Biol. 2003 Jan 17;325(3):411-20.PMID: 12498792Jedrzejas MJ.The structure and function of novel proteins of Bacillus anthracis and other spore-forming bacteria: development of novelprophylactic and therapeutic agents.Crit Rev Biochem Mol Biol. 2002;37(5):339-73.PMID: 12449428van der Oost J, Huynen MA, Verhees CH.Molecular characterization of phosphoglycerate mutase in archaea.FEMS Microbiol Lett. 2002 Jun 18;212(1):111-20.PMID: 12076796","","Wed Jan 29 13:27:40 2003","1","","","" "AA02060","1403550","1402096","1455","ATGAATATTGAACAAATTACCGCCTATATTATCCCGGTATTGATCTGGATTCTGACCATTGCCATTACCATTCGTCTGGTGATCAAAAAGCAATCGGTGTCTGCTATGCTGTCTTGGTTGATGGTGATTTATGTGTTTCCCATCGTAGGCATTGTGGCGTATTTGATTTTCGGTGAAATCAATCTCGGGAAGCGCCGGGCCGCACTGTTTAATCAACTGAAACCGAAGTTTATGGCATGGTTTGAGAAGCTGTCGCAGTGCGATAATTTGGTGAATACCCAAACCAATCTACTCTATCGTCCGATTTTCGATTTAGCCAAACAACGCCTCGGCATTCCTTGCGTGCTGGGCAACGAACTGCATATTTTAGATACGCCGGAAAGTATCATGCGCAGCATTATCGAGGACATCAAAGGCGCTGAAAAATCCATCAATATGGTGTTCTATATTTGGTCTGCGAAAGGCTTGGTTGATGAGGTGATGGAAGCCCTTATCGCCGCCCGTCAACGCGGTGTGGAAATTCGTATTTTGCTGGATTCCGTGGGCAGCCGTCCGTTCTTAAAAAGCCAAGATTGCCGTCTCATGCAGGAACAAGGCATTGAAATCACCGAAACCCTGCATGTGAATTTGTTCCGTATGTTCTTCAGCCGCATAGACTTGCGCCAACACCGTAAAATTATCGTGATCGATAACCAAATTGCCTACACCGGCAGCATGAACATGGTGGATCCGAAGTTCTTCAAAAAAGACAGCAATGTGGGCGAATGGATTGACATTATGGTGCGTATTAACGGCCCTGTGTCGGCAGTGCTTAACGGCCTACATGCTTGGGATTGGGAGATTGAAACCGGGCAATCCGTCCCGCTGCATATTCCTGACAGCCCGTTGTTACCGCTGGAACAAAATAACTCGCACGCCGTGCAAATTCTCGCCACCGGTCCGAGTTTCCCCGATGATTTAATGGCGCAATCTCTTGCCATTGCGATTTTCTCCGCGCGTAAAAGCATTGTGATCACCTCGCCTTATTTCGTGCCGAGCCACAACATTGCCGAAGCCTTACGCATTGCGGCTCTGCGTGGCGTGGAGGTGTCCATTATTCTGCCGAAAGAAAACGATTCCATGATGGTACGCTGGGCAAGTCGTACCTTTTTTGATGATTTACTTGCCGCCGGCGTAAAAATTTATAATTTCAAGAAAGGGTTATTGCACACTAAAAGTATGCTCATTGATAACAAGCTCGCTTTGGTCGGCACCGTTAACATGGATATGCGCAGCTTTTTATTGAATTTTGAAGTGACTATGGTGGTGGAAGATCCGGCGTTCGCCAATGAAATTTCCTTGCTCCACGAAGGTTACATCAACAATTCAGAATTACCTGATCATGCCAAGTGGGCAAATCGTTCCGTTTATCAACGCATTATCGAAAAATTGTTTTTCCTCTTCAGCCCGCTGTTG","","","55092","MNIEQITAYIIPVLIWILTIAITIRLVIKKQSVSAMLSWLMVIYVFPIVGIVAYLIFGEINLGKRRAALFNQLKPKFMAWFEKLSQCDNLVNTQTNLLYRPIFDLAKQRLGIPCVLGNELHILDTPESIMRSIIEDIKGAEKSINMVFYIWSAKGLVDEVMEALIAARQRGVEIRILLDSVGSRPFLKSQDCRLMQEQGIEITETLHVNLFRMFFSRIDLRQHRKIIVIDNQIAYTGSMNMVDPKFFKKDSNVGEWIDIMVRINGPVSAVLNGLHAWDWEIETGQSVPLHIPDSPLLPLEQNNSHAVQILATGPSFPDDLMAQSLAIAIFSARKSIVITSPYFVPSHNIAEALRIAALRGVEVSIILPKENDSMMVRWASRTFFDDLLAAGVKIYNFKKGLLHTKSMLIDNKLALVGTVNMDMRSFLLNFEVTMVVEDPAFANEISLLHEGYINNSELPDHAKWANRSVYQRIIEKLFFLFSPLL","1402096","[FUNCTION] Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. Affects resistance to the gyrase inhibitor novobiocin.[CATALYTIC ACTIVITY] 2 Phosphatidylglycerol = diphosphatidylglycerol + glycerol.[SUBUNIT] Monomer.[SUBCELLULAR LOCATION] Membrane-bound.","cardiolipin synthase","Inner membrane, Cytoplasm","","
InterPro
IPR001736
Domain
Phospholipase D/Transphosphatidylase
PF00614\"[218-245]T\"[398-425]TPLDc
SM00155\"[218-245]T\"[398-425]TPLDc
PS50035\"[218-245]T\"[398-425]TPLD
noIPR
unintegrated
unintegrated
G3DSA:3.30.870.10\"[126-258]T\"[318-463]Tno description
PIRSF006046\"[1-485]TCardiolipin synthase
PTHR21248\"[256-473]TPHOSPHOLIPASE D ENDONUCLEASE SUPERFAMILY
signalp\"[1-21]?signal-peptide
tmhmm\"[10-28]?\"[37-57]?transmembrane_regions


","BeTs to 13 clades of COG1502COG name: Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthases and related enzymesFunctional Class: IThe phylogenetic pattern of COG1502 is a--p--y-v--lbcefghsnujxi-wNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.9e-06) to 1/2 blocks of the IPB001736 family, which is described as \"Phospholipase D/Transphosphatidylase\". Interpro entry for IP:IPR001736. IPB001736B 403-422 1.9e-06 IPB001736B 223-242 1.1e-05","Residues 329 to 438 match (1e-27) PD:PD186377 which is described as ENDONUCLEASE PROTEOME COMPLETE D PHOSPHOLIPASE SUPERFAMILY CARDIOLIPIN SYNTHASE PROBABLE TRANSMEMBRANE ","","","","","","","","","","","Mon Jan 13 09:48:55 2003","Mon Jan 13 09:48:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02060 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 398 to 425 (E-value = 1.2e-07) place AA02060 in the PLDc family which is described as Phospholipase D. Active site motif (PF00614)","","","","","Milkman,R. An Escherichia coli homologue of eukaryotic potassium channel proteins. Proc. Natl. Acad. Sci. U.S.A. 91 (9): 3510-3514 (1994) [PubMed: 8170937].Ivanisevic,R., Milic,M., Ajdic,D., Rakonjac,J. and Savic,D.J. Nucleotide sequence, mutational analysis, transcriptional start site, and product analysis of nov, the gene which affects Escherichia coli K-12 resistance to the gyrase inhibitor novobiocin. J. Bacteriol. 177 (7): 1766-1771 (1995) [PubMed: 7896699].Tropp,B.E., Ragolia,L., Xia,W., Dowhan,W., Milkman,R., Rudd,K.E., Ivanisevic,R. and Savic,D.J. Identity of the Escherichia coli cls and nov genes . J. Bacteriol. 177 (17): 5155-5157 (1995) [PubMed: 7665497].Hiraoka,S., Nukui,K., Uetake,N., Ohta,A. and Shibuya,I.Amplification and substantial purification of cardiolipin synthase of Escherichia coli. J. Biochem. 110 (3): 443-449 (1991) [PubMed: 1663113].Tropp,B.E. Cardiolipin synthase from Escherichia coli . Biochim. Biophys. Acta 1348 (1-2): 192-200 (1997) [PubMed: 9370333].","","Mon Jan 13 09:48:55 2003","1","","","" "AA02062","1404472","1403567","906","GTGTACGAAGGTTTGCTCATTATTTTAGTGCCGATGTTTGTCGGCTACATGGTTAAAACGAAAAATCAGATGATTTTGCACGCATTGGGGCGATTAACCATGGTTCTGCTTTACATGATCTTGTTCTCCATGGGCTTTTCTCTCGGTCAACTGAATGATTTGGCACAACAATTACCGCAAATCGGCGTTTATGCCCTAACCTTTATTTTATTGACGCAAGGGTTTAATTTTATCGGCTTGTTGGTTTACGACAAACTTCACCCGCAACCCCTAAAACACAATGCGGAAAAAATGCCTTCCCGCTGGCATATTTTGCCGGATTCCTTGAAATTATGTGCCGTTGTGGCAATCGGTTTTGTCGCCGGTTGGTTGGCGAAAGGACATTTTGCCCTCTCCCACAACACGACGACTTATGTGCTGGTTGTGATGATTTTCTGTGTGGGCGTACAACTGCGCAATAACGGGATTTCCATGCGGGCGGTGTTTTTCAACAAACGGGGCTTGGCAATGGGCGGCATTTTTATCCTGACCTCTTTGCTGGGTGGCATTGTCGGTGCGCAGGTATTGTCCATGCCGATGGTACAAGGTTTAGCGGTGTCTTCCGGCTTCGGCTGGTATTCTTTATCCAGCGTGACCCTAAGCAATGCCTGGGGACCGGTTTGGGGCAGTATTGCGTTTTTTAATGATTTATCCCGTGAACTGATTAGCTTATTTATTATCCCATTATTTATGCAAAACTATCGTTCTACGGCGGTAGGCTTTGCCGGCGCCACGGCACTGGATGTCACCCTGCCGATTATCCAAAAAGCGGGCGGCATGGAAGTGTTACCGCTGGCGTTTAGTTTTGGCTTTATTGCCAACATTACGCCCCCGATTTTATTGATGTTATTTACCTCGGCCCCTTTA","","","32928","VYEGLLIILVPMFVGYMVKTKNQMILHALGRLTMVLLYMILFSMGFSLGQLNDLAQQLPQIGVYALTFILLTQGFNFIGLLVYDKLHPQPLKHNAEKMPSRWHILPDSLKLCAVVAIGFVAGWLAKGHFALSHNTTTYVLVVMIFCVGVQLRNNGISMRAVFFNKRGLAMGGIFILTSLLGGIVGAQVLSMPMVQGLAVSSGFGWYSLSSVTLSNAWGPVWGSIAFFNDLSRELISLFIIPLFMQNYRSTAVGFAGATALDVTLPIIQKAGGMEVLPLAFSFGFIANITPPILLMLFTSAPL","1403567","","conserved hypothetical protein (probable membrane protein)","Inner membrane, Extracellular","","
InterPro
IPR005642
Family
Protein of unknown function DUF340, prokaryotic membrane
PD022789\"[204-294]TQ9CNG6_PASMU_Q9CNG6;
PF03956\"[109-299]TDUF340
noIPR
unintegrated
unintegrated
signalp\"[1-45]?signal-peptide
tmhmm\"[24-42]?\"[61-83]?\"[107-125]?\"[131-151]?\"[166-186]?\"[192-212]?\"[221-241]?\"[247-267]?\"[277-297]?transmembrane_regions


","BeTs to 6 clades of COG2431COG name: Uncharacterized membrane proteinFunctional Class: SThe phylogenetic pattern of COG2431 is ----kz--------e-gh-n------Number of proteins in this genome belonging to this COG is","","Residues 1 to 88 match (5e-15) PD:PD354883 which is described as PROTEOME COMPLETE MEMBRANE VC1151 SURFACE TRANSMEMBRANE INNER PM0465 YBJE ","","","","","","","","","","","","Fri Jan 31 14:42:43 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02062 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 109 to 299 (E-value = 8.9e-100) place AA02062 in the DUF340 family which is described as Membrane protein of unknown function (DUF340) (PF03956)","","","","","","","","1","","","" "AA02063","1404591","1405277","687","TTGATTTTCTCCATGACGTTTCAAATTGTATTTCAACATCCTGATTTTATCGTGATTAACAAACCGAACGGTATCAGCGTACACAAAGACGATGCCGACATCGGCTTAACCCGACTGGTGGCGCAACAGCTTGGCGTGCCGCAGGTTTGGCTGGTTCATCGGCTGGATAAAGTGACCTCGGGGTTATTAATGTTAGCATTAAATGAACAGGCTGCAGTGACGTTGTCACAAAAGTTTGCATATCATCAAATTCAGAAAACTTACCTCGCACTGGCAGCTCACAAACCAAAGAAAAAGCAGGGGAGAATCAGCGGTGATATGCAAAAAGCGCGCCGAGGTGCTTGGAAACTGACCCAAAGCAAAGAAAATCCTGCCGTGACAGATTTTGTGTCCCATAGTCTCGCACCAAATTTGCGCTTATTTATTCTGCAACCGAAAACCGACAAAACCCATCAGCTCCGTGTCGCTATGAAAAGTTTAGGCAGTCCGATTTTAGGCGATGCTTTGTATGGCGGCGATAGCGCCGATCGCACCTATCTGCACGCTTATCAATTATCGTTTGACTATTTCGGACAGGCGGTTCAAATTAAAGGGGAACCGCTCAAAGACGAAAAGTGCGGTGATTTTTTTCAGCGTTTTTGGGCAGACATCGAAAAACACGTCAATGCCGACGCCGAAAAAACACCT","","","25740","LIFSMTFQIVFQHPDFIVINKPNGISVHKDDADIGLTRLVAQQLGVPQVWLVHRLDKVTSGLLMLALNEQAAVTLSQKFAYHQIQKTYLALAAHKPKKKQGRISGDMQKARRGAWKLTQSKENPAVTDFVSHSLAPNLRLFILQPKTDKTHQLRVAMKSLGSPILGDALYGGDSADRTYLHAYQLSFDYFGQAVQIKGEPLKDEKCGDFFQRFWADIEKHVNADAEKTP","1405277","","23S rRNA psedouridine synthase, Rlu family protein","Periplasm, Cytoplasm","","
InterPro
IPR006145
Domain
Pseudouridine synthase
PD001819\"[52-91]TQ9CN15_PASMU_Q9CN15;
PF00849\"[15-159]TPseudoU_synth_2
InterPro
IPR006224
Family
Pseudouridine synthase, Rlu
PS01129\"[52-66]TPSI_RLU
InterPro
IPR006508
Family
Pseudouridine synthase RluA-like
TIGR01621\"[6-223]TRluA-like: pseudouridine synthase Rlu famil
noIPR
unintegrated
unintegrated
PTHR10436\"[2-189]TRIBOSOMAL PSEUDOURIDINE SYNTHASE


","No hits to the COGs database.","Significant hit ( 4.1e-46) to 4/4 blocks of the IPB000613 family, which is described as \"Pseudouridine synthase\". Interpro entry for IP:IPR000613. IPB000613A 9-29 4.2e-10 IPB000613B 52-91 1.1e-18 IPB000613C 147-171 3.3e-10 IPB000613D 177-190 0.013Significant hit ( 2e-42) to 3/3 blocks of the IPB002990 family, which is described as \"Pseudouridine synthase, Rlu family\". Interpro entry for IP:IPR002990. IPB002990A 9-29 1.4e-09 IPB002990B 52-90 1.8e-18 IPB002990C 147-171 1.6e-11","Residues 10 to 91 match (9e-08) PD:PD483014 which is described as SYNTHASE PROTEOME COMPLETE PSEUDOURIDINE LARGE RIBOSOMAL SUBUNIT C LYASE PSEUDOURIDYLATE ","","","","","","","","","","","","Fri Jan 31 15:43:53 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02063 is paralogously related to AA02913 (2e-17), AA02276 (4e-17), AA01355 (3e-13) and AA00513 (8e-13).","","","","","","Residues 15 to 159 (E-value = 1.6e-36) place AA02063 in the PseudoU_synth_2 family which is described as RNA pseudouridylate synthase (PF00849)","","","","","Corollo D, Blair-Johnson M, Conrad J, Fiedler T, Sun D, Wang L, Ofengand J, Fenna R.Crystallization and characterization of a fragment of pseudouridine synthase RluC from Escherichia coli.Acta Crystallogr D Biol Crystallogr. 1999 Jan;55 ( Pt 1):302-4.PMID: 10089432 Conrad J, Sun D, Englund N, Ofengand J.The rluC gene of Escherichia coli codes for a pseudouridine synthase that is solely responsible for synthesis of pseudouridine at positions 955, 2504, and 2580 in 23 S ribosomal RNA.J Biol Chem. 1998 Jul 17;273(29):18562-6.PMID: 966082","","Fri Jan 31 15:43:53 2003","1","","","" "AA02066","1405374","1405255","120","ATGCAAATAATGGCTTTTTGGTATGACGTTGTTTTGATTTTCGTCTGCATAACGGGCTTCCTTGGGTTTTATCGCCGAAAAGTGCGGTCAGATTTTAAGGTGTTTTTTCGGCGTCGGCAT","","","5032","MQIMAFWYDVVLIFVCITGFLGFYRRKVRSDFKVFFRRRH","1405255","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide
tmhmm\"[4-24]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 16:31:36 2004","Wed Feb 25 16:31:36 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02066 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 16:31:36 2004","","","","","","","","","","","","","1","","","" "AA02067","1405373","1406185","813","ATGATCTTTGCCTACATTAGCATTGCCTTGATGGGCGTGTTCGTCAAATACGCTTCCGACGAATTGCCTTCCAGTGAAATCCTATTTTCTCGCTTTCTTATCGGCTTCATTTTTTTATTGCCCTTTATGATTCGCGACGGCGATTTCAAAGTGGAACTGAGTCAATGGCCGTTTCTCGTCATGCGTAATCTTGCCGGCATCGCCAGTATGTTGCTGACTTTTTACGCCATCAAATATTTGCCGATTTCCATCGCCGTTTTATTGATGAACACCTCGGCGTTATTCGTGCCGTTATTATTGTTTGTGTTACGCACCCGAACTCCGCTGAAAGTATTGGCGTGCAGTTTCCTTGGTTTTGCGGGCGTTTCCATTATCATGTTGACGGATTCCTCCAAACATTTTGAACTCTTACATATCGGCTATGCACTGGGCGCGGCATTCTTAGCCGCCATGGCGTTTATCAGCTTGCAGGAGCTCAACAAACACAACTCACCGAAAAACATCGTGTTCTACTTCCATTTATTAGGCTCCCTGTTGCTGCCGTTATTTTTCGCCGCACAATGGGAAATTCCTACGGCTCACGGCTTTCTTTTATTGCTCTTAGTGGGCGGTTTCGGCTTAATCTTCCAATTATTGCTCACCCGCGCCTTTAAATACGCCCCGGCGAACGTCATCACCCCGTTTGCTTTCACCGGCGTGATTTTTTCCAGCATTTGCGACTGGCTGTTCTGGCACAACGTGCCGACGCTCAATTTCTGGATCGGCTCATTCGTTATTATCCTGTCCGTCAGTTTATTGGCGAAAATGCGCCGT","","","32281","MIFAYISIALMGVFVKYASDELPSSEILFSRFLIGFIFLLPFMIRDGDFKVELSQWPFLVMRNLAGIASMLLTFYAIKYLPISIAVLLMNTSALFVPLLLFVLRTRTPLKVLACSFLGFAGVSIIMLTDSSKHFELLHIGYALGAAFLAAMAFISLQELNKHNSPKNIVFYFHLLGSLLLPLFFAAQWEIPTAHGFLLLLLVGGFGLIFQLLLTRAFKYAPANVITPFAFTGVIFSSICDWLFWHNVPTLNFWIGSFVIILSVSLLAKMRR","1406185","","conserved hypothetical protein; possible membrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR000620
Domain
Protein of unknown function DUF6, transmembrane
PF00892\"[6-127]T\"[147-268]TDUF6
noIPR
unintegrated
unintegrated
PTHR22911\"[20-271]TACYL-MALONYL CONDENSING ENZYME-RELATED
signalp\"[1-18]?signal-peptide
tmhmm\"[24-44]?\"[59-77]?\"[81-103]?\"[108-128]?\"[138-156]?\"[168-188]?\"[194-214]?\"[224-244]?\"[250-268]?transmembrane_regions


","BeTs to 16 clades of COG0697COG name: Permeases of the drug/metabolite transporter (DMT) superfamilyFunctional Class: G,E,RThe phylogenetic pattern of COG0697 is aompkzyqvd-lbcefghsnujxit-Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Mon Jan 13 10:10:43 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02067 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 147 to 268 (E-value = 1.6e-13) place AA02067 in the DUF6 family which is described as Integral membrane protein DUF6 (PF00892)","","","","","","","","1","","","" "AA02069","1406271","1406591","321","ATGGAATACCCAAGTTGCCTATCTTGCAAAGGCGAAAACACCTACCACGATTCAATCCAATTCGTCTGCCCCGATTGCGGATACGAATGGACTGGCAACGAAACCGAAGAACAGGATGATGATCAGCTTATCGTTAAGGACAGCAACGGCAACTTACTCGCCGACGGTGACGACGTGCTGCTCATCAAAGACTTAAAACTCAAAGGCTCTTCCGAGGTGTTAAAGAAAGGCACCAAATTCAAAAACATCCGCCTCACCCACGGCGACCACAATGTCGATTGTGGCAAAATTATGTTGAAATCGGAGTTTTTGAAGAAGGCG","","","11998","MEYPSCLSCKGENTYHDSIQFVCPDCGYEWTGNETEEQDDDQLIVKDSNGNLLADGDDVLLIKDLKLKGSSEVLKKGTKFKNIRLTHGDHNVDCGKIMLKSEFLKKA","1406591","","alkylphosphonate uptake protein","Cytoplasm","","
InterPro
IPR004624
Family
PhnA protein
TIGR00686\"[2-107]TphnA: alkylphosphonate utilization operon p
InterPro
IPR013987
Domain
PhnA protein, N-terminal
PF08274\"[2-31]TPhnA_Zn_Ribbon
InterPro
IPR013988
Domain
PhnA protein, C-terminal
PF03831\"[44-95]TPhnA


","No hits to the COGs database.","Significant hit ( 3.4e-06) to 1/1 blocks of the IPB001222 family, which is described as \"TFIIS zinc ribbon domain\". Interpro entry for IP:IPR001222. IPB001222 6-42 3.2e-06","","","","","","","","","","","","","Mon Jan 13 10:13:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02069 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 44 to 95 (E-value = 7.7e-30) place AA02069 in the PhnA family which is described as PhnA protein (PF03831)","","","","","Chen,C.M., Ye,Q.Z., Zhu,Z.M., Wanner,B.L. and Walsh,C.T. Molecular biology of carbon-phosphorus bond cleavage. Cloning and sequencing of the phn (psiD) genes involved in alkylphosphonate uptake and C-P lyase activity in Escherichia coli B. J. Biol. Chem. 265(8):4461-4471,1990. PubMed: 2155230.","","Fri Feb 7 13:25:53 2003","1","","","" "AA02070","1407544","1406648","897","GTGTTTGAATTAACTACAGAGAAAGGTGAAACTTTTTCTGTTGATGTAAACTTTCTTTTAAATTTTGATTCTGAAGATGATTATTATAAGGCGAGAGCATTTAACAGCTACTTAAATAACTTTACTTTTTTTTATGGTTTAAATGAATGGGGTAAAGTAATTTTACAGCATTTCACTGAATATCAGATAAATAATGACACATTAGAAGAGCTAATAAAAAAAGATTTAATATCAGATGAAAAACTTAAAGAAGAAAAAGAATTCGATGATATATTAACTGAGTTTCACAGCTTAAAAACAAAACCTGATTTCATTAATAGACTATATGATATAACTATAAAGCAAGCCAAAAGAATGAGGTTAGGAAATATATACTTTTCTTACAAAATAATTAACTATGAAGACGCTGAATTAGCTAATAATTTAGAGAAAGAAGTCAAAGAGATAATTGATTCTTTCTTAAAAAATAATTTTACTTATGATTTAAAGTTACGTAATTTTTTCCCTTTTGGAGAAAGTGATGATATTTTTGCAAAATTTCTTGAAGAGAAAATTGAAGAATACAAAAAAACGCCCAAGTCTCAAGATATCTTAACCCCATTTCTTAGATATTTTGAAGATAGGAGTTATCTGTATGAAAACCTAAACTTAGATTCTATTTCAAAGGAACAATTAAAAGAGATAATTTGGATAGATATTAATGACAAACAATATCGAAGACAGTTTATAGCTTCCGTAGTACACCATCCTGCATTTTCTGAAAATAAGCGAGAAGAAATTCGTCAATGGACCGTAGATATTCTCCGAGAAGAAGCTACTGATAATCCTGATAGTAAAGCAGTTATTGAAATGTGGTTAAATGACACTAATGAACTAAAAGATTTAAAAAAATATCTG","","","36791","VFELTTEKGETFSVDVNFLLNFDSEDDYYKARAFNSYLNNFTFFYGLNEWGKVILQHFTEYQINNDTLEELIKKDLISDEKLKEEKEFDDILTEFHSLKTKPDFINRLYDITIKQAKRMRLGNIYFSYKIINYEDAELANNLEKEVKEIIDSFLKNNFTYDLKLRNFFPFGESDDIFAKFLEEKIEEYKKTPKSQDILTPFLRYFEDRSYLYENLNLDSISKEQLKEIIWIDINDKQYRRQFIASVVHHPAFSENKREEIRQWTVDILREEATDNPDSKAVIEMWLNDTNELKDLKKYL","1406648","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Jan 13 10:14:53 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02070 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02071","1408341","1407613","729","ATGGCAACTACTGAAAAAATTGAAGAAAAATTATTAAACCTTATCAATCAAGCAGACTCTTTTGCTACTGCACTTACAGGTGAATGGGGAATTGGTAAAACGCATTTCTGGAAGAATTTCTATGAAAAGAATCATAATAATTTCAAAATGAATAAGTATTCTTATGTTTCGTTATTTGGTATTGATTCCTTAGAATCATTTAAATATCAAATTGCTATAAACACTCATGATACAAAGCAGAAAAAAGATTATTTATTACATATAAAGAAAGCATTTTCATCTATTATAAGTAACATTGACTTCCCAAAACTAGAAGCCAAAGGTTTTAGTCTTTCAGTTACTCAAAGTATGATAAACAGCATAATATCAAACTTTATTGAAGATACTGTCATTTGTATTGATGATTTTGAGAGAAAATCAGATAAATTAGACACAAGAGAAATCATGGGTCTCATTAATTTTCTAAAAGAGGAAAAGAAATGTAAAATTATAATGATTTTACATGAAGATAAATCTAAGGATCTAGAAGTATTCAGGGAATATAAAGAAAAAGTATTTGATGATGTCTTAATATTAGATGAAAACATATCAATCATCAGAAAACTAATTAATAACAACGAAAATTTTGATATATATGAAAATTTCTACAATATTTTAAAATATAAAAATTTAAGATTTTATATAAAAGTAGATAAGGATTACAGAAACATAACTTCTTTAAATAAAATT","","","28787","MATTEKIEEKLLNLINQADSFATALTGEWGIGKTHFWKNFYEKNHNNFKMNKYSYVSLFGIDSLESFKYQIAINTHDTKQKKDYLLHIKKAFSSIISNIDFPKLEAKGFSLSVTQSMINSIISNFIEDTVICIDDFERKSDKLDTREIMGLINFLKEEKKCKIIMILHEDKSKDLEVFREYKEKVFDDVLILDENISIIRKLINNNENFDIYENFYNILKYKNLRFYIKVDKDYRNITSLNKI","1407613","","conserved hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","Residues 5 to 234 match (6e-07) PD:PD144654 which is described as PROTEOME COMPLETE SLR1135 ","","","","","","","","","","","","Fri Jan 31 14:33:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02071 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02072","1408741","1409163","423","ATGATCCGAGAGTGGCTAGAACTGAAAGACCTTTTGGGAGTAGCTGGACTACCAGAAACTGTTCAAGGGGTAACTAAAAAAGCCAAATTAGAAAACTGGGAAAGACGACTTATAAAAGGAAGAAAAGGGAAAACATACGAATACCATTATTTATCCATGCCTTACGAGGTGCAGCGCGCCCTAGGCTTTAAACGCAATATAATAGAAGAGCCTACCGCACAATATAACGCATCAAAAGAAGACTTAACGGAAGTAAGCAAGGCGCGCTTTTTAACGGCGATCAGCACACTTGAAGAAATCTTAGCAATGACACGCAAAACCATGGAGCCAGAAGCCAAGGCGCAAATGGTATGGATGATTTATGAATTACTAAGCGAAGAAAGCGCTAACGAGAAGATTATTAATTTAGTTAAATTGGTTGCA","","","16320","MIREWLELKDLLGVAGLPETVQGVTKKAKLENWERRLIKGRKGKTYEYHYLSMPYEVQRALGFKRNIIEEPTAQYNASKEDLTEVSKARFLTAISTLEEILAMTRKTMEPEAKAQMVWMIYELLSEESANEKIINLVKLVA","1409163","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003314
Domain
Transposase MuA/Repressor CI, DNA-binding
PF02316\"[9-140]TMu_DNA_bind
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[2-69]Tno description


","No hits to the COGs database.","Significant hit ( 1.4e-11) to 2/6 blocks of the IPB003314 family, which is described as \"Mu DNA-binding domain\". Interpro entry for IP:IPR003314. IPB003314A 16-40 1e-05 IPB003314B 43-56 0.00047","Residues 3 to 61 match (8e-07) PD:PD016666 which is described as DNA DNA-BINDING TRANSPOSASE REPRESSOR ELEMENT REGULATION RECOMBINATION CI INTEGRATION EXCISION ","","","","","","","","","","","","Mon Jan 13 10:26:47 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02072 is paralogously related to AA02149 (3e-60) and AA01765 (3e-07).","","","","","","Residues 9 to 140 (E-value = 9.6e-06) place AA02072 in the Mu_DNA_bind family which is described as Mu DNA-binding domain (PF02316)","","","","","","","","1","","","" "AA02074","1409716","1409480","237","GTGCGGTTGATTTTCACCGCACTTAAAAATCATATAAACATCAAGTCAATATCACTTGAAAATGTAACTCGTTTTACTAAAATTTACATATTATTTTCATTTTATGGATGTAAAACACCGAACAAAATGAGAAAAAGGAATAAACTAGGGAGAATGTTGAATCAAGCGGGAATAAGTGGAACAAAACCAATGAAAACAAGGGCGCAAGAAAAAACGGCGTCCTTTTTTATTGAAGAA","","","9153","VRLIFTALKNHINIKSISLENVTRFTKIYILFSFYGCKTPNKMRKRNKLGRMLNQAGISGTKPMKTRAQEKTASFFIEE","1409480","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Jan 13 10:28:26 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02074 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02075","1409794","1410039","246","ATGCACACAAAAACATGGTTGGCTTCTTTGGTGGGGTTGGTGATTTCAGGAACGGTGTGGGCGAATCCGCCGCAGGCGCAGGCACCTTATTTTAATAAAACGGGTAACGGCTATGATTTGCAATTCTCGCCGAAAACCTACCGCACTTTGGAGGCGAAGGTGAACGGGGAAACCGTGAAATTCCGTGCTTTTGAGAAGATTGTGTATGTGCAGCAGCCGCTTGAACCGGATTATCAAACGCTGATT","","","9289","MHTKTWLASLVGLVISGTVWANPPQAQAPYFNKTGNGYDLQFSPKTYRTLEAKVNGETVKFRAFEKIVYVQQPLEPDYQTLI","1410039","","conserved hypothetical protein","Periplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Fri Jan 31 14:36:48 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02075 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02076","1410066","1411154","1089","GTGGCGAGTGTGGGCGCACGCGGGCGGACGCTGGAGAAAGACGGAAAATATACCGGCAAGGCGCCGGCGGCGATTATCGATTTGAAATCGGCGGTGCGTTATTTGCATTTTAATGATGAGGTGATGCCGGGCGATGCCAATAAAATTATTTCTAATGGCACCAGTGCCGGCGGGGCGTTGTCCGCCTTGTTAGGGGCGAGCGGCGATAATCCGGATTATGCCCATTATTTAAAACACGCGGGCGCGGCAGAAGCGAGTGATGCAATTTTTGCGGTTTCTGCCTATTGTCCGATTACCAATTTGGAGCACGCCGATAGCGCTTATGAATGGGAGTTTAACGGTTTAAACGAATATCGCCGTATGGATATGAGTCGTTTAAATGCGGACAGTTATAACGATCGTTCTCAAGCAGCGGCAAAAGCGACCATTGACGGCACGTTGACGGCGCAGGAAATTACGCTGTCCGATCAGCTAAAAGCCGAATTTCCCGCCTATTTAAATAGTTTGAAATTGAAAGACGAAAAAGGCAATGGGTTAACGTTAGACGCGCAAGGCAACGGTTCTTTTAAGGATTATGTGAAATCGGTGATTATACGGGCAGCGGATAAGGCGCATAAAAACGGCACCTCTTTTGCCGATCAGCCTTGGGTGAACGTCAGCAAAGAAGGTGTTACCGACATTGATTGGGACGGTTATATTCACGCGGAAAAACGAATGAAATCGCCACCGGCATTTGATGCGCTGAATTTGAGTTCGGACGAAAATAATTTATTTGGTACGGAAACCGTGAATAATCAGCATTTCACCGTTTTTTCTTGGCAACACAGCACGGAAAAGGGAAAGATGGCGGATAAAAATGTGGTGCGCTTAATGAACGCCATGAATTATGTGGATCAAAGTAAAACGCAGCATTGGCGCACTCGGGTCGGCACCTCCGACCGTGATACTTCGCACGCTATTGGTGCTATGTTAGCTATAAAATTGCGTATGGCGGGTAAGCAGGTGGATTATGAAACGCCATGGGGCGTGCCGCATGCGGGGGATTATGATTTGGATGAGTTGTTTCAGTGGGTGGATAGTATTAGCAAA","","","40749","VASVGARGRTLEKDGKYTGKAPAAIIDLKSAVRYLHFNDEVMPGDANKIISNGTSAGGALSALLGASGDNPDYAHYLKHAGAAEASDAIFAVSAYCPITNLEHADSAYEWEFNGLNEYRRMDMSRLNADSYNDRSQAAAKATIDGTLTAQEITLSDQLKAEFPAYLNSLKLKDEKGNGLTLDAQGNGSFKDYVKSVIIRAADKAHKNGTSFADQPWVNVSKEGVTDIDWDGYIHAEKRMKSPPAFDALNLSSDENNLFGTETVNNQHFTVFSWQHSTEKGKMADKNVVRLMNAMNYVDQSKTQHWRTRVGTSDRDTSHAIGAMLAIKLRMAGKQVDYETPWGVPHAGDYDLDELFQWVDSISK","1411154","","conserved hypothetical protein","Extracellular","","
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1820\"[22-346]Tno description


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Jan 13 10:30:22 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02076 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02077","1412768","1411434","1335","GTGGCAACAACCCTCACGGGCTGTGCCAATATTGGCGATTCTTATCGGGCCAGCCTTAAGAACTACAAACAATATGAAGAAATCACCAAACAATACAATATTAAGAATGATTGGTGGAAGCTTTATAAAGATGCCCAGTTAAATCGTGTGGTCGAAAAAGCCCTATTGAATAATAAAGATTTAGCTAAAGCCACAATTTCCGTTAATCGCGCCCTTTATAGTGCGAACCTTGCCGGTGCGAATTTAGTTCCTGCATTCAGCGGTTCCACCCGCTCCACAGCACAAAAGAATATAAAAACCGGCGGCAACTCAACGATCAGCCATACAGGTTCTTTAAATGTCAGCTATACCTTAGATTTATGGTTCCGCTTAGCAGATACCGCAGACGCGGCAGAATGGGCACATAAAGCTACGGTCCAGGATATGGAATCCACTAAGCTTTCCTTAATTAATTCTGTGGTTACCACCTATTACCAAATCGCCTATTTAAACGATGCCATTAGCACGACAAAGGAAAGTATTAAATATTACACCGATATTAGTAATATCATGCGCAACCGCCTGGCACAGGGTGTAGCAGATAGCATCAGTGTAGATCAAGCACAACAGGCAGTGTTAACGGCACGTAATAATTTAATCACTTATCAACTCAATCGTAAAACTGCAGAACAAACACTCCGCAATTTACTTAACTTAAAACCGGACGAAACATTAAAAATTACCTTCCCGCATATTTTGAAAGTTAAATCCGTAGGTGTAAATTTGAACGTACCGGTTTCCGTCATCGCCAATCGTCCTGATATAAAAGGCTATCAAGCACGCTTAAGTAGTGCATTTAAAAATGTCAAAGCGACTGAAAAAAGCTGGTTCCCGGAAATTACCTTAGGCGGTAGCTTAAATTCGAGCGGTAAAAAATTGAATAGCGCAACAAATACACTTATCGGTGGAGGTGCATTAGGTATTAGTCTGCCGTTCTTAAACTGGAATACGGTTAAATGGAATGTAAAAATTTCCGAAGCAGATTATGAAACAGCGCGTTTGAATTATGAAAAAAGTATCACTGTCGCATTAAATGATGTGGATACTAATTATTTCTCATTTACACAAGCCAAAAAACGCTTTACTAATGCCCAAAAAACCTACATTTACAATCAGCGTATTACGCAGTACTACCGCAACCGGTATAATGCAGGTGTATCCGAATTACGTGAATGGTTAACCGCTGCAAATACCGAAAAAAATTCCCAACTCTCTATTTTACAAGCCAAATATAACGTAATTCAGGCCGAAAATGCGGTTTACAGTTCTATGGCGGGTTATTATTCCGTAAAAAAA","","","51106","VATTLTGCANIGDSYRASLKNYKQYEEITKQYNIKNDWWKLYKDAQLNRVVEKALLNNKDLAKATISVNRALYSANLAGANLVPAFSGSTRSTAQKNIKTGGNSTISHTGSLNVSYTLDLWFRLADTADAAEWAHKATVQDMESTKLSLINSVVTTYYQIAYLNDAISTTKESIKYYTDISNIMRNRLAQGVADSISVDQAQQAVLTARNNLITYQLNRKTAEQTLRNLLNLKPDETLKITFPHILKVKSVGVNLNVPVSVIANRPDIKGYQARLSSAFKNVKATEKSWFPEITLGGSLNSSGKKLNSATNTLIGGGALGISLPFLNWNTVKWNVKISEADYETARLNYEKSITVALNDVDTNYFSFTQAKKRFTNAQKTYIYNQRITQYYRNRYNAGVSELREWLTAANTEKNSQLSILQAKYNVIQAENAVYSSMAGYYSVKK","1411434","","toxin and drug export protein, TolC family","Outer membrane, Extracellular","","
InterPro
IPR003423
Family
Outer membrane efflux protein
PF02321\"[47-231]T\"[254-438]TOEP
InterPro
IPR010131
Family
RND efflux system, outer membrane lipoprotein, NodT
TIGR01845\"[1-440]Touter_NodT: efflux transporter, outer membr


","BeTs to 9 clades of COG1538COG name: Outer membrane proteinFunctional Class: M,NThe phylogenetic pattern of COG1538 is -------q-----cefghsnujx---Number of proteins in this genome belonging to this COG is","","Residues 5 to 46 match (7e-13) PD:PD318325 which is described as PROTEOME COMPLETE HI1462 PM0527 ","","","","","","","","","","","","Mon Jan 13 10:32:04 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02077 is paralogously related to AA02142 (6e-24).","","","","","","Residues 254 to 438 (E-value = 3.3e-33) place AA02077 in the OEP family which is described as Outer membrane efflux protein (PF02321)","","",""," Crosby JA, Kachlany SC.TdeA, a TolC-like protein required for toxin and drug export in Aggregatibacter (Actinobacillus) actinomycetemcomitans.Gene. 2007 Feb 15;388(1-2):83-92. Epub 2006 Oct 17.PMID: 17116373 ","","","","1","","","" "AA02078","1412752","1412853","102","GTGAGGGTTGTTGCCACCACTATAGTTAAGGTTAATTTTTTTATTGTGAACATTGTTTTTTCCCTTTTTTATAAAAGTGCGGTCAAAAATTATAGAGAATTC","","","3995","VRVVATTIVKVNFFIVNIVFSLFYKSAVKNYREF","1412853","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide
tmhmm\"[4-24]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 16:29:42 2004","Wed Feb 25 16:29:42 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02078 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 16:29:42 2004","","","","","","","","","","","","","1","","","" "AA02080","1414854","1412884","1971","ATGCCCCGATTATCTTCTAAAGTGCGGTGGGTTTCGACGATGAATATAATTGAAATCAAGCAGCTCAACCGTTATTTTGGCGAAGGTGAAAACCGCGTTCATGTTTTAAAAGACATTTCCCTTTCCATCGAAAGAGGTGATTTTGTCGCCATTATGGGACAATCTGGTTCAGGCAAATCCACACTGATGAATATCATTGGTTGTTTGGACACGGCAACCGGTGGTTCATCCAAAATTGATGGAAAAGAAACCATTGAATTAACCAACGATCAGCTTTCCGATTTACGCAGCCAAAAATTCGGTTTTATTTTCCAACGCTATAACCTATTAAGCAGCTTAACCGCCGCAGAAAACGTCGCCTTACCTGCAATTTATGCGGGAATGCCACAAAGCCAACGCTTGGAACGTGCCAAACAATTATTGGAAAAACTGGGATTGGGCGATAAATGGCAAAACAAGCCGAACCAGCTTTCAGGCGGTCAACAACAGAGAGTGAGTATTGCCCGTGCATTGATGAACGGCGGAGAAATTATCCTTGCCGACGAACCCACAGGTGCGCTGGATTCGCACAGCGGTGAAAATGTGATGGAAATCCTCCGTCAACTGCACGAGGAAGGCCACACCATTATTATGGTGACCCACGACAAGCACATTGCTGCCAGTGCCAATCGGATCATTGAAATCAAAGATGGTGAAATTATCAGTGATACGCAAAAACGTCAGGTAAAAAGTGCGGTTAAAAATCCAAGTGTTTTTAAAGGTCGTTTCGGTTTCAGCAAAGATCAACTTATGGAAGCCTTCCGTATGTCCGTCAGTGCCATTGTAGCGCACAAAATGCGCTCATTGCTGACCATGCTGGGAATTATCATCGGGATCACTTCCGTCGTTTCCGTGGTGGCGTTAGGAAATGGTTCACAACAAAAGATTTTGGAAAATATTCGCGGTATCGGCACAAACACAATGACGATTTTTAACGGTAATGGTTTCGGTGACCGTCGTTCACGGCACATTCAAAACCTAAAAATCAGCGATGCCAATACGTTATCGAAACAAAGTTATATTCAAAGCGTTACTCCAAATACCTCTTCCAGCGGCATTTTAGTGGTCGGTAACAAATCCTTCACATCCGCCAATTTATATGGTATCGGTGAACAATATTTTGATGTAGAAGGCTTGAAGTTAAAACAGGGCCGTTTATTAACCGAGGACGATGTGGATCAAAGCAACCAGGTGGTCGTGCTGGACGAAAGTGCAAAAAAAGCCATTTTTGCCAACGAAAATCCCCTTGGCAAAACGGTGATTTTTAATAAGCGACCATTTCGTGTCATTGGCGTGGTGTCAGATCAACAGCTGGGCGGATTTCCCGGTAATTCGTTAAATCTATATTCTCCTTATAGTACTGTATTAAATAAAATTACCGGTGGCAGTCGAATTGGTTCCATCACAGTAAAAATTAGTGATGACGTAAATTCTACCGTGGCGGAGAAAAGCCTAACGGAATTATTGAAATCTCTGCATGGCAAAAAAGACTTTTTTATCATGAACAGTGACACTATTAAGCAGACCATTGAAAATACTACCGGCACGATGAAATTACTCATCTCTTCTATTGCTTTTATTTCCTTAATTGTAGGCGGTATCGGCGTGATGAACATTATGTTAGTGTCAGTGACGGAACGCACAAAAGAAATTGGTGTACGCATGGCAATCGGCGCCCGTCAGATTAATATTTTGCAGCAGTTTTTAATTGAAGCGGTGTTAATTTGTTTAATCGGTGGCGTGGCCGGAATTTTGTTATCTGTCCTCATCGGCGTGTTGTTTAATAGCTTTATAACGGATTTCAGCATGGATTTTTCCACTGCATCCATTGTTACCGCCGTATTATTCTCCACCCTAATCGGCGTGTTATTCGGCTATATGCCGGCAAAGAAAGCAGCAGAATTAAATCCGATTACAGCGTTGGCGCAAGAA","","","72425","MPRLSSKVRWVSTMNIIEIKQLNRYFGEGENRVHVLKDISLSIERGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSSKIDGKETIELTNDQLSDLRSQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQSQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADEPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDGEIISDTQKRQVKSAVKNPSVFKGRFGFSKDQLMEAFRMSVSAIVAHKMRSLLTMLGIIIGITSVVSVVALGNGSQQKILENIRGIGTNTMTIFNGNGFGDRRSRHIQNLKISDANTLSKQSYIQSVTPNTSSSGILVVGNKSFTSANLYGIGEQYFDVEGLKLKQGRLLTEDDVDQSNQVVVLDESAKKAIFANENPLGKTVIFNKRPFRVIGVVSDQQLGGFPGNSLNLYSPYSTVLNKITGGSRIGSITVKISDDVNSTVAEKSLTELLKSLHGKKDFFIMNSDTIKQTIENTTGTMKLLISSIAFISLIVGGIGVMNIMLVSVTERTKEIGVRMAIGARQINILQQFLIEAVLICLIGGVAGILLSVLIGVLFNSFITDFSMDFSTASIVTAVLFSTLIGVLFGYMPAKKAAELNPITALAQE","1412884","","ABC transporter, ATP-binding/permease","Inner membrane, Outer membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[156-199]TQ7NUJ3_CHRVO_Q7NUJ3;
PF00005\"[46-231]TABC_tran
PS50893\"[17-255]TABC_TRANSPORTER_2
PS00211\"[157-171]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[45-232]TAAA
InterPro
IPR003838
Domain
Protein of unknown function DUF214, permase predicted
PF02687\"[478-650]TFtsX
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[14-258]Tno description
PTHR19222\"[17-242]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF32\"[17-242]TABC TRANSPORTER
tmhmm\"[282-302]?\"[537-557]?\"[577-611]?\"[621-639]?transmembrane_regions


","BeTs to 3 clades of COG0577COG name: ABC-type transport systems, involved in lipoprotein release, permease componentsFunctional Class: RThe phylogenetic pattern of COG0577 is aom----qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 1e-38) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 35-81 3.9e-16 IPB001140B 154-192 3.2e-15 IPB001140C 208-237 0.00019Significant hit ( 1e-27) to 2/2 blocks of the IPB003838 family, which is described as \"DUF214\". Interpro entry for IP:IPR003838. IPB003838A 549-596 1.2e-24 IPB003838B 641-654 0.12","Residues 127 to 199 match (5e-07) PD:PD446731 which is described as ATP-BINDING ABC PROTEOME COMPLETE TRANSPORTER ","","","","","","","","","","","Thu May 13 15:14:56 2004","Thu May 13 15:09:33 2004","","","Thu May 13 15:14:56 2004","Thu May 13 15:09:33 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02080 is paralogously related to AA01616 (2e-46), AA02440 (3e-46), AA00415 (7e-34), AA01524 (2e-33), AA00858 (3e-31), AA01422 (2e-29), AA01656 (6e-29), AA02718 (1e-28), AA01051 (4e-27), AA00700 (7e-27), AA02353 (3e-26), AA01645 (2e-25), AA01684 (1e-24), AA01867 (2e-23), AA02324 (3e-23), AA00207 (3e-21), AA02140 (1e-20), AA02609 (2e-20), AA02606 (2e-20), AA02805 (4e-20), AA00933 (1e-19), AA01961 (2e-19), AA02898 (4e-19), AA02320 (3e-18), AA02484 (1e-17), AA01510 (1e-17), AA01456 (1e-17), AA02899 (3e-17), AA01779 (3e-17), AA01393 (6e-17), AA02786 (1e-16), AA01820 (5e-16), AA00799 (5e-16), AA01824 (1e-15), AA01509 (8e-15), AA02550 (2e-14), AA01757 (2e-14), AA01947 (1e-13), AA02438 (4e-13), AA01568 (7e-13), AA00934 (3e-12), AA02331 (4e-12), AA00061 (4e-12), AA01569 (5e-12), AA01555 (2e-11), AA00751 (2e-11), AA02573 (3e-11), AA02152 (2e-09), AA02642 (3e-09), AA02146 (4e-09), AA01291 (8e-09), AA02225 (5e-08), AA01615 (9e-08), AA00591 (9e-08), A02145 (1e-05), AA02226 (6e-05) and AA01618 (4e-04).","Thu May 13 15:09:33 2004","","","","","Residues 478 to 650 (E-value = 4.1e-50) place AA02080 in the FtsX family which is described as Predicted permease (PF02687)","Thu May 13 15:09:33 2004","",""," Crosby JA, Kachlany SC.TdeA, a TolC-like protein required for toxin and drug export in Aggregatibacter (Actinobacillus) actinomycetemcomitans.Gene. 2007 Feb 15;388(1-2):83-92. Epub 2006 Oct 17.PMID: 17116373 ","","","Thu May 13 15:14:56 2004","1","","","" "AA02081","1416019","1414838","1182","ATGAAGAAAAAACCTCTTATTATTACTGCTATTGCAGCTGCTGTGATTACCGGCGGTTATTTTTTTGTACGCGATTCCAGCGCACAAACCACTTACTTAACGGAAGAGGTCAAACGCGGCAATATTGAAAAGAACGTGGTTGCTACCGGTTCCATCGAAAGTATCAATACTGTTGATGTGGGCGCGCAGGTGTCAGGGAAAGTCACCAAACTTTATGTCAAACTGGGACAACAGGTGAAAAAAGGCGATTTAATTGCCGAGATTGATTCCACCACCCAAATTAATACGTTAAACACCCGCAAAGCCGCCTTGGCGAGTTATCAAGCCCAATTAGTTGCACGCAAAACCGCTTACGATGTGGCACTTTCCAATTACAATCGCTTGTCCAAATTATACGGGCAAAAAGCCACTTCATTGGACACATTAAATACCGCTAAAGCCACCTTGAATAATGCCAAAGCGGAAATGGACGTGGTACAGGAAAATATTAAACAGGCGGAAATTGAAGTGAACACCGCCGAAACCAACGTGGGCTACACCAAAATCACCTCCCCGATTGACGGCACGGTCATTTCCACACCGGTATCCGAAGGGCAAACGGTAAACTCCAATCAGACCACGCCGACTATCATTAAAGTGGCGGATTTAAGCAAAATGCGCATTAAGCCGGAAATTTCCGAAGGCGACATTACCAAAGTCAAAGCGGGGCAAGATGTGACCTTCACTATTTTATCCGACAATAAAACCGTTTATCACGCCAAAATTGATTCCGTAGACCCGGCAACAACCACCATCAGCGACAATTCAAGCTCAAACAGTTCAAGCTCAGGTTCCAGTTCCTCCTCCGGTTCAAGCAGCAGCGCAGTATATTATTACGCCAACATTATCGTTGAAAATCCCGAACATGTTTTGCGTATTGGTATGACCACGGAAAATAACATTAAAATTGCCGATGTGCAAAATGTGTTGTTTATTCCGAATTTGGCAGTGCAAAAGCAGCAAGACAAATATGTAGTCAATGTACTAAACGGCAATACAACACAAGAACGGGAAATCGAAATCGGCGTGCAAAATGATTTCCAAACGGAAGTCAAATCCGGTTTAACGGAAGGCGAAAAAGTAGTGATTTCACAAGTTGCTGCCGGTGAAACCTTCGGCGATCCTGATGCCCCGATTATCTTC","","","42294","MKKKPLIITAIAAAVITGGYFFVRDSSAQTTYLTEEVKRGNIEKNVVATGSIESINTVDVGAQVSGKVTKLYVKLGQQVKKGDLIAEIDSTTQINTLNTRKAALASYQAQLVARKTAYDVALSNYNRLSKLYGQKATSLDTLNTAKATLNNAKAEMDVVQENIKQAEIEVNTAETNVGYTKITSPIDGTVISTPVSEGQTVNSNQTTPTIIKVADLSKMRIKPEISEGDITKVKAGQDVTFTILSDNKTVYHAKIDSVDPATTTISDNSSSNSSSSGSSSSSGSSSSAVYYYANIIVENPEHVLRIGMTTENNIKIADVQNVLFIPNLAVQKQQDKYVVNVLNGNTTQEREIEIGVQNDFQTEVKSGLTEGEKVVISQVAAGETFGDPDAPIIF","1414838","","periplasmic protein","Inner membrane, Extracellular","","
InterPro
IPR006143
Family
Secretion protein HlyD
PF00529\"[56-207]THlyD
TIGR01730\"[32-391]TRND_mfp
noIPR
unintegrated
unintegrated
SSF111369\"[43-234]TSSF111369


","BeTs to 14 clades of COG0845COG name: Membrane-fusion proteinFunctional Class: QThe phylogenetic pattern of COG0845 is -------qvd-lbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-16) to 2/3 blocks of the IPB002215 family, which is described as \"HlyD family secretion protein\". Interpro entry for IP:IPR002215. IPB002215A 54-90 2e-13 IPB002215B 181-215 0.12Significant hit ( 1.1e-06) to 3/7 blocks of the PR01490 family, which is described as \"Gram-negative bacterial RTX secretion protein D signature\". Prints database entry for PR:PR01490. PR01490B 68-88 0.0023 PR01490D 228-252 3.1 PR01490F 304-319 49","","","","","","","","","","","","Thu May 13 15:15:41 2004","Thu May 13 15:15:41 2004","","","Thu May 13 15:19:12 2004","","yes","Fri Feb 20 15:41:32 MST 1998","AA02081 is paralogously related to AA01340 (8e-17), AA01732 (7e-08) and AA02139 (3e-04).","Thu May 13 15:15:41 2004","","","","","","","",""," Crosby JA, Kachlany SC.TdeA, a TolC-like protein required for toxin and drug export in Aggregatibacter (Actinobacillus) actinomycetemcomitans.Gene. 2007 Feb 15;388(1-2):83-92. Epub 2006 Oct 17.PMID: 17116373 ","","","Thu May 13 15:15:41 2004","1","","","" "AA02082","1416241","1417908","1668","ATGAGCACAGAAACTGTATTAGAAACGGCGGAAAATAGCCGTCCGCACAATTTTATTACTCAAATTATTAATGAAGATTTAAAAAGCGGTAAACACAATAACGTTTATACGCGTTTCCCGCCTGAACCAAACGGTTATTTACACATCGGTCATGCTAAATCCATTTGCTTGAATTTTGGTATTGCAAAAGATTACCAAGGGCTATGTAATTTGCGTTTTGACGACACCAACCCGGTGAAAGAAGATGTGGAATATGTGGATTCTATTAAAGCTGATGTAGAATGGTTAGGTTTCCATTGGGCGGGCGAAGTGCATTATGCGTCCGATTATTTTGACGCGCTTTATGGTTATGCCATTGAGCTTATCAAAAAAGGTTTGGCGTATGTGGATGAACTTTCGCCGGAAGAAATGCGCGAATATCGCGGCACCTTAACCGAACCGGGTAAAAACAGCCCATATCGTGATCGCAGCGTGGAAGAAAACCTGGCTTTATTTGAAAAAATGAAAAACGGCGAATTTGCCGAAGGTAAAGCGAGCTTGCGGGCAAAAATTGATATGGCGTCGCCGTTTATGGTGATGCGCGATCCGGTGCTTTATCGCATAAAATTCGCCAGCCATCACCAAACAGGCGACAAATGGTGCATTTATCCGATGTACGATTTCACTCATTGTATTTCCGATGCTATTGAGCGTATCACGCACTCCTTATGTACCCTTGAATTCCAAGATAACCGTCGTTTGTATGATTGGGTGTTGGAAAATATCAGCATTGAACGCCCGCTGCCGCACCAATATGAATTTTCCCGTTTAAATTTAGAAGGCACCTTAACCTCTAAACGCAAACTCTTAAAATTGGTGAATGATGAAATCGTGGACGGCTGGAACGATCCGCGTATGCCAACCATTTCAGGCTTGCGCCGTCGTGGTTATACACCGGCGTCCATTCGTGAATTTTGCCGTCGTATTGGCGTGACCAAACAAGATAACGTGGTGGAATATAGTGCATTAGAAGCCTGCATTCGTGATGATTTAAACCAAAATGCACCACGCGCCATGGCGGTGATCGATCCGGTGAAAGTGGTGATTGAAAACTTTGACGGTGAAGAAATATTGACTGCGCCAAATCACCCGAATCGTCCAGAACTAGGAGAACGCCAATTACCGTTCACAAAAGAAATCTATATTGATTGTGCCGATTTCCGCGAAGAAGCGAATAAACAATATAAACGCTTAGTGCTGGGCAAGGAAGTGCGTTTGCGCAATGCTTATGTGATCAAAGCGAAACGCGTAGAAAAAGATGTGAACGGTGAAATTACCACGATTTACTGCACTTATGATCCGGAAACCTTGGGTAAAAATCCGGCAGATGGTCGCAAAGTAAAAGGCGTGATTCACTGGGTGTCTGCGGTGCATAATCACCCGGCAGAGTTCCGTTTATACGATCGTTTATTCACCGTGCCGAATCCGGGCGCGGAAGAAGATATCGAAAGCGTATTAAACCCAACTTCTTTAGTGGTGAAACAGGGTTTTGTGGAGCAAAGCCTTGGCAACGCGGAAGCGGAGAAGGGCTATCAATTCGAACGTGAAGGTTATTTCTGTGCCGACAGCAAAGACAGCCGCTCCGAACATTTGGTATTCAACCTGACAGTGAGTTTGAAAGAAGGATTT","","","64821","MSTETVLETAENSRPHNFITQIINEDLKSGKHNNVYTRFPPEPNGYLHIGHAKSICLNFGIAKDYQGLCNLRFDDTNPVKEDVEYVDSIKADVEWLGFHWAGEVHYASDYFDALYGYAIELIKKGLAYVDELSPEEMREYRGTLTEPGKNSPYRDRSVEENLALFEKMKNGEFAEGKASLRAKIDMASPFMVMRDPVLYRIKFASHHQTGDKWCIYPMYDFTHCISDAIERITHSLCTLEFQDNRRLYDWVLENISIERPLPHQYEFSRLNLEGTLTSKRKLLKLVNDEIVDGWNDPRMPTISGLRRRGYTPASIREFCRRIGVTKQDNVVEYSALEACIRDDLNQNAPRAMAVIDPVKVVIENFDGEEILTAPNHPNRPELGERQLPFTKEIYIDCADFREEANKQYKRLVLGKEVRLRNAYVIKAKRVEKDVNGEITTIYCTYDPETLGKNPADGRKVKGVIHWVSAVHNHPAEFRLYDRLFTVPNPGAEEDIESVLNPTSLVVKQGFVEQSLGNAEAEKGYQFEREGYFCADSKDSRSEHLVFNLTVSLKEGF","1417908","[CATALYTIC ACTIVITY] ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln).[SUBUNIT] Monomer (By similarity).[SUBCELLULAR LOCATION] Cytoplasmic.","glutaminyl-tRNA synthetase","Cytoplasm","","
InterPro
IPR000924
Family
Glutamyl-tRNA synthetase, class Ic
PR00987\"[38-50]T\"[52-63]T\"[67-80]T\"[217-227]TTRNASYNTHGLU
PTHR10119\"[38-555]TGLUTAMYL/GLUTAMINYL-TRNA SYNTHETASE
PF00749\"[34-346]TtRNA-synt_1c
PF03950\"[348-535]TtRNA-synt_1c_C
InterPro
IPR001412
Family
Aminoacyl-tRNA synthetase, class I
PS00178\"[41-52]TAA_TRNA_LIGASE_I
InterPro
IPR004514
Family
Glutaminyl-tRNA synthetase
PTHR10119:SF3\"[38-555]TGLUTAMINYL-TRNA SYNTHETASE (GLUTAMINE--TRNA LIGASE) (GLNRS)
TIGR00440\"[35-556]TglnS: glutaminyl-tRNA synthetase
noIPR
unintegrated
unintegrated
G3DSA:1.10.1160.10\"[269-347]Tno description
G3DSA:2.40.240.10\"[356-472]Tno description
G3DSA:3.90.800.10\"[108-216]Tno description


","No hits to the COGs database.","Significant hit ( 2.3e-05) to 1/2 blocks of the IPB001412 family, which is described as \"Aminoacyl-transfer RNA synthetases class-I\". Interpro entry for IP:IPR001412. IPB001412A 41-51 2.3e-05","Residues 104 to 194 match (7e-09) PD:PD565634 which is described as LIGASE CYTOPLASMIC AMINOACYL-TRNA GLUTAMYL-TRNA GLURS SYNTHETASE ATP-BINDING SYNTHETASE GLUTAMATE--TRNA BIOSYNTHESIS ","","","","","","","","","","","Mon Jan 13 11:58:32 2003","Mon Jan 13 11:58:32 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02082 is paralogously related to AA00214 (2e-12).","","","","","","Residues 348 to 535 (E-value = 1.6e-102) place AA02082 in the tRNA-synt_1c_C family which is described as tRNA synthetases class I (E and Q), anti-codon binding domain (PF03950)","","","","","Uemura,H., Conley,J., Yamao,F., Rogers,J. and Soll,D. Escherichia coli glutaminyl-tRNA synthetase: a single amino acid replacement relaxes rRNA specificity Protein Seq. Data Anal. 1 (6), 479-485 (1988) PubMed: 2464170 Yamao,F., Inokuchi,H., Cheung,A., Ozeki,H. and Soll,D. Escherichia coli glutaminyl-tRNA synthetase. I. Isolation and DNA sequence of the glnS gene J. Biol. Chem. 257 (19), 11639-11643 (1982) PubMed: 6288695.Hoben,P., Uemura,H., Yamao,F., Cheung,A., Swanson,R., Sumner-Smith,M. and Soll,D. Misaminoacylation by glutaminyl-tRNA synthetase: relaxed specificity in wild-type and mutant enzymes. Fed. Proc. 43 (15): 2972-2976 (1984) [PubMed: 6389180].Hoben,P., Royal,N., Cheung,A., Yamao,F., Biemann,K. and Soll,DEscherichia coli glutaminyl-tRNA synthetase. II. Characterization of the glnS gene product. J. Biol. Chem. 257 (19): 11644-11650 (1982) [PubMed: 6749844].Rould,M.A., Perona,J.J., Soll,D. and Steitz,T.A. Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 A resolution. Science 246 (4934): 1135-1142 (1989) [PubMed: 2479982].Hoben,P., Royal,N., Cheung,A., Yamao,F., Biemann,K. andSoll,D. Escherichia coli glutaminyl-tRNA synthetase. II. Characterization of the glnS gene product J. Biol. Chem. 257 (19), 11644-11650 (1982) PubMed: 6749844 ","","Mon Jan 13 11:58:32 2003","1","","","" "AA02084","1417983","1418414","432","ATGCAATTAGAACCCGATTTTTGGCTACACAAAACCTTACTTGACATGAACGATGCCGAGTGGGAGGCGTTATGTGACGGGTGTGGGAAATGTTGCTATCGTAAATATATTGACGGCTATGGCAAATATGGACATTTGTATTACACGCGCATTGCCTGCAATCTGTTGGAGTTGGAAACGGGAAAGTGCGGTCAATATTCACGGCGTTTTGAATTGGAAGAAGACTGCACCAAGCTCACCAAAGAAAACTTGTCGGATTTCGATTGGTTACCCGCCACCTGTGCTTATCGTTTATTACATGAAGGAAAACCGTTGCCCTCATGGCATCCGCTTATCAGCGGCGATCCCGATAGCGTGAAAAAAGCCGATATTTTGATTAAATACGGCATTCATGAACGGGATGTTATTGATTGGTTCGATTTTATTCTTGAT","","","16878","MQLEPDFWLHKTLLDMNDAEWEALCDGCGKCCYRKYIDGYGKYGHLYYTRIACNLLELETGKCGQYSRRFELEEDCTKLTKENLSDFDWLPATCAYRLLHEGKPLPSWHPLISGDPDSVKKADILIKYGIHERDVIDWFDFILD","1418414","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR005358
Family
Protein of unknown function UPF0153
PF03692\"[24-95]TUPF0153
InterPro
IPR008228
Family
Uncharacterised conserved protein UCP006173
PD021710\"[7-108]TYD55_HAEIN_P44168;
PIRSF006173\"[5-144]TUncharacterised conserved protein


","BeTs to 5 clades of COG2983COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG2983 is --m-----------efgh---j----Number of proteins in this genome belonging to this COG is","","Residues 7 to 143 match (6e-58) PD:PD021710 which is described as COMPLETE PROTEOME CYTOPLASMIC YCGN R01011 HI1355 MLL2411 PA1299 YPO2083 STY1941 ","","","","","","","","","","","","Mon Jan 13 11:59:41 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02084 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 144 (E-value = 3.9e-89) place AA02084 in the DUF838 family which is described as Bacterial protein of unknown function (DUF838) (PF05779)","","","","","","","","1","","","" "AA02086","1418517","1419074","558","ATGCAAATTCCAGACTCCATCAAGCAATCCACAGAAAAATTAGAACTTGCTTTAGCTCATTATGATAGTGGCAGGCATTTAATTTATGCCAGTACGCAAACGTTATCGTATTTTATCAAATTACCACAGCCGCCTAATAAATCAGAGTGTTCTAAAGGGGAATTTGATGATGTGATTACGATGTTTAATAATGACATGATCTATTATGATTTGACCCGTTTATCTCTTCCTTCTTGTTCATTACATTACCAACTCTTTGATGAACAGGGCAATAAGTGTGCAGAACACTCCCTTTTCGATTTTCCATCTATTCAACTTTCTCAGCAGCCTTTCAGATACTACCAATTAAGGCATTTGATGCATTTAAAAAAGCATAGGGCGGGGCATTGTTGTATTAATGTCTTGGACATCTTCGAATACCAAGATCAGCAGGCGGAAGAAAATACTGTCGGTTGGCGTAAGAAATTAAGCAAATCATTCGATCTTATTTTCAATGATGAATACATTGCTTCGTTTTTCTGTTTAATCAAGCACGCAACGCTTAGCGAGGATTCATTA","","","21774","MQIPDSIKQSTEKLELALAHYDSGRHLIYASTQTLSYFIKLPQPPNKSECSKGEFDDVITMFNNDMIYYDLTRLSLPSCSLHYQLFDEQGNKCAEHSLFDFPSIQLSQQPFRYYQLRHLMHLKKHRAGHCCINVLDIFEYQDQQAEENTVGWRKKLSKSFDLIFNDEYIASFFCLIKHATLSEDSL","1419074","[CATALYTIC ACTIVITY] Transfers a segment of a (1,4)-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or (1,4)-alpha-D-glucan.","4-alpha-glucanotransferase","Cytoplasm","","No hits reported.","No hits to the COGs database.","","Residues 7 to 126 match (6e-17) PD:PD142933 which is described as COMPLETE PROTEOME DISPROPORTIONATING AMYLOMALTASE 4-ALPHA-GLUCANOTRANSFERASE GLYCOSYLTRANSFERASE MALQ CARBOHYDRATE TRANSFERASE ENZYME ","","","","","","","","","","","Mon Jan 13 12:02:10 2003","Mon Jan 13 12:02:10 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02086 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02087","1419074","1421266","2193","ATGACTCAATTAGTAGCGCAATCAGTTATCAATCAATTTTTTGACGGCACACATGGTGATCCGTTTTCCGTATTGGGTATGCACGAAACCGAAAAGGGTATTGAAATTCGTGCGTTGTTGCCGGATGCAAGTCGTGTTTTGGTCATTGAAAAAGAAAATCAGGAAACGTTGTGTGAATTAACCCATTTAGATGACAGAGGCTTTTTTGCCGGCGTGGTGCCGGATACGCGGAATTTCTTTGCTTATCAACTACAGGTGTATTGGGGTAAAGAGTCACAAATTATTGAAGACCCGTACCGTTATCACCCGATGATTAATGATTTGGATGAATGGTTGTTGGCGGAAGGTTCGTTTTTACGTCCGTATGAAGTATTAGGCGCGCATTTCATTGAATGTGACGGTGTCTCAGGCGTGAATTTCCGTTTGTGGGCGCCAAATGCCAAACGGGTTTCTGTGGTAGGCGATTTTAACTATTGGGACGGTTGTCGCCATCCAATGCGCTTACACCCGGCAAGCGGCGTGTGGGAATTGTTCCTGCCGAAAGTCTCTTTGGGGCAACTGTATAAATTTGAATTAATCGATTGCCATGGCAACCTCCGCTTAAAAGCCGACCCTTATGCCTTCAGTTCTCAGTTACGTCCCGATACCGCGTCACAAATCAGTCCGTTGCCGAGTGTCGTGCCGATGACGGAAGCCCGTCGTAAAGCTAACCAATGGGATCAGCCGATTTCCATTTATGAGGTGCATTTAGGCTCTTGGCGACGTAACTTGGAAAACAATTTCTGGCTGGATTACGATCAAATCGCCGACGAATTGATTCCTTACGTGCAGGAAATGGGCTTCACCCATATTGAATTTTTACCGTTGTCCGAGTTTCCGTTTGACGGTTCTTGGGGTTATCAACCGCTTGGCTTGTATTCGCCGACCAGCCGTTTTGGTACGCCGGAAGGCTTTAAACGCTTGGTAGAGCGGGCGCATGATGCCGGTATTAATGTGATTCTCGACTGGGTGCCGGGGCATTTCCCGAGCGATACCCACGGTTTGGTGGCATTTGGCGGTACGGCATTGTATGAGCACGCCGATCCGCGCGAAGGCTATCACCAAGATTGGAATACGCTGATTTACAACTACGGACGCAACGAAGTTAAGAATTTCTTATCCAGTAATGCGTTGTATTGGCTTGAACGCTTCGGTATCGACGGCATTCGGGTCGATGCGGTGGCGTCTATGATTTATCGTGATTACAGTCGCGCCGAAGGGCAGTGGATTCCGAATCAATACGGCGGGCGGGAAAACTTAGAAGCCATTGAATTTTTGAAACATACCAACTGGAAAATCCATAGCGAAGTACCGGGTTCTATCGCCATTGCGGAAGAATCCACCGCCTTTACCGGCGTGACCCATCCGAGCGAACAGGGCGGTTTAGGTTTTAATTTCAAGTGGAACATGGGTTGGATGAACGACACCTTATCCTACATGGAAAAAGACCCCGTTTATCGCCAATATCACCACAACCAAATGACTTTCGGCATGATGTATCAATACAGCGAAAACTTCGTGTTGCCGCTTTCTCATGACGAAGTGGTGCATGGCAAATGTTCTCTTATCGGCAAAATGCCGGGCGATGCGTGGCAAAAATTTGCCAATTTGCGTGCCTATTATGGCTATATGTGGGGTTATCCGGGCAAAAAATTGCTATTTATGGGCAATGAATTCGCCCAAGGTCGCGAATGGAATTACCGTGAAAGTCTGGATTGGTTCCTGCTAGATGAAGGCATCGGCGGTCAATGGCATATCGGCGTACAACAGCTGGTGAAAGATCTCAATAAAATTTACCGCGAAAACGCACCGCTCTTTGAGCTGGATTCCGATCCGCAGGGCTTTGATTGGTTGGTGGCAGATGACGCACAAAATTCCGTTTTCGCTTTTGAACGCCGCAGCCGTGATGGCGGACGTATTCTTGTAATCAGCAACTTCACGCCGGTGCCGCGTCATGATTATCGTCTCGGTGTGAATGTTGCCGGCGAATATCACGAAATTTTAAATACCGACTCCGCCTATTACGCCGGTTCAAATGTGGGTAATTTAGGCGCTGTACACAGCGAAGACATCGCCAGCCATAATCGGGCGAACTCCATTTCCGTCTCTATTCCGCCATTGGCAACCATTTATTTGAAATATCAGGGTAAAGCA","","","83713","MTQLVAQSVINQFFDGTHGDPFSVLGMHETEKGIEIRALLPDASRVLVIEKENQETLCELTHLDDRGFFAGVVPDTRNFFAYQLQVYWGKESQIIEDPYRYHPMINDLDEWLLAEGSFLRPYEVLGAHFIECDGVSGVNFRLWAPNAKRVSVVGDFNYWDGCRHPMRLHPASGVWELFLPKVSLGQLYKFELIDCHGNLRLKADPYAFSSQLRPDTASQISPLPSVVPMTEARRKANQWDQPISIYEVHLGSWRRNLENNFWLDYDQIADELIPYVQEMGFTHIEFLPLSEFPFDGSWGYQPLGLYSPTSRFGTPEGFKRLVERAHDAGINVILDWVPGHFPSDTHGLVAFGGTALYEHADPREGYHQDWNTLIYNYGRNEVKNFLSSNALYWLERFGIDGIRVDAVASMIYRDYSRAEGQWIPNQYGGRENLEAIEFLKHTNWKIHSEVPGSIAIAEESTAFTGVTHPSEQGGLGFNFKWNMGWMNDTLSYMEKDPVYRQYHHNQMTFGMMYQYSENFVLPLSHDEVVHGKCSLIGKMPGDAWQKFANLRAYYGYMWGYPGKKLLFMGNEFAQGREWNYRESLDWFLLDEGIGGQWHIGVQQLVKDLNKIYRENAPLFELDSDPQGFDWLVADDAQNSVFAFERRSRDGGRILVISNFTPVPRHDYRLGVNVAGEYHEILNTDSAYYAGSNVGNLGAVHSEDIASHNRANSISVSIPPLATIYLKYQGKA","1421266","[CATALYTIC ACTIVITY] Formation of 1,6-glucosidic linkages of glycogen.[PATHWAY] Glycogen biosynthesis; third step.[SUBUNIT] Monomer (By similarity).","1,4-alpha-glucan branching enzyme","Cytoplasm","","
InterPro
IPR004193
Domain
Glycoside hydrolase, family 13, N-terminal
PF02922\"[124-207]TIsoamylase_N
InterPro
IPR006047
Domain
Glycosyl hydrolase, family 13, catalytic region
PF00128\"[264-338]TAlpha-amylase
InterPro
IPR006048
Domain
Alpha-amylase, C-terminal all beta
PF02806\"[630-730]TAlpha-amylase_C
InterPro
IPR006407
Domain
1,4-alpha-glucan branching enzyme, core region
TIGR01515\"[109-726]Tbranching_enzym: 1,4-alpha-glucan branching
InterPro
IPR013780
Domain
Glycosyl hydrolase, family 13, all-beta
G3DSA:2.60.40.1180\"[625-730]Tno description
InterPro
IPR013781
Domain
Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80\"[230-614]Tno description
InterPro
IPR013782
Family
1,4-alpha-glucan branching enzyme
PIRSF000463\"[12-730]T1,4-alpha-glucan branching enzyme
InterPro
IPR013783
Domain
Immunoglobulin-like fold
G3DSA:2.60.40.10\"[112-223]Tno description
noIPR
unintegrated
unintegrated
PTHR10357\"[204-725]TAMYLASE
PTHR10357:SF13\"[204-725]T1,4-ALPHA-GLUCAN BRANCHING ENZYME


","No hits to the COGs database.","","","","","","","","","","","","","Mon Jan 13 12:05:27 2003","Mon Jan 13 12:05:27 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02087 is paralogously related to AA02088 (4e-07).","","","","","","Residues 247 to 596 (E-value = 3.6e-06) place AA02087 in the Alpha-amylase family which is described as Alpha amylase, catalytic domain (PF00128)","","","",""," Baecker,P.A., Greenberg,E. and Preiss,J. Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli 1,4-alpha-D-glucan:1,4-alpha-D-glucan6-alpha-D-(1, 4-alpha-D-glucano)-transferase as deduced from thenucleotide sequence of the glg B gene. J. Biol. Chem. 261 (19): 8738-8743 (1986) [PubMed: 3013861].","","Mon Jan 13 12:05:27 2003","1","","","" "AA02088","1421422","1422153","732","ATGGTTAATTCCGACAACGTGTGGCATTTGGCGTTAAGCGGGGTGGCAAACGGAACCCAATATGGCTTCAGAATCACATCAAAAAATGACCGCACTTTGACGGCAAATCCGCAGAAATTGATGCTGGACCCTTATGCCAAGGCCGTGGTGGGCAAACCGGATTTAAGCTCGCCTGAAACGCAAGCGTGGTTTTTGTTGAGCGACGAGCGGGATAACGCCCGCTATGCACCGAAAGCGGTGGTGGTTGATCGTGCATTTGACTGGCAGAGTGACAAAGCGCCGAATACGCCCTGGACCGAAACCATTGTGTATGAGTTGAGTGTGAAAGGTTTTACCAAATTACAAACGGAATTACCAGAGAAAATACGTGGCACCTATGCCGGTTTGGCATATGCGCAAACGATTGCGTATTTGAAAAAGTTAGGTATAACGGCAGTCGAGTTGTTGCCCGTAAATTACGCGGTAAGCGAACCGCACTTACAACAAAGAGGGTTATCCAATTATTGGGGTTACAACCCGTTAGCCATGTTTGCCGTGGAACCGAAATATTGCTCGCAAGCCAATATGGCGAACCCGTTAAATGAATTTAAACACATGGTGAAAGCCTTGCATGAGGCAGGCATTGAAGTGATTTTAGACGTGGTGTTCAACCATACGGCGGAATCGGAAAAATACTTCCCAACCTTTAGTCAACGTGGCATTGATGACGAAACCTATTATTGGCAAACCCCG","","","33589","MVNSDNVWHLALSGVANGTQYGFRITSKNDRTLTANPQKLMLDPYAKAVVGKPDLSSPETQAWFLLSDERDNARYAPKAVVVDRAFDWQSDKAPNTPWTETIVYELSVKGFTKLQTELPEKIRGTYAGLAYAQTIAYLKKLGITAVELLPVNYAVSEPHLQQRGLSNYWGYNPLAMFAVEPKYCSQANMANPLNEFKHMVKALHEAGIEVILDVVFNHTAESEKYFPTFSQRGIDDETYYWQTP","1422153","[FUNCTION] This protein may be part of a glycogen biosynthetic/ catabolic operon but is not required for glycogensynthesis. ","glycogen operon protein","Periplasm","","
InterPro
IPR004193
Domain
Glycoside hydrolase, family 13, N-terminal
PF02922\"[1-46]TIsoamylase_N
InterPro
IPR006047
Domain
Glycosyl hydrolase, family 13, catalytic region
PF00128\"[79-226]TAlpha-amylase
InterPro
IPR013781
Domain
Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80\"[85-241]Tno description
InterPro
IPR013783
Domain
Immunoglobulin-like fold
G3DSA:2.60.40.10\"[4-83]Tno description
noIPR
unintegrated
unintegrated
PTHR10357\"[77-242]TAMYLASE
PTHR10357:SF25\"[77-242]TGLYCOGEN DEBRANCHING ENZYME


","BeTs to 10 clades of COG1523COG name: Pullulanase and related glycosidasesFunctional Class: GThe phylogenetic pattern of COG1523 is --------vdrlbcefgh---j-i--Number of proteins in this genome belonging to this COG is","","Residues 6 to 123 match (2e-20) PD:PD022336 which is described as HYDROLASE PROTEOME GLYCOGEN COMPLETE GLYCOSIDASE GLYCOSYL 3.2.1.- DEBRANCHING ENZYME OPERON ","","","","","","","","","","","Mon Jan 13 12:18:43 2003","Mon Jan 13 12:18:43 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02088 is paralogously related to AA02087 (1e-07).","","","","","","","","","","","Romeo,T., Kumar,A. and Preiss,J. Analysis of the Escherichia coli glycogen gene cluster suggests that catabolic enzymes are encoded among the biosynthetic genes. Gene 70 (2): 363-376 (1988) [PubMed: 2975249].","","Mon Jan 13 12:18:43 2003","1","","","" "AA02089","1422190","1423272","1083","ATGCTGAATTTGTCCAATCACATTACCCGTCGCTGGGTAGTGGATTGCCTGCGTTATTGGGTGGAAGAATGCCATGTAGACGGTTTCCGTTTCGATTTGGCGACTGCGTTAGGGCGCGAAACACCGGATTTTAATCACCATGCGGCGTTGTTTAACGACATTGCGCAAACGTCGAGTTTGCAGCGGGTGAAATTAATCAGTGAGCCTTGGGACATCGGACATTATGGCTATCAATTAGGCAATTTTCCCCATTATTTCGCTGAATGGAACGACCGTTTTCGTGATGATATGTGCCGTTTCTGGTTGTGGAAAAGTGGGGAAGTGGGCGCCTTTGCCGAACGTCTGGCGGGCTCCGGCGACATTTTTAAACAGGAACGGCGCCTGCCGCATACGTCGCTGAATTTTATTACCGCTCATGATGGCTTCACCTTGCGCGATTTAACCAGTTATAACCAAAAACACAATGAAGCCAATGGCGAAGAAAACCGTGACGGGCGCAATGAAAATTACAGTTATAACCATGGCTTTGAAGGCAGCGAATTGGATTTAACCGATCCGCACCAAAGTGCGGTAGAAAATCAGCGAGTTTTAACGGCAGGCAGTTTGCTCATGAGCTTATTGCTTTCCAACGGCACGCCGATGCTGTTGGCGGGCGACGAGTTCGGCAACAGTCAATTCGGCAATAACAATGCCTATTGTCAGGATAACGAAATCACCTGGTTAAAATGGCAGTCATTTAATCAGGATTTATTTAACCTAACCAGCCAAACGATCGCGTTACGAAAAAAAATTGCAAGTTTACTGAGTGATCATTGGTGGTCACAAGAAAATGTGTCTTGGCTTAATGCTCATGGGGAACTGATGAGCCTTGATGATTGGCACAATCGAGAAAATAAAACGCTACAAGTAGTATTAGATGAGCAATGGATTTTCTTAATCAATGCCAAAGCGGAAAAACAACATTTTACATTGCCTATGCAAGCGGTAAGTCAATGGAAACATGTATGCGGGACAACACACTTAACGTTGCACGAAAATCAGGTGGAAGTCGATGGGGTGGCATTTTGTGTGTTGCGGAAATAT","","","41886","MLNLSNHITRRWVVDCLRYWVEECHVDGFRFDLATALGRETPDFNHHAALFNDIAQTSSLQRVKLISEPWDIGHYGYQLGNFPHYFAEWNDRFRDDMCRFWLWKSGEVGAFAERLAGSGDIFKQERRLPHTSLNFITAHDGFTLRDLTSYNQKHNEANGEENRDGRNENYSYNHGFEGSELDLTDPHQSAVENQRVLTAGSLLMSLLLSNGTPMLLAGDEFGNSQFGNNNAYCQDNEITWLKWQSFNQDLFNLTSQTIALRKKIASLLSDHWWSQENVSWLNAHGELMSLDDWHNRENKTLQVVLDEQWIFLINAKAEKQHFTLPMQAVSQWKHVCGTTHLTLHENQVEVDGVAFCVLRKY","1423272","[FUNCTION] This protein may be part of a glycogen biosynthetic / catabolic operon but is not required for glycogen synthesis. ","glycogen operon protein","Cytoplasm, Extracellular","","
InterPro
IPR013781
Domain
Glycoside hydrolase, catalytic core
G3DSA:3.20.20.80\"[2-267]Tno description
noIPR
unintegrated
unintegrated
PTHR10357\"[4-332]TAMYLASE
PTHR10357:SF25\"[4-332]TGLYCOGEN DEBRANCHING ENZYME


","BeTs to 10 clades of COG1523COG name: Pullulanase and related glycosidasesFunctional Class: GThe phylogenetic pattern of COG1523 is --------vdrlbcefgh---j-i--Number of proteins in this genome belonging to this COG is","","Residues 211 to 255 match (1e-07) PD:PD487304 which is described as GLYCOGEN OPERON PROTEOME COMPLETE DEBRANCHING ENZYME GLGX ","","","","","","","","","","","Mon Jan 13 12:22:09 2003","Mon Jan 13 12:22:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02089 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Romeo,T., Kumar,A. and Preiss,J. Analysis of the Escherichia coli glycogen gene clustersuggests that catabolic enzymes are encoded among thebiosynthetic genes. Gene 70 (2): 363-376 (1988) [PubMed: 2975249].","","Mon Jan 13 12:22:09 2003","1","","","" "AA02090","1423302","1424609","1308","ATGAAAAGTAGTCTTTCCCAATTACCCAACAAATACGATCTTGTTAAAGATACGCTTGTTCTTATTTTAGCCGGCGGTCGCGGTTCACGTCTTCATGAGCTGACAGATAAACGTGCGAAACCGGCACTTTACTTCGGGGGGAATCGTCGTATCATTGACTTCGCACTTTCCAACTGTATTAATTCCGGCTTAAACCGTATCGGTGTGGTTACGCAATATGCCGCCCATTCTTTGTTGCGCCATTTGCAAAAAGGCTGGTCGTTCTTACCGCAGGAACGCGGCGAATTTATCGATATGTTGCCGGCGCGTCAGCAAATTGACGATTCCACCTGGTATCGCGGCACGGCGGACGCGGTGTATCAAAATATGGCGATTATCCGCAATCACTATAAACCGAAATACATCCTGATCTTAGCCGGTGACCATATTTACAAACAGGATTACAGCCAAATGCTGTTAGACCATGTGACCAGCGGGGCGAAATGTACCGTCGGCTGTATTGAAGTGCCGCGTTCCGAAGCCAGTGAATTCGGCGTTATGGCGGTAAATGAAAATCTGAAAGTCAAAGCCTTCGTGGAAAAACCGAAAGATCCGCCGGCAATGGCAGGCAGACCGGATACCTCATTGGCATCCATGGGGATTTATGTGTTTAACGCCGATTATCTCTATGAAATGCTGAATCGGGAAGTCAACACGCCTTGCACCTCTCACGACTTTGGTAAAGACGTATTGCCGAAATGTCTGGAAGAAGGCGCGTTATACGCTCACCCGTTCAGCCGCTCCTGCATGGGACGTAATACCGAAGGCGATATTTACTGGCGTGACGTAGGTACATTGGACAGCTTCTGGCAATCCAATATCGATTTGGTTTCCGAAAGTCCGCAATTCGATATTTACGACCAAACCTGGCCGATTCGTGGCAATCCGGTGCAAGCCTATCCATCTAAATTCTTTTATAAAAACACCAATATCAAACCGGTGGATAACTCTCTTATCGGTGGCGGCTGCGTGATTACCGATGCATCAATCAGTTATTCCGTGTTGTTTGACCGCATCAAAATTAACGAAGGCTCGCAAATCGATCATTCCGTGGTGTTACCGCAAGTGGAAATCGGGAAAAACTGCGTGTTAACACATTGTATTATCGATCGCCACTGTATTATCCCGGACGGTATGCATATCGATGTGGATAAAGAATTAGATCGCCAACGTTTCCGTGTCAGTTCCAGCGGTAAAGTGGTGTTGGTTACCCCTTCTATGTTGAAAAAATTAGAAGGGCGTGAAGTTGTCGATGAAGAGCACCTGGAT","","","49571","MKSSLSQLPNKYDLVKDTLVLILAGGRGSRLHELTDKRAKPALYFGGNRRIIDFALSNCINSGLNRIGVVTQYAAHSLLRHLQKGWSFLPQERGEFIDMLPARQQIDDSTWYRGTADAVYQNMAIIRNHYKPKYILILAGDHIYKQDYSQMLLDHVTSGAKCTVGCIEVPRSEASEFGVMAVNENLKVKAFVEKPKDPPAMAGRPDTSLASMGIYVFNADYLYEMLNREVNTPCTSHDFGKDVLPKCLEEGALYAHPFSRSCMGRNTEGDIYWRDVGTLDSFWQSNIDLVSESPQFDIYDQTWPIRGNPVQAYPSKFFYKNTNIKPVDNSLIGGGCVITDASISYSVLFDRIKINEGSQIDHSVVLPQVEIGKNCVLTHCIIDRHCIIPDGMHIDVDKELDRQRFRVSSSGKVVLVTPSMLKKLEGREVVDEEHLD","1424609","[PATHWAY] Glycogen biosynthesis; first step.","glucose-1-phosphate adenylyltransferase","Cytoplasm","","
InterPro
IPR005835
Domain
Nucleotidyl transferase
PF00483\"[19-292]TNTP_transferase
InterPro
IPR005836
Family
ADP-glucose pyrophosphorylase
PS00808\"[24-43]TADP_GLC_PYROPHOSPH_1
PS00809\"[111-119]TADP_GLC_PYROPHOSPH_2
PS00810\"[210-220]TADP_GLC_PYROPHOSPH_3
InterPro
IPR011831
Family
Glucose-1-phosphate adenylyltransferase
TIGR02091\"[18-396]TglgC: glucose-1-phosphate adenylyltransfera
noIPR
unintegrated
unintegrated
G3DSA:3.90.550.10\"[19-305]Tno description
PTHR22572\"[26-406]TSUGAR-1-PHOSPHATE GUANYL TRANSFERASE
PTHR22572:SF10\"[26-406]TGLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE


","BeTs to 9 clades of COG0448COG name: ADP-glucose pyrophosphorylaseFunctional Class: GThe phylogenetic pattern of COG0448 is --------vdrlbce-gh---j-i--Number of proteins in this genome belonging to this COG is","Significant hit (3.5e-127) to 9/9 blocks of the IPB001825 family, which is described as \"ADP-glucose pyrophosphorylase\". Interpro entry for IP:IPR001825. IPB001825A 22-75 8.1e-38 IPB001825B 95-104 0.011 IPB001825C 107-130 9.8e-11 IPB001825D 157-197 1.3e-20 IPB001825E 207-226 3.7e-08 IPB001825F 232-245 0.00069 IPB001825G 272-286 3.1e-09 IPB001825H 294-336 1.7e-16 IPB001825I 344-378 2e-06","Residues 37 to 91 match (4e-11) PD:PD150179 which is described as COMPLETE PROTEOME MEMBRANE EFFLUX SECRETION FUSION RESISTANCE MULTIDRUG PLASMID TRANSMEMBRANE ","","","","","","","","","","","Mon Jan 13 12:27:17 2003","Mon Jan 13 12:27:17 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02090 is paralogously related to AA02646 (5e-06).","","","","","","Residues 19 to 292 (E-value = 9.8e-76) place AA02090 in the NTP_transferase family which is described as Nucleotidyl transferase (PF00483)","","","","","Baecker,P.A., Furlong,C.E. and Preiss,J. Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli ADP-glucose synthetase as deduced from the nucleotide sequence of the glg C gene. J. Biol. Chem. 258 (8): 5084-5088 (1983) [PubMed: 6300111].Ghosh,P., Meyer,C., Remy,E., Peterson,D. and Preiss,J. Cloning, expression, and nucleotide sequence of glgC gene from an allosteric mutant of Escherichia coli B. Arch. Biochem. Biophys. 296 (1): 122-128 (1992) [PubMed: 1339262].Meyer,C.R., Ghosh,P., Nadler,S. and Preiss,J. Cloning, expression, and sequence of an allosteric mutant ADP glucose pyrophosphorylase from Escherichia coli B. Arch. Biochem. Biophys. 302 (1): 64-71 (1993) [PubMed: 8385906].Kumar,A., Ghosh,P., Lee,Y.M., Hill,M.A. and Preiss,J. Biosynthesis of bacterial glycogen. Determination of the amino acid changes that alter the regulatory properties of a mutant Escherichia coli ADP-glucose synthetase. J. Biol. Chem. 264 (18): 10464-10471 (1989) [PubMed: 2543670].Parsons,T.F. and Preiss,J. Biosynthesis of bacterial glycogen. Isolation and characterization of the pyridoxal-P allosteric activator site and the ADP-glucose-protected pyridoxal-P binding site of Escherichia coliB ADP-glucose synthase. J. Biol. Chem. 253 (21): 7638-7645 (1978) [PubMed: 359552].Kumar,A., Tanaka,T., Lee,Y.M. and Preiss,J. Biosynthesis of bacterial glycogen. Use of site-directed mutagenesis to probe the role of tyrosine 114 in the catalytic mechanism of ADP-glucose synthetase from Escherichia coli. J. Biol. Chem. 263 (29): 14634-14639 (1988) [PubMed: 2844780].Hill,M.A., Kaufmann,K., Otero,J. and Preiss,J. Biosynthesis of bacterial glycogen. Mutagenesis of a catalytic site residue of ADP-glucose pyrophosphorylase from Escherichia coli. J. Biol. Chem. 266 (19): 12455-12460 (1991) [PubMed: 1648099].","","Mon Jan 13 12:27:17 2003","1","","","" "AA02091","1424581","1424727","147","GTGAAGTTGTCGATGAAGAGCACCTGGATTAAAGTGCGGTCGTTTTTCACGATGATTTTTATTATGATGGTGTATGTTTTATTGTATGTGTCTAAAATAAAAGCGTTTATTATAGGCACACATCGAAAGACGCACCACTATCATTAT","","","5978","VKLSMKSTWIKVRSFFTMIFIMMVYVLLYVSKIKAFIIGTHRKTHHYHY","1424727","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-35]?signal-peptide
tmhmm\"[9-29]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:49:32 2004","Wed Feb 25 15:49:32 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02091 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:49:32 2004","","","","","","","","","","","","","1","","","" "AA02092","1424814","1426250","1437","ATGAAAGTATTACACGTTTGCTCGGAGTTATATCCTTTACTGAAAACCGGCGGGTTAGCCGATGTGATGGGCGCCTTGCCTTTTGCGCAGAAAGAAATCGGCATTGATACGCGAATTGTATTACCGGCATATCCTGCTATTGCAGCCGGTATTCCGCATACTTCCGTCGTGGCAGAATTTGATAATTTCGCCGGACACATTATTTTACGTTATGGTGAATACAACGGCATCGGCGTTTATTTGATTGACGCGCCGTATTTGTACGCACGCGAAGGTAATCCTTATCACGATGCCAATTACAACGATTACGGCGACAATTATAAACGCTTCGCCCTGTTGGGTTGGGTCGGTGCAGAACTGGCGATCGGTTTGGACAGCTGGTGGCGCGCAGAAGTGGTGCATGCCCACGACTGGCACGCCGGATTGACCGCCGCGTATTTATATCATAAAGGTCGCCCTGCCAAGTCGGTGTTCACCATTCATAATCTGGCGTATCAAGGTCCGTTTGATTATCGCCATTTATTTGAAATCGGTTTGCCGGCAGAAATGTTCCATGTGAACGGTTTGGAATTCTTCGGACAAATTTCTTATTTGAAAGCCGGTTTATATTATTCCGATGTGGTCACGGCGGTGAGCCCGACCTATGCGAAAGAAATTACCACGCCGGAATTTGCGTACGGTTTACAAGGTTTATTGTCCACTCTCGATCAAGAGGGTCGCTTGGTGGGTATCTTAAACGGGGTCGATGAAAAAATCTGGCACCCGAATTGCGATCAATACATTCAGCACGCGTATAAATTGAAATACATGGGCGGAAAAGGGAAAAATAAAGCGGATCTACAGGCTTATTTCAACTTACCGCAGCAATCTGATGCGCTGTTGTTTGTGATGGTCACCCGCTTAACGGAACAAAAAGGCGTGGATTTACTGTTGGAAAGCGCCGATGAAATCGTTAAACAAGGCGGGCAACTTGCGATTCTTGGCTCAGGCGCACCGCACTTGGAAGTGGGAATTCGCAAATTAGCGAAAGATTATCCGCAGAACGTTGCCGTGAAAATCGGCTACGATGAAGCGTTATCCCATTTAATGCTTGCCGGCGGGGATGTGATTTTAGTCCCAAGTCGTTTTGAGCCTTGCGGTTTAACCCAATTATACGGACTGAAATACGGCACATTACCATTAGTCCGCGCAACCGGTGGTTTGGCGGATACAGTGGTTAACGCTTCCGTCGAAAATATTCAAACGCGAACAGCAACAGGTTTTGTCTTTACACACGCAACAGCTGATGACTTACGTCATGCGTTGCAAGCGGCATTTGCTTTATGGAAAAAACAACGCTTATGGGCAAGTGTTCGCGTTATTGCAATGGAACAAGATTTCAGTTGGCAAATCTCTGCAACCCACTACCAATATTTATATCAACGAATTTTATCTAAG","","","53188","MKVLHVCSELYPLLKTGGLADVMGALPFAQKEIGIDTRIVLPAYPAIAAGIPHTSVVAEFDNFAGHIILRYGEYNGIGVYLIDAPYLYAREGNPYHDANYNDYGDNYKRFALLGWVGAELAIGLDSWWRAEVVHAHDWHAGLTAAYLYHKGRPAKSVFTIHNLAYQGPFDYRHLFEIGLPAEMFHVNGLEFFGQISYLKAGLYYSDVVTAVSPTYAKEITTPEFAYGLQGLLSTLDQEGRLVGILNGVDEKIWHPNCDQYIQHAYKLKYMGGKGKNKADLQAYFNLPQQSDALLFVMVTRLTEQKGVDLLLESADEIVKQGGQLAILGSGAPHLEVGIRKLAKDYPQNVAVKIGYDEALSHLMLAGGDVILVPSRFEPCGLTQLYGLKYGTLPLVRATGGLADTVVNASVENIQTRTATGFVFTHATADDLRHALQAAFALWKKQRLWASVRVIAMEQDFSWQISATHYQYLYQRILSK","1426250","[PATHWAY] Glycogen biosynthesis; second step.","glycogen synthase","Cytoplasm","","
InterPro
IPR001296
Domain
Glycosyl transferase, group 1
PF00534\"[280-455]TGlycos_transf_1
InterPro
IPR011835
Domain
Glycogen/starch synthases, ADP-glucose type
TIGR02095\"[1-476]TglgA: glycogen/starch synthases, ADP-glucos
InterPro
IPR013534
Domain
Starch synthase catalytic region
PF08323\"[2-234]TGlyco_transf_5
noIPR
unintegrated
unintegrated
PTHR12526\"[2-70]T\"[104-260]T\"[281-476]TGLYCOSYLTRANSFERASE
PTHR12526:SF17\"[2-70]T\"[104-260]T\"[281-476]TSTARCH SYNTHASE


","BeTs to 12 clades of COG0297COG name: Glycogen synthaseFunctional Class: GThe phylogenetic pattern of COG0297 is --m-k--qvd-lbcefgh---j-i--Number of proteins in this genome belonging to this COG is","","Residues 211 to 394 match (6e-08) PD:PD563764 which is described as STARCH SYNTHASE ","","","","","","","","","","","Mon Jan 13 12:29:25 2003","Mon Jan 13 12:29:25 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02092 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 280 to 455 (E-value = 2.7e-06) place AA02092 in the Glycos_transf_1 family which is described as Glycosyl transferases group 1 (PF00534)","","","","","Kumar,A., Larsen,C.E. and Preiss,J. Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli ADP-glucose:alpha-1,4-glucan,4-glucosyltransferase as deduced from the nucleotide sequence ofthe glgA gene. J. Biol. Chem. 261 (34): 16256-16259 (1986) [PubMed: 3097003].Baecker,P.A., Furlong,C.E. and Preiss,J. Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli ADP-glucose synthetase as deduced from thenucleotide sequence of the glg C gene. J. Biol. Chem. 258 (8): 5084-5088 (1983) [PubMed: 6300111].","","Mon Jan 13 12:29:25 2003","1","","","" "AA02094","1426376","1428838","2463","ATGATAATGGATAACTTCGATTCTCCATTCTTGTACGATCATCCCGAAATCAATGTGGCATCATTGAAGAAGGCGATCGTCTATAAACTGATTTTTCTTATCGGGCGCTCGCCTAAAGAGGCAAGTCAGCGCGATTGGTTAAACGCGACCTTATATGCAGTGCGTGATTTTGTGACGGAAGGTTGGATCACCACAGCCCGCCGAGCCAGAACGGAAGGTTCACGTCGCGTTTATTATTTATCCATGGAGTTTTTGATCGGTCGCACTTTGTCTAACGCCATGATTGCCGAAGGGCTTTATGAAGTCACCCGCGATGCGCTTTCCGAGCTTAATGTTGATTTGGAAGAAATTATTCAAAAGGAAGTGGACCCGGGTTTGGGGAACGGCGGTTTAGGTCGTTTGGCGGCTTGTTTTATGGATTCTATTGCAACGTTGGGCTTACCGGGCATGGGGTATGGTATTCGTTACGAATATGGAATGTTCCGGCAAAAAATTGAAGACGGTCAACAGGTAGAACGCCCGGATGCGTGGTTGGAAAAAGGTGCACCGTGGGAGTTTATTCGCCCGTCTAAACGTTTCACTATTCCTTTCGGCGGCAGCATTCACTTTGAAGACAAAAAATGTATTTGGGACATCGGTGAGCGCGTCGTAGCGTTGGCCTATGACCAAGTTATCCCGGGCTATCAAAATGATTCTGCAGCAACCTTACGTTTATGGGCGGCACACGCCGGTGAAATGTTCAATTTAGAAGATTTCAACCGTGGTCAACATATTGCGGCGATGGAAAGCCGTGCATCAATTAAAAACCTTTCCCGTGTGTTATATCCGGACGATTCCACCTGGAACGGTCGTGAATTGCGTTTACGTCAGGAATATTTCCTGGTTTCCGCGTCATTGCAAGACATTATTCGTCGTCATAAACGTACCCATAACACCATTGAAAATCTGGCGGAAAAAGTGGCGATTCACTTAAATGACACCCACCCGGCATTGGCGATTCCTGAATTAATGCGCATCTTAATCGATGAAGAAGGTTTCGCATGGCAAAAAGCCTGGGATATGACCCGTCGTATTTTCTCTTACACCTGCCACACCTTAATGTCCGAAGCATTGGAAACCTGGCCGGTAGAAATGATGGCGAAAATCCTGCCACGTCATTTACAAATGATTTTTGAAATTAACGATCACTTCCTCGAATATGTGAAAACCTACATCACTACCGATATGGATTTCATCCGTCGCGTATCTTTGGTGGAAGAAGGTGACCAACGTAAAGTGCGCATGGGCTGGTTGTCCGTAGTCGGTTCTCACAAAGTCAACGGTGTGGCGGCAATTCACTCCGATTTAATGGTAACCTCAACCTTTGCCGATTTTGCCCGTATTTATCCGGAACGATTCACTAACGTCACCAACGGTATTACTCCACGTCGTTGGTTAGCCGTAGCGAACCCGAAATTGGCATCGCTTTTTGATCAATATATCGGCAGCGATTGGCGTTGCGATTTAAGCCAAATTGCATTGCTGAAAGAACACGCCAATGAAGCCGAATTTAAACGTGCGATTGCCGACATTAAATTCGATAACAAAGTGCGTCTTGCCAATTACGTCAAAAAAGAATTGGGTATTGAACTTGACCCGCACGCCTTGTTTGATGTTCAGGTGAAACGTATTCACGAATATAAACGCCAAATTCTCAACGTGTTGCACATCATCGCACGTTACAACGAGATGTTGACGCACCCGGAAAAAGACTGGCAGCCGCGCGTCTTTATCTTAGCCGGTAAAGCCGCTTCCGCTTACTACGCGGCAAAACAAACTATTCATTTGATTAATGACGTTGCCAACGTGATTAATAACGATGTGCGTTTGCGCGGTCGCTTAAAAGTGGTATTCATTCCGAACTACAGCGTCAGTCTGGCGCAGTTAATCATTCCGGCGGCGGATATTTCCGAGCAAATTTCTCTGGCGGGTACGGAAGCCTCCGGTACCGGTAACATGAAGTTTGCCCTTAACGGCGCCTTAATATTAGGTACGTTGGACGGCGCAAACGTGGAAATTCTGGAAAATGTCGGTAAAGACAACATCTTCATTTTCGGTAACACCGTTGAGCAAGTAGCGCAGTTACGCCGTGACGGTTATCGTCCGTTTGATTATTATCAAAATGACGCGGAATTAAGAACGGTGGTTGATCAAATCATCAACGGCGCGTTCTCACCGAATGACCCGAATCGCTATCTGCAATTGTTACAGGGTCTCCAATATCACGACTATTATCAGGCATTCGCCGATTTCCGCAGTTATGTGGATATGCAAAAAGTGGTGGACGAGAAGTATAAAAATCGAGATGCGTGGATTGAAAGCACCATTCAAAACATCGTCAACATGGGCTATTTCTCCTCGGACCGGACGATTAAGGAATATGCGGAAAATATCTGGAATATTGAACCGCTAAAACCGGCAAAA","","","94233","MIMDNFDSPFLYDHPEINVASLKKAIVYKLIFLIGRSPKEASQRDWLNATLYAVRDFVTEGWITTARRARTEGSRRVYYLSMEFLIGRTLSNAMIAEGLYEVTRDALSELNVDLEEIIQKEVDPGLGNGGLGRLAACFMDSIATLGLPGMGYGIRYEYGMFRQKIEDGQQVERPDAWLEKGAPWEFIRPSKRFTIPFGGSIHFEDKKCIWDIGERVVALAYDQVIPGYQNDSAATLRLWAAHAGEMFNLEDFNRGQHIAAMESRASIKNLSRVLYPDDSTWNGRELRLRQEYFLVSASLQDIIRRHKRTHNTIENLAEKVAIHLNDTHPALAIPELMRILIDEEGFAWQKAWDMTRRIFSYTCHTLMSEALETWPVEMMAKILPRHLQMIFEINDHFLEYVKTYITTDMDFIRRVSLVEEGDQRKVRMGWLSVVGSHKVNGVAAIHSDLMVTSTFADFARIYPERFTNVTNGITPRRWLAVANPKLASLFDQYIGSDWRCDLSQIALLKEHANEAEFKRAIADIKFDNKVRLANYVKKELGIELDPHALFDVQVKRIHEYKRQILNVLHIIARYNEMLTHPEKDWQPRVFILAGKAASAYYAAKQTIHLINDVANVINNDVRLRGRLKVVFIPNYSVSLAQLIIPAADISEQISLAGTEASGTGNMKFALNGALILGTLDGANVEILENVGKDNIFIFGNTVEQVAQLRRDGYRPFDYYQNDAELRTVVDQIINGAFSPNDPNRYLQLLQGLQYHDYYQAFADFRSYVDMQKVVDEKYKNRDAWIESTIQNIVNMGYFSSDRTIKEYAENIWNIEPLKPAK","1428838","[FUNCTION] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. ","glycogen phosphorylase; glycogen synthase","Cytoplasm","","
InterPro
IPR000811
Family
Glycosyl transferase, family 35
PIRSF000460\"[17-819]TGlucan phosphorylase
PTHR11468\"[49-818]TGLYCOGEN PHOSPHORYLASE
PF00343\"[106-816]TPhosphorylase
PS00102\"[659-671]TPHOSPHORYLASE
InterPro
IPR011833
Family
Glycogen/starch/alpha-glucan phosphorylase
TIGR02093\"[18-814]TP_ylase: glycogen/starch/alpha-glucan phosp
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2000\"[18-502]Tno description


","BeTs to 13 clades of COG0058COG name: Glucan phosphorylaseFunctional Class: GThe phylogenetic pattern of COG0058 is --m-k-yq-drlbcefgh---j-i--Number of proteins in this genome belonging to this COG is","","Residues 7 to 63 match (8e-10) PD:PD584855 which is described as GLYCOGEN COMPLETE PHOSPHORYLASE PROTEOME TRANSFERASE GLYCOSYLTRANSFERASE METABOLISM PHOSPHATE CARBOHYDRATE PYRIDOXAL ","","","","","","","","","","","Mon Jan 13 12:35:17 2003","Mon Jan 13 12:35:17 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02094 is paralogously related to AA01982 (0.0).","","","","","","","","","","","Choi,Y.L., Kawamukai,M., Utsumi,R., Sakai,H. and Komano,T. Molecular cloning and sequencing of the glycogen phosphorylase gene from Escherichia coli. FEBS Lett. 243 (2): 193-198 (1989) [PubMed: 2645169].Yu,F., Jen,Y., Takeuchi,E., Inouye,M., Nakayama,H., Tagaya,M. and Fukui,T. Alpha-glucan phosphorylase from Escherichia coli. Cloning of the gene, and purification and characterization of the protein. J. Biol. Chem. 263 (27): 13706-13711 (1988) [PubMed: 3047129].Romeo,T., Kumar,A. and Preiss,J. Analysis of the Escherichia coli glycogen gene cluster suggeststhat catabolic enzymes are encoded among the biosynthetic genes. Gene 70 (2): 363-376 (1988)[PubMed: 2975249].Choi,Y.-L., Kawase,S., Kawamukai,M., Utsumi,R., Sakai,H. and Komano,T. Nucleotide sequence of the glycerol-3-phosphate dehydrogenase gene of Escherichia coli and regulation by the cAMP-CRP complex. Agric. Biol. Chem. 53, 1135-1143 (1989) Kumar,A., Larsen,C.E. and Preiss,J. Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli ADP-glucose:alpha-1,4-glucan,4-glucosyltransferase as deduced from the nucleotide sequence ofthe glgA gene. J. Biol. Chem. 261 (34): 16256-16259 (1986) [PubMed: 3097003].","","Mon Jan 13 12:35:17 2003","1","","","" "AA02096","1428894","1429016","123","ATGAAAAGTGCGGTTGAAATTTTCAGTGTTTTTGAAGTGAAAAGTGCATCAAAGACGACCGCACTTTTAGTTGGCGGGTTTTGTTTTGCGTGCTTTATACCATTTCCAGGCAACGAATATGAC","","","4434","MKSAVEIFSVFEVKSASKTTALLVGGFCFACFIPFPGNEYD","1429016","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
tmhmm\"[15-35]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:47:00 2004","Wed Feb 25 15:47:00 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02096 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:47:00 2004","","","","","","","","","","","","","1","","","" "AA02097","1429565","1428963","603","ATGGAATTTTTAATTAGCTTTTTTACCGATTACGGTTATTTCGCCGTTTTATTCGTGTTGATTATTTGTGGCTTTGGCGTGCCGATTCCGGAAGATATTACTTTAGTTTCCGGCGGTGTCATTTCAGGTTTGGGCTACGCCAATGTGCACGTTATGTTGCTGGTCAGCTTCTTCGGCGTGTTGTTGGGCGACAGCACCATGTATTGGTTGGGGCGTATTTATGGCGTGAAAATCTTACGCTTTCGCCCGATTCGCCGCTTCCTAACAGTAGAACGCTTACGTTTGGTTCGCAATAAATTTGATCAGTACGGCAACCGTGTATTATTTATCGCCCGCTTTCTGCCGGGATTACGCGCACCGATTTACATGGTTGCAGGCATTACCCGTCGTGTCAGTTTTATCCGCTTTCTTTTGTTGGATTTATTCGCTTCCATTATTTCCGTTCCGATTTGGGTATATTTAGGCGATTTCGGTGCCAGTAATCTGGATTGGTTGCACGAACAAATAAAAAAAGGACAGTCGGTGATTTATATTCTGGTTGCCGTTTTAGTCATATTCGTTGCCTGGAAATGGTATAAAGCACGCAAAACAAAACCCGCCAAC","","","23057","MEFLISFFTDYGYFAVLFVLIICGFGVPIPEDITLVSGGVISGLGYANVHVMLLVSFFGVLLGDSTMYWLGRIYGVKILRFRPIRRFLTVERLRLVRNKFDQYGNRVLFIARFLPGLRAPIYMVAGITRRVSFIRFLLLDLFASIISVPIWVYLGDFGASNLDWLHEQIKKGQSVIYILVAVLVIFVAWKWYKARKTKPAN","1428963","","DedA-family integral membrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR015414
Domain
SNARE associated Golgi protein
PF09335\"[29-157]TSNARE_assoc
noIPR
unintegrated
unintegrated
signalp\"[1-26]?signal-peptide
tmhmm\"[10-30]?\"[44-62]?\"[137-155]?\"[174-192]?transmembrane_regions


","BeTs to 14 clades of COG0586COG name: Uncharacterized membrane-associated proteinFunctional Class: SThe phylogenetic pattern of COG0586 is ---p-----drlbcefghsnuj--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 2.3e-07) to 3/3 blocks of the IPB000252 family, which is described as \"DedA family\". Interpro entry for IP:IPR000252. IPB000252A 3-12 16 IPB000252B 68-75 0.038 IPB000252C 104-113 0.13","Residues 100 to 155 match (5e-12) PD:PD002864 which is described as COMPLETE PROTEOME DEDA MEMBRANE TRANSMEMBRANE ALKALINE PHOSPHATASE INTEGRAL PROTEIN FAMILY ","","","","","","","","","","","","Mon Jan 13 12:38:38 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02097 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 14 to 173 (E-value = 3.3e-49) place AA02097 in the DedA family which is described as DedA family (PF00597)","","","","","","","","1","","","" "AA02099","1429779","1430063","285","ATGGCATTTAAATTTAACGCTGAAGTTCGTACGGCGCAAGGTAAGGGTGCGAGCCGCCGCCTGCGTCATAACGGTCAAATTCCTGCTATCGTTTACGGTGGTAGTGAAGCGCCGGTTTCCATCATTTTAAATCATGATGATGTAAACAATGCACAAGTGCACGATACTTTCTATTCCGACGTGATTACGCTAGTGATTGATGAAAAAGAAGTGGCCGTGAAAGTGCAGGCAATGCAACGTCACCCGTTCAAACCAAAATTGGTTCACATTGACTTCAAACGTGTT","","","10663","MAFKFNAEVRTAQGKGASRRLRHNGQIPAIVYGGSEAPVSIILNHDDVNNAQVHDTFYSDVITLVIDEKEVAVKVQAMQRHPFKPKLVHIDFKRV","1430063","[FUNCTION] Binds to the 5S rRNA.","50S ribosomal protein L25","Cytoplasm","","
InterPro
IPR001021
Family
Ribosomal protein L25
PD012503\"[4-95]TQ9CN10_PASMU_Q9CN10;
PF01386\"[5-92]TRibosomal_L25p
noIPR
unintegrated
unintegrated
G3DSA:2.40.240.10\"[2-95]Tno description


","BeTs to 13 clades of COG1825COG name: Ribosomal protein L25 (general stress protein Ctc)Functional Class: JThe phylogenetic pattern of COG1825 is -------qvdr-bcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 8.2e-34) to 2/2 blocks of the IPB001021 family, which is described as \"Ribosomal protein L25\". Interpro entry for IP:IPR001021. IPB001021A 10-32 1.4e-15 IPB001021B 61-92 7.6e-17","Residues 4 to 95 match (6e-40) PD:PD012503 which is described as RIBOSOMAL PROTEOME COMPLETE L25 50S RRNA-BINDING PROBABLE SUBUNIT CTC STRESS ","","","","","","","","","","","Mon Jan 13 12:58:48 2003","Mon Jan 13 12:58:48 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02099 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 92 (E-value = 4.8e-50) place AA02099 in the Ribosomal_L25p family which is described as Ribosomal L25p family (PF01386)","","","","","Uemura,Y., Isono,S. and Isono,K. Cloning, characterization, and physical location of the rplY gene which encodes ribosomal protein L25 in Escherichia coli K12. Mol. Gen. Genet. 226(1-2): 341-344.1991 PubMed: 2034228. Dovgas,N.V., Markova,L.F., Mednikova,T.A., Vinokurov,L.M.,Alakhov,Y.B. and Ovhinnikov,Y.A. The primary structure of the 5S RNA binding protein L25 from Escherichia coli ribosomes. FEBS Lett. 53(3): 351-354 1975. PubMed: 1093874. Bitar,K.G. and Wittmann-Liebold,B. The primary structure of the 5s rRNA binding protein L25 of Escherichia coli ribosomes. Hoppe-Seyler\"s Z. Physiol. Chem. 356(9): 1343-1352. 1975. PubMed: 1100506. Stoldt,M., Wohnert,J., Gorlach,M. and Brown,L.R. The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases. EMBO J. 17(21): 6377-6384. 1998. PubMed: 9799245.","","Mon Jan 13 12:58:48 2003","1","","","" "AA02100","1430214","1430819","606","ATGAACAAATTTACTAAAATCAGTGCAACTGCTTTATTTGCTCTTTTCTTGACTGCTTGTGATAAACCGGTAGACAAAGCGCCGGATGCAAAACCGGAAGCGGCAGCCCAAACACAATCAGCACCGGCGACTGCCGAAGCGGCAAAAGCCGATGAGACGGCTGATTATAAAAAATTAGTAGATTGGAACAAATCTCAAGAACAAACCCAGCTTCAAGCACAACAAAAATTCCAGCAGGATTTAGTTGCTGCAGTGCAAGCGAAAGATGATAAGAAAGTTCAAGAAGCTATTGATGTTTTCAATAAATCCGTACAAGACACCATCGCCAGTTTAGATGCGTTGAATATCAGTTCCGATTCTGTGAAGGCGGTGAAAGAACAAACCAAAAACGTACTTGGTTTAGCCAGCAACTTATTGGTTGAACAAGCAAATGTAAGTTTAGCGAACCCGACACCGGAACAACAGAAAACTTACATGGAAAAAGCAGAAAAATTAAGAGATGCGATGTTAGAGCTACAAAAACAAAGCGTCGCTTTAGAACAAAAATTTAATCCTGCTCCGGCTGCACCTACAGCAGAACCTGCAGCGCCGGCTCAAGAATCTAAA","","","24033","MNKFTKISATALFALFLTACDKPVDKAPDAKPEAAAQTQSAPATAEAAKADETADYKKLVDWNKSQEQTQLQAQQKFQQDLVAAVQAKDDKKVQEAIDVFNKSVQDTIASLDALNISSDSVKAVKEQTKNVLGLASNLLVEQANVSLANPTPEQQKTYMEKAEKLRDAMLELQKQSVALEQKFNPAPAAPTAEPAAPAQESK","1430819","","lipoprotein","Periplasm, Inner membrane","","
noIPR
unintegrated
unintegrated
PS51257\"[1-20]TPROKAR_LIPOPROTEIN
signalp\"[1-20]?signal-peptide


","No hits to the COGs database.","","Residues 56 to 183 match (8e-07) PD:PD332359 which is described as PROTEOME COMPLETE LIPOPROTEIN P27 HLP HLPB PM1077 PM1805 ","","","","","","","","","","","","Mon Jan 13 13:00:27 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02100 is paralogously related to AA02511 (6e-06).","","","","","","","","","","","","","","1","","","" "AA02101","1430970","1431248","279","ATGTTAAAAAATGTTTTTCCTTTGTTGATTCTGTTGCCTGCTGTTGCCATAGCGCAGTCTTATGTGGTGTATGATTTTACCCATAATAAAGTATTGGAAAGCGGTGCACCGAATACCGTGCGTCCTATCGCTTCCGTCACCAAACTGATGACAGCAAAAGTATTTCTGGAACACAACAAAAACCCCCGCTATACTGCTTCCATTACTGATGATGATTTTGACTACATTAAAGGCACGCACACCAAATTAAATATACGCCGATTTCTTGCCGTGAATTGC","","","10477","MLKNVFPLLILLPAVAIAQSYVVYDFTHNKVLESGAPNTVRPIASVTKLMTAKVFLEHNKNPRYTASITDDDFDYIKGTHTKLNIRRFLAVNC","1431248","[FUNCTION] Cell wall formation. May play a specialized role in remodeling the cell wall. Specifically hydrolyse the DD-diaminopimelate-alanine bonds in high-molecular-mass murein sacculi (by similarity). ","penicillin-binding protein 7","Periplasm, Cytoplasm","","
InterPro
IPR001967
Family
Peptidase S11, D-alanyl-D-alanine carboxypeptidase A
PF00768\"[18-57]TPeptidase_S11
noIPR
unintegrated
unintegrated
G3DSA:3.40.710.10\"[18-92]Tno description
signalp\"[1-18]?signal-peptide
tmhmm\"[5-23]?transmembrane_regions


","BeTs to 7 clades of COG1686COG name: D-alanyl-D-alanine carboxypeptidaseFunctional Class: MThe phylogenetic pattern of COG1686 is ----------rlb-efghsn-jxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 3e-05) to 1/3 blocks of the PR00725 family, which is described as \"D-Ala-D-Ala carboxypeptidase 1 (S11) family signature\". Prints database entry for PR:PR00725. PR00725A 44-55 3.5e-05","Residues 19 to 83 match (5e-18) PD:PD455514 which is described as PENICILLIN-BINDING PROTEOME PEPTIDOGLYCAN COMPLETE SYNTHESIS PERIPLASMIC HOMOLOG D-ALANYL-D- ALANINE-ENDOPEPTIDASE SIGNAL ","","","","","","","","","","","Mon Jan 13 13:03:07 2003","Mon Jan 13 13:03:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02101 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02103","1431245","1431844","600","TTGCTGAAAATGATGTTGGTGCATTCCGATAATTATGCCGCTCACGCCTTGTCCCGCTCCGCCGGTATGACACGCTTACAATTTATCGGCAAAATGAATGAAAAAGCCAGACAATTGGGGATGAAATCCACCCGTTTTAGCGACAGTTCGGGTTTGTCTAACCATAACGTATCCAGCGTGATGGACTTGGTGAAACTTACCAAATATTCCATGAAAAAAACGGAAATCAAGGCATTTTCCAACATTTCCTCCACGTATGTGAAAGCCGGGAAACGCAATGTGTTTGTGAAAAATACCAACAAATTGGTGCGTGATGAAATGTTCAGTGCGGCAATCAATAAAACCGGCTACATTCGCGAATCGGGCTACAATCTGGTGTTCGTCAATAAAGTGCCTTGCAATAATCGTGCCACCATCGGCGTGATTAGCCTGAATAACAGTTCTTCGGCATATCGCTCCAGTTTCACCAAAAATAAATTGGAAAAATATGGTTGTACCGCGTTAAACAGCAAGGTGCTGCGAGACTTTGTGGATGATATGCAGTATGAAGAGGGCTATGATGAAGCCGGAATGGACGAATTAATCCGAAAAGTGGCGGGC","","","22376","LLKMMLVHSDNYAAHALSRSAGMTRLQFIGKMNEKARQLGMKSTRFSDSSGLSNHNVSSVMDLVKLTKYSMKKTEIKAFSNISSTYVKAGKRNVFVKNTNKLVRDEMFSAAINKTGYIRESGYNLVFVNKVPCNNRATIGVISLNNSSSAYRSSFTKNKLEKYGCTALNSKVLRDFVDDMQYEEGYDEAGMDELIRKVAG","1431844","[FUNCTION] Cell wall formation.","D-alanyl-D-alanine-endopeptidase; penicillin-binding protein 7","Periplasm, Outer membrane, Extracellular","","
InterPro
IPR001967
Family
Peptidase S11, D-alanyl-D-alanine carboxypeptidase A
PR00725\"[1-18]T\"[28-41]TDADACBPTASE1
PF00768\"[1-127]TPeptidase_S11
noIPR
unintegrated
unintegrated
G3DSA:3.40.710.10\"[1-167]Tno description
PTHR21581\"[1-130]TD-ALANYL-D-ALANINE CARBOXYPEPTIDASE


","BeTs to 11 clades of COG1686COG name: D-alanyl-D-alanine carboxypeptidaseFunctional Class: MThe phylogenetic pattern of COG1686 is ----------rlb-efghsn-jxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-15) to 2/3 blocks of the PR00725 family, which is described as \"D-Ala-D-Ala carboxypeptidase 1 (S11) family signature\". Prints database entry for PR:PR00725. PR00725B 1-18 3.7e-07 PR00725C 28-41 1e-06","Residues 5 to 68 match (9e-20) PD:PD003024 which is described as CARBOXYPEPTIDASE COMPLETE PROTEOME D-ALANYL-D-ALANINE PENICILLIN-BINDING HYDROLASE PRECURSOR PEPTIDOGLYCAN CELL SYNTHESIS ","","","","","","","","","","","Mon Jan 13 13:07:31 2003","Mon Jan 13 13:07:31 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02103 is paralogously related to AA00254 (1e-07).","","","","","","","","","","","","","","1","","","" "AA02105","1432025","1433350","1326","ATGCTTGAAACATCACAAACAATCCCCGAACTGGTTTCATGGGCGAAAGAACGCGAATTTTCGCTGAATTTACCCACCGATCGTCTGGCGTTTTTATTGGCAATTGCCATTTATAATAACGAACGTTTTGACGGTGAAATGATCGAATCGGATCTGGTGGACATTTTTCGCCACGTTTCCGGCGCCTTTGACCAATCCCAGGAAACCATTGCTACCCGCGCCAATAACGCCATTAACGAATTGGTAAAACAACGCTTTCTTAACCGCTTCAGCAGTGAATTTACCGAAGGTTTGGCGATTTATCGCTTAACCCCGCTGGGTGTCGGCGTCTCCGATTACTACATTCGTCAACGCGAATTTTCCGCCTTGCGCCTTTCCGTTCAGCTTTCCATTGTCGCCGATGAAATTCAACGTGCCTCTGACGCCGCCGAAGAAGATGGCGACGAACATTATTGGCGTCGTAACGTCTTTGCGCCGTTAAAATATTCCGTGGCAGAAATTTTCGACAGCATCGACTTATCGCAACGTATTATGGACGAAAACCAGCAGATCATTAAGGACGAAATTGCCGGTTTATTAACCAAAGATTGGCAGGCGGCGATTTCCAGTTGTGAACAATTATTAGACGAAACCTCAGGCAATTTACGGGAACTACAAGATACCCTTAACGCCGCCGGCGACAAATTGCAGGCGCAATTATTGCGGATTCAGGACTGCGTTATCGGGCGCGGTGAACTGTATTTTATTGATGAGCTGATCACCAATTTACAAACAAAACTAGACCGCATTATCAGTTGGGGACAACAAGCCATTGATTTGTGGATCGGCTATGACCGCCATGTGCACAAGTTTATCCGTACCGCCATTGATATGGATAAAAATCGGGTTTTCTCCCAGCGTTTACGCAATTCCATTCACAATTATTTCGATCACCCATGGTTCTTATGGGCGGCTCAGGCAGAGCGTTTGGTCGATTTACGCGACGAGGAATTAACCCTACGTGAAGAAGATGCGCTGGGTGAATTACCGAAAGAGTTGCAATACGAATCTTTGGCAGATATTCGCGAGCAAATTGTGGAACATATGCAAACCTTGCTCATTGACTATCGTGAACATCAACGTCCGATTAATTTGAGTATGGTATTAAAACAACAACTGGAAAGCTATCCGCTGTCACAACATTTTGATGTGGCGCGAATTATCGTGGATCAGGCGGTACGTCTGGGTATGGCAAGCGATGATTTAAGCGGTATTTATCCGATTTGGGAAAGCATTAACAAACGCGGCGCAGAAGTCCAGGCGAACGTCATTGATGAATATAAAAGC","","","51194","MLETSQTIPELVSWAKEREFSLNLPTDRLAFLLAIAIYNNERFDGEMIESDLVDIFRHVSGAFDQSQETIATRANNAINELVKQRFLNRFSSEFTEGLAIYRLTPLGVGVSDYYIRQREFSALRLSVQLSIVADEIQRASDAAEEDGDEHYWRRNVFAPLKYSVAEIFDSIDLSQRIMDENQQIIKDEIAGLLTKDWQAAISSCEQLLDETSGNLRELQDTLNAAGDKLQAQLLRIQDCVIGRGELYFIDELITNLQTKLDRIISWGQQAIDLWIGYDRHVHKFIRTAIDMDKNRVFSQRLRNSIHNYFDHPWFLWAAQAERLVDLRDEELTLREEDALGELPKELQYESLADIREQIVEHMQTLLIDYREHQRPINLSMVLKQQLESYPLSQHFDVARIIVDQAVRLGMASDDLSGIYPIWESINKRGAEVQANVIDEYKS","1433350","[FUNCTION] Killing factor; cause inhibition of protein biosynthesis and killing of cells (by similarity). ","killing protein","Cytoplasm","","
InterPro
IPR005582
Family
Prokaryotic chromosome segregation and condensation protein MukF
PF03882\"[1-440]TKicB
noIPR
unintegrated
unintegrated
PD025185\"[1-440]TMUKF_HAEIN_P45185;


","No hits to the COGs database.","","Residues 1 to 440 match (2e-199) PD:PD025185 which is described as COMPLETE PROTEOME MUKF KILLING KICB FACTOR HOMOLOG ","","","","","","","","","","","Mon Jan 13 13:11:39 2003","Mon Jan 13 13:11:39 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02105 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Feng,J., Yamanaka,K., Niki,H., Ogura,T. and Hiraga,S. New killing system controlled by two genes located immediately upstream of the mukB gene in Escherichia coli. Mol. Gen. Genet. 243(2): 136-147, 1994. PubMed: 7513784. Yamazoe M, Onogi T, Sunako Y, Niki H, Yamanaka K, IchimuraT, Hiraga S. Complex formation of MukB, MukE and MukF proteins involved in chromosome partitioning in Escherichia coli. EMBO J. 1999 Nov 1;18(21):5873-84. PMID: 10545099 Yamanaka K, Ogura T, Niki H, Hiraga S. Identification of two new genes, mukE and mukF, involved in chromosome partitioning in Escherichia coli. Mol Gen Genet. 1996 Feb 25;250(3):241-51. PMID: 8602138","","Mon Jan 13 13:11:39 2003","1","","","" "AA02106","1433381","1433515","135","ATGAACGACAAAACACTTAAAATTTTATTCACAATCTCACTTGTTCGCTTGTGCACCCCTTACGGGGCCGTCGGCAAAGCCGACGTTCAAAATCCGCTGGATTTTGTCACCACACTTTTGGCAGCAAGAACAAAT","","","4906","MNDKTLKILFTISLVRLCTPYGAVGKADVQNPLDFVTTLLAARTN","1433515","","hypothetical protein","Cytoplasm","There are no significant matches to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-25]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:44:06 2004","Wed Feb 25 15:44:06 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA1800 , and to AA1436.AA02106 is paralogously related to AA02736 (2e-06), AA02219 (5e-05) and AA01953 (1e-04).","Wed Feb 25 15:44:06 2004","","","","","","","","","","","","","1","","","" "AA02108","1433533","1436703","3171","ATGAAAGAATTACTTAAAATCCGCGGCTTTTTACCTTATCTCGCCATCGCGTTTTTAAATGCGGGCGTGGATTTGGCGCATAAAATTAATATTCAAAACGTGCTGTTAAAAAGTTTCGACGGCGATACGTTAGTAGTGCTGACGGCTTTAGTCAACGCCATGATTTTGTTGCCTTTCGTGTTTTTATTTTCGCCCGCCGGTTTTATTAACGATAAATATTCCCAAACAAAAGTCATTCGCTATGCCGCTACTGCCAGCGTGTTAATTTCCTTTGCGATTTTCCTCAGCTACTTTTTCGGTGCATTTGAGCTTGCTTTCCTGTTGACCTTGATTCTGGCGGCGCAAAGTGCGGTCTATTCTCCCGCCAAATATGGGATTATCAAATCTATTGTGGGTACGGAAAATCTGGGCGCCGCCAACGGTATTATCCAAGCCTTAACCATCGTGGCGATTTTATTCAGTTCCTTTGCCTTCTCTTATCTTTTTGAAGCCATTTATGTGGCAAGCAACAACCCGGCGGATATACTTTCCAGTATTTATGTGATCGGTTTCTTAATGTTGATTTTCAGCGCATTTGAAGTCATTTTCGCCTTTAGATTGCCTTATTTTCCACCGGCAGAAAGTGAAGAAAAAACACATTTCAGCAGCAAAAAATATTTTTCTTTAAGCTACTTAAGAGAAAACATGAAATTAGTTCGCGCCGATAAGAATATTTTGCTCAGCATTGTCGGATTAAGCATTTTCTGGGGCGTATCACAGGTGATTGTGGCGGCATTTCCGGCACATTACAAAATGCTGTTTAACGATGATAACGCGTTAATCATTCAGATGATTTTAGCCGTCAGCGGCATCGGTTTAATTGTCGGCTCCTACATTGCGGGCGCCATGTCCAAACACCACATTGAATTAGGCATTGTTCCCCTCGGTGCGCTAGGTTTGTTTGTTTCCTTATTTTTCTTAGCGCCATCTACGAATGTAACATTGATTAGCTTCTGTTCTTTCTGTTTCGGTTTATTCGGCGGATTATTTATCGTGCCGTTAAACGCTACCATTCAGTTCTTCGCACCGGAAGCCAAAATGGGGAAAATTATCGCCGGCAATAACTTCATCCAAAACATCGCCATGATCGGCTTTTTGTTGTTAAGTATCGCCTTTGTTTACGCGGATATTTCCACCACAGGCTTATTTATTTTTGTTTCTGTGGTCTGTTTTGTCGGTTCCTTATATGCCATTTTGCAATTGCCGCATTTATTCACCCGCTTATTTTTATTACTTTTCCTAAAAACCGGCTACCGCTTCCATGTGGAAGGCTTAAAAAATTTACCGCAACGTGGCGGTGTATTGTTATTAGGCAATCATATCAGCTGGATCGACTGGTTAGTGCTACAAGCCGCCAGCCCGCGCGCCATTAAATTCGTGATGTATCGCGGTATTTACAACAAATGGTATCTCACCTGGATTTTCAAATTCTTCAAGGTAATTCCTATCGGTGTAGGTTCCAGCAAAGAAAGTATCGAAGCCATTCGTCAATATTTGGAAAATGGCGAAGTGGTGGCGCTTTTCCCGGAAGGGCATATCAGCTATAACGGACAAATTAACGAATTTCAACGTGGCTACGAATTAAGTATTAAAGAGTGGCAAGACGTGTGCGTTGTGCCGTTTTATTTGCGTGGTTTATGGGGTTCCAGCTTCTCCCGTGCGGACGAGCATTATAAAGAACTCACCAAGCAACGCGGTAAACGTGACATTATCGTGGCATTCGGCAAACCGATTCGTGAGTTTATCGATCATGTTGCCATGAAACAAAAAGTGGTGGAGTTATCTTTCTCTTCTTGGGAAAGCTTTATTTCCCGTCAACAGCCGTTGACCTATTCTTGGCTGGAAATGGCAAAAAGCAATTTATTCCGCGAATGTGTTGCCGACAGCATGGGGACGGAATTAACCAATGCAAAATTTATCAGTGCTGTGTTGGTTTTCAGCAAACTGTTTAAACAAACCCTGAACAACGAGAAAAATATCGGTGTGTTACTGCCAAGCTCCGCCATGGGTGCCATTGTCAATATGGCGTTATTTGTGAACGGTAAAGTGCCGGTGAATCTGAATTACACCTTAAGCGAACAAAGTATGGCGTTGGCGCTGAAAAAAGCCAATATTCAACAGGTGATTACGTCCGAAAAATTCCTCGCGAAATTAAGCGGTAAAGGTTTTGATTATCAGGCGTTGTTAGCCGACAAAGCCGTGATGATGGAAACATTGGGCAAGTCTGTGAGCAAAACACAAAAAACGCTGGCATTTTTGACCGCACTTTTTGTCCCGGCAGGCTGGATTAAATTACTGAATTTTGCCGATGTAAGTTTAGACGACACCGCAACCATCTTATTCAGTAGCGGCAGTGAAGGGGAGCCGAAAGGTATTGAATTAACCAATAAAAATCTATTAACCAACATTCGCCAAATCAGCGATTTGTTGAATTTCAGAAAAGACGATGTGATTTTAAACTCGTTACCGATTTTCCATTCTTTCGGTTTAACCGTGACAACGTTACTTCCGTTATGTGAAGGGGTAAAAATGGTGAGCGTACCGGACCCGACAGACGGTGCTGCAGTAGGGAAAATGGCAGCGCGCCATAATGCCAGCATTTTGTTCGGCACTTCAACCTTCTTCCGTCTATACAATCGAAATAAAAAATTGCATCCGTTAATGTTCCAGAATATCCGCATGGTGGTTGCCGGCGCGGAAAAACTGAAAGCCGATGTGAAAGAAGCGTTCCGCTTGAAATTCGGTTTAGACATTTACGAAGGCTACGGCACTACGGAAACCGCGCCGGTTGCAGCGGTGAATATGCCGAATATTTTGGAAAAAGAAACGTTAAAAGAGCTGACGTTTAACAAACAGGGCTCTGTCGGGATGCCGTTGCCGGGGACGATTATTAAAATTGTGGATCCGGAAACCTTGCAGGAATTAGCAACGGGAGAAGACGGGCTAATTTTAATCGGCGGCGGACAAGTGATGAAAGGCTACTTAAACGATGCCGAAAAAACCGCTGACGTCATTGCCGAAATTGACGACGTGCGTTATTACAAAACGGGTGATAAAGGGGGCATATTGATGAGAACGGTTTTATTACTATCGTTGACCGTTATTCCCGCTTTGCGAAAGTCGGTGGCGAAA","","","116884","MKELLKIRGFLPYLAIAFLNAGVDLAHKINIQNVLLKSFDGDTLVVLTALVNAMILLPFVFLFSPAGFINDKYSQTKVIRYAATASVLISFAIFLSYFFGAFELAFLLTLILAAQSAVYSPAKYGIIKSIVGTENLGAANGIIQALTIVAILFSSFAFSYLFEAIYVASNNPADILSSIYVIGFLMLIFSAFEVIFAFRLPYFPPAESEEKTHFSSKKYFSLSYLRENMKLVRADKNILLSIVGLSIFWGVSQVIVAAFPAHYKMLFNDDNALIIQMILAVSGIGLIVGSYIAGAMSKHHIELGIVPLGALGLFVSLFFLAPSTNVTLISFCSFCFGLFGGLFIVPLNATIQFFAPEAKMGKIIAGNNFIQNIAMIGFLLLSIAFVYADISTTGLFIFVSVVCFVGSLYAILQLPHLFTRLFLLLFLKTGYRFHVEGLKNLPQRGGVLLLGNHISWIDWLVLQAASPRAIKFVMYRGIYNKWYLTWIFKFFKVIPIGVGSSKESIEAIRQYLENGEVVALFPEGHISYNGQINEFQRGYELSIKEWQDVCVVPFYLRGLWGSSFSRADEHYKELTKQRGKRDIIVAFGKPIREFIDHVAMKQKVVELSFSSWESFISRQQPLTYSWLEMAKSNLFRECVADSMGTELTNAKFISAVLVFSKLFKQTLNNEKNIGVLLPSSAMGAIVNMALFVNGKVPVNLNYTLSEQSMALALKKANIQQVITSEKFLAKLSGKGFDYQALLADKAVMMETLGKSVSKTQKTLAFLTALFVPAGWIKLLNFADVSLDDTATILFSSGSEGEPKGIELTNKNLLTNIRQISDLLNFRKDDVILNSLPIFHSFGLTVTTLLPLCEGVKMVSVPDPTDGAAVGKMAARHNASILFGTSTFFRLYNRNKKLHPLMFQNIRMVVAGAEKLKADVKEAFRLKFGLDIYEGYGTTETAPVAAVNMPNILEKETLKELTFNKQGSVGMPLPGTIIKIVDPETLQELATGEDGLILIGGGQVMKGYLNDAEKTADVIAEIDDVRYYKTGDKGGILMRTVLLLSLTVIPALRKSVAK","1436703","[FUNCTION] Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-acp intermediate in the presence of ATP and Mg(2+). its physiological function is to regenerate ptdetn from 2-acyl-gpe formed by transacylation reactions or degradation by phospholipase A1. ","2-acylglycerophosphoethanolamine acyltransferase; acyl-acyl carrier protein synthetase","Inner membrane, Cytoplasm","","
InterPro
IPR000873
Domain
AMP-dependent synthetase and ligase
PR00154\"[787-798]T\"[799-807]TAMPBINDING
PF00501\"[673-1033]TAMP-binding
PS00455\"[792-803]TAMP_BINDING
InterPro
IPR002123
Domain
Phospholipid/glycerol acyltransferase
PF01553\"[432-557]TAcyltransferase
SM00563\"[447-559]TPlsC
InterPro
IPR011701
Family
Major facilitator superfamily MFS_1
PF07690\"[13-387]TMFS_1
noIPR
unintegrated
unintegrated
G3DSA:2.30.38.10\"[965-1044]Tno description
G3DSA:3.40.50.980\"[785-945]Tno description
PTHR11968\"[656-1031]TATP-DEPENDENT AMP-BINDING ENZYME FAMILY MEMBER
PTHR11968:SF19\"[656-1031]TACYLGLYCEROPHOSPHOETHANOLAMINE ACYLTRANSFERASE
signalp\"[1-26]?signal-peptide
tmhmm\"[9-27]?\"[43-63]?\"[78-98]?\"[104-122]?\"[142-162]?\"[176-198]?\"[239-259]?\"[273-293]?\"[303-321]?\"[327-347]?\"[368-388]?\"[392-412]?\"[674-694]?transmembrane_regions


","BeTs to 17 clades of COG0318COG name: Acyl-CoA synthetases (AMP-forming)/AMP-acid ligases IIFunctional Class: I,QThe phylogenetic pattern of COG0318 is aomp-zy--drlbcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 5.7e-06) to 2/2 blocks of the IPB000873 family, which is described as \"AMP-dependent synthetase and ligase\". Interpro entry for IP:IPR000873. IPB000873A 794-809 0.0068 IPB000873B 829-839 0.4Significant hit ( 3.4e-05) to 2/2 blocks of the IPB002123 family, which is described as \"Phospholipid and glycerol acyltransferase (from 'motifs_6.msf')\". Interpro entry for IP:IPR002123. IPB002123A 443-458 0.00035 IPB002123B 518-526 48","Residues 278 to 404 match (1e-07) PD:PD332778 which is described as PROTEOME COMPLETE EFFLUX TC0009 CP0009 ","","","","","","","","","","","Mon Jan 13 13:18:32 2003","Mon Jan 13 13:18:32 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02108 is paralogously related to AA02598 (1e-27), AA00231 (7e-16), AA02512 (2e-08), AA01191 (1e-07) and AA01193 (2e-07).","","","","","","Residues 648 to 1056 (E-value = 5.9e-51) place AA02108 in the AMP-binding family which is described as AMP-binding enzyme (PF00501)","","","","","Jackowski,S., Jackson,P.D. and Rock,C.O. Sequence and function of the aas gene in Escherichia coli . J. Biol. Chem. 269 (4): 2921-2928 (1994) [PubMed: 8300626].","","Mon Jan 13 13:18:32 2003","1","","","" "AA02109","1436703","1436993","291","ATGATTAGTTTAGGCAGTGTAGAAGAACAAATTGCACAGGTTTTGAATGGCGATGTGCAATTTACCGCTGCAAATGTGCCGGATGATAAAAAAGGTGAAGCGGTGGTGCTTTTAGTGAAAACCGAATCGGATATTAATGAGGTCGTCAATATGTTGAAAAATTCAGCCATACCACCGTTAATGCAGCCGTCTTTTGTCTTTAAAGTAGATGAAATTCCGACCTTGGCAAGTGGTAAAGTCGATTTCAAAGGGGCGAAAAAACTCGCCGTCGCATTAGTGCAAAATAACGAA","","","10379","MISLGSVEEQIAQVLNGDVQFTAANVPDDKKGEAVVLLVKTESDINEVVNMLKNSAIPPLMQPSFVFKVDEIPTLASGKVDFKGAKKLAVALVQNNE","1436993","[FUNCTION] Plays a role in lysophospholipid acylation.Transfers fatty acids to the 1-position via an enzyme-boundacyl-acp intermediate in the presence of ATP and Mg(2+).its physiological function is to regenerate ptdetn from2-acyl-gpe formed by transacylation reactions ordegradation by phospholipase A1. ","2-acylglycerophosphoethanolamine acyltransferase; acyl-acyl carrier protein synthetase","Periplasm, Extracellular","","
noIPR
unintegrated
unintegrated
PTHR11968\"[1-97]TATP-DEPENDENT AMP-BINDING ENZYME FAMILY MEMBER
PTHR11968:SF19\"[1-97]TACYLGLYCEROPHOSPHOETHANOLAMINE ACYLTRANSFERASE


","BeTs to 10 clades of COG0318COG name: Acyl-CoA synthetases (AMP-forming)/AMP-acid ligases IIFunctional Class: I,QThe phylogenetic pattern of COG0318 is aomp-zy--drlbcefghsnujxi--Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","Mon Jan 13 13:21:27 2003","Mon Jan 13 13:21:27 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02109 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Jackowski,S., Jackson,P.D. and Rock,C.O. Sequence and function of the aas gene in Escherichia coli .J. Biol. Chem. 269 (4): 2921-2928 (1994) [PubMed: 8300626].","","Mon Jan 13 13:21:27 2003","1","","","" "AA02111","1437017","1437754","738","ATGACAGAAAATAACCTAGATGTAATTTCCCCGAAATTGGCAGCCGCCATTGCCAATCCGTTATTTCCGGCGGTGGATAGCCAATTGCGTTCCGGTAAACATATCGGCACGGAGCATTTAGATAACCACGCCTTTTTACTTGATTTTCAATCGGAGCTGGATTTGTTTTATCGTCGTTATAACGTGGAACTTATCCGTGCGCCGGAAGGTTTTTTCTATTTACGCCCGAAAGCGACGACGTTAATCGCGCGTTCCGTGTTAACGGAATTGGAAATGTTAGTGGGCAAAGTGTTGTGTTATTTGTATTTAAGCCCGGAACGCCTGGCACAGCAGGGGATTTTCAGCACCCAGGAAGTGTATGACGAACTGTTGAATTTAGCCGATGAAAGTAAATTGCTGAAGGCGGTGAATCAGCGTTCCAGCGGTTCCGATTTGGATAAACAAAAATTGGCGGAAAAAGTGCGTGCGGCGATCGGTCGTTTGCGTCGTTTAGGCATGATTTATACGGTGGGTGAACCGAACAGCGGTAAATTTACCATTTCCGAATCCGTGTTCCGCTTTGGTGCCGAAGTGCGCGCCGGCGATGATCCGATTGAAGCGCAATTACGTTTAATTCGTGATGGTGAAGCGGCAACCCCGCAATCCTTACAGGCAGAAAAACTGGCGTTACAAAATGATGCCGAAAACAGCGAAAACGATGCGGAAGTGGAAGAAGAAGTCGTAGAAGAGGAACAAGAA","","","27544","MTENNLDVISPKLAAAIANPLFPAVDSQLRSGKHIGTEHLDNHAFLLDFQSELDLFYRRYNVELIRAPEGFFYLRPKATTLIARSVLTELEMLVGKVLCYLYLSPERLAQQGIFSTQEVYDELLNLADESKLLKAVNQRSSGSDLDKQKLAEKVRAAIGRLRRLGMIYTVGEPNSGKFTISESVFRFGAEVRAGDDPIEAQLRLIRDGEAATPQSLQAEKLALQNDAENSENDAEVEEEVVEEEQE","1437754","","killing protein suppressor","Cytoplasm","","
InterPro
IPR007385
Family
Prokaryotic chromosome segregation and condensation protein MukE
PF04288\"[9-244]TMukE
InterPro
IPR013166
Domain
Citrate lyase ligase, C-terminal
SM00764\"[14-103]Tno description
noIPR
unintegrated
unintegrated
PD037941\"[12-219]TMUKE_HAEIN_P45186;


","BeTs to 3 clades of COG3095COG name: Uncharacterized protein involved in chromosome partitioningFunctional Class: DThe phylogenetic pattern of COG3095 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 12 to 222 match (5e-100) PD:PD037941 which is described as COMPLETE PROTEOME MUKE KICA PARTITIONING HOMOLOG CHROMOSOME ORF ","","","","","","","","","","","","Mon Jan 13 13:24:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02111 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 9 to 244 (E-value = 4.2e-153) place AA02111 in the MukE family which is described as MukE-like family (PF04288)","","","","","Feng,J., Yamanaka,K., Niki,H., Ogura,T. and Hiraga,S. New killing system controlled by two genes located immediately upstream of the mukB gene in Escherichia coli. Mol. Gen. Genet. 243(2): 136-147, 1994. PubMed: 7513784. Yamazoe M, Onogi T, Sunako Y, Niki H, Yamanaka K, IchimuraT, Hiraga S. Complex formation of MukB, MukE and MukF proteins involved in chromosome partitioning in Escherichia coli. EMBO J. 1999 Nov 1;18(21):5873-84. PMID: 10545099 Yamanaka K, Ogura T, Niki H, Hiraga S. Identification of two new genes, mukE and mukF, involved in chromosome partitioning in Escherichia coli. Mol Gen Genet. 1996 Feb 25;250(3):241-51. PMID: 8602138","","Mon Jan 13 13:24:00 2003","1","","","" "AA02112","1437757","1442244","4488","ATGACTGAAGAATTATCCCTGGAAAATGACGTAATGTATACGACGGCTGAAGCCGCACCTGTTATCTTTAGCCAAAACAGTGGGGTAGAACGCGGTAAATTTCGTTCTTTAACGCTTATCAACTGGAACGGATTTTTCGCTCGTACCTTTGATTTGGACGAATTGGTCACCACCTTATCGGGCGGTAACGGTGCCGGTAAATCCACCACTATGGCGGGATTTGTGACGGCGCTTATTCCCGATTTAACCTTATTGCATTTCCGTAACACCACGGAAGCCGGTGCAACAAGCGGCTCGCGCGACAAAGGTTTGCACGGAAAATTGCGTCCGGGAGTTTGTTACGCGGCGCTGGATACCATTAATTCTCGCCATCAACGGATTATTGTCGGCGTGCGTCTACAACAGGTGGCAGGACGCGATAAAAAAGTAGATTTAAAAACCTTTTCTATTCAAGGCGTAGAATTATCCGTAAATCCGACCGCACTTTTCACCGAAACCCTCAATGAACGCCAAGCCCGCGTGCTTACGTTGAACGAATTAAAAGACAAAGTGGAGCAAAGCGGCGCGCAATTTAAGCAATACCATTCCATCACCGACTATCACGGCATGATGTTCGATTTGGGAATTATCCCGAAACGTTTACGTTCTTCTTCCGACCGCAGTAAATTCTACAAACTCATCGAAGCCTCTTTATACGGTGGTATTTCCAGCGCCATTACCCGTTCTTTACGTGATTATTTATTGCCGGAAAATCTTGGGGTGAAAAAAGCATTCCAAGATATGGAAAGTGCTTTGCGCGAAAACCGCATGACTTTGGAAGCGATTAAAGTGACTCAAGCGGATCGCGATTTATTCAAGCATTTAATCACCGAATCCACTAATTATGTGGCGGCGGATTATATGCGCAATGCCAATGAACGCCGTGGCAATATCGAAAGCGCGTTAAATTTCCGTCAGGAATGGTATAAAGCCAAATCCGAACAGGATTTATCTCAACATCGCTTAGTGGATTTAAGCCGCGAAGCTGCCGAATTGGCAGAAAATGAAAAAACGTTGGAAGTAGATCACCAAAGCGCGTTAGATCATTTGAATTTAGTGCTGAATGCGTTACGTCATCAGGAAAAAATTTCCCGCTATCAAGAAAATGTCGGCGAGCTGACAGAGCGGTTAGAAGAACAAAAAATGGTGGTAGAAACCGCCAACGAGCAGTTAGAAGAAAGCCAAGCGCAATTTGAACAAACGGAACAGGAAGTTGACAACCTACGTTCGCAATTGGCGGATTATCAACAGGCGTTGGATGCGCAACAAACCCGCGCATTGCAATATCAACAAGCCATTCAAGCCTTAGAAAAAGCCAAAACGTTGTGCGGTTTGGCGGATTTAGCCGTGAAAAATGTGGATGTTTACCACGAAGAATTTGAAGCGCAAGCGGAAGTGCTAACGGATAAAGTGCTTGAACTTGAACAAAAAATGTCTATTTCCGAAGCGGCAAAAACGCAATTCGACAAAGCCTATCAGTTGGTTTGCAAAATTGTCGGCGATGTACCTCGTTCTGCTGCGTGGGAAAGTGCGAAAGAATTGTTGCGTGAATATCCGACACAAAAACTGCAAGCACAGCAAACACCGCAACTACGCGCCAAGTTACATGAATTGGAACAACGTCTGAATCAACAACAAAGTGCGGTCAGATTATTAAACGATTTTAATCAACGCGCCAATTTGTCTTTAGAAACCGCAGATGAATTAGAAGAATTTTATGGTGAACAGGAAGCTTTAATTGAGGATTTGTCGGCTGAACTTTCGGACTTGGTAGTGCAGCGTTCAACCTTTCGCCAAAAACGTGAAAATTTGACCGCACTTTATGAGGAAAACGCCCGTAAAGCGCCGGCATGGCTCACGGCACAAGCGGCGTTGGAACGATTGCAGGATCAAAGCGGTGAGCAATTTGCCGACAGCCAAGGCGTGATGAATTTCATGCAGGCACAGTTGGTTAAAGAGCGTGAATTCACCATGGAGCGCGATCAGCTTGAGTTACAACGTCAGCAATTAGATGAGCAAATCAGCCGATTAAGTCAGCCCGACGGATCCGAAGATGCCCGTTTGAACGTACTTGCGGAACGTTTCGGCGGCGTGTTGCTTTCCGAGTTGTATGATGATGTGCCGATTGAAGACGCGCCTTATTTCTCCGCGCTATACGGTCCGGCGCGTCATGCTATTGTCGTGCGTGATCTGAATGCGGTAAAAGAACAACTTGCCAATCTGGAAGATTGCCCGGAGGATTTATATTTAATTGAAGGCGATCCGGCGGCGTTTGATGATAGCGTACTTTCCGCACAGGAATTGGAACTGGGCGTTGTGGTGCAAGTGTCCGATCGTGAATTGCGTTATTCTAAATTCCCGGAAATTCCGTTGTTTGGTCGTGCCGCTCGTGAAAAACATTTGGAAGAATTACAGGCAAAACGTGAGGAAGTGGCGGAACATTACGCTCAACGCGCTTTTGACGTGCAAAAATGCCAGCGTTTACACGAACATTTCAGCCAATTTGTCGGTTTACATTTAGCATTAGCGTTCCAAGATAATCCAGAACAGGTCATGGCTCGGACCAATCAGCAGCGCAATGAAATTGAACGCGAACTAAACCAATTCCTGACCGGCGAACAACAAATTCGCATTCGTTTGGATGATGCGAAAGAACGTATGCAGTTGTTGAATAAATTAATTCCGCAATTGCCATTATTGGCGGATGACAGTTTAACCGATCGCATTGAAGAATGCCGCGAACAGCTGGATTTAGCCGAACAGGATGAGTTATTTATTCGTCAATACGGCGTCACGTTGTCACAATTAGAGCCGATTGCCAATACTTTGCAAAGCGATCCGGAAAATTATGAACACTTAAAAGCCGACTATGAGCAAGCCATTCAGTTGCAAAAACAGGTGCAACAAAAAGTGTTTGCTTTGGCGGATGTGGTGCAACGTAAAGCCCATTTCAACTACGCAGAAAGCGTGCAAACGGAAACCTCCGAATTAAACGAACAATTGCGCGCCCGTTTGGAGCAAATGCAACAACAACGCGAAACACAGCGCGAGCAATTGCGTCAGGTTCAAGCGCAATATGCACAATACAATCAAGTGTTGATTCAATTGCAAAGTTCTTTCAACAGTAAAAACCAAATGTTGCAGGAATTAATGCAGGAAATCGGCGAATTGGGTGTACGTGCCGACGAAGGCGCGGAAGAACGTGCAAAAATCCGTCGGGATGAGTTGTATCAACAACTTTCCACTAATCGTCAGTGCCGTTCTTACATTGAAAAACAACTCACCCTCATTGAAAGCGAAGCGGAAAATCTTACCCGCCGCATTCGTAAAGCGGAACGGGACTACAAAACCCAGCGCGAATTGGTAACGGCGGCTAAAATGAGCTGGTGCGTGGTGCTGCGTTTATCTCGCAATTCTGATGTGGAAAAACGCTTAAATCGTCGTGAATTGGCATATTTATCCGCCGATGAGCTACGTTCCATGTCGGACAAAGCCCTTGGTGCGTTGCGTACGGCGGTTGCCGATAACGAATATCTGCGCGATGCCTTACGTTTATCGGAAGACAGTCGCAAACCGGAAAATAAAGTGCGGTTCTTTATTGCGGTATACCAACATCTACGCGAACGTATCCGTCAGGATATTCTGAAAACCGACGACCCGATTGATGCCATCGAGCAAATGGAAATCGAGCTTTCCCGCTTAACGGAAGAGTTAACCGGTCGTGAACAGAAACTGGCGATCAGCTCTGAAAGCGTGGCAAACATTATGCGTAAAACCATTCAACGTGAACAAAATCGTATTCGTATGCTGAATCAAGGCTTGCAAAATATCGCCTTCGGTCAGGTGAAATCAGTGCGTTTGGTGGTGAATATTCGTGATACGCACGCCATGTTGTTGGATGCGCTTTCCGGCAACCAATCGGATTATCAGGATTTATTTACCGACAATCGTATGACTTTTTCCGAGGCTATTGCGAAATTATATCAACGCCTGAATCCGCATATTGATGTAGGACAACGCACGGCACAAACCATCGGTGAAGAATTACTGGATTACCGTAATTACCTTGATTTGGAAGTAGAGGTGTACCGTGGCGCAGACGGTTGGTTACGCGCGGAAAGCGGTGCATTATCCACCGGTGAAGCCATCGGTACCGGTATGTCCATCCTCTTAATGGTGGTGCAAAGCTGGGAAGAAGAAAGCCGCCGTATTCGTGGCAAAGATATTGTGCCGTGCCGCTTATTGTTCTTGGACGAAGCGGCGCGTTTGGATGCCAAATCTATTTCCACTTTATTCGAGCTGTGCGAACGGCTAGATATGCAATTGCTCATCGCCGCCCCGGAAAATATCAGCCCGGAAAAAGGCACAACCTACAAACTGGTGCGGAAAATTTCCGGTAATCACGAACACGTTCATGTAGTCGGCTTACGCGGATTCGGCACAACAGAG","","","171562","MTEELSLENDVMYTTAEAAPVIFSQNSGVERGKFRSLTLINWNGFFARTFDLDELVTTLSGGNGAGKSTTMAGFVTALIPDLTLLHFRNTTEAGATSGSRDKGLHGKLRPGVCYAALDTINSRHQRIIVGVRLQQVAGRDKKVDLKTFSIQGVELSVNPTALFTETLNERQARVLTLNELKDKVEQSGAQFKQYHSITDYHGMMFDLGIIPKRLRSSSDRSKFYKLIEASLYGGISSAITRSLRDYLLPENLGVKKAFQDMESALRENRMTLEAIKVTQADRDLFKHLITESTNYVAADYMRNANERRGNIESALNFRQEWYKAKSEQDLSQHRLVDLSREAAELAENEKTLEVDHQSALDHLNLVLNALRHQEKISRYQENVGELTERLEEQKMVVETANEQLEESQAQFEQTEQEVDNLRSQLADYQQALDAQQTRALQYQQAIQALEKAKTLCGLADLAVKNVDVYHEEFEAQAEVLTDKVLELEQKMSISEAAKTQFDKAYQLVCKIVGDVPRSAAWESAKELLREYPTQKLQAQQTPQLRAKLHELEQRLNQQQSAVRLLNDFNQRANLSLETADELEEFYGEQEALIEDLSAELSDLVVQRSTFRQKRENLTALYEENARKAPAWLTAQAALERLQDQSGEQFADSQGVMNFMQAQLVKEREFTMERDQLELQRQQLDEQISRLSQPDGSEDARLNVLAERFGGVLLSELYDDVPIEDAPYFSALYGPARHAIVVRDLNAVKEQLANLEDCPEDLYLIEGDPAAFDDSVLSAQELELGVVVQVSDRELRYSKFPEIPLFGRAAREKHLEELQAKREEVAEHYAQRAFDVQKCQRLHEHFSQFVGLHLALAFQDNPEQVMARTNQQRNEIERELNQFLTGEQQIRIRLDDAKERMQLLNKLIPQLPLLADDSLTDRIEECREQLDLAEQDELFIRQYGVTLSQLEPIANTLQSDPENYEHLKADYEQAIQLQKQVQQKVFALADVVQRKAHFNYAESVQTETSELNEQLRARLEQMQQQRETQREQLRQVQAQYAQYNQVLIQLQSSFNSKNQMLQELMQEIGELGVRADEGAEERAKIRRDELYQQLSTNRQCRSYIEKQLTLIESEAENLTRRIRKAERDYKTQRELVTAAKMSWCVVLRLSRNSDVEKRLNRRELAYLSADELRSMSDKALGALRTAVADNEYLRDALRLSEDSRKPENKVRFFIAVYQHLRERIRQDILKTDDPIDAIEQMEIELSRLTEELTGREQKLAISSESVANIMRKTIQREQNRIRMLNQGLQNIAFGQVKSVRLVVNIRDTHAMLLDALSGNQSDYQDLFTDNRMTFSEAIAKLYQRLNPHIDVGQRTAQTIGEELLDYRNYLDLEVEVYRGADGWLRAESGALSTGEAIGTGMSILLMVVQSWEEESRRIRGKDIVPCRLLFLDEAARLDAKSISTLFELCERLDMQLLIAAPENISPEKGTTYKLVRKISGNHEHVHVVGLRGFGTTE","1442244","[FUNCTION] Essential for chromosome partitioning. Implicated in ATP-dependent chromosome partitioning during cell division. (by similarity). ","cell division protein","Cytoplasm","","
InterPro
IPR007406
Domain
Prokaryotic chromosome segregation and condensation protein MukB, N-terminal
PF04310\"[29-253]TMukB
InterPro
IPR010978
Domain
tRNA-binding arm
SSF46589\"[364-429]TtRNA_binding_arm
InterPro
IPR012090
Family
Chromosome partition protein MukB
PIRSF005246\"[1-1496]TMukB
noIPR
unintegrated
unintegrated
G3DSA:3.40.1140.10\"[28-253]TG3DSA:3.40.1140.10


","No hits to the COGs database.","","Residues 1006 to 1129 match (1e-08) PD:PD000023 which is described as COIL COILED ATP-BINDING COMPLETE PROTEOME MOTOR REPEAT MICROTUBULES CHROMOSOME MYOSIN ","","","","","","","","","","","Mon Jan 13 13:27:28 2003","Mon Jan 13 13:27:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02112 is paralogously related to AA02347 (2e-07) and AA00579 (9e-04).","","","","","","Residues 29 to 253 (E-value = 1.7e-165) place AA02112 in the MukB family which is described as MukB N-terminal (PF04310)","","","","","Yamanaka,K., Mitani,T., Feng,J., Ogura,T., Niki,H. and Hiraga,S. Two mutant alleles of mukB, a gene essential for chromosome partition in Escherichia coli. FEMS Microbiol. Lett. 123(1-2): 27-31, 1994. PubMed: 7988894. Niki,H., Jaffe,A., Imamura,R., Ogura,T. and Hiraga,S. The new gene mukB codes for a 177 kd protein with coiled-coil domains involved in chromosome partitioning of E. coli. EMBO J. 10(1): 183-193, 1991. PubMed: 1989883.","","Mon Jan 13 13:27:28 2003","1","","","" "AA02113","1442323","1443174","852","ATGCACAATCTCATTATCGCCGTCCTCTGTAGCGTAGCGGTTTCCGTACTATTGAAAGTTGCCCGCAAGCGTAATATCGTTATTCAACAAGCTATTGCATTTAACTATACTGTTGCGTTGTCACTTTCTTGGTTTTTGTTAAAACCGGATTTCAAAGGGCTTGAATTTACGGATTTCATCGCACAAAGTGAAAATATGCCGATTTTCTTGGCATTAGGTATTTTGTTACCAAGCGTATTTATTATTATGTCCAAAGCGGTGGAATTCGCCGGTATTGTACGTTCCGATGCGGCACAGCGTTTATCCTTATTCTTACCGATTCTCGCCGCATTTTTAATCTTTCATGAAACCTTAAGCCAACCAAAGCTTGTCGGAATTGTGTTGGCGTTTATCGGGTTATTTTGTCTATTAAGCAAACCGAATCTACAAAGTGCGGTCGATCTTCGTGGTATTTTGGGATTGGTTGGCGTATGGTTCGGCTACGGTATTATTGATATTTTATTCAAACAAGTAGCGAAAAGCGGCGGCGCATTCCCAACAACCTTGTTTATCGCGTTCTCATTGGCAGCCTGCATTATGTTCATTTATTTGCTGTTTAAACAAACCAAATGGAATATAGAGAGCTTTGTAGGCGGCATTATTTTAGGTGTGCTGAATTTCTTTAATATTTTGTTTTACATTAAAGCGCATCAAAGTTTTGGCTCTAATCCAACGTTGGTTTTTGCCGGTATGAATATCGGTGTAATTTGTTTAGGCACCTTCACCGGCGCATTAATTTTTAAAGAGAAAATAACCAAAATTAATTGGTTAGGTATTGTATTTAGCTTAACGGCAATCTTTTGTTTGTATTAT","","","31302","MHNLIIAVLCSVAVSVLLKVARKRNIVIQQAIAFNYTVALSLSWFLLKPDFKGLEFTDFIAQSENMPIFLALGILLPSVFIIMSKAVEFAGIVRSDAAQRLSLFLPILAAFLIFHETLSQPKLVGIVLAFIGLFCLLSKPNLQSAVDLRGILGLVGVWFGYGIIDILFKQVAKSGGAFPTTLFIAFSLAACIMFIYLLFKQTKWNIESFVGGIILGVLNFFNILFYIKAHQSFGSNPTLVFAGMNIGVICLGTFTGALIFKEKITKINWLGIVFSLTAIFCLYY","1443174","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR000620
Domain
Protein of unknown function DUF6, transmembrane
PF00892\"[159-284]TDUF6
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide
tmhmm\"[4-22]?\"[27-47]?\"[66-84]?\"[96-114]?\"[120-138]?\"[148-168]?\"[178-198]?\"[208-226]?\"[240-260]?\"[265-283]?transmembrane_regions


","No hits to the COGs database.","","Residues 1 to 140 match (7e-38) PD:PD404586 which is described as COMPLETE PROTEOME TRANSMEMBRANE NMB1028 HI1376 INTEGRAL MEMBRANE PM0610 ","","","","","","","","","","","","Mon Jan 13 13:29:04 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02113 is paralogously related to AA02980 (3e-04).","","","","","","","","","","","","","","1","","","" "AA02114","1443197","1444630","1434","TTGAGAAAAATGATGGCAAAAAACGACTTTAGTTTTTTTATTTATGATTATGAAAGTTTTGGGGTCAATCCCGCAACGGATCGCCCGGCACAATTCGGTGGCATTCGCACTGACGAGGATTTTAATATTATCGGTGAGCCGATTGTTCTTTATTGCAAGCAAACTAACGATTATTTGCCTGCACCAGAAGCGGTTTTAGTCACCGGAATTACACCACAGGAATGCAACGAAAAAGGGCTGTCGGAACCCGAATTTGCCGCCAAAATTTTACAGGAATTCAGCCGTCCGAATACTTGCGTGATGGGCTTTAATAACATTCGTTATGACGATGAAATGACCCGTTATACGTTTTACCGTAATTTTATCGATCCTTATGAATACAGCTGGAAAAACGGCAATTCCCGTTGGGATTTACTGGATTTGGTGCGTGCTTGCTATGCGTTGCGCCCGGACGGTATTGAATGGCCTTTAGATGATGAAGGTATGCCGAGTTTCCGCCTGGAAAAACTGACAGAGGCCAATGGAATAGCGCACGATAGTGCGCATGATGCCATGTCAGATGTGTATGCCACTATTGAAATGGCAAAGCTCATCAAGCGGAAACAGCCTAAATTATTCCAATATTTCTTTGAAAATCGGGGTAAAAAGGAGGTTGAAAAGCTCATCGATACCGCAGAAATGATGCCATTGGTACATGTGTCGGGAATGTTGGGGAATTATCGCGGAAATACCACGTTAATTGCACCTTTAGCCTGGCATCCGACGAATAAAAATGCCGTTATTGTCTGTGATTTAACTGCCGATATTGATGATTTATTAACAAAATCGGTAGGGGAGTTGCGTGAAAATCTTTACACCAAAAAAGAGACCTTATTGGCTGCCGGTGCATTGCCTGTGCCATTGAAGCTCATTCATATCAATAAATGTCCGATTGTTGCGCCGGCTAAAACTTTGTTGCCACAAAACGCCGAACGTTTAGGTATTGATCAGGAGTTATGTGCGCAAAACCGACAACGTTTGCAGGAAGCAAAAGATATTCGCCAAAAAGTAATGGATATTTTTCATCAGGAACGTGAATTTGACGCTTCCGATAATGTTGAAACCGAACTGTATAACGGCTTTTTTAGTGACGCCGATAAAAACAATATGGCGATTTTACGCAGTTTGGAACCCGAAAAATTGGCTAAACATAATCTTAGTTTTCAAGATCCACGAATTCCTGAATTGCTGTTCCATTATCGTGCCAGACATTTCTATCGTACATTGAACCGTGCGGAACAAATTAAATGGCAAAAATACTGCCGTAAAAAATTAGATGCCGAGGCTTTGCAATTTGAACAACGTCTTCAAGAATTAGCCGAACAATATTCCAACAATGAAGAAAATCTTATGTTATTGCAAAAGGTCTATGAATATGGAACGAAAATAATCGGT","","","55353","LRKMMAKNDFSFFIYDYESFGVNPATDRPAQFGGIRTDEDFNIIGEPIVLYCKQTNDYLPAPEAVLVTGITPQECNEKGLSEPEFAAKILQEFSRPNTCVMGFNNIRYDDEMTRYTFYRNFIDPYEYSWKNGNSRWDLLDLVRACYALRPDGIEWPLDDEGMPSFRLEKLTEANGIAHDSAHDAMSDVYATIEMAKLIKRKQPKLFQYFFENRGKKEVEKLIDTAEMMPLVHVSGMLGNYRGNTTLIAPLAWHPTNKNAVIVCDLTADIDDLLTKSVGELRENLYTKKETLLAAGALPVPLKLIHINKCPIVAPAKTLLPQNAERLGIDQELCAQNRQRLQEAKDIRQKVMDIFHQEREFDASDNVETELYNGFFSDADKNNMAILRSLEPEKLAKHNLSFQDPRIPELLFHYRARHFYRTLNRAEQIKWQKYCRKKLDAEALQFEQRLQELAEQYSNNEENLMLLQKVYEYGTKIIG","1444630","[FUNCTION] Also functions as a DNA deoxyribophosphodiesterase that release deoxyribose-phosphate moieties following the cleavage DNA at an apurinic/apyrimidinic (ap) site by either an ap endonuclease ap lyase.[CATALYTIC ACTIVITY] Degradation of single-stranded DNA. It acts progressively in a 3'- to 5'-direction, releasing nucleoside 5'-phosphates.","exodeoxyribonuclease I","Cytoplasm","","
InterPro
IPR013520
Domain
Exonuclease, RNase T and DNA polymerase III
PF00929\"[12-191]TExonuc_X-T
InterPro
IPR013620
Domain
Exonuclease C-terminal
PF08411\"[213-476]TExonuc_X-T_C
noIPR
unintegrated
unintegrated
G3DSA:3.30.420.10\"[2-198]Tno description


","No hits to the COGs database.","","Residues 421 to 477 match (3e-12) PD:PD257491 which is described as COMPLETE I PROTEOME DNA EXONUCLEASE DEOXYRIBOPHOSPHODIESTERASE NUCLEASE EXODEOXYRIBONUCLEASE SBCB DRPASE ","","","","","","","","","","","Tue Jan 28 15:02:45 2003","Mon Jan 13 13:34:10 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02114 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 12 to 191 (E-value = 9.9e-25) place AA02114 in the Exonuc_X-T family which is described as Exonuclease (PF00929)","","","","","Phillips,G.J. and Kushner,S.R. Determination of the nucleotide sequence for the exonuclease I structural gene (sbcB) of Escherichia coli K12. J. Biol. Chem. 262 (1): 455-459 (1987) [PubMed: 3539937].Sandigursky,M. and Franklin,W.A. DNA deoxyribophosphodiesterase of Escherichia coli is associated with exonuclease I. Nucleic Acids Res. 20 (18): 4699-4703 (1992) [PubMed: 1329027].","","Mon Jan 13 13:34:10 2003","1","","","" "AA02115","1444668","1445051","384","TTGAGGTGCAGATTATGTCTTACTCTTATCAATTTCGTTAAAAAACTATCAAACAGGTCACCGAGCAGGATTTTGGTATCCGTGAGGTGGCTAAATTTCATCAGATTTCTCGTTCTCAAGTCATTTATTGGAAAAGCCTTTCGTGAAAGAGGGCTTAATGGCGTAAAATCCCCTTATATAAACCCTCAACGCCCTAAAATAGTGAAGCCAAAGATGAAAAAGAAAGCGATTGAAATCCCGGAACAAACAGACTTTTCCCCAAAAGCGTTTAAAAAGCTGCAACGAGAGCTGGCATTAGCACGTGCACAGATTGCTTACCTAAAGGAGTTGGAGGCACTCGACCGTCAAAAACAGCGACAGAAAAAAGAAAAATCATTGAAAGAT","","","15047","LRCRLCLTLINFVKKLSNRSPSRILVSVRWLNFIRFLVLKSFIGKAFRERGLNGVKSPYINPQRPKIVKPKMKKKAIEIPEQTDFSPKAFKKLQRELALARAQIAYLKELEALDRQKQRQKKEKSLKD","1445051","","hypothetical protein","Periplasm, Cytoplasm","There are no significant matches to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:41:43 2004","Wed Feb 25 15:41:43 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA0348, and to AA0834.AA02115 is paralogously related to AA01289 (4e-69), AA01075 (4e-69), AA00008 (4e-69), AA02340 (2e-66), AA00535 (1e-22), AA01267 (4e-18), AA00631 (1e-13), AA00227 (2e-11), AA01404 (6e-11) and AA01549 (0.001).","Wed Feb 25 15:41:43 2004","","","","","","","","","","","","","1","","","" "AA02116","1445228","1445350","123","ATGGGTTTCCATTTGAATCATAAAACGGTGTTAAAACTGATGAATGCGTTAGGTATTCATTCTATTTTACGCAAGAAAAGACATGGAAAACGAGGAAAACATCGCATATTGCCCCGAATGTGC","","","4810","MGFHLNHKTVLKLMNALGIHSILRKKRHGKRGKHRILPRMC","1445350","","hypothetical protein","Cytoplasm","There are no significant matches to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:39:11 2004","Wed Feb 25 15:39:11 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA0945.AA02116 is paralogously related to AA02341 (1e-20), AA01288 (1e-20), AA01076 (1e-20), AA00009 (1e-20), AA01444 (3e-12) and AA01268 (3e-12).","Wed Feb 25 15:39:11 2004","","","","","","","","","","","","","1","","","" "AA02117","1445347","1445853","507","GTGCTAAATCGTGATTTTACAGCGACGGCGCTCAATCAAAAATGGGTAACCGATGTCACTGAGTTTCGAGTTGGGGAAGAAAAGCTCTATTTTTCACCGTTGATGGATTTAGCGAACCGGGAAATTATTGCCTATAATTTTGCGAAACGCCCTAAGTTCTCATTGGTAAAAAGAATGCCGGAAGAAGGACTTGGCAAACTAAAACCGAGCGAATGCCCGATTATTCACAGCGACCAAGGGGTATTGTACGGCTCAGCAGAATGGGTAAAGATGTTGGAAGGCAAGGCGATACAAAGTATGAGTCGCCGAGGGAATTGCTATGATAATGCGGTGATTGAAAGCTTTTTTGCGATATTAAAATCTGAGTGTTTTTACTCACGCACTTATACTTCGATTGCCGAATTACAGGCGGAAATTGAAGAATATTTGGTGTATTACAACCAAGAACGAATTAAACTTGATTTAAAAGGATTAACCGCGTTATTAATGCTTTATTTAATTCTTCTT","","","19513","VLNRDFTATALNQKWVTDVTEFRVGEEKLYFSPLMDLANREIIAYNFAKRPKFSLVKRMPEEGLGKLKPSECPIIHSDQGVLYGSAEWVKMLEGKAIQSMSRRGNCYDNAVIESFFAILKSECFYSRTYTSIAELQAEIEEYLVYYNQERIKLDLKGLTALLMLYLILL","1445853","[FUNCTION] Involved in the transposition of the insertion sequence IS150. ","probable transposase","Cytoplasm","","
InterPro
IPR001584
Domain
Integrase, catalytic core
PF00665\"[7-165]Trve
PS50994\"[7-168]TINTEGRASE


","No hits to the COGs database.","","Residues 115 to 157 match (6e-07) PD:PD467292 which is described as COMPLETE TRANSPOSASE PROTEOME PLASMID ORFB ELEMENT TRANSPOSASE-LIKE ISRSO11-TRANSPOSASE TNIBDELTA1 TNIA ","","","","","","","","","","","Mon Jan 13 13:49:48 2003","Mon Jan 13 13:49:48 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02117 is paralogously related to AA02342 (2e-89), AA01444 (2e-89), AA01287 (2e-89), AA01268 (2e-89), AA01077 (2e-89), AA00010 (2e-89), AA00145 (3e-17) and AA02420 (4e-17).","","","","","","Residues 7 to 165 (E-value = 1.9e-28) place AA02117 in the rve family which is described as Integrase core domain (PF00665)","","","","","Schwartz,E., Kroger,M. and Rak,B. IS150: distribution, nucleotide sequence and phylogenetic relationships of a new E. coli insertion element. Nucleic Acids Res. 16 (14B): 6789-6802 (1988) [PubMed: 2841644].Hall,B.G., Parker,L.L., Betts,P.W., DuBose,R.F., Sawyer,S.A. and Hartl,D.L. IS103, a new insertion element in Escherichia coli: characterization and distribution in natural populations. Genetics 121 (3): 423-431 (1989) [PubMed: 2541046].Sofia,H.J., Burland,V., Daniels,D.L., Plunkett,G. III and Blattner,F.R. Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes. Nucleic Acids Res. 22 (13): 2576-2586 (1994) [PubMed: 8041620].","","Mon Jan 13 13:49:48 2003","1","","","" "AA02118","1445999","1445883","117","ATGTTTGTTCACTCATTTTTATTTTTTATCCGATTTATTACGCGTTTTAAAAAACGCCAAATAAACAAAATTAATAGTAATTTAAGCATGTTGTTTATATTAAAAAGGGGCGGTCAA","","","4760","MFVHSFLFFIRFITRFKKRQINKINSNLSMLFILKRGGQ","1445883","","hypothetical protein","Cytoplasm","There are no significant matches to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-16]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:35:58 2004","Wed Feb 25 15:35:58 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02118 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:35:58 2004","","","","","","","","","","","","","1","","","" "AA02119","1446512","1446640","129","TTGCGGAAAATGCAGGGCGAAGGCTTGCAGCCCGGTAAACAATGCTCGATGTTATTCGGGCATTTTTATTTTTTGCGCGCGCTTAAATTTAAGCGAGAAATGAAAATTTCCCGCCCCTGCAAATACCCT","","","5133","LRKMQGEGLQPGKQCSMLFGHFYFLRALKFKREMKISRPCKYP","1446640","","hypothetical protein","Periplasm, Cytoplasm","There are no significant matches to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:34:37 2004","Wed Feb 25 15:34:37 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02119 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:34:37 2004","","","","","","","","","","","","","1","","","" "AA02120","1447321","1447803","483","ATGCTTAGTAAAGTGATTACAGCAAAATTAAATGAGCAAATTAATCTGGAGTTTTACTCATCAAATGTTTATTTGCAAATGAGTGCGTGGTGTTATAAGCAAGGTTATGAAGGTGCTGCGGCATTTTTACTTCGCCATGCAGATGAAGAGTTGGAGCATATGCAAAAGTTATTCACTTATGTGAGCGAAACCAGCGGTATGCCATTATTAGGTAAAATTAAAGCCCCTAAACATGACTATGCGTCATTAAAAGAAGTTTTCGAGATTACCCTTGAGCATGAAAAGTTAGTTACGTCTAAAATTAATGAATTAGTGGAATGTACCTTTGCCGAAAAAGATTACTCTAGTTTTAACTTTTTACAATGGTATGTTGCGGAACAACATGAAGAAGAAAAATTGTTCAATAGCATTGTGGACAAATTTAAACTTCTTGGCAAAAGCGGCACTGCCCTTTACTACATTGATCGTGATTTAAAAACGTTA","","","18925","MLSKVITAKLNEQINLEFYSSNVYLQMSAWCYKQGYEGAAAFLLRHADEELEHMQKLFTYVSETSGMPLLGKIKAPKHDYASLKEVFEITLEHEKLVTSKINELVECTFAEKDYSSFNFLQWYVAEQHEEEKLFNSIVDKFKLLGKSGTALYYIDRDLKTL","1447803","[FUNCTION] Iron storage protein.","nonheme ferritin","Cytoplasm","","
InterPro
IPR001519
Domain
Ferritin, N-terminal
PD000971\"[10-58]TFTN1_HAEIN_P43707;
PTHR11431\"[1-161]TFERRITIN
InterPro
IPR008331
Family
Ferritin and Dps
PF00210\"[7-144]TFerritin
InterPro
IPR009040
Domain
Ferritin-like
PS50905\"[1-145]TFERRITIN_LIKE
InterPro
IPR012347
Family
Ferritin-related
G3DSA:1.20.1260.10\"[1-159]Tno description
noIPR
unintegrated
unintegrated
PIRSF002559\"[1-161]TFerritin
PTHR11431:SF4\"[1-161]TFERRITIN


","BeTs to 11 clades of COG1528COG name: Ferritin-like proteinFunctional Class: PThe phylogenetic pattern of COG1528 is a-m-----v-r-b-e-gh--u----wNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-32) to 3/3 blocks of the IPB001519 family, which is described as \"Ferritin\". Interpro entry for IP:IPR001519. IPB001519A 7-61 4.3e-20 IPB001519B 90-142 1.9e-10 IPB001519C 148-159 38","Residues 1 to 62 match (2e-21) PD:PD096450 which is described as FERRITIN PROTEOME COMPLETE IRON STORAGE PRECURSOR SIGNAL SUBUNIT HEAVY IRON-CONTAINING ","","","","","","","","","","","Mon Jan 13 13:53:52 2003","Mon Jan 13 13:53:52 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02120 is paralogously related to AA02121 (1e-57).","","","","","","Residues 7 to 144 (E-value = 1.4e-49) place AA02120 in the Ferritin family which is described as Ferritin-like domain (PF00210)","","","","","Wai,S.N., Nakayama,K., Umene,K., Moriya,T. and Amako,K. Construction of a ferritin-deficient mutant of Campylobacter jejuni: contribution of ferritin to iron storage and protection against oxidative stress Mol. Microbiol. 20 (6), 1127-1134 (1996) PubMed: 8809765 Hudson,A.J., Andrews,S.C., Hawkins,C., Williams,J.M., Izuhara,M., Meldrum,F.C., Mann,S., Harrison,P.M. and Guest,J.R.Overproduction, purification and characterization of the Escherichia coli ferritin. Eur. J. Biochem. 218 (3): 985-995 (1993) [PubMed: 8281950].Treffry,A., Zhao,Z., Quail,M.A., Guest,J.R. and Harrison,P.M. How the presence of three iron binding sites affects the iron storage function of the ferritin (EcFtnA) of Escherichia coli. FEBS Lett. 432 (3): 213-218 (1998) [PubMed: 9720927].Escherichia.3. Izuhara,M., Takamune,K. and Takata,R. Cloning and sequencing of an Escherichia coli K12 gene which encodes a polypeptide having similarity to the human ferritin Hsubunit. Mol. Gen. Genet. 225 (3): 510-513 (1991) [PubMed: 2017145].","","Mon Jan 13 13:53:52 2003","1","","","" "AA02121","1447822","1448316","495","ATGTTATCAAATGATGTGGTTAAACTATTAAACGACCAAATGAATTTAGAGTTTTATTCTTCTAATTTATATTTACAAATGAGCGCCTGGTGTGAACAACAAGGCTTAGAAGGCGCGGCAAAATTCTTATCTGCACACGCAGCTGAAGAAATGCAACATATGCGTAAACTGTTCACTTATTTAAATGAAACCGGCGCATTGGCTGTCATTACTGCAATTGATGAACCGCCACACCAATTCGCTTCGTTAAAACAAGTACTTGAATTAACATACGAACATGAAAAATTGATTACTGCCAAAATCAATGAATTGGTTGGTAGAACATTTGAAGAGAAGGACTACTCTGCTTTTAACTTCTTACAATGGTACGTTGAAGAACAGCACGAAGAAGAAAAATTATTCAGCGGAATTTTGGATAAACTGAATCTTCTTGGCGAAGATGGAAAAGGTTTATTCCTTGTTGATAAAGATTTAGGCGCTTTAGCAGAAAGCAAC","","","18824","MLSNDVVKLLNDQMNLEFYSSNLYLQMSAWCEQQGLEGAAKFLSAHAAEEMQHMRKLFTYLNETGALAVITAIDEPPHQFASLKQVLELTYEHEKLITAKINELVGRTFEEKDYSAFNFLQWYVEEQHEEEKLFSGILDKLNLLGEDGKGLFLVDKDLGALAESN","1448316","[FUNCTION] Iron storage protein. ","nonheme ferritin","Cytoplasm","","
InterPro
IPR001519
Domain
Ferritin, N-terminal
PD000971\"[3-58]TFerritin
PTHR11431\"[1-161]TFerritin_N
InterPro
IPR008331
Family
Ferritin and Dps
PF00210\"[7-144]TFerritin
InterPro
IPR009040
Domain
Ferritin-like
PS50905\"[1-145]TFERRITIN_LIKE
InterPro
IPR009078
Family
Ferritin/ribonucleotide reductase-like
SSF47240\"[2-162]TFerritin/RR_like
InterPro
IPR012347
Family
Ferritin-related
G3DSA:1.20.1260.10\"[1-165]TFerritin_rel
noIPR
unintegrated
unintegrated
PIRSF002559\"[1-165]TFerritin
PTHR11431:SF4\"[1-161]TPTHR11431:SF4


","BeTs to 11 clades of COG1528COG name: Ferritin-like proteinFunctional Class: PThe phylogenetic pattern of COG1528 is a-m-----v-r-b-e-gh--u----wNumber of proteins in this genome belonging to this COG is","Significant hit ( 9.6e-31) to 3/3 blocks of the IPB001519 family, which is described as \"Ferritin\". Interpro entry for IP:IPR001519. IPB001519A 7-61 9.7e-18 IPB001519B 90-142 8.6e-10 IPB001519C 148-159 3.5","Residues 88 to 159 match (2e-29) PD:PD366900 which is described as PROTEOME COMPLETE FERRITIN IRON STORAGE LIKE NONHEME IRON-CONTAINING RSGA UU427 ","","","","","","","","","","","Mon Jan 13 14:34:25 2003","Mon Jan 13 14:34:25 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02121 is paralogously related to AA02120 (1e-57).","","","","","","Residues 7 to 144 (E-value = 7.6e-49) place AA02121 in the Ferritin family which is described as Ferritin-like domain (PF00210)","","","","","Wai,S.N., Nakayama,K., Umene,K., Moriya,T. and Amako,K. Construction of a ferritin-deficient mutant ofCampylobacter jejuni: contribution of ferritin to iron storage andprotection against oxidative stress Mol. Microbiol. 20 (6),1127-1134 (1996) PubMed: 8809765 Hudson,A.J., Andrews,S.C., Hawkins,C., Williams,J.M.,Izuhara,M., Meldrum,F.C., Mann,S., Harrison,P.M. andGuest,J.R. Overproduction, purification and characterization of theEscherichia coli ferritin. Eur. J. Biochem. 218 (3):985-995 (1993) [PubMed: 8281950]. Treffry,A., Zhao,Z., Quail,M.A., Guest,J.R. andHarrison,P.M. How the presence of three iron binding sitesaffects the iron storage function of the ferritin (EcFtnA)of Escherichia coli. FEBS Lett. 432 (3): 213-218 (1998)[PubMed: 9720927]. Escherichia.3. Izuhara,M., Takamune,K. and Takata,R. Cloning and sequencing of an Escherichia coli K12 genewhich encodes a polypeptide having similarity to the humanferritin Hsubunit. Mol. Gen. Genet. 225 (3): 510-513 (1991)[PubMed: 2017145].","","Mon Jan 13 14:34:25 2003","1","","","" "AA02123","1448551","1448384","168","ATGGCTGCTGAAAAACTGACTAAGAAACGCTTAATTCAAATTCTCATTATGCTGATAGTCCTGCTTACCGCATTTTTTTATCGCACGTTTTATTATGAAGCCAGTGGAACAGGTCAACCACCGGCAAAAACACTTGAAAAAAACACCGCACTTTCTGAGAATAAAAAT","","","6363","MAAEKLTKKRLIQILIMLIVLLTAFFYRTFYYEASGTGQPPAKTLEKNTALSENKN","1448384","","hypothetical protein","Cytoplasm","There are no significant matches to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-24]?signal-peptide
tmhmm\"[12-32]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:33:17 2004","Wed Feb 25 15:33:17 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02123 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:33:17 2004","","","","","","","","","","","","","1","","","" "AA02124","1448660","1449430","771","ATGAAAATTTTAGCGACAGAAACAAAATTAGGACGTCGAGTTCAATCCGGGGGGTGTGCCATTCATTGCCAAAATTGTAGCATTAGCCAGCTATGTATTCCTTTTACTTTGAATCAACACGAATTAGATCAGTTAGATAATATTATTGAACGTAAAAAACCTATACAGAAATCCCAAGTACTTTTTAAAGCGGGCGATGAGCTGACCTCACTCTACGCTATCCGTTCCGGCACAATCAAATCTTATACCATTAGCGAAACAGGCGAAGAACAAATTACCTCTTTTCATTTACCGGGCGATTTGGTGGGGTTCGATGCCATTATGAATATGCAACATCCGAGTTTTGCTCAAGCGTTAGAAACGGCAATGGTATGTGAAATTCCGTTCGATATTTTGGATGATTTATCCGGCAAAATGCCTAAACTGCGCCAGCAAATTATGCGTTTAATGAGTAATGAAATTAAAAGTGATCAGGAAATGATTTTATTACTCTCTAAAATGAATGCAGAAGAACGTCTTGCCGCATTTATTTATAACTTATCTCAACGCTACTCCGCCCGAGGTTTTTCTGCCAGGGAATTCCGCTTAACCATGACTCGTGGTGATATCGGCAATTATCTCGGTTTAACCGTCGAAACTATCAGTCGTTTACTCGGTCGCTTCCAAAAACTTGGTGTATTATCGGTTCAAGGAAAATACATTACGATTAATAATATGGCGGAATTAATCGAACTATCCGGTACCAACAAAAACAAAATTCAACTGATTATT","","","28915","MKILATETKLGRRVQSGGCAIHCQNCSISQLCIPFTLNQHELDQLDNIIERKKPIQKSQVLFKAGDELTSLYAIRSGTIKSYTISETGEEQITSFHLPGDLVGFDAIMNMQHPSFAQALETAMVCEIPFDILDDLSGKMPKLRQQIMRLMSNEIKSDQEMILLLSKMNAEERLAAFIYNLSQRYSARGFSAREFRLTMTRGDIGNYLGLTVETISRLLGRFQKLGVLSVQGKYITINNMAELIELSGTNKNKIQLII","1449430","[FUNCTION] It is involved in the activation of genes necessary for anaerobic respiration. It probably also activates genes involved in the production of virulence factors.","anaerobic regulatory protein; transcription regulator Fnr","Cytoplasm","","
InterPro
IPR000595
Domain
Cyclic nucleotide-binding
PF00027\"[52-141]TcNMP_binding
SM00100\"[33-154]TcNMP
PS50042\"[33-116]TCNMP_BINDING_3
SSF51206\"[28-167]TcNMP_binding
InterPro
IPR001808
Domain
Bacterial regulatory protein, Crp
PR00034\"[196-212]T\"[212-227]THTHCRP
PF00325\"[196-227]TCrp
SM00419\"[190-238]THTH_CRP
PS00042\"[198-221]THTH_CRP_1
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[167-255]TWing_hlx_DNA_bd
InterPro
IPR012318
Domain
Helix-turn-helix motif, Crp-type
PS51063\"[167-240]THTH_CRP_2
InterPro
IPR014710
Domain
RmlC-like jelly roll fold
G3DSA:2.60.120.10\"[37-161]TRmlC-like_jellyroll
noIPR
unintegrated
unintegrated
SSF46785\"[168-247]TSSF46785


","BeTs to 14 clades of COG0664COG name: cAMP-binding domains - Catabolite gene activator and regulatory subunit of cAMP-dependent protein kinasesFunctional Class: TThe phylogenetic pattern of COG0664 is ------yqvdrlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is","Significant hit ( 7.1e-41) to 2/2 blocks of the IPB001808 family, which is described as \"Bacterial regulatory proteins, Crp family\". Interpro entry for IP:IPR001808. IPB001808A 65-116 1.1e-24 IPB001808B 196-227 6.2e-15","Residues 21 to 73 match (3e-09) PD:PD080629 which is described as TRANSCRIPTION REGULATION BD DNA-BINDING CYTOCHROME ","","","","","","","","","","","Mon Jan 13 14:40:03 2003","Mon Jan 13 14:40:03 2003","","Thu Aug 4 09:52:44 2005","Thu Aug 4 09:52:44 2005","Thu Aug 4 09:52:44 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA02124 is paralogously related to AA01308 (4e-09).","Thu Aug 4 09:52:44 2005","","","","","Residues 196 to 227 (E-value = 3.4e-14) place AA02124 in the Crp family which is described as Bacterial regulatory proteins, crp family (PF00325)","Thu Aug 4 09:52:44 2005","","","Kokeguchi,S., Hirosue,M., Maeda,H., Miyamoto,M., Takashiba,S. and Murayama,Y. Molecular characterization of the hlyX-like gene of Actinobacillus actinomycetemcomitans Y4. Res. Microbiol. 151 (9): 721-725 (2000) PubMed: 11130862Hattori,T., Takahashi,K., Nakanishi,T., Ohta,H., Fukui,K.,Taniguchi,S. and Takigawa,M.Novel FNR homologues identified in four representative oralfacultative anaerobes: Capnocytophaga ochracea, Capnocytophagasputigena, Haemophilus aphrophilus, and ActinobacillusactinomycetemcomitansFEMS Microbiol. Lett. 137 (2-3), 213-220 (1996)PubMed: 96236880.MacInnes JI, Kim JE, Lian CJ, Soltes GA.Actinobacillus pleuropneumoniae hlyX gene homology with the fnr gene of Escherichia coli.J Bacteriol. 1990 Aug;172(8):4587-92.PMID: 2198268Baltes N, N'diaye M, Jacobsen ID, Maas A, Buettner FF, Gerlach GF.Deletion of the anaerobic regulator HlyX causes reduced colonization and persistence of Actinobacillus pleuropneumoniae in the porcine respiratory tract.Infect Immun. 2005 Aug;73(8):4614-9.PMID: 16040973","Shaw,D.J. and Guest,J.R. Nucleotide sequence of the fnr gene and primary structure of the Fnr protein of Escherichia coli. Nucleic Acids Res. 10 (19): 6119-6130 (1982) PubMed: 6292868. Trageser,M., Spiro,S., Duchene,A., Kojro,E., Fahrenholz,F., Guest,J.R. and Unden,G. Isolation of intact FNR protein (Mr 30,000) of Escherichia coli . Mol. Microbiol. 4 (1): 21-27 (1990) PubMed: 2181237.Lazazzera,B.A., Bates,D.M. and Kiley,P.J. The activity of the Escherichia coli transcription factor FNR is regulated by a change in oligomeric state. Genes Dev. 7 (10): 1993-2005 (1993) PubMed: 8406003.Khoroshilova,N., Popescu,C., Munck,E., Beinert,H. and Kiley,P.J.Iron-sulfur cluster disassembly in the FNR protein of Escherichia coli by O2: [4Fe-4S] to [2Fe-2S] conversion with loss of biologicalactivity. Proc. Natl. Acad. Sci. U.S.A. 94 (12): 6087-6092 (1997) [PubMed: 9177174.Ralph,E.T., Scott,C., Jordan,P.A., Thomson,A.J., Guest,J.R. and Green,J. Anaerobic acquisition of [4FE 4S] clusters by the inactive FNR(C20S) variant and restoration of activity by second-site aminoacid substitutions. Mol. Microbiol. 39 (5): 1199-1211 (2001) PubMed: 11251837.","Thu Aug 4 09:52:44 2005","Thu Aug 4 09:52:44 2005","1","","","" "AA02125","1449552","1450481","930","ATGAAATTCAATAAGATACTGGTGGTTTTAAACCCCGAAAATGACAAACAATATGCCCTTGCCAGAGCAGTTCGTCTGGCGCAAGAACAAAAAAGCCCATCTCCTGTCAAAATTACCCTTTTCCTCGCAATTTACGATTTATCTTATGAAATGTCGGCGTTACTTTCTTCGGAAGAACGCTCCGAAATGCATAACAACGTTATTGAACAGCGTAAATTAGCTATCCGGCCTTATATTGAAAAATATGCTTCTGATGGAATTGAATTTGCTACTACCGTTGTTTGGAAAAGCAATGAAGCGGAAGCCATCACAACGGAAGTTGAAACGCAAGGCTATGATTTGGTCGTGAAATATACGAAAGCTGAAGAAAGCTTGAAATCGCTTATTGTTACACCTGTAGATTGGCAATTATTACGCAAATGCCCGGTACCGATTTTAGTAGTAAAAGACGGTGACTGGAAACATCAGCGTCGGATTTTAGTTGCCGTGAACGTATCTGATGATGAAAATGAAGCCCATAGTTCTTTTAATGATGAACTGGTTTCATTAAGTATGGATTTAGCTGATTCTTTAGATCGTGGCAATATTCATCTTGTCACAGCCTATCCACCGACACCGATTAATATGGTAATTGATTTGCCGGAATTCAGTTCAGGTGAATATAGCACCGGTTTGCGTGGACAATATTTAATCAATATGAAGGCGCTGCGTCAGAAATATGGCATCAGTGAGGATCACACTCATGTACTTGAAGGCTTCCCGGAAGATGTCATCCCTCAGGTCGCAGAGAGAATTGAAGCCGAATTAGTGATTTTGGGTACTATTGGTAGAACCGGGCTTTCAGCTGCCTTTTTAGGCAATACGGCAGAACATGTAATTAGTAAGCTTAACTCCAATTTGCTGGCGATTAAGCCGTCAAAGAACAATGAT","","","38374","MKFNKILVVLNPENDKQYALARAVRLAQEQKSPSPVKITLFLAIYDLSYEMSALLSSEERSEMHNNVIEQRKLAIRPYIEKYASDGIEFATTVVWKSNEAEAITTEVETQGYDLVVKYTKAEESLKSLIVTPVDWQLLRKCPVPILVVKDGDWKHQRRILVAVNVSDDENEAHSSFNDELVSLSMDLADSLDRGNIHLVTAYPPTPINMVIDLPEFSSGEYSTGLRGQYLINMKALRQKYGISEDHTHVLEGFPEDVIPQVAERIEAELVILGTIGRTGLSAAFLGNTAEHVISKLNSNLLAIKPSKNND","1450481","","conserved hypothetical protein; possible universal stress protein","Cytoplasm","","
InterPro
IPR006015
Family
Universal stress protein (Usp)
PR01438\"[156-174]T\"[264-276]T\"[282-304]TUNVRSLSTRESS
InterPro
IPR006016
Domain
UspA
PF00582\"[2-149]T\"[210-304]TUsp
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620\"[2-153]T\"[156-310]Tno description


","BeTs to 16 clades of COG0589COG name: Universal stress protein UspA and related nucleotide-binding proteinsFunctional Class: TThe phylogenetic pattern of COG0589 is aompkzyq-drlbcefgh-n-jx---Number of proteins in this genome belonging to this COG is","","Residues 247 to 305 match (7e-21) PD:PD471486 which is described as PROTEOME COMPLETE STRESS PA1789 YDAA UNIVERSAL HI1426 VC1433 PA4328 VCA0159 ","","","","","","","","","","","","Mon Jan 13 14:46:22 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02125 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 155 to 304 (E-value = 5.4e-07) place AA02125 in the Usp family which is described as Universal stress protein family (PF00582)","","","","","","","","1","","","" "AA02126","1450611","1451444","834","ATGAAAAAATCATTACTAATTACACTATTAGGATTAAGTAGTTTAACACAAGCGCATGATCTATGGGTGACCGCACCGTCCCATATTAGTGCGGAAGATATATTAAAAGCAGATTTAGGATACGGACATCATTTCCCATATGCAGAAAAAATTGCTGATGATCGACTGCATTTTTTTGCACCACTTGAATTAACCGATAAAAACGGAAATACCACCGAATTGAAGCAACAAGGCGAAAATTATCAATACACCGCTGAAAAACCGTTGGCAGAGGGTTCTTATTGGGTCTCAGCTACCTATAAACCGATTTTCTGGTCACAAAATGCTAAAGGCTGGAAACAAGAAAATATGCAACAAATGAAAGATGCTACCTACTGTGAGCAAACTCAAATGTTTGGTAAAAGTTTGGTTACTGTCGGTGGCAAAATAGATTCGACAATTTATAAAGAAAAATTAGGGCAAGAGTTAGAAATTGTACCACTAAAAAGTCCCGCAGAACTCAAAGCTGGTGAAGTTTTCCCGTTACAAATTTTTTATAAAGGTAAGCCATTAGCCGGCGAGGTTGTTATCGCAACAGCTGACACCGTGCTAGTTAAAGATATTGAATCAGCGGAAGACCACCGTGAAGTACAAGGTTTTTCGAGTAAAACGGACAAAGATGGCAAAGTTAATTTCTTACCGTTAGTTGAAGGTTTATGGAAAGTAAAAGTTATACACAAGATTCCGTTTGGTGACCCTAAAGTGTGTCAACATTCGGCAAATTACGCGACGCTGGTATTGCCGGTGGGAGAAAAACGCGCGGAATATAAACCTCACGAACATCACCACCATCAC","","","34909","MKKSLLITLLGLSSLTQAHDLWVTAPSHISAEDILKADLGYGHHFPYAEKIADDRLHFFAPLELTDKNGNTTELKQQGENYQYTAEKPLAEGSYWVSATYKPIFWSQNAKGWKQENMQQMKDATYCEQTQMFGKSLVTVGGKIDSTIYKEKLGQELEIVPLKSPAELKAGEVFPLQIFYKGKPLAGEVVIATADTVLVKDIESAEDHREVQGFSSKTDKDGKVNFLPLVEGLWKVKVIHKIPFGDPKVCQHSANYATLVLPVGEKRAEYKPHEHHHHH","1451444","","conserved hypothetical protein","Periplasm, Cytoplasm","","
noIPR
unintegrated
unintegrated
PD115091\"[105-258]TQ88HM7_PSEPK_Q88HM7;
signalp\"[1-18]?signal-peptide


","No hits to the COGs database.","","Residues 1 to 263 match (4e-86) PD:PD125647 which is described as COMPLETE PROTEOME HI1427 SIGNAL PRECURSOR NMB1475 ","","","","","","","","","","","","Mon Jan 13 14:48:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02126 is paralogously related to AA01751 (1e-07).","","","","","","","","","","","","","","1","","","" "AA02128","1454138","1451535","2604","ATGAGTAAATCCTTAGTTATTGTGGAGTCGCCGGCAAAGGCGAAAACCATTAATAAATATTTAGGAAACAATTATGTAGTGAAATCCAGCGTGGGGCATATTCGCGATTTGCCAACCGTGGGTTCCTCCACTGGAGAAAAAGCCAAAGCCATTTCCACCAAAGGGCTCAGTACGGAAGAAAAACAGGCGATAAAACACAAAAAAGAACAGGAAGCTTTAGTCAAACGCATGGGCATTGACCCTTATCACAGTTGGAAAGCCAACTATCAAATTCTCCCCGGCAAAGAAAAAGTGGTTGCCGAACTGAAATCTCTCGCAAAAAAAGTTGATCATATTTACCTCGCCACCGATTTGGATAGAGAAGGAGAGGCGATTGCCTGGCATTTGCGTGAAGTCATCGGCGGCGATGATGAACGTTATAGCCGCGTGGTGTTTAATGAAATTACCAAAAACGCCATTAAACAAGCCTTTGAACACCCCGAACATTTGAATATGGATCGCGTTAACGCACAGCAAACCCGCCGCTTTTTGGACCGCGTGGTAGGCTTTATGGTCTCACCGTTACTTTGGAAAAAAGTGGCGCGCGGTTTATCTGCCGGTCGTGTGCAATCGGTGGCGGTGAAGTTAATCGTTGAGCGTGAACGTGAAATTAAGGCTTTCGTGCCACAGGAATATTGGGAAGTCTCCGTGCTCACCAATACACCGAAAGGCGATGAAATTCGCTTGGATGTGGTTCAATTTAAAGGTAAGAAATTCGAACCGAAAAATGCCGAGCAGGCGCAAAGTGCGGTGGATTTTTTAAGTAAATCCGACTATGTGATTTCCGATTTGGAAACCAAGCCGACCAGTTCCCGCCCAAGAGCGCCGTTTATTACCTCAACCTTACAACAAACCGCTAGCACCCGTTTAGGCTTCGGTGTGAAAAAAACCATGATGTTGGCGCAACGTTTGTATGAAGCCGGTTACATCACTTATATGCGTACCGACTCCACCAATTTAAGCCAGGATGCGCTGAATATGGTACGCGGCTACATTGAAAAACAGTACGGTCAAACCTATTTGCCGGCAAAACCGAATTTTTATTCCAGCAAAGAAAATGCGCAGGAAGCCCATGAAGCTATTCGTCCGTCCGATATCAATGTGGGCTTGGATGACTTAGCGGGCATGGAAAAAGACGCGGTGCGTTTATATGATTTAATCTGGCGTCAATTTGTGGCATGTCAAATGCCTGCGGCACAATATGACAGCACAACATTAACCGTAACAGCGGGGGATTACAGTTTAACCGCGAAAGGGCGCATTTTACGTTTTGACGGTTGGACCAAAGTGTTACTGCAACAAAGTAAATCTGCAGAAGATCAGGCGTTACCGGCGGTTTCCGTTAACGATAAACTTAACTTGTCGGAAGTGCAACCGCAGCAATATTTCACCAAACCGCCGGCACGTTTCTCTGAAGCAGCGTTGGTAAAAGAATTGGAAAAACGTGGTATCGGCCGTCCTTCCACTTATGCAGCGATTATCTCTACAATTCAGGAACGCGGTTATGTACGCACCGAAAATCGTCGTTTCTATGCGGAAAAAATGGGGGAAATCGTAACGGATCGGTTGAATCAGTCTTTCGCCGATTTAATGAACTACGATTTCACCGCTAATATGGAAGACGTGCTGGACCAAATTGCTTCCGGGGATAAAAACTGGAAAACCGAATTAAACCAATTCTTCAAAGACTTCTCGACCCAATTGACCAAAGCGGAATTAGATGAATTGGAGGGCGGTATGCGCCCGAATAATTTGGTTGAGACGGATATTTGTTGCCCGACTTGCGGTCGCAATATGGCGATCAGAACCGCCAGTACAGGCGTATTCTTAGGCTGCACCGGCTATGCCTTACCACCGAAAGCACGTTGCAAAACCACCATTAACCTGGTTCCTGAAGCGGAACTATTAAATGTGTTGGACGACGCGTCGGAAACCAAAGCGCTAATGGAACGTAAACGCTGCCCGAAATGCGGTACGGCGATGGACAGTTATATTATCGATCCTCATCGAAAACTACATATTTGCGGCAATAACCTGAATTGTGACGGCTATTTAGTCGAAGAAGGTAAGTTTAAGATTAAAGGTTATGACGGCCCAATCGTTGAATGCGATAAATGCGGCGGTGATATGCACCTTAAACTGGGGCGCTTCGGTAAGTATATGGCGTGTACACAATGCGATAATACGCGCAAAATTCTGAAAAACGGCGAAGTGGCGCCACCGAAAGAAGAACCGATTCATTTCCCGGAATTAAAATGCGAAAAATCCGATGCTTATTTCGTCTTGCGAGATGGTGCGGGCGGGGTGTTTATGTCCGCGCATAATTTCCCGAAATCCCGTGAAACCCGTGCACCTAAAGTGGCGGAATTGGCGTTATATCGTGAGCGGCTGCCGGAAAAATTAAGCTATCTGGCTGACGCACCACAAACGGATCCGGAAGGCAGTGAAGCCATCATTCGCTTTAGTCGTAAAGAAAAACGTCAATATGTCACCTCCGAAAAGAATGGCAAGGCGACAAAATGGATAGTGGATTTTGTTGATGGGAAGTGGGTAGAGCGAAAGAAA","","","97837","MSKSLVIVESPAKAKTINKYLGNNYVVKSSVGHIRDLPTVGSSTGEKAKAISTKGLSTEEKQAIKHKKEQEALVKRMGIDPYHSWKANYQILPGKEKVVAELKSLAKKVDHIYLATDLDREGEAIAWHLREVIGGDDERYSRVVFNEITKNAIKQAFEHPEHLNMDRVNAQQTRRFLDRVVGFMVSPLLWKKVARGLSAGRVQSVAVKLIVEREREIKAFVPQEYWEVSVLTNTPKGDEIRLDVVQFKGKKFEPKNAEQAQSAVDFLSKSDYVISDLETKPTSSRPRAPFITSTLQQTASTRLGFGVKKTMMLAQRLYEAGYITYMRTDSTNLSQDALNMVRGYIEKQYGQTYLPAKPNFYSSKENAQEAHEAIRPSDINVGLDDLAGMEKDAVRLYDLIWRQFVACQMPAAQYDSTTLTVTAGDYSLTAKGRILRFDGWTKVLLQQSKSAEDQALPAVSVNDKLNLSEVQPQQYFTKPPARFSEAALVKELEKRGIGRPSTYAAIISTIQERGYVRTENRRFYAEKMGEIVTDRLNQSFADLMNYDFTANMEDVLDQIASGDKNWKTELNQFFKDFSTQLTKAELDELEGGMRPNNLVETDICCPTCGRNMAIRTASTGVFLGCTGYALPPKARCKTTINLVPEAELLNVLDDASETKALMERKRCPKCGTAMDSYIIDPHRKLHICGNNLNCDGYLVEEGKFKIKGYDGPIVECDKCGGDMHLKLGRFGKYMACTQCDNTRKILKNGEVAPPKEEPIHFPELKCEKSDAYFVLRDGAGGVFMSAHNFPKSRETRAPKVAELALYRERLPEKLSYLADAPQTDPEGSEAIIRFSRKEKRQYVTSEKNGKATKWIVDFVDGKWVERKK","1451535","[FUNCTION] The reaction catalyzed by topoisomerases leads to the conversion of one topological isomer of DNA to another. [CATALYTIC ACTIVITY] ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.","DNA topoisomerase I","Cytoplasm, Periplasm","","
InterPro
IPR000380
Family
DNA topoisomerase, type IA
PR00417\"[112-125]T\"[197-215]T\"[320-329]T\"[396-412]T\"[496-510]TPRTPISMRASEI
PTHR11390\"[12-37]T\"[61-577]TPROKARYOTIC DNA TOPOISOMERASE
PS00396\"[315-329]TTOPOISOMERASE_I_PROK
InterPro
IPR003601
Domain
DNA topoisomerase, type IA, domain 2
SM00436\"[139-227]TTOP1Bc
InterPro
IPR003602
Domain
DNA topoisomerase, type IA, DNA-binding
SM00437\"[278-533]TTOP1Ac
InterPro
IPR005733
Domain
DNA topoisomerase I, bacterial-type
TIGR01051\"[5-643]TtopA_bact: DNA topoisomerase I
InterPro
IPR006154
Domain
Toprim subdomain
SM00493\"[3-138]TTOPRIM
InterPro
IPR006171
Domain
TOPRIM
PF01751\"[3-146]TToprim
InterPro
IPR013263
Domain
DNA topoisomerase I, zinc ribbon-like, bacterial-type
PF08272\"[760-800]T\"[827-868]TTopo_Zn_Ribbon
InterPro
IPR013497
Domain
DNA topoisomerase, type IA, central
PF01131\"[160-559]TTopoisom_bac
InterPro
IPR013498
Domain
DNA topoisomerase, type IA, zn finger
PF01396\"[602-645]T\"[713-748]Tzf-C4_Topoisom
InterPro
IPR013824
Domain
DNA topoisomerase, type IA, central region, subdomain 1
G3DSA:1.10.460.10\"[170-237]T\"[469-598]Tno description
InterPro
IPR013826
Domain
DNA topoisomerase, type IA, central region, subdomain 3
G3DSA:1.10.290.10\"[286-410]Tno description
noIPR
unintegrated
unintegrated
G3DSA:2.20.25.10\"[811-868]Tno description
G3DSA:3.30.65.10\"[747-810]Tno description
G3DSA:3.40.50.140\"[1-169]Tno description


","BeTs to 23 clades of COG0550COG name: Topoisomerase IAFunctional Class: LThe phylogenetic pattern of COG0550 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit (2.7e-182) to 12/12 blocks of the IPB000380 family, which is described as \"Prokaryotic DNA topoisomerase I\". Interpro entry for IP:IPR000380. IPB000380A 5-17 6.6e-08 IPB000380B 20-37 9.6e-11 IPB000380C 112-129 6.5e-13 IPB000380D 142-153 5.8e-06 IPB000380E 168-191 2.4e-15 IPB000380F 197-228 1.3e-23 IPB000380G 289-319 2.4e-21 IPB000380H 321-337 1e-11 IPB000380I 363-377 2.2e-06 IPB000380J 395-412 2.3e-12 IPB000380K 477-516 7.2e-31 IPB000380L 540-558 4e-08","Residues 198 to 228 match (1e-08) PD:PD011342 which is described as TOPOISOMERASE ISOMERASE DNA PROTEOME COMPLETE ENZYME I DNA-BINDING OMEGA-PROTEIN UNTWISTING ","","","","","","","","","","","Mon Jan 13 14:51:51 2003","Mon Jan 13 14:51:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02128 is paralogously related to AA00789 (5e-28), AA00578 (3e-06) and AA00021 (8e-04).","","","","","","Residues 713 to 748 (E-value = 4.3e-12) place AA02128 in the zf-C4_Topoisom family which is described as Topoisomerase DNA binding C4 zinc finger (PF01396)","","","","","Tse-Dinh,Y.C. and Wang,J.C. Complete nucleotide sequence of the topA gene encoding Escherichia coli DNA topoisomerase I J. Mol. Biol. 191 (3), 321-331 (1986) PubMed: 3029379 Lima,C.D., Wang,J.C. and Mondragon,A. Three-dimensional structure of the 67K N-terminal fragment of E. coli DNA topoisomerase I Nature 367 (6459), 138-146 (1994) PubMed: 8114910 ","","Mon Jan 13 14:51:51 2003","1","","","" "AA02130","1454173","1454361","189","TTGCCCGCTATATTGCTGACTATCTTTAAGCAGGTCAACTACTTTTTTCCAAACGGCGCAATAAATGGACAAACTCAACGCAATTTAGATAAAATTTGGTGGCGAAGGTCAAAGCCTTTATTGACTCATCAGCCAGCTGGATTTGTGCAGGGTAACACCTTAAAGTGCGGTCGTTTTACAAGGTATTTT","","","7365","LPAILLTIFKQVNYFFPNGAINGQTQRNLDKIWWRRSKPLLTHQPAGFVQGNTLKCGRFTRYF","1454361","","hypothetical protein","Periplasm","There are no significant matches to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:31:49 2004","Wed Feb 25 15:31:49 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02130 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:31:49 2004","","","","","","","","","","","","","1","","","" "AA02131","1455212","1454379","834","ATGACAAAATACGATTTACACTGCCACAGTACGGCGTCCGATGGGGTGTTGTCACCAACGGAGGTGGTGTTGCGGGCACATGAAAAGGGCGTAAATGTGCTGGCGTTGACCGATCATGATACCGTTGCCGGCGTGTCGGAAGCGCGTCAACAAGCGGAAAAATCGGGTATTCGGCTTATTAACGGCGTGGAGATTTCAACCTTATGGGAAAACCGCTCCATTCATATTGTGGGCTTAGGGTTTGATATTTCACATGAAAAATTGACCGCACTTTTAGCGGAGCAAGCGTGTTTGCGTGATATTCGGGCGCAGGAAATCGGGGCAAAACTGGAAAAAATCGGTGTGGAAAATGCTTACGCAGAAGCCAGAAAACTAGCCGGTGAAGGCGAAGTCACCAGAGCGCATTATGCGCGTCATTTAGTGCAAATCGGCAAAGTCTCTAACGACGGGCAAGCCTTTAAACGTTATTTGGGACAGGGCAAGTCTGCTTATGTGAAGCCGCAATGGGCGGACATTCCAACCACCATTGACATTATTCACCAAGCCGGTGGCGCTGCCGTGTTGGCGCATCCGTTGCGTTACACCATGACTATGAAATGGGTGCGAAAACTAGCGGAGAATTTTAAAAGTTGGGGCGGTGATGCCATGGAAATTTCCGGTTGCGGGCAACGTCCCGATCAATTTCAATTGCTGGTAAAACTGGCTGAGGAACACCAATTGGCGGGTTCGATGGGATCGGATTTTCACTTTCCTTGCGCGTGGGTGGAACTAGGAAAACTAAAACCGCTGCCGGAACACATTCCTTTTGTCTTAAATATAAAAAATGACCTTGCC","","","31805","MTKYDLHCHSTASDGVLSPTEVVLRAHEKGVNVLALTDHDTVAGVSEARQQAEKSGIRLINGVEISTLWENRSIHIVGLGFDISHEKLTALLAEQACLRDIRAQEIGAKLEKIGVENAYAEARKLAGEGEVTRAHYARHLVQIGKVSNDGQAFKRYLGQGKSAYVKPQWADIPTTIDIIHQAGGAAVLAHPLRYTMTMKWVRKLAENFKSWGGDAMEISGCGQRPDQFQLLVKLAEEHQLAGSMGSDFHFPCAWVELGKLKPLPEHIPFVLNIKNDLA","1454379","","conserved hypothetical protein (possible TrpH protein)","Cytoplasm","","
InterPro
IPR003141
Domain
Polymerase and histidinol phosphatase, N-terminal
SM00481\"[4-69]TPOLIIIAc
InterPro
IPR004013
Domain
PHP, C-terminal
PF02811\"[4-252]TPHP
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.140\"[1-68]Tno description
PTHR11276\"[5-65]TDNA POLYMERASE TYPE-X FAMILY MEMBER
PTHR11276:SF1\"[5-65]TDNA POLYMERASE TYPE-X FAMILY MEMBER


","BeTs to 12 clades of COG0613COG name: Predicted metal-dependent phosphoesterases (PHP family)Functional Class: RThe phylogenetic pattern of COG0613 is aom--z-qvd--bcefgh-n------Number of proteins in this genome belonging to this COG is","Significant hit ( 3.1e-13) to 2/3 blocks of the IPB003141 family, which is described as \"PHP domain N-terminal region\". Interpro entry for IP:IPR003141. IPB003141A 2-39 5.3e-12 IPB003141B 136-151 16","Residues 1 to 194 match (1e-09) PD:PD308241 which is described as PROTEOME COMPLETE VNG2493C ","","","","","","","","","","","","Fri Jan 31 15:46:38 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02131 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 132 to 257 (E-value = 1.2e-12) place AA02131 in the PHP_C family which is described as PHP domain C-terminal region (PF02811)","","","","","","","","1","","","" "AA02132","1456245","1455229","1017","ATGTATTCTTTGATTCGTAAAGGGATTTTCGCCCTTGATGCCGAAAATGCCCATAACCTAGCCATAAAAACCCTTGCTTTGGCAGCCTATCCGCCGTTACATTTTCTGTTAAAACAGCTTTTAAATTGCCCGTCGGGTACGCCGAAAACCGTCATGGGTATTACGTTTAAAAACCCTATCGGCTTGGCGGCGGGCGCAGATAAAAACGGCGAAGCCATTGATGGTTTCGGCGCCATGGGATTCGGTTTTATTGAAGTGGGCACCGTCACGCCTTTAGCGCAAGAGGGCAATGCAAAGCCGCGTCAATTCCGTTTAATTGAAGCGGAGGGTATTATTAATCGCAACGGTTTCAATAATTATGGTATCGATCATCTCATTGAAAACGTGAAAAAAGCCAAATACGACGGTGTGCTTGGCATTAATATCGGTAAAAATAAGCTAACGCCATTAGAACAAGGCAAGGATGATTACATCATTTGCCTCAATAAAGCCTATAACTATGCGGGCTACATCACCGTAAATATTTCTTCGCCGAATACGCCGGATTTACGTCAATTACAATACGGCGATTATTTTGATGATTTGCTGCAAAGCATTAAAAGACGCCAACAAGCGCTGGCGGAACAATATCAAAAATATGTACCTATTGCGGTGAAAATCGCCCCGGATTTAACGGAAGCGGAGCTGGTTCAAATTGCCGATACGTTATTACGTCATAAAATGGACGGCGTGATTGCCACCAATACGACAATTTCTCGCGACAACGTCACAAATTTAAAAAATGCCGAACAGCAGGGCGGATTAAGCGGAAAACCGCTACAACATAAAAGCACGGTAATTATCGCCCGATTACATCAGGAACTAAAAGGACAAATCCCAATTATCGGCAGTGGCGGCATTGACGGTGTACAAAACGCACAAGAAAAAATCCGGGCGGGCGCCGAGCTTTTGCAAGTGTATTCAGGATTGATTTACCACGGACCGAAATTGGTGAAAACATTAGTTGAGGCGATTAAA","","","36975","MYSLIRKGIFALDAENAHNLAIKTLALAAYPPLHFLLKQLLNCPSGTPKTVMGITFKNPIGLAAGADKNGEAIDGFGAMGFGFIEVGTVTPLAQEGNAKPRQFRLIEAEGIINRNGFNNYGIDHLIENVKKAKYDGVLGINIGKNKLTPLEQGKDDYIICLNKAYNYAGYITVNISSPNTPDLRQLQYGDYFDDLLQSIKRRQQALAEQYQKYVPIAVKIAPDLTEAELVQIADTLLRHKMDGVIATNTTISRDNVTNLKNAEQQGGLSGKPLQHKSTVIIARLHQELKGQIPIIGSGGIDGVQNAQEKIRAGAELLQVYSGLIYHGPKLVKTLVEAIK","1455229","[CATALYTIC ACTIVITY] (S)-dihydroorotate + O(2) = orotate + H(2)O(2).[COFACTOR] Binds 1 FMN per subunit.[PATHWAY] Pyrimidine biosynthesis; fourth step.[SUBUNIT] Homodimer.","dihydroorotate dehydrogenase","Cytoplasm","","
InterPro
IPR001295
Domain
Dihydroorotate dehydrogenase, core
PF01180\"[50-339]TDHO_dh
PS00911\"[82-101]TDHODEHASE_1
PS00912\"[294-314]TDHODEHASE_2
InterPro
IPR005719
Family
Dihydroorotate dehydrogenase, class 2
TIGR01036\"[2-339]TpyrD_sub2: dihydroorotate oxidase
InterPro
IPR012135
Family
Dihydroorotate dehydrogenase, classes 1 and 2
PIRSF000164\"[52-339]TDihydroorotate oxidase
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[4-339]Tno description
noIPR
unintegrated
unintegrated
PTHR11938\"[1-339]TFAD NADPH DEHYDROGENASE/OXIDOREDUCTASE
PTHR11938:SF7\"[1-339]TDIHYDROOROTATE DEHYDROGENASE


","BeTs to 22 clades of COG0167COG name: Dihydroorotate dehydrogenaseFunctional Class: FThe phylogenetic pattern of COG0167 is aompkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 7.6e-78) to 8/8 blocks of the IPB001295 family, which is described as \"Dihydroorotate dehydrogenase\". Interpro entry for IP:IPR001295. IPB001295A 53-64 2.1e-07 IPB001295B 80-103 1e-13 IPB001295C 112-121 0.00023 IPB001295D 168-182 2.4e-07 IPB001295E 215-225 0.00031 IPB001295F 232-250 8e-10 IPB001295G 263-276 0.0026 IPB001295H 292-322 9.3e-17","Residues 1 to 53 match (1e-11) PD:PD477119 which is described as DIHYDROOROTATE BIOSYNTHESIS DHODASE PROTEOME DEHYDROGENASE OXIDASE COMPLETE FLAVOPROTEIN DHODEHASE DHOD ","","","","","","","","","","","Mon Jan 13 14:57:26 2003","Mon Jan 13 14:57:26 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02132 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 46 to 339 (E-value = 1.6e-157) place AA02132 in the DHO_dh family which is described as Dihydroorotate dehydrogenase (PF01180)","","","","","Li X, Weinstock GM, Murray BE. Generation of auxotrophic mutants of Enterococcus faecalis. J Bacteriol. 1995 Dec;177(23):6866-73. PMID: 7592480 Frick,M.M., Neuhard,J. and Kelln,R.A. Cloning, nucleotide sequence and regulation of the Salmonella typhimurium pyrD gene encoding dihydroorotate dehydrogenase. Eur. J. Biochem. 194(2): 573-578, 1990. PubMed: 2269282. Larsen,J.N. and Jensen,K.F. Nucleotide sequence of the pyrD gene of Escherichia coli and characterization of the flavoprotein dihydroorotate dehydrogenase. Eur. J. Biochem. 151(1): 59-65, 1985. PubMed: 2992959. ","","Mon Jan 13 14:57:26 2003","1","","","" "AA02134","1458927","1456321","2607","ATGTACGCTAAAGCCAAATACAGAAAAGATTACCAAACCCCCGATTTCACCGTCACCGATATTTATCTTGATTTTCAATTAGAACCGGAAAAAACCATCGTTGTTGCCACAAGTAAATATCAACGTCTTAACGAAAAAAGCACCACATTGCGTTTAGACGGACATGATTTTCAATTTTCCTCCATCAAATTAAACGGCAAACCGTTTTCACAATATCAGCAGGATCACGAAAGTTTAACTTTGGACTTGGTTCAAGTGGCTGCAGAGCAATTTGAACTGGAAATTACCACCGTTTTAAATCCTGCCGCCAATACGTCTTTACAGGGCTTGTATCAATCCGGCGACGCATTTTGTACCCAATGCGAAGCGGAAGGATTTCGTCAGATTACTTATATGTTAGACCGCCCCGATGTGTTGGCGCGTTACACCACTAAAATCACGGCGGACAAAGCCAAATATCCGTATTTGCTTTCTAACGGCAATCGCATTGCCGGTGGTGACTTGGATGATGGACGTCATTGGGTGGAGTGGAATGATCCCTTCCCGAAACCGAGTTATTTATTTGCCTTAGTGGCAGGGGGTTTTGATGTTCTGCAAGACAAATTCGTGACCAAAAGTGGGCGGGAAGTGGCATTGGAATTGTATGTCAATCGCGGCAATTTAGACCGTGCCGATTGGGCGATGCAAAGCCTGAAACGCGCCATGAAATGGGATGAAGACCGTTTTGGTTTGGAATACGACCTGGATATTTACATGATTGTCGCCGTGGATTTCTTCAACATGGGCGCAATGGAAAATAAAGGGTTAAATATCTTTAATGACAAATATGTGCTTGCCAATCCGCAAACCGCAACAGATGATGATTATTTAGCCATTGAAAGCGTCATCGCACACGAATATTTCCATAACTGGACGGGCAACCGCGTGACTTGTCGTGACTGGTTCCAATTAAGTTTAAAAGAAGGCTTGACGGTTTTTCGCGATCAGGAATTTTCCTCCGACACCGGCTCACGCCCGGTAAATCGCATTAATAACGTGAAATTCTTACGCACCGTGCAATTCGCCGAGGATGCCGGCCCGATGGCACATCCGATTCGTCCGGAAAAAGTGATTGAAATGAATAATTTCTATACGGTGACCGTGTATGAAAAAGGCGCAGAAGTCATTCGTATGTTGCACACCTTATTGGGCGAAAAAGGCTTCCAAAAAGGCATGAAGTTATACATCGCGGAAAATGACGGCAAAGCGGCGACCTGTGAAGATTTTGTTTCTGCGATGGAACGTGCCAATGAGTTGGATTTAACCCAATTTCGCCGTTGGTACAGCCAATCCGGTACGCCTGAATTGACCATCAGCGATCGTTATGACGAGAAAAATCATGTGTATCAATTGCAGGTTTCTCAATTAACTCCACCGACCGCCGACCAAATGGAAAAAGTGAATTTACATATTCCGTTGAAAATTGCGTTGTATGACGAAAACGGCGTCGCGCAAACCTTATATGATTCCGAAGGTGTGGTGGATAATGTGTTGAACATTACCCAAAAAGACCAAACGTTTGAATTCCACAATATTTACACCAAACCGGTGCCTGCCTTGTTGTCTGATTTCTCCGCACCGGTGAAATTGGATTATGATTACAAAACCAGCCAGCTGATTACTTTGGTAAAATTTGCTGAAAACGGGTTTATTCGCTGGGATGCAGTGCAAATGTTACTTAACGCAGAGTTACGACGTAACGTAAGTAACTATCAGCAGGGCATTGAGTTAGATTTATCTGCCGAAACGATTGCGGTGCTACAGCAAATTCTGACGAATTATCAAAAAGATATTGAGTTAACCAGTTTGATTTTAACCTTGCCGAAAGCAACCGAGTTCGCCGAATTATTTAAAACCATTGACCCGGATACCATCAGCGCCGTGCGTGAATTCATGGCGCGTGCCATTGCCGAAAATCTGCAGGAATTATTGTTTAAAACCTACAATCAAATTCGCTTGGATGAATATAAAATTGAGCGTCAGGACATTGCTTTACGCAAACTGCGCAACGTTTGTTTGAGCTATCTGGCTTACACCAATATGGGCAATAACCTGGTGAATAAACATTATTCCTATTCCAACAATATGACCGACACGCTTGCGGCGTTAACCGCTGCAACGCAAGCCAAATTGCCTTGCCGCGATAATCTGTTGGCGGATTTTGAACAAAAATGGCAACAAGACGGCTTGGTGATGGACAAATGGTTTGCTTTGCAAGCCAGCCGCCCGGAAGAAAATGTGTTGAACAATGTGATGCAGTTAATGGAGCACCCGAGCTTCAATTTCAATAATCCGAATCGTGTACGTTCGTTAGTCGGCACATTCGCAGGGCAAAATTTAAAAGCCTTCCATGCCATTGACGGTTCCGGCTATCGTTTCTTAACGGATATTTTGATTAAACTGAATAAAAGCAACCCGCAAGTAGCTTCTCGCTTAATTGAACCGTTAATTCGTTTTGTCCGTTATGATGCGCAACGCCAAACGTTGATGAAACGCGCCTTAGAACGTATCAGCGAAACGGAAGATTTATCCCGCGATTTGTACGAGAAAATCGAAAAAGCATTACAG","","","99984","MYAKAKYRKDYQTPDFTVTDIYLDFQLEPEKTIVVATSKYQRLNEKSTTLRLDGHDFQFSSIKLNGKPFSQYQQDHESLTLDLVQVAAEQFELEITTVLNPAANTSLQGLYQSGDAFCTQCEAEGFRQITYMLDRPDVLARYTTKITADKAKYPYLLSNGNRIAGGDLDDGRHWVEWNDPFPKPSYLFALVAGGFDVLQDKFVTKSGREVALELYVNRGNLDRADWAMQSLKRAMKWDEDRFGLEYDLDIYMIVAVDFFNMGAMENKGLNIFNDKYVLANPQTATDDDYLAIESVIAHEYFHNWTGNRVTCRDWFQLSLKEGLTVFRDQEFSSDTGSRPVNRINNVKFLRTVQFAEDAGPMAHPIRPEKVIEMNNFYTVTVYEKGAEVIRMLHTLLGEKGFQKGMKLYIAENDGKAATCEDFVSAMERANELDLTQFRRWYSQSGTPELTISDRYDEKNHVYQLQVSQLTPPTADQMEKVNLHIPLKIALYDENGVAQTLYDSEGVVDNVLNITQKDQTFEFHNIYTKPVPALLSDFSAPVKLDYDYKTSQLITLVKFAENGFIRWDAVQMLLNAELRRNVSNYQQGIELDLSAETIAVLQQILTNYQKDIELTSLILTLPKATEFAELFKTIDPDTISAVREFMARAIAENLQELLFKTYNQIRLDEYKIERQDIALRKLRNVCLSYLAYTNMGNNLVNKHYSYSNNMTDTLAALTAATQAKLPCRDNLLADFEQKWQQDGLVMDKWFALQASRPEENVLNNVMQLMEHPSFNFNNPNRVRSLVGTFAGQNLKAFHAIDGSGYRFLTDILIKLNKSNPQVASRLIEPLIRFVRYDAQRQTLMKRALERISETEDLSRDLYEKIEKALQ","1456321","[FUNCTION] Aminopeptidase n is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation. [CATALYTIC ACTIVITY] RRelease of an N-terminal amino acid, Xaa-|-Xbb- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.","aminopeptidase N","Cytoplasm, Inner membrane, Extracellular","","
InterPro
IPR001930
Family
Peptidase M1, membrane alanine aminopeptidase
PTHR11533\"[99-834]TPROTEASE M1 ZINC METALLOPROTEASE
InterPro
IPR006025
Binding_site
Peptidase M, neutral zinc metallopeptidases, zinc-binding site
PS00142\"[295-304]?ZINC_PROTEASE
InterPro
IPR012779
Family
Peptidase M1, alanyl aminopeptidase
PTHR11533:SF8\"[99-834]TAMINOPEPTIDASE
TIGR02414\"[10-868]TpepN_proteo: aminopeptidase N
InterPro
IPR014782
Domain
Peptidase M1, membrane alanine aminopeptidase, N-terminal
PR00756\"[127-142]T\"[177-192]T\"[259-269]T\"[295-310]T\"[314-326]TALADIPTASE
PF01433\"[14-385]TPeptidase_M1


","No hits to the COGs database.","Significant hit ( 4.5e-31) to 5/5 blocks of the PR00756 family, which is described as \"Membrane alanyl dipeptidase (M1) family signature\". Prints database entry for PR:PR00756. PR00756A 127-142 0.00025 PR00756B 177-192 0.0017 PR00756C 259-269 0.00046 PR00756D 295-310 4.7e-09 PR00756E 314-326 0.0031","Residues 1 to 50 match (1e-12) PD:PD583293 which is described as AMINOPEPTIDASE PROTEOME COMPLETE N HYDROLASE ZINC ALPHA-AMINOACYLPEPTIDE METALLOPROTEASE PEPN MEMBRANE ","","","","","","","","","","","Mon Jan 13 15:06:51 2003","Mon Jan 13 15:06:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02134 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 13 to 385 (E-value = 3.3e-95) place AA02134 in the Peptidase_M1 family which is described as Peptidase family M1 (PF01433)","","","","","Foglino,M., Gharbi,S. and Lazdunski,A. Nucleotide sequence of the pepN gene encoding aminopeptidase N of Escherichia coli Gene 49 (3), 303-309 (1986) PubMed: 2436977 McCaman,M.T. and Gabe,J.D. The nucleotide sequence of the pepN gene and its over-expression in Escherichia coli Gene 48 (1) , 145-153 (1986) PubMed: 3549459 McCaman,M.T. and Gabe,J.D. Sequence of the promoter and 5' coding region of pepN, and the amino-terminus of peptidase N from Escherichia coli K-12. Mol. Gen. Genet. 204 (1): 148-152 (1986) [PubMed: 3018440].Bally,M., Foglino,M., Bruschi,M., Murgier,M. and Lazdunski,A.Nucleotide sequence of the promoter and amino-terminal encoding region of the Escherichia coli pepN gene. Eur. J. Biochem. 155 (3): 565-569 (1986) [PubMed: 2869947].","","Mon Jan 13 15:06:51 2003","1","","","" "AA02135","1459026","1459127","102","TTGTGTAAATATTATTTCCTAAAACCGGCAAAGCCTCTGAAATCCCTGTGTTTAAATAACCTAAATACGCTGTGTAAAACACCGAAAAGACTGACCGCACTT","","","3893","LCKYYFLKPAKPLKSLCLNNLNTLCKTPKRLTAL","1459127","","hypothetical protein","Cytoplasm","There are no significant matches to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:30:29 2004","Wed Feb 25 15:30:29 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02135 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:30:29 2004","","","","","","","","","","","","","1","","","" "AA02135.1","1459143","1458952","192","TTGATCGCATCAGCTAAAGTGCGGTCAGTCTTTTCGGTGTTTTACACAGCGTATTTAGGTTATTTAAACACAGGGATTTCAGAGGCTTTGCCGGTTTTAGGAAATAATATTTACACAAACGTTTGGATAAGGTTGCGGAAGAAAATCTATTTGCAACTTAGCGCTAAAAATCATATCCTTAACGGCAATTTT","11.00","6.21","7231","LIASAKVRSVFSVFYTAYLGYLNTGISEALPVLGNNIYTNVWIRLRKKIYLQLSAKNHILNGNF","","","hypothetical protein","Cytoplasm, Extracellular","No significant hits in gapped BLAST.AA02135.1 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus ducreyi gene.AA02135.1 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus influenzae Rd gene.","
noIPR
unintegrated
unintegrated
signalp\"[1-29]?signal-peptide


","No hits to the COGs database.","","","Fri Feb 27 12:04:21 2004","Sat Feb 28 17:11:00 2004","Sat Feb 28 17:11:00 2004","Sat Feb 28 17:11:00 2004","Fri Feb 27 12:04:21 2004","Fri Feb 27 12:04:21 2004","Fri Feb 27 12:04:21 2004","Fri Feb 27 12:04:21 2004","Fri Feb 27 12:04:21 2004","Fri Feb 27 12:04:21 2004","Fri Feb 27 12:04:21 2004","Fri Feb 27 12:04:21 2004","Fri Feb 27 12:04:21 2004","Fri Feb 27 12:04:21 2004","Fri Feb 27 12:04:21 2004","Fri Feb 27 12:04:21 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02135.1 has no significant similarity (blastp p-value < 1e-03) to any other gene in this genome.AA02135.1 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Fri Feb 27 12:04:21 2004","Fri Feb 27 12:04:21 2004","No hits to the PDB database.","","","No significant hits to the Pfam 7.7 database.","Fri Feb 27 12:04:21 2004","","","","","","","1","Fri Feb 27 12:04:21 2004","","" "AA02136","1459349","1460536","1188","ATGTTTGAAAATATTGTTGCCGCTCCGGCAGATCCGATTTTAGGTTTAGGCGAAGCATTCAAAGCGGAGACCCGCGCTAACAAAATCAATTTAGGCATTGGCGTATATAAAGACGCAAAAGGCAATACGCCTATCGTAAAAGCAGTAAAAGAAGCGGAAAAACGCTTGTTAGAACAAGAAAATACCAAAAACTACCTGCCGATTGACGGCGTTGCCGATTTCAACGCACGCACCAAAGAACTCTTATTCGGCGCCGATTCCGACATCGTGAAAAATAACCGTGCCAGAACCGTGCAAAGTTTAGGCGGAACCGGCGCATTACGCATTGCAGCGGAATTTATTAAACGTCAAACTAAAGCACAAAATGTTTGGATCAGCACGCCGACCTGGCCGAATCACAACGCCATTTTTAATGCCGTGGGCATGACCATTCGCGAATACCGTTATTACAACCCGCAAACCAAAGCCTTGGATTGGGATAATTTAATCGCCGATTTAAGCCAGGCCGGTGAAGGCGATGTGGTGTTATTCCACGGTTGCTGCCACAACCCGACCGGTATCGACCCGACCCCCGAACAATGGAATAAATTGGCGGAAATGTCGGAGAAAAAAGGCTGGCTACCTTTATTCGATTTTGCTTATCAAGGTTTCGCTAACGGCTTGCAGGAAGATGCTTACGGCCTACGCGCCTTTGCAAAAAATCACAAAGAACTCTTGGTAGCAAGCTCTTTCTCGAAAAACTTCGGGTTATATAATGAGCGTGTAGGGGCTTTCACCGTCGTAGCGGAAAACGCCGACATCGCCGCAACGGCATTGACCCAAGTGAAAATCATCGTCCGCACCCTCTACTCCAACCCGTCGGCACACGGTGCCACCGCCGTCGCCTTGGTGTTAAACGACGCGCAATTACGCCGCGATTGGGAAAATGAATTAACCGAAATGCGCGATCGCATTAAACAAATGCGTCACCTTTTCGTGCAGTTATTGAAAGAATACGGCGCGCAACAAGATTTTGGTTTTATCATCAATCAAAACGGTATGTTCTCTTTCAGCGGCTTAACCGCTGAACAGGTTGACCGTCTGAAAAACGAATTCGCCATTTACGCCGTGCGTTCCGGACGCATTAACGTTGCCGGCATTACCGAAGGTAACATTCGTTACCTCTGCGAAAGCATTGTAAAAGTGTTG","","","47141","MFENIVAAPADPILGLGEAFKAETRANKINLGIGVYKDAKGNTPIVKAVKEAEKRLLEQENTKNYLPIDGVADFNARTKELLFGADSDIVKNNRARTVQSLGGTGALRIAAEFIKRQTKAQNVWISTPTWPNHNAIFNAVGMTIREYRYYNPQTKALDWDNLIADLSQAGEGDVVLFHGCCHNPTGIDPTPEQWNKLAEMSEKKGWLPLFDFAYQGFANGLQEDAYGLRAFAKNHKELLVASSFSKNFGLYNERVGAFTVVAENADIAATALTQVKIIVRTLYSNPSAHGATAVALVLNDAQLRRDWENELTEMRDRIKQMRHLFVQLLKEYGAQQDFGFIINQNGMFSFSGLTAEQVDRLKNEFAIYAVRSGRINVAGITEGNIRYLCESIVKVL","1460536","","aspartate aminotransferase","Cytoplasm","","
InterPro
IPR000796
Family
Aspartate/other aminotransferase
PR00799\"[175-194]T\"[206-220]T\"[241-261]T\"[273-298]T\"[341-359]T\"[367-385]TTRANSAMINASE
PTHR11879\"[1-396]TASPARTATE AMINOTRANSFERASE
InterPro
IPR004838
Binding_site
Aminotransferases class-I pyridoxal-phosphate-binding site
PS00105\"[243-256]TAA_TRANSFER_CLASS_1
InterPro
IPR004839
Domain
Aminotransferase, class I and II
PF00155\"[26-392]TAminotran_1_2
InterPro
IPR015421
Domain
Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10\"[45-314]Tno description


","BeTs to 8 clades of COG1448COG name: Aspartate/aromatic aminotransferaseFunctional Class: EThe phylogenetic pattern of COG1448 is ------y-------efghsn-j-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 5e-15) to 3/3 blocks of the IPB001511 family, which is described as \"Aminotransferases class-I\". Interpro entry for IP:IPR001511. IPB001511A 65-75 1.4 IPB001511B 176-190 2.4e-05 IPB001511C 243-256 1.8e-05","Residues 2 to 114 match (8e-09) PD:PD483751 which is described as PHOSPHATE 1700083M11RIK PYRIDOXAL ","","","","","","","","","","","","Mon Jan 13 15:19:46 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02136 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 80 to 396 (E-value = 8.5e-111) place AA02136 in the Aminotran_1_2 family which is described as Aminotransferase class I and II (PF00155)","","","","","Kuramitsu,S., Okuno,S., Ogawa,T., Ogawa,H. andKagamiyama,H. Aspartate aminotransferase of Escherichia coli: nucleotide sequence of the aspC gene J. Biochem. 97 (4), 1259-1262 (1985) PubMed: 3897210 Fotheringham,I.G., Dacey,S.A., Taylor,P.P., Smith,T.J., Hunter,M.G., Finlay,M.E., Primrose,S.B., Parker,D.M. and Edwards,R.M. The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes Biochem. J. 234 (3), 593-604 (1986) PubMed: 3521591 Kondo,K., Wakabayashi,S., Yagi,T. and Kagamiyama,H. The complete amino acid sequence of aspartate aminotransferase from Escherichia coli: sequence comparison with pig isoenzymes. Biochem. Biophys. Res. Commun. 122 (1): 62-67 (1984) [PubMed: 6378205].Kondo,K., Wakabayashi,S. and Kagamiyama,H. Structural studies on aspartate aminotransferase from Escherichia coli. Covalent structure. J. Biol. Chem. 262 (18): 8648-8657 (1987) [PubMed: 3298240].Inoue,K., Kuramitsu,S., Okamoto,A., Hirotsu,K., Higuchi,T. and Kagamiyama,H. Site-directed mutagenesis of Escherichia coli aspartate aminotransferase: role of Tyr70 in the catalytic processes. Biochemistry 30 (31): 7796-7801 (1991) [PubMed: 1868057].Yano,T., Kuramitsu,S., Tanase,S., Morino,Y., Hiromi,K. and Kagamiyama,H. The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase. J. Biol. Chem. 266 (10): 6079-6085 (1991) [PubMed: 2007566].Smith,D.L., Almo,S.C., Toney,M.D. and Ringe,D. 2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli. Biochemistry 28 (20): 8161-8167 (1989) [PubMed: 2513875].","","Mon Jan 13 15:19:46 2003","1","","","" "AA02137","1461153","1460593","561","ATGAATAATCAGGATGTTCGGGTGCTTCGAACCGATAGACTTATTCGTGATGCGTTTTTGACATTGTTGGCAGAAAAAGGCTTTGAAGCCATGACGGTACAGGATATTTTGGATCTGACGAAAATTAACCGTTCTACCTTTTATAAGCATTTCGCCAATAAAAACGCCGTGGCGAAAATGCTGGTGGAAGAGCTCAAAGCCTTGGTGGCGGAACGATTAAAACAGCGTTTTTCCGTGCCGACAAAGGAATTTATTCATAGCGTCCAACCGCTTTTTGAACAACATCACCAACTGATTTACCTGATCGGTCAAATCGAAACACCGAAAATTCATTTATATAACGACATTCATAAAATGGTTAAAGAAAAATATGTTGAACATTTGAAAACTGAAAAGGCACAAATCTCCCAAAATGCAGATTTGGATTTTCAAGGTCACCTGTTCGCTACCATGACGCTAGGCATAATGAAATATATTATTGAAAAGGGCGAAATGCCACAGGTGGAGGCACTGATAGAAAATGTGAATTCGGTGTTTGATATGTTTATGGTTCAAGAGGTG","","","21965","MNNQDVRVLRTDRLIRDAFLTLLAEKGFEAMTVQDILDLTKINRSTFYKHFANKNAVAKMLVEELKALVAERLKQRFSVPTKEFIHSVQPLFEQHHQLIYLIGQIETPKIHLYNDIHKMVKEKYVEHLKTEKAQISQNADLDFQGHLFATMTLGIMKYIIEKGEMPQVEALIENVNSVFDMFMVQEV","1460593","","transcriptional regulators (TetR/AcrR family)","Cytoplasm","","
InterPro
IPR001647
Domain
Bacterial regulatory protein, TetR
PR00455\"[15-28]T\"[36-59]THTHTETR
PF00440\"[15-61]TTetR_N
PS50977\"[9-69]THTH_TETR_2
InterPro
IPR012287
Domain
Homeodomain-related
G3DSA:1.10.10.60\"[9-58]Tno description


","BeTs to 11 clades of COG1309COG name: Transcriptional regulatorFunctional Class: KThe phylogenetic pattern of COG1309 is aom-k--qvdrlbcefghsnuj---wNumber of proteins in this genome belonging to this COG is","Significant hit ( 4.5e-08) to 1/1 blocks of the IPB001647 family, which is described as \"Bacterial regulatory proteins, TetR family\". Interpro entry for IP:IPR001647. IPB001647 27-57 4.4e-08","","","","","","","","","","","","","Mon Jan 13 15:22:18 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02137 is paralogously related to AA01511 (1e-04).","","","","","","Residues 15 to 61 (E-value = 3.1e-10) place AA02137 in the TetR_N family which is described as Bacterial regulatory proteins, tetR family (PF00440)","","","","","","","","1","","","" "AA02139","1461301","1462278","978","ATGAAAGCAAAATATTTCGTGTTCGGTTTCATTATTATCGGTGCCGTCGGTTTCGCCATTTGGAAAAACAGGCAATTACAGGCCAGTGAACTGAACGGCATTGCGGCAGTTAACGGACGTTTGGAATTAAAACGGCTGGACATTGCCACCCTTTATCCCGGCCGTGTAGAAGGAATTTTGGTGCAGGAAGGTAATGAAGTAAAACGCAATCAACCACTGGCACGGCTTTCTTCCAGCATTTCGCAAGCGCAGGTTTCCGCCGCACAGGCACAAAAGAAACGGGCGGAAGAATCCGTTGCCCGCGCCCTATCAGAAATTGATGCCCGCCAACAACAAGTCAACGTAACGAAATTGGAATTGAATAACGCACAAAAATTGCGCCTCGATAATCTGATTTCAAGCAGCGAATTAGAACACCGCCAAGCCGCTTATAAGGCGTCACTCGCTGCCGTGAACACCACGCAAGCCGCCAAAGCCGAAGCACAAGCCGCCGTCGCACAGGCGCAAGCGCAGTTAGAACAAGCGCAATCGCAAAATACCGATATGCTGATTAAAGCGCCGAAAGACGGACGGGTGGAATATCAAATTGCGGAAGTAGGCAATGTTCTCGGTGCCGGTGGCAAAGTGGTCAGTTTGCTCGATCCGACGGATACCTATATCAATGTTTTCCTCACTGCGCCACAAATGAATCAACTAAAATTGGGGGATGAGGCCCGCATAGTGATTGATGGCATGGATGCCGTTTTCCCCGCCAACATTACGTTCATCGCCAATAACGCGCAATTCACCCCCAAATCCGTGGAAACCACGGAAGAACGCGCCAAATTGATGTTTAAGGTGAAATTGCAGCTTCCCGTGGATATTGCACTGAAATATAAGCTTTTATTAAAAGGCGGCATGACGGGGCTGGGCTATGTGAAATACGATCAGCAGGCGCAATGGCCGGCACAGTTAAACGTGAGACTTCCGCAGGGTGAA","","","35619","MKAKYFVFGFIIIGAVGFAIWKNRQLQASELNGIAAVNGRLELKRLDIATLYPGRVEGILVQEGNEVKRNQPLARLSSSISQAQVSAAQAQKKRAEESVARALSEIDARQQQVNVTKLELNNAQKLRLDNLISSSELEHRQAAYKASLAAVNTTQAAKAEAQAAVAQAQAQLEQAQSQNTDMLIKAPKDGRVEYQIAEVGNVLGAGGKVVSLLDPTDTYINVFLTAPQMNQLKLGDEARIVIDGMDAVFPANITFIANNAQFTPKSVETTEERAKLMFKVKLQLPVDIALKYKLLLKGGMTGLGYVKYDQQAQWPAQLNVRLPQGE","1462278","","possible membrane protein","Periplasm, Inner membrane, Outer membrane","","
InterPro
IPR006143
Family
Secretion protein HlyD
PF00529\"[44-307]THlyD
noIPR
unintegrated
unintegrated
signalp\"[1-17]?signal-peptide
tmhmm\"[5-23]?transmembrane_regions


","BeTs to 8 clades of COG0845COG name: Membrane-fusion proteinFunctional Class: QThe phylogenetic pattern of COG0845 is -------qvd-lbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 3.7e-09) to 2/3 blocks of the IPB002215 family, which is described as \"HlyD family secretion protein\". Interpro entry for IP:IPR002215. IPB002215A 42-78 5.1e-06 IPB002215B 183-217 0.24Significant hit ( 3e-05) to 1/7 blocks of the PR01490 family, which is described as \"Gram-negative bacterial RTX secretion protein D signature\". Prints database entry for PR:PR01490. PR01490B 56-76 3e-05","Residues 184 to 284 match (1e-07) PD:PD561729 which is described as PREDICTED PROTEOME PERMEASE EFFLUX COMPLETE CATION PUMP ","","","","","","","","","","","","Tue Mar 16 15:39:11 2004","","","Tue Mar 16 15:39:11 2004","Tue Mar 16 15:39:11 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02139 is paralogously related to AA01340 (1e-08), AA01732 (2e-06) and AA02081 (3e-04).","Tue Mar 16 15:39:11 2004","","","","","Residues 44 to 307 (E-value = 2.6e-12) place AA02139 in the HlyD family which is described as HlyD family secretion protein (PF00529)","Tue Mar 16 15:39:11 2004","","","","","","","1","","","" "AA02140","1462284","1465025","2742","ATGACAGCCATTCGACCTGCCGTTGCGGTGGAACATCTCTCACATTCATACGGAAAAACTACCGCACTTTATGATGTCAGCCTGCGCATTCCCCGTGGCGCGACCGTCGGGCTAATCGGACCGGACGGCGTGGGCAAATCCACGCTGCTTTCCCTCATCGCGGGTGTCAAAATAATTCAGACCGGCAGCGTGCAGGTGTTTGATTTAAATGTCGCGGAGAAAAAAGCGCGGGATGCCCTTTCTCATAAAATCGCCTTTATGCCGCAAGGGCTGGGCAAAAATCTGTATCTCACCCTGTCCATTTATGAAAATATTGATTTTCACGCCCGCCTGTTCGGATTAAACAAACCACAACGGCAAGCCCGCATTCAGCGCTTATTGAATGCCACGGGGTTAGCTCCTTTTGCCGATCGGGCGGCAGGCAAATTATCGGGCGGGATGAAGCAAAAACTCAGCCTTTGTTGCGCCTTGGTGCACAGCCCCGATTTATTAATTTTAGATGAACCCACTACCGGCGTGGATCCGCTCTCCCGCCGTCAATTCTGGCAATTGGTGGAGGATTTACGCCGTGAAGAAAACGGCATGACGGTGATTGTGGCGACGGCATACATTGACGAAGCGGAACGTTTTGAACATATTCTTGCCATGGATGACGGCAAGCTCATCGCCAATGCGCCCACTAAGCAGGTGATTGCCGACACGCAAAGTCACAATCTGGAAGAAGCCTATGTCAAATTGCTGCCGGCAGAAAAACGCGGTGCGGAAAACGGCTTGCATATTCAGCCCTTTAAACCCAATGCCGAGAAACCGCCGGTTATCGTTGCCAAAGGTTTAACCAAGAAATTCGGTGATTTCGTTTCGGTGGATAACGTCAGTTTTACCATTCCGAAAGGAGAAATTTTCGGCTTTTTAGGCTCCAACGGTTGCGGCAAATCCACCACCATGAAAATGCTTACCGGCTTGCTGGATCCGACGGAAGGCTCTGCCACGCTGCTCGGTCAGCCTATTGATGCGGGCAATATCGACACGCGAAAACGGGTGGGTTATATGTCCCAAGCGTTTTCCTTATATGAAGAACTCAGCGTTTATCAAAATCTGGAATTGCACGCCAAGCTCTATCAAACTCCCCGCGCGCAATGGGCACACTATGTGCAATCCGTCATGCAGCAATTCGATTTAATTCAACTTGCCGATGAATACCCTTCCGCGCTGCCTCTTGGCATTCGGCAACGTTTGCAGCTTGCCGCCGCCTGTTTGCATAAACCCGAAGTGCTGATTCTGGACGAACCTACTTCAGGGGTTGACCCCGCCGCGCGGGATATGTTCTGGGAATATCTGATTAAACTGTCGCGCGAAGATAAAATCACCATTTTCGTCACCACCCATTTTATGAACGAAGCGGCGCGTTGTGATCGCATTTCCTTTATGCACCGTGGGCGTGTGTTGGCGGTAGGCACGCCGGAATCGCTACGTCTTGAGAAAAAAGCCCCGACGCTGGAAGAAGCCTTTATCGCTTATCTGGAAGAACAGGCGGATGACATTACCGCGCCTAAAATGGATAAACGCGATCAAAGTGCGGTCAATATTTCAGGTGTTTCTGCCGATTCGCCGGAAAAAGGCATACTGGCGTGGTGGTCGTTGGTGTGGACGTTTGCGGTACGGGAAGGAAAAGAATTATTACGGGATCGCATTCGTTTATTTTTCGCCTTGCTCGGTCCGGTGATTATGTTGTTCGCCATGGCATCCAGTATTTCTTTTGACGTACATCCGTCGAATTTTACCGTGCTGGATTATGACAACAGCTCGGAAAGCCGCCGTTTTATCGAATATTTCGACGGATCCCGCTATTTCGTGCGCCAACCGGATATTCATTCTCCGCAGGAAATTAATCAGGTGTTGCAATCTTCAAAAGTGAAACTGGTGATTGAAATCCCCCCTGATTTCGGCAAAAAAGTGTTGCAACGACAAATGCCGGAAGTGGGCTTTTTTATCGACGGCGCCTTTCCTTCCACCGCTGAAAATCTGCGCGGCTCCGTGGTGGGTGCAATCAACCAATATGTGCAGGAAACCTTAACGCAACAAGGAGTTAACGTTCCGAACAATACCGTGCTGGAACCCCGCTTTGTGTACAACCCGGATTTTAAAAGCATTTTCGCCATGACACCAGGCGTGATCATGCTTACCATGATGTTGATTCCGTCCATGATGACGGCGTTAGGCGTGGTGCGTGAAAAAGAAATCGGCTCCATTATGAATCTGTACGGCTCCCCTGCCGGTGCGGTGCAATTTTTGCTCGGTAAACAACTGCCTTACATTTTGCTGGCGTTTATCAGTTATCTGATTATGGTGTGGATGTCGGTGATGGTCTTTAACGTGCCGGTCAAAGGCTCTATGTGGGCAATGACCTTGGGGGCACTTTTTATTATCACCGCCTCAACGGCGTTCGGGCTGTTCGTTTCCAGCTTTGTAAAATCGCAAATTGCGGCGATTTTCGCCACGGCAATTATCGTGATTATCCCGACCATGAACTTCTCCGGCATGCTTTATCCGACATCCACCCTGCCGCCTCATGTTTATATGGTCGCACAACTCTTCCCCGGTTATTGGTTTCTGATTATCAGCTTAGGCGGTTTCACGAAAGGATTGGGTTTTATGGATTTTCTCAGTAGCTACGGCGCGTTGTTGGCGATTTACGCCGTGTATTTCTGCGGGGCGGTCGCCCTGTTGAAGAAACAGGAGAAA","","","101175","MTAIRPAVAVEHLSHSYGKTTALYDVSLRIPRGATVGLIGPDGVGKSTLLSLIAGVKIIQTGSVQVFDLNVAEKKARDALSHKIAFMPQGLGKNLYLTLSIYENIDFHARLFGLNKPQRQARIQRLLNATGLAPFADRAAGKLSGGMKQKLSLCCALVHSPDLLILDEPTTGVDPLSRRQFWQLVEDLRREENGMTVIVATAYIDEAERFEHILAMDDGKLIANAPTKQVIADTQSHNLEEAYVKLLPAEKRGAENGLHIQPFKPNAEKPPVIVAKGLTKKFGDFVSVDNVSFTIPKGEIFGFLGSNGCGKSTTMKMLTGLLDPTEGSATLLGQPIDAGNIDTRKRVGYMSQAFSLYEELSVYQNLELHAKLYQTPRAQWAHYVQSVMQQFDLIQLADEYPSALPLGIRQRLQLAAACLHKPEVLILDEPTSGVDPAARDMFWEYLIKLSREDKITIFVTTHFMNEAARCDRISFMHRGRVLAVGTPESLRLEKKAPTLEEAFIAYLEEQADDITAPKMDKRDQSAVNISGVSADSPEKGILAWWSLVWTFAVREGKELLRDRIRLFFALLGPVIMLFAMASSISFDVHPSNFTVLDYDNSSESRRFIEYFDGSRYFVRQPDIHSPQEINQVLQSSKVKLVIEIPPDFGKKVLQRQMPEVGFFIDGAFPSTAENLRGSVVGAINQYVQETLTQQGVNVPNNTVLEPRFVYNPDFKSIFAMTPGVIMLTMMLIPSMMTALGVVREKEIGSIMNLYGSPAGAVQFLLGKQLPYILLAFISYLIMVWMSVMVFNVPVKGSMWAMTLGALFIITASTAFGLFVSSFVKSQIAAIFATAIIVIIPTMNFSGMLYPTSTLPPHVYMVAQLFPGYWFLIISLGGFTKGLGFMDFLSSYGALLAIYAVYFCGAVALLKKQEK","1465025","","ABC transporter ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR000412
Family
ABC-2
PS51012\"[680-912]TABC_TM2
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[143-185]T\"[404-446]TQ6NBZ4_RHOPA_Q6NBZ4;
PF00005\"[33-219]T\"[298-479]TABC_tran
PS50893\"[8-243]T\"[273-503]TABC_TRANSPORTER_2
PS00211\"[143-157]?ABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[32-220]T\"[297-488]TAAA
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[674-849]Tno description
InterPro
IPR013525
Domain
ABC-2 type transporter
PF01061\"[696-879]TABC2_membrane
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[2-234]T\"[267-494]Tno description
PTHR19222\"[273-534]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF16\"[273-534]TABC TRANSPORTER
tmhmm\"[566-586]?\"[723-743]?\"[772-792]?\"[802-822]?\"[828-848]?\"[858-878]?\"[888-908]?transmembrane_regions


","BeTs to 15 clades of COG1131COG name: ABC-type multidrug transport system, ATPase componentFunctional Class: QThe phylogenetic pattern of COG1131 is aompkzy-vdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is","Significant hit ( 1e-33) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 287-333 1.3e-14 IPB001140B 401-439 2.8e-11 IPB001140C 456-485 8.6e-05 IPB001140C 196-225 0.47Significant hit ( 4.9e-05) to 1/5 blocks of the IPB001324 family, which is described as \"Phosphoribulokinase family\". Interpro entry for IP:IPR001324. IPB001324A 297-318 4.9e-05","Residues 143 to 208 match (4e-08) PD:PD328804 which is described as ATP-BINDING PROTEOME COMPLETE ABC TRANSPORTER DNA REPAIR REPEAT C24F3.5 CG1801 ","","","","","","","","","","","","Mon Jan 13 15:28:42 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02140 is paralogously related to AA00207 (8e-32), AA02786 (3e-31), AA02718 (3e-28), AA02353 (5e-28), AA00700 (2e-26), AA02320 (3e-26), AA00415 (5e-26), AA00751 (8e-26), AA02484 (9e-25), AA01051 (3e-24), AA01656 (3e-23), AA02573 (3e-22), AA02440 (6e-22), AA00858 (1e-21), AA02324 (5e-21), AA01645 (5e-21), AA02080 (1e-20), AA01456 (2e-20), AA01824 (6e-19), AA02899 (1e-18), AA02225 (1e-18), AA02550 (2e-18), AA00799 (4e-18), AA01867 (6e-18), AA01616 (6e-18), AA01820 (1e-17), AA01422 (1e-17), AA02642 (2e-16), AA01510 (2e-16), AA02152 (3e-16), AA01779 (5e-16), AA02898 (1e-15), AA01568 (1e-15), AA01684 (2e-15), AA02805 (3e-15), AA01961 (5e-15), AA01524 (1e-14), AA00933 (3e-14), AA01555 (1e-13), AA02606 (2e-13), AA02141 (2e-13), AA02609 (3e-13), AA01393 (2e-12), AA01509 (5e-12), AA01757 (1e-11), AA02331 (1e-10), AA01947 (1e-10), AA00591 (9e-09), AA00061 (2e-08), AA01569 (3e-08), AA02146 (9e-06), AA02226 (1e-05), AA00934 (3e-05) and A02145 (0.001).","","","","","","Residues 298 to 479 (E-value = 3e-50) place AA02140 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Allikmets,R., Gerrard,B., Court,D. and Dean,M. Cloning and organization of the abc and mdl genes of Escherichia coli: relationship to eukaryotic multidrug resistance Gene 136 (1-2), 231-236 (1993) PubMed: 7904973 ","","Mon Jan 13 15:28:42 2003","1","","","" "AA02141","1465030","1466154","1125","ATGTTCAGATGGATAAAAAATGTGTTTTATTTATCGGGCAAAGAACTGCGCAGTTTATTTTCCGATCCGGTTCTGGTGGTGTTAATTATTTATATGTTCACCGTCGCTATTTACACCGTTGCCAATTCGATTACCTTGGAAGTGAAAAATGCCTCCGTTGCCATTGTGGATAACGATCACTCGGCGTTGTCTTATCGCCTGCAACAAAGCCTGATTACGCCGAACTTCCGTAAAGTGCATACAATTCATGCACAACAGGCGGATCGCCTGATGGACACAGGAGAATATACGTTCATTTTAGATATTCCGCCGAATTATGAACGTGATGTACTTGCGGGGCGTAACCCGCTGATTCAGTTATTATCCGACGCCACGGCAATGACGCAAGCCGCCATCGGTTCCGCTTATATTTCACAAATTTTTCACGGTGAAATTAACGATTTTCTGCGCCTTCAAAGCAATAACGGCATACTCATTCAACCCACCATTAATGTGCTTTATAACCCGAATTTTTCCGGTAACTGGTTTATGGGCGGCATGAACATTGTGGGCTATTTGAATTTATTAACCATGTTGCTGGTGGGCGCCGCTGTCATTCGGGAACGGGAGCGCGGCACGCTGGAACATATTTTGGTGATGCCCGTACGCTCCAGCGAAATTGCTATGGCGAAAATCGTGGCGAACGAACTGGTGTTGCTCACCGTCGTGATGTTTTCACTCTATTTTGTGGTGCATAAAATCATCGGCACGCCCCTGCCGCAAGGTGCCTTTTCGCTTTATATTTTAGGCGCGGCAGTGTTTATTTTTTCCATTGCCTCCCTTGGCATTATGCTGGCGATTTTTGCCCCGACCATGCCTCAATTCGGTTTGTTGGTTCTGCCGGTGTATATCACGATGTATCTGCTTTCCGGCACCATGTCGCCGTTGGAAAATATGCCGGAATTCGTACAAAAACTGATCCAATTCTCCCCCACCGCCATTTTCGGGGCTTATGCGCAAGATGTGCTGTTTCGTGGCACAGGGCTTGATGTGGTGTGGGATAAACTGCTCCAAATTGCGGCGTTGGGCGCATTATTCTTAGGTATCGCACTTGCCCAGTTTAAATCCATGTTGTCGCGCCAAGGC","","","41573","MFRWIKNVFYLSGKELRSLFSDPVLVVLIIYMFTVAIYTVANSITLEVKNASVAIVDNDHSALSYRLQQSLITPNFRKVHTIHAQQADRLMDTGEYTFILDIPPNYERDVLAGRNPLIQLLSDATAMTQAAIGSAYISQIFHGEINDFLRLQSNNGILIQPTINVLYNPNFSGNWFMGGMNIVGYLNLLTMLLVGAAVIRERERGTLEHILVMPVRSSEIAMAKIVANELVLLTVVMFSLYFVVHKIIGTPLPQGAFSLYILGAAVFIFSIASLGIMLAIFAPTMPQFGLLVLPVYITMYLLSGTMSPLENMPEFVQKLIQFSPTAIFGAYAQDVLFRGTGLDVVWDKLLQIAALGALFLGIALAQFKSMLSRQG","1466154","","ABC transporter, permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR000412
Family
ABC-2
PS51012\"[125-370]TABC_TM2
InterPro
IPR013525
Domain
ABC-2 type transporter
PF01061\"[161-337]TABC2_membrane
noIPR
unintegrated
unintegrated
signalp\"[1-36]?signal-peptide
tmhmm\"[21-41]?\"[181-199]?\"[220-242]?\"[256-278]?\"[288-308]?\"[349-367]?transmembrane_regions


","BeTs to 13 clades of COG0842COG name: ABC-type multidrug transport system, permease componentFunctional Class: RThe phylogenetic pattern of COG0842 is aompkzy-vdrlbcefghs-uj----Number of proteins in this genome belonging to this COG is","","Residues 114 to 226 match (2e-24) PD:PD115342 which is described as COMPLETE PROTEOME ABC ATP-BINDING TRANSPORTER MEMBRANE TRANSMEMBRANE PERMEASE TRANSPORTER INNER ","","","","","","","","","","","","Mon Jan 13 15:32:19 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02141 is paralogously related to AA02140 (6e-14).","","","","","","","","","","","","","","1","","","" "AA02142","1466177","1467592","1416","ATGGCAAATAAATTCGCTTTTAAATTCACATTCATCGCGGCGTTTATCACCCTCAGCGCTTGCACGACCAATGTCGATTTATCTTCTCAAGTGGAAATGCCTGCACAATTTGAGCAAACACAAAATGCGGCGACCTCTAAAAACATACAGGAAATCGCCCGTTGGTGGCAAAACTGGCGGGATCCGCAATTGACCCGATTAATCGAACTGGGACTACAAAATAACCTTGATATTGAAATCGCCAAAGCCCGTTTGCAGGAAGCGCAGGCGAACAGTCAATATACGCAGGCGGATCTGGGCCCTAAAGTCGGCGCGCAAGGTTCGGCGGGCATGATTCATTCTCATGGGGAAAATCCGTTGACACAGCGTACTTATGATCGGTCAGGAAATGTGCAACATGCGGGAATCACGGCAAGCTGGGAGTTGGATTTCTTCGGTAAAAAACGTAGCGATCGCGATGCGGCACAAGCTGCCGTCCTAGCCGCACAACAACAGGTTTATGCCGCCCAAATGTTGGTTGCCGGGCAAATCGCCGAAAGTTATGCCAATATTGCCGCCTTACATCAGCAAAATGCGCTGTTACAACAAAACGAAACATACTTACGCCGATTGAAAGGTTATGCGGAAGGTCGCTTCCGCGCCGGACAAGCGAACGCCAACGATGTGTTGCAGGTGGAAAGCCGAATCAGCGCCGTGCAGGCGCAACAAGCCACGCTGAACGCACAAATCGCCGGTAACGAACGCGCCATTGCTATTCTTATCGGCAAACCGCCGCAAGACTTCCGTCTTAACAAAAGTGCGGTGGATTTTCTCGGTGTTTTACCAGCCGCCCCGCATGGTGTAATGCCCGGCAATGTATTGGAACGCCGCCCCGATTTACGCACTTATCGCGCCCAAGTACAAGCGCTGGCGGCAAAACTGGCTTCTGCCAAAGCGGATTTATACCCGCGCTTTGAGATTCAATTTTTAGGACAAACAGGGCGCATTGACATCAACACGGACATTCCCGATTTAAAAGGTTGGGGCAATTTGTTGAGCCTCGACATTAGCCTGCCGATTTTCACTAACGGACGCATTCAAGCCAACATTGACGCCGCCGACGCCCGCCTGAAAGCTGCCTTACTTCAATACGACAAAGGCTTGCTGCAAGCCCTTGCCGATGTAGATAACAGCTATCAGGCACAAGCCGCATTAAATCGCCAAACCCAATTGCTACAAACCGCCTGCCAACAGGCGCAAAAGCAGGCAGGCAATGCGGAGAAATTATTTAACTACGGCGAAAAAACCTTAGACAACGCCCTCACCGCCCGCCTCACCGCACTGGATTACCAAAACCAACTCATCCAAAGCCGTTTAGCGGGGGCGAAGAATTTGATTAGTTTGTATAAAGCACTAGGTGGCGGTTGGTCCGAGCGA","","","53846","MANKFAFKFTFIAAFITLSACTTNVDLSSQVEMPAQFEQTQNAATSKNIQEIARWWQNWRDPQLTRLIELGLQNNLDIEIAKARLQEAQANSQYTQADLGPKVGAQGSAGMIHSHGENPLTQRTYDRSGNVQHAGITASWELDFFGKKRSDRDAAQAAVLAAQQQVYAAQMLVAGQIAESYANIAALHQQNALLQQNETYLRRLKGYAEGRFRAGQANANDVLQVESRISAVQAQQATLNAQIAGNERAIAILIGKPPQDFRLNKSAVDFLGVLPAAPHGVMPGNVLERRPDLRTYRAQVQALAAKLASAKADLYPRFEIQFLGQTGRIDINTDIPDLKGWGNLLSLDISLPIFTNGRIQANIDAADARLKAALLQYDKGLLQALADVDNSYQAQAALNRQTQLLQTACQQAQKQAGNAEKLFNYGEKTLDNALTARLTALDYQNQLIQSRLAGAKNLISLYKALGGGWSER","1467592","[FUNCTION] Component of the mexA-mexB-oprM efflux system that confers multidrug resistance. This operon is also implicated in the secretion of the siderophore, pyoverdine. oprM is probably involved in the efflux of the siderophore across the outer membrane. ","outer membrane protein OprM precursor","Outer membrane, Periplasm","","
InterPro
IPR003423
Family
Outer membrane efflux protein
PF02321\"[64-255]T\"[283-466]TOEP
InterPro
IPR010131
Family
RND efflux system, outer membrane lipoprotein, NodT
TIGR01845\"[12-468]Touter_NodT: efflux transporter, outer membr
noIPR
unintegrated
unintegrated
PS51257\"[1-21]TPROKAR_LIPOPROTEIN
signalp\"[1-21]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","BeTs to 5 clades of COG1538COG name: Outer membrane proteinFunctional Class: M,NThe phylogenetic pattern of COG1538 is -------q-----cefghsnujx---Number of proteins in this genome belonging to this COG is","","Residues 64 to 466 match (2e-58) PD:PD005023 which is described as PROTEOME COMPLETE MEMBRANE OUTER LIPOPROTEIN PRECURSOR EFFLUX PROBABLE SIGNAL PLASMID ","","","","","","","","","","","Mon Jan 13 15:38:23 2003","Mon Jan 13 15:38:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02142 is paralogously related to AA02077 (6e-24).","","","","","","Residues 283 to 466 (E-value = 4.8e-19) place AA02142 in the OEP family which is described as Outer membrane efflux protein (PF02321)","","","","","Poole,K., Heinrichs,D.E. and Neshat,S. Cloning and sequence analysis of an EnvCD homologue in Pseudomonas aeruginosa: regulation by iron and possible involvement in the secretion of the siderophore pyoverdine. Mol. Microbiol. 10 (3): 529-544 (1993) [PubMed: 7968531].Poole,K., Krebes,K., McNally,C. and Neshat,S. Multiple antibiotic resistance in Pseudomonas aeruginosa: evidence for involvement of an efflux operon. J. Bacteriol. 175 (22): 7363-7372 (1993) [PubMed: 8226684].Nakajima,A., Sugimoto,Y., Yoneyama,H. and Nakae,T. Localization of the outer membrane subunit OprM of resistance-nodulation-cell division family multicomponent efflux pump in Pseudomonas aeruginosa. J. Biol. Chem. 275 (39): 30064-30068 (2000) [PubMed: 10889211].","","Mon Jan 27 15:37:34 2003","1","","","" "AA02143","1467573","1467701","129","GTGGCGGTTGGTCCGAGCGATGAAAAAAACGTTTGCGAAATCGACCGCACTTTTGCGTTTTGTAAAAGTGCGGTGGTTTTCCCGATGTTTTTCACTGCGCCCGCCTTACCCCAAACTCGCTATATAAAA","","","4778","VAVGPSDEKNVCEIDRTFAFCKSAVVFPMFFTAPALPQTRYIK","1467701","","hypothetical protein","Periplasm, Cytoplasm","There are no significant matches to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:29:05 2004","Wed Feb 25 15:29:05 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02143 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:29:05 2004","","","","","","","","","","","","","1","","","" "AA02144","1467723","1468739","1017","ATGGGCACTTTTAAAACTCACCGCACTTTTCTGATGAATAAAAACAGATTTATTTTTATATTACTTGCCTTATTACTTGTCGGGCTGGCGTTGTTTTCGTTGTCTTGGGGGCGATTTGCCATTCCTGTTGAGAATGTGGTGCAAACGCTGACGGGGAATAACCCGAACGAGGTGCAGAACAACATTATTTTTAACCTGCGTTTACCGCGCATTCTTGCGTCGCTCTTGGTCGGGGCGGCGCTGGCGCTTGCCGGGGCGACTTTTCAGGGGATTTTCCGTAATCCGTTAGTTTCGCCCGATTTGCTCGGTGTGTCCGGCGGCGCCTGTATCGGCGCGGCGGTGGCGATTTTGCTGGGACTTGGCTTGTTTGCCATTCAGGGTTTTGCATTCGTGGGCGGTTTGCTGGCAGTGCTAATGACCATGAGCCTGCTGAAACTGGTGCGACGGGATTCGACGATTATTTTGGTGCTGTCGGGTATTATCATATCCGGTTTTATGATGGCGTGTTTGGGGTTGGTGAAATATCTTGCCGACCCGGAAACCCAGCTCGCAGACATTGTTTATTGGCAAATGGGCAGCCTGACTAAAGCGGATTATCAAAATTTGCGTCTGCTTGCACCGATGATTCTGTTCACCACCGCGGCGTTATTGATGATGCGTTGGCGCATTAATGTGCTGTCTTTGGGTGATCGGGAAGCAAAACTCATCGGCGCCAATATTCGTTTTGAACGCAATCTGATGGTGATGTTCGCCACGTTGCTCACCGCCTCCGCCGTGTGCTTAAGCGGCACCACCGGTTGGATCGGCTTGATTATTCCCCATTTGGCGCGTATGTTTATCGGCGACAACAATTTACGCACCCTTCCCCTTTCAGCCCTTATCGGCGCGATTTTCCTGTTGATTATCGACACTTTGGCACGCAATTTATACACGCAGGAAATTCCTCTCGGTATTCTCACGGGCTTTATAGGCGCGCCGTTCTTTGCTTGGGTGTTAGTGAAACAAAAGGTGGCGGAC","","","37128","MGTFKTHRTFLMNKNRFIFILLALLLVGLALFSLSWGRFAIPVENVVQTLTGNNPNEVQNNIIFNLRLPRILASLLVGAALALAGATFQGIFRNPLVSPDLLGVSGGACIGAAVAILLGLGLFAIQGFAFVGGLLAVLMTMSLLKLVRRDSTIILVLSGIIISGFMMACLGLVKYLADPETQLADIVYWQMGSLTKADYQNLRLLAPMILFTTAALLMMRWRINVLSLGDREAKLIGANIRFERNLMVMFATLLTASAVCLSGTTGWIGLIIPHLARMFIGDNNLRTLPLSALIGAIFLLIIDTLARNLYTQEIPLGILTGFIGAPFFAWVLVKQKVAD","1468739","","iron (III) ABC transporter, permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR000522
Family
Bacterial transport system permease protein
PF01032\"[25-334]TFecCD
noIPR
unintegrated
unintegrated
signalp\"[1-40]?signal-peptide
tmhmm\"[15-35]?\"[72-92]?\"[102-122]?\"[128-148]?\"[153-173]?\"[199-219]?\"[249-271]?\"[285-305]?\"[315-333]?transmembrane_regions


","BeTs to 18 clades of COG0609COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, permease componentsFunctional Class: P,HThe phylogenetic pattern of COG0609 is aompkz--vd-lbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is","Significant hit ( 7.8e-47) to 3/3 blocks of the IPB000522 family, which is described as \"FecCD transport family\". Interpro entry for IP:IPR000522. IPB000522A 67-108 3.3e-27 IPB000522B 263-277 2.6e-06 IPB000522C 311-334 1.6e-10","Residues 223 to 334 match (1e-21) PD:PD001557 which is described as PROTEOME COMPLETE PERMEASE ABC SYSTEM TRANSPORTER IRON MEMBRANE TRANSPORTER TRANSMEMBRANE ","","","","","","","","","","","","Mon Jan 13 15:50:03 2003","","","Thu Mar 18 09:30:57 2004","Thu Mar 18 09:30:57 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02144 is paralogously related to AA02153 (2e-78), AA00798 (5e-38), AA00796 (3e-37), AA01826 (2e-24) and AA01825 (5e-09).","Thu Mar 18 09:30:57 2004","","","","","Residues 37 to 334 (E-value = 7.9e-91) place AA02144 in the FecCD family which is described as FecCD transport family (PF01032)","Thu Mar 18 09:30:57 2004","","","","","","","1","","","" "AA02145","1468742","1469236","495","ATGACAATGTTAAAAATTAATCAACTTTACTTTCAGCATCAACGTAATATTCCGTTGCTTAATGGCATTGATTTGGAACTGAAGGCGGGCGAGCTGCTCACTATTCTCGGCGCCAACGGCACGGGGAAATCCACCCTGTTAAATTGCATTGCCGGCTTACTGAAACCAAAGTGCGGTGAAATTTTTCTGCAAAATAAGGAAATCAAACAACTTTCCGCCAAACAAATTGCCCGCCAAGTGGCTTATGTTTCGCAGCATTCGCCGCAGACGTATCAATACAAGGTGCTGGATTACGTGGTACTGGGGCGAGCCGCCCATCTATCTAGGCTTGTTCGGCAAACCGCGCGAAGAAGATTATCATTTGGCGGAACGGGCGCTGGCACAACTGAGCATTCGCCATTTTGCAGACAAAATCTATATGCAAATGAGCGGCGGCGAAAAGCAGCTGGTGAATTTAGCCAAAATTCTGGTGCAACAGCCGCAACTGATTTTGTT","10.80","12.80","18278","MTMLKINQLYFQHQRNIPLLNGIDLELKAGELLTILGANGTGKSTLLNCIAGLLKPKCGEIFLQNKEIKQLSAKQIARQVAYVSQHSPQTYQYKVLDYVVLGRAAHLSRLVRQTARRRLSFGGTGAGTTEHSPFCRQNLYANERRRKAAGEFSQNSGATAATDFV","","","iron(III) ABC transporter, ATP-binding protein","Inner membrane, Outer membrane, Cytoplasm","AA02145 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus ducreyi gene.AA02145 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus influenzae Rd gene.","
InterPro
IPR003439
Domain
ABC transporter related
PF00005\"[30-103]TABC_tran
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[3-106]Tno description
PTHR19222\"[4-109]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF31\"[4-109]TMETAL ABC TRANSPORTER


","BeTs to 16 clades of COG1120COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, ATPase componentsFunctional Class: P,HThe phylogenetic pattern of COG1120 is aompk---vdrlbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is","Significant hit ( 3.5e-13) to 1/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 19-65 3.1e-13","Residues 20 to 71 match (1e-09) PD:PD000005 which is described as ATP-BINDING COMPLETE PROTEOME ABC TRANSPORTER TRANSPORTER PROBABLE TRANSMEMBRANE COMPONENT PLASMID ","Fri Feb 27 12:13:28 2004","Sat Feb 28 17:12:15 2004","Sat Feb 28 17:12:15 2004","Sat Feb 28 17:12:15 2004","Fri Feb 27 12:13:28 2004","Fri Feb 27 12:13:28 2004","Fri Feb 27 12:13:28 2004","Fri Feb 27 12:13:28 2004","Fri Feb 27 12:13:28 2004","Fri Feb 27 12:13:28 2004","Fri Feb 27 12:13:28 2004","Fri Feb 27 12:13:28 2004","Fri Feb 27 12:13:28 2004","Fri Feb 27 12:13:28 2004","Fri Feb 27 12:13:28 2004","Fri Feb 27 12:13:28 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02145 is paralogously related to AA1394, a ferric enterobactin transport; ABC transporter ATP-binding protein (4e-13), AA0519, an iron(III) dicitrate transport ATP-binding protein f (2e-11), AA0986, an ABC system transport protein, ATP binding (9e-11), AA1057, a lipoprotein releasing system ATP-binding protein (3e-10), AA1672, an iron (chelated) ABC transporter, ATP-binding protein (1e-09), AA1184, an iron(III) ABC transporter, ATP-binding protein (2e-09), AA1713, an ABC transporter, ATP-binding protein (9e-09), AA0987, an ABC transporter, ATP-binding protein (9e-09), AA0454, an iron(III) ABC transporter, ATP-binding protein (3e-08), AA0275, a D-methionine ABC transporter, ATP-binding protein (3e-08), AA1530, a spermidine / putrescine transport ATP-binding (4e-08), AA0931, a cell division protein E, ABC system ATP-binding protein (4e-08), AA0913, an ABC transporter, ATP-binding protein (4e-08), AA1902, an oligopeptide ABC transporter, ATP-binding protein (6e-08), AA0608, a sugar(aldose) ABC transporter, ATP-binding protein (6e-08), AA1210, a thiamine transport ATP-binding protein (1e-07), AA0693, an iron (III) ABC transporter, ATP-binding protein (1e-07), AA1514, an ABC transporter, ATP-binding protein; possible leukotoxin secretion ATP-binding protein (2e-07), AA1844, a leukotoxin expression protein B; hemolysin secretion protein (2e-07), AA1099, a sulfate permease A protein; ABC transporter, ATP-binding protein (4e-07), AA1734, an ABC transporter, ATP-binding protein (7e-07), AA1077, a ferric transport ABC-related ATP-binding protein (9e-07), AA1507, an ABC transporter ATP binding protein (2e-06), AA1440, an ABC transporter ATP-binding protein (2e-06), AA1788, a spermidine/putrescine ABC transporter, ATP-binding protein (3e-06), AA1688, an ABC transporter, ATP-binding protein (3e-06), AA1592, an ABC transporter, ATP-binding protein (3e-06), AA1348, a macrolide-specific ABC-type efflux carrier (3e-06), AA1082, a maltose/maltodextrin transport ATP-binding protein (3e-06), AA1025, a dipeptide transport system ATP-binding protein (3e-06), AA0487, a galactoside ABC transporter, ATP-binding protein (3e-06), AA0044, a cytochrome c-type biogenesis ATP-binding protein (8e-06), AA1830, a ribose ABC transporter; ATP-binding (1e-05), AA1439, an ABC transporter ATP-binding protein (1e-05), AA0998, an amino acid ABC transporter, ATP-binding protein (1e-05), AA1712, an ABC transporter, ATP-binding protein (2e-05), AA1504, an ABC transporter ATP-binding protein (3e-05), AA1269, a MDR ABC transporter, ATP-binding/permease protein (5e-05), AA1016, an ABC transporter, ATP-binding protein (5e-05), AA0143, a D-ribose ABC transporter, ATP-binding protein / galactoside ABC transporter, ATP-binding protein (5e-05), AA1624, an ABC transporter, ATP-binding protein (9e-05), AA0950, a D-xylose ABC transporter, ATP-binding protein (9e-05), AA1182, a high-affinity zinc uptake system ATP-binding protein (1e-04), AA0559, an arginine ABC transporter, ATP-binding protein (1e-04), AA1385, an ABC transporter ATP-binding protein (2e-04), AA0385, an ABC transporter, ATP-binding protein (3e-04), AA1156, a molybdenum ABC transporter, ATP-binding protein (6e-04) and AA1144, a cobalt transport ATP-binding protein (7e-04).A02145 is paralogously related to AA02152 (4e-13), AA00799 (2e-11), AA01509 (8e-11), AA01616 (3e-10), AA02550 (1e-09), AA01824 (2e-09), AA02609 (7e-09), AA01510 (7e-09), AA00700 (2e-08), AA00415 (2e-08), AA02353 (4e-08), AA01422 (4e-08), AA01393 (4e-08), AA02899 (5e-08), AA00933 (5e-08), AA01867 (8e-08), AA01051 (8e-08), AA02331 (1e-07), AA02805 (2e-07), AA01684 (3e-07), AA02642 (5e-07), AA01645 (7e-07), AA02324 (1e-06), AA02226 (2e-06), AA02718 (2e-06), AA02573 (2e-06), AA02440 (2e-06), AA02080 (3e-06), AA01656 (3e-06), AA01568 (3e-06), AA00751 (3e-06), AA00061 (6e-06), AA02786 (7e-06), AA02225 (7e-06), AA01524 (7e-06), AA02606 (2e-05), AA02320 (2e-05), AA01961 (4e-05), AA01555 (4e-05), AA00207 (4e-05), AA02484 (6e-05), AA01456 (6e-05), AA01820 (1e-04), AA00858 (1e-04), AA02140 (1e-04), AA00591 (2e-04), AA01779 (4e-04) and AA01757 (5e-04).","Fri Feb 27 12:13:28 2004","Sat Feb 28 17:11:48 2004","pdb1JJ71JJ7-A CRYSTAL STRUCTURE OF THE C-TERMINAL ATPASE 54.7 1e-08pdb1JI01JI0-A CRYSTAL STRUCTURE ANALYSIS OF THE ABC 53.5 2e-08pdb1G6H1G6H-A CRYSTAL STRUCTURE OF THE ADP CONFORMATION OF 53.1 3e-08pdb1GAJ1GAJ-A CRYSTAL STRUCTURE OF A NUCLEOTIDE-FREE 53.1 3e-08pdb1L2T1L2T-A DIMERIC STRUCTURE OF MJ0796, A BACTERIAL ABC 51.9 6e-08pdb1F3O1F3O-A CRYSTAL STRUCTURE OF MJ0796 ATP-BINDING 51.9 6e-08pdb1JSQ1JSQ-A STRUCTURE OF MSBA FROM ESCHERICHIA COLI: A 51.2 1e-07pdb1B0U1B0U-A ATP-BINDING SUBUNIT OF THE HISTIDINE PERMEASE 50.8 1e-07pdb1L7V1L7V-C BACTERIAL ABC TRANSPORTER INVOLVED IN B12 50.4 2e-07pdb1G291G29-1 MALK 47.3 2e-06","","","Residues 30 to 86 (E_value = 3.4e-18) place AA1389 in the ABC_Tran family which is described as ABC transporter.","Fri Feb 27 12:13:28 2004","","","","","","","1","Fri Feb 27 12:13:28 2004","","" "AA02146","1468968","1469537","570","TTGCCCGCCAAGTGGCTTATGTTTCGCAGCATTCGCCGCAGACGTATCAATACAAGGTGCTGGATTACGTGGTACTGGGGCGAGCCGCCCATCTATCTAGGCTTGTTCGGCAAACCGCGCGAAGAAGATTATCATTTGGCGGAACGGGCGCTGGCACAACTGAGCATTCGCCATTTTGCAGACAAAATCTATATGCAAATGAGCGGCGGCGAAAAGCAGCTGGTGAATTTAGCCAAAATTCTGGTGCAACAGCCGCAACTGATTTTGTTTGATGAACCCACCTCCGCGTTAGATTACGGCAATGTATTTAAGACATTAAGCCTGATTAAAGGGTTATCACATCAGCAATTTTCTATTATTATGACAACACATAACCCCGATCATCCGATGTTGCTTAATGAAGTCATTCCGAACAGCAAAGTAGCGATTTTAACGAAATCGGGAAAATTGCATTGCGGTTTCACCGAGGCTATTCTCACGGAAGACAATCTGCGAGAACTTTACCAAACGGATTTGCGGTTAATTGATGTACCTGAATTACAACGTAAAATCTGTGCCATTACGCATATT","","","24102","LPAKWLMFRSIRRRRINTRCWITWYWGEPPIYLGLFGKPREEDYHLAERALAQLSIRHFADKIYMQMSGGEKQLVNLAKILVQQPQLILFDEPTSALDYGNVFKTLSLIKGLSHQQFSIIMTTHNPDHPMLLNEVIPNSKVAILTKSGKLHCGFTEAILTEDNLRELYQTDLRLIDVPELQRKICAITHI","1469537","","iron(III) ABC transporter, ATP-binding protein","Cytoplasm, Inner membrane","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[66-109]TQ8NNS5_CORGL_Q8NNS5;
PF00005\"[26-127]TABC_tran
PS00211\"[67-81]?ABC_TRANSPORTER_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[35-169]Tno description
PTHR19222\"[37-182]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF31\"[37-182]TMETAL ABC TRANSPORTER
signalp\"[1-18]?signal-peptide


","BeTs to 15 clades of COG1120COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, ATPase componentsFunctional Class: P,HThe phylogenetic pattern of COG1120 is aompk---vdrlbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.7e-11) to 1/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140B 64-102 1.6e-11","Residues 66 to 109 match (8e-07) PD:PD000006 which is described as ATP-BINDING COMPLETE PROTEOME ABC TRANSPORTER TRANSPORTER PROBABLE TRANSMEMBRANE COMPONENT PLASMID ","","","","","","","","","","","","Mon Jan 13 16:46:27 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02146 is paralogously related to AA02152 (9e-27), AA02440 (2e-14), AA01757 (6e-13), AA00799 (1e-12), AA02550 (1e-11), AA00858 (2e-11), AA01824 (4e-11), AA01524 (1e-10), AA02320 (2e-10), AA02080 (8e-10), AA01456 (5e-09), AA01779 (2e-08), AA01422 (2e-08), AA01616 (2e-08), AA02718 (3e-08), AA01684 (3e-08), AA01947 (8e-08), AA01645 (1e-07), AA00207 (1e-07), AA01820 (2e-07), AA00700 (2e-07), AA01051 (3e-07), AA01867 (4e-07), AA00751 (4e-07), AA00415 (4e-07), AA02898 (1e-06), AA02140 (1e-06), AA02225 (2e-06), AA02899 (2e-06), AA02786 (2e-06), AA00934 (3e-06), AA02805 (4e-06), AA02353 (5e-06), AA01656 (5e-06), AA01510 (2e-05), AA02484 (2e-05), AA02606 (4e-05), AA01291 (6e-05), AA00933 (6e-05), AA02324 (8e-05), AA02609 (1e-04), AA01555 (1e-04), AA02573 (2e-04), AA01509 (2e-04), AA01393 (2e-04) and AA00591 (3e-04).","","","","","","Residues 8 to 141 (E-value = 6.3e-06) place AA02146 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","","","","1","","","" "AA02147","1469808","1469677","132","TTGTTTCGCTTTTTTTTTTTTGCGATTTTTAAAATCTTTCGCATTTTTGGTTTTTATCTATTCTTCAATAAAAAAGGACGCCGTTTTTCTTGCGCCCTTGTTTTCATTGGTTTTGTTCCACTTGTTCCCGCT","","","5319","LFRFFFFAIFKIFRIFGFYLFFNKKGRRFSCALVFIGFVPLVPA","1469677","","hypothetical protein","Cytoplasm","There are no significant matches to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-17]?signal-peptide
tmhmm\"[4-22]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:26:56 2004","Wed Feb 25 15:27:15 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA1343.AA02147 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:26:56 2004","","","","","","","","","","","","","1","","","" "AA02148","1469702","1469577","126","TTGGTTTTGTTCCACTTGTTCCCGCTTAATTCAACATTCTCCCTAGCTTATTCCTTTTTCTCATTTTGTTCGGTGTTTTACAACGGAAAATGCCAGCAGGGTAGCCGCAAAAAGTGCGGTGTGTTT","","","8153","LVLFHLFPLNSTFSLAYSFFSFCSVFYNGKCQQGSRKKCGVF","1469577","","hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-16]?signal-peptide
tmhmm\"[10-28]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Jan 13 16:47:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02148 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02149","1470702","1470058","645","ATGAATTCTAAAAATGTTAATGAGTGGGTTACCGCTGAAATGGTGGCGGGAATGGGGGAATTGCCAAAATCCGCCAGTAACGTAACAAGACGAGCCACAAAGGAAAATTGGGTAAAAAGACAAAAAAGAGGTAAGAGAGGGGTGGCTTATGAATATCATTATTCATCGCTTCCTGACGAAGTTCAAAGGCTGTTGGGCTTTGGTTTAAACGACGGCGGAGAATGGATAGAGTTAAAAGACCTTTTAGGCGTAGCTGGATTGCCCGAAACAGTACAGGGAGTTACTAAAAAAGCAAAAGCGGAAAATTGGGAACGTAGGCTTATAGAGGGAAGAAAAGGCAAAACCTTTGAATATCAGATATCTTCAATGCCCTTAGCTCTCCAAAACAAGCTAAACTTTTCAAAAAACTTAATAAACGAGCCAGTAGCGCCGTATCGTATTGAACGACGGACAAACGACGAAGACTTAACAGAAGTAAGCAAGGCGCGCTTTTTAACGGCGATCAGCACATTAGAAGAAATCTTAGCAATGACACGCAAAACCATGGAGCCAGAAGCCAAGGCGCAAATGGTATGGATGATTTATGAATTACTAAGCGAAGAAAGCGCTAACGAGAAGATTATTAATTTAGTTAAATTGGTTGCA","","","24477","MNSKNVNEWVTAEMVAGMGELPKSASNVTRRATKENWVKRQKRGKRGVAYEYHYSSLPDEVQRLLGFGLNDGGEWIELKDLLGVAGLPETVQGVTKKAKAENWERRLIEGRKGKTFEYQISSMPLALQNKLNFSKNLINEPVAPYRIERRTNDEDLTEVSKARFLTAISTLEEILAMTRKTMEPEAKAQMVWMIYELLSEESANEKIINLVKLVA","1470058","[FUNCTION] This transposase is essential for integration, replication-transposition, and excision of mu DNA.[MISCELLANEOUS] Mu can transpose its DNA into multiple sites in many bacterial genomes and mediate a variety of DNA rearrangements. Transposition requires both transposase (encoded by gene A) and transposition enhancer (encoded by gene B). Unlike other transposons mu has dissimilar sequences at its left and right ends. transposase apparently binds 3 specific blocks of sequences at each end of mu DNA. The a gene is regulated by the repressor C, which binds to an operator sequence & turns off transcription. Repressor C can, at high concentrations, occupy almost the exact same sites on mu ends as the transposase, and transposase can bind to fragments containing the mu operator sequence. ","possible transposase","Cytoplasm","","
InterPro
IPR003314
Domain
Transposase MuA/Repressor CI, DNA-binding
PF02316\"[13-149]TMu_DNA_bind
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[6-71]T\"[72-139]Tno description


","No hits to the COGs database.","Significant hit ( 7.2e-16) to 2/6 blocks of the IPB003314 family, which is described as \"Mu DNA-binding domain\". Interpro entry for IP:IPR003314. IPB003314A 20-44 2.3e-09 IPB003314B 47-60 8e-05 IPB003314B 113-126 0.039","Residues 74 to 131 match (3e-07) PD:PD016666 which is described as DNA DNA-BINDING TRANSPOSASE REPRESSOR ELEMENT REGULATION RECOMBINATION CI INTEGRATION EXCISION ","","","","","","","","","","","Mon Jan 13 17:01:27 2003","Mon Jan 13 17:01:27 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02149 is paralogously related to AA02072 (6e-60) and AA01765 (8e-07).","","","","","","Residues 13 to 149 (E-value = 1.6e-05) place AA02149 in the Mu_DNA_bind family which is described as Mu DNA-binding domain (PF02316)","","","","","Harshey,R.M., Getzoff,E.D., Baldwin,D.L., Miller,J.L. and Chaconas,G. Primary structure of phage mu transposase: homology to mu repressor . Proc. Natl. Acad. Sci. U.S.A. 82 (22): 7676-7680 (1985) [PubMed: 2999776].Toussaint,A., Faelen,M., Desmet,L. and Allet,B. The products of gene A of the related phages Mu and D108 differ in their specificities. Mol. Gen. Genet. 190 (1): 70-79 (1983) [PubMed: 6222246].Clubb,R.T., Omichinski,J.G., Savilahti,H., Mizuuchi,K., Gronenborn,A.M. and Clore,G.M. A novel class of winged helix-turn-helix protein: the DNA-binding domain of Mu transposase. Structure 2 (11): 1041-1048 (1994) [PubMed: 7881904].Schumacher,S., Clubb,R.T., Cai,M., Mizuuchi,K., Clore,G.M. and Gronenborn,A.M. Solution structure of the Mu end DNA-binding ibeta subdomain of phage Mu transposase: modular DNA recognition by two tethereddomains. EMBO J. 16 (24): 7532-7541 (1997) [PubMed: 9405381].","","Mon Jan 13 17:01:27 2003","1","","","" "AA02150","1470833","1471045","213","ATGACAAAAAAGAAAAGAGTCACTGATATGAGTAACCATGAGATTAGAGGTGAACTGATGAAAAAAGGGAAATCATTATCTCAGTTAGGAATTGAAAACGGACTAGCAAAAACAACCGTTCGGAATGCGCTAGATAAACCATACCCTAAAGGCGAGCAAATTATTGCAGATGCGTTAGGGCTATCTCCCGCGGAAATATGGCCTTCGCGCTAT","","","7894","MTKKKRVTDMSNHEIRGELMKKGKSLSQLGIENGLAKTTVRNALDKPYPKGEQIIADALGLSPAEIWPSRY","1471045","","conserved hypothetical protein","Cytoplasm, Periplasm","This sequence is similar to gi37527592, a hypothetical protein from Photorhabdus luminescens subsp. laumondii TTO1.","
noIPR
unintegrated
unintegrated
G3DSA:1.10.260.40\"[2-71]Tno description


","BeTs to 3 clades of COG3423COG name: Predicted transcriptional regulatorFunctional Class: KThe phylogenetic pattern of COG3423 is --------------e--h-n------Number of proteins in this genome belonging to this COG is","","Residues 9 to 71 match (2e-07) PD:PD508526 which is described as DNA-BINDING PROTEOME COMPLETE ","","","","","","","","","","","","Wed Feb 25 15:24:07 2004","Wed Feb 25 15:24:56 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02150 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:24:56 2004","","","","","","","","","","","","","1","","","" "AA02151","1471826","1470996","831","ATGAAAAAACTCCTGCCGTTCAGTCTGATTAGTTTGGCTGTCATTTCAACCTTTACCCACGCACACGCAGAAGACACGCAAAATTTAGATGAAATTCAAGTGACCGCCGAACAGCAAGTGAAACAGTCACTGGGCGTGTCCGTCATCACGGAAAAAGATCTGGAACGAAATCCCATTGAAAATGATGCGTCTGAAATCATCGCCAAACAACCGGGTGTCACTTTAAGTACCAATGCACCGGGCGGCGCACGCGGCAATAAACGCCAAGTGGATATTCGTGCTATGGGGCCGGAAAACACCTTGATTCTGGTGAACGGCAAACCGGTAAAATCCCGTAATTCCGAACGCTATGGCAGAAACGGCATGCGGAATACCCGCGGCGACACCAACTGGGTGCCGGCAGATGCTATTGAGTCCATTGAAGTCTTGCGAGGTCCGGCAGCAGCACGTTATGGTTCAGGCGCCATGGGCGGGGTGGTGAACATTAAAACCAAAGCACCAACCGCAGAATATCACGGCAGTTTAAATCTATTTACCGAGCAACCGGAAGACAGCAAAGAAGGCCATACCAACCGTCTGGGTTTTAATTTCAGCGGTCCGTTGATTAAAGATGTTTTAGGCTTCCGTTTACACATAACTAACCCCTTTTACACCTTCTACTTGTTTTCGCTCCCATCCTTCCTTTGTTGCTCGTCTTGTTACGTTACTGGCGGATTTTGGCAATCCACCTATCCCTGCTATTTCACTTGCATAAACCCAATCTTTCATGATTGCTTCCTTAATAGCGCGAAGGCCATATTTCCGCGGGAGATAGCCCTAACGCATCTGCAA","","","30518","MKKLLPFSLISLAVISTFTHAHAEDTQNLDEIQVTAEQQVKQSLGVSVITEKDLERNPIENDASEIIAKQPGVTLSTNAPGGARGNKRQVDIRAMGPENTLILVNGKPVKSRNSERYGRNGMRNTRGDTNWVPADAIESIEVLRGPAAARYGSGAMGGVVNIKTKAPTAEYHGSLNLFTEQPEDSKEGHTNRLGFNFSGPLIKDVLGFRLHITNPFYTFYLFSLPSFLCCSSCYVTGGFWQSTYPCYFTCINPIFHDCFLNSAKAIFPREIALTHLQ","1470996","[FUNCTION] Specific receptor for the siderophore ferric enterobactin. ","ferric enterobactin receptor; TonB-dependent outer membrane siderophore receptor protein","Outer membrane, Cytoplasm","","
InterPro
IPR012910
Domain
TonB-dependent receptor, plug
PF07715\"[38-159]TPlug
noIPR
unintegrated
unintegrated
G3DSA:2.170.130.10\"[22-164]Tno description
signalp\"[1-23]?signal-peptide


","No hits to the COGs database.","Significant hit ( 6.4e-06) to 2/3 blocks of the IPB000531 family, which is described as \"TonB-dependent receptor protein\". Interpro entry for IP:IPR000531. IPB000531A 93-106 20 IPB000531B 152-169 0.00016","Residues 32 to 90 match (3e-10) PD:PD005173 which is described as RECEPTOR COMPLETE PROTEOME OUTER MEMBRANE ENTEROBACTIN FERRIC IRON SIDEROPHORE TONB ","","","","","","","","","","","Mon Jan 13 17:05:25 2003","Mon Jan 13 17:05:25 2003","","","Thu Mar 18 09:31:39 2004","Thu Mar 18 09:31:39 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02151 is paralogously related to AA02157 (4e-10), AA00762 (3e-05), AA02202 (6e-05) and AA02865 (4e-04).","Thu Mar 18 09:31:39 2004","","","","","","","",""," Haraszthy VI, Jordan SF, Zambon JJ.,Identification of Fur-regulated genes in Actinobacillus actinomycetemcomitans.Microbiology. 2006 Mar;152(Pt 3):787-96.PMID: 16514158","Dean,C.R. and Poole,K. Cloning and characterization of the ferric enterobactin receptor gene (pfeA) of Pseudomonas aeruginosa. J. Bacteriol. 175 (2): 317-324 (1993) [PubMed: 8419284].Lundrigan,M.D. and Kadner,R.J. Nucleotide sequence of the gene for the ferrienterochelin receptor FepA in Escherichia coli. Homology among outer membrane receptors that interact with TonB. J. Biol. Chem. 261 (23): 10797-10801 (1986) [PubMed: 3015941].Pettis,G.S., Brickman,T.J. and McIntosh,M.A. Transcriptional mapping and nucleotide sequence of the Escherichia coli fepA-fes enterobactin region. Identification of a uniqueiron-regulated bidirectional promoter. J. Biol. Chem. 263 (35): 18857-18863 (1988) [PubMed: 2974033].Armstrong,S.K., Francis,C.L. and McIntosh,M.A. Molecular analysis of the Escherichia coli ferric enterobactin receptor FepA. J. Biol. Chem. 265 (24): 14536-14543 (1990) [PubMed: 2201687].","","Mon Jan 13 17:07:02 2003","1","","","" "AA02152","1472670","1471924","747","ATGAATTTAGTGGAAACCCGTGATTTAGCCATTGGCTACGGCGATAAAATACTGGTGAACAACATCAATTTCCGTTTACAGGAAAAGCAAATTTGTTGTTTATTGGGGGCAAACGGCGCGGGCAAAAGCACCTTTCTGAAAACCTTGTTAGGGCTACAAGCTCCGCTACAGGGGGAAGTGTATTGGCGGCAACGTCCTTTATCGGATTACAGCCAAGGGGAATTGGCGTGCAACATTGCTTATGTGCCGCAAGCTCATCAGCATTTATTCCCTTTTTTGGTGCAGGATATGGTGCTGATGGGACGTTCGGCGTATCTCAAATGGTATCAATCACCGAAAGCCGAAGATCGTGATTTGGCGCTTTCCGCCCTTGCCGGTTTACAAATCGAACATCTCGCCAAGCGTTATTATCACCAACTGAGTGGGGGAGAGAAACAGTTGGTGCTGATTGCCCGCGCCATTGCGCAACAGGCAACATTATTGATCATGGACGAACCCACCGCGAGCCTGGATTTCGGCAATCAAATTCGTGTGTTGGAAAAAATAAAACACCTGCAAACGCAAAATATCGCCTTATTGATCACCACACATAACCCGCAGCAAGCGATGTATTTGGCGGAAAACATTCTGTTGCTCGATCAAGAATACGGTTTTCAGCAAGGCTCAAGAGAAGCGCTGTTGACCTTGGAAAACTTGGCAAAAATCTACCGCACTTCAGAACAGCAATTACGCCGGCATTTGTGTTTT","","","28267","MNLVETRDLAIGYGDKILVNNINFRLQEKQICCLLGANGAGKSTFLKTLLGLQAPLQGEVYWRQRPLSDYSQGELACNIAYVPQAHQHLFPFLVQDMVLMGRSAYLKWYQSPKAEDRDLALSALAGLQIEHLAKRYYHQLSGGEKQLVLIARAIAQQATLLIMDEPTASLDFGNQIRVLEKIKHLQTQNIALLITTHNPQQAMYLAENILLLDQEYGFQQGSREALLTLENLAKIYRTSEQQLRRHLCF","1471924","","ferric enterobactin transport; ABC transporter ATP-binding protein","Cytoplasm, Inner membrane","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[139-182]TYC72_HAEIN_Q57243;
PF00005\"[29-215]TABC_tran
PS50893\"[4-239]TABC_TRANSPORTER_2
PS00211\"[140-154]?ABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[28-222]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[4-237]Tno description
PTHR19222\"[4-237]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF31\"[4-237]TMETAL ABC TRANSPORTER


","BeTs to 15 clades of COG1120COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, ATPase componentsFunctional Class: P,HThe phylogenetic pattern of COG1120 is aompk---vdrlbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.3e-26) to 2/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 18-64 4.1e-11 IPB001140B 137-175 8.1e-14","Residues 16 to 199 match (3e-08) PD:PD055535 which is described as ATP-BINDING ABC PROTEOME COMPLETE TRANSPORTER ","","","","","","","","","","","","Mon Jan 13 17:17:48 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02152 is paralogously related to AA02550 (5e-30), AA02146 (1e-26), AA00799 (1e-26), AA01824 (7e-23), AA02718 (6e-22), AA01820 (1e-21), AA01645 (2e-21), AA01616 (2e-20), AA01656 (1e-19), AA02353 (1e-19), AA01051 (2e-19), AA00700 (3e-19), AA01524 (5e-19), AA00415 (6e-19), AA02440 (2e-18), AA00858 (2e-18), AA01456 (5e-18), AA02320 (2e-17), AA01757 (5e-17), AA01510 (6e-17), AA02140 (8e-17), AA01779 (8e-17), AA02324 (1e-16), AA02786 (2e-16), AA01422 (2e-16), AA01684 (3e-16), AA02899 (2e-15), AA00933 (3e-15), AA01867 (2e-14), AA02225 (4e-14), AA02805 (6e-14), AA01509 (8e-14), AA01961 (1e-13), AA02898 (3e-13), AA02609 (3e-13), AA00751 (3e-13), AA02606 (7e-13), A02145 (7e-13), AA01393 (1e-12), AA00207 (6e-12), AA01568 (7e-12), AA02080 (5e-10), AA00591 (7e-10), AA00061 (7e-10), AA01569 (9e-10), AA02331 (1e-09), AA02573 (1e-08), AA02484 (1e-08), AA01947 (1e-07), AA01555 (2e-07), AA02642 (3e-06), AA01291 (6e-06), AA00934 (8e-06) and AA02226 (2e-05).","","","","","","Residues 29 to 215 (E-value = 1.4e-50) place AA02152 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Bearden SW, Staggs TM, Perry RD. An ABC transporter system of Yersinia pestis allows utilization of chelated iron by Escherichia coli SAB11. J Bacteriol 1998 Mar;180(5):1135-47. PubMed: 9495751","","Mon Jan 13 17:18:16 2003","1","","","" "AA02153","1473680","1472670","1011","ATGCAAAATCTTATCCAACGTGCGCCACGCCTGTTCTTTTTATTGCTGACGGGAATTTTAGTCGGCAGTATTTTACTTGCCCTGAACGTGGGGAAATTTCCCGTTTCACCAAGTCAATTATGGCAAACGCTCGTTTGTTCCGTGAATTCACAATGTGACACAAACTCACCGATTCACACCGTGTTATGGCAAATTCGCTTGCCTCGCATTGCGGTGGCTTGTTTGGTCGGTGCCGCTTTAGCCTGCGCGGGGGCGACCTATCAGGGGATGTTTAAAAATCCATTGGTTTCGCCGGATATTTTGGGCGTATCCGCCGGCGCCGGGTTTGGGGCGTCACTGGCAATTTTCTACAATTTACCGATGTTTTATATTCAGCTTTTTGCCTTTCTTGGCGGCATTGCCACGGTATTTTGCGTTTCCCTTATCGCAACCCGTAGCAAAGACCAAGACCCGATTCTCGTTCTCGTATTATCGGGAATTGCCATCGGTTCGTTGCTTGGCGCGGGGATTTCGTTGTTGAAAATTCTCGCCGATCCTTTTACCCAACTGCCTTCCATTACTTTTTGGCTACTAGGAAGCTTAACCGCCATTAGTCCGCAAGATGTGTTGCAACTGGCGCCGATTTTATTGCTCGGTATGGCGCCGCTATTTTTACTTCGTTGGCGTTTAAATTTGCTTTCTTTAGAGGAAGAAGAAGCGTGCAGCCTTGGCGTACCGATAAAAATGACCCGCTACATTTTGATTATTTTTACCACCCTTTGCACGGCAAGTGCGGTGTCTATTACAGGCATTATCGGTTGGGTCGGCTTATTGGTGCCGCATATTGCCCGTTTATTGGTGGGCGCCAATTTTATCCTGTTGCTTCCGACATCTTTGCTTCTCGGCGCCGCTTTTCTGTTATTAACGGACACTTTAGCGCGCACCATTGCCGACATTGAGCTGCCTCTTGGCATTTTGACATCTGCCTGCGGCGCACCGTTTTTCCTTTATTTATTATTGCGGGGCAGACGA","","","36012","MQNLIQRAPRLFFLLLTGILVGSILLALNVGKFPVSPSQLWQTLVCSVNSQCDTNSPIHTVLWQIRLPRIAVACLVGAALACAGATYQGMFKNPLVSPDILGVSAGAGFGASLAIFYNLPMFYIQLFAFLGGIATVFCVSLIATRSKDQDPILVLVLSGIAIGSLLGAGISLLKILADPFTQLPSITFWLLGSLTAISPQDVLQLAPILLLGMAPLFLLRWRLNLLSLEEEEACSLGVPIKMTRYILIIFTTLCTASAVSITGIIGWVGLLVPHIARLLVGANFILLLPTSLLLGAAFLLLTDTLARTIADIELPLGILTSACGAPFFLYLLLRGRR","1472670","","iron(III) ABC transporter, permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR000522
Family
Bacterial transport system permease protein
PF01032\"[19-334]TFecCD
noIPR
unintegrated
unintegrated
signalp\"[1-27]?signal-peptide
tmhmm\"[10-30]?\"[65-85]?\"[94-116]?\"[122-142]?\"[152-172]?\"[201-219]?\"[246-268]?\"[282-302]?\"[312-332]?transmembrane_regions


","BeTs to 18 clades of COG0609COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, permease componentsFunctional Class: P,HThe phylogenetic pattern of COG0609 is aompkz--vd-lbcefgh-nuj---wNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.6e-45) to 3/3 blocks of the IPB000522 family, which is described as \"FecCD transport family\". Interpro entry for IP:IPR000522. IPB000522A 66-107 4e-23 IPB000522B 263-277 2.5e-08 IPB000522C 311-334 3e-11","Residues 131 to 215 match (4e-07) PD:PD247701 which is described as PROTEOME COMPLETE PERMEASE ABC MEMBRANE IRON SYSTEM TRANSPORTER FERRICHROME TRANSMEMBRANE ","","","","","","","","","","","","Mon Jan 13 17:20:52 2003","","","Tue Mar 16 15:41:23 2004","Tue Mar 16 15:41:23 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02153 is paralogously related to AA02144 (2e-78), AA00798 (1e-43), AA00796 (2e-36), AA01826 (1e-23), AA01825 (9e-11), AA02552 (6e-07), AA02551 (1e-06) and AA01818 (4e-06).","Tue Mar 16 15:41:23 2004","","","","","Residues 86 to 335 (E-value = 1.1e-05) place AA02153 in the ABC-3 family which is described as ABC 3 transport family (PF00950)","Tue Mar 16 15:41:23 2004","","","","","","","1","","","" "AA02154","1474681","1473683","999","ATGAAAAAATGGTTTATGCTGTTACTTCCGCTGACATTTATCGGCAGCCTTTGGGCGCAGGAAGCGCCTTCCCCCTTTCTTGCCGGGGAATTACCGGCAGCGCAAAAAATCGAAAAAGTCTTAAGCGCCGGTAATCCGAGTGATGCGTTATTGCTGGCCGCCGCGCCGCAAAAAATGGTCGGACTGGCGGGCTTTAAGATGGCATCCAAAGGCGGCAAATTATTTCCTGTGCAACAACAAGCGTTGCCGACCATCGGCAAAATTGCCGGAAAGGGCAGTACGTTTTCCGCCGAAAAAATCGTGGCGCTTCAACCGAATTTGATTATTGATGTGGGCAATGTGGCGCCGAATTACATCGATCAGGCAAAACGCACCTTTGCGCAAACCGGTGTGCCTTATTTATTGCTGGACGGCAGACTCGCCGAAACGCCGAAAACCTTGCGTGAGTTGGGCAAATTGCTAGGTGCGGAAACCTTCACGGAGCCACAGGCGCAATACGCGGAAGAAACTCTTAAAAGTGCGGGGGATTTTGCCGGCGTTTTACAACAAACCGCCTATTTGGCGCGCAGTGCCGACGGTTTACAAACAGGGCAAAAGGGATCCATTCATACGGAGGCTATGGAGTTGGTCGGCTTGCGCAATGTGGTGGAAGGCGAGCATAAAGGGTTAACACAGGTTTCTATGGAGCAGCTTCTGCTGTGGAATCCCGACATTATTTTGACCCAATACGCCGAATTTTTTCAAACCATCAAAGACAATCCCCAATGGCAGCAATTAAGTGCGGTCAAAAATCAGCGCGTTTTTTTCATTCCCAATCAGCCTTTCGGTTGGCTGGATTCCCCGCCGGGATTGAATCGCTTGCTCGGTGTGCGGTGGTTACAACATTTATTAAGCAATAAACCGATGGACGATTTTGCACCCGAAGTGCAACGGTTTTATAAATTGTTCTACCACATTGATTTATCAAAAGCGCAAGCTGAGCAGTTGCTACAGGGACAA","","","36672","MKKWFMLLLPLTFIGSLWAQEAPSPFLAGELPAAQKIEKVLSAGNPSDALLLAAAPQKMVGLAGFKMASKGGKLFPVQQQALPTIGKIAGKGSTFSAEKIVALQPNLIIDVGNVAPNYIDQAKRTFAQTGVPYLLLDGRLAETPKTLRELGKLLGAETFTEPQAQYAEETLKSAGDFAGVLQQTAYLARSADGLQTGQKGSIHTEAMELVGLRNVVEGEHKGLTQVSMEQLLLWNPDIILTQYAEFFQTIKDNPQWQQLSAVKNQRVFFIPNQPFGWLDSPPGLNRLLGVRWLQHLLSNKPMDDFAPEVQRFYKLFYHIDLSKAQAEQLLQGQ","1473683","","possible ATP-binding protein of ABC transporter","Periplasm","","
InterPro
IPR002491
Family
Periplasmic binding protein
PF01497\"[207-274]TPeripla_BP_2
PS50983\"[39-301]TFE_B12_PBP
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1980\"[182-301]Tno description
signalp\"[1-19]?signal-peptide


","No hits to the COGs database.","","Residues 221 to 270 match (4e-07) PD:PD413465 which is described as PROTEOME COMPLETE ABC PERIPLASMIC PROTEIN TRANSPORTER PERIPLASMIC-BINDING SIGNAL FERRIC FERRICHROME-BINDING ","","","","","","","","","","","","Tue Mar 16 15:43:33 2004","","","","Tue Mar 16 15:43:33 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02154 is paralogously related to AA02380 (7e-09) and AA00795 (0.001).","Tue Mar 16 15:43:33 2004","","","","","Residues 37 to 274 (E-value = 4.2e-08) place AA02154 in the Peripla_BP_2 family which is described as Periplasmic binding protein (PF01497)","Tue Mar 16 15:43:33 2004","","","","","","","1","","","" "AA02156","1474721","1475386","666","TTGAAATTTTCTTTGCCACGTTCAACTTGTGTAAACGGCATGAATTTTACTAAAACGCTATATATTTTTAAATATACTGGCGAACTTTTCGCGATTTTTATTTATAATGAAGACGCTATGTTTTTAAATATACATCGTTATATTTTTCTCACATTCTGTTGGGGTAACATCATGAAATTTGAAGTCATTTACAAATTCCTGTTGTTGTGTGTGCTGATTATCAGTTTGTTGTGTGTTGTGATAAGCGGCGCCGGATTATTCTACGGTTGGCAATTGAGCATGCTGTTCAATATTCATGTGAGCTTTGCCGTTTTGCTGGTCGCCGCGTTGTTACTGCATATTCTGAACCGCAAAAATAAATTGGCGAAAATCAATACCCAATTTGCCGATTTGGTCTTACACAATAAATACCCGAGTTATTGCAATTTAGACCGCTTGATCATGACGTTCGAGCATTTTTCCGTTGTGCAAATTGCCGAACAGTTAAACCTGGATTTGGATGCGCTGCTAAAAGAACTCGCCGAAGGAAAAATAAACGTCAAAAATTCCCACAGCACTTTACGGGAGAATTTTCCCCATAATGATGAAAAGATTTTTGCTGCGATCACCATCGTGCTGCAACTTCGTTTAATTAATCCTATCCCTGCTTTTAACTTAAAAGGACAT","","","25595","LKFSLPRSTCVNGMNFTKTLYIFKYTGELFAIFIYNEDAMFLNIHRYIFLTFCWGNIMKFEVIYKFLLLCVLIISLLCVVISGAGLFYGWQLSMLFNIHVSFAVLLVAALLLHILNRKNKLAKINTQFADLVLHNKYPSYCNLDRLIMTFEHFSVVQIAEQLNLDLDALLKELAEGKINVKNSHSTLRENFPHNDEKIFAAITIVLQLRLINPIPAFNLKGH","1475386","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-83]?signal-peptide
tmhmm\"[65-87]?\"[93-115]?transmembrane_regions


","No hits to the COGs database.","","Residues 98 to 210 match (6e-23) PD:PD080107 which is described as HI1266 PROTEOME TRANSMEMBRANE COMPLETE ","","","","","","","","","","","","Mon Jan 13 17:24:43 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02156 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02157","1475391","1476365","975","ATGAAAAAGACACTGCTTTATACCGCCATCGCTATGGCTTGCTTACCGGCGTATGCCGAAGAAGTTTTTACCCTTGGGCAAATTGAGGTGATTGCCGATAGATCAACGGATTTAAGCACCACACGCATTGAACAGGCTGACTTACAGAAAAACAATCAAACCAATGTCGCCGAGGTGGCGAAAACCACACCGGGCGTATTTTTGGATCGTAGCGGCGCACGCAATGAACATAATTTGTTGGTACGCGGATTTAAAGCCAATCGCGTGCCAGTGTTTATTGACGGCATTCCGGTGTATGTGCCCTATGACGGCAATATGGACATTGGTCGCTTCACCACCTTCGATTTATCCCGCATTGATATTTCCAAGGGCGCAAGTTCCGTGCTTTATGGCGCCAACACGCTGGGCGGTGCGGTAAATCTCATTACGCAAAAACCGACCAAACCGTTTGAAGGCACTATCGGCTACGGATTTGCTCACGGTAGAAGCGGCAGCACGGGCACCAATCAAACCTACTTTAATTTAGGTTCAAAACAAGACTATTTTTATGCCCAATTAAGCGGTTCATTTTTAGAAAAACAAGGGCTTCAACTGTCGCGTCATTATCATCGGGTTTTACCAAGCGGTGATGATGGCGCACGGGCGGAAAATTCCGTACAACGGGATAAAAAACTCAGTTTGAAAGTGGCGTTTACCCCAAACGCAACGGATGAATATGCTTTGGTGCTTTCGACCCAAAAAAGCGCGAAACAACAGCCGTTATATTCCGGCAAAACCGCCCGTTCCGAACGCTATTGGCGCTGGCCGCAATGGGATAAAGACAGCATTTATTTCTTATCTCATACGCAATTTGATTCACATAATATTTATTTGAATACCAAAGCGTTCTTCGATACCTTCAAAAATGAATTGGACAGCTTTGATGATGCCGGCTTCAGCCGACAAACCGGTAGTAACCGCTTACGGCACAGGATT","","","36410","MKKTLLYTAIAMACLPAYAEEVFTLGQIEVIADRSTDLSTTRIEQADLQKNNQTNVAEVAKTTPGVFLDRSGARNEHNLLVRGFKANRVPVFIDGIPVYVPYDGNMDIGRFTTFDLSRIDISKGASSVLYGANTLGGAVNLITQKPTKPFEGTIGYGFAHGRSGSTGTNQTYFNLGSKQDYFYAQLSGSFLEKQGLQLSRHYHRVLPSGDDGARAENSVQRDKKLSLKVAFTPNATDEYALVLSTQKSAKQQPLYSGKTARSERYWRWPQWDKDSIYFLSHTQFDSHNIYLNTKAFFDTFKNELDSFDDAGFSRQTGSNRLRHRI","1476365","","TonB-dependent outer membrane receptor","Outer membrane, Extracellular","","
InterPro
IPR012910
Domain
TonB-dependent receptor, plug
PF07715\"[32-138]TPlug
noIPR
unintegrated
unintegrated
G3DSA:2.170.130.10\"[34-149]Tno description
signalp\"[1-19]?signal-peptide


","BeTs to 10 clades of COG1629COG name: Outer membrane receptor proteins, mostly Fe transportFunctional Class: PThe phylogenetic pattern of COG1629 is -------q-----cefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 6.4e-07) to 2/3 blocks of the IPB000531 family, which is described as \"TonB-dependent receptor protein\". Interpro entry for IP:IPR000531. IPB000531A 82-95 0.00095 IPB000531B 131-148 0.3","Residues 151 to 304 match (4e-15) PD:PD141743 which is described as RECEPTOR MEMBRANE OUTER TONB DEPENDENT PROBABLY COMPLETE TONB-DEPENDENT RECEPTOR PROTEOME ","","","","","","","","","","","","Mon Jan 13 17:33:39 2003","","","Thu Mar 18 09:32:17 2004","Thu Mar 18 09:32:17 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02157 is paralogously related to AA02151 (4e-10), AA00590 (2e-06), AA00762 (4e-06), AA02202 (6e-04) and AA02782 (0.001).","Thu Mar 18 09:32:17 2004","","","","","","","","","","","","","1","","","" "AA02158","1476295","1477377","1083","ATGAATTGGACAGCTTTGATGATGCCGGCTTCAGCCGACAAACCGGTAGTAACCGCTTACGGCACAGGATTTGAGTTAGGCGGCGATTTAACATCGAATGACACATTGAAATTTTCCGCCATATTAAAACAAGACGTTCATCGTGAACATAATAGCAATGAACCAACCGCCGTCGATAAAGACCGCACTTATAGCTTCGGGTTGGAAAATACCTACCGTTTCAGCGAACGAACCAAATTGATTACCGGCATGAGTTTTGATCGCCGCGAAGCTAAACGGGCGGAAAATTATCAGGCACGCTGCCCGACCACAAACGTTCGTTCGCAAAGCATTTGCCCGTTTAATGTCGCCGACAAAAATGCTTTTAATTATCAAATTAAATTGGTTCACAGTTTCGACGAGCAGGATGAATTCAGCCTTGGTTTTGCGAAGAAAACCCGCTTCCCGACCATGAAAGATCGCTATTCTTATCGTTTAAATCGGGCGGAACCCAATCCGTTCTTGGATCCTGAAATCGCCTACCACTACGAAGCCGGCTATACGCGCACCTTCGGCAATTGGTTAAGACTGGACGGCGCGTTGTTCTATTCCGAAGTGCGTGATGCCATTGAACTTGTGGCGCATCCGACAATTTCCAATAAAGAACAAAATCAAAACTACGGCAAAGAAGTGTTTAAGGGTGTGGAACTTGCCGCCGCAATTTTTGCGACGGATAACCTGACATTGGGTGCCAACTACACTTATACCCGCGCAAAAAATAAAACCTACACGAACTTTATTGTGCGCGATATTCCGCAACATAAATTCTTCGCTTATGTGGATTGGAAAATTGTGCCTAACCTTTCCCTTTATGTCAGTCAAGAAGCGGAACACGGTCGTTATAGCAGAGATGGTTTCGGCAGCCGGGCGCCGACGGTTAGACTTTCCGGCTTCGGCAATACCAATGCCAAACTCACTTACAACGTTACCGAACAATTCATCGTGGAAGCCGGCGTATTCAACCTGTTTGATAAAAACTACTATTATGAAGCCGGTTATCCGGAAGCGGGACGAGTGTATTTTTCTAACTTGAAATATCGTTTT","","","41540","MNWTALMMPASADKPVVTAYGTGFELGGDLTSNDTLKFSAILKQDVHREHNSNEPTAVDKDRTYSFGLENTYRFSERTKLITGMSFDRREAKRAENYQARCPTTNVRSQSICPFNVADKNAFNYQIKLVHSFDEQDEFSLGFAKKTRFPTMKDRYSYRLNRAEPNPFLDPEIAYHYEAGYTRTFGNWLRLDGALFYSEVRDAIELVAHPTISNKEQNQNYGKEVFKGVELAAAIFATDNLTLGANYTYTRAKNKTYTNFIVRDIPQHKFFAYVDWKIVPNLSLYVSQEAEHGRYSRDGFGSRAPTVRLSGFGNTNAKLTYNVTEQFIVEAGVFNLFDKNYYYEAGYPEAGRVYFSNLKYRF","1477377","","TonB-dependent outer membrane receptor","Outer membrane, Cytoplasm","","
InterPro
IPR000531
Domain
TonB-dependent receptor
PF00593\"[123-361]TTonB_dep_Rec
noIPR
unintegrated
unintegrated
G3DSA:2.40.170.20\"[60-361]Tno description


","No hits to the COGs database.","","Residues 64 to 361 match (6e-08) PD:PD141745 which is described as MEMBRANE OUTER COMPLETE PROTEOME PRECURSOR C NOSA SIGNAL RECEPTOR OPRC ","","","","","","","","","","","","Mon Jan 13 17:34:40 2003","","","","Thu Mar 18 09:32:46 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02158 is paralogously related to AA02865 (4e-06).","Thu Mar 18 09:32:46 2004","","","","","","","","","","Ye C, Xu J.Prevalence of iron transport gene on pathogenicity-associated island of uropathogenic Escherichia coli in E. coli O157:H7 containing Shiga toxin gene.J Clin Microbiol. 2001 Jun;39(6):2300-5.PMID: 11376076 ","","Tue Jan 28 14:12:44 2003","1","","","" "AA02159","1477886","1477473","414","ATGTCTATTGTGAAAAAATTTAATCAACTTGTTGATTTACCTGAACTGGCTAAGCTTATTTTACGTGTTGGTTTTTCAGTGTTATTTTTACTACACGGCGTGCATAAATTAAAAACCGGTGTAGATTTCGTCGCTATGAAGTTTATGGAATTCGGTTTACCGGCATCATTTGCATATCTTGCTTATTTGGCGGAAGTCGTTGCACCGGTTCTAATGATTTTAGGGGTTTATACCCGTATCGCCGCGTTTATTGCTGCGAGTGGTTCGGTGGTCATCATGATTTTAATGTATTCCGCCGATCTCTTCACGTTAACTAAAGTTGGTTCATGGACTGCAGAAGGCATTGCGACTTTCTTGTTTGCGTTTGTTGCCGTTATGCTTTTAGGTTCCGGCAAATATGCGTTAAAAGCAGAT","","","14960","MSIVKKFNQLVDLPELAKLILRVGFSVLFLLHGVHKLKTGVDFVAMKFMEFGLPASFAYLAYLAEVVAPVLMILGVYTRIAAFIAASGSVVIMILMYSADLFTLTKVGSWTAEGIATFLFAFVAVMLLGSGKYALKAD","1477473","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR011637
Family
DoxX
PF07681\"[17-98]TDoxX
noIPR
unintegrated
unintegrated
signalp\"[1-36]?signal-peptide
tmhmm\"[10-30]?\"[56-76]?\"[81-101]?\"[115-135]?transmembrane_regions


","BeTs to 7 clades of COG2259COG name: Predicted membrane proteinFunctional Class: SThe phylogenetic pattern of COG2259 is -o-------dr-b-efgh-n-j----Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Mon Jan 13 17:36:01 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02159 is paralogously related to AA02909 (9e-07).","","","","","","Residues 16 to 137 (E-value = 2.6e-12) place AA02159 in the DoxD family which is described as DoxD-like family (PF04173)","","","","","","","","1","","","" "AA02160","1477934","1478989","1056","TTGCTACATATTTATCAATATAGCTTGGAAAAAAGCTGTCTTTCCGAATCTTCAATAATTGGATTACACAACCCCCGTCGGTTCATATATAATATGCCGCCTTTTACGCAATCCGATACAGACAACCCTATGACAATAACGCAAACCGAGAAGAAAAAAAGCTATAATTTCAATAAATTGCAAAAACGTCTACGCCGAAATGTGGGAAACGCAATTGCAGATTTTAATATGATCGAAGAAGGCGACAAGGTGATGGTGTGTTTATCCGGCGGGAAGGACAGCTATACGCTGTTAGATATTTTGTTGAATTTACAGCAAAATGCGCCGATAAAATTCCGGATTGTGGCGGTTAATTTAGACCAAAAACAACCGGGCTTTCCGGAACATATTTTGCCTGGGTATCTGCAAGGTATCGGGGTGGGTTACAAAATCGTGGAAGAAAACACCTATGGCATCGTGAAAGAAAAAATTCCCGAAGGCAAAACCACTTGCTCCCTCTGCTCCCGTTTACGCCGCGGGATTTTATATCGTACCGCAACGGAACTCGGTGCCACCAAAATTGCCTTAGGACACCACCGCGACGATATGTTGGCGACCCTCTTTTTAAATATGTTTTACGGCGGAAAATTAAAATCCATGCCGCCGAAGCTGATTTCCGACGACGGCAAACAAATCGTGATTCGCCCGTTGGCGTACTGCAAAGAAAAAGACATTGAAAAATATGCCGTCGCGAAGGCTTTTCCGATTATTCCTTGCAATCTGTGCGGTTCGCAACCGAATCTGCAACGTCAAGTGGTAAAAGAAATGCTGAATACCTGGGATCGCCAATATCCGGGACGCTTGGAAACCATGTTCAGCGCCATGCAAAACATTACGTTGTCTCACCTGTGTGATCCAAAACTTTTTGATTTCAAAGGCATTAAACACGGTCAATTGATTGAAGGCGTGGAAGGCGATACGGCATTTGATGAAGAAAACATCACGCCGATGCAATTTGATGATGAAGATCAGGCGGATTTCAGCGAGCATGAAATGATCGCCTTTAAGGAAGTGCGG","","","40071","LLHIYQYSLEKSCLSESSIIGLHNPRRFIYNMPPFTQSDTDNPMTITQTEKKKSYNFNKLQKRLRRNVGNAIADFNMIEEGDKVMVCLSGGKDSYTLLDILLNLQQNAPIKFRIVAVNLDQKQPGFPEHILPGYLQGIGVGYKIVEENTYGIVKEKIPEGKTTCSLCSRLRRGILYRTATELGATKIALGHHRDDMLATLFLNMFYGGKLKSMPPKLISDDGKQIVIRPLAYCKEKDIEKYAVAKAFPIIPCNLCGSQPNLQRQVVKEMLNTWDRQYPGRLETMFSAMQNITLSHLCDPKLFDFKGIKHGQLIEGVEGDTAFDEENITPMQFDDEDQADFSEHEMIAFKEVR","1478989","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR011063
Domain
PP-loop
PF01171\"[83-246]TATP_bind_3
InterPro
IPR012089
Family
PP-loop ATPase, YdaO-related
PIRSF004976\"[35-319]TPredicted PP-loop ATPase, YdaO type
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620\"[69-251]Tno description
noIPR
unintegrated
unintegrated
PTHR11807\"[91-329]TATPASES OF THE PP SUPERFAMILY-RELATED
PTHR11807:SF4\"[91-329]TATPASES OF THE PP SUPERFAMILY


","No hits to the COGs database.","Significant hit ( 2.4e-21) to 4/6 blocks of the IPB000541 family, which is described as \"Uncharacterized protein family UPF0021\". Interpro entry for IP:IPR000541. IPB000541B 82-100 1.4e-06 IPB000541D 171-209 9.5e-09 IPB000541E 225-261 1 IPB000541F 263-285 5.2","Residues 47 to 76 match (2e-07) PD:PD261025 which is described as COMPLETE PROTEOME YDAO HI1371.1 VC1432 STY1412 YPO2335 PM0606 ATPASE ORF ","","","","","","","","","","","","Mon Jan 13 17:36:58 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02160 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 83 to 287 (E-value = 6.9e-11) place AA02160 in the ATP_bind_3 family which is described as PP-loop family (PF01171)","","","","","","","","1","","","" "AA02162","1479575","1479090","486","ATGCGTATTTCTTTTAAATCTCTACTTATTTGTTGTTCTGTCCTGGCGTTAGCCGCCTGTTCCGGAGGACCGTCAAAATCCTCGCGGATTAATTACAAAGGGCAGATAAACGATCCTATTATGGCGATTGCGCTTTTAAGCGAACAGCAATACGAATGGGCGGGAACGCCTTATCGTATCGGCGGACAAAGTCGCAGTGGCGTGGATTGCTCCGGTTTCGTGCAAACCACCTTTTTCGATCGCTTCGGCATAAAATTGCCGCGACAAACCAAAGATCAGGCAAATTACGGTCAGTATATTGAAAAAGGCGATATTCAAACCGGTGATTTGGTGTTCTTTAAAACCGGTCGCGGTCCTCATGGCTATCATGTGGGCATTTATGTGAAGGAAGACAAATTTCTGCACGCGTCTACTAAGGGTGGCGTGATTTATTCCTCGTTGAACAGCGATTATTGGCGTAAGGCATATTGGCAGGCAAGACGAATT","","","18137","MRISFKSLLICCSVLALAACSGGPSKSSRINYKGQINDPIMAIALLSEQQYEWAGTPYRIGGQSRSGVDCSGFVQTTFFDRFGIKLPRQTKDQANYGQYIEKGDIQTGDLVFFKTGRGPHGYHVGIYVKEDKFLHASTKGGVIYSSLNSDYWRKAYWQARRI","1479090","","lipoprotein","Outer membrane, Periplasm, Extracellular","","
InterPro
IPR000064
Domain
NLP/P60
PF00877\"[55-161]TNLPC_P60
InterPro
IPR000583
Domain
Glutamine amidotransferase, class-II
PS00443\"[1-16]?GATASE_TYPE_II
noIPR
unintegrated
unintegrated
PTHR21666\"[49-162]TPEPTIDASE-RELATED
PTHR21666:SF1\"[49-162]TNLP/P60 FAMILY SECRETED PROTEIN
PS51257\"[1-20]TPROKAR_LIPOPROTEIN
signalp\"[1-18]?signal-peptide


","BeTs to 13 clades of COG0791COG name: Cell wall-associated hydrolases (invasion-associated proteins)Functional Class: MThe phylogenetic pattern of COG0791 is ---------drlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 8.6e-20) to 3/3 blocks of the IPB000064 family, which is described as \"NLP/P60\". Interpro entry for IP:IPR000064. IPB000064A 58-78 2.2e-07 IPB000064B 103-113 0.012 IPB000064C 123-140 2.9e-06","Residues 45 to 154 match (1e-46) PD:PD001396 which is described as COMPLETE PROTEOME LIPOPROTEIN PRECURSOR SIGNAL SECRETED HYDROLASE MEMBRANE FAMILY REPEAT ","","","","","","","","","","","","Mon Jan 13 17:39:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02162 is paralogously related to AA00644 (3e-35).","","","","","","Residues 55 to 161 (E-value = 8e-49) place AA02162 in the NLPC_P60 family which is described as NlpC/P60 family (PF00877)","","","","","Hara,H., Abe,N., Nakakouji,M., Nishimura,Y. and Horiuchi,K.Overproduction of penicillin-binding protein 7 suppresses thermosensitive growth defect at low osmolarity due to an sprmutation of Escherichia coli. Microb. Drug Resist. 2 (1): 63-72 (1996) [PubMed: 9158724]. ","","Mon Jan 13 17:39:35 2003","1","","","" "AA02163","1479923","1479630","294","ATGACATTAACTAAAGTAGAACTCGCCGAAAATCTTATTGAGAAATTCCATCTCAGTAAACGTGAGGCAAAGGATTTGGTCGAAAGCTTTTTTGAAGAAATCCGTGTGGCTTTGGAAACAGGAAATGACGTGAAATTATCTGGTTTTGGTAATTTTGAATTACGTGATAAAGCTTCCCGTCCGGGTAGAAACCCGAAAACCGGTGAAAGCGTACCGGTTTCTGCCCGTCGTGTGGTGGTGTTCAAACCGGGACAAAAATTGCGCAACCGGGTTGAAAAGGTCAAACCGAAAGCT","","","11077","MTLTKVELAENLIEKFHLSKREAKDLVESFFEEIRVALETGNDVKLSGFGNFELRDKASRPGRNPKTGESVPVSARRVVVFKPGQKLRNRVEKVKPKA","1479630","From GenBank:[FUNCTION] This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control (by similarity). ","integration host factor alpha-subunit","Cytoplasm, Periplasm","","
InterPro
IPR000119
Family
Histone-like bacterial DNA-binding protein
PD000945\"[10-97]TIHFA_PASMU_Q9CN18;
PR01727\"[42-57]T\"[60-73]T\"[76-90]TDNABINDINGHU
G3DSA:4.10.520.10\"[3-92]Tno description
PF00216\"[3-92]TBac_DNA_binding
SM00411\"[3-92]TBHL
PS00045\"[48-67]THISTONE_LIKE
InterPro
IPR005684
Family
Integration host factor, alpha subunit
TIGR00987\"[2-97]ThimA: integration host factor, alpha subuni


","BeTs to 19 clades of COG0776COG name: Bacterial nucleoid DNA-binding proteinFunctional Class: LThe phylogenetic pattern of COG0776 is ---p---qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 3e-17) to 1/1 blocks of the IPB000119 family, which is described as \"Bacterial histone-like DNA-binding protein\". Interpro entry for IP:IPR000119. IPB000119 38-68 2.9e-17","Residues 1 to 41 match (1e-10) PD:PD244007 which is described as REGULATION FACTOR INTEGRATION ALPHA-SUBUNIT HOST IHF-ALPHA TRANSCRIPTION RECOMBINATION TRANSLATION DNA ","","","","","","","","","","","Tue Jan 28 15:58:31 2003","Mon Jan 13 17:42:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02163 is paralogously related to AA02527 (9e-15) and AA00972 (1e-12).","","","","","","Residues 3 to 92 (E-value = 6.2e-44) place AA02163 in the Bac_DNA_binding family which is described as Bacterial DNA-binding protein (PF00216)","","","","","Miller,H.I. Primary structure of the himA gene of Escherichia coli: homology with DNA-binding protein HU and association with the phenylalanyl-tRNA synthetase operon Cold Spring Harb. Symp. Quant. Biol. 49, 691-698 (1984) PubMed: 6397321 Lee,E.C., Hales,L.M., Gumport,R.I. and Gardner,J.F. The isolation and characterization of mutants of the integration host factor (IHF) of Escherichia coli with altered, expanded DNA-binding specificities EMBO J. 11 (1), 305-313 (1992) PubMed: 1531459 ","","Tue Jan 28 15:58:31 2003","1","","","" "AA02164","1482317","1479930","2388","ATGAAATTTAGTGAACAATGGGTACGTGAATGGGTTAATCCGGTAATTTCCACGGAGCAACTTTGCGATCAAATTACCATGTTGGGTTTGGAAGTTGACGGTGTGGAAAAGGTTGCCGGCGATTTCACTGGCGTTGTTGTAGGCGAAGTGGTGGAATGCGCGCAACACCCGGATGCGGATAAATTACGCGTGACCAAAGTAAATGTGGGCGGCGAACGTTTATTGGATATTGTGTGCGGCGCACCGAATTGCCGTCAAGGGTTGAAAGTGGCTTGTGCGGTAGAAGGCGCAAAATTGCCGGGCAATTTCAAAATCAAGAAAACCAAATTACGCGGTCAACCTTCCGAAGGTATGCTCTGTTCATTCAGCGAACTCGGTATTGAATCCGACGCTAACGGCATTATCGAATTGCTGCAAGACGCGCCGATTGGCACGAATTTACGTGATTATTTGAAATTAGATGATAACGCCATTGAAATCAGTTTAACGCCAAACCGTGCCGACTGTTTAAGCATTGCCGGGGTTGCGCGTGAATTGGCGGTGGTTAATAAACTCCACGAAAATCCACCGCACTTTAAAGCGGTTCAGCCTACTATCGACGATAAAGTACAAATTGATGTGCTGGCGCCGGAAGCCTGTCCGCGTTATTTATTGCGTGTGGTGCGAAATGTTAACGTAAAAGCCCAATCACCGATGTGGATGCAGGAAAAATTACGTCGTTGCGGCATTCGTTCTATTGATCCGATTGTGGACATCACTAATTATGTTTTACTGGAATTAGGTCAACCGATGCACGCTTTTGATATGGCAAAAGTGGCGCAACCGGTTCAGGTACGCATGGCGAAAGAAAACGAAGAGTTGGTGTTACTGGACGGCACGACCGCGAAGTTACAACCGAATACGCTGGTTATCGCCGACCAAAATGGCGCTTTGGCAATGGCGGGGATTTTCGGCGGTGAAGCCAGTGGGGTGAATGCGGAAAGCACAAAAGATGTGATTTTAGAAGCGGCATTCTTTGCACCGTTAGCAATTACCGGTCGCGCCCGTCAGTATGGCTTGCATACCGATTCTTCCCACCGTTTTGAACGTGGCGTAGATTTTGAATTGCCACGCAAAGCGATGGAAAGAGCGACCGCACTTTTACTTGACATCTGCGGTGGTGAAGCCGGTGAAATTTACGAGGTGGTTAATGCGCAATATTTACCGAAACGCCAACAAGTCACATTACAACGTCACAAATTAGATGCGTTACTTGGACACCATATTGCTACCGAAACCATTACGGAGATTCTTCAACGCCTTGGTTTACAGGTTTCTTATGCCGCTGACACTTGGACGGCAATTGCACCATCTTGGCGTTTTGATATTGAAATTGCCGAGGATTTAATTGAAGAAATCGCCCGCATTTACGGTTATAACAGCATTCCGAATAATGCGCCGTTAGCACATTTGTGTATGCGTGAACATAAAGAAGCGGATATTGAACTATCTCGCATTAAAGCCGCTCTAACCAGTTGTGATTTTTATGAAGCCATTACTTATAGCTTCGTTGATCCGAAAATCCAAAGTTTGCTGCATCCTGATGTTAAACCGATGGTTTTACCGAACCCGATTTCCGTTGAAATGTCCGCCATGCGTGTTTCATTATTGACCGGTTTATTGGGCGCAGTGATTTATAATCAAAACCGCCAACAAAGTCGCGTGCGTTTGTTTGAGCACGGTTTACGTTTTATTCCGGACGAAAAGGCCGAATTCGGCGTGCACCAAGAGCCGGTTTTTGCCGCGGTGATGACAGGGTTAAAATCAAACGAACAGTGGAGCGAAAAAGCCGTACCGGCAGATTTTTACGACTTAAAAGGCTACATTGAAAACTTACTTTCGTTAAGTTCTGCTGGAAATCGGGCAAAATTTGTAGCAAAATCATACACAGCATTGCATCCGGGTCAATCTGCGGCCATTATGCTGGATGGTGAAGAAATCGGATTTATTGGTCAACTTCACCCGACTATCGCGCAAAAAATTGGTCTTACCGGAAAAGCATTTGTTTGTGAAATTTCGGTCGCACACATTTCTCGACGAGAAGTCGCCCGTGCCAAAGAAATTTCCCGTTTCCCTGCTAATCGTCGTGATTTGGCGGTTGTGGTTGCGGATAATATCCCTGCAAATGACGTGCTGGAAGTGTGTCGTACAGCAGGCGGAGATAAATTAACCCAAATCAATTTATTTGATGTTTACCACGGAACCGGTGTTGCTGCAGGGCATAAGAGCTTAGCTATCAGCTTAGTAATTCAAGATAATGAAAAAACCCTTGAAGAAGATGAAATTAACGCGGTAATTTCAACGGTATTATCTGAGTTAAAACAATGTTTTAATGCTTATTTGAGAGAT","","","87586","MKFSEQWVREWVNPVISTEQLCDQITMLGLEVDGVEKVAGDFTGVVVGEVVECAQHPDADKLRVTKVNVGGERLLDIVCGAPNCRQGLKVACAVEGAKLPGNFKIKKTKLRGQPSEGMLCSFSELGIESDANGIIELLQDAPIGTNLRDYLKLDDNAIEISLTPNRADCLSIAGVARELAVVNKLHENPPHFKAVQPTIDDKVQIDVLAPEACPRYLLRVVRNVNVKAQSPMWMQEKLRRCGIRSIDPIVDITNYVLLELGQPMHAFDMAKVAQPVQVRMAKENEELVLLDGTTAKLQPNTLVIADQNGALAMAGIFGGEASGVNAESTKDVILEAAFFAPLAITGRARQYGLHTDSSHRFERGVDFELPRKAMERATALLLDICGGEAGEIYEVVNAQYLPKRQQVTLQRHKLDALLGHHIATETITEILQRLGLQVSYAADTWTAIAPSWRFDIEIAEDLIEEIARIYGYNSIPNNAPLAHLCMREHKEADIELSRIKAALTSCDFYEAITYSFVDPKIQSLLHPDVKPMVLPNPISVEMSAMRVSLLTGLLGAVIYNQNRQQSRVRLFEHGLRFIPDEKAEFGVHQEPVFAAVMTGLKSNEQWSEKAVPADFYDLKGYIENLLSLSSAGNRAKFVAKSYTALHPGQSAAIMLDGEEIGFIGQLHPTIAQKIGLTGKAFVCEISVAHISRREVARAKEISRFPANRRDLAVVVADNIPANDVLEVCRTAGGDKLTQINLFDVYHGTGVAAGHKSLAISLVIQDNEKTLEEDEINAVISTVLSELKQCFNAYLRD","1479930","[CATALYTIC ACTIVITY] ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe).[COFACTOR] Binds 2 magnesium ions per tetramer (By similarity).[SUBUNIT] Tetramer of two alpha and two beta chains (By similarity).[SUBCELLULAR LOCATION] Cytoplasmic.","phenylalanyl-tRNA synthetase, beta chain","Cytoplasm","","
InterPro
IPR002547
Domain
t-RNA-binding region
PF01588\"[45-146]TtRNA_bind
PS50886\"[39-148]TTRBD
InterPro
IPR004532
Family
Bacterial phenylalanyl-tRNA synthetase, beta subunit
TIGR00472\"[1-795]TpheT_bact: phenylalanyl-tRNA synthetase, be
InterPro
IPR005121
Domain
Ferredoxin-fold anticodon-binding
G3DSA:3.30.70.380\"[704-788]Tno description
PF03147\"[702-795]TFDX-ACB
InterPro
IPR005146
Domain
B3/4
PF03483\"[212-386]TB3_4
InterPro
IPR005147
Domain
tRNA synthetase, B5
G3DSA:3.30.56.20\"[404-477]Tno description
PF03484\"[404-472]TB5
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[38-154]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.30.930.10\"[490-687]Tno description
G3DSA:3.50.40.10\"[190-401]Tno description
PTHR10947\"[1-796]TPHENYLALANYL-TRNA SYNTHETASE BETA CHAIN


","No hits to the COGs database.","Significant hit ( 1.6e-13) to 2/2 blocks of the IPB002547 family, which is described as \"Putative tRNA binding domain\". Interpro entry for IP:IPR002547. IPB002547A 56-70 0.00022 IPB002547B 104-121 2e-07","Residues 494 to 678 match (9e-07) PD:PD560268 which is described as PROBABLE LIGASE PROTEOME PHENYLALANYL-TRNA CHAIN BETA SYNTHETASE COMPLETE ","","","","","","","","","","","Mon Jan 13 17:47:49 2003","Mon Jan 13 17:47:49 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02164 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 702 to 795 (E-value = 4.5e-42) place AA02164 in the FDX-ACB family which is described as Ferredoxin-fold anticodon binding domain (PF03147)","","","","","Fayat,G., Mayaux,J.F., Sacerdot,C., Fromant,M., Springer,M., Grunberg-Manago,M. and Blanquet,S. Escherichia coli phenylalanyl-tRNA synthetase operon region. Evidence for an attenuation mechanism. Identification of the gene for the ribosomal protein L20 J. Mol. Biol. 171 (3), 239-261 (1983) PubMed: 6317865 Kast,P. and Hennecke,H. Amino acid substrate specificity of Escherichia coli phenylalanyl-tRNA synthetase altered by distinct mutations J. Mol. Biol. 222 (1), 99-124 (1991) PubMed: 1942071 Kast,P., Wehrli,C. and Hennecke,H. Impaired affinity for phenylalanine in Escherichia coli phenylalanyl-tRNA synthetase mutant caused by Gly-to-Asp exchange in motif 2 of class II tRNA synthetases FEBS Lett. 293 (1-2), 160-163 (1991) PubMed: 1959653 Kast,P., Keller,B. and Hennecke,H. Identification of the pheS5 mutation, which causes thermosensitivity of Escherichia coli mutant NP37 J. Bacteriol. 174 (5), 1686-1689 (1992) PubMed: 1537809 ","","Wed Jan 29 15:01:16 2003","1","","","" "AA02166","1483326","1482340","987","ATGCAGCATCTTAAAGATCTTGTGGAGAAAGCAAGAAATGCTATAGACAGTATTGAAAATAAAAGCCTGGCGGCACTTGATGAAATTCGGGTGGAATATTTTGGTAAAAAAGGGCATTTTACCCAATTAATGCAAGAACTACGCAATGTGGCGGCGGAAGAGCGTCCGGCGGTGGGTGCAAAAATTAACGAAGCCAAACAAGCGGCGTTGGATTTTTTAAACGCGAAAAAAGCAGAGTGGGAACAAGCCTTATTAGACGCCAAACTGGAAAATGAACGCATTGATGTGAGCCTGCCGGGGCGTAAAGTGGAAATGGGCGGTTTACATCCGGTTTCCATCACTATTGAACGCGTCACCAAATTTTTCTCCGAATTGGGTTTCTCCGTGGAATCCGGCCCTGAAATCGAAAGCGATTACTATAACTTTGATGCCTTAAATATCCCGAAACATCACCCGGCACGCGCTGATCACGATACCTTCTGGTTTAATCCTGAATTATTGTTAAGAACCCAAACCTCCGGTGTACAAATTCGTACCATGCAAAAACAACAGCCGCCGATTCGCATTATGGCGCCAGGGCGTGTGTATCGTAACGATTACGACCAAACCCACACACCGATGTTCCATCAAATCGAATTATTGTATGTGGACAAACACGCCAATTTCACCGAATTAAAAGGCTTGTTACATGATTTCTTACGCGCCTTTTTTGAGGAAGATTTGCAGGTGCGTTTCCGTCCGTCTTATTTCCCGTTCACCGAACCTTCCGCTGAAGTGGATGTGATGGGGAAAAACGGTAAATGGCTGGAAGTGTTGGGTTGCGGCATGGTGCATCCGAACGTATTGCGCAATGTCGGCATTGACCCGAACGAATATTCCGGTTTTGCGGTGGGCATGGGTGTAGAACGTTTGACCATGTTACGCTACAACGTCACGGATTTACGTTCATTCTTTGAGAATGACTTACGCTTTTTGAAACAGTTTAAA","","","37920","MQHLKDLVEKARNAIDSIENKSLAALDEIRVEYFGKKGHFTQLMQELRNVAAEERPAVGAKINEAKQAALDFLNAKKAEWEQALLDAKLENERIDVSLPGRKVEMGGLHPVSITIERVTKFFSELGFSVESGPEIESDYYNFDALNIPKHHPARADHDTFWFNPELLLRTQTSGVQIRTMQKQQPPIRIMAPGRVYRNDYDQTHTPMFHQIELLYVDKHANFTELKGLLHDFLRAFFEEDLQVRFRPSYFPFTEPSAEVDVMGKNGKWLEVLGCGMVHPNVLRNVGIDPNEYSGFAVGMGVERLTMLRYNVTDLRSFFENDLRFLKQFK","1482340","[CATALYTIC ACTIVITY] ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe).[COFACTOR] Binds 2 magnesium ions per tetramer (By similarity).[SUBUNIT] Tetramer of two alpha and two beta chains (By similarity).[SUBCELLULAR LOCATION] Cytoplasmic.","phenylalanyl-tRNA synthetase, alpha subunit","Cytoplasm","","
InterPro
IPR002319
Family
Phenylalanyl-tRNA synthetase, class IIc
PTHR11538\"[1-329]TPHENYLALANYL-TRNA SYNTHETASE
PF01409\"[93-328]TtRNA-synt_2d
InterPro
IPR004188
Domain
Aminoacyl tRNA synthetase, class II, N-terminal
PF02912\"[18-90]TPhe_tRNA-synt_N
InterPro
IPR004529
Family
Phenylalanyl-tRNA synthetase, alpha subunit
TIGR00468\"[39-329]TpheS: phenylalanyl-tRNA synthetase, alpha s
InterPro
IPR006195
Domain
Aminoacyl-transfer RNA synthetase, class II
PS50862\"[118-327]TAA_TRNA_LIGASE_II
noIPR
unintegrated
unintegrated
G3DSA:3.30.930.10\"[7-328]Tno description


","No hits to the COGs database.","","Residues 9 to 89 match (3e-15) PD:PD409709 which is described as SYNTHETASE ALPHA LIGASE CHAIN PROTEOME COMPLETE AMINOACYL-TRNA PHENYLALANYL-TRNA ATP-BINDING BIOSYNTHESIS ","","","","","","","","","","","Mon Jan 13 17:50:41 2003","Mon Jan 13 17:50:41 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02166 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 110 to 315 (E-value = 2.7e-133) place AA02166 in the tRNA-synt_2d family which is described as tRNA synthetases class II core domain (F) (PF01409)","","","","","ayat,G., Mayaux,J.F., Sacerdot,C., Fromant,M., Springer,M., Grunberg-Manago,M. and Blanquet,S. Escherichia coli phenylalanyl-tRNA synthetase operonregion. Evidence for an attenuation mechanism. Identification of the gene for the ribosomal protein L20 J. Mol. Biol. 171 (3), 239-261 (1983) PubMed: 6317865 Kast,P. and Hennecke,H. Amino acid substrate specificity of Escherichia coli phenylalanyl-tRNA synthetase altered by distinct mutations J. Mol. Biol. 222 (1), 99-124 (1991) PubMed: 1942071 Kast,P., Wehrli,C. and Hennecke,H. Impaired affinity for phenylalanine in Escherichia coli phenylalanyl-tRNA synthetase mutant caused by Gly-to-Asp exchange in motif 2 of class II tRNA synthetases FEBS Lett. 293 (1-2), 160-163 (1991) PubMed: 1959653 Kast,P., Keller,B. and Hennecke,H. Identification of the pheS5 mutation, which causes thermosensitivity of Escherichia coli mutant NP37 J. Bacteriol. 174 (5), 1686-1689 (1992) PubMed: 1537809 ","","Wed Jan 29 15:02:43 2003","1","","","" "AA02167","1483534","1483427","108","TTGAACGTTGGCTTTTCCAACCGCCCGTTAGGGGTGAAGAAACGAGAGAGCGAGTTTGTAAATAATTTTTTCGGGCGTTTTTTATCGGTATCCTTTTCTACTCACGAA","","","4130","LNVGFSNRPLGVKKRESEFVNNFFGRFLSVSFSTHE","1483427","","hypothetical protein","Cytoplasm, Extracellular","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:19:49 2004","Wed Feb 25 15:19:49 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02167 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:19:49 2004","","","","","","","","","","","","","1","","","" "AA02168","1484541","1483669","873","ATGATGCGCATTTTACTTTTCTTAGCCACGAACATGGCGGTTTTACTGGTTTTCAACATCATTTTATCTTTAACCGGCATTCAAGCCCGTGACGCGTCCGGGTTAATGATTTTCGCGGCACTGTTCGGTTTTGCCGGTTCCATCATTTCCTTATTTATGTCTAAAACTATGGCGATTCGCGCCGTCGGTGCGGAAGTGATTCAACAACCGCGTAATGAAACGGAACGTTGGTTGGTGGATACCGTGTATTCGCAAGCAGAACGTGCCGGTTTACCGCGCCCTGAAGTGGCTATTTATCATTCCGCTGATGTCAACGCCTTTGCTACCGGTGCGAGCAAAAATAATTCGCTGGTTGCCGTAAGTACGGGGCTGTTAAACAAAATGACGCGCGGTGAAGCGGAAGCGGTATTGGCGCATGAAGTGAGCCATATTAAAAACGGTGACATGGTCACGATGGCATTACTGCAAGGCGTGCTGAATACCTTCGTCATTTTCTTATCGCGCTTAATCGCGAATGTGGTCGCCAATTCTCGTAATCAGGGCAGTGAAAGTTCAAGCAATTCCGGTATTTATTTCTTGGTGTCCATGGTGCTGGAAGTGGTGTTCGGTTTCTTGGCAAGCATGATCGCCATGTGGTTCTCCCGTCAACGTGAATTCAGAGCGGATGCCGGTTCGGCGGATTTGGTGGGCAAACAAAAAATGATTGATGCGTTAAAACGTCTGCAAAGTTTGCATGAACCGCAAGAATTAGAAGGCTCCGCCTTAGCTGCATTTGCCATTAACGGTAAACGTGGTGGCGGTTTGAAAGAGTTACTTTTAAGCCACCCGCCGTTGGAAAAACGTATTGAAGCGTTGCAACAGTTGCGTCAGTTA","","","35930","MMRILLFLATNMAVLLVFNIILSLTGIQARDASGLMIFAALFGFAGSIISLFMSKTMAIRAVGAEVIQQPRNETERWLVDTVYSQAERAGLPRPEVAIYHSADVNAFATGASKNNSLVAVSTGLLNKMTRGEAEAVLAHEVSHIKNGDMVTMALLQGVLNTFVIFLSRLIANVVANSRNQGSESSSNSGIYFLVSMVLEVVFGFLASMIAMWFSRQREFRADAGSADLVGKQKMIDALKRLQSLHEPQELEGSALAAFAINGKRGGGLKELLLSHPPLEKRIEALQQLRQL","1483669","","possible protease; heat shock protein","Inner membrane, Cytoplasm","","
InterPro
IPR001915
Family
Peptidase M48, Ste24p
PF01435\"[78-290]TPeptidase_M48
InterPro
IPR009481
Domain
Peptidase M48B, HtpX peptidase N-terminal
PF06509\"[1-77]THtpX_N
noIPR
unintegrated
unintegrated
signalp\"[1-29]?signal-peptide
tmhmm\"[5-23]?\"[33-53]?\"[153-171]?\"[190-210]?transmembrane_regions


","No hits to the COGs database.","","Residues 87 to 174 match (9e-24) PD:PD544974 which is described as PROTEOME COMPLETE HEAT SHOCK ","","","","","","","","","","","","Mon Jan 13 17:59:38 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02168 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 78 to 290 (E-value = 1.1e-52) place AA02168 in the Peptidase_M48 family which is described as Peptidase family M48 (PF01435)","","","","","Shimohata N, Chiba S, Saikawa N, Ito K, Akiyama Y. The Cpx stress response system of Escherichia coli senses plasma membrane proteins and controls HtpX, a membrane protease with a cytosolic active site. Genes Cells. 2002 Jul;7(7):653-62. PMID: 12081643 Vickerman MM, Mather NM, Minick PE, Edwards CA. Initial characterization of the Streptococcus gordonii htpX gene. Oral Microbiol Immunol. 2002 Feb;17(1):22-31. PMID: 11860552 Kornitzer D, Teff D, Altuvia S, Oppenheim AB. Isolation, characterization, and sequence of an Escherichia coli heat shock gene, htpX. J Bacteriol. 1991 May;173(9):2944-53. PMID: 1826904 ","","Wed Jan 29 14:39:32 2003","1","","","" "AA02169","1484578","1484724","147","ATGCTTGGCTATAATGGCGATAAAAACAGGAAAATCAAGTGTACCGATGAATTTTCTACGGAAGAGTGGCAATTTAATGGGAAAACATACAAAAAAGTGCAGTCGGTTTTAAGGACGTTTTTTGAAAAGAAAAATGGAGTTGGTCGA","","","5790","MLGYNGDKNRKIKCTDEFSTEEWQFNGKTYKKVQSVLRTFFEKKNGVGR","1484724","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:18:28 2004","Wed Feb 25 15:18:28 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02169 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:18:28 2004","","","","","","","","","","","","","1","","","" "AA02171","1485224","1486156","933","ATGGACTATTTACACATCGCTCAGGAAACCCTGGGTGTGGAAGAAAACGCCCTCGGGCAACTTAAACAAAGATTAGACGGCACTTTCGCCGACGTCGTAAATTTGATTCTGAACTGCAAAGGTCGTTTGGTTATCGGCGGCATCGGCAAGTCCGGATTGGTAGGCAAAAAAATGGTTGCCACTTTCGCTTCCACCGGCACGCCAAGTTTCTTCTTACACCCGACGGAAGCTTTCCACGGTGATTTAGGGATGCTTAAACCCATTGATGTGGTTATGCTCATATCTTATAGCGGCGAAACCGACGATGTGAACAAACTCATTCCAAGCCTGAAAAACTTCGGTAATAAAATCATCGCTTTAACCTCGAATAAAAATTCTACGCTGGCGCGCCATGCGGATTATGTGTTGGACATCACCGTAGAACGCGAAGTCTGCCCGAATAATCTGGCACCGACCACCTCCGTTATTGTCACCATGGCATTGGGCGACGCATTAGCCGTCTGTTTAATGCGCGCCCGCGATTTCCAACCAGAAGATTTCGCCAAATTCCACCCTGGCGGCAGTTTGGGACGCCGTTTGTTATGCCGCGTGAAAGATCAAATGCAAACCCACTTGCCGATCGCCGCATTAACCACTACCTTCACCGATTGTTTAAGCATCATGAACGAAGGCAGAATGGGCGTGGCGTTGGTGATGGAACAACAGCAACTGCGCGGCATTATTACCGATGGCGATATTCGACGCGCGCTCACCGCAAACGGTGCAGAAACCTTGAATAAAACTGCGCAGGAGCTCATGACGTCTCATCCGAAGACCATTCACCAAGACACCTATATTTCGGAAGCGGAAAATTACATGAAAGCGCATAAAATTCATTCTTTGGTTGTAGTGGATGATGCGCAACACGTGGTCGGTTTAGTGGAGTTTTCAAGT","","","33906","MDYLHIAQETLGVEENALGQLKQRLDGTFADVVNLILNCKGRLVIGGIGKSGLVGKKMVATFASTGTPSFFLHPTEAFHGDLGMLKPIDVVMLISYSGETDDVNKLIPSLKNFGNKIIALTSNKNSTLARHADYVLDITVEREVCPNNLAPTTSVIVTMALGDALAVCLMRARDFQPEDFAKFHPGGSLGRRLLCRVKDQMQTHLPIAALTTTFTDCLSIMNEGRMGVALVMEQQQLRGIITDGDIRRALTANGAETLNKTAQELMTSHPKTIHQDTYISEAENYMKAHKIHSLVVVDDAQHVVGLVEFSS","1486156","","polysialic acid capsule expression protein","Cytoplasm","","
InterPro
IPR000644
Domain
Cystathionine-beta-synthase
PF00571\"[199-307]TCBS
SM00116\"[204-251]T\"[269-311]TCBS
InterPro
IPR001347
Domain
Sugar isomerase (SIS)
PF01380\"[36-169]TSIS
InterPro
IPR004800
Family
KpsF/GutQ
TIGR00393\"[41-308]TkpsF: sugar isomerase, KpsF/GutQ family
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.10490\"[1-184]Tno description
PTHR11911\"[196-308]TINOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED
PTHR11911:SF5\"[196-308]TINOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED


","BeTs to 13 clades of COG0794COG name: Predicted sugar phosphate isomerase involved in capsule formationFunctional Class: MThe phylogenetic pattern of COG0794 is a-m-kz-q----b-efghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 5.3e-11) to 3/3 blocks of the IPB000281 family, which is described as \"Helix-turn-helix domain, RpiR family\". Interpro entry for IP:IPR000281. IPB000281A 47-65 14 IPB000281B 74-121 3.4e-08 IPB000281C 144-166 18Significant hit ( 2e-10) to 2/2 blocks of the IPB001347 family, which is described as \"SIS domain\". Interpro entry for IP:IPR001347. IPB001347A 72-80 2.8 IPB001347B 89-114 2.5e-08","Residues 254 to 309 match (3e-16) PD:PD471072 which is described as PROTEOME COMPLETE ATP-BINDING REPEAT DOMAIN CBS CAPSULE EXPRESSION POLYSIALIC ISOMERASE ","","","","","","","","","","","","Mon Jan 13 18:09:39 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02171 is paralogously related to AA02468 (6e-07) and AA00629 (4e-04).","","","","","","Residues 264 to 311 (E-value = 1.4e-06) place AA02171 in the CBS family which is described as CBS domain (PF00571)","","","","","Simpson,D.A., Hammarton,T.C. and Roberts,I.S. Transcriptional organization and regulation of expression of region 1 of the Escherichia coli K5 capsule gene cluster J. Bacteriol. 178 (22), 6466-6474 (1996) PubMed: 8932302 Tzeng YL, Datta A, Strole C, Kolli VS, Birck MR, Taylor WP, Carlson RW, Woodard RW, Stephens DS. KpsF is the arabinose-5-phosphate isomerase required for 3-deoxy-D-manno-octulosonic acid biosynthesis and for both lipooligosaccharide assembly and capsular polysaccharide expression in Neisseria meningitidis. J Biol Chem. 2002 Jul 5;277(27):24103-13. PMID: 11956197 Cieslewicz M, Vimr E. Reduced polysialic acid capsule expression in Escherichia coli K1 mutants with chromosomal defects in kpsF. Mol Microbiol. 1997 Oct;26(2):237-49. PMID: 9383150Cieslewicz,M.J., Steenbergen,S.M. and Vimr,E.R. Cloning, sequencing, expression, and complementation analysis of the Escherichia coli K1 kps region 1 gene, kpsE, and identificationof an upstream open reading frame encoding a protein with homologyto Gut J. Bacteriol. 175 (24): 8018-8023 (1993) [PubMed: 8253690].","","Mon Jan 13 18:09:39 2003","1","","","" "AA02172","1486159","1486710","552","ATGACAGCAGAATTACAGGAAAAATTGAAACGGGTGAAGTTCGTCATCACCGATGTGGACGGCGTATTAACGGACGGTTTATTGCACTACGATGCCAACGGCGAAGCGATCAAAAGTTTTCATGTACGCGACGGTTTAGGTATCCGAATGTTGATGGAAGCCGGCGTGCAGATCGCCGTCTTATCCGGGCGTGATTCGGCGATTTTACGCAAACGCATTGCCGATTTAGGCATTAAACGCTTCTTTTTGGGTAAATTGGAAAAAGAAAGCGCCTGTTTGGAATTATGCCGCCAAGCCGGCGTTGTGCCCGAACAAACCGCCTACATCGGCGACGACAGTGTTGACCTCCCCGCCTTTGCCGTTTGTGGCATATCTTTTGCCGTTGCCGACGCCCCCGAATATGTCAAAGATTGTGCCGATTACGTCTTGGGTTTAGGCGGTGGCAAAGGGGCGTTTCGTGAAATGTCCGACATGATCTTAAATGCCCAAGGCAAAAGCGACATTTACAGCTCCGCACAAGGATTTTTGAAAACAGCGAAGAAGATGGCACAG","","","19840","MTAELQEKLKRVKFVITDVDGVLTDGLLHYDANGEAIKSFHVRDGLGIRMLMEAGVQIAVLSGRDSAILRKRIADLGIKRFFLGKLEKESACLELCRQAGVVPEQTAYIGDDSVDLPAFAVCGISFAVADAPEYVKDCADYVLGLGGGKGAFREMSDMILNAQGKSDIYSSAQGFLKTAKKMAQ","1486710","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR005834
Domain
Haloacid dehalogenase-like hydrolase
PF00702\"[48-132]THydrolase
InterPro
IPR006549
Domain
HAD-superfamily hydrolase, subfamily IIIA
TIGR01662\"[13-131]THAD-SF-IIIA: hydrolase, HAD-superfamily, su
InterPro
IPR008230
Family
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase
PIRSF006118\"[3-177]T3-deoxy-D-manno-octulosonate 8-phosphate phosphatase
InterPro
IPR010023
Domain
Phosphatase kdsC
TIGR01670\"[12-165]TYrbI-phosphatas: 3-deoxy-D-manno-octulosona
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1000\"[5-184]Tno description
PTHR21485\"[22-146]TCMP-N-ACETYLNEURAMINIC ACID SYNTHASE
PTHR21485:SF10\"[22-146]TN-ACYLNEURAMINATE-9-PHOSPHATASE


","BeTs to 9 clades of COG1778COG name: Uncharacterized proteins of HAD superfamily, CMP-Neu5Ac homologsFunctional Class: RThe phylogenetic pattern of COG1778 is -------q------efghsnu-----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.3e-05) to 3/3 blocks of the IPB000150 family, which is described as \"Cof protein\". Interpro entry for IP:IPR000150. IPB000150A 11-25 17 IPB000150B 55-64 4.9 IPB000150C 107-139 0.061","Residues 5 to 184 match (2e-74) PD:PD186741 which is described as COMPLETE PROTEOME TRANSFERASE ACID FIXI NUCLEOTIDYLTRANSFERASE SYNTHETASE YRBI COF FAMILY ","","","","","","","","","","","","Mon Jan 13 18:11:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02172 is paralogously related to AA00128 (6e-04).","","","","","","","","","","","","","","1","","","" "AA02173","1486881","1488425","1545","ATGTCCTCCGCTTTTATTCAAACGTTTACGCAAAATGTCCCTTATCACAGCGATCCTACCGCAATTTTCGCCACATTATGTGAAAACAAACCGAACACCCTGCTTTTAGAATCCGCCGAAATTTCCAGCAAAAACAGTTTAAAAAGTTTATTACTCGTCAATGCCGCCATCAAAATTTCCTGTTTGGGGCAACGGGTGAGGTTTCACGCATTAACCCAGAACGGCGCGGCGGTATTGCCGTTAATCGAGCAAAAATTAGCGGCGCACGTCAGTGTAAAATCCCGCACAAGCGAGCAATTGGACGTGGAGTTTTCCCCGGCCGATAACAATGCCGATGAAGACAGCAAATTGCTGGCGGCAAGCATTTTCGACGGCTTACGCTGCTTCACCGAACTCTACAAGGCAAGCCCGTTACCGGTATTTTTAGGCGGTTTGTTCGCTTACGATTTGGTGGCGAATTTTATTCCGATGAAAAACATTCAGTTGCAAGATGATGGCATTACCTGTCCGGATTATTGCTTTTATTTAGCTGAACAATTACTGGTGATCGACCATCAATTACAACAGGCGGAATTACAAACTTTCTGCTTTGCACAACATCAAGAAAATGCGTTGCAACAGGAAGCGCAGGACATTGCCAAAAAACTCTTGGAAATTCGACCGCACTTACCACTCAAACCTGCCTCAACGGAGGTTTCCGTTAATCTGAACGATGATAAATTCAAGAAAATTATTGAGCGTTTGAAACAGCATATTTATTGCGGCGATGTGTTCCAAATCGTGCCTTCCCGCCGTTTTTCTCTAGAATGCCCGAACACCCTGGCAACATATCGTCAACTCAAACAAAACAACCCGAGCCCTTATATGTTCTTCATTCAGGATGCGGATTTCACCCTGTTCGGCGCCTCGCCGGAAAGTGCCTTGAAATATTCGCAAGCCACCCGCCAACTGGAAATTTACCCGATTGCCGGTTCCCGTCCGCGCGGTTTTGATGCTGATGGCAATATCGATCCGGAATTGGATTCCCGCCTGGAATTGGAATTACGTTTAGATCACAAAGAACAGGCGGAACATTTGATGTTGGTGGATTTGGCGCGTAACGACATCGCCCGCGTATGTGAAAGCAAAACCCGTCATGTGAAGGATTTGATGCAGGTAGATCGCTATTCGCACATTATGCACTTGGTTTCCCGCGTAGTGGGTAAACTCCGTCCTGAACTGGATGCGTTGCACGCTTATCAAGCCTGTATGAACATGGGCACACTAACCGGCTCGCCGAAAATTAAAGCCATGCAGCTGATTTATCAATTTGAACAGGAAAAACGCCACAGTTACGGCGGTGCGGTGGGGTATCTGCAATCCGACGGCAATTTTGACACCTGTATCGTGATTCGTTCCGCTTTCGTGCAAAACGGCATTGCCCACGTACAAGCCGGCTGTGGCACGGTGTTGGATTCCGACCTGCAAATGGAAGCCGACGAAACCCGCCACAAAGCCCGCGCGGTAATTAACGCCATCGTACAAACCAACAACAAAGCGAATCAA","","","58692","MSSAFIQTFTQNVPYHSDPTAIFATLCENKPNTLLLESAEISSKNSLKSLLLVNAAIKISCLGQRVRFHALTQNGAAVLPLIEQKLAAHVSVKSRTSEQLDVEFSPADNNADEDSKLLAASIFDGLRCFTELYKASPLPVFLGGLFAYDLVANFIPMKNIQLQDDGITCPDYCFYLAEQLLVIDHQLQQAELQTFCFAQHQENALQQEAQDIAKKLLEIRPHLPLKPASTEVSVNLNDDKFKKIIERLKQHIYCGDVFQIVPSRRFSLECPNTLATYRQLKQNNPSPYMFFIQDADFTLFGASPESALKYSQATRQLEIYPIAGSRPRGFDADGNIDPELDSRLELELRLDHKEQAEHLMLVDLARNDIARVCESKTRHVKDLMQVDRYSHIMHLVSRVVGKLRPELDALHAYQACMNMGTLTGSPKIKAMQLIYQFEQEKRHSYGGAVGYLQSDGNFDTCIVIRSAFVQNGIAHVQAGCGTVLDSDLQMEADETRHKARAVINAIVQTNNKANQ","1488425","[PATHWAY] Tryptophan biosynthesis; first step.","anthranilate synthase component I","Cytoplasm","","
InterPro
IPR005257
Family
Anthranilate synthase component I, TrpE
TIGR00565\"[15-511]TtrpE_proteo: anthranilate synthase componen
InterPro
IPR005801
Domain
Anthranilate synthase component I and chorismate binding protein
PD000779\"[15-501]TQ9CN59_PASMU_Q9CN59;
PR00095\"[346-359]T\"[360-373]T\"[440-454]T\"[455-469]TANTSNTHASEI
PF00425\"[237-506]TChorismate_bind
InterPro
IPR006805
Domain
Anthranilate synthase component I, N-terminal
PF04715\"[15-192]TAnth_synt_I_N
noIPR
unintegrated
unintegrated
G3DSA:3.60.120.10\"[2-506]Tno description
PTHR11236\"[138-511]TAMINOBENZOATE/ANTHRANILATE SYNTHASE
PTHR11236:SF9\"[138-511]TANTHRANILATE SYNTHASE COMPONENT I


","No hits to the COGs database.","Significant hit ( 4.9e-32) to 4/4 blocks of the PR00095 family, which is described as \"Anthranilate synthase component I signature\". Prints database entry for PR:PR00095. PR00095A 346-359 7.6e-06 PR00095B 360-373 2.9e-10 PR00095C 440-454 0.00048 PR00095D 455-469 6e-07","Residues 431 to 506 match (3e-32) PD:PD000779 which is described as SYNTHASE PROTEOME COMPLETE ANTHRANILATE COMPONENT I LYASE BIOSYNTHESIS TRYPTOPHAN ISOCHORISMATE ","","","","","","","","","","","Mon Jan 13 18:15:10 2003","Fri May 20 08:05:30 2005","","Fri May 20 08:05:30 2005","Fri May 20 08:05:30 2005","Fri May 20 08:05:30 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA02173 is paralogously related to AA00085 (5e-12) and AA01609 (8e-10).","Fri May 20 08:05:30 2005","","","","","Residues 237 to 506 (E-value = 3.5e-146) place AA02173 in the Chorismate_bind family which is described as chorismate binding enzyme (PF00425)","Fri May 20 08:05:30 2005","","","","Yanofsky,C., Platt,T., Crawford,I.P., Nichols,B.P., Christie,G.E., Horowitz,H., VanCleemput,M. and Wu,A.M. The complete nucleotide sequence of the tryptophan operon of Escherichia coli. Nucleic Acids Res. 9 (24): 6647-6668 (1981) [PubMed: 7038627]. Nichols,B.P., van Cleemput,M. and Yanofsky,C. Nucleotide sequence of Escherichia coli trpE. Anthranilate synthetase component I contains no tryptophan residues. J. Mol. Biol. 146 (1): 45-54 (1981) [PubMed: 7021857].","","Mon Jan 13 18:15:10 2003","1","","","" "AA02175","1488439","1489026","588","ATGGCAACCATTTTATTTTTAGATAACTTTGATTCCTTTACTTACAATTTGGTGGATCAGTTTCGCGGTTTAGGGCATCAGGTGAACATTTACCGCAATGATTGCGACTTAGATCTGTTGGAAAAAACCGCATTGGCGCAACCCGATACCATTCTCGCCCTTTCCCCGGGGCCGGGCACACCCGACGAAGCAGGAAACATGATTCCGTTGATTAAACGCTTAATCGGCAAAGTCCCGATGTTGGGCATTTGTTTGGGACATCAGGCGTTAATTGAAGCGTTCGGTGGCAAAGTAGTTCATGCAGGTGAAATTCTGCACGGAAAAGTATCCGGAATCGAACACGATAACGAAGCCATGTTCAAAGGCTTAAGCAACCCTATGCCGGTGGCGCGCTACCATTCGTTAATGGGCATCAATCTCCCCGACGACCTGATTCCGAACGCCGCCTACAACGGCATAAACATGGCAATTCGCCACCGCACGTTGCCAATTTGCAGCTTCCAGTTCCATCCCGAATCCATTTTAACGGTACAAGGCGCGCAATTATTGGCACAATCGGTGAACTGGTTGTTGGCGCGAAAAACGCCG","","","21419","MATILFLDNFDSFTYNLVDQFRGLGHQVNIYRNDCDLDLLEKTALAQPDTILALSPGPGTPDEAGNMIPLIKRLIGKVPMLGICLGHQALIEAFGGKVVHAGEILHGKVSGIEHDNEAMFKGLSNPMPVARYHSLMGINLPDDLIPNAAYNGINMAIRHRTLPICSFQFHPESILTVQGAQLLAQSVNWLLARKTP","1489026","[PATHWAY] Tryptophan biosynthesis; first step.","anthranilate synthase component II","Cytoplasm","","
InterPro
IPR000991
Domain
Glutamine amidotransferase class-I
PF00117\"[5-189]TGATase
InterPro
IPR001317
Domain
Carbamoyl-phosphate synthase, GATase region
PR00099\"[49-63]T\"[79-95]TCPSGATASE
InterPro
IPR006220
Domain
Anthranilate synthase component II/delta crystallin
PR00097\"[4-18]T\"[52-61]T\"[79-90]T\"[104-112]T\"[124-136]T\"[166-179]TANTSNTHASEII
InterPro
IPR006221
Domain
Glutamine amidotransferase of anthranilate synthase
TIGR00566\"[3-189]TtrpG_papA: glutamine amidotransferase of an
InterPro
IPR011702
Domain
Glutamine amidotransferase superfamily
PR00096\"[52-61]T\"[79-90]T\"[166-179]TGATASE
InterPro
IPR012998
Active_site
Glutamine amidotransferase, class I, active site
PS00442\"[79-90]?GATASE_TYPE_I
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.880\"[2-193]Tno description
PIRSF001375\"[3-195]TGMP synthase/anthranilate synthase component II
PTHR11922\"[3-184]TGMP SYNTHASE-RELATED


","BeTs to 22 clades of COG0512COG name: Anthranilate/para-aminobenzoate synthases component IIFunctional Class: E,HThe phylogenetic pattern of COG0512 is aompkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 8e-12) to 2/2 blocks of the IPB000991 family, which is described as \"Glutamine amidotransferase class-I\". Interpro entry for IP:IPR000991. IPB000991A 79-88 5.2e-06 IPB000991B 164-174 0.00053Significant hit ( 2.3e-08) to 3/10 blocks of the IPB001674 family, which is described as \"GMP synthase C terminal domain\". Interpro entry for IP:IPR001674. IPB001674A 4-30 1.1e+02 IPB001674B 79-88 0.0023 IPB001674D 165-186 0.024","Residues 4 to 61 match (2e-10) PD:PD002064 which is described as SYNTHASE ANTHRANILATE GLUTAMINE PROTEOME COMPLETE AMIDOTRANSFERASE COMPONENT II LYASE BIOSYNTHESIS ","","","","","","","","","","","Mon Jan 13 18:18:20 2003","Mon Jan 13 18:18:20 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02175 is paralogously related to AA01611 (7e-22) and AA01913 (2e-04).","","","","","","Residues 5 to 189 (E-value = 3.2e-73) place AA02175 in the GATase family which is described as Glutamine amidotransferase class-I (PF00117)","","","","","Yanofsky,C., Platt,T., Crawford,I.P., Nichols,B.P., Christie,G.E., Horowitz,H., VanCleemput,M. and Wu,A.M. The complete nucleotide sequence of the tryptophan operon of Escherichia coli. Nucleic Acids Res. 9 (24): 6647-6668 (1981) [PubMed: 7038627].Horowitz,H., Christie,G.E. and Platt,T. Nucleotide sequence of the trpD gene, encoding anthranilate synthetase component II of Escherichia coli. J. Mol. Biol. 156 (2): 245-256 (1982) [PubMed: 6283099].Li,S.L., Hanlon,J. and Yanofsky,C. Structural homology of the glutamine amidotransferase subunits of the anthranilate synthetases of Escherichia coli, Salmonellatyphimurium and Serratia marcescens. Nature 248 (443): 48-50 (1974) [PubMed: 4594441].","","Mon Jan 13 18:18:20 2003","1","","","" "AA02177","1489103","1489492","390","ATGATCACAGTATATGGCTTAAAACGCACCCTTTCCCCGCGCAAATCCGCCGTGGCGGAAGTGATTTATAACTGCCTGGAACTCGGTTTAGATGTGGCAAAAGGCAAGCACGCACTCCGTTTTATTTGCTTGGAAGATGATGATTTTTACTATCCGCACACCGCCAACCGTAGCGATAACTACATGGTGATTGAAATCAATTTAATGCAAGGACGCCTGGAGCAAACCAAAAAGCGCCTGATAAAAATGCTGTTCAGCGAATTTGAATATAAATTAGGTATCAGCCCGTTTGACGTGGAAATCACTATCAAGGAGCAACCCGCACATTGCTGGGGCTTCCGTGGCATGACCGGCGATGAAGCGCGTGATTTGGATTACGATATTAATAAA","","","15100","MITVYGLKRTLSPRKSAVAEVIYNCLELGLDVAKGKHALRFICLEDDDFYYPHTANRSDNYMVIEINLMQGRLEQTKKRLIKMLFSEFEYKLGISPFDVEITIKEQPAHCWGFRGMTGDEARDLDYDINK","1489492","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR014347
Domain
Tautomerase
G3DSA:3.30.429.10\"[1-130]Tno description


","No hits to the COGs database.","","Residues 2 to 128 match (7e-52) PD:PD174893 which is described as PROTEOME COMPLETE HI1388.1 ALR4568 ","","","","","","","","","","","","Mon Jan 13 18:19:56 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02177 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02179","1489507","1490505","999","ATGGAAAGCCAAGCCCTGTTAGAAAAACTGTATGGCGGACACGCCTTAACCGCAGCGGAAAGTGAAATTCTATTTAACGCCATTATGTCGGGCGCGTTAAGCAACGAACAAATCGCCGCCATGTTAATTGCCTTAAAAGTACGCGGCGAAACCATTGATGAGGTGAACGGCGCCGTGTTAGCCGCGGTAAAAAACGCCAAGCTGTTCCCTACACCCGCCTACCCTTTTGCCGACATCGTAGGTACGGGCGGTGACGGAGCCAACACCATTAACATTTCCACCGCATCCGCCATTGTCGCGGCAAGTTGCGGCGCGAAAGTGGCAAAACACGGCAACCGCAGCGTTTCCGGCAAAACCGGTTCAAGCGATTTATTAACCGCACTTGGTGTCAACATCGCCATGTCACCGGAACAAGCCCGCAAAGCATTGGACGACATCGGCATCTGTTTTTTATTCGCCCAACAATATCACCCGGGCTTCAAATACGTAGTTCCCGTGCGCCAAGCCTTAAAAACCCGTACGCTATTTAATATCCTCGGTCCGCTGATTAATCCCGCCCGCCCGAAACGCCAGCTACTCGGCGTGTATTCCCCCGAACTCATTGACGTTTATGCCAAAACCGTCGCCCAATTAGGACATGAACACACCATTATCGTACATGGCAGCGGTTTGGACGAAGTGGCAATCCACGGCATCACACAAGTGGCAGAAGTGCGCAACGGCAATATCGAACGTTACACCCTAACGCCGCAGGATTTCGGCTTCCAAGCAAAACCTTTAGAGACTTTGCGCGGTGGCGAACCGGCTGAAAATGCACAAATGATCACCGCACTGTTACAAGGCAACGGCAAAGCGGAACACAACCAAGCCGTCGCCATGAACACCGCCTTATTGCTAAAACTGTTCGGACAAGATGACCTTAAACACAATGCACAACAGGTGTTAGATGTCATTGCTCAAGGTAAACCGTTTGAAACGTTGCAGAAATTGACGGCGTAT","","","35402","MESQALLEKLYGGHALTAAESEILFNAIMSGALSNEQIAAMLIALKVRGETIDEVNGAVLAAVKNAKLFPTPAYPFADIVGTGGDGANTINISTASAIVAASCGAKVAKHGNRSVSGKTGSSDLLTALGVNIAMSPEQARKALDDIGICFLFAQQYHPGFKYVVPVRQALKTRTLFNILGPLINPARPKRQLLGVYSPELIDVYAKTVAQLGHEHTIIVHGSGLDEVAIHGITQVAEVRNGNIERYTLTPQDFGFQAKPLETLRGGEPAENAQMITALLQGNGKAEHNQAVAMNTALLLKLFGQDDLKHNAQQVLDVIAQGKPFETLQKLTAY","1490505","[PATHWAY] Tryptophan biosynthesis; first step.[PATHWAY] Tryptophan biosynthesis; second step.","anthanilate phosphoribosyltransferase","Cytoplasm","","
InterPro
IPR000312
Domain
Glycosyl transferase, family 3
PD001864\"[74-312]TTRPD_PASMU_P57856;
G3DSA:1.20.970.10\"[1-67]Tno description
G3DSA:3.40.1030.10\"[71-333]Tno description
PF00591\"[73-324]TGlycos_transf_3
PF02885\"[2-67]TGlycos_trans_3N
InterPro
IPR005940
Domain
Anthranilate phosphoribosyl transferase
TIGR01245\"[7-333]TtrpD: anthranilate phosphoribosyltransferas
noIPR
unintegrated
unintegrated
PTHR11922\"[1-263]TGMP SYNTHASE-RELATED


","BeTs to 22 clades of COG0547COG name: Anthranilate phosphoribosyltransferaseFunctional Class: EThe phylogenetic pattern of COG0547 is aompkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-57) to 2/2 blocks of the IPB000312 family, which is described as \"Glycosyl transferase family\". Interpro entry for IP:IPR000312. IPB000312A 84-130 1.2e-30 IPB000312B 153-195 7.1e-26Significant hit ( 1.4e-07) to 4/8 blocks of the IPB000053 family, which is described as \"Thymidine/pyrimidine-nucleoside phosphorylase\". Interpro entry for IP:IPR000053. IPB000053A 6-34 3.2 IPB000053B 37-67 0.06 IPB000053D 98-128 1.2 IPB000053G 262-282 1.4e+02","Residues 16 to 61 match (5e-07) PD:PD571708 which is described as TRANSFERASE ANTHRANILATE GLYCOSYLTRANSFERASE PHOSPHORIBOSYLTRANSFERASE COMPLETE PROTEOME TRYPTOPHAN BIOSYNTHESIS GLUTAMINE COMPONENT ","","","","","","","","","","","Mon Jan 13 18:23:31 2003","Mon Jan 13 18:23:31 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02179 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 73 to 324 (E-value = 8.3e-137) place AA02179 in the Glycos_transf_3 family which is described as Glycosyl transferase family, a/b domain (PF00591)","","","","","Yanofsky,C., Platt,T., Crawford,I.P., Nichols,B.P., Christie,G.E., Horowitz,H., VanCleemput,M. and Wu,A.M. The complete nucleotide sequence of the tryptophan operon of Escherichia coli. Nucleic Acids Res. 9 (24): 6647-6668 (1981) [PubMed: 7038627]. Horowitz,H., Christie,G.E. and Platt,T. Nucleotide sequence the trpD gene, encoding anthranilate synthetase component II of Escherichia coli. J. Mol. Biol. 156 (2): 245-256 (1982) [PubMed: 6283099].Li,S.L., Hanlon,J. and Yanofsky,C. Structural homology of the glutamine amidotransferase subunits of the anthranilate synthetases of Escherichia coli, Salmonella typhimurium and Serratia marcescens. Nature 248 (443): 48-50 (1974) [PubMed: 4594441].","","Mon Jan 13 18:23:31 2003","1","","","" "AA02180","1490603","1490878","276","ATGATTTTATCTTTCAAACATAAGGGACTTGAACAATTTTTTAAAACCGGTTCGACCGCAGGAATTCAAGCCAAACACGCCAAGAAATTAAATCTGCAATTGGCCACATTAAATAATGCGGAAACGCCTCTTGCTATGAGTGTTCCCAGCTGGAATTTGCACAAACTTAAAGGTGATTTGCAAGAGCATTGGGCAGTTACCGTAAACGGAAATTGGCGCTTAACATTTAAATTTGAAAATGGTCATGCTGAAGTTGTTGATTATCAGGATTATCAT","","","10474","MILSFKHKGLEQFFKTGSTAGIQAKHAKKLNLQLATLNNAETPLAMSVPSWNLHKLKGDLQEHWAVTVNGNWRLTFKFENGHAEVVDYQDYH","1490878","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR007711
Family
Plasmid maintenance system killer
PF05015\"[1-92]TPlasmid_killer


","BeTs to 3 clades of COG3549COG name: Plasmid maintenance system killer proteinFunctional Class: NThe phylogenetic pattern of COG3549 is ----------------ghs--j----Number of proteins in this genome belonging to this COG is","","Residues 1 to 92 match (2e-24) PD:PD029323 which is described as PROTEOME COMPLETE KILLER PROTEIC R01051 R03059 PLASMID PROTEIN REPEAT ALL2924 ","","","","","","","","","","","","Mon Jan 13 18:25:43 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02180 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 92 (E-value = 1.6e-41) place AA02180 in the Plasmid_killer family which is described as Plasmid maintenance system killer protein (PF05015)","","","","","","","","1","","","" "AA02181","1490891","1491166","276","ATGAGAATGCACAATCCTCCACACCCGGGAGAACTGTTAAAAGAATATATTGATGGCGTGAGTGTCACGAAGGTTGCCCAAAAATTAGGTGTTTCGCGTGTTACGCTTTCCCGCATTCTTAATGGGAAAGCAAGTATAACGCCTGAAATGGCTGTGCGATTAAGCGAATTATTGAATACCACAACACCGAAATTATGGCTGGGTATGCAAGCAGACTACGATTTATGGCAAATTGAACAACAACACGCCGTATTCAACATCCAACCATTATTTAAT","","","10409","MRMHNPPHPGELLKEYIDGVSVTKVAQKLGVSRVTLSRILNGKASITPEMAVRLSELLNTTTPKLWLGMQADYDLWQIEQQHAVFNIQPLFN","1491166","","possible proteic killer active protein","Cytoplasm","","
InterPro
IPR001387
Domain
Helix-turn-helix type 3
PF01381\"[13-65]THTH_3
SM00530\"[12-65]THTH_XRE
PS50943\"[13-65]THTH_CROC1
InterPro
IPR013430
Family
Addiction module antidote protein, HigA
TIGR02607\"[3-81]Tantidote_HigA: addiction module antidote pr
noIPR
unintegrated
unintegrated
G3DSA:1.10.260.40\"[10-81]Tno description


","BeTs to 5 clades of COG3093COG name: Plasmid maintenance system antidote proteinFunctional Class: NThe phylogenetic pattern of COG3093 is --------------efghs--j----Number of proteins in this genome belonging to this COG is","Significant hit ( 3.7e-05) to 1/4 blocks of the IPB001822 family, which is described as \"Site-specific recombinase\". Interpro entry for IP:IPR001822. IPB001822D 19-38 3.9e-05","Residues 21 to 89 match (2e-07) PD:PD477940 which is described as ORF PLASMID ","","","","","","","","","","","","Mon Jan 13 18:31:13 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02181 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 13 to 65 (E-value = 8.8e-12) place AA02181 in the HTH_3 family which is described as Helix-turn-helix (PF01381)","","","","","Katz,M.E., Strugnell,R.A. and Rood,J.I. Molecular characterization of a genomic region associated with virulence in Dichelobacter nodosus. Infect. Immun. 60 (11): 4586-4592 (1992) PubMed: .Tian QB, Ohnishi M, Murata T, Nakayama K, Terawaki Y, Hayashi T. Specific protein-DNA and protein-protein interaction in the hig gene system, a plasmid-borne proteic killer gene system of plasmidRts1.Plasmid. 2001 Mar;45(2):63-74.PMID: 11322821 Tian QB, Hayashi T, Murata T, Terawaki Y.Gene product identification and promoter analysis of hig locus of plasmid Rts1.Biochem Biophys Res Commun. 1996 Aug 14;225(2):679-84.PMID: 8753818 Tian QB, Ohnishi M, Tabuchi A, Terawaki Y.A new plasmid-encoded proteic killer gene system: cloning, sequencing, and analyzing hig locus of plasmid Rts1.Biochem Biophys Res Commun. 1996 Mar 18;220(2):280-4.PMID: 8645296 ","","Tue Jan 28 13:27:50 2003","1","","","" "AA02182","1491178","1491927","750","ATGATCACACAAGACTTCTCCAAACCACTCGAAGCTGCGACGGTGCTACAAAAAATCGTTCTCGACAAAGCTCAATGGGTGAAAGCCAAAGCGGCGGAATTTCCGTTGAGTGCCGAAAAAAACATCGAAAAATCCGACCGCACTTTTTATGGTGCGTTGGCGCAAGGTTCGCATGAAAAGCCGGCATATATTCTGGAATGTAAAAAAGCCTCGCCTTCCAAAGGATTGATTCGCAGTGAATTTAAACCGACAGAGATTGCACAGGTGTATAAAAATTACGCGAGCGTGATTTCCGTGCTAACCGATGAAAAATATTTCCAAGGGGATTTTGCCTATATTCAGCAAGTTCGCGACGTTGTCACGCAACCGGTGTTGTGCAAAGACTTTATAATCAACGAATATCAGGTTTATTTGGCACGTTTTCATCAAGCCGACGCCATTTTACTGATGCTTTCCGTGGTGAACGACGAAACCTATCGCATTTTGGCGGATTTGGCCCATTCCCTCGGCATGGGCGTGCTGACCGAAACCAGCAACGAGGAAGAATTTGAACGCGCCTTGGCGTTAGGCGCAAAAATTATCGGCGTGAACAATCGTAACCTGCATGATTTAACGGTAGATTTAAATCGCGTGGTGGAACTCACCGCCAAATATGCGGATAAAATCCCTGAGGATGTGCGAATCATCAGCGAATCGGGCATCTATAATCATCAACAAGTGCGTGAATTACAACACGTTGCCCATGGCTTT","","","28207","MITQDFSKPLEAATVLQKIVLDKAQWVKAKAAEFPLSAEKNIEKSDRTFYGALAQGSHEKPAYILECKKASPSKGLIRSEFKPTEIAQVYKNYASVISVLTDEKYFQGDFAYIQQVRDVVTQPVLCKDFIINEYQVYLARFHQADAILLMLSVVNDETYRILADLAHSLGMGVLTETSNEEEFERALALGAKIIGVNNRNLHDLTVDLNRVVELTAKYADKIPEDVRIISESGIYNHQQVRELQHVAHGF","1491927","From Genbank: [gi:1174787]The product of this gene is a bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the trpF domain; the second reaction is catalyzed by the synthase, coded by the trpC domain.","tryptophan biosynthesis protein trpCF","Cytoplasm","Its nearest neighbor in the NR database is gi:1174787 from Haemophilus influenzae.","
InterPro
IPR001468
Domain
Indole-3-glycerol phosphate synthase, central region
PD001511\"[46-207]TTRPC_HAEIN_P46451;
PS00614\"[63-81]TIGPS
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[12-250]Tno description
InterPro
IPR013798
Domain
Indole-3-glycerol phosphate synthase
PF00218\"[15-250]TIGPS
noIPR
unintegrated
unintegrated
PTHR22854\"[36-244]TTRYPTOPHAN BIOSYNTHESIS PROTEIN
PTHR22854:SF2\"[36-244]TINDOLE-3-GLYCEROL PHOSPHATE SYNTHASE


","No hits to the COGs database.","Significant hit ( 2e-48) to 4/5 blocks of the IPB001468 family, which is described as \"Indole-3-glycerol phosphate synthase\". Interpro entry for IP:IPR001468. IPB001468A 64-75 4.2e-07 IPB001468B 97-108 2.1e-08 IPB001468C 123-154 2.8e-20 IPB001468D 193-206 4e-08","Residues 47 to 81 match (5e-08) PD:PD590082 which is described as SYNTHASE PHOSPHATE INDOLE-3-GLYCEROL BIOSYNTHESIS LYASE TRYPTOPHAN PROTEOME IGPS COMPLETE DECARBOXYLASE ","","","","","","","","","","","Fri May 20 08:40:52 2005","Fri May 20 08:40:52 2005","Fri May 20 08:40:52 2005","Fri May 20 08:40:52 2005","Fri May 20 08:40:52 2005","Fri May 20 08:40:52 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA02182 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Fri May 20 08:40:52 2005","","","","","Residues 15 to 250 (E-value = 4.1e-117) place AA02182 in the IGPS family which is described as Indole-3-glycerol phosphate synthase (PF00218)","Fri May 20 08:40:52 2005","","","","Christie,G.E. and Platt,T. Gene structure in the tryptophan operon of Escherichia coli. Nucleotide sequence of trpC and the flanking intercistronic regions. J. Mol. Biol. 142 (4): 519-530 (1980) [PubMed: 7007653].Horowitz,H., Van Arsdell,J. and Platt,T. Nucleotide sequence of the trpD and trpC genes of Salmonella typhimurium. J. Mol. Biol. 169 (4): 775-797 (1983) [PubMed: 6355484].Wilmanns,M., Priestle,J.P., Niermann,T. and Jansonius,J.N. Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphatesynthase from Escherichia coli refined at 2.0 A resolution. J. Mol. Biol. 223 (2): 477-507 (1992) [PubMed: 1738159].Wilmanns,M., Schlagenhauf,E., Fol,B. and Jansonius,J.N. Crystallization and structure solution at 4 A resolution of the recombinant synthase domain of N-(5'-phosphoribosyl)anthranilateisomerase:indole-3-glycerol-phos hate synthase from Escherichiacoli complexed to a substrate analogue. Protein Eng. 3 (3): 173-180 (1990) [PubMed: 2184433].","","Fri May 20 08:40:52 2005","1","","","" "AA02184","1491945","1492601","657","ATGGGCAGCGCGGATTTAAATAACACCGTGCGCGAAGTGATTTTCGGTGAAAACAAAGTGTGTGGCTTAACCCGTGCGCAGGATGTGAAAACTGCTTACGACAACGGCGCTTTATACGGTGGGCTAATTTTCGCCGAACAGTCTAAACGCTGCGTCAGTTTACGTCAGGCGCAGGAATTGGTGACCGCCGCCCCACTGCGTTTTGTGGGCGTGTTCCAAAATCAGAACATTGATTTTATTGTGAAAATCGCCCAACAGCTACAACTCCACGCCGTTCAGCTACACGGTGACGAAACGCCGGCATTTATCACCGCACTTCGTGCTCAATTGCCGCAACATATTCGTATTTGGAAAGCCATTTCTGTAGATGTGAAGCATAAAAGTGCGGTTAATTTTGACGACGTTTCTGAGGTGGATCGTTTTGTTTTCGACAGCAAATCAGGTACACAACAAGGCGGCACGGGGGCGACTTTTGATTGGTCACTGATTCCGCAGGAATTGAAATATAAAATTATTCTGGCGGGCGGCATTAGCCCGAGTAATATTGAAGACGCATTGGCACAACATTGTGTGGGTGTTGATCTCAATTCCGGCGTAGAAAGCGCCCCGGGCGTGAAAAATGCCGAAAAAGTGCGGTCGGTTTTTGCGAAGATTTTG","","","23821","MGSADLNNTVREVIFGENKVCGLTRAQDVKTAYDNGALYGGLIFAEQSKRCVSLRQAQELVTAAPLRFVGVFQNQNIDFIVKIAQQLQLHAVQLHGDETPAFITALRAQLPQHIRIWKAISVDVKHKSAVNFDDVSEVDRFVFDSKSGTQQGGTGATFDWSLIPQELKYKIILAGGISPSNIEDALAQHCVGVDLNSGVESAPGVKNAEKVRSVFAKIL","1492601","[FUNCTION] Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the trpF domain; the second reaction is catalyzed by the synthase, coded by the trpC domain. [PATHWAY] Tryptophan biosynthesis; third step. [PATHWAY] Tryptophan biosynthesis; fourth step.","anthranilate isomerase; indole-3-glycerol phosphate synthase; phosphoribosylanthranilate isomerase","Cytoplasm","","
InterPro
IPR001240
Domain
N-(5'phosphoribosyl)anthranilate isomerase (PRAI)
PF00697\"[18-217]TPRAI
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[17-219]Tno description
noIPR
unintegrated
unintegrated
PTHR22854\"[1-219]TTRYPTOPHAN BIOSYNTHESIS PROTEIN
PTHR22854:SF5\"[1-219]TTRYPTOPHAN BIOSYNTHESIS PROTEIN TRPCF


","No hits to the COGs database.","","Residues 19 to 65 match (7e-17) PD:PD089350 which is described as ISOMERASE TRYPTOPHAN BIOSYNTHESIS PRAI N-5'-PHOSPHORIBOSYLANTHRANILATE SYNTHASE COMPLETE PROTEOME PHOSPHATE INDOLE-3-GLYCEROL ","","","","","","","","","","","Wed Jan 15 13:15:30 2003","Wed Jan 15 13:15:30 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02184 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 18 to 217 (E-value = 5.1e-87) place AA02184 in the PRAI family which is described as N-(5'phosphoribosyl)anthranilate (PRA) isomerase (PF00697)","","","","","Christie,G.E. and Platt,T. Gene structure in the tryptophan operon of Escherichia coli. Nucleotide sequence of trpC and the flanking intercistronic regions. J. Mol. Biol. 142 (4): 519-530 (1980) [PubMed: 7007653].Horowitz,H., Van Arsdell,J. and Platt,T. Nucleotide sequence of the trpD and trpC genes of Salmonella typhimurium. J. Mol. Biol. 169 (4): 775-797 (1983) [PubMed: 6355484].Wilmanns,M., Priestle,J.P., Niermann,T. and Jansonius,J.N. Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphatesynthase from Escherichia coli refined at 2.0 A resolution. J. Mol. Biol. 223 (2): 477-507 (1992) [PubMed: 1738159].Wilmanns,M., Schlagenhauf,E., Fol,B. and Jansonius,J.N. Crystallization and structure solution at 4 A resolution of the recombinant synthase domain of N-(5'-phosphoribosyl)anthranilateisomerase:indole-3-glycerol-phos hate synthase from Escherichiacoli complexed to a substrate analogue. Protein Eng. 3 (3): 173-180 (1990) [PubMed: 2184433]. ","","Wed Jan 15 13:15:30 2003","1","","","" "AA02187","1492743","1492907","165","ATGTTTTGGTTGTACATCTTTAAGGTTCTGCTATTCTTTAATTTTATTAATATTGATAAACAACCATATACCGACACGAAAAAACACCACAAAAAAACCACCGCACTTTTTACCCCGCTTACCAGTGTTGAAGCCCCCCCCTGCATTCTCCTATCGACCCGAATT","","","6514","MFWLYIFKVLLFFNFINIDKQPYTDTKKHHKKTTALFTPLTSVEAPPCILLSTRI","1492907","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:16:56 2004","Wed Feb 25 15:16:56 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02187 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:16:56 2004","","","","","","","","","","","","","1","","","" "AA02188","1492925","1493026","102","GTGCAGCTCACGCAGGATTGCCTGCGCATGATTTTATCTATGCCAACAAAACAACCGAAATTTGATCCGGATCGCCGAAACCTGTTTAACGCCATGATAAAA","","","4032","VQLTQDCLRMILSMPTKQPKFDPDRRNLFNAMIK","1493026","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:15:36 2004","Wed Feb 25 15:15:36 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02188 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:15:36 2004","","","","","","","","","","","","","1","","","" "AA02190","1493059","1493331","273","ATGTGTTTAGGTGTGCCGGGACAAATCGTTAAAATCGGCGATAGCGCGTTACAACTCGCCACCGTGGACGTGTGTGGCGTTCAACGCGACATCAATATTTCATTAATCTGCAACGACGACCCCAAACTGCTCCTTGGCAAATGGGTCCTCGTCCACGTTGGCTTCGCCATGAGCATCATCGACGAAGAAGAAGCCAAACAAACCCAAGAAGCTTTGATCGCCATGAGTCAGTTGGAACATGAAGTGGGCGATTTTTTGGGGTTGAATCAGGGG","","","9787","MCLGVPGQIVKIGDSALQLATVDVCGVQRDINISLICNDDPKLLLGKWVLVHVGFAMSIIDEEEAKQTQEALIAMSQLEHEVGDFLGLNQG","1493331","[FUNCTION] May have a specific role in the maturation of the large subunits of hyd1 and hyd2. Is required for the formation of all three hydrogenase isoenzymes. May bind to the precursor form of the large subunit of dehydrogenases to keep them in a conformation accessible for metal incorporation. ","hydrogenase-2 component protein","Cytoplasm","","
InterPro
IPR001109
Family
Hydrogenase expression/formation protein (HUPF/HYPC)
PD003112\"[1-77]TYFRC_PROVU_P20927;
PR00445\"[2-9]T\"[20-36]T\"[45-61]T\"[63-75]THUPFHYPC
PIRSF005618\"[1-91]T[NiFe]-hydrogenase maturation chaperone
PF01455\"[1-82]THupF_HypC
TIGR00074\"[1-86]ThypC_hupF: hydrogenase assembly chaperone H
PS01097\"[1-9]THUPF_HYPC


","No hits to the COGs database.","Significant hit ( 5.3e-33) to 3/3 blocks of the IPB001109 family, which is described as \"Hydrogenase expression/formation protein (HUPF/HYPC)\". Interpro entry for IP:IPR001109. IPB001109A 1-12 1.5e-05 IPB001109B 20-36 4.2e-06 IPB001109C 46-72 3.4e-18","Residues 1 to 75 match (8e-21) PD:PD003112 which is described as HYDROGENASE EXPRESSION/FORMATION HYPC PROTEOME COMPLETE HUPF HYDROGENASE-2 OPERON ISOENZYMES FORMATION ","","","","","","","","","","","Wed Jan 15 13:23:28 2003","Wed Jan 15 13:23:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02190 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 82 (E-value = 3.7e-33) place AA02190 in the HupF_HypC family which is described as HupF/HypC family (PF01455)","","","","","Cole,S.T. Nucleotide sequence and comparative analysis of the frd operon encoding the fumarate reductase of Proteus vulgaris. Extensivesequence divergence of the membrane anchors and absence of anfrd-linked ampC cephalosporinase gene. Eur. J. Biochem. 167 (3): 481-488 (1987) [PubMed: 3308458].Menon,N.K., Chatelus,C.Y., Dervartanian,M., Wendt,J.C., Shanmugam,K.T., Peck,H.D. Jr. and Przybyla,A.E. Cloning, sequencing, and mutational analysis of the hyb operon encoding Escherichia coli hydrogenase 2. J. Bacteriol. 176 (14): 4416-4423 (1994) [PubMed: 8021226].Lutz,S., Jacobi,A., Schlensog,V., Bohm,R., Sawers,G. and Bock,A. Molecular characterization of an operon (hyp) necessary for the activity of the three hydrogenase isoenzymes in Escherichia coli. Mol. Microbiol. 5 (1): 123-135 (1991) [PubMed: 1849603]. Drapal,N. and Bock,A. Interaction of the hydrogenase accessory protein HypC with HycE, the large subunit of Escherichia coli hydrogenase 3 during enzymematuration. Biochemistry 37 (9): 2941-2948 (1998) [PubMed: 9485446].","","Wed Jan 15 13:23:28 2003","1","","","" "AA02191","1493832","1493458","375","ATGGCAACGAAAAATACACAGGTTAAAGCAAAAAATTCTGTAGGGAATGAAATTAGCTTATCTCATAGCCAAACAGATAGTCCTATTCTTGATGTAAATTCTCTTGAACGCTTAAATACATTTCGACCTGATTTGGTTGATTTTGTTATTAAAGAAACTGGAGAAGAAGCTAAAAATCGCCGTAGACGTGAAGTTAAAATTGATTGGTTTACTTTTATTGAAAGAATGGGGGCGTTGCTTCTTGCAGCAGGTATAGCAACAGGTGGTATATTCGGTTCCATTTATGCTGCTGCAAATGGATATGAAAAGCTTTCTTGGATCATTGCGAGTACGTGTATTGGTTCATTGGCGATCGCTTTTCTAAAAAGAAATAGA","","","13803","MATKNTQVKAKNSVGNEISLSHSQTDSPILDVNSLERLNTFRPDLVDFVIKETGEEAKNRRRREVKIDWFTFIERMGALLLAAGIATGGIFGSIYAAANGYEKLSWIIASTCIGSLAIAFLKRNR","1493458","","hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
tmhmm\"[77-95]?\"[101-121]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Jan 15 13:38:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02191 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02193","1494359","1494622","264","ATGACTTCGGCAGAACTTTTCGGTGAAGGAATTAATCTGATGTTTTCAGGGATGGGTTTTGTGTTGGTCTTTTTGCTCATTTTGATTTGGGCAATCGGGCTGATGTCGAAACTTATCAATAAATATTTTCCCGAGCCTCAACCCTCGCCAAAAACTCCGCTAAATCCCACCGCACTTTCTGCGGCTTCCAGTGACGATTTTGAGCGTTTGCGCCCTGTGATTACAGCGGCTATCGCGCACCATCGCCGTACCCAACAGTTCAAA","","","10459","MTSAELFGEGINLMFSGMGFVLVFLLILIWAIGLMSKLINKYFPEPQPSPKTPLNPTALSAASSDDFERLRPVITAAIAHHRRTQQFK","1494622","[FUNCTION] Lyase and sodium transporter (by similarity). ","oxaloacetate decarboxylase gamma chain","Inner membrane, Cytoplasm","","
InterPro
IPR005899
Family
Sodium pump decarboxylase, gamma subunit
PF04277\"[7-84]TOAD_gamma
TIGR01195\"[3-86]ToadG_fam: sodium pump decarboxylases, gamma
noIPR
unintegrated
unintegrated
signalp\"[1-36]?signal-peptide
tmhmm\"[14-34]?transmembrane_regions


","BeTs to 3 clades of COG3630COG name: Na+-transporting methylmalonyl-CoA/oxaloacetate decarboxylase, gamma subunitFunctional Class: CThe phylogenetic pattern of COG3630 is a---k-----------gh------t-Number of proteins in this genome belonging to this COG is","","Residues 1 to 86 match (3e-07) PD:PD298208 which is described as DECARBOXYLASE PROBABLE PROTEOME TRANSMEMBRANE SODIUM CHAIN COMPLETE GAMMA OXALOACETATE LYASE ","","","","","","","","","","","Wed Jan 15 13:55:06 2003","Wed Jan 15 13:55:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02193 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 6 to 86 (E-value = 1.6e-29) place AA02193 in the OAD_gamma family which is described as Oxaloacetate decarboxylase, gamma chain (PF04277)","","","","","Laussermair,E., Schwarz,E., Oesterhelt,D., Reinke,H., Beyreuther,K. and Dimroth,P. The sodium ion translocating oxaloacetate decarboxylase of Klebsiella pneumoniae. Sequence of the integral membrane-bound subunits beta and gamma. J. Biol. Chem. 264 (25): 14710-14715 (1989) [PubMed: 2549031].van der Rest,M.E., Siewe,R.M., Abee,T., Schwarz,E., Oesterhelt,D. and Konings,W.N. Nucleotide sequence and functional properties of a sodium-dependent citrate transport system from Klebsiella pneumoniae. J. Biol. Chem. 267 (13): 8971-8976 (1992) [PubMed: 1577734].","","Wed Jan 15 13:55:06 2003","1","","","" "AA02195","1494641","1496434","1794","ATGACTAAAAAAATTAAAGTGACCGAACTGGTGCTTCGTGATGCCCACCAATCGCTTTTTGCAACCCGTTTGCGTCTTGATGACATGTTGCCGATTGCCCATGAACTGGACGACATCGGTTATTGGTCGCTGGAAGCTTGGGGCGGTGCGACATTTGACAGCTGTATTCGTTTTTTGGGTGAAGATCCGTGGGTGCGTTTGCGTGAGTTGAAAAAAGCCTGCCCGAAAACCCCGCTACAAATGCTGTTGCGCGGTCAAAATCTGCTGGGTTATCGCCACTATGCCGATGACGTGGTGGAGCGTTTTGTGGAACGCTGCGTGGCGAACGGTATGGATGTGTTCCGTGTGTTCGATGCCCTTAATGACCCGCGTAATATGAAAGCGGCGTTGCAAGCGGTGCGTAAATTCGGCGGCCATGCGCAAGGGACGTTAAGTTACACCACCAGCCCCGTTCACACCATGCAAACCTGGCTCGACACCACCGAACAATTGCTTGAAATCGGGATCGACAGCCTCGTGATTAAAGATATGTCGGGCATTTTGAATCCGATGGCGGCGGCAGAACTAGTACGCGAAATCAAAAAACGTTTCGACGTGGAATTGCATTTACACTGCCACTCCACCACCGGCATGGCGGAAATGGCCCTGTTAAAAGCCATTGAAGCGGGTGTGGACGGTGTGGATACAGCGATTTCCTCCATGTCCGCCACCTACGGTCACCCTGCTACAGAATCCATCGTGGCGACCTTGCAAGGCACTGAATACGACACCGGCTTGGATATTCCACGCCTGGAAAAAATCGCAGCGTATTTTCGCAATGTACGTAAAAAATATGCAAAATTTGAAGGTCAGCTTCGCGGCGTGGACAGCCGAATTTTGGTGGCGCAAGTGCCGGGCGGTATGCTCACCAACCTGGAAAACCAATTAAAACAACAAAACGCCTCCGACAAATTGGATCTGGTGTTGGAAGAAATTCCGCGTGTACGCAAAGATTTGGGTTACATTCCGTTGGTGACTCCGACATCACAAATCGTCGGTACCCAATCCGTAATTAATGTGCTCACAGACGAACGCTACAAAACCATCGCCAAAGAAACCGCCGGTATCTTAAAAGGCGAATACGGCAAAACACCGGCGCCGGTGGATAGCGCGCTACAAGCCCGCGTATTGGAAGGCGCTGCGCCGATGACCGACCGCCCTGCCGATCACATTGCCCCTGAAATGGCAAAAATTGAAGCGGAAGTCGCCGAACAAGCCAAAGCGAAAGGGGTGAAATTGTCCGAAAATGCCGTAGATGATGCCTTAATCGTCGCCCTTTTCCCGCAAATCGCGTGGAAATTCCTGGAAAATCGCAACAATCCTGCCGCCTTTGAACCGGCACCGACGAGTAATGAAAGTGCGGTCGAAAATAAACCTGTTTCGAAAGCCGCACCGGCGGCATCAGGATCTGCCGTTTACACCGTGGAATTGGAAGGCAAAGCCTTTGTGGTGAAAGTGAGCGAAGGCGGTGACATTTCTCATATGGCAACTACCACACCACAAGCAGCGCCGCAAGCCGCACCGGCACCTGCGCCAACCAGCGGCGGCACACCGGTCACTGCGCCGATGGCGGGTAACATCTGGAAAGTGGTGGCAACAGAAGGACAAACCGTTGTCGCAGGTGATGTGTTATTCATTCTTGAAGCAATGAAAATGGAAACCGAAATAAAGGCGGCGAAAGGCGGCACAGTGCGTGGCATTGTGGTGAAAGCCGGCGACGCCGTGGCGGTGGGTGATACCGTAATGACCCTCGTG","","","64598","MTKKIKVTELVLRDAHQSLFATRLRLDDMLPIAHELDDIGYWSLEAWGGATFDSCIRFLGEDPWVRLRELKKACPKTPLQMLLRGQNLLGYRHYADDVVERFVERCVANGMDVFRVFDALNDPRNMKAALQAVRKFGGHAQGTLSYTTSPVHTMQTWLDTTEQLLEIGIDSLVIKDMSGILNPMAAAELVREIKKRFDVELHLHCHSTTGMAEMALLKAIEAGVDGVDTAISSMSATYGHPATESIVATLQGTEYDTGLDIPRLEKIAAYFRNVRKKYAKFEGQLRGVDSRILVAQVPGGMLTNLENQLKQQNASDKLDLVLEEIPRVRKDLGYIPLVTPTSQIVGTQSVINVLTDERYKTIAKETAGILKGEYGKTPAPVDSALQARVLEGAAPMTDRPADHIAPEMAKIEAEVAEQAKAKGVKLSENAVDDALIVALFPQIAWKFLENRNNPAAFEPAPTSNESAVENKPVSKAAPAASGSAVYTVELEGKAFVVKVSEGGDISHMATTTPQAAPQAAPAPAPTSGGTPVTAPMAGNIWKVVATEGQTVVAGDVLFILEAMKMETEIKAAKGGTVRGIVVKAGDAVAVGDTVMTLV","1496434","","oxaloacetate decarboxylase alpha chain","Cytoplasm","","
InterPro
IPR000089
Domain
Biotin/lipoyl attachment
PF00364\"[530-597]TBiotin_lipoyl
PS50968\"[530-597]TBIOTINYL_LIPOYL
InterPro
IPR000891
Domain
Pyruvate carboxyltransferase
PF00682\"[13-277]THMGL-like
PS50991\"[5-265]TPYR_CT
InterPro
IPR001882
Binding_site
Biotin-binding site
PS00188\"[554-571]TBIOTIN
InterPro
IPR003379
Domain
Conserved carboxylase region
PF02436\"[292-503]TPYC_OADA
InterPro
IPR005776
Family
Oxaloacetate decarboxylase, alpha subunit
TIGR01108\"[7-594]ToadA: oxaloacetate decarboxylase alpha subu
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[3-275]Tno description
noIPR
unintegrated
unintegrated
G3DSA:2.40.50.100\"[522-597]Tno description
PTHR18866\"[1-598]TCARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE
PTHR18866:SF1\"[1-598]TPYRUVATE CARBOXYLASE


","BeTs to 4 clades of COG3632COG name: Na+-transporting oxaloacetate decarboxylase, alpha subunitFunctional Class: CThe phylogenetic pattern of COG3632 is --------v--l----gh------t-Number of proteins in this genome belonging to this COG is","Significant hit (2.6e-167) to 7/7 blocks of the IPB003379 family, which is described as \"Conserved carboxylase domain\". Interpro entry for IP:IPR003379. IPB003379A 7-29 1.7e-14 IPB003379B 42-70 6.4e-24 IPB003379C 71-97 9.5e-19 IPB003379D 98-133 1.5e-25 IPB003379E 153-196 4.6e-20 IPB003379F 197-242 3.1e-31 IPB003379G 285-329 3.7e-26Significant hit ( 1.5e-18) to 1/8 blocks of the IPB001882 family, which is described as \"Biotin-requiring enzymes attachment site.\". Interpro entry for IP:IPR001882. IPB001882H 535-580 1.5e-18Significant hit ( 1.9e-05) to 2/3 blocks of the IPB002215 family, which is described as \"HlyD family secretion protein\". Interpro entry for IP:IPR002215. IPB002215A 526-562 0.00057 IPB002215B 568-598 16","Residues 456 to 508 match (6e-07) PD:PD265830 which is described as BIOTIN PM1422 PROTEOME DECARBOXYLASE CHAIN COMPLETE OXALOACETATE ALPHA ","","","","","","","","","","","","Wed Jan 15 14:33:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02195 is paralogously related to AA00183 (4e-11) and AA01986 (6e-06).","","","","","","Residues 530 to 597 (E-value = 9.8e-23) place AA02195 in the Biotin_lipoyl family which is described as Biotin-requiring enzyme (PF00364)","","","","","Woehlke,G., Wifling,K. and Dimroth,P. Sequence of the sodium ion pump oxaloacetate decarboxylase from Salmonella typhimurium. J. Biol. Chem. 267(32):22798-22803,1992. PubMed: 1331067. Laussermair,E., Schwarz,E., Oesterhelt,D., Reinke,H., Beyreuther,K. and Dimroth,P. The sodium ion translocating oxaloacetate decarboxylase of Klebsiella pneumoniae. Sequence of the integral membrane-bound subunits beta and gamma. J. Biol. Chem. 264(25):14710-14715,1989. PubMed: 2549031. Bott,M., Pfister,K., Burda,P., Kalbermatter,O., Woehlke,G. and Dimroth,P. Methylmalonyl-CoA decarboxylase from Propionigenium modestum--cloning and sequencing of the structural genes and purification of the enzyme complex. Eur. J. Biochem. 250(2):590-599, 1997. PubMed: 9428714. Schmid M, Vorburger T, Pos KM, Dimroth P. Role of conserved residues within helices IV and VIII of the oxaloacetate decarboxylase beta subunit in the energy coupling mechanism of the Na+ pump. Eur J Biochem. 2002 Jun;269(12):2997-3004. PMID: 12071964 Schmid M, Wild MR, Dahinden P, Dimroth P. Subunit gamma of the oxaloacetate decarboxylase Na(+) pump: interaction with other subunits/domains of the complex and binding site for the Zn(2+) metal ion. Biochemistry. 2002 Jan 29;41(4):1285-92. PMID: 11802728 ","","Wed Jan 15 14:33:06 2003","1","","","" "AA02196","1496448","1497752","1305","ATGGATAGCATTATTATTGCATTAATTCAAGGCATGGGGATATTTCACCTGCAATGGGGGCAGGCGGTAATGATTGGTATCAGCCTGCTCCTGCTGTGGCTTGCCATTGCCCGCAAGTTTGAGCCGTTGCTGCTTTTGCCTATCGGTTTCGGCGGTTTGCTGTCAAACATTCCGGAAGCCGGGCTTGCCATGAGCGCATTGGAAAACCTGCTCCATCTGGGATCGCCGGAACAAATCGCCGTGATCGCCGCACAATTAGGCGTTGCGCCTGATCCGGCGATCATCAAAACAGCCATTGCTTCTGCGCCGACTTCCATGATTAACCAGCTGGAAACCTTGGCAGTGGATATGGGTTACAGCGCAGGCATTCTGGCGTTGTTCTATAAAGTCGCTATCGGCTACGGCATTGCGCCGCTGGTGATTTTCATGGGCGTGGGCGCCATGACGGATTTTGGTCCGTTACTGGCAAATCCGAAAACCCTACTCCTCGGTGCGGCGGCACAGTTCGGTATTTTCGCCACCGTGCTTGGCGCGTTAGGATTAAATTATTTCGGCATTATTGAATTTACGCTGCCGCAAGCCGCTTCCATCGGCATTATCGGCGGAGCGGACGGTCCGACGGCGATTTATCTCACCAGTAAACTCGCGCCGGAATTGCTCGGCGCCATTGCCGTCGCGGCGTATTCTTACATGGCGTTAGTGCCGTTGATCCAACCGCCGATCATGAAAGCCCTCACCACAGAAGAAGAACGCAAAATTCGCATGACGCAATTACGCCATGTGAGCAATCGGGAAAAAATCCTGTTTCCGGTGATTTTGCTGTTGCTTGTTGGCTTATTATTGCCGGATGCCGCGCCATTGCTCGGTATGTTCTGTTTCGGCAATCTGATGCGCGTGAGCGGCGTGGTAGAACGTTTAAGCGACACCACCCAAAACGCGTTAATTAACATCGTCACCATCGTGCTTGGCTTGTCCGTGGGTTCCAAACTCATTGCCGATAAATTCCTGCAACCGCAAACCCTGGGCATTTTAATTCTCGGCGTGGTTGCTTTCTGCATTGGTACAGGCAGCGGCGTGTTAATGGCGAAAACAATGAACAAATTCAGCAAAACCAAAATTAATCCGCTTATCGGCTCCGCCGGAGTGTCCGCCGTGCCAATGGCAGCGCGCGTCTCCAACAAGGTGGGATTGGAAGCGGATAACCAAAACTTCCTGCTCATGCACGCCATGGGTCCGAATGTTGCCGGTGTTATCGGCTCCGCCATTGCCGCCGGGGTGATGCTGAAATATGTGGGCGCAATGTTG","","","45338","MDSIIIALIQGMGIFHLQWGQAVMIGISLLLLWLAIARKFEPLLLLPIGFGGLLSNIPEAGLAMSALENLLHLGSPEQIAVIAAQLGVAPDPAIIKTAIASAPTSMINQLETLAVDMGYSAGILALFYKVAIGYGIAPLVIFMGVGAMTDFGPLLANPKTLLLGAAAQFGIFATVLGALGLNYFGIIEFTLPQAASIGIIGGADGPTAIYLTSKLAPELLGAIAVAAYSYMALVPLIQPPIMKALTTEEERKIRMTQLRHVSNREKILFPVILLLLVGLLLPDAAPLLGMFCFGNLMRVSGVVERLSDTTQNALINIVTIVLGLSVGSKLIADKFLQPQTLGILILGVVAFCIGTGSGVLMAKTMNKFSKTKINPLIGSAGVSAVPMAARVSNKVGLEADNQNFLLMHAMGPNVAGVIGSAIAAGVMLKYVGAML","1497752","[FUNCTION] Lyase and sodium transporter (by similarity). ","oxaloacetate decarboxylase beta chain","Inner membrane, Cytoplasm","","
InterPro
IPR005661
Family
Na+-transporting methylmalonyl-CoA/oxaloacetate decarboxylase, beta subunit
PIRSF015658\"[5-432]TNa(+)-transporting methylmalonyl-CoA/oxaloacetate decarboxylase, beta subunit
PF03977\"[18-432]TOAD_beta
TIGR01109\"[20-426]TNa_pump_decarbB: sodium ion-translocating d
noIPR
unintegrated
unintegrated
signalp\"[1-37]?signal-peptide
tmhmm\"[19-37]?\"[42-62]?\"[126-146]?\"[161-181]?\"[219-237]?\"[267-287]?\"[312-332]?\"[342-362]?\"[413-433]?transmembrane_regions


","BeTs to 6 clades of COG1883COG name: Na+-transporting methylmalonyl-CoA/oxaloacetate decarboxylase, beta subunitFunctional Class: CThe phylogenetic pattern of COG1883 is a---k---v--l----gh------t-Number of proteins in this genome belonging to this COG is","","Residues 20 to 82 match (2e-08) PD:PD009982 which is described as DECARBOXYLASE BETA PROTEOME COMPLETE LYASE OXALOACETATE CHAIN SODIUM TRANSMEMBRANE SUBUNIT ","","","","","","","","","","","Wed Jan 15 14:35:52 2003","Wed Jan 15 14:35:52 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02196 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 18 to 432 (E-value = 3.1e-295) place AA02196 in the OAD_beta family which is described as Na+-transporting methylmalonyl-CoA/oxaloacetate decarboxylase, beta subunit (PF03977)","","","","","econdary Laboratory Evidence:Woehlke,G., Wifling,K. and Dimroth,P. Sequence of the sodium ion pump oxaloacetate decarboxylasefrom Salmonella typhimurium. J. Biol. Chem.267(32):22798-22803,1992. PubMed: 1331067. Laussermair,E., Schwarz,E., Oesterhelt,D., Reinke,H.,Beyreuther,K. and Dimroth,P. The sodium ion translocating oxaloacetate decarboxylase ofKlebsiella pneumoniae. Sequence of the integralmembrane-bound subunits beta and gamma. J. Biol. Chem.264(25):14710-14715,1989. PubMed: 2549031. Bott,M., Pfister,K., Burda,P., Kalbermatter,O., Woehlke,G.and Dimroth,P. Methylmalonyl-CoA decarboxylase from Propionigeniummodestum--cloning and sequencing of the structural genesand purification of the enzyme complex. Eur. J. Biochem.250(2):590-599, 1997. PubMed: 9428714. Schmid M, Vorburger T, Pos KM, Dimroth P. Role of conserved residues within helices IV and VIII ofthe oxaloacetate decarboxylase beta subunit in the energycoupling mechanism of the Na+ pump. Eur J Biochem. 2002Jun;269(12):2997-3004. PMID: 12071964 Schmid M, Wild MR, Dahinden P, Dimroth P. Subunit gamma of the oxaloacetate decarboxylase Na(+) pump:interaction with other subunits/domains of the complex andbinding site for the Zn(2+) metal ion. Biochemistry. 2002Jan 29;41(4):1285-92. PMID: 11802728 ","","Wed Jan 15 14:35:52 2003","1","","","" "AA02199","1497767","1497961","195","TTGCGAAAACCGACCGCACTTTTTAATGAATATAAGATGGTGCACGTTTCACCGGCGTGTACCTTTTCTTTCGCGAGAATCTATTTAAAAACCCACCGCACTTTTACTTCCCACCGGTATGCTTTAATTCTTCTTTTACCCGACATACAAACCAAAAGTTGGCACTCATGCCGCAAGCGAAGGATTGATGTTGGT","","","7704","LRKPTALFNEYKMVHVSPACTFSFARIYLKTHRTFTSHRYALILLLPDIQTKSWHSCRKRRIDVG","1497961","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Jan 15 14:36:50 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02199 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02201","1499325","1498162","1164","GTGGATCAGAAACAAGAACATTTAAAAGGGAGGGGAACGAAAGAATCACCGCACTTTTATAAAATTCATCCTCCGGTTCTGAAAACCACGGATTTTTGTGATTATAAAAGTACTTTAACCGAACTATCTTGTATTACACGCAAAATTAGAGGTAAGAATTACTATGTCGCCATACGTGACAACATGTCGCTGGGTAAATATGTTGATTTCGGTATAGGAGGACGGTATGACATTTATCGTGCCCATAGCGACGATCCATTAATCAGCCGGGCTGGTTATCGTAATTTCTCATGGAATGCGGGTGTCGTACTAAAACCAACCGAATGGCTGGATTTTTCTTACCGTATTTCAACCGGTTTCCGTGTGCCGAGTTTCGACGAACTGTATGGCCGGAGATCGGGAAGCAAAAAAGTTTATGTGGCCAAATTTGAACCTGAAAAATCCCTTAACCAAGAGTTCGGTATTGTCTTAAAAGGCGATTTGGGTAGCTTTGAAATAAGTCATTTCCGTAATTCCTACAAAGGGTTGATAGCATTTGGCGAAAGTGTGCGAAAAGGCGGAAGATTAGGACTAATCGGTAGAGGCGATTATGGTTTCCGCAATGCACAAGATGCAAAATTAGTGGGTATTAATATTCTTGCACAATTGGAATGGCATAGTGTATGGAAAGCCTTGCCTTATGGCTTATACTCTACTTTTGCCTACAATCGTATTAAAGTAAAAGATAATCGAGTCAGACCGAATTTAGTTACTGTTACTAACCATTTATTTGATGCCATTCAACCGGCACGTTACGTTATAGGCTTGGGCTATGATGCGCCGACCGGTAAATGGGGCATGAATGCTATTTATACACATTCTCAGGCTAAGTCCGAAGATGAACTGACAGGTACTCGTAAACATATTCAACAATCACGGAAAGTTAAAGCGGCAAAAGTAACAACCTCATCTTGGCATACGGTGGATTTATCGGGTTATGTCACATTGGCCGACTTTATGACGGCACGTTTTGGTGTATATAATTTGTTCAATTCCCGTTATTCAACATGGGAGTCTGTCCGACAAAGCGCTACAGGTGCAATAAACCAGCACACCAGGGTAGGTAACTATAACCGCTATGTTGCACCGGGGCGAAATTATGCAATAACAATAGAAATGAAGTTT","","","44698","VDQKQEHLKGRGTKESPHFYKIHPPVLKTTDFCDYKSTLTELSCITRKIRGKNYYVAIRDNMSLGKYVDFGIGGRYDIYRAHSDDPLISRAGYRNFSWNAGVVLKPTEWLDFSYRISTGFRVPSFDELYGRRSGSKKVYVAKFEPEKSLNQEFGIVLKGDLGSFEISHFRNSYKGLIAFGESVRKGGRLGLIGRGDYGFRNAQDAKLVGINILAQLEWHSVWKALPYGLYSTFAYNRIKVKDNRVRPNLVTVTNHLFDAIQPARYVIGLGYDAPTGKWGMNAIYTHSQAKSEDELTGTRKHIQQSRKVKAAKVTTSSWHTVDLSGYVTLADFMTARFGVYNLFNSRYSTWESVRQSATGAINQHTRVGNYNRYVAPGRNYAITIEMKF","1498162","[FUNCTION] Acts as a transferrin receptor and is required for transferrin utilization (by similarity). ","transferrin-binding protein 1 precursor","Outer membrane, Extracellular","","
InterPro
IPR000531
Domain
TonB-dependent receptor
PF00593\"[97-388]TTonB_dep_Rec
InterPro
IPR010917
Domain
TonB-dependent receptor, C-terminal
PS01156\"[371-388]TTONB_DEPENDENT_REC_2
noIPR
unintegrated
unintegrated
G3DSA:2.40.170.20\"[52-388]Tno description


","BeTs to 7 clades of COG1629COG name: Outer membrane receptor proteins, mostly Fe transportFunctional Class: PThe phylogenetic pattern of COG1629 is -------q-----cefghsnuj----Number of proteins in this genome belonging to this COG is","","Residues 259 to 388 match (2e-09) PD:PD589930 which is described as A TRANSFERRIN BINDING ","","","","","","","","","","","Wed Jan 15 14:45:06 2003","Wed Jan 15 14:45:06 2003","","Thu Aug 4 09:57:42 2005","","Thu Aug 4 09:57:42 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA02201 is paralogously related to AA00764 (5e-19) and AA00763 (6e-04).","Thu Aug 4 09:57:42 2005","","","","","Residues 4 to 388 (E-value = 9.5e-06) place AA02201 in the TonB_dep_Rec family which is described as TonB dependent receptor (PF00593)","Thu Aug 4 09:57:42 2005","",""," Haraszthy VI, Jordan SF, Zambon JJ.,Identification of Fur-regulated genes in Actinobacillus actinomycetemcomitans.Microbiology. 2006 Mar;152(Pt 3):787-96.PMID: 16514158Kim TJ, Lee JI.Cloning and expression of genes encoding transferrin-binding protein A and B from Actinobacillus pleuropneumoniae serotype 5.Protein Expr Purif. 2005 Jul.PMID: 16005639"," Legrain,M., Mazarin,V., Irwin,S.W., Bouchon,B., Quentin-Millet,M.J., Jacobs,E. and Schryvers,A.B. Cloning and characterization of Neisseria meningitidis genes encoding the transferrin-binding proteins Tbp1 and Tbp2. Gene 130 (1): 73-80 (1993) [PubMed: 8344530]. Griffiths,E., Stevenson,P., Byfield,P., Ala'Aldeen,D.A., Borriello,S.P., Holland,J., Parsons,T. and Williams,P. Antigenic relationships of transferrin-binding proteins from Neisseria meningitidis, N. gonorrhoeae and Haemophilus influenzae:cross-reactivity of antibodies to NH2-terminal peptides. FEMS Microbiol. Lett. 109 (1): 85-91 (1993) [PubMed: 8319886].","Thu Aug 4 09:57:42 2005","Thu Aug 4 09:57:42 2005","1","","","" "AA02202","1500603","1499593","1011","GTGGTCGAGCAAGGTCGGGGCACCTCTTCCGGTTATTCCATTCGCGGAATGGATCGTAATAGAATTTCATTAAGTGTAGATGGTCTACCTCAAAGTCAGTCTTATGTGGTTCAAGGTCCACCGGCGGCCGGCAACGGTTATGCCGGTACAGGTGCAATTAACGAAGTTGAATATGAAAACATAAAATCCATTGAAATCAGTAAAGGTTCCAGTTCTTCAGAATATGGTAATGGTGCATTGGCCGGTGCTGTAGCGTTTCGTACTAAAACAGCGGATGACATTATCCAGCCCGGTAAAAACTGGGGGTTACAGACTAAGAACGCCTATGCCAGTAAAAATCGTGCTTCCACACATTCCATTGCAATAGCGGGAAAAAACGATGGGTTTGAGGGTCTATTCATCTACACGGATCGTCGAGGCAAAGAAGCACAAATTCATCGTGATGCACGCAGGGGAAGACAGCGTTATTCCCGCCAGGTTGCCGTACCGGGTACGGGCGGTACATATAACTATTTTCTTTTGCAAGAGGATTGTCCGTCCGGTAATGTTGATTTATGCAAAGGTTACATAAAGCCACTGGCAAGAGTTATTCCTGAGCAAGAAGAGACGGCTAGTCAGGGAGAGTATACCGGTGAGAATCGTGTTGCGCCGAACCCGATGAAATCTCGTAGTCAATCTTGGTTTTTCCGCCCGGGTTATCACTTTTCCGAGCAACATTATCTCGGGGCGGTTATGGAATATACTAAACAGCGCTTTGATATTCGCGATATGACATTACCTGCATATATCTTGCCTTATTCTCGTGAAAAGCCTCATATTGGTGGTTCCCAAGGGATCTATCAAGGACAAAATTACGGGCAATTCCAACGTGCGAGACATAACCAGCTGGGCTTCAGTTATGGGCGGGGTAGGTTCTATGATGAACACCACAGAAAAAAACGTATAGGTATTGAGTATATTTATAAAAATGCGCAAAAAAGCTGGATTGATCAGTTGCGTTTAAGTTTTGAT","","","37819","VVEQGRGTSSGYSIRGMDRNRISLSVDGLPQSQSYVVQGPPAAGNGYAGTGAINEVEYENIKSIEISKGSSSSEYGNGALAGAVAFRTKTADDIIQPGKNWGLQTKNAYASKNRASTHSIAIAGKNDGFEGLFIYTDRRGKEAQIHRDARRGRQRYSRQVAVPGTGGTYNYFLLQEDCPSGNVDLCKGYIKPLARVIPEQEETASQGEYTGENRVAPNPMKSRSQSWFFRPGYHFSEQHYLGAVMEYTKQRFDIRDMTLPAYILPYSREKPHIGGSQGIYQGQNYGQFQRARHNQLGFSYGRGRFYDEHHRKKRIGIEYIYKNAQKSWIDQLRLSFD","1499593","[FUNCTION] Acts as a transferrin receptor and is requiredfor transferrin utilization (by similarity). [SIMILARITY] Local to other tonB-dependent receptor proteins. ","transferrin-binding protein 1 precursor","Outer membrane, Extracellular","","
InterPro
IPR000169
Active_site
Peptidase, cysteine peptidase active site
PS00639\"[116-126]?THIOL_PROTEASE_HIS
InterPro
IPR012910
Domain
TonB-dependent receptor, plug
PF07715\"[1-83]TPlug
noIPR
unintegrated
unintegrated
G3DSA:2.170.130.10\"[2-88]Tno description


","BeTs to 7 clades of COG1629COG name: Outer membrane receptor proteins, mostly Fe transportFunctional Class: PThe phylogenetic pattern of COG1629 is -------q-----cefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 9.1e-12) to 2/3 blocks of the IPB000531 family, which is described as \"TonB-dependent receptor protein\". Interpro entry for IP:IPR000531. IPB000531A 15-28 0.00045 IPB000531B 76-93 6.4e-06","Residues 93 to 146 match (1e-10) PD:PD010103 which is described as RECEPTOR BINDING MEMBRANE A OUTER PROTEOME COMPLETE SIGNAL PRECURSOR HEMOGLOBIN ","","","","","","","","","","","Wed Jan 15 14:48:55 2003","Wed Jan 15 14:48:55 2003","","Thu Aug 4 09:58:12 2005","Thu Aug 4 09:58:12 2005","Thu Aug 4 09:58:12 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA02202 is paralogously related to AA00762 (4e-21), AA02782 (6e-08), AA02865 (5e-07), AA00590 (5e-06), AA02151 (8e-05) and AA02157 (6e-04).","Thu Aug 4 09:58:12 2005","","","","","","","",""," Haraszthy VI, Jordan SF, Zambon JJ.,Identification of Fur-regulated genes in Actinobacillus actinomycetemcomitans.Microbiology. 2006 Mar;152(Pt 3):787-96.PMID: 16514158Kim TJ, Lee JI.Cloning and expression of genes encoding transferrin-binding protein A and B from Actinobacillus pleuropneumoniae serotype 5.Protein Expr Purif. 2005 Jul.PMID: 16005639","Legrain,M., Mazarin,V., Irwin,S.W., Bouchon,B.,Quentin-Millet,M.J., Jacobs,E. and Schryvers,A.B. Cloning and characterization of Neisseria meningitidisgenes encoding the transferrin-binding proteins Tbp1 andTbp2. Gene 130 (1): 73-80 (1993) [PubMed: 8344530]. Griffiths,E., Stevenson,P., Byfield,P., Ala'Aldeen,D.A.,Borriello,S.P., Holland,J., Parsons,T. and Williams,P. Antigenic relationships of transferrin-binding proteinsfrom Neisseria meningitidis, N. gonorrhoeae and Haemophilusinfluenzae:cross-reactivity of antibodies to NH2-terminalpeptides. FEMS Microbiol. Lett. 109 (1): 85-91 (1993)[PubMed: 8319886].","Thu Aug 4 09:58:12 2005","Thu Aug 4 09:58:12 2005","1","","","" "AA02204","1501322","1501113","210","ATGGCGTTACCAAATCCGGCGGTGGCGCCGGTAACCAATGCGATTCTTGTCATCATTATTTCTCCTTATCTTGTGGAATTTGTACGTGATGAAAATTCATGTGGAAAAATCACCGCACTTTTGCTTGAATGCGAAACATACTACTCCACTAGTACAGAAAAATATAGAACTTTTATTAAGAAACTTGAAGGCGGGGAAGGAAAAGTGCGG","","","7749","MALPNPAVAPVTNAILVIIISPYLVEFVRDENSCGKITALLLECETYYSTSTEKYRTFIKKLEGGEGKVR","1501113","","hypothetical protein","Cytoplasm, Periplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-30]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Jan 15 14:49:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02204 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02205","1501310","1502044","735","TTGGTAACGCCATTTGGTAACGCCATTTGCCGAACCTTATTGAATGCCGGTTATTCGGTGATCGGCACCGGCAGAAGAAGCGAACGTTTAGCGCAGCTTCAACAAGAATACGGCAAACATTTCTTCCCTCTCACCTTTGATATTTCTGACCGTCACGCCGCTGAAAATGCGTTGAAAACCCTACCGCCGCAATGGCAGGCAATCGATTTGTTAGTCAACAATGCAGGGCTGGCATTAGGCTTGGAATCCGCCGATAAGGTGAATTTAGACGATTGGAACAAAATGATTGATACCAATGTGAAAGGCTTAGTCACTATGACCCGCTTAGTGTTGCCGCAAATGGTGGCGCGTAATCAGGGGCACATTATCAACTTCGGTTCTATCACCGGCACCTATCCTTACCCTGGCGGCAATGTTTATGGCGGTACCAAAGCCTTTGTAAAACAATTTAGCTTAAACCTACGTGCCGATCTTGCCGGAACCAATATTCGCGTTTCCAATGTAGAACCGGGACTGTGCGGCGGCACGGAATTTTCTAACGTACGTTTTAAAGGCGATAACGCCCGCGCGGAAAAACTCTACGAAAACGTACAATATGTTACGCCACAAGATATTGCCAATATCGTGTTGTGGCTCAATCAACAACCGGAACACGTCAACATTAACCGCATTGAAGTGATGCCGACGGCGCAAACCTTCGCCCCGCTTAATGTAGCAAGGAATTTAAATTTAGAT","","","27053","LVTPFGNAICRTLLNAGYSVIGTGRRSERLAQLQQEYGKHFFPLTFDISDRHAAENALKTLPPQWQAIDLLVNNAGLALGLESADKVNLDDWNKMIDTNVKGLVTMTRLVLPQMVARNQGHIINFGSITGTYPYPGGNVYGGTKAFVKQFSLNLRADLAGTNIRVSNVEPGLCGGTEFSNVRFKGDNARAEKLYENVQYVTPQDIANIVLWLNQQPEHVNINRIEVMPTAQTFAPLNVARNLNLD","1502044","","short chain dehydrogenase/reductase","Periplasm, Cytoplasm","","
InterPro
IPR002198
Family
Short-chain dehydrogenase/reductase SDR
PR00080\"[66-77]T\"[120-128]T\"[140-159]TSDRFAMILY
PTHR19410\"[6-230]TSHORT-CHAIN DEHYDROGENASES/REDUCTASE FAMILY MEMBER
PF00106\"[5-159]Tadh_short
PS00061\"[127-155]?ADH_SHORT
InterPro
IPR002347
Family
Glucose/ribitol dehydrogenase
PR00081\"[66-77]T\"[114-130]T\"[140-159]T\"[161-178]T\"[195-215]TGDHRDH
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[5-228]Tno description
PTHR19410:SF42\"[6-230]TSHORT-CHAIN DEHYDROGENASE-RELATED


","BeTs to 10 clades of COG0300COG name: Short-chain dehydrogenases of various substrate specificitiesFunctional Class: RThe phylogenetic pattern of COG0300 is -o----y---rlb-ef-hsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 4.5e-12) to 1/1 blocks of the IPB002198 family, which is described as \"Short-chain dehydrogenase/reductase (SDR) superfamily\". Interpro entry for IP:IPR002198. IPB002198 120-155 4.3e-12","Residues 5 to 38 match (5e-08) PD:PD058480 which is described as OXIDOREDUCTASE COMPLETE PROTEOME DEHYDROGENASE REDUCTASE SHORT-CHAIN DEHYDROGENASE/REDUCTASE PROBABLE FAMILY NADP ","","","","","","","","","","","","Wed Jan 15 14:56:26 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02205 is paralogously related to AA01109 (2e-19), AA00269 (2e-16), AA00912 (2e-14), AA01179 (2e-10) and AA02383 (5e-05).","","","","","","Residues 5 to 230 (E-value = 4.2e-57) place AA02205 in the adh_short family which is described as short chain dehydrogenase (PF00106)","","","","","Henrich,B., Becker,S., Schroeder,U. and Plapp,R. dcp gene of Escherichia coli: cloning, sequencing, transcript mapping, and characterization of the gene product. J. Bacteriol. 175 (22): 7290-7300 (1993) [PubMed: 8226676].Borodovsky,M., Rudd,K.E. and Koonin,E.V. Intrinsic and extrinsic approaches for detecting genes in a bacterial genome. Nucleic Acids Res. 22 (22): 4756-4767 (1994) [PubMed: 7984428].Link,A.J., Robison,K. and Church,G.M. Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis 18 (8): 1259-1313 (1997) [PubMed: 9298646].","","Wed Jan 15 14:56:26 2003","1","","","" "AA02206","1502057","1503247","1191","ATGGCGGAAACGATTTTAAACCCGTATTTCGGGGAATTCGGCGGAATGTATGTGCCGGAAATTCTAGTGCCGGTGTTGCAACAGTTGGAAAAAGCGTTTGTAGAAGCCAAGGCGGATCCTGCATTTCAGCGCGAATTTCAGGATTTATTGAAAAATTATGCCGGCAGACCCACCGCACTTACCCTTTGTCGCAATCTCACCAAAGGCACCAACGCCAAAATCTATTTAAAACGGGAAGATTTATTACACGGCGGCGCACATAAAACCAACCAGGTATTAGGTCAGATTTTGCTTGCCAAACGCATGGGCAAAACCCGCATTATTGCCGAAACCGGCGCGGGACAGCACGGTGTCGCCACTGCTCTCGCCTGCGCCATGTTGGATATGCCGTGCCGTGTTTATATGGGCGCGAAAGATGTGGAACGCCAATCGCCGAATGTGTTTCGTATGCGTTTAATGGGCACGGAAGTGGTACCGGTGCAAAAAGGTTCCTGTTCTTTGAAAGACGCTTGCTGCGAAGCCATGCGTGACTGGTCGGCAAATTATGAAAATACGCACTATTTGCTCGGCACAGCGGCAGGTCCGCACCCTTTTCCGACTATCGTGCGTGAATTCCAGAAAATGATCGGGGAAGAAACCAAACGCCAAATGCTGGAAAAAGAAGGTCGTTTACCGGACGCGGTAATTGCGGCAGTCGGCGGTGGCTCAAATGCGATCGGAATGTTTACCGATTTTATTGACGAAAAAGAGGTGCGTTTAATCGGCGTGGAACCTGCCGGCAAAGGCATTGAAACGGGCAAACACGGCGCGCCGTTAGGTCATGCCAAAGTGGGAATTTATTTCGGTATGAAATCACCGTTGATGCAAACGGAAGACGGTCAAGTGGAAGAATCCTATTCCATTTCGGCGGGCTTGGATTTCCCTTCCGTGGGGCCGCAACACGCCTATTTACAAAGCATCGGTCGTGCGGAATACCCAAGTATTACCGATAATGAAGCCCTTGACGCGTTCCAAGCATTGGCAAAACACGAAGGCATTATTCCTGCGTTAGAAAGCTCCCACGCCCTCGCCCAAGCCTTAAAAATGATCCGTCAGGAACCAAATAAAGCGCAAATTTTGGTGGTGAATTTGTCCGGTCGCGGCGATAAAGATATTTTCACCGTAGATAAAATTTTAAATGAAAAAGGAATG","","","43295","MAETILNPYFGEFGGMYVPEILVPVLQQLEKAFVEAKADPAFQREFQDLLKNYAGRPTALTLCRNLTKGTNAKIYLKREDLLHGGAHKTNQVLGQILLAKRMGKTRIIAETGAGQHGVATALACAMLDMPCRVYMGAKDVERQSPNVFRMRLMGTEVVPVQKGSCSLKDACCEAMRDWSANYENTHYLLGTAAGPHPFPTIVREFQKMIGEETKRQMLEKEGRLPDAVIAAVGGGSNAIGMFTDFIDEKEVRLIGVEPAGKGIETGKHGAPLGHAKVGIYFGMKSPLMQTEDGQVEESYSISAGLDFPSVGPQHAYLQSIGRAEYPSITDNEALDAFQALAKHEGIIPALESSHALAQALKMIRQEPNKAQILVVNLSGRGDKDIFTVDKILNEKGM","1503247","[FUNCTION] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine (by similarity). ","tryptophan synthase, beta chain","Cytoplasm","","
InterPro
IPR001926
Domain
Pyridoxal-5'-phosphate-dependent enzyme, beta subunit
PF00291\"[51-380]TPALP
InterPro
IPR006653
Domain
Tryptophan synthase, beta chain and related
PS00168\"[81-95]TTRP_SYNTHASE_BETA
InterPro
IPR006654
Family
Tryptophan synthase, beta chain
TIGR00263\"[8-392]TtrpB: tryptophan synthase, beta subunit
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1100\"[174-395]Tno description
PIRSF001413\"[1-397]TTryptophan synthase, beta subunit
PTHR10314\"[16-393]TSER/THR DEHYDRATASE, TRP SYNTHASE
PTHR10314:SF3\"[16-393]TTRYPTOPHAN SYNTHASE BETA CHAIN


","BeTs to 21 clades of COG0133COG name: Tryptophan synthase beta chainFunctional Class: EThe phylogenetic pattern of COG0133 is aom-k-yqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is","Significant hit (7.3e-192) to 7/7 blocks of the IPB000993 family, which is described as \"Tryptophan synthase, beta chain\". Interpro entry for IP:IPR000993. IPB000993A 42-66 1.7e-13 IPB000993B 97-135 2.1e-35 IPB000993C 139-191 1.3e-41 IPB000993D 199-248 1e-39 IPB000993E 251-293 3.1e-25 IPB000993F 328-357 1.9e-21 IPB000993G 374-385 3.5e-08Significant hit ( 2.9e-14) to 2/2 blocks of the IPB001926 family, which is described as \"Pyridoxal-5'-phosphate-dependent enzymes, beta family\". Interpro entry for IP:IPR001926. IPB001926A 108-135 2.8e-12 IPB001926B 347-355 2.7","Residues 324 to 380 match (3e-10) PD:PD001075 which is described as CYSTEINE SYNTHASE LYASE COMPLETE PROTEOME O-ACETYLSERINE PHOSPHATE PYRIDOXAL BIOSYNTHESIS SULFHYDRYLASE ","","","","","","","","","","","Wed Jan 15 15:01:54 2003","Fri May 20 08:45:28 2005","","Fri May 20 08:45:28 2005","Fri May 20 08:45:28 2005","Fri May 20 08:45:28 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA02206 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Fri May 20 08:45:28 2005","","","","","Residues 51 to 380 (E-value = 1.4e-121) place AA02206 in the PALP family which is described as Pyridoxal-phosphate dependent enzyme (PF00291)","Fri May 20 08:45:28 2005","","","","Yanofsky,C., Platt,T., Crawford,I.P., Nichols,B.P., Christie,G.E., Horowitz,H., VanCleemput,M. and Wu,A.M. The complete nucleotide sequence of the tryptophan operon of Escherichia coli. Nucleic Acids Res. 9 (24): 6647-6668 (1981) [PubMed: 7038627].Crawford,I.P., Nichols,B.P. and Yanofsky,C. Nucleotide sequence of the trpB gene in Escherichia coli and Salmonella typhimurium. J. Mol. Biol. 142 (4): 489-502 (1980) [PubMed: 7007651].Higgins,W., Miles,E.W. and Fairwell,T. Location of three active site residues in the NH2-terminal sequence of the beta 2 subunit tryptophan synthase from Escherichia coli. J. Biol. Chem. 255 (2): 512-517 (1980) [PubMed: 6985892].Fluri,R., Jackson,L.E., Lee,W.E. and Crawford,I.P. Tryptophan synthetase 2 subunit. Primary structure of the pyridoxyl peptide from the Escherichia coli enzyme. J. Biol. Chem. 246 (21): 6620-6624 (1971) [PubMed: 4943677].Cotton,R.G. and Crawford,I.P. Tryptophan synthetase B 2 subunit. Application of genetic analysis to the study of primary structure. J. Biol. Chem. 247 (6): 1883-1891 (1972) [PubMed: 4552018].","","Wed Jan 15 15:01:54 2003","1","","","" "AA02208","1503253","1504056","804","ATGAGCCGTTTTGAAACCACATTTGCCCAATTACACGCGCAAAATGAAGGCGCATTCGTTCCTTTCGTGACCTTATGCGACCCGACTTTCGACCGTTCTTTTGACATTATTTGCACCCTGGTGGATAACGAGGCGGACGCATTGGAACTGGGTTTTCCGTTCTCCGATCCCTTATTGGACGGACCGGTGATTCAAGCCGCCAACAATCGTGCGTTAAACGCCGGTCACAGCACGGAAGACAGCTTTAAATTGCTGGAAAAAGTGCGGTCAAAATATCCGGAGATTCCGATGAGTTTGCTGCTTTGCGCCAATTTAATTTTTGCCAAAGGCTTGGATAATTTTTATCAGCGTTGCGCCGACGTGGGCGTGGACGCCGTGTTGGTTGCCGATATTCCGTTGTTGGCGAAAGACGATTATGTCGCCGCCGCGAAAAGACACGGTATTCAACCCGTTTTTATTTGCCCGCCGAATGCAGACGAAAAAACCATTCAAGATGTGGCGCAAAATAGTGAAGGTTACACGTATTTGGTTTCCCGCGCGGGCGTGACCGGTGCAGAAAATCAAAGCCATACGGCGAATCTGGACAGCTTAGTAGAACGACTCAAAGCCCACCACGCCGCTCCAATTCTGCAAGGCTTCGGCATCGCCCAACCGGCGCAGGTAAAAGAAGCACTGCAACTGGGCGCGGCAGGGGCGATTTCCGGTTCCGCTACGGTGAAAATCATTGCGCGAAATTTGGATAACCACGCCCAATGTTTAACTGAACTCGGCGAATTCGTACGCAATATGAAAGCGGCGACGAAA","","","28883","MSRFETTFAQLHAQNEGAFVPFVTLCDPTFDRSFDIICTLVDNEADALELGFPFSDPLLDGPVIQAANNRALNAGHSTEDSFKLLEKVRSKYPEIPMSLLLCANLIFAKGLDNFYQRCADVGVDAVLVADIPLLAKDDYVAAAKRHGIQPVFICPPNADEKTIQDVAQNSEGYTYLVSRAGVTGAENQSHTANLDSLVERLKAHHAAPILQGFGIAQPAQVKEALQLGAAGAISGSATVKIIARNLDNHAQCLTELGEFVRNMKAATK","1504056","[FUNCTION] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate","tryptophan synthase, alpha subunit","Cytoplasm","","
InterPro
IPR002028
Domain
Tryptophan synthase, alpha chain
PD001535\"[1-132]TTRPA_HAEIN_P43759;
PF00290\"[8-268]TTrp_syntA
TIGR00262\"[8-264]TtrpA: tryptophan synthase, alpha subunit
PS00167\"[48-61]TTRP_SYNTHASE_ALPHA
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[1-267]Tno description
noIPR
unintegrated
unintegrated
PTHR10314\"[54-239]TSER/THR DEHYDRATASE, TRP SYNTHASE
PTHR10314:SF4\"[54-239]TTRYTOPHAN SYNTHASE ALPHA SUBUNIT


","BeTs to 23 clades of COG0159COG name: Tryptophan synthase alpha chainFunctional Class: EThe phylogenetic pattern of COG0159 is aompkzyqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-40) to 5/5 blocks of the IPB002028 family, which is described as \"Tryptophan synthase alpha chain\". Interpro entry for IP:IPR002028. IPB002028A 44-65 9.7e-14 IPB002028B 96-111 0.0045 IPB002028C 172-184 1.3e-07 IPB002028D 208-224 1.1e-06 IPB002028E 229-239 0.0063","Residues 180 to 259 match (5e-29) PD:PD233252 which is described as TRYPTOPHAN SYNTHASE LYASE BIOSYNTHESIS ALPHA CHAIN COMPLETE PROTEOME CHLOROPLAST PYRIDOXAL ","","","","","","","","","","","Wed Jan 15 15:05:50 2003","Fri May 20 08:51:21 2005","","Fri May 20 08:51:21 2005","Fri May 20 08:51:36 2005","Fri May 20 08:51:21 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA02208 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Fri May 20 08:51:21 2005","","","","","Residues 8 to 268 (E-value = 9.5e-140) place AA02208 in the Trp_syntA family which is described as Tryptophan synthase alpha chain (PF00290)","Fri May 20 08:51:21 2005","","","","Nichols,B.P., Blumenberg,M. and Yanofsky,C. Comparison of the nucleoside sequence of trpA and sequences immediately beyond the trp operon of Klebsiella aerogenes. Salmonella typhimurium and Escherichia coli. Nucleic Acids Res. 9 (7): 1743-1755 (1981) [PubMed: 6262736].Guest,J.R., Drapeau,G.R., Carlton,B.C. and Yanofsky,C. The amino acid sequence of the A protein (alpha subunit) of the tryptophan synthetase of Escherichia coli. J. Biol. Chem. 242 (22): 5442-5446 (1967) [PubMed: 4863752].Link,A.J., Robison,K. and Church,G.M. Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis 18 (8): 1259-1313 (1997) [PubMed: 9298646].","","Wed Jan 15 15:05:50 2003","1","","","" "AA02210","1504334","1506016","1683","ATGTCTCACACCCAATTTCTTCCAATTACCGATCCGAATCGACCGGATTTTGCCTGGCTTAATGAAGACAGCAAATTGTTTTTACAACGTGGTTATCTGTTAGAAGGCACCTCCGCCTTAGAGCGCATTCGTTTCATCGCCGATTACGCCGAACAAAAACTCGGCATTGAAGGCTATGCGGATAAATTTTATCACTACATGGCGCGCGGCTATTATTCCCTTTCCTCACCGATTTGGTCGAACTTCGGCTTAAGCCGCGGTTTAAGCATCAGCTGCTTCGGTTCCTATATCGGTGATTCCATCAACAGCATTATGTCCACCGTGGCGGAAATCGGCGTGATGAGCAAACTCGGCGGTGGCACCTCAGGCTATTTCGGCGATATTCGCCCGCGCGGTTCCAACATCACCAATAACGGTAAATCCAACGGTTCTTTCGCCTTCACTAAACTGTTTGAAGCTACTATTGACACCATCAGCCAAGGCACCAGCCGTAAAGGGATGTTCGCCGGTTATATTGACATCGACCACGGCGACATTGAAGAATGGCTGGATATTCACACCGAAGGCAACCCGATTCAGTTAATGTATTACGGCGTGTGCGTCAGCCACGAATGGTTAGAAGCAATGAAAGCCGGCGATCCGTACAAGCGCCAAATCTGGGCAAAATTGTTACAACGTAAGACGGAAACGGGCATTCCCTATTTGTTCTTCAAGGATAACGCCAATGCCGGTCGCCCGGACGTGTATAAAGATCGCAACATGATGATTCACGCCTCCAATTTATGTAGTGAAATCGCCTTGCCGTCCAGCGAAGACGAAAGTTTCGTGTGTTGTTTATCTTCTATGAATTTGCTCTATTTTGATGAATGGAAAGACACCGACGCACCGGAAGTGCTGACCTATTTCCTGGATACGGTGATGAGCGAGTTCATTGCACAAAGCGCCAATATTCAATACATGGAAAAAGCCAATAAATTCGCCCGTCATCATCGTGCGCTGGGCTTAGGTGTGCTGGGCTGGCACAGCTATTTGCAATCGAAAAATATCGCTTTCGACAGCTTTGAAGCCATGCAATATAACAATATGATTTTCAAATTGTTACAGGAAAAAACCTTAAAAGCCTCGAAAGAGCTGGCCCATCGTTTCGGTGAACCGGAAATTCTGAAAGGTTATGGTCGCCGTAATACCACCTTAATGAGCGTGGCGCCGACCAAATCCAGCAGCTTTATTTTAGGCAGCGTATCGCCATCTATCGAACCGTTTAAATCCAATTACTACGTGAAAGATTTGTCCAAAATTAAAGTGGTCTATAAAAACCCGTTTTTGGAAGCGTTGCTCAAACAAAAAGGCCTGGATCGCGAAGATATTTGGGAAAGCATTCTGTTCAATGACGGTTCCGTACAGCATTTAAACGAGCTGACCGAACAGGAAAAAGAGGTGTTTAAAACCTTCTCGGAAATCAGTCAACTTTCCGTGATTCAACAGGCGGCACAACGTCAAAAATACATCGACCAAGGGCAAAGCGTTAATATCATGGTGCATCCGGCAACCCCGGCACGTGATTTAAACCAGCTTTACCTCACCGCCGAAGAACTGGGTTTGAAATCCATTTATTACCAATACAGCATGAGTGCGGCGCAAGTGTTTAACCGTAACCTGCTTAATTGCAGCAGTTGTGAAGGT","","","63578","MSHTQFLPITDPNRPDFAWLNEDSKLFLQRGYLLEGTSALERIRFIADYAEQKLGIEGYADKFYHYMARGYYSLSSPIWSNFGLSRGLSISCFGSYIGDSINSIMSTVAEIGVMSKLGGGTSGYFGDIRPRGSNITNNGKSNGSFAFTKLFEATIDTISQGTSRKGMFAGYIDIDHGDIEEWLDIHTEGNPIQLMYYGVCVSHEWLEAMKAGDPYKRQIWAKLLQRKTETGIPYLFFKDNANAGRPDVYKDRNMMIHASNLCSEIALPSSEDESFVCCLSSMNLLYFDEWKDTDAPEVLTYFLDTVMSEFIAQSANIQYMEKANKFARHHRALGLGVLGWHSYLQSKNIAFDSFEAMQYNNMIFKLLQEKTLKASKELAHRFGEPEILKGYGRRNTTLMSVAPTKSSSFILGSVSPSIEPFKSNYYVKDLSKIKVVYKNPFLEALLKQKGLDREDIWESILFNDGSVQHLNELTEQEKEVFKTFSEISQLSVIQQAAQRQKYIDQGQSVNIMVHPATPARDLNQLYLTAEELGLKSIYYQYSMSAAQVFNRNLLNCSSCEG","1506016","[FUNCTION] Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides, precursors that are necessary for dna synthesis (by similarity). ","ribonucleoside-diphosphate reductase alpha chain","Cytoplasm, Outer membrane","","
InterPro
IPR000788
Domain
Ribonucleotide reductase large subunit, C-terminal
PR01183\"[164-183]T\"[331-353]T\"[392-419]TRIBORDTASEM1
PTHR11573\"[71-539]TRIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN
PF02867\"[88-544]TRibonuc_red_lgC
InterPro
IPR013350
Family
Ribonucleoside-diphosphate reductase alpha chain
TIGR02510\"[9-561]TNrdE-prime: ribonucleoside-diphosphate redu
InterPro
IPR013509
Domain
Ribonucleotide reductase large subunit, N-terminal
PF00317\"[18-87]TRibonuc_red_lgN
noIPR
unintegrated
unintegrated
G3DSA:3.90.244.10\"[254-539]Tno description


","BeTs to 25 clades of COG0209COG name: Ribonucleotide reductase alpha subunitFunctional Class: FThe phylogenetic pattern of COG0209 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.7e-26) to 6/10 blocks of the IPB000788 family, which is described as \"Ribonucleotide reductase large subunit\". Interpro entry for IP:IPR000788. IPB000788C 64-94 3.9e-05 IPB000788D 114-150 44 IPB000788E 164-186 0.00019 IPB000788G 254-273 4.1e-07 IPB000788I 381-419 0.41 IPB000788J 530-539 1.8","Residues 91 to 185 match (2e-10) PD:PD003934 which is described as REDUCTASE RIBONUCLEOSIDE-DIPHOSPHATE CHAIN OXIDOREDUCTASE REPLICATION DNA LARGE COMPLETE PROTEOME RIBONUCLEOTIDE ","","","","","","","","","","","Wed Jan 15 15:09:07 2003","Wed Jan 15 15:09:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02210 is paralogously related to AA01637 (2e-20).","","","","","","Residues 88 to 544 (E-value = 1.5e-20) place AA02210 in the Ribonuc_red_lgC family which is described as Ribonucleotide reductase, barrel domain (PF02867)","","","","","","","","1","","","" "AA02212","1506152","1507138","987","ATGAACGCCACCGCAAAACGCAGCTTATTTACCCCACGCTTTGAAATTAAACCTTACGAATATCCCGAACTGCTTGAATTTAAAGACGCTATCCGCCATTCTTACTGGCTTCACACGGAATTTAATTTCACCGGCGACATTCAGGATTTTCGCACCCATATCAGCGATGTTGAACGTGCCGTTATCACCAAAACCATGCTTGCCATTTCGCAAATTGAAGTAAGCGTCAAACGCTTCTGGGGCAATCTCTATAATTATTTCCCGAAACCGGAAATTGAAGATGTGGGCGGCAGTTTTCTGGAATCGGAAATTCGCCACAAAGATGCCTATTCTTTCCTGCTGGAAAAACTCGGGTTGAATGAAATGTTCCGCAACGTGCGTCAATACAAAGCCATCATGGCGCGCATTGAGTACATGGAAGCCTTCATGCGTAAAAAAGACGTGAGCCAACAGGATTTTGTGCTTTCACTGGTGATGTTTTCACTGTTCGTGGAACACATTTCGCTGTTCAGCCAGTTTGTTATCATGATGAGCTTCAACAAACATAAAAACCTGTTCAAAGGCATTTCTAATGCGGTAGAAGCCACATCCAAAGAAGAAGAAATTCACGGGCGTTTTGGTATTAGCCTTTATCATCTTTTACGCGAAGAACAGCCGGAATTATTTACCGACGAGTTCTATGCGGAATTAAAAGAACTCTCCGAGCAAGCTTTCAACGCAGAAAAAGCGATTTTGGACTGGATTTTCGAAGACTGCGAATTGAGTTTCTTAAGCAAAGCCACCGTCGAAAATTACATTGCCAACCGTTACAACAACTCTCTTGTGACGTTAGGTTTGGAACCGATTTACAACATCAATCCGGCGCAATTGAAGGAAACGGAATGGTTTGACATTGAAATTCTCTCCACCAAGGAAACGGATTTCTTCAACAAGCGCTCCACCGATTACAGTAAAAAAATGAAACAAATCACGGCAGACGATTTATTT","","","39789","MNATAKRSLFTPRFEIKPYEYPELLEFKDAIRHSYWLHTEFNFTGDIQDFRTHISDVERAVITKTMLAISQIEVSVKRFWGNLYNYFPKPEIEDVGGSFLESEIRHKDAYSFLLEKLGLNEMFRNVRQYKAIMARIEYMEAFMRKKDVSQQDFVLSLVMFSLFVEHISLFSQFVIMMSFNKHKNLFKGISNAVEATSKEEEIHGRFGISLYHLLREEQPELFTDEFYAELKELSEQAFNAEKAILDWIFEDCELSFLSKATVENYIANRYNNSLVTLGLEPIYNINPAQLKETEWFDIEILSTKETDFFNKRSTDYSKKMKQITADDLF","1507138","[FUNCTION] Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides, precursors that are necessary for DNA synthesis (by similarity). ","ribonucleoside-diphosphate reductase beta chain","Cytoplasm","","
InterPro
IPR000358
Family
Ribonucleotide reductase
PTHR23409\"[11-327]TRIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN
PF00268\"[4-291]TRibonuc_red_sm
InterPro
IPR012348
Family
Ribonucleotide reductase-related
G3DSA:1.10.620.20\"[19-284]Tno description
noIPR
unintegrated
unintegrated
PTHR23409:SF5\"[11-327]TRIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN
tmhmm\"[153-175]?transmembrane_regions


","BeTs to 16 clades of COG0208COG name: Ribonucleotide reductase beta subunitFunctional Class: FThe phylogenetic pattern of COG0208 is -o----yq-drlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 5.8e-11) to 4/5 blocks of the IPB000358 family, which is described as \"Ribonucleotide reductase\". Interpro entry for IP:IPR000358. IPB000358A 20-74 0.028 IPB000358B 95-120 24 IPB000358C 172-212 0.32 IPB000358E 306-316 0.03","Residues 103 to 318 match (5e-17) PD:PD000938 which is described as REDUCTASE RIBONUCLEOTIDE SMALL CHAIN SUBUNIT RIBONUCLEOSIDE-DIPHOSPHATE OXIDOREDUCTASE IRON DNA REPLICATION ","","","","","","","","","","","Wed Jan 15 15:14:04 2003","Wed Jan 15 15:14:04 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02212 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 293 (E-value = 4.1e-07) place AA02212 in the Ribonuc_red_sm family which is described as Ribonucleotide reductase, small chain (PF00268)","","","","","","","","1","","","" "AA02213","1507225","1507136","90","GTGTTTAGACATAATCGGTTACGGTTTCCCCATGAAAAAAGTGCGGTGAAAAAACACATTAATTTTCTACCGCACTTTTTGAAGCTAAAA","","","3720","VFRHNRLRFPHEKSAVKKHINFLPHFLKLK","1507136","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:14:18 2004","Wed Feb 25 15:14:18 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02213 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:14:18 2004","","","","","","","","","","","","","1","","","" "AA02214","1507388","1508830","1443","ATGTCCAGAAGACTAAGAAGAACGAAAATTGTATGTACTATGGGACCTTCAACAGACCGTGGTAACAATTTAGAAAAAATCATTGCTGCCGGTGCCAACGTAGTACGTATGAATTTCTCACATGGCTCACCAGAAGATCATATCGCCCGCGCAGAACATGTACGTGAAATTGCCAAAAAATTAGGTAAAACCGTGGCGATTTTAGGTGACTTACAAGGCCCTAAAATTCGCGTATCCACCTTTAAAGACGGCAAAATCTTCTTAAACGTCGGCGATAAATTCGTATTAGACGCAGAATTACCGAAAGGTGAAGGTACACAAGAAGTTGTCGGCTTAGACTACAAAACCCTTCCACAAGACGTTGTACCGGGCGATATTCTGTTATTAGACGATGGTCGCGTACAATTAAAAGTATTATCCACCGAAGGCGCGAAAGTCTTCACCGAAGTGACTGTAGGCGGCCCGTTATCCAACAACAAAGGGATTAACAAATTAGGCGGCGGCTTATCTGCCAATGCCTTAACCGAAAAAGACAAAGCGGACATCATTACCGCCGCGCGTATCGGCGTTGACTACCTTGCCGTCTCCTTCCCGCGCTCCAGCGCAGATTTAAACTACGCCCGTCAATTAGCCCAAGAAGCCGGCTTAAATGCCAAAATCGTTGCCAAAGTTGAACGTGCCGAAACCGTTGTTGACGATGCTTCGATGGACGACATCATTCTGGCTTCCGACATCATAATGGTTGCCCGTGGTGACTTAGGGGTGGAAATCGGTGATCCGGAATTGGTCGGCGTACAGAAAAAATTAATCCGCCGCTCCCGTAAATTAAATCGCGTGGTAATCACCGCGACACAAATGATGGAATCTATGATCAGCAACCCAATGCCAACCCGTGCGGAAGTCATGGACGTGGCGAACGCGGTATTGGACGGCACCGACGCAGTAATGCTTTCTGCCGAAACCGCCGCCGGTCAATACCCCGCCGAAACCGTTGCCGCCATGGCGAAAGTATGTTTAGGTGCGGAAAAAATGCCTAGCGTAAATACTTCTCATCATCGTATGGATATGGAATTCGACAATCCTGAAGAAACCATTGCCATGTCCGCCATGTTCGCTGCCAATCACATGAAAGGCGTGACTGCAATTATCGCTATGACCAGTTCCGGTCGCACCCCGCTGTTAATGTCTCGCATTAGCTCCGGTCTGCCAATTTTTGCCTTATCCCGTAATCAAAATACCTTAAACCTGTGTGCGTTGTATCGCGGTGTAACTCCGATTTATTACGATGATGTCAGCCGCACCATCGAAGGCGCGCAAAAAGCCATTAATCTGTTAAAAGAAAAAGGCTTCTTAATGTCCGGCGACACCGTGTTATTAACCCAAGGTGCAGAATTCGCCAACAGCGGTTCCAACACCAACACCTGTCGTATCCTTACCGTTGAA","","","53946","MSRRLRRTKIVCTMGPSTDRGNNLEKIIAAGANVVRMNFSHGSPEDHIARAEHVREIAKKLGKTVAILGDLQGPKIRVSTFKDGKIFLNVGDKFVLDAELPKGEGTQEVVGLDYKTLPQDVVPGDILLLDDGRVQLKVLSTEGAKVFTEVTVGGPLSNNKGINKLGGGLSANALTEKDKADIITAARIGVDYLAVSFPRSSADLNYARQLAQEAGLNAKIVAKVERAETVVDDASMDDIILASDIIMVARGDLGVEIGDPELVGVQKKLIRRSRKLNRVVITATQMMESMISNPMPTRAEVMDVANAVLDGTDAVMLSAETAAGQYPAETVAAMAKVCLGAEKMPSVNTSHHRMDMEFDNPEETIAMSAMFAANHMKGVTAIIAMTSSGRTPLLMSRISSGLPIFALSRNQNTLNLCALYRGVTPIYYDDVSRTIEGAQKAINLLKEKGFLMSGDTVLLTQGAEFANSGSNTNTCRILTVE","1508830","","pyruvate kinase II","Cytoplasm","","
InterPro
IPR001697
Family
Pyruvate kinase
PTHR11817\"[7-481]TPYRUVATE KINASE
TIGR01064\"[6-480]Tpyruv_kin: pyruvate kinase
InterPro
IPR015793
Domain
Pyruvate kinase, barrel
PD001009\"[6-139]T\"[174-342]TKPYK_HAEIN_P43924;
PR01050\"[63-79]T\"[190-204]T\"[223-249]T\"[250-274]T\"[275-299]T\"[300-318]T\"[319-335]TPYRUVTKNASE
PF00224\"[5-351]TPK
PS00110\"[218-230]TPYRUVATE_KINASE
InterPro
IPR015794
Domain
Pyruvate kinase, alpha/beta
G3DSA:3.40.1380.20\"[343-480]Tno description
PF02887\"[362-479]TPK_C
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.60\"[5-341]Tno description


","BeTs to 21 clades of COG0469COG name: Pyruvate kinaseFunctional Class: GThe phylogenetic pattern of COG0469 is -ompkzy-vdrlbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is","Significant hit (4.1e-146) to 8/8 blocks of the IPB001697 family, which is described as \"Pyruvate kinase family\". Interpro entry for IP:IPR001697. IPB001697A 12-47 2.3e-21 IPB001697B 65-79 3.5e-06 IPB001697C 112-138 2.2e-13 IPB001697D 156-204 7.3e-23 IPB001697E 231-275 8.5e-22 IPB001697F 276-298 1.5e-15 IPB001697G 299-331 3.2e-26 IPB001697H 381-408 1e-09 IPB001697H 403-430 0.00043","Residues 363 to 480 match (1e-08) PD:PD538456 which is described as KINASE PROTEOME II PYRUVATE COMPLETE ","","","","","","","","","","","","Wed Jan 15 15:19:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02214 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 362 to 479 (E-value = 3.1e-52) place AA02214 in the PK_C family which is described as Pyruvate kinase, alpha/beta domain (PF02887)","","","","","Gonzalez R, Tao H, Shanmugam KT, York SW, Ingram LO. Global gene expression differences associated with changes in glycolytic flux and growth rate in Escherichia coli during the fermentation of glucose and xylose. Biotechnol Prog. 2002 Jan-Feb;18(1):6-20. PMID: 11822894 Ponce E, Flores N, Martinez A, Valle F, Bolivar F. Cloning of the two pyruvate kinase isoenzyme structural genes from Escherichia coli: the relative roles of these enzymes in pyruvatebiosynthesis. J Bacteriol. 1995 Oct;177(19):5719-22. PMID: 7559366","","Wed Jan 15 15:19:16 2003","1","","","" "AA02215","1509239","1508940","300","ATGTTTGCAATGTTGGTAGAAATTAATATCAAGGAAGGTAAAGAGCTGGAATTTCTCGACGTCTTTGAGCGTAATCATATCGGTACCCGACAGGAGCCGGGCAATTTGCGTTTTGATGTGTTACGTGATCCGGAAATTCGTACCCGTTTTTACGCTTATGAAGTTTATGTGAACGAAGCTGCTTTGGAAGAGCATCGCAAAACGACGCATTATCATCGCTGTGTTACCGAGTTGGAACCCATAATGACCGGCAGTCGAAGTAAAAAAATCTTTGAATGGGTGTTTCCTGAAACCGTTAAT","","","11990","MFAMLVEINIKEGKELEFLDVFERNHIGTRQEPGNLRFDVLRDPEIRTRFYAYEVYVNEAALEEHRKTTHYHRCVTELEPIMTGSRSKKIFEWVFPETVN","1508940","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR007138
Domain
Antibiotic biosynthesis monooxygenase
PF03992\"[10-73]TABM
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.900\"[2-94]Tno description


","BeTs to 7 clades of COG1359COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG1359 is -o-------drlbcefgh-n-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 6.8e-20) to 2/2 blocks of the IPB003771 family, which is described as \"DUF176\". Interpro entry for IP:IPR003771. IPB003771A 8-42 8.4e-09 IPB003771B 50-85 1.4e-09","Residues 1 to 96 match (8e-41) PD:PD020128 which is described as COMPLETE PROTEOME PLASMID INNER CC2132 MLL2956 ATU3160 RSC2595 ATU4528 RA1082 ","","","","","","","","","","","","Wed Jan 15 15:20:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02215 is paralogously related to AA00343 (2e-04).","","","","","","Residues 10 to 73 (E-value = 6.5e-20) place AA02215 in the ABM family which is described as Antibiotic biosynthesis monooxygenase (PF03992)","","","","","","","","1","","","" "AA02217","1509895","1509275","621","ATGTGCACCCGCGGTATTTTGCGTAGCGTCGTGCCGCCCTCCACCCGCAAACCTGTTGTGTTGCGTTCATCCGGTGCCAATTCGATTTTGACTGAATTATCCAACGAAGCGGTGGCGGTGTGTGTGGAAGATGCTTTGCGCCTGAATGTATCCGCCATGGCGGCACAGGTGTATATCGGTTCGCAACATGAACATCAATCCATTAAAAATATTATTCAGTTGGTGGATCAGGGGACGCGTTACGGTATGCCGACCATGGCGGTAACGGGCGTAGGTAAAGATATGGCGCGGGATCAGCGCTATTTTTCCTTGGCAACCCGTATCGCGGCGGAAATGGGTGCGCATATCATCAAAACCTATTATGTGGATAAAGGCTTTGAACGTGTAACTGCCGGTTGCCCGGTACCGATTGTCATTGCCGGCGGTAAAAAACTCCCGGAACAAGAGGCGCTGGATATGTGCTACAAAGCCATTGATCAAGGGGCTTCCGGTGTGGATATGGGGCGTAATATCTTCCAATCCGACGCGCCGATTGCCATGTTAAAAGCGGTACATGCCATCGTTCACGGCGGTGAAAATGCAGAAAAAGCCTATCAATTATATCTGCATGAAAAAAATGCG","","","22361","MCTRGILRSVVPPSTRKPVVLRSSGANSILTELSNEAVAVCVEDALRLNVSAMAAQVYIGSQHEHQSIKNIIQLVDQGTRYGMPTMAVTGVGKDMARDQRYFSLATRIAAEMGAHIIKTYYVDKGFERVTAGCPVPIVIAGGKKLPEQEALDMCYKAIDQGASGVDMGRNIFQSDAPIAMLKAVHAIVHGGENAEKAYQLYLHEKNA","1509275","","deoxyribose-phosphate aldolase","Cytoplasm","","
InterPro
IPR002915
Family
Deoxyribose-phosphate aldolase/phospho-2-dehydro-3-deoxyheptonate aldolase
PF01791\"[57-174]TDeoC
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[1-200]Tno description


","BeTs to 9 clades of COG1830COG name: DhnA-type fructose-1,6-bisphosphate aldolase and related enzymesFunctional Class: GThe phylogenetic pattern of COG1830 is aom-kz-q------e--h---j-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-15) to 3/3 blocks of the IPB002915 family, which is described as \"Deoxyribose-phosphate aldolase\". Interpro entry for IP:IPR002915. IPB002915A 32-52 6.7 IPB002915B 82-115 8.3e-06 IPB002915C 137-163 2.2e-06","Residues 1 to 199 match (5e-103) PD:PD008351 which is described as ALDOLASE PROTEOME COMPLETE BASE SCHIFF LYASE 4.2.1.- FRUCTOSE-BISPHOSPHATE I FBP ","","","","","","","","","","","","Wed Jan 29 13:37:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02217 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 27 to 189 (E-value = 3.7e-05) place AA02217 in the DeoC family which is described as Deoxyribose-phosphate aldolase (PF01791)","","","","","Galperin MY, Aravind L, Koonin EV.Aldolases of the DhnA family: a possible solution to the problem of pentose and hexose biosynthesis in archaea.FEMS Microbiol Lett. 2000 Feb 15;183(2):259-64.PMID: 10675594Sgarrella F, Poddie FP, Meloni MA, Sciola L, Pippia P, Tozzi MG.Channelling of deoxyribose moiety of exogenous DNA into carbohydrate metabolism: role of deoxyriboaldolase.Comp Biochem Physiol B Biochem Mol Biol. 1997 Jun;117(2):253-7.PMID: 9226884 Stura EA, Ghosh S, Garcia-Junceda E, Chen L, Wong CH, Wilson IA.Crystallization and preliminary crystallographic data for class I deoxyribose-5-phosphate aldolase from Escherichia coli: anapplication of reverse screening.Proteins. 1995 May;22(1):67-72.PMID: 7675789 Sgarrella F, Del Corso A, Tozzi MG, Camici M.Deoxyribose 5-phosphate aldolase of Bacillus cereus: purification and properties.Biochim Biophys Acta. 1992 Jan 9;1118(2):130-3.PMID: 1730028","","Wed Jan 29 13:37:06 2003","1","","","" "AA02218","1510146","1509898","249","ATGGCAGATTTAGATGACATCAGAGACGGTAAAGATTTCGGTTTGGATCGACCGCAAACCAATCAGGCGTTTTATTTAAAAGGTGCCGGCGCGTTGGATTGGGGAATGCAATCCCGTTTGGCGAATATTTTTAATCCGAAAACCGGCAGAACTATTATGCTGGCGTTCGACCATGGTTACTTCCAAGGGCCGACTACGGGGCTGGAACGTATTGATCTGCACATCGCCCCGTTATTTGAATATACCGAC","","","9335","MADLDDIRDGKDFGLDRPQTNQAFYLKGAGALDWGMQSRLANIFNPKTGRTIMLAFDHGYFQGPTTGLERIDLHIAPLFEYTD","1509898","","deoxyribose-phosphate aldolase (fragment?)","Cytoplasm","","
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[34-79]Tno description


","No hits to the COGs database.","","Residues 1 to 34 match (2e-09) PD:PD094876 which is described as COMPLETE PROTEOME ALDOLASE BASE SCHIFF LYASE 4.2.1.- YNEB FRUCTOSE-16-BISPHOSPHATE ORF ","","","","","","","","","","","","Wed Jan 29 13:40:05 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02218 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Galperin MY, Aravind L, Koonin EV. Aldolases of the DhnA family: a possible solution to the problem of pentose and hexose biosynthesis inarchaea. FEMS Microbiol Lett. 2000 Feb 15;183(2):259-64. PMID: 10675594 Sgarrella F, Poddie FP, Meloni MA, Sciola L, Pippia P, Tozzi MG. Channelling of deoxyribose moiety of exogenous DNA into carbohydrate metabolism: role of deoxyriboaldolase. Comp Biochem Physiol B Biochem Mol Biol. 1997 Jun;117(2):253-7. PMID: 9226884 Stura EA, Ghosh S, Garcia-Junceda E, Chen L, Wong CH, Wilson IA. Crystallization and preliminary crystallographic data for class I deoxyribose-5-phosphate aldolase fromEscherichia coli: an application of reverse screening. Proteins. 1995 May;22(1):67-72. PMID: 7675789 Sgarrella F, Del Corso A, Tozzi MG, Camici M. Deoxyribose 5-phosphate aldolase of Bacillus cereus: purification and properties. Biochim Biophys Acta. 1992 Jan 9;1118(2):130-3. PMID: 1730028","","Wed Jan 29 13:40:05 2003","1","","","" "AA02219","1511267","1510173","1095","ATGAAAACGCGTGTAAAATTATTCACAAACTCGATCTCTCGTTTGTTCACCCCTAACGGGGCCGTTGGCAAAGCCAACGTTCAAAAAACGCCGTTTTTTGTGACCGCACTTTCCGTGTTACTCGGTTTATCCGTTGTGGCGACGGCACAGTCAGCTGACCGTATCGCCTTTATTCCTAAACTGGTAGGCGTCGGCTTCTTTACCAGTGGCGGGCAAGGTGCTACCGAAATGGGAAAAACCTTGAGCGTAGATGTCACTTATGATGGTCCGACAGAACCGAGCGTGCCCAATCAGGTGCAACTGATCAATAACTTCGTGAACCAAGGCTACAACGCGATTGTAGTGTCGGCGGTTTCCCCGGACGGTTTATGTTCTACTTTGCAACGCGCCATGAAACGCGGTGTAAAAGTATTGACTTGGGACTCCGACACCAAACCGGAATGCCGTAGTCACTATATCAACCAAGGCACACCGGAACAGTTAGGTTCTATGTTGGTAGATATGGCGGCAAACCAAATCAGCAAACCGAAAGCCAAAGTGGCGTTTTTCTATTCCAGCCCGACGGTCACCGACCAAAATCAATGGGTGAAAGAAGCTAAAGCGAAAATTGCCAAAGATCATCCGGAATGGGAAATTGTAATCACTCAATTTGGTTATAACGACGCTATTAAATCCCTGCAAACCGCCGAAAGCATTTTGAAAGCCTACCCTGATTTAGATGCCATTATCGCACCGGATGCCAACGCATTACCGGCGGCTGCACAGGCGGCGGAAAATCTGAAAGTCAATTCCGTGGTTATTGTTGGGTTTAGTACCCCGAATGTGATGCGCCCTTATGTGAAACGCGGCACGGTGAAACAATTCGGTTTATGGGATGTAGTGCAACAAGGCAAAATTTCTGTGGCTGCCGCCAATGCCTTATTGAAAGGTGAAAAATTAAATGTGGGCGATAAATTGAACGTGCAAGGTATCGGCACGATTGAAGTCTCGCCGAACAAAGTACAAGGCTACGAATATGAAGCGGACGGCAACGGCATTATTTTATTGCCTGAACGCGTGGTATTCACCAAAGACAATATCGACAACTACAATTTC","","","39635","MKTRVKLFTNSISRLFTPNGAVGKANVQKTPFFVTALSVLLGLSVVATAQSADRIAFIPKLVGVGFFTSGGQGATEMGKTLSVDVTYDGPTEPSVPNQVQLINNFVNQGYNAIVVSAVSPDGLCSTLQRAMKRGVKVLTWDSDTKPECRSHYINQGTPEQLGSMLVDMAANQISKPKAKVAFFYSSPTVTDQNQWVKEAKAKIAKDHPEWEIVITQFGYNDAIKSLQTAESILKAYPDLDAIIAPDANALPAAAQAAENLKVNSVVIVGFSTPNVMRPYVKRGTVKQFGLWDVVQQGKISVAAANALLKGEKLNVGDKLNVQGIGTIEVSPNKVQGYEYEADGNGIILLPERVVFTKDNIDNYNF","1510173","","LACI-type transcriptional regulator","Periplasm","","
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2300\"[52-199]Tno description
signalp\"[1-49]?signal-peptide
tmhmm\"[32-52]?transmembrane_regions


","BeTs to 4 clades of COG1879COG name: Periplasmic sugar-binding proteinsFunctional Class: GThe phylogenetic pattern of COG1879 is --------v-rlb-efgh---j--t-Number of proteins in this genome belonging to this COG is","","Residues 51 to 153 match (3e-07) PD:PD562605 which is described as ABC PROTEOME COMPLETE PERIPLASMIC TRANSPORTER SUGAR-BINDING BINDING SUGAR TRANSPORTER PLASMID ","","","","","","","","","","","","Wed Jan 15 16:16:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02219 is paralogously related to AA00932 (2e-14), AA01953 (3e-11), AA00209 (4e-08) and AA02106 (4e-04).","","","","","","","","","","","","","","1","","","" "AA02220","1512296","1511295","1002","ATGTTGACGTTGAAAAGATACGGCTGGGAATTGACGTTATTCTGTTTGGTCATCATTGAAATTCTCGGTTTCGGCGCTTTCAATCCGCGTATGCTGGATTTAAACGTGCTGCTTTACAGCACCAGCGATTTTATTTATATCGGTATGCTTGCCTTGCCGTTGACCATGATTATCGTCAGTGGCGGCATGGATATTTCCTTCGGCTCCACCGTCGGCTTATGTGCTATTACCTTGGGTGTGTTGTTTAAAGCCGATGTGCCGTTGATATTGGCGATTCCGTTAACTTTTGTTGCTGGCATATTATGCGGTTTGATTAATGCCGGATTGATTCTCTACACCAAAGTGAATCCATTGGTGATCACCTTAGGCACTATGTACCTATTCGGCGGTGGTGCGTTGTTGCTGTCCGGTTTTGCCGGCGCGACAGGTTATGAAGGCATCGGTGGCTTTCCTGATGCGTTGCTGGACTTCGCCAATCAAACCTTATTCGGCATTCCGACGCCGATCCTGTATTTTCTGTTAATGACGCTGATCTTTTGGTTATTAATGCACAAAACCACCATCGGCAGAAGCACGTTTTTAATCGGGCAAAGTGAACGCACTTCCCGTTACAGCGCCGTGCCGATTCGTTGCACATTATTATTGATTTATTCCTTTATTGGCGTTATTGCTGCGTTTGTGGCGGTGTTGCTGGTGTCTTATTTCGGTTCCGCCCGCTCCGACTTAGGCAGTTCCCTGCTGATGCCGGTATTGACCGCCGTGGTGTTGGGCGGTGCCAATATCTATGGCGGAGCCGGTTCCATTATCGGCACGGCGATTGCCGCCATGCTCATCGGTTATTTGCAACAAGGATTGCAAATGATCGGTATTCCCAATGAAATTTCCGGTGCTTTATCCGGCGCCTTACTTATTATCGTGTTAAGCGGCAAGTCCGTCAGTTTGCATTATGGTGCTATTGTGCAATGGGTTCGTCGGCGAACCGAACGTCAGGCAGCAGTAGAT","","","35457","MLTLKRYGWELTLFCLVIIEILGFGAFNPRMLDLNVLLYSTSDFIYIGMLALPLTMIIVSGGMDISFGSTVGLCAITLGVLFKADVPLILAIPLTFVAGILCGLINAGLILYTKVNPLVITLGTMYLFGGGALLLSGFAGATGYEGIGGFPDALLDFANQTLFGIPTPILYFLLMTLIFWLLMHKTTIGRSTFLIGQSERTSRYSAVPIRCTLLLIYSFIGVIAAFVAVLLVSYFGSARSDLGSSLLMPVLTAVVLGGANIYGGAGSIIGTAIAAMLIGYLQQGLQMIGIPNEISGALSGALLIIVLSGKSVSLHYGAIVQWVRRRTERQAAVD","1511295","[FUNCTION] Probably part of a binding-protein-dependent transport system ego; ydeYZ. Probably responsible for the translocation of the substrate across the membrane. ","ABC transport system permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR001851
Family
Bacterial inner-membrane translocator
PF02653\"[36-307]TBPD_transp_2
noIPR
unintegrated
unintegrated
signalp\"[1-25]?signal-peptide
tmhmm\"[10-28]?\"[42-60]?\"[62-82]?\"[88-108]?\"[118-138]?\"[162-182]?\"[213-235]?\"[249-269]?\"[271-291]?\"[297-319]?transmembrane_regions


","BeTs to 6 clades of COG1172COG name: Ribose/xylose/arabinose/galactoside ABC-type transport systems, permease componentsFunctional Class: GThe phylogenetic pattern of COG1172 is --------v-rlb-efgh---j--t-Number of proteins in this genome belonging to this COG is","","Residues 276 to 326 match (9e-10) PD:PD409969 which is described as COMPLETE PROTEOME PERMEASE ABC SUGAR TRANSPORTER TRANSPORTER MEMBRANE SYSTEM PLASMID ","","","","","","","","","","","Wed Jan 15 16:40:39 2003","Wed Jan 15 16:34:13 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02220 is paralogously related to AA00208 (1e-32), AA02224 (1e-28), AA02785 (1e-27), AA00753 (4e-27), AA01457 (2e-21), AA00936 (3e-20) and AA00935 (7e-11).","","","","","","Residues 36 to 307 (E-value = 1.6e-67) place AA02220 in the BPD_transp_2 family which is described as Branched-chain amino acid transport system / permease component (PF02653)","","","","","","","","1","","","" "AA02222","1512429","1512313","117","TTGGTGTTTGACGGACGGATTCGCGTGATGATCGCCAATAATTTGAAATTACAACGTTATGCCCGTTTTCTGAAAGATGAAAATAGCACGGGCGTTGATATAAAAGTGCGGTCGAAA","","","4548","LVFDGRIRVMIANNLKLQRYARFLKDENSTGVDIKVRSK","1512313","","conserved hypothetical protein","Cytoplasm","This sequence is similar to gi15603140, an unknown from Pasteurella multocida.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:12:29 2004","Wed Feb 25 15:12:29 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02222 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:11:56 2004","","","","","","","","","","","","","1","","","" "AA02224","1513342","1512422","921","ATGATGGGAAAATTGATGCTGAAACTGATTCAGGATAATCGTGAACTGACCATTCTTATTGCCATTGGCTTGTTATTTTTACTGTTAGGTTTTGTCGGAAACGGCTTTCATCTGCAAACGTTAAGCATGGTGTTTAATTCCGCGCAAATCGTGATTTTGCTGGCGATTGGCGCCACTTTCGTCATTTTAACCCGCAACATCGACGTGTCCGTCGGTTCTACCATGGGGCTTTGTGCGGTCATTGTCGGCAGCTTGTTAAACGCCGGTTATGGTTTAGTCTCCGCTTTTCTTATTACTTTATGCTGTGGCTTGGCGGCGGGATTATTAAACGGTGTATTGGTAACCACGTTACGCATTCCCGCCATTGTCACCACCTTGGGAACGCTGGGGTTATATAAAGGCATTATGTTGTTGATTACCGGTGGGAAATGGATTGAAGGCTTGCCGCAAGAATTGAAAATGCTCTCCGAACCGGTTTTTTTACATATTTCGCCTATCGGTTGGATCTTGCTTATCCTGATTCTCGCTACGTATTATTTCTTAACGAAACTCCCCGCCGGACGTAATTTTTATGCCGTGGGGGATAATCTGCAAGGGGCGCTGCAACTAGGCGTGCGTATTGATCAGGTGAGAATCGTGGCTTTCGCCATAAACGGCATGATGGCGGCAATTGCCGGGATTGTTTTTGCCTCGCAAATCGGTTTTGTGCCGAATTCTACCGGCAACGGCTTGGAAATGAAGGCGATCGCTGCCTGCGTACTGGGCGGGATCAGCTTGCTCGGCGGCACGGGGAATTTAATCGGCGCGGTGTTGGGCGCCTATTTCCTGATTCAAATCGATACGATTTTGGTGCTGCTTAAAGTGCCTGCCTATTTGGAACAATTTTGTTGCCGGTATCGTACTGCTCGCCGTATTGGTGTT","","","32531","MMGKLMLKLIQDNRELTILIAIGLLFLLLGFVGNGFHLQTLSMVFNSAQIVILLAIGATFVILTRNIDVSVGSTMGLCAVIVGSLLNAGYGLVSAFLITLCCGLAAGLLNGVLVTTLRIPAIVTTLGTLGLYKGIMLLITGGKWIEGLPQELKMLSEPVFLHISPIGWILLILILATYYFLTKLPAGRNFYAVGDNLQGALQLGVRIDQVRIVAFAINGMMAAIAGIVFASQIGFVPNSTGNGLEMKAIAACVLGGISLLGGTGNLIGAVLGAYFLIQIDTILVLLKVPAYLEQFCCRYRTARRIGV","1512422","[FUNCTION] Probably part of a binding-protein-dependenttransport system ego; ydeYZ. Probably responsible for thetranslocation of the substrate across the membrane. ","ABC transport system permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR001851
Family
Bacterial inner-membrane translocator
PF02653\"[40-291]TBPD_transp_2
noIPR
unintegrated
unintegrated
signalp\"[1-35]?signal-peptide
tmhmm\"[15-33]?\"[43-63]?\"[68-88]?\"[94-114]?\"[119-139]?\"[161-181]?\"[212-234]?\"[248-277]?transmembrane_regions


","BeTs to 7 clades of COG1172COG name: Ribose/xylose/arabinose/galactoside ABC-type transport systems, permease componentsFunctional Class: GThe phylogenetic pattern of COG1172 is --------v-rlb-efgh---j--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.7e-08) to 2/2 blocks of the IPB001851 family, which is described as \"Binding-system dependent bacterial transporters (araH, livH/limM families)\". Interpro entry for IP:IPR001851. IPB001851A 186-200 0.029 IPB001851B 245-256 0.00024","Residues 39 to 81 match (3e-10) PD:PD385083 which is described as COMPLETE PROTEOME PERMEASE ABC SUGAR TRANSPORTER MEMBRANE TRANSPORTER SYSTEM PLASMID ","","","","","","","","","","","Wed Jan 15 16:43:16 2003","Wed Jan 15 16:43:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02224 is paralogously related to AA00208 (7e-34), AA02785 (2e-32), AA01457 (4e-30), AA02220 (9e-29), AA00753 (3e-28), AA00936 (2e-20) and AA00935 (9e-13).","","","","","","Residues 40 to 292 (E-value = 1.8e-37) place AA02224 in the BPD_transp_2 family which is described as Branched-chain amino acid transport system / permease component (PF02653)","","","","","","","","1","","","" "AA02225","1514652","1513342","1311","GTGCGACAAAATAAGCTTTCTCCGAATAAAGCCCATCAGCTAGGTATTTATTTGGTGCCGCAGGAACCGCTGTTATTTCCGAACTTAACGGTGAAGGAAAATATTTTATTCGGCTTAGCCCGTCATGAAAAAACATCGGAAAAACTGACCGCACTTTTAGCTGAACTGAACTCCCATTTAAAGCTGGATATGCCCGCGGGTTCGTTGGAAGTTGCCGATCAACAGCTGGTGGAAATCATGCGTGGCCTTATGCGTAATGCGTCTATTCTGATTCTGGACGAACCCACCGCCTCTTTAACGCCAATTGAAACGGAGAACCTGTTTAATAAAATTCGTTCGTTATTGGAAAAGGGTGTGGGCATTGTCTTCATTTCTCACAAACTGCCCGAAGTGTGGCAGATTTCTCATCGTATTAGCGTCATGCGCGACGGCTATATTGCACTAACCGGCAGTACTGCCGAGTTGAATAAAGACGATGTGATTACCGCCATCACGCCGAAGGCGAAAAATGCCCAATTAACGGAAAGCCAAAAATTATGGCTGGCGTTGCCGGGACATAACCGTGTGAAAGCTACCGATAAGCCGATTTTGCAGGTGCAGGATTTGACGGGCGAAGGATTTAAAAATGTCACTTTTGATATTTATCCCGGTGAAATTTTAGGCTTGGCGGGCGTGGTTGGCGCAGGGCGAACCGAATTGGCGGAAACCTTATATGGCTCACGTAAACAAAAGTGCGGTCAGATTTTCCTCGATAATCAGGAAATCAGCGGGTACGATATTAAAGATCGCCTACACCAAGGCATTGTTTACTTACCGGAAGATCGTCAGGCTTCCGGATTATATCTGGATTCGCCGTTAACCTGGAATGTCTGCGGGTTGACCTATAACGATATGGGATTCTGGCTGGACACGACGAAGGAAAGCGCTATTCTGGAGCGCTATTATCGCGCTATCGGCATTAAGTTCAGTGACGAGCGACAGGCGGTCAGAACGCTGTCCGGCGGGAATCAGCAAAAAGTGTTGATTGCCAAGTGTCTGGAAGCGGATCCGGCGTTATTGATTGTGGACGAGCCGACACGCGGTGTGGATGTGGGGGCACGTGCGGATATTTATCAGCTCATCAAAAATATCTCCAAGCAAAATGTGGCGGTGCTGTTTATTTCTTCCGATTTAGAAGAAATTGAACATATGTCCGATAGAGTATTGGTCATGCATGCGGGCAAATTAGCCATTCTTTGGTCGGTGAGGCGATTAATACCAACAATATCATGCAAATGGCGTTCGGCAGTACGCACGGGTAAGGAGAGACGA","","","48771","VRQNKLSPNKAHQLGIYLVPQEPLLFPNLTVKENILFGLARHEKTSEKLTALLAELNSHLKLDMPAGSLEVADQQLVEIMRGLMRNASILILDEPTASLTPIETENLFNKIRSLLEKGVGIVFISHKLPEVWQISHRISVMRDGYIALTGSTAELNKDDVITAITPKAKNAQLTESQKLWLALPGHNRVKATDKPILQVQDLTGEGFKNVTFDIYPGEILGLAGVVGAGRTELAETLYGSRKQKCGQIFLDNQEISGYDIKDRLHQGIVYLPEDRQASGLYLDSPLTWNVCGLTYNDMGFWLDTTKESAILERYYRAIGIKFSDERQAVRTLSGGNQQKVLIAKCLEADPALLIVDEPTRGVDVGARADIYQLIKNISKQNVAVLFISSDLEEIEHMSDRVLVMHAGKLAILWSVRRLIPTISCKWRSAVRTGKERR","1513342","[FUNCTION] Probably part of a binding-protein-dependenttransport system ego; ydeYZ. Probably responsible for thetranslocation of the substrate across the membrane. [FUNCTION] Part of the binding-protein-dependent transport system for ribose. Probably responsible for energy coupling to the transport system. ","ABC transporter ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[74-111]T\"[331-374]TQ9CLG1_PASMU_Q9CLG1;
PF00005\"[4-144]T\"[217-407]TABC_tran
PS50893\"[1-168]T\"[189-431]TABC_TRANSPORTER_2
PS00211\"[332-346]?ABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[216-408]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[4-172]T\"[190-419]Tno description
PTHR19222\"[7-240]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF12\"[7-240]TSUGAR ABC TRANSPORTER


","No hits to the COGs database.","Significant hit ( 3e-14) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 206-252 1e-06 IPB001140B 329-367 5.6e-05 IPB001140C 384-413 58","Residues 69 to 178 match (5e-07) PD:PD535848 which is described as ABC PROTEOME BINDING/ATPASE NUCLEOTIDE COMPLETE TRANSPORTER ","","","","","","","","","","","Wed Jan 15 16:47:25 2003","Wed Jan 15 16:47:25 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02225 is paralogously related to AA00207 (8e-64), AA02786 (4e-62), AA01456 (5e-60), AA00751 (6e-58), AA00933 (6e-23), AA00934 (5e-22), AA02140 (6e-19), AA02899 (3e-18), AA02320 (5e-18), AA02718 (2e-15), AA01820 (8e-15), AA02898 (1e-14), AA01645 (2e-14), AA01616 (3e-14), AA00415 (3e-14), AA02152 (7e-14), AA01568 (3e-13), AA01051 (5e-13), AA00700 (6e-13), AA02353 (8e-13), AA01684 (1e-12), AA01569 (4e-12), AA00858 (1e-11), AA01779 (7e-11), AA01524 (7e-11), AA02550 (1e-10), AA01656 (2e-10), AA02805 (2e-10), AA01422 (6e-10), AA02440 (2e-09), AA01867 (3e-09), AA02609 (5e-09), AA02324 (7e-09), AA01947 (9e-09), AA02080 (3e-08), AA01393 (3e-08), AA02573 (6e-08), AA00799 (6e-08), AA01961 (2e-07), AA02606 (3e-07), AA02484 (4e-07), AA02331 (6e-07), AA01509 (1e-06), AA01291 (2e-06), AA01757 (2e-06), AA01555 (3e-06), AA01824 (4e-06), AA00591 (4e-06), AA02146 (5e-06), AA01510 (9e-06), A02145 (3e-05), AA02642 (1e-04) and AA00061 (5e-04).","","","","","","Residues 217 to 407 (E-value = 2.3e-27) place AA02225 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Bell,A.W., Buckel,S.D., Groarke,J.M., Hope,J.N., Kingsley,D.H. and Hermodson,M.A. The nucleotide sequences of the rbsD, rbsA, and rbsC genes of Escherichia coli K12. J. Biol. Chem. 261 (17): 7652-7658 (1986) [PubMed: 3011793].Burland,V., Plunkett,G. III, Daniels,D.L. and Blattner,F.R. DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication. Genomics 16 (3): 551-561 (1993) [PubMed: 7686882].Buckel,S.D., Bell,A.W., Rao,J.K. and Hermodson,M.A. An analysis of the structure of the product of the rbsA gene of Escherichia coli K12. J. Biol. Chem. 261 (17): 7659-7662 (1986) [PubMed: 3086314].","","Wed Jan 15 16:47:25 2003","1","","","" "AA02226","1514866","1514642","225","ATGCAAACTCACATTTCAGAGCCAAAATGCTTAATATCCGCCCGAAACATCGGTAAGTCGTTTTCCGGCGTGGAAGTGCTGAAAGCCATTGATTTTTCCTTATATGCCGGTGAAGTGCACGCACTGCTCGGCGGTAACGGGGCGGGGAAATCCACGCTGATGAAAATTATCGCCGGCATTCAGCCGCAAGATAGCGGAGAACTGGAGGTTCGGGGTGCGACAAAA","","","7824","MQTHISEPKCLISARNIGKSFSGVEVLKAIDFSLYAGEVHALLGGNGAGKSTLMKIIAGIQPQDSGELEVRGATK","1514642","[FUNCTION] Probably part of a binding-protein-dependenttransport system ego; ydeYZ. Probably responsible for thetranslocation of the substrate across the membrane. ","ABC transporter ATP-binding protein","Cytoplasm, Inner membrane","","
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[5-72]Tno description
PTHR19222\"[12-72]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF12\"[12-72]TSUGAR ABC TRANSPORTER


","No hits to the COGs database.","Significant hit ( 4.1e-14) to 1/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 26-72 3.4e-14","Residues 27 to 72 match (1e-14) PD:PD000005 which is described as ATP-BINDING COMPLETE PROTEOME ABC TRANSPORTER TRANSPORTER PROBABLE TRANSMEMBRANE COMPONENT PLASMID ","","","","","","","","","","","Wed Jan 15 16:50:05 2003","Wed Jan 15 16:50:05 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02226 is paralogously related to AA02786 (1e-13), AA00207 (3e-12), AA00933 (3e-11), AA00751 (1e-10), AA01656 (2e-09), AA01524 (3e-09), AA01616 (8e-09), AA01456 (8e-09), AA02718 (1e-08), AA01051 (1e-08), AA02320 (7e-08), AA02484 (2e-07), AA01568 (2e-07), AA00700 (2e-07), AA02573 (3e-07), AA01422 (3e-07), AA02642 (3e-07), AA02440 (3e-07), AA02353 (3e-07), AA01645 (3e-07), A02145 (4e-07), AA02140 (4e-07), AA01824 (1e-06), AA01820 (1e-06), AA01555 (2e-06), AA02152 (3e-06), AA02080 (3e-06), AA02899 (4e-06), AA01867 (2e-05), AA00858 (7e-05), AA02331 (2e-04), AA01510 (2e-04), AA02550 (3e-04), AA01684 (3e-04), AA00591 (3e-04), AA02805 (4e-04), AA01961 (6e-04) and AA02609 (0.001).","","","","","","","","","","","","","","1","","","" "AA02228","1515121","1516071","951","ATGACGGATAATCAAGAAACGATCCAAAGTTTCGGCGAAGAAGAATTGTTGGCACGAATTGCCTGGTTTTATTATCACGATAACCTGACACAAAGCGAAATCGGCGACAGACTAAAACTGCCGCGTTTAAAAGTATCCAGGCTACTGGAAAAAGGGCGTCAGTCCGGCATTATTAAAGTGCAAATCAACTCCCGCTTTACCGGTTGTCTGGAACTGGAAGAAGTGCTACAACAACACTTCCGATTAAAGCATATACGTATTCTGCCAACGCTGGAACAACATGAAATCAATGAGCGATTAGGCGTCGGCGCGGCACAAATGCTGATGTCGTTGCTTAAACCGAATCAGATGCTGGCAATCGGTTTCGGCGACACCATTATGAAAACGCTGAAATACGCCAATGAATTCATCACACACAATGCAATTAAATTAATCACCTTATCGGGCGGTGTCGGAACTTATATGAAAGGTATCGGACAATTAGACGGTTCCTGCTCGGTAAGTATCATTCCCGCACCTTTGCGGGCGTCTTCAATTGAAGCGGCAAAACTATTCAAACGGGAAGCCTGTGTGCGCGATATTATGCTGGCGGCTTGTAGTGCCAATGCGGCAATCGTCGGTATCGGCGCCACCCGCCAAAAAGGACAGGCGACACTGCTCCGCTCCGGTTATATCACCGAAGAAAAACAACAAATTATTCGGAATCAGGGCGCAGTGGGCGATATTCTCGGTTATTTCATGCGTAAAGACGGCAGTTTACAACCGGATATGCCGTTACATGAGGAATTAATCAGCGTTTCGTTAGAAAATTTGAAAAAAATTCCGCATGTTATCGGTGTCGCCGGTGGTGAAGACAAAGTCGAAGCGATTTTAAGCGCATTACAGGGTAATCATATTAATTCATTGGTTACGGAAGAAAACACGGCTCGAATGATGTTGGCGCAGTTGGTT","","","35478","MTDNQETIQSFGEEELLARIAWFYYHDNLTQSEIGDRLKLPRLKVSRLLEKGRQSGIIKVQINSRFTGCLELEEVLQQHFRLKHIRILPTLEQHEINERLGVGAAQMLMSLLKPNQMLAIGFGDTIMKTLKYANEFITHNAIKLITLSGGVGTYMKGIGQLDGSCSVSIIPAPLRASSIEAAKLFKREACVRDIMLAACSANAAIVGIGATRQKGQATLLRSGYITEEKQQIIRNQGAVGDILGYFMRKDGSLQPDMPLHEELISVSLENLKKIPHVIGVAGGEDKVEAILSALQGNHINSLVTEENTARMMLAQLV","1516071","","regulatory protein, sorC family","Cytoplasm","","
InterPro
IPR007324
Domain
Putative sugar-binding region
PF04198\"[64-314]TSugar-bind


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Jan 15 16:52:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02228 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 64 to 314 (E-value = 2.8e-90) place AA02228 in the Sugar-bind family which is described as Putative sugar-binding domain (PF04198)","","","","","","","","1","","","" "AA02230","1516124","1517677","1554","ATGAACAATCAAGCTGTTTACCTGATGGCATTAGATGCCGGCACAGGAAGTGTTCGGGCGGTTATTTTTGATTTAGACGGTAATCAAATCGCCGCCGCTCAACGGGAATGGACGCACTTATCCGATCCCGATATTCCCGGTTCAATGGAATTTGATTTAGCCAATAATTGGCAGTTAACCTGCGATTGTATTCGTCAAGTATTGAATAAATCTCAAGTTCAGCCACAGCAAATTGCCGCCATTTCCACCTGTTCCATGCGTGAAGGAATCGTACTTTACGATGAGCATAAAACACCGATTTGGGCGTGTGGTAACGTAGATGCCCGTGCGGTGGAAGAAGTCAAAGAGCTAAAAACGCTACATAACTATACGTTTGAACAACAGCTGTATTCCGTCTCCGGTCAAACGTTGGCACTGAGCGCCGTTCCCCGCCTACTATGGCTGGCACATCATCGCCCCGATATTTATCGCCACACTAAAGCCATTTCCATGATCAGCGATTGGCTGGCATTTATGTTAAGCGGCGAACTGGCGGTGGAACCTTCCAATGCGGGCACGACCGGCATGTTGAACCTGACAACACGTCAATGGTCGCCGGAATTACTGGATATGGCGGGGTTAAATTCAAATATTCTGACGCCGATAAAAGAAACCGGTACGCGTTTAGGTGAAGTGACTTCAGAAGTTGCACAACAAACCGGTTTAATACAGGGCACACCGGTTGTGGTCGGCGGCGGGGACGTGCAGTTAGGTTGTATTGGTTTAGGCGTCACCGAGCCCGCTCAAGCGGCAGTTATCGGCGGTACGTTCTGGCAACAAGTGGTGAATTTACCGCAGGCGGTGACCGACCCGGAAATGAATGTACGTATTAACCCGCACGTTATCCCGCCGTTAGTACAGGCGGAATCCATTAGCTTTTTCACCAGATTAACCATGCGCTGGTTCCGTGATGCATTTTGCGAAGAAGAAAAGAGACTGGCGGAAAAACTGGGTACCGATGCTTATGCGTTGCTGGAACAAATGGCGGAACGCGTGCCCGTCGGCGCCAATGACGTGATCCCGATTTTCTCCGATGCCATGCATTTTAAAGCCTGGTATCACGCCGCACCGTCTTTTATTAATCTCTCTATCGATCCCGACAAATGCAACAAAGCCGTATTATTCCGCGCCTTGGAAGAAAATGCTGCTATCGTTTCTTCCTGCAATTTGGATCAGGTGCAAAAATTCTCAGGAGTTAAATTAACCTCCATTGTCTTTGCCGGCGGCGGGTCTAAAGGCAAATTATGGAGCCAGATCTTAGCCGATGTCACCGGATTAACGGTAAACATTCCGATTGTCAAAGAAGCTACAGCGCTGGGTTGTGCCATTGCCGCAGGCGTCGGAGTCGGCATTTATCCGACCTTAGCCGAGGCGGGGAAAAAACTGGTTAAATTTGAACGGCAACATCAACCGAATCCCGATAACTATGCTTTATACCAAGCTCACAAAGCACAATGGGCAGATATTTATAAAAAACAATTACAACTGGTTGATAGCGGATTAACTACTTCTTTG","","","56563","MNNQAVYLMALDAGTGSVRAVIFDLDGNQIAAAQREWTHLSDPDIPGSMEFDLANNWQLTCDCIRQVLNKSQVQPQQIAAISTCSMREGIVLYDEHKTPIWACGNVDARAVEEVKELKTLHNYTFEQQLYSVSGQTLALSAVPRLLWLAHHRPDIYRHTKAISMISDWLAFMLSGELAVEPSNAGTTGMLNLTTRQWSPELLDMAGLNSNILTPIKETGTRLGEVTSEVAQQTGLIQGTPVVVGGGDVQLGCIGLGVTEPAQAAVIGGTFWQQVVNLPQAVTDPEMNVRINPHVIPPLVQAESISFFTRLTMRWFRDAFCEEEKRLAEKLGTDAYALLEQMAERVPVGANDVIPIFSDAMHFKAWYHAAPSFINLSIDPDKCNKAVLFRALEENAAIVSSCNLDQVQKFSGVKLTSIVFAGGGSKGKLWSQILADVTGLTVNIPIVKEATALGCAIAAGVGVGIYPTLAEAGKKLVKFERQHQPNPDNYALYQAHKAQWADIYKKQLQLVDSGLTTSL","1517677","[PATHWAY] L-lyxose utilization.","sugar kinase","Cytoplasm","","
InterPro
IPR000577
Family
Carbohydrate kinase, FGGY
PTHR10196\"[57-509]TXYLULOSE KINASE
PF00370\"[7-254]TFGGY_N
PF02782\"[402-493]TFGGY_C
noIPR
unintegrated
unintegrated
PTHR10196:SF10\"[57-509]TXYLULOSE KINASE


","No hits to the COGs database.","Significant hit ( 1.2e-20) to 3/9 blocks of the IPB000577 family, which is described as \"Carbohydrate kinase, FGGY family\". Interpro entry for IP:IPR000577. IPB000577B 80-95 12 IPB000577E 177-215 9.9e-08 IPB000577I 417-453 6.9e-10","Residues 117 to 214 match (3e-07) PD:PD024458 which is described as KINASE PROTEOME COMPLETE RHAMNULOKINASE TRANSFERASE METABOLISM RHAMNOSE RHAMNULOSE L-FUCULOSE L-FUCULOKINASE ","","","","","Wed Feb 19 15:06:32 2003","","","","Wed Feb 19 15:06:32 2003","","Wed Jan 15 16:59:32 2003","Wed Feb 19 08:23:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02230 is paralogously related to AA01451 (2e-26), AA00937 (1e-14) and AA00938 (1e-04).","","","","","","Residues 257 to 493 (E-value = 2e-09) place AA02230 in the FGGY_C family which is described as FGGY family of carbohydrate kinases, C-terminal domain (PF02782)","","","","","Lokman,B.C., van Santen,P., Verdoes,J.C., Kruse,J., Leer,R.J., Posno,M. and Pouwels,P.H. Organization and characterization of three genes involved in D-xylose catabolism in Lactobacillus pentosus. Mol. Gen. Genet. 230 (1-2): 161-169 (1991) [PubMed: 1660563]. Wilhelm,M. and Hollenberg,C.P. Nucleotide sequence of the Bacillus subtilis xylose isomerase gene: extensive homology between the Bacillus and Escherichia coli enzyme. Nucleic Acids Res. 13 (15): 5717-5722 (1985) [PubMed: 2994009].Sanchez,J.C., Gimenez,R., Schneider,A., Fessner,W.D., Baldoma,L., Aguilar,J. and Badia,J. Activation of a cryptic gene encoding a kinase for L-xylulose opens a new pathway for the utilization of L-lyxose by Escherichia coli. J. Biol. Chem. 269 (47): 29665-29669 (1994) [PubMed: 7961955].Reizer,J., Charbit,A., Reizer,A. and Saier,M.H.Jr. Novel phosphotransferases system genes revealed by bacterial genome analysis: operons encoding homologues of sugar-specific permeasedomains of the phosphotransferase system and pentose catabolicenzymes. Genome Sci. Technol. 1, 53-75 (1996)","","Wed Feb 19 08:23:24 2003","1","","","" "AA02231","1518515","1517790","726","ATGAGTAGTTTTTTTGTTACCGGTACGGACACCGATGTAGGTAAAACTGTTGTTAGTCGCGCGATTATGCAGGCTTTACAGAAAATCGGCATACAGGTCGTCGGTTATAAGCCAATTGCATTCGGTCAAGAAGACGTGATTTATCCCGACAGCCAAAAGCAAACTGCCGGCGATTATGACAGGAAAGACAATCCCGACGTATTAACGTTAATAAACAGTACTAAAGAAAAAGTGCATTACGAAGACGTCAACAGCTATACCTTCCGGCATTCCATGCCCATTTTGAATGAAAGTTGCAAACGTGTTCAAATTAATAAGCTAAATGTGGATTTAGCACGTTTGTGTTCCCGTTACCAATCTGTTTTAGTAGAAGGCGCCTTCGGTTGGCTAACACCGATCAATAAGGATTACAGTTTTGCCGATTGGGCCGGTGAGCAAAAAATGCCTGTTGTTTTAGTAGTGGGTTTTAAAGAGGGGTGCATTAATCACACATTATTAACCGTGCAATCGATTCTTGAACGTGGTTTACCGCTGCTCGGCTGGGTCGCAAACCGAATAAACCCGGGTTTAGGACATTATGCCGAAGTGATCGAAACCCTAAAACAAAAAGTCGATGCGCCACTGCTGGGTGAGGTTTCTTATATTCACAAACCGGAAGAACAAGATCTCAGCCGTTTCATCACCGACATCGACCGCTTGACGTATATGCAAACGGAACCGGTGGCA","","","27212","MSSFFVTGTDTDVGKTVVSRAIMQALQKIGIQVVGYKPIAFGQEDVIYPDSQKQTAGDYDRKDNPDVLTLINSTKEKVHYEDVNSYTFRHSMPILNESCKRVQINKLNVDLARLCSRYQSVLVEGAFGWLTPINKDYSFADWAGEQKMPVVLVVGFKEGCINHTLLTVQSILERGLPLLGWVANRINPGLGHYAEVIETLKQKVDAPLLGEVSYIHKPEEQDLSRFITDIDRLTYMQTEPVA","1517790","[PATHWAY] Bioconversion of pimelate into dethiobiotin.","probable dethiobiotin synthetase 1","Cytoplasm","","
InterPro
IPR002586
Domain
Cobyrinic acid a,c-diamide synthase
PF01656\"[4-225]TCbiA
InterPro
IPR004472
Family
Dethiobiotin synthase
PIRSF006755\"[1-239]TDethiobiotin synthetase
TIGR00347\"[5-184]TbioD: dethiobiotin synthase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[1-233]Tno description
PTHR21343\"[3-237]TDETHIOBIOTIN SYNTHETASE


","BeTs to 13 clades of COG0132COG name: Dethiobiotin synthetaseFunctional Class: HThe phylogenetic pattern of COG0132 is --m---yq--r-bcefghsnuj-i--Number of proteins in this genome belonging to this COG is","","Residues 39 to 96 match (5e-12) PD:PD485359 which is described as DETHIOBIOTIN COMPLETE SYNTHETASE PROTEOME PROBABLE LIGASE BIOTIN DTBS ATP-BINDING BIOD1 ","","","","","","","","","","","Wed Jan 15 17:02:45 2003","Wed Jan 15 17:02:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02231 is paralogously related to AA00276 (1e-10).","","","","","","Residues 3 to 220 (E-value = 4.2e-32) place AA02231 in the CbiA family which is described as Cobyrinic acid a,c-diamide synthase (PF01656)","","","","","","","","1","","","" "AA02232","1519821","1518595","1227","ATGAAAAAGGAAGACAAAACCCCATCTCGTTTAATTCAGCTTGGTAAAATTTACCGTTTAATAGAGCAGTTTGAAGAAATCTCACGTATTGAATTATCAAAACTTTCCGGTTTAGCGCCGGCATCCATTACATCGTTGAGCCGTTCCCTCATTGAAAAACGATTGATTATGGAAAAAACCTCAAGAAATACCGACAACCGCGGACGTCCTGCCATTGCCCTGTGTGTTTCGCCGTTTTATTGGCAAGCTTTATGTGCCACGTTAGTGGAGGATCGGTTTGAAATTATTTTGAGTGAATTGGACGGCGTAATTATTGAACAAAGCGTTTTCCCCTTGCAAAAAGATGATTTAGAATGTCTGGATAAATTTCTGGTAAAAAGCGTCAAACAATTTCTGGCTGAAACCCACTCACTTGCCCGCCCGATAACCTTTTCCGTTACCGTGGGCGGTGAATTGGATAAAAATGGTTATTTAATTAAACTGGGATGTACGAAATTCGCCCATTTGGATCTGAAATCCTTGTTTACACCGTATTTCAATATTCCGATTTTAATTGCCGAATATTTCAAAACCTGGTTATTGGCGGAATCCACCTTGGGTAATGTGATCAACTGTGATGATGTACTGTTTTTACAGTTGGACGATGAAATTAACCTCAGCGTGTTATCAGAAGGGGAGCTGTTATTTAGCAGGGAACAGGACAAAATCAATATTAATCATTTGATTGTGCCGCGCTTAAACGAGCTTCAAGCGCTCATTAATCACGATTTACCGGAAGTTGAGCGTTACCAGGTACAACATCAAGTCACCCATCGGGCGATTGCACAGTTTATTGATGCCCTTTATCCGAATCGTGTTTTCAGCAACAATTCCGAGAAAATGAATTTCCTGTGTGAACAGATTCAATTAAAAGATAAAAACGCGTTGCGGATTATTGAACATATTACCGATTGCCTGGCTTATATCTTAATGAATCTGGTTCATATTTTTTCCGCGCGGCGGGTGATGCTGAACTCCAGCTTGCTGCAACTGAAAGATTTCCTGCTCGAACAGCTTAATCGTAAATTAAAATCCTATTTAGTCGATAACATCAGCACAGTTTCGGTGATTGCCGGCAAATATGAATGGAATAGCCCGATCGTCGCTGCTTCTGCGATTAAGCAGGGCATATATGACGGAAGTTTGCTGACTTCGTTGGTAAAACAAGAAGAAAACATCATAAATTTC","","","46751","MKKEDKTPSRLIQLGKIYRLIEQFEEISRIELSKLSGLAPASITSLSRSLIEKRLIMEKTSRNTDNRGRPAIALCVSPFYWQALCATLVEDRFEIILSELDGVIIEQSVFPLQKDDLECLDKFLVKSVKQFLAETHSLARPITFSVTVGGELDKNGYLIKLGCTKFAHLDLKSLFTPYFNIPILIAEYFKTWLLAESTLGNVINCDDVLFLQLDDEINLSVLSEGELLFSREQDKININHLIVPRLNELQALINHDLPEVERYQVQHQVTHRAIAQFIDALYPNRVFSNNSEKMNFLCEQIQLKDKNALRIIEHITDCLAYILMNLVHIFSARRVMLNSSLLQLKDFLLEQLNRKLKSYLVDNISTVSVIAGKYEWNSPIVAASAIKQGIYDGSLLTSLVKQEENIINF","1518595","[FUNCTION] May be a regulator in specific sugar metabolism. May influence the rate of glucose uptake or glycolysis in cells inthe rich medium. ","NagC-like transcriptional regulator","Cytoplasm","","
noIPR
unintegrated
unintegrated
PTHR18964\"[305-392]TROK FAMILY
PTHR18964:SF37\"[305-392]TGLUCOSE KINASE


","BeTs to 6 clades of COG1940COG name: Transcriptional regulatorsFunctional Class: KThe phylogenetic pattern of COG1940 is ao-p-z-qvdrlbce-gh---j--t-Number of proteins in this genome belonging to this COG is","","Residues 297 to 386 match (3e-11) PD:PD001669 which is described as COMPLETE PROTEOME KINASE TRANSCRIPTIONAL REPRESSOR FAMILY REGULATOR ROK GLUCOSE XYLOSE ","","","","","","","","","","","Wed Jan 15 17:39:31 2003","Fri Jan 24 14:06:30 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02232 is paralogously related to AA01880 (1e-25).","","","","","","","","","","","Hosono,K., Kakuda,H. and Ichihara,S. Decreasing accumulation of acetate in a rich medium by Escherichia coli on introduction of genes on a multicopy plasmid. Biosci. Biotechnol. Biochem. 59 (2): 256-261 (1995) [PubMed: 7766024].","","Wed Jan 15 17:39:31 2003","1","","","" "AA02233","1520017","1521417","1401","ATGACAAAAATTGCATCAATTGTAAATGTGCTGCAAGGCAAAATTGCAATTGGCGAAAAAGTGACTGTGCGCGGCTGGGTGCGCACCCGTCGCGACTCCAAAGCAGGCCTATCCTTTCTTGCCGTTTATGACGGTTCTTGCTTCGCACCCATTCAAGCTATTGTAAATAATGACATTGCCAATTATGAATCTGAAGTTTTACGCTTAACGGCGGGTTGTTCCGTGGTTGTCGCCGGCACCGTAGTCGAATCGCCGGCAGAAGGTCAGGCAGTAGAATTACAAGCGGAAAAAGTGGAAGTCACCGGTTGGGTAGAAGATCCGGAAACTTACCCGATGGCGGCAAAACGTCACTCTATCGAATATTTACGCGAAGTGGCGCACCTACGCCCGCGCACCAATATTATCGGTGCAGTTGCCCGTGTTCGTCATTGCTTGGCACAAGCCATTCATCGTTTCTTTCATGAACAAGGTTTCTACTGGGTTGCCACCCCACTAATCACCGCTTCCGATACCGAAGGTGCGGGTGAAATGTTCCGCGTTTCCACCTTAGATTTAGAAAATTTGCCACGTACCGACAAAGGTGCGGTGGATTTTAGCCAGGATTTCTTCGGTAAAGAATCTTTCCTCACAGTGTCCGGTCAGTTAAACGGTGAAACCTATGCTTGCGCATTAAGTAAAATTTACACCTTCGGGCCAACCTTCCGCGCTGAAAACTCCAACACAACCCGTCACTTAGCGGAATTCTGGATGATTGAACCGGAAGTGGCATTCGCCACGCTTGCCGATAATGCCAAACTTGCCGAAGATATGTTGAAATACGTCTTCCGTGCCGTATTGGCAGAACGTCGCGATGATTTGGAATTCTTTGCCAAACACGTTGACGGCGATGTGATTAATCGTTTGGAACGTTTCATTAACTCCGATTTCGCACAAGTGGATTACACCGACGCCATTGAGATTTTACTGAAATCCGGTAAAACCTTTGAATTCCCGGTTTCTTGGGGCATTGACCTTTCCTCCGAACATGAGCGCTATTTGGCAGAAGATTATTTCAAATCCCCTGTTGTGGTGAAAAACTATCCGAAAGAAATTAAAGCCTTCTATATGCGCTTAAATGACGATGGACAAACCGTTGCGGCAATGGATGTTTTAGCGCCGGGCATTGGTGAAATTATCGGCGGTTCGCAACGTGAAGAACGTTTAGACGTATTAGACAAACGCATGGCGGAAATGGGGCTAAATCCGGAAGATTATTGGTGGTATCGTGATTTGCGTCGTTACGGCACGGTTCCGCATTCCGGCTTTGGCTTGGGCTTTGAACGTTTAATTGTTTATGTGACAGGGTTGCAAAATATTCGTGATGTGATCCCGTTCCCACGTGCTCCGCGTAACGCAAATTTC","","","52579","MTKIASIVNVLQGKIAIGEKVTVRGWVRTRRDSKAGLSFLAVYDGSCFAPIQAIVNNDIANYESEVLRLTAGCSVVVAGTVVESPAEGQAVELQAEKVEVTGWVEDPETYPMAAKRHSIEYLREVAHLRPRTNIIGAVARVRHCLAQAIHRFFHEQGFYWVATPLITASDTEGAGEMFRVSTLDLENLPRTDKGAVDFSQDFFGKESFLTVSGQLNGETYACALSKIYTFGPTFRAENSNTTRHLAEFWMIEPEVAFATLADNAKLAEDMLKYVFRAVLAERRDDLEFFAKHVDGDVINRLERFINSDFAQVDYTDAIEILLKSGKTFEFPVSWGIDLSSEHERYLAEDYFKSPVVVKNYPKEIKAFYMRLNDDGQTVAAMDVLAPGIGEIIGGSQREERLDVLDKRMAEMGLNPEDYWWYRDLRRYGTVPHSGFGLGFERLIVYVTGLQNIRDVIPFPRAPRNANF","1521417","","asparaginyl-tRNA synthetase","Cytoplasm","","
InterPro
IPR002312
Family
Aspartyl-tRNA synthetase, class IIb
PR01042\"[209-221]T\"[225-238]T\"[382-398]T\"[422-436]TTRNASYNTHASP
InterPro
IPR004364
Domain
tRNA synthetase, class II (D, K and N)
PF00152\"[118-463]TtRNA-synt_2
InterPro
IPR004365
Domain
Nucleic acid binding, OB-fold, tRNA/helicase-type
PF01336\"[21-101]TtRNA_anti
InterPro
IPR004522
Family
Asparaginyl-tRNA synthetase, class IIb
TIGR00457\"[4-467]TasnS: asparaginyl-tRNA synthetase
InterPro
IPR006195
Domain
Aminoacyl-transfer RNA synthetase, class II
PS50862\"[145-457]TAA_TRNA_LIGASE_II
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[16-107]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.30.930.10\"[108-467]Tno description
PTHR22594\"[89-178]T\"[197-463]TASPARTYL/LYSYL-TRNA SYNTHETASE
PTHR22594:SF6\"[89-178]T\"[197-463]TASPARTYL-TRNA SYNTHETASE


","BeTs to 17 clades of COG0017COG name: Aspartyl/asparaginyl-tRNA synthetasesFunctional Class: JThe phylogenetic pattern of COG0017 is aompkzy--d-lbce-ghs-----twNumber of proteins in this genome belonging to this COG is","Significant hit ( 5.4e-06) to 2/2 blocks of the IPB002106 family, which is described as \"Aminoacyl-transfer RNA synthetases class-II\". Interpro entry for IP:IPR002106. IPB002106A 152-164 0.064 IPB002106B 438-452 0.041","Residues 390 to 460 match (2e-10) PD:PD583290 which is described as LIGASE SYNTHETASE CYTOPLASMIC AMINOACYL-TRNA BIOSYNTHESIS SYNTHETASE ASNRS ATP-BINDING ASPARAGINYL-TRNA ASPARAGINE-- ","","","","","","","","","","","","Wed Jan 15 17:51:18 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02233 is paralogously related to AA01743 (2e-09), AA02856 (4e-08) and AA00801 (4e-07).","","","","","","Residues 118 to 463 (E-value = 9.9e-177) place AA02233 in the tRNA-synt_2 family which is described as tRNA synthetases class II (D, K and N) (PF00152)","","","","","Anselme,J. and Hartlein,M. Asparaginyl-tRNA synthetase from Escherichia coli has significant sequence homologies with yeast aspartyl-tRNA synthetase Gene 84 (2), 481-485 (1989) PubMed: 2693216 Aoki,H., Yaworsky,P.J., Patel,S.D., Margolin-Brzezinski,D., Park,K.S. and Ganoza,M.C. The asparaginyl-tRNA synthetase gene encodes one of the complementing factors for thermosensitive translation in the Escherichia coli mutant strain, N4316 Eur. J. Biochem. 209 (2), 511-521 (1992) PubMed: 1425658 Anselme,J. and Hartlein,M. Tyr-426 of the Escherichia coli asparaginyl-tRNA synthetase, an amino acid in a C-terminal conserved motif, is involved in ATP binding. FEBS Lett. 280 (1): 163-166 (1991) [PubMed: 2009959].Madern,D., Anselme,J. and Hartlein,M. Asparaginyl-tRNA synthetase from the Escherichia coli temperature-sensitive strain HO202. A proline replacement in motif2 is responsible for a large increase in Km for asparagine and ATP. FEBS Lett. 299 (1): 85-89 (1992) [PubMed: 1544480]. ","","Wed Jan 15 17:51:18 2003","1","","","" "AA02234","1521582","1521481","102","TTGTTCGATCATCAAATAAAAAACACTGAAAAAAGATACCGCACTTTGGTATCTTTTTTGTTATCGGGGAAACAAAAGTGTGGTCGTTTTTTCCGGCAGTTT","","","4175","LFDHQIKNTEKRYRTLVSFLLSGKQKCGRFFRQF","1521481","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:09:40 2004","Wed Feb 25 15:09:40 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02234 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:09:40 2004","","","","","","","","","","","","","1","","","" "AA02235","1522044","1521586","459","ATGGAATATAAATCCTCACCGAAACGCCCCTATTTATTAAGGGCTTATTACGATTGGTTAATTGATAACGACTTCACGCCGTATTTAGTGGTAGATGCCACGTATTGGGGCGTAAAAGTGCCGGTGGAGTATGTCAAAGACGGACAAATCGTTTTGAATTTGTCTGCCAATGCCACCGGTAATTTACAATTGACTAATGATTTTATTCAATTTAACGCGCGTTTTCGTGGTGTGTCTCAGGATATTTATATTCCGCTTGGCGCTGCATTAGCGATTTATGCCCGTGAAAATGGTGACGGTGTGATGTTTGAACCTGAAGCCGCTTATGAACACCCTGAGCAGGCAGAAGAACAACCGACAGGTTTTGAAAATGCCGTAGATAAAGCGGATCAAAAGGATAAATCGGATAAACCAAAATCAGGCGATAAAAAATCCACCTCCCATTTACGCATTGTAAAA","","","17311","MEYKSSPKRPYLLRAYYDWLIDNDFTPYLVVDATYWGVKVPVEYVKDGQIVLNLSANATGNLQLTNDFIQFNARFRGVSQDIYIPLGAALAIYARENGDGVMFEPEAAYEHPEQAEEQPTGFENAVDKADQKDKSDKPKSGDKKSTSHLRIVK","1521586","[FUNCTION] Seems to act in concert with sspa in the regulation of several proteins during exponential and stationary-phasegrowth. The exact function of sspB is not yet known. ","stringent starvation protein B","Periplasm","","
InterPro
IPR007481
Family
Stringent starvation protein B
PIRSF005276\"[5-153]TClpX-specific adaptor protein SspB
PF04386\"[5-153]TSspB


","BeTs to 6 clades of COG2969COG name: Stringent starvation protein BFunctional Class: RThe phylogenetic pattern of COG2969 is --------------efghsn------Number of proteins in this genome belonging to this COG is","","Residues 9 to 110 match (3e-46) PD:PD021091 which is described as PROTEOME COMPLETE B STRINGENT STARVATION SSPB PILE REGULATOR EXPRESSION MACROPHAGE ","","","","","","","","","","","Wed Jan 15 17:56:06 2003","Wed Jan 15 17:56:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02235 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 153 (E-value = 5.1e-94) place AA02235 in the SspB family which is described as Stringent starvation protein B (PF04386)","","","","","Williams,M.D., Ouyang,T.X. and Flickinger,M.C. Starvation-induced expression of SspA and SspB: the effects of a null mutation in sspA on Escherichia coli protein synthesis and survival during growth and prolonged starvation Mol. Microbiol. 11 (6), 1029-1043 (1994) PubMed: 8022275 Williams,M.D., Fuchs,J.A. and Flickinger,M.C. Null mutation in the stringent starvation protein of Escherichia coli disrupts lytic development of bacteriophage P1. Gene 109 (1): 21-30 (1991) [PubMed: 1721886].Serizawa,H. and Fukuda,R. Structure of the gene for the stringent starvation protein of Escherichia coli. Nucleic Acids Res. 15 (3): 1153-1163 (1987) [PubMed: 3029697].","","Wed Jan 15 17:56:06 2003","1","","","" "AA02236","1522697","1522059","639","ATGACAAGCTCTGCAAATAAACGTTCTGTAATGACGCTATTTTCAAACAAAACCGATGTTTATTGCCACCAAGTGCGCATCGTGTTAGCAGAGAAAGGCGTAGCTTATGAAACGGAAATTGTAGATCAGCAAGCATTATCAGAAGATTTAATGGAACTTAATCCGTATGGTACCTTGCCGACTTTAGTTGATCGTGATCTCGTCTTATTTAATTCCCGTATTATTATGGAATACCTGGATGAACGTTTTCCACATCCGCCGTTAATGCCGGTTTATCCTGTTGCGCGCGGCAAAAGTCGTTTATTAATGTTACGCATTGAACAGGATTGGTATCCAACCTTAGAAAAAGCACAATGCGACTTATCCGACACAGAGCGCGCCGCTGCATTGAAGCAATTGAAAGAAGAAATTCTGGCTGTTGCGCCGATTTTTAATCAGAACACCTATTTTATGAGTGACGAATTTAGCTTAATCGACTGCTATATGGCACCGTTGTTATGGCGTATGCAGGAATTAGGCGTAGAATTCAGCGGTGCCGGCAGCAAAGCGATTAAAGCCTATATGACCCGCGTGTTTGAACGGGATTCTTTCCTGCAATCCGTGGGCGAATTAGCGCCGAAAAATCTGATGGATGAAAAA","","","24436","MTSSANKRSVMTLFSNKTDVYCHQVRIVLAEKGVAYETEIVDQQALSEDLMELNPYGTLPTLVDRDLVLFNSRIIMEYLDERFPHPPLMPVYPVARGKSRLLMLRIEQDWYPTLEKAQCDLSDTERAAALKQLKEEILAVAPIFNQNTYFMSDEFSLIDCYMAPLLWRMQELGVEFSGAGSKAIKAYMTRVFERDSFLQSVGELAPKNLMDEK","1522059","[FUNCTION] Forms an equimolar complex with the RNA polymerase holoenzyme (rnaP) but not with the core enzyme,it is synthesized predominantly when cells are exposed to amino acid starvation, at which time it accounts for over 50% of the total protein synthesized. It is involved in the transition from P1 early to P1 late gene expression. rnR and sspA can functionally replace P.aeruginosa alginate regulatory gene algR2. (by similarity). ","stringent starvation protein A","Cytoplasm","","
InterPro
IPR004045
Domain
Glutathione S-transferase, N-terminal
PF02798\"[9-81]TGST_N
InterPro
IPR004046
Domain
Glutathione S-transferase, C-terminal
PF00043\"[101-195]TGST_C
InterPro
IPR012335
Domain
Thioredoxin fold
G3DSA:3.40.30.10\"[9-112]Tno description
noIPR
unintegrated
unintegrated
PTHR11260\"[11-201]TGLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING


","BeTs to 9 clades of COG0625COG name: Glutathione-S-transferasesFunctional Class: OThe phylogenetic pattern of COG0625 is ------y----l-cefghsn-jx---Number of proteins in this genome belonging to this COG is","","Residues 11 to 80 match (4e-30) PD:PD410965 which is described as TRANSFERASE PROTEOME COMPLETE GLUTATHIONE S-TRANSFERASE ISOMERASE CATABOLISM PROBABLE MALEYLACETOACETATE STARVATION ","","","","","","","","","","","Thu Jan 16 09:35:10 2003","Thu Jan 16 09:35:10 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02236 is paralogously related to AA02492 (6e-09).","","","","","","Residues 89 to 195 (E-value = 4.5e-09) place AA02236 in the GST_C family which is described as Glutathione S-transferase, C-terminal domain (PF00043)","","","","","Williams,M.D., Ouyang,T.X. and Flickinger,M.C. Starvation-induced expression of SspA and SspB: the effects of a null mutation in sspA on Escherichia coli protein synthesis and survival during growth and prolonged starvation Mol. Microbiol. 11 (6), 1029-1043 (1994) PubMed: 8022275 Theisen,M. and Potter,A.A. Cloning, sequencing, expression, and functional studies of a 15,000-molecular-weight Haemophilus somnus antigen similar to Escherichia coli ribosomal protein S9 J. Bacteriol. 174 (1), 17-23 (1992) PubMed: 1729207 Egland PG, Du LD, Kolenbrander PE. Identification of independent Streptococcus gordonii SspA and SspB functions in coaggregation with Actinomyces naeslundii. Infect Immun. 2001 Dec;69(12):7512-6. PMID: 11705927 Bronstein PA, Miao EA, Miller SI. InvB is a type III secretion chaperone specific for SspA. J Bacteriol. 2000 Dec;182(23):6638-44. PMID: 11073906 ","","Tue Feb 4 17:31:59 2003","1","","","" "AA02237","1523352","1522900","453","ATGGACGATATTCAAATTTCCGTACAGGAGCAGCCTTTTGATCAAAATGCGGTTTACCATTGGTTAAGCGGGCAACATTCCGTGGGCGCTGTGGTGATTTTTGTAGGTAAAGTGCGTGATATGAATTTGGGCGAGGAAGTCAGCAGTTTATATTTGGAGCATTACCCCGCCATGACCCATAAAGCCTTGCTGGATATTGCGCAACAGGCGAAAGTGCGGTGGAATTTACAGAAGATTTCCATTATCCATAGGGTCGGATTATTGCATACGGGCGATGAAATCGTGCTGGTGGGAACGGCTTCGGCACACCGTGGCGATGCTTATCACGCCAATGAATTCATTATGGATTATTTAAAAACCAAAGCGCCTTTTTGGAAAAAGGAACAAATAGAAAAAGGCGAGCGTTGGATTGAAGAGCGAGATAGTGATTATGTCGCTGCCGATAAATGGAAA","","","17374","MDDIQISVQEQPFDQNAVYHWLSGQHSVGAVVIFVGKVRDMNLGEEVSSLYLEHYPAMTHKALLDIAQQAKVRWNLQKISIIHRVGLLHTGDEIVLVGTASAHRGDAYHANEFIMDYLKTKAPFWKKEQIEKGERWIEERDSDYVAADKWK","1522900","[FUNCTION] Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group (By similarity).[PATHWAY] Molybdenum cofactor biosynthesis.[SUBUNIT] Heterodimer of 2 moaD subunits and 2 moaE subunits (By similarity).","molybdopterin biosynthesis protein E chain","Cytoplasm","","
InterPro
IPR003448
Family
Molybdopterin biosynthesis MoaE
PF02391\"[5-122]TMoaE
noIPR
unintegrated
unintegrated
G3DSA:3.90.1170.40\"[1-150]Tno description
PTHR23404\"[53-141]TMOLYBDOPTERIN SYNTHASE RELATED
PTHR23404:SF2\"[53-141]TMOLYBDOPTERIN SYNTHASE LARGE SUBUNIT 2


","BeTs to 18 clades of COG0314COG name: Molybdopterin converting factor, large subunitFunctional Class: HThe phylogenetic pattern of COG0314 is aompkz-q-dr-bcefgh--uj----Number of proteins in this genome belonging to this COG is","Significant hit ( 5.4e-34) to 2/2 blocks of the IPB003448 family, which is described as \"Molydopterin converting factor subunit 2\". Interpro entry for IP:IPR003448. IPB003448A 29-42 1.7e-07 IPB003448B 83-126 4e-25","Residues 27 to 133 match (1e-11) PD:PD307165 which is described as MOLYBDOPTERIN PROTEOME COMPLETE BIOSYNTHESIS SUBUNIT COFACTOR LARGE MOLYBDENUM SYNTHASE FACTOR ","","","","","","","","","","","Thu Jan 16 10:31:00 2003","Thu Jan 16 10:31:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02237 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 122 (E-value = 1.8e-55) place AA02237 in the MoaE family which is described as MoaE protein (PF02391)","","","","","Rivers,S.L., McNairn,E., Blasco,F., Giordano,G. and Boxer,D.H. Molecular genetic analysis of the moa operon of Escherichia coli K-12 required for molybdenum cofactor biosynthesis. Mol. Microbiol. 8 (6): 1071-1081 (1993) [PubMed: 8361352].Pitterle,D.M. and Rajagopalan,K.V. The biosynthesis of molybdopterin in Escherichia coli. Purification and characterization of the converting factor. J. Biol. Chem. 268 (18): 13499-13505 (1993) [PubMed: 8514782]. Rudolph,M.J., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation. Nat. Struct. Biol. 8 (1): 42-46 (2001) [PubMed: 11135669].","","Thu Jan 16 10:31:00 2003","1","","","" "AA02239","1523601","1523356","246","ATGTTACGCGTTTTATTTTTTGCGCAAACCCGAGAATTAATCGGCTTGGATTTTATTGAAGTGGAAAGCGATTTCACAACGGCAGAAGATGTGCGCCAATACTTAGTAGCTGAGAAAGGCGATAAATGGGCGCTGGCATTGCAATCGGATAAATTATTGGTTGCTATAAATCAAACTCTGATGCCGCTGGAAAGTGCGGTCAAAAATGGCGATGAAATTGCGTTTTTCCCGCCGGTCACCGGGGGC","","","10848","MLRVLFFAQTRELIGLDFIEVESDFTTAEDVRQYLVAEKGDKWALALQSDKLLVAINQTLMPLESAVKNGDEIAFFPPVTGG","1523356","[FUNCTION] Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur atoms are provided by the active form of the small subunit (By similarity).[PATHWAY] Molybdenum cofactor biosynthesis.","molybdopterin biosynthesis protein D","Cytoplasm","","
InterPro
IPR003749
Family
ThiamineS
PF02597\"[4-82]TThiS
InterPro
IPR010034
Family
Molybdopterin converting factor, subunit 1
TIGR01682\"[2-82]TmoaD: molybdopterin converting factor, subu
InterPro
IPR012675
Domain
Beta-grasp fold, ferredoxin-type
G3DSA:3.10.20.30\"[1-82]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-15]?signal-peptide


","BeTs to 15 clades of COG1977COG name: Molybdopterin converting factor, small subunitFunctional Class: HThe phylogenetic pattern of COG1977 is ao-pk--q-dr-bcefgh--uj----Number of proteins in this genome belonging to this COG is","","Residues 1 to 82 match (5e-29) PD:PD407084 which is described as MOLYBDOPTERIN SUBUNIT COMPLETE PROTEOME CONVERTING BIOSYNTHESIS COFACTOR MOLYBDENUM FACTOR SMALL ","","","","","","","","","","","Thu Jan 16 10:45:19 2003","Thu Jan 16 10:45:19 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02239 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 22 to 82 (E-value = 1.4e-14) place AA02239 in the ThiS family which is described as ThiS family (PF02597)","","","","","Rivers,S.L., McNairn,E., Blasco,F., Giordano,G. and Boxer,D.H. Molecular genetic analysis of the moa operon of Escherichia coli K-12 required for molybdenum cofactor biosynthesis Mol. Microbiol. 8 (6), 1071-1081 (1993) PubMed: 8361352 Pitterle,D.M. and Rajagopalan,K.V. The biosynthesis of molybdopterin in Escherichia coli. Purification and characterization of the converting factor J. Biol. Chem. 268 (18), 13499-13505 (1993) PubMed: 8514782 ","","Thu Jan 16 10:45:19 2003","1","","","" "AA02241","1524122","1523604","519","TTGAAAAATAGCAAGAAAATCAACCGCACTTTAATTATCATGGTCACATTTACTCACATTAATTCCCATGGGGAAGCCAATATGGTGGACGTTTCCGCCAAAGCCGAAACCGTCCGTGAAGCCCGCGCTGAGGCTTATGTTTGTATGGCGCCCGAAACCTTACAAATGATCCTGTCCGGTCAGCATCACAAAGGCGATGTGTTCGCCACCGCCCGCATTGCCGGCATTCAGGCGGCAAAACGCACGTGGGAATTGATTCCCTTGTGCCATCCGTTATTGCTTTCGAAAGTTGAAGTGAGCTTAACGGCACTTCCTGAAACCAATCAGGTGCGTATTGAAAGCCTGTGTAAATTAACCGGTAAAACAGGCGTGGAAATGGAAGCCTTAACTGCGGCGAGTGTTGCCGCCTTGACGATTTATGATATGTGCAAAGCGGTGCAAAAAGATATGGTGATTGAATCCGTACGCTTGCTGGAAAAGTGCGGTGGAAAATCCGGGCATTTTATCGCGGAGGAAAAA","","","18888","LKNSKKINRTLIIMVTFTHINSHGEANMVDVSAKAETVREARAEAYVCMAPETLQMILSGQHHKGDVFATARIAGIQAAKRTWELIPLCHPLLLSKVEVSLTALPETNQVRIESLCKLTGKTGVEMEALTAASVAALTIYDMCKAVQKDMVIESVRLLEKCGGKSGHFIAEEK","1523604","[FUNCTION] Together with moaA, is involved in the conversion of aguanosine derivative (GXP) into molybdopterin precursor Z.[PATHWAY] Molybdenum cofactor biosynthesis; first step.","molybdenum cofactor biosynthesis protein C","Cytoplasm, Periplasm","","
InterPro
IPR002820
Domain
Molybdopterin cofactor biosynthesis MoaC region
PD003575\"[32-168]TMOAC_VIBCH_Q9KT79;
G3DSA:3.30.70.640\"[14-172]Tno description
PF01967\"[28-163]TMoaC
TIGR00581\"[17-165]TmoaC: molybdenum cofactor biosynthesis prot
InterPro
IPR012087
Family
Molybdenum cofactor precursor Z biosynthesis MoaC
PIRSF003315\"[16-172]TMolybdenum cofactor precursor Z biosynthesis protein MoaC
noIPR
unintegrated
unintegrated
PTHR22960\"[17-171]TMOLYBDOPTERIN COFACTOR SYNTHESIS PROTEIN A
signalp\"[1-26]?signal-peptide


","BeTs to 18 clades of COG0315COG name: Molybdenum cofactor biosynthesis enzymeFunctional Class: HThe phylogenetic pattern of COG0315 is aompkz-q-dr-bcefgh--uj----Number of proteins in this genome belonging to this COG is","Significant hit ( 4.9e-64) to 3/3 blocks of the IPB002820 family, which is described as \"MoaC family\". Interpro entry for IP:IPR002820. IPB002820A 28-44 1.2e-09 IPB002820B 64-94 4.9e-27 IPB002820C 119-144 9e-25","Residues 24 to 168 match (5e-65) PD:PD003575 which is described as BIOSYNTHESIS COFACTOR MOLYBDENUM PROTEOME COMPLETE C MOAC MOLYBDOPTERIN PROBABLE BIOSYNTHETIC ","","","","","","","","","","","Thu Jan 16 13:21:06 2003","Thu Jan 16 13:21:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02241 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 28 to 163 (E-value = 5.3e-93) place AA02241 in the MoaC family which is described as MoaC family (PF01967)","","","","","Kuykendall,L.D. and Hunter,W.J. The sequence of a symbiotically essential Bradyrhizobium japonicum operon consisting of trpD, trpC and a moaC-like gene Biochim. Biophys. Acta 1350 (3), 277-281 (1997) PubMed: 9061023 Rivers,S.L., McNairn,E., Blasco,F., Giordano,G. and Boxer,D.H. Molecular genetic analysis of the moa operon of Escherichia coli K-12 required for molybdenum cofactor biosynthesis Mol. Microbiol. 8 (6), 1071-1081 (1993) PubMed: 8361352 ","","Thu Jan 16 13:21:06 2003","1","","","" "AA02242","1525148","1524138","1011","ATGCAAACCATTCCAATCAAAAATGTTGGGGCGACTCAACTAGTTGATTCGTTCCAACGTGCGTATTACTATTTGCGACTGTCAATTACCGATGTGTGTAATTTCCGTTGCAATTATTGTCTGCCTGACGGTTATCAACCGGAACCCAATAAGCCGAGCTTTTTGACCTTAGATGAAATTCGTCGTTTGGTGAATAGTTTCAGCATTATGGGAACGGAAAAAGTACGCCTCACCGGCGGCGAACCTACGCTCCGCAAGGATTTTCTCGCTATTGCTGAAACGATCAGCCAAATTGAAGGTATTAAACAAATTGCCTTAACCACCAATGGATTTCGTTTATTAAAAGACGTTGAGCACTGGAAAAATGCCGGCATTACATCCATTAATGTAAGTGTTGACAGCTTGGATGTCAGAATGTTCCAACGGATTACCGGCGTAGATAAATTTGATGACATTATGCGTGGCATTGATCGCGCTTTTGAATGCGGCTATCAAAAAATCAAAGTAAATTCCGTGCTGATGAAAGACTTAAATGACAAGGATTTTTCCGGTTTTCTGGCGTGGATTAAAGATAAGCCCATTCAGATGCGTTTTATCGAATTAATGCAAACCGGCGAGATGAATGCTTTCTTCCAAAGACATCATTTATCCGGGCAGGTACTGGAACAAAAATTACTGCGTTCAGGTTGGCAGCTGCAGATGAAAAATCGCTCTGATGGTCCAGCAAAAGTGTTTCGCCATCCGGATTACGTAGGCGAAATTGGCTTAATCATGCCTTATGAGAAAAATTTCTGCGCCAGCTGTAACCGTTTACGGGTTTCCGCCAAAGGGAAATTGCACCTTTGTTTATTCGGCGAGGAAGGCATTGAATTACGCGATTTGTTACAATACGATAAGCAGCAACTCATTTTGCAATCAAGAATTTTTTCTGCGTTACAAGGTAAGCGTGAACATCATTATCTGCACATCGGCGATAGTGGCGTACGTAGTCATTTGGCAAGTATCGGCGGT","","","38591","MQTIPIKNVGATQLVDSFQRAYYYLRLSITDVCNFRCNYCLPDGYQPEPNKPSFLTLDEIRRLVNSFSIMGTEKVRLTGGEPTLRKDFLAIAETISQIEGIKQIALTTNGFRLLKDVEHWKNAGITSINVSVDSLDVRMFQRITGVDKFDDIMRGIDRAFECGYQKIKVNSVLMKDLNDKDFSGFLAWIKDKPIQMRFIELMQTGEMNAFFQRHHLSGQVLEQKLLRSGWQLQMKNRSDGPAKVFRHPDYVGEIGLIMPYEKNFCASCNRLRVSAKGKLHLCLFGEEGIELRDLLQYDKQQLILQSRIFSALQGKREHHYLHIGDSGVRSHLASIGG","1524138","[FUNCTION] Together with moaC, is involved in the conversion of a guanosine derivative (GXP) into molybdopterin precursor Z.[PATHWAY] Molybdenum cofactor biosynthesis; first step.","molybdenum cofactor biosynthesis protein A","Cytoplasm","","
InterPro
IPR000385
Domain
MoaA/nifB/pqqE, iron-sulphur binding
PS01305\"[29-40]TMOAA_NIFB_PQQE
InterPro
IPR006638
Domain
Elongator protein 3/MiaB/NifB
SM00729\"[23-230]TElp3
InterPro
IPR007197
Domain
Radical SAM
PF04055\"[27-189]TRadical_SAM
InterPro
IPR010505
Domain
Molybdenum cofactor synthesis C-terminal
PF06463\"[194-321]TMob_synth_C
InterPro
IPR013483
Family
Molybdenum cofactor biosynthesis protein A
TIGR02666\"[14-337]TmoaA: molybdenum cofactor biosynthesis prot
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[19-165]Tno description
noIPR
unintegrated
unintegrated
PTHR22960\"[150-305]TMOLYBDOPTERIN COFACTOR SYNTHESIS PROTEIN A


","BeTs to 18 clades of COG2896COG name: Molybdenum cofactor biosynthesis enzymeFunctional Class: HThe phylogenetic pattern of COG2896 is aompkz-q-dr-bcefgh--uj----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.7e-24) to 5/5 blocks of the IPB000385 family, which is described as \"MoaA / nifB / pqqE family\". Interpro entry for IP:IPR000385. IPB000385A 25-36 0.00039 IPB000385B 74-85 0.00072 IPB000385C 103-115 0.014 IPB000385D 168-179 0.0028 IPB000385E 265-277 0.0024","Residues 100 to 179 match (3e-30) PD:PD000790 which is described as COFACTOR BIOSYNTHESIS PROTEOME COMPLETE MOLYBDENUM A IRON-SULFUR SYNTHESIS MOLYBDOPTERIN PQQ ","","","","","","","","","","","Thu Jan 16 13:23:54 2003","Thu Jan 16 13:23:54 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02242 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 194 to 321 (E-value = 4.7e-42) place AA02242 in the Mob_synth_C family which is described as Molybdenum Cofactor Synthesis C (PF06463)","","","","","Rivers,S.L., McNairn,E., Blasco,F., Giordano,G. and Boxer,D.H. Molecular genetic analysis of the moa operon of Escherichia coli K-12 required for molybdenum cofactor biosynthesis Mol. Microbiol. 8 (6), 1071-1081 (1993) PubMed: 8361352 ","","Thu Jan 16 13:23:54 2003","1","","","" "AA02243","1525506","1526471","966","ATGGCGGACTTTAACGGCTATCAACAACACGAAAATCTGAGCAAAATAAAAAAAATCGTGGCGATTGGCGGAGGACACGGATTAGGTCGGGTCATGTCAGCCTTAAGTTTTATGAACGAACGCCTCACCGCCATTGTCACCACCACCGATAACGGCGGTTCCACCGGACGCATTCGTAGCGCTCAAGGCGGCATAGCCTGGGGCGATTTACGCAATTGTTTAAATCAAATCATTACGCAGCCGAGCACTGCCTCCGCCTTATTTGAATATCGCTTCAGCGGCAACGGCGAACTGGCGGGACACAATCTCGGCAATCTGATGCTAAAAGCATTGGAAGATTTACATATTCGCCCGATGGAAGCGGTTAATCTGATTCGTGATTTGCTTGATGTCAAATCCTTCATCATCCCAATGTCGGAGCAGCCCGTGCATCTCGCCGCCATTTCAGGCAGCGGCGCCAGCGTGGTAGGCGAAGTGAGCGTGGACAGCTTAACCGAACTACCAAAATCCATTTTTCTTGTTCCCTATGTGCAAGCCACGCCGGAAGCCATTAGCGCATTAAAAGAAGCTGAAGTGATTTTATTCGGTCCCGGCAGTTTTTTAACCAGCATTCTACCGCCGATTCTCTTGTCTGAAGTCATTGAACAACTGCAACAAAGCCAAGCCAAGAAAATTTTTATTGATAATCTCGGTATCGAACGCAGCCCCGCAGCAAGGCTTTCCCTTGCTGATCGCATCCGTTGGATTAACGACACCATCGGCAAACCGATCATTGATGCCGCCATTGTTCCTTTTGACAACGCACCGGAAAATCTGCACGACATCAAAATCCTCGCCGGTCGCCTCAACGCCGACGACATCACCTACCGCCACGACCGCGCCCTCCTCTGCTCCGCCATTGACGAGCTATTGGGCGAACTGCTGGAATCGCACGACGACGAAGAACATTTGGAAGCCATTAATATC","","","34913","MADFNGYQQHENLSKIKKIVAIGGGHGLGRVMSALSFMNERLTAIVTTTDNGGSTGRIRSAQGGIAWGDLRNCLNQIITQPSTASALFEYRFSGNGELAGHNLGNLMLKALEDLHIRPMEAVNLIRDLLDVKSFIIPMSEQPVHLAAISGSGASVVGEVSVDSLTELPKSIFLVPYVQATPEAISALKEAEVILFGPGSFLTSILPPILLSEVIEQLQQSQAKKIFIDNLGIERSPAARLSLADRIRWINDTIGKPIIDAAIVPFDNAPENLHDIKILAGRLNADDITYRHDRALLCSAIDELLGELLESHDDEEHLEAINI","1526471","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR002882
Family
Protein of unknown function UPF0052 and CofD
PF01933\"[19-308]TUPF0052
InterPro
IPR010119
Family
Conserved hypothetical protein, CofD related
TIGR01826\"[19-305]TCofD_related: conserved hypothetical protei


","BeTs to 12 clades of COG0391COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG0391 is aom---yqvdrlbce-gh--------Number of proteins in this genome belonging to this COG is","Significant hit ( 3.4e-29) to 2/3 blocks of the IPB002882 family, which is described as \"Uncharacterised protein family\". Interpro entry for IP:IPR002882. IPB002882A 19-56 5.2e-17 IPB002882C 187-210 9.2e-11","Residues 17 to 300 match (7e-110) PD:PD006387 which is described as PROTEOME COMPLETE YBHK YPO1158 LIN2616 CAC0512 YJIF 5'REGION SAV0766 SPY0653 ","","","","","","","","","","","","Thu Jan 16 13:26:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02243 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 19 to 308 (E-value = 7.7e-106) place AA02243 in the UPF0052 family which is described as Uncharacterised protein family UPF0052 (PF01933)","","","","","","","","1","","","" "AA02244","1527435","1526542","894","ATGGCGAAATTATTTAGTACAAGTATAGATAATATTAGCTTGCACCTTAAAAATATATATTTGGAGCATGAGCTTGATGAAATTTTAACTACCGAGGATTTCTCGGTAGTTCGACAAGAAGGTAAACGTAAGGTTAAGCGTACAATTAAATATTACAATCTCGATGCTATCATTTCCGTCGGATATCGAATTAGTTCTAAGCGGGCAACGCAATTCCGTCAATGGGCTACACAAACCTTGAAGCAATATTTGGTACAGGGTTACGCATTAAATGATCGACGCTTACAAGAACGAGGGATTGAATTTGAACAAGTGATAGGTTTGCTTGGGCAGACCTTGAGTAATCAATCTTTGTTATCTGACGAAGGCAAAGCCGTATTGTCTGTTGTGCAGGATTATGCTAGGAGTTGGAGTTTGTTACAGGCTTACGATGAGCAAAGTCTAACGGCTAATCAGCATAAGCAAAATAATATGGTTCTGTTGGTGTTAGATGACGTATTACAGGCAATTTCTCAATTAAAACAGGCGTTAGTGGAAAAAGGGGAAGCGACGGCGTTGTTTGGACAACAACGAAATTCCGGTTTAGCCTCTGCCATTGCCACGATTGAACAAGGATTCGGTGACACGCTTTTTTATCCGAATGTTGCCAGCCGAGCGGCGAATTTATTGTATTTTATTATCAAAAATCATCCGTTGACCGATGGCAATAAACGCACGGGATCTTTCCTGTTTTTATGGTATTTGCGGTTGAATCAACACTTATTGGCAAGGCCGGTAGAACAATTGATTAATGACAATACTTTAGTGGCATTAGCATTGCTTGTGGCGGAAAGTTTGCCTGAACAGAAAGAACTCATGATTAAGTTGATTGAGCATTTTATTTTGCTAAAAAAC","","","37571","MAKLFSTSIDNISLHLKNIYLEHELDEILTTEDFSVVRQEGKRKVKRTIKYYNLDAIISVGYRISSKRATQFRQWATQTLKQYLVQGYALNDRRLQERGIEFEQVIGLLGQTLSNQSLLSDEGKAVLSVVQDYARSWSLLQAYDEQSLTANQHKQNNMVLLVLDDVLQAISQLKQALVEKGEATALFGQQRNSGLASAIATIEQGFGDTLFYPNVASRAANLLYFIIKNHPLTDGNKRTGSFLFLWYLRLNQHLLARPVEQLINDNTLVALALLVAESLPEQKELMIKLIEHFILLKN","1526542","","conserved hypothetical protein (probable DNA-binding protein; death-on-curing family protein0","Inner membrane, Cytoplasm","","
InterPro
IPR006440
Family
Death-on-curing protein
PF05012\"[173-279]TDOC
TIGR01550\"[164-292]TDOC_P1: death-on-curing family protein


","No hits to the COGs database.","","Residues 57 to 92 match (1e-07) PD:PD486674 which is described as PROTEOME DNA-BINDING COMPLETE CYTOPLASMIC ","","","","","","","","","","","","Fri Feb 7 14:37:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02244 is paralogously related to AA01475 (1e-23).","","","","","","","","","","","","","","1","","","" "AA02245","1527681","1527586","96","ATGCTGACTTGGTTATTTTTATTAAGCAAAAAATGTGAATTTTGTGATCTGCGTAGCGATTTAAGTGCGGTCATCTTTTTCGGTGTTTTGCTTTTC","","","3739","MLTWLFLLSKKCEFCDLRSDLSAVIFFGVLLF","1527586","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-17]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:07:37 2004","Wed Feb 25 15:07:37 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02245 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:07:37 2004","","","","","","","","","","","","","1","","","" "AA02246","1527714","1528415","702","ATGCAAAAAATGTTACTGCTTAGCGGTTCACGATATGGCAATACGGGGTATTTGGAACACACGATTCCGTGGCTACAAGATTTTTTAGCAGCGTATCAAGGCAAGAAAATCGCCTTTGTACCTTACGCGGGTGTGCGCCAAAACAACGATCAATATGAGCAAAAAGTACAACAAATTCTGGCGCCGTTGAACATGGAAATTCAGTCGGTACACCACGGCAAGCCACATCGTGCCATTATTGAACAGGCGGATGTGATCGCTATCGGCGGCGGCAATACGTTCTGTTTGTTAAAGCAAATGTATGAGCATGATTTATTGAGCATTATTCGTGAAAAAGTCAAAAGCGGCACGCCTTATTTCGGTTGGAGTGCCGGCGCCAATGTAGCGAGCAAATCCATTATGACTACAAACGATATGCCCATTACGTACCCGCCGTCATTTGATGCGCTTAATCTGTTCCCTTATCAAATTAATCCGCATTTCATTTCCGGCAAAGTCCCGGGACATAACGGCGAAAGCCGAGAAGAACGATTTGAGGAATTTTTACTGGTCAATCCGACAGCGCAGATTTACGCCCTTCCGGAAGGCACGGCGTTGTTAATTAACGGCAACCAGGTGAAAACCCTCGGCGATCATAACATTTTGCGTTTTAGTGAAAATATGCAACGACATGAAATCCCTGCCGGTTCCGTGTTTGAAATG","","","26277","MQKMLLLSGSRYGNTGYLEHTIPWLQDFLAAYQGKKIAFVPYAGVRQNNDQYEQKVQQILAPLNMEIQSVHHGKPHRAIIEQADVIAIGGGNTFCLLKQMYEHDLLSIIREKVKSGTPYFGWSAGANVASKSIMTTNDMPITYPPSFDALNLFPYQINPHFISGKVPGHNGESREERFEEFLLVNPTAQIYALPEGTALLINGNQVKTLGDHNILRFSENMQRHEIPAGSVFEM","1528415","[FUNCTION] Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids (By similarity).[CATALYTIC ACTIVITY] Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides.","peptidase E","Cytoplasm","","
InterPro
IPR005320
Family
Peptidase S51, dipeptidase E
PF03575\"[52-205]TPeptidase_S51
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.880\"[2-232]Tno description
PTHR20842\"[1-225]TPROTEASE S51 ALPHA-ASPARTYL DIPEPTIDASE


","BeTs to 4 clades of COG3340COG name: Peptidase EFunctional Class: EThe phylogenetic pattern of COG3340 is ---------d--b-e--h--------Number of proteins in this genome belonging to this COG is","","Residues 4 to 232 match (8e-92) PD:PD017222 which is described as DIPEPTIDASE HYDROLASE SERINE 3.4.-.- PROTEASE PEPTIDASE PROTEOME COMPLETE ASP-SPECIFIC ALPHA-ASPARTYL ","","","","","","","","","","","Thu Jan 16 13:42:28 2003","Thu Jan 16 13:42:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02246 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 48 to 225 (E-value = 1.6e-57) place AA02246 in the Peptidase_S51 family which is described as Peptidase family S51 (PF03575)","","","","","","","","1","","","" "AA02249","1529959","1528505","1455","ATGAAATTTATCGTCAAATTATTTCCTGAAATTATGATTAAAAGCGAATCCGTGCGGAAACGGTTCGTGAAAATTCTGACCGGCAATATTCGTAACGTATTGGCAAAGCACGACGACACCATCGCCGTGGTGAAACATTGGGATTACATCGAAGTGCGGTCAAAAATCGAAGAGAATTTACCGATGCTCATTGAGCAGTTGCAACGCATCCCGGGGATTCATCATTTTCTACAAGTGGAAGAAAAACCCTTTAGCAGCCTCCATGATATTTTTGAACAAACCCTGTCTGATGTGGCTCTGCAACTGGAAAACAAGAGTTTTTGCGTGCGGGTGAAACGTAAAGGCAAACATGAATTTAATTCGCTGGATGCGGAACGCTATATCGGCGGCGGGCTGAATCAACATATCGCCAGTGCCAAAGTGCAGCTGAAAAATCCTGACGTGACGGTACGCATTGAAATTGAAGACGACAAAATGATGCTGGTACGCGCCCGTTATGAAGGCATCGGCGGCTACCCAATTGGCACGCAGGAAGACGTGCTGTCGTTGATTTCCGGCGGGTTTGATTCAGGTGTGTCCAGCTATATGCTGTTGCGTCGCGGTTCGCGCGTACATTATTGCTTCTTTAATTTAGGCGGCGCGGCGCACGAAATCGGCGTGAAACAAATGGCGTATCACATTTGGCAACGTTACGGCAGCTCGCACAAAGTGCGTTTTGTGGCGATTAATTTTGAAGGCGTGGTGGGCGAGATTCTGGAAAACGTGGATAACGGACAAATGGGCGTGGTGCTTAAACGCATGATGGTACGTGCCGCGTCTAAAATTGCCCAACGTTTCGACATTCAGGCGATCGTCACCGGTGAGGCGTTAGGACAGGTTTCCAGCCAAACCTTAACCAATTTACGTTTAATAGATGAAGCCGCCGAGGGATTGGTTCTACGCCCGTTAATCACGCACGACAAAGAACAAATCATCGCCATGGCGAAACACATTGGCACTGATGATATTGCCAAATCTATGCCGGAATTTTGCGGCGTGATTTCCAAAAATCCGACGGTAAAAGCCATCAAAGCGAAAATCGAGCAGGAAGAAGGCAATTTCAATTTTGCCGTGTTGGAAAGTGCGGTGGAAAATGCGCAATATTTGGATATTCGTCAAATCGCCGAGCAGACGGAGAAAGAGGTGGTTTCCGTCGATACCATTTCCGTGCTGGGCACCAATGACGTGATCATCGACATCCGCAGCCCGGAGGAAATCGACGAAAAACCGCTACATATTGAAAAGCAAACGATGATTTTGTTGCCGTTTTACAAACTGTCCAATCAATTTGCCGAACTGGATCAAAGCAAAAACTATGTGCTGTATTGCGAACGCGGCGTGATGAGCAAATTGCAGGCGCTGTATTTGAAAGAGAGTGGATTTAATAATGTGAAGGTGTTCAAAAAGATACTTTCC","","","54854","MKFIVKLFPEIMIKSESVRKRFVKILTGNIRNVLAKHDDTIAVVKHWDYIEVRSKIEENLPMLIEQLQRIPGIHHFLQVEEKPFSSLHDIFEQTLSDVALQLENKSFCVRVKRKGKHEFNSLDAERYIGGGLNQHIASAKVQLKNPDVTVRIEIEDDKMMLVRARYEGIGGYPIGTQEDVLSLISGGFDSGVSSYMLLRRGSRVHYCFFNLGGAAHEIGVKQMAYHIWQRYGSSHKVRFVAINFEGVVGEILENVDNGQMGVVLKRMMVRAASKIAQRFDIQAIVTGEALGQVSSQTLTNLRLIDEAAEGLVLRPLITHDKEQIIAMAKHIGTDDIAKSMPEFCGVISKNPTVKAIKAKIEQEEGNFNFAVLESAVENAQYLDIRQIAEQTEKEVVSVDTISVLGTNDVIIDIRSPEEIDEKPLHIEKQTMILLPFYKLSNQFAELDQSKNYVLYCERGVMSKLQALYLKESGFNNVKVFKKILS","1528505","[FUNCTION] Required for the synthesis of the thiazole moiety (By similarity).[PATHWAY] Thiamine biosynthesis.","thiamine biosynthesis protein","Cytoplasm","","
InterPro
IPR001763
Domain
Rhodanese-like
SM00450\"[391-485]TRHOD
PS50206\"[404-483]TRHODANESE_3
InterPro
IPR003720
Family
Thiamine biosynthesis protein
PF02568\"[175-369]TThiI
TIGR00342\"[4-377]TTIGR00342: thiamine biosynthesis/tRNA modif
InterPro
IPR004114
Domain
THUMP
PF02926\"[75-165]TTHUMP
PS51165\"[61-165]TTHUMP
noIPR
unintegrated
unintegrated
G3DSA:3.40.250.10\"[376-481]Tno description


","BeTs to 15 clades of COG0301COG name: Thiamine biosynthesis ATP pyrophosphataseFunctional Class: HThe phylogenetic pattern of COG0301 is aompkz--v--lb-efgh------twNumber of proteins in this genome belonging to this COG is","Significant hit ( 8.8e-72) to 4/4 blocks of the IPB003720 family, which is described as \"Thiamine biosynthesis protein (ThiI)\". Interpro entry for IP:IPR003720. IPB003720A 19-30 0.0013 IPB003720B 130-154 3.7e-11 IPB003720C 168-201 5.1e-23 IPB003720D 268-321 5.2e-30","Residues 1 to 59 match (3e-22) PD:PD034339 which is described as BIOSYNTHESIS THIAMINE THII COMPLETE PROTEOME THIAMIN ","","","","","","","","","","","Thu Jan 16 14:06:54 2003","Thu Jan 16 14:06:54 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02249 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 175 to 369 (E-value = 2.2e-86) place AA02249 in the ThiI family which is described as Thiamine biosynthesis protein (ThiI) (PF02568)","","","","","","","","1","","","" "AA02250","1530265","1531362","1098","ATGTCAAAAACAAAAAAAATTATAACCGCACTTTGCCTGATGGGGCTGGGTGCCGGTGCGTTGTGGGGAACGCAGGTTGTCATGCACGAAACCGGCACGCCGGAATTTTGTGTCAGCTGCCATTCCATGAGCCATCCGCAGCAGGAATGGGAAGGTTCCAGCCATTTTGCCAACGCCAAAGGCATCCGCGCCGAATGTGCGGATTGTCACGTACCGCAAGAAGGCTGGCATTATGTCAAAGCCAAATTCATTGCGTTGAAAGATATTTGGTACGAAATGCAGGGCAAATTGGACAGCAAAGAAAAATACGAAGAACACCGTGCGGAAATGGCGCAGCGCGTGTGGAACGATATGAAAGCCACCGATTCGGAAACCTGTCGCAGCTGTCACAGCTTCGATGCTATGGAGCTTTCCGCCCAAACAAAATTAGCCAAACAAACCCATATTGACGCCAAAGCCAACGGACAAACCTGTATCGATTGCCACAAAGGCATCGTGCATTTTTTGCCTGAAGTTCACGCCGATCAAACGACGGCAAAATCCGGCGCACCGAAGGGCAGAATGATAACCGAAAACACCACTTTATATGCCACCGAAATGGTGAAAGCCCAAGGGGCGAAAGGCGGTGAAGTTCGCTTAATGCCCTTTGCCGAAGTGACGGAATGGCAGGCGCAGGGAGATCAAATCCACGGCACGTTACACGGCTGGCAACAAGTGGGCGCGGAATCCGTGGTGTATTTGGATTTAGGCAAACGGATTACAGTGGCGTTGGTGGATGAAGACGCTCGCAGTAACGCACAAGTGTTGCAAACCAAACATGACGATGTGACCGATTCCGAATGGAAAGAAGTGACTTTTGCCGTAAATGTGGCGAAAGAAAAAATGTCTTCAGATTTGACCGCACTTAATCAATACGGCAACCATTTGAATCAAACCAACTGTAGCGGTTGCCATGCTGCAATCGGTGCCGATCACTATACGGCGAACCAATGGATCGGCGTGGTGAATTCCATGAAAGATCGCACGTCCATGACCAAAGACGAAGTACGCGCCGTGACGATTTATTTACAACGCAACGCCAAAGATATGAAAGCAAAA","","","40650","MSKTKKIITALCLMGLGAGALWGTQVVMHETGTPEFCVSCHSMSHPQQEWEGSSHFANAKGIRAECADCHVPQEGWHYVKAKFIALKDIWYEMQGKLDSKEKYEEHRAEMAQRVWNDMKATDSETCRSCHSFDAMELSAQTKLAKQTHIDAKANGQTCIDCHKGIVHFLPEVHADQTTAKSGAPKGRMITENTTLYATEMVKAQGAKGGEVRLMPFAEVTEWQAQGDQIHGTLHGWQQVGAESVVYLDLGKRITVALVDEDARSNAQVLQTKHDDVTDSEWKEVTFAVNVAKEKMSSDLTALNQYGNHLNQTNCSGCHAAIGADHYTANQWIGVVNSMKDRTSMTKDEVRAVTIYLQRNAKDMKAK","1531362","[FUNCTION] Part of the anaerobic respiratory chain of trimethylamine-N-oxide reductase torZ. Required for electron transfert to the torZ terminal enzyme (By similarity)","possible cytochrome c-type protein","Periplasm, Cytoplasm, Inner membrane","","
InterPro
IPR005126
Domain
NapC/NirT cytochrome c, N-terminal
PD004960\"[64-171]TTORY_HAEIN_P44799;
PF03264\"[1-172]TCytochrom_NNT
InterPro
IPR009154
Family
Membrane-bound tetrahaem cytochrome TorC/YecK
PIRSF000014\"[1-366]TMembrane-bound tetrahaem cytochrome TorC/YecK
InterPro
IPR011031
Domain
Multihaem cytochrome
PS51008\"[32-167]T\"[309-323]TMULTIHEME_CYTC
noIPR
unintegrated
unintegrated
signalp\"[1-19]?signal-peptide
tmhmm\"[7-27]?transmembrane_regions


","BeTs to 5 clades of COG3005COG name: Nitrate/TMAO reductases, membrane-bound tetraheme cytochrome c subunitFunctional Class: CThe phylogenetic pattern of COG3005 is --------------efgh--u-----Number of proteins in this genome belonging to this COG is","Significant hit ( 4.7e-05) to 3/4 blocks of the PR00609 family, which is described as \"Class III cytochrome C signature\". Prints database entry for PR:PR00609. PR00609B 64-71 9.7 PR00609C 156-167 0.39 PR00609D 311-318 5.9","Residues 172 to 232 match (1e-11) PD:PD105708 which is described as INNER ELECTRON C-TYPE TORY PROTEOME TRANSMEMBRANE COMPLETE MEMBRANE HEME CYTOCHROME ","","","","","","","","","","","Thu Jan 16 14:11:08 2003","Thu Jan 16 14:08:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02250 is paralogously related to AA00546 (3e-33).","","","","","","Residues 1 to 172 (E-value = 5.1e-100) place AA02250 in the Cytochrom_NNT family which is described as NapC/NirT cytochrome c family, N-terminal region (PF03264)","","","","","del Campillo Campbell,A. and Campbell,A. Alternative gene for biotin sulfoxide reduction in Escherichia coli K-12. J. Mol. Evol. 42 (2): 85-90 (1996) [PubMed: 8919859].Gon,S., Patte,J.C., Mejean,V. and Iobbi-Nivol,C. The torYZ (yecK bisZ) operon encodes a third respiratory trimethylamine N-oxide reductase in Escherichia coli. J. Bacteriol. 182 (20): 5779-5786 (2000) [PubMed: 11004177].Abraham R. Identification of TOR Signaling Complexes. More TORC for the Cell Growth Engine. Cell. 2002 Oct 4;111(1):9. PMID: 12372295 [PubMed - in process] Gon S, Jourlin-Castelli C, Theraulaz L, Mejean V. An unsuspected autoregulatory pathway involving apocytochrome TorC and sensor TorS in Escherichia coli. Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11615-20. PMID: 11562502 Gon S, Giudici-Orticoni MT, Mejean V, Iobbi-Nivol C. Electron transfer and binding of the c-type cytochrome TorC to the trimethylamine N-oxide reductase in Escherichia coli. J Biol Chem. 2001 Apr 13;276(15):11545-51. PMID: 11056172 ","","Thu Jan 16 14:11:08 2003","1","","","" "AA02251","1531426","1533903","2478","ATGAAAAACAGCAACATTAATCATACCCGCCGTGAGTTTTTGAAAAAAACCTCTCTCGGTGTAGCAGGGGCATCGCTTTCCGGCGGTGTGGTCGGTTCCGTTGTATCACCGAAGGCGGCGGCTGCCGAAAAAAGCATGCAAACCGTGGTCACCGCGGCCCACTGGGGGCCTATCGGCGTGGTGGTACAAGACGGCAAAGTGGTGAAATCCGGCCCGGCAATTGAGCCTGCTGCACCGAACGAATTGCAATCGGTCGTGCCGGATCAGCTTTACAGCGAAACCCGCGTGAAATACCCGATGGTGCGTAAAGGCTTCTTAGACAAGCCGGGCAAAAGCGACACCACCATGCGCGGACGTGACGAATGGGTGCGCGTGTCTTGGGATGAAGCGCTGGATTTGGTGCACGAACAATTAAAACGCGTGCGTGATGAACACGGCCCGACAGGCATTTTCGCCGGTTCTTACGGCTGGTTTAGCTGTGGCGCATTACACGCTTCCCGCACCTTATTACAACGTTATATGAACGCCACTGGCGGTTTTGTCGGACATAAAGGCGACTACTCCACCGGCGCGGCGCAAGTGATTATGCCGCACGTGCTTGGCACCATCGAAGTGTATGAGCAACAAACCAGTTGGGAATCCGTGCTGGAACACAGCGATATTATCGTACTTTGGTCGGCAAACCCGCTCACCACCATGCGTATTGCGTGGATGTCCACCGATCAACACGGCATTGACTATTTCAAAAAATTCCAAGCCACCGGCAAACGCATTATTTGTATCGATCCGCAAAAAAGTGAAACCTGCCAGATGCTGAACGCAGAATGGTTGCCGATCAATACCGCAACAGACGTGCCGTTAATGCTCGGCATTGCGCATACCTTAGTCAGCGAAAATAAACACGATAAAGACTTCCTGAAAAAATACACCGCCGGTTATGGCAAATTTGAAGATTACCTGTTGGGCAAAACCGACCAGCAACCGAAAGATGCGGAGTGGGCGAGCAAAATCTGCGGTATTCCGGCAGACACCATAAAACAATTGGCGAAAGATTTCTCAAGCAACCGCACCATGTTAATGGGCGGTTGGGGCATGCAACGCCAACGCCACGGCGAACAAAGCCACTGGATGCTCGTCACCCTCGCTGCCATGCTCGGACAAATCGGCTTGCCGGGTGGCGGATTCGGTTTGAGCTACCATTATTCCAACGGCGGCGTGCCAAGCGCAACCGGCGGGATTATCGGTTCCATCACCGCCAGCCCATCCGCCAAGGCCGGCGCGAAAACCTGGTTGGACGACACCTCTAAGTCTGCATTCCCGTTAGCACGGATTGCCGATGTGTTGCTCAATCCGGGCAAAACCATTCACTATAATGGCACGGAAATCACCTATCCGGACATCAAAGCCGTCTATTGGGCGGGTGGCAATCCGTTTGTACACCATCAAGACACCAACACCTTGGTGAAAGCCTTCCAACGACCCGATGTGGTCATTGTGAACGAAGTGAACTGGACGCCGACTGCACGCATGGCGGACATTGTGTTGCCGGCAACCACCAGTTACGAACGTAACGACCTCACCATGGCGGGCGATTATTCCATGATGAGCGTTTACCCAATGAAACAGGTGGTGCCGCCACAATTTGAAGCGAAAAATGACTACGACATTTTCGTCGAACTGGCAAAACGTGCGGGCGTGGAAGAACAATACACTGAAGGCAAAACGGAAATGGAATGGCTGGAAGAATTCTATAAAGCCGCCTTCACCGCAGCGCGGGCTAACCGCGTTGCCATGCCGCGCTTTGAAAAATTCTGGGTGGAAAATAAACCGTTACGTTTTGAAGCCAATGACGCGGCGAAAAAATGGGTACGCTACGGCGAATTCCGTGAAGATCCGTTGTTAAATCCGCTCGGCACGCCGTCCGGTAAAATTGAAATTTATTCCGACGTGGTCGCCAAAATGAATTACGACGATTGCAAAGGTCACCCAAGTTGGATGGAACCGGAAGAATTTGCCGGCAATGTGACGGAAGAATATCCACTTGCCTTAGTGACACCGCACCCGTATTACCGACTGCACAGCCAATTGGCGCACACTTCATTGCGTCAAAAATATGCGGTGAATGATCGTGAACCGGTGATGATCCACCCGGAAGATGCCGCCCCGCGTGGTATCAAAGACGGTGACATCGTGCGCATTCACAGCAAACGCGGACAAGTGCTTGCCGGCGCCGTGGTCACCGAAAACATCATCAAGGGCACCATTGCCTTGCATGAAGGCGCGTGGTACGACCCGATGGATTTAGGCGAAAGCGAAAAACCATTGTGTAAAAACGGCTGCCCGAACGTGCTCACCCGCGACGAAGGCACTTCCAAACTGGCACAAGGTAACTCACCGAATACCTTTATCGTGCAGGTAGAAAAATTTGTCGGTCAAGCCCCTGAAGTCACTGTGTTTAAACAACCGAAACACGCCGCG","","","91439","MKNSNINHTRREFLKKTSLGVAGASLSGGVVGSVVSPKAAAAEKSMQTVVTAAHWGPIGVVVQDGKVVKSGPAIEPAAPNELQSVVPDQLYSETRVKYPMVRKGFLDKPGKSDTTMRGRDEWVRVSWDEALDLVHEQLKRVRDEHGPTGIFAGSYGWFSCGALHASRTLLQRYMNATGGFVGHKGDYSTGAAQVIMPHVLGTIEVYEQQTSWESVLEHSDIIVLWSANPLTTMRIAWMSTDQHGIDYFKKFQATGKRIICIDPQKSETCQMLNAEWLPINTATDVPLMLGIAHTLVSENKHDKDFLKKYTAGYGKFEDYLLGKTDQQPKDAEWASKICGIPADTIKQLAKDFSSNRTMLMGGWGMQRQRHGEQSHWMLVTLAAMLGQIGLPGGGFGLSYHYSNGGVPSATGGIIGSITASPSAKAGAKTWLDDTSKSAFPLARIADVLLNPGKTIHYNGTEITYPDIKAVYWAGGNPFVHHQDTNTLVKAFQRPDVVIVNEVNWTPTARMADIVLPATTSYERNDLTMAGDYSMMSVYPMKQVVPPQFEAKNDYDIFVELAKRAGVEEQYTEGKTEMEWLEEFYKAAFTAARANRVAMPRFEKFWVENKPLRFEANDAAKKWVRYGEFREDPLLNPLGTPSGKIEIYSDVVAKMNYDDCKGHPSWMEPEEFAGNVTEEYPLALVTPHPYYRLHSQLAHTSLRQKYAVNDREPVMIHPEDAAPRGIKDGDIVRIHSKRGQVLAGAVVTENIIKGTIALHEGAWYDPMDLGESEKPLCKNGCPNVLTRDEGTSKLAQGNSPNTFIVQVEKFVGQAPEVTVFKQPKHAA","1533903","[FUNCTION] Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions (By similarity).[CAUTION] Was originally (Ref.1) assigned to be a biotin sulfoxide reductase hence the original gene designation of bisC.[COFACTOR] Molybdenum (Molybdopterin) (By similarity).","biotin sulfoxide reductase; Trimethylamine-N-oxide reductase precursor","Periplasm","","
InterPro
IPR006311
Domain
Twin-arginine translocation pathway signal
TIGR01409\"[8-41]TTAT_signal_seq: Tat (twin-arginine transloc
InterPro
IPR006655
Family
Prokaryotic molybdopterin oxidoreductase
PS00490\"[505-522]TMOLYBDOPTERIN_PROK_2
PS00932\"[720-747]TMOLYBDOPTERIN_PROK_3
InterPro
IPR006656
Domain
Molybdopterin oxidoreductase
PF00384\"[95-563]TMolybdopterin
InterPro
IPR006657
Domain
Molydopterin dinucleotide-binding region
PF01568\"[681-803]TMolydop_binding
InterPro
IPR006658
Family
Molybdopterin guanine dinucleotide-containing S/N-oxide reductase
TIGR00509\"[52-826]TbisC_fam: molybdopterin guanine dinucleotid
noIPR
unintegrated
unintegrated
G3DSA:2.40.40.20\"[656-825]Tno description
G3DSA:3.40.228.10\"[188-415]Tno description
G3DSA:3.90.55.10\"[524-613]Tno description
PTHR11615\"[164-632]T\"[663-815]TNITRATE, FROMATE, IRON DEHYDROGENASE
PTHR11615:SF19\"[164-632]T\"[663-815]TTRIMETHYLAMINE N-OXIDE REDUCTASE


","BeTs to 18 clades of COG0243COG name: Anaerobic dehydrogenases, typically selenocysteine-containingFunctional Class: CThe phylogenetic pattern of COG0243 is aompkz-q-dr-bcefgh--uj----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-28) to 3/3 blocks of the IPB001467 family, which is described as \"Prokaryotic molybdopterin oxidoreductases\". Interpro entry for IP:IPR001467. IPB001467A 80-102 0.0014 IPB001467B 119-141 3.9e-12 IPB001467C 497-522 8.7e-10","Residues 440 to 487 match (2e-11) PD:PD525838 which is described as REDUCTASE SULFOXIDE PROTEOME BIOTIN COMPLETE OXIDOREDUCTASE 1.-.-.- MOLYBDENUM DIMETHYL SIGNAL ","","","","","","","","","","","Thu Jan 16 14:22:56 2003","Mon Oct 4 16:15:31 2004","","Mon Oct 4 16:15:31 2004","Mon Oct 4 16:15:31 2004","Mon Oct 4 16:15:31 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02251 is paralogously related to AA01137 (6e-84), AA02699 (4e-25), AA00552 (6e-18) and AA02676 (1e-07).","Mon Oct 4 16:15:31 2004","","","","","Residues 681 to 803 (E-value = 2.1e-52) place AA02251 in the Molydop_binding family which is described as Molydopterin dinucleotide binding domain (PF01568)","Mon Oct 4 16:15:31 2004","","","","del Campillo Campbell,A. and Campbell,A. Alternative gene for biotin sulfoxide reduction in Escherichia coli K-12 J. Mol. Evol. 42 (2), 85-90 (1996) M:97077292 Pierson,D.E. and Campbell,A. Cloning and nucleotide sequence of bisC, the structural gene for biotin sulfoxide reductase in Escherichia coli J. Bacteriol. 172 (4), 2194-2198 (1990) M:90202748 Yamamoto,I., Wada,N., Ujiiye,T., Tachibana,M., Matsuzaki,M., Kajiwara,H., Watanabe,Y., Hirano,H., Okubo,A., Satoh,T. and Yamazaki,S. Cloning and nucleotide sequence of the gene encoding dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans Biosci. Biotechnol. Biochem. 59 (10), 1850-1855 (1995) M:96068928 ","","Thu Jan 16 14:22:56 2003","1","","","" "AA02252","1534756","1533980","777","ATGGCAAAACAACCTTTAACCCAACAACTCCTGGATTACGTTTTAAAACAATACGGTACGCAGCCGGAATACTTGTGGAAAAGCCATCCTGATTATGCGGTGTTGCGCCATGGAGATAATCGCAAATGGTATGCCATAGTGATGAACGTGGAAAAAAACGCATTGGGGTTAAGCGGTGCGGGGAAGATGCCGATCATGAATGTGAAATGTTCCCCGGAGATGCTCAGTTTATTTTTGCCGCAAGCGGGATTTTTGCCGGCGTATCACATGAATAAAAATCACTGGTTGACGGTGTTGCTGGACGGTTCGGTGGACAAGGAGACAATTCTGTTTTTGTTGAATGCCAGTTTTGATCTCACCGCTAGCCGACAGGCGAAAAAGCAACTGGGTATCGCCCGTTATACGGAATGGATCGTGCCCGCTAATCCGAAATATTACGATGTGGAAAAAGACTTGCGCGAAGGTGGCGAGCTTCATTGGAAACAGAGTAATAACATTGCGGTGGATGACATTGTTTATATGTATGTCACCGAACCCACCGGTGCGATTCGCTATAAATGTTTGGTGCTGGAAGTGAACATTCCTTATCGTAAAAAACGAACGGACAATTTGCAGGTGAAACGGGTGATGAAAATCCGCTGTCTGAAAGAATACGACAAAACCCTCATTCCCCGCGCTAAAATGGCACAATTCGGCGTGACCGCCGTGCGCGGACCTCGGCACATGCCCTATGCGTTAAAGCAGGAAATTGCGTTATTGAATGGGGAAGGGGAGCGT","","","29819","MAKQPLTQQLLDYVLKQYGTQPEYLWKSHPDYAVLRHGDNRKWYAIVMNVEKNALGLSGAGKMPIMNVKCSPEMLSLFLPQAGFLPAYHMNKNHWLTVLLDGSVDKETILFLLNASFDLTASRQAKKQLGIARYTEWIVPANPKYYDVEKDLREGGELHWKQSNNIAVDDIVYMYVTEPTGAIRYKCLVLEVNIPYRKKRTDNLQVKRVMKIRCLKEYDKTLIPRAKMAQFGVTAVRGPRHMPYALKQEIALLNGEGER","1533980","","conserved hypothetical protein","Periplasm, Cytoplasm","","
InterPro
IPR007351
Family
Protein of unknown function DUF419
PF04237\"[14-121]TDUF419


","No hits to the COGs database.","","Residues 137 to 242 match (2e-16) PD:PD458649 which is described as PROTEOME COMPLETE SPY1552 ","","","","","","","","","","","","Thu Jan 16 14:24:03 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02252 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 14 to 121 (E-value = 3.1e-33) place AA02252 in the DUF419 family which is described as Protein of unknown function (DUF419) (PF04237)","","","","","","","","1","","","" "AA02253","1534745","1534846","102","TTGTTTTGCCATATTTGGACCTCGCTTCAGATTGTTTATCGTTCTATTCTACGCCAAAACGGCTGGATTGTGGCGGTCTTGATCGCCCTTAAAAAACACCGC","","","4059","LFCHIWTSLQIVYRSILRQNGWIVAVLIALKKHR","1534846","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-17]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:06:07 2004","Wed Feb 25 15:06:07 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02253 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:06:07 2004","","","","","","","","","","","","","1","","","" "AA02254","1534986","1536440","1455","ATGGAAGGTAAAACAATAACGCCGGTAGAAGTAAAACTCGGCTTCAAATGGCAAGGATTATTGCTTTCGGTTTTGGTCAGTTTGGCGATTTGGTTTATACCGATACCGGAAGGGCTATCAACCAAAGCCTGGGGCATGCTTGCCTTATTCGTCGCCACCATTGTCGCCATTATCGCCAAAGCCATGCCGATGGGTGCAGCGACCTTAGTGGCATTAGTTATCAGTGGGCTGACAGGTCTCACACCGCTTTCGCCAAAACAAGGCGAAGTCGGTATGTTATCGGGCTTTGCTAACGGAACAATTTGGCTAATCGCCATTGCCATGTTTTTATCCCGCGCAGTGATCAAAACAGGGCTTGGGAAACGCATCGCCCTCTACTTCGTCGCGCGCCTTGGTAAAAAAATGATGGGCGTGGCTTACGGCATGGCGTTAGCCGATGTGGTTATCGGTCCAGGCATTCCCTCCGCCTCGGCGCGTGGTGGCGGTATTATGTACCCGATTATGCAATCTATCGCCGATGCTTATGATTCCAAACCAGGTCCGACCGCAAGACGTGCCGGCGCATTTTTGGCGATCGCCGTCTCACAAATCGACACCATCGTGTGTACCATGTTTCTCACCGCCATGGCAGGTAACCCGTTAATCACCGAATTGGCGAAAGGTCAAGGTGTTGAAATCACTTGGATGACCTGGTTTTTGGGCGCCATCGTACCGGGTGTGATTAGCCTCATTGTGTTGCCGTATTTCGTCTATTTAATCTATCCGCCGGAACTCAAAGATACGCCGAAAATGGCAGAAATGGCGCGGGAAGAATTGCGTAACACGGGACCAATGAGCAAAGCGGAATGGATCTTAGCGCTGGATTTCATCTTATTGTTGTTCTTATGGACAGTGGGCGATTTGATTTTCCATATTCCCGCAACCGTTTCCACCTTTATCGGCTTAGTGATATTGCTGCTCACCAATATCATGAGTTGGAAAAACATCGTTGCAGAAACCACCGCGTGGGACACTATGTTTTGGTTTGCGGTTTTAGTGATGATGGCGAATGCACTCAATAAATACGGCGCTATTGCGTGGATTTCCAGCCACATTTCCTCTTCCGTTGGCGCGTTCAGTTGGCCGGTTGCCTTTACGATTTTAGTCTTGGTGTATTTTTACACCCGCTATTTCTTCGCTTCCGCCGTGGCGCATATTTCTGCTATGTATTTGGCTTTCGTCGCTGCCGCCATCTCTGTCGGCACACCGCCGATTATCGCCGCACTCGGCTTAGGTTACACCTCCACATTATCCATGAGCTTAACCCAATATGCCGGCGGCCCCGGTCCGGCACTTTACGGATCCGGCTATAACTCAACCAGTCAATGGTGGGGCGTGAGTTTCGTCACCTCCATCATTTCCCTCATTATCTGGTTCGGTGCAGGCGGGTTATGGATGAAATTATTGGGTTGGTGG","","","52073","MEGKTITPVEVKLGFKWQGLLLSVLVSLAIWFIPIPEGLSTKAWGMLALFVATIVAIIAKAMPMGAATLVALVISGLTGLTPLSPKQGEVGMLSGFANGTIWLIAIAMFLSRAVIKTGLGKRIALYFVARLGKKMMGVAYGMALADVVIGPGIPSASARGGGIMYPIMQSIADAYDSKPGPTARRAGAFLAIAVSQIDTIVCTMFLTAMAGNPLITELAKGQGVEITWMTWFLGAIVPGVISLIVLPYFVYLIYPPELKDTPKMAEMAREELRNTGPMSKAEWILALDFILLLFLWTVGDLIFHIPATVSTFIGLVILLLTNIMSWKNIVAETTAWDTMFWFAVLVMMANALNKYGAIAWISSHISSSVGAFSWPVAFTILVLVYFYTRYFFASAVAHISAMYLAFVAAAISVGTPPIIAALGLGYTSTLSMSLTQYAGGPGPALYGSGYNSTSQWWGVSFVTSIISLIIWFGAGGLWMKLLGWW","1536440","[FUNCTION] Transports carbon skeletons into chloroplasts for net glutamate synthesis. This translocator exchanges malate for internal succinate, fumarate and 2-oxoglutarate but not for aspartate and glutamate. ","2-oxoglutarate/malate translocator","Inner membrane, Cytoplasm","","
InterPro
IPR001898
Family
Sodium/sulphate symporter
PF00939\"[14-485]TNa_sulph_symp
TIGR00785\"[34-479]Tdass: transporter, divalent anion:Na+ sympo
noIPR
unintegrated
unintegrated
PTHR10283\"[35-485]TCATION TRANSPORTER RELATED
PTHR10283:SF13\"[35-485]TSODIUM/CARBOXYLATE COTRANSPORTER RELATED
signalp\"[1-29]?signal-peptide
tmhmm\"[15-35]?\"[41-63]?\"[65-85]?\"[91-111]?\"[188-208]?\"[235-255]?\"[276-294]?\"[300-320]?\"[341-361]?\"[371-393]?\"[403-423]?\"[456-478]?transmembrane_regions


","BeTs to 11 clades of COG0471COG name: Di- and tricarboxylate transportersFunctional Class: PThe phylogenetic pattern of COG0471 is -om-k-yq-d-lbcefghsnu--i--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.7e-11) to 5/8 blocks of the IPB001898 family, which is described as \"Sodium:sulfate symporter family\". Interpro entry for IP:IPR001898. IPB001898A 57-80 1.1e+02 IPB001898B 102-128 0.076 IPB001898E 226-250 44 IPB001898F 275-301 0.029 IPB001898G 333-362 0.14","Residues 401 to 483 match (4e-13) PD:PD016140 which is described as COMPLETE PROTEOME TRANSLOCATOR 2-OXOGLUTARATE/MALATE MEMBRANE TRANSMEMBRANE TRANSPORTER INNER CITRATE CARRIER ","","","","","","","","","","","Thu Jan 16 14:28:31 2003","Thu Jan 16 14:28:31 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02254 is paralogously related to AA00741 (5e-72), AA00941 (6e-31) and AA01784 (8e-04).","","","","","","Residues 14 to 485 (E-value = 2.9e-166) place AA02254 in the Na_sulph_symp family which is described as Sodium:sulfate symporter transmembrane region (PF00939)","","","","","","","","1","","","" "AA02257","1536658","1536909","252","ATGACAAGCCTTGTTTTAACCGATGTTGTCGCCAGCATCACCGAATTAAAAACCAATCCCATGGCGGTACTTCGTGAAGCCGGTGGAAAACCGCTGGCAATTTTAAACCGTAATGAACCCGCATTTTATTGCGTCCCACCGGCAATTTATGAATATCTAATGGAATTAGTCGATGATGCCGAATTAGCAAAAATTGTGGAAGAACGTCAACATGAAAAAAGTTATCCTGTTGATTTAGAGGATTTACTACAA","","","12141","MTSLVLTDVVASITELKTNPMAVLREAGGKPLAILNRNEPAFYCVPPAIYEYLMELVDDAELAKIVEERQHEKSYPVDLEDLLQ","1536909","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003756
Family
Protein of unknown function DUF172
PF02604\"[8-75]TPhdYeFM
InterPro
IPR006442
Family
Prevent-host-death protein
TIGR01552\"[10-61]Tphd_fam: prevent-host-death family protein


","No hits to the COGs database.","","Residues 1 to 82 match (4e-19) PD:PD019736 which is described as PROTEOME COMPLETE PLASMID CYTOPLASMIC REPLICON VCA0445 VCA0477 INCF STBD STABILITY ","","","","","","","","","","","","Thu Jan 16 14:29:43 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02257 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02259","1537006","1537188","183","GTGCCGAAAATCCGAGTGCCATCCGCCAAATTACACGGCATGAAAGATTGCTATAAAATCAAATTACGCAATGTAGGGTATCATTTGGTGTATCAGGTTATTGATGAACGCATTGTGGTCAAAATCATCGCCGTAGGAAAACGCGATCGAAATTTTGTTTATACCAAAGCCAAAAGCAGGCTT","","","7108","VPKIRVPSAKLHGMKDCYKIKLRNVGYHLVYQVIDERIVVKIIAVGKRDRNFVYTKAKSRL","1537188","","possible RelE-like protein","Cytoplasm","","
InterPro
IPR007712
Family
Plasmid stabilization system
PF05016\"[10-52]TPlasmid_stabil


","BeTs to 3 clades of COG2026COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG2026 is a-m-kz----r--ce-g---------Number of proteins in this genome belonging to this COG is","","Residues 6 to 50 match (4e-10) PD:PD020125 which is described as COMPLETE PROTEOME PLASMID RELE INNER CYTOPLASMIC VLP VCA0478 STBE STABILITY ","","","","","","","","","","","","Thu Jan 16 14:31:50 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02259 is paralogously related to AA02767 (4e-11).","","","","","","","","","","","Saul,D., Spiers,A.J., McAnulty,J., Gibbs,M.G., Bergquist,P.L. and Hill,D.F. Nucleotide sequence and replication characteristics of RepFIB, a basic replicon of IncF plasmids. J. Bacteriol. 171 (5): 2697-2707 (1989) [PubMed: 2651415].","","Thu Jan 16 14:31:50 2003","1","","","" "AA02260","1538022","1537207","816","ATGCACGCCATTTCAACAAGATTAAGGCAAAACATGAAAATCGCATTAGGTGTGGAATACGACGGAAAACATTACTTTGGCTGGCAACGACAAGAAAAAGTTGCCAGCATACAGGCGGAATTAGAACGGGCGATTTCCGTAATTGCCAATGAGGACATCGGCATTTTCTGCGCCGGTCGCACCGATTCCGGCGTGCACGCCACAGGGCAAGTGATCCATTTTGAAACCACGGCACAACGCCCTGAAAAAGCCTGGAGTTTCGGTGTGAACGCCAATTTGCCCGATGATATCGCCGTGCGTTGGGCGAAAGTCGTGGAGGACGATTTTCATGCCCGCTTTAGCGCTACTGCGCGGCGTTATCGTTACATTTTATATTGTAATAAACTGCGCTCGGCGATTTTGCCGCAAGGCGTAACCCATTGCCATTTAGAACTCGATCATCAATTAATGCACGACGCGGGACAGGCGCTGCTCGGCGAAAATGATTTCAGCTCCTTCCGCGCCGCTCAATGCCAATCCAACACCCCATGGCGCAACGTCCATCATTTAAACGTCACTCGTCAGGGGCAGTACATTATCGTGGATATTCAAGCTAACGCTTTTGTGCATCACATGGTGCGTAATATCGTCGGCAGCCTTATTGAAGTGGGCTGTTGCAATCAACCCGTTGAGTGGATGAAATGGTTGTTGGAGCAAAAAGACCGCGCCCTCGCCGCGCCCACCGCGAAACCGGAAGGGTTGTATCTGGTGAATGTCATTTACCCCGACAACTTTAATCTGCCGAAAATGCCAATGGGACCGTTGTTTCTGGCGGAT","","","30819","MHAISTRLRQNMKIALGVEYDGKHYFGWQRQEKVASIQAELERAISVIANEDIGIFCAGRTDSGVHATGQVIHFETTAQRPEKAWSFGVNANLPDDIAVRWAKVVEDDFHARFSATARRYRYILYCNKLRSAILPQGVTHCHLELDHQLMHDAGQALLGENDFSSFRAAQCQSNTPWRNVHHLNVTRQGQYIIVDIQANAFVHHMVRNIVGSLIEVGCCNQPVEWMKWLLEQKDRALAAPTAKPEGLYLVNVIYPDNFNLPKMPMGPLFLAD","1537207","[FUNCTION] Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs (By similarity).","pseudouridylate synthase I","Cytoplasm","","
InterPro
IPR001406
Family
tRNA pseudouridine synthase
G3DSA:3.30.70.580\"[9-115]Tno description
G3DSA:3.30.70.660\"[116-252]Tno description
PTHR11142\"[14-256]TPSEUDOURIDYLATE SYNTHASE
PF01416\"[16-114]T\"[153-255]TPseudoU_synth_1
TIGR00071\"[13-249]ThisT_truA: tRNA pseudouridine synthase A


","BeTs to 24 clades of COG0101COG name: Pseudouridylate synthase (tRNA psi55)Functional Class: JThe phylogenetic pattern of COG0101 is aompk-yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 6.2e-70) to 6/6 blocks of the IPB001406 family, which is described as \"tRNA pseudouridine synthase\". Interpro entry for IP:IPR001406. IPB001406A 13-41 2.9e-13 IPB001406B 58-74 3e-12 IPB001406C 93-124 5.3e-21 IPB001406D 157-168 0.0069 IPB001406E 198-213 7.7e-10 IPB001406F 240-249 0.0031","Residues 12 to 254 match (3e-116) PD:PD003202 which is described as SYNTHASE PSEUDOURIDINE TRNA I PROTEOME COMPLETE PSEUDOURIDYLATE LYASE A PROCESSING ","","","","","","","","","","","Thu Jan 16 14:36:24 2003","Thu Jan 16 14:36:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02260 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 153 to 255 (E-value = 2.1e-31) place AA02260 in the PseudoU_synth_1 family which is described as tRNA pseudouridine synthase (PF01416)","","","","","Kammen,H.O., Marvel,C.C., Hardy,L. and Penhoet,E.E. Purification, structure, and properties of Escherichia coli tRNA pseudouridine synthase I J. Biol. Chem. 263 (5), 2255-2263 (1988) PubMed: 3276686 Huang,L., Pookanjanatavip,M., Gu,X. and Santi,D.V. A conserved aspartate of tRNA pseudouridine synthase is essential for activity and a probable nucleophilic catalyst Biochemistry 37 (1), 344-351 (1998) PubMed: 9425056 Huang,L., Pookanjanatavip,M., Gu,X. and Santi,D.V. A conserved aspartate of tRNA pseudouridine synthase is essential for activity and a probable nucleophilic catalyst. Biochemistry 37 (1): 344-351 (1998) [PubMed: 9425056].Nonet,M.L., Marvel,C.C. and Tolan,D.R. The hisT-purF region of the Escherichia coli K-12 chromosome. Identification of additional genes of the hisT and purF operons. J. Biol. Chem. 262 (25): 12209-12217 (1987) [PubMed: 3040734].Arps,P.J., Marvel,C.C., Rubin,B.C., Tolan,D.A., Penhoet,E.E. and Winkler,M.E. Structural features of the hisT operon of Escherichia coli K-12 . Nucleic Acids Res. 13 (14): 5297-5315 (1985) [PubMed: 2991861]","","Thu Jan 16 14:36:24 2003","1","","","" "AA02261","1538542","1538153","390","ATGGCAGAGAATCAAAACTACGGCACAGGTCGCCGCAAAAGCTCTTCAGCTCGTGTATTTATCAAACCGGGCAATGGTAAGATCACTATCAACCAACGTGAATTAGACGTTTACTTCGGTCGCGAAACTGCACGCATGGTAGTTCGTCAACCGTTAGAATTGGTTGAATTAACTGATAAATTAGACCTATACATCACTGTTAAAGGTGGTGGTATTTCCGGTCAAGCGGGTGCAATTCGTCATGGTATTACCCGTGCATTGATGGAATACGATGAAACCCTACGCCCTGTACTTCGTGCAGCAGGCTTCGTTACTCGTGACGCACGTCGCGTTGAACGTAAAAAAGTGGGTTTGCACAAAGCACGTCGTCGTCCACAATACTCCAAACGT","","","14754","MAENQNYGTGRRKSSSARVFIKPGNGKITINQRELDVYFGRETARMVVRQPLELVELTDKLDLYITVKGGGISGQAGAIRHGITRALMEYDETLRPVLRAAGFVTRDARRVERKKVGLHKARRRPQYSKR","1538153","","30S ribosomal protein S9","Cytoplasm, Extracellular","","
InterPro
IPR000754
Domain
Ribosomal protein S9
PD001627\"[1-88]TRS9_PASMU_Q9CNB1;
PF00380\"[10-130]TRibosomal_S9
PS00360\"[69-87]TRIBOSOMAL_S9
InterPro
IPR014721
Domain
Ribosomal protein S5 domain 2-type fold
G3DSA:3.30.230.10\"[3-130]Tno description
noIPR
unintegrated
unintegrated
PTHR21569\"[1-130]TRIBOSOMAL PROTEIN S9


","No hits to the COGs database.","Significant hit ( 3.8e-55) to 3/3 blocks of the IPB000754 family, which is described as \"Ribosomal protein S9\". Interpro entry for IP:IPR000754. IPB000754A 10-32 2.4e-12 IPB000754B 51-88 1.5e-21 IPB000754C 103-130 1.3e-18","Residues 7 to 89 match (5e-35) PD:PD001627 which is described as RIBOSOMAL 30S S9 COMPLETE PROTEOME 40S CHLOROPLAST S16 S9P TRANSIT ","","","","","","","","","","","","Thu Jan 16 14:41:20 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02261 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 10 to 130 (E-value = 6.4e-66) place AA02261 in the Ribosomal_S9 family which is described as Ribosomal protein S9/S16 (PF00380)","","","","","Isono,S., Thamm,S., Kitakawa,M. and Isono,K. Cloning and nucleotide sequencing of the genes for ribosomal proteins S9 (rpsI) and L13 (rplM) of Escherichia coli Mol. Gen. Genet. 198 (2), 279-282 (1985) PubMed: 3884974 Chen,R. and Wittmann-Liebold,B. The primary structure of protein S9 from the 30S subunit of Escherichia coli ribosomes FEBS Lett. 52 (1), 139-140 (1975) PubMed: 1091515 Urlaub,H., Kruft,V., Bischof,O., Muller,E.C. and Wittmann-Liebold,B. Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies. EMBO J. 14 (18): 4578-4588 (1995) [PubMed: 7556101].Marsh,R.C. and Parmeggiani,A. Requirement of proteins S5 and S9 from 30S subunits for the ribosome-dependent GTPase activity of elongation factor G. Proc. Natl. Acad. Sci. U.S.A. 70 (1): 151-155 (1973) [PubMed: 4346030].Arnold,R.J. and Reilly,J.P. Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry. Anal. Biochem. 269 (1): 105-112 (1999) [PubMed: 10094780].","","Thu Jan 16 14:41:20 2003","1","","","" "AA02262","1538987","1538562","426","ATGAAAACTTTTGTAGCAAAACCGGAAACGGTTAAACACGACTGGTATGTAGTTGATGCGACAGGTAAAACTTTAGGTCGTTTGGCGACTGAATTGGCACGTCGTCTTCGTGGTAAACATAAAGCTGAATATACGCCGCACGTTGATACAGGTGATTACATCATCGTGATTAACGCGGACAAAGTTGCTGTAACCGGTAACAAAGAAAGCGATAAAATTTACTACTGGCACACAGGCTATGTAGGTGGTATCAAACAAGCGACTTTCAAAGAAATGATCGCGCGCCGTCCTGAAGCAGTGATTGAAATTGCGGTTAAAGGTATGTTGCCAAAAGGTCCATTGGGCCGCGCAATGTTCCGCAAATTAAAAGTGTACGCAGGTGCTGAACACCAACACGCTGCACAACAACCACAAGTATTAGACATT","","","15900","MKTFVAKPETVKHDWYVVDATGKTLGRLATELARRLRGKHKAEYTPHVDTGDYIIVINADKVAVTGNKESDKIYYWHTGYVGGIKQATFKEMIARRPEAVIEIAVKGMLPKGPLGRAMFRKLKVYAGAEHQHAAQQPQVLDI","1538562","[FUNCTION] This protein is one of the early assembly proteins of the 50S ribosomal subunit. ","50S ribosomal protein L13","Cytoplasm, Periplasm","","
InterPro
IPR005822
Family
Ribosomal protein L13
PD001791\"[51-122]TRL13_HAEIN_P44387;
PTHR11545\"[1-142]TRIBOSOMAL PROTEIN L13
PF00572\"[15-142]TRibosomal_L13
PS00783\"[105-127]TRIBOSOMAL_L13
InterPro
IPR005823
Family
Ribosomal protein L13, bacterial and organelle form
PTHR11545:SF2\"[1-142]T50S RIBOSOMAL PROTEIN L13
TIGR01066\"[3-142]TrplM_bact: ribosomal protein L13
noIPR
unintegrated
unintegrated
G3DSA:3.90.1180.10\"[15-142]Tno description


","BeTs to 26 clades of COG0102COG name: Ribosomal protein L13Functional Class: JThe phylogenetic pattern of COG0102 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-27) to 2/2 blocks of the IPB001074 family, which is described as \"Ribosomal protein L13\". Interpro entry for IP:IPR001074. IPB001074A 36-63 2.2e-18 IPB001074B 95-110 9.4e-08","Residues 17 to 127 match (1e-08) PD:PD335764 which is described as RIBOSOMAL 60S 50S COMPLETE PROTEOME L13P L13A FAMILY MULTIGENE ANTIGEN ","","","","","","","","","","","Thu Jan 16 14:44:50 2003","Thu Jan 16 14:44:50 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02262 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 15 to 142 (E-value = 8e-88) place AA02262 in the Ribosomal_L13 family which is described as Ribosomal protein L13 (PF00572)","","","","","Sanchez C, Blanco G, Mendez C, Salas JA. Cloning, sequencing and transcriptional analysis of a Streptomyces coelicolor operon containing the rplM and rpsI genes encoding ribosomal proteins ScoL13 and ScoS9. Mol Gen Genet. 1997 Dec;257(1):91-6. PMID: 943957Isono,S., Thamm,S., Kitakawa,M. and Isono,K. Cloning and nucleotide sequencing of the genes for ribosomal proteins S9 (rpsI) and L13 (rplM) of Escherichia coli. Mol. Gen. Genet. 198 (2): 279-282 (1985) [PubMed: 3884974].Mende,L. The primary structure of protein L13 from the large subunit of Escherichia coli ribosomes. FEBS Lett. 96 (2): 313-316 (1978) [PubMed: 365580].Link,A.J., Robison,K. and Church,G.M. Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis 18 (8): 1259-1313 (1997) [PubMed: 9298646].","","Thu Jan 16 14:44:50 2003","1","","","" "AA02263","1539825","1539232","594","ATGACAAAATGGGATGAGCGTTATCAAACGGAAGACTATATTTTTGGTACGGAACCCAATGAATTTATCGCCAGAATTCAATCTTATCTGCCCACTTCCGGGCGAGCATTGGATCTGGCTACCGGAGAAGGGCGTAATGGTGTCTTTTTAGCTTTGCATGGATTGGAAACGGAAGGGGTTGATATGTCTAAAGTGGGTTTGCTCAAAGCGCAAGCGTTGGCGCGTAAGCAAAATGTTTCGTTTACTACAAGATTGGCCAATATTGCAGAGATGGATATGCCGACAGCATATTATGCCGTAATTACTTCCGTTTTTTGTCATTTTATGGAACCGCAAAGAACGCAAGTGATGCAACGTATTGTGAATGCATTGCAACCGGGTGGGTTATTTGCCGGCGTGTTTTATCATCCGGACCAAATTCATTATGGCACCGGTGGACCCGGTCAGGTTGAAATGTTGGGTACATTGGCACAGATGCAGCAGGCGTTAGCAGGCTTGGAATGGCTTATTGCAGAGCATAGCGTGCGCGAGATGAATGAAGGAAATCGCCATATCGGCACCAGTTCGGTAATTTGTCTGTTGGGACGTAAGCCT","","","21936","MTKWDERYQTEDYIFGTEPNEFIARIQSYLPTSGRALDLATGEGRNGVFLALHGLETEGVDMSKVGLLKAQALARKQNVSFTTRLANIAEMDMPTAYYAVITSVFCHFMEPQRTQVMQRIVNALQPGGLFAGVFYHPDQIHYGTGGPGQVEMLGTLAQMQQALAGLEWLIAEHSVREMNEGNRHIGTSSVICLLGRKP","1539232","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR013216
Domain
Methyltransferase type 11
PF08241\"[37-132]TMethyltransf_11
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[16-141]Tno description
PTHR10108\"[4-131]TMETHYLTRANSFERASE


","BeTs to 13 clades of COG0500COG name: SAM-dependent methyltransferasesFunctional Class: Q,RThe phylogenetic pattern of COG0500 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 135 to 197 match (6e-08) PD:PD074389 which is described as PROTEOME COMPLETE PA5115 SLR1183 ","","","","","","","","","","","","Thu Jan 16 14:46:22 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02263 is paralogously related to AA01984 (1e-07).","","","","","","","","","","","","","","1","","","" "AA02265","1541817","1539841","1977","ATGTTAGCTTTATTATCCCAACTCAAAGAAAAGGGCATCATCAACGCCGCTGACTATTATTTCGCCGAGTTTATTCACCGCAAACAACAGCCTTTTCACTATGCATCGTCTATCCAGAACCTGGCGGTGCTTATGGCGGCGTTGTGCAACTTCAGTTATCGGCAGGGCAACACCTGTATTTTACTGAATCACGCCACGGAGCAGGATTTGTTCGGTTTACAGGATTATTTTAACGAACGCGTTTATTTAACGGATATTCAGCAAAAAATTGATTATTTGCCCATTGAACGCTGGCAGGCAGCCTTGCTGGCGGCGCAACATATCGCTTTCACCGCCGCGCCTTTGCAACAGATCGCGCCCCTGGTGTTGCAGTTTGAGCGCTTGTATTTTTATCGCATCTGGCAGGATGAGTTTCGTATCGCCGATTACTTTAAAAGTGCGGTCCGTTTTCAACACGTTTTTTCAGCCGAACAGACGGCGCAAATCGCCCCGATTTTGAACCGCTATTTTTATGAAGAACAGGGCATCGACTGGCAAAAAATCGCGGTGGCGATGGCATTGCGTCAACGATTTTGCCTCATTACCGGCGGGCCGGGCACGGGCAAAACCACTACCGTCACCAAACTCCTATTGACCTTGCAGGAGCTTCATCAAAACGGCTTGCGCATTAAACTTGTCGCCCCGACAGGGAAAGCGGCGGCGCGGCTTACGGAATCCATTGTGGACGCGGTAGATCGCCTGAAACAGACTTTTTCCACGGAAAAACACGAGCGAGAAATCATCGAAAATCTGCGCATTCCCATGAATGCGGAAACCATTCATCGCTTGCTCGGCGTGCGTTTTTTCAGTGAGGAAACCCGCTATCATGTCGACAATCCTTTGCCCGTGGATGTGTTGGTGGTGGACGAAGCATCCATGATCGATTTAACCTTGATGGCGAAGCTGCTCAATGCCCTTAAACCGGAAACCAAATTGATTTTATTGGGTGATAAAGATCAGCTGGCTTCTGTAGAAGCCGGGGGGATTTTGGGTGAATTAGGGCGTTTCGTGAATGCGTCGGCGCCGACGTATAGCCTCGTAATGACACGATATTTACAGGCGACCACGGGCAGTTCTCTTGCTGCGTCGGATAGCGTCAATCCTATCGGTGATAGCATTTGTTATTTGCAGGTCAGCCGCCGTTTCGGGGCAAATCCGGAAGTGGGTGCGTTGGCGGCTGCGGTGAATTCAGGCGACGCGGTGAAAAGCTGGCAGTTATTGCAGCAATATCAGCAATATCAAGCAAAAAAATGCGGCGTATATTTAACGGATTTTGCTCATTATTTAAATAACAAAGAAGATATTCAGCAACGTAAAACCTGCGTGAAGCTCATCGTGGAACGTGCGGCAGAGGAATATCGCCGTTATTTGCAGTTGATTTTACAAGAAGGGCAGATGGATGAAGAAAAAGTGCGGTCGATTTTCGCGGCGTTTAACGGCATTCGTTTTTTAGCGGCGTTGCGTGTGGGCGAATTCGGCGTGGAGCAATTAAATCTCGCCATCGCAGAAAAATTACGCCAAAAACGCCTGTTGCAATTTCATCAGGAACGGGAATGGTACATCGGCAAACCGATTATGGTGACGCAAAATGATGGCAATGTGGGCTTGTATAACGGTGACATCGGCATGTATTTGGGAAACGGACGGGTATGGTTCGAGCAGGGACAAAACAGTTATAAAACTGTGCTGGCAAGCCGCGTGCCGAATCATGAAACCGCCTTCGTCATGACGGTACACAAATCCCAAGGTTCGGAATTTCCGCATACTTTCCTGATTTTGCCATTGGAAAACAGCCCCGTGTTATCCAAAGAACTGGTTTACACCGGCATCACCCGCACCAAGGATTTTTTAACGGTGTTCGCGCTACAAAGCGTATGGGAAAGTGCGGTGAAAAATCCGGTGCAACGGCAAAGCGGATTGGGTCAATTACTGGAAATC","","","74720","MLALLSQLKEKGIINAADYYFAEFIHRKQQPFHYASSIQNLAVLMAALCNFSYRQGNTCILLNHATEQDLFGLQDYFNERVYLTDIQQKIDYLPIERWQAALLAAQHIAFTAAPLQQIAPLVLQFERLYFYRIWQDEFRIADYFKSAVRFQHVFSAEQTAQIAPILNRYFYEEQGIDWQKIAVAMALRQRFCLITGGPGTGKTTTVTKLLLTLQELHQNGLRIKLVAPTGKAAARLTESIVDAVDRLKQTFSTEKHEREIIENLRIPMNAETIHRLLGVRFFSEETRYHVDNPLPVDVLVVDEASMIDLTLMAKLLNALKPETKLILLGDKDQLASVEAGGILGELGRFVNASAPTYSLVMTRYLQATTGSSLAASDSVNPIGDSICYLQVSRRFGANPEVGALAAAVNSGDAVKSWQLLQQYQQYQAKKCGVYLTDFAHYLNNKEDIQQRKTCVKLIVERAAEEYRRYLQLILQEGQMDEEKVRSIFAAFNGIRFLAALRVGEFGVEQLNLAIAEKLRQKRLLQFHQEREWYIGKPIMVTQNDGNVGLYNGDIGMYLGNGRVWFEQGQNSYKTVLASRVPNHETAFVMTVHKSQGSEFPHTFLILPLENSPVLSKELVYTGITRTKDFLTVFALQSVWESAVKNPVQRQSGLGQLLEI","1539841","[FUNCTION] Exhibits several catalytic activities, including ATP-dependent exonuclease, ATP-stimulated endonuclease,ATP-dependent unwinding and DNA-dependent atpase activities. strand cleavage occurs 5' to 3' during the unwinding of duplex DNA at chi sequences, which locally stimulate recombination (by similarity). ","exodeoxyribonuclease V, alpha chain","Cytoplasm, Inner membrane","","
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[188-393]TAAA
InterPro
IPR006344
Family
Exodeoxyribonuclease V, alpha subunit
TIGR01447\"[5-657]TrecD: exodeoxyribonuclease V, alpha subunit
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[165-333]Tno description


","No hits to the COGs database.","Significant hit ( 3.2e-11) to 4/7 blocks of the IPB000212 family, which is described as \"UvrD/REP helicase\". Interpro entry for IP:IPR000212. IPB000212A 196-206 0.0042 IPB000212B 223-240 4.9 IPB000212F 586-604 0.0034 IPB000212G 614-626 57","Residues 221 to 289 match (4e-07) PD:PD000627 which is described as HELICASE COMPLETE PROTEOME DNA ATP-BINDING HYDROLASE ATP-DEPENDENT EXODEOXYRIBONUCLEASE II DNA-BINDING ","","","","","","","","","","","Thu Jan 16 14:50:59 2003","Thu Jan 16 14:50:59 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02265 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Finch,P.W., Storey,A., Brown,K., Hickson,I.D. and Emmerson,P.T. Complete nucleotide sequence of recD, the structural gene for the alpha subunit of Exonuclease V of Escherichia coli. Nucleic Acids Res. 14 (21): 8583-8594 (1986) [PubMed: 3537961].Finch,P.W., Storey,A., Chapman,K.E., Brown,K., Hickson,I.D. and Emmerson,P.T. Complete nucleotide sequence of the Escherichia coli recB gene . Nucleic Acids Res. 14 (21): 8573-8582 (1986) [PubMed: 3537960].","","Thu Jan 16 14:50:59 2003","1","","","" "AA02266","1545482","1541820","3663","ATGCAAGCACTCAATCCGATTTCCATTCCGTTAAACGCCATCAGTCTTATTGAAGCCTCTGCAGGGACGGGCAAAACCTACACCATGGGTTCTCTTTATTTGCGTCTGTTGTTGCAGGCGGGGGAAAATGCCTTTCCTCATGTGTTAAATGTGGAGCAAATTTTGGTGGTGACCTTTACCGAAATGGCAACGGAGGAACTGAAACGTAAAATTCGCGAGCGGATTTATGACGCCAAACAAAAATTGACGGCGTATCAACAAACGCAGGATCCGACGGTGTTTGAACACGATGACTTTTTACGCCAATTAGCCGATACCATCACGGATTTCCCTCTTGCCATTCAGCGCCTGACTTTGGCGGAACAAAACATGGATTTGGCGGCGATTTATACCATTCATGGATTTTGCCGTCGAATGCTCATGCAATATGCGTTTAATTCGGGCATTCATTTCAACTTGGAATTAAGCGGTGAAGAAGACGAATTGTTGCTACATTTGGCGCAAAAACTGTGGCGGGCACATTTCTATTCGCAGCCTTATGCCGTTGCCGAGTTTATTCAAAAACACCTGATTTCACCGGCAAACGTCATTCATAATATTAAAAAGTTTGCCGGCACGGAATTAAAACTCCCGCAAAATCGACCGTACTTTTTTGACGGCGCATTGCCGGATTTTCTCGCTAAACTTGCCGATTATTCGCAACAACTTTCCGCACAAATTGCGGAAGTGAAAGAGAATTGGCTAAAAAATGAAGAGGAGATTACGCAGTTAATCGAAACGGAAGTGAATACCAAGTATAAAAGCGCAAAAGAACAAAAATTAAACCGACGCAGTTTTACCTCCGCAACCCGCCCGAAATGGCTTGCCATGATGAAAGCTTGGGCTGAAAGCGATAAAGCGGATTTTCCGGATTGTTTTTCCCGTTTCGGGCAAACGGCGATAAATGCTCAAAAGGGCGAGGAGGCGAAAGACGCCTTAACCCATTCGCTTTTTGTGCAAATTAATGCCTTGTTGGCACTGTCCGAGCAAAAGGCGTTATTATCCCAAGCCTTGTGGTTCCATTATTTACAAATGCTGAATGCGCAGCTGGTGGAATATAAACTTAACCACAGCGAAAAAAGTTTTAACGATTTGCTACGCTTGCTGAAAGAAGCCTTGTATCACCCGGATAACACGGAATTTGCCCGCCTGATTCGTTATCAATTTCCTTTTGCCATGATTGATGAATTTCAGGACACGGATGCGGTGCAGTATCAGATTTTTTCTAAAATTTATGTGGAACAACCTCAGACAGACGCTCAATCTGATAGCGGCTTTATTATGATTGGCGACCCGAAACAGGCGATTTATAAATTCCGTGGCGCCGACATTTTTACTTATTTCCAAGCCACCCGCCAAGCGCAACATCGTTTTAATTTAACGAAAAATTACCGCTCCCATCAACACGTGGTGGACTGTGTGAATCGGTTGTTTGATTTTAGCGAACAACCGCCGTTTCTCTATAAAGACATTCAATTTATGCCGGTCGGTGCAAGAACGGATCACCCGCAATTTTGGTTAAGCGGGCAGCCGGAACCTGCGGTGCGTTTTTATGTGGATGAAGCCTCCGTTAAAGAAAACATGGCAAAAGCTTGCGCCGTTTCTATCCAATATTGGCTACAAAGTGCGGTGGAAAACTCTGCCGTTTTTCGCCTTGATGATGGTGACAAAAAAACGCTGAAACCGGAAAGTATCGCCGTGTTGGTGCGTAGCCGTAAAGAAGCCGAGTTGGTGAAAAATGAATTGCGTCACTTGGGCATTGCCTCCGTGTATTTGTCTGAAGACAGCAATGTGTTCGACAGCAGCGCGGCAAAAGATTTGTTAATGATTCTCACGGCGTGCCTCAATCCGTTTTCCGAACGCCATATTTTAAACGCCATTGCCACAGCAATTTTTGCCCAAACCAGCGCCGACATTCAGCGCATTCGTATGGATGAAACCCGCTGGGAGCATTGGGTGGAGAAGTTTATTCATTACCAAAGAACCTGGCAAAAACAAGGCGTGTTGGTGATGTTACATCAGTTGTTCCAGCAGGAAAAAATCACGGAAAAACTTTACCCCACGGTGGACGGCAAACGCTTGGTGACGGACTTGCTGCATTTGGCGGAATTGCTGCAGGAAGCGGCTACCCTGAACGAAAGCGAAGCGGCATTGTTACGTTGGTTTGAGAAACAAATTCAAGGGGAAAATCGCCAAAAAGAGCAACAGGTTAGGTTGGAGAGCGAATTGCAGTTGGTGAAAATCGTCACTATTCATAAATCCAAGGGGTTGGAATACGATCTGGTTTGGTTGCCGTTTATCGGCTATGCTTCCACCTTCCGAGGCGATCGCATCACTACTTATTATGACGAAACACAAGGCGCGGTGCTGTGGGATTACGATAAATCCCATGAAGCGTTGGTGCAACAGGAAGATTTTGCCGAACAGCTACGCCTGCTTTATGTAGCGTTGACCCGCGCCAAATACCAGTTGGTGATCGGCGTGCCGCAAACCTTTGAGACGAAATGGAGCAGTTTGTTATATGTGCTGACCCACGGAGCGATCCAAACGCGCGAAAAACCGAATGCTTACGACAGCCTCTCTTTATTGGAAAAACTTGTGGCGCGTGCGCCGCAGGGCAGTGTACAAATTGCCAACACGGCAGATCTGACACCGCTGGCATTGCAAGCCCACGCCGAAGCACAGATACCGTTACATGCGGCAAAATTCACCGGTAACATCGAACAAAACTGGACGGTCACCAGTTTCAGCGCCATAGAAGCCATTCATCAGAATAAAGCCTATTTCAAAGCGCAACAGATGGCGGAAAGTGCGGTCGATTTTCCAAGTGTTTTTGACTTAGGGAAAGACTATGATTTTAACGAACAAGGGAAATCAACCGAGAGTATTCAGGAAACGGTTGCCGACGAATCCGCCTATCCTTTCGGCTATTCGCCTTTTGATTTCCCGCACGGTATTAACATCGGCACGGCATTACACCGTTTTCTGGAAAAAACGGATTTTGATCGCCCGTTAAACGAAGACAAAATCCAAAAACTCTGCCAATGGTTACAGTTAGAGGAAACCTGGCTACCGTCTTTACAGCAATGGATAAACGCCATTTTGCATACGCCGTTAAGCACGCAGGATTCTACTTTGCAACTGGTGAATTTAACCCGCCAATATTGCGTGAAAGAAATGCAGTTTTATTTGAAGTTAAATCAAACATTTGACGTGGCGGTGTTTAATCAAGCGTTACAACAGCATCACCACTTACCCTCAGAACCCCTGCAATTTGAAGCGATTAAAGGAATGTTACGCGGTTTCATGGATTTGGTGTTTTATCATAACGGAAAATATTATTTGGCGGATTACAAATCCAATTTTCTTGGCGTGGAAGCGCAAAACTACGTCGGCACAAGCCTTCAGCAAGCCATGCTAACTAATCATTACGACTGGCAATATTTATTTTACACGCTGGCATTGCACCGTTATTTACAACAACGTGACGCAAACTATGACTATGACACCCATTTCGGCGGTGTGTTTTATTGTTTCTTACGTGGCATGAACGGCGAAAATCAAAACGGCGTGTTTTTTGATAAACCGGATTACGTGTTAATTCAGGCTTTGGAGAATTTGTTC","","","146553","MQALNPISIPLNAISLIEASAGTGKTYTMGSLYLRLLLQAGENAFPHVLNVEQILVVTFTEMATEELKRKIRERIYDAKQKLTAYQQTQDPTVFEHDDFLRQLADTITDFPLAIQRLTLAEQNMDLAAIYTIHGFCRRMLMQYAFNSGIHFNLELSGEEDELLLHLAQKLWRAHFYSQPYAVAEFIQKHLISPANVIHNIKKFAGTELKLPQNRPYFFDGALPDFLAKLADYSQQLSAQIAEVKENWLKNEEEITQLIETEVNTKYKSAKEQKLNRRSFTSATRPKWLAMMKAWAESDKADFPDCFSRFGQTAINAQKGEEAKDALTHSLFVQINALLALSEQKALLSQALWFHYLQMLNAQLVEYKLNHSEKSFNDLLRLLKEALYHPDNTEFARLIRYQFPFAMIDEFQDTDAVQYQIFSKIYVEQPQTDAQSDSGFIMIGDPKQAIYKFRGADIFTYFQATRQAQHRFNLTKNYRSHQHVVDCVNRLFDFSEQPPFLYKDIQFMPVGARTDHPQFWLSGQPEPAVRFYVDEASVKENMAKACAVSIQYWLQSAVENSAVFRLDDGDKKTLKPESIAVLVRSRKEAELVKNELRHLGIASVYLSEDSNVFDSSAAKDLLMILTACLNPFSERHILNAIATAIFAQTSADIQRIRMDETRWEHWVEKFIHYQRTWQKQGVLVMLHQLFQQEKITEKLYPTVDGKRLVTDLLHLAELLQEAATLNESEAALLRWFEKQIQGENRQKEQQVRLESELQLVKIVTIHKSKGLEYDLVWLPFIGYASTFRGDRITTYYDETQGAVLWDYDKSHEALVQQEDFAEQLRLLYVALTRAKYQLVIGVPQTFETKWSSLLYVLTHGAIQTREKPNAYDSLSLLEKLVARAPQGSVQIANTADLTPLALQAHAEAQIPLHAAKFTGNIEQNWTVTSFSAIEAIHQNKAYFKAQQMAESAVDFPSVFDLGKDYDFNEQGKSTESIQETVADESAYPFGYSPFDFPHGINIGTALHRFLEKTDFDRPLNEDKIQKLCQWLQLEETWLPSLQQWINAILHTPLSTQDSTLQLVNLTRQYCVKEMQFYLKLNQTFDVAVFNQALQQHHHLPSEPLQFEAIKGMLRGFMDLVFYHNGKYYLADYKSNFLGVEAQNYVGTSLQQAMLTNHYDWQYLFYTLALHRYLQQRDANYDYDTHFGGVFYCFLRGMNGENQNGVFFDKPDYVLIQALENLF","1541820","[FUNCTION] Required for efficient DNA repair; it catalyzes the unwinding of double-stranded DNA and the cleavage of single-stranded DNA and it stimulates local genetic recombination. All of these activities require concomitant hydrolysis of ATP. ","exodeoxyribonuclease V beta chain","Cytoplasm","","
InterPro
IPR000212
Family
UvrD/REP helicase
PTHR11070\"[11-76]T\"[122-183]T\"[327-517]T\"[559-793]T\"[816-854]TUVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER
PF00580\"[2-732]TUvrD-helicase
InterPro
IPR004586
Family
Exodeoxyribonuclease V, beta subunit
TIGR00609\"[4-1221]TrecB: exodeoxyribonuclease V, beta subunit
InterPro
IPR014016
Domain
Helicase superfamily 1, UvrD-related
PS51198\"[1-480]TUVRD_HELICASE_ATP_BIND
InterPro
IPR014017
Domain
UvrD-like DNA helicase, C terminal
PS51217\"[497-769]TUVRD_HELICASE_CTER
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[2-473]T\"[474-865]Tno description
G3DSA:3.90.320.10\"[912-1221]Tno description


","No hits to the COGs database.","Significant hit ( 8.4e-51) to 7/7 blocks of the IPB000212 family, which is described as \"UvrD/REP helicase\". Interpro entry for IP:IPR000212. IPB000212A 19-29 0.00086 IPB000212B 54-71 1.7e-05 IPB000212C 407-418 3.2e-05 IPB000212D 442-455 9.2e-07 IPB000212E 473-491 8.9e-06 IPB000212F 759-777 4.3e-09 IPB000212G 821-833 0.0001","Residues 402 to 492 match (8e-07) PD:PD434517 which is described as HELICASE DNA PROTEOME COMPLETE DNA-BINDING 3.6.1.- II CDNA HYDROLASE FIS ","","","","","","","","","","","Thu Jan 16 14:55:08 2003","Thu Jan 16 14:55:08 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02266 is paralogously related to AA00527 (5e-10), AA02666 (6e-06) and AA00021 (3e-04).","","","","","","Residues 4 to 732 (E-value = 1.9e-71) place AA02266 in the UvrD-helicase family which is described as UvrD/REP helicase (PF00580)","","","","","Arnold,D.A. and Kowalczykowski,S.C. Facilitated loading of RecA protein is essential to recombination by RecBCD enzyme J. Biol. Chem. 275 (16), 12261-12265 (2000) PubMed: 10766864 Finch,P.W., Storey,A., Chapman,K.E., Brown,K., Hickson,I.D. and Emmerson,P.T. Complete nucleotide sequence of the Escherichia coli recB gene Nucleic Acids Res. 14 (21), 8573-8582 (1986) PubMed: 3537960 Finch,P.W., Storey,A., Brown,K., Hickson,I.D. and Emmerson,P.T. Complete nucleotide sequence of recD, the structural gene for the alpha subunit of Exonuclease V of Escherichia coli. Nucleic Acids Res. 14 (21): 8583-8594 (1986) [PubMed: 3537961].","","Thu Jan 16 14:55:08 2003","1","","","" "AA02267","1545936","1545556","381","TTGATTAAATTAAATAGGTTAATCATTATGCAAAAAATTCTTTTTATCTTAAATGACTCGCCATACGGCGGTGAAAAAACTTTTAATGGATTACGTTTTGCCATTAACTTGCAGGAAGATCACGGCAAAGAAGTGGACATTAAAGTGTTCTGTTTCTCCGATTCGATTTTAAGCGGTCTTGCCGGTCAAAATCCGAACGAGGGATCCAATGTGCAACAATTAATGGATATTTTGATTGCACAGGGCGCAGAAGTGAAACTTTGCACCAGTTGCGTAAAAGCACGCGGGTTATTGGATGCCAAATTAATTGACGGCGTCACCCTCGGCACCTTGGCTGATGTATCAGACTGGACCTTATGGGCTGATAAAGTCATCAGTCTC","","","13862","LIKLNRLIIMQKILFILNDSPYGGEKTFNGLRFAINLQEDHGKEVDIKVFCFSDSILSGLAGQNPNEGSNVQQLMDILIAQGAEVKLCTSCVKARGLLDAKLIDGVTLGTLADVSDWTLWADKVISL","1545556","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003787
Family
DsrE-like protein
PF02635\"[11-127]TDrsE
noIPR
unintegrated
unintegrated
G3DSA:3.40.1260.10\"[10-127]Tno description
signalp\"[1-24]?signal-peptide


","No hits to the COGs database.","Significant hit ( 6e-21) to 4/5 blocks of the IPB003787 family, which is described as \"DsrE-like protein\". Interpro entry for IP:IPR003787. IPB003787A 11-32 0.0041 IPB003787C 50-72 0.0055 IPB003787D 82-95 0.0055 IPB003787E 96-127 1.7e-06","Residues 46 to 126 match (2e-18) PD:PD586458 which is described as PROTEOME COMPLETE YPO3130 YCHN ACR STY1283 INVOLVED REDUCTION SULFUR INTRACELLULAR ","","","","","","","","","","","","Thu Jan 16 14:55:59 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02267 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 11 to 127 (E-value = 3.5e-25) place AA02267 in the DrsE family which is described as DsrE/DsrF-like family (PF02635)","","","","","","","","1","","","" "AA02268","1546033","1545932","102","TTGCTAAAATCAGCCGAAAATGCCTTTCTTAACTTTTTATCGTCTTTATTTTTTCAGGTTGGAAATCACAATGGAAAATTAATATTTTCTACTGTTTTTGAT","","","3801","LLKSAENAFLNFLSSLFFQVGNHNGKLIFSTVFD","1545932","","hypothetical protein","Cytoplasm, Extracellular","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:04:15 2004","Wed Feb 25 15:04:15 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02268 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:04:15 2004","","","","","","","","","","","","","1","","","" "AA02269","1546864","1546337","528","ATGAACACTTGTACTCCAAATATCAAAGACAGTTACACTTACGAAGATTTATTGGCTTCAGGACGTGGTGAATTGTTTGGCAAAGAAGGCCCGCAATTGCCGGCACCGACCATGCTTATGATGGATCGTATCGTAAAAATGACTGAAGACGGCGGTACATTTGGCAAAGGCTACATTGAAGCCGAGTTGGATATTCATCCTGATCTACCGTTCTTTGCCTGCCACTTTATCGGCGACCCTGTCATGCCGGGGTGTTTGGGTTTAGATGCCATGTGGCAATTAGTCGGCTTCTTCTTAGGCTGGGTCGGCGGCAAGGGCAAAGGCAGAGCCTTAGGTGTTGGCGAAGTGAAATTTACCGGACAAATTCTCCCGACGGCAAAAAAAGTCGTTTATCGCATTAACATGAAACGCATGATTAACCGCAAATTAGTCATGGGCATGGCAGACGGCGAAGTGGAAGTGGACGGTCGTGTTATTTACACCGCAACGGACTTGAAAGTCGGCTTGTTTCAAGATACCTCAAGTTTC","","","19295","MNTCTPNIKDSYTYEDLLASGRGELFGKEGPQLPAPTMLMMDRIVKMTEDGGTFGKGYIEAELDIHPDLPFFACHFIGDPVMPGCLGLDAMWQLVGFFLGWVGGKGKGRALGVGEVKFTGQILPTAKKVVYRINMKRMINRKLVMGMADGEVEVDGRVIYTATDLKVGLFQDTSSF","1546337","[FUNCTION] Necessary for the introduction of cis unsaturation into fatty acids. Catalyzed the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP.[PATHWAY] Key step in the anaerobic pathway of unsaturated fatty acid synthesis in bacteria. ","3-hydroxydecanoyl-(acyl-carrier protein) dehydratase","Cytoplasm","","
InterPro
IPR000794
Domain
Beta-ketoacyl synthase
PTHR11712\"[51-91]TPOLYKETIDE SYNTHASE-RELATED
InterPro
IPR010083
Family
Beta-hydroxyacyl-(acyl-carrier-protein) dehydratase FabA
TIGR01749\"[9-176]TfabA: beta-hydroxyacyl-(acyl-carrier-protei
InterPro
IPR013114
Domain
Beta-hydroxyacyl-(acyl-carrier-protein) dehydratase, FabA/FabZ
PF07977\"[33-163]TFabA
noIPR
unintegrated
unintegrated
PD838104\"[15-176]TFABA_HAEDU_Q7U343;
G3DSA:3.10.129.10\"[6-176]Tno description
PTHR11712:SF23\"[51-91]T3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE


","BeTs to 11 clades of COG0764COG name: 3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratasesFunctional Class: IThe phylogenetic pattern of COG0764 is -------qvd-lbcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 3.1e-05) to 2/3 blocks of the IPB001143 family, which is described as \"Bacterial thioester dehydrase\". Interpro entry for IP:IPR001143. IPB001143B 49-102 8.1e-05 IPB001143C 108-150 1.5e+02","Residues 7 to 176 match (3e-71) PD:PD013327 which is described as COMPLETE PROTEOME DEHYDRATASE LIPID LYASE DEHYDRASE BIOSYNTHESIS CARRIER 4.2.1.- 3R-HYDROXYMYRISTOYL-ACYL ","","","","","","","","","","","Thu Jan 16 15:08:52 2003","Thu Jan 16 15:08:52 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02269 is paralogously related to AA00611 (8e-06).","","","","","","","","","","","Marrakchi H, Choi KH, Rock CO. A new mechanism for anaerobic unsaturated fatty acid formation in streptococcus pneumoniae. J Biol Chem. 2002 Sep 16 [epub ahead of print] PMID: 12237320 Zhang YM, Marrakchi H, Rock CO. The FabR (YijC) transcription factor regulates unsaturated fatty acid biosynthesis in Escherichia coli. J Biol Chem. 2002 May 3;277(18):15558-65. PMID: 11859088Cronan,J.E. Jr., Li,W.B., Coleman,R., Narasimhan,M., de Mendoza,D. and Schwab,J.M. Derived amino acid sequence and identification of active site residues of Escherichia coli beta-hydroxydecanoyl thioesterdehydrase. J. Biol. Chem. 263 (10): 4641-4646 (1988) [PubMed: 2832401]. Henry,M.F. and Cronan,J.E. Jr. A new mechanism of transcriptional regulation: release of an activator triggered by small molecule binding. Cell 70 (4): 671-679 (1992) [PubMed: 1505031].","","Thu Jan 16 15:08:52 2003","1","","","" "AA02270","1548728","1547010","1719","GTGACTGAAATTCCCTCACAACCTCAGGACTTTTTCTCTCTACAACCCCGTGCGGGCAAAGCCATCCGCAATTTCATCCGAAATTCCCACCGCACTTTATTGGTGCTGAAAGCCGATGACCAAGCGGAGTACGCCACTTTATTAGAAAGTTTTATTGCAAAACAACAACCGGAGCTTGCGGTGAACGGCGTGCAATACATTGTGGAACAGGGCGACTCTTTTTCTTTCCCGCGTGTTTATACGGAACCGGCGCAATCGGTAGAGGACAATTTTGCCGCACAGAAAACCGTCGCAACGGCATTGTATTTCGATCAATTTCAGTTATTCGGTTCCGTTAAAATTCATGCGTCTTCAAATGATATTCAGCTTCATACCGGCTTGGTTCATCAGCTGAATCACGGCGTGTTGATTATCAGCGCCGGCGCGTTATTGGCGCAATTTAATTTATGGCAACGCCTGAAACAGATTTTAACGACAGGGATGTTTGATTGGTATTCCGCCCATCCGTTTAAGCCCCTGCCTTGTGAAGTTCCAAGCTATCCGTTGCAATTGAAAGTCATCGTGCTGGGCAATCGCACGGAATTAGGCATGTTGGAAGAATTGGAAGAAGGGCTTTATCATCTGGCGGATTACGCGGAAATTGAAAGTTATTGCAGTGTGGAAACGGCGGAACAGCAGCAACAATGGATGAATTATGTGCAAACCGTTGCACAGCAAAATCACTTACCGCCGTTAGATTTAAGCGGTTTTAATAAACTGTATCAATTGTTGGTGCGTGACAGTGAAAATCATCATTTGATTAATGTGTCGCCGTTGAAATTAAAAACGTTGCTCACAGAGACCGCACTTTTAAGCGAATCCGATTCACTAAGTGCGGTGGATTTTGAACGGTATTTTTTACATAAAACGGCACAATATGGCTTTTTGCGTGAACAAACCTATGACGCTATTTTGCAGGAACAAATTTATGTAGCGACCGAAGGTGAAATGGTTGGGCAAATTAACGGCTTATCGGTGATTGAATATCCGGGCACGCCTTTATCTTTCGGAGAACCCTCTCGAATCAGTTGTATTGTGCAATTCGGCGACGGCGAAATCGTCGATGTGGAACGCAAAAATGAACTGGCGGGCAACATTCACAGCAAAGGCATTATGATTGCCGAAGCCTGTTTGGCGAATATTCTCGAATTTCCGTCACAACTGCCGTTTTCCGCTTCTTTGGTGTTTGAGCAATCTTACGGTGAAATTGACGGTGACAGTGCCTCACTCGCCGGTTTTTGTGTATTATTGAGCGCATTGTCCGCTTTGCCTCTGCCGCAATCTATCGCCATTACGGGCGCTATTGACCAATTCGGCTTGGTGCATTCCGTGGGGGGCGTGAATGACAAAATCGAAGGGTTTTTCACCCTTTGCCAACGTCGTGGCTTAACGGGCAAACAAGGCGTGATGATTCCGAGTGCGGTGCTTAATCAGCTAAGCTTGTCCGAAGCGGTGGTAAGTGCGGTTAAAAATCAGGAATTTTTTATTTATCCGGTGGAAACCGTGGATCAAGCTTGTGAGATTTTATTACAACGGGATTTGGTGGAGCAGGAGAATAAAAAGTACGATTTCAGCACACTGCCATTGTCCCGTTTGATCAATCAGCGTATTGAGCAATATTCCGAGCAACAATCTCACAAGCACGGTCTTTGGGATTTATTCTTCGGCAGAAAAAATCGT","","","66405","VTEIPSQPQDFFSLQPRAGKAIRNFIRNSHRTLLVLKADDQAEYATLLESFIAKQQPELAVNGVQYIVEQGDSFSFPRVYTEPAQSVEDNFAAQKTVATALYFDQFQLFGSVKIHASSNDIQLHTGLVHQLNHGVLIISAGALLAQFNLWQRLKQILTTGMFDWYSAHPFKPLPCEVPSYPLQLKVIVLGNRTELGMLEELEEGLYHLADYAEIESYCSVETAEQQQQWMNYVQTVAQQNHLPPLDLSGFNKLYQLLVRDSENHHLINVSPLKLKTLLTETALLSESDSLSAVDFERYFLHKTAQYGFLREQTYDAILQEQIYVATEGEMVGQINGLSVIEYPGTPLSFGEPSRISCIVQFGDGEIVDVERKNELAGNIHSKGIMIAEACLANILEFPSQLPFSASLVFEQSYGEIDGDSASLAGFCVLLSALSALPLPQSIAITGAIDQFGLVHSVGGVNDKIEGFFTLCQRRGLTGKQGVMIPSAVLNQLSLSEAVVSAVKNQEFFIYPVETVDQACEILLQRDLVEQENKKYDFSTLPLSRLINQRIEQYSEQQSHKHGLWDLFFGRKNR","1547010","","endopeptidase La; lon protease; protease La homolog; ATP-dependent protease LA (lon-1)","Cytoplasm","","
InterPro
IPR001984
Family
Peptidase S16, Lon protease
PR00830\"[331-347]T\"[414-433]T\"[444-463]TENDOLAPTASE
noIPR
unintegrated
unintegrated
PTHR10046\"[311-562]TATP DEPENDENT LON PROTEASE FAMILY MEMBER


","No hits to the COGs database.","","Residues 416 to 465 match (3e-12) PD:PD001169 which is described as PROTEASE COMPLETE PROTEOME ATP-BINDING DNA REPAIR ATP-DEPENDENT HYDROLASE SERINE HOMOLOG ","","","","","","","","","","","","Thu Jan 16 15:13:04 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02270 is paralogously related to AA02395 (7e-06).","","","","","","","","","","","","","","1","","","" "AA02271","1548763","1548861","99","GTGTTATTAGATAAAGAAGATAAAATCACGTTAATCTCTGGGTTATATTTAATTTGCGCGCATTATCGCATATTTCTTCGCGTCTTTATTAATCTCGCG","","","3847","VLLDKEDKITLISGLYLICAHYRIFLRVFINLA","1548861","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
tmhmm\"[10-30]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:02:46 2004","Wed Feb 25 15:02:46 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02271 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:02:46 2004","","","","","","","","","","","","","1","","","" "AA02272","1548938","1549381","444","ATGAAATATCAAAAGTTAGAAAATCAAGAAGCCCATTGGAAATGGGCTTATTTAACGAAAAAAGCCCGTGAAGGCGAAAACGTTACCCGTTATGAAGAAAAAAGTTTGCAGGAAGACATCGTTAAGCAACTCATCGGCTGTCAAAATTACCCGCAAAAAATTGAAGAATGGATAAAAACCCATTTGGCGCCGAAATTGGTGATCAAGCTAGACCAAGCCATTCGTGCCAGAAGAAAACGTTTTTTCAACGGTGAAAAACAATATACCAAGAAAAAATCCATTGATTTGGAATATGCCGTTTGGCTGCGTTTGTCCAAATATTCCCGCAAAATGAAAATGACGCTGTCGGAAACCATTTCCTACATGATTGACGAGCGCGAGAAAAAAGCCTTGTACGAAAATCAAATGTCCGCCATGAAAGCGGGCTTGAAAGATCTACTGAAA","","","17854","MKYQKLENQEAHWKWAYLTKKAREGENVTRYEEKSLQEDIVKQLIGCQNYPQKIEEWIKTHLAPKLVIKLDQAIRARRKRFFNGEKQYTKKKSIDLEYAVWLRLSKYSRKMKMTLSETISYMIDEREKKALYENQMSAMKAGLKDLLK","1549381","","conserved hypothetical protein","Cytoplasm, Extracellular","","
InterPro
IPR009390
Family
Protein of unknown function DUF1047
PF06303\"[1-148]TDUF1047
noIPR
unintegrated
unintegrated
PD033720\"[1-148]TY482_PASMU_Q9CNF0;


","BeTs to 3 clades of COG3120COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3120 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 1 to 148 match (2e-49) PD:PD033720 which is described as PROTEOME COMPLETE CYTOPLASMIC YCBG STY1090 HI1323 YPO1433 VC1481 PM0482 ","","","","","","","","","","","","Thu Jan 16 15:14:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02272 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 148 (E-value = 9e-97) place AA02272 in the DUF1047 family which is described as Protein of unknown function (DUF1047) (PF06303)","","","","","","","","1","","","" "AA02273","1549659","1549453","207","ATGGAAGTTGGTGTTGTTAAATGGTTTAATAATGCAAAAGGATTTGGCTTTATTTCCGTTGAAGGCAGTGATACCGATATCTTTGCACATTATTCAGTGATTGAAATGGAAGGGTATCGTTCATTAAAAGCAGGTCAAAAAGTCCGGTTTGAAGTGATTCACGGCGACAAAGGTTCTCACGCGACAAAAATCATTCCCGTTGTAGAA","","","7641","MEVGVVKWFNNAKGFGFISVEGSDTDIFAHYSVIEMEGYRSLKAGQKVRFEVIHGDKGSHATKIIPVVE","1549453","[FUNCTION] Inhibits DNA replication at both initiation and elongation steps, most probably by binding to the opened, single-stranded regions at replication forks. Plays a regulatory role in chromosomal replication in nutrient-depleted cells. ","cold shock-like protein","Cytoplasm","","
InterPro
IPR002059
Domain
Cold-shock protein, DNA-binding
PD000621\"[26-67]TQ9CNF1_PASMU_Q9CNF1;
PR00050\"[4-19]T\"[25-34]T\"[40-58]TCOLDSHOCK
PF00313\"[1-67]TCSD
PS00352\"[15-34]TCOLD_SHOCK
InterPro
IPR011129
Domain
Cold shock protein
SM00357\"[3-67]TCSP
InterPro
IPR012156
Family
Cold shock, CspA
PIRSF002599\"[2-67]TCold shock protein, CspA type
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[1-67]Tno description
InterPro
IPR012751
Family
CspD, cold shock
TIGR02381\"[1-68]TcspD: cold shock domain protein CspD
noIPR
unintegrated
unintegrated
PTHR11544\"[1-66]TCOLD SHOCK DOMAIN CONTAINING PROTEINS


","No hits to the COGs database.","Significant hit ( 1.1e-28) to 2/2 blocks of the IPB002059 family, which is described as \"Cold-shock DNA-binding domain\". Interpro entry for IP:IPR002059. IPB002059A 4-18 2e-09 IPB002059B 26-64 7.9e-18","Residues 21 to 66 match (8e-07) PD:PD580670 which is described as TRANSCRIPTION COLD DNA-BINDING REGULATION ACTIVATOR PROTEOME COMPLETE SHOCK SHOCK-LIKE FAMILY ","","","","","","","","","","","Thu Jan 16 15:27:14 2003","Thu Jan 16 15:27:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02273 is paralogously related to AA00213 (4e-10).","","","","","","Residues 1 to 67 (E-value = 1.2e-34) place AA02273 in the CSD family which is described as 'Cold-shock' DNA-binding domain (PF00313)","","","","","Doniger,J., Landsman,D., Gonda,M.A. and Wistow,G. The product of unr, the highly conserved gene upstream of N-ras, contains multiple repeats similar to the cold-shock domain (CSD), a putative DNA-binding motif. New Biol. 4 (4): 389-395 (1992) PubMed: 1622933.Yamanaka,K., Zheng,W., Crooke,E., Wang,Y.H. and Inouye,M. CspD, a novel DNA replication inhibitor induced during the stationary phase in Escherichia coli. Mol. Microbiol. 39 (6): 1572-1584 (2001) PubMed: 11260474.Weber MH, Volkov AV, Fricke I, Marahiel MA, Graumann PL.Localization of cold shock proteins to cytosolic spaces surrounding nucleoids in Bacillus subtilis depends on active transcription.J Bacteriol. 2001 Nov;183(21):6435-43.PMID: 11591689","","Tue Feb 4 16:15:20 2003","1","","","" "AA02274","1549841","1549752","90","GTGTTTTTGCAGCAAAATTTTAATAATTTTTGTGATCTCTGTTTGATTTTGAGACTTTTTTTATTGCGCAACCAACAAATTTACTTAATA","","","3698","VFLQQNFNNFCDLCLILRLFLLRNQQIYLI","1549752","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-25]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 15:01:31 2004","Wed Feb 25 15:01:31 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02274 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 15:01:31 2004","","","","","","","","","","","","","1","","","" "AA02275","1550015","1549869","147","ATGTTAGATAACGATTTATTACATTTAACCCATGAACAGCAGCAACTTGCCGTGGAAAAAATTCAGGAATTAATGGCGCAAGGCGTGGGCAGCGGCGAGGCTATCGCTTTAGTGGCCAAAAAAGTTAGGGGAACAAAATCGGGCAGA","","","5296","MLDNDLLHLTHEQQQLAVEKIQELMAQGVGSGEAIALVAKKVRGTKSGR","1549869","","conserved hypothetical protein","Cytoplasm","This sequence is similar to gi|15831774, a predicted hypothetical protein from Escherichia coli O157:H7.","
InterPro
IPR005371
Family
Protein of unknown function UPF0181
PF03701\"[1-49]TUPF0181
noIPR
unintegrated
unintegrated
PD026807\"[1-43]TY480_PASMU_Q9CNF2;


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 14:59:50 2004","Wed Feb 25 14:59:50 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02275 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 14:59:50 2004","","","","","Residues 1 to 49 (E-value = 1.9e-23) place AA02275 in the UPF0181 family which is described as Uncharacterised protein family (UPF0181) (PF03701)","","","","","","","","1","","","" "AA02276","1550782","1550072","711","ATGAATTTAGCGGTTTTGTATCAGGATGATGTACTGGTTGCGGTGAATAAGCCGGCGGGGATGTTGGTGCATCGCAGTTGGCTTGATCGCCATGAAACACAATTTGTGATGCAAATCTTGCGCGATCAAATCGGGCAGTTGGTGTATCCCATTCATCGTTTGGATCGCCCTACATCAGGCGTATTGTTGTTTGCGTTGAACAGCGAAACGGCAAATTTGGTATGTCACCAATTTGAGCAAAAACAAACGGAAAAACAGTATCTAGCAGTGGTTCGTGGCTATGTGACAGGGCAGGGTGAAATTGATTATCCGTTGAAAGTGCAGTTGGATAAAATCGCCGATAAGTTCGCACAGCAGGATAAAGCACCGCAAAGTGCGGTTACTTTTTACGACGGATTGAAAACCGTTGAAATGCCTTATGGCGTGGGGCGTTATGCCGCTTCTCGCTATTCGTTGGTTCGCTTAACGCCGAAAACTGGGCGCAAGCACCAGCTTCGTCGTCACATGAAACATATTTTTCATCCGATTTTAGGTGATACGCAATACGGCGATTTGCATCAAAATCGCGCTTTAACGGAACACATCGGTTGTTCCCGTTTAATGTTACACGCCGAAAAATTAACCTTTGTTCACCCGCTGACAGGACAACCGATAACCATTGAAGCGGGATTGGATGAACAATGGAAACATTTAATGCGGACATTTCAGTGG","","","27312","MNLAVLYQDDVLVAVNKPAGMLVHRSWLDRHETQFVMQILRDQIGQLVYPIHRLDRPTSGVLLFALNSETANLVCHQFEQKQTEKQYLAVVRGYVTGQGEIDYPLKVQLDKIADKFAQQDKAPQSAVTFYDGLKTVEMPYGVGRYAASRYSLVRLTPKTGRKHQLRRHMKHIFHPILGDTQYGDLHQNRALTEHIGCSRLMLHAEKLTFVHPLTGQPITIEAGLDEQWKHLMRTFQW","1550072","[FUNCTION] Responsible for synthesis of pseudouridine from uracil-746 in 23S ribosomal RNA and position 32 in the anticodonstem and loop of transfer rnas. ","pseudouridine synthase Rlu family","Cytoplasm","","
InterPro
IPR006145
Domain
Pseudouridine synthase
PD001819\"[51-93]TTRUC_HAEIN_P44197;
PF00849\"[11-171]TPseudoU_synth_2
InterPro
IPR006224
Family
Pseudouridine synthase, Rlu
PS01129\"[51-65]TPSI_RLU
noIPR
unintegrated
unintegrated
PTHR10436\"[1-232]TRIBOSOMAL PSEUDOURIDINE SYNTHASE


","BeTs to 19 clades of COG0564COG name: Pseudouridylate synthases, 23S RNA-specificFunctional Class: JThe phylogenetic pattern of COG0564 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.7e-53) to 4/4 blocks of the IPB000613 family, which is described as \"Pseudouridine synthase\". Interpro entry for IP:IPR000613. IPB000613A 5-25 1.8e-09 IPB000613B 51-90 9e-18 IPB000613C 159-183 5.7e-16 IPB000613D 199-212 1e-05Significant hit ( 2.1e-46) to 3/3 blocks of the IPB002990 family, which is described as \"Pseudouridine synthase, Rlu family\". Interpro entry for IP:IPR002990. IPB002990A 5-25 1.9e-09 IPB002990B 51-89 4.7e-18 IPB002990C 159-183 4.2e-16Significant hit ( 2.3e-05) to 3/4 blocks of the IPB000748 family, which is described as \"Pseudouridine synthase, Rsu family\". Interpro entry for IP:IPR000748. IPB000748B 16-31 69 IPB000748C 51-83 0.0072 IPB000748D 155-189 17","Residues 5 to 90 match (4e-07) PD:PD580558 which is described as COMPLETE PROTEOME RLU FAMILY PSEUDOURIDINE SYNTHASE TP0231 TP0339 LARGE SUBUNIT ","","","","","","","","","","","Thu Jan 16 15:32:22 2003","Thu Jan 16 15:32:22 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02276 is paralogously related to AA00513 (6e-26), AA02913 (9e-25), AA01355 (2e-17) and AA02063 (4e-17).","","","","","","Residues 11 to 171 (E-value = 7.6e-51) place AA02276 in the PseudoU_synth_2 family which is described as RNA pseudouridylate synthase (PF00849)","","","","","Corollo D, Blair-Johnson M, Conrad J, Fiedler T, Sun D, Wang L, Ofengand J, Fenna R. Crystallization and characterization of a fragment of pseudouridine synthase RluC from Escherichia coli. Acta Crystallogr D Biol Crystallogr. 1999 Jan;55 ( Pt 1):302-4. PMID: 10089432Wrzesinski,J., Nurse,K., Bakin,A., Lane,B.G. and Ofengand,J. A dual-specificity pseudouridine synthase: an Escherichia coli synthase purified and cloned on the basis of its specificity forpsi 746 in 23S RNA is also specific for psi 32 in tRNA(phe). RNA 1 (4): 437-448 (1995) [PubMed: 7493321]. ","","Thu Jan 16 15:32:22 2003","1","","","" "AA02278","1551093","1550782","312","ATGTATCAACAAACCCGGTTACATTTACAAAATTTGCAGAAAACCATGGAGCGTTTGGCACTGTGGCAAACCATGCCGCCGCAGGAAGACGCTTTTTTGAGTGAACAACCTTTTGCGTTGGATACCATGAGTCCGACGGAATGGCTGCAATGGATTTTTATTCCGCGTATGTACGCATTGTTGGAAAGCCAAGCGCCGTTGCCGAGCCAAATTGCCATCAGTCCGTATTTAGAGGAAGTGTTAAAGGAAGATGGTTATTTGGCGGAGTTATTGCTCCCGATCATTGAAATCGAAAAGTTGCTGCAACAACAA","","","13365","MYQQTRLHLQNLQKTMERLALWQTMPPQEDAFLSEQPFALDTMSPTEWLQWIFIPRMYALLESQAPLPSQIAISPYLEEVLKEDGYLAELLLPIIEIEKLLQQQ","1550782","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR007384
Family
Protein of unknown function DUF446
PD020262\"[9-83]TQ9CNF4_PASMU_Q9CNF4;
PIRSF006257\"[2-104]TUncharacterised conserved protein
PF04287\"[1-102]TDUF446


","No hits to the COGs database.","","Residues 9 to 83 match (2e-20) PD:PD020262 which is described as COMPLETE PROTEOME YQCC EXOENZYME CYTOPLASMIC REGULATION HI1436 PA4698 PM0478 VC0887 ","","","","","","","","","","","","Thu Jan 16 15:33:41 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02278 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 102 (E-value = 6.3e-52) place AA02278 in the DUF446 family which is described as Domain of unknown function, DUF446 (PF04287)","","","","","","","","1","","","" "AA02279","1551188","1551979","792","ATGTTATCCGCTATGTATTTAATCGACGCTTTTTTCTCTCGCCAAAACAATCAATTTCACTTGGAACAACAAAGCCATTGCGTTAACCAAATTATCGAGCAATGGCGTTATAACGGGCAAATTATCGGGCGTGAAATTCCGCAATTTGTCGCCGAACAGAAAAACCAACAAGGCTTGGCAGTGCGTGTCACCTGCCCCGAGCAAACCTCTCTTTTAGCGGAATTTAACAATCAACCGGTGAACGATGCCCTTCAAACGGCAGAAAAGTGCGGTGTATCTTTTGAGAGTTTTCATATTGTGGCGGAAGATCTCAATTCTGAAATCACCGCCACGGAAACACCCGCTTGGCAACTGCTCTACACCACCTATTTGCAGTCTTGTTCTCCCCTGCAAAGCGGTGAATCCCTGCAACCGATTCCGCTGTATAAACAACTGAAAAACATACCGCACTTAGCAATGGATTTGGTTAAATGGCAGGAAAATTGGCAGGCGTGCGATCAATTGCAAATGAACGGTTCCGTGTTGGAACAACAGGCTTTGGTGCAAATTTCAGACACCCAAAGCACGCTGTTTAAGCATGGTTACCATCTAACGCAGGAAATTGAGCGACACAGCGGCATTCCTACTTACTATTATTTATACCGCATCGGTGGAAAAAGCTGTGAAGCGGAGCTGCAATCACGCTGTCCGTTATGTAAAAGAAAATGGACGTTAAGCCACCCGCTTTTTGACTTCTTATATTTTAAATGTGATCATTGTCGCCTCGTTTCAAACCTCTCATGGCATTGGCAA","","","30667","MLSAMYLIDAFFSRQNNQFHLEQQSHCVNQIIEQWRYNGQIIGREIPQFVAEQKNQQGLAVRVTCPEQTSLLAEFNNQPVNDALQTAEKCGVSFESFHIVAEDLNSEITATETPAWQLLYTTYLQSCSPLQSGESLQPIPLYKQLKNIPHLAMDLVKWQENWQACDQLQMNGSVLEQQALVQISDTQSTLFKHGYHLTQEIERHSGIPTYYYLYRIGGKSCEAELQSRCPLCKRKWTLSHPLFDFLYFKCDHCRLVSNLSWHWQ","1551979","","conserved hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","Residues 5 to 67 match (5e-14) PD:PD412676 which is described as PROTEOME COMPLETE HI1292 PM0477 ","","","","","","","","","","","","Thu Jan 16 15:35:47 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02279 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02280","1551991","1552827","837","ATGCACTACCAAGACCCCAGCCTGAACGCCTTAAAACTCGGTCAGCAAACAAAATATGCGGAAAAATATGACCGCACTTTATTACAACCCGTGCCACGCCACCTCAATCGTGACTCGTTGGGCATTACGCAAATCCAGCCGTTTTCCACCGGCGCCGACATTTGGACCGCGTATGAAATTTCATGGCTGAACCCGAAAGGCGTGCCGCAGGTGGCGATCGCCGATGTGCAAATTGATTTTCGCAGTGAAAATTTGATCGAATCGAAAAGTTTTAAACTGTATTTAAACAGCTTCAACCAAACAAAATTTGCCGATTTAGTTGATGTTCAGCACATTTTGCAACAGGATTTACAAGATTGCGCCAAGGGTGAAGTCAAAGTGCGGTTAAATTCACTGGCGAATTATACGGATCAACCCATTGCGATGTTACATGGCGACTGTATTGACGGGCTGGATATTGATATTGAGGATTATGCGTTTAATGCGGAATGGCTGAAAGATTGCACGAGCAGCGATGTTGTGGAAGAAACGCTGGTCAGCCATTTGCTCAAATCCAACTGCCTTATTACCCAACAACCGGACTGGGGCAGCCTGCAAATTCATTATGTGGGCAAGCAAATCAATCGCGAACAACTGCTACGCTACATCATCTCATTTCGTCAACACAACGAATTCCACGAACAATGCGTCGAACGCATTTTCTGCGATCTCATGCACTACGCCAAACCGGAAAAACTCACCGTTTACGCGCGCTACACCCGCCGCGGCGGGTTGGACATCAACCCATACCGCTCCAACTTTGAACCTTTACCACCGAATTTACGACTGGCACGGCAG","","","34168","MHYQDPSLNALKLGQQTKYAEKYDRTLLQPVPRHLNRDSLGITQIQPFSTGADIWTAYEISWLNPKGVPQVAIADVQIDFRSENLIESKSFKLYLNSFNQTKFADLVDVQHILQQDLQDCAKGEVKVRLNSLANYTDQPIAMLHGDCIDGLDIDIEDYAFNAEWLKDCTSSDVVEETLVSHLLKSNCLITQQPDWGSLQIHYVGKQINREQLLRYIISFRQHNEFHEQCVERIFCDLMHYAKPEKLTVYARYTRRGGLDINPYRSNFEPLPPNLRLARQ","1552827","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR001474
Family
GTP cyclohydrolase I
PF01227\"[214-271]TGTP_cyclohydroI
InterPro
IPR001579
Active_site
Glycoside hydrolase, chitinase active site
PS01095\"[148-156]TCHITINASE_18


","BeTs to 13 clades of COG0780COG name: Enzyme related to GTP cyclohydrolase IFunctional Class: RThe phylogenetic pattern of COG0780 is -----z-qv---bcefghsnujx---Number of proteins in this genome belonging to this COG is","","Residues 187 to 249 match (6e-29) PD:PD010789 which is described as PROTEOME COMPLETE I YQCD BH2241 SP1777 GTP CJ1724C SLR0711 SAV0728 ","","","","","","","","","","","","Thu Jan 16 15:36:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02280 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 176 to 271 (E-value = 3.5e-07) place AA02280 in the GTP_cyclohydroI family which is described as GTP cyclohydrolase I (PF01227)","","","","","","","","1","","","" "AA02281","1553534","1552983","552","ATGAATGTACACAAAATGATAATATTAATAGAGCTAATTAAAGAAACAAAATCAGGGACTTTAATTATTAAGAATGTGCATTATCTTCCTGTTGAAGAACAACAATATTTAATTCAGATTTTACATCATGACGAGAGTCAATTCCGTTTAATTTTGCTTAGTGATATAGAACTTAACGAATTAATTCGCTGTCGGCAGATAAGTGCCGAGTTTTATTATTTTTTTATTTATACTCAAATTGAAATGCTGCCGTTACGTAAACATATCACTGATGTGGCAGATATTTTTACTCATTATGTGAAAAATATTTGTGTCAGATTAAATAAACCCATCGTAATCCCGGATAAAAAAATGTTGCAAAATTTACGCAATAAAGAATGGCATGGAAATGTGAAAGAATTGATTAACGTCGCGGAACTTTATGCAATCGGCTTACTTTCTCATATTACTTTGGTGGTTCCTCCTGTATTTAATGATTCGCAGATGAGTTCTTTAGATGAACAATTGAATCAATATGAAAAACAACTTATTGAAGATGCTCTGGTTTTTTAT","","","21777","MNVHKMIILIELIKETKSGTLIIKNVHYLPVEEQQYLIQILHHDESQFRLILLSDIELNELIRCRQISAEFYYFFIYTQIEMLPLRKHITDVADIFTHYVKNICVRLNKPIVIPDKKMLQNLRNKEWHGNVKELINVAELYAIGLLSHITLVVPPVFNDSQMSSLDEQLNQYEKQLIEDALVFY","1552983","[FUNCTION] Member of the two-component regulatory system pgtB/pgtA that regulates the inducible phosphoglycerate transport system. When activated by pgtB it acts in conjunction with sigma-54 as a transcriptional activator. ","phosphoglycerate transport system activator protein","Cytoplasm","","
InterPro
IPR002078
Domain
RNA polymerase sigma factor 54, interaction
PS50045\"[12-143]TSIGMA54_INTERACT_4
noIPR
unintegrated
unintegrated
G3DSA:1.10.8.60\"[87-143]Tno description
G3DSA:3.40.50.300\"[9-86]Tno description


","BeTs to 8 clades of COG2204COG name: Response regulator containing CheY-like receiver, AAA-type ATPase, and DNA-binding domainsFunctional Class: TThe phylogenetic pattern of COG2204 is -------q----b-efghsnujxit-Number of proteins in this genome belonging to this COG is","","Residues 9 to 79 match (3e-08) PD:PD087393 which is described as COMPLETE PROTEOME SENSORY PGTA TRANSCRIPTION REGULATORY TRANSDUCTION REGULATION DNA-BINDING PHOSPHORYLATION ","","","","","","","","","","","Thu Jan 16 15:40:36 2003","Thu Jan 16 15:40:36 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02281 is paralogously related to AA01579 (4e-05).","","","","","","","","","","","Yu,G.Q. and Hong,J.S. Identification and nucleotide sequence of the activator gene of the externally induced phosphoglycerate transport system of Salmonellatyphimurium. Gene 45 (1): 51-57 (1986) [PubMed: 3023201].Yang,Y.L., Goldrick,D. and Hong,J.S. Identification of the products and nucleotide sequences of two regulatory genes involved in the exogenous induction ofphosphoglycerate transport in Salmonella typhimurium. J. Bacteriol. 170 (9): 4299-4303 (1988) [PubMed: 2842311].","","Thu Jan 16 15:40:36 2003","1","","","" "AA02282","1553904","1553497","408","ATGGATAGCCAAATTCCGGTGATTATGATTACCGGGCATGGTGATGTTCCCATGGCGGTAGAAGCTGTCAAGAAAGGGGCGACAAATTTCTTTGAAAAACCGGTTTCCCCTGAAAAATTACTTATTCAAGTCGATAACGCTTTAAAAAAACGGAAAAAGGTGATTGAAAAGCGCCAATGGCAAATGGAAAAAATTAATGACGTTTTTATTGGCAGCAGTGTTTGGATTAACGAGTTAAAAAAACAATTACAGAAGCTGGCCAATTCGAATCTACCGGTTTTTATTTGGGGAGAGATTGGCACCGGTCGTCATTTAGCGGCGACTTATCTGCATAAATTAAGCGATCGAAAAACACTACCGATGGTTTTTCATGAATGTACACAAAATGATAATATTAATAGAGCTAAT","","","15866","MDSQIPVIMITGHGDVPMAVEAVKKGATNFFEKPVSPEKLLIQVDNALKKRKKVIEKRQWQMEKINDVFIGSSVWINELKKQLQKLANSNLPVFIWGEIGTGRHLAATYLHKLSDRKTLPMVFHECTQNDNINRAN","1553497","[FUNCTION] Member of the two-component regulatory system pgtB/pgtA that regulates the inducible phosphoglycerate transport system. When activated by pgtB it acts in conjunction with sigma-54 as a transcriptional activator. ","phosphoglycerate transport system transcriptional regulatory protein","Cytoplasm","","
InterPro
IPR001789
Domain
Response regulator receiver
PD000039\"[2-49]TQ9CKZ0_PASMU_Q9CKZ0;
PF00072\"[2-45]TResponse_reg
PS50110\"[1-48]TRESPONSE_REGULATORY
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2300\"[1-68]Tno description
G3DSA:3.40.50.300\"[69-126]Tno description
PTHR23283\"[3-53]TSENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF21\"[3-53]TTWO-COMPONENT SYSTEM SENSOR HISTIDINE KINASE/RESPONSE REGULATOR (INTESTINAL BACTERIA - BACTEROIDES THETAIOTAOMICRON)


","BeTs to 12 clades of COG2204COG name: Response regulator containing CheY-like receiver, AAA-type ATPase, and DNA-binding domainsFunctional Class: TThe phylogenetic pattern of COG2204 is -------q----b-efghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-09) to 1/3 blocks of the IPB002078 family, which is described as \"Sigma-54 factor interaction protein family\". Interpro entry for IP:IPR002078. IPB002078A 93-127 1.1e-09Significant hit ( 2.8e-06) to 1/4 blocks of the IPB001867 family, which is described as \"Transcriptional regulatory protein, C terminal\". Interpro entry for IP:IPR001867. IPB001867B 6-50 2.5e-06","","","","","","","","","","","","Thu Jan 16 15:44:20 2003","Thu Jan 16 15:44:20 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02282 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Yu,G.Q. and Hong,J.S. Identification and nucleotide sequence of the activator gene of the externally induced phosphoglycerate transport system of Salmonella typhimurium. Gene 45 (1): 51-57 (1986) [PubMed: 3023201]. Yang,Y.L., Goldrick,D. and Hong,J.S. Identification of the products and nucleotide sequences of two regulatory genes involved in the exogenous induction of phosphoglycerate transport in Salmonella typhimurium. J. Bacteriol. 170 (9): 4299-4303 (1988) [PubMed: 2842311].","","Thu Jan 16 15:44:20 2003","1","","","" "AA02283","1554122","1553922","201","ATGTTTAATTATCAGAATAATGTTTTATTAATTGATGATGATTTTGATATTTTGGAATCGTATGCCGATTTATTACAACAAGAAGGCTATTCTGTATTTGCAACTGCCGAACCTAAAGAGATTATTAATCAAATTCCGGAAAATTGGTATGGCGTTGTGATTTGCGACGTATTATTGCTGGGCATTTCAGGATTAGATGAT","","","7597","MFNYQNNVLLIDDDFDILESYADLLQQEGYSVFATAEPKEIINQIPENWYGVVICDVLLLGISGLDD","1553922","[FUNCTION] Member of the two-component regulatory system pgtB/pgtA that regulates the inducible phosphoglycerate transport system. When activated by pgtB it acts in conjunction with sigma-54 as a transcriptional activator. ","possible phosphoglycerate transport system activator protein","Cytoplasm","","
InterPro
IPR001789
Domain
Response regulator receiver
PD000039\"[7-65]TQ9CKZ0_PASMU_Q9CKZ0;
PF00072\"[6-66]TResponse_reg
PS50110\"[7-67]TRESPONSE_REGULATORY
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2300\"[8-66]Tno description


","BeTs to 6 clades of COG2204COG name: Response regulator containing CheY-like receiver, AAA-type ATPase, and DNA-binding domainsFunctional Class: TThe phylogenetic pattern of COG2204 is -------q----b-efghsnujxit-Number of proteins in this genome belonging to this COG is","","Residues 7 to 65 match (2e-10) PD:PD000039 which is described as SENSORY TRANSDUCTION PHOSPHORYLATION COMPLETE PROTEOME REGULATOR RESPONSE TRANSCRIPTION DNA-BINDING REGULATION ","","","","","","","","","","","Thu Jan 16 15:46:34 2003","Thu Jan 16 15:46:34 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02283 is paralogously related to AA00997 (4e-05) and AA00757 (0.001).","","","","","","","","","","","Yu,G.Q. and Hong,J.S. Identification and nucleotide sequence of the activator gene of the externally induced phosphoglycerate transport system of Salmonella typhimurium. Gene 45 (1): 51-57 (1986) [PubMed: 3023201]. Yang,Y.L., Goldrick,D. and Hong,J.S. Identification of the products and nucleotide sequences of two regulatory genes involved in the exogenous induction of phosphoglycerate transport in Salmonella typhimurium. J. Bacteriol. 170 (9): 4299-4303 (1988) [PubMed: 2842311].","","Thu Jan 16 15:46:34 2003","1","","","" "AA02284","1556097","1554118","1980","ATGAAAAAATGGCTTAAACGCTTGGATATTAGCACAAGTTTACAACTATCACTTATTATCAGCGCGTTGTTTTGCCTGTTTATCGGTGCCGTCGGTTTATATACATGGCATCAGCAACGGATAGAAATTGATCTTGCTATTGATCAGAATTTTCCAAAGATTCAAGCCGCTTTCCGCATGGAGGAACAAATTAATTTATTGGAAAATACATTATTAAATGCAAATAATATTCGAAATACAGAAGAAAAAATTAAATGGTTTAATGCGTTACAGAAACAAATTAAAACGCTAAAAGACATGACCCAATCATTAAATGAAGATTTGAATGATGAAATTTCCACTATCGTAATTGAACAAGCCAATCTTCTACAAGAGTTATCATTAAATATTGATAATCAATTAATCTTAAATACGAAATTTAATAAAACGTTATCGGAAATAAATTGGTTGCATAATGATTTTCGAGATGAATTTACGGCGTTGTTGCAGGAAATTGTTTGGCAACAAACAACATTAGCCAATCATCTTACTGATAATTTAACTAGATCTAAACAAATCGAACAACTTAGAGAATTCCAGCATGAATTATTGTTACTTTATGATTTCCTTACTTATGAAGAACAAATTGTCACGGAACTAAAACAACATATCGTCAGCCGCTCTGATTATTCATTAGTTGCACTCACAAATTCCCTTAATTATTTAAAGAATTTAATTGATCAAAAAGTTAAGTCTTTAGATAAACATACTTCAAGTTATACGATTAAACAAATTATTGAGTCCTTGCTGGCTATCGGAGAAAATGAACAATCGTTACCTCATTTATTAGTTGAAAGAAAACAACTGGATATTTCCCAACGGCAATTAATGAATGAAAGTGAATTGGTCATTTCTAAATTAAGAAGGAAAATTAACAGTCAGATTGGTGATAATCAAAAACAATTAGAATTGTTTCATTATTTAATAAATAAAAGCACCAGAATAAATGGCTTGATTATTCTGTCTGCCGTCTTATTTGTTTTTCTTTTTGTTGCAGCAATTAATTTTTATTATATTCGACGGAGATTAATAGGGCGTTTTCAATCTCTTAATCAATCTGTTGAACGGCTTATTAACGGCGAATCTTCCGTTAAAATTTCAGTTTATGGTAATGATGAATTAGGGCGTATCGCAAAATTATTGCGATTATTTTTATTTGAAGTTAACACAAAAAATGAAGAATTAGAAAGAAGAAATCAAATTTTATTAAATGAAATTAGTGAACGTATTGCAATCCAGGAAAAACTTATCAATACACAACAAGAACTAATTCAAGCGGCAAAATTAGCGGTAGTAGGACAAACTTTGACATCTATTAGCCATGAAATCACACAACCGCTAAATGCAATGAATGCGTATATTTTCAGTACAAAAAGAGCGGTCAAAAATAATGATGTTTTTTCTGCGAATAACTATTTAGAGAAAATAGAAAATTTAGTGGAGCGTACGGCGCTGGTGGTGAAAAGACTGCGCCATTTTTCCCGCCAAACCACAAATACATTACAGAAAATTAATTTATTGATGTGTATAAATAATGCGTGGGATTTACTTGAGCCAAAACATAAATATCTGAATGCTCGGTTATCTCTTCCTACAGATTTACCTGATGTATTAGGTGATGAAATTTTATTAGAGCAAATATTTGTGAATATTTTCCTGAACTCACTGGAAGCTATGCAGCATGAAAAACCGGAGATTGAGATAAAAATACAAAATATATCGGATCAGAGAGTAGAATTATGGGTTTCTGATAATGGTTCCGGTTGGCCGTTGTCAGATAAATTACTACAACCTTTCTCCAGTAGTAAATCCATTAATTTAGGCTTAGGATTATCAATAAGTCTATCCATTATGCAACAATGTCAAGGAAACTTATTAATTGCTTCTACATTGACAAAAAATGCGCTGGTTATTTTGGAATTTAAGGTGGTAGATAATGTT","","","78354","MKKWLKRLDISTSLQLSLIISALFCLFIGAVGLYTWHQQRIEIDLAIDQNFPKIQAAFRMEEQINLLENTLLNANNIRNTEEKIKWFNALQKQIKTLKDMTQSLNEDLNDEISTIVIEQANLLQELSLNIDNQLILNTKFNKTLSEINWLHNDFRDEFTALLQEIVWQQTTLANHLTDNLTRSKQIEQLREFQHELLLLYDFLTYEEQIVTELKQHIVSRSDYSLVALTNSLNYLKNLIDQKVKSLDKHTSSYTIKQIIESLLAIGENEQSLPHLLVERKQLDISQRQLMNESELVISKLRRKINSQIGDNQKQLELFHYLINKSTRINGLIILSAVLFVFLFVAAINFYYIRRRLIGRFQSLNQSVERLINGESSVKISVYGNDELGRIAKLLRLFLFEVNTKNEELERRNQILLNEISERIAIQEKLINTQQELIQAAKLAVVGQTLTSISHEITQPLNAMNAYIFSTKRAVKNNDVFSANNYLEKIENLVERTALVVKRLRHFSRQTTNTLQKINLLMCINNAWDLLEPKHKYLNARLSLPTDLPDVLGDEILLEQIFVNIFLNSLEAMQHEKPEIEIKIQNISDQRVELWVSDNGSGWPLSDKLLQPFSSSKSINLGLGLSISLSIMQQCQGNLLIASTLTKNALVILEFKVVDNV","1554118","[FUNCTION] Member of the two-component regulatory system pgtB/pgtA that regulates the inducible phosphoglycerate transport system. activates pgtA by phosphorylation. ","phosphoglycerate transport; protein for signal transmission","Inner membrane, Cytoplasm","","
InterPro
IPR003594
Domain
ATP-binding region, ATPase-like
G3DSA:3.30.565.10\"[510-656]Tno description
PF02518\"[552-657]THATPase_c
SM00387\"[552-658]THATPase_c
InterPro
IPR003660
Domain
Histidine kinase, HAMP region
PF00672\"[334-403]THAMP
SM00304\"[354-406]THAMP
PS50885\"[354-406]THAMP
InterPro
IPR003661
Domain
Histidine kinase A, N-terminal
PF00512\"[444-512]THisKA
SM00388\"[444-512]THisKA
InterPro
IPR005467
Domain
Histidine kinase
PS50109\"[451-658]THIS_KIN
noIPR
unintegrated
unintegrated
PTHR23283\"[1-7]T\"[434-656]TSENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF24\"[1-7]T\"[434-656]TTWO COMPONENT HISTIDINE KINASE (SPORULATION KINASE)
signalp\"[1-32]?signal-peptide
tmhmm\"[14-34]?\"[331-351]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 6.9e-05) to 3/4 blocks of the PR00344 family, which is described as \"Bacterial sensor protein C-terminal signature\". Prints database entry for PR:PR00344. PR00344A 591-605 5.3 PR00344B 607-617 1.3e+02 PR00344C 618-636 0.043","Residues 422 to 509 match (3e-22) PD:PD003857 which is described as KINASE TRANSFERASE PROTEOME COMPLETE SENSORY TRANSDUCTION PHOSPHORYLATION SENSOR HISTIDINE TWO-COMPONENT ","","","","","","","","","","","Thu Jan 16 17:47:05 2003","Thu Jan 16 17:47:05 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02284 is paralogously related to AA00757 (1e-12) and AA00995 (2e-04).","","","","","","Residues 552 to 657 (E-value = 1.3e-13) place AA02284 in the HATPase_c family which is described as Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase (PF02518)","","","","","Yang,Y.L., Goldrick,D. and Hong,J.S. Identification of the products and nucleotide sequences of two regulatory genes involved in the exogenous induction ofphosphoglycerate transport in Salmonella typhimurium. J. Bacteriol. 170 (9): 4299-4303 (1988) PubMed: 2842311.Jiang,S.Q., Yu,G.Q., Li,Z.G. and Hong,J.S. Genetic evidence for modulation of the activator by two regulatory proteins involved in the exogenous induction of phosphoglycerate transport in Salmonella typhimurium. J. Bacteriol. 170 (9): 4304-4308 (1988) PubMed: 2842312.","","Tue Feb 4 16:54:13 2003","1","","","" "AA02285","1557344","1556097","1248","ATGTCAGGGATAAAACGAGGTTATTTTCATTCTCTGCTTGTCGTGCCGGTCATCGCTTTATTCTGTTTAGGAAGGGCGTATAGCAATGAATTGGTCATTGGTACGACATTTTCACCGGAGTCCCTTTCTTATTTAATTACCGAGTGGGAAAAGCAACCGAATGCCACGTCGATAAGAATGCTAAACAGAACAAGCAACTCATTAAACAAACTATTTGATGACGAAAAAAACGATAATATTGATCTTGTTTTAAGTTCCTCTCCTATGCTGTTTTATCACTTGCAGGAAAAACAACGATTGGCTGCTTTGCCGGATAAATTCAGCCAAGGAAAAAAATTCGTACCGGAGATTTTACAAAAAACAACCGTAGCATTTTCACTATCGGGATGTGGTATTTTTTCCAATGTAGCACTACTGGAAAATGCAGAAGTGGATGTTCCTACTGACTGGTCCGGGCTTATTTCTCCCAATTTGCAGGGATTGGTTATTATGAGTAGTCCGAGCCGTTCCGATACGACGCACATTATGATTGAGGCATTATTACAGAAACAGGGCTGGCAGCAAGGTTGGGCATTAATTCATCAAGTTATGGCGAATGTCGGAACCATTTCCTCCCGTAGTTTTGGTGTCGTTGATAAAGTTCAGGCAGGGTTAGGTGCCGCAGGGATTACCATTGATAATTACGCAAATTTGCTCACACATTACAATGTAGATCCGCATTCAGCTTTGATTTTTAAATATTTTCCGAATTTCCCCGTTTCTCCGACGTTTATCGCAATAACAACAAATAGTACCAATAGCCGGCAAGCATCGGCGTTTATCCATTTTCTTTTAAGTGATCCTGGGCAAAGTACGTTATATCACAGCAAAATGGGAAAATATCCGATTATTCCGTTAGCCAAATCCCATCCGCTATATGCAACTCAACAATTTTTATTTTCCCAACCGACGATTGATTATCAGCTGCTGTTAAAACGTCAGGAGGTGGTTAAACTGATGTTTGAGCATCAGATCATTCATCGGTTAGCTCAAATTCAAGAAAACTGGAAAATTCTTTATCAAAAGGAACAACAAGCAGGACATCCATTGCCGGAATTGCGGGAAATTTTGACCGCACTTCCTATAACGGAAAAGCAGGCTACTGACGAAAATTATTTGGAAACGTTTAAGGCAAATGAGGCGTTACTGCATTGGCAACACTTTTTCATGTTACAGCAAATGCGATTTGTCGATACAGTGGAAAAATTA","","","47425","MSGIKRGYFHSLLVVPVIALFCLGRAYSNELVIGTTFSPESLSYLITEWEKQPNATSIRMLNRTSNSLNKLFDDEKNDNIDLVLSSSPMLFYHLQEKQRLAALPDKFSQGKKFVPEILQKTTVAFSLSGCGIFSNVALLENAEVDVPTDWSGLISPNLQGLVIMSSPSRSDTTHIMIEALLQKQGWQQGWALIHQVMANVGTISSRSFGVVDKVQAGLGAAGITIDNYANLLTHYNVDPHSALIFKYFPNFPVSPTFIAITTNSTNSRQASAFIHFLLSDPGQSTLYHSKMGKYPIIPLAKSHPLYATQQFLFSQPTIDYQLLLKRQEVVKLMFEHQIIHRLAQIQENWKILYQKEQQAGHPLPELREILTALPITEKQATDENYLETFKANEALLHWQHFFMLQQMRFVDTVEKL","1556097","[FUNCTION] Required for pgtP expression, it may act jointly with the pgtA/pgtB signaling proteins. ","phosphoglycerate transport regulatory protein","Inner membrane, Cytoplasm","","
InterPro
IPR011587
Domain
Prokaryotic extracellular metal-binding protein
PD008688\"[248-286]TPGTC_SALTY_P37591;
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[145-286]Tno description
signalp\"[1-28]?signal-peptide
tmhmm\"[9-29]?transmembrane_regions


","BeTs to 5 clades of COG1840COG name: ABC-type iron/thiamine transport systems, periplasmic componentFunctional Class: HThe phylogenetic pattern of COG1840 is -o--kz---d-lbcefghsnuj--t-Number of proteins in this genome belonging to this COG is","","Residues 227 to 292 match (1e-07) PD:PD038035 which is described as COMPLETE PROTEOME PERIPLASMIC ABC BINDING TRANSPORTER TRANSPORTER SPERMIDINE/PUTRESCINE-BINDING PRECURSOR SPERMIDINE/PUTRESCINE ","","","","","","","","","","","Thu Jan 16 17:50:49 2003","Thu Jan 16 17:50:49 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02285 is paralogously related to AA01642 (5e-04).","","","","","","","","","","","Yang,Y.L., Goldrick,D. and Hong,J.S. Identification of the products and nucleotide sequences of two regulatory genes involved in the exogenous induction of phosphoglycerate transport in Salmonella typhimurium. J. Bacteriol. 170 (9): 4299-4303 (1988) [PubMed: 2842311].Jiang,S.Q., Yu,G.Q., Li,Z.G. and Hong,J.S. Genetic evidence for modulation of the activator by two regulatory proteins involved in the exogenous induction of phosphoglycerate transport in Salmonella typhimurium. J. Bacteriol. 170 (9): 4304-4308 (1988) [PubMed: 2842312].","","Thu Jan 16 17:50:49 2003","1","","","" "AA02286","1557718","1558596","879","ATGAATAAGAAATTCACCTCAGGCTTAATTGCACTCAGTTTAGGACTTTCCATCAGCGGTATGGCTGTCGCCCAAGACAAACTCATCGTTTACACCTCCATGAAAGAATCCCTCATCGGGGCGTTAAAAGCCAAATTTAATGAAAAATACCCGGACATTGCGATGGACTATCAATCTGCCGGTGCGGGCAAACTCATGGCAAAAATTGCCACGGAAAAAGAATCCGGTCAGATTATGGCAGATGTTATTTGGACCAGTGAAGTCCCTGACTTCTTCAATATGAAAGAAACCGGCATGCTAGAAACTTATATTTCGCCCGAAGTAGAAAATATCATTAATCCGATTCCCGATTTCGACGGTTCTTTTACGCCGATACGCTTAGGCACATTAGGTATCGCCTACAACACCCGCTTTGTGAAAAAAGAACCGCCGGCACAATGGGCGGATATTCTTACTCCGCAATTTAAAGGCGCATTCGGTATTGCCAACCCTGCCCTAAACATTTACAATAATCCGGTGAATAAATTCGTGTTTAATTTCATTGGGCTATCCAATCAGTTGAACGTCAATTTGTCTGCGCAAGGTGTCACTATTGATCATTGTGAAGGTGTTTTTAATATTCAACCGACGCCTCCGGCAGAATTATTGGTTCAGGGTAAAGCACTTCTGGCAAGCCGCCCGTCGGAAATTGAATTTGTCAATCAAGGCGGAATTCCCGGCATCGTGAAACGCCGTTCTTACTTAGGTGAAGTCATTGATTACAGTGTTCACATCGGTGATCAAGAACTGCGCGTACAAAAAGGACGCCGTGACCCGTTATTAAACGAAGGCGAATCATGTCAAATTCAGTTTACCAAACTGCATTGGTATCCCGCCGAA","","","32519","MNKKFTSGLIALSLGLSISGMAVAQDKLIVYTSMKESLIGALKAKFNEKYPDIAMDYQSAGAGKLMAKIATEKESGQIMADVIWTSEVPDFFNMKETGMLETYISPEVENIINPIPDFDGSFTPIRLGTLGIAYNTRFVKKEPPAQWADILTPQFKGAFGIANPALNIYNNPVNKFVFNFIGLSNQLNVNLSAQGVTIDHCEGVFNIQPTPPAELLVQGKALLASRPSEIEFVNQGGIPGIVKRRSYLGEVIDYSVHIGDQELRVQKGRRDPLLNEGESCQIQFTKLHWYPAE","1558596","","sugar ABC transporter, ATP-binding protein","Periplasm, Inner membrane, Cytoplasm","","
InterPro
IPR013611
Domain
Transport-associated OB
PF08402\"[223-292]TTOBE_2
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[27-183]Tno description
signalp\"[1-24]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","BeTs to 7 clades of COG1840COG name: ABC-type iron/thiamine transport systems, periplasmic componentFunctional Class: HThe phylogenetic pattern of COG1840 is -o--kz---d-lbcefghsnuj--t-Number of proteins in this genome belonging to this COG is","","Residues 21 to 164 match (5e-07) PD:PD590160 which is described as PROTEOME COMPLETE PLASMID RB0157 RB0158 RA0275 ","","","","","","","","","","","","Thu Jan 16 17:54:48 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02286 is paralogously related to AA00696 (4e-13), AA00698 (1e-10) and AA01642 (4e-10).","","","","","","","","","","","","","","1","","","" "AA02288","1559263","1558730","534","ATGGAACATAAAATCGAAGATTTAATCCATATTTTTAATCAATGTTTTGAACAGGAATACAACACCAAATTAGTCAAGGGTGGCGATGAGCCTTTGTACGTGCCGGCAAATGAAGATTGTCCTTACAACGCTATCTATTTTGCCCGCGGATTCTACAGCAGTGGATTACATGAAATCGCCCATTGGCTGGTTGCAGGCAAAGAGCGTCGCAAACTGGAAGATTTTGGTTATTGGTATGAACCCGACGGGCGATCGGAAGAGCAACAACGCTTATTTGAAAAAGTGGAAGTGAAACCGCAAGCGTTGGAATGGATTCTAGCCACTGCCGCCGGTTTTCGTTATTACGCCAGCGCCGACAACCTCAACGGACAGCCGGGAGACACCCGACCGTTCAAACAGGCAGTATATGAACAAGTGAAAACCTATGCCGAAAAAGGTTTGCCTAAACGCGCCGAAACTCTGCGTCAAGCCCTCACCAAGTTTTACGGCACAGAAGATCACATTGATTTGACGAAGTTTGATGTAACGAGAATT","","","20752","MEHKIEDLIHIFNQCFEQEYNTKLVKGGDEPLYVPANEDCPYNAIYFARGFYSSGLHEIAHWLVAGKERRKLEDFGYWYEPDGRSEEQQRLFEKVEVKPQALEWILATAAGFRYYASADNLNGQPGDTRPFKQAVYEQVKTYAEKGLPKRAETLRQALTKFYGTEDHIDLTKFDVTRI","1558730","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR006025
Binding_site
Peptidase M, neutral zinc metallopeptidases, zinc-binding site
PS00142\"[54-63]?ZINC_PROTEASE
InterPro
IPR007411
Family
Protein of unknown function DUF462
PF04315\"[1-176]TDUF462
noIPR
unintegrated
unintegrated
PD022441\"[84-165]TYFCM_HAEIN_P44255;


","BeTs to 3 clades of COG3101COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3101 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 1 to 164 match (2e-78) PD:PD022441 which is described as PROTEOME COMPLETE CYTOPLASMIC YPO2754 TRANSPORTING YFCM PM0469 HI1563 VC2113 ATPASE ","","","","","","","","","","","","Thu Jan 16 17:55:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02288 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 176 (E-value = 3.9e-143) place AA02288 in the DUF462 family which is described as Protein of unknown function, DUF462 (PF04315)","","","","","","","","1","","","" "AA02289","1561279","1559363","1917","GTGGTTGTGGCCATTGTCATGATGACTGCATATCAAAGTTTTAATACCACTTCCGGCGGAGGGATAACGGATTATACGACATTCATTTCGGATGTTGAAAATAATCAGGTACGTCAGGCTAAATTTGAAGATAATGAAATTTTAGTCACTAAAACCGACGGCACTAAATATACAACAGTTATTCCATTGGAAGACAAAGATCTTTTGAATGATTTGTTGAAGAAAAAAGTGAAAGTTGAAGGCACGCCGCCGGAAAGAAGAAGTTTGTTATCCCAAATCTTGATTTCTTGGTTCCCGATGCTGTTATTAATCGGCGTTTGGGTTTTCTTCATGCGACAAATGCAAGGCGGTGGCGGCAAAGCGATGAGCTTTGGTAAAAGCCGTGCACGCATGATGACACAAGAGCAAATCAAAACAACATTTGCCGATGTGGCGGGTTGTGATGAAGCAAAAGAAGAAGTGGGTGAGATCGTTGACTTCTTGCGTGAACCGAAAAAATTCCAAAATTTAGGTGGTAAAATTCCAAAAGGGATTTTAATGGTCGGACCTCCAGGTACCGGTAAAACCTTATTAGCAAAAGCTATTGCCGGCGAAGCGAAAGTGCCGTTTTTCACCATTTCAGGTTCAGACTTTGTAGAAATGTTCGTTGGTGTTGGTGCTTCCCGTGTTCGTGATATGTTTGAAAAAGCGAAGAAAAATGCACCATGCTTAATTTTTATTGATGAAATTGATGCTGTTGGTCGCCAACGTGGTGCAGGTCTTGGTGGCGGTCACGATGAACGTGAGCAGACCTTAAACCAAATGTTGGTGGAAATGGACGGTTTCGAAGGCAACGAAGGTGTTATTGTTATTGCCGCAACGAACCGCCCGGATGTTCTGGACCCGGCTTTAACCCGTCCCGGACGTTTTGATCGTCAGGTTGTTGTCGGTTTGCCGGATGTAAAAGGTCGTGAACAAATCCTCAAAGTGCATATGCGTAAGGTGCCGGTTGCGCCGGATGTGGATGCCATGACTTTGGCGCGCGGAACTCCGGGTTATTCCGGTGCGGATTTGGCGAACCTGGTTAATGAAGCTGCGTTGTTTGCTGCACGCACTAATAAGCGCACGGTAACCATGGTAGAGTTTGAAAAAGCAAAAGATAAAATCAACATGGGACCCGAACGTCGTACTATGATCATGACCGATAAGCAAAAAGAATCCACCGCTTATCACGAAGCCGGTCATGCTATTGTTGGTTATTTAGTGCCGGAACATGATCCGGTACATAAAGTTACGATTATTCCGCGCGGACGCGCTTTAGGTGTTACCTTCTTCTTACCTGAGGGAGACCAAATCAGTATCAGCCAAAAACAGTTGGAAAGTAAACTTTCCACGTTATACGCAGGTCGTTTGGCAGAAGATTTGATTTACGGTGAAGAAAATATTTCTACCGGGGCGTCCAATGATATTAAAGTGGCAACCAACATCGCCCGTAATATGGTGACTCAGTGGGGTTTCTCCGATAAACTTGGTCCAATTCTTTATGCCGAAGACGACGGGGAAGTATTCTTAGGGCGTTCCATGGCGAAAGCCAAACACATGTCCGATGAAACCGCACATGTGATCGATGAGGAAGTTCGCGCTATTGTGAACCGAAATTATGGTCGCGCGAGACAGATTTTAATCGATAATATGGATATTCTACACGCGATGAAAGATGCGCTGGTGAAATACGAAACTATTGAAGAAGAACAAATCAAGCAGTTAATGAATCGTCAACCAGTGACACCGCCTCCAGGTTGGGAAGAACCAAAGAATACAGATAAAGCCGAACCTCAGCAGCCGAAAGCTGAAGAGCCAAAAATGGCAGATGATGCGCAGGGCGTGGAAACACAAAGTGCGGTGGAAAAAAATGATGATTCCAAATCTTTTAATAGC","","","71846","VVVAIVMMTAYQSFNTTSGGGITDYTTFISDVENNQVRQAKFEDNEILVTKTDGTKYTTVIPLEDKDLLNDLLKKKVKVEGTPPERRSLLSQILISWFPMLLLIGVWVFFMRQMQGGGGKAMSFGKSRARMMTQEQIKTTFADVAGCDEAKEEVGEIVDFLREPKKFQNLGGKIPKGILMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEKAKKNAPCLIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGVIVIAATNRPDVLDPALTRPGRFDRQVVVGLPDVKGREQILKVHMRKVPVAPDVDAMTLARGTPGYSGADLANLVNEAALFAARTNKRTVTMVEFEKAKDKINMGPERRTMIMTDKQKESTAYHEAGHAIVGYLVPEHDPVHKVTIIPRGRALGVTFFLPEGDQISISQKQLESKLSTLYAGRLAEDLIYGEENISTGASNDIKVATNIARNMVTQWGFSDKLGPILYAEDDGEVFLGRSMAKAKHMSDETAHVIDEEVRAIVNRNYGRARQILIDNMDILHAMKDALVKYETIEEEQIKQLMNRQPVTPPPGWEEPKNTDKAEPQQPKAEEPKMADDAQGVETQSAVEKNDDSKSFNS","1559363","[FUNCTION] Seems to act as an ATP-dependent zinc metallopeptidase. Involved in the degradation of sigma-32. Degrades carboxy-terminal-tagged cytoplasmic proteins. These proteins are tagged with an 11-amino-acid nonpolar destabilizing tail via a mechanism involving the 10sa (ssrA) stable RNA. ","cell division protein H, a metalloprotease","Inner membrane, Cytoplasm","","
InterPro
IPR000642
Domain
Peptidase M41
PF01434\"[371-582]TPeptidase_M41
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[174-313]TAAA
InterPro
IPR003959
Domain
AAA ATPase, core
PF00004\"[177-364]TAAA
InterPro
IPR003960
Domain
AAA ATPase, subdomain
PS00674\"[281-299]TAAA
InterPro
IPR005936
Domain
Peptidase M41, FtsH
TIGR01241\"[89-584]TFtsH_fam: ATP-dependent metallopeptidase Hf
InterPro
IPR011546
Domain
Peptidase M41, FtsH extracellular
PF06480\"[21-151]TFtsH_ext
noIPR
unintegrated
unintegrated
G3DSA:1.10.8.60\"[312-380]Tno description
G3DSA:3.40.50.300\"[127-309]Tno description
PTHR23076\"[1-573]TMETALLOPROTEASE M41 FTSH
PTHR23076:SF10\"[1-573]TCELL DIVISION PROTEIN FTSH HOMOLOG
tmhmm\"[93-111]?transmembrane_regions


","BeTs to 19 clades of COG0465COG name: ATP-dependent Zn proteasesFunctional Class: OThe phylogenetic pattern of COG0465 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit (8.8e-205) to 7/7 blocks of the IPB000642 family, which is described as \"Peptidase family M41\". Interpro entry for IP:IPR000642. IPB000642A 141-189 1.8e-40 IPB000642B 207-251 5.7e-45 IPB000642C 280-324 1.3e-43 IPB000642D 339-364 4.2e-20 IPB000642E 396-432 1.7e-29 IPB000642F 460-471 0.0064 IPB000642G 475-500 1.5e-16Significant hit ( 4.1e-65) to 4/12 blocks of the IPB003338 family, which is described as \"Amino-terminal subdomain, VAT-Nn\". Interpro entry for IP:IPR003338. IPB003338H 129-168 0.055 IPB003338I 182-226 1.6e-14 IPB003338J 227-251 4e-12 IPB003338K 269-322 2.1e-32Significant hit ( 3.6e-56) to 2/2 blocks of the IPB003960 family, which is described as \"AAA-protein subfamily\". Interpro entry for IP:IPR003960. IPB003960A 217-250 4.4e-23 IPB003960B 267-313 6.5e-32Significant hit ( 6.3e-05) to 1/8 blocks of the IPB001984 family, which is described as \"ATP-dependent serine proteases, Lon family\". Interpro entry for IP:IPR001984. IPB001984C 175-211 6.2e-05","Residues 449 to 510 match (4e-07) PD:PD522714 which is described as ATP-BINDING PROTEOME CELL DIVISION COMPLETE ZINC TRANSMEMBRANE PROTEASE 3.4.24.- METALLOPROTEASE ","","","","","","","","","","","Thu Jan 16 18:01:19 2003","Thu Jan 16 18:01:19 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02289 is paralogously related to AA00460 (8e-07), AA00120 (2e-06) and AA02728 (2e-04).","","","","","","Residues 370 to 582 (E-value = 1.4e-124) place AA02289 in the Peptidase_M41 family which is described as Peptidase family M41 (PF01434)","","","","","Krzywda S, Brzozowski A, Verma C, Karata K, Ogura T, Wilkinson A. The Crystal Structure of the AAA Domain of the ATP-Dependent Protease FtsH of Escherichia coli at 1.5 A Resolution. Structure (Camb). 2002 Aug;10(8):1073. PMID: 12176385 Chiba S, Akiyama Y, Ito K. Membrane protein degradation by FtsH can be initiated from either end. J Bacteriol. 2002 Sep;184(17):4775-82. PMID: 12169602 Tomoyasu,T., Yuki,T., Morimura,S., Mori,H., Yamanaka,K., Niki,H., Hiraga,S. and Ogura,T. The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions,cell cycle control, and gene expression. J. Bacteriol. 175 (5): 1344-1351 (1993) [PubMed: 8444796].Ogura,T., Tomoyasu,T., Yuki,T., Morimura,S., Begg,K.J., Donachie,W.D., Mori,H., Niki,H. and Hiraga,S. Structure and function of the ftsH gene in Escherichia coli . Res. Microbiol. 142 (2-3): 279-282 (1991) [PubMed: 1925026].Herman,C., Ogura,T., Tomoyasu,T., Hiraga,S., Akiyama,Y., Ito,K., Thomas,R., D'Ari,R. and Bouloc,P. Cell growth and lambda phage development controlled by the same essential Escherichia coli gene, ftsH/hflB. Proc. Natl. Acad. Sci. U.S.A. 90 (22): 10861-10865 (1993) [PubMed: 8248182]. Akiyama,Y., Shirai,Y. and Ito,K. Involvement of FtsH in protein assembly into and through the membrane. II. Dominant mutations affecting FtsH functions. J. Biol. Chem. 269 (7): 5225-5229 (1994) [PubMed: 8106505]. ","","Tue Dec 2 11:19:49 2003","1","","","" "AA02290","1562048","1561422","627","ATGGGCAAGAAAAAACGTTCGGCGAGTTCAACCCGTTGGTTAAACGAGCATTTTAAAGATCCTTTCGTACAAAAGGCGCACAAGCAAAAATTGCGTTCCCGAGCCTATTTCAAACTGGATGAAATTCAACAAACCGACCGCTTATTCAAGCCAGGTATGACGGTGGTTGATTTAGGTGCAGCGCCGGGCGGATGGTCGCAGTATGTGGTAAGCCAAATTGGGCGCAATGGACGGATTATTGCCTGTGATCTTCTGGAAATGGATCCTATTGTAGGCGTGGATTTTCTACAAGGCGATTTCCGTGATGAAAATGTGTTAAACATTTTATTGGAGCGGGTCGGTGAAGGCAAAGTAGATGTGGTGATGTCAGATATGGCACCGAATTTCAGTGGGATGCCATCAGTGGATATTCCGCGTGCGATGTATTTGGTAGAACTTGCGCTTGATATGTGCAAGCAGATTCTCGCTAATAAAGGAAGTTTTGTAGTAAAAGTTTTTCAGGGGGAAGGTTTTGATGAATACTTAAAAGAGATCCGTTCTCTGTTTAGTGTAGTCAAAGTTCGTAAACCTGAAGCCTCCCGAGACCGATCTCGGGAAGTTTATATTGTTGCAAGCGGTTATAAACAC","","","23665","MGKKKRSASSTRWLNEHFKDPFVQKAHKQKLRSRAYFKLDEIQQTDRLFKPGMTVVDLGAAPGGWSQYVVSQIGRNGRIIACDLLEMDPIVGVDFLQGDFRDENVLNILLERVGEGKVDVVMSDMAPNFSGMPSVDIPRAMYLVELALDMCKQILANKGSFVVKVFQGEGFDEYLKEIRSLFSVVKVRKPEASRDRSREVYIVASGYKH","1561422","[FUNCTION] Specifically methylates the uridine in position 2552 of 23S rRNA in the 50S particle (by similarity). ","cell division protein J; ribosomal RNA large subunit methyltransferase J","Cytoplasm","","
InterPro
IPR002877
Domain
Ribosomal RNA methyltransferase RrmJ/FtsJ
PF01728\"[31-209]TFtsJ
InterPro
IPR004512
Family
Ribosomal RNA large subunit methyltransferase J
TIGR00438\"[20-207]TrrmJ: ribosomal RNA large subunit methyltra
InterPro
IPR015507
Family
Ribosomal RNA methyltransferase J
PTHR10920\"[17-208]TRIBOSOMAL RNA METHYLTRANSFERASE
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[30-209]Tno description
PIRSF005461\"[13-209]T23S ribosomal RNA methyltransferase


","BeTs to 14 clades of COG0293COG name: Methyltransferase involved in cell divisionFunctional Class: JThe phylogenetic pattern of COG0293 is aomp--y-------efghsn-jx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 4.2e-57) to 4/4 blocks of the IPB002877 family, which is described as \"FtsJ cell division protein\". Interpro entry for IP:IPR002877. IPB002877A 20-43 2.2e-11 IPB002877B 55-68 3.9e-10 IPB002877C 119-136 4.6e-09 IPB002877D 164-204 3e-22","Residues 1 to 30 match (8e-10) PD:PD591659 which is described as METHYLTRANSFERASE RRNA FTSJ J DIVISION URIDINE-2'-O--METHYLTRANSFERASE 23S PROTEOME SUBUNIT RIBOSOMAL ","","","","","","","","","","","Thu Jan 16 18:08:50 2003","Thu Jan 16 18:08:50 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02290 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 31 to 209 (E-value = 7.6e-81) place AA02290 in the FtsJ family which is described as FtsJ-like methyltransferase (PF01728)","","","","","Caldas,T., Binet,E., Bouloc,P., Costa,A., Desgres,J. and Richarme,G. The FtsJ/RrmJ heat shock protein of Escherichia coli is a 23 S ribosomal RNA methyltransferase. J. Biol. Chem. 275 (22): 16414-16419 (2000) PubMed: 10748051.Caldas,T., Binet,E., Bouloc,P. and Richarme,G. Translational defects of Escherichia coli mutants deficient in the Um(2552) 23S ribosomal RNA methyltransferase RrmJ/FTSJ. Biochem. Biophys. Res. Commun. 271 (3): 714-718 (2000) PubMed: 10814528.Hager J, Staker BL, Bugl H, Jakob U. Active Site in RrmJ, a Heat Shock-induced Methyltransferase. J Biol Chem. 2002 Nov 1;277(44):41978-86. PMID: 12181314 Bugl H, Fauman EB, Staker BL, Zheng F, Kushner SR, Saper MA, Bardwell JC, Jakob U. RNA methylation under heat shock control. Mol Cell. 2000 Aug;6(2):349-60. PMID: 10983982 Caldas T, Binet E, Bouloc P, Costa A, Desgres J,Richarme G. The FtsJ/RrmJ heat shock protein of Escherichia coli is a 23 S ribosomal RNA methyltransferase. J Biol Chem. 2000 Jun 2;275(22):16414-9. PMID: 10748051","","Wed Jan 29 15:19:30 2003","1","","","" "AA02291","1563007","1562186","822","ATGGGTTTTCTTTTTATCTTAATGTTACGCATTATGATTCAAAATAAAATCTTACTGACCGATTGCCCTGACGATAAAGGGCTCATTTCTAAAATTACCAATATTTGCTATAAACATCAGTTGAATATTGTGCACAATAATGAGTTTGTTGATTTTGAAACCAAACATTTTTTTATGAGAACGGAATTGCAGGGTATTTTTAATGAAGAAACCCTGTTAGCCGATTTGGAACTGAGTTTACCGCCGGGAACGAATTGTCGTTTAATTAGCACAAAATATAAGCGAATTGTCATTTTAGTTACTAAAGAAGCCCATTGCCTCGGTGATATTTTAATGAAAAACTATTATGGTGGTTTGAATGTAGAAATTGCAGGGGTGATTGGTAATCATGAAACATTACGCAGTTTGGCGGAGCGGTTTGATATTCCATTTTTCTGGATCAGCCATCAAAATTTAACCCGTGAAGAACATGATTATTTGTTAGCCGAAAAAATTGACGAATTGGCACCGGATTATATTGTGTTGGCAAAATATATGCGGGTCTTAAATCCGAAATTTGTAGCGCGTTATCCTAATCGGGTGATTAACATTCACCATTCGTTTTTGCCTGCATTTATCGGCGCAAAACCTTATCAGCAGGCTTATGAGCGCGGTGTAAAAATTATCGGTGCGACAGCGCATTTTATTAATATTGATCACACCTATAGTGTGGAAGCCATGATGAAAGCCGGACGAGACGTGGAAAAAACAGTATTAAGCCGTGCACTGGATCTTGCGTTACATGATCGTATTTTTGTGTATAAGAACAAAACGATTGTTTTA","","","31670","MGFLFILMLRIMIQNKILLTDCPDDKGLISKITNICYKHQLNIVHNNEFVDFETKHFFMRTELQGIFNEETLLADLELSLPPGTNCRLISTKYKRIVILVTKEAHCLGDILMKNYYGGLNVEIAGVIGNHETLRSLAERFDIPFFWISHQNLTREEHDYLLAEKIDELAPDYIVLAKYMRVLNPKFVARYPNRVINIHHSFLPAFIGAKPYQQAYERGVKIIGATAHFINIDHTYSVEAMMKAGRDVEKTVLSRALDLALHDRIFVYKNKTIVL","1562186","[FUNCTION] Produces formate from formyl-tetrahydrofolate. Provides the major source of formate for the purT-dependent synthesis of 5'-phosphoribosyl-n-formylglycinamide (fgaR) during aerobic growth. Has a role in regulating the one-carbon pool. ","formyltetrahydrofolate deformylase","Cytoplasm","","
InterPro
IPR002376
Domain
Formyl transferase, N-terminal
G3DSA:3.40.50.170\"[94-273]Tno description
PF00551\"[94-256]TFormyl_trans_N
InterPro
IPR002912
Domain
Amino acid-binding ACT
PF01842\"[16-77]TACT
InterPro
IPR004810
Family
Formyltetrahydrofolate deformylase
PR01575\"[18-44]T\"[50-62]T\"[95-117]T\"[117-144]TFFH4HYDRLASE
PIRSF036480\"[12-274]TFormyltetrahydrofolate deformylase
TIGR00655\"[16-274]TPurU: formyltetrahydrofolate deformylase
noIPR
unintegrated
unintegrated
PTHR10520\"[172-273]TPHOSPHORIBOSYLAMINE-GLYCINE LIGASE-RELATED
PTHR10520:SF7\"[172-273]TFORMYLTETRAHYDROFOLATE DEFORMYLASE
signalp\"[1-20]?signal-peptide


","BeTs to 13 clades of COG0788COG name: Formyltetrahydrofolate hydrolaseFunctional Class: FThe phylogenetic pattern of COG0788 is -o-----q-dr-bcefghs-uj----Number of proteins in this genome belonging to this COG is","","Residues 18 to 113 match (2e-07) PD:PD407153 which is described as FORMYLTETRAHYDROFOLATE DEFORMYLASE COMPLETE PROTEOME HYDROLASE PROBABLE BIOSYNTHESIS PURINE FORMYL-FH4 ONE-CARBON ","","","","","","","","","","","Wed Jan 22 16:18:45 2003","Wed Jan 22 16:18:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02291 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 94 to 256 (E-value = 5.4e-51) place AA02291 in the Formyl_trans_N family which is described as Formyl transferase (PF00551)","","","","","Nagy,P.L., McCorkle,G.M. and Zalkin,H. purU, a source of formate for purT-dependent phosphoribosyl-N-formylglycinamide synthesis. J. Bacteriol. 175 (21): 7066-7073 (1993) [PubMed: 8226647].Bosl,M. and Kersten,H. Organization and functions of genes in the upstream region of tyrT of Escherichia coli: phenotypes of mutants with partial deletion of a new gene (tgs). J. Bacteriol. 176 (1): 221-231 (1994) [PubMed: 8282700].Nagy,P.L., Marolewski,A., Benkovic,S.J. and Zalkin,H. Formyltetrahydrofolate hydrolase, a regulatory enzyme that functions to balance pools of tetrahydrofolate and one-carbontetrahydrofolate adducts in Escherichia coli. J. Bacteriol. 177 (5): 1292-1298 (1995) [PubMed: 7868604].","","Thu Jan 16 18:13:26 2003","1","","","" "AA02292","1563457","1563062","396","ATGTCCGATGTATTAAAAATATTAACGAATATTCGTAGCTTGCGTATGGTCGCGCGTGATTTAGCATTAGAACAGCTTGAAAGTATTTTGGAAAAATTGCAATTAGTCGTTACGGAAAAGAAAGAAGAGATTTTAAAGGCTCAGCAAGAAGAAAACGAGCGACAAGAACGTATTGCCAAATATAAAGAATTATTAAAGCAAGAAGGTATCACTGCAGACGAATTAGCAGAGATTTTAGGTTCTGATGCGGTTCGTAAGAAAAGAGATACTCGTCCTGCAAAATATCAATATGTTGATGAAAAGGGCGTAACGAAAACTTGGACAGGTCAAGGCAGAACACCGAAAGCAATCCAAGCACAATTAGATAAAGGTAAGTCTTTATCTTCTTTTAAAATT","","","16584","MSDVLKILTNIRSLRMVARDLALEQLESILEKLQLVVTEKKEEILKAQQEENERQERIAKYKELLKQEGITADELAEILGSDAVRKKRDTRPAKYQYVDEKGVTKTWTGQGRTPKAIQAQLDKGKSLSSFKI","1563062","[FUNCTION] H-NS binds tightly to ds-DNA, increases its thermal stability and inhibits transcription. It also binds to ss-DNA and RNA but with a much lower affinity. H-NS has possible histone-like function. May be a global transcriptional regulator through its ability to bind to curved dna sequences, which are found in regions upstream of a certain subset of promoters. It plays a role in the thermal control of pili production. It is subject to transcriptional auto-repression. It binds preferentially to the upstream region of its own gene recognizing two segments of DNA on both sides of a bend centered around -150. ","DNA-binding protein H-NS","Cytoplasm","","
InterPro
IPR001801
Family
Histone-like nucleoid-structuring protein H-NS
PD007337\"[37-132]TQ9CMF7_PASMU_Q9CMF7;
PF00816\"[21-127]THistone_HNS
SM00528\"[85-132]THNS
noIPR
unintegrated
unintegrated
G3DSA:4.10.430.10\"[89-132]Tno description


","BeTs to 3 clades of COG2916COG name: DNA-binding protein H-NSFunctional Class: RThe phylogenetic pattern of COG2916 is --------------e-ghs-------Number of proteins in this genome belonging to this COG is","Significant hit ( 7.7e-37) to 3/3 blocks of the IPB001801 family, which is described as \"H-NS histone family\". Interpro entry for IP:IPR001801. IPB001801A 2-44 6.9e-15 IPB001801B 87-119 2.2e-17 IPB001801C 122-132 0.13","Residues 1 to 130 match (3e-28) PD:PD007337 which is described as DNA-BINDING H-NS PROTEOME COMPLETE REGULATION TRANSCRIPTION REPRESSOR HISTONE-LIKE STPA HLP-II ","","","","","","","","","","","Thu Jan 16 18:19:53 2003","Thu Jan 16 18:19:53 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02292 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 21 to 127 (E-value = 6.5e-36) place AA02292 in the Histone_HNS family which is described as H-NS histone family (PF00816)","","","","","Pon,C.L., Calogero,R.A. and Gualerzi,C.O. Identification, cloning, nucleotide sequence and chromosomal map location of hns, the structural gene for Escherichia coliDNA-binding protein H-NS. Mol. Gen. Genet. 212 (2): 199-202 (1988) [PubMed: 2841565].Goransson,M., Sonden,B., Nilsson,P., Dagberg,B., Forsman,K., Emanuelsson,K. and Uhlin,B.E. Transcriptional silencing and thermoregulation of gene expression in Escherichia coli. Nature 344 (6267): 682-685 (1990) [PubMed: 1691451].Falconi,M., Gualtieri,M.T., La Teana,A., Losso,M.A. and Pon,C.L.Proteins from the prokaryotic nucleoid: primary and quaternary structure of the 15-kD Escherichia coli DNA binding protein H-NS. Mol. Microbiol. 2 (3): 323-329 (1988) [PubMed: 3135462].Ueguchi,C. and Ito,K. Multicopy suppression: an approach to understanding intracellular functioning of the protein export system. J. Bacteriol. 174 (5): 1454-1461 (1992) [PubMed: 1537791].May,G., Dersch,P., Haardt,M., Middendorf,A. and Bremer,E. The osmZ (bglY) gene encodes the DNA-binding protein H-NS (H1a), a component of the Escherichia coli K12 nucleoid. Mol. Gen. Genet. 224 (1): 81-90 (1990) [PubMed: 2177526].Yamada,H., Muramatsu,S. and Mizuno,T. An Escherichia coli protein that preferentially binds to sharply curved DNA. J. Biochem. 108 (3): 420-425 (1990) [PubMed: 2126011]. ","","Thu Jan 16 18:19:53 2003","1","","","" "AA02293","1563671","1563769","99","GTGGATAACGGTGAAGAAAATGGAAAGGAACGTTTGCCGAAATCAGTTAAAAGTCATTTTAATTGGTTGGTGACGTCTTCGAAAGAACCGTCACTGTCA","","","3682","VDNGEENGKERLPKSVKSHFNWLVTSSKEPSLS","1563769","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 14:52:45 2004","Wed Feb 25 14:52:45 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02293 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 14:52:45 2004","","","","","","","","","","","","","1","","","" "AA02294","1563898","1565427","1530","ATGGAACTCATTGATTATTCGTCATCAGTCTGGTCGGTATTACCACCGTTATTTGCGTTGTTACTCGCCATCATTACCCGCCGCGTATTGCTCTCTTTGAGCGTAGGTATTTTTGTCGGTGCTATTATGCTGACAGATGTGAATCTAACAAGTACCTTAGTTTATTTAAAAAATAACGTATCCTCCCTCTTCGTCAAGGAAGATGGTTTAAATACCAACAATATCAACATTATTCTTTTCTTATTATTACTCGGAATTTTGACCGCCCTTTTAAGTATGTCCGGCAGTAACCGCGCCTTTGCAGAATGGTCACAAAAACAGATTAAAGATCGCCGTGGGGCAAAATTGGTTGCCGCTTCGTTAGTCTTCGTCACCTTCATCGATGACTATTTCCACAGTTTAGCCGTAGGTGCTATTACCCGCCCGATTACCGATAAATTCAAAGTCTCCCGCGCCAAATTAGCTTATATTCTTGACTCTACCGCTGCACCGATGTGCGTACTCATGCCGGTATCTAGTTGGGGCGCATATATCATTACCTTAGTCGCTGGCTTATTAGCCACTTATTCCATCACAGGCTACTCACCAATCGGTGCATTTATGGCAATGAGTGCTATGAACTATTACGCTATTTTCTCTATTTTAATGGTGTTCTTCGTAGCCTATTTCAGCTTTGACATCGGTCCCATGGCAAGACATGAAAGGCTGGCATTGGAAACAGAAAATACGCAAGGAGAAGCGCTTTCAGGCATAAACGGTCATGTACGCAATTTAGTATTACCAATTATCACCCTTATTATCATAACAATTTCTGCCATGCTATACACTGGTAACCTAGCCTTAACAGCTAGCGGAAAGCCGTTCAGTATACTTGGTGCCTTTGAAAATACCACCGTAGGTGTATCTTTAGTCACCGGTGGTGTAAGTGCGGTGATTATTGCGTCCATTTGTATTTTATCCGATCGTCTGGTAAGCCTGCATGAATATGTCAAAGCCTGGGTACTGGGCGTGAAATCCATGCTTGGCGCCATTTTAATTCTGTTTTTTGCCTGGACAATCAATAACGTGGTCAGCGATATAAAAACCGGCACTTATTTAGCCTCCTTGGTATCCTACGCCTTACCGCTTGCGTTCTTACCGGCACTGCTCTTTATTTTAGCCGCCATTATGGCATTTTCCACCGGCACCAGTTGGGGAACCTTCGGAATTATGCTGCCCATCGCCGCGGCCATCGCTTCCCACGCGATGCATGGTTCCGTGGAATTTATGTTACCATGCTTATCGGCGGTCATGGCAGGCGCCGTATGTGGTGACCACTGTTCACCAGTGTCGGACACTACTATTCTGTCTTCCACCGGTGCAAAATGCGACCACATGGATCATGTCACTTCCCAATTGCCTTATGCTATCACCATCGCCACCGCGAGCATTGCAGGCTATATTGTAGTTGGTTTCACTTATTCCGGTTTACTTGGATTCATCACCACGGGTATTGTCCTCGCCTTGTTGGTGCTTATCTTTAAGAAACGT","","","54482","MELIDYSSSVWSVLPPLFALLLAIITRRVLLSLSVGIFVGAIMLTDVNLTSTLVYLKNNVSSLFVKEDGLNTNNINIILFLLLLGILTALLSMSGSNRAFAEWSQKQIKDRRGAKLVAASLVFVTFIDDYFHSLAVGAITRPITDKFKVSRAKLAYILDSTAAPMCVLMPVSSWGAYIITLVAGLLATYSITGYSPIGAFMAMSAMNYYAIFSILMVFFVAYFSFDIGPMARHERLALETENTQGEALSGINGHVRNLVLPIITLIIITISAMLYTGNLALTASGKPFSILGAFENTTVGVSLVTGGVSAVIIASICILSDRLVSLHEYVKAWVLGVKSMLGAILILFFAWTINNVVSDIKTGTYLASLVSYALPLAFLPALLFILAAIMAFSTGTSWGTFGIMLPIAAAIASHAMHGSVEFMLPCLSAVMAGAVCGDHCSPVSDTTILSSTGAKCDHMDHVTSQLPYAITIATASIAGYIVVGFTYSGLLGFITTGIVLALLVLIFKKR","1565427","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR004770
Family
Na+/H+ antiporter NhaC
PF03553\"[165-485]TNa_H_antiporter
noIPR
unintegrated
unintegrated
signalp\"[1-32]?signal-peptide
tmhmm\"[4-24]?\"[29-49]?\"[75-95]?\"[116-136]?\"[155-175]?\"[177-199]?\"[205-225]?\"[259-279]?\"[298-318]?\"[333-353]?\"[372-392]?\"[394-416]?\"[422-442]?\"[463-483]?\"[487-507]?transmembrane_regions


","BeTs to 11 clades of COG1757COG name: Na+/H+ antiporterFunctional Class: CThe phylogenetic pattern of COG1757 is -o--kz------b---gh-nu---t-Number of proteins in this genome belonging to this COG is","","Residues 163 to 369 match (4e-07) PD:PD490046 which is described as PROTEOME COMPLETE INTEGRAL MEMBRANE ","","","","","","","","","","","","Tue Jan 21 08:45:33 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02294 is paralogously related to AA01459 (6e-09).","","","","","","Residues 165 to 485 (E-value = 6.6e-97) place AA02294 in the Na_H_antiporter family which is described as Na+/H+ antiporter family (PF03553)","","","","","","","","1","","","" "AA02296","1566210","1566641","432","ATGCTTTCAGCACTTATCTCTCCCGCACTTAGCTACCCGGCTATGCGTCTGGCGACACAACCGGAACACCAGCGGTGCGTCCACTCCGGTCCTCTCGTACTAGGAGCAGCCCCAACCAATTCTCCTACGCCCACGGCAGATAGGGACCGAACTGTCTCACGACGTTCTAAACCCAGCTCGCGTACCACTTTAAATGGCGAACAGCCATACCCTTGGGACCTACTTCAGCCCCAGGATGTGATGAGCCGACATCGAGGTGCCAAACACCGCCGTCGATATGAACTCTTGGGCGGTATCAGCCTGTTATCCCCGGAGTACCTTTTATCCGTTGAGCGATGGCCCTTCCATGCAGAACCACCGGATCACTATGACCTACTTTCGTACCTGCCCGACCTGTCCGTCTCGCAGTTAAGCTTGCTTATACCATTGCAC","","","16179","MLSALISPALSYPAMRLATQPEHQRCVHSGPLVLGAAPTNSPTPTADRDRTVSRRSKPSSRTTLNGEQPYPWDLLQPQDVMSRHRGAKHRRRYELLGGISLLSPEYLLSVERWPFHAEPPDHYDLLSYLPDLSVSQLSLLIPLH","1566641","","conserved hypothetical protein (possible cell wall-associated hydrolase)","Periplasm","","
noIPR
unintegrated
unintegrated
PD293281\"[1-104]TQ8CME1_BBBBB_Q8CME1;


","No hits to the COGs database.","","Residues 1 to 122 match (1e-33) PD:PD293281 which is described as PROTEOME COMPLETE TC0114 ","","","","","","","","","","","","Fri Dec 5 15:44:47 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02296 is paralogously related to AA01262 (8e-83), AA00620 (8e-83), AA00411 (1e-61) and AA01567 (3e-33).","","","","","","","","","","","","","","1","","","" "AA02297","1569960","1569760","201","ATGGCGTATACAGAGGGTAACCAACCAGCGATGGGGAGTGAATCTCAGAAAGTGCGTCTAAGTTCGGATTGGAGTCTGCAACTCGACTCCATGAAGTCGGAATCGCTAGTAATCGCGAATCAGAATGTTGCGGTGAATACGTTCCCGGGCCTTGTACACACCGCCCGTCACACCATGGGAGTGGGTTGTACCAGAAGTGGA","","","7166","MAYTEGNQPAMGSESQKVRLSSDWSLQLDSMKSESLVIANQNVAVNTFPGLVHTARHTMGVGCTRSG","1569760","","conserved hypothetical protein","Periplasm","This sequence is similar to gi|27359373, a predicted conserved hypothetical protein from Vibrio vulnificus CMCP6.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 14:50:57 2004","Wed Feb 25 14:50:57 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02297 is paralogously related to AA01566 (7e-35), AA01261 (7e-35), AA00621 (7e-35), AA00412 (7e-35) and AA02421 (2e-27).","Wed Feb 25 14:50:57 2004","","","","","","","","","","","","","1","","","" "AA02298","1570728","1571060","333","ATGCTATTAACACACCAACCTTCCTCAATACCGAAAGAACTTTACAACCCGAAGGCCTTCTTCATTCACGCGGCATGGCTGCGTCAGGGTTGCCCCCATTGCGCAATATTCCCCACTGCTGCCTCCCGTAGGAGTCCGGGCCGTGTCTCAGTCCCGGTGTGGCTGGCCATCCTCTCAGACCAGCTAGCGATCGTCGGCTTGGTAGGCCCTTACCCCACCAACTACCTAATCACACTTGGGTTCATCTCATGGCATGCGGCCATAAAGTCCCGCACTTTCGTCTCCCGACCCTACGCGGTATTAGCGACAGTTTCCCGTCGTTATCCCCCTCCA","","","12310","MLLTHQPSSIPKELYNPKAFFIHAAWLRQGCPHCAIFPTAASRRSPGRVSVPVWLAILSDQLAIVGLVGPYPTNYLITLGFISWHAAIKSRTFVSRPYAVLATVSRRYPPP","1571060","","conserved hypothetical protein","Inner membrane, Cytoplasm","This sequence is similar to gi|27360487, a predicted conserved hypothetical protein from Vibrio vulnificus CMCP6.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 14:47:18 2004","Wed Feb 25 14:47:18 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02298 is paralogously related to AA02422 (1e-63), AA00622 (1e-63), AA00413 (9e-63), AA01565 (2e-30) and AA01260 (4e-13).","Wed Feb 25 14:47:18 2004","","","","","","","","","","","","","1","","","" "AA02300","1572312","1571488","825","ATGGACATTCAAACAAAACCCACAATTCTTTTTTTTGATTCCGGCGTCGGCGGCTTTAGTGTTTATCATGAGGTTAAGCAACTTTTGCCTGACTATCACTATTTGTATTGCTTTGATAACGCTTACTTTCCTTATTCCGAGAAGCCTGAAGAAAAGATCATCGAACGTACGTTAAAAATCTGCCAACGCATAGATCAAATGTATCCGTTGGATCTTATTGTCATCGCCTGTAATACGGCAAGCACCGTTGTGTTGCCCTCATTGCGCGAACATTTTTCAATTCCGATTGTAGGCACCGTGCCCGCGATTAAACCGGCAGCAGCGCAAACAACCACGAAACATATCGGGTTACTAGCCACCAAGGGAACGGTAAACCGAAAATATTTATCTGATTTGATTGATAAATATGCCGCTGATTGCCGTGTGGAAAAAATTGGCAGTACGAAGTTGGTAGAATTGGCTGAACGTAAATTTCATGGTTATCCTATTGATTTAAATGAAATTAAATCTGAAGTGCTAACGTGGGTTACAATGAGTGATTTAGATTGTGTGGTGCTGGGATGTACGCACTTCCCTCTGATAAAATCAGAGATTCAACAATGTTTGCCGCAAGTCATCTATTTTATTGATTCGGGTGCTGCCGTTGCGAAACGGGTGGAATCCTTGCTTAGTGACGTAAAAGTGCGGTCAAAAAATCAAACAAATAATCAAGTGTTTTGCACAAAAATGATCTCACCGGAAGACGGTTTACCAAATTTAATTCAGTCTTTAGGATTTGAAACGCTGCGTTTATTAGATGTCGATAGTGAGGTTTTGAGAGAAATT","","","30952","MDIQTKPTILFFDSGVGGFSVYHEVKQLLPDYHYLYCFDNAYFPYSEKPEEKIIERTLKICQRIDQMYPLDLIVIACNTASTVVLPSLREHFSIPIVGTVPAIKPAAAQTTTKHIGLLATKGTVNRKYLSDLIDKYAADCRVEKIGSTKLVELAERKFHGYPIDLNEIKSEVLTWVTMSDLDCVVLGCTHFPLIKSEIQQCLPQVIYFIDSGAAVAKRVESLLSDVKVRSKNQTNNQVFCTKMISPEDGLPNLIQSLGFETLRLLDVDSEVLREI","1571488","[FUNCTION] Provides the (R)-glutamic acid required for cell wall biosynthesis (by similarity).[PATHWAY] Peptidoglycan biosynthesis.","glutamate racemase","Cytoplasm","","
InterPro
IPR001920
Family
Asp/Glu racemase
PF01177\"[8-224]TAsp_Glu_race
PS00923\"[74-82]TASP_GLU_RACEMASE_1
PS00924\"[184-194]TASP_GLU_RACEMASE_2
InterPro
IPR004391
Family
Glutamate racemase
TIGR00067\"[7-257]Tglut_race: glutamate racemase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1860\"[7-152]Tno description
PTHR21198\"[3-275]TGLUTAMATE RACEMASE


","BeTs to 13 clades of COG0796COG name: Glutamate racemaseFunctional Class: MThe phylogenetic pattern of COG0796 is -------q-drlbcefgh-nuj--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-44) to 4/4 blocks of the IPB001920 family, which is described as \"Aspartate and glutamate racemases\". Interpro entry for IP:IPR001920. IPB001920A 9-40 3e-14 IPB001920B 70-100 2.3e-13 IPB001920C 115-126 0.012 IPB001920D 182-198 9.4e-10","Residues 9 to 217 match (1e-17) PD:PD002869 which is described as ISOMERASE ","","","","","","","","","","","Tue Jan 21 08:49:41 2003","Tue Jan 21 08:49:41 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02300 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 224 (E-value = 5e-84) place AA02300 in the Asp_Glu_race family which is described as Asp/Glu/Hydantoin racemase (PF01177)","","","","","de Dios A, Prieto L, Martin JA, Rubio A, Ezquerra J, Tebbe M, Lopez de Uralde B, Martin J, Sanchez A, LeTourneau DL, McGee JE, Boylan C, Parr TR Jr, Smith MC. 4-Substituted D-glutamic acid analogues: the first potent inhibitors of glutamate racemase (MurI) enzyme with antibacterial activity. J Med Chem. 2002 Sep 26;45(20):4559-70. PMID: 12238935 Doublet,P., van Heijenoort,J., Bohin,J.P. and Mengin-Lecreulx,D. The murI gene of Escherichia coli is an essential gene that encodes a glutamate racemase activity. J. Bacteriol. 175(10): 2970-2979, 1993. PubMed: 8098327. Doublet,P., van Heijenoort,J. and Mengin-Lecreulx,D.Identification of the Escherichia coli murI gene, which is required for the biosynthesis of D-glutamic acid, a specific component of bacterial peptidoglycan. J. Bacteriol. 174(18): 5772-5779, 1992. PubMed: 1355768. Doublet,P., van Heijenoort,J., Bohin,J.P. and Mengin-Lecreulx,D. The murI gene of Escherichia coli is an essential gene that encodes a glutamate racemase activity. J. Bacteriol. 175 (10): 2970-2979 (1993) [PubMed: 8098327].","","Tue Jan 21 08:52:53 2003","1","","","" "AA02301","1572855","1572346","510","GTGAGATTTATAGCAATGCCTGATTCTATTTTTGCCCAGCTGCATTGGTTGGCGGAAGATGCGCCACAGGCGAAGCAACTGCCGCGTTCAGTTCACTGCTGGTTGTTTGATAAACAATCGCTGACCGTTAAATTAAAACAGACTTGTGCACGATTTGACGTGAAAGTGTGGTCAGAAAAATGGATAGAAAAAACATTTGAAAATGAGACTGCACTTTTGCCGGCGGGAGCCTATTGGTGCCGTGAAGTTTTATTGCTTGGTGACGGCAAACCTTGGATCGAGGCTCGAACGCTCATTCCCCAGACGCTATTTGTCTATCACCAAGAACTGTCAATGTTAGGCAAAAAACCTATCGGCGAATGGCTATTTCAGCAAACGCCACAAAGGCGGTTAATCCAATGGGCGCAAGATCCTCAAAGCGGATTATATGCCCGTCGTTCCTTGTTTTGGGTCCAAAACATACCGATGTTAATCAGCGAGCTTTTCCTTGAGAACCGCCTTATAAGCGAA","","","20012","VRFIAMPDSIFAQLHWLAEDAPQAKQLPRSVHCWLFDKQSLTVKLKQTCARFDVKVWSEKWIEKTFENETALLPAGAYWCREVLLLGDGKPWIEARTLIPQTLFVYHQELSMLGKKPIGEWLFQQTPQRRLIQWAQDPQSGLYARRSLFWVQNIPMLISELFLENRLISE","1572346","[PATHWAY] Ubiquinone biosynthesis; first step.","chorismate lyase","Cytoplasm","","
InterPro
IPR007440
Family
Chorismate lyase
PF04345\"[27-163]TChor_lyase
noIPR
unintegrated
unintegrated
G3DSA:3.40.1410.10\"[8-169]Tno description


","BeTs to 4 clades of COG3161COG name: 4-Hydroxybenzoate synthetase (chorismate lyase)Functional Class: HThe phylogenetic pattern of COG3161 is a-m-------r---efgh-n------Number of proteins in this genome belonging to this COG is","","Residues 69 to 114 match (9e-13) PD:PD006894 which is described as TRANSCRIPTION REGULATION DNA-BINDING ATP-BINDING COMPLETE PROTEOME REGULATOR SENSORY TRANSDUCTION PHOSPHORYLATION ","","","","","","","","","","","Tue Jan 21 08:58:58 2003","Tue Jan 21 08:58:58 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02301 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 10 to 168 (E-value = 4.6e-30) place AA02301 in the Chor_lyase family which is described as Chorismate lyase (PF04345)","","","","","Nichols,B.P. and Green,J.M. Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase. J. Bacteriol. 174 (16): 5309-5316 (1992) [PubMed: 1644758].Siebert,M., Bechthold,A., Melzer,M., May,U., Berger,U., Schroder,G., Schroder,J., Severin,K. and Heide,L. Ubiquinone biosynthesis. Cloning of the genes coding for chorismate pyruvate-lyase and 4-hydroxybenzoate octaprenyl transferase from Escherichia coli. FEBS Lett. 307 (3): 347-350 (1992) [PubMed: 1644192].Nishimura,K., Nakahigashi,K. and Inokuchi,H. Location of the ubiA gene on the physical map of Escherichia coli . J. Bacteriol. 174 (17): 5762 (1992) [PubMed: 1512213].Wu,G., Williams,H.D., Gibson,F. and Poole,R.K. Mutants of Escherichia coli affected in respiration: the cloning and nucleotide sequence of ubiA, encoding the membrane-boundp-hydroxybenzoate:octaprenyltransferase. J. Gen. Microbiol. 139 (Pt 8): 1795-1805 (1993) [PubMed: 8409922]. ","","Tue Jan 21 08:58:58 2003","1","","","" "AA02303","1574914","1572836","2079","ATGAGCACCCAATTATTAGATGCGATTCCGTTAACGGCAATTTCCGGTGTTGGTGCCGCTGTGGCGGAAAAGTTAGGTAAATTGGGGATCTTCAATCTGCAAGATCTGTTATTTCACCTTCCCCTCCGTTATGAAGATCGCACCCGCATCACACCCATTGCCGATTTGCAGGCAGAGCAGTACGCCACTATTGAAGGCGTCGTGCAAAGTAGCGAAGTGCAATTCGGGCGTCGTCCGATGTTGATGGTCTATCTTTCCGACAGTACCGCCAAATTGGCGTTGCGCTTTTTTAATTTTAACGCCGGTATGAAAAACAGCTTGCAGCCAGGTGCTCGGGTGAAAGCCTTTGGTGAGGTGCGTCGCGGGCGTTTCATGGCGGAAATTCATCATCCTGAATATCAGATTATTCATGACAATAAACCGCTGGTTCTGGCAGAAACCCTCACGCCCATTTACCCTGCTACGGAAGGGTTGAAACAAACCGCTTTGCGAAAATTAATTGCGCAAGCCTTGTTGGTGTTGGATAAAACGCCCATAGCCGAATTGTTACCGGCGGAATGTAATCCGCATCCTTTTGATTTAAAATTCGCCATTCAGTTCTTACATAACCCGCCACCCGATGTGTCATTAACGACCTTGGAAGAAGGTAGACATCCCGCCCAGCAACGACTGATTTTTGAAGAGTTGCTGGCATATAACCTGGCGATGCAAAAAGTGCGGTCAGGAATTCAAGCGAATTTTGCCGAGCCTTTGTCGTATCAATCAGATTTAAAAGCACGTTTTTTAGCGCAGTTGCCGTTTCAGCCGACAAATGCACAGTTGCGTGTGACGGAAGATATTGAACGGGATGTGGCGCAACCTTACCCGATGATGCGTCTGGTGCAGGGGGATGTCGGCTCCGGTAAAACCTTAGTGGCGGCGTTAGCGGCACTGCTCGCCATTGATAACGGTAAACAGGTGGCATTGATGGCGCCGACGGAAATCTTAGCGGAACAGCACGCCGTGAACTTCCGCCGTTGGTTTGAACCGCTTGGCATTCAAGTGGGCTGGCTGGCAGGAAAAGTCAAAGGCAAACAACGGGTTGCCGAGCTAGAGAAAATAAAAAGCGGTGCGGTACAAATGGTGGTGGGAACGCACGCGTTATTCCAGGAAGAGGTGGAATTTCATCGTTTGAGCTTGGTGATTGTTGACGAACAGCACCGTTTCGGCGTGCACCAACGACTCATGCTGCGGGAAAAAGGTAATCAGGCAGGCGTGTATCCTCATCAGTTAATCATGACCGCCACACCGATTCCACGTACGCTTGCCATGACGGTGTATGCGGATTTGGATACTTCGATTATCGACGAATTGCCACCGGGGCGCACGCCGATTACCACCATTGCAATTTCCGAAGATCGTCGTGCAGAGATTATCGAACGGGTGAATGTGGCGTGTACGCAGGAAAAACGGCAGGCTTATTGGGTTTGCACTCTGATTGATGAATCGGAAATGTTGGAGGCGCAGGCGGCGGAAGCGGTGGCGGAAGATCTCCGTAAAATTCTACCGCACTTACGCATCGGCTTGGTACACGGGCGAATGAAACCGAATGAAAAACAAGCGGTAATGGCGCAGTTTAAGCTTGCCGAATTAGATTTACTGGTCGCTACGACCGTGATTGAAGTGGGCGTGGATGTGCCGAATGCCAGTTTGATGATTATTGAAAACGCTGAGCGCCTTGGCTTGTCCCAGCTTCACCAGTTACGTGGGCGGGTCGGGCGTGGCAGTACAGCTTCGTTTTGTGTGTTAATGTACAAACCGCCGCTCGGTAAAATTTCGCAAAAACGCTTACAAGTCATGCGCGACACGCAGGATGGTTTCGTGATTTCGGAAAAAGATCTGGAAATTCGTGGTCCGGGGGAAGTGCTTGGCACGAAACAAACAGGAATTACCGAATTTAAAGTGGCGAACCTCATGCGCGATCGCAAAATGCTGCCGACAGTGCAGTTTTATGCAAAACAACTAGTACAGAAATATCCGCAAACGGCGGACTTGTTGATTCGCCGCTGGCTAAATAATCGTGAGATTTATAGCAATGCC","","","77592","MSTQLLDAIPLTAISGVGAAVAEKLGKLGIFNLQDLLFHLPLRYEDRTRITPIADLQAEQYATIEGVVQSSEVQFGRRPMLMVYLSDSTAKLALRFFNFNAGMKNSLQPGARVKAFGEVRRGRFMAEIHHPEYQIIHDNKPLVLAETLTPIYPATEGLKQTALRKLIAQALLVLDKTPIAELLPAECNPHPFDLKFAIQFLHNPPPDVSLTTLEEGRHPAQQRLIFEELLAYNLAMQKVRSGIQANFAEPLSYQSDLKARFLAQLPFQPTNAQLRVTEDIERDVAQPYPMMRLVQGDVGSGKTLVAALAALLAIDNGKQVALMAPTEILAEQHAVNFRRWFEPLGIQVGWLAGKVKGKQRVAELEKIKSGAVQMVVGTHALFQEEVEFHRLSLVIVDEQHRFGVHQRLMLREKGNQAGVYPHQLIMTATPIPRTLAMTVYADLDTSIIDELPPGRTPITTIAISEDRRAEIIERVNVACTQEKRQAYWVCTLIDESEMLEAQAAEAVAEDLRKILPHLRIGLVHGRMKPNEKQAVMAQFKLAELDLLVATTVIEVGVDVPNASLMIIENAERLGLSQLHQLRGRVGRGSTASFCVLMYKPPLGKISQKRLQVMRDTQDGFVISEKDLEIRGPGEVLGTKQTGITEFKVANLMRDRKMLPTVQFYAKQLVQKYPQTADLLIRRWLNNREIYSNA","1572836","[FUNCTION] Critical role in recombination and DNA repair. Help process holliday junction intermediates to mature products bycatalysing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3' to 5' polarity.recG unwind branched duplex DNA (y-DNA) (by similarity). ","ATP-dependent DNA helicase","Cytoplasm","","
InterPro
IPR001650
Domain
Helicase, C-terminal
PF00271\"[512-589]THelicase_C
SM00490\"[505-589]THELICc
PS51194\"[482-628]THELICASE_CTER
InterPro
IPR004365
Domain
Nucleic acid binding, OB-fold, tRNA/helicase-type
PF01336\"[62-136]TtRNA_anti
InterPro
IPR004609
Family
ATP-dependent DNA helicase RecG
TIGR00643\"[28-665]TrecG: ATP-dependent DNA helicase RecG
InterPro
IPR011545
Domain
DEAD/DEAH box helicase, N-terminal
PF00270\"[270-438]TDEAD
InterPro
IPR014001
Domain
DEAD-like helicases, N-terminal
SM00487\"[265-459]TDEXDc
InterPro
IPR014021
Domain
Helicase superfamily 1 and 2 ATP-binding
PS51192\"[283-448]THELICASE_ATP_BIND_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[285-402]T\"[469-629]Tno description
PTHR10967\"[293-628]TDEAD BOX ATP-DEPENDENT RNA HELICASE
signalp\"[1-22]?signal-peptide


","BeTs to 15 clades of COG1200COG name: RecG-like helicasesFunctional Class: L,KThe phylogenetic pattern of COG1200 is -------qvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","","Residues 17 to 171 match (1e-08) PD:PD119598 which is described as DNA HELICASE ATP-BINDING RECG ATP-DEPENDENT PROTEOME COMPLETE RECOMBINATION DNA-BINDING 3.6.1.- ","","","","","","","","","","","Tue Dec 2 11:23:05 2003","Tue Jan 21 09:03:36 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02303 is paralogously related to AA00861 (4e-69), AA00148 (3e-06), AA01335 (4e-06) and AA02480 (3e-05).","","","","","","Residues 512 to 589 (E-value = 1e-20) place AA02303 in the Helicase_C family which is described as Helicase conserved C-terminal domain (PF00271)","","","","","Lloyd, R.G. and Sharples, G.J. 1991. Molecular organization and nucleotide sequence of the recG locus of Escherichia coli K-12. J. Bacteriol. 173(21): 6837-6843. PubMed: 1938888. Kalman, M., Murphy, H. and Cashel, M. 1992. The nucleotide sequence of recG, the distal spo operon gene in Escherichia coli K-12. Gene 110(1): 95-99. PubMed: 1544582. Whitby,M.C., Vincent,S.D. and Lloyd,R.G. 1994. Branch migration of Holliday junctions: identification of RecG protein as a junction specific DNA helicase. EMBO J. 13(21): 5220-5228. PubMed: 7957087.","","Tue Jan 21 09:03:36 2003","1","","","" "AA02305","1577038","1574918","2121","TTGTATTTATTCGAAGGTTTACATCACATTATTCAGGCATATTTGCCGCCTGAACAAATTGAATTAGTCAAACGTGCATTTGTGATTGCCCGCGATGCACACGAAGGACAATCACGCTCCAGCGGCGAACCTTACATCACCCATCCGGTTGCCGTCGCTTCGATCATCGCCGAAATGCGACTGGATCACGAAGCGGTCATGGCCGCCTTATTACATGATGTCATTGAAGACACGCCTTACACGGAAGAACAACTGAAAGCCGAATTCGGCGCCAGTGTCGCGGAAATCGTAGAAGGCGTTTCAAAACTCGACAAACTCAAATTCAGAACCCGTCAAGAAGCGGAAGTGGCAAATTTCCGTAAAATGATCCTTGCCATGACCAGGGATATTCGTGTGGTTCTCATCAAACTTGCCGACCGAACCCACAACATGCGCACCCTCAGCGCATTACGTCCCGATAAACGCCGTCGTATCGCCAAAGAAACCCTGGAAATTTATGCACCGTTGGCGCATCGCTTGGGGATCGAGCACATCAAAAACGAACTGGAAGATCTTGGTTTTGAAGCCATGTATCCGCAACGTTATGCGGTTTTGCAAAAAGTCGTACAGATTGCGCGCGGTAATCGCAAAGACATGATTGAACGAATTTCCGACGAAATCAAAGGGCGTTTGCAGGATGTGGGTATTCAAGCGCGGGTATTCGGGCGTGAAAAGCATTTGTATGCCATCTACCAAAAAATGCACTTAAAAGATCAGCAGTTTCATTCCATTATGGATATTTACGCGTTCCGCACCGTGGTGAACAACGTGGATACCTGCTATCGTGTGCTTGGACAAATGCACAGCCTTTATAAACCGCGCCCGGGTCGGGTAAAAGATTATATTGCCGTGCCGAAAGCCAATGGCTATCAGTCCTTACATACGTCGATGATTGGTCCGCACGGCGTGCCGGTGGAAGTGCAAATTCGTACCGAAGAAATGGATCAAATGGCGGAAATGGGGGTCGCGGCGCATTGGGCGTATAAACAGGGCGGTCGTAACGACAGCACGCCGGCACAAATTAAAGCGCAACGTTGGCTACAAAGTTTAATTGAATTACAACAAAGTGCGGGTAATTCTTTTGAATTTATCGAAAGCGTAAAATCGGAATTTTTCCCGAAAGAAATTTATGTGTTTACACCGAAAGGGCGCATTGTAGAGCTACCGAAAGGCGCAACGCCGGTGGATTTTGCCTATGCCGTGCACACAGATGTGGGCAGAAATTGTGTCGCCGCCAATGTGGATCGTAAACCTTATCCGTTATCGCAAGCCTTGGAATCCGGGCAGACCATTGATATTTTAACCTCGCCGAATGACAAACCTAATGTGGCTTGGCTTAATTTTGTGGTGACCGCCAAAGCTCGTTCCAGTATTCGTCACGCTTTAAAAGATTTGTGTCGTGATGAAGCCATTGAATCCGGTAAGCGCCAATTAGCGCACGCTTTGAGTCCGTTAAAATTAGAAGAACTCAATATTGAATATACCCAAAATGTCTTAGCGGATCTGAAATTAGCAAGTTTAAATGATTTATTTATGGAAATCGGTTTAGGCAACCAAATGAGCACCGTCATTGCGCATCGTTTGCTGGGCGAATCCATTGAAATTGATACGGACGGCAACCCTGACAACCACACCGGTCCGTTGGAAATCAGCGGTAACGGCGGTTTGTTGACTACCTTTGCGCAATGTTGCCATCCTGTACCGGGCGATCCGATTATCGCTTATGCCAGCCCGGGTAAAGGATTGGTGATCCACCATGAATCCTGCTCAAACTTGAAAGATCGCGAAGATAATACGAAAAATTATATGTCCGTTGATTGGGAAAAAAGCGATACGCAAATTGAATTTGAAGCGGAATTGCGTATCGAAATGATTAATCAGCAAGGCACGTTACCGCACTTGATGTCAACCATTTCCGCCATGGACAGCAACATTCAAAGCATTTGGACGGAAGAACAGGAAGGGCGTTTGTATCAAATCATCGTGCTGTTAACGGTCAAAGACAAAAAACACCTTGCCCACATCATTCGCAAAATCAAATCAATGCCTGAACTAATCAGCATTGAACGCAATATTAATCAA","","","79971","LYLFEGLHHIIQAYLPPEQIELVKRAFVIARDAHEGQSRSSGEPYITHPVAVASIIAEMRLDHEAVMAALLHDVIEDTPYTEEQLKAEFGASVAEIVEGVSKLDKLKFRTRQEAEVANFRKMILAMTRDIRVVLIKLADRTHNMRTLSALRPDKRRRIAKETLEIYAPLAHRLGIEHIKNELEDLGFEAMYPQRYAVLQKVVQIARGNRKDMIERISDEIKGRLQDVGIQARVFGREKHLYAIYQKMHLKDQQFHSIMDIYAFRTVVNNVDTCYRVLGQMHSLYKPRPGRVKDYIAVPKANGYQSLHTSMIGPHGVPVEVQIRTEEMDQMAEMGVAAHWAYKQGGRNDSTPAQIKAQRWLQSLIELQQSAGNSFEFIESVKSEFFPKEIYVFTPKGRIVELPKGATPVDFAYAVHTDVGRNCVAANVDRKPYPLSQALESGQTIDILTSPNDKPNVAWLNFVVTAKARSSIRHALKDLCRDEAIESGKRQLAHALSPLKLEELNIEYTQNVLADLKLASLNDLFMEIGLGNQMSTVIAHRLLGESIEIDTDGNPDNHTGPLEISGNGGLLTTFAQCCHPVPGDPIIAYASPGKGLVIHHESCSNLKDREDNTKNYMSVDWEKSDTQIEFEAELRIEMINQQGTLPHLMSTISAMDSNIQSIWTEEQEGRLYQIIVLLTVKDKKHLAHIIRKIKSMPELISIERNINQ","1574918","[FUNCTION] In eubacteria ppgpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the degradation of ppgpp into gdp. It may also be capable of catalyzing the synthesis of ppgpp. ","guanosine-3',5'-bis(diphosphate)3'- pyrophosphohydrolase","Cytoplasm","","
InterPro
IPR003607
Domain
Metal-dependent phosphohydrolase, HD region
SM00471\"[41-153]THDc
InterPro
IPR004095
Domain
TGS
PF02824\"[389-448]TTGS
InterPro
IPR004811
Family
RelA/SpoT protein
TIGR00691\"[26-703]TspoT_relA: RelA/SpoT family protein
InterPro
IPR006674
Domain
Metal-dependent phosphohydrolase, HD region, subdomain
PF01966\"[45-144]THD
InterPro
IPR007685
Domain
RelA/SpoT
PF04607\"[235-345]TRelA_SpoT
InterPro
IPR012675
Domain
Beta-grasp fold, ferredoxin-type
G3DSA:3.10.20.30\"[388-451]Tno description
InterPro
IPR013173
Domain
DNA primase DnaG, DnaB-binding
SM00766\"[17-123]Tno description
noIPR
unintegrated
unintegrated
PTHR21262\"[116-706]TGUANOSINE-3',5'-BIS(DIPHOSPHATE) 3'-PYROPHOSPHOHYDROLASE


","BeTs to 16 clades of COG0317COG name: Guanosine polyphosphate pyrophosphohydrolases/synthetasesFunctional Class: T,KThe phylogenetic pattern of COG0317 is -------qvdrlbcefghsnuj--twNumber of proteins in this genome belonging to this COG is","","Residues 164 to 233 match (2e-07) PD:PD543082 which is described as KINASE/PHOSPHOHYDROLASE KINASE HYDROLASE ","","","","","","","","","","","Tue Dec 2 11:26:51 2003","Tue Dec 2 11:26:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02305 is paralogously related to AA01072 (1e-103).","","","","","","Residues 385 to 448 (E-value = 6.1e-26) place AA02305 in the TGS family which is described as TGS domain (PF02824)","","","","","Sarubbi,E., Rudd,K.E., Xiao,H., Ikehara,K., Kalman,M.and Cashel,M. 1989. Characterization of the spoT gene of Escherichia coli. J. Biol. Chem. 264(25): 15074-15082. PubMed: 2549050. Xiao,H., Kalman,M., Ikehara,K., Zemel,S., Glaser,G. and Cashel,M. 1991. Residual guanosine 3\",5\"-bispyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations. J. Biol. Chem. 266(9): 5980-5990. PubMed: 2005134.","","Tue Dec 2 11:26:51 2003","1","","","" "AA02306","1577350","1577087","264","ATGGCTCGCGTAACCGTACAAGACGCAGTAGAAAAAATTGGTAACCGTTTCGATTTAATTTTAACCGCTGCCCGTCGCGCAAGACAATTACAGTTGCATACGCGTGAACCTTTGGTGCCGGAAGATAATGATAAACCGACCGTTATCGCACTGCGTGAAATTGAAAAAGGTTTAATTAATAACGAAATTTTGGATGCGCAAGATCGTCATGAACATTTGGTGCAGGAAAGAGTGGAAGTGAACGCCGTTTCTTTGTTATCCGAA","","","10042","MARVTVQDAVEKIGNRFDLILTAARRARQLQLHTREPLVPEDNDKPTVIALREIEKGLINNEILDAQDRHEHLVQERVEVNAVSLLSE","1577087","[FUNCTION] Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits (By similarity).","DNA-directed RNA polymerase, omega chain","Cytoplasm","","
InterPro
IPR003716
Family
RNA polymerase, omega subunit
TIGR00690\"[1-66]TrpoZ: DNA-directed RNA polymerase, omega su
InterPro
IPR006110
Family
RNA polymerase Rpb6
PF01192\"[12-65]TRNA_pol_Rpb6


","BeTs to 9 clades of COG1758COG name: DNA-directed RNA polymerase subunit K/omegaFunctional Class: KThe phylogenetic pattern of COG1758 is aompkzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 3.3e-51) to 3/3 blocks of the IPB003716 family, which is described as \"RNA polymerase omega subunit\". Interpro entry for IP:IPR003716. IPB003716A 1-31 3e-27 IPB003716B 37-60 1.2e-20 IPB003716C 68-88 1.4","Residues 1 to 64 match (7e-23) PD:PD027461 which is described as RNA POLYMERASE OMEGA DNA-DIRECTED CHAIN SUBUNIT PROTEOME TRANSCRIPTION COMPLETE TRANSFERASE ","","","","","","","","","","","Wed Feb 5 13:47:59 2003","Tue Jan 21 09:10:26 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02306 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 12 to 65 (E-value = 2.6e-19) place AA02306 in the RNA_pol_Rpb6 family which is described as RNA polymerase Rpb6 (PF01192)","","","","","Kojima I, Kasuga K, Kobayashi M, Fukasawa A, Mizuno S, Arisawa A, Akagawa H. The rpoZ Gene, Encoding the RNA Polymerase Omega Subunit, Is Required for Antibiotic Production and Morphological Differentiation in Streptomyces kasugaensis. J Bacteriol. 2002 Dec 1;184(23):6417-6423. PMID: 12426327 Kormanec J, Novakova R, Homerova D, Rezuchova B. Streptomyces aureofaciens sporulation-specific sigma factor sigma(rpoZ) directs expression of a gene encoding protein similar to hydrolases involved in degradation of the lignin-related biphenyl compounds. Res Microbiol. 2001 Dec;152(10):883-8. PMID: 11766963 Novakova R, Sevcikova B, Kormanec J. A method for the identification of promoters recognized by RNA polymerase containing a particular sigma factor: cloning of a developmentally regulated promoter and corresponding gene directed by the Streptomyces aureofaciens sigma factor RpoZ. Gene. 1998 Feb 16;208(1):43-50. PMID: 9479043 Gentry,D.R. and Burgess,R.R. The cloning and sequence of the gene encoding the omega subunit of Escherichia coli RNA polymerase Gene 48 (1), 33-40 (1986) PubMed: 3549461 ","","Wed Feb 5 13:47:59 2003","1","","","" "AA02307","1578118","1577411","708","ATGACCGCACTTTTGCTGATTTTTTATCGGTTTAGGGGCATAATAGGCAAAATTAATCACAAGAGAAGCATTATGTTACAAGGCAATTTGTATATCATTTCGGCACCCAGCGGTGCAGGTAAATCTTCATTAATCGCCGCATTGTTAAAACAAAATAATAACCATAAAATGATGGTATCCGTTTCCCACACCACCAGACAGTCGCGCCCGGGCGAACAAGAAGGCGTGCATTATTATTTTGTTTCTCAAGGGGAATTTGAAACCTTAATCGAACAAAATGCCTTTTTGGAATACGCGAAAGTCTTTGGCGGCAATTATTACGGCACGTCTTTATTCGCTATTGAAGAAAATTTAGCTAAAGGCATTGATATTTTTTTGGATATTGATTGGCAGGGCGCACAACAAATTCGCAAAAAAGTGCCGAATGTTAAGAGTATTTTTGTTTTACCGCCGTCGTTGGATGAATTGGAAAGACGCTTAATCGGACGCGGTCAGGACAGTGCGGACGTGATTGCCGACAGAATGGCGAAAGCGATGAGCGAAATTTCTCATTACAATGAATATGATTATGTGATCGTCAACGATAATTTTGAACAGGCGCTTGTGGATTTGCAGGCAATTCTGCGTGCTGAGCGATTGACATTGGCGCATCAGCAGCAAGAAAATCAAGGCCTGATTGAACAACTACTGGAAAAATCAGCTGCATTC","","","26685","MTALLLIFYRFRGIIGKINHKRSIMLQGNLYIISAPSGAGKSSLIAALLKQNNNHKMMVSVSHTTRQSRPGEQEGVHYYFVSQGEFETLIEQNAFLEYAKVFGGNYYGTSLFAIEENLAKGIDIFLDIDWQGAQQIRKKVPNVKSIFVLPPSLDELERRLIGRGQDSADVIADRMAKAMSEISHYNEYDYVIVNDNFEQALVDLQAILRAERLTLAHQQQENQGLIEQLLEKSAAF","1577411","[FUNCTION] Essential for recycling GMP and indirectly, cGMP.","5'-guanylate kinase","Cytoplasm","","
InterPro
IPR008144
Family
Guanylate kinase
PF00625\"[65-170]TGuanylate_kin
PS50052\"[28-209]TGUANYLATE_KINASE_2
PS00856\"[64-81]TGUANYLATE_KINASE_1
InterPro
IPR008145
Domain
Guanylate kinase/L-type calcium channel region
SM00072\"[27-212]TGuKc
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[90-210]Tno description
PTHR23117\"[49-226]TGUANYLATE KINASE-RELATED
PTHR23117:SF1\"[49-226]TGUANYLATE KINASE
signalp\"[1-16]?signal-peptide


","BeTs to 18 clades of COG0194COG name: Guanylate kinaseFunctional Class: FThe phylogenetic pattern of COG0194 is ------yqvdrlbcefghsnujxi-wNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.7e-36) to 3/3 blocks of the IPB000619 family, which is described as \"Guanylate kinase\". Interpro entry for IP:IPR000619. IPB000619A 31-48 0.00022 IPB000619B 61-82 3.8e-14 IPB000619C 85-137 5.3e-15","Residues 32 to 70 match (6e-10) PD:PD467617 which is described as KINASE GUANYLATE TRANSFERASE ATP-BINDING GMP COMPLETE PROTEOME ACETYLATION HOMOLOG A56R ","","","","","","","","","","","Tue Jan 21 09:14:53 2003","Tue Jan 21 09:14:53 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02307 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 65 to 170 (E-value = 3e-50) place AA02307 in the Guanylate_kin family which is described as Guanylate kinase (PF00625)","","","","","Gentry,D., Bengra,C., Ikehara,K. and Cashel,M. Guanylate kinase of Escherichia coli K-12. J. Biol. Chem. 268 (19), 14316-14321 (1993) PubMed: 8390989.","","Tue Jan 21 09:14:53 2003","1","","","" "AA02309","1578288","1579289","1002","ATGGCAATTAAAATTGGTATCAATGGTTTCGGTCGTATCGGCCGTATCGTATTCCGTGCAGCTCAACTTCGTGATGACATTGAAGTAGTAGGTATCAACGACTTAATCGACGTTGAATACATGGCGTATATGTTGAAATACGATTCAACTCACGGTCGGTTCGACGGCACAGTTGAAGTGAAAGACGGCAACTTAGTCGTAAACGGTAAAGCGATTCGCGTAACGGCTGAACGTGATCCGGCAAACTTAAACTGGGGTGCAATCGGTGTTGATGTTGCAGTTGAAGCAACCGGTTTATTCTTAACTGACGAAACTGCCCGTAAACACATCACTGCCGGCGCGAAAAAAGTGGTTTTAACCGGTCCTTCCAAAGACAGCACACCAATGTTCGTACGCGGTGTAAACTTTGATGCTTATAAAGGTCAAGACATTGTTTCCAATGCTTCTTGCACAACTAACTGCTTAGCGCCATTAGCAAAAGTTATCAACGACAAATTCGGTATCAAAGACGGTTTAATGACAACCGTTCACGCTACAACCGCAACACAAAAAACCGTTGACGGTCCATCTGCAAAAGACTGGCGTGGTGGTCGTGGCGCTTCCCAAAACATCATCCCATCTTCAACCGGTGCGGCTAAAGCCGTAGGTAAAGTTATTCCTGCATTAAACGGTAAATTAACCGGTATGGCGTTCCGTGTTCCCACTACAAACGTGTCCGTTGTTGACTTAACCGTTAACCTTGAAAAACCTGCAACTTACGCAGAAATCTGTGCGGAATTAAAACGCGCTTCCGAAAATGAAATGAAAGGTGTTTTAGGCTACACTGAAGATGCCGTAGTTTCTACCGACTTCAACGGTTGTTCCTTAACTTCCGTATTTGACGCGGCAGCAGGTATTGCATTAACCGATACTTTCGTAAAACTGGTATCTTGGTATGACAACGAAGCCGGTTATTCTCACAAAGTATTAGACTTAGTTGCACACGTTTACAACTACAAGGGC","","","35579","MAIKIGINGFGRIGRIVFRAAQLRDDIEVVGINDLIDVEYMAYMLKYDSTHGRFDGTVEVKDGNLVVNGKAIRVTAERDPANLNWGAIGVDVAVEATGLFLTDETARKHITAGAKKVVLTGPSKDSTPMFVRGVNFDAYKGQDIVSNASCTTNCLAPLAKVINDKFGIKDGLMTTVHATTATQKTVDGPSAKDWRGGRGASQNIIPSSTGAAKAVGKVIPALNGKLTGMAFRVPTTNVSVVDLTVNLEKPATYAEICAELKRASENEMKGVLGYTEDAVVSTDFNGCSLTSVFDAAAGIALTDTFVKLVSWYDNEAGYSHKVLDLVAHVYNYKG","1579289","[PATHWAY] Second phase of glycolysis; first step.","glyceraldehyde 3-phosphate dehydrogenase","Cytoplasm","","
InterPro
IPR000173
Family
Glyceraldehyde 3-phosphate dehydrogenase
PR00078\"[109-122]T\"[144-162]T\"[171-187]T\"[228-245]T\"[268-283]TG3PDHDRGNASE
PTHR10836\"[3-332]TGLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE
PF00044\"[3-150]TGp_dh_N
PF02800\"[155-312]TGp_dh_C
PS00071\"[148-155]TGAPDH
InterPro
IPR006424
Family
Glyceraldehyde-3-phosphate dehydrogenase, type I
TIGR01534\"[4-324]TGAPDH-I: glyceraldehyde-3-phosphate dehydro
noIPR
unintegrated
unintegrated
G3DSA:3.30.360.10\"[148-314]Tno description


","No hits to the COGs database.","Significant hit (1.4e-157) to 6/6 blocks of the IPB000173 family, which is described as \"Glyceraldehyde 3-phosphate dehydrogenase\". Interpro entry for IP:IPR000173. IPB000173A 4-15 3.2e-08 IPB000173B 89-125 1.3e-19 IPB000173C 144-178 3.1e-31 IPB000173D 182-235 6.4e-48 IPB000173E 249-302 3.6e-31 IPB000173F 305-325 1.1e-13","Residues 134 to 172 match (1e-07) PD:PD585222 which is described as OXIDOREDUCTASE DEHYDROGENASE NAD GLYCOLYSIS GLYCERALDEHYDE 3-PHOSPHATE COMPLETE PROTEOME GLYCERALDEHYDE-3-PHOSPHATE GAPDH ","","","","","","","","","","","Tue Jan 21 09:21:58 2003","Tue Jan 21 09:21:58 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02309 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 151 to 312 (E-value = 5.1e-118) place AA02309 in the Gp_dh_C family which is described as Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain (PF02800)","","","","","Branlant,G. and Branlant,C. 1985. Nucleotide sequence of the Escherichia coli gap gene. Different evolutionary behavior of the NAD+-binding domain and of the catalytic domain of D-glyceraldehyde-3-phosphate dehydrogenase. Eur. J. Biochem. 150(1): 61-66. PubMed: 2990926. Nelson,K., Whittam,T.S. and Selander,R.K. 1991. Nucleotide polymorphism and evolution in the glyceraldehyde-3-phosphate dehydrogenase gene (gapA) in natural populations of Salmonella and Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 88(15): 6667-6671. PubMed: 1862091.Doolittle,R.F., Feng,D.F., Anderson,K.L. and Alberro,M.R. A naturally occurring horizontal gene transfer from a eukaryote to a prokaryote. J. Mol. Evol. 31 (5): 383-388 (1990) PubMed: 2124629.Duee,E., Olivier-Deyris,L., Fanchon,E., Corbier,C., Branlant,G. and Dideberg,O. Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde 3-phosphate dehydrogenases: implication for NAD binding and cooperativity. J. Mol. Biol. 257 (4): 814-838 (1996) PubMed: 8636984.","","Wed Jan 29 13:41:54 2003","1","","","" "AA02310","1579802","1579389","414","ATGAATTGGGTCTGGTTTGCGATCGGTTCCGCATTTTTTGCCGGATTAACGGCAATTTTAGGCAAATTAGGTGTGGAAGGCTTGAATAGTAATTTAGCGACATTTATTCGTACAGTAGTGATTTTATTTGTGATTGTGGCGATTATTTCGATGCGTAATGAATGGCAATTGCCTCAACATATTGCGACCAAGCCGGTTATTTTCCTTGTGTTATCCGGGGTGGCGACGGGATTTTCCTGGCTTTGTTACTATCGCGCTTTACAACTTGCGCCGGCATCTTGGGTCGCACCTATTGATAAACTCAGCGTGGTTATTGCCATTGTGTTAGGTGTGACTATCTTGGGCGAGCCGGTGAGTATGAAATTATTGATTGGGGCAGGATTGATTCTTTCGGGCGTGTTGGTCTTGGCGTTT","","","15787","MNWVWFAIGSAFFAGLTAILGKLGVEGLNSNLATFIRTVVILFVIVAIISMRNEWQLPQHIATKPVIFLVLSGVATGFSWLCYYRALQLAPASWVAPIDKLSVVIAIVLGVTILGEPVSMKLLIGAGLILSGVLVLAF","1579389","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR000620
Domain
Protein of unknown function DUF6, transmembrane
PF00892\"[12-138]TDUF6
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide
tmhmm\"[5-23]?\"[33-51]?\"[66-84]?\"[103-137]?transmembrane_regions


","BeTs to 6 clades of COG2510COG name: Predicted membrane proteinFunctional Class: SThe phylogenetic pattern of COG2510 is --m-k--q-------f---n------Number of proteins in this genome belonging to this COG is","","Residues 75 to 136 match (9e-07) PD:PD406685 which is described as COMPLETE PROTEOME MEMBRANE PAB1426 ATU3299 PLASMID PH0613 PH1270 INTEGRAL NMB1840 ","","","","","","","","","","","","Tue Jan 21 09:24:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02310 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 12 to 138 (E-value = 3.9e-18) place AA02310 in the DUF6 family which is described as Integral membrane protein DUF6 (PF00892)","","","","","","","","1","","","" "AA02312","1579815","1580300","486","ATGTTTCTGCAATATTTCCTTTATAATATACCAACTTTTTCATCCACAACCTTAATCTGTATGGCTATTGTTAATCAATCGACGCTCGTTGCATACAACGCGCAACAAATGTATCGGCTTTTAAATGATTATGAGCGTTATCCCGAGTTTTTGCCAGGCTGTGTCGGCAACCTCACGTTAAATAAAAGTGCGGTGCAATTAACCGGTGAATCGGAAATCAGCAAGGCGGGCATTCGACAAAAGTTTACCACCTGTAATACAATGAAAGAAAATCAATCAATTAGAATGCAATTCGTTGACGGTCCGTTTAAATTTCTGCAAGGTGAAAAGTTTACCGATCCGGATAAAAAAAGCTGTCAGACTCGACTTTATTTAGCATCTGAATTTTCAAATCCACCGGTTGGATTTGCCTTCGGTCAGATCTTTACCCATTTAACCAATAAAATGATTGATGCATTGAAACAGCGAGCAAAACAAATTTATGGT","","","18520","MFLQYFLYNIPTFSSTTLICMAIVNQSTLVAYNAQQMYRLLNDYERYPEFLPGCVGNLTLNKSAVQLTGESEISKAGIRQKFTTCNTMKENQSIRMQFVDGPFKFLQGEKFTDPDKKSCQTRLYLASEFSNPPVGFAFGQIFTHLTNKMIDALKQRAKQIYG","1580300","","conserved hypothetical protein","Periplasm, Cytoplasm","","
InterPro
IPR005031
Family
Streptomyces cyclase/dehydrase
PF03364\"[30-154]TPolyketide_cyc
noIPR
unintegrated
unintegrated
PD275159\"[37-161]TQ9CP89_PASMU_Q9CP89;
G3DSA:3.30.530.30\"[21-162]Tno description
signalp\"[1-22]?signal-peptide


","BeTs to 6 clades of COG2867COG name: Oligoketide cyclase/lipid transport proteinFunctional Class: IThe phylogenetic pattern of COG2867 is ------y---r---efghsn-jx---Number of proteins in this genome belonging to this COG is","","Residues 21 to 161 match (1e-42) PD:PD406158 which is described as PROTEOME COMPLETE OLIGOKETIDE NMA1006 PM0165 CC1736 III BMEI0860 ATU1441 RSC1425 ","","","","","","","","","","","","Tue Jan 21 09:23:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02312 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 21 to 162 (E-value = 5.4e-46) place AA02312 in the ARPF family which is described as Aromatic-Rich Protein Family (PF03654)","","","","","","","","1","","","" "AA02313","1580296","1580586","291","ATGGTTAATAAAATCAATATTCAAATTGCCTATGCGTTTCCTGATCATCATTATCTGAAATCGTTTAGTGTAGGTGAAGGCACTATGGTGCAAACCGCCATTTTACAGTCCGGCATTTTACAACAATTTACCGACATTGATTTACGCGAAAATAAAATCGGCATTTTCAGCCGTCCCGTGAAATTAACGGATCAGCTGAAAGACGGCGATCGCATTGAAATTTACCGCCCGCTGTTGGCGGATCCGAAAGAAATTCGACGCAAACGTGCGGAAGAACAAGCAAAGAAAAAA","","","11210","MVNKINIQIAYAFPDHHYLKSFSVGEGTMVQTAILQSGILQQFTDIDLRENKIGIFSRPVKLTDQLKDGDRIEIYRPLLADPKEIRRKRAEEQAKKK","1580586","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR005346
Family
Protein of unknown function UPF0125
PF03658\"[5-88]TUPF0125


","BeTs to 6 clades of COG2914COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG2914 is --------------efghsn------Number of proteins in this genome belonging to this COG is","","Residues 14 to 82 match (1e-12) PD:PD413547 which is described as PROTEOME COMPLETE NMA1005/NMB0796 XF2346 ","","","","","","","","","","","","Tue Jan 21 09:25:49 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02313 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 88 (E-value = 1.5e-55) place AA02313 in the UPF0125 family which is described as Uncharacterised protein family (UPF0125) (PF03658)","","","","","","","","1","","","" "AA02315","1580622","1581812","1191","ATGAACAAATTTTGTTTACCTCAAAATATTACACCGGAAATCTTTTTACGCGATTACTGGCAGAAAAAACCGTTATTAATTCGACGCGGTTTACCAGAAATTATCGGTATGCTTGAACCACGCGACATCACCGAATTAGCCAAAACGGAAGAAGTGGTCGCGCGCTTGATCAAGCAACATTCCGATGACAATTGGGAATTTCGCACCAGTCCGTTATCCAAAGAAGATTTTGATAACCTGCCTGAAAAATGGTCGGTTTTAGTGCAAGATATGGAGCAATGGTCGCCGTTATTAGGCAATTTATGGCGAAAATTCGACTTTATTCCGCAATGGCAACGTGATGACATCATGGTATCTTTCGCGCCACAAGGCGGTTCTGTCGGCAAACATTATGATGAATACGATGTCTTCCTGGTGCAGGCTTACGGTCATCGCCGTTGGCAGCTTGGCAAATGGTGCGAACCGACCACAGAATTCAAACCGAACCAACCGATTCGTATTTTTGACGACATGGGCGAACTGATTTTAGACGAAGTGATGGCGCCGGGCGATGTGCTGTACGTGCCTTCCCGTCTGGTTCACTACGGCGTAGCGCAAGATGACTGCTTAACCGTATCCTTCGGGTTGCGCTACCCAAATACATCGGAACTACTGGAAAGTATTAGAAATCACCTTTACCATCCAAGTTTGGAAGTGAATGAACTGGCTATCCCGTTCCGTTTAAGTCCTTCAGAACAAAAAACCGGCGAATTGACACCGCAAGACGTACAACAAATGAAAGCGTTATTTTTACAACAGCTGGCAAATTCTGCACAGTTCGACACCTTATTCCAACAAGCGCTTGCAACAACCGTCAGCCGTCGGCGCTATGAATTACTGGAAGTCGCCGGTTTTTCCGATCCGGAAGACGTGTTGGAAAGCTTTGAACATGGCGGCAGATTACGTCAAGACAACAATTGCAAATTGGTTTATACCCAAGATCCGTTCCGAATTTATGCCAACGGCGAATGGCTGGATGAATTGACCTACGCCGAAGCGGAAATTTTGAAACAACTTGCCGATGGTCAAACCGTTGATTTTGCTTTTTTAACCCGCTTAATCGGCAGCCTGCAGGATCAACAGATTTCCATGGAAGTGTTGGTCGATAGCATTTGCAATTGGCTGGACGACGGCTGGGCGTTGTTAACCGAG","","","46384","MNKFCLPQNITPEIFLRDYWQKKPLLIRRGLPEIIGMLEPRDITELAKTEEVVARLIKQHSDDNWEFRTSPLSKEDFDNLPEKWSVLVQDMEQWSPLLGNLWRKFDFIPQWQRDDIMVSFAPQGGSVGKHYDEYDVFLVQAYGHRRWQLGKWCEPTTEFKPNQPIRIFDDMGELILDEVMAPGDVLYVPSRLVHYGVAQDDCLTVSFGLRYPNTSELLESIRNHLYHPSLEVNELAIPFRLSPSEQKTGELTPQDVQQMKALFLQQLANSAQFDTLFQQALATTVSRRRYELLEVAGFSDPEDVLESFEHGGRLRQDNNCKLVYTQDPFRIYANGEWLDELTYAEAEILKQLADGQTVDFAFLTRLIGSLQDQQISMEVLVDSICNWLDDGWALLTE","1581812","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003347
Domain
Transcription factor jumonji/aspartyl beta-hydroxylase
SM00558\"[83-222]TJmjC
PS51184\"[97-226]TJMJC
InterPro
IPR013109
Family
Cupin 4
PTHR13096\"[13-194]TMINA53 (MYC INDUCED NUCLEAR ANTIGEN)
PF08007\"[12-321]TCupin_4


","BeTs to 6 clades of COG2850COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG2850 is ------------b-ef-hsn------Number of proteins in this genome belonging to this COG is","","Residues 228 to 395 match (3e-47) PD:PD136906 which is described as PROTEOME COMPLETE PM0167 HI0396 ","","","","","","","","","","","","Mon Jan 6 09:14:04 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02315 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02316","1581822","1583153","1332","ATGAGCGATAACATTTACTCGGTCAGCCAATTAAACCAATCCGTTCGCCTGATGTTAGAAAATCAGCTCGGACAAGTTTGGCTCACCGGGGAAATATCTAACTTTACCCAACCAGTTTCGGGGCATTGGTATTTAAGTTTAAAAGACGAAAACGCCCAAGTGCGCTGCGCCATGTTCCGCATGAAAAATCTGCGCGTGGGTTTTCGTCCGTCTAATGGCATGCAGGTATTGGTGCGTGCTAGTGTCAGTTTGTATGAGCCGCGCGGTGATTATCAACTGATTATCGAAAGTATGCACCTTGCCGGCGAAGGGTTACTGATGCAGCAATTTGAAGCGCTGAAACTCAAATTAGCGGCAGAAGGATTGTTCGCTCAAAATCACAAGAAAAACCTACCGCACTTTAGTCAAGCGGTAGGCATTATTACCTCTAAAACCGGGGCGGCATTGCAGGATATTTTGCATATTCTACAACGTCGTGATCCGAGTCTGAAAGTCATTATTTATCCCACAGCCGTGCAAGGTAAAGATGCGGCGGCTGAAATCGCACAAATGATTGAAATCGCCAACCGGCGACAAGAGGCGGATGTATTAATCGTGGGGCGCGGCGGTGGTTCGCTGGAAGATTTGTGGTGCTTTAATGAAGAAATTGTGGCGCGCGCGATGTTTCATTCCGTCATTCCAATCATTAGCGCTGTCGGTCATGAAACCGATATTACCATTGCCGATTTTGTCGCCGATTTACGCGCACCGACCCCTTCTGCCGCGGCAGAGCTGGTGAGCCGCGATCAAACGGAATTATTACAGCAGTTACAATATCGTCAACAACGCATTGAAATCGCTTTGGATCGCATTTTTATCGAGAAGAAACGGCAATTACAGCATCTTTTCTTACGTCTGCAAAACCAACACCCACAAGCGCAACTACGTATTCAACAGCAACTTATCGCCCAATTACGTCATCGCTTGCAGCAAAGTCTGTGTCATCACCGGCAAAAAACAGCGGAAAATCTGACCGCACTTTCGGCGCGGTTATATAAAAATCCGCTGCCGTTAAAGTTACAACAACAGAAACAACTGCTGGCGCAACTTAAAGTGCGGTTAAATTCCGAGATGAATTTGAAGGTGGGGCTTCAACAAAAACAACTGGCGCATTTATGTGGCAAATTAGACAGTTTAAGCCCGTTGAAGGTATTAGCGCGGGGATATTCCATCACCCAAAATCAACATAACCAAGCCATTACATCAATTCATGCGGTGAACATCGGCGAGCAAATCCAAACACGCGTTGCCGACGGGATTATCATCAGCCAGATTAATCGGTTAGAGAAGAAA","","","50191","MSDNIYSVSQLNQSVRLMLENQLGQVWLTGEISNFTQPVSGHWYLSLKDENAQVRCAMFRMKNLRVGFRPSNGMQVLVRASVSLYEPRGDYQLIIESMHLAGEGLLMQQFEALKLKLAAEGLFAQNHKKNLPHFSQAVGIITSKTGAALQDILHILQRRDPSLKVIIYPTAVQGKDAAAEIAQMIEIANRRQEADVLIVGRGGGSLEDLWCFNEEIVARAMFHSVIPIISAVGHETDITIADFVADLRAPTPSAAAELVSRDQTELLQQLQYRQQRIEIALDRIFIEKKRQLQHLFLRLQNQHPQAQLRIQQQLIAQLRHRLQQSLCHHRQKTAENLTALSARLYKNPLPLKLQQQKQLLAQLKVRLNSEMNLKVGLQQKQLAHLCGKLDSLSPLKVLARGYSITQNQHNQAITSIHAVNIGEQIQTRVADGIIISQINRLEKK","1583153","From Genbank:[gi:2507019]This protein bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides which are then degraded furthur into small acid-soluble oligonucleotides. It can also degrade 3'or 5' single stranded regions extending from the termini of duplex DNA molecules and displaced single stranded regions.","exodeoxyribonuclease VII large subunit","Cytoplasm","","
InterPro
IPR003753
Family
Exonuclease VII, large subunit
PF02601\"[194-369]TExonuc_VII_L
TIGR00237\"[7-438]TxseA: exodeoxyribonuclease VII, large subun
InterPro
IPR004365
Domain
Nucleic acid binding, OB-fold, tRNA/helicase-type
PF01336\"[26-101]TtRNA_anti


","BeTs to 14 clades of COG1570COG name: Exonuclease VII, large subunitFunctional Class: LThe phylogenetic pattern of COG1570 is --------vdrlb-efghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit (2.1e-172) to 7/7 blocks of the IPB003753 family, which is described as \"Exonuclease VII, large subunit\". Interpro entry for IP:IPR003753. IPB003753A 25-60 1.1e-28 IPB003753B 61-94 2.7e-21 IPB003753C 110-148 6.6e-24 IPB003753D 184-216 7.5e-25 IPB003753E 217-257 8.7e-34 IPB003753F 265-315 2.3e-15 IPB003753G 361-405 1.6e-17 IPB003753F 355-405 0.078 IPB003753F 310-360 0.19","Residues 335 to 438 match (5e-19) PD:PD407053 which is described as LARGE SUBUNIT VII PROTEOME COMPLETE EXONUCLEASE EXODEOXYRIBONUCLEASE HYDROLASE NUCLEASE PROBABLE ","","","","","","","","","","","Mon Jan 6 14:09:03 2003","Mon Jan 6 09:18:21 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02316 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 194 to 369 (E-value = 6.8e-70) place AA02316 in the Exonuc_VII_L family which is described as Exonuclease VII, large subunit (PF02601)","","","","","Chase,J.W., Rabin,B.A., Murphy,J.B., Stone,K.L. and Williams,K.R. Escherichia coli exonuclease VII. Cloning and sequencing of the gene encoding the large subunit (xseA) J. Biol. Chem. 261 (32), 14929-14935 (1986) PubMed: 3021756 Vales,L.D., Rabin,B.A. and Chase,J.W. Subunit structure of Escherichia coli exonuclease VII J. Biol. Chem. 257 (15), 8799-8805 (1982) PubMed: 6284744 ","","Mon Jan 6 09:18:21 2003","1","","","" "AA02317","1583947","1583165","783","ATGGGCTATTATTGTGTGGATAATCTCCCTCTGGATTTATTGCCCCAGCTGATTCAGATTTTGTCCGCCGGGCAACCTGCCGTTGCCATTAGTTTAGACATTCGCAACCTGCCGACTTCCCCGCAAATCCTGGAAAATACGATTAATGATTTGCAGCAGAAACATAATGTTAAAATTATTTTCTTGGATGCCGATACCGGCACATTAATTCGCCGCTATAGCGATTCCCGCCGTCTGCACCCGTTATCCACACAGGACCTTTCCTTAGAAGCCGCCATTGAAGAAGAACGTAACCGTCTTGATCCTCTCGTGCAACAAGCCAATTTGCTGATTGACACTGCCGCTTTATCTACCCACGAATTAGCGGAGCGATTGCGTGAGTTTTTGAGCGGGCATTCCGATAAAGAATTGAAAATAGTGGTGGAATCTTTCGGTTTTAAATATGGCATTCCGTTAGATGCGGATTACGTGTTTGATGTGCGTTTCCTGCCGAATCCGCATTGGAATCAGGGGTTACGCCCGCTGACCGGTTTGGATGAAGAAGTGGCGGAATTCTTAAATAAGCACAATGAAGTGCATCAATTTATCTACCTCACCCGTTCTTATATCGAAACCTGGCTGCCGTCGCTGGAACAGAATAACCGCAGCTATTTGACCATTGCTATCGGTTGTACGGGCGGCAAACACCGTTCTGTTTACATTGCCGAACAACTGGGGAAATATTTTCAGGATAAAGGTAAAAATGTCAAAATTTTGCATTGCTCACTGGCAAAGCATAAAAAA","","","32109","MGYYCVDNLPLDLLPQLIQILSAGQPAVAISLDIRNLPTSPQILENTINDLQQKHNVKIIFLDADTGTLIRRYSDSRRLHPLSTQDLSLEAAIEEERNRLDPLVQQANLLIDTAALSTHELAERLREFLSGHSDKELKIVVESFGFKYGIPLDADYVFDVRFLPNPHWNQGLRPLTGLDEEVAEFLNKHNEVHQFIYLTRSYIETWLPSLEQNNRSYLTIAIGCTGGKHRSVYIAEQLGKYFQDKGKNVKILHCSLAKHKK","1583165","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR005337
Family
P-loop ATPase protein
PIRSF005052\"[1-261]TPredicted P-loop kinase
PF03668\"[1-259]TATP_bind_2


","No hits to the COGs database.","","Residues 1 to 125 match (3e-38) PD:PD473567 which is described as COMPLETE PROTEOME ATP-BINDING KINASE YVCJ YHBJ LIN2617 PTSN-PTSO PREDICTED YJIE ","","","","","","","","","","","","Mon Jan 6 09:33:05 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02317 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 259 (E-value = 2.6e-151) place AA02317 in the ATP_bind_2 family which is described as P-loop ATPase protein family (PF03668)","","","","","","","","1","","","" "AA02319","1584565","1584047","519","ATGAAATTTACTGAATTATTAACACCGGAAAGTATCCGTCAGGGCATGATTTTGTCCAGCAAAAAGCGTGTGTTTGAGTTAATCTCACACATTGTGGCTGAAAAATTGCAGCTGGAAAACGGTGAACAATGCTGTTTTGAGTGTTTGTTCAGCCGTGAAAAACTGGGCAACTCCGGTCTCGGCGGCGGCGTGGCAATGCCAAAAGGACGTTTGCCGGCAGAAGCCCAACCTATCGCCGTATTCATTCAATTAGACTCGCCTATTGACTATGAGGCAGCGGATCACCGTGAAGTGGATTTAATCTTTGCGGTGTTGATTCCGGAAAATATGTGTGCCGCGTATGTTCAGTATTTGCCTAAATTAGCGGAAAATTTAACGGATAAATCTTTGTGCAAGCAGTTGCGGGCGGCGAAAAGTGCGGATGAAATTTTGCAAATTTTTTTTCATTATGATCAAACCGATGTGAATGAAGCGGTTCCTACGGAACAGGATGTAACGGAATCGCAGCGTAATTTTACT","","","19396","MKFTELLTPESIRQGMILSSKKRVFELISHIVAEKLQLENGEQCCFECLFSREKLGNSGLGGGVAMPKGRLPAEAQPIAVFIQLDSPIDYEAADHREVDLIFAVLIPENMCAAYVQYLPKLAENLTDKSLCKQLRAAKSADEILQIFFHYDQTDVNEAVPTEQDVTESQRNFT","1584047","","nitrogen regulatory IIA protein","Cytoplasm","","
InterPro
IPR002178
Domain
Phosphotransferase system, phosphoenolpyruvate-dependent sugar EIIA 2
PD001689\"[7-142]TQ9CP84_PASMU_Q9CP84;
G3DSA:3.40.930.10\"[1-157]Tno description
PF00359\"[5-150]TPTS_EIIA_2
PS51094\"[5-150]TPTS_EIIA_TYPE_2
InterPro
IPR006320
Family
Phosphotransferase system, IIA-like nitrogen-regulatory protein PtsN
TIGR01419\"[2-149]Tnitro_reg_IIA: PTS IIA-like nitrogen-regula


","No hits to the COGs database.","Significant hit ( 4.4e-05) to 1/1 blocks of the IPB002178 family, which is described as \"phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2\". Interpro entry for IP:IPR002178. IPB002178 52-69 4.6e-05","Residues 21 to 143 match (6e-07) PD:PD541347 which is described as (see also SP:O32346_CAUCR_O32346).","","","","","","","","","","","","Mon Jan 6 09:38:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02319 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 150 (E-value = 1.7e-08) place AA02319 in the PTS_EIIA_2 family which is described as Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2 (PF00359)","","","","","Powell,B.S., Court,D.L., Inada,T., Nakamura,Y., Michotey,V., Cui,X., Reizer,A., Saier,M.H. Jr. and Reizer,J. Novel proteins of the phosphotransferase system encoded within the rpoN operon of Escherichia coli. Enzyme IIANtr affects growth on organic nitrogen and the conditional lethality of an erats mutant J. Biol. Chem. 270 (9), 4822-4839 (1995) PubMed: 7876255 Bordo,D., van Monfort,R.L., Pijning,T., Kalk,K.H., Reizer,J., Saier,M.H. Jr. and Dijkstra,B.W. The three-dimensional structure of the nitrogen regulatory protein IIANtr from Escherichia coli J. Mol. Biol. 279 (1), 245-255 (1998) PubMed: 9636714 ","","Mon Jan 6 09:52:37 2003","1","","","" "AA02320","1585294","1584572","723","ATGGCGATTCTGTATGCTGAAAATTTAGCGAAAAGTTATAAAAACCGCCAAGTGGTTTCCGATGTGAGTTTAACGGTGAATTCCGGCGAAATCGTCGGTTTGTTGGGGCCTAACGGTGCCGGTAAAACTACCACCTTCTACATGGTGGTGGGCTTGGTAAATCATGATCAAGGAAAAATCCGCATTGACGAGGAAGACATCAGTCTGTTACCGATACACAATCGAGCGCAAAAAGGCATCGGTTATTTGCCGCAGGAAGCCTCCATCTTCCGCCGTTTAAGCGTGTACGATAATTTAATGGCGGTGTTGGAAATACGCAAAGATTTGACCGCACTTCAACGCCGCGAGAGAGCTGACGAGTTAATTGAAGAATTTAATATCAGTCATATCCGTGATAATTTAGGGCAATCTTTGTCGGGCGGGGAGCGCCGTCGTGTGGAAATCGCCCGTGCGTTGGCGGCAAATCCGAAATTTATTTTGTTAGATGAGCCTTTCGCCGGGGTTGACCCGATTTCGGTGATTGATATTAAGAAAATCATTAAAGACTTGCGTGATCGCGGCTTGGGCGTATTAATTACCGACCACAATGTGCGCGAAACACTGGATGTGTGTGAGCGCGCTTATATTGTGAGCGCCGGTAAAATGATTGCCACCGGCACACCGCAAGAGATTATGAACAACAAATTGGTAAAAGACGTTTATTTAGGCGCCGATTTCCAACTT","","","26827","MAILYAENLAKSYKNRQVVSDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGLVNHDQGKIRIDEEDISLLPIHNRAQKGIGYLPQEASIFRRLSVYDNLMAVLEIRKDLTALQRRERADELIEEFNISHIRDNLGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKKIIKDLRDRGLGVLITDHNVRETLDVCERAYIVSAGKMIATGTPQEIMNNKLVKDVYLGADFQL","1584572","From PF00005:ABC transporters are a large family of proteins responsible for translocation of a variety of compounds across biological membranes.ABC transporters are the largest family of proteins in many completely sequenced bacteria. ","ABC transporter ATP-binding protein","Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[138-173]TYHBG_HAEIN_P45073;
PF00005\"[29-213]TABC_tran
PS50893\"[4-237]TABC_TRANSPORTER_2
PS00211\"[138-152]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[28-202]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[3-241]Tno description
PTHR19222\"[4-234]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF15\"[4-234]TABC TRANSPORTER


","BeTs to 15 clades of COG1137COG name: ABC-type (unclassified) transport system, ATPase componentFunctional Class: RThe phylogenetic pattern of COG1137 is -------qvd---cefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 9.1e-30) to 2/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 18-64 2.8e-14 IPB001140B 135-173 4.2e-14Significant hit ( 5.3e-05) to 2/5 blocks of the IPB001324 family, which is described as \"Phosphoribulokinase family\". Interpro entry for IP:IPR001324. IPB001324A 28-49 0.0017 IPB001324E 159-207 15","Residues 103 to 195 match (3e-07) PD:PD241888 which is described as ATP-BINDING PROTEOME COMPLETE ABC TRANSPORTER HOMOLOG COBALT COMPONENT A2 EXPORTER ","","","","","","","","","","","Mon Jan 6 10:10:40 2003","Mon Jan 6 09:57:53 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02320 is paralogously related to AA01051 (2e-28), AA00700 (2e-27), AA01656 (3e-27), AA02718 (4e-27), AA02140 (6e-27), AA02353 (8e-27), AA02324 (3e-26), AA00207 (4e-25), AA00415 (1e-24), AA00933 (5e-24), AA00858 (5e-24), AA02550 (1e-23), AA01524 (1e-23), AA00799 (2e-23), AA00751 (1e-22), AA01510 (2e-22), AA01645 (4e-22), AA01867 (6e-22), AA01456 (2e-20), AA02440 (8e-19), AA01779 (8e-19), AA02080 (1e-18), AA01824 (1e-18), AA01616 (1e-18), AA02786 (2e-18), AA02225 (2e-18), AA01684 (7e-18), AA02152 (2e-17), AA01820 (2e-17), AA02805 (3e-17), AA01422 (7e-17), AA02898 (2e-16), AA02899 (3e-16), AA01393 (3e-15), AA02642 (9e-15), AA01568 (9e-15), AA01757 (3e-14), AA02484 (4e-14), AA02331 (6e-14), AA01961 (2e-13), AA01569 (6e-13), AA01509 (2e-12), AA02609 (4e-12), AA01947 (5e-12), AA02573 (2e-11), AA00061 (8e-11), AA02606 (1e-10), AA02146 (3e-10), AA01291 (4e-10), AA00591 (3e-09), AA01555 (4e-09), AA02226 (4e-07), AA00934 (2e-06) and A02145 (4e-05).","","","","","","Residues 29 to 213 (E-value = 1.4e-62) place AA02320 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Higgins CF, Hyde SC, Mimmack MM, Gileadi U, Gill DR, Gallagher MPBinding protein-dependent transport systems.J Bioenerg Biomembr 1990 Aug;22(4):571-92PMID: 2229036 ","","Mon Jan 6 10:10:40 2003","1","","","" "AA02321","1585818","1585303","516","ATGAAATCAGTAAGCAATAACATTTTTTTTGCTTCCATGTTAATGCTGGTGTCTTTGTCTACTTTTGCATTGAAAGACGATACCAATCAGCCCATTAATATCGTTTCCGATAACCAATCCTTAGACATGACCAGTCGGGTAGTGATCTTTACAGACAACGTTGTCATTACTCAAGGTTCTATCGTGGTGAAAGCGAATAAAGTGATCATCACCCGTCCGGAAGAAAATTCCAAGAAAAAAGACACTGTTGAGGCGTTTGGCAATCCGGTGACATTCCATCAGGTAATGGACGACGGCAAGCCCGTGGACGGCAAAGCCAATAAAGTGTTTTATGATTTAGGCACGGAGTTTTTAACCTTAACCGGTAATGCCGAATTAAAACAGCTGGATAGCAAAATCAACGGTAATGTGATCACTTATGATGTGAAAAAACAACAACTCAAAGCCAACGGTTCTTCCGGTTCACGCGTCACCACCGTGTTAATTCCGGTTCAACTCAATAATGCAAAAGGGAAA","","","18782","MKSVSNNIFFASMLMLVSLSTFALKDDTNQPINIVSDNQSLDMTSRVVIFTDNVVITQGSIVVKANKVIITRPEENSKKKDTVEAFGNPVTFHQVMDDGKPVDGKANKVFYDLGTEFLTLTGNAELKQLDSKINGNVITYDVKKQQLKANGSSGSRVTTVLIPVQLNNAKGK","1585303","","conserved hypothetical protein","Periplasm","","
InterPro
IPR005653
Family
OstA-like protein
PF03968\"[5-146]TOstA
InterPro
IPR014340
Family
Cell envelope biogenesis YhbN
TIGR03002\"[23-164]Touter_YhbN: cell envelope biogenesis protei
noIPR
unintegrated
unintegrated
signalp\"[1-23]?signal-peptide
tmhmm\"[4-24]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Jan 6 10:14:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02321 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 16 to 166 (E-value = 4.1e-65) place AA02321 in the OstA family which is described as OstA-like protein (PF03968)","","","","","","","","1","","","" "AA02323","1586383","1585802","582","TTGTATTGTATGAATATTCGTTTGAATATTATCTTAGCCGTGATTGCGCTGGGTTTATTGGCCTGGTTTTATAGCCTGAATAAAGAGGACGGAAGTTTGAAAGATCTGATTAAAACGGCAGATAGTCCGGAATATGTCGGGCAGAAAATGAGCACTACCGTGTATTCGCCCACCGGCAAAAAACAATATTTAGCGACCTCCGCAAAAGTGGAACATTATACCTCGGATGGACATACGGATTTTCAACAACCGGTCGTGTTGTTGTTAGATATTGAAATTCAAAATACGGATAAAGAAAGCTGGAAACTCAGCGCTGACAAAGCACGATTGACCAAAGACAATATGCTGTATCTGGATGGCAATGTCATCGCACAAAGCCTTTCCGCGCAATCTCGTTTGCAACGCATTGAAACCCAACGCGCGGTGGTTAATTTGACAACACAGGACATCAGCTCGGATCAAATGGTAAAACTTAACGGGCAGAATTTTAATTCCACAGGCTTAAAATTAACCGGCAACTTGCAGCAACAAGTGGCTACATTAAAAGAACAGGTGAAAACATATTATGAAATCAGTAAGCAA","","","21799","LYCMNIRLNIILAVIALGLLAWFYSLNKEDGSLKDLIKTADSPEYVGQKMSTTVYSPTGKKQYLATSAKVEHYTSDGHTDFQQPVVLLLDIEIQNTDKESWKLSADKARLTKDNMLYLDGNVIAQSLSAQSRLQRIETQRAVVNLTTQDISSDQMVKLNGQNFNSTGLKLTGNLQQQVATLKEQVKTYYEISKQ","1585802","","conserved hypothetical protein","Outer membrane, Periplasm, Extracellular","","
InterPro
IPR010664
Family
Protein of unknown function DUF1239
PF06835\"[13-190]TDUF1239
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","","Residues 22 to 193 match (3e-51) PD:PD036325 which is described as PROTEOME COMPLETE YRBK TRANSMEMBRANE EXPORTED PM0173 VC2525 INNER HI1150 POSSIBLE ","","","","","","","","","","","","Mon Jan 6 10:32:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02323 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 13 to 190 (E-value = 1.1e-62) place AA02323 in the DUF1239 family which is described as Protein of unknown function (DUF1239) (PF06835)","","","","","","","","1","","","" "AA02324","1586658","1587452","795","ATGAACGAAACGTTAATTGAAGTAAAACACCTTACGTTTAAACGCGGTGAACGGATTATTTACCACGATCTGAATTTGCGCGTTCCCCGCGACAAAATTACCGCCATTATGGGACCGTCAGGGATTGGTAAAACCACCCTTTTGAAACTCATCGGCGGTCAGCTGATGCCTTCCGAAGGTGAAATTCTGTTCGACGGGCAAGATATTTGCAAATTATCCAACAGTGAACTTTATGATGTGCGCAAACGCATGGGTATGCTGTTTCAATCCGGCGCATTATTCACCGATATTTCCACCTTTGATAATGTGGCATTTCCTATTCGAGAGCACACCAATCTGCCTCCGTCGTTGATTAGAAAAATAGTATTAATGAAACTCGAAGCGGTGGGCTTGCGCGGTGCCGCCGATTTAATGCCTTCCGAACTTTCCGGCGGGATGGCGCGTCGTGCCGCGCTCGCCCGTGCCATTGCGTTAGATCCGGATTTAATCATGTTCGACGAACCCTTTACGGGACAAGATCCCATCAGCATGGGCGTGATTATCAGCTTAATCAAACGGCTAAATGAAGCGTTGAATTTAACGTCTATTGTGGTCTCCCATGATGTGCAGGAAGTATTGAGCATCGCCGATTATGCCTATATTATCGCCGATCAGCATGTGATTGCCGAAGGCTCATCGGAGCAGCTATTGGCGAGCCAAGATCCCCAAGTGAAACAGTTTTTACAAGGTCAGGCGGACGGTCCGGTACGTTTTCACTACCCTGCGCCAAATTACATTGAGGAGTTGTTTGAATGC","","","29336","MNETLIEVKHLTFKRGERIIYHDLNLRVPRDKITAIMGPSGIGKTTLLKLIGGQLMPSEGEILFDGQDICKLSNSELYDVRKRMGMLFQSGALFTDISTFDNVAFPIREHTNLPPSLIRKIVLMKLEAVGLRGAADLMPSELSGGMARRAALARAIALDPDLIMFDEPFTGQDPISMGVIISLIKRLNEALNLTSIVVSHDVQEVLSIADYAYIIADQHVIAEGSSEQLLASQDPQVKQFLQGQADGPVRFHYPAPNYIEELFEC","1587452","From PF00005: ABC transporters are a large family of proteins responsible fortranslocation of a variety of compounds across biological membranes.ABC transporters are the largest family of proteins in many completely sequenced bacteria. ","ABC transporter ATP binding protein","Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[141-184]TQ8EAF2_SHEON_Q8EAF2;
PF00005\"[31-218]TABC_tran
PS50893\"[6-242]TABC_TRANSPORTER_2
PS00211\"[142-156]?ABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[30-226]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[3-245]Tno description
PTHR19222\"[6-262]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF52\"[6-262]TABC TRANSPORTER


","BeTs to 12 clades of COG1127COG name: ABC-type exporter of toluene and related compounds, ATPase componentFunctional Class: NThe phylogenetic pattern of COG1127 is -------q--r--cefghsnujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-23) to 2/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 20-66 9.7e-16 IPB001140B 139-177 1.7e-06Significant hit ( 1.9e-05) to 1/4 blocks of the PR00364 family, which is described as \"Disease resistance protein signature\". Prints database entry for PR:PR00364. PR00364A 33-48 1.9e-05","Residues 185 to 224 match (2e-07) PD:PD000383 which is described as ATP-BINDING PROTEOME COMPLETE ABC TRANSPORTER TRANSPORTER OLIGOPEPTIDE PLASMID BINDING/ATPASE NUCLEOTIDE ","","","","","","","","","","","Mon Jan 6 10:38:56 2003","Mon Jan 6 10:35:31 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02324 is paralogously related to AA01645 (6e-33), AA00415 (1e-32), AA00700 (3e-32), AA02718 (9e-30), AA01051 (2e-27), AA01524 (2e-26), AA02320 (3e-26), AA01422 (1e-25), AA02440 (1e-24), AA00858 (2e-24), AA02080 (1e-23), AA01867 (1e-23), AA02353 (3e-23), AA00799 (3e-22), AA02899 (4e-22), AA01616 (9e-22), AA02140 (1e-21), AA01824 (1e-21), AA01779 (1e-20), AA01820 (7e-19), AA01656 (9e-19), AA01509 (2e-18), AA02805 (2e-17), AA01757 (4e-17), AA00061 (4e-17), AA02331 (6e-17), AA02898 (8e-17), AA02152 (1e-16), AA01947 (1e-15), AA02786 (1e-14), AA02550 (2e-14), AA01684 (1e-13), AA02609 (6e-13), AA02484 (6e-13), AA01510 (2e-12), AA01961 (5e-12), AA01456 (6e-12), AA01568 (1e-11), AA00933 (4e-11), AA00751 (2e-10), AA02606 (2e-10), AA00207 (1e-09), AA01393 (3e-09), AA02573 (4e-09), AA02225 (4e-09), AA01569 (2e-08), AA02642 (9e-08), AA00591 (1e-06), A02145 (2e-06), AA00934 (7e-06), AA02146 (1e-04), AA01291 (1e-04) and AA01555 (5e-04).","","","","","","Residues 31 to 218 (E-value = 1.6e-53) place AA02324 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Higgins CF, Hyde SC, Mimmack MM, Gileadi U, Gill DR, Gallagher MP Binding protein-dependent transport systems. J Bioenerg Biomembr 1990 Aug;22(4):571-92 PMID: 2229036 Higgins CF, Gallagher MP, Mimmack ML, Pearce SR.A family of closely related ATP-binding subunits from prokaryotic and eukaryotic cells.Bioessays 1988 Apr;8(4):111-6PMID: 3288195 Higgins CF, Hiles ID, Salmond GP, Gill DR, Downie JA, Evans IJ, Holland IB, Gray L, Buckel SD, Bell AW, et al.A family of related ATP-binding subunits coupled to many distinct biological processes in bacteria.Nature 1986 Oct 2-8;323(6087):448-50PMID: 3762694","","Mon Jan 6 10:38:56 2003","1","","","" "AA02325","1587449","1588231","783","ATGCTAACCAATTTAATTTCAGCCCTCGGACGTAACGCTATTAACTTTGCCCGCGCAATGGGTCGTGCAGGCTTTTTGCTATTCGGCGCGCTTATCGGCAAACCGCAAATTAACAAGCATTTCCCGTTATTAATCAAACAACTCCATGTCCTCGGCGTGCAGTCTTTATTGATTATCATGCTATCCGGTTTGTTTATCGGCATGGTGTTAGGTTTGCAAGGCTATGTGGTATTGGTGGATTTCTCGGCAGAAACCAGCTTAGGGCAACTCGTAGCATTATCGCTGCTGCGCGAATTAGGTCCGGTAGTGACCGCACTTTTATTCGCCGGACGCGCCGGTTCCGCATTAACTGCCGAAATCGGCTTAATGAAAGCCACGGAACAATTATCCAGTTTGGAAATGATGGCGGTGGATCCGCTACGTCGGGTTATCGCCCCGCGTTTTTGGGCGGGAGTGATTGCCATGCCGATTCTTTCCATTATTTTTATCGCCATCGGCATTTGGGGCGGTTCCTTAGTGGGCGTGGATTGGAAAGGCGTGGATTCGGGCAGTTTCTGGTCGGTCATGCAAAGCTCTGTTACCTGGAGCCACGATATTCTTAACGGTTTTATTAAAAGCCTGTTCTTCGCCATTGCGGTGGTTTGGATTGCATTGTTTAACGGCTACGACTGTATTCCGACTTCGGAAGGCATCAGCAAAGCCACCACCAGAACCGTTGTACACGCGTCATTAGTAGTATTAGGTTTAGACTTCGTACTGACCGCCATCATGTTCGGTGCGAAT","","","27862","MLTNLISALGRNAINFARAMGRAGFLLFGALIGKPQINKHFPLLIKQLHVLGVQSLLIIMLSGLFIGMVLGLQGYVVLVDFSAETSLGQLVALSLLRELGPVVTALLFAGRAGSALTAEIGLMKATEQLSSLEMMAVDPLRRVIAPRFWAGVIAMPILSIIFIAIGIWGGSLVGVDWKGVDSGSFWSVMQSSVTWSHDILNGFIKSLFFAIAVVWIALFNGYDCIPTSEGISKATTRTVVHASLVVLGLDFVLTAIMFGAN","1588231","","membrane protein; possible ABC transporter, permease","Inner membrane, Cytoplasm","","
InterPro
IPR003453
Domain
Protein of unknown function DUF140
PF02405\"[13-258]TDUF140
TIGR00056\"[1-260]TTIGR00056: conserved hypothetical protein
noIPR
unintegrated
unintegrated
signalp\"[1-71]?signal-peptide
tmhmm\"[15-33]?\"[52-72]?\"[148-168]?\"[199-219]?\"[240-260]?transmembrane_regions


","BeTs to 12 clades of COG0767COG name: ABC-type toluene export system, permease componentFunctional Class: RThe phylogenetic pattern of COG0767 is -------q--r--cefghsnujx---Number of proteins in this genome belonging to this COG is","Significant hit (2.5e-123) to 4/4 blocks of the IPB003453 family, which is described as \"Domain of unknown function DUF140\". Interpro entry for IP:IPR003453. IPB003453A 18-67 1.6e-23 IPB003453B 83-126 6.8e-34 IPB003453C 143-187 1.7e-32 IPB003453D 191-239 3.4e-30","Residues 18 to 146 match (3e-42) PD:PD004289 which is described as COMPLETE PROTEOME ABC MEMBRANE PERMEASE TRANSMEMBRANE PROBABLE TRANSPORTER TOLUENE TOLERANCE ","","","","","","","","","","","","Tue Mar 16 16:34:28 2004","","","Tue Mar 16 16:34:28 2004","Tue Mar 16 16:16:06 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02325 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Tue Mar 16 16:16:06 2004","","","","","Residues 13 to 258 (E-value = 1.9e-125) place AA02325 in the DUF140 family which is described as Domain of unknown function DUF140 (PF02405)","Tue Mar 16 16:16:06 2004","","","","","","","1","","","" "AA02326","1588257","1588763","507","ATGCGACAAACAATTAAATATGAATTTTGGGTCGGTTTATTTTTACTCCTTGGTATCGGCTCGCTTATCTTCTTAGGCTTAAAAGTGGCGAACGTGCAAGGTTTCAGTGAAGCAAAATCTTATCACGTTTATGCAACTTTCGATAATATCGGTGGACTAAAAGTACGCGCCCCGCTTAAAGTGGGCGGCGTTGTGATTGGGCGGGTATCCGAAATCACATTGGATCCGCAAACGTATTTACCGAAAGTCACCATCGCCATTAATCAGGAATACAATGAAATTCCGGAAACCAGTTCGTTATCCATCAAAACCTCCGGTTTATTGGGCGAACAATACATTGCGCTAAGCATCGGTTTTAATGACGGCGAAATTGCGATGTTGAAAGATGGCGACAAAATTGTCGATACCAAATCCGCCATAGTGCTGGAAGATCTGATCGGACAATTTTTATACGGTGACAAAGACAAAAAGGCGGCAGAGGAAACAAACGATGCCACAGAAAGTAAT","","","18422","MRQTIKYEFWVGLFLLLGIGSLIFLGLKVANVQGFSEAKSYHVYATFDNIGGLKVRAPLKVGGVVIGRVSEITLDPQTYLPKVTIAINQEYNEIPETSSLSIKTSGLLGEQYIALSIGFNDGEIAMLKDGDKIVDTKSAIVLEDLIGQFLYGDKDKKAAEETNDATESN","1588763","","conserved hypothetical protein; possible ABC transporter","Outer membrane, Cytoplasm","","
InterPro
IPR003399
Domain
Mammalian cell entry related
PF02470\"[39-118]TMCE
noIPR
unintegrated
unintegrated
signalp\"[1-30]?signal-peptide
tmhmm\"[9-27]?transmembrane_regions


","BeTs to 10 clades of COG1463COG name: Permease component of an ABC-transporterFunctional Class: RThe phylogenetic pattern of COG1463 is -------q--r--cefghsnujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 8.7e-47) to 4/4 blocks of the IPB003399 family, which is described as \"mce related protein\". Interpro entry for IP:IPR003399. IPB003399A 9-19 0.18 IPB003399B 40-84 6.6e-17 IPB003399C 89-119 3e-12 IPB003399D 120-154 1.1e-11 IPB003399A 15-25 0.83","Residues 38 to 115 match (2e-08) PD:PD035621 which is described as PROTEOME COMPLETE ABC SECRETED VIRULENCE BINDING PERIPLASMIC FAMILY SUBSTRATE-BINDING MCE ","","","","","","","","","","","","Mon Jan 6 10:55:57 2003","","","Tue Mar 16 16:36:01 2004","Tue Mar 16 16:36:01 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02326 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Tue Mar 16 16:36:01 2004","","","","","Residues 11 to 156 (E-value = 1e-40) place AA02326 in the MCE family which is described as mce related protein (PF02470)","Tue Mar 16 16:36:01 2004","","","","","","","1","","","" "AA02327","1588795","1589433","639","ATGTTAAAAATCAAGTTTAAAAACTGGTTAACAAAAACGCTGGTAATTTTCACCGCACTTTTTGCGATGCAACAGGTCATGGCGGAAGATAACCCGCAAACCTTAACACAACAGGTTTCCGATAAATTATTCAGCGACATTAAAGCGAATCAAAGCCGAATCAAACAGGATCCGAACTATTTAAAAACCATCGTACGTCAGGATTTAATGCCGTATGTGCATGTTAAATATGCCGGTTCAAAAATTTTAGGACAAAACTACAAAACTGTCACTCAGGAAGAACGCGAACGTTATTTCGCTGTATTGGATAAGTACATTGAGCAAGTGTATGCGCAAGTATTAACGCTCTATACCGACCAAAACATTCAAGTCGGCAAAATGAAAGAAGAATCCGGCAGCCTTGCCATCGTGAACGTAAAAGTGGCACAACCAAATAATCAACCGCCGTTAAATGTGGATTTTTACTGGTATAAAAACAGCAAAACCGGGCAATGGCAAGTGTATGACATGACCGCCGGCGGCGCCAGCATGGTCAATACCAAACAGCAGGAATGGAGCCCGATTATCCGTAAACAAGGCTTGGATGCGTTGACCGCAAAATTACAAAAATCTGCCGACACTCCAATTACGTTGAGTAAA","","","27647","MLKIKFKNWLTKTLVIFTALFAMQQVMAEDNPQTLTQQVSDKLFSDIKANQSRIKQDPNYLKTIVRQDLMPYVHVKYAGSKILGQNYKTVTQEERERYFAVLDKYIEQVYAQVLTLYTDQNIQVGKMKEESGSLAIVNVKVAQPNNQPPLNVDFYWYKNSKTGQWQVYDMTAGGASMVNTKQQEWSPIIRKQGLDALTAKLQKSADTPITLSK","1589433","From InterPro: IPR008869Toluene tolerance.Toluene tolerance is mediated by increased cell membrane rigidity resulting from changes in fatty acid and phospholipid compositions, exclusion of toluene from the cell membrane, and removal of intracellular toluene by degradation. Many proteins are involved in these processes. This family is a transporter which shows similarity to ABC transporters. ","possible ABC-type transport system","Periplasm, Extracellular","","
InterPro
IPR008869
Family
Toluene tolerance
PF05494\"[27-205]TTol_Tol_Ttg2
noIPR
unintegrated
unintegrated
signalp\"[1-28]?signal-peptide


","BeTs to 8 clades of COG2854COG name: ABC-type exporter of toluene and related compounds, periplasmic componentFunctional Class: NThe phylogenetic pattern of COG2854 is --------------efghsnujx---Number of proteins in this genome belonging to this COG is","","Residues 38 to 202 match (3e-52) PD:PD037359 which is described as COMPLETE PROTEOME SIGNAL EXPORTED PERIPLASMIC PRECURSOR TOLERANCE TOLUENE YRBC ATP&MEMB ","","","","","","","","","","","Tue Mar 16 16:29:45 2004","Tue Mar 16 16:31:14 2004","","","","Tue Mar 16 16:29:45 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02327 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Tue Mar 16 16:29:45 2004","","","","","Residues 27 to 205 (E-value = 1.7e-78) place AA02327 in the Tol_Tol_Ttg2 family which is described as Toluene tolerance, Ttg2 (PF05494)","Tue Mar 16 16:29:45 2004","","","","Kim K, Lee S, Lee K, Lim D.Isolation and characterization of toluene-sensitive mutants from the toluene-resistant bacterium Pseudomonas putida GM73.J Bacteriol. 1998 Jul;180(14):3692-6.PMID: 9658016Ramos JL, Duque E, Rodrguez-Herva JJ, Godoy P, Hadour A, Reyes F, Fernndez-Barrero A.Mechanisms for solvent tolerance in bacteria.J Biol Chem. 1997 Feb;272(7):3887-90.PMID: 9020089","","Tue Mar 16 16:31:14 2004","1","","","" "AA02328","1589440","1589796","357","ATGCAAGCAACACAAAGTTTACATTGGGAATCAAACCAACATGATGATAAGATAACGCTTCGCCTGAAAGGGGAGCTATCTCGAAACACGTTGTTGCCGCTTTGGCAGCAACGTGCTTCTTTTTTATTGGCACGGAAAACGGAAACGCTTGATGTTCATTGGGATTTGTCCCAAGTCAATCGCATTGATTCCGCAGGGTTTGCGTTGTTATGCGATTTTCTGCAACATAATCAAACCTTATTAACAAACGAACGGAAACAACTTTTGCAAAATCCGCCGTCCCAATTATTGACACTCGCAGATCTGTTTGGTTTATCGGACTGGATTGCGCAATTTAGCAAAACCGATGGAAATAGT","","","13670","MQATQSLHWESNQHDDKITLRLKGELSRNTLLPLWQQRASFLLARKTETLDVHWDLSQVNRIDSAGFALLCDFLQHNQTLLTNERKQLLQNPPSQLLTLADLFGLSDWIAQFSKTDGNS","1589796","From PF01740:STAS domainThis protein belongs to the STAS family which is described as STAS domain. The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is found in the C terminal region of Sulphatetransporters and bacterial antisigma factor antagonists. It has been suggested that this domain may have a general NTP binding function.","anti-sigma factor B antagonist","Cytoplasm, Extracellular","","
InterPro
IPR002645
Domain
Sulfate transporter/antisigma-factor antagonist STAS
G3DSA:3.30.750.24\"[4-118]Tno description
PF01740\"[8-118]TSTAS
PS50801\"[7-119]TSTAS


","BeTs to 5 clades of COG3113COG name: STAS domain proteinFunctional Class: RThe phylogenetic pattern of COG3113 is --------------e-ghsn------Number of proteins in this genome belonging to this COG is","","Residues 6 to 105 match (3e-27) PD:PD080833 which is described as PROTEOME COMPLETE FACTOR ANTI-SIGMA YRBB B ANTAGONIST STAS PM0178 DOMAIN ","","","","","","","","","","","Fri Jan 10 11:07:23 2003","Fri Jan 10 10:56:46 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02328 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 118 (E-value = 4e-05) place AA02328 in the STAS family which is described as STAS domain (PF01740)","","","","","Aravind L, Koonin EVThe STAS domain - a link between anion transporters and antisigma-factor antagonists.Curr Biol 2000 Jan 27;10(2):R53-5PMID: 10662676","","Fri Jan 10 11:00:49 2003","1","","","" "AA02329","1589799","1590053","255","ATGGAAACTCAAGAAATCGAAAAAATCTTAAAAGAAGCACTGAATCTTGATGAGGTGTATGTACAGGGTGAAGACGCACATTACGGTGTAATCGCTGTGAGCGATCAATTTGAAGGGCTTTCTAAAGTCAAGCAGCAACAAATGATTTATGCTCCGCTCTTAAACCACATTTCCAGAAATGAAATTCATGCGCTTTCCATCCGTACTTATACCGTCGAAAAATGGAAACGTGAACGTTTACTTAATCAACCCGCC","","","9893","METQEIEKILKEALNLDEVYVQGEDAHYGVIAVSDQFEGLSKVKQQQMIYAPLLNHISRNEIHALSIRTYTVEKWKRERLLNQPA","1590053","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR002634
Family
BolA-like protein
PTHR12735\"[23-79]TBOLA-LIKE PROTEIN-RELATED
PF01722\"[1-75]TBolA
noIPR
unintegrated
unintegrated
G3DSA:3.30.300.90\"[1-81]Tno description


","BeTs to 10 clades of COG0271COG name: Stress-induced morphogen (activity unknown)Functional Class: TThe phylogenetic pattern of COG0271 is -o----y------cefghsn-jx---Number of proteins in this genome belonging to this COG is","Significant hit ( 8.3e-25) to 2/2 blocks of the IPB002634 family, which is described as \"BolA-like protein\". Interpro entry for IP:IPR002634. IPB002634A 23-57 2.4e-16 IPB002634B 62-75 6.1e-07","Residues 1 to 73 match (4e-25) PD:PD004789 which is described as COMPLETE PROTEOME BOLA FAMILY TRANSCRIPTION BOLA/YRBA ACTIVATOR HOMOLOG REGULATOR REGULATION ","","","","","","","","","","","","Mon Jan 6 13:41:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02329 is paralogously related to AA01039 (4e-09).","","","","","","Residues 1 to 75 (E-value = 6.5e-31) place AA02329 in the BolA family which is described as BolA-like protein (PF01722)","","","","","","","","1","","","" "AA02330","1590073","1591341","1269","ATGCAAAAATTTCGAGTTTACGGACAATCTTGTTTAAAAGGAACCGTGGAGATTTCCGGTGCGAAAAATGCGGCATTGCCGATTTTATTTGCCGCAATTTTAGCAACGGAACCGGTCACCTTAACTAATGTGCCGGATCTAAAAGATATCGAAACCACGCTGAAAATTTTACGTCAGTTAGGTGTAGTCGTAGAACAAAATGAACCCGGTACGGTTCGTTTAGATGCCTCTAAAATCGATCATTTCATCGCGCCGTACGAGTTGGTGAAAACCATGCGCGCTTCCATTTGGGCATTGGCACCACTAGTTGCACGTTTCAATCAAGGTCAGGTTTCCTTACCGGGAGGTTGCTCTATCGGCGCCCGACCGGTAGATTTGCACATTAGCGGCTTAGAACGCCTTGGCGCAAAAATCGCCCTTGAAGACGGTTATGTAAAAGCCTATGTGGATGGACGCCTAAACGGCACCCGTATCGTGATGGAAAAAGTGAGCGTGGGCGCCACCCTCTCCATTATGATTGCGGCGACTTTGGCAAAAGGCACCACCGTTATCGAAAACGCCGCCCGTGAACCGGAAATTGCCGACACGGCGGAATTCTTAAATAAAATGGGCGCCAAAATCAGCGGTGCAGGTTCTGATGCCATCACGATCGAAGGCGTAAATCGCTTAACCGGTTGTGAGCATAGCATCGTGCCGGATCGCATTGAAACCGGGACATTCTTAGTGGCAGCCGCCATTTCCGGCGGTCGCATTGTATGTAAAAACACCAAAGCCAACACCTTAGACGCGGTGATCGATAAATTACGCGAAGCTGGCGCGCAGGTGGATGTCACCGAAGATACCATCACGTTAGATATGTGGGGCAATCGTCCGAAAGCGGTGAATATTCGTACCGCACCTTACCCGGGCTTCCCGACCGATATGCAGGCGCAATTCACCTTATTAAACATGGTTGCTAACGGCACCAGCATCATCACCGAAACCATTTTTGAAAATCGCTTCATGCACATTCCAGAGCTGATTCGTATGGGCGGTAAAGCAGAAATTGAAGGCAACACCGCCATTTGCCATGGGGTTTCCCATTTATCCGGTGCAGAAGTCATGGCAACGGATCTGCGCGCTTCTATCAGCTTAGTGCTGGCAGGCTGTATCGCCACCGGTGAAACCATTGTGGATCGTATCTACCATATCGACCGCGGCTATGAACATATTGAAGAAAAGCTCCGCGGCTTAGGCGCTCGTATTGAACGTTTTTCGGAAGAAATAGAA","","","45452","MQKFRVYGQSCLKGTVEISGAKNAALPILFAAILATEPVTLTNVPDLKDIETTLKILRQLGVVVEQNEPGTVRLDASKIDHFIAPYELVKTMRASIWALAPLVARFNQGQVSLPGGCSIGARPVDLHISGLERLGAKIALEDGYVKAYVDGRLNGTRIVMEKVSVGATLSIMIAATLAKGTTVIENAAREPEIADTAEFLNKMGAKISGAGSDAITIEGVNRLTGCEHSIVPDRIETGTFLVAAAISGGRIVCKNTKANTLDAVIDKLREAGAQVDVTEDTITLDMWGNRPKAVNIRTAPYPGFPTDMQAQFTLLNMVANGTSIITETIFENRFMHIPELIRMGGKAEIEGNTAICHGVSHLSGAEVMATDLRASISLVLAGCIATGETIVDRIYHIDRGYEHIEEKLRGLGARIERFSEEIE","1591341","From Genbank:[gi:13431690] This protein is involved in cell wall formation. It adds enolpyruvyl to UDP-N-Acetylglucosamine.","UDP-N-acetylglucosamine enolpyruvyl transferase","Cytoplasm","","
InterPro
IPR001986
Domain
3-phosphoshikimate 1-carboxyvinyltransferase
PD001867\"[12-413]TMURA_PASMU_P57821;
G3DSA:3.65.10.10\"[21-230]T\"[261-369]Tno description
PF00275\"[6-408]TEPSP_synthase
InterPro
IPR005750
Family
UDP-N-acetylglucosamine 1-carboxyvinyltransferase
PTHR21090:SF4\"[73-418]TUDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE
TIGR01072\"[1-417]TmurA: UDP-N-acetylglucosamine 1-carboxyviny
noIPR
unintegrated
unintegrated
PTHR21090\"[73-418]TAROM/DEHYDROQUINATE SYNTHASE
signalp\"[1-36]?signal-peptide


","BeTs to 17 clades of COG0766COG name: UDP-N-acetylglucosamine enolpyruvyl transferaseFunctional Class: MThe phylogenetic pattern of COG0766 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 5.3e-07) to 3/9 blocks of the IPB001986 family, which is described as \"EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase)\". Interpro entry for IP:IPR001986. IPB001986A 14-54 0.0029 IPB001986C 112-138 0.36 IPB001986H 234-286 1.4e+02","Residues 1 to 413 match (4e-198) PD:PD001867 which is described as TRANSFERASE 1-CARBOXYVINYLTRANSFERASE SYNTHASE COMPLETE PROTEOME UDP-N-ACETYLGLUCOSAMINE 3-PHOSPHOSHIKIMATE EPSP BIOSYNTHESIS ACID ","","","","","","","","","","","Mon Jan 6 14:17:56 2003","Mon Jan 6 14:00:03 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02330 is paralogously related to AA02758 (2e-05).","","","","","","Residues 8 to 408 (E-value = 2.1e-177) place AA02330 in the EPSP_synthase family which is described as EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase) (PF00275)","","","","","Griffiths E, Gupta RS. Protein signatures distinctive of chlamydial species: horizontal transfers of cell wall biosynthesis genes glmU from archaea to chlamydiae and murA between chlamydiae and Streptomyces. Microbiology. 2002 Aug;148(Pt 8):2541-9. PMID: 12177347 Dai HJ, Parker CN, Bao JJ. Characterization and inhibition study of MurA enzyme by capillaryelectrophoresis. J Chromatogr B Analyt Technol Biomed Life Sci. 2002 Jan 5;766(1):123-32. PMID: 11820287 Marquardt,J.L., Siegele,D.A., Kolter,R. and Walsh,C.T. Cloning and sequencing of Escherichia coli murZ and purification of its product, a UDP-N-acetylglucosamine enolpyruvyl transferase J. Bacteriol. 174 (17), 5748-5752 (1992) PubMed: 1512209 Skarzynski,T., Mistry,A., Wonacott,A., Hutchinson,S.E., Kelly,V.A. and Duncan,K. Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin Structure 4 (12), 1465-1474 (1996) PubMed: 8994972","","Mon Jan 6 14:15:08 2003","1","","","" "AA02331","1592095","1593039","945","ATGCTATTTTCTGGAATTCATGCCTCTATTGCGGCTTTAGAACAAATACTAATTTTATGGGTTGGTGAAACCCTAGTAATTGAAAATACAATGACATTGGGTATGTATGTTGCTTTTAATTCTTACCGAGGTTTATTTTCTTCACGTATGACAAACCTAATTAATATTTTCTTCAATATAAGAATTTTAGCTCTGTATAGAGAACGAATTGCAGATATAGCACTAAATGAAGCAGAAGAAGATACTTATCAGAATTTGACGAATATACCTAAAAAAGTAGCAACACTCGAACTAAAGAATCTTACATTCTCTTATAATCAATTTGATAAACCGATAATAAAAGATATTAGTTTAATCATTCCTGCAGGTAAAAGTGTAGCTATTAAAGCGCCATCAGGCTTTGGAAAAACAACATTACTTAAGTTGATGTCAGGTTTATTAAAGTCTACATCAGGAGAAGTTTATTTTGATGGTATAAATATTAATCAGATTGGATTACCAAATTATCGTTCAAAAATTGCTATGGTTTTACAAGAGGATAAATTCTTTTCAGGCTCAATAATTGAGAATATTGTCAGCTTTGAAGATCAATATGATCTGGAATTTGCTATTAAGTGTGCAAAATTAGCTAAGATTCATAATGAAATTATGAAAATGCCAATGAATTACGAAACTCGTTTAGGAGAACTAGGAAATAACCTTTCCGGGGGCCAACGCCAAAGGTTATTTATCGCTCGTGCTCTATACAAAAGACCATATATTTTATTTATGGATGAAGCGACTAGCTACTTAGATGAGAAAAATGAAAAAGCAATTAACATCTCAATTTCCCAGTTAAATATTACTCGGGTTATAGTAGCTCACAGGCAATCTACTATTGACTCAGCAGACTATTGTGTTGAGCTAGATAAACTAAATAAAAATTCAAAATACACTATAAATCTA","","","35689","MLFSGIHASIAALEQILILWVGETLVIENTMTLGMYVAFNSYRGLFSSRMTNLINIFFNIRILALYRERIADIALNEAEEDTYQNLTNIPKKVATLELKNLTFSYNQFDKPIIKDISLIIPAGKSVAIKAPSGFGKTTLLKLMSGLLKSTSGEVYFDGININQIGLPNYRSKIAMVLQEDKFFSGSIIENIVSFEDQYDLEFAIKCAKLAKIHNEIMKMPMNYETRLGELGNNLSGGQRQRLFIARALYKRPYILFMDEATSYLDEKNEKAINISISQLNITRVIVAHRQSTIDSADYCVELDKLNKNSKYTINL","1593039","From Genbank:[gi:126357] This protein is involved in the export of leukotoxin.","ABC transporter, ATP-binding protein; possible leukotoxin secretion ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[234-273]TQ9LAL5_MORCA_Q9LAL5;
PF00005\"[123-305]TABC_tran
PS50893\"[96-315]TABC_TRANSPORTER_2
PS00211\"[234-248]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[122-308]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[61-304]Tno description
PTHR19242\"[1-303]TATP-BINDING CASSETTE TRANSPORTER
PTHR19242:SF58\"[1-303]TCOLICIN V SECRETION ABC TRANSPORTER
signalp\"[1-24]?signal-peptide


","No hits to the COGs database.","Significant hit ( 4.3e-40) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 112-158 3.6e-16 IPB001140B 231-269 1.5e-19 IPB001140C 282-311 0.17","Residues 1 to 39 match (1e-07) PD:PD167059 which is described as ATP-BINDING SECRETION CVAB BACTERIOCIN TRANSMEMBRANE PLASMID V MICROCIN H47 PROBABLE ","","","","","","","","","","","Mon Jan 6 15:00:10 2003","Mon Jan 6 15:02:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02331 is paralogously related to AA02805 (1e-40), AA01961 (2e-37), AA01510 (2e-31), AA01393 (4e-25), AA01509 (3e-24), AA02718 (2e-19), AA02609 (5e-19), AA01645 (2e-18), AA00700 (2e-18), AA02440 (5e-18), AA02606 (5e-17), AA01656 (6e-17), AA02324 (8e-17), AA00415 (2e-16), AA01867 (5e-16), AA00591 (5e-16), AA01616 (1e-15), AA01422 (1e-15), AA02353 (3e-15), AA02573 (2e-14), AA00799 (3e-14), AA02320 (8e-14), AA00858 (2e-13), AA01456 (1e-12), AA02080 (2e-12), AA01524 (3e-12), AA02550 (4e-12), AA01051 (2e-11), AA02140 (4e-11), AA01820 (4e-11), AA00207 (8e-11), AA01568 (1e-10), AA02899 (1e-10), AA02484 (1e-10), AA02898 (2e-10), AA00933 (9e-10), AA00751 (1e-09), AA02152 (2e-09), AA01757 (2e-09), AA01684 (4e-09), AA02786 (5e-09), AA01824 (6e-09), AA01555 (6e-09), AA01779 (1e-08), AA01947 (4e-08), A02145 (3e-07), AA02225 (4e-07), AA02642 (1e-06), AA00061 (4e-06) and AA01291 (3e-05).","","","","","","Residues 123 to 305 (E-value = 3.5e-43) place AA02331 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","Guthmiller JM, Kolodrubetz D, Kraig E. Mutational analysis of the putative leukotoxin transport genes inActinobacillus actinomycetemcomitans. Microb Pathog. 1995 May;18(5):307-21. PMID: 7476096 Spitznagel J Jr, Kraig E, Kolodrubetz D. Regulation of leukotoxin in leukotoxic and nonleukotoxic strains of Actinobacillus actinomycetemcomitans. Infect Immun. 1991 Apr;59(4):1394-401. PMID: 2004819 Guthmiller JM, Kolodrubetz D, Cagle MP, Kraig E. Sequence of the lktB gene from Actinobacillus actinomycetemcomitans. Nucleic Acids Res. 1990 Sep 11;18(17):5291. PMID: 2402457","Gilson L, Mahanty HK, Kolter R.Genetic analysis of an MDR-like export system: the secretion of colicin V.EMBO J 1990 Dec;9(12):3875-94PMID: 2249654Davies RL, Campbell S, Whittam TS. Mosaic structure and molecular evolution of the leukotoxin operon(lktCABD) in Mannheimia (Pasteurella) haemolytica, Mannheimia glucosida, and Pasteurella trehalosi. J Bacteriol. 2002 Jan;184(1):266-77. PMID: 11741868 Schmitt L. The first view of an ABC transporter: the X-ray crystal structure of MsbA from E. coli. Chembiochem. 2002 Mar 1;3(2-3):161-5.PMID: 11921393 Chang G, Roth CB.Structure of MsbA from E. coli: a homolog of themultidrug resistance ATP binding cassette (ABC) transporters. Science. 2001 Sep 7;293(5536):1793-800. PMID: 11546864 Dobrindt,U., Blum-Oehler,G., Hartsch,T., Gottschalk,G., Ron,E.Z., Funfstuck,R. and Hacker,J. S-Fimbria-encoding determinant sfa(I) is located on pathogenicity island III(536) of uropathogenic Escherichia coli strain 536 Infect. Immun. 69 (7), 4248-4256 (2001) PubMed: 11401961 ","Mon Jan 6 14:57:53 2003","Mon Jan 6 14:58:23 2003","1","","","" "AA02332","1594452","1593391","1062","ATGCGTAGTCTTATTGAACGTTATTTATATAGTCCTCTTATATCTAGTATGGAAGGAGGGCTATCTTCGGTCTCTACCAAAAAAGAAGGGCTTTCAGTATGTATTATAGTAAGGAATGAGGAAAAATGTATCTTAAGGTGTATACAAAGTGTTGTTGATATTTCTGATGAGATTGTTGTTGTAGACTCAGGATCTACTGACAACACTGTAGATATAGTCAGGGAAATAAAATCCGGTAACATAGTGCTTAAGTACAAAGGTTGGAATTCTAATTTTTCTGAATTAAGAAATTTTGCTCTGGAATGTTCTGGCTATTCGTGGGTATTTTTTATAGATGCTGATGAGTGGGTTGATGGCAGAGCGTACAGAGACCTTCGATACTTTCTTATTATGTATGGTAGATGCAACGACGCAACAGTTTTTTGCCCTAGGTTTTTGGATTCTAAAAATAATAAAAATTATGGTGTTGGGAGAATATTCAAAAATAATGGACTCATTAAATACAATGGAAGAGTGCATGAATACCCATATTCTAAAAATAACATAGTTAATATACCTATAAAAATTGATAGAAATATAAGGCTATTAGAGATAAATCAAATAGAGGATCCTTATAATATAAGATGGAAGTTTTTTCTCGCTAGGGATAATTTTAATTATAAAAAAGATGTTTCTTTTTTGATTGATTTTTTGGATTTTTTTTATTCATTTAATTTCCCTGATACAGGGTATTTTAAACGGGCATATATTATGCTTATTTTTAATTTTTTAGAAGACGGGCGTGTAGATAAAGCTATTGGGCTTATAGAAAGATATGATCATTTTATAGATGATAAAAGTATAAATTTTTATTTTGTTAAAAAAATATCTCTAATTAAGTTATCTTTAGGGACCGTTTCATTGTTGGATAATGTTATTAACGAGTCAAATAAGGTTAAAAATTCATTTTTGGATAATGAATTATATAGGTTTTCATCAATAAAATCTGAAGGGAGGCATTTAGATGAAATTATCATGTTTGCTAACGAATTAAGAGACTTTTTTAAATTTAATTTTGGTTTT","","","41581","MRSLIERYLYSPLISSMEGGLSSVSTKKEGLSVCIIVRNEEKCILRCIQSVVDISDEIVVVDSGSTDNTVDIVREIKSGNIVLKYKGWNSNFSELRNFALECSGYSWVFFIDADEWVDGRAYRDLRYFLIMYGRCNDATVFCPRFLDSKNNKNYGVGRIFKNNGLIKYNGRVHEYPYSKNNIVNIPIKIDRNIRLLEINQIEDPYNIRWKFFLARDNFNYKKDVSFLIDFLDFFYSFNFPDTGYFKRAYIMLIFNFLEDGRVDKAIGLIERYDHFIDDKSINFYFVKKISLIKLSLGTVSLLDNVINESNKVKNSFLDNELYRFSSIKSEGRHLDEIIMFANELRDFFKFNFGF","1593391","","conserved hypothetical protein; possible glycosyltransferase","Cytoplasm","","
InterPro
IPR001173
Domain
Glycosyl transferase, family 2
PF00535\"[32-117]TGlycos_transf_2
InterPro
IPR001969
Active_site
Peptidase aspartic, active site
PS00141\"[59-70]?ASP_PROTEASE
noIPR
unintegrated
unintegrated
G3DSA:3.90.550.10\"[31-118]Tno description
PTHR22916\"[37-354]TGLYCOSYLTRANSFERASE


","BeTs to 12 clades of COG0463COG name: Glycosyltransferases involved in cell wall biogenesisFunctional Class: MThe phylogenetic pattern of COG0463 is aompkzyqvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Mon Jan 6 15:24:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02332 is paralogously related to AA01402 (2e-07).","","","","","","Residues 32 to 192 (E-value = 3.1e-18) place AA02332 in the Glycos_transf_2 family which is described as Glycosyl transferase (PF00535)","","","","","","","","1","","","" "AA02333","1595244","1594957","288","ATGAGCACATTGAAATGTCAGGCGGAAGAAGCAAAAGTTTGCTGTTGTGTCGAGGTGGGTACGGTGATTGACGGTTCTGACTGCACGGTGGATTTTGAACAGGTTTATGCAACGGAAGAAGCAGCAAAAGAAGCATTAAGCTGTTTAACCGAAAAAGCCAAAGCGGCGGAAAGTGATCCATGCAAAATCAGTAGTGAAATAAGTGTGGTGGAAAATGGCTTCAAATTAACTGCCAAATTTGAATTTAGCTGCCAGGCGGAATCCATGATTTTCCAACTTTCTACCCGT","","","10375","MSTLKCQAEEAKVCCCVEVGTVIDGSDCTVDFEQVYATEEAAKEALSCLTEKAKAAESDPCKISSEISVVENGFKLTAKFEFSCQAESMIFQLSTR","1594957","","conserved hypothetical protein","Cytoplasm, Periplasm","","
InterPro
IPR005272
Family
Conserved hypothetical protein 743
PF04175\"[5-96]TDUF406
TIGR00743\"[2-96]TTIGR00743: conserved hypothetical protein


","BeTs to 3 clades of COG3691COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3691 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 5 to 96 match (4e-23) PD:PD015399 which is described as COMPLETE PROTEOME ORF CYTOPLASMIC HI0636 YPO2745 YFCZ PM1070 STY2622 HI0400 ","","","","","","","","","","","","Mon Jan 6 15:25:42 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02333 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 96 (E-value = 1.8e-50) place AA02333 in the DUF406 family which is described as Protein of unknown function (DUF406) (PF04175)","","","","","","","","1","","","" "AA02334","1595447","1596874","1428","ATGACAACCCGCAAATTTACTCAAACCCTTCTATCCACGCTGTTATTAACTGCTGCCGGAGGTGCGTCCGCCGCGGCATTCCAATTAGCAGAAATTTCCACCTCCGGTTTAGGTCGTGCCTATGCCGGTGAAGCCGCCATCGCAGACAATGCTGCTGTGGTCGCCACCAACCCGGCATTAATGAGCCTGTTCAAACAAAACGAATTTTCTGCCGGTGGCGTTTATGTGGATTCGCGAATTCATATAAATGGTCCTGTAACTGCTTATATCAGAGGACAAAAAGTTGCTTCCGGAAGCGCTAATGCCCATAGCGTTGTTCCAGGTGCATTCATTCCAAATATGTATTTTATCTCACCTATCAATGATAAGTTTACTTTAGGTGCGGGAATGAATGTTAACTTTGGTTTAAAGAGTGAATATTCCCGCGATTATGATGCCGGTATTTTTGGCGGTATAACGGATTTAACCGCCATTAGTCTGAATCTTAGTGGGTCATACCGTATTACTAATAATTTAACTGCCGGTTTCGGTTTAAATGGTGTCTATGCGAAAGCAGAACTTGATCGCACTGCCGGTATCGCCATTACCGGCGTCAAAAATGCACTGAATTCTATGGGTGAGGACAATGTAAAAAGATTATTAAGCGCGAGAATAAGAGCCAAAAATCCGACAATTCCGCAGGCTATTGCTGACGGTTTAGCACAAAGAACTATCAATAATTTAAAAAATCTGGATAAAGCAGATTCGCTTGTACACCTAAGAGACAATGCTTGGGGATTCGGTTGGAATACAGGTTTGGTTTACGAGTTTGATCAAGATAATCGTCTTGGTCTCGCCTACCATTCCAAAGTCGATATTGATTTTAAAGATCGCAATGCACTCAGTTTACAACAACATAATGGTGTACTAGGTCCTTATATCGGTAAAGGCAGTTTAACCTTAAAATTACCGGCTTACTGGGAACTATCAGGATTCCATCAATTAACCGATCAATGGGCTATCCACTATAGCTATAAATATACAGAATGGAGTCGTTTTAAAGAATTACGCGGCAAATATCAAGATGGTTCCGGCTATGAGGCCTTTACCAAGAAAGAGGAATACAAAGACAACTCCCGTTTTGCTATTGGTACAACATATAGCCTAAATGATGCTTTAACATTACGTGCAGGTTTGGCTTACGATAAAGCCGCGAGTAAAACGCATTTATCTGCGTCCATTCCTGATACCGACCGTATGTGGTATAGTATAGGAGCCACCTATAAATTCACCCCGAATTTATCTGTTGATGTCGGCTTCGCTCATTTACGTGGTAAGAAGAAACATTTTGTTGAGACCCAAAATATCAAGGGGTTATTGCTTGTTGAGGCGGATTACACCACTAAAGCCACCGCTAACCTCTACGGTTTGAATCTAAATTACCGTTTC","","","51964","MTTRKFTQTLLSTLLLTAAGGASAAAFQLAEISTSGLGRAYAGEAAIADNAAVVATNPALMSLFKQNEFSAGGVYVDSRIHINGPVTAYIRGQKVASGSANAHSVVPGAFIPNMYFISPINDKFTLGAGMNVNFGLKSEYSRDYDAGIFGGITDLTAISLNLSGSYRITNNLTAGFGLNGVYAKAELDRTAGIAITGVKNALNSMGEDNVKRLLSARIRAKNPTIPQAIADGLAQRTINNLKNLDKADSLVHLRDNAWGFGWNTGLVYEFDQDNRLGLAYHSKVDIDFKDRNALSLQQHNGVLGPYIGKGSLTLKLPAYWELSGFHQLTDQWAIHYSYKYTEWSRFKELRGKYQDGSGYEAFTKKEEYKDNSRFAIGTTYSLNDALTLRAGLAYDKAASKTHLSASIPDTDRMWYSIGATYKFTPNLSVDVGFAHLRGKKKHFVETQNIKGLLLVEADYTTKATANLYGLNLNYRF","1596874","","outer membrane protein P1","Outer membrane, Extracellular","","
InterPro
IPR005017
Family
Membrane protein involved in aromatic hydrocarbon degradation
PF03349\"[15-476]TToluene_X
noIPR
unintegrated
unintegrated
signalp\"[1-24]?signal-peptide
tmhmm\"[10-30]?transmembrane_regions


","BeTs to 8 clades of COG2067COG name: Long-chain fatty acid transport proteinFunctional Class: IThe phylogenetic pattern of COG2067 is -------q------efghsnuj----Number of proteins in this genome belonging to this COG is","","Residues 257 to 421 match (2e-09) PD:PD269117 which is described as MEMBRANE TODX OUTER PLASMID FACILITATOR TBUX XYLN ","","","","","","","","","","","","Mon Jan 6 15:32:32 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02334 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 15 to 476 (E-value = 3.4e-162) place AA02334 in the Toluene_X family which is described as Outer membrane protein transport protein (OMPP1/FadL/TodX) (PF03349)","","","","","Bolduc,G.R., Bouchet,V., Jiang,R.Z., Geisselsoder,J.,Truong-Bolduc,Q.C., Rice,P.A., Pelton,S.I. and Goldstein,R.Variability of outer membrane protein P1 and its evaluation as avaccine candidate against experimental otitis media due tonontypeable Haemophilus influenzae: an unambiguous, multifacetedapproachInfect. Immun. 68 (8), 4505-4517 (2000)PubMed: 10899849Munson,R. Jr. and Grass,S. Purification, cloning, and sequence of outer membrane protein P1 of Haemophilus influenzae type b Infection and immunity. 56 (9), 2235-2242 (1988) PubMed: 2842261 Said,B., Ghosn,C.R., Vu,L. and Nunn,W.D. Nucleotide sequencing and expression of the fadL gene involved in long-chain fatty acid transport in Escherichia coli Mol. Microbiol. 2 (3), 363-370 (1988) PubMed: 2840553 Black,P.N. Primary sequence of the Escherichia coli fadL gene encoding an outer membrane protein required for long-chain fatty acid transport J. Bacteriol. 173 (2), 435-442 (1991) PubMed: 1987139 ","","Mon Jan 6 15:32:32 2003","1","","","" "AA02335","1596954","1597490","537","ATGACCGCACTTTTTTATCGTTACTACCCTTCACCTATGGGTAATTTATTAATGCTATCTGATGGCAAAAATCTCACTCATCTGGATTTTGAACTGGAGCAATTAGCACCGAATCCCAAATGGCAGGAAAAGAATGAATTACCTGTTTTTACGCAAGTATGCGCGGCACTTGACCACTACTTTAATGGAGAACCGGAAACCTTCGCGGATATTCCGCTGGCACCACGAGGCACCGAGTTTCAACAACAAATTTGGCAGGCATTGCGTCAAATCGGCTATGGACAAACTGCCAGTTACGGTGAGTTGGCAAAACGCATCAATAATCCGAAAGCGGTGCGTGCGGTAGGTGGTGCGGTGGGTAGCAACCCTATCAGCATTATCATTCCCTGCCATCGCATTTTGGGCAAAGACGGAACGCTTACCGGCTTCGGTGGCGGTTTGGTTGCCAAGCGCTTTTTGTTGCAACTGGAAAATATTTCTTATATCGACAAAGGCAAAGAGATCGTTAAACCGCGTTTTTTCAAGAAGTATCGCCAA","","","20118","MTALFYRYYPSPMGNLLMLSDGKNLTHLDFELEQLAPNPKWQEKNELPVFTQVCAALDHYFNGEPETFADIPLAPRGTEFQQQIWQALRQIGYGQTASYGELAKRINNPKAVRAVGGAVGSNPISIIIPCHRILGKDGTLTGFGGGLVAKRFLLQLENISYIDKGKEIVKPRFFKKYRQ","1597490","From Genbank:[gi:118247] This protein is involved in the repair of alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the 0-6 position to a cysteine residue in the enzyme.This is a suicide reaction: the enzyme is irreversibly inactivated.From PF02870.The major mutagenic and carcinogenic effect of methylating agents in DNA is the formation of 06-alkyguanine. The repair of DNA containing 06-alkylated guanine is carried out by the enzyme 6-0-methylguanine-DNA methyltransferase (methylated-DNA--protein-cysteine methyltransferase)(MGMT). The alkyl group at the 0-6 position is transfered to a cysteine residue in the enzyme. This is a suicide reaction since the enzyme is irreversibly inactivated and the methylated protein accumulates as a dead-end product.","6-O-methylguanine-DNA methyltransferase","Cytoplasm","","
InterPro
IPR001497
Active_site
Methylated-DNA-[protein]-cysteine S-methyltransferase, active site
PS00374\"[128-134]?MGMT
InterPro
IPR008332
Domain
Methylguanine DNA methyltransferase, ribonuclease-like
PF02870\"[3-75]TMethyltransf_1N
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[77-163]Tno description
InterPro
IPR014048
Domain
Methylated-DNA-[protein]-cysteine S-methyltransferase, DNA binding
PF01035\"[77-162]TDNA_binding_1
TIGR00589\"[78-157]Togt: methylated-DNA-[protein]-cysteine S-me
noIPR
unintegrated
unintegrated
PTHR10815\"[41-159]TMETHYLATED-DNA--PROTEIN-CYSTEINE METHYLTRANSFERASE


","BeTs to 22 clades of COG0350COG name: Methylated DNA-protein cysteine methyltransferaseFunctional Class: LThe phylogenetic pattern of COG0350 is aompkzyqv-rlb-efghsnuj-it-Number of proteins in this genome belonging to this COG is","Significant hit ( 4.7e-53) to 2/2 blocks of the IPB001497 family, which is described as \"Methylated-DNA--protein-cysteine methyltransferase\". Interpro entry for IP:IPR001497. IPB001497A 77-103 5.2e-17 IPB001497B 104-154 7e-35","Residues 1 to 75 match (7e-23) PD:PD593559 which is described as METHYLTRANSFERASE COMPLETE PROTEOME ALKYLTRANSFERASE METHYLGUANINE-DNA METHYLATED-DNA--PROTEIN-CYSTEINE DNA 6-O- TRANSFERASE DAT1 ","","","","","","","","","","","Mon Jan 6 15:55:30 2003","Mon Jan 6 15:55:30 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02335 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 77 to 162 (E-value = 2.2e-53) place AA02335 in the Methyltransf_1 family which is described as 6-O-methylguanine DNA methyltransferase, DNA binding domain (PF01035)","","","","","Potter,P.M., Wilkinson,M.C., Fitton,J., Carr,F.J., Brennand,J., Cooper,D.P. and Margison,G.P. Characterisation and nucleotide sequence of ogt, the O6-alkylguanine-DNA-alkyltransferase gene of E. coli Nucleic Acids Res. 15 (22), 9177-9193 (1987) PubMed: 2825131 Harris,L.C., Potter,P.M. and Margison,G.P. Site directed mutagenesis of two cysteine residues in the E. coli ogt O6-alkylguanine DNA alkyltransferase protein Biochem. Biophys. Res. Commun. 187 (1), 425-431 (1992) PubMed: 1520330 ","","Mon Jan 6 15:46:10 2003","1","","","" "AA02337","1597490","1598155","666","ATGATCCCGCAAACCACCGAGGCATTACTCTCCCGCGCACAGTCTATTGCCGGTCTCACCTTCGGTGAACTGGCGGCGCAATGGCATATTTCTGTGCCACCGAATTTAAAACGTGATAAAGGCTGGGTCGGTATGCTGCTTGAAACGGCGTTAGGCGCCACCGCAGGTAGTAAAGCGGAACAGGATTTCACCCATTTAGGCATTGAGCTGAAAACCCTGCCCATCAATGAACAAGGTTATCCACTGGAAACTACTTTTGTGAGTCTCGCGCCACTTATTCAAAACAGTGGCGTGAACTGGCAAAATTCCCATGTCCGCCATAAATTATCCCGCGTTCTTTGGATTCCCATTGAAGGCAGCCGCCATATTCCGCTCGCGGAGCGACATATCGGAACACCGATTTTGTGGCAACCCAACGAGCGGCAAGAAGCTCTGTTAAAACAGGATTGGGAAGAGCTGATGGATTATATCGTGCTGGGTCAATTGGATAAAATTAATGCTCGTTTAGGCGAGGTGTTACAGCTTCGCCCGAAAGCTGCCAATAGTAAGGCGCTCACCAAAGGTATTGGTAAAAATGGCGAAATTATTGACACTCTCCCCCTCGGTTTTTATTTGCGCAAAGAGTTTACCTACCAAATTTTACAACAATTTGTGCAACAAGCTATT","","","24900","MIPQTTEALLSRAQSIAGLTFGELAAQWHISVPPNLKRDKGWVGMLLETALGATAGSKAEQDFTHLGIELKTLPINEQGYPLETTFVSLAPLIQNSGVNWQNSHVRHKLSRVLWIPIEGSRHIPLAERHIGTPILWQPNERQEALLKQDWEELMDYIVLGQLDKINARLGEVLQLRPKAANSKALTKGIGKNGEIIDTLPLGFYLRKEFTYQILQQFVQQAI","1598155","From Genbank:[gi:730086]This enzyme is a sequence-specific endonuclease that cleaves unmethylated GATC sequences. It is involved in DNA mismatch repair.","DNA mismatch repair protein","Cytoplasm","","
InterPro
IPR004230
Family
DNA mismatch repair enzyme MutH
PF02976\"[50-149]TMutH
TIGR02248\"[2-218]TmutH_TIGR: DNA mismatch repair endonuclease
noIPR
unintegrated
unintegrated
G3DSA:3.40.600.10\"[3-221]Tno description


","BeTs to 3 clades of COG3066COG name: DNA mismatch repair proteinFunctional Class: LThe phylogenetic pattern of COG3066 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 3 to 214 match (3e-95) PD:PD037848 which is described as REPAIR COMPLETE PROTEOME MISMATCH DNA MUTH ENDONUCLEASE METHYL-DIRECTED HYDROLASE 3D-STRUCTURE ","","","","","","","","","","","Mon Jan 6 15:59:35 2003","Mon Jan 6 15:59:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02337 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 50 to 149 (E-value = 9e-55) place AA02337 in the MutH family which is described as DNA mismatch repair enzyme MutH (PF02976)","","","","","Ban,C. and Yang,W.Structural basis for MutH activation in E.coli mismatch repair andrelationship of MutH to restriction endonucleasesEMBO J. 17 (5), 1526-1534 (1998)PubMed: 9482749Grafstrom,R.H. and Hoess,R.H.Nucleotide sequence of the Escherichia coli mutH geneNucleic Acids Res. 15 (7), 3073-3084 (1987)PubMed: 3031619","","Mon Jan 6 15:59:35 2003","1","","","" "AA02338","1598223","1598945","723","ATGTTTGAATGGCTATTGAGTCCCGAGGCGCTAATCGCCTTATTCACCCTGACAGCACTGGAAATCGTACTGGGTATTGACAACATTGTTTTAATCAGCATTTTGGTCTCCAAACTCCCACCAAAACAACGTCAACCGGGACGTATTATCGGTTTAACCTTGGCTATGGGAACCCGCATTTTACTGCTATTGACTCTTTCTTGGATGATACACCTTACCGAACCGCTCTTTGAGTTATTCGGCAAAGGCTTTTCCGGTCGGGATTTAATTTTATTTTTTGGTGGATTATTCTTAATTATAAAAAGTACTAACGAGATTCGTGAAGCCATGACACCACACACAGAAGAAGAACATCACCAAATCAGCAAAAAAGTTAGTTTCCTCGGAGTATTAATTGAAATTGCCTTATTAGATATTGTTTTCTCGTTAGATTCTGTCATCACTGCCGTCGGCATAGTAAATCAAATCGAAATCATGGTGACCGCAATTGTCATTGCCGTTGGTATGATGATGTTCGCAGCCAAACCTATCGGCGATTTTGTTGAAAATCATCCGACATTTAAAATTTTAGCACTCGCCTTCCTGATCCTGATCGGTGTCACCTTAATTATCGAGAGCTTCAGCATCCATGTGCCGAAAGCGTATATTTACTCCGCTATGGGCTTTTCCGTATTTGTGGAAATTCTCAATACCCAAATGCGTAAACGCTTGGGCGCTAAAATT","","","27596","MFEWLLSPEALIALFTLTALEIVLGIDNIVLISILVSKLPPKQRQPGRIIGLTLAMGTRILLLLTLSWMIHLTEPLFELFGKGFSGRDLILFFGGLFLIIKSTNEIREAMTPHTEEEHHQISKKVSFLGVLIEIALLDIVFSLDSVITAVGIVNQIEIMVTAIVIAVGMMMFAAKPIGDFVENHPTFKILALAFLILIGVTLIIESFSIHVPKAYIYSAMGFSVFVEILNTQMRKRLGAKI","1598945","","conserved hypothetical protein; possible integral membrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR005496
Family
Integral membrane protein TerC
PF03741\"[13-118]TTerC
noIPR
unintegrated
unintegrated
signalp\"[1-25]?signal-peptide
tmhmm\"[10-30]?\"[51-71]?\"[77-99]?\"[127-149]?\"[155-173]?\"[188-208]?\"[214-232]?transmembrane_regions


","No hits to the COGs database.","","Residues 158 to 235 match (3e-16) PD:PD013316 which is described as COMPLETE PROTEOME MEMBRANE TRANSMEMBRANE INTEGRAL CBS DOMAIN REPEAT PLASMID INNER ","","","","","","","","","","","","Tue Jan 7 07:49:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02338 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 13 to 227 (E-value = 1.3e-91) place AA02338 in the TerC family which is described as Integral membrane protein TerC family (PF03741)","","","","","","","","1","","","" "AA02340","1599027","1599401","375","TTGAGGTGCAGATTATGTCTTACTCTTATCAATTTCGTTAAAAAACTATCAAACAGGTCACCGAGCAGGATTTTGGTATCCGTGAGGTGGCTAAATTTCATCAGATTTCTCGTTCTCAAGTCATTTATTGGAAAAGCCTTTCGTGAAAGAGGGCTTAATGGCGTAAAATCCCCTTATATAAACCCTCAACGCCCTAAAATAGTGAAGCCAAAGATGAAAAAGAAAGCGATTGAAATCCCGGAACAAACAGACTTTTCCCCAAAAGCGTTTAAAAAGCTGCAACGAGAGCTGGCATTAGCACGTGCACAGATTGCTTACCTAAAGGAGTTGGAGGCACTCGACCGTCAAAAACAGCGACAGAAAAAAGAAAATCAT","","","14727","LRCRLCLTLINFVKKLSNRSPSRILVSVRWLNFIRFLVLKSFIGKAFRERGLNGVKSPYINPQRPKIVKPKMKKKAIEIPEQTDFSPKAFKKLQRELALARAQIAYLKELEALDRQKQRQKKENH","1599401","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 11:26:13 2004","Wed Feb 25 11:23:59 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA0348 and to AA0834.AA02340 is paralogously related to AA02115 (2e-66), AA01289 (2e-66), AA01075 (2e-66), AA00008 (2e-66), AA00535 (9e-23), AA01267 (4e-18), AA00631 (1e-12), AA01404 (1e-11), AA00227 (4e-10) and AA01549 (0.001).","Wed Feb 25 11:21:31 2004","","","","","","","","","","","","","1","","","" "AA02341","1599586","1599708","123","ATGGGTTTCCATTTGAATCATAAAACGGTGTTAAAACTGATGAATGCGTTAGGTATTCATTCTATTTTACGCAAGAAAAGACATGGAAAACGAGGAAAACATCGCATATTGCCCCGAATGTGC","","","4810","MGFHLNHKTVLKLMNALGIHSILRKKRHGKRGKHRILPRMC","1599708","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 11:26:11 2004","Wed Feb 25 11:26:30 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA0945, and to AA0835.AA02341 is paralogously related to AA02116 (1e-20), AA01288 (1e-20), AA01076 (1e-20), AA00009 (1e-20), AA01444 (3e-12) and AA01268 (3e-12).","Wed Feb 25 11:19:40 2004","","","","","","","","","","","","","1","","","" "AA02342","1599705","1600211","507","GTGCTAAATCGTGATTTTACAGCGACGGCGCTCAATCAAAAATGGGTAACCGATGTCACTGAGTTTCGAGTTGGGGAAGAAAAGCTCTATTTTTCACCGTTGATGGATTTAGCGAACCGGGAAATTATTGCCTATAATTTTGCGAAACGCCCTAAGTTCTCATTGGTAAAAAGAATGCCGGAAGAAGGACTTGGCAAACTAAAACCGAGCGAATGCCCGATTATTCACAGCGACCAAGGGGTATTGTACGGCTCAGCAGAATGGGTAAAGATGTTGGAAGGCAAGGCGATACAAAGTATGAGTCGCCGAGGGAATTGCTATGATAATGCGGTGATTGAAAGCTTTTTTGCGATATTAAAATCTGAGTGTTTTTACTCACGCACTTATACTTCGATTGCCGAATTACAGGCGGAAATTGAAGAATATTTGGTGTATTACAACCAAGAACGAATTAAACTTGATTTAAAAGGATTAAGCCCGGTGCAATACCGAGCTCAATATTTAAGT","","","19548","VLNRDFTATALNQKWVTDVTEFRVGEEKLYFSPLMDLANREIIAYNFAKRPKFSLVKRMPEEGLGKLKPSECPIIHSDQGVLYGSAEWVKMLEGKAIQSMSRRGNCYDNAVIESFFAILKSECFYSRTYTSIAELQAEIEEYLVYYNQERIKLDLKGLSPVQYRAQYLS","1600211","","ISRSO11/IS150 related transposase, orfB","Cytoplasm","","
InterPro
IPR001584
Domain
Integrase, catalytic core
PF00665\"[7-165]Trve
PS50994\"[7-168]TINTEGRASE


","No hits to the COGs database.","","Residues 55 to 114 match (3e-09) PD:PD001459 which is described as TRANSPOSASE COMPLETE PROTEOME PLASMID ORFB IS629 INSERTION ELEMENT SEQUENCE FOR ","","","","","","","","","","","","Tue Jan 7 07:57:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02342 is paralogously related to AA01444 (1e-95), AA01287 (1e-95), AA01268 (1e-95), AA01077 (1e-95), AA00010 (1e-95), AA02117 (2e-89), AA00145 (2e-23) and AA02420 (4e-17).","","","","","","Residues 7 to 165 (E-value = 5.6e-31) place AA02342 in the rve family which is described as Integrase core domain (PF00665)","","","","","","","","1","","","" "AA02343","1601719","1600313","1407","ATGCCCAGCGCGATTGAGAATGTATTTAAACTCATTGAAGAAAATGACATTAAATTTGTATTACTGCGTTTTACCGATATTCAAGGCAAAGAACATGGCGTATCTCTGCCGGTGAATTTGATTGATGAAGATTTATTTGAAGACGGCAAAATGTTTGACGGTTCTTCTGTAGAAGGCTGGAAGGCGATTAATAAAGCGGATATGTTATTAATGCCGATTGCCGAAACCGCCATAGTTGACCCTTTTGCACAAATCCCGACACTTTCACTTCGTTGTAGTATTTTTGAACCGACCACTATGCAAAGCTATGACCGCGACCCGCGTTCTATCGCTATTCGTGCGGAAAACTATATGCGTTCTACCGGCGTGGCGGATCAAGTGTTCTTCGGGCCGGAGCCGGAATTCTTCTTATTTGATGACGTTCGTTTTGATGTATCTATGAACGGCAATTCTTACCAAGTAGATGATATTGAAGCCGCATGGAACAGTAACAAACGTTATGAGGACGGTAATAACGCTTATCGTCCGTTGAAAAAAAGCGGTTACTGCGCCGTGGCGCCGAATGATACGGCGCATGATATTCGTTCTGAAATGTGCTTATTAATGGAAGAAATGGGTTTGGTCATCGAAGCGCACCACCATGAAGTGGCAACTGCAGGACAAAATGAAATTGCAACCAAATTCAACAGCCTCACTTTAAAAGCAGACGAAACCCAGATTTATAAATATATCGTACGTAATGTGGCATATGAACACGGCAAAACCGCTTGTTTTATGCCGAAACCGATTACTGGTGATAACGGTTCAGGTATGCACTGCAATATGTCTTTAAGCAAAGACGGCAAAAATATTTTCCAAGGGGATAAATATGCCGGTCTTTCCGAAACGGCACTTTATTACATCGGCGGTATTATTAAACACGCCAAAGCCTTAAACGCCTTTACCAACCCAAGTACCAACTCTTATAAGCGTTTGGTACCGGGCTTTGAAGCACCGGTATTGTTGGCCTATTCCGCTAGTAACCGTTCCGCTTCCATTCGTATTCCGGCGGTGACTAGCCCTAAAGCCATTCGTATTGAAGCCCGCTTTCCTGATCCGCTTGCTAACCCGTATTTGGCATTTGCCGCATTATTAATGGCAGGTTTGGATGGTGTCATAAATAAAATTCATCCGGGTGATGCCATGGATAAAAATCTGTACGATTTACCGCCGGAAGAATTAAAAGATATTCCGGCTGTTGCAGGTTCTTTGGAAGAAGCGTTGAATGCGCTGGAGAATGATTTTGAATTCTTAACACAAAGCAATGTGTTCACCAAAGACTTTATTTATGCCTTTATCGGTATTAAACGCAAAGAAGTGGAACGTTTAAATATGACACCACACCCGGTAGAATTTGAAATGTATTAT","","","53283","MPSAIENVFKLIEENDIKFVLLRFTDIQGKEHGVSLPVNLIDEDLFEDGKMFDGSSVEGWKAINKADMLLMPIAETAIVDPFAQIPTLSLRCSIFEPTTMQSYDRDPRSIAIRAENYMRSTGVADQVFFGPEPEFFLFDDVRFDVSMNGNSYQVDDIEAAWNSNKRYEDGNNAYRPLKKSGYCAVAPNDTAHDIRSEMCLLMEEMGLVIEAHHHEVATAGQNEIATKFNSLTLKADETQIYKYIVRNVAYEHGKTACFMPKPITGDNGSGMHCNMSLSKDGKNIFQGDKYAGLSETALYYIGGIIKHAKALNAFTNPSTNSYKRLVPGFEAPVLLAYSASNRSASIRIPAVTSPKAIRIEARFPDPLANPYLAFAALLMAGLDGVINKIHPGDAMDKNLYDLPPEELKDIPAVAGSLEEALNALENDFEFLTQSNVFTKDFIYAFIGIKRKEVERLNMTPHPVEFEMYY","1600313","From PF03951:Glutamine synthetase plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine.","glutamine synthetase","Cytoplasm","","
InterPro
IPR001637
PTM
Glutamine synthetase class-I, adenylation site
PS00182\"[388-400]TGLNA_ADENYLATION
InterPro
IPR004809
Family
Glutamine synthetase type I
TIGR00653\"[6-469]TGlnA: glutamine synthetase, type I
InterPro
IPR008146
Domain
Glutamine synthetase, catalytic region
PD001057\"[113-469]TGLNA_PASMU_Q9CLP2;
PF00120\"[104-385]TGln-synt_C
PS00181\"[261-276]TGLNA_ATP
InterPro
IPR008147
Domain
Glutamine synthetase, beta-Grasp
PF03951\"[16-97]TGln-synt_N
PS00180\"[52-70]TGLNA_1
InterPro
IPR014746
Domain
Glutamine synthetase/guanido kinase, catalytic region
G3DSA:3.30.590.10\"[107-469]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.10.20.70\"[1-106]Tno description
PTHR20852\"[19-138]T\"[162-469]TGLUTAMINE SYNTHETASE
PTHR20852:SF7\"[19-138]T\"[162-469]TGLUTAMINE SYNTHETASE BACTERIA


","No hits to the COGs database.","Significant hit (3.6e-232) to 9/9 blocks of the IPB001637 family, which is described as \"Glutamine synthetase class-I adenylation site\". Interpro entry for IP:IPR001637. IPB001637A 6-37 3.5e-17 IPB001637B 46-82 1.3e-21 IPB001637C 111-143 2e-18 IPB001637D 170-221 3.4e-30 IPB001637E 241-288 6.3e-37 IPB001637F 290-320 2.7e-26 IPB001637G 321-349 5.3e-23 IPB001637H 353-406 1.4e-45 IPB001637I 460-469 0.00095Significant hit ( 1.3e-59) to 7/7 blocks of the IPB001691 family, which is described as \"Glutamine synthetase\". Interpro entry for IP:IPR001691. IPB001691A 50-62 3.3e-05 IPB001691B 128-137 8.6e-05 IPB001691C 173-184 37 IPB001691D 191-238 4.3e-23 IPB001691E 267-276 4.9e-06 IPB001691F 281-297 4.4e-05 IPB001691G 358-371 1.2e-06","Residues 7 to 103 match (4e-47) PD:PD228027 which is described as LIGASE GLUTAMINE SYNTHETASE GLUTAMATE--AMMONIA PROTEOME COMPLETE I GS FIXATION NITROGEN ","","","","","","","","","","","Mon Jan 27 14:54:54 2003","Tue Jan 7 07:59:30 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02343 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 104 to 385 (E-value = 3.6e-166) place AA02343 in the Gln-synt_C family which is described as Glutamine synthetase, catalytic domain (PF00120)","","","","","Kumada Y, Benson DR, Hillemann D, Hosted TJ, Rochefort DA, Thompson CJ, Wohlleben W, Tateno Y.Evolution of the glutamine synthetase gene, one of the oldest existing and functioning genes.Proc Natl Acad Sci U S A 1993 Apr 1;90(7):3009-13PMID: 8096645Steglitz-Morsdorf,U., Morsdorf,G. and Kaltwasser,H.Cloning, heterologous expression, and sequencing of the Proteusvulgaris glnAntrBC operon and implications of nitrogen control onheterologous urease expressionFEMS Microbiol. Lett. 106 (2), 157-164 (1993)PubMed: 8095910Gill,H.S. and Eisenberg,D.The crystal structure of phosphinothricin in the active site ofglutamine synthetase illuminates the mechanism of enzymaticinhibitionBiochemistry 40 (7), 1903-1912 (2001)PubMed: 11329256Miranda-Rios,J., Sanchez-Pescador,R., Urdea,M. and Covarrubias,A.A. 1987. The complete nucleotide sequence of the glnALG operon of Escherichia coli K12. Nucleic Acids Res. 15(6):2757-2770. PubMed: 2882477. Colombo,G. and Villafranca,J.J. 1986. Amino acid sequence of Escherichia coli glutamine synthetase deduced from the DNA nucleotide sequence. J. Biol. Chem. 261(23):10587-10591. PubMed: 2874141. Covarrubias,A.A. and Bastarrachea,F. 1983. Nucleotide sequence of the glnA control region of Escherichia coli. Mol. Gen. Genet. 190(1):171-175. PubMed: 6134228. ","","Tue Jan 7 08:10:46 2003","1","","","" "AA02344","1602106","1603956","1851","ATGACAGATCAAATCGATATTAACAAATTACGCAACATCGCAATTATCGCGCATGTTGACCATGGCAAAACCACCTTAGTGGATAAATTATTACAACAATCCGGCACACTAGAAGCCTCCCGCAGTGGCGATGCCGATGAGCGTGTCATGGATTCCAACGATTTAGAAAAAGAGCGCGGCATCACTATTTTAGCGAAAAATACTGCCATTAACTGGAATAGCTACCGTATTAACATTGTAGACACCCCGGGGCACGCGGACTTCGGTGGCGAAGTGGAACGCGTACTTTCCATGGTGGATTCCGTATTATTGATGGTGGATGCCTTCGACGGCCCGATGCCGCAAACCCGTTTTGTTACGCAAAAAGCCTTCTCCCACGGTTTAAAACCTATCGTAGTCATCAATAAAGTTGACCGCCCGGGCGCCCGCCCTGACTGGGTAGTGGATCAAGTCTTCGATTTATTCGTGAACCTTGGCGCCACCGACGAACAACTAGACTTTCCGATTATTTATACTTCCGCGTTAAACGGCGTAGCCGGCTTGGATCACGAAGATCTGGCAGCCGACATGACGCCGTTATTTGAAGCCATCGTAGAACACGTTGAACCGCCAAAAGTCGAACTCAACGCGCCGTTCCAAATGCAAATTTCACAGTTGGATTACAACAGCTACGTGGGTGTTATCGGCATCGGTCGCATTAAGCGCGGTACGGTGAAACCGAACCAAAGCGTCACCATCATCGACAGTTTCGGTAAAACCCGCAACGGTAAAATCGGGCAAGTGTTAGGGCATTTAGGCTTACAACGTTACGAAGAAGACATCGCCAGCGCCGGCGACATCGTAGCGATTACCGGTTTAGGCGAGCTAAATATTTCCGATACCATCTGCGACATCAATAATGTAGAAGCCTTGCCGGCATTAAGTGTTGATGAACCGACCGTCACCATGTTCTTCTGCGTCAACACCTCGCCGTTTTGTGGCAAAGAAGGCAAATATGTGACTTCCCGCCAAATTTTAGAGCGTTTGAACAAAGAGCTAGTACACAACGTGGCATTGCGCGTAGAAGAAACCCCTAACCCGGATGAATTCCGCGTTTCCGGTCGCGGCGAATTGCATTTATCCGTGTTAATCGAGAACATGCGGCGCGAAGGCTACGAATTAGCCGTGTCCCGCCCGAAAGTTATCTTCAAACAAGTTGATGGTCATAAACAAGAACCCTTTGAACAAGTGACGATTGACATTGAAGAACAACATCAGGGCGCGGTCATGGAAGCCCTAGGTATCCGTAAGGGCGAAGTGAAAGACATGGTTCCGGATGGCAAAGGTCGCACTCGTTTGGAATACGTGATCCCAAGCCGTGGCTTAATCGGTTTCCGTAACGAATTTATGACCATGACTTCCGGCACCGGACTGCTCTACTCCAGTTTCAGTCATTACGATGATGTAAAACCGGGCGAAATCGGGCAGCGTAAAAACGGCGTATTAATTTCCAACGCTACCGGCAAAGCCTTGGCTTATGCCTTATGGGGCTTACAAGAACGCGGCAAATTGATGATCGATCATGGTACCGAAGTCTATGAAGGGCAAATTATCGGTATTCACAGCCGCTCCAACGACTTAACCGTAAACTGCCTGCAAGGGAAAAAACTCACCAATATGCGCGCCTCCGGTAAAGATGATGCTATTGCATTAACCACACCGATTAAATTCAGTCTTGAACAAGCTATTGAATTTATTGATGACGACGAATTGGTTGAGATTACCCCGCAATCTATCCGCATTCGTAAAAAATTATTAACGGAAACGGATCGCAAACGTGCGAACAGAACCACAACCAGTACCAGCACACAT","","","70058","MTDQIDINKLRNIAIIAHVDHGKTTLVDKLLQQSGTLEASRSGDADERVMDSNDLEKERGITILAKNTAINWNSYRINIVDTPGHADFGGEVERVLSMVDSVLLMVDAFDGPMPQTRFVTQKAFSHGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLGATDEQLDFPIIYTSALNGVAGLDHEDLAADMTPLFEAIVEHVEPPKVELNAPFQMQISQLDYNSYVGVIGIGRIKRGTVKPNQSVTIIDSFGKTRNGKIGQVLGHLGLQRYEEDIASAGDIVAITGLGELNISDTICDINNVEALPALSVDEPTVTMFFCVNTSPFCGKEGKYVTSRQILERLNKELVHNVALRVEETPNPDEFRVSGRGELHLSVLIENMRREGYELAVSRPKVIFKQVDGHKQEPFEQVTIDIEEQHQGAVMEALGIRKGEVKDMVPDGKGRTRLEYVIPSRGLIGFRNEFMTMTSGTGLLYSSFSHYDDVKPGEIGQRKNGVLISNATGKALAYALWGLQERGKLMIDHGTEVYEGQIIGIHSRSNDLTVNCLQGKKLTNMRASGKDDAIALTTPIKFSLEQAIEFIDDDELVEITPQSIRIRKKLLTETDRKRANRTTTSTSTH","1603956","","GTP-binding protein, elongation factor typA/bipA","Cytoplasm","","
InterPro
IPR000640
Domain
Translation elongation factor EFG/EF2, C-terminal
G3DSA:3.30.70.240\"[405-494]Tno description
PF00679\"[402-491]TEFG_C
InterPro
IPR000795
Domain
Protein synthesis factor, GTP-binding
PR00315\"[12-25]T\"[58-66]T\"[78-88]T\"[130-139]TELONGATNFCT
PF00009\"[8-205]TGTP_EFTU
PS00301\"[51-66]TEFACTOR_GTP
InterPro
IPR004161
Domain
Translation elongation factor EFTu/EF1A, domain 2
PF03144\"[226-296]TGTP_EFTU_D2
InterPro
IPR005225
Domain
Small GTP-binding protein domain
TIGR00231\"[8-187]Tsmall_GTP: small GTP-binding protein domain
InterPro
IPR006298
Family
GTP-binding protein TypA
TIGR01394\"[10-606]TTypA_BipA: GTP-binding protein TypA
noIPR
unintegrated
unintegrated
G3DSA:2.40.30.10\"[206-306]Tno description
G3DSA:3.40.50.300\"[9-179]Tno description
PTHR23115\"[3-328]TTRANSLATION FACTOR
PTHR23115:SF14\"[3-328]TGTP-BINDING PROTEIN TYPA/BIPA


","BeTs to 13 clades of COG1217COG name: Predicted membrane GTPase involved in stress responseFunctional Class: NThe phylogenetic pattern of COG1217 is ---------drlbcefghsnujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 4.4e-49) to 5/6 blocks of the IPB000640 family, which is described as \"Elongation factor G, C-terminus\". Interpro entry for IP:IPR000640. IPB000640A 10-35 6.3e-15 IPB000640B 50-72 4.4e-06 IPB000640C 77-104 1e-12 IPB000640D 111-139 1.1e-06 IPB000640F 399-433 0.018Significant hit ( 1.3e-29) to 3/3 blocks of the IPB000795 family, which is described as \"GTP-binding elongation factor\". Interpro entry for IP:IPR000795. IPB000795A 12-27 8.2e-10 IPB000795B 80-111 4.9e-13 IPB000795C 115-139 0.0012Significant hit ( 9.3e-17) to 4/8 blocks of the IPB000178 family, which is described as \"Initiation factor 2\". Interpro entry for IP:IPR000178. IPB000178A 9-47 0.17 IPB000178B 77-109 0.00018 IPB000178C 110-149 1.1e-06 IPB000178D 152-193 1.4e+02","Residues 108 to 153 match (7e-08) PD:PD000134 which is described as FACTOR ELONGATION GTP-BINDING BIOSYNTHESIS INITIATION PROTEOME COMPLETE TRANSLATION TU EF-TU ","","","","","Wed Feb 19 16:16:03 2003","","","","Wed Feb 19 16:16:03 2003","","","Tue Jan 7 09:09:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02344 is paralogously related to AA03003 (2e-39), AA00564 (7e-24), AA01852 (2e-18), AA00931 (5e-17), AA00563 (5e-17), AA01922 (2e-14) and AA00892 (1e-05).","","","","","","Residues 402 to 490 (E-value = 5.7e-32) place AA02344 in the EFG_C family which is described as Elongation factor G C-terminus (PF00679)","","","","","Farris,M., Grant,A., Richardson,T.B. and O\"Connor,C.D. BipA: a tyrosine-phosphorylated GTPase that mediates interactions between enteropathogenic Escherichia coli (EPEC) and epithelial cells Mol. Microbiol. 28 (2), 265-279 (1998) PubMed: 9622352 Freestone,P., Trinei,M., Clarke,S.C., Nystrom,T. and Norris,V. Tyrosine phosphorylation in Escherichia coli J. Mol. Biol. 279 (5), 1045-1051 (1998) PubMed: 9642082 ","","Tue Dec 2 11:33:53 2003","1","","","" "AA02346","1604069","1603959","111","TTGAATATATTTTTAATAGGAAATAGAAATGTAAATTATAGATATAAAAGTGCGGTATTTTTTACAAAACTTTTACAAAACACACCGCACTTTTTCTCTATCAAAATTAAT","","","4414","LNIFLIGNRNVNYRYKSAVFFTKLLQNTPHFFSIKIN","1603959","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 11:29:43 2004","Wed Feb 25 11:29:43 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02346 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 11:17:45 2004","","","","","","","","","","","","","1","","","" "AA02347","1604107","1606842","2736","TTGTGTTCTTTTTCAAAAAAGTACTGCATTGTAATATATTTAACATCTTATTTTTATATAACTATAAATCCTAACTCTATGAAAATTTTACTGAAACCTTTCCGCTATTCTGTTATAGCAACAACCATCGCATTGGTATTTAATCAACCGGCATTTGCGTCAGAGTTTAATGCTCAAATAAATAATCAACCGTCTTCTCAGGCTAAAACAAAAAGTAAAACCAATATTAAAAAAAATATGCAGAACAACATATCTAATTCTGCAAAAGAATCCGTTAATACTTATCAAACGGAAATTCAGCGTATCACTGCCGCACAAAAACTTGCCCGTCAAAAAGCTGAGATGGCACAAAAAGAAGCGGAAGCCCGTGCAATAGCACAAGTAAAAGAGAAACGTCAACAAAGCCAAATTAAAGCACAAGAATTAGAACAGAAAAAGGCGGAACTTGTTCAACGTGAGTATTTAGAAGCTAAGCGTCAAGTCCGTGAACAAGAAATGGCACGCCAGAAGGCAGAAGAAGATCGTAAAGTAGCAGAGGCACTTGCGGCCGTCAAACTAAAGAATTCCACCCAACAACGTTTAACTAAAGAGCAGCTGGCAGCACAGAAAGAAGCGGAACGTTTGGCTAATGAACAAGAAATCGCCCGCAAAAAAATTAAAGCAAATGAGCTTCAACGTGCCATTAACGAACAAAGTAAATTAGCCGAAGTTGCCCGAGTAAAGCGCACTCTTATTGAGCAAAAACAAGTAATTTCACCTCAAAAAGAAGATGAAATACTTCGCCAACAAGCGATTGAAGAACAGCGCAAAAAAGAAGCATTGGCGAATGCAGAACGCAAGCGTTTAGAAGCGGAACGTCTTGCCCGCGAGGAAGAAATTGCAAATCAAAAGGCAGAAGAAGCCCGCAAAAAATCTGAAGAACTTGCCCGCCGTGAGCGTGATCGTTTGGCACGCGAACAGGAAATTGCCCGTCAAAAAGCAGCGGAAGAAGAACGTCAACGCGCTATTGAAGCCCAACGTCAGCAGGAAGAAAATGCCCGTATTGAACGCGAACGTGCAAAACGTGAAGAAGCCGACCGTCTAGCCCGCGAACAGGAAATTGCCCGTCAAAAAGCAGTGGAAGAAGAACGTCAACGCGCTATTGAAGCGCAACGTCAGCAGGAAGAAAATGCCCGTATTGAACGCGAACGTGTCCAACGTGAAGAAGCCGACCGTCTAGCCCGTGAGCAGGAAATTGCCCGTCAAAAAGCGGTGGAAGAAGAACGCCAACGCGCTATTGAAACGCAACGTCAGCAGGAAGAAAATGCCCGTATTGAACGCGAACGTGCCGAACGTGAAGAAGCCGACCGTCTAGCCCGTGAGCAAGAAATTGCAGCTCAACAAGTTGAAGAAAAACCGGAAGAAAGCCCTGTTATTCTTGTTCGCTCTACTGCCCCTACGGATTTACCTAGTGATATGGCACCATTAGATCTTGAGGACATTCAAGGAGAAAACAGTGGTGTCGAAAAAACCGTTACTGTAGCGCCTAAAGAACACATTGAGATGATTCATGATGAAACAAACTCGGAAACTAAAACTGAAGACGTTGCGCTAAAAGTAGATAGCACACTAGAATCGCAGGAGAGCAGTAACAGTCAGCCTGAAGTAGCTGAACAAGCTTCGGTAGAACAAGTTGTCGCTTCTCACGAAGAAACAGCCCATCAACTGAATGCTGAAGAAACCATTTCTGTGGTTAAACGTTTAACTACAGAAATCGCATCGGCAATACATGCCAATCTTGAACCTAGTGTGGCTGACGCTGAGGTTATCGCTAATTCGGAAGTTAGGGAATCTGAGGAAATAGAAGTAGCACCACAAGCCCCAACGATATATAACCCAAATGAAATTCTCGTTGCCAATGCGATCGCTTCCAATGTAGCAATCTTGAATACATTAAATTTAGATCTTTCCGGGCGCTTAGACAGAAAATTAGGCAGAACAAGTTTCTACCGCACTCTTGGTGGTGTTTGGGTTGAATACGTTAATAGCGATATGCACGGTCACGGTGGTGATACCAATAATTACCGCGCTAAAAGTAACCAAATTACGTTAGGTAATGATGAAGCCCAATTGGATAACGGCGTGGTTTTAGGCGGCACATTTACTCATGCCAAAACCGATAACCAATACGGTCCATTGAGTGGAAAAGATACCCTCACTAAAATCACAGCCTACGCTAAACAAAACTTTGATCAATACAGTAAAGCACTTGATATTGGTTATGGTTGGTCAAGCAGTAAAATTGGCAATAGCAAATTGAAACGTAAAATCATTAGTGTCGGTATGAATTTTGCCTACGACTTCGAACTTGAAGATTTCAAAGTGACGCCAATTTGGGGACTTCGTTATCACCATCTAAGCTCTACCGGTGGTGAAATCAACGGGTTAAACGTGAGAAGTCCCGGCTTTAGTCTGGTCGCTTACCATACAGGCTTAAAATTCAGTAATACCTACAATGTTGATGGTATTGAAGTGACGCCGGCATTCTCAACCTATTATGTAACAACATTAGGAAAATCTTATAGCCAAAATATTAATGGTAAAGAGTTTGGTGTCGCTATTGGTCCTTATTGGCATAATAACGCAAGTTTAAGCATTGGTTTGCGAGATTGGAAAATATCTGCCTACGCAGCTGTGAACCAGGGTAAACATGGGGAACGCCAAAACCAACTTGGTGTAAAACTGAATTACTACTGG","","","103668","LCSFSKKYCIVIYLTSYFYITINPNSMKILLKPFRYSVIATTIALVFNQPAFASEFNAQINNQPSSQAKTKSKTNIKKNMQNNISNSAKESVNTYQTEIQRITAAQKLARQKAEMAQKEAEARAIAQVKEKRQQSQIKAQELEQKKAELVQREYLEAKRQVREQEMARQKAEEDRKVAEALAAVKLKNSTQQRLTKEQLAAQKEAERLANEQEIARKKIKANELQRAINEQSKLAEVARVKRTLIEQKQVISPQKEDEILRQQAIEEQRKKEALANAERKRLEAERLAREEEIANQKAEEARKKSEELARRERDRLAREQEIARQKAAEEERQRAIEAQRQQEENARIERERAKREEADRLAREQEIARQKAVEEERQRAIEAQRQQEENARIERERVQREEADRLAREQEIARQKAVEEERQRAIETQRQQEENARIERERAEREEADRLAREQEIAAQQVEEKPEESPVILVRSTAPTDLPSDMAPLDLEDIQGENSGVEKTVTVAPKEHIEMIHDETNSETKTEDVALKVDSTLESQESSNSQPEVAEQASVEQVVASHEETAHQLNAEETISVVKRLTTEIASAIHANLEPSVADAEVIANSEVRESEEIEVAPQAPTIYNPNEILVANAIASNVAILNTLNLDLSGRLDRKLGRTSFYRTLGGVWVEYVNSDMHGHGGDTNNYRAKSNQITLGNDEAQLDNGVVLGGTFTHAKTDNQYGPLSGKDTLTKITAYAKQNFDQYSKALDIGYGWSSSKIGNSKLKRKIISVGMNFAYDFELEDFKVTPIWGLRYHHLSSTGGEINGLNVRSPGFSLVAYHTGLKFSNTYNVDGIEVTPAFSTYYVTTLGKSYSQNINGKEFGVAIGPYWHNNASLSIGLRDWKISAYAAVNQGKHGERQNQLGVKLNYYW","1606842","From Genbank:[gi:1170514] This protein acts as a virulence factor. It cleaves host immunoglobulin A producing intact FC and FAB fragments.","immunoglobulin A1 protease precursor","Outer membrane, Cytoplasm, Extracellular","","
InterPro
IPR005546
Domain
Autotransporter beta-domain
PF03797\"[663-904]TAutotransporter
PS51208\"[662-912]TAUTOTRANSPORTER
InterPro
IPR006315
Domain
Outer membrane autotransporter barrel
TIGR01414\"[516-912]Tautotrans_barl: outer membrane autotranspor
InterPro
IPR013982
Domain
AICARFT/IMPCHase bienzyme, formylation region
SM00798\"[503-749]Tno description


","No hits to the COGs database.","Significant hit ( 6.5e-07) to 2/26 blocks of the IPB001101 family, which is described as \"Plectin repeat\". Interpro entry for IP:IPR001101. IPB001101N 86-140 0.67 IPB001101P 261-315 0.00038","Residues 669 to 910 match (2e-19) PD:PD007723 which is described as PROTEASE SERINE HYDROLASE IGA1 ZYMOGEN PRECURSOR TRANSMEMBRANE SIGNAL COMPLETE PROTEOME ","","","","","","","","","","","Tue Jan 7 09:34:22 2003","Tue Jan 7 09:34:22 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02347 is paralogously related to AA02832 (8e-16), AA01922 (6e-11), AA00450 (2e-09), AA02112 (1e-07), AA01808 (5e-07), AA01211 (1e-04), AA02910 (2e-04), AA02511 (7e-04) and AA00579 (7e-04).","","","","","","Residues 650 to 912 (E-value = 7.3e-05) place AA02347 in the Autotransporter family which is described as Autotransporter beta-domain (PF03797)","","","","","Pohlner J, Halter R, Beyreuther K, Meyer TF.Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease.Nature 1987 Jan 29-Feb 4;325(6103):458-62PMID: 3027577Poulsen,K., Brandt,J., Hjorth,J.P., Thogersen,H.C. and Kilian,M.Cloning and sequencing of the immunoglobulin A1 protease gene (iga) of Haemophilus influenzae serotype bInfect. Immun. 57 (10), 3097-3105 (1989)PubMed: 2506130Poulsen,K., Reinholdt,J. and Kilian,M.A comparative genetic study of serologically distinct Haemophilusinfluenzae type 1 immunoglobulin A1 proteasesJ. Bacteriol. 174 (9), 2913-2921 (1992)PubMed: 1373717","","Tue Jan 7 09:37:52 2003","1","","","" "AA02348","1607373","1606912","462","ATGGAAACATTAAAAGCCGGTGAAAATGCACCGCACTTTACCTTGTTGGATCAACATAACCAATCGGTTTCTTTAACCCAATTTCAAGGTAAAAAAGTATTGGTTTATTTTTACCCGAAAGCCTTAACACCTGGCTGTACCACACAAGCCTGCGGTTTACGCGATAGCAAAGCGGAATTGGACAGATTAGGTGTGGTTGTTCTCGGCATTAGCCCGGACAGCCCGAAAAAATTAGCCCAATTTGCAGAAAAGAAAGTATTGAACTTCATTTTATTATCCGACGAAAACCATCAGGTCGCGGAACAATTCGGTGTGTGGGGCGAGAAAAAATTTATGGGACGCACATATGACGGCATTCACCGGATCAGCTTTTTAATTGATGAACAGGGAAAAGTCGAACAGGTATTTGATAAATTTAAAGCGATGGATCACCATCAAGTGGTGCTGGATTATTTGCAGAAG","","","17438","METLKAGENAPHFTLLDQHNQSVSLTQFQGKKVLVYFYPKALTPGCTTQACGLRDSKAELDRLGVVVLGISPDSPKKLAQFAEKKVLNFILLSDENHQVAEQFGVWGEKKFMGRTYDGIHRISFLIDEQGKVEQVFDKFKAMDHHQVVLDYLQK","1606912","","bacterioferritin comigratory protein","Cytoplasm","","
InterPro
IPR000866
Domain
Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen
PF00578\"[6-135]TAhpC-TSA
InterPro
IPR012335
Domain
Thioredoxin fold
G3DSA:3.40.30.10\"[4-153]Tno description
noIPR
unintegrated
unintegrated
PTHR10681\"[1-154]TPEROXIREDOXIN
PTHR10681:SF5\"[1-154]TBACTERIOFERRITIN COMIGRATORY PROTEIN


","BeTs to 18 clades of COG1225COG name: PeroxiredoxinFunctional Class: OThe phylogenetic pattern of COG1225 is -o-p-zyqvdr-bcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 5.5e-13) to 3/3 blocks of the IPB000866 family, which is described as \"AhpC/TSA family\". Interpro entry for IP:IPR000866. IPB000866A 34-49 5.9e-07 IPB000866B 67-81 0.17 IPB000866C 112-121 0.91","Residues 80 to 153 match (5e-10) PD:PD449879 which is described as COMIGRATORY BACTERIOFERRITIN PROTEOME COMPLETE OXIDOREDUCTASE PROBABLE DEHYDROGENASE BCP-1 AT3G26060/MPE11_21 Q-LIKE ","","","","","","","","","","","","Tue Jan 7 09:41:46 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02348 is paralogously related to AA02462 (3e-04).","","","","","","Residues 6 to 149 (E-value = 2e-55) place AA02348 in the AhpC-TSA family which is described as AhpC/TSA family (PF00578)","","","","","Jeong W, Cha MK, Kim IH.Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin comigratory protein (BCP) as a new member of the thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide peroxidase C (AhpC) family.J Biol Chem 2000 Jan 28;275(4):2924-30PMID: 10644761","","Tue Jan 7 09:47:52 2003","1","","","" "AA02349","1607531","1608421","891","ATGTCAAATCATCCTTTATTTCAAGGCAGTATTGTTGCATTAGTGACACCAATGGACAGCCATGGTGAAGTCGATTTTAAAACCTTAAAAAAATTAGTGGAATTTCACATCAAGAGCGGCACCGATGCTATCGTTTCCGTCGGAACCACCGGTGAGTCTGCCACCTTGAGCATTGATGAAAATGTAAAAGCTATTTTAAAAACCGTTGAATTTGCCGATGGACGTATTCCGGTTATTGCCGGCACCGGTGCTAATGCCACCAGCGAGGCCATCACCATGACCAAATTACTCAACAACAGTGGCATTGCCGGTTGTTTATCCGTTGTGCCTTACTACAACAAGCCGACTCAAGAAGGCATGTATCAACACTTCAAAGCCATCGCCGAATGCACCAATATTCCACAAATTCTTTATAATGTACCGGGACGCACCGGCAGTGACTTATTGCCTGAAACCATCGGTCGTTTGGCAAAAATCAGCAACATTGTGGGGATTAAAGAAGCTACCGGCGATGTCAGTCGTGTACAAAAGATCAAACAACTTGCCGGCGAAGATTTCATCATTTTAAGCGGCGACGATGCTACCGGTTTGGAAGCCATGAAACTGGGCGCGCAAGGCGTGATTTCCGTCACGAACAACGTGGCAGCCACCGATATGGCAAAAATGTGCCATCTCGCCCGCGCGGGTAAATTTGATGAGGCAGAACAAATCAACCAACGCTTAATGCCGCTACACAAAAATCTGTTCGTCGAATCAAATCCAATTCCGGTGAAATGGGCGTGTTACAAATTAGGCTTGATTCAGGAGCCGGTATTACGTCTGCCGCTCACCACATTAAGCGAACAGGCACAGCCGAAAGTCTTAGATGCATTAAAAGCCGCCGGCTTGCTT","","","31765","MSNHPLFQGSIVALVTPMDSHGEVDFKTLKKLVEFHIKSGTDAIVSVGTTGESATLSIDENVKAILKTVEFADGRIPVIAGTGANATSEAITMTKLLNNSGIAGCLSVVPYYNKPTQEGMYQHFKAIAECTNIPQILYNVPGRTGSDLLPETIGRLAKISNIVGIKEATGDVSRVQKIKQLAGEDFIILSGDDATGLEAMKLGAQGVISVTNNVAATDMAKMCHLARAGKFDEAEQINQRLMPLHKNLFVESNPIPVKWACYKLGLIQEPVLRLPLTTLSEQAQPKVLDALKAAGLL","1608421","From PF00701.Dihydropicolinate synthase (DHDPS) is the key enzyme in lysine biosynthesis via the diaminopimelate pathway of prokaryotes,some phycomycetes and higher plants.The enzyme catalyses the condensation of L-aspartate-beta-semialdehyde and pyruvate to dihydropicolinic acid via a ping-pong mechanism in which pyruvate binds to the enzyme by forming a Schiff-base with a lysine residue.","dihydrodipicolinate synthetase","Cytoplasm","","
InterPro
IPR002220
Family
Dihydrodipicolinate synthetase
PD001859\"[9-77]TDAPA_PASMU_Q9CLZ7;
PR00146\"[40-61]T\"[76-94]T\"[108-124]T\"[133-150]TDHPICSNTHASE
PIRSF001365\"[7-297]TDihydrodipicolinate synthase
PTHR12128\"[1-297]TDIHYDRODIPICOLINATE SYNTHASE
PF00701\"[6-295]TDHDPS
PS00665\"[43-60]TDHDPS_1
PS00666\"[138-168]TDHDPS_2
InterPro
IPR005263
Family
Dihydrodipicolinate synthase subfamily
TIGR00674\"[9-294]TdapA: dihydrodipicolinate synthase
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[7-297]Tno description


","No hits to the COGs database.","Significant hit ( 3.4e-84) to 7/7 blocks of the IPB002220 family, which is described as \"Dihydrodipicolinate synthetase\". Interpro entry for IP:IPR002220. IPB002220A 13-25 0.0041 IPB002220B 40-61 1.3e-10 IPB002220C 80-127 7e-29 IPB002220D 134-145 1.2e-06 IPB002220E 184-198 0.00021 IPB002220F 203-216 1.3e-05 IPB002220G 241-265 4.5e-16","Residues 2 to 47 match (2e-09) PD:PD543014 which is described as BIOSYNTHESIS DHDPS LYSINE PROTEOME COMPLETE DIAMINOPIMELATE DIHYDRODIPICOLINATE SYNTHASE LYASE ","","","","","","","","","","","Tue Jan 7 10:03:05 2003","Tue Jan 7 09:58:03 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02349 is paralogously related to AA02466 (4e-22).","","","","","","Residues 6 to 295 (E-value = 2.3e-165) place AA02349 in the DHDPS family which is described as Dihydrodipicolinate synthetase family (PF00701)","","","","","Mirwaldt C, Korndorfer I, Huber R.The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution.J Mol Biol 1995 Feb 10;246(1):227-39PMID: 7853400Richaud,F., Richaud,C., Ratet,P. and Patte,J.C.Chromosomal location and nucleotide sequence of the Escherichiacoli dapA geneJ. Bacteriol. 166 (1), 297-300 (1986)PubMed: 3514578Tiedeman,A.A., DeMarini,D.J., Parker,J. and Smith,J.M.DNA sequence of the purC gene encoding 5'-phosphoribosyl-5-aminoimidazole-4-N-succinocarboxamidesynthetase and organization of the dapA-purC region of Escherichiacoli K-12J. Bacteriol. 172 (10), 6035-6041 (1990)PubMed: 2120198Laber,B., Gomis-Ruth,F.X., Romao,M.J. and Huber,R.Escherichia coli dihydrodipicolinate synthase. Identification ofthe active site and crystallizationBiochem. J. 288 (Pt 2), 691-695 (1992)PubMed: 1463470","","Tue Jan 7 10:07:51 2003","1","","","" "AA02350","1608538","1609239","702","ATGAAAAAATGGCTATTAACCGTAGCAATCGTCACCGCACTCAGCGCCTGCTCCACCGGTAACGAAAGTAAACAACAAGCAGGTGATACCTATCAAAAATCCAACAGCGAATTACCATATTTTACTCCGTTAGCCAGTGGCGGCGTGAATCTGCCGGCACAAAGCGCGGAATATCAATTACCACCAGTTAAAATCAGCAGAACCGACGGTGTAGATATTCGTCCGCCATCCTTGCCATTGGCAATCATCAGTAATTCCGTCACACAATTTGACGGCGAACGTGCACTGATCGCTTATACGCCGGACAAACAAAGAGTTTACAATCTAACCCAAGTGGAACGCCTGCTCAAAGAACAAGACATCAGCTACACCGTCGAAGGCAATAAATTATTAACCGACTGGGCGAATACCGGTCGTGCCGACGATTTGGAAAACACCAAAATCCGCTACCAAATTGAAGAAATCAATGCCCCGCACGCCAGTGCATTGGTTGTTTCCGTGTTGCAAATGAAACGTGATGACACCATTTTCACGCCGGATTTTACGGACAGGCAACGCTACGCCTCCGATCGCTTAAATCAATTGGTGGGGGAATTGAATTCCGCTTACCAAAAACAACAGCAGGATCTTAACGGCGCAGCCTCCTCACCAATTCAGTCCGCCATCGCCACCGACGCCAACGGCAGAACCGCAGACATCATT","","","25764","MKKWLLTVAIVTALSACSTGNESKQQAGDTYQKSNSELPYFTPLASGGVNLPAQSAEYQLPPVKISRTDGVDIRPPSLPLAIISNSVTQFDGERALIAYTPDKQRVYNLTQVERLLKEQDISYTVEGNKLLTDWANTGRADDLENTKIRYQIEEINAPHASALVVSVLQMKRDDTIFTPDFTDRQRYASDRLNQLVGELNSAYQKQQQDLNGAASSPIQSAIATDANGRTADII","1609239","","possible lipoprotein","Outer membrane, Periplasm","","
InterPro
IPR010653
Family
NlpBDapX lipoprotein
PF06804\"[4-234]TLipoprotein_18
noIPR
unintegrated
unintegrated
PS51257\"[1-17]TPROKAR_LIPOPROTEIN
signalp\"[1-20]?signal-peptide


","BeTs to 3 clades of COG3317COG name: Uncharacterized lipoproteinFunctional Class: MThe phylogenetic pattern of COG3317 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 2 to 189 match (5e-46) PD:PD036841 which is described as PROTEOME COMPLETE LIPOPROTEIN-34 LIPOPROTEIN OUTER MEMBRANE NLPB HI0256 SIGNAL PRECURSOR ","","","","","","","","","","","","Tue Jan 7 10:12:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02350 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 234 (E-value = 3.4e-34) place AA02350 in the Lipoprotein_18 family which is described as NlpB/DapX lipoprotein (PF06804)","","","","","","","","1","","","" "AA02351","1609373","1609528","156","ATGCAGCTGCCGGACTTGGAAAAAGGCACTTACCAAATGCAGCTTGCCGCTGTAGGTAAACAAAGTGCGGTGGTTATTTCCGACGAAAATAAAACCGCCCTCTCCGGCGAACAGGCACAGCTTATTTATCAAGCGTTGCAGAATGTATTGGCAAAA","","","5617","MQLPDLEKGTYQMQLAAVGKQSAVVISDENKTALSGEQAQLIYQALQNVLAK","1609528","","conserved hypothetical protein","Periplasm, Cytoplasm","This sequence is similar to gi|15602915, an unknown from Pasteurella multocida.","
InterPro
IPR010653
Family
NlpBDapX lipoprotein
PF06804\"[4-51]TLipoprotein_18


","No hits to the COGs database.","","Residues 6 to 52 match (4e-11) PD:PD033242 which is described as PROTEOME COMPLETE LIPOPROTEIN-34 LIPOPROTEIN OUTER MEMBRANE PM1050 NLPB SIGNAL PRECURSOR ","","","","","","","","","","","","Wed Feb 25 11:33:26 2004","Wed Feb 25 11:33:26 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02351 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 11:17:04 2004","","","","","","","","","","","","","1","","","" "AA02352","1609708","1611174","1467","ATGTTACTTACCCACCTATGGCTCTCTTTATCGGCATTGCTAATTGCAGTAGTAATTGCTGTACCTATTGCAGTATTATTGTCACGCAAACGCCACATGGCGGAAATAGTGTTACAATTTACTAATGTGCTGCAAACCATTCCATCTCTCGCTCTGCTTGGCTTATTGATTCCCTTTGTTGGCATTGGTTCACCACCGGTACTAATTGCCCTAACACTCTATGCTCTGTTACCGATCTTCCAAAATGCCTATTTGGGATTAAGCCAAATCGATCAATCTATTCAAGATGCTTACACCGCTTTCGGCTTATCTCGGTGGCAATCGTTATGGCGAATTGAACTGCCGATGGCCTTGCCGGCAATGATGTCGGGCATCCGTACGGCGGCAGTATTAATTATCGGGACTGCAACCCTGGCGGCATTAATCGGGGCGGGCGGGTTAGGCAGTCTTATTTTACTCGGTATCGATCGCAATAATATGGTGATGATTTTTACCGGTGCCTTACTTTCTGCATTATTGGCAGTCGGAGTAAGCGGTTTGATTGCTATTTTACAAAAAGTACGATGCAAACGTCCCCTTGCTATCGTTTTGATTTTAGGGCTAAGTGCGGTTGGTTTTTCGCAAATTTCTCTCACATCCCAAACTCAAAAAGTAGTGATTGCGGGTAAACTTGGCAGTGAACCTGATATTCTTATCAATATGTACAAACTGTTGATTGAGCAGGAAAACAAAACTATTCAAGTAGAGCTTAAACCGAATTTCGGCAAAACCTCTTTTTTATTCAATGCTCTCAACAGCGGTGAAATTGATATTTATCCTGAATTTACCGGCACAGTGCTGGAAGCCTTAGTGCAAGTGTTACCCGAACAAAAAAATCATCACCGCTCTCCTGAAACCACTTATCAGCTGAGTAAACAATTACTGGCGGAACAGTTCCGGCTTGAATTTTTACCGCCGATGGCATATCAAAATACCTATGCATTAGCAGTGAAAGAAGCCTATGGAGCAACACATGGGCTTGCAACAATCAGCGATTTACATCATGTGGCAGGTGACATTCGCGCCGGCTTCACACTGGAATTTCTCGATCGAGTCGATGGCTATAAAGGAATAAAATCACAAGGCATTACTTTAGTTCATATTGTCACCCTTGAACCTGCTTTGCGTTATACGGCGTTACTCAACAATAAAATTGATTTAATCGAAGCATTTTCTACTGACGCAGAACTCAAACAACATCAGCTCCGCTTACTGAAAGACGACATTAATTTATTCCCTGCCTATCAAGGTGCGCCACTAATGAAAGCCGATTTTGCAGCAAAAAATCCGCAGGTTCTGACCGCACTTAACCGCCTCGCCAATCGTATTTCCGAACAAGAAATGAGTGAAATGAATTATCAAGTTAAAGTACTGGGCGAAAGCCCGGAGAAAGTGGCGAGGGAGTATTTGAAGAAAATGAAATTGCTA","","","55116","MLLTHLWLSLSALLIAVVIAVPIAVLLSRKRHMAEIVLQFTNVLQTIPSLALLGLLIPFVGIGSPPVLIALTLYALLPIFQNAYLGLSQIDQSIQDAYTAFGLSRWQSLWRIELPMALPAMMSGIRTAAVLIIGTATLAALIGAGGLGSLILLGIDRNNMVMIFTGALLSALLAVGVSGLIAILQKVRCKRPLAIVLILGLSAVGFSQISLTSQTQKVVIAGKLGSEPDILINMYKLLIEQENKTIQVELKPNFGKTSFLFNALNSGEIDIYPEFTGTVLEALVQVLPEQKNHHRSPETTYQLSKQLLAEQFRLEFLPPMAYQNTYALAVKEAYGATHGLATISDLHHVAGDIRAGFTLEFLDRVDGYKGIKSQGITLVHIVTLEPALRYTALLNNKIDLIEAFSTDAELKQHQLRLLKDDINLFPAYQGAPLMKADFAAKNPQVLTALNRLANRISEQEMSEMNYQVKVLGESPEKVAREYLKKMKLL","1611174","From PF00528.Bacterial binding protein-dependent transport systems are multicomponent systems typically composed of a periplasmic substrate-binding protein, one or two reciprocally homologous integral inner-membrane proteins and one or two peripheral membrane ATP-binding proteins that couple energy to the active transport system. The integral inner-membrane proteins translocate the substrate across the membrane. It has been shown that most of these proteins contain a conserved region located about 80 to 100 residues from their C-terminal extremity. This region seems to be located in a cytoplasmic loop between two transmembrane domains. ","glycine betaine/carnitine/choline ABC transporter","Inner membrane, Cytoplasm","","
InterPro
IPR000515
Family
Binding-protein-dependent transport systems inner membrane component
PF00528\"[2-190]TBPD_transp_1
PS50928\"[2-181]TABC_TM1
InterPro
IPR007210
Domain
Substrate-binding region of ABC-type glycine betaine transport system
PF04069\"[216-485]TOpuAC
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[211-373]T\"[390-489]Tno description
signalp\"[1-20]?signal-peptide
tmhmm\"[10-28]?\"[43-61]?\"[67-87]?\"[129-151]?\"[161-183]?\"[193-211]?transmembrane_regions


","No hits to the COGs database.","","Residues 45 to 125 match (3e-07) PD:PD439245 which is described as COMPLETE PROTEOME PERMEASE ABC SYSTEM TRANSPORTER MEMBRANE OSMOPROTECTION INNER PROBABLE ","","","","","","","","","","","Tue Jan 7 10:23:25 2003","Tue Jan 7 10:15:03 2003","","","","Wed Mar 17 08:16:21 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02352 is paralogously related to AA00416 (1e-15), AA02719 (6e-07), AA01682 (8e-06) and AA01780 (9e-05).","Wed Mar 17 08:16:21 2004","","","","","Residues 217 to 487 (E-value = 5.6e-67) place AA02352 in the OpuAC family which is described as Substrate binding domain of ABC-type glycine betaine transport system (PF04069)","Wed Mar 17 08:16:21 2004","","","","Ames GFBacterial periplasmic transport systems: structure, mechanism, and evolution.Annu Rev Biochem 1986;55:397-425PMID: 3527048Saurin W, Koster W, Dassa E.Bacterial binding protein-dependent permeases: characterization ofdistinctive signatures for functionally related integral cytoplasmic membrane proteins.Mol Microbiol 1994 Jun;12(6):993-1004PMID: 7934906","","Tue Jan 7 10:23:25 2003","1","","","" "AA02353","1611492","1612325","834","ATGAAAAGTAATCGCACACCTTTTATCGAATTTCGCGGCGTAAGCAAATATTATGACGGACAACATGCAGTGCAAACGCTAAATCTGACCATCTATCAAGGCGAATTCTTCGTATTGGTCGGAGGTTCAGGTAGCGGTAAATCCACAACATTGCGCATGATCAACGCCCTCACCGAACCTACAGATGGAGATGTATATTTTCAAGGTAAACGGATCAAAGATTACAACATCCATACCTTACGTCATCGCATCGGTTATGTATTACAACAAATCGCCCTATTCCCCACCATGACAGTAGCGCAAAACATTGCCTTAATGCCCGATATTCTTGGGTGGCACAAAAATGAGCGAAAATCCCGTGTGAATACATTACTTGAATTAGTGAATTTGCCACCTGCGCAATATCAGGATCGCTATCCGCGCGAACTTTCCGGTGGAGAACAACAACGGATAGGCATTTTACGGGCTATTGCTGCTAATCCCCATTTATTGCTCATGGATGAACCATTTTCTGCACTTGATCCACTGGTGCGGGCTGCCTTACAAGATCAAATTTCGTTGATCCATAAAAAATTCGGCACAACTATCGTGTTCGTTACTCATGACATGCAAGAAGCCTTAAAACTTGCTTGTCGCATTGGCGTCATGCAGAATGGGAAGCTGGTACAAGTAGGTAAACCAAACGAAATCCAGCAACAGCCTGCCAATAGTTACGTAAAATCGCTATTCGCTTCGTCTGAACAGGCGTTAACGGTAGAGAAAGTGATTATGCAATATGAGCAATTAAGTAAGACTGAACAAGCAAGTGTACGGAAATGGCTAGCACGTAATGGT","","","31371","MKSNRTPFIEFRGVSKYYDGQHAVQTLNLTIYQGEFFVLVGGSGSGKSTTLRMINALTEPTDGDVYFQGKRIKDYNIHTLRHRIGYVLQQIALFPTMTVAQNIALMPDILGWHKNERKSRVNTLLELVNLPPAQYQDRYPRELSGGEQQRIGILRAIAANPHLLLMDEPFSALDPLVRAALQDQISLIHKKFGTTIVFVTHDMQEALKLACRIGVMQNGKLVQVGKPNEIQQQPANSYVKSLFASSEQALTVEKVIMQYEQLSKTEQASVRKWLARNG","1612325","From: PF00005ABC transporters for a large family of proteins are responsible for translocation of a variety of compounds across biological membranes. They are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domainABC membrane. ","spermidine / putrescine transport ATP-binding","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[143-183]TQ8DU54_STRMU_Q8DU54;
PF00005\"[34-219]TABC_tran
PS50893\"[9-243]TABC_TRANSPORTER_2
PS00211\"[143-157]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[33-220]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[3-252]Tno description
PTHR19222\"[9-268]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF48\"[9-268]TGLYCINE BETAINE/L-PROLINE ABC TRANSPORTER


","No hits to the COGs database.","Significant hit ( 1.6e-29) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 23-69 5.9e-14 IPB001140B 140-178 5.2e-12 IPB001140C 196-225 1.8Significant hit ( 3.2e-05) to 1/5 blocks of the IPB001324 family, which is described as \"Phosphoribulokinase family\". Interpro entry for IP:IPR001324. IPB001324A 33-54 3.3e-05","Residues 188 to 238 match (1e-08) PD:PD000174 which is described as ATP-BINDING COMPLETE PROTEOME ABC TRANSPORTER TRANSPORTER CASSETTE SYSTEM BINDING OLIGOPEPTIDE ","","","","","","","","","","","Tue Jan 7 10:53:27 2003","Tue Jan 7 10:50:53 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02353 is paralogously related to AA01656 (1e-46), AA02718 (6e-44), AA01051 (2e-39), AA00700 (1e-38), AA01645 (7e-35), AA00415 (2e-34), AA00858 (1e-33), AA01524 (1e-31), AA02140 (1e-28), AA02899 (3e-28), AA02320 (9e-27), AA02080 (1e-26), AA01422 (1e-26), AA01616 (1e-25), AA01779 (3e-24), AA02440 (4e-24), AA01947 (6e-24), AA02324 (4e-23), AA01684 (1e-22), AA01820 (3e-22), AA01568 (1e-21), AA01867 (2e-21), AA02898 (5e-21), AA02805 (2e-20), AA00799 (1e-19), AA02152 (1e-19), AA01510 (1e-19), AA01961 (4e-19), AA01393 (9e-19), AA00933 (5e-18), AA02786 (2e-17), AA02609 (2e-16), AA01824 (2e-16), AA00207 (3e-16), AA02331 (2e-15), AA01456 (5e-15), AA00751 (5e-15), AA01509 (2e-14), AA01569 (1e-13), AA02225 (5e-13), AA02606 (6e-13), AA02642 (2e-12), AA02550 (3e-12), AA02484 (1e-11), AA02573 (2e-11), AA00061 (1e-09), AA01757 (2e-08), AA00591 (2e-08), AA00934 (4e-08), A02145 (7e-08), AA02226 (2e-06), AA01555 (5e-06), AA02146 (9e-06) and AA01291 (5e-04).","","","","","","Residues 34 to 219 (E-value = 1.1e-63) place AA02353 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Higgins CF, Gallagher MP, Mimmack ML, Pearce SR.A family of closely related ATP-binding subunits from prokaryotic and eukaryotic cells.Bioessays 1988 Apr;8(4):111-6PMID: 3288195 Furuchi,T., Kashiwagi,K., Kobayashi,H. and Igarashi,K. Characteristics of the gene for a spermidine and putrescine transport system that maps at 15 min on the Escherichia coli chromosome J. Biol. Chem. 266 (31), 20928-20933 (1991) PubMed: 1939142 Kashiwagi K, Innami A, Zenda R, Tomitori H, Igarashi K. The ATPase activity and the functional domain of PotA, a component of the spermidine-preferential uptake system in Escherichia coli. J Biol Chem. 2002 Jul 5;277(27):24212-9. PMID: 11976340 ","","Tue Jan 7 10:54:30 2003","1","","","" "AA02354","1613068","1612376","693","ATGGATAATATTCGACATAATTTACAGCTGGTTCAGCAAAAAATAACCCAAATCTGCCATATGATTGGGTCCTCACCAAGTGCGGTTACTTTACTGGCTGTTTCTAAAACCAAGCCCGTTGAAGATATTTTAACAGCGTATGAAGCGGGACAGGAGGCATTCGGAGAAAATTATGTACAGGAGGGAGTGGAAAAAATTCAATTCTGCCAACAGCACAATATTAACTTGGAATGGCATTTTATCGGCCCGTTGCAATCCAATAAAACCCGTTTGGTGGCGGAATATTTTGACTGGATGCAAACCCTTGATCGCGCCAAAATCGCCGATCGTTTAAATGAACAACGTTCTCCGCATAAAGCGCCGCTCAATGTCTTAATTCAGGTGAATATCAGCAATGAAGCCAGTAAATACGGCGTCCAGCCCGGTGAAATTTTAGACCTTGCAAAACACCTGGAAAACTTACCGCACTTATGCCTGCGTGGCTTAATGGCGATTCCCGAACCTACCGATGATGTGGCTCGGCAGGAGCAAGTGTTTTATCAAATGCGTGTGTTGTTTGAACAATTACAACAAGCCTTGCCGAACGCCCAAATCGACACCTTATCCATGGGCATGACCGATGATATGCAGATGGCAATCAAATGTGGTTCCACCATGGTTCGTGTAGGTACAGCAATTTTTGGAAAACGGGTT","","","28062","MDNIRHNLQLVQQKITQICHMIGSSPSAVTLLAVSKTKPVEDILTAYEAGQEAFGENYVQEGVEKIQFCQQHNINLEWHFIGPLQSNKTRLVAEYFDWMQTLDRAKIADRLNEQRSPHKAPLNVLIQVNISNEASKYGVQPGEILDLAKHLENLPHLCLRGLMAIPEPTDDVARQEQVFYQMRVLFEQLQQALPNAQIDTLSMGMTDDMQMAIKCGSTMVRVGTAIFGKRV","1612376","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR001608
Domain
Alanine racemase, N-terminal
PF01168\"[2-231]TAla_racemase_N
InterPro
IPR011078
Family
Predicted pyridoxal 5'-phosphate-dependent enzyme, YBL036C type
PTHR10146\"[3-231]TPROLINE SYNTHETASE ASSOCIATED PROTEIN
TIGR00044\"[1-230]TTIGR00044: conserved hypothetical protein T
PS01211\"[78-92]TUPF0001
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.10\"[4-230]Tno description
PIRSF004848\"[6-231]TPredicted pyridoxal 5'-phosphate-dependent enzyme, YBL036c type


","BeTs to 15 clades of COG0325COG name: Predicted enzyme with a TIM-barrel foldFunctional Class: RThe phylogenetic pattern of COG0325 is ------yqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 7.1e-72) to 6/6 blocks of the IPB001608 family, which is described as \"Uncharacterized pyridoxal-5'-phosphate dependent enzyme family UPF0001\". Interpro entry for IP:IPR001608. IPB001608A 31-65 2.5e-21 IPB001608B 78-88 2e-08 IPB001608C 100-112 0.0042 IPB001608D 126-139 2.7e-05 IPB001608E 155-165 0.00011 IPB001608F 201-228 1.3e-21","Residues 141 to 230 match (5e-11) PD:PD556117 which is described as PROTEOME COMPLETE RV2148C ML0919 PLASMID CC3745 YLME DR1368 RSP0683 PA0394 ","","","","","","","","","","","","Tue Jan 7 10:56:49 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02354 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 230 (E-value = 9.3e-40) place AA02354 in the Ala_racemase_N family which is described as Alanine racemase, N-terminal domain (PF01168)","","","","","","","","1","","","" "AA02355","1614473","1613064","1410","ATGTATTATTTTTATAGGTGTAAAATGTATACTTCAAATCTAACGAATTTAATTCTAAATACAGATAGTTATAAAGCATCTCATTGGCTGCAATATCCGCCTGATAGCGAATATGTCTCTTTTTATATCGAAGCCCGTAAAAGTGAGTTTGATGTTGTTTTCTTCGGATTGCAGGCCTTTCTCAAGGAATACCTAACTAAACCGGTTACTCTACAAGATATAAATGAAGCTGAAAATTTATTGATTGCACATGGCTTACCTTTCAATCGACAAGGGTGGCTTGCTATTTTGGAAAAATATAAAGGTTATCTTCCGCTTCGAATTCAGGCTGTGGCAGAGGGGTTAGTATTGCCTGCCGGTAATGTGGTGTGCCAGGTTGTTAATACAGATCCGGAATTTTTCTGGTTATCAAGTTATTTGGAAACGGCACTTCTGCGTGGTATTTATTACCCTGCTACGGTAGCAAGTCTATCTTATTATTGTAAACAAATACTTAAACGCGCATTGGAAAGATCTGCTGATGATCTGAGTGGTTTGCCGTTTAAATTACATGATTTCGGTGCACGCGGAGCCAGTAGTTTGGAGTCGGTGGCTCTTGGCAGCTTGGCGCATTTGGTAAATTTTTGTGGAACAGATAGTCTCAGCGGTATTATTGGTGCAGCCCGTTGGTATGAGGTCGAAAATATGCCGGCATTTTCAATTCCTGCGGCAGAACACAGTACAGTTACCAGTTGGGGAAAAGAACATGAGATCGCAGCCTATGAAAATATATTTCAGCAATTTGCCGGTAAATATCCTGCATTCGCCATTGTGTCTGACAGCTATGATTTATGGCAGGTGGTTAATGAAGTTTGGGGGGAACGATTTAAGCAGCAGATTTCACAAATGTCGGGAACTTTGATAATTCGTCCTGACAGCGGTGAACCGGGCACGGTAATTTGTCGCGTACTGGATATTTTGGCTGAAAAGTTCGGAACAAGAATAAATAGTAAGGGTTATAAAGTATTGCCGGATTGCATTCGTGTCATTCAGGGGGATGGAATTAATTATACTTCATTGACACACATACTGGATGCTGTCATGGCACATGGATTCAGCGTGGATAATGTGAATTTCGGTATGGGAGGCGGCTTGTTGCAACAGGTTAACCGTGACATGATGGGCTGGGCGATGAAGGCAAGTGCGGTGAGTGTTGCAGGCAAATGGCGTGATGTATATAAAGATCCCGTTACCGGTGCGGAAAAACGTTCGAAAAAAGGACGGCTTGCCTTAGTCAGAAGAAATGGCGAATATCTAACTTTGCGCGAAGAAGAAGTGGATAAGCAAGAAAATCTATTGCGTACAGTGTATTTAAATGGAAAACTATTACATATTGAAACACTTGAACAAATCAGGCGGCGTACCAATGGA","","","55145","MYYFYRCKMYTSNLTNLILNTDSYKASHWLQYPPDSEYVSFYIEARKSEFDVVFFGLQAFLKEYLTKPVTLQDINEAENLLIAHGLPFNRQGWLAILEKYKGYLPLRIQAVAEGLVLPAGNVVCQVVNTDPEFFWLSSYLETALLRGIYYPATVASLSYYCKQILKRALERSADDLSGLPFKLHDFGARGASSLESVALGSLAHLVNFCGTDSLSGIIGAARWYEVENMPAFSIPAAEHSTVTSWGKEHEIAAYENIFQQFAGKYPAFAIVSDSYDLWQVVNEVWGERFKQQISQMSGTLIIRPDSGEPGTVICRVLDILAEKFGTRINSKGYKVLPDCIRVIQGDGINYTSLTHILDAVMAHGFSVDNVNFGMGGGLLQQVNRDMMGWAMKASAVSVAGKWRDVYKDPVTGAEKRSKKGRLALVRRNGEYLTLREEEVDKQENLLRTVYLNGKLLHIETLEQIRRRTNG","1613064","From PF04095Nicotinate phosphoribosyltransferase is the rate limiting enzyme that catalyses the first reaction in the NAD salvage synthesis. This family also includes Pre-B cell enhancing factor that is a cytokine. This family is related to Quinolinate phosphoribosyltransferase QRPTase. ","nicotinamide phosphoribosyl transferase","Cytoplasm","","
InterPro
IPR007229
Family
Nicotinate phosphoribosyltransferase and related
PF04095\"[181-454]TNAPRTase
noIPR
unintegrated
unintegrated
PTHR11098\"[75-466]TNICOTINATE PHOSPHORIBOSYLTRANSFERASE
PTHR11098:SF2\"[75-466]TNICOTINATE PHOSPHORIBOSYLTRANSFERASE RELATED PRE-B CELL ENHANCING FACTOR


","No hits to the COGs database.","","","","","","","","","","","","","Tue Jan 7 11:03:12 2003","Tue Jan 7 11:00:52 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02355 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 16 to 454 (E-value = 5.8e-161) place AA02355 in the NAPRTase family which is described as Nicotinate phosphoribosyltransferase (NAPRTase) family (PF04095)","","","","","Martin,P.R., Shea,R.J. and Mulks,M.H. Identification of a plasmid-encoded gene from Haemophilus ducreyi which confers NAD independence J. Bacteriol. 183 (4), 1168-1174 (2001) PubMed: 11157928 Samal,B., Sun,Y., Stearns,G., Xie,C., Suggs,S. and McNiece,I. Cloning and characterization of the cDNA encoding a novel human pre-B-cell colony-enhancing factor Mol. Cell. Biol. 14, 1431-1437 (1994) PubMed: 8289818 ","","Tue Jan 7 11:04:52 2003","1","","","" "AA02356","1614588","1614716","129","TTGACAATAAAAGTAAATTTCGGTATTTCTAAGCACATTCTTTTTTCACACAAAAACACCATGAAAAACAACCGCACTTTTATTATGATGCCAACCACCATGACCATGATTATGATCAATGGGGCGGGC","","","4868","LTIKVNFGISKHILFSHKNTMKNNRTFIMMPTTMTMIMINGAG","1614716","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:24:11 2004","Wed Feb 25 13:24:11 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02356 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 11:15:47 2004","","","","","","","","","","","","","1","","","" "AA02357","1614808","1617252","2445","ATGCGCGTACTTAAATTTGGGGGCACTTCCTTAGCCAATCCGGAACGGTTTTTGCAGGCGGCGGAGCTTATCGAAAAGGCCCATTTGGAAGAACAGGCTGCAGGCGTTTTATCGGCACCTGCAAAAATCACCAATCACCTTGTCGCCCTTTCCGAAAAAGCCAGTTTAAATCAACCTACCGATTCTCATTTCAACGAAGCATTAGATATTTTCTACACCATCATTAACGGTTTACACGCCAAAAATAACCATTTTGATCTTGCCGGCACCAAACAAATCATCGATCAAGAATTCCAACAAATTGCGTCATTATTAGAAAAAATCCGTCAGGAAGGCAAAGTAGACGATGCGCTCAAAGCGACCATCGATTGCCGCGGTGAAAAACTTTCCATCGCCATGATGAAAGCCTGGTTTGAAGCCAACGATTATGAAGTGCATGTGGTTGATCCGGTGAAACAATTATTAGCCCAAGGCAGCTATTTGGAATCTTCCGTGGATATTGAAGAATCCACCAAACGGGTGGATGCCAAATCCATCGGCAAAAATAAAGTGGTGTTAATGGCGGGCTTTACCGCTTGTAACGATCAAGACGAACTCGTGTTATTGGGACGTAATGGTTCCGACTACTCCGCCGCTTGTTTAGCCGCCTGTTTGGGCGCCAGCGTATGCGAAATCTGGACCGACGTTGACGGCGTTTACACCTGTGACCCGCGTTTAGTGCCGGATGCGCGTCTATTACCGAGCCTGTCTTATCGTGAAGCTATGGAGCTTTCCTACTTCGGCGCCAAGGTCATTCATCCGCGCACCATCGGTCCGTTAGTACGCCCGAACATTCCGTGTTTAATTAAAAACACCGGCAACCCGAGTGCACCGGGTTCGGTTATCGCCGGCGACATCAAATCCGAAGACTTACAGGTAAAAGGCATTACCAATTTAGATAATGTGGCGATGTTCAATGTTTCCGGCCCGGGTATGCAAGGCATGGTAGGCATGGCTTCCCGCGTATTTTCCGCTATGTCTAATGCGAAAGTTTCGGTGATTTTAATCACCCAATCCTCCTCCGAATACAGCATCAGCTTCTGCGTGCCGGTAAAATCCGTTGATGTGGCGTTAAAAGCCTTAGAAGCGGAATTTGCGCAGGAATTAAAAGCCCATCAATTGGATCCGATTGAAGTGATTAAAGATTTATCCATTATTTCCGTAGTAGGCGATGGTATGCGCCAAGCTAAAGGCATTGCCGCGCGCTTCTTCTCTGCGCTGGCACAGGCAAACATCAGCATTAACGCCATTGCCCAAGGTTCTTCCGAACGTTCAATTTCCGCCGTGGTGGCGCAAAATAAAGCCATTGAGGCCGTAAAAGCAACGCACCAAGCGTTATTTAATAACAAAAAGATCGTTGAAGTGTTTCTTGTGGGTGTCGGCGGTGTCGGCGGCGAATTAATTGAGCAAATCAAACACCAAAAAGAGTATTTAGCAAAGAAAGACATTGAAATTCGCGTTTGCGCCCTCGCGAATTCCAACAAAATGTTGCTCAATGAAAACGGCTTAAATTTAGATCATTGGCAAACGGACTTAGAAAACGCCACCCAACCGTCGGATTTCGACGTACTGCTCTCTTTCATTAAATTGCATCATGTGGTGAACCCGGTTTTCGTGGATTGCACGTCGGCGGAATCCTTGGCCGGTTTATACGAACGCGCCTTAGCGGAAGGGTTCCATGTGGTGACTCCGAATAAAAAAGCCAATACCCGCGCGTTGGATTATTATCACAAATTACGTGAACTGGCACATAAAAACCAACGTAAATTCCTGTATGAAACCAATGTCGGCGCAGGCTTGCCGGTCATTGAAAACTTACAGAATCTATTGGCGGCAGGCGATGAAGTAGAACGCTTTGACGGGATTTTATCCGGTTCCCTTTCCTTTATTTTCGGTAAACTGGAAGAAGGCTTAACCCTTTCCCAAGCCACCGCACTTGCCCGCGAAAAAGGCTTCACCGAACCGGATCCACGCGACGATCTTTCCGGTCAGGATGTTGCACGTAAATTACTGATTTTAGCCCGTGAAAGCGGATTAGAATTGGAGCTGGAAGATGTAGACGTAGAAGGCGTGTTACCAAAAGGCTTTGCCGAAGGGAAATCCGCCGAAGAATTCATGGCATTATTGCCGCAGTTGGATGACGAATTCAATGCTCGCATCGAAAAAGCGCAGGCAGAAGAAAAAGTATTACGTTATGTGGGGCAAATCGAAAACGGCAAATGCAAAGTTTCTATTGTTGAAGTAGGCAAAGAAGATCCGCTATACAAAGTGAAAAACGGTGAAAACGCCCTTGCATTTTATACTCGTTATTACCAGCCAATTCCGTTATTATTACGCGGTTACGGCGCCGGTAATGCAGTGACTGCCGCCGGTATTTTCGCCGACATTTTAAGAACCTTGAAACAC","","","92647","MRVLKFGGTSLANPERFLQAAELIEKAHLEEQAAGVLSAPAKITNHLVALSEKASLNQPTDSHFNEALDIFYTIINGLHAKNNHFDLAGTKQIIDQEFQQIASLLEKIRQEGKVDDALKATIDCRGEKLSIAMMKAWFEANDYEVHVVDPVKQLLAQGSYLESSVDIEESTKRVDAKSIGKNKVVLMAGFTACNDQDELVLLGRNGSDYSAACLAACLGASVCEIWTDVDGVYTCDPRLVPDARLLPSLSYREAMELSYFGAKVIHPRTIGPLVRPNIPCLIKNTGNPSAPGSVIAGDIKSEDLQVKGITNLDNVAMFNVSGPGMQGMVGMASRVFSAMSNAKVSVILITQSSSEYSISFCVPVKSVDVALKALEAEFAQELKAHQLDPIEVIKDLSIISVVGDGMRQAKGIAARFFSALAQANISINAIAQGSSERSISAVVAQNKAIEAVKATHQALFNNKKIVEVFLVGVGGVGGELIEQIKHQKEYLAKKDIEIRVCALANSNKMLLNENGLNLDHWQTDLENATQPSDFDVLLSFIKLHHVVNPVFVDCTSAESLAGLYERALAEGFHVVTPNKKANTRALDYYHKLRELAHKNQRKFLYETNVGAGLPVIENLQNLLAAGDEVERFDGILSGSLSFIFGKLEEGLTLSQATALAREKGFTEPDPRDDLSGQDVARKLLILARESGLELELEDVDVEGVLPKGFAEGKSAEEFMALLPQLDDEFNARIEKAQAEEKVLRYVGQIENGKCKVSIVEVGKEDPLYKVKNGENALAFYTRYYQPIPLLLRGYGAGNAVTAAGIFADILRTLKH","1617252","","bifunctional protein: aspartokinase I; homoserine dehydrogenaseI","Cytoplasm","","
InterPro
IPR001048
Domain
Aspartate/glutamate/uridylate kinase
G3DSA:3.40.1160.10\"[207-306]Tno description
PF00696\"[1-284]TAA_kinase
InterPro
IPR001341
Domain
Aspartate kinase region
TIGR00657\"[1-461]Tasp_kinases: aspartate kinase
PS00324\"[3-11]TASPARTOKINASE
InterPro
IPR001342
Domain
Homoserine dehydrogenase, catalytic
PF00742\"[614-810]THomoserine_dh
PS01042\"[660-682]THOMOSER_DHGENASE
InterPro
IPR002912
Domain
Amino acid-binding ACT
PF01842\"[324-379]T\"[400-460]TACT
InterPro
IPR005106
Domain
Homoserine dehydrogenase, NAD-binding
PF03447\"[472-606]TNAD_binding_3
InterPro
IPR011147
Family
Bifunctional aspartokinase/homoserine dehydrogenase I
PIRSF000727\"[1-815]TBifunctional aspartokinase/homoserine dehydrogenase I
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[462-647]Tno description
PTHR21499\"[111-815]TASPARTATE KINASE
PTHR21499:SF1\"[111-815]TASPARTATE KINASE


","BeTs to 20 clades of COG0527COG name: AspartokinasesFunctional Class: EThe phylogenetic pattern of COG0527 is aompkzyqvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-49) to 5/5 blocks of the IPB001342 family, which is described as \"Homoserine dehydrogenase\". Interpro entry for IP:IPR001342. IPB001342A 466-487 2.6e-07 IPB001342B 605-616 0.00011 IPB001342C 634-644 0.001 IPB001342D 660-688 3.5e-19 IPB001342E 790-809 1.4e-08Significant hit ( 8.1e-44) to 5/5 blocks of the IPB001341 family, which is described as \"Aspartokinase, N-terminus\". Interpro entry for IP:IPR001341. IPB001341A 1-13 4.8e-05 IPB001341B 35-45 0.15 IPB001341C 126-136 0.44 IPB001341D 200-233 3.1e-22 IPB001341E 433-459 1.6e-07","Residues 184 to 274 match (1e-09) PD:PD547421 which is described as KINASE PROTEOME COMPLETE ASPARTATE ","","","","","","","","","","","","Fri May 20 11:32:53 2005","","Fri May 20 11:32:53 2005","Fri May 20 11:32:53 2005","Fri May 20 11:32:53 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA02357 is paralogously related to AA00596 (4e-04).","Fri May 20 11:32:53 2005","","","","","Residues 614 to 810 (E-value = 1.6e-100) place AA02357 in the Homoserine_dh family which is described as Homoserine dehydrogenase (PF00742)","Fri May 20 11:32:53 2005","","","","","","","1","","","" "AA02358","1617268","1618209","942","ATGTTACGAATCTATGCGCCCGCTTCCAGTGCCAATATCAGTGTCGGTTTCGACACGCTGGGCGTGGCAATTTCGCCGATTGACGGTTCACTGTTGGGCGATGTGGTACAAATTGAACCTATCGCCGACGGTTTTGAACTGGAAAGTGCGGGCTATTTTGTGCGTAAATTACCGAAAGAACCGCAAAAAAACATCGTTTATCAGGCATATGTGCTATTCACCGAACGGCTCAAATTACGCAATGTGAAGGTGAAGTCCTTACGCCTAACCTTAGAAAAGAATATGCCGATCAGTTCCGGTTTAGGCTCCAGCGCCTGCTCTATCGTTGCGGCTCTGGTGGCGCTGAACAAATACCATAATGAGCCTTTTTCCAAAATGGAATTATTAGAAATGATGGGCGAATTGGAAGGTCGGATTTCCGGTTCCATTCATTATGATAATGTTGCACCTTGCTATTTAGGCGGTGTACAGTTTATGGTGCAATCCCTCGGCAATATTTGCCAGAAATTGCCATTTTTTGACCACTGGTATTGGGTGTTGGCATACCCCGGCATTGAAGTTTCCACGGCAGAAGCCCGTGCCATTTTGCCCAAAAGCTACACCCGTCAGGATGTGATTGCACACGGTCGCCACCTTGGCGGATTTGTGCACGCTTGCCATACGCAGCAGGAAAATCTGGCGGCAATGATGATGAAAGATGTCATCGCGGAACCTTATCGTGAAGCTTTGCTGCCGAACTACCCGGAAGTCAAACAGGCAACCCGTGATTTAGGCGCACTAGCCACCGGGATTTCCGGTTCCGGACCGACGATTTTCGCTATCGCACCGGATTTAAATTATGCTACCAAACTGGCAACTTATTTAGAGAACCACTATTTACAAAACAATGAAGGCTTTGTACATATCTGCAAAGTCGATAATGCCGGTACCAGAGAACTGGGC","","","34500","MLRIYAPASSANISVGFDTLGVAISPIDGSLLGDVVQIEPIADGFELESAGYFVRKLPKEPQKNIVYQAYVLFTERLKLRNVKVKSLRLTLEKNMPISSGLGSSACSIVAALVALNKYHNEPFSKMELLEMMGELEGRISGSIHYDNVAPCYLGGVQFMVQSLGNICQKLPFFDHWYWVLAYPGIEVSTAEARAILPKSYTRQDVIAHGRHLGGFVHACHTQQENLAAMMMKDVIAEPYREALLPNYPEVKQATRDLGALATGISGSGPTIFAIAPDLNYATKLATYLENHYLQNNEGFVHICKVDNAGTRELG","1618209","","homoserine kinase","Cytoplasm","","
InterPro
IPR000870
Family
Homoserine kinase
PR00958\"[9-24]T\"[102-117]T\"[142-155]T\"[180-197]T\"[259-274]THOMSERKINASE
PIRSF000676\"[2-313]THomoserine kinase
TIGR00191\"[2-313]TthrB: homoserine kinase
InterPro
IPR006203
Domain
GHMP kinase, ATP-binding region
PS00627\"[95-106]?GHMP_KINASES_ATP
InterPro
IPR006204
Domain
GHMP kinase
PF00288\"[88-155]TGHMP_kinases_N
InterPro
IPR013750
Domain
GHMP kinase, C-terminal
PF08544\"[215-294]TGHMP_kinases_C
InterPro
IPR014721
Domain
Ribosomal protein S5 domain 2-type fold
G3DSA:3.30.230.10\"[2-119]Tno description
noIPR
unintegrated
unintegrated
PTHR20861\"[42-314]THOMOSERINE/4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE


","BeTs to 18 clades of COG0083COG name: Homoserine kinaseFunctional Class: EThe phylogenetic pattern of COG0083 is -ompkzyqvdrlbce-ghs-uj----Number of proteins in this genome belonging to this COG is","Significant hit ( 4e-46) to 5/5 blocks of the PR00958 family, which is described as \"Homoserine kinase signature\". Prints database entry for PR:PR00958. PR00958A 9-24 2.8e-08 PR00958B 102-117 2.6e-06 PR00958C 142-155 5.1e-08 PR00958D 180-197 7.1e-09 PR00958E 259-274 2.9e-08","Residues 2 to 155 match (4e-07) PD:PD323924 which is described as DECARBOXYLASE BIOSYNTHESIS KINASE MEVALONATE DIPHOSPHOMEVALONATE PROTEOME COMPLETE THREONINE HK ATP-BINDING ","","","","","","","","","","","","Tue Jan 7 11:34:50 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02358 is paralogously related to AA02745 (3e-04).","","","","","","Residues 86 to 279 (E-value = 3.7e-40) place AA02358 in the GHMP_kinases family which is described as GHMP kinases putative ATP-binding protein (PF00288)","","","","","Madsen,S.M., Albrechtsen,B., Hansen,E.B. and Israelsen,H. Cloning and transcriptional analysis of two threonine biosynthetic genes from Lactococcus lactis MG1614 J. Bacteriol. 178 (13), 3689-3694 (1996) PubMed: 8682767 Wizemann,T.M., Moskovitz,J., Pearce,B.J., Cundell,D., Arvidson,C.G., So,M., Weissbach,H., Brot,N. and Masure,H.R. Peptide methionine sulfoxide reductase contributes to the maintenance of adhesins in three major pathogens Proc. Natl. Acad. Sci. U.S.A. 93 (15), 7985-7990 (1996) PubMed: 8755589 Parsot,C. Evolution of biosynthetic pathways: a common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase EMBO J. 5 (11), 3013-3019 (1986) PubMed: 3098560 ","","Tue Jan 7 11:38:02 2003","1","","","" "AA02359","1618240","1618677","438","ATGAAAAAAATTCTTACCGCACTTTTTTGCAGTTGTCTCATTTCCCCTCTCACAAACGCTGAAACCTTGTCTGATGGTTTACCACCACAGGCAGCTGGTGATTATGTGTTCTTGGACCCGCATCAAAACAATACGGATATACAATTTCGTTTAAAACTTAAAGGCAAACAATGGCTGGCAGACGGTTCCCAAAATGCCGGCAAAAGCTGGTCGCCTGTGTGCGAAGTCAGTGGCGAATGCAAACTGGAGACATCCTCCAAAGCGGAAATCGAACGCTTCTTTGAGCAATATCCGCAAGTACTAAACCGAACAGATGTCAGCTGCATTCACAATATGGCGTTCGCTTTCTGCGGGTTAACTTTAGATAAAAAAACCGATTATGTGATGGTCGCATTAGTGACCAATCCGCCACAAGTCACATCGTATAACCGAATTAAG","","","16266","MKKILTALFCSCLISPLTNAETLSDGLPPQAAGDYVFLDPHQNNTDIQFRLKLKGKQWLADGSQNAGKSWSPVCEVSGECKLETSSKAEIERFFEQYPQVLNRTDVSCIHNMAFAFCGLTLDKKTDYVMVALVTNPPQVTSYNRIK","1618677","","hypothetical protein","Periplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-20]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Tue Jan 7 11:40:54 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02359 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02360","1618736","1620007","1272","ATGAATTTATACAACATCAAACACCCCGAAGAACAAGTCAATTTCGCTCAAGCAGTGCGCCAAGGGTTAGGCAAAGATCAAGGCTTATTTTTCCCGCAAAACATACCGCACTTAACGAATATCGACGAACTGTTGGCATTGCCGTTGATTGAACGCAGCCAAAAAATTCTCGGTGCGTTAATCGGTGAAGAAATCCCGCCGGCACAGCTTGAACAAGTGGTGCGCAACGCCTTCACCTTCCCCGCGCCGGTGGTGAAAGTGGAAGACAATATTTATGCGCTAGAATTATTCCACGGACCGACACTCGCCTTTAAAGATTTCGGCGGACGCTTCATGGCGCAAGCTTTAGCCACCGTACGCGGTGATGGCAAAATCACCATTTTAACCGCCACTTCCGGCGACACCGGCGCGGCGGTAGCGCATGCCTTCTACGGTTTAGACAATATTGAAGTGGTGATTTTATATCCGAAAGGCAAAATCAGCCCGTTACAGGAAAAACTCTTCTGCACCCTCGGCGGCAATATTCGCACCGTCGCTATCAACGCCGATTTCGATGCTTGCCAAGCGTTAGTGAAACAAGCTTTTGATGACGCCGAATTACGTCAAGCCATCGGCTTAAACTCTGCCAATTCCATCAATATCAGCCGCTTATTGGCGCAAGTGTGCTATTACTTTGAAGCGGCGGCGCAATTACCGAAAAAACAGCGTGAAAATCTCGTAGTCTCCGTGCCAAGCGGCAACTTCGGCAACCTCACCGCCGGCTTAATCGCCAAAACCCTTGGCTTGCCGATCAAACGCTTTATCGCCGCCACCAATGCAAACGACACCGTGCCGCGCTATTTACACAGTGGCAACTGGTCACCGAACGCCACCGTTGCCACCCTTTCCAACGCCATGGACGTTTCCCGCCCGAATAACTGGCCGCGTGTGGAAGAATTGTTCAAACGTAACGGCTGGACATTAACCGAATTACATTCCGCCGCCATTTCCGATGGGCAAACGGAAGAAACATTACGCGCAATGCACAAACTCGGTTATTTATGCGAGCCGCACGGCGCGGTGGCGTATGAGGTGCTTAAACAGGATTTACAAACGGGTGAAACCGGTTTATTCCTTTGCACCGCCCACCCGGCGAAATTCAAGGAATCTGTTGAGCGCATTCTGGATTTAACCCTGCCATTGCCGGAAGCCTTGGATAAACATAACAAACTGCCGTTGTTATCCGATGAAATGGAAAACGATTTTGCGCAGTTAAGAGCTTATTTGTTGAAA","","","46557","MNLYNIKHPEEQVNFAQAVRQGLGKDQGLFFPQNIPHLTNIDELLALPLIERSQKILGALIGEEIPPAQLEQVVRNAFTFPAPVVKVEDNIYALELFHGPTLAFKDFGGRFMAQALATVRGDGKITILTATSGDTGAAVAHAFYGLDNIEVVILYPKGKISPLQEKLFCTLGGNIRTVAINADFDACQALVKQAFDDAELRQAIGLNSANSINISRLLAQVCYYFEAAAQLPKKQRENLVVSVPSGNFGNLTAGLIAKTLGLPIKRFIAATNANDTVPRYLHSGNWSPNATVATLSNAMDVSRPNNWPRVEELFKRNGWTLTELHSAAISDGQTEETLRAMHKLGYLCEPHGAVAYEVLKQDLQTGETGLFLCTAHPAKFKESVERILDLTLPLPEALDKHNKLPLLSDEMENDFAQLRAYLLK","1620007","","threonine synthase","Cytoplasm","","
InterPro
IPR000634
Binding_site
Serine/threonine dehydratase, pyridoxal-phosphate-binding site
PS00165\"[95-109]TDEHYDRATASE_SER_THR
InterPro
IPR001926
Domain
Pyridoxal-5'-phosphate-dependent enzyme, beta subunit
PF00291\"[75-376]TPALP
InterPro
IPR004450
Domain
Threonine synthase
TIGR00260\"[50-396]TthrC: threonine synthase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1100\"[186-401]Tno description
G3DSA:3.90.1380.10\"[1-83]Tno description
PTHR10314\"[3-374]TSER/THR DEHYDRATASE, TRP SYNTHASE
PTHR10314:SF1\"[3-374]TTHREONINE SYNTHASE


","No hits to the COGs database.","Significant hit ( 1.9e-13) to 3/3 blocks of the IPB000634 family, which is described as \"Serine/threonine dehydratase pyridoxal-phosphate attachment site\". Interpro entry for IP:IPR000634. IPB000634A 94-108 2.5e-06 IPB000634B 243-253 0.11 IPB000634C 254-273 0.094 IPB000634B 130-140 0.62","Residues 260 to 385 match (5e-10) PD:PD005074 which is described as THREONINE SYNTHASE COMPLETE PROTEOME LYASE PHOSPHATE PYRIDOXAL BIOSYNTHESIS PROBABLE TS ","","","","","","","","","","","","Tue Jan 7 11:41:46 2003","","Fri May 20 13:22:53 2005","Fri May 20 13:22:53 2005","Fri May 20 13:22:53 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA02360 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Fri May 20 13:22:53 2005","","","","","Residues 75 to 376 (E-value = 4.3e-31) place AA02360 in the PALP family which is described as Pyridoxal-phosphate dependent enzyme (PF00291)","Fri May 20 13:22:53 2005","","","","Parsot,C., Cossart,P., Saint-Girons,I. and Cohen,G.N.Nucleotide sequence of thrC and of the transcription terminationregion of the threonine operon in Escherichia coli K12Nucleic Acids Res. 11 (21), 7331-7345 (1983)PubMed: 6316258","","Tue Jan 7 14:18:05 2003","1","","","" "AA02362","1620045","1620785","741","TTGACCGCACTTTTCTTACTGCCTATGACTACCCTCATCGCTTGGGGAAACATTCAAACGCCCTTCCCTTTTCAAGATATACCGTCGGCGCTCGTTCCGCCAAATTTACTCGCCTTAAACAGTGATAACCCGCGCGTGCAACAACGTTGGCAATGTCGCCGGCTGGCGCATTTTCTGTTGTGGCAGTTATTAAAAACGTCGGGAAAAACAACCGCAATTTTAGGACAAATTGCCCGCACAGCAAGCGGTCGTCCCTACTTTCCCGTTCCCGACATTGATTTCAATATCAGCCATTCCGGCGATTGGGTCGCGGTGATTTTTCATATTAACGACAACGGCGAAAAAAGTGCGGTCGGAATTGACATCGAATCGCCACGTAAAGAACGCCCTTACTTAGCCCTTTTGGCACATTTTGCGCCGGCTGAAGAAATCCGCTGGTTTCAACAACAACTCAATGAAAAATCGGCGTTTTATCGCATTTGGTGTTTGCGTGAAGCGGTGCTGAAATCCCAAGGCGCAGGCATTGTAAAATTATCGGAAGTCACCCATTTGCCAGACACGCAAGAGATTTATTCCCGTTACTGCCCGCGCGGGCAATTGATTTTTACTGCGGAACTGCCTTTTTATTTAGCGTTTTTCGTCAATCAAAATCCGCCGCATTCATTGCATTACTTTCTCTGGAATGGAAAACAATTTGAGGCGCAAACACCTTTGCAAAAAATTCGCTACGATGTGAACATT","","","28360","LTALFLLPMTTLIAWGNIQTPFPFQDIPSALVPPNLLALNSDNPRVQQRWQCRRLAHFLLWQLLKTSGKTTAILGQIARTASGRPYFPVPDIDFNISHSGDWVAVIFHINDNGEKSAVGIDIESPRKERPYLALLAHFAPAEEIRWFQQQLNEKSAFYRIWCLREAVLKSQGAGIVKLSEVTHLPDTQEIYSRYCPRGQLIFTAELPFYLAFFVNQNPPHSLHYFLWNGKQFEAQTPLQKIRYDVNI","1620785","","conserved hypothetical protein","Periplasm, Inner membrane, Cytoplasm","","
InterPro
IPR008278
Domain
4'-phosphopantetheinyl transferase
PF01648\"[118-180]TACPS
noIPR
unintegrated
unintegrated
PTHR12215\"[76-175]TPHOSPHOPANTETHEINE TRANSFERASE
signalp\"[1-16]?signal-peptide


","BeTs to 5 clades of COG2091COG name: Phosphopantetheinyl transferaseFunctional Class: QThe phylogenetic pattern of COG2091 is ------y-----bce--hs-------Number of proteins in this genome belonging to this COG is","","Residues 9 to 246 match (7e-66) PD:PD096555 which is described as PROTEOME COMPLETE PM0116 HI0152 ","","","","","","","","","","","","Tue Jan 7 14:22:48 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02362 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 118 to 180 (E-value = 2.4e-06) place AA02362 in the ACPS family which is described as 4'-phosphopantetheinyl transferase superfamily (PF01648)","","","","","","","","1","","","" "AA02363","1620884","1622134","1251","ATGTCGTTAAACGGTTCAGATCAAGATCCTTGGGGCAAACCAACGCAAAACGGACAATCGTCAGGAAACTCCTCTTCCGATAAAAACGAAGGTCAGTCCAATTGGGATCGTTCTTCCAATTCACAAAAAAAGAACGAGCAATCACCGCCCGATTTAGAAGAAGTTTTCAATAATTTATTGAAAAAAATGGGCGGGAAAGGCGCCAAAAATAACAATTCCAATCATGCCAATTTGCCTTCCGGCTTAGGTAAATTATTGCCGATTGCCATTGCGGCAGGCGTGATTTTATGGGGCGCCAGCGGTTTTTATACCATCAAAGAAGCGGAGCGCGGCGTGGTGTTGCGTTTGGGGCAGTTCCATTCCATCGAACAACCGGGTTTAAACTGGAAACCGACCTTCATTGATCGCGTCATTCCGGTCAATGTGGAACGCGTACAGGAATTAAAAACTCAAGGCTCCATGCTGACACAAGATGAAAACATGGTGAAAGTGGAAATGACCGTGCAATATCGCGTGCAAAATCCTGAAAAATATTTATTCAGTGCCGTAAATGCCAACGACAGTTTAAACCAAGCCACCGACAGTGCATTGCGTTATGTTATTGGTCACATGACTATGAACGATATTTTGACTACCGGTCGTTCCGTGGTGCGTGAAAATACCTGGAAGGCACTGAATCAAATTATCGAGCCGTATGATATGGGCTTGGAAGTGATTGATGTGAACTTCCAATCCGCCCGTCCGCCGGAAGAAGTAAAAGACGCCTTCGACGACGCCATTAAAGCACAGGAAGACGAACAACGTTATATTCGTGAAGCGGAAGCCTATGCCCGTGAGAAAGAACCGATTGCACGCGGTAACGCCCAACGCATTTTGGAAGAAGCGACGGCCTATAAAGATCGTGTCGTGCTGGATGCCAAAGGGGAAGTGGAACGTTTCCAACCGCTGTTACCTGAATTTAAAGCCGCACCGGATGTTTTCCGTGAGCGTTTGTATATTCAATCGATGGAAAAAGTTATGGCGAATACACCGAAAGTGATGCTGGATGCCGCTAACGGCAATAACCTCACCGTACTACCGTTGGAACAGTTACTCAAAGGCAAAAAAACCTATTCCGCCAACGCCAATGGTGAAGAAATCCAACAAAGTGCGGTCAATTCTGCGCCTGTTTCCCGCAGCGAAAATCGGGCAAACACCCCGAACCGTCCATCAGAAATCGGAAATGAAAGTAGTCGTCAAGGGAGATTTAAC","","","46458","MSLNGSDQDPWGKPTQNGQSSGNSSSDKNEGQSNWDRSSNSQKKNEQSPPDLEEVFNNLLKKMGGKGAKNNNSNHANLPSGLGKLLPIAIAAGVILWGASGFYTIKEAERGVVLRLGQFHSIEQPGLNWKPTFIDRVIPVNVERVQELKTQGSMLTQDENMVKVEMTVQYRVQNPEKYLFSAVNANDSLNQATDSALRYVIGHMTMNDILTTGRSVVRENTWKALNQIIEPYDMGLEVIDVNFQSARPPEEVKDAFDDAIKAQEDEQRYIREAEAYAREKEPIARGNAQRILEEATAYKDRVVLDAKGEVERFQPLLPEFKAAPDVFRERLYIQSMEKVMANTPKVMLDAANGNNLTVLPLEQLLKGKKTYSANANGEEIQQSAVNSAPVSRSENRANTPNRPSEIGNESSRQGRFN","1622134","From Genbank:[gi:1170267] hflC and hflK could encode or regulate a protease.","hflK protein","Periplasm, Extracellular","","
InterPro
IPR001107
Family
Band 7 protein
PF01145\"[101-277]TBand_7
SM00244\"[100-260]TPHB
InterPro
IPR001972
Family
Stomatin
PR00721\"[107-129]T\"[154-175]T\"[189-206]TSTOMATIN
InterPro
IPR010201
Family
HflK
TIGR01933\"[102-362]ThflK: HflK protein
noIPR
unintegrated
unintegrated
PTHR10264\"[85-340]TSTOMATIN-RELATED
tmhmm\"[85-105]?transmembrane_regions


","BeTs to 22 clades of COG0330COG name: Membrane protease subunits, stomatin/prohibitin homologsFunctional Class: OThe phylogenetic pattern of COG0330 is aompkzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 5.9e-40) to 5/5 blocks of the IPB001972 family, which is described as \"Band 7 protein family/Stomatin\". Interpro entry for IP:IPR001972. IPB001972A 102-118 2.7e-05 IPB001972B 140-170 4.8e-06 IPB001972C 178-227 4.3e-07 IPB001972D 231-276 2.9e-16 IPB001972E 327-342 88","Residues 99 to 203 match (2e-07) PD:PD549319 which is described as PROTEOME PROTEASE ACTIVITY COMPLETE HFLK MODULATOR ","","","","","","","","","","","Tue Jan 7 18:25:58 2003","Tue Jan 7 17:11:26 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02363 is paralogously related to AA02365 (4e-14) and AA02591 (5e-12).","","","","","","Residues 102 to 277 (E-value = 9.5e-50) place AA02363 in the Band_7 family which is described as SPFH domain / Band 7 family (PF01145)","","","","","Noble,J.A., Innis,M.A., Koonin,E.V., Rudd,K.E., Banuett,F. and Herskowitz,I. The Escherichia coli hflA locus encodes a putative GTP-binding protein and two membrane proteins, one of which contains a protease-like domain Proc. Natl. Acad. Sci. U.S.A. 90 (22), 10866-10870 (1993) PubMed: 8248183 Banuett,F. and Herskowitz,I. Identification of polypeptides encoded by an Escherichia coli locus (hflA) that governs the lysis-lysogeny decision of bacteriophage lambda J. Bacteriol. 169 (9), 4076-4085 (1987) PubMed: 3040675 ","","Tue Jan 7 18:23:47 2003","1","","","" "AA02365","1622137","1623021","885","ATGCGTAAACTGTTATTACCTGTCATTTTAGTTATCATCGCTATCATCTACTCCAGTATCGTGGTGGTCACCGAAGGCACACGCGGTATTATGTTGCGTTTCGGCAAAGTACAACGCGATGCCGACAATAAAATTGCCATTTACACGCCGGGACTGCATTTTAAAATCCCGTTTATTGATAACCTGAAAGTGCTTGATGCACGTATTCAAACCTTAGACGGGCAAGCGGATCGTTTCGTTACTGTTGAGAAAAAAGACCTCTTGGTGGATTCCTACGTGAAATGGCGTATCAATGATTTAGGTCGTTTCTTCACCACGACCGGTGGTGGCGATTATGCACAAGCAGCCAACTTATTACGTCGTAAAGTCAATGACCGTTTGCGTTCCGAAATCGGTTCCCGCACCATTAAAGACATCGTTTCCGGTACACGAGGCGAACTCATGGTAGGCACGAAAAAAGCGCTCAACAGTGGGCAAGACAGCACCGCCGAACTGGGGATTGAAGTGCTCGACGTACGGATTAAACAAATTAACTTGCCGGATGAAGTGTCTTCCTCCATTTACCAGCGTATGCGCGCCGAACGGGATGCGGTAGCCCGTGAACACCGCTCTCAAGGTAAAGAAAAAGCGGCATTTATTCAGGCGGATGTAGATCGTAAAGTCACCTTAATTATCGCCAATGCGGAAAAAACCGCACAGGAATTACGCGGTGACGGCGACGCGACCGCAGCCAAAATCTTTGCCGATGCCTTTGGTAAAGAGCCTGAATTTTACAGCTTCATTCGTAGCCTGAAAGCCTATGAAAGCAGCTTCGCCGACTCGGACAATTTGTTGATTTTAAAACCGGACAGTGACTTCTTCCGTTTTATGCAATCACCAAGTAAA","","","33026","MRKLLLPVILVIIAIIYSSIVVVTEGTRGIMLRFGKVQRDADNKIAIYTPGLHFKIPFIDNLKVLDARIQTLDGQADRFVTVEKKDLLVDSYVKWRINDLGRFFTTTGGGDYAQAANLLRRKVNDRLRSEIGSRTIKDIVSGTRGELMVGTKKALNSGQDSTAELGIEVLDVRIKQINLPDEVSSSIYQRMRAERDAVAREHRSQGKEKAAFIQADVDRKVTLIIANAEKTAQELRGDGDATAAKIFADAFGKEPEFYSFIRSLKAYESSFADSDNLLILKPDSDFFRFMQSPSK","1623021","From Genbank:[gi|123094] hflC and hflK could encode or regulate a protease. ","hflC protein","Cytoplasm, Inner membrane","","
InterPro
IPR001107
Family
Band 7 protein
PF01145\"[19-208]TBand_7
SM00244\"[18-191]TPHB
InterPro
IPR010200
Family
HflC
TIGR01932\"[1-291]ThflC: HflC protein
noIPR
unintegrated
unintegrated
PTHR10264\"[4-250]TSTOMATIN-RELATED
signalp\"[1-26]?signal-peptide
tmhmm\"[5-23]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 2.6e-16) to 3/5 blocks of the IPB001972 family, which is described as \"Band 7 protein family/Stomatin\". Interpro entry for IP:IPR001972. IPB001972A 20-36 0.033 IPB001972B 65-95 6.1 IPB001972D 162-207 1.2e-10","Residues 101 to 154 match (2e-17) PD:PD155803 which is described as PROTEOME HFLC COMPLETE PROTEASE 3.4.-.- HYDROLASE TRANSMEMBRANE SERINE FOR MEMBRANE ","","","","","","","","","","","Tue Jan 7 18:29:47 2003","Tue Jan 7 18:29:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02365 is paralogously related to AA02363 (3e-14) and AA02591 (7e-12).","","","","","","Residues 20 to 208 (E-value = 1.4e-56) place AA02365 in the Band_7 family which is described as SPFH domain / Band 7 family (PF01145)","","","","","Banuett,F. and Herskowitz,I. Identification of polypeptides encoded by an Escherichia coli locus (hflA) that governs the lysis-lysogeny decision of bacteriophage lambda. J. Bacteriol. 169 (9), 4076-4085 (1987). PubMed: 3040675.","","Tue Jan 7 18:29:12 2003","1","","","" "AA02366","1623312","1623160","153","GTGATTCCTTTTCTGACTAAAGTTAAAACAAACGTTGAATCAATCAACGGGCATACTTTGCCGAAAAGCGAAAAAACGCGCGAGAAAGTGACCGCACTTTTGGGATCCCGGTCGCAAAATCAAGAAAAGTGCGGTGGGAATTTGGGGGTGTTT","","","5538","VIPFLTKVKTNVESINGHTLPKSEKTREKVTALLGSRSQNQEKCGGNLGVF","1623160","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:25:34 2004","Wed Feb 25 13:27:47 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02366 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 11:13:47 2004","","","","","","","","","","","","","1","","","" "AA02367","1623314","1623640","327","ATGAAAGCAATGAAACATCTTTTGGCTTCGCTGTTCGTGTTAGGTTCGGTGTTTGCGGGTTCTGCCGTGGCGGCGGAAAAAGCGGCTGAACCGGCGGTACAAACGGAGCAGCCGGCGGCAACGGCAGCGGTCGGTGAGAAAGTGAATATTAACACCGCCAGTGCTGCGGAAATTCAAAAAGCCCTTGTAGGCATCGGTGCGAAAAAAGCGGAAGCGGTGGTGCAGTATCGTGAAAAACACGGTAATTTCAGCGCCGTGGAGCAGTTGCTGGAAGTGCAGGGCATCGGCAAAGCGACCTTAGAAAAAAATCGCGACCGTATCGCCTTA","","","13083","MKAMKHLLASLFVLGSVFAGSAVAAEKAAEPAVQTEQPAATAAVGEKVNINTASAAEIQKALVGIGAKKAEAVVQYREKHGNFSAVEQLLEVQGIGKATLEKNRDRIAL","1623640","","conserved hypothetical protein","Inner membrane, Cytoplasm, Periplasm","","
InterPro
IPR003583
Domain
Helix-hairpin-helix DNA-binding, class 1
SM00278\"[57-76]T\"[87-106]THhH1
InterPro
IPR004509
Domain
Competence protein ComEA helix-hairpin-helix region
TIGR00426\"[46-109]TTIGR00426: competence protein ComEA helix-h
noIPR
unintegrated
unintegrated
PTHR21180\"[47-109]TFAMILY NOT NAMED
PTHR21180:SF4\"[47-109]Tgb def: ComEA protein-related protein
signalp\"[1-24]?signal-peptide


","BeTs to 11 clades of COG1555COG name: DNA uptake protein and related DNA-binding proteinsFunctional Class: LThe phylogenetic pattern of COG1555 is --------vdrlbcefghsnu-----Number of proteins in this genome belonging to this COG is","","Residues 48 to 102 match (4e-13) PD:PD011817 which is described as COMPLETE PROTEOME RNA-BINDING ACCESSORY TRANSCRIPTION SPT6 EMB-5 FIS CDNA DOMAIN ","","","","","","","","","","","","Tue Jan 7 18:31:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02367 is paralogously related to AA01213 (6e-12) and AA00939 (7e-04).","","","","","","","","","","","","","","1","","","" "AA02368","1623684","1624346","663","ATGTTCCTCGTCTTTTTTATTGGGCGCAGTTATAATACGGGGCATTTTTCAACCGCACTTGAGAGAACAAACATGAAGCAAAAAATTGTATTGGCGACCGGCAACCAAGGCAAGGTCAGAGAAATGGCGGATGTGTTGGCGGATTTCGGTTTTGACGTGATTGCGCAGACGGATTTGGGTATCGACAGCCCGGAAGAAACGGGGCTGACGTTCGTTGAAAATGCCATTTTAAAAGCGCGTTATGCCGCCGAAAAATCCGGTTTACCTGCCATTGCCGACGATTCCGGGTTGGTGGTTGACGCGTTGAACGGCGCGCCGGGGTTATATTCCGCACGCTATGCCGGCGAAGAGGGCAATGACGCGAAAAATCGCGCCAAATTATTGGCGGAATTAGCCCATGTGCCGGCTGAACAGCGCAAAGCCAAATTCGTCAGCACCATCGTGTTGTTGCAGCATCCAACGGATCCGTCACCGATTATCGCGCAAGGCGAATGCCATGGCGTCATTGCTTTTGAAGAAAAAGGCGAAAACGGGTTCGGTTACGACGCATTATTTTTCAGCCCGCAGCAGGGTTGTACCTTCGCCGAACTGGATACCGTCGAGAAAAAGAAAATTTCCCACCGCGCCCGCGCGTTAGCGGTGCTTAAAACGAAGTTGAGCGCA","","","24408","MFLVFFIGRSYNTGHFSTALERTNMKQKIVLATGNQGKVREMADVLADFGFDVIAQTDLGIDSPEETGLTFVENAILKARYAAEKSGLPAIADDSGLVVDALNGAPGLYSARYAGEEGNDAKNRAKLLAELAHVPAEQRKAKFVSTIVLLQHPTDPSPIIAQGECHGVIAFEEKGENGFGYDALFFSPQQGCTFAELDTVEKKKISHRARALAVLKTKLSA","1624346","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR002637
Family
Ham1-like protein
PTHR11067\"[25-215]TINOSINE TRIPHOSPHATE PYROPHOSPHATASE/HAM1 PROTEIN
PF01725\"[29-219]THam1p_like
TIGR00042\"[28-220]TTIGR00042: non-canonical purine NTP pyropho
noIPR
unintegrated
unintegrated
G3DSA:3.90.950.10\"[4-219]Tno description
PTHR11067:SF1\"[25-215]THAM1 PROTEIN-RELATED


","BeTs to 23 clades of COG0127COG name: Xanthosine triphosphate pyrophosphataseFunctional Class: FThe phylogenetic pattern of COG0127 is aompkzyqvdrlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is","Significant hit ( 6.7e-43) to 3/3 blocks of the IPB002637 family, which is described as \"Ham1 family\". Interpro entry for IP:IPR002637. IPB002637A 28-43 1.2e-07 IPB002637B 89-110 2.7e-14 IPB002637C 178-212 4.3e-18","Residues 28 to 212 match (5e-13) PD:PD387047 which is described as PROTEOME BH1160 COMPLETE ","","","","","","","","","","","","Wed Jan 8 08:31:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02368 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 29 to 219 (E-value = 5e-111) place AA02368 in the Ham1p_like family which is described as Ham1 family (PF01725)","","","","","","","","1","","","" "AA02369","1624388","1624708","321","ATGATTATCACCACTACACCTCACATTGAAGGCAAGCAAATCGTGGAATACAAACAACTGGTTTTCGGCGAAGTGGTCGCCGGATCGAATTTTATCCGTGATTTTTTTGCCGGCATCACCGACATTATCGGCGAACGTTCCGGTATGTATGAATCGCGTATCACCAAATCGCGCAAAGACGCTTTGGATGAAATGGAGAAAAATGCCAAAGCCTTGGGCGCCAATGCGGTTGTGGGGGTAGAAGTGAATTACACCACCATCACCTCCGATTCCAAAAGTATGTTCATGATCGTGGCAAGCGGCACCGCCGTGGTTGTGCGT","","","11650","MIITTTPHIEGKQIVEYKQLVFGEVVAGSNFIRDFFAGITDIIGERSGMYESRITKSRKDALDEMEKNAKALGANAVVGVEVNYTTITSDSKSMFMIVASGTAVVVR","1624708","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR002765
Family
Protein of unknown function DUF74
G3DSA:3.30.110.70\"[1-106]Tno description
PF01906\"[1-107]TDUF74


","BeTs to 11 clades of COG0393COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG0393 is aompk---v-rlbce-gh---j----Number of proteins in this genome belonging to this COG is","Significant hit ( 3.2e-21) to 2/2 blocks of the IPB002765 family, which is described as \"Domain of unknown function DUF74\". Interpro entry for IP:IPR002765. IPB002765A 44-83 7.7e-17 IPB002765B 99-107 0.0084","Residues 1 to 106 match (9e-37) PD:PD385470 which is described as COMPLETE PROTEOME SLL118 CC2377 PLASMID PXO2-45 PM1668 BH1111 PLCB MJ1413 ","","","","","","","","","","","","Wed Jan 8 08:32:59 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02369 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 107 (E-value = 6.8e-53) place AA02369 in the DUF74 family which is described as Domain of unknown function DUF74 (PF01906)","","","","","","","","1","","","" "AA02371","1624720","1625877","1158","ATGACTTTAAATCCCTTGGTGTTGCCTCCGCTGAGTTTATACGTTCATATTCCGTGGTGCGTGCAGAAATGCCCGTACTGCGATTTCAATTCGCACGCGCAAAAAGGCGTGATTCCCGAACAGGATTATGTGCAGCATTTGCTGGCGGATTTAACGGCGGATTTGGCGCGTTATCAGGAAAGCGTGCAACAACGTCCGCTTCATTCCATTTTCATCGGCGGCGGCACGCCGAGCCTGTTTTCCCCGGATACCATCGCGTATTTGTTAGCGCGGATAGAACAACACATTCCTTTTGCGCCGAATATCGAAATCACCTTGGAAGCCAATCCCGGCACGGCGGAAGCGGCGCGTTTTCGCGGTTATGCGCAGGCGGGCGTGAATCGAATTTCCATGGGCATTCAAAGTTTTTCCGATGAAAAATTGCAAAAGCTGGGGCGCATTCATAACGCCGAAGAAGCCAAAAGTGCGGTGGGTTTTGCCGGCGTTTCGCATCTACTCAGTTTCAATCTGGATTTAATGCACGGTTTGCCGAATCAAACCTTAAACGAGGCGCTGGACGATTTACGCCAAGCCATTGCACTGGCGCCGCCGCATTTGTCTTGGTATCAGCTCACCATCGAACCGAACACCATGTTTGCTTATCGCCCGCCGACGCTGCCCGACGATGACGAACTGTGGGATATTTTCGAGCAAGGGCATCAATTACTCACTGCCGCCGGTTATCAACAATACGAAACCTCTGCCTACGCCAAAGCGGGTTTTCAGTGCCAACATAATTTAAATTATTGGCGATTCGGCGATTATCTTGCCATCGGTTGCGGCGCACACGGCAAGCTCAATTTTCCTAATGGCAATATTCTGCGTTACAGCAAAACCAAGCACCCGAAAGGCTATATGCGCGGAGAGTATTTGTATGAGGAACGACTGGTGAGCGCGGAAGATCGTCCGTTCGAGTTCTTTATGAATCGCTTCCGCTTGTTGGAACCCGTCCCGAAAAGCGACTTTGAGCAGCTTACCGGCTTGCCTTTAAGTGCGGTAGAAAATGCCATCGTGTGGGCGCAGGAGCAAAAATTCATCACGGAAACCGACCGCACTTGGCAGATCACCGAGCACGGCAAATTATTTTTAAATGAACTGTTGGAACGCTTTTTGCCGGAA","","","44176","MTLNPLVLPPLSLYVHIPWCVQKCPYCDFNSHAQKGVIPEQDYVQHLLADLTADLARYQESVQQRPLHSIFIGGGTPSLFSPDTIAYLLARIEQHIPFAPNIEITLEANPGTAEAARFRGYAQAGVNRISMGIQSFSDEKLQKLGRIHNAEEAKSAVGFAGVSHLLSFNLDLMHGLPNQTLNEALDDLRQAIALAPPHLSWYQLTIEPNTMFAYRPPTLPDDDELWDIFEQGHQLLTAAGYQQYETSAYAKAGFQCQHNLNYWRFGDYLAIGCGAHGKLNFPNGNILRYSKTKHPKGYMRGEYLYEERLVSAEDRPFEFFMNRFRLLEPVPKSDFEQLTGLPLSAVENAIVWAQEQKFITETDRTWQITEHGKLFLNELLERFLPE","1625877","","oxygen-independent coproporphyrinogen III oxidase","Cytoplasm","","
InterPro
IPR004559
Family
Putative oxygen-independent coproporphyrinogen III oxidase
TIGR00539\"[11-376]ThemN_rel: putative oxygen-independent copro
InterPro
IPR006638
Domain
Elongator protein 3/MiaB/NifB
SM00729\"[10-231]TElp3
InterPro
IPR007197
Domain
Radical SAM
PF04055\"[14-191]TRadical_SAM
InterPro
IPR010723
Domain
HemN, C-terminal
PF06969\"[260-374]THemN_C
noIPR
unintegrated
unintegrated
PTHR13932\"[1-385]TCOPROPORPHYRINIGEN III OXIDASE


","BeTs to 18 clades of COG0635COG name: Coproporphyrinogen III oxidase and related Fe-S oxidoreductasesFunctional Class: HThe phylogenetic pattern of COG0635 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-29) to 4/8 blocks of the IPB003401 family, which is described as \"Oxygen-independent coproporphyrinogen III oxidase\". Interpro entry for IP:IPR003401. IPB003401B 12-27 6.9e-07 IPB003401C 67-80 0.49 IPB003401D 103-148 5.5e-09 IPB003401E 164-208 8.5e-08","Residues 187 to 230 match (1e-07) PD:PD590025 which is described as COMPLETE PROTEOME III PORPHYRIN OXIDASE XF1507 FAMILY COPROPHORPHYRINOGEN OXIDOREDUCTASE OXYGEN-INDEPENDENT ","","","","","Sat Jan 25 14:35:04 2003","","","","","","","Wed Jan 8 08:37:19 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02371 is paralogously related to AA00194 (1e-21).","","","","","","Residues 260 to 374 (E-value = 2.3e-26) place AA02371 in the HemN_C family which is described as HemN C-terminal region (PF06969)","","","","","Layer G, Verfurth K, Mahlitz E, Jahn D. Oxygen-independent Coproporphyrinogen-III Oxidase HemN from Escherichia coli. J Biol Chem. 2002 Sep 13;277(37):34136-42. PMID: 12114526 Homuth G, Rompf A, Schumann W, Jahn D. Transcriptional control of Bacillus subtilis hemN and hemZ. J Bacteriol. 1999 Oct;181(19):5922-9. PMID: 10498703 Lieb C, Siddiqui RA, Hippler B, Jahn D, Friedrich B. The Alcaligenes eutrophus hemN gene encoding the oxygen-independent coproporphyrinogen III oxidase, is required for heme biosynthesis during anaerobic growth. Arch Microbiol. 1998 Jan;169(1):52-60. PMID: 939683","","Sat Jan 25 14:35:04 2003","1","","","" "AA02374","1625979","1626632","654","ATGGATCAACTTGAAATGAAAAAAATCGCCGCGCAAGCGGCTTTACAATTTGTGAAGCCGGAAATGATCGTGGGCGTAGGCAGCGGTTCTACCGTCAATTGTTTTATTGAAGCCTTGGGCGCGTTAAAAAATCAAATTAAAGGTGCGGTTGCGGCATCCAAAAAATCGGAAGAATTGTTGCGCCAACAAGGCATTGAGGTGTTCAGCACCAATGATGTTTCAGGTTTGGATATTTATGTGGACGGTGCCGATGAAATCAATCCGCAAAAAATGATGATTAAAGGCGGTGGTGCGGCGCTGACACGTGAAAAAATTGTGGCTGCACTAGCAAAAAATTTCATCTGCATTGTGGATAGTAGCAAGCAGGTTGATGTGTTAGGCTCTACTTTCCCGCTGCCAATCGAAGTGATTCCTATGGCGCGTTCGCAGGTGGCGCGTAAATTAGTGGCGTTAGGCGGCGCACCGGAATATCGCGAAGGCGTGGTGACCGATAACGGCAACATTATTTTGGATGTGCATAATTTTGAGATTATGAATCCGGTGGCGATGGAAAAAGAATTAAACGACATTGCGGGTGTGGTGACCAACGGCATCTTCGCGTTACGGTCGGCGGATACGGTAATTGTCGGCACCCCGAATGGCGCAAAAATCATT","","","23066","MDQLEMKKIAAQAALQFVKPEMIVGVGSGSTVNCFIEALGALKNQIKGAVAASKKSEELLRQQGIEVFSTNDVSGLDIYVDGADEINPQKMMIKGGGAALTREKIVAALAKNFICIVDSSKQVDVLGSTFPLPIEVIPMARSQVARKLVALGGAPEYREGVVTDNGNIILDVHNFEIMNPVAMEKELNDIAGVVTNGIFALRSADTVIVGTPNGAKII","1626632","","ribose 5-phosphate isomerase A","Cytoplasm","","
InterPro
IPR004788
Family
Ribose 5-phosphate isomerase
PD005813\"[9-126]TRPIA_HAEIN_P44725;
PTHR11934\"[1-218]TRIBOSE-5-PHOSPHATE ISOMERASE
PF06026\"[47-216]TRib_5-P_isom_A
TIGR00021\"[6-216]TrpiA: ribose 5-phosphate isomerase A
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1360\"[1-146]Tno description


","No hits to the COGs database.","","Residues 167 to 218 match (3e-09) PD:PD366044 which is described as ISOMERASE 5-PHOSPHATE RIBOSE PROTEOME COMPLETE PHOSPHORIBOISOMERASE PROBABLE A RIBOSE-5-PHOSPHATE REGULATION ","","","","","","","","","","","","Wed Jan 8 08:49:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02374 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 47 to 216 (E-value = 1.2e-98) place AA02374 in the Rib_5-P_isom_A family which is described as Ribose 5-phosphate isomerase A (phosphoriboisomerase A) (PF06026)","","","","","Rangarajan ES, Sivaraman J, Matte A, Cygler M.Crystal structure of D-ribose-5-phosphate isomerase (RpiA) from Escherichia coli.Proteins. 2002 Sep 1;48(4):737-40.PMID: 12211039","","Wed Jan 8 08:55:46 2003","1","","","" "AA02375","1626654","1627802","1149","ATGACAGTCAAAGTTTCATTAGATAAATCTAAAATCAAATTCGTGTTATTGGAAGGCGTTCACCAAAGCGCCTTAGACACCTTGCACGACGCAGGTTACACCAATATCGATTACCATAAAAAAGCCTTGGACGGCGATGAGTTGAAAGAGGAGATCAAAGATGCACATTTCATCGGTTTGCGTTCGCGCACCAATCTTACCGCCGACATGATTGCCGCCGCGCCGAAACTTATTGCAGTGGGCTGTTTCTGTATCGGCACCAACCAAGTGGATTTAAACGCCGCCAAAGCGCGCGGCATTCCGGTGTTTAATGCACCGTTCTCCAACACCCGTTCCGTGGCGGAGTTAGTGCTGGGCGAAATTTTGTTATTAATGCGCAACATCCCGCAAGCCAATGCCGAAGTGCATCGTGGGTTATGGAATAAATCCGCCGTAGGTTCACACGAAGTGCGCGGCAAAAAACTGGGTATCGTAGGTTATGGTCATATCGGCTCCCAGCTGAGCATCATTGCCGAATCTTTGGGGATGGATGTGCATTTCTATGACATTGAAAACAAGCTCCCGCTCGGTAACGCCAAACAAGTACGTAGCCTGGAGGAATTGCTCGGATCCTGTGATGTGATTTCCCTGCACGTGCCGGATTTGCCTTCCACCCGTAATTTAATCAGCGCGGAGCGCATCGCGCAGTTAAAGCAGGATTCCATTTTAATTAACGCGGCACGCGGCACGGTGGTGGATATTGACGCATTAGCAAAAGCTTTGGAAGAAGGCAAAGTGCGTGGTGCGGCAATTGACGTGTTCCCGAAAGAACCGGCTTCCATTAATGAAGAATTCGTTTCACCGTTACGCAAATTCGACAACGTGCTATTAACCCCGCATATCGGCGGTTCAACTGCCGAAGCGCAGGAAAATATCGGTTTTGAAGTGGCAGGTAAATTCGTGAAATATTCCGACAACGGTTCAACCCTGTCCTCCGTCAACTTCCCGGAAGTTTCCCTGCCGGAACACGCAGGCTCCAAACGCTTGTTGCACATTCACGAAAACCCGTCCGGGCGTGCTCAATCGCATCAACCAGATTTTCGTAGAAGCCAACGTGAATATCGCCGCACAATACTTACAAACCGACCCGAAAATCGGTTACGTCGTCAT","","","44596","MTVKVSLDKSKIKFVLLEGVHQSALDTLHDAGYTNIDYHKKALDGDELKEEIKDAHFIGLRSRTNLTADMIAAAPKLIAVGCFCIGTNQVDLNAAKARGIPVFNAPFSNTRSVAELVLGEILLLMRNIPQANAEVHRGLWNKSAVGSHEVRGKKLGIVGYGHIGSQLSIIAESLGMDVHFYDIENKLPLGNAKQVRSLEELLGSCDVISLHVPDLPSTRNLISAERIAQLKQDSILINAARGTVVDIDALAKALEEGKVRGAAIDVFPKEPASINEEFVSPLRKFDNVLLTPHIGGSTAEAQENIGFEVAGKFVKYSDNGSTLSSVNFPEVSLPEHAGSKRLLHIHENPSGRAQSHQPDFRRSQREYRRTILTNRPENRLRRH","1627883","From PF00389This enzyme catalyzes the oxidation of D-3-phosphoglycerate to 3-phosphohydroxypyruvate. This reaction is the first committed step in the 'phosphorylated' pathway of serine biosynthesis.","D-3-phosphoglycerate dehydrogenase","Cytoplasm","","
InterPro
IPR006139
Domain
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic region
PF00389\"[15-327]T2-Hacid_dh
InterPro
IPR006140
Domain
D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding
PF02826\"[118-295]T2-Hacid_dh_C
PS00065\"[155-182]TD_2_HYDROXYACID_DH_1
PS00670\"[201-223]TD_2_HYDROXYACID_DH_2
PS00671\"[230-246]TD_2_HYDROXYACID_DH_3
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[110-298]Tno description
PIRSF000121\"[11-375]TD-3-phosphoglycerate dehydrogenase with ACT domain
PTHR10996\"[6-348]T2-HYDROXYACID DEHYDROGENASE
PTHR10996:SF18\"[6-348]TD-3-PHOSPHOGLYCERATE DEHYDROGENASE


","BeTs to 20 clades of COG0111COG name: Phosphoglycerate dehydrogenase and related dehydrogenasesFunctional Class: EThe phylogenetic pattern of COG0111 is aompkzyqvdrlbcefghs-uj----Number of proteins in this genome belonging to this COG is","Significant hit ( 4e-72) to 5/5 blocks of the IPB002162 family, which is described as \"D-isomer specific 2-hydroxyacid dehydrogenase\". Interpro entry for IP:IPR002162. IPB002162A 89-126 4.2e-19 IPB002162B 152-164 8.5e-06 IPB002162C 198-211 0.00017 IPB002162D 218-267 2.5e-27 IPB002162E 282-301 9e-10","Residues 112 to 223 match (2e-14) PD:PD349508 which is described as PROTEOME COMPLETE DEHYDROGENASE OXIDOREDUCTASE REDUCTASE 2-HYDROXYACID HYDROXYPYRUVATE PYRUVATE D-ISOMER SPECIFIC ","","","","","","","","","","","Wed Jan 8 09:30:11 2003","Wed Jan 8 09:19:32 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02375 is paralogously related to AA01614 (3e-35) and AA02916 (4e-23).","","","","","","Residues 113 to 293 (E-value = 9.5e-97) place AA02375 in the 2-Hacid_dh_C family which is described as D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain (PF02826)","","","","","Bell JK, Pease PJ, Bell JE, Grant GA, Banaszak LJ.De-regulation of D-3-phosphoglycerate dehydrogenase by domain removal.Eur J Biochem. 2002 Sep;269(17):4176-84.PMID: 12199695Grant GA, Hu Z, Xu XL.Cofactor binding to Escherichia coli D-3-phosphoglycerate dehydrogenase induces multiple conformations which alter effector binding.J Biol Chem. 2002 Oct 18;277(42):39548-53.PMID: 12183470Grant GA, Hu Z, Xu XL.Amino acid residue mutations uncouple cooperative effects in Escherichia coli D-3-phosphoglycerate dehydrogenase.J Biol Chem. 2001 May 25;276(21):17844-50.PMID: 11278587Kawabata S, Terao Y, Hamada S. Molecular cloning, sequence and characterization of a novelstreptococcal phosphoglycerate dehydrogenase gene. Oral Microbiol Immunol. 2000 Feb;15(1):58-62. PMID: 11155166Tobey,K.L. and Grant,G.A.The nucleotide sequence of the serA gene of Escherichia coli andthe amino acid sequence of the encoded protein,D-3-phosphoglycerate dehydrogenaseJ. Biol. Chem. 261 (26), 12179-12183 (1986)PubMed: 3017965","","Wed Jan 8 09:27:14 2003","1","","","" "AA02378","1628021","1627893","129","TTGCCATCAGGACGTGATGTTGAGAAAGAAGAAATATTTTGCGAATCGAATATGTCGTTTTTGATTAGGCGCACTAAAAAAGTGCGGTGGAAAAACACAATGAATTTCCACCGCACTTTTTATCATGAC","","","5330","LPSGRDVEKEEIFCESNMSFLIRRTKKVRWKNTMNFHRTFYHD","1627893","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:28:17 2004","Wed Feb 25 13:28:17 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02378 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 11:12:45 2004","","","","","","","","","","","","","1","","","" "AA02379","1628094","1628183","90","TTGATAGAATTCAGGGCGTTTAAAAAACATGATTTTTTATCACCGCACTTTCCCTTTGTTTTAGGTAATAAAGGTCTCTTTCACTTCGAT","","","3587","LIEFRAFKKHDFLSPHFPFVLGNKGLFHFD","1628183","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:31:03 2004","Wed Feb 25 13:31:03 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02379 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 11:11:51 2004","","","","","","","","","","","","","1","","","" "AA02380","1628197","1629240","1044","ATGAAGTTTAAAACGCTACTTGGCGCGCTCTTATTGAGCGTGTTTTCCACTTCCGTTTGGGCTGATCGCGTGATTACCGATCAACTTGATCGACAAGTGACCATCCCCGACCATATTCATCGCGCTGTGATATTACAGCACCAGACCTTAAATCTCGCGGTGCAACTGGATGCCACCAAACAAATTGCGGGCGTGCTTTCCAACTGGCAAAAACAGCTGGGCAAAGACTTCGTGCGCCTTGCGCCGGAATTGGCAAATTTACCGATGCCCGGTGATTTGAATACGGTCAATATTGAAAGCCTAATGGAAATCAAACCGGATGTTGTTTTCGTGACCAATTACGCGCCGAAAGAAATGATTGAAAAAATCAGCCAAATGAACGTGCCGGTGATTGCCATTTCGTTACGCAGCGGCGATAAAACCGAACAAAGCAAACTCAACCCGACCCTTGCCGATGAAAACAATGCCTACAACGAAGGGTTAAAACGCGGGATTGAAATTATTGCCGATGTTTTTGATAAAAAAGCGCAAGGTGAGGAATTGATTAAAGCCACATTCGCCAATCGCGAAATGCTGGCGGCACGCTTGGGCAATATTCCGGCGGAAAAACGCGTACGCACTTATATTGCCAACCCGAATCTCGGGACTTACGGCTCGGGCAAATATACCGGTTTAATGCTGGAGCATGCGGGGGCATATAATGTGGCGGCGGAAAGCGTAAAAGGCTTTCAAACGGTTTCTATGGAAGAAGTTTTAAAATGGAATCCTGCCGTTATTTTGGTGCAGGATCGTTATCCGAAAGTGGTGGATGACATTGTAAACGACAACGTGTGGGAGACCATTGAGGCAGTAAAAAATCATCGCGTATTGTTAATGCCCGAATATGCCAAAGCCTGGGGCTATCCGATGCCTGAAGCGATTGCGTTGGGCGAAGTATGGCTTGCCAAAGAACTTTACCCGGCGCTTTTTCGCGATGTGGATTTAGATAAAATGGTTAACGACTATTATTTGAAATTCTATCGCCAGCCTTATAAAGCAGCAAAA","","","39178","MKFKTLLGALLLSVFSTSVWADRVITDQLDRQVTIPDHIHRAVILQHQTLNLAVQLDATKQIAGVLSNWQKQLGKDFVRLAPELANLPMPGDLNTVNIESLMEIKPDVVFVTNYAPKEMIEKISQMNVPVIAISLRSGDKTEQSKLNPTLADENNAYNEGLKRGIEIIADVFDKKAQGEELIKATFANREMLAARLGNIPAEKRVRTYIANPNLGTYGSGKYTGLMLEHAGAYNVAAESVKGFQTVSMEEVLKWNPAVILVQDRYPKVVDDIVNDNVWETIEAVKNHRVLLMPEYAKAWGYPMPEAIALGEVWLAKELYPALFRDVDLDKMVNDYYLKFYRQPYKAAK","1629239","","iron chelatin ABC transporter,periplasmic-binding protein","Periplasm, Inner membrane, Cytoplasm","","
InterPro
IPR002491
Family
Periplasmic binding protein
PF01497\"[44-295]TPeripla_BP_2
PS50983\"[41-322]TFE_B12_PBP
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1980\"[38-186]T\"[202-318]Tno description
signalp\"[1-21]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","BeTs to 16 clades of COG0614COG name: ABC-type cobalamin/Fe3+-siderophores transport systems, periplasmic componentsFunctional Class: PThe phylogenetic pattern of COG0614 is aompkz--vdrlbcefgh-nuj----Number of proteins in this genome belonging to this COG is","","Residues 2 to 336 match (2e-09) PD:PD187492 which is described as COMPLETE PROTEOME CEUE IRON-BINDING ABC IRONIII PERIPLASMIC TRANSPORTER ","","","","","","","","","","","Wed Jan 8 09:43:28 2003","Wed Jan 8 09:33:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02380 is paralogously related to AA02154 (7e-09) and AA01827 (4e-04).","","","","","","Residues 44 to 296 (E-value = 1.5e-37) place AA02380 in the Peripla_BP_2 family which is described as Periplasmic binding protein (PF01497)","","","","","Van Hove B, Staudenmaier H, Braun V.Novel two-component transmembrane transcription control: regulation of iron dicitrate transport in Escherichia coli K-12.J Bacteriol. 1990 Dec;172(12):6749-58.PMID: 2254251Staudenmaier H, Van Hove B, Yaraghi Z, Braun V.Nucleotide sequences of the fecBCDE genes and locations of the proteins suggest a periplasmic-binding-protein-dependent transport mechanism for iron(III) dicitrate in Escherichia coli.J Bacteriol 1989 May;171(5):2626-33PMID: 2651410","","Wed Feb 5 14:49:33 2003","1","","","" "AA02381","1629970","1629332","639","ATGTCATACACAACTAACCAACTCATTGAAAAATTTCGTCAATTAAAAGTCGTGCCGGTGATTGCTTTAGACAACGCGGAAGATATTTTACCTCTGGCAGACACCTTGGCGCAAAATGGTTTGCCGGTGGCGGAAATCACCTTTCGCTCCCCTGCCGCCGCAGAAGCCATTCGTTTATTACGTCAACAGCGCCCGGAATTTCTGATTGCGGCGGGAACCGTATTGACCGCCGAACAGGTCGTCGCCGCTAAAAACAGCGGTGCAGATGTGGTCGTCACACCGGGATTTAATCCTAAAATCGTGCAATTATGTCAGGATTTAGCGTTGCCCATCACACCGGGGGTAAACAATCCGATGGCAATTGAAGCCGCGTTGGACGTCGGTATTGAAACCGTGAAATTCTTCCCGGCGGAAGCCTCTGGTGGCGTGAAAATGATTAAAGCCTTGTTAGGCCCTTACGCACAGTTGCAAATTATGCCGACCGGCGGTATCGGTATGCAGAATATTAAAGACTATCTGGCAATTCCCAATGTGGTGGCATGTGGCGGTTCTTGGTTTGTAGAAAAGAAACTTATCAATGAAAAAAGCTGGCAGGAAATCGGTCGGTTAACCAAAGAGGTGGCGGAATGGATCAACACT","","","22921","MSYTTNQLIEKFRQLKVVPVIALDNAEDILPLADTLAQNGLPVAEITFRSPAAAEAIRLLRQQRPEFLIAAGTVLTAEQVVAAKNSGADVVVTPGFNPKIVQLCQDLALPITPGVNNPMAIEAALDVGIETVKFFPAEASGGVKMIKALLGPYAQLQIMPTGGIGMQNIKDYLAIPNVVACGGSWFVEKKLINEKSWQEIGRLTKEVAEWINT","1629331","From PF01081This enzyme catalyzes the interconversion of 4-hydroxy-2-oxoglutarate into pyruvate and glyoxylate. ","4-hydroxy-2-oxoglutarate aldolase","Cytoplasm, Inner membrane","","
InterPro
IPR000887
Family
KDPG and KHG aldolase
PF01081\"[8-203]TAldolase
TIGR01182\"[8-211]Teda: 2-dehydro-3-deoxyphosphogluconate aldo
PS00159\"[40-49]?ALDOLASE_KDPG_KHG_1
PS00160\"[128-141]TALDOLASE_KDPG_KHG_2
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[5-212]Tno description


","BeTs to 11 clades of COG0800COG name: 2-keto-3-deoxy-6-phosphogluconate aldolaseFunctional Class: GThe phylogenetic pattern of COG0800 is --------v--lbcefghsnuj--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 9.5e-58) to 3/3 blocks of the IPB000887 family, which is described as \"KDPG and KHG aldolase\". Interpro entry for IP:IPR000887. IPB000887A 17-61 3.4e-23 IPB000887B 65-97 1.4e-16 IPB000887C 110-142 2.1e-15","Residues 83 to 138 match (5e-18) PD:PD328925 which is described as ALDOLASE COMPLETE PROTEOME 4-HYDROXY-2-OXOGLUTARATE KHG/KDPG 2-DEHYDRO-3-DEOXYPHOSPHOGLUCONATE LYASE INCLUDES: 2-KETO-4-HYDROXYGLUTARATE 2-KETO-3-DEOXY-6-PHOSPHOGLUCONATE ","","","","","","","","","","","Wed Jan 8 10:19:41 2003","Wed Jan 8 09:46:41 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02381 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 203 (E-value = 1.3e-116) place AA02381 in the Aldolase family which is described as KDPG and KHG aldolase (PF01081)","","","","","Vlahos CJ, Dekker EE.The complete amino acid sequence and identification of the active-site arginine peptide of Escherichia coli 2-keto-4-hydroxyglutarate aldolase.J Biol Chem 1988 Aug 25;263(24):11683-91PMID: 3136164 Vlahos,C.J. and Dekker,E.E.Active-site residues of 2-keto-4-hydroxyglutarate aldolase fromEscherichia coli. Bromopyruvate inactivation and labeling ofglutamate 45J. Biol. Chem. 265 (33), 20384-20389 (1990)PubMed: 1978721Patil,R.V. and Dekker,E.E.Cloning, nucleotide sequence, overexpression, and inactivation ofthe Escherichia coli 2-keto-4-hydroxyglutarate aldolase geneJ. Bacteriol. 174 (1), 102-107 (1992)PubMed: 1339418Egan,S.E., Fliege,R., Tong,S., Shibata,A., Wolf,R.E. Jr. andConway,T.Molecular characterization of the Entner-Doudoroff pathway inEscherichia coli: sequence analysis and localization of promotersfor the edd-eda operonJ. Bacteriol. 174 (14), 4638-4646 (1992)PubMed: 1624451","","Wed Jan 8 10:23:37 2003","1","","","" "AA02382","1631382","1629982","1401","ATGAAACAATTTATGGATGAAGATTTCCTTCTTTCAACAAATACAGCTAAAACGCTTTATCACGACTATGCAAAACATCAGCCTATTTTTGATTACCATTGTCATTTAAGTCCAAAAGAAGTGGCTGAAAATCGCCAATTTAAAGATTTAGCTGAAATTTGGTTAGAAGGTGATCACTATAAATGGCGTGCTTTACGCACAGCGGGTGTGCCGGAAGAATTAATTACAGGTAAAGCGAATAATTACCAAAAATATTTGGCTTGGGCAAGGACTGTTCCGCTTTGTATTGGCAATCCAATTTATCACTGGACCCATTTAGAACTACGTCGCCCTTTTGGTATTACCAACACATTATTTAATCCGCAAAACGCAGATAAAATTTGGCATCAGTGCAATGAAATGTTGCAACAGCCTGAATTTTCAGCGCGTAGTATTATGCAGCAAATGAATGTGAAATTGGTTGGAACAACAGATGATCCAATCGATTCATTGGAATATCATCAAGCGATAAAAAATGATGACAGCTTTGATATTGATGTCGTGCCAAGTTGGCGTCCGGATAAAGTCTTTAAAATTGAATTGCCACAATTCAATGATTATATCGCTCAGCTTGACCAAGTCACCGATGTTGATATTCGCTCATTTTCTGATTTACAAAAAGCATTAGTAAAACGCTTAAACCATTTTGATGAACAAGGTTGCAAATCGGCTGATCATGGTATGGAGATTGTTCGTTTTGCCCCAATTCCGGACGAATCTATACTCGATGCTATTCTTCAAAAACGTTTGCAAAATCAACCGCTCTTAGAAGAAGAAATTGCGCAATTTAGTACAGCAATTTTGGTATGGCTAGCTTCTGAATATTGTAAACGCCAATGGGTGATGCAAATGCATATTGGGGCAATCCGTAACAACAATAGTAGAATGTTTGCGTTGCTTGGTGCGGATAGTGGATTTGATTCTATTGGTGATCGTACTTATGCCGAGCCACTTTCTCATTTATTGGATGCAATGGATTGCCAAGATCAGTTACCAAAAACGATTTTGTATTGTTTGAATCCGCGTGATAACGAGGTGATTGGCAGTATGATTGGTAATTTCCAAACCGGTGGGGTAGCTGGCAAAATTCAATTTGGTTCAGGTTGGTGGTTTAATGACCAAAAAGATGGTATGGAACGTCAACTACAGCAACTTTCTCAATTGGGTTTATTAAGCCAATTTGTAGGTATGCTCACTGATTCACGTAGTTTCTTATCCTATACTCGCCACGAATATTTCCGTCGTATTTTATGTGAAATGGTCGGAAATTGGGTTGAAAATGGTGAAGTGCCAAACGATATCCCTTTATTAAGTAAAATGATTGAAGATATTTGTTTTAACAATGCAAAACGTTACTTTAAA","","","54140","MKQFMDEDFLLSTNTAKTLYHDYAKHQPIFDYHCHLSPKEVAENRQFKDLAEIWLEGDHYKWRALRTAGVPEELITGKANNYQKYLAWARTVPLCIGNPIYHWTHLELRRPFGITNTLFNPQNADKIWHQCNEMLQQPEFSARSIMQQMNVKLVGTTDDPIDSLEYHQAIKNDDSFDIDVVPSWRPDKVFKIELPQFNDYIAQLDQVTDVDIRSFSDLQKALVKRLNHFDEQGCKSADHGMEIVRFAPIPDESILDAILQKRLQNQPLLEEEIAQFSTAILVWLASEYCKRQWVMQMHIGAIRNNNSRMFALLGADSGFDSIGDRTYAEPLSHLLDAMDCQDQLPKTILYCLNPRDNEVIGSMIGNFQTGGVAGKIQFGSGWWFNDQKDGMERQLQQLSQLGLLSQFVGMLTDSRSFLSYTRHEYFRRILCEMVGNWVENGEVPNDIPLLSKMIEDICFNNAKRYFK","1629981","From Accession number: PF02614This is a family of Glucuronate isomerases also known as D-glucuronate isomerase, uronic isomerase, uronate isomerase, or uronic acid isomerase. This enzyme catalyses the reactions: D-glucuronate <=> D-fructuronate and D-galacturonate <=> D-tagaturonate.","glucuronate/uronate isomerase","Cytoplasm","","
InterPro
IPR003766
Family
Glucuronate isomerase
PF02614\"[1-467]TUxaC
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.140\"[98-466]Tno description


","BeTs to 3 clades of COG1904COG name: Glucuronate isomeraseFunctional Class: GThe phylogenetic pattern of COG1904 is --------v--lb-e------j----Number of proteins in this genome belonging to this COG is","Significant hit (3.6e-161) to 9/9 blocks of the IPB003766 family, which is described as \"Glucuronate isomerase\". Interpro entry for IP:IPR003766. IPB003766A 11-40 1.2e-20 IPB003766B 47-80 5e-19 IPB003766C 84-112 4.2e-23 IPB003766D 125-135 0.016 IPB003766E 167-203 1.6e-16 IPB003766F 228-241 2.2e-06 IPB003766G 258-301 1.8e-18 IPB003766H 302-320 6.9e-09 IPB003766I 390-434 3.1e-35","Residues 377 to 464 match (6e-30) PD:PD042971 which is described as ISOMERASE COMPLETE PROTEOME URONATE GLUCURONATE URONIC HRMI ACID HEXURONIC PLASMID ","","","","","","","","","","","Wed Aug 13 09:16:09 2003","Tue Dec 2 12:05:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02382 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 467 (E-value = 1.2e-295) place AA02382 in the UxaC family which is described as Glucuronate isomerase (PF02614)","","","","","","","","1","","7","" "AA02383","1632237","1631395","843","ATGAATATTGCAGCTAACCATAATTTAGAAAATAAATTGATCGTCATTACCGGTGCTGGCGGTGTGTTGTGCGCATTCTTAGCTAAACAACTCGCACACACTAAAGCAAATCTTGCTTTATTGGATATTAATTTTGAAGCGGCCGACAAAGTCGCACAAGAGATTAATCAAGCGGGCGGTCGTGCAAAAGCCTATAAAACAAATGTGTTAGAACTTGAAAATATTAAAGAAGTCAGAAATCAAATTGAAGCCGATTTCGGCACTTGTGACATTTTAATTAATGGTGCCGGTGGTAATAATCCAAAAGCGACTACCGATAATGAATTTCATCAATTTGACTTGAATGAAACAACAAAAACGTTCTTTGATTTAGATAAGTCAGGCATTGAATTTGTATTTAATCTAAACTATTTAGGTACATTATTACCTACACAGGTTTTTGCGAAAGATATGATTGGTAAAAAAGGTGCAAATATCATCAATATTTCAAGTATGAATGCCTTTACACCACTAACAAAAATTGCAGCTTATTCCGGTGCTAAAGCTGCAATTAGTAACTTCACGCAATGGCTTGCCGTTTACTTTTCTAAAGTAGGTCTTCGTTGTAATGCCATTGCACCTGGCTTTTTAGTCAGTAACCAAAATCGTGCATTGTTGTTTGATGCAGAAGGTAAACCAACCGCTCGCGCGAATAAAATTTTAACCAATACGCCAATGGGGCGTTTTGGTGAACCGGAAGAATTACTTGGTGCATTGTTATTCTTGATTGATGAAAATTATTCAAGTTTTGTCAATGGTGTGATCATGCCGGTTGATGGTGGGTTCTCTGCTTATAGCGGTGTG","","","30297","MNIAANHNLENKLIVITGAGGVLCAFLAKQLAHTKANLALLDINFEAADKVAQEINQAGGRAKAYKTNVLELENIKEVRNQIEADFGTCDILINGAGGNNPKATTDNEFHQFDLNETTKTFFDLDKSGIEFVFNLNYLGTLLPTQVFAKDMIGKKGANIINISSMNAFTPLTKIAAYSGAKAAISNFTQWLAVYFSKVGLRCNAIAPGFLVSNQNRALLFDAEGKPTARANKILTNTPMGRFGEPEELLGALLFLIDENYSSFVNGVIMPVDGGFSAYSGV","1631394","From PF00106The short-chain dehydrogenases/reductases family (SDR) is a very large family of enzymes, most of which are NAD- or NADP-dependent oxidoreductases. Most members of this family are proteins of about 250 to 300 amino acid residues. Most dehydrogenases possess at least 2 domains, the first binding the coenzyme, often NAD, and the second binding the substrate.","oxidoreductase","Cytoplasm","","
InterPro
IPR002198
Family
Short-chain dehydrogenase/reductase SDR
PR00080\"[87-98]T\"[157-165]T\"[177-196]TSDRFAMILY
PTHR19410\"[8-100]T\"[118-273]TSHORT-CHAIN DEHYDROGENASES/REDUCTASE FAMILY MEMBER
PF00106\"[12-196]Tadh_short
PS00061\"[164-192]?ADH_SHORT
InterPro
IPR002347
Family
Glucose/ribitol dehydrogenase
PR00081\"[13-30]T\"[87-98]T\"[151-167]T\"[177-196]T\"[198-215]T\"[238-258]TGDHRDH
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[8-275]Tno description
PTHR19410:SF62\"[8-100]T\"[118-273]TSHORT-CHAIN DEHYDROGENASE


","BeTs to 22 clades of COG1028COG name: Dehydrogenases with different specificities (related to short-chain alcohol dehydrogenases)Functional Class: Q,RThe phylogenetic pattern of COG1028 is ao-pkzyqvdrlbcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 5.6e-10) to 1/1 blocks of the IPB002198 family, which is described as \"Short-chain dehydrogenase/reductase (SDR) superfamily\". Interpro entry for IP:IPR002198. IPB002198 157-192 5.4e-10","Residues 68 to 108 match (1e-07) PD:PD328608 which is described as OXIDOREDUCTASE PROTEOME COMPLETE D-MANNONATE DEHYDROGENASE ALCOHOL SHORT-CHAIN PROBABLE ","","","","","","","","","","","Wed Jan 8 11:23:31 2003","Wed Jan 8 11:23:31 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02383 is paralogously related to AA00269 (4e-21), AA01179 (2e-09), AA00912 (2e-08), AA01109 (1e-05) and AA02205 (6e-05).","","","","","","Residues 14 to 275 (E-value = 9e-43) place AA02383 in the adh_short family which is described as short chain dehydrogenase (PF00106)","","","","","Jornvall H, Persson B, Krook M, Atrian S, Gonzalez-Duarte R, Jeffery J, Ghosh D.Short-chain dehydrogenases/reductases (SDR).Biochemistry 1995 May 9;34(18):6003-13PMID: 7742302 ","","Wed Jan 8 11:23:31 2003","1","","7","" "AA02384","1633193","1632252","942","ATGAAAAAAATAGCATTTATCGGCGAGTGCATGATTGAACTGAATGGAAAGCCATTTGGCGAAATGTGGCAAAGCTATGGTGGAGATACATTAAATTCGGCCACTTATCTTAGCCGAATGAGTTCGCCAAATGACATTCAAGTTTACTATGTTTCTGCGTTAGGCTCGGATAATTTAAGCGAGCAAATGCGAATGCATTGGCAAGCGGATGGGGTGAATACGGATTGGGTGTTAAAAGATGAAAACCACCAACCAGGTTTATATCTTATCCAGCTTGATGAACAAGGCGAGCGCACTTTTCTCTATTGGCGTAACCAATCTGCTGCTCATTATATGGTACAACATCATGATTTTTCACAGGTTTTATCAGCACTAGAACAAGTGGATATGATTTACTTGAGTGGCATTTCACTTGCGATCTTACCTAAAAATGACCGCACTTTTTTGCTTGAACAGCTTATAAAATTAGCTAAAAAAGGCGTGCAAATCTCTTTTGATAGTAATTTTAGACCTAAACTCTGGGATTCATTCCAAGAGGCTCAAGATTGTTATTTGCAATTATTACCTTGTGTGAGTCTCGCGCTTGTTACCTTTGATGATGAGCAATTATTGTGGAACGATACAAATGAACCGGCCACGCTAACGCGCTTACATCAAATTGGCATACCAAAAGTAGTTGTAAAGTGCGGTCGAAATGGTGCGATTTTTTCAGATTCTCAAACTTCTCAATATGGACAAGTTGTGCCGAAACCTATTTCAAATGTTGTTGACACCACATCAGCAGGAGATTCTTTTAATGCCGGCTTTTTGAATGGTTATTTACGAAATAAACCTTTAGACATTTGCTGCCGACAAGGCAATTATGTCGCGGGCATTGTGATTCAACATAAAGGCGCGATTATTGATAAACACGCCACTTCTCATCTTCAATCTGAATTTAAT","","","37216","MKKIAFIGECMIELNGKPFGEMWQSYGGDTLNSATYLSRMSSPNDIQVYYVSALGSDNLSEQMRMHWQADGVNTDWVLKDENHQPGLYLIQLDEQGERTFLYWRNQSAAHYMVQHHDFSQVLSALEQVDMIYLSGISLAILPKNDRTFLLEQLIKLAKKGVQISFDSNFRPKLWDSFQEAQDCYLQLLPCVSLALVTFDDEQLLWNDTNEPATLTRLHQIGIPKVVVKCGRNGAIFSDSQTSQYGQVVPKPISNVVDTTSAGDSFNAGFLNGYLRNKPLDICCRQGNYVAGIVIQHKGAIIDKHATSHLQSEFN","1632251","","2-dehydro-3-deoxygluconokinase","Outer membrane, Cytoplasm","","
InterPro
IPR002173
Family
Carbohydrate kinase, PfkB
PS00584\"[257-270]TPFKB_KINASES_2
InterPro
IPR011611
Domain
PfkB
PF00294\"[1-306]TPfkB
noIPR
unintegrated
unintegrated
G3DSA:3.40.1190.20\"[3-301]Tno description
PTHR10584\"[5-302]TSUGAR KINASE RELATED
PTHR10584:SF35\"[5-302]T2-DEHYDRO-3-DEOXYGLUCONOKINASE


","BeTs to 17 clades of COG0524COG name: Sugar kinases, ribokinase familyFunctional Class: GThe phylogenetic pattern of COG0524 is aompkzy-vdrlbcefghs--j----Number of proteins in this genome belonging to this COG is","Significant hit ( 2.6e-10) to 2/2 blocks of the IPB002173 family, which is described as \"PfkB family of carbohydrate kinases\". Interpro entry for IP:IPR002173. IPB002173A 26-41 0.085 IPB002173B 256-270 1.1e-06","Residues 14 to 299 match (4e-12) PD:PD008398 which is described as KINASE COMPLETE PROTEOME RIBOKINASE TRANSFERASE ADENOSINE SUGAR FRUCTOKINASE CARBOHYDRATE PURINE ","","","","","","","","","","","","Wed Jan 8 11:45:37 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02384 is paralogously related to AA00212 (1e-16), AA02797 (8e-09) and AA00333 (2e-04).","","","","","","Residues 3 to 306 (E-value = 1.3e-83) place AA02384 in the PfkB family which is described as pfkB family carbohydrate kinase (PF00294)","","","","","","","","1","","7","" "AA02385","1634240","1633251","990","ATGCAAATCAAAAAAAATGTTTTTTCTTATGCATTGGTCTTGGCGTTATCAGCTGGGATGGCGTTCTCAGCTTCTGCTAAAACCGTACTAAAATTAAGTCATAATAATGACAAAACTCACCCTGTGCATATTTCGATGCAATATATGGCAGATGAAGTTAAAAAATTAACAAATGGTGAAGTGGTGATCCGAATTTACCCAAATAGCCAGCTTGGTAGCCAGCGTGAATCAATGGAATTATTGCAATCCGGGTCACTAGATATGGCAAAATCAAACGCAAGTGAATTAGAAGCATTTGAGCCATCTTATGGTGCATACAATATTCCGTATCTTTTCCATAATGTTGATCATTATTATCGTGCTCTACTTGATCCTGAAGTTGGGCAAAAAATTCTTGATTCATCAAAGGGCAAAGGTTTCATTGGGTTGACTTATTATGATGGTGGTGCGCGTAGTTTCTATGCGGGTAAGGCAATTAAATCGCCTGCGGACCTCAAAGGTATGAAAATTCGCGTTCAACCAAGCCCAACCGCAGTAGAAATGATCAAATTAATGGGTGCTTCTCCAACACCTTTAGCTTATGGTGAACTCTATACCGCACTCCAACAAAAAGTGGTTGATGGCGCGGAAAATAACCAAACAGCATTAACCTTAGCTCGTCATGGTGAAGTGGCTAAATTCTTTAGTGAAGATGAACATACTATGATTCCTGATGTGCTCGTAATTGGTCAAAAATCTTGGGATAAATTAACTCCAGAACAACAAAATGCACTTAAAAAAGCCGCTGATGATTCAATGATGTATCACAAAGATTTATGGCAAAAAATGATTGCTGAAACCACTCAAGAAGCTAAAGATAAATTGGGTGTAGAATTTGTGAAAGTAGATAAACAACCTTTCATTGATGCAACAAAAAGCATGCATGATGCGGCAAAAGCCAATCCTTTGCTTAAAGAATACATTGAACGTATTGATAGTTTGGCAACCAAG","","","36623","MQIKKNVFSYALVLALSAGMAFSASAKTVLKLSHNNDKTHPVHISMQYMADEVKKLTNGEVVIRIYPNSQLGSQRESMELLQSGSLDMAKSNASELEAFEPSYGAYNIPYLFHNVDHYYRALLDPEVGQKILDSSKGKGFIGLTYYDGGARSFYAGKAIKSPADLKGMKIRVQPSPTAVEMIKLMGASPTPLAYGELYTALQQKVVDGAENNQTALTLARHGEVAKFFSEDEHTMIPDVLVIGQKSWDKLTPEQQNALKKAADDSMMYHKDLWQKMIAETTQEAKDKLGVEFVKVDKQPFIDATKSMHDAAKANPLLKEYIERIDSLATK","1633250","","dicarboxylate-binding periplasmic protein","Periplasm","","
InterPro
IPR004682
Family
TRAP dicarboxylate transporter- DctP subunit
PF03480\"[32-315]TSBP_bac_7
TIGR00787\"[32-288]TdctP: TRAP transporter solute receptor, Dct
noIPR
unintegrated
unintegrated
signalp\"[1-23]?signal-peptide
tmhmm\"[10-30]?transmembrane_regions


","BeTs to 7 clades of COG1638COG name: Dicarboxylate-binding periplasmic proteinFunctional Class: GThe phylogenetic pattern of COG1638 is --------v---bcefgh---j----Number of proteins in this genome belonging to this COG is","","Residues 233 to 326 match (4e-11) PD:PD220991 which is described as PROTEOME COMPLETE PERIPLASMIC C4-DICARBOXYLATE DICARBOXYLATE-BINDING PLASMID ABC BINDING SIGNAL PRECURSOR ","","","","","","","","","","","","Wed Jan 8 13:12:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02385 is paralogously related to AA02473 (1e-35).","","","","","","Residues 32 to 315 (E-value = 4.7e-94) place AA02385 in the SBP_bac_7 family which is described as Bacterial extracellular solute-binding protein, family 7 (PF03480)","","","","","","","","1","","7","" "AA02386","1634686","1634790","105","TTGAAAATTCTCCAATTAATCAAAATCGCTTACAACTTATCATTAACCTTATCAGTGTCTCATTTGCAGCCGTTATTATGTGCTATGGTGGATTTAAACTCGTTA","","","3862","LKILQLIKIAYNLSLTLSVSHLQPLLCAMVDLNSL","1634790","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 13:32:35 2004","Wed Feb 25 13:32:35 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02386 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 11:09:52 2004","","","","","","","","","","","","","1","","7","" "AA02387","1634953","1636251","1299","ATGGAATGGTCAAATATCATTATACTTTGCTCTAGTTTCTTCATGCTGCTATTTATTGGTGTACCAATTTCATTTTCTATCGGTATCGCATCACTTCTTACCATTATGCTATCAATTCCTTTTGATGCGGCTATTGCTGTAATTTCACAAAAAATGGCATCTGGCTTAGATAGTTTCTCCTTACTTGCTATTCCATTCTTTATTTTAGCCGGTAACATTATGAATCGCGGTGGCATTGCAATACGATTAATTGAATTTGCTAAAGTTATCGGAGGTCGCCTACCTGGTTCTCTTGCTCACGTAAACGTATTGGCTAACATGATGTTTGGTTCAATTTCAGGTTCCGCAGTAGCATCAGGTGCAGCGATGGGCGGGATTATGTCCCCATTACAAAAGAAAGAAGGTTATGACCCGTCTTTTTCTGCAGCTGTTAATATAGCGTCTTGCCCAACCGGATTATTAATTCCACCAAGTAATACCTTCATTGTGTATTCCTTGATTTCAGGTGGCACATCTATCGGCGCATTATTCCTTGCTGGTTACATTCCAGGTATTTTGATGGGACTATCGATCATGGTTATCGTCGCTGTTATTGCGAAAAAAAGAAAATACCCGGTTTCTCCAAAACCAACGCGTTCTGAAGCGATGAAAAAAACGCTGGATGCGTTACCAAGTCTTGGGTTGATCATTGTTATCATGGGAGGAATCATCGGCGGTATCTTCACTGCAACAGAAGCGTCTGCTTTCGCTGTTGTTTATACCTTAATTCTTGCCGTTGTTTTCTATCGTGAAGTAACCATCAAAGAATTACCAAAAATTATTTTAGATTCTGTTGTAACAACCGCCATTGTACTTCTCTTAATTGGTACATCAATGGGTATGTCTTGGGCAATGGCAAATGCGGATATTCCTTACACTATTAGTGATGCACTATTAAACATTTCTGACAATCCAATTGTTATCCTATTAATCATCAACATTATTCTATTAATTGTCGGCGTATTCATGGATATGACACCTGCATTACTTATTTTCACTCCAATTTTCTTACCTATCGTCACTGAATTAGGTATGGATCCGGTTCACTTTGGTGTATTAATGGCATTCAACCTTTCTATCGGTATCTGTACTCCACCGGTTGGTAGTGCATTATTCATCGGTTGTTCTGTTGGCGGCATAAAAATTAATCAGGTTATTAATCCATTGTTACCATTTTATTTTGCCCTCATTATGACGTTATTACTGGTGACTTATGTTCCATCATTAAGTTTAGCATTACCACGAATGTTATTAGGTTAT","","","46634","MEWSNIIILCSSFFMLLFIGVPISFSIGIASLLTIMLSIPFDAAIAVISQKMASGLDSFSLLAIPFFILAGNIMNRGGIAIRLIEFAKVIGGRLPGSLAHVNVLANMMFGSISGSAVASGAAMGGIMSPLQKKEGYDPSFSAAVNIASCPTGLLIPPSNTFIVYSLISGGTSIGALFLAGYIPGILMGLSIMVIVAVIAKKRKYPVSPKPTRSEAMKKTLDALPSLGLIIVIMGGIIGGIFTATEASAFAVVYTLILAVVFYREVTIKELPKIILDSVVTTAIVLLLIGTSMGMSWAMANADIPYTISDALLNISDNPIVILLIINIILLIVGVFMDMTPALLIFTPIFLPIVTELGMDPVHFGVLMAFNLSIGICTPPVGSALFIGCSVGGIKINQVINPLLPFYFALIMTLLLVTYVPSLSLALPRMLLGY","1636250","From Accession number: PF00597The function of this family is unknown.The proteins contain predicted transmembrane helices and may be membrane transport proteins.Members of this family are found in bacteria and archaea. ","integral membrane transport protein","Inner membrane, Cytoplasm","","
InterPro
IPR004681
Family
TRAP dicarboxylate transporter, DctM subunit
TIGR00786\"[20-427]TdctM: TRAP transporter, DctM subunit
InterPro
IPR010656
Domain
TRAP C4-dicarboxylate transport system permease DctM subunit
PF06808\"[10-423]TDctM
noIPR
unintegrated
unintegrated
signalp\"[1-26]?signal-peptide
tmhmm\"[5-39]?\"[53-73]?\"[103-123]?\"[164-198]?\"[219-241]?\"[247-262]?\"[277-299]?\"[318-336]?\"[341-361]?\"[371-393]?\"[402-422]?transmembrane_regions


","BeTs to 12 clades of COG1593COG name: Integral membrane protein, possible transporterFunctional Class: SThe phylogenetic pattern of COG1593 is ao---z--vd--bcefgh---j--t-Number of proteins in this genome belonging to this COG is","","Residues 56 to 199 match (1e-32) PD:PD014325 which is described as PROTEOME COMPLETE TRANSMEMBRANE MEMBRANE PERMEASE TRANSPORTER GLUCONATE INNER C4-DICARBOXYLATE PLASMID ","","","","","","","","","","","Wed Aug 13 10:28:13 2003","Wed Jan 8 13:25:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02387 is paralogously related to AA02474 (1e-79), AA01784 (1e-04), AA00136 (2e-04) and AA00615 (5e-04).","","","","","","Residues 138 to 295 (E-value = 4.7e-08) place AA02387 in the DedA family which is described as DedA family (PF00597)","","","","","","","","1","","7","" "AA02388","1636278","1638650","2373","ATGAAAACGATTAAAAATTGGCTTTTTGTAGAAAATCATAATCATCGCATTTATATTTCTTGTGATCATGGCTACCAACTTCATATTTTCGTATTAGAAAATGACATGTTGCGAGTTGCTTTCACGAAAAATAATGAATTTAAAGTGCCACATACTTGGGCAATTACACCAAATCAAACCGATGTTGATTGGCAAGGTCGTGATAAATGGTCATTAGTTGGTTTCTCATGTCCTGATTATGAAATCAAACAAACAGAAAAAACACTTGAAATTTCAACCGCACTTTTAAGGGTAACTATTCATCAACCACTCTATTTAGAATGGGAATATAAACAAGATGGGGAGTGGAAAACACTCTTTGCTGATAGAAAAACCGGTGCTTATTTAATGGGTATTTCAAGTACAGAAGTCTCTCATTATTTACAAAGAAGTGTCCAAGATCACTATTATGGTCTTGGCGAAAAAGCCGGTAATCTCAACCGTCACGGTCGTCGATTTGAAATGCGTAACCTTGATGCGATGGGCTATAACGCAGAATATACCGATCCACTTTATAAACATATTCCGTTTTATATTACTCACACAGAAGATGTTAGTTATGGTCTATATTACGATAATCTTGCGCCATGTTGGTTTATTTTAGGTAGTGAAATTGATAACTACCACGCTTATTACCGCACTTACAAAGCAGAAGACGGAAATCTTGATTACTACGTCATTTTAGGTCCTAAAATTTTAGATGTGACGAAAAAATATTGCCAATTAACCGGTGGCACTATCTTCGGCCCCAAATGGAGCTTGGGTTATAGCGGTTCTACAATGTATTACACCGATGCACCTGATGCACAAGAGCAACTTAAAAAATTCGTAGATTTATGCGATGAACATAACATTCCCTGTGATTCATTCCAGCTCTCATCAGGTTATACATCTATTAATGGGAAACGTTATGTCTTTAACTGGAATTATGACAAAGTTCCACAACCAAAAGAAATGACAAAACATTTCCACCATGCTGGAATGAAATTAGCTGCAAATATTAAACCTTGTTTATTACAAGACCATCCACGCTATCAAGAAGTGGAAAAATTAGGACTATTTATTAAAGATTCTGAATCTGATAGCCCTGAAAGATCCATGTTTTGGGATGATGAAGGTTCACATTTAGATTTTACTAATATGGATACTGTCAATTGGTGGAAAACAAATGTAAAACAGCAATTACTGGATTATGGTATTGATTCTACATGGAATGACAATAATGAATTTGAAGTGTGGGATAACCAAGCCAAATGCCATTATTTTGGAAAAGGTATGCCAATTAACTTATTACGCCCATTACAACCACTATTGATGATGAAATCATCTTATGAAGCGCAATTAGAGTATGCACCAAATAAACGCCCATATTTAATTTCTCGTTCAGGTTCTCCAGGCATGAATCGCTATGTTCAAACTTGGTCTGGTGATAACCGTACAAGCTGGAATACATTACGCTATAACATCAAAATGGGATTAGGGATGAGTCTCTCAGCCCTTTATAACGTCGGTCATGATGTTGGTGGTTTTTCAGGCGAGAAGCCAGATCCGGAGTTATTTGTCCGCTGGGTTCAAAATGGCGTGATGCACCCACGTTTTACCATTCACTCTTGGAATGATGACAAAACCGTCAACGAACCTTGGATGTATCCACAAGTGACAAATATTATTCGTGATGCAATTGAACTACGTTATGTATTAATGCCTTATTTATACAATACACTTTGGAAAGCACATCAAGATAACGAACCTATATTGCGTCCAACTTTCCTTGATCATGAACATGATAAAAACACATTTGCAGAAAATGATGATTATCTTCTTGGTGAAGATTTATTAGTCGCATCTGTGGTAGAACCAAATCAAAGAGTACGGGATGTTTATCTTCCACAAAATTTTGCAGGCTGGTATGACTTTTACACTCATAAATGGTTTAATGGCGGCGAAAAAATCACGGTAGATACGCCATTAGAAAGGATCCCTTTATTTTTAAGAGCTGGAAGTGTCATTCCAATGGCGAGAAAAGGTCATAAAAATACATTATCTGATGATTATCGAGAATTATTAATTATGCCTTTTATTAATCAAGGAGAAAGAAATATCACAGTGTTTGATGATGATGGCGAAAGTTTTGATTATCTCAAAGGTAAATATTTAGAGCTTCACATTCATCTAAAATGCACGAACCAAACAATAGAACTCAATTTAGAAAAATCAGGTGATTATTTACCTAAATACACAGAAATTAATTTCCGTCTTCCTGAAAATGAAAGAAGAAAATTAATCATTAATGGTAAATTAGCTAATCAAAACTATAAATTGAGTTTATCAAAC","","","92778","MKTIKNWLFVENHNHRIYISCDHGYQLHIFVLENDMLRVAFTKNNEFKVPHTWAITPNQTDVDWQGRDKWSLVGFSCPDYEIKQTEKTLEISTALLRVTIHQPLYLEWEYKQDGEWKTLFADRKTGAYLMGISSTEVSHYLQRSVQDHYYGLGEKAGNLNRHGRRFEMRNLDAMGYNAEYTDPLYKHIPFYITHTEDVSYGLYYDNLAPCWFILGSEIDNYHAYYRTYKAEDGNLDYYVILGPKILDVTKKYCQLTGGTIFGPKWSLGYSGSTMYYTDAPDAQEQLKKFVDLCDEHNIPCDSFQLSSGYTSINGKRYVFNWNYDKVPQPKEMTKHFHHAGMKLAANIKPCLLQDHPRYQEVEKLGLFIKDSESDSPERSMFWDDEGSHLDFTNMDTVNWWKTNVKQQLLDYGIDSTWNDNNEFEVWDNQAKCHYFGKGMPINLLRPLQPLLMMKSSYEAQLEYAPNKRPYLISRSGSPGMNRYVQTWSGDNRTSWNTLRYNIKMGLGMSLSALYNVGHDVGGFSGEKPDPELFVRWVQNGVMHPRFTIHSWNDDKTVNEPWMYPQVTNIIRDAIELRYVLMPYLYNTLWKAHQDNEPILRPTFLDHEHDKNTFAENDDYLLGEDLLVASVVEPNQRVRDVYLPQNFAGWYDFYTHKWFNGGEKITVDTPLERIPLFLRAGSVIPMARKGHKNTLSDDYRELLIMPFINQGERNITVFDDDGESFDYLKGKYLELHIHLKCTNQTIELNLEKSGDYLPKYTEINFRLPENERRKLIINGKLANQNYKLSLSN","1638649","","alpha-glucosidase","Cytoplasm, Extracellular","","
InterPro
IPR000322
Family
Glycoside hydrolase, family 31
PTHR22762\"[90-760]TALPHA-GLUCOSIDASE
PF01055\"[238-683]TGlyco_hydro_31
noIPR
unintegrated
unintegrated
PTHR22762:SF7\"[90-760]TNEUTRAL ALPHA-GLUCOSIDASE AB PRECURSOR (GLUCOSIDASE II ALPHA SUBUNIT) (ALPHA GLUCOSIDASE 2)


","BeTs to 5 clades of COG1501COG name: Alpha-glucosidases, family 31 of glycosyl hydrolasesFunctional Class: GThe phylogenetic pattern of COG1501 is ---p--y-v--lb-e------j----Number of proteins in this genome belonging to this COG is","Significant hit ( 2.9e-12) to 4/5 blocks of the IPB000322 family, which is described as \"Glycoside hydrolase family 31\". Interpro entry for IP:IPR000322. IPB000322B 336-351 1.2e+02 IPB000322C 374-399 2.2 IPB000322D 468-494 4.6e-08 IPB000322E 509-550 23","Residues 91 to 360 match (1e-09) PD:PD567346 which is described as COMPLETE PROTEOME LMO2444 LIN0221 LMO2446 LMO0182 CPE1046 LIN2538 LIN2540 ","","","","","","","","","","","","Wed Jan 8 13:32:42 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02388 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 81 to 764 (E-value = 6e-24) place AA02388 in the Glyco_hydro_31 family which is described as Glycosyl hydrolases family 31 (PF01055)","","","","","Kashiwabara,S., Azuma,S., Tsuduki,M. and Suzuki,Y.The primary structure of the subunit in Bacillusthermoamyloliquefaciens KP1071 molecular weight 540,000homohexameric alpha-glucosidase II belonging to the glycosylhydrolase family 31Biosci. Biotechnol. Biochem. 64 (7), 1379-1393 (2000)PubMed: 10945254","","Wed Jan 8 13:32:42 2003","1","","7","" "AA02389","1638668","1639420","753","ATGAACTTAGATGACTTACGATCCTATAAAAAAATAGGAAATGAATTAAAAGAACAACTTGCCAATCATCAATATCAAATAGGTGGTAAATTACCTGCTGAGCGAGATCTAGCTGAATATTTTAATGTTAGTCGTACAGTCATCAGAGAAGCACTCATCATGCTTGAAATTGAAAATCTCATCGAAGTACGAAAAGGTTCTGGTGTATATGTCATCGCCTTACCTCAGCGTGCTGCAAGCAATGATGATTTTTTGGATAAAGTGGATGTAGGCCCTTTTGAATTATTACAAGCCCGTCAGTTATTAGAAAGCAGTATGGCTGAATTTGCTGCATTACAAGCAACAAGAGCAGATATTACAAAATTGAAAGATATTCTAGCAACAGAACGAGCAACACTTGAGCAGGGTAATGAAGACTATGTTGCCGATGAAGATTTTCATCGCACCATTGCTGAAATTACTCAAAATGAAGTGATTGTACAAATGCAAAAAGCGCTCTGGGATCTCCGTGTTAATAGCCAAATGTGGAAAGGGCTTCATCTCCATATTCCAAATCAAAGTTATCGACATCTCTGGTTGCAAGATCATGAGAATATTATTACAGCATTGCAAAGAAAAGATCCTGCAATGGCTAAAAAAGCAATGTGGCAACATTTAGAAAATGTTAAACAAAAGCTCTTTGAATTATCAGATGTAGATGATCCTAATTTTGATGGCTATTTGTTTAACATGAGTCCAATTGTTGTTGAACGT","","","28990","MNLDDLRSYKKIGNELKEQLANHQYQIGGKLPAERDLAEYFNVSRTVIREALIMLEIENLIEVRKGSGVYVIALPQRAASNDDFLDKVDVGPFELLQARQLLESSMAEFAALQATRADITKLKDILATERATLEQGNEDYVADEDFHRTIAEITQNEVIVQMQKALWDLRVNSQMWKGLHLHIPNQSYRHLWLQDHENIITALQRKDPAMAKKAMWQHLENVKQKLFELSDVDDPNFDGYLFNMSPIVVER","1639419","","transcriptional repressor for uxu operon","Cytoplasm","","
InterPro
IPR000524
Domain
Bacterial regulatory protein GntR, HTH
PR00035\"[31-45]T\"[45-61]THTHGNTR
PF00392\"[8-71]TGntR
SM00345\"[12-71]THTH_GNTR
PS50949\"[6-74]THTH_GNTR
InterPro
IPR011711
Domain
GntR, C-terminal
PF07729\"[94-221]TFCD
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[1-74]Tno description
noIPR
unintegrated
unintegrated
PTHR11751\"[12-72]TSUBGROUP I AMINOTRANSFERASE RELATED
PTHR11751:SF1\"[12-72]TTRANSCRIPTION REGULATOR AMINOTRANSFERASE GNTR-RELATED


","No hits to the COGs database.","Significant hit ( 2.6e-19) to 1/1 blocks of the IPB000524 family, which is described as \"Bacterial regulatory proteins, GntR family\". Interpro entry for IP:IPR000524. IPB000524 31-71 2.5e-19","Residues 98 to 220 match (2e-07) PD:PD357532 which is described as COMPLETE PROTEOME TRANSCRIPTIONAL REGULATOR TRANSCRIPTION GNTR FAMILY PLASMID REGULATOR REGULATION ","","","","","","","","","","","","Wed Jan 8 14:56:02 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02389 is paralogously related to AA00081 (1e-04).","","","","","","Residues 8 to 71 (E-value = 5.4e-23) place AA02389 in the GntR family which is described as Bacterial regulatory proteins, gntR family (PF00392)","","","","","Hugouvieux-Cotte-Pattat N, Robert-Baudouy J.Regulation of expression of the uxu operon and of the uxuR regulatory gene in Escherichia coli K12.J Gen Microbiol. 1983 Nov;129 ( Pt 11):3345-53.PMID: 6420508Ritzenthaler P, Blanco C, Mata-Gilsinger M.Genetic analysis of uxuR and exuR genes: evidence for ExuR and UxuR monomer repressors interactions.Mol Gen Genet. 1985;199(3):507-11.PMID: 3929016","","Wed Jan 8 14:58:39 2003","1","","7","" "AA02390","1639443","1640624","1182","ATGGAACAAGCATGGCGTTGGTATGGCCCTAAAGATCCCGTTTCTTTATCAGATATTCGACAAGCCGGAGCAACCGGTATTGTCACCGCACTTCATCATATCCCTAACGGTGAAATTTGGAGCATTGAAGAAATCGAAAAACGTAAAAAAGAGGTTGAAAATGCCGGCTTAACATGGTCGGTGGTCGAAAGCGTGCCAGTTCACGAAGAAATCAAAACCCAAACCGGCAATTATCAAAAATGGATTGATAACTACAAACAAACCTTACGCAATTTAGCAAAATGCGGCATTGATACAGTTTGTTATAACTTTATGCCGGTTTTGGACTGGACAAGAACCGACTTAGCTTATGAGCTCCCTGACGGCTCAAAAGCGTTACGTTTTGATCAAATCGCCTTTGCAGCCTTTGAGCTTCATATTTTAAAACGCCCAGGTGCAGAACAAACCTATAACAAAGACGAAATAGCCGCAGCAAAAGCCTATTACGAAAAAATGAGTGATCAAGATATTCAACAGCTTACTCGTAATATTATTGCAGGCTTACCGGGGGCAGAAGAAGGCTATACCTTAGATGAATTTCAAGGTCAGTTAGATCGCTATAAAGATATTTCACCTGAAGTGTTCCACACTCACTTAGCTTATTTTTTAAATGAAATTGTACCGGTCGCTCAAGAAGTCGATATTAAAATGGCGATTCACCCTGATGATCCACCACGTCCAATTTTAGGTTTACCACGTATTGTATCCACCATTGAAGATATGCAATGGTTTGTCGAAACTCAACCATTACCGGCTAATGGCTTTACAATGTGTACCGGTTCTTATGGGGTGCGTTCTGATAATGATTTAGTGAAAATGACGGAACAATTTTCCGACCGAATTTATTTCGCACACTTACGTTCGACTCAACGTGAAGATAACCCATTAAGTTTCCATGAAGCCGCCCATTTAGAAGGTGATGTGGATATGTTCAACGTGGTAAAAGCCTTATTAACTGAAGAATATCGCCGATTAGATAACGGCGAAACTCGTTTAATCCCAATGCGTCCTGACCATGGTCATCAAATGTTGGATGATTTACATAAAAAAAACAATCCTGGCTATTCTGCTATCGGTCGATTAAAAGGTTTAGCTGAATTTCGTGGTTTAGAAATGGCATTAAAAAAAGTGTATTTCAATAAA","","","31813","MEQAWRWYGPKDPVSLSDIRQAGATGIVTALHHIPNGEIWSIEEIEKRKKEVENAGLTWSVVESVPVHEEIKTQTGNYQKWIDNYKQTLRNLAKCGIDTVCYNFMPVLDWTRTDLAYELPDGSKALRFDQIAFAAFELHILKRPGAEQTYNKDEIAAAKAYYEKMSDQDIQQLTRNIIAGLPGAEEGYTLDEFQGQLDRYKDISPEVFHTHLAYFLNEIVPVAQEVDIKMAIHPDDPPRPILGLPRIVSTIEDMQWFVETQPLPANGFTMCTGSYGVRSDNDLVKMTEQFSDRIYFAHLRSTQREDNPLSFHEAAHLEGDVDMFNVVKALLTEEYRRLDNGETRLIPMRPDHGHQMLDDLHKKNNPGYSAIGRLKGLAEFRGLEMALKKVYFNK","1640624","From PF03786This protein is required for hexuronate degradation.","mannonate dehydratase","Cytoplasm","","
InterPro
IPR004628
Family
Mannonate dehydratase
PF03786\"[1-389]TUxuA
TIGR00695\"[1-394]TuxuA: mannonate dehydratase
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.150\"[1-394]Tno description


","BeTs to 5 clades of COG1312COG name: D-mannonate dehydrataseFunctional Class: GThe phylogenetic pattern of COG1312 is ---p----v--lb-e--h---j----Number of proteins in this genome belonging to this COG is","","Residues 1 to 37 match (8e-16) PD:PD324615 which is described as COMPLETE PROTEOME HYDROLASE DEHYDRATASE MANNONATE D-MANNONATE LYASE DEHYDROLASE PLASMID ","","","","","","","","","","","Wed Jan 8 15:59:04 2003","Wed Jan 8 15:59:04 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02390 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 389 (E-value = 1.9e-275) place AA02390 in the UxuA family which is described as D-mannonate dehydratase (UxuA) (PF03786)","","","","","Blanco,C., Ritzenthaler,P. and Kolb,A.The regulatory region of the uxuAB operon in Escherichia coli K12Mol. Gen. Genet. 202 (1), 112-119 (1986)PubMed: 3083215","","Wed Jan 8 15:59:04 2003","1","","7","" "AA02391","1640665","1641219","555","TTGTTTATTCTCCCACTTCTGCCGTTAGCCGCTTTAGCACAGGATAATCTGACTTATGATAAACCTGTCCAAAGCATAATTAAAAGTGGCTCTATTGATTATTTTATCCAAGGGAAAGGTGGTCCTGGAGAGAAAAATAATCAAATTTGTGAAGATGGGTTGTTTTTTAACGATCATTATCTTGCCGTTTTTGATGGTGCTACTGATAAATCAGGCAAAAAATATGATAGTAAAAAAAGTGGACGCGTTAGTCGTGATATTATTCAAGATGTTTTTCAATCGTTACCTCCTAATACTGATAAAAAAGTAGTATTGCAAAAAATCAATGAGAAATTCAGAGAGTTTTATAACAAAAACTCCGATATGGATTTTGAGAAAAATCCTTTATTTAGACCAACGGCAACATTAATTTGGTACAACCTAGATTCAAATGAATTGGTTGCAATTGGTGATTCAAAAGCCAGAATTGATGGCGTGAATTACAATGATGAGGCTAAATATGTAGATGTTTTAAATAGTGCATTAAGAGTAAAAATTCTGAAATCTGAAAGATCT","","","20903","LFILPLLPLAALAQDNLTYDKPVQSIIKSGSIDYFIQGKGGPGEKNNQICEDGLFFNDHYLAVFDGATDKSGKKYDSKKSGRVSRDIIQDVFQSLPPNTDKKVVLQKINEKFREFYNKNSDMDFEKNPLFRPTATLIWYNLDSNELVAIGDSKARIDGVNYNDEAKYVDVLNSALRVKILKSERS","1641219","","hypothetical protein","Periplasm, Outer membrane","","
noIPR
unintegrated
unintegrated
signalp\"[1-13]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Jan 9 09:29:34 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02391 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","7","" "AA02392","1641652","1642539","888","ATGAAAAAATACACCGGCGAGCTTCTCCTTTTTATCGTCACATTCATTGCTGCATCAGGCTGGTTCTTTTCTAAATATTCTTTAGAAGGCATGCCTACAATGGGATTTATTGGCCTGCGTTTCACGTTGGCATGTCTAATTTTTCTGCCATTATCTTTTAAAGCAATAATTAAACTCACTACTTCTCAAAAATTAAAAGCGGCATCTGTAGGTTTGGCTTATATTGTCAATATGGTTCTATGGATTACCGGATTAATTTATAGTGAAGATTTGGGAGAAGGTGCTTTTTTATATAGTTTGGCAATGCTGATTGCGCCAGTGATATCTTGGATATTGTTTCAATATCAGCCTAAATATGTTTTTTGGTTTTGTTTACCACTTGCAATTTCTGGTTTATATTTGCTTTCAAATGAAGACGGAAAGGGATTACATCTCTCGTATGGTAATATACTCTTTTTACTAGCTTCATGTTCTGCAGCCTTATATTTTGTTTTAAATAATCAATTTTCTAAAAATATCCCAACCTTATCTTTAACTACGATTCAATTAGGTGTTATTGGTTTCTTAGCTGGAAGTTACTCGTTAATTTTTGAAAAATGGTATTTTCCTATTCCTGAAAATACTTGGTTTTGGTTTGTTGGCAGTACTCTTATAGCTACCAATCTGCGAGTGTTTTTACAAACAGTCGCGCAAAAGCATTGTGATATTAATAATGCAGCTATTATCATGTTATTAGAACTTATTTGGACAATGGTTTTTAGTACGATTATATTGAATGAGTCTATGAGCAGGCAAAAAATGTTAGGTTGTATTCTGATTTTAAGTGCACTTATTGTTTATTGTTTTCCTGGGATGTTAAAACGAAGAACAAATAAAGGTATGTTTTAT","","","33841","MKKYTGELLLFIVTFIAASGWFFSKYSLEGMPTMGFIGLRFTLACLIFLPLSFKAIIKLTTSQKLKAASVGLAYIVNMVLWITGLIYSEDLGEGAFLYSLAMLIAPVISWILFQYQPKYVFWFCLPLAISGLYLLSNEDGKGLHLSYGNILFLLASCSAALYFVLNNQFSKNIPTLSLTTIQLGVIGFLAGSYSLIFEKWYFPIPENTWFWFVGSTLIATNLRVFLQTVAQKHCDINNAAIIMLLELIWTMVFSTIILNESMSRQKMLGCILILSALIVYCFPGMLKRRTNKGMFY","1642539","","permease","Inner membrane, Cytoplasm","","
InterPro
IPR000620
Domain
Protein of unknown function DUF6, transmembrane
PF00892\"[15-137]T\"[157-282]TDUF6
noIPR
unintegrated
unintegrated
signalp\"[1-20]?signal-peptide
tmhmm\"[2-24]?\"[30-50]?\"[65-85]?\"[95-115]?\"[120-135]?\"[145-165]?\"[175-197]?\"[207-225]?\"[240-258]?\"[268-286]?transmembrane_regions


","BeTs to 15 clades of COG0697COG name: Permeases of the drug/metabolite transporter (DMT) superfamilyFunctional Class: G,E,RThe phylogenetic pattern of COG0697 is aompkzyqvd-lbcefghsnujxit-Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Thu Jan 9 09:31:48 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02392 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 157 to 282 (E-value = 4.2e-15) place AA02392 in the DUF6 family which is described as Integral membrane protein DUF6 (PF00892)","","","","","","","","1","","","" "AA02393","1644322","1642571","1752","ATGTTAAAAAAATGGTTTCTTTCTAAAAATGTGTTCTTGGCGGTTAAACCTTTCAGCGCGCTAAAAGACAGTTTTCGTGCGGGCTACAGCTCCCGTCATTTGGTCAAAGACATTATCGCCGGTCTCACCGTCGGGATTATCGCCATTCCGCTTTCCATGGCATTGGCAATCGCCAGCGGTGTGCCGCCACAGCATGGGTTATATACGGCCATTGTGGCGGGGATTATTATCGCCCTCGCCGGCGGTTCCCGCTTTAATATTTCCGGACCGACCGCCGCCTTTGTGGTGATTTTATATCCCGTCACCCAACAATTCGGGCTAAGCGGCTTATTGATGGCAACCCTGCTGTCGGGCATTATTCTGGTACTCATGGCGCTGTTCCGTTTAGGGCGATTAATCGAATATATTCCGTTGCCGGTCACGCTCGGCTTCACATCGGGTATCGGCATTGTTATCGCCACCTTGCAAATCAAGGATTTTCTCGGTTTAGACATTGTCCAAATGCCCTCTCATTACCTTGAAAAAATACAAGTAATTTTGACCGCACTTCCAAGCATCAACTGGGCGGATACCGCCGTCGGCGTCGTCACGCTGTTTGTCTTAACCCAATGGCACAAACTACGCCTGCCGATTCCGGGGCATTTGCCTGCGGTCATTATCGCCACCTTGTTATCGCTAGGGCTAACCCATTTCGGCTTTTCCGTCGTAACCATCGGATCTCAATTTCAATACACCCTATCCGATGGTAGCACCGGTTTTGGCATTCCAAGCGTTCTGCCGGAATTTGTCTTGCCGTGGAACATTCCCGATGCACAAGGTAATCTGATTAACTGGAACTTCGACACCATTCAAAGTTTGCTTCCTGCCGCATTTTCCATGGCGGTATTGGGTGCTATCGAATCCTTATTATGTGCGGTCGTATTAGACAATATGACCGACACCAAACACCATTCCAATAACGAACTGTTGGCGCAAGGTTTGGGCAATATCGCCTCCCCGTTCTTCGGCGGGATCACCGCCACTGCCGCCATCGCCCGTTCGGTGGTGAACGTCAAATCCGGTGCGGTCTCGCCGCTTTCCGGTGTAGTGCATGCGTTATTGGTGCTTTTCGCCCTGTTATTCTTCGCACCGGCACTTTCCTATTTACCGTTATCCTCCATGGCGGCGTTATTATTAGTCGTCGCCTGGCACATGGCGGATTTACCGCAAATCATTCAGCTCATCCGCCGCTCCGGACGCAATGAAATCACCGTGTTATTGGTTTGCTTGGTGCTCACGGTGCTTTTCGACATGGTTATCGCCATCTCGGTAGGCGTCTTACTGGCGAGTTTATTATTTATCCGCACCATTGCCGAAATGACCAAATCCATCAGCATTGCCGTGCCAGAGGATTTAGACGACGTGTTAATTTATCGTATCAGCGGACCGCTCTTTTTCGCGGCGGCAGATAATCTCTTCGCCGATTTGCACGATAAAACCGTGCACACGGATCACGAAATCAAACATATCGTTTTACAATGCGATGCCGTGACCGTGTTAGATACCGGGGGCATCCATGCCCTCACCCGCTTTGTGCAGCATATGCTTCCGCATCAACAACTTTATATGTGCAATATGCAATTCCAACCGCTGCGGACGATTGTCAAATCCGGTAGCCTGCCGGAAATCAAAAAAATCAACTTCGCCACGGATTTGCCGGAAGCATTGAATAAGATTCGGGAGTTTGAGGGAATCGAGGTGAAGAGTGAGAGT","","","62987","MLKKWFLSKNVFLAVKPFSALKDSFRAGYSSRHLVKDIIAGLTVGIIAIPLSMALAIASGVPPQHGLYTAIVAGIIIALAGGSRFNISGPTAAFVVILYPVTQQFGLSGLLMATLLSGIILVLMALFRLGRLIEYIPLPVTLGFTSGIGIVIATLQIKDFLGLDIVQMPSHYLEKIQVILTALPSINWADTAVGVVTLFVLTQWHKLRLPIPGHLPAVIIATLLSLGLTHFGFSVVTIGSQFQYTLSDGSTGFGIPSVLPEFVLPWNIPDAQGNLINWNFDTIQSLLPAAFSMAVLGAIESLLCAVVLDNMTDTKHHSNNELLAQGLGNIASPFFGGITATAAIARSVVNVKSGAVSPLSGVVHALLVLFALLFFAPALSYLPLSSMAALLLVVAWHMADLPQIIQLIRRSGRNEITVLLVCLVLTVLFDMVIAISVGVLLASLLFIRTIAEMTKSISIAVPEDLDDVLIYRISGPLFFAAADNLFADLHDKTVHTDHEIKHIVLQCDAVTVLDTGGIHALTRFVQHMLPHQQLYMCNMQFQPLRTIVKSGSLPEIKKINFATDLPEALNKIREFEGIEVKSES","1642571","","conserved hypothetical protein; possible sulfate transporter","Inner membrane, Cytoplasm","","
InterPro
IPR001902
Family
Sulphate anion transporter
TIGR00815\"[17-568]TsulP: sulfate permease
InterPro
IPR002645
Domain
Sulfate transporter/antisigma-factor antagonist STAS
PF01740\"[456-568]TSTAS
PS50801\"[466-572]TSTAS
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[306-453]Tno description
InterPro
IPR011547
Domain
Sulphate transporter
PF00916\"[124-450]TSulfate_transp
noIPR
unintegrated
unintegrated
PTHR11814\"[29-570]TSULFATE TRANSPORTER
PTHR11814:SF6\"[29-570]TSULFATE TRANSPORTER
signalp\"[1-21]?signal-peptide
tmhmm\"[38-58]?\"[67-87]?\"[106-126]?\"[135-155]?\"[178-200]?\"[215-235]?\"[288-308]?\"[355-375]?\"[381-401]?\"[416-447]?transmembrane_regions


","BeTs to 10 clades of COG0659COG name: Sulfate permease and related transporters (MFS superfamily)Functional Class: PThe phylogenetic pattern of COG0659 is ------yq--rlbcefgh--uj-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.6e-33) to 2/3 blocks of the IPB001902 family, which is described as \"Sulfate transporter\". Interpro entry for IP:IPR001902. IPB001902B 49-99 1.2e-11 IPB001902C 112-163 1.7e-20Significant hit ( 1e-06) to 2/2 blocks of the IPB002645 family, which is described as \"STAS domain\". Interpro entry for IP:IPR002645. IPB002645A 137-156 0.071 IPB002645B 321-335 0.0062","Residues 396 to 442 match (6e-07) PD:PD002020 which is described as SULFATE TRANSPORTER PROTEOME COMPLETE TRANSMEMBRANE PERMEASE ANION GLYCOPROTEIN FAMILY AFFINITY ","","","","","","","","","","","","Thu Jan 9 10:16:46 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02393 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 456 to 568 (E-value = 1.2e-16) place AA02393 in the STAS family which is described as STAS domain (PF01740)","","","","","","","","1","","","" "AA02395","1644753","1647167","2415","ATGATGAGAGCAAAAAAATCAGAATTACAAACCATACCGGTATTGCCATTGCGCGATGTTGTCGTGTTTCCTTACATGGTGATGCCGTTATTTGTCGGCAGACCGCGATCCATTAGCAGTCTTGACGAAGCCATGAATAATGAAAAACAGCTGTTGTTGGTTTCGCAAAAACAGGCGGAATTGGAAGAGCCGGGCATTGAAGATTTATATGATGTGGGCACTATTGCCAACATTATTCAGCTGCTAAAGTTGCCGGACGGCACAGTAAAAGTGTTGGTAGAAGGGCAACAACGCGCCAAAATTCATCATATTGAAGATTCCGGAGTGCATTTTCAGGCACAGATTGAGCCGTTGAACAGTACGCTTGGCAATAAGAAAGAATTGCAGGTCGTCCACAAAGCAGCGTTGGATGAATTTCAAAACTATTTGAATTTAAACAAAAAAGTTCAGCCTGATATTCTTTCCGCATTACAGCAAATTGAAAATCTTGAACAATTAAGTGATACCTTGGCGTCTCATTTGCCGGTTTCCGTCGCACAAAAACAGACCGTGCTGGAAATGAACAACGTAGTGGAACGTTTTGAATATTTGCTTGGTTTGATGCAATCGGAAGCGGATTTATTGCAGGTCGAAAAACGCATTCGCGGTCGCGTTAAGAAACAAATGGAAAAAAGCCAGCGCGATTATTATTTGAATGAGCAAATTAAAGCAATTCAAAAAGAGCTCGGTGAAGTAGAAAATACCGTGAGTGAAATTGAGCACCTGCGCCAAAAAATTGAACAGGCGAAAATGCCGTTGGAAGCGCACGAGAAAACCGAAGCCGAATTACAAAAATTAAAAATGATGTCGCCGATGTCGGCGGAAGCAACGGTGGTGCGCAGTTATATTGATTGGATGTTACAAGTGCCTTGGCACAAACGTAGTAAAGTGAAAAAAGATCTTGCCAAAGCGCAGGAAATTTTAGATGCCGATCATTACGGTTTGGAGCGGGTGAAAGAACGTATTCTGGAGTACCTTGCGGTGCAAACCCGTTTAAATCAGTTGAAAGGCCCGATTCTTTGTTTGGTGGGACCACCGGGGGTAGGTAAAACTTCTTTAGGACAGTCTATCGCCAATGCAACAGGGCGTAAATATGTGCGTATGGCGCTGGGGGGCGTGCGTGACGAAGCGGAAATTCGCGGTCACCGTAAAACTTACATTGGATCACTGCCGGGCAAACTTATTCAGAAAATGGCGAAAGTCGGTGTGAAAAACCCGCTCTTCCTGTTAGATGAAATTGATAAAATGTCTTCCGATATGCGCGGTGATCCGGCGTCTGCTTTGTTGGAAGTATTGGATCCGGAACAAAATGCCCACTTTAACGATCATTATCTGGAAGTGGATTATGATTTATCCGACGTAATGTTTGTGGCGACGTCCAACTCCATGCATATTCCGACCCCATTGTTGGATCGTATGGAAGTGATTCGTTTATCCGGTTATACGGAAGATGAAAAATTAAATATCGCCACCCGTCATTTAATCGCCAAACAAATGGAGCGTAATGGCTTAAAAACGGGTGAATTAACCATTGATGAAAGTGCGATTGTGGATATTATCCGCTACTATACCCGTGAAGCCGGAGTGCGTAATCTGGAACGTGAGATTTCGAAAATCTGTCGTAAGGCAGTAAAAACCTTACTGTTAGATAAGAAATTAAAATCCATCAAAGTGAATGCGAAGAACCTGCATGATTACCTTGGGGTAAAACGCTTTGAATTCGGTCGTGCCGATACGCAAAATCGCGTCGGTGAAGTCACCGGCTTGGCATGGACGGAAGTAGGTGGTGATTTACTCACCATTGAAACCGCGTCGGTGCCGGGCAAAGGCAAACTCAGCTATACCGGTTCTCTTGGTGATGTGATGAAAGAATCCATTCAAGCGGCGATGACCGTAGTGCGCTCCCGTGCGGATAAACTGGGCATTAACCCTGAATTCCACGAAAAACGTGATATTCACATCCATGTGCCGGACGGCGCCACACCGAAAGATGGCCCGAGCGCAGGGATTGCAATGTGCACCGCATTGGTTTCCTGTTTAACCGGCAATCCGGTGAAATCAGAGGTGGCGATGACCGGTGAAATCAGTCTGCGCGGCAAAGTGTTGCCGATTGGCGGTTTAAAAGAGAAGTTGCTGGCGGCACACCGTGGCGGAATTAAAACCGTGATTATTCCGAAAGATAATGTGAAGGATTTGGAAGATATTCCGGAAAATGCAAAACGTGATCTGAAGATTCATGCGGTGGAGACCATCGACGAAGTGCTAGGCCTTGCACTGGAAAATCCGCCGTTAGGCGTTGAGTTTGTCAAGCTGGATCCAATTTCGGCAGTGAAAAGCGGTCGTCGTAAGAAAACCGTTTCCAGAAGTGCGGTCAAT","","","89861","MMRAKKSELQTIPVLPLRDVVVFPYMVMPLFVGRPRSISSLDEAMNNEKQLLLVSQKQAELEEPGIEDLYDVGTIANIIQLLKLPDGTVKVLVEGQQRAKIHHIEDSGVHFQAQIEPLNSTLGNKKELQVVHKAALDEFQNYLNLNKKVQPDILSALQQIENLEQLSDTLASHLPVSVAQKQTVLEMNNVVERFEYLLGLMQSEADLLQVEKRIRGRVKKQMEKSQRDYYLNEQIKAIQKELGEVENTVSEIEHLRQKIEQAKMPLEAHEKTEAELQKLKMMSPMSAEATVVRSYIDWMLQVPWHKRSKVKKDLAKAQEILDADHYGLERVKERILEYLAVQTRLNQLKGPILCLVGPPGVGKTSLGQSIANATGRKYVRMALGGVRDEAEIRGHRKTYIGSLPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNAHFNDHYLEVDYDLSDVMFVATSNSMHIPTPLLDRMEVIRLSGYTEDEKLNIATRHLIAKQMERNGLKTGELTIDESAIVDIIRYYTREAGVRNLEREISKICRKAVKTLLLDKKLKSIKVNAKNLHDYLGVKRFEFGRADTQNRVGEVTGLAWTEVGGDLLTIETASVPGKGKLSYTGSLGDVMKESIQAAMTVVRSRADKLGINPEFHEKRDIHIHVPDGATPKDGPSAGIAMCTALVSCLTGNPVKSEVAMTGEISLRGKVLPIGGLKEKLLAAHRGGIKTVIIPKDNVKDLEDIPENAKRDLKIHAVETIDEVLGLALENPPLGVEFVKLDPISAVKSGRRKKTVSRSAVN","1647167","From Genbank:[gi:1170813] This enzyme degrades short-lived regulatory and abnormal proteins in the presence of ATP.It degrades the regulatory proteins RCSA and SULA. It hydrolyzes two ATPs for each peptide bond cleaved in the protein substrate. ","ATP-dependent proteinase","Cytoplasm","","
InterPro
IPR001984
Family
Peptidase S16, Lon protease
PR00830\"[357-376]T\"[596-612]T\"[674-693]T\"[704-723]T\"[727-745]TENDOLAPTASE
InterPro
IPR003111
Domain
Peptidase S16, lon N-terminal
PF02190\"[11-203]TLON
SM00464\"[11-203]TLON
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[349-493]TAAA
InterPro
IPR003959
Domain
AAA ATPase, core
PF00004\"[352-546]TAAA
InterPro
IPR004815
Family
Peptidase S16, ATP-dependent protease La
TIGR00763\"[13-772]Tlon: ATP-dependent protease La
InterPro
IPR008268
Active_site
Peptidase S16, active site
PS01046\"[677-685]TLON_SER
InterPro
IPR008269
Domain
Peptidase S16, lon C-terminal
PF05362\"[570-774]TLon_C
noIPR
unintegrated
unintegrated
G3DSA:1.10.8.60\"[492-585]Tno description
G3DSA:3.40.50.300\"[319-487]Tno description
PTHR10046\"[204-804]TATP DEPENDENT LON PROTEASE FAMILY MEMBER


","BeTs to 17 clades of COG0466COG name: ATP-dependent Lon protease, bacterial typeFunctional Class: OThe phylogenetic pattern of COG0466 is ------yqvd--b-efghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2e-288) to 10/10 blocks of the IPB003111 family, which is described as \"ATP-dependent protease La (LON) domain\". Interpro entry for IP:IPR003111. IPB003111A 209-243 4.1e-28 IPB003111B 275-304 1.2e-22 IPB003111C 313-358 2.7e-36 IPB003111D 387-425 9.9e-33 IPB003111E 426-474 2.2e-44 IPB003111F 524-557 4.3e-27 IPB003111G 597-615 1.5e-12 IPB003111H 621-647 2.1e-18 IPB003111I 665-684 7.2e-17 IPB003111J 685-731 2.1e-39Significant hit (1.6e-170) to 8/8 blocks of the IPB001984 family, which is described as \"ATP-dependent serine proteases, Lon family\". Interpro entry for IP:IPR001984. IPB001984A 24-33 0.00032 IPB001984B 161-194 5.5e-09 IPB001984C 350-386 1.5e-32 IPB001984D 434-474 6.8e-37 IPB001984E 532-555 1.2e-22 IPB001984F 597-615 1.1e-12 IPB001984G 621-647 1.5e-18 IPB001984H 665-691 2.5e-25Significant hit ( 1.8e-05) to 2/8 blocks of the PR00819 family, which is described as \"CbxX/CfqX superfamily signature\". Prints database entry for PR:PR00819. PR00819A 321-335 0.23 PR00819B 352-367 0.04","Residues 11 to 284 match (8e-07) PD:PD565330 which is described as PROTEASE ATP-DEPENDENT PROTEOME COMPLETE LONA ","","","","","","","","","","","Thu Jan 9 10:24:18 2003","Thu Jan 9 10:19:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02395 is paralogously related to AA02844 (1e-05), AA02270 (1e-05), AA02735 (2e-05) and AA01211 (0.001).","","","","","","Residues 570 to 774 (E-value = 5.6e-153) place AA02395 in the Lon_C family which is described as Lon protease (S16) C-terminal proteolytic domain (PF05362)","","","","","Thomas,C.D., Modha,J., Razzaq,T.M., Cullis,P.M. and Rivett,A.J. Controlled high-level expression of the lon gene of Escherichia coli allows overproduction of Lon protease Gene 136 (1-2), 237-242 (1993) PubMed: 8294008 Amerik,A.Iu, Chistiakov,L.G., Ostroumova,N.I., Gurevich,A.I. and Antonov,V.K. Cloning, expression and structure of the functionally active shortened lon gene in Escherichia coli Bioorg. Khim. 14 (3), 408-411 (1988) PubMed: 3289547 Chin,D.T., Goff,S.A., Webster,T., Smith,T. and Goldberg,A.L. Sequence of the lon gene in Escherichia coli. A heat-shock gene which encodes the ATP-dependent protease La J. Biol. Chem. 263 (24), 11718-11728 (1988) PubMed: 3042779 ","","Thu Jan 9 10:19:55 2003","1","","","" "AA02397","1649082","1647235","1848","ATGGATCAAAATCCACAGTCTCAATTGAAACTACTCATCGCACAAGGGAAAGAGCAAGGTTATTTAACCTACGCCGAGGTCAATGACAGCCTCCCCGAAGAATTAGCCGATGCAGATCAAATTGAAGATATTATTCAGATGATTAATGATATGGGGATTCAGGTGTTGGAGACCGCACCGGATGCCGATGATCTGATGCTCAATGAAAATATCACCGATGAAGATGTCGTTGAAGAAGCAACCCAAGTATTATCCAGCGTGGAAGCAGAATTAGGGCGGACTACCGACCCTGTACGTATGTATATGCGTGAAATGGGTAGCGTAGAATTGCTTACCCGTGAAGGCGAAATTGATATTGCCAAACGCATTGAAGAAGGTATTAACGAAGTACAAAGCGCCATTGCCGCTTACCCTGAAGCCATCACTTACTTAATTGAGCAATATGATTTGGTAGAAAATGGCGGTGTACGCTTAGCCGACTTAATTACCGGTTTCGTTGATCCTAATGTGCTAACCGAATCCGAGACTGAAGAATTGGCAGAAGATTTTAATTCCGAAGAAGGTGGCGATATTGATAGTGAAAGCGAGGAGGAAGAAGATAACGAAGGGGGAAGTAGCGATGACAGTGATAGTGATAACAGTGTTGATCCTGAAATTGCACGGGAAAAATTTACCGCACTTAAGCAGCAACATCAAAAGACCTTAGAGAGCATTGCCAAACATGGTCGTACGGCGAAAAAAGCAAAAGATGAAATTCAAGTGTTATCAGACATCTTCACTCAATTCCGCTTAGTACCAAAACAATTCGATATGCTAGTGCTATCTATACGTGGTATTATGAAACGTGTTCGCGGTCAGGAACGTTTCATTCAGCGGATTGTGGTGGACAATGCCAAAATGCCAAAATCCGGTTTCCAAAAAAGCTTTATAGGACATGAAACAACTGATACGTGGTTAGTGAAAGCCTTGTCTGCCGGTAAATCCTGGTCGGAAAAATTGGTACAATATGAAAACCAATTACGCCAAGCCATCACCAATTTGGTGCAAATCGAACAAGATACCCATCTGACGATTCCACAAATCCGAGAAATCGGTGAGCGCATCACACAAGGTGAATTAAAAGCCCGTCGTGCAAAAAAAGAAATGGTAGAAGCAAATCTGCGCTTAGTAATTTCTATTGCTAAAAAATACACCAATCGCGGATTACAATTTCTTGATCTTATTCAAGAGGGTAATATCGGCTTAATGAAAGCAGTGGATAAATTTGAATACCGGCGCGGCTATAAATTCTCTACTTATGCCACTTGGTGGATTCGTCAGGCAATTACCCGTTCTATTGCCGATCAAGCCCGCACCATTCGTATTCCGGTACATATGATTGAAACTATTAATAAACTCAATCGTATTTCCCGTCAAATGCTGCAGGAAATGGGACGCGAAGCCTCGCCGGAAGAACTGGCAGAACGCATGGGCATGCCGGAAGATAAAATCCGTAAAGTGCTGAAGATTGCGAAAGAGCCGATTTCGATGGAAACCCCAATTGGCGATGACGATGATTCCCATTTAGGCGATTTTATCGAGGATTCCACTTTAGAGCTTCCGTTAGATTCCGCGACCGTGCAAAGCCTGAAAGCAGCAACGCATGAAGTACTGGAAGGTTTAACCCCACGGGAGGCTAAAGTCTTGCGTATGCGCTTTGGTATCGACATGAATACCGATCATACTTTAGAAGAGGTGGGTAAACAATTTGACGTAACCCGTGAACGTATTCGCCAAATCGAAGCCAAAGCGTTACGTAAACTGCGCCATCCAAGCCGTTCCGAAACTTTACGCAGCTTTCTGGATGAG","","","70051","MDQNPQSQLKLLIAQGKEQGYLTYAEVNDSLPEELADADQIEDIIQMINDMGIQVLETAPDADDLMLNENITDEDVVEEATQVLSSVEAELGRTTDPVRMYMREMGSVELLTREGEIDIAKRIEEGINEVQSAIAAYPEAITYLIEQYDLVENGGVRLADLITGFVDPNVLTESETEELAEDFNSEEGGDIDSESEEEEDNEGGSSDDSDSDNSVDPEIAREKFTALKQQHQKTLESIAKHGRTAKKAKDEIQVLSDIFTQFRLVPKQFDMLVLSIRGIMKRVRGQERFIQRIVVDNAKMPKSGFQKSFIGHETTDTWLVKALSAGKSWSEKLVQYENQLRQAITNLVQIEQDTHLTIPQIREIGERITQGELKARRAKKEMVEANLRLVISIAKKYTNRGLQFLDLIQEGNIGLMKAVDKFEYRRGYKFSTYATWWIRQAITRSIADQARTIRIPVHMIETINKLNRISRQMLQEMGREASPEELAERMGMPEDKIRKVLKIAKEPISMETPIGDDDDSHLGDFIEDSTLELPLDSATVQSLKAATHEVLEGLTPREAKVLRMRFGIDMNTDHTLEEVGKQFDVTRERIRQIEAKALRKLRHPSRSETLRSFLDE","1647235","From Genbank:[gi:1710680] The sigma factor is an initiation factor that promotes attachment of the RNA polymerase to specific initiation sites and then is released. This is the primary sigma-factor of this bacteria.","RNA polymerase sigma factor sigma-70","Cytoplasm","","
InterPro
IPR000943
Domain
RNA polymerase, Sigma-70 factor
PR00046\"[406-419]T\"[430-438]T\"[554-566]T\"[575-590]T\"[590-601]TSIGMA70FCT
PS00715\"[406-419]TSIGMA70_1
PS00716\"[575-601]TSIGMA70_2
InterPro
IPR007127
Domain
RNA polymerase sigma factor 70, region 1.1
PF03979\"[1-81]TSigma70_r1_1
InterPro
IPR007624
Domain
RNA polymerase sigma-70 region 3
PF04539\"[456-538]TSigma70_r3
InterPro
IPR007627
Domain
RNA polymerase sigma-70 region 2
PF04542\"[382-452]TSigma70_r2
InterPro
IPR007630
Domain
RNA polymerase sigma-70 region 4
PF04545\"[550-603]TSigma70_r4
InterPro
IPR007631
Domain
RNA polymerase sigma factor 70, non-essential region
PF04546\"[137-351]TSigma70_ner
InterPro
IPR009042
Domain
RNA polymerase, Sigma-70 region 1.2
PF00140\"[95-131]TSigma70_r1_2
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[455-506]T\"[536-614]Tno description
InterPro
IPR012760
Domain
RNA polymerase sigma factor RpoD, C-terminal
TIGR02393\"[378-615]TRpoD_Cterm: RNA polymerase sigma factor Rpo
InterPro
IPR013256
Family
Chromatin SPT2
SM00784\"[167-249]Tno description
InterPro
IPR014284
Domain
RNA polymerase sigma-70
TIGR02937\"[377-605]Tsigma70-ECF: RNA polymerase sigma factor, s
noIPR
unintegrated
unintegrated
G3DSA:1.10.601.10\"[110-451]Tno description


","BeTs to 18 clades of COG0568COG name: DNA-directed RNA polymerase sigma subunits (sigma70/sigma32)Functional Class: KThe phylogenetic pattern of COG0568 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.1e-41) to 1/1 blocks of the IPB000943 family, which is described as \"Sigma-70 factor family\". Interpro entry for IP:IPR000943. IPB000943 395-446 2e-41","Residues 93 to 126 match (7e-07) PD:PD000305 which is described as SIGMA FACTOR RNA POLYMERASE TRANSCRIPTION DNA-BINDING DNA-DIRECTED REGULATION COMPLETE PROTEOME ","","","","","","","","","","","Thu Jan 9 10:43:59 2003","Thu Jan 9 10:39:04 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02397 is paralogously related to AA00560 (2e-21).","","","","","","Residues 550 to 603 (E-value = 4.2e-23) place AA02397 in the Sigma70_r4 family which is described as Sigma-70, region 4 (PF04545)","","","","","Burton,Z., Burgess,R.R., Lin,J., Moore,D., Holder,S. and Gross,C.A. The nucleotide sequence of the cloned rpoD gene for the RNA polymerase sigma subunit from E coli K12 Nucleic Acids Res. 9 (12), 2889-2903 (1981) PubMed: 6269063 Malhotra,A., Severinova,E. and Darst,S.A. Crystal structure of a sigma 70 subunit fragment from E.coli RNA polymerase Cell 87 (1), 127-136 (1996) PubMed: 8858155 Hengge-Aronis R. Recent insights into the general stress response regulatory network in Escherichia coli.J Mol Microbiol Biotechnol. 2002 May;4(3):341-6. PMID: 11931567 ","","Thu Jan 9 10:39:04 2003","1","","","" "AA02398","1650915","1649161","1755","ATGAAAGGCTCCATTCCACGCACCTTCATAGACGATATTTTAACCAAAATTAACATCGTCGATTTAATCAATTCCCGCGTAAAACTGAAAAAAGCCGGTCGCGATTATCAAGCCTGTTGCCCGTTTCATCACGAGAAAACACCGTCTTTTACGGTGAGCGACAAAAAGCAGTTTTATCATTGTTTCGGTTGCGGCGCGCACGGTAACGCCATTTCCTTTTTGATGGAATATGACAAGCTGGAATTTGTGGAAGCGGTGGAGGAACTGGCGGGCTTTCTCGGTTTGGAAATTCCCTACGAGAAACGACCGCACTTTAATGATGGCGGCAAGCAGGTTAATTTCCAAACCAAGCGAAATCTGTATGAATTAATGCAGGAAATCGCCAAATTCTACCAACAGCAGCTGCCGTTAAATATTCCCGCGCAAAGTTATCTGCAACAACGCGGACTGTCGGCGGAGGTGATTGAACGCTTTCAAATCGGCTATGTGCCGAACGCCATGGATTCCGTTTATCGCCAATTCGGTAAAAACCGCGAGGAGCAACAAAAACTGTTCGATTTGGGGATGCTGTCGCGTAACGATCGCGGCAATGTGTACGATAAATTCCGCAATCGAGTTATGTTTCCCATTCGCGATCGGCGCGGTCGCACCGTTGCTTTTGGCGGACGGGTTTTAACCGATGAAAAACCAAAATACCTGAACTCGCCGGAAACCGTGACCTATCACAAAGGGAGCGAACTTTACGGTTTATATGAAGCGCTTCAAGCGGACGATTCACCGCAAAAATTGCTGGTCGTCGAAGGCTATATGGATGTGGTGGCGTTGGCGCAGTTCGGCGTAAATTATGCGGTGGCGTCTCTCGGCACGTCCACAACTTCGGAGCAAATTCAGCTGCTTTTCCGTTCCACAGAACAGGTGGTGTGCTGTTATGACGGCGACCGAGCGGGACGCGATGCGGCTTGGCGTGCCTTAGAAAATGCGCTGCCGTATTTGGAAGACGGTCGTCAGCTGAAATTTATCTTTTTACCCGACGGCGAAGATCCTGATACGTTTATTCGCCAATATGGCAAACAAGGGTTTGAGGAATATCTCGACAACGCGCAGTCTTTAAGCGAATTTTTATTTGCCCATTTAACGCCGCAAGTGGATTTTTCCTCAAAAGAAGGCAAAGCCAAACTCGCTGCGTTAGCAATTCCGTTAATTAAACAAATTCCCGGCGATGTGTTGCGTTTGGATTTACGCAATACGCTCGCTAAAAAATTGGGGATTTTGGATCCCGCGCAATTGGAAAGCATGCTCCCGAATCAGGTAAAAGCGGAAGGGCCCGTCGCGCCAACCATGCAATTCAAACGCACTCCAATGCGTATTCTGATTGCATTATTGTTACAAAATCCGGAATTGGTGAAGTTTGTGCCGGATTTGGAACCTTTAAGAAATCTTAATGAACCGGGTTACGATTTGCTCGCGGAATTGACCGCACTTTGTCGTGAAAAAGTGGGGATTAGCTCGGGGCAATTATTGGAATATTGGCGCGATACAACACAGCAAAGTACGCTTGAAAAATTGCTCGCGTGGAACCATTTGATTGAAGACGATAAGATTGAAGACACGTTCCGCGAAACATTACGTTATTTCTACCTGCAACTCGTTGATAAACGAATAAACTGGCTCATCGCTAAAGATCGCGCGGAAGGCTTGGATCTGAACGAGAAAAAAGAACTTTCACATTTGTTAGTAAAAAAACAAGAAAAGAGA","","","67118","MKGSIPRTFIDDILTKINIVDLINSRVKLKKAGRDYQACCPFHHEKTPSFTVSDKKQFYHCFGCGAHGNAISFLMEYDKLEFVEAVEELAGFLGLEIPYEKRPHFNDGGKQVNFQTKRNLYELMQEIAKFYQQQLPLNIPAQSYLQQRGLSAEVIERFQIGYVPNAMDSVYRQFGKNREEQQKLFDLGMLSRNDRGNVYDKFRNRVMFPIRDRRGRTVAFGGRVLTDEKPKYLNSPETVTYHKGSELYGLYEALQADDSPQKLLVVEGYMDVVALAQFGVNYAVASLGTSTTSEQIQLLFRSTEQVVCCYDGDRAGRDAAWRALENALPYLEDGRQLKFIFLPDGEDPDTFIRQYGKQGFEEYLDNAQSLSEFLFAHLTPQVDFSSKEGKAKLAALAIPLIKQIPGDVLRLDLRNTLAKKLGILDPAQLESMLPNQVKAEGPVAPTMQFKRTPMRILIALLLQNPELVKFVPDLEPLRNLNEPGYDLLAELTALCREKVGISSGQLLEYWRDTTQQSTLEKLLAWNHLIEDDKIEDTFRETLRYFYLQLVDKRINWLIAKDRAEGLDLNEKKELSHLLVKKQEKR","1649161","From Genbank:[gi:18202820] DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments on both template strands at replication forks during chromosomal DNA synthesis","DNA primase","Cytoplasm","","
InterPro
IPR002694
Domain
Zinc finger, CHC2-type
PD002988\"[19-89]TPRIM_HAEIN_Q08346;
PF01807\"[5-102]Tzf-CHC2
SM00400\"[36-90]TZnF_CHCC
InterPro
IPR003778
Domain
Allophanate hydrolase subunit 2
SM00797\"[277-467]Tno description
InterPro
IPR006154
Domain
Toprim subdomain
SM00493\"[261-332]TTOPRIM
InterPro
IPR006171
Domain
TOPRIM
PF01751\"[261-343]TToprim
InterPro
IPR006295
Domain
DNA primase
TIGR01391\"[4-421]TdnaG: DNA primase
InterPro
IPR006647
Domain
Toprim, primase
PD002276\"[130-414]TPRIM_HAEIN_Q08346;
InterPro
IPR007693
Domain
DnaB-like helicase, N-terminal
G3DSA:1.10.860.10\"[437-584]Tno description
InterPro
IPR013173
Domain
DNA primase DnaG, DnaB-binding
PF08278\"[453-578]TDnaG_DnaB_bind
SM00766\"[453-578]Tno description
InterPro
IPR013264
Domain
DNA primase catalytic core, N-terminal
G3DSA:3.90.980.10\"[119-242]Tno description
PF08275\"[130-254]TToprim_N
noIPR
unintegrated
unintegrated
G3DSA:1.20.50.20\"[370-435]Tno description
G3DSA:3.40.1360.10\"[243-369]Tno description
G3DSA:3.90.580.10\"[1-103]Tno description


","No hits to the COGs database.","Significant hit (8.7e-134) to 7/7 blocks of the IPB002694 family, which is described as \"CHC2 zinc finger\". Interpro entry for IP:IPR002694. IPB002694A 40-85 6e-45 IPB002694B 144-164 4.3e-12 IPB002694C 199-223 5.5e-19 IPB002694D 230-249 6.1e-12 IPB002694E 264-301 1.7e-25 IPB002694F 303-316 3.1e-07 IPB002694G 342-352 2.3e-05","Residues 450 to 577 match (2e-45) PD:PD011358 which is described as DNA PRIMASE COMPLETE PROTEOME 2.7.7.- TRANSFERASE ZINC-FINGER REPLICATION METAL-BINDING POLYMERASE ","","","","","","","","","","","Thu Jan 9 11:07:38 2003","Thu Jan 9 11:04:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02398 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 261 to 343 (E-value = 2.2e-25) place AA02398 in the Toprim family which is described as Toprim domain (PF01751)","","","","","Erickson,B.D., Burton,Z.F., Watanabe,K.K. and Burgess,R.R. 1985 Nucleotide sequence of the rpsU-dnaG-rpoD operon from Salmonella typhimurium and a comparison of this sequence with the homologous operon of Escherichia coli. Gene 40(1):67-78 PubMed: 3005129. Burton,Z.F., Gross,C.A., Watanabe,K.K. and Burgess,R.R. 1983. The operon that encodes the sigma subunit of RNA polymerase also encodes ribosomal protein S21 and DNA primase in E. coli K12. Cell 32(2):335-349 PubMed: 6186393 Smiley,B.L., Lupski,J.R., Svec,P.S., McMacken,R. and Godson,G.N. 1982. Sequences of the Escherichia coli dnaG primase gene and regulation of its expression. Proc. Natl. Acad. Sci. U.S.A. 79(15):4550-4554. PubMed: 6750604 Versalovic,J. and Lupski,J.R. 1993. The Haemophilus influenzae dnaG sequence and conserved bacterial primase motifs. Gene 136(1-2):281-286. PubMed: 8294018","","Thu Jan 9 12:09:07 2003","1","","","" "AA02399","1651252","1651040","213","ATGCCTGTAATTAAAGTTCGTGAAAATGAATCCTTTGACGTAGCATTACGTCGTTTCAAACGCTCTTGCGAAAAAGCTGGTATTTTAGCAGAAGTTCGTGCGCGTGAATTCTACGAAAAACCAACAACTATTCGTAAACGTGAAAATGCAACTCGTGCAAAACGTCACGCAAAACGCTTAGCTCGTGAAAACGCACGCAACACACGTTTATAC","","","8486","MPVIKVRENESFDVALRRFKRSCEKAGILAEVRAREFYEKPTTIRKRENATRAKRHAKRLARENARNTRLY","1651040","From PF01165Ribosomes are ribonucleoprotein particles that are the site of protein synthesis. The structure of the ribosome is well conserved across the prokaryotic and eukaryotic lineages, reflecting the early origin of their essential function. They comprise two subunits, which can dissociate on heating. In prokaryotes, the small subunit contains a single large RNA moeity denoted, according to its sedimentation coefficient, 16S rRNA, and 21 different ribosomal proteins, designated S1-S21.","30S ribosomal protein S21","Cytoplasm","","
InterPro
IPR001911
Family
Ribosomal protein S21
PD005521\"[15-56]TRS21_PASMU_Q9CLJ0;
PR00976\"[5-13]T\"[13-22]T\"[25-35]T\"[37-47]TRIBOSOMALS21
PF01165\"[2-55]TRibosomal_S21
TIGR00030\"[2-59]TS21p: ribosomal protein S21
PS01181\"[13-25]TRIBOSOMAL_S21


","BeTs to 14 clades of COG0828COG name: Ribosomal protein S21Functional Class: JThe phylogenetic pattern of COG0828 is -------q---lbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.2e-34) to 1/1 blocks of the IPB001911 family, which is described as \"Ribosomal protein S21\". Interpro entry for IP:IPR001911. IPB001911 6-48 1.8e-34","Residues 6 to 55 match (1e-09) PD:PD005521 which is described as RIBOSOMAL 30S S21 COMPLETE PROTEOME A P1 B DNA CHROMOSOME ","","","","","","","","","","","Thu Jan 9 12:52:47 2003","Thu Jan 9 12:18:30 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02399 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 55 (E-value = 4e-31) place AA02399 in the Ribosomal_S21 family which is described as Ribosomal protein S21 (PF01165)","","","","","Burton,Z.F., Gross,C.A., Watanabe,K.K. and Burgess,R.R.The operon that encodes the sigma subunit of RNA polymerase alsoencodes ribosomal protein S21 and DNA primase in E. coli K12Cell 32 (2), 335-349 (1983)PubMed: 6186393 Lupski,J.R., Smiley,B.L. and Godson,G.N.Regulation of the rpsU-dnaG-rpoD macromolecular synthesis operonand the initiation of DNA replication in Escherichia coli K-12Mol. Gen. Genet. 189 (1), 48-57 (1983)PubMed: 6222240","","Thu Jan 9 12:18:30 2003","1","","","" "AA02400","1651287","1651451","165","TTGCAATTTAAATTTTTATTTGTTGCCGCGCCTGCGGCAGATTCAATAAAGGACGCAATTTTAATCCAAATCACGCATGAAAGTAAAGGGCAGATTGACGTTTTCCTGAAATCCGCATCGGAAAACTGGTTAAAATCGTGTAAAGCGGGTAAAATTCAGCGCCAA","","","6115","LQFKFLFVAAPAADSIKDAILIQITHESKGQIDVFLKSASENWLKSCKAGKIQRQ","1651451","","hypothetical protein","Periplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 14:34:22 2004","Wed Feb 25 14:34:22 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02400 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 11:04:09 2004","","","","","","","","","","","","","1","","","" "AA02402","1651477","1652502","1026","ATGCGAATTTTAGGCATTGAAACGTCCTGCGATGAAACGGGCGTTGCCATTTATGACGAAGAAAAAGGCTTAGTCGCCAATCAACTCCACACCCAAATTGCGCTGCACGCAGATTACGGCGGTGTAGTGCCGGAACTGGCGTCGCGCGATCATATCCGCAAACTGGCGCCACTATTACAAGCCGCATTAAAAGAAGCGAATTTAACTCCCGAAGACATCAACGGCGTGGCTTATACCAGCGGTCCGGGCTTGGTCGGCGCGTTGTTGGTGGGCGCCACCGTTGCGCGCGCCTTGGCTTATGCGTGGAATGTACCGGCAATCGGCATACATCATATGGAAGGGCATTTGTTGGCGCCCATGCTTGAGGAAAATCCACCGCACTTTCCTTTCGTGGCTTTGCTGGTATCCGGCGGGCATACCCAATTGGTGCGGGTGGACGGCGTAGGGCGTTATGAATTGCTGGGTGAATCCATTGATGACGCGGCGGGTGAAGCTTTTGATAAAACCGCCAAATTGCTCGGTTTGGATTACCCGGGCGGTGCGGCACTAGCGCGTTTAGCGCTTAACGGCACGCCGAATCTTTTTGCTTTTCCGCGCCCGATGACCGATCGTCCCGGTTTGGATTTCAGTTTTTCCGGTTTAAAAACTTTCGCCGCCAACACCCTTCATCAGGTATTACAAGAAGAGGGCAATCTGAGCGAACAAAGCAAGGCGGATATTGCCCATGCTTTCCAGGAAGCGGTGGTGGACACACTGGCAATAAAATGTAAGCGTGCGTTAAAACAAACCGGTTTGAAACGCTTGGTGATTGCGGGCGGCGTGAGCGCCAACACACAGTTGCGCCAAACCTTGGCGGAGCTTATGCAACAACTGGGCGGCGAGGTATTTTACCCGCAGCCGCAATTTTGCACGGACAACGGCGCCATGATCGCCTATACCGGTTTCTTACGTTTAAAACAGGGGCAACAACAGGGGTTGGCAATTGAAGTCCGTCCGCGTTGGGCGATGACCGAATTAACCACGATT","","","36682","MRILGIETSCDETGVAIYDEEKGLVANQLHTQIALHADYGGVVPELASRDHIRKLAPLLQAALKEANLTPEDINGVAYTSGPGLVGALLVGATVARALAYAWNVPAIGIHHMEGHLLAPMLEENPPHFPFVALLVSGGHTQLVRVDGVGRYELLGESIDDAAGEAFDKTAKLLGLDYPGGAALARLALNGTPNLFAFPRPMTDRPGLDFSFSGLKTFAANTLHQVLQEEGNLSEQSKADIAHAFQEAVVDTLAIKCKRALKQTGLKRLVIAGGVSANTQLRQTLAELMQQLGGEVFYPQPQFCTDNGAMIAYTGFLRLKQGQQQGLAIEVRPRWAMTELTTI","1652502","From Genbank:[gi:544376] This enzyme is a neutral metalloprotease that cleaves specificallyO-sialoglycoproteins such as glycophorin A.From PF00814O-Sialoglycoprotein endopeptidase is secreted by the bacterium Pasteurella haemolytica and digests only proteins that are heavily sialylated, in particular those with sialylated serine and threonine residues. Substrate proteins include glycophorin A and leukocyte surface antigens CD34, CD43, CD44 and CD45.Removal ofglycosylation, by treatment with neuraminidase, completely negates susceptibility to O-sialoglycoprotein endopeptidase digestion.","O-sialoglycoprotein endopeptidase","Cytoplasm, Extracellular","","
InterPro
IPR000905
Domain
Peptidase M22, glycoprotease
PD002367\"[236-289]TGCP_PASHA_P36175;
PR00789\"[4-17]T\"[76-96]T\"[97-116]T\"[131-143]T\"[154-175]T\"[268-277]TOSIALOPTASE
PF00814\"[23-312]TPeptidase_M22
TIGR00329\"[4-311]Tgcp: metalloendopeptidase, putative, glycop
PS01016\"[96-116]TGLYCOPROTEASE
InterPro
IPR009180
Family
Peptidase M22, O-sialoglycoprotein endopeptidase
PIRSF004537\"[1-342]TO-sialoglycoprotein endopeptidase
PTHR11735\"[97-342]TO-SIALOGLYCOPROTEIN ENDOPEPTIDASE


","No hits to the COGs database.","Significant hit ( 5e-99) to 8/8 blocks of the IPB000905 family, which is described as \"Glycoprotease, (M22) metallo-protease family\". Interpro entry for IP:IPR000905. IPB000905A 3-17 5.6e-12 IPB000905B 40-51 1.4e-05 IPB000905C 72-112 2.6e-27 IPB000905D 131-143 1e-08 IPB000905E 154-181 4e-19 IPB000905F 207-218 3e-06 IPB000905G 272-281 0.012 IPB000905H 302-311 3.5e-07","Residues 3 to 68 match (1e-07) PD:PD579372 which is described as ZINC 3.4.24.- METALLOPROTEASE HYDROLASE PROTEASE O-SIALOGLYCOPROTEIN METAL-BINDING C01G10.10 2610001M19RIK ENDOPEPTIDASE ","","","","","","","","","","","Fri Jan 10 07:58:40 2003","Thu Jan 9 13:00:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02402 is paralogously related to AA02600 (2e-05).","","","","","","Residues 2 to 283 (E-value = 2.4e-137) place AA02402 in the Peptidase_M22 family which is described as Glycoprotease family (PF00814)","","","","","Mellors A, Lo RY.O-sialoglycoprotease from Pasteurella haemolytica.Methods Enzymol 1995;248:728-40PMID: 7674959Sun,S., Schilling,B., Tarantino,L., Tullius,M.V., Gibson,B.W. and Munson,R.S. Jr., Cloning and characterization of the lipooligosaccharide galactosyltransferase II gene of Haemophilus ducreyi. J. Bacteriol. 182 (8), 2292-2298 (2000). PubMed: 10735874Abdullah,K.M., Lo,R.Y. and Mellors,A. Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene J. Bacteriol. 173 (18), 5597-5603 (1991) PubMed: 1885539 ","","Fri Jan 10 07:58:40 2003","1","","","" "AA02404","1652518","1652796","279","GTGGAAAAAACACATAAATTTTTCACCGCACTTTCAATAAAAAGGAAAACACATGGACAAAATCAAATTCAGAGCAATGCGTGCCGCCGGCATCGGCTGTTTCGTTATGTTAGCGATTATCGCCTTTTTCGTGTTTACCACGCCCACGGACGTGCTGATCGATTTCTTAACGGAAGTCGGCAAAATGGCAGGCGGGCGCACCACCATCGGCGTGCTTATTTTAGCCGCGCTGCCACCGGTGACCGGCTTCATTTGCTACCATTTCTGGCGCTGGGTGCT","","","11008","VEKTHKFFTALSIKRKTHGQNQIQSNACRRHRLFRYVSDYRLFRVYHAHGRADRFLNGSRQNGRRAHHHRRAYFSRAATGDRLHLLPFLALGA","1652796","","hypothetical protein","Cytoplasm, Extracellular","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Fri Jan 10 08:00:56 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02404 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02405","1652570","1652800","231","ATGGACAAAATCAAATTCAGAGCAATGCGTGCCGCCGGCATCGGCTGTTTCGTTATGTTAGCGATTATCGCCTTTTTCGTGTTTACCACGCCCACGGACGTGCTGATCGATTTCTTAACGGAAGTCGGCAAAATGGCAGGCGGGCGCACCACCATCGGCGTGCTTATTTTAGCCGCGCTGCCACCGGTGACCGGCTTCATTTGCTACCATTTCTGGCGCTGGGTGCTTAAA","0.00","0.00","8552","MDKIKFRAMRAAGIGCFVMLAIIAFFVFTTPTDVLIDFLTEVGKMAGGRTTIGVLILAALPPVTGFICYHFWRWVLK","","","conserved hypothetical protein","Inner membrane, Cytoplasm","Matches in gapped BLAST to an unknown from Pasteurella multocida.AA02405 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus ducreyi gene.AA02405 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus influenzae Rd gene.","
noIPR
unintegrated
unintegrated
signalp\"[1-29]?signal-peptide
tmhmm\"[10-30]?\"[52-72]?transmembrane_regions


","BeTs to 4 clades of COG1124COG name: ABC-type dipeptide/oligopeptide/nickel transport system, ATPase componentFunctional Class: E,PThe phylogenetic pattern of COG1124 is ao-pkz-qvd-lb-efgh--uj-itwNumber of proteins in this genome belonging to this COG is","","Residues 2 to 77 match (1e-15) PD:PD390229 which is described as PROTEOME COMPLETE PM1237 ","Fri Feb 27 15:59:37 2004","Sat Feb 28 17:15:58 2004","Sat Feb 28 17:15:58 2004","Sat Feb 28 17:15:58 2004","Fri Feb 27 15:59:37 2004","Fri Feb 27 15:59:37 2004","Fri Feb 27 15:59:37 2004","Sat Feb 28 17:15:58 2004","Fri Feb 27 15:59:37 2004","Fri Feb 27 15:59:37 2004","Fri Feb 27 15:59:37 2004","Fri Feb 27 15:59:37 2004","Fri Feb 27 15:59:37 2004","Fri Feb 27 15:59:37 2004","Fri Feb 27 15:59:37 2004","Fri Feb 27 15:59:37 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02405 has no significant similarity (blastp p-value < 1e-03) to any other gene in this genome.AA02405 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Fri Feb 27 15:59:37 2004","Fri Feb 27 15:59:37 2004","No hits to the PDB database.","","","No significant hits to the Pfam 7.7 database.","Fri Feb 27 15:59:37 2004","","","","","","","1","Fri Feb 27 15:59:37 2004","","" "AA02407","1652806","1653300","495","ATGGCTAAATTGTATTTTTACTATTCCACCATGAATGCAGGAAAATCCACCACCTTGTTGCAATCTTCCTATAATTACCGCGAACGTAACATGAACACGCTGGTTTATACAGCGGCGATAGACGATCGTTTCGGCGTAGGGCAGGTGACTTCCCGCATCGGGATTAGCGAACGGGCGAATACCTTTACCCGCAATACGAATTTGTTCGCTGAAATTGAACAACATCTGGCGCAGGAGCCGCTTCATTGTATTTTGGTGGATGAGGCACAGTTTTTAACCAAAGAACAGGTTTATCAACTGAGCGATGTGGTGGATAAACTACATATTCCCGTGTTGTGCTACGGTTTGCGCACCGATTTCCAAGCGGAATTATTTGAAGGCAGTCGCTATTTACTGGCGTGGGCGGATCAGCTGGAAGAACTCAAAACCATTTGTTACTGCGGTCGCAAAGCCAATTTTGTGTTACGTCTTAACGAACAGGGCGAAGTGGTTAAA","","","19026","MAKLYFYYSTMNAGKSTTLLQSSYNYRERNMNTLVYTAAIDDRFGVGQVTSRIGISERANTFTRNTNLFAEIEQHLAQEPLHCILVDEAQFLTKEQVYQLSDVVDKLHIPVLCYGLRTDFQAELFEGSRYLLAWADQLEELKTICYCGRKANFVLRLNEQGEVVK","1653300","From Genbank:[gi:20138784] This enzyme phosphorylates both thymidine and deoxyuridine.","thymidine kinase","Cytoplasm","","
InterPro
IPR001267
Family
Thymidine kinase
PTHR11441\"[1-164]TTHYMIDINE KINASE
PF00265\"[2-165]TTK


","No hits to the COGs database.","Significant hit ( 7.9e-37) to 3/4 blocks of the IPB001267 family, which is described as \"Thymidine kinase cellular-type\". Interpro entry for IP:IPR001267. IPB001267A 9-21 1.5e-05 IPB001267B 80-94 7.9e-06 IPB001267C 104-148 1.9e-22","Residues 11 to 165 match (6e-71) PD:PD100754 which is described as KINASE THYMIDINE COMPLETE PROTEOME TRANSFERASE DNA ATP-BINDING SYNTHESIS ALLOSTERIC ENZYME ","","","","","","","","","","","Fri Jan 10 08:15:04 2003","Fri Jan 10 08:07:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02407 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 165 (E-value = 1.1e-70) place AA02407 in the TK family which is described as Thymidine kinase (PF00265)","","","","","Franke CA, Bolman TM, Ottum SA, Jones KF, Hruby DE. Streptococcus gordonii strains resistant to fluorodeoxyuridine contain mutations in the thymidine kinase gene and are deficient in thymidine kinase activity. Antimicrob Agents Chemother. 2000 Mar;44(3):787-9. PMID: 10681361 McNab R. Cloning and sequence analysis of thymidine kinase from the oral bacterium Streptococcus gordonii. FEMS Microbiol Lett. 1996 Jan 1;135(1):103-10. PMID: 8598265 ","","Fri Jan 10 08:07:00 2003","1","","","" "AA02409","1655464","1653455","2010","ATGACAACCTCAATTCAACAACAAATCGACGACCTTAGAAAAACCTTACGCCACCACGAATATCAATACCACGTTTTAGACGATCCGCAGATTCCCGACAGCGAGTATGATCGCCTGTTTCATCAGCTTAAAGCGTTGGAACAACAACATCCCGAACTGGTTACCGCCGATTCGCCGACCCAACGCGTGGGTGCGCGTCCGTTGTCCGAATTTGCACAAATTCGCCATGAAATTCCCATGCTGTCCTTGGATAACGCCTTTTCCAATGAGGAATTTTTCTCCTTCGTCAAACGCATTCAAGATCGCCTGGCACTCGTGCCGGAACCACTGACCTTTTGCTGCGAACCGAAACTGGACGGTTTGGCGGTCAGCATTTTGTACGTGAACGGCGTATTGTCCCAAGCGGCAACCCGTGGTGACGGCACCACCGGTGAAGACATTACGCAAAATATCCGCACCATTCGCAACATTCCGTTGCAACTGCTGACGGATAATCCGCCGGCGCGTTTGGAAGTGCGCGGCGAGGTGTTCATGCCGCACGCGGGCTTTGAGCGATTAAATGAACGCGCATTGGAACACGGCGAGAAAACCTTTGCCAATCCGCGCAATGCGGCGGCGGGCTCACTACGTCAATTGGATCCGAAAATCACCAGCCAACGCCCGTTAATGCTCAATGCGTATAGTATCGGCATTGCCGAAGGTGTGGAACTGCCGCCGACCCATTTTGAACGCCTGCAATGGCTGAAATCCGTGGGTATTCCGGTAAACAATGAAATTCAGTTGTGCGACGGCATTGAAAACGTGTTGAATTTCTACCGCACTATTATGGCGAAACGCAGTTCCCTCGGTTATGACATCGACGGCGCGGTGCTGAAAATCAACGATATTGCGCTGCAACAACGCCTTGGTTTTATTTCCAAAGCACCACGTTGGGCGATTGCTTATAAATTCCCCGCAGAAGAAGTTAGAACAAGATTATTGGATGTTGAATTCCAAATTGGTAGAACAGGAGCTGTTACTCCCGTTGCTAAACTAGAACCTGTTTCTGTTGGAGGGGTTACCGTAAGTAACGCAACTTTACACAATAATGATGAAATAAAAAGATTAGGAATATCCATTGGTGATATTGTCTTAATAAGACGCGCTGGAGACGTTATTCCTCAAGTTATTAAACTCGTACATAAAGCCAAAAAAGGGAATAAACCAATTGTGTTTCCGACACACTGCCCCGTTTGTGATTCTTTGATTATCCGTATCGAAGGTGAAGCCGTCGCACGCTGCACCGGCGGATTATTCTGCGCGGCGCAACGCAAAGAAGCGTTAAAACACTTTGTGTCACGCAAAGCCATGGACATCGACAGTGTGGGCGGCAAGCTCATTGAACAGCTGGTGGATCGCGAATTGATTCATACCCCGGCAGATTTGTTCAAGTTGGATTTAACCACCCTCACCCGCCTTGAACGAATGGGACCGAAATCCGCCGAAAATGCCTTAGCCAGCTTAGAAAAAGCGAAAAATACCACCCTTGCCCGTTTCATTTTCGCCTTGGGCATTCGTGACGTGGGCGAAGCCACCGCGTTAAATCTGGCAAATCATTTCAAGACCTTGGAAGCGTTGCAAAATGCCGATTTGGAACAGTTACAACAGGTGCCCGACGTAGGCGAAGTGGTAGCAAATCGGATTTTTGTGTTCTGGCGTGAAGCGCATAATGTCGCCGTGGTGGAAGATCTCATCGCCCAAGGCGTGCATTGGGAAACCGTTGACGTGCAGGAAGTGAAGGAAAATCCGTTCAAAGGCAAAACTGTGGTGCTCACCGGCACCCTCTCGCAAATGGGACGCAACGACGCCAAAGCCTTGTTACAACAACTCGGCGCCAAAGTCAGCGGCAGTGTTTCCGCCAAAACCGACTATGTTATCGCCGGTGAAGCCGCCGGCTCAAAACTAAGCAAAGCGGCGGAGTTAGGGGTGCAGGTGTTGAGTGAGGAAGAATTTTTGGGCTGGATCAACGGA","","","74109","MTTSIQQQIDDLRKTLRHHEYQYHVLDDPQIPDSEYDRLFHQLKALEQQHPELVTADSPTQRVGARPLSEFAQIRHEIPMLSLDNAFSNEEFFSFVKRIQDRLALVPEPLTFCCEPKLDGLAVSILYVNGVLSQAATRGDGTTGEDITQNIRTIRNIPLQLLTDNPPARLEVRGEVFMPHAGFERLNERALEHGEKTFANPRNAAAGSLRQLDPKITSQRPLMLNAYSIGIAEGVELPPTHFERLQWLKSVGIPVNNEIQLCDGIENVLNFYRTIMAKRSSLGYDIDGAVLKINDIALQQRLGFISKAPRWAIAYKFPAEEVRTRLLDVEFQIGRTGAVTPVAKLEPVSVGGVTVSNATLHNNDEIKRLGISIGDIVLIRRAGDVIPQVIKLVHKAKKGNKPIVFPTHCPVCDSLIIRIEGEAVARCTGGLFCAAQRKEALKHFVSRKAMDIDSVGGKLIEQLVDRELIHTPADLFKLDLTTLTRLERMGPKSAENALASLEKAKNTTLARFIFALGIRDVGEATALNLANHFKTLEALQNADLEQLQQVPDVGEVVANRIFVFWREAHNVAVVEDLIAQGVHWETVDVQEVKENPFKGKTVVLTGTLSQMGRNDAKALLQQLGAKVSGSVSAKTDYVIAGEAAGSKLSKAAELGVQVLSEEEFLGWING","1653455","From Genbank:[gi:1169385] This protein catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. From PF01653: NAD-dependent DNA ligase adenylation domainDNA ligase catalyse the crucial step of joining the breaks in duplex DNA during DNA replication, repair and recombination, utilizing either ATP or NAD(+) as a cofactor. There are two forms of DNA ligase: one requires ATP and the other NAD. Bacterial DNA ligases are NAD-dependent.They are proteins of about 75 to 85 Kd whose sequence is well conserved.","DNA ligase","Cytoplasm","","
InterPro
IPR000445
Domain
Helix-hairpin-helix motif
PF00633\"[535-564]THHH
InterPro
IPR001357
Domain
BRCT
PF00533\"[592-668]TBRCT
SM00292\"[594-670]TBRCT
PS50172\"[592-670]TBRCT
InterPro
IPR001679
Family
NAD-dependent DNA ligase
TIGR00575\"[12-664]Tdnlj: DNA ligase, NAD-dependent
PS01055\"[117-146]TDNA_LIGASE_N1
PS01056\"[333-348]TDNA_LIGASE_N2
InterPro
IPR003583
Domain
Helix-hairpin-helix DNA-binding, class 1
SM00278\"[447-466]T\"[481-500]T\"[513-532]T\"[545-564]THhH1
InterPro
IPR004149
Domain
Zinc-finger, NAD-dependent DNA ligase C4-type
PF03119\"[407-435]TDNA_ligase_ZBD
InterPro
IPR004150
Domain
NAD-dependent DNA ligase, OB-fold
PD003944\"[319-393]TQ8DFK5_VIBVU_Q8DFK5;
PF03120\"[322-403]TDNA_ligase_OB
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[321-393]Tno description
InterPro
IPR013839
Domain
NAD-dependent DNA ligase, adenylation
PF01653\"[3-320]TDNA_ligase_aden
InterPro
IPR013840
Domain
NAD-dependent DNA ligase, N-terminal
SM00532\"[4-449]TLIGANc
noIPR
unintegrated
unintegrated
G3DSA:1.10.150.20\"[436-504]T\"[505-587]Tno description
G3DSA:1.10.287.610\"[5-62]Tno description
G3DSA:3.30.470.30\"[121-254]Tno description
G3DSA:3.40.50.10190\"[590-668]Tno description
PIRSF001604\"[2-670]TDNA ligase (NAD), LigA type
PTHR11107\"[1-669]TBRCT DOMAIN-CONTAINING PROTEIN
PTHR11107:SF5\"[1-669]TDNA LIGASE, NAD-DEPENDENT


","No hits to the COGs database.","Significant hit (2.2e-258) to 11/11 blocks of the IPB001679 family, which is described as \"NAD-dependent DNA ligase\". Interpro entry for IP:IPR001679. IPB001679A 19-44 1.1e-15 IPB001679B 58-94 3.3e-22 IPB001679C 112-158 5.6e-39 IPB001679D 198-222 6.2e-20 IPB001679E 279-329 5.5e-36 IPB001679F 348-390 2.1e-28 IPB001679G 405-414 2.4e-05 IPB001679H 433-475 2.5e-26 IPB001679I 496-537 1.1e-24 IPB001679J 599-609 5.5e-05 IPB001679K 624-656 5.3e-24","Residues 400 to 444 match (4e-10) PD:PD483811 which is described as LIGASE PROTEOME COMPLETE DNA ","","","","","","","","","","","Tue Dec 2 12:12:10 2003","Fri Jan 10 08:17:56 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02409 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 592 to 668 (E-value = 4.9e-19) place AA02409 in the BRCT family which is described as BRCA1 C Terminus (BRCT) domain (PF00533)","","","","","Ishino,Y., Shinagawa,H., Makino,K., Tsunasawa,S., Sakiyama,F. and Nakata,A. Nucleotide sequence of the lig gene and primary structure of DNA ligase of Escherichia coli Mol. Gen. Genet. 204 (1), 1-7 (1986) PubMed: 3018436 Georlette,D., Jonsson,Z.O., Van Petegem,F., Chessa,J.-P., Van Beeumen,J., Huebscher,U. and Gerday,C. A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures Eur. J. Biochem. 267, 3502-3512 (2000)","","Fri Jan 10 08:19:13 2003","1","","","" "AA02410","1656603","1655569","1035","ATGGATTTAAATACAATTTTGATTATCTTGGGCGTTATTGCATTATTGGCATTGGTTGCGCACGGAATTTGGTCAAACCGTCGCGAAAAATCCCAATATTTCAAAAACGCCAATACCTTTGCACAAAATCAGCAGCCAAACCGTTTTAATGCGCCGAACCCAACGGCGCGCCCCGTCACCGACGCACCTATCGCCGAAAAACCAAAACACGCCTTTGTCGAAGAAACCCCGCCACCGCAACAACAAGCACTGGATTTTGAAGAAGCGGCGGCACCAAGCGCGGCCGAAAACCAATCTATCGAACGCGCCGTAGATGAAATTAAAATCACGCTGCCGAGTGGGGTGTCAAACGCATTTCATCAGGCTGAACCTGCACCGCAATACGCGCAGAATGAGCAAGGGCTACAGCGACCACAATATCCGCAAGCGCCCCAAAGCAGACCCAACGACACGCCGTTTCAACCTTACGGCGAGCCTTCGCCTTACGCCGATCCGAACCGCGTTTCCATCACGCAAATGGAAGAAGAATACACCACACCGACGGTTTCTTTGACGCCGTTGGAACAGGAAAGCCACGAACCAACCACCGAAATGCAGGCAACGCCGCAACCGACGGAAAGCAAGGGGGAAAATCCGGCGAAACCGTCTTTCATTATGTTGTATGTGGTAGCACCGGAAAACCGTGAATTCAACGGTGGGCGCTTAGCACAAGCCTTGGACGATTTAGGTTTTATTTTCGGCGATCAGCACATTTATCACCGCCATTTGGATTTAACCTCCGCCAGTCCGGTGTTATTCAGCATCGCCAATTTACAACAGCCCGGCACCTTTGATCCTTACGACATGGACAATCTGTTCACCGTGGGCATTGCGCTGTTTATGCAATTACCTTCCCCGGGCAACGACACCGTCAACTTAAAAACTATGATTCGCGCTGCACGCAATTTGGCGGACGAATTAGGCGGTTTTGTGTTGACCGACAAACAGGAAATTTTCAACGACCATGCCGAACAGGAATATTTAGCCAAAGTGGCT","","","47309","MDLNTILIILGVIALLALVAHGIWSNRREKSQYFKNANTFAQNQQPNRFNAPNPTARPVTDAPIAEKPKHAFVEETPPPQQQALDFEEAAAPSAAENQSIERAVDEIKITLPSGVSNAFHQAEPAPQYAQNEQGLQRPQYPQAPQSRPNDTPFQPYGEPSPYADPNRVSITQMEEEYTTPTVSLTPLEQESHEPTTEMQATPQPTESKGENPAKPSFIMLYVVAPENREFNGGRLAQALDDLGFIFGDQHIYHRHLDLTSASPVLFSIANLQQPGTFDPYDMDNLFTVGIALFMQLPSPGNDTVNLKTMIRAARNLADELGGFVLTDKQEIFNDHAEQEYLAKVA","1655569","From Genbank:[gi:1175529] This protein interacts directly with the cell division protein ftsZ.It is a probable receptor for the septal ring structure, it may anchor it to the inner-membrane.From PF04354:ZipA, C-terminal FtsZ-binding domain.This family represents the ZipA C-terminal domain.ZipA is involved in septum formation in bacterial cell division. Its C-terminal domain binds FtsZ, a major component of the bacterial septal ring.","cell division protein","Periplasm, Inner membrane","","
InterPro
IPR007449
Domain
ZipA, C-terminal FtsZ-binding region
PF04354\"[214-344]TZipA_C
SM00771\"[214-344]Tno description
InterPro
IPR011919
Family
Cell division protein ZipA
TIGR02205\"[2-344]Tseptum_zipA: cell division protein ZipA
noIPR
unintegrated
unintegrated
G3DSA:3.30.1400.10\"[212-344]Tno description
signalp\"[1-22]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","","Residues 218 to 344 match (2e-45) PD:PD035754 which is described as CELL DIVISION INNER PROTEOME TRANSMEMBRANE COMPLETE MEMBRANE ZIPA SEPTATION HOMOLOG ","","","","","","","","","","","Mon Jan 13 18:11:25 2003","Mon Jan 13 18:02:13 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02410 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 214 to 344 (E-value = 3.6e-71) place AA02410 in the ZipA_C family which is described as ZipA, C-terminal FtsZ-binding domain (PF04354)","","","","","Moy FJ, Glasfeld E, Mosyak L, Powers R.Solution structure of ZipA, a crucial component of Escherichia coli cell division.Biochemistry 2000 Aug 8;39(31):9146-56PMID: 10924108Ohashi T, Hale CA, de Boer PA, Erickson HP.Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain.J Bacteriol. 2002 Aug;184(15):4313-5.PMID: 12107152Hale CA, de Boer PA.ZipA is required for recruitment of FtsK, FtsQ, FtsL, and FtsN to the septal ring in Escherichia coli.J Bacteriol. 2002 May;184(9):2552-6.PMID: 11948172Pichoff S, Lutkenhaus J.Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli.EMBO J. 2002 Feb 15;21(4):685-93.PMID: 11847116","","Mon Jan 13 18:10:38 2003","1","","","" "AA02411","1656743","1657564","822","ATGTTGAAACACGCGGAAATGAAATCCGGTTTTGAATATTTTGTGATGGGTTGGCATTTGATTTTACAGAAAGGGCTGCGCCGTTTTGTGATCATGCCGATCCTGTTAAATATGCTGTTATTAGGCGGTCTGTTTTGGCTTTTTGTGAACCAAATCGGCGGTTATATTGACGGCATTATTTCCTACATTCCCGATTGGCTGAGTTGGTTGAGCGGCGTTTTGCTGCTGCTTTCCATTCTTATGATTCTCGTTCTGTTTTACTTCGTCTTTACCACGCTGTCGGGCTTTATCGCCGCGCCTTTTAATGGCTTGCTGGCGGAAAAAGTGGAAAAAATGCTGACCGGAGAAAATTTGCAGGATATGTCCCTGTGGGATTTTATGAAAGATGTGCCGCGGATGCTGGTACGGGAATGGCAAAAGCTGGTTTACAGCTTGCCAAAAATCATCGCGTTGTTTTTATTGGGATTTGTGCCTTTGCTGGGGCAAACCATGATTCCCGTAGCGACCTTTTTATTCACCGCATGGATGATGGCGATTCAATATTGCGACTATCCTTTTGATAACCACAAAATCCCTTTCGGCATAATGAAAAACGAACTGGCGATTAAGCGCAATGTGACGATGACCTTCGGCAGTTTGGTGACGCTTTGTACTTTTGTGCCGGTGGTGAATCTGGTGATTATTCCCGTGGCAGTGTGTGGCGCAACGGCAATGTGGGTAACGGAATACCGTGCTTTATTTAAGCGCTCGCAACAAGGGCAAACCGGCACTGAAGTGAATGTGAATCGTCGCTCTTCCGGCGACGGTGTTATCGTCAGAAAA","","","40906","MLKHAEMKSGFEYFVMGWHLILQKGLRRFVIMPILLNMLLLGGLFWLFVNQIGGYIDGIISYIPDWLSWLSGVLLLLSILMILVLFYFVFTTLSGFIAAPFNGLLAEKVEKMLTGENLQDMSLWDFMKDVPRMLVREWQKLVYSLPKIIALFLLGFVPLLGQTMIPVATFLFTAWMMAIQYCDYPFDNHKIPFGIMKNELAIKRNVTMTFGSLVTLCTFVPVVNLVIIPVAVCGATAMWVTEYRALFKRSQQGQTGTEVNVNRRSSGDGVIVRK","1657564","","cysteine synthetase","Inner membrane, Cytoplasm","","
InterPro
IPR007496
Family
Protein of unknown function DUF540
PF04401\"[47-248]TDUF540
noIPR
unintegrated
unintegrated
signalp\"[1-94]?signal-peptide
tmhmm\"[29-49]?\"[68-90]?\"[148-182]?\"[206-240]?transmembrane_regions


","No hits to the COGs database.","","Residues 10 to 244 match (3e-73) PD:PD018629 which is described as PROTEOME COMPLETE MEMBRANE CYSZ CYSTEINE INNER TRANSMEMBRANE BIOSYNTHESIS HOMOLOG INTEGRAL ","","","","","","","","","","","","Fri Jan 10 08:59:02 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02411 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 47 to 248 (E-value = 6.6e-98) place AA02411 in the DUF540 family which is described as Protein of unknown function (DUF540) (PF04401)","","","","","Byrne,C.R., Monroe,R.S., Ward,K.A. and Kredich,N.M.DNA sequences of the cysK regions of Salmonella typhimurium andEscherichia coli and linkage of the cysK regions to ptsHJ. Bacteriol. 170 (7), 3150-3157 (1988)PubMed: 3290198Levy,S. and Danchin,A.Phylogeny of metabolic pathways: O-acetylserine sulphydrylase A ishomologous to the tryptophan synthase beta subunitMolecular microbiology. 2 (6), 777-783 (1988)PubMed: 3062311","","Fri Jan 10 09:00:04 2003","1","","","" "AA02412","1657668","1658612","945","ATGACTATTTACAGTGACAATTCTTATTCTATCGGCAATACCCCGTTAGTACGTTTAAAACATTTCGGCAACGGCAATATTGTCGTGAAAATTGAAGGGCGCAACCCGAGTTTCAGCGTAAAATGTCGCATCGGTTCTAACATGATATGGCAGGCGGAAAAAGACGGCAGGCTGACGAAAGGCAAAGAAATCGTTGATGCTACCAGCGGTAATACCGGGATTGCATTGGCGTATGTCGCGGCAGCGCGTGGTTATAAAATCACCCTTACCATGCCGGAGACCATGAGTACCGAGCGTAAACGTTTGTTGCGTGGTCTCGGTGTAAATTTAGTGCTGACTGAAGGTGCCAAAGGAATGAAAGGTTCCATTGCTAAAGCAGAAGAAATCATGGCGTCCGATCCGAATCGTTATGTGATGTTAAAACAATTTGAAAACCCGGCGAACCCGGATATCCACCGCAAAACCACCGGTGAAGAAATCTGGAAAGGCACCGAGGGCAAAATTGACATATTGGTTGCCGGTGTAGGCACAGGCGGTACGATTACCGGCATTTCCCGCGCAATCAAATTAGATCACGGTAAACAAATCACTTCCGTTGCCGTAGAACCGGCAGAATCTCCGGTTATCACTCAAACGCTCGCGGGCGAAGAAGTGAAACCGGGACCACACAAAATTCAAGGTATCGGCGCAGGCTTTATTCCGAAAAACTTAGATCTTTCCTTAGTGGATCGTGTGGAAACTGTAGATAGCGACACCGCCATTGCCACCGCCCGCCGTTTGATGGCGGAAGAAGGGATTCTTGCCGGGATTTCTTCCGGCGCTGCTGTAGCGGCTGCTGACCGCTTGGCGAACCTGCCCGAATTTAAAGACAAACTGATCGTCGTTATCCTACCGTCTGCTGCCGAACGCTATTTAAGTACCGCACTTTTTAATGGAATTGAGGTT","","","35347","MTIYSDNSYSIGNTPLVRLKHFGNGNIVVKIEGRNPSFSVKCRIGSNMIWQAEKDGRLTKGKEIVDATSGNTGIALAYVAAARGYKITLTMPETMSTERKRLLRGLGVNLVLTEGAKGMKGSIAKAEEIMASDPNRYVMLKQFENPANPDIHRKTTGEEIWKGTEGKIDILVAGVGTGGTITGISRAIKLDHGKQITSVAVEPAESPVITQTLAGEEVKPGPHKIQGIGAGFIPKNLDLSLVDRVETVDSDTAIATARRLMAEEGILAGISSGAAVAAADRLANLPEFKDKLIVVILPSAAERYLSTALFNGIEV","1658612","From PF00291: Pyridoxal-phosphate dependent enzymeCysteine synthetase belongs to the pyridoxal-phosphate dependent enzyme family.Pyridoxal-5'-phosphate-dependent enzymes (B6 enzymes) catalyze manifold reactions in the metabolism of amino acids. Most of these enzymes can be assigned to one of three different families of homologous proteins, the alpha, beta and gamma families. The alpha and gamma family might be distantly related with one another, but are clearly not homologous with the beta family. The beta family includes L- and D-serine dehydratase, threonine dehydratase, the beta subunit of tryptophan synthase, threonine synthase and cysteine synthase. These enzymes catalyze beta-replacement or beta-elimination reactions. ","cysteine synthetase","Cytoplasm","","
InterPro
IPR001216
Binding_site
Cysteine synthase/cystathionine beta-synthase P-phosphate-binding site
PS00901\"[30-48]TCYS_SYNTHASE
InterPro
IPR001926
Domain
Pyridoxal-5'-phosphate-dependent enzyme, beta subunit
PF00291\"[7-300]TPALP
InterPro
IPR005856
Family
Cysteine synthase K/M
TIGR01136\"[7-310]TcysKM: cysteine synthases
InterPro
IPR005859
Family
Cysteine synthase A
TIGR01139\"[7-310]TcysK: cysteine synthase A
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1100\"[115-308]Tno description
PTHR10314\"[26-313]TSER/THR DEHYDRATASE, TRP SYNTHASE
PTHR10314:SF8\"[26-313]TCYSTEINE SYNTHASE


","No hits to the COGs database.","Significant hit (7.8e-142) to 6/6 blocks of the IPB001216 family, which is described as \"Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site\". Interpro entry for IP:IPR001216. IPB001216A 11-20 1.1e-05 IPB001216B 27-71 3.4e-26 IPB001216C 76-125 1.4e-28 IPB001216D 138-178 2.1e-28 IPB001216E 220-274 1.4e-36 IPB001216F 278-307 2e-10Significant hit ( 1e-17) to 2/2 blocks of the IPB001926 family, which is described as \"Pyridoxal-5'-phosphate-dependent enzymes, beta family\". Interpro entry for IP:IPR001926. IPB001926A 64-91 1.2e-13 IPB001926B 145-153 0.019Significant hit ( 9e-05) to 2/7 blocks of the IPB000993 family, which is described as \"Tryptophan synthase, beta chain\". Interpro entry for IP:IPR000993. IPB000993B 53-91 0.54 IPB000993F 248-277 0.082","Residues 186 to 229 match (4e-08) PD:PD482216 which is described as A CYSTEINE SULFHYDRYLASE O-ACETYLSERINE PHOSPHATE CSASE PROTEOME PLASMID COMPLETE THIOL-LYASE ","","","","","","","","","","","Fri Jan 10 09:11:25 2003","Fri Jan 10 09:06:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02412 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 300 (E-value = 3.1e-123) place AA02412 in the PALP family which is described as Pyridoxal-phosphate dependent enzyme (PF00291)","","","","","Alexander FW, Sandmeier E, Mehta PK, Christen P.Evolutionary relationships among pyridoxal-5'-phosphate-dependent enzymes.Regio-specific alpha, beta and gamma families.Eur J Biochem 1994 Feb 1;219(3):953-60PMID: 8112347Byrne,C.R., Monroe,R.S., Ward,K.A. and Kredich,N.M. DNA sequences of the cysK regions of Salmonella typhimurium and Escherichia coli and linkage of the cysK regions to ptsH. J. Bacteriol. 170(7): 3150-3157,1988. PubMed: 3290198. Fernandez M,Kleerebezem M, Kuipers OP,Siezen RJ, van Kranenburg R. Regulation of the metC-cysK operon, involved in sulfur metabolism in Lactococcus lactis. J Bacteriol. 2002 Jan;184(1):82-90. PMID: 11741847 ","","Fri Jan 10 09:11:25 2003","1","","","" "AA02414","1658981","1658838","144","ATGGGTGTTCACCGGTGCGAGACCGCCCTGTGTTATCTGCACACGCCAAAAAAACGCGATGTGGGTTTGGTAACTGTGCCGGGCAGCACCATTGCATTAAATTTATATGCCGCCATTACCATGTTATTCCTCGGTATGCGATCG","","","5233","MGVHRCETALCYLHTPKKRDVGLVTVPGSTIALNLYAAITMLFLGMRS","1658838","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
tmhmm\"[21-39]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 14:36:07 2004","Wed Feb 25 14:36:07 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02414 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 11:00:22 2004","","","","","","","","","","","","","1","","","" "AA02415","1658786","1658583","204","GTGAATGTGAATCAGGGAACATTTCCTCTCCCCAAAGAGGCCGGCTTATTCGTAATCCAGGGTAATTTTTACCCTAGATTACATGGCATTGGTTTGCTATTTTACACTAGTAAAAGTGCGGTCATTTTCATGAACGTTTTTCAACAGGCAAAGTCGTTAATTAACAATGTATTAAACCTCAATTCCATTAAAAAGTGCGGTACT","10.70","5.17","7497","VNVNQGTFPLPKEAGLFVIQGNFYPRLHGIGLLFYTSKSAVIFMNVFQQAKSLINNVLNLNSIKKCGT","","","hypothetical protein","Periplasm, Extracellular","No significant hits in gapped BLAST found.AA02415 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus ducreyi gene.AA02415 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus influenzae Rd gene.","No hits reported.","No hits to the COGs database.","","","Sat Feb 28 10:15:48 2004","Sat Feb 28 17:20:43 2004","Sat Feb 28 17:20:43 2004","Sat Feb 28 17:20:43 2004","Sat Feb 28 10:15:48 2004","Sat Feb 28 10:15:48 2004","Sat Feb 28 10:15:48 2004","Sat Feb 28 10:15:48 2004","Sat Feb 28 10:15:48 2004","Sat Feb 28 10:15:48 2004","Sat Feb 28 10:15:48 2004","Sat Feb 28 10:15:48 2004","Sat Feb 28 10:15:48 2004","Sat Feb 28 10:15:48 2004","Sat Feb 28 10:15:48 2004","Sat Feb 28 10:15:48 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02415 has no significant similarity (blastp p-value < 1e-03) to any other gene in this genome.AA02415 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sat Feb 28 10:15:48 2004","Sat Feb 28 10:15:48 2004","No hits to the PDB database.","","","No significant hits to the Pfam 7.7 database.","Sat Feb 28 10:15:48 2004","","","","","","","1","Sat Feb 28 10:15:48 2004","","" "AA02416","1659638","1659060","579","ATGGCTACCTTCACCCAAATTAAACATGCCATCATGTCTGATCTGCAAAATCAATCCTTTACCGAGCGCGGTATTGAACCGCTGTTTGCGGCACCGACAGGGGCGCGCATTAATGTTGTCGGACAAGCGCCCGGAGTGAAAGCGGAGCAAACCCGTTTGTACTGGAACGATAAAAGCGGCGATCGATTGCGTGAATGGTTGGACGTAGATCGTGAGACCTTTTATCATTCCGGGCTATTTGCCGTGCTCCCCATGGATTTTTATTATCCGGGTAAAGGTAAATCGGGGGATTTGCCGCCGCGGAAAGGTTTTGCGGAAAAATGGCATCCATCGATTTTAACAGGTTTGCCCAATATCGAACTGACCATTGTGATCGGACAATATGCGCAACAATATTACCTGCCGCAGAATAAACGCAACGTCACCGAAACGGTGAAAAATTACCGTGAATTTCTACCGCACTTTTTGCCGTTGGTACACCCTTCACCGCGTAATCAGCTTTGGCTGGCTAAAAATCCGTGGTTTATGCAGGATGTGGTGCCAACCCTGCAACAACTGGTCAAACAAATTCTCTTCCGT","","","22313","MATFTQIKHAIMSDLQNQSFTERGIEPLFAAPTGARINVVGQAPGVKAEQTRLYWNDKSGDRLREWLDVDRETFYHSGLFAVLPMDFYYPGKGKSGDLPPRKGFAEKWHPSILTGLPNIELTIVIGQYAQQYYLPQNKRNVTETVKNYREFLPHFLPLVHPSPRNQLWLAKNPWFMQDVVPTLQQLVKQILFR","1659060","","conserved hypothetical protein","Periplasm","","
InterPro
IPR005122
Family
Uracil-DNA glycosylase superfamily
PF03167\"[28-188]TUDG
noIPR
unintegrated
unintegrated
G3DSA:3.40.470.10\"[2-162]Tno description


","No hits to the COGs database.","","Residues 24 to 191 match (2e-73) PD:PD179728 which is described as PROTEOME COMPLETE SPY0472 GLYCOSYLASE RSC1329 YSID R01880 SP0624 MLL0558 URACIL-DNA ","","","","","","","","","","","","Fri Jan 10 09:14:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02416 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 30 to 188 (E-value = 4.8e-09) place AA02416 in the UDG family which is described as Uracil DNA glycosylase superfamily (PF03167)","","","","","","","","1","","","" "AA02417","1661038","1659950","1089","ATGGGATTCAAATGTGGCATCGTGGGCTTGCCGAATGTGGGCAAATCGACGCTTTTCAACGCTTTAACCAAAGCCGGAATTGAAGCGGCGAACTATCCGTTTTGTACTATCGAACCGAATACCGGCGTCGTGCCGATGCCTGATCCGCGTTTGGACGCGTTGGCAGAAATTGTCAAGCCGGAACGCGTGTTGCCGACCACCATGGAATTTGTGGACATCGCGGGCTTGGTTGCCGGCGCAAGCAAAGGAGAAGGCTTGGGGAACAAATTCTTGGCGAACATTCGCGAAACCGACGCGATCGGTCACGTAGTGCGTTGCTTTGAAAACGACGACATCGTGCACGTTGCGGGCAAAATCGATCCGTTAAATGACATCGACACCATCAACACCGAACTGGCGCTCGCCGATTTAGACAGCTGCGAACGCGCTATTCAACGTTTGCAAAAACGTGCCAAAGGCGGCGACAAAGACGCGAAATTTGAACTTTCCGTGATGGAAAAAATCCTGCCGGTGCTTTCCGAAGCGGGCATGATTCGTTCCGTGCCGTTAGACAAAGACGAATTATTGGCGATTAAAAGCTACAATTTCTTAACCTTAAAACCGACCATGTACATCGCCAACGTGAACGAAGACGGTTTTGAAAACAATCCGTATCTCGACAAAGTACGGGAATTCGCCGAAAAAGAAGGTTCCGTGGTGGTACCGGTATGTGCCGCAATCGAGGCGGAAATCGCCGAACTGGACGATGACGAGAAACTGGAATTCTTACAGGACCTCGGCATTGAAGAACCGGGCTTAAACCGCGTGATTCGCGCAGGTTACGCCTTATTGAATTTACAAACCTACTTCACCGCCGGCGTGAAAGAAGTACGCGCGTGGACGGTTTCCGTCGGCGCCACCGCACCGAAAGCCGCCGCCGTCATCCACACGGATTTCGAAAAAGGCTTTATCCGTGCGGAAGTGATCGCCTATGAAGACTTTATTCAATACAAAGGCGAAAACGGCGCGAAAGAAGCAGGCAAATGGCGTTTGGAAGGGAAAGATTACATCGTGCAGGACGGCGATGTGATGCACTTCCGCTTCAACGTA","","","39788","MGFKCGIVGLPNVGKSTLFNALTKAGIEAANYPFCTIEPNTGVVPMPDPRLDALAEIVKPERVLPTTMEFVDIAGLVAGASKGEGLGNKFLANIRETDAIGHVVRCFENDDIVHVAGKIDPLNDIDTINTELALADLDSCERAIQRLQKRAKGGDKDAKFELSVMEKILPVLSEAGMIRSVPLDKDELLAIKSYNFLTLKPTMYIANVNEDGFENNPYLDKVREFAEKEGSVVVPVCAAIEAEIAELDDDEKLEFLQDLGIEEPGLNRVIRAGYALLNLQTYFTAGVKEVRAWTVSVGATAPKAAAVIHTDFEKGFIRAEVIAYEDFIQYKGENGAKEAGKWRLEGKDYIVQDGDVMHFRFNV","1659950","From PF01018: GTP1/OBG familySeveral proteins have recently been shown to contain the 5 structural motifs characteristic of GTP-binding proteinsThese include murine DRG protein; GTP1 protein from Schizosaccharomyces pombe; OBG protein from Bacillus subtilis; and several others. Although the proteins contain GTP-binding motifs and are similar to each other, they do not share sequence similarity to other GTP-binding proteins, and have thus been classed as a novel group, the GTP1/OBG family. As yet, the functions of these proteins is uncertain, but they have been shown to be important in development and normal cell metabolism","GTP-binding protein","Cytoplasm","","
InterPro
IPR000583
Domain
Glutamine amidotransferase, class-II
PS00443\"[1-9]?GATASE_TYPE_II
InterPro
IPR002917
Domain
GTP-binding protein, HSR1-related
PF01926\"[3-120]TMMR_HSR1
InterPro
IPR004396
Family
Conserved hypothetical protein 92
TIGR00092\"[1-363]TTIGR00092: GTP-binding protein YchF
InterPro
IPR006073
Domain
GTP1/OBG
PR00326\"[5-25]T\"[26-44]T\"[70-85]T\"[87-105]TGTP1OBG
InterPro
IPR012675
Domain
Beta-grasp fold, ferredoxin-type
G3DSA:3.10.20.30\"[279-363]Tno description
InterPro
IPR013029
Domain
Protein of unknown function DUF933
PF06071\"[279-362]TDUF933
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[1-278]Tno description
PTHR23305\"[1-363]TGTP-BINDING PROTEIN-RELATED
PTHR23305:SF4\"[1-363]TGTP-BINDING PROTEIN


","BeTs to 26 clades of COG0012COG name: Predicted GTPaseFunctional Class: RThe phylogenetic pattern of COG0012 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 6.5e-28) to 1/1 blocks of the IPB000765 family, which is described as \"GTP1/OBG family\". Interpro entry for IP:IPR000765. IPB000765 3-46 6.2e-28","Residues 183 to 228 match (4e-07) PD:PD470686 which is described as PROTEOME COMPLETE GTP-BINDING PROBABLE PROTEIN NMA0618 PA4673 SLL0245 ","","","","","","","","","","","Fri Jan 10 09:31:21 2003","Fri Jan 10 09:18:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02417 is paralogously related to AA02886 (1e-13).","","","","","","Residues 124 to 363 (E-value = 5.4e-175) place AA02417 in the DUF933 family which is described as Protein of unknown function (DUF933) (PF06071)","","","","","","","","1","","","" "AA02418","1661871","1661230","642","TTGAGAAAAAACCGACTTTCCGCTACAATACGCGCCATTCTTTTTAGCAAGCAAAGCACTATGTCAGAAATCAAACTTATCGTCGGGATTGGCAATCCCGGTGACAAATATGCGGACACCCGTCACAATGCAGGTGTGTGGTTAATGGAGCGTTTAGCGCGCCGTTTTAACGTTATCTTAAATCCGGAAAACAAATTTTTCGGCTACACCGCGCGTGCCGTGGTGAACGGCAAAGAAGTGCGTTTTTTGGTGCCGACGACATTTATGAATTTAAGCGGCAAAGCAGTGGGCACACTGGCGAATTTTTACCGTATTAAGCCGGAAGAAATTTTGGTTCTGCACGATGAGTTGGATTTACCGCCCGGCACGGCGAAACTCAAATTGGGTGGCGGACACGGCGGGCATAACGGGCTGAAAGACATCGTGGCGCAGCTGGGCAATAGCAATAATTTTCACCGTTTACGCATCGGCATTGGTCACCCCGGGCATCGCGATTTGGTGGCGGGTTATGTGTTAAATAAGCCCGCGCCAAGCGAACGCGACGCGTTAGACAAAGCCCTGGACGAAGCGACGGATTGCGTAGAGTTGCTTTTTAAAGACGGCATGGTGAAAGCCACCCATCGGCTAAACAGTTTTAAAATT","","","24936","LRKNRLSATIRAILFSKQSTMSEIKLIVGIGNPGDKYADTRHNAGVWLMERLARRFNVILNPENKFFGYTARAVVNGKEVRFLVPTTFMNLSGKAVGTLANFYRIKPEEILVLHDELDLPPGTAKLKLGGGHGGHNGLKDIVAQLGNSNNFHRLRIGIGHPGHRDLVAGYVLNKPAPSERDALDKALDEATDCVELLFKDGMVKATHRLNSFKI","1661230","From PF01195: Peptidyl-tRNA hydrolase.Peptidyl-tRNA hydrolase is a bacterial enzyme that cleavespeptidyl-tRNA or N-acyl-aminoacyl-tRNA to yield free peptides or N-acyl-amino acids and tRNA. The natural substrate for this enzyme may be peptidyl-tRNA which drop off the ribosome during protein synthesis.Bacterial PTH has been found to be evolutionary related to a yeast protein. ","peptidyl-tRNA hydrolase","Cytoplasm","","
InterPro
IPR001328
Family
Peptidyl-tRNA hydrolase
PD005324\"[91-158]TPTH_HAEIN_P44682;
G3DSA:3.40.50.1470\"[8-210]Tno description
PTHR17224\"[24-211]TPEPTIDYL-TRNA HYDROLASE
PF01195\"[26-210]TPept_tRNA_hydro
TIGR00447\"[24-211]Tpth: peptidyl-tRNA hydrolase
PS01195\"[37-50]TPEPT_TRNA_HYDROL_1
PS01196\"[131-141]TPEPT_TRNA_HYDROL_2


","BeTs to 19 clades of COG0193COG name: Peptidyl-tRNA hydrolaseFunctional Class: JThe phylogenetic pattern of COG0193 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 7e-55) to 4/4 blocks of the IPB001328 family, which is described as \"Peptidyl-tRNA hydrolase\". Interpro entry for IP:IPR001328. IPB001328A 26-45 1.3e-14 IPB001328B 82-93 1.5e-05 IPB001328C 110-141 5.1e-23 IPB001328D 151-161 2.5e-07","Residues 26 to 87 match (7e-24) PD:PD580762 which is described as HYDROLASE COMPLETE PROTEOME PEPTIDYL-TRNA PTH PEPTIDYL TRNA V SPORULATION STAGE ","","","","","","","","","","","Mon Jan 13 18:20:36 2003","Mon Jan 13 18:17:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02418 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 26 to 210 (E-value = 4.5e-109) place AA02418 in the Pept_tRNA_hydro family which is described as Peptidyl-tRNA hydrolase (PF01195)","","","","","Menez J, Buckingham RH, Zamaroczy Md M, Campelli CK. Peptidyl-tRNA hydrolase in Bacillus subtilis, encoded by spoVC, isessential to vegetative growth,whereas the homologous enzyme inSaccharomyces cerevisiae is dispensable. Mol Microbiol. 2002 Jul;45(1):123-9. PMID: 12100553 Bonin PD, Choi GH, Trepod CM, Mott JE, Lyle SB, Cialdella JI, Sarver RW, Marshall VP, Erickson LA. Expression, purification, and characterization of peptidyl-tRNA hydrolase from Staphylococcus aureus. Protein Expr Purif. 2002 Feb;24(1):123-30. PMID: 11812233 Menez J, Remy E, Buckingham RH. Suppression of thermosensitive peptidyl-tRNA hydrolase mutation inEscherichia coli by gene duplication. Microbiology. 2001 Jun;147(Pt 6):1581-9. PMID: 11390689 Garcia-Villegas,M.R., De La Vega,F.M., Galindo,J.M., Segura,M., Buckingham,R.H. and Guarneros,G. Peptidyl-tRNA hydrolase is involved in lambda inhibition of host protein synthesis EMBO J. 10 (11), 3549-3555 (1991) PubMed: 1833189 ","","Mon Jan 13 18:18:28 2003","1","","","" "AA02419","1661871","1662014","144","ATGAAAGGGAAGACCAAACCGCACTTTGATCTGCCCCCAAAAGCTAGGCACCACAGCTCACCAATTAAGGTGCAGATTATTATGGGTAAACATTATTCAATCGAATTCAAAAATCACATCGTCAACCTAGCACAGCGAGAAAAA","","","5599","MKGKTKPHFDLPPKARHHSSPIKVQIIMGKHYSIEFKNHIVNLAQREK","1662014","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 14:38:31 2004","Wed Feb 25 14:38:31 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA1011.AA02419 is paralogously related to AA02681 (0.001).","Wed Feb 25 10:56:55 2004","","","","","","","","","","","","","1","","","" "AA02420","1662210","1662728","519","TTGAAGATTATCGAGCTCTCCCGTTCGACCTTCTATTACACGCCGAAACCCAAAGACCACGGCGACATGCGCCAACGTATTTTAGCCCCTTATCAGCAAAACGAAGGGCGCAATGGGTATCGAATGATTCGAATAAAACTACGTAAAGAAGGGATATTCATCAGTGGTAAAACAGTGTTGGCATTGGGAATTCGTTCTTGTGTGAGAGTGAAAAAACGTAAGGAAGTGGGGAAAACGAGCCATATTGCGCTGAATTTGCTGCAATGCAACTTTACCGCTGCGAAGTTGAAGGAGAAATGGGTAATGCCCGGAGCTAAAACGGATGTGACCGAACTTCGGGTGGGGCGTGAGAAACTGTATCTTTCCCCCATGATGGACTTAGCCAATCAGGAGATTATCGCCTTTAGAACGGGACGACGCCCGATATTCGGTTTGGTCTCATCAATGTTGAAAAAGACATTAAGGCAATTAAAGGAAACGGATTTACCGATTAGAGACAATTTTCAGTTTAGGATGAAG","","","20339","LKIIELSRSTFYYTPKPKDHGDMRQRILAPYQQNEGRNGYRMIRIKLRKEGIFISGKTVLALGIRSCVRVKKRKEVGKTSHIALNLLQCNFTAAKLKEKWVMPGAKTDVTELRVGREKLYLSPMMDLANQEIIAFRTGRRPIFGLVSSMLKKTLRQLKETDLPIRDNFQFRMK","1662728","","ISRSO11 related transposase","Cytoplasm","","
noIPR
unintegrated
unintegrated
PD688335\"[31-62]TQ70Q80_ECOLI_Q70Q80;


","BeTs to 7 clades of COG2801COG name: Putative transposaseFunctional Class: LThe phylogenetic pattern of COG2801 is ---p-----drlbcefgh-n-j---wNumber of proteins in this genome belonging to this COG is","","","","","","","Sat Jan 25 13:48:13 2003","","","","","","","Mon Jan 13 18:42:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02420 is paralogously related to AA01444 (3e-25), AA01268 (3e-25), AA02342 (5e-17), AA02117 (5e-17), AA01287 (5e-17), AA01077 (5e-17), AA00010 (5e-17) and AA00643 (0.001).","","","","","","","","","","","","","","1","","","" "AA02421","1667360","1667184","177","ATGGGGAGTGAATCTCAGAAAGTGCGTCTAAGTTCGGATTGGAGTCTGCAACTCGACTCCATGAAGTCGGAATCGCTAGTAATCGCGAATCAGAATGTTGCGGTGAATACGTTCCCGGGCCTTGTACACACCGCCCGTCACACCATGGGAGTGGGTTGTACCAGAAAGTGGATAGCT","","","6457","MGSESQKVRLSSDWSLQLDSMKSESLVIANQNVAVNTFPGLVHTARHTMGVGCTRKWIA","1667184","","conserved hypothetical protein","Periplasm, Cytoplasm","This sequence is similar to gi|27359373, a predicted conserved hypothetical from Vibrio vulnificus CMCP6. See also gi|23015882 from Magnetospirillum magnetotacticum.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 14:41:31 2004","Wed Feb 25 14:41:31 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02421 is paralogously related to AA02297 (2e-27), AA01566 (2e-27), AA01261 (2e-27), AA00621 (2e-27) and AA00412 (2e-27).","Wed Feb 25 10:54:25 2004","","","","","","","","","","","","","1","","","" "AA02422","1668154","1668486","333","ATGCTATTAACACACCAACCTTCCTCAATACCGAAAGAACTTTACAACCCGAAGGCCTTCTTCATTCACGCGGCATGGCTGCGTCAGGGTTGCCCCCATTGCGCAATATTCCCCACTGCTGCCTCCCGTAGGAGTCCGGGCCGTGTCTCAGTCCCGGTGTGGCTGGCCATCCTCTCAGACCAGCTAGCGATCGTCGGCTTGGTAGGCCCTTACCCCACCAACTACCTAATCACACTTGGGTTCATCTCATGGCATGCGGCCATAAAGTCCCGCACTTTCGTCTCCCGACCCTACGCGGTATTAGCGACAGTTTCCCGTCGTTATCCCCCTCCA","","","12310","MLLTHQPSSIPKELYNPKAFFIHAAWLRQGCPHCAIFPTAASRRSPGRVSVPVWLAILSDQLAIVGLVGPYPTNYLITLGFISWHAAIKSRTFVSRPYAVLATVSRRYPPP","1668486","","conserved hypothetical protein","Inner membrane, Cytoplasm","This sequence is similar to gi27360487, a predicted conserved hypothetical protein from Vibrio vulnificus CMCP6.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 14:44:40 2004","Wed Feb 25 14:47:51 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02422 is paralogously related to AA02298 (1e-63), AA00622 (1e-63), AA00413 (9e-63), AA01565 (2e-30) and AA01260 (4e-13).","Wed Feb 25 10:50:51 2004","","","","","","","","","","","","","1","","","" "AA02423","1670312","1669242","1071","ATGTTACTGACGTTAATTTTTACATTTTGGGGAGCATTTTTAACTTTACTCGTGATGCGTCCCGCTGCAATTCGATTCGGCTTGGTGGATAAACCTAACTACCGTAAACGCCATCAGGGCGCGGTTCCGTTAATCGGTGGAATTTCATTGTTTATGGGTAACCTTTGTTTTTACCTGATGCAATGGGATCAAACCCGTTTACCTTACCTTTATTTATTCAGTATTTTGGTGTTGTTATTAATGGGGATCATTGATGACCGCTATGACATTAGTCCTTTTCTGCGCGCCGGTATTCAGGCATTTTTAGCCATTCTGATGATTGATATGGGGAATGTTTACCTCGATCATCTGGGGCAAATTCTTGGTCCGTTTCAGTTAACGTTAGGATCTATCGGTTTAATTATTACTGTGTTGGCGACCATTGGGATCATTAACGCATTTAATATGATTGACGGAATTGACGGTTTGCTCGGCGGCTTGTCTTGTGTCTCTTTTGCGGCGATTGGTATTTTGATGTACCGCGACGGACAAATGGATTTGGCGTATTGGAGTTTTGGTTTAATCATTGCGATTCTTCCTTATTTATTGATGAATCTGGGGATTCCGCTGGGACCAAAATTTAAAGTATTTATGGGGGATGCGGGCAGTACGTTAATCGGCTTTACGATTATTTGGATTCTTTTACTAAGCACACAAGGCAAAGGGCATCCGATGAATCCGGTGACCGCCCTTTGGGTGATTGCGATTCCGTTGGTAGATATGGTGGCAATTATTTATCGTCGTTTACGCAAAGGCAAAAGCCCGTTCCGTCCGGATCGATTGCACGTACATCATTTAATGGTGCGCGCCGGTTTAACTTCCCGCCAGGCGTTTTTATTAATTACCTTTGTGGCGGCGTTATGTGCCGGGTTCGGTATTTTGGGTGAGATCTACTACATTAATGAATGGGTGATGTTTATTGCTTTCATTATTCTGTTCTTCTTATATTCTTACTCTATTACACGGGCGTGGAAAATTACCCGCTGGATACGTCGCATGAAGCGCCGTGCTGCAAGACGTTCTAAAATTAAA","","","41831","MLLTLIFTFWGAFLTLLVMRPAAIRFGLVDKPNYRKRHQGAVPLIGGISLFMGNLCFYLMQWDQTRLPYLYLFSILVLLLMGIIDDRYDISPFLRAGIQAFLAILMIDMGNVYLDHLGQILGPFQLTLGSIGLIITVLATIGIINAFNMIDGIDGLLGGLSCVSFAAIGILMYRDGQMDLAYWSFGLIIAILPYLLMNLGIPLGPKFKVFMGDAGSTLIGFTIIWILLLSTQGKGHPMNPVTALWVIAIPLVDMVAIIYRRLRKGKSPFRPDRLHVHHLMVRAGLTSRQAFLLITFVAALCAGFGILGEIYYINEWVMFIAFIILFFLYSYSITRAWKITRWIRRMKRRAARRSKIK","1669240","From Genbank:[gi:2507110] This protein catalyzes the synthesis of Und-PP-GlcNAc (Lipid I), the first lipid-linked intermediate involved in ECA synthesis. This lipid is also an acceptor for the addition of subsequent sugars to complete the biosynthesis of O-antigen.","undecaprenyl-phosphate alpha-N-acetylglucosaminyltransferase","Inner membrane, Cytoplasm","","
InterPro
IPR000715
Family
Glycosyl transferase, family 4
PTHR22926\"[20-353]TPHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE
PF00953\"[68-236]TGlycos_transf_4
InterPro
IPR003524
Family
Phospho-N-acetylmuramoyl-pentapeptide transferase
PS01348\"[145-156]TMRAY_2
InterPro
IPR012750
Family
Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphatetransferase
TIGR02380\"[2-346]TECA_wecA: undecaprenyl-phosphate alpha-N-ac
noIPR
unintegrated
unintegrated
PTHR22926:SF2\"[20-353]TGLYCOSYL TRANSFERASE
signalp\"[1-23]?signal-peptide
tmhmm\"[4-24]?\"[39-59]?\"[69-84]?\"[94-114]?\"[128-148]?\"[153-173]?\"[179-199]?\"[209-229]?\"[239-259]?\"[290-312]?\"[318-338]?transmembrane_regions


","BeTs to 15 clades of COG0472COG name: UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N- acetylglucosamine-1-phosphate transferaseFunctional Class: MThe phylogenetic pattern of COG0472 is --m-k-yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","","Residues 2 to 66 match (5e-18) PD:PD467609 which is described as TRANSFERASE LIPOPOLYSACCHARIDE 2.4.1.- GLYCOSYLTRANSFERASE UNDECAPRENYL-PHOSPHATE ALPHA-N-ACETYLGLUCOSAMINYLTRANSFERASE BIOSYNTHESIS TRANSMEMBRANE GLCNAC-1-PHOSPHATE UDP-GLCNAC:UNDECAPRENYL-PHOSPHATE ","","","","","","","","","","","Tue Jan 14 09:16:23 2003","Tue Jan 14 08:18:53 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02423 is paralogously related to AA00839 (2e-04).","","","","","","Residues 68 to 236 (E-value = 1.1e-08) place AA02423 in the Glycos_transf_4 family which is described as Glycosyl transferase (PF00953)","","","","","Ohta,M., Ina,K., Kusuzaki,K., Kido,N., Arakawa,Y. and Kato,N.Cloning and expression of the rfe-rff gene cluster of EscherichiacoliMol. Microbiol. 5 (8), 1853-1862 (1991)PubMed: 1722555Anderson,M.S., Eveland,S.S. and Price,N.P.Conserved cytoplasmic motifs that distinguish sub-groups of thepolyprenol phosphate:N-acetylhexosamine-1-phosphate transferasefamilyFEMS Microbiol. Lett. 191 (2), 169-175 (2000)PubMed: 11024259Amer,A.O. and Valvano,M.A.Conserved aspartic acids are essential for the enzymic activity ofthe WecA protein initiating the biosynthesis of O-specificlipopolysaccharide and enterobacterial common antigen inEscherichia coliMicrobiology 148 (Pt 2), 571-582 (2002)PubMed: 11832520","","Tue Jan 14 09:16:23 2003","1","","","" "AA02425","1670441","1671721","1281","ATGATAAATTCAACCGCACTTTTTTCCCGCGCCCAACAAGTAATTCCCGGCGGGGTGAACTCTCCCGTTCGCGCCTTTAACAGCGTCGGCGGAACACCGGTCTTCATTGAGAAGGCTGAAGGCGCATACATTTACGATACGGAAGGCAAACAATATATCGATTACGTCGGTTCATGGGGGCCGATGATTTTAGGACACAACCACCCGTCCATCTTAAACGCCGTCATCAAAACTGCACAAAACGGGCTCAGTTTCGGTGCACCGACGCCGTTGGAAATCGAGCTTGCCGAATTGGTGTGCAGCCTGGTTCCGTCTATTGAAATGGTCAGAATGGTCAGCTCCGGCACCGAAGCCACCATGTCCGCCATTCGTTTGGCGCGCGGCTACACCAAGCGCGACAAAATCATTAAATTTGAAGGTTGCTATCACGGTCATGCAGATTCACTGCTGGTAAAAGCCGGTTCCGGCGCATTAACGCTGGGGCAACCCAACTCACCGGGCGTGCCGGCGGATTTCGCCAAACACACCCTCACCTGCACCTACAACGATCTTGATTCCGTCCAACAAGCATTTGAACAATACCCTGATGACATCGCCTGCGTGATCGTCGAACCGGTTGCCGGTAATATGAACTGCGTGCCACCGAAAAATGATTTTCTGCAAGGTTTGCGCAAACTCTGCGATCAATACGGCGCGGTTTTTATTATTGACGAAGTGATGACCGGCTTCCGCGTGGCGCTTGATGGTGCACAAAGCTACTATAATGTCGCGCCGGATTTAACCTGTTTGGGCAAAGTCATCGGCGGCGGTATGCCGGTGGGGGCGTTCGGCGGTAAAAAAGAGATCATGCAACACATTGCGCCAACCGGTCCTGTTTATCAGGCGGGTACCTTATCCGGCAACCCCATTGCCATGGCGGCGGGTATCGCTTGTTTAACGGAATTAAAACGCGCCGGCAACGAACAAAAACTCGCCCGACAAACGAAAAAACTGGCGCAAGGCTTACAACAACTGGCGGCCAAACATCAAGTGCCGTTTGCGGTCAATTATGTCGGCGGGATGTTTGGCATCTTCTTTACCGAGAAAAAAGCTGTTACCTGTTATCAGGACGTGATGGCGTGCGACACGGAAAAATTTAAACGCTTCTTCCACAAAATGTTGGATCTCGGCGTTTACCTGGCACCATCGGCATTTGAAGCGGGCTTTATGTCCCTCGCCCATTCCGATGAGGATATTGACCGCACTTTAGCGGCGGCAGATATTGCCTTTGTCGAATTGGCT","","","45776","MINSTALFSRAQQVIPGGVNSPVRAFNSVGGTPVFIEKAEGAYIYDTEGKQYIDYVGSWGPMILGHNHPSILNAVIKTAQNGLSFGAPTPLEIELAELVCSLVPSIEMVRMVSSGTEATMSAIRLARGYTKRDKIIKFEGCYHGHADSLLVKAGSGALTLGQPNSPGVPADFAKHTLTCTYNDLDSVQQAFEQYPDDIACVIVEPVAGNMNCVPPKNDFLQGLRKLCDQYGAVFIIDEVMTGFRVALDGAQSYYNVAPDLTCLGKVIGGGMPVGAFGGKKEIMQHIAPTGPVYQAGTLSGNPIAMAAGIACLTELKRAGNEQKLARQTKKLAQGLQQLAAKHQVPFAVNYVGGMFGIFFTEKKAVTCYQDVMACDTEKFKRFFHKMLDLGVYLAPSAFEAGFMSLAHSDEDIDRTLAAADIAFVELA","1671719","From InterPro Entry:IPR004639 This enzyme, glutamate-1-semialdehyde-2,1-aminomutase(glutamate-1-semialdehyde aminotransferase, GSA aminotransferase)catalyses the conversion of (S)-4-amino-5-oxopentanoateto 5-aminolevulinate during the second step of porphyrin biosynthesis by the C5 pathway. It contains a pyridoxal phosphate attached at a Lys residue at position 283 of the seed alignment. It is in the family of class III aminotransferases.Note: Similarity to Hduc and H.influenzae are to diaminobutyrate--2-oxoglutarate aminotransferase that belong to the same family of class III aminotransferases.","glutamate-1-semialdehyde aminotransferase","Cytoplasm, Periplasm","","
InterPro
IPR004639
Family
Tetrapyrrole biosynthesis, glutamate-1-semialdehyde aminotransferase
TIGR00713\"[3-426]ThemL: glutamate-1-semialdehyde-2,1-aminomut
InterPro
IPR005814
Family
Aminotransferase class-III
PTHR11986\"[21-426]TAMINOTRANSFERASE CLASS III
PF00202\"[35-361]TAminotran_3
PS00600\"[234-270]TAA_TRANSFER_CLASS_3
InterPro
IPR015421
Domain
Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10\"[69-317]Tno description
noIPR
unintegrated
unintegrated
PTHR11986:SF5\"[21-426]TGLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE


","No hits to the COGs database.","Significant hit ( 7.2e-54) to 4/4 blocks of the IPB000954 family, which is described as \"Aminotransferase class-III pyridoxal-phosphate\". Interpro entry for IP:IPR000954. IPB000954A 46-75 4.2e-15 IPB000954B 208-247 3.2e-20 IPB000954C 255-270 7e-06 IPB000954D 294-312 2.4e-08","Residues 60 to 118 match (7e-11) PD:PD541512 which is described as SYNTHETASE COMPLETE PROTEOME PHOSPHOPANTETHEINE AMINOTRANSFERASE PEPTIDE GLUTAMATE-1-SEMIALDEHYDE A SYNTHASE TRANSFERASE ","","","","","Sat Jan 25 14:36:55 2003","","","","","","Sat Jan 25 13:58:24 2003","Tue Jan 14 10:18:26 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02425 is paralogously related to AA00280 (3e-23).","","","","","","Residues 23 to 427 (E-value = 4.8e-124) place AA02425 in the Aminotran_3 family which is described as Aminotransferase class-III (PF00202)","","","","","Hennig M, Grimm B, Contestabile R, John RA, Jansonius JN.Crystal structure of glutamate-1-semialdehyde aminomutase: an alpha2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivity.Proc Natl Acad Sci U S A. 1997 May 13;94(10):4866-71.PMID: 9144156Contestabile R, Jenn T, Akhtar M, Gani D, John RA.Reactions of glutamate 1-semialdehyde aminomutase with R- and S-enantiomers of a novel,mechanism-based inhibitor, 2,3-diaminopropyl sulfate.Biochemistry. 2000 Mar 21;39(11):3091-6.PMID: 10715130 Contestabile R, Angelaccio S, Maytum R, Bossa F, John RA.The contribution of a conformationally mobile, active site loop to the reaction catalyzed by glutamate semialdehyde aminomutase.J Biol Chem. 2000 Feb 11;275(6):3879-86.PMID: 10660","","Sat Jan 25 14:36:55 2003","1","","","" "AA02426","1674286","1671803","2484","GTGGATCAATTCATCGCCAACCGCACCGCGTTTTACGATCAATTACTCGCCCGTTTGTGGCGACATTTTCAATTCGCCGACGATTCTACGTTGAGCCTTATTGCGGTGGGCGGCTACGGGCGGGAGGAAATGTTTCCCCTTTCCGATTTGGATATTTTAATTTTAACCGAACAACCCGCGACACCTGCGCTACAGGAAAATCTGGGGCAATTTGTGCAGTTTTTATGGGATTGCGGTTTTAATGTGGGACACAGTATTCGTACTCTTGAAGAATGTAAAACGGAGGGGCTGGCGGACATTACCATCGCCACCAATTTGCTGGAAGTGCGCTATTTATGCGGCAACCGTAATGTGTTTAAAGCGCTGGTGAATTTGGTGCAACAATCGGATTTTTGGTCGAAAACGGATTTCTGTCAGGCAAAAATTCAGGAGAAAATCGAACGTTATCAACGTTATAACAACACCTCATACAATCTTGAGCCGGACATCAAATACAGTCCGGGCGGGTTGCGCGATTTGCATTTGTTGTATTGGATCGCGTTGCGCCATAACGGGGCTAAAAATTTACAGGAAATTTTACAGGCGGGGTTTATTCATCCGGCAGAACACGCCTTGTTACTAAAAAGCCAGCAATTTCTGTTTAAAGTGCGGTACGCTTTGCACTTAATTTTAAAGCGTTATGACAACCGCCTGTTGTTTGATCGCCAACTGAAAGTCAGCGAATTGTTGGGTTTCCAGGGGGAAGGCAATCAAGGCGTGGAAGCCATGATGAAGCGCTTTTTTCAGGCGTTGCATTCCATTTCGTTACTAAGCGAATTGTTGGTAAAACATTATCAGGAACATTTTTTAACCCGTCATGCAGTGGTGAGCGAGCAAATACTCGATGACAATTTCAGCCTGATCAATCAATCCATTTGCTTACGTAATCATCAATGCTTTGAGCAGCAGCCGGAAAGCATTCTTGACCTTTTTTATCATTTAACCCAATATCCGCAGGCGGAAATTCATTCCTTTGTCTTGCGCGAGCTTTATTTGGCGCTGGAGCAACGGCAGGGCTATTTGTGTGATTTGCCAGCGGCGCGGGAAAAATTCGTGCGCCTGTTTAATCAGCCGAATGCGATTAAACGTGCTTTTTTCCCTATGCACCAATACGGCGTGCTTACCGCCTATTTACCGCAATGGGGCAACGTCGTCGGTTTAATGCAGTTTGATTTATTTCATTGTTACACCGTGGACGAGCATATTCTGCGCGTGATGTTAAAACTGGAAAGTTTTTTAGAGGGCGCTTCGGCACAAAGCCATCCCATTTGCCATCAAATATTCAGCCGAATTTCCGACCGCACTTTGTTGTATATTGCCGCTTTATTTCACGACATCGCCAAAGGGCGCGGCGGTTCTCATGAATTATTGGGTGCGGTGGATGTGCGCGAATTTGCCGTTCGGCACGGTTTTGATCAACGGGAAACGGAAACCATGGTGTGGCTGGTGGAGCAGCATTTGCTTATGTCGGTCACGGCACAACGGCGGGATATTCATGATCCGGAAATTGTACTGAATTTCGCCGAACTGGTGCGTAATCAGGTGCGTTTGGATTATTTAACCTGCCTGACCGTCGCCGATATTGTGGCGACCAATGAAACTTTGTGGAATAGCTGGAAGCGTTCTTTGCTGGCGACTTTGTACGATTACGCCACCCAACAATTCGCCCAAGGGCTGGAAAGTATCTTGGATAATCAAGCGAAAGCGAAAGGACACCGCCGATTAGCACTGCAGGAAATACGTGAAAAAACCACCGCACTTTCCGACAAACACATCGAAAAATTGTGGCAGCGTTTTCCGATAGATTATTTCTTGCGCAATTCGCCACAACAAATTGGTTGGCATACCCGTTTGCTTGCCGAATTTGAAGGGGAATTGTTGGTGAAAGTCAGTAACCGGTTTTCTGCCGGCGGCACGGAAATTTTCATTTATACCAAAGACCGACCGAACCTGTTTCACAAAGTGGTAAGTACTATCGGCGCGAAAAAACTCAGTATCCATGATGCGCAAATTATCACCGCCAAAGACGGCTATGTGTTGGACAGTTTTATTGTGACGGAATTAGACGGTTCCGTGCTGCCTTTTGATCGCCGCCGAATGTTGGAAGATGCGCTCACGGAAAGTTTAACTTCCGATGCGGTTAACAAACAGCGTCTGCGTGAAAATCATCAATTGGCACATTTTCATGTCAAAACCGAAGTGCGTTTTTTGAATCTCGAAAAAACCGATCAAACGGAAATGGAACTGTTCGCCTTAGATCAGGCGGGCTTGCTGGCAGATGTCAGCGCGGTATTCTGCGAACTGGAACTAAATTTGCTTAACGCCAAAATCACCACAATTGGTGAAAAAGCAGAAGACTTTTTTATTCTGACGAATAAGGTGGACAAAGCATTAAACGAAGAAGAAAGGGCGAGGTTATTGAATCGTTTATTGCAGATTTTGAGT","","","101814","VDQFIANRTAFYDQLLARLWRHFQFADDSTLSLIAVGGYGREEMFPLSDLDILILTEQPATPALQENLGQFVQFLWDCGFNVGHSIRTLEECKTEGLADITIATNLLEVRYLCGNRNVFKALVNLVQQSDFWSKTDFCQAKIQEKIERYQRYNNTSYNLEPDIKYSPGGLRDLHLLYWIALRHNGAKNLQEILQAGFIHPAEHALLLKSQQFLFKVRYALHLILKRYDNRLLFDRQLKVSELLGFQGEGNQGVEAMMKRFFQALHSISLLSELLVKHYQEHFLTRHAVVSEQILDDNFSLINQSICLRNHQCFEQQPESILDLFYHLTQYPQAEIHSFVLRELYLALEQRQGYLCDLPAAREKFVRLFNQPNAIKRAFFPMHQYGVLTAYLPQWGNVVGLMQFDLFHCYTVDEHILRVMLKLESFLEGASAQSHPICHQIFSRISDRTLLYIAALFHDIAKGRGGSHELLGAVDVREFAVRHGFDQRETETMVWLVEQHLLMSVTAQRRDIHDPEIVLNFAELVRNQVRLDYLTCLTVADIVATNETLWNSWKRSLLATLYDYATQQFAQGLESILDNQAKAKGHRRLALQEIREKTTALSDKHIEKLWQRFPIDYFLRNSPQQIGWHTRLLAEFEGELLVKVSNRFSAGGTEIFIYTKDRPNLFHKVVSTIGAKKLSIHDAQIITAKDGYVLDSFIVTELDGSVLPFDRRRMLEDALTESLTSDAVNKQRLRENHQLAHFHVKTEVRFLNLEKTDQTEMELFALDQAGLLADVSAVFCELELNLLNAKITTIGEKAEDFFILTNKVDKALNEEERARLLNRLLQILS","1671801","From Genbank:[gi:21362567]: This protein modifies, by uridylylation or deuridylylation the PII (glnB) regulatory protein.","uridylyltransferase","Cytoplasm","","
InterPro
IPR002912
Domain
Amino acid-binding ACT
PF01842\"[652-716]T\"[758-828]TACT
InterPro
IPR002934
Domain
DNA polymerase, beta-like region
PF01909\"[16-107]TNTP_transf_2
InterPro
IPR003607
Domain
Metal-dependent phosphohydrolase, HD region
SM00471\"[407-554]THDc
InterPro
IPR006674
Domain
Metal-dependent phosphohydrolase, HD region, subdomain
PF01966\"[411-545]THD
InterPro
IPR010043
Family
Protein-PII uridylyltransferase
PTHR13734:SF1\"[74-821]T[PROTEIN-PII] URIDYLYLTRANSFERASE (PII URIDYLYL- TRANSFERASE) (URIDYLYL REMOVING ENZYME) (UTASE)
TIGR01693\"[1-828]TUTase_glnD: protein-P-II uridylyltransferas
InterPro
IPR013546
Domain
GlnD PII-uridylyltransferase
PF08335\"[135-343]TGlnD_UR_UTase
noIPR
unintegrated
unintegrated
PTHR13734\"[74-821]TTRNA-NUCLEOTIDYLTRANSFERASE/POLY(A) POLYMERASE FAMILY MEMBER


","BeTs to 6 clades of COG2844COG name: UTP:GlnB (protein PII) uridylyltransferaseFunctional Class: OThe phylogenetic pattern of COG2844 is ----------r---efgh-n-j----Number of proteins in this genome belonging to this COG is","","Residues 758 to 806 match (5e-13) PD:PD309136 which is described as TRANSFERASE URIDYLYL URIDYLYLTRANSFERASE NUCLEOTIDYLTRANSFERASE COMPLETE PROTEIN-PII PROTEOME UTASE ENZYME REMOVING ","","","","","","","","","","","Mon Jan 27 14:55:51 2003","Tue Jan 14 14:54:12 2003","","Mon Oct 4 07:59:58 2004","","Mon Oct 4 07:59:58 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02426 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Oct 4 07:59:58 2004","","","","","Residues 411 to 545 (E-value = 2.5e-17) place AA02426 in the HD family which is described as HD domain (PF01966)","Mon Oct 4 07:59:58 2004","","","","Hesketh A, Fink D, Gust B, Rexer HU, Scheel B, Chater K, Wohlleben W, Engels A. The GlnD and GlnK homologues of Streptomyces coelicolor A3(2) are functionally dissimilar to their nitrogen regulatory system counterparts from enteric bacteria. Mol Microbiol. 2002 Oct;46(2):319-330. PMID: 12406211 Perlova O, Nawroth R, Zellermann E, Meletzus D. Isolation and characterization of the glnD gene of Gluconacetobacter diazotrophicus, encoding a putative uridylyltransferase/uridylyl-removing enzyme. Gene. 2002 Sep 4;297(1-2):159. PMID: 12384297 Kim IH, Kwak SJ, Kang J, Park SC. Transcriptional control of the glnD gene is not dependent on nitrogen availability in Escherichia coli. Mol Cells. 1998 Aug 31;8(4):483-90. PMID: 9749538 ","","Tue Jan 14 14:54:12 2003","1","","","" "AA02427","1674456","1674325","132","TTGACTGAAATCCGTTGTGTTTTTCATGGCGGATTTTTTCTATTTCTGCTTTTTTATCACGACCTATGCTTTTTCCTTACGATACGCAAACCGACATCAGCCCAAGTGCGGTCAAAATTCAAAAAGAAAATT","","","5280","LTEIRCVFHGGFFLFLLFYHDLCFFLTIRKPTSAQVRSKFKKKI","1674325","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-34]?signal-peptide
tmhmm\"[10-28]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 10:08:13 2004","Wed Feb 25 10:08:13 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02427 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 10:08:13 2004","","","","","","","","","","","","","1","","","" "AA02429","1675257","1674460","798","ATGATTCCATTAAGAACGGAAGCTGAAATTGTTAAATTGCGGAAAGCATGTAAATTGGCATCTGATATTTTGGTGATGATTGAGCCTTATGTTAAAGAAGGCGTAACAACCGGTGAATTGGATCGTATCTGCCATGATTATATGGTGAATGAACAAAAAGCGATTCCGGCATGCTTGAATTATCATGGTTTTCCAAAATCCATTTGTACCTCTATTAATGAGGTGGTTTGTCATGGTATTCCGAATGATGATAAACGATTGAAATACGGCGATATTATAAATATTGACGTCACGGTCATCAAAGATGGTTATTACGGCGATAACTCTAAAATGTATATTGTGGGTGAAACCAATTTACGTAGTAAAAAATTGGTGGAAGCGGCACAAGAAGCGCTTTACGTGGGCTTGCGTACGGTAAAACCGGGGATTCGTCTCAATGAAATCGGTCGCGCGGTGCAAAAATATACGGAATCGCAAACCTTCAGTGTGGTACGCGAATATTGCGGGCATGGCGTGGGCACGGAATTCCACTGCGAACCGCAAGTGTTACATTATTACGCGGACGACGGCGGCGTGATTTTAAAACCGGGCATGGTGTTTACCATCGAGCCGATGATTAACGCCGGTAAAAAAGAAGTGCGTTTAATGGGCGACGGTTGGACGGTGAAAACCAAAGATCGTAGCCATTCCGCCCAATTCGAGCATCAACTGGTGGTCACCGAAAATGGTTGTGAAGTCATGACCATTCGTGATGAAGAAATTGCCGAAGGGCGTATTCAGCGTTTTATGGTGAATGTT","","","30306","MIPLRTEAEIVKLRKACKLASDILVMIEPYVKEGVTTGELDRICHDYMVNEQKAIPACLNYHGFPKSICTSINEVVCHGIPNDDKRLKYGDIINIDVTVIKDGYYGDNSKMYIVGETNLRSKKLVEAAQEALYVGLRTVKPGIRLNEIGRAVQKYTESQTFSVVREYCGHGVGTEFHCEPQVLHYYADDGGVILKPGMVFTIEPMINAGKKEVRLMGDGWTVKTKDRSHSAQFEHQLVVTENGCEVMTIRDEEIAEGRIQRFMVNV","1674458","From Genbank:[gi:1168444]This enzyme removes the amino-terminal methionine from nascent proteins.","methionine aminopeptidase","Cytoplasm","","
InterPro
IPR000994
Domain
Peptidase M24, catalytic core
G3DSA:3.90.230.10\"[1-263]Tno description
PTHR10804\"[55-263]TPROTEASE FAMILY M24 (METHIONYL AMINOPEPTIDASE, AMINOPEPTIDASE P)
PF00557\"[11-249]TPeptidase_M24
InterPro
IPR001714
Family
Peptidase M24, methionine aminopeptidase
PR00599\"[68-81]T\"[91-107]T\"[161-173]T\"[192-204]TMAPEPTIDASE
InterPro
IPR002467
Family
Peptidase M24A, methionine aminopeptidase, subfamily 1
PTHR10804:SF13\"[55-263]TMETHIONINE AMINOPEPTIDASE 1
TIGR00500\"[2-250]Tmet_pdase_I: methionine aminopeptidase, typ
PS00680\"[167-185]TMAP_1


","BeTs to 24 clades of COG0024COG name: Methionine aminopeptidaseFunctional Class: JThe phylogenetic pattern of COG0024 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit (1.3e-109) to 6/6 blocks of the IPB002467 family, which is described as \"Methionine aminopeptidase, subfamily 1\". Interpro entry for IP:IPR002467. IPB002467A 31-48 2.7e-10 IPB002467B 60-81 1.7e-21 IPB002467C 87-115 4e-19 IPB002467D 160-185 1.3e-20 IPB002467E 194-206 1.2e-10 IPB002467F 218-248 6.9e-21 IPB002467A 139-156 0.018Significant hit ( 1.4e-38) to 4/4 blocks of the PR00599 family, which is described as \"Methionine aminopeptidase-1 signature\". Prints database entry for PR:PR00599. PR00599A 68-81 3.2e-10 PR00599B 91-107 4.3e-09 PR00599C 161-173 8.5e-08 PR00599D 192-204 1.1e-06Significant hit ( 1.4e-11) to 4/5 blocks of the IPB001131 family, which is described as \"Proline dipeptidase\". Interpro entry for IP:IPR001131. IPB001131B 91-112 9.8 IPB001131C 166-178 4.5 IPB001131D 194-207 1.4e-05 IPB001131E 230-248 2.9","Residues 35 to 98 match (1e-17) PD:PD523104 which is described as AMINOPEPTIDASE METHIONINE HYDROLASE PEPTIDASE M MAP COBALT PROTEOME COMPLETE AMINOPEPTIDASE-LIKE ","","","","","","","","","","","Tue Jan 14 15:05:28 2003","Tue Jan 14 15:05:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02429 is paralogously related to AA01360 (8e-04).","","","","","","Residues 165 to 238 (E-value = 1.1e-26) place AA02429 in the Peptidase_M24 family which is described as metallopeptidase family M24 (PF00557)","","","","","Lowther,W.T., Zhang,Y., Sampson,P.B., Honek,J.F. and Matthews,B.W.Insights into the mechanism of Escherichia coli methionineaminopeptidase from the structural analysis of reaction productsand phosphorus-based transition-state analoguesBiochemistry 38 (45), 14810-14819 (1999)PubMed: 10555963","","Tue Jan 14 15:10:03 2003","1","","","" "AA02430","1675391","1675729","339","ATGACAGAGATATCAGTTCCGTTAACTTTTACCGACGCAGCTGCGCAAAAAGTTAAGACCTTAATTACCGAAGAAGAAAATCCGGCACTTAAATTGCGCGTATACATCACCGGTGGCGGTTGCAGCGGGTTCCAATACGGTTTCACCTTCGACGAAAAAGTCAACGACGGTGACCTCACCGTGGAAAATTCGGGCGTACAATTAGTCATTGATCCAATGAGCTTACAATATTTAATCGGCGGCACCGTTGATTACACCGAAGGTTTGGAAGGTTCACGTTTTGTCGTAAACAACCCAAACGCCACCTCCACTTGCGGTTGCGGTTCTTCCTTCAGTATC","","","13420","MTEISVPLTFTDAAAQKVKTLITEEENPALKLRVYITGGGCSGFQYGFTFDEKVNDGDLTVENSGVQLVIDPMSLQYLIGGTVDYTEGLEGSRFVVNNPNATSTCGCGSSFSI","1675727","From PF01521:HesB-like domainThis family includes HesB which may be involved in nitrogen fixation; the hesB gene is expressed only under nitrogen fixation conditions. Other members of this family include various hypothetical proteins. ","conserved hypothetical protein","Periplasm, Extracellular","","
InterPro
IPR000361
Family
HesB/YadR/YfhF
PD002183\"[32-94]TYADR_HAEIN_P45344;
PTHR10072\"[1-113]THES-B
PF01521\"[8-99]TFe-S_biosyn
TIGR00049\"[8-113]TTIGR00049: iron-sulfur cluster assembly acc
PS01152\"[94-111]THESB
noIPR
unintegrated
unintegrated
G3DSA:2.60.300.12\"[8-99]Tno description
PTHR10072:SF26\"[1-113]THES-B


","BeTs to 13 clades of COG0316COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG0316 is ------yq-dr-bcefghsn-jx---Number of proteins in this genome belonging to this COG is","Significant hit ( 8.2e-35) to 2/2 blocks of the IPB000361 family, which is described as \"Hypothetical hesB/yadR/yfhF family\". Interpro entry for IP:IPR000361. IPB000361A 32-52 1.5e-12 IPB000361B 80-111 6.9e-21","","","","","","","","","","","","Tue Jan 14 15:22:18 2003","Tue Jan 14 15:19:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02430 is paralogously related to AA00711 (4e-17) and AA01221 (3e-04).","","","","","","Residues 7 to 112 (E-value = 3.3e-57) place AA02430 in the HesB family which is described as HesB-like domain (PF01521)","","","","","","","","1","","","" "AA02431","1675734","1675946","213","ATGGATTTTCAATTCACCGCCTATCAAGGCAATATCATCACCAAGCGTTCCATGGAATATAGCGTTTTCGCTAATCGGTTTAACATCGAAGTGCGGTCGGATCCACAGTTAAATCGATCACAAACGGAATTAGAAGAGATAGGTTTTATTGTAACGCCACAATCATTGCCTTTTGCAGCATTGAAAATTTCGCCCGTTTTCTGCACCCTTAAT","","","8147","MDFQFTAYQGNIITKRSMEYSVFANRFNIEVRSDPQLNRSQTELEEIGFIVTPQSLPFAALKISPVFCTLN","1675944","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR008249
Family
Uncharacterised conserved protein UCP006287
PD020773\"[1-34]TYH24_HAEIN_P44297;
PF06062\"[1-35]TUPF0231


","No hits to the COGs database.","","","","","","","","","","","","","","Tue Jan 14 17:48:08 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02431 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02432","1675995","1678385","2391","ATGGCAAAGACACAAGATCACAACTCCTCCACCGAACAGCAACCGACAAAGCCGAAAAGATCTTGGAAAATCCTGATGTTAAAAACGGCATTTACCGCCTTGTGCATGCTGTTTTGCTATTCTGCCTATCTGGATTGGCAAATCCGCAGCAAAATGGACGGGCAAATTTGGCGTTTGCCGGCGGAAGTGTATAGTCGCATTGAAAACATTCGGGTCAGCGACGAACCGAGTTTTGAGCAAATCAAACAAATTTTACTGGATAACGAATATCGCCAAACCACCATGATTGCCGCGCCGGGCGATTTCAAAATTGAAGACAATACCATCGTGTTACTGCGTCGCGGCTTCCCGTTTCCCGGTACACCGGAAGCGCAACGGGTTTTCCGCCTGCGTTTCCAACAGGAAAAATTGGCGATGATTGAAGATCTGATTAACGTTAAAACCATCGACGAATTCCGCATGGCGCCGAAACTCATCGCCATTTTACAATCAGACAAAGAAGAACGCCTTGCCATTTCCTTGCAACAGTATCCTCGCCTACTCATCGACGCCTTATTACTTACCGAAGATCGCCGTTTCTTTGAACATGACGGCATCAGCCCGCTCGGCATTTTACGCGCCATGATCACCAATATTCAGGCGGGGCAAACGGTGCAAGGCGGCAGCACCCTCACCCAACAACTGGTCAAAAATCTGTTCCTAAGTAACGAACGTACCCTCAGCCGCAAAATTAACGAAGCCTTAATGGCGTTGATTCTGGACTGGCGTTACGACAAAAACCGCATTCTGGAAACCTACTTAAACGAAATTTACCTCGGACAAAACGGCGACAACCAAATCCATGGTTTTGAATTAGCCAGTCAGTTTTATTTCGGGCGTTCCGTGCGGGAAATCAGCCTGGATCAAATTGCGTTGTTGGTGGGCATGGTAAAAGGTCCGTCGCTGTATAATCCATGGCGCAACCCGAAAAACGCGCTCGAACGTCGAAACGTGGTGTTGCATTTGATGCTGGAACACAAAGTTATCGGTGAAGAACTTTATCAATTATTGAGCCAACGCCCACTCGGCGTACAGGAAAAAGGGAAAATCAGCCGTAAATATCCGGCATTTATTCAAACCCTGCAAACGGAATTACGCCATCACCTCGGCGAAGGCAAAGCCGCGAATTTATTGGGCGCACGGATTTTCTCCACCTTAGACGTGAAACAACAGAATTACGCCGAACAGGCGGTGATTAACGCCGTATCCGATTTACAGACGAAACATAAAAATCCGCACTTGGAATCCGCCATGGTGGTTGCCGATTATCAAACCGGCGAAGTGCGCGCCATCGTGGGCGGCTTACAAACTCAATTTGCCGGCTTCAACCGCGCTTTGACGGCGAAGCGGCAAATCGGTTCTTTAGTAAAACCATCCATTTATTTGACCGCACTTATGTACCCGGATCAGTTCCGCCTGAATACGCCGATCAACAATCAACCGATTACCATTAACATCAAAGGCAGTCCACCGTGGCAACCGCGCAATTACGATCGCAAATACAGCGGTTCGGTGATGTTGATGGACGCCCTGGTACGCTCCTTGAATATCCCGACGGTGAACATCGGCATGAAGCTCGGTTTGACGAAGGTGATTTCTGTGCAACAAGCCATGGGCTGGGATAAAGTCGCCATTCCGAAAGTGCCGTCAACCCTGCTCGGTTCTTATTCCATTTCGCCTTATGGTGTGACTAAACTCTATCAAACCATTGCCAACGAAGGTGCCAGCGTACCATTGAACACCATCAACAGTGTGGTGGATAGACAAGGCAATGTGATTTATGAGCGAGAATTCGCACCACAGCAAGTGGTGCCGCAAGAAGCCGCTTTCCAAACCTTATTTGCTCTGCAGCAAGTGGTAGATCGCGGCACGGCACGTAGCCTACAAAAAGACTTCGCCCACTTACATTTGGCGGGCAAAACCGGCACTACAAATAATGCGCGTGATACCTGGTTCGTGGGGATCGATGGCGAAAACGTCACCACCGTTTGGCTGGGGCGCGATGACAACGGAGAAACCAAACTCACCGGTGCCAGCGGCGCATTACAGGTTTATAAAGATTATTTACAACGTTCTGCTATCCGTCCGTTAAAACTGCATAAACCGCAAGACATCAAATGGGTCGGCATCAATTCCTACGGCGGCTGGGATTGCGCCAGTTCACGCACCATCCCCGTTTGGGCTGACAGAAATCAATCCTTCTGCCAACAAGCCGTGTTGACCCAAACCGCCAACATCATCACCAACGCCCCAACCCAAACCAACGCCAACACCGCAACCAAACCGGAAAGCGTGTGGGATGTGCTAAAAGAAGACAAATCGGTACCGGTGGAAGAAGCAAAGCCGTCAAAT","","","89984","MAKTQDHNSSTEQQPTKPKRSWKILMLKTAFTALCMLFCYSAYLDWQIRSKMDGQIWRLPAEVYSRIENIRVSDEPSFEQIKQILLDNEYRQTTMIAAPGDFKIEDNTIVLLRRGFPFPGTPEAQRVFRLRFQQEKLAMIEDLINVKTIDEFRMAPKLIAILQSDKEERLAISLQQYPRLLIDALLLTEDRRFFEHDGISPLGILRAMITNIQAGQTVQGGSTLTQQLVKNLFLSNERTLSRKINEALMALILDWRYDKNRILETYLNEIYLGQNGDNQIHGFELASQFYFGRSVREISLDQIALLVGMVKGPSLYNPWRNPKNALERRNVVLHLMLEHKVIGEELYQLLSQRPLGVQEKGKISRKYPAFIQTLQTELRHHLGEGKAANLLGARIFSTLDVKQQNYAEQAVINAVSDLQTKHKNPHLESAMVVADYQTGEVRAIVGGLQTQFAGFNRALTAKRQIGSLVKPSIYLTALMYPDQFRLNTPINNQPITINIKGSPPWQPRNYDRKYSGSVMLMDALVRSLNIPTVNIGMKLGLTKVISVQQAMGWDKVAIPKVPSTLLGSYSISPYGVTKLYQTIANEGASVPLNTINSVVDRQGNVIYEREFAPQQVVPQEAAFQTLFALQQVVDRGTARSLQKDFAHLHLAGKTGTTNNARDTWFVGIDGENVTTVWLGRDDNGETKLTGASGALQVYKDYLQRSAIRPLKLHKPQDIKWVGINSYGGWDCASSRTIPVWADRNQSFCQQAVLTQTANIITNAPTQTNANTATKPESVWDVLKEDKSVPVEEAKPSN","1678383","From Genbank:[gi:1172033] This protein is involved in cell wall formation and in the synthesis of cross-linked peptidoglycan from the lipid intermediates. This enzyme has a penicillin-insensitive transglycosylase N-terminal domain and a penicillin-sensitive transpeptidase C-terminal domain. ","penicillin-binding protein 1B","Inner membrane, Cytoplasm","","
InterPro
IPR001264
Domain
Glycosyl transferase, family 51
PD001895\"[239-290]TQ9CNH5_PASMU_Q9CNH5;
PF00912\"[152-322]TTransgly
InterPro
IPR001460
Domain
Penicillin-binding protein, transpeptidase
PF00905\"[429-703]TTranspeptidase
InterPro
IPR011813
Family
Penicillin-binding protein 1B
TIGR02071\"[24-749]TPBP_1b: penicillin-binding protein 1B
noIPR
unintegrated
unintegrated
G3DSA:3.40.710.10\"[398-703]Tno description
signalp\"[1-41]?signal-peptide
tmhmm\"[24-44]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 6.8e-63) to 3/3 blocks of the IPB001264 family, which is described as \"Glycosyltransferase family 51\". Interpro entry for IP:IPR001264. IPB001264A 172-211 9.8e-18 IPB001264B 220-272 5.4e-33 IPB001264C 281-307 1.3e-09","Residues 629 to 705 match (4e-07) PD:PD011751 which is described as PENICILLIN-BINDING COMPLETE PROTEOME CELL PEPTIDOGLYCAN SYNTHESIS WALL 1A DIVISION BINDING ","","","","","","","","","","","Wed Jan 15 08:05:24 2003","Wed Jan 15 07:53:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02432 is paralogously related to AA01304 (2e-44), AA01690 (3e-39) and AA00780 (6e-17).","","","","","","Residues 429 to 703 (E-value = 2.1e-07) place AA02432 in the Transpeptidase family which is described as Penicillin binding protein transpeptidase domain (PF00905)","","","","","Broome-Smith,J.K., Edelman,A., Yousif,S. and Spratt,B.G.The nucleotide sequences of the ponA and ponB genes encodingpenicillin-binding protein 1A and 1B of Escherichia coli K12Eur. J. Biochem. 147 (2), 437-446 (1985)PubMed: 3882429Wang,C.C., Schultz,D.E. and Nicholas,R.A.Localization of a putative second membrane association site inpenicillin-binding protein 1B of Escherichia coliBiochem. J. 316 (Pt 1), 149-156 (1996)PubMed: 8645198Lefevre,F., Remy,M.H. and Masson,J.M.Topographical and functional investigation of Escherichia colipenicillin-binding protein 1b by alanine stretch scanningmutagenesisJ. Bacteriol. 179 (15), 4761-4767 (1997)PubMed: 9244263Edelman,A., Bowler,L., Broome-Smith,J.K. and Spratt,B.G.Use of a beta-lactamase fusion vector to investigate theorganization of penicillin-binding protein 1B in the cytoplasmicmembrane of Escherichia coliMol. Microbiol. 1 (1), 101-106 (1987)PubMed: 3330753Zijderveld,C.A., Aarsman,M.E., den Blaauwen,T. and Nanninga,N.Penicillin-binding protein 1B of Escherichia coli exists in dimeric formsJ. Bacteriol. 173 (18), 5740-5746 (1991)PubMed: 1885547Vollmer,W., von Rechenberg,M. and Holtje,J.V.Demonstration of molecular interactions between the mureinpolymerase PBP1B, the lytic transglycosylase MltA, and thescaffolding protein MipA of Escherichia coliJ. Biol. Chem. 274 (10), 6726-6734 (1999)PubMed: NOT_FOUNDTerrak,M., Ghosh,T.K., van Heijenoort,J., Van Beeumen,J.,Lampilas,M., Aszodi,J., Ayala,J.A., Ghuysen,J.M. andNguyen-Disteche,M.The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coliMol. Microbiol. 34 (2), 350-364 (1999)PubMed: 10564478Goffin,C. and Ghuysen,J.M.Multimodular penicillin-binding proteins: an enigmatic family oforthologs and paralogsMicrobiol. Mol. Biol. Rev. 62 (4), 1079-1093 (1998)PubMed: 9841666","","Wed Jan 15 08:26:25 2003","1","","","" "AA02433","1678440","1678535","96","GTGGGCACAAGATCCTCCCCACAAAACACCTTTAAAAACAACCGCACTTTTTCTCCCTCTCATCAAATTCCCCTGCAACAAAATGTTACAAAAATG","","","3626","VGTRSSPQNTFKNNRTFSPSHQIPLQQNVTKM","1678535","","hypothetical protein","Cytoplasm, Periplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 10:04:37 2004","Wed Feb 25 10:04:37 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02433 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 10:04:37 2004","","","","","","","","","","","","","1","","","" "AA02434","1678687","1680591","1905","ATGCGTCTTTCCCGTTGGTATCAATGTATTCTTTTCAGTCTGTTTATTTTATTCTCGGCGTTTACTCATGCGGAAGATAACTATCAAGCATGGGTGCAGGATATTGAAAATCGGCTGGATAAAACCTCCGCACTTTACGCCGAGAACAAAACCGATGATGCTCAAACGGAAGTGCAAATGGCGTATTTTGAGGTGTTTGAAAATCTGGAAGGTCCGATTCGCATTAACTTCTCCGCACAAAAAAGCTATCAAATGGAAGCCACTTTCGGTGAAATTCGCAAAATGATTCGTGACGGATTGCCGCAAGATCAGGTAAAAGCCAAAATCGACGGGCTGAAAGCCGAGCTTCAGGAAGTGCTTCCCTCTTTAAAAGAAGGTCATCAACTCAACGCCTCCGGTCAACATGGCGTGTATGAAAACCAAACCATCGCCGCCCACTGGCAAAAAAGTTTTAAAACCATTGACGATCTATTAGCCCAAGCAATTACCGCTTATGAAGCCCAAGATTACGCCACGGCGAAAAAACTGGTGCAACAAGCGCAGTATGAGGGGTACAAAAATTCCGAAATGGAAATGTCTATTCGGCAAAATCGTTCCGCCGCCATTTCCGCCAACTTCAATCAACAATTTTACGATCTCATCAAACTCAGCGAAGTGCCTGATCAAATTAGCAATTTCGGCTATCAAATCACGACCTTGCTGCAAGACATTGAAGAACAACTTCCGGACTTGCCGACCACCCGTGACGATCAAATTGAACAACCTGCCAATCAAACCGTCGCCGATACCACGTCGGACAAAGACTGGGCGCAAATCAGCGTGCAGGTGAATGCAGGAATTCAGCAAGCCATTAAACTGTATGAGCAAGGCGAAGCGAAAAAAGCCATGTTAACGGTGCAGGATACCTATTTTGATATTTTTGAAAACACCGGTATGGAAAACAAAATCGGTTCCCGCAACAGCAACTTTAAAGCGCAACTGGAAGGCTATTTCACCCGTTTGGTGAGCTTAATGAAAGCCGGTGCGGAGAAAGAAAAGTTACAGGAACAAGCCACAGGGTTAAGTCAGGATTTAAGCAAAGCGGTAGACATGTTACAGGGCGGAGAACAAACCGCCTGGAGTATGTTCTTATACAGCCTGTTAATTATTGTACGTGAAGGCTTGGAAGCCTTGCTGATTGTTGCCGCGATCGTGGCGTATTTAGTGAAAAACGACCATCAGGACAAACTGCCCGTTATTCGCCAGTCCGTGTATGTGGCATTACTCGGTAGCGTCATCACCGCCGCCATCTTCCAGATGATTTTCTCTAATTCCGGCGCCAGCCGCGAATTGCTGGAAGGCTTCACCATGATCATCGCCGTGGTAATGCTGTTCATGATGAGCTACTGGTTATTATCCAAAGTGGAAGCACAAAACTGGAAACGATATTTAGAAGGCAAACTGTCCACCGCGTTGACCACAGGTTCTTTAGTAGGCTTATGGCTCACCAGCTTCCTGGCGGTTTATCGTGAAGGTGCGGAAACCGTGCTGTTTTACTACGCCCTTGCCGGCGACGCCAAAAGTGCGGTGGATTATTTCTATCTTTTCGGCGGCTTCTTCCTCGGTGTGATTATCCTCGCCGTGTGCTATTTCATTATGCGCTACACCGTGGTGAAATTGCCGCTTAAACCGTTCTTTATGTTCACCGGTTCCTTTATGTATTTAATGGCGTTCGTGTTCGCCGGTAAAAGCGTGCTGGAGCTGATTGAAGGCAAATTATTTGAGCCGACCCTCATTTCCGGCATGACAGAAATCCCGTGGTTGGGTATTTATCCTTATGTAGAAACATTGGTTCCGCAGGTTGTGCTGTTGGTCGCCGCTGTTTTTGCGTTAATTTATATGAAGTACCAAAGCAAAAAATCTATT","","","71865","MRLSRWYQCILFSLFILFSAFTHAEDNYQAWVQDIENRLDKTSALYAENKTDDAQTEVQMAYFEVFENLEGPIRINFSAQKSYQMEATFGEIRKMIRDGLPQDQVKAKIDGLKAELQEVLPSLKEGHQLNASGQHGVYENQTIAAHWQKSFKTIDDLLAQAITAYEAQDYATAKKLVQQAQYEGYKNSEMEMSIRQNRSAAISANFNQQFYDLIKLSEVPDQISNFGYQITTLLQDIEEQLPDLPTTRDDQIEQPANQTVADTTSDKDWAQISVQVNAGIQQAIKLYEQGEAKKAMLTVQDTYFDIFENTGMENKIGSRNSNFKAQLEGYFTRLVSLMKAGAEKEKLQEQATGLSQDLSKAVDMLQGGEQTAWSMFLYSLLIIVREGLEALLIVAAIVAYLVKNDHQDKLPVIRQSVYVALLGSVITAAIFQMIFSNSGASRELLEGFTMIIAVVMLFMMSYWLLSKVEAQNWKRYLEGKLSTALTTGSLVGLWLTSFLAVYREGAETVLFYYALAGDAKSAVDYFYLFGGFFLGVIILAVCYFIMRYTVVKLPLKPFFMFTGSFMYLMAFVFAGKSVLELIEGKLFEPTLISGMTEIPWLGIYPYVETLVPQVVLLVAAVFALIYMKYQSKKSI","1680589","","membrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR004923
Family
Iron permease FTR1
PF03239\"[157-554]TFTR1
noIPR
unintegrated
unintegrated
signalp\"[1-24]?signal-peptide
tmhmm\"[10-30]?\"[381-401]?\"[416-436]?\"[446-466]?\"[481-501]?\"[525-545]?\"[555-575]?\"[609-627]?transmembrane_regions


","No hits to the COGs database.","","Residues 584 to 632 match (7e-07) PD:PD410457 which is described as COMPLETE PROTEOME MEMBRANE B. PROTEINS SUBTILIS INTEGRAL PM0453 SOME ","","","","","","","","","","","","Wed Jan 15 08:29:27 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02434 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 157 to 554 (E-value = 1.2e-71) place AA02434 in the FTR1 family which is described as Iron permease FTR1 family (PF03239)","","","","","","","","1","","","" "AA02436","1680637","1681155","519","ATGAAAAAAACGTTAATCGCTACCGCACTTTTAGCAGGTATGATCACCGCGCCTGCCGCTTTAGGTTTTAAAGAATACCCAATCGGCGAACCTGTCACCATGAACGAAATGGAAATCGCCGCCGTGTATTTGCAACCGGTTGACATGGAACCGCGTGGCATGGGCTTGCCGGCTGCCAAATCCGACATTCACTTAGAAGCCGACATTCACGCCACCAAAGGCAACAAAAACGGTTTCGGTGAAGGCGAATGGATGCCGTATTTAACCATTCAGTATACTTTAGTGAACGCCGATACCGGTGAAAAACAAGAAGGAACATTCATGCCGATGGTTGCCAGCGATGGCCCGCACTACGGCGCAAACATCAAAATGATGGGCGTGGGTAACTATAAATTAACTTACCATATCGACCCGCCGCCAAAAGCCGGTATGCACCGTCACACCGATGAAGAAACCGGCGTCGGTCGTTGGTGGAAACCGTTCGACGTGAACTATGAATTTAAATTCACCGGTTTGAAA","","","19093","MKKTLIATALLAGMITAPAALGFKEYPIGEPVTMNEMEIAAVYLQPVDMEPRGMGLPAAKSDIHLEADIHATKGNKNGFGEGEWMPYLTIQYTLVNADTGEKQEGTFMPMVASDGPHYGANIKMMGVGNYKLTYHIDPPPKAGMHRHTDEETGVGRWWKPFDVNYEFKFTGLK","1681153","","periplasmic protein","Periplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide
tmhmm\"[5-23]?transmembrane_regions


","No hits to the COGs database.","","Residues 1 to 172 match (3e-83) PD:PD109199 which is described as PROTEOME COMPLETE ANTIGEN MEMBRANE PERIPLASMIC PATHOGEN-SPECIFIC REGION: P19 FROM UNSTABLE ","","","","","","","","","","","","Wed Mar 17 09:13:31 2004","","","","Wed Mar 17 09:11:47 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02436 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Mar 17 09:11:47 2004","","","","","","","","","","","","","1","","","" "AA02437","1681297","1682724","1428","ATGAACTATTTCTTTGTTTTTCTCATTCAAACCCTACTCCCGATTTCTCTGCTGCTCGGTTGCAGCTGGGTGCGTTACCCACAAACCAATTTCAAGAAACTCATTTGGCTTTCGCTTTTCGGTTTTATTATCGGCAGCCTTATTACGTTAAATTTACCCGCGACACAAAGTGCAAAACTCGCCGTCGCCCTTGTCGCACTCTGTATTTTATTGTTTGCGTATTGCTTTCAATTTATTCATTGGCAAAAACTTAACGGCTTTTGGCATATTATGCTGTCCGTGCTTGCCGGGTATTTATGGGCGAAAGATCCGAATATCGCCGCCATCACCGACACCAACGTGATTAACACGGAATTTTTACTCCACCTCAGCGCCATCATTCTCGGTTTTATTTTCTGCCTGATCGTCGCCGGCTGGCTGTATATTTTATTTCAACAACAAAAAACACCGGAAAAAACAACCGCACTTTCCGTCCTATTAACCACAATTTTCACCCTGCTATTGATTACTCCGCTCATCGGCGACGTACTGCTCATATTAATGAAATTGCAAGTGCTGGAACTGACCAAAGTGCGGTTAAGTTTTGTGGCGAAATCGGGCAATATTTCCGCTTATTTGAATTACATCAACGCCACCGTACTGGCGTTTATCGTGCTTATTTTTGCCGTTAAAACACACTTGCCTCGCATTCGTCAGGTCAATATCGAACAACAACCTATCGCAAAACGCAAAGCCATTGCCGCCAAACGTACTTCCGCCAAAATCATCGGTTACGGTTTAACGGCTGTGGCAATCATTTTGGCATCGCAACTCTATTGGGACAAAATCGCCTCCCAGCCGCCGCAACTTTCGGAAGCACAACGAATCACCTTAGACGCAGAAAACAACGTGCGCATTCCCATCGAACAGGTGAAAGACGGCAAATTACACCGTTTCCTTTGGATTGCCGACGACGGCAAAGCGGTGCGTTTCTTTATCATCAATCGCCTTGCCGAAAAGCTCAGCCTCGCCGTCGTATTCGATGCCTGCATTTTATGCGGCGACCAAGGTTATGTGATGGAAGGCAACCAAGTGGTGTGCGTGGGTTGCGGCGTGCGTTTATTTACGCCGTCCATCGGCAAACCGGGCGGCTGCAATCCGGTGCCGATTGATGATTGGAAGCAAACAGAAACGGAAGTCATCATCAGCAAGAAAAGCTTGGAAGAAGGTTTGAATTATTTCACCACGGTGATTGAAATTGAAGTCGTGGATCCCGTCAACGGCAAAAAACTCACCAACACCAAAACGGAACACAAATACAGCTATGACGGCAAAACCTACTTCTTCAGCGATGAAAAGAACCTGAATCTGTTCCGCGATAATCCGGAAGTGTATCTCAACAAAACCGCTGCGGATTCCACCACGGATTCAATAATGAAAGAGGAAAAA","","","53474","MNYFFVFLIQTLLPISLLLGCSWVRYPQTNFKKLIWLSLFGFIIGSLITLNLPATQSAKLAVALVALCILLFAYCFQFIHWQKLNGFWHIMLSVLAGYLWAKDPNIAAITDTNVINTEFLLHLSAIILGFIFCLIVAGWLYILFQQQKTPEKTTALSVLLTTIFTLLLITPLIGDVLLILMKLQVLELTKVRLSFVAKSGNISAYLNYINATVLAFIVLIFAVKTHLPRIRQVNIEQQPIAKRKAIAAKRTSAKIIGYGLTAVAIILASQLYWDKIASQPPQLSEAQRITLDAENNVRIPIEQVKDGKLHRFLWIADDGKAVRFFIINRLAEKLSLAVVFDACILCGDQGYVMEGNQVVCVGCGVRLFTPSIGKPGGCNPVPIDDWKQTETEVIISKKSLEEGLNYFTTVIEIEVVDPVNGKKLTNTKTEHKYSYDGKTYFFSDEKNLNLFRDNPEVYLNKTAADSTTDSIMKEEK","1682722","","integral membrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR007029
Domain
YHS
PF04945\"[418-462]TYHS
InterPro
IPR013248
Family
Shr3 amino acid permease chaperone
SM00786\"[116-307]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-20]?signal-peptide
tmhmm\"[4-24]?\"[34-54]?\"[60-80]?\"[85-100]?\"[119-141]?\"[156-178]?\"[203-223]?\"[255-273]?transmembrane_regions


","No hits to the COGs database.","","Residues 1 to 460 match (5e-139) PD:PD217006 which is described as COMPLETE PROTEOME MEMBRANE REGION: FROM UNSTABLE INTEGRAL PM0451 KBASES ","","","","","","","","","","","","Wed Jan 15 08:33:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02437 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 418 to 462 (E-value = 6e-14) place AA02437 in the YHS family which is described as YHS domain (PF04945)","","","","","","","","1","","","" "AA02438","1682730","1684052","1323","ATGTTGGCAAGAATGTTATTTCAATCCTGGCGTTATGATTTAAAGCGCAAACTCCTCGCCATTGTGACCATTTTCCTCGCTGCCGGATTAATTTCCGCCTTGCTTGCGGTGTCCATCGACATCGGCGACAAAATGGCGAAAGAGCTTAAATCCTACGGCGCCAATATTCTGGTGGAGCCCGCCAGCAGCGCCATTTTGCCTGATGAAGTGAGCCGTAATAATTCTCTCGCCACGCAAGATTTTTTGGACGAAAAAGAACTGCCGAACATTAAAGACATTTTTTGGCGTAACAATATTGTAGGCTTCGCCCCGTTACTCAGCGCACAAGTCAAAGCCGATGGACCAAACGGCAAGGCGCAAGACATCGACATTCTCGGCACGTTTTTTGATCATCAAATCGCCGTGCCGGATGAAGACGATTACCACACCGGGCAAAAAATCATCAACCCTTATTGGCAGGTGGAAGGCGAATGGGTGAACGATGCCACCGATGATTTCAGCGAACAGGTTCCTGCGTTACTCGGCGCACAACTTGCCAAACAACATCAGTGGAAAATAGGCGACGCCATAATCTTGCGCTATCAACAAGATGAACAGTCTCCGCAACAACAGCTTAAGGTTATCGTAAAAGGCATTGTGAAAACCGGCGGCACGGAAGAACAACAACTGATTCTGCCATTAAGTGCGGTGCAAAATTTACTTGGATTGGAAGGCAAAGTGCAGGCGGTGAAAGTGTCCGCCCTCACCGTACCGGAAAACGATTTATCGCGCAAAGCCCGCGCCAACGTGGACGGCTTGGCGGCGGAAGAATATGACCGCTGGTATTGCACCGCCTATGTTTCCTCCATTTCTCACCAATTGGAAGAAGCCATTTCCGGCGCCATTGTTCGTCCGATTTGGCAAGTCGCCGCCTCCGAAGGTGTAGTCATTGAGAAAATTCAATTATTACTCGCCGTAGTGACCCTCGCCGCGCTCATTGCCGCCGCCATGGGGATCGCCTCTCTCATGACCACCACCATTATCGAACGCAGCAAAGAAATCGGCTTAATGAAAGCCCTCGGCGCTTATCAATGGCAAATCGTGCTGCTGTTTTATTGTGAAGCCATCATCAGCGGTTTAATCGGCGGCATTTTAGGCTGTGCTGCCGGCTGGGGCTTGGCACGCTTTATCGGCGCCACCCTGTTCGGCGCACCGCTCAGCTTCGCGTGGATTGTGGTGCCTTGCGTACTGGTGATTTCCGTATTGATTGCGGTCATCGGTGCGTGGTTCCCGGCACATCGAATTGCCCGTCTTTATCCTATTGAGGTGCTTTATGGCAGACAA","","","48191","MLARMLFQSWRYDLKRKLLAIVTIFLAAGLISALLAVSIDIGDKMAKELKSYGANILVEPASSAILPDEVSRNNSLATQDFLDEKELPNIKDIFWRNNIVGFAPLLSAQVKADGPNGKAQDIDILGTFFDHQIAVPDEDDYHTGQKIINPYWQVEGEWVNDATDDFSEQVPALLGAQLAKQHQWKIGDAIILRYQQDEQSPQQQLKVIVKGIVKTGGTEEQQLILPLSAVQNLLGLEGKVQAVKVSALTVPENDLSRKARANVDGLAAEEYDRWYCTAYVSSISHQLEEAISGAIVRPIWQVAASEGVVIEKIQLLLAVVTLAALIAAAMGIASLMTTTIIERSKEIGLMKALGAYQWQIVLLFYCEAIISGLIGGILGCAAGWGLARFIGATLFGAPLSFAWIVVPCVLVISVLIAVIGAWFPAHRIARLYPIEVLYGRQ","1684050","","membrane protein; possible ABC transporter permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR003838
Domain
Protein of unknown function DUF214, permase predicted
PF02687\"[271-433]TFtsX
noIPR
unintegrated
unintegrated
signalp\"[1-33]?signal-peptide
tmhmm\"[21-41]?\"[315-335]?\"[360-382]?\"[401-423]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.1e-24) to 2/2 blocks of the IPB003838 family, which is described as \"DUF214\". Interpro entry for IP:IPR003838. IPB003838A 332-379 1.4e-19 IPB003838B 424-437 0.0013","Residues 1 to 314 match (9e-14) PD:PD212453 which is described as COMPLETE MEMBRANE PROTEOME INTEGRAL PROTEINS SIMILAR PM0449 MANY ","","","","","","","","","","","","Wed Mar 17 09:06:02 2004","","","Wed Mar 17 09:06:02 2004","Wed Mar 17 09:06:02 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02438 is paralogously related to AA02439 (2e-31), AA02080 (3e-13) and AA01615 (1e-07).","Wed Mar 17 09:06:02 2004","","","","","Residues 271 to 433 (E-value = 3.5e-39) place AA02438 in the FtsX family which is described as Predicted permease (PF02687)","Wed Mar 17 09:06:02 2004","","","","","","","1","","","" "AA02439","1684042","1685178","1137","ATGGCAGACAATAGACCCATCAATATGTTCCGGCGCTTGGTATTACGCGCCTTACGGCTACGTTTGCAACGGGTGTTTATCATCTTTGCCGCGCTCACGGTAGGCGCCAGTATCGTCACCGCCATGGCGGCGGTGTATTTCGACATCAACACCAAAATGAGTCAGGAACTGCGCACCTTCGGCGCTAACTTTTATATCGGCTCAAACAATGGTGGTTTGATTAAAATGGATCAGGTGCAAGAAATCATTAACCTAGCGCCTAAAGGCTTAATTACCGCCGCCAGCCCTTATTTATACGGTGTAACCCGTAGTGATTTGGAAAAAATCGTCATCATGGGCGTGTGGTTTGAAGACATGAAAACCCTCGCGCCCTACTGGCAAATCACCGGCACGCCCACCGGTGTCAACTTTGACGAACGCAACGCCATGATCGGCAAAACCCTCGCCGAACGCTTAAACCTGAAAGTGGGCAGTAAGCTGACCTTAAGCCTGAATTCGGTAGATAAACACCAGTTTACGATTAAAGCCATCGTGGAAGCGGGCGACGCCACCGACAATATGCTCATCGTGAGCCTGGATTTCGCGCAAAACTGGCTGGAAAAAGAAAACTTTGCCACCAATGCCCTGCTTAACGTGAAAAATGATCAGGGGCAAGTGGAACAATTCGCACAGCAACTTCAGCAACAATATCCCGATTTGGATATTCATCCGATCCGCAAAGTCTCCGCCTCCGAAGGGCAAATTCTGGATAAGATTAAAGGCTTGATGGGCTTGATTTCCGTGGTGATTCTGATTTTAGCCACCCTCTGCGTGAACACCACTCTCATCGCCATCGTGGGCGAACGGGCAAAAGAATTCGCGTTGCAAAAAGCCCTCGGCGCGAAAAGCCGGGACATCATCAAACAAATCGGCGAGGAAACCTTAATTATCGCCGTATGCGCGATCATCAGCGGCTTAATTATCGGTTATTTACTGGCGCAAGTACTCGGCTTAACCGTCTTCAAAGCCTACATCGACATGCGCCTGCCGGTGTTGCCGATCACCATCGGATTATCCTTATTAGTGGCGTTTATCGCAGTTATCGTACCGACCCGCCGCGCCTTAGACATTCAAACCGCCAATGTGTTAAAAGGGGAA","","","44287","MADNRPINMFRRLVLRALRLRLQRVFIIFAALTVGASIVTAMAAVYFDINTKMSQELRTFGANFYIGSNNGGLIKMDQVQEIINLAPKGLITAASPYLYGVTRSDLEKIVIMGVWFEDMKTLAPYWQITGTPTGVNFDERNAMIGKTLAERLNLKVGSKLTLSLNSVDKHQFTIKAIVEAGDATDNMLIVSLDFAQNWLEKENFATNALLNVKNDQGQVEQFAQQLQQQYPDLDIHPIRKVSASEGQILDKIKGLMGLISVVILILATLCVNTTLIAIVGERAKEFALQKALGAKSRDIIKQIGEETLIIAVCAIISGLIIGYLLAQVLGLTVFKAYIDMRLPVLPITIGLSLLVAFIAVIVPTRRALDIQTANVLKGE","1685176","","integral membrane protein; possible ABC transporter permease","Inner membrane, Cytoplasm","","
InterPro
IPR003838
Domain
Protein of unknown function DUF214, permase predicted
PF02687\"[205-372]TFtsX
noIPR
unintegrated
unintegrated
signalp\"[1-36]?signal-peptide
tmhmm\"[25-47]?\"[259-279]?\"[308-328]?\"[342-362]?transmembrane_regions


","BeTs to 20 clades of COG0577COG name: ABC-type transport systems, involved in lipoprotein release, permease componentsFunctional Class: RThe phylogenetic pattern of COG0577 is aom----qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 9.1e-14) to 2/2 blocks of the IPB003838 family, which is described as \"DUF214\". Interpro entry for IP:IPR003838. IPB003838A 271-318 4e-12 IPB003838B 363-376 6","Residues 25 to 199 match (3e-07) PD:PD214317 which is described as COMPLETE ABC PROTEOME PERMEASE SIMILAR POSSIBLE EG MEMBRANE SYSTEM PM0450 ","","","","","","","","","","","","Wed Mar 17 08:29:04 2004","","","Wed Mar 17 08:29:04 2004","Wed Mar 17 08:29:04 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02439 is paralogously related to AA02438 (2e-31), AA01615 (2e-07) and AA01618 (2e-04).","Wed Mar 17 08:29:04 2004","","","","","Residues 205 to 372 (E-value = 1.8e-37) place AA02439 in the FtsX family which is described as Predicted permease (PF02687)","Wed Mar 17 08:29:04 2004","","","","","","","1","","","" "AA02440","1685183","1685851","669","ATGGCTAAAACCGTGATTGAAACACAGCATTTATATAAAAGATTCGGGCAAGTGACCGCACTTGAAGACATTAATATTCAAATTGCCGAAGGGGAATTTGTTGCCATCATGGGCGCTTCCGGCTCGGGGAAAACCACCTTAATGAACATTCTCACCGGCTTGGACACCGCCAGCGAAGGCAAAGTGATTTTAGACGGCGTAGATGCGGCGCAACTGGACGAAACGGGCAGGCAACGCTTCCGTGCGGAGAAAATCGGCTTGGTGTTCCAACAATTCCATTTAATTCCCTATTTAACCGCGTTGGAAAACGTGATGTTGGCGCAACATTATCACAGCGTGGTGGATGAAGCCGCCGCCAAAGCGGTGCTGGAACAGGTGGGGTTGGCACATCGAATGGATCACCGCCCTAGCCAACTTTCCGGCGGGGAACAGCAACGGGTGTGTATCGCCCGCGCATTGGTCAATCAACCGCCGGTGATTTTTGCCGACGAACCGACAGGCAACCTCGACGAGAAAAATGAACATTTGGTGCTGGATTTGCTCACCGAGTTAAACCGACAAGGACGCACGATCGTAATGGTGACCCACAACCCCGATTTAGGCAAACTCACCAATCGCATTCTTTATTTACAACACGGCAAACTGTTAAGCGAGGAACAAAATGTGGGC","","","24596","MAKTVIETQHLYKRFGQVTALEDINIQIAEGEFVAIMGASGSGKTTLMNILTGLDTASEGKVILDGVDAAQLDETGRQRFRAEKIGLVFQQFHLIPYLTALENVMLAQHYHSVVDEAAAKAVLEQVGLAHRMDHRPSQLSGGEQQRVCIARALVNQPPVIFADEPTGNLDEKNEHLVLDLLTELNRQGRTIVMVTHNPDLGKLTNRILYLQHGKLLSEEQNVG","1685849","From PF00005: ABC transporterABC transporters for a large family of proteins are responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain ABC_membrane. ","ABC transporter, ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[138-181]TQ9CNI3_PASMU_Q9CNI3;
PF00005\"[31-213]TABC_tran
PS50893\"[6-222]TABC_TRANSPORTER_2
PS00211\"[139-153]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[30-214]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[5-216]Tno description
PTHR19222\"[6-220]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF32\"[6-220]TABC TRANSPORTER


","BeTs to 22 clades of COG1136COG name: ABC-type transport systems, involved in lipoprotein release, ATPase componentsFunctional Class: RThe phylogenetic pattern of COG1136 is aom--z-qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1e-40) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 20-66 7.6e-17 IPB001140B 136-174 8.3e-17 IPB001140C 190-219 0.00033Significant hit ( 3.7e-05) to 1/6 blocks of the PR00988 family, which is described as \"Uridine kinase signature\". Prints database entry for PR:PR00988. PR00988A 31-48 3.8e-05","Residues 184 to 218 match (5e-07) PD:PD000383 which is described as ATP-BINDING PROTEOME COMPLETE ABC TRANSPORTER TRANSPORTER OLIGOPEPTIDE PLASMID BINDING/ATPASE NUCLEOTIDE ","","","","","","","","","","","Wed Jan 15 08:52:13 2003","Wed Jan 15 08:49:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02440 is paralogously related to AA02080 (8e-47), AA01616 (3e-42), AA02718 (2e-33), AA01524 (3e-32), AA01645 (2e-31), AA01422 (4e-31), AA00415 (8e-31), AA00858 (4e-29), AA00700 (2e-26), AA01051 (3e-26), AA01656 (4e-26), AA01867 (5e-26), AA02324 (9e-25), AA00933 (1e-24), AA02353 (3e-24), AA02609 (5e-23), AA02140 (1e-22), AA01961 (2e-22), AA01510 (5e-22), AA01684 (9e-22), AA02805 (1e-21), AA01779 (4e-21), AA02898 (6e-21), AA01509 (2e-20), AA01456 (6e-20), AA00207 (6e-20), AA02320 (7e-19), AA02550 (9e-19), AA02152 (2e-18), AA02606 (3e-18), AA02331 (4e-18), AA01824 (4e-18), AA01820 (8e-18), AA01393 (1e-17), AA02899 (2e-17), AA02786 (7e-17), AA00061 (2e-16), AA00591 (3e-16), AA00751 (1e-15), AA01757 (1e-15), AA02146 (3e-14), AA00799 (2e-13), AA02484 (2e-13), AA01947 (3e-13), AA02573 (2e-12), AA01568 (2e-12), AA01569 (2e-11), AA00934 (4e-11), AA02642 (6e-10), AA02225 (8e-10), AA01555 (4e-09), AA01291 (5e-07), AA02226 (2e-06) and A02145 (3e-06).","","","","","","Residues 31 to 213 (E-value = 1.2e-65) place AA02440 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Higgins CF, Gallagher MP, Mimmack ML, Pearce SR.A family of closely related ATP-binding subunits from prokaryotic and eukaryotic cells.Bioessays 1988 Apr;8(4):111-6PMID: 3288195Higgins CF, Hiles ID, Salmond GP, Gill DR, Downie JA, Evans IJ, Holland IB, Gray L, Buckel SD, Bell AW, et al.A family of related ATP-binding subunits coupled to many distinct biological processes in bacteria.Nature 1986 Oct 2-8;323(6087):448-50PMID: 3762694","","Wed Jan 15 08:52:13 2003","1","","","" "AA02442","1685844","1686332","489","ATGTGGGCTAACGTCATTCGCTTTCTCGCCATAAGTGCGGTCATTTTTCTCAGCGTTTCTTGCAAGGAAGAAAACGCGCAGCTCGGACAACCTGCGCCGGAAATTGCCGCCTTCGATTTACAAGGCAACAAAGCCACGTTAAGCGACTGGCAAGACAAAACCGTGCTTATCAATTTCTGGTCGGAAACCTGCGGTGCCTGCATTGTGGAACTGCAAACCCTGCAACAATGGGCGGAAAAATACCCGAACCGCGTCCAACTGGTCACCATGAACATCGACGGCGAAAATGCCGACACCCAAGCCGTCGTCACCAAACGTCAATTAAATTTGCCCGTGTTTAAAGATCAAATGAAAATCACCGCCGAACGCTACCAACTCATCGGCACCCCAACCTCATTTGTCATCGACCCGAACGGCAAACTATTACGCAAATTTGAAGGGTTACTTTCCGAAAACGATTTACAACAATTATTCAACCCGACGAAAAGC","","","18348","MWANVIRFLAISAVIFLSVSCKEENAQLGQPAPEIAAFDLQGNKATLSDWQDKTVLINFWSETCGACIVELQTLQQWAEKYPNRVQLVTMNIDGENADTQAVVTKRQLNLPVFKDQMKITAERYQLIGTPTSFVIDPNGKLLRKFEGLLSENDLQQLFNPTKS","1686330","","thioredoxin-family protein","Periplasm, Inner membrane","","
InterPro
IPR011594
Domain
Thioredoxin-like
PD003679\"[75-154]TQ9CNI4_PASMU_Q9CNI4;
InterPro
IPR012335
Domain
Thioredoxin fold
G3DSA:3.40.30.10\"[1-155]Tno description
InterPro
IPR013740
Domain
Redoxin
PF08534\"[27-162]TRedoxin
noIPR
unintegrated
unintegrated
PTHR10681\"[24-141]TPEROXIREDOXIN
PS51257\"[1-21]TPROKAR_LIPOPROTEIN
signalp\"[1-21]?signal-peptide


","BeTs to 19 clades of COG0526COG name: Thiol-disulfide isomerase and thioredoxinsFunctional Class: O,CThe phylogenetic pattern of COG0526 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 9 to 135 match (6e-09) PD:PD303909 which is described as POSSIBLE PROTEOME COMPLETE PERIPLASMIC THIREDOXIN ","","","","","","","","","","","","Wed Jan 15 09:08:47 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02442 is paralogously related to AA00040 (8e-08), AA00054 (3e-07) and AA02915 (1e-04).","","","","","","","","","","","","","","1","","","" "AA02443","1686342","1686650","309","ATGAAAAAACGCGACTTTACTTTCTTTCTCCTCGCTTGCTGCGCCATCACCGCCGCCCAAGCCGAACCCGACATTGCGCACGGACAAAAAGTCTATAACCGCTCCTGTGCCCTTTGCCACGGCAAACAGGCAGAAAAACCGGCAATGGGACAATCCCAAATCATCAACACCTTCACCCAAGACCAAATCATCAACGCTCTGCAAGACCGCAAGAGCGGTAAAATCGAAGGCGCCGGCAACCGCGCCAAATCCACCCTCAGCGAACAGGATATGCAAGATGTGGCAGGCTATGTGGAAACGTTGAAGAAA","8.50","3.28","11305","MKKRDFTFFLLACCAITAAQAEPDIAHGQKVYNRSCALCHGKQAEKPAMGQSQIINTFTQDQIINALQDRKSGKIEGAGNRAKSTLSEQDMQDVAGYVETLKK","","","cytochrome C related protein","Periplasm","Matches in gapped BLAST to cytochrome precursors, for example see gi 15602311 from P.multocida.AA1594 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus ducreyi gene.AA1594 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus influenzae Rd gene.","
InterPro
IPR003088
Domain
Cytochrome c, class I
PF00034\"[25-102]TCytochrom_C
InterPro
IPR008169
Domain
Bacterial cytochrome c, class IC
PD004020\"[24-98]TC554_THINE_P25938;
InterPro
IPR009056
Domain
Cytochrome c, monohaem
PS51007\"[23-102]TCYTC
InterPro
IPR012282
Domain
Cytochrome c region
G3DSA:1.10.760.10\"[27-101]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide


","No hits to the COGs database.","Significant hit ( 4.1e-06) to 2/2 blocks of the PR00605 family, which is described as \"Class IC cytochrome C signature\". Prints database entry for PR:PR00605. PR00605A 34-45 0.22 PR00605B 76-98 0.0095","Residues 16 to 102 match (1e-16) PD:PD472387 which is described as CYTOCHROME PROTEOME COMPLETE PERIPLASMIC C-553 HEME ELECTRON C C553 SIGNAL ","Sat Feb 28 10:25:52 2004","Sat Feb 28 17:22:34 2004","Sat Feb 28 17:22:34 2004","Sat Feb 28 17:22:34 2004","Sat Feb 28 10:25:52 2004","Sat Feb 28 10:25:52 2004","Sat Feb 28 10:25:52 2004","Sat Feb 28 10:25:52 2004","Sat Feb 28 10:25:52 2004","Sat Feb 28 10:25:52 2004","Sat Feb 28 10:25:52 2004","Sat Feb 28 10:25:52 2004","Sat Feb 28 17:22:34 2004","Sat Feb 28 10:25:52 2004","Sat Feb 28 10:25:52 2004","Sat Feb 28 10:25:52 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02443 has no significant similarity (blastp p-value < 1e-03) to any other gene in this genome.AA02443 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sat Feb 28 10:25:52 2004","Sat Feb 28 17:22:34 2004","pdb1C6S1C6S THE SOLUTION STRUCTURE OF CYTOCHROME C6 FROM 40.2 1e-04pdb1C531C53 CYTOCHROME C553 98.8 2e-22pdb1C6S1C6S THE SOLUTION STRUCTURE OF CYTOCHROME C6 FROM 85.2 3e-18pdb1ETP1ETP-A CRYSTAL STRUCTURE OF CYTOCHROME C4 FROM 81.3 4e-17pdb2DVH2DVH THE Y64A MUTANT OF CYTOCHROME C553 FROM 81.3 4e-17pdb1DVH1DVH CYTOCHROME C553 (REDUCED) (NMR, 36 STRUCTURES) 81.3 4e-17pdb1CYJ1CYJ CYTOCHROME C6 61.4 4e-11pdb1GDV1GDV-A CRYSTAL STRUCTURE OF CYTOCHROME C6 FROM RED 58.3 4e-10pdb1A2S1A2S THE SOLUTION NMR STRUCTURE OF OXIDIZED 50.5 8e-08pdb1KIB1KIB-A CYTOCHROME C6 FROM ARTHROSPIRA MAXIMA: AN 50.1 1e-07","","","Residues 26 to 102 (E-value = 7.8e-06) place AA02443 in the Cytochrom_C family which is described as Cytochrome c (PF00034)","Sat Feb 28 10:25:52 2004","","","","","","","1","Sat Feb 28 10:25:52 2004","","" "AA02444","1686695","1686315","381","TTGTTCTCAAAAAACATTTCCAAAACCGACCGCACTTTTCCATTATTTCTTCAACGTTTCCACATAGCCTGCCACATCTTGCATATCCTGTTCGCTGAGGGTGGATTTGGCGCGGTTGCCGGCGCCTTCGATTTTACCGCTCTTGCGGTCTTGCAGAGCGTTGATGATTTGGTCTTGGGTGAAGGTGTTGATGATTTGGGATTGTCCCATTGCCGGTTTTTCTGCCTGTTTGCCGTGGCAAAGGGCACAGGAGCGGTTATAGACTTTTTGTCCGTGCGCAATGTCGGGTTCGGCTTGGGCGGCGGTGATGGCGCAGCAAGCGAGGAGAAAGAAAGTAAAGTCGCGTTTTTTCATGGTTGGTTAGCTTTTCGTCGGGTTGAA","","","13668","LFSKNISKTDRTFPLFLQRFHIACHILHILFAEGGFGAVAGAFDFTALAVLQSVDDLVLGEGVDDLGLSHCRFFCLFAVAKGTGAVIDFLSVRNVGFGLGGGDGAASEEKESKVAFFHGWLAFRRVE","1686313","","hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
tmhmm\"[21-43]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Jan 15 09:21:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02444 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02446","1686981","1687643","663","ATGCTACAAGCGATCATCTTTGATATGGACGGCGTCATTGTCGATACCGAATTTTTAGAATACGACTTACAGGCGCAATTCATTGAAGCCATTAAGGAACACGACCGCACGTTAACCCCGCTCGAACGTTCGGAAGTGATAGGCAAAGGACTGGCGGAAATCCCCGAAATCGTGAAAAAATTAAGCGGTTCCTCGCTCTCTTTGGAAGAAATCAGGCAGCGCTATTTTGATTTCTTCAAACAGCTTTTTGCCACCGTGGATTACCGTTCAATTTTCCGAGCCGACATTCAGCAAATCATCGATTTCGCCAAGCAAAACAGTATCAAATTGGCGGTCGCCTCCTCTTCTCACCTCGACCATATTCAAAACATCCTGACCGAATGCGGCATCATTCAGCACTTTGACTTTATCGTCAGCGGCGAACAATTTAAACGCAGCAAACCGGGTCCGACAATTTACCGTTACACCCTCGAAAAATTAGGCGTACAAGCCCAAAACGCCGTAGCGATTGAAGATTCTTTTTTCGGCATTCAAGCCGCTAAAACCGCCGGCATTCCCGTCATCGCCTACGAAGAAAAACGCATGCTCATCGACCAATCCGAAGCCGATTATTGCGGTAAAGACATGAAAGAAATCTTGCGCGTTATTCAACAGTTGCATCAT","","","25219","MLQAIIFDMDGVIVDTEFLEYDLQAQFIEAIKEHDRTLTPLERSEVIGKGLAEIPEIVKKLSGSSLSLEEIRQRYFDFFKQLFATVDYRSIFRADIQQIIDFAKQNSIKLAVASSSHLDHIQNILTECGIIQHFDFIVSGEQFKRSKPGPTIYRYTLEKLGVQAQNAVAIEDSFFGIQAAKTAGIPVIAYEEKRMLIDQSEADYCGKDMKEILRVIQQLHH","1687641","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR005833
Family
Haloacid dehydrogenase/epoxide hydrolase
PR00413\"[2-13]T\"[103-116]T\"[134-150]T\"[152-172]T\"[179-192]THADHALOGNASE
InterPro
IPR005834
Domain
Haloacid dehalogenase-like hydrolase
PF00702\"[2-193]THydrolase
InterPro
IPR006402
Domain
HAD-superfamily hydrolase, subfamily IA, variant 3
TIGR01509\"[4-190]THAD-SF-IA-v3: HAD-superfamily hydrolase, su
InterPro
IPR006439
Family
HAD-superfamily hydrolase, subfamily IA, variant 1
TIGR01549\"[4-184]THAD-SF-IA-v1: HAD-superfamily hydrolase, su
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1000\"[70-211]Tno description
PTHR18901\"[2-216]T2-DEOXYGLUCOSE-6-PHOSPHATE PHOSPHATASE 2


","BeTs to 9 clades of COG0637COG name: Predicted phosphatase/phosphohexomutaseFunctional Class: RThe phylogenetic pattern of COG0637 is ----k-y-vdrlbcefghsn-j-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.5e-07) to 3/7 blocks of the PR00413 family, which is described as \"Haloacid dehalogenase/epoxide hydrolase family signature\". Prints database entry for PR:PR00413. PR00413A 2-13 0.019 PR00413E 134-150 0.04 PR00413F 152-172 57","Residues 99 to 203 match (3e-15) PD:PD000816 which is described as COMPLETE PROTEOME HYDROLASE PHOSPHATASE PHOSPHOGLYCOLATE FAMILY HALOACID DEHALOGENASE-LIKE HYDROLASE PGP ","","","","","","","","","","","","Wed Jan 15 09:29:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02446 is paralogously related to AA01421 (3e-10), AA00521 (2e-06) and AA01159 (7e-06).","","","","","","Residues 2 to 193 (E-value = 4.2e-22) place AA02446 in the Hydrolase family which is described as haloacid dehalogenase-like hydrolase (PF00702)","","","","","","","","1","","","" "AA02449","1687715","1687888","174","ATGACCGCACTTTTTGATGATTATGCCGAGATACGATTTATTGATAGCGCACGCTTCCCAGCGTGTGCTTGTAACCTGTTGATATTTCAGGCACACGTTAGGAAACCACAGCTGTTCGAAACCTTAACTTGGAACCCAAAGACGGTCAACACCGCTTGGGTCTCCGCCACAAAT","","","6631","MTALFDDYAEIRFIDSARFPACACNLLIFQAHVRKPQLFETLTWNPKTVNTAWVSATN","1687888","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 10:02:21 2004","Wed Feb 25 10:02:21 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02449 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 10:02:21 2004","","","","","","","","","","","","","1","","","" "AA02450","1688284","1687841","444","ATGGTTATACAATCGGATTATAATGTCAGATTATTTAATAAGGAAAATAAAGAAACCCGACATATTTTTCGATTAATTATCGCGAGATTAAAAGAGAAGGATGAAGAGATTTACTTTCTGGCAAACCATGCGGATTATTCGGCAACGGAAATAGCTGAGTTATATAAGAGACGTTGGGAAATCGAAGTTTTTTTCAAATTTATTAAGCAACATTTAGACTTCAGCCATTTACTTTCACGTAATGAAAATGGCATGAAAGTGGAAATGTATATGACGTTAATTACGGCGATTTTATTAATTGTTTATAAGAAAGAGAACGGTTTATCCGGTTATAAGATGGCGAAGTTAAAATTAGCCATTGAAATTGAAAGTCTTTTAATTAAAGAGATAGTTTTAATTTGTGGCGGAGACCCAAGCGGTGTTGACCGTCTTTGGGTTCCAAGT","","","17428","MVIQSDYNVRLFNKENKETRHIFRLIIARLKEKDEEIYFLANHADYSATEIAELYKRRWEIEVFFKFIKQHLDFSHLLSRNENGMKVEMYMTLITAILLIVYKKENGLSGYKMAKLKLAIEIESLLIKEIVLICGGDPSGVDRLWVPS","1687839","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR002559
Domain
Transposase, IS4-like
PF01609\"[21-98]TTransposase_11


","BeTs to 5 clades of COG3385COG name: Predicted transposaseFunctional Class: LThe phylogenetic pattern of COG3385 is -o-p-----d--bce-----------Number of proteins in this genome belonging to this COG is","Significant hit ( 1.8e-13) to 1/1 blocks of the IPB002559 family, which is described as \"Transposase IS4 family\". Interpro entry for IP:IPR002559. IPB002559 51-72 1.8e-13","","","","","","","","","","","","","Wed Jan 15 09:33:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02450 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02451","1688986","1688297","690","ATGAAACTCAGAGAAATCTTAGGCTATATTCCGAAAGAACAGTTAAGAATGTTTGCATTGGAATATCAAGTTGACCGTCAAGTGAAAAAATTAAGCGGTGAAGTGATGTTTTATTTACTGCTATTTTCATCATTAAATGTACGACATAACAGCTTAAGAACATTAGAGCAATTTTACAGTTCTCCGACCTTTACCGGATTATTTGATAAACCGATAAAGCATGCAAAATATAATTCGATTAGCGACCGATTAAGAACCATTAATGCAGATTATTTTAAAGCCATTTTCGAGTCGGTATTAAGTCGATATAGTGACAGTTATTTAAAACCGAGAGATAACATTATCGCTTTTGATTCCACAATCGTGACGCTTTCAAGTAAGTTATTAAAAACGGGAATGAAAGTGGGGAGTTATCAGGGTGTAAACGGAATCAAGTTCAGTGTGGCGTTTTCGAGCGTACCGGTAAAATCAAAACTGTTTACGCAACGGGTTTATTCCTCGGAAGATGTTGCGCTCAAAGAGCTGATTGTAGAATATCCGTTGAGCCGGGATAATATCTTATTGTTTGATATGGGAATTCAGTCAAGAAATACGTTTGATGAATTTAGCGATAAACATTTTACCTTTGTGACCCGGGTTCGTGAGATAGCGCGTTATCGGGTCATGAGTGAAAATCCGGTAGAAATTCGG","","","26758","MKLREILGYIPKEQLRMFALEYQVDRQVKKLSGEVMFYLLLFSSLNVRHNSLRTLEQFYSSPTFTGLFDKPIKHAKYNSISDRLRTINADYFKAIFESVLSRYSDSYLKPRDNIIAFDSTIVTLSSKLLKTGMKVGSYQGVNGIKFSVAFSSVPVKSKLFTQRVYSSEDVALKELIVEYPLSRDNILLFDMGIQSRNTFDEFSDKHFTFVTRVREIARYRVMSENPVEIR","1688295","","conserved hypothetical protein","Outer membrane, Cytoplasm","","No hits reported.","No hits to the COGs database.","","Residues 27 to 113 match (3e-07) PD:PD070482 which is described as ROX1-SPE3 ","","","","","","","","","","","","Wed Jan 15 09:38:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02451 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02453","1690394","1689087","1308","ATGGATATTAACAATAGAGAATTAGCAACTGCAATATGGATGGTGATCTTATTTACATATTTATTTTATTTTCATAAGAATATTAGAGATGGTTTTTATAATGTAATAGATTGCTTTTTCAATAAAAAGATTTTATTTGTAATAGCCCTAGCTGCTATATGGATGAGTATTGGTGTATTTATTTTATATGAAGTGGGAGTCTGGAAAGAGAATAATATAAAAACGACTTTAGTATGGTTTTCAACCTCAATAATCACAATGGTTATTGGTGTTAGTAAAGTTGAGGACAAAAAGGATTATTTCTTATCATTGTTAAAAGAAAATATTAATGTTGGTGTATTCTTGATATTTGTTCTTGAACTTTATTCTTTTTCTTTTTTAATAGAGTTTATTATGATACCTTTTTCAACGTTTTTATTTTTATATATCAAATGCAATTCATTAAATGAAAACAATAAAAAGATAAGTTGTTTTATTTATATAATACTCAGTTTATGGATTGTGATATATTTTTTACATTCAATATATTTATCTGTTTTGTTATTTGATGCAAATTCTTTATGGGGCAACATTCTAGAGTTGTTTTTGCCATCTATCCTTTCTTTAATATGTATTCCTTTTTTGTATTTTTTATCTATATATATGGAGTATGAACGAGTATTTGCATCTTTGAAAATATATTTTAATGATAATGGTTTATTTGAGTATGCCAAAAAGTTAAGTTTAAAATATTTTAAGTTTAATGTTGATTATTTAAGACGATGGAATAGAAATATTAGAATCTACCAAATAAGAGATAAAGAAGATTTAGAAAGAAGTGTATGTAACATAAAGAAATTAAAAGGTGTAGAATCTAATCCTCCTTTTGTTCCTTCAAAGAAAGGCTGGTCTCCATATTTGGCTAGAAATTTTCTTAAAAATGACAAAATTATAATGACTGACTATCACCCTGGCTATGATAATAGATGGTGGGCGTATAGTAGGCCATTACTAATAGATCAAGAAAATTCATTTTCAGATATGATTACATATTATATATATGGAGATGAAAAAATTGTTGGTAATTTAAAATTAAAAGTTTATATTAATAATGTATCCATATCGGAATCTACAAAAGAAGTTATCTTAAAGGTATTTAGTGGTTTATTGCTTAATTCAATAAAGTGTGATTCTATTAAAATAAATAATTGGTTGAAAAAAACTCCTTTTTCGATGGAGAAAGATAATTATATTATAAGTTTTACTAAGGAGAATTTTACAAATAATAGAGGCTATACTTTGGAATTGAATATATCAATTAAATTAGAA","","","51729","MDINNRELATAIWMVILFTYLFYFHKNIRDGFYNVIDCFFNKKILFVIALAAIWMSIGVFILYEVGVWKENNIKTTLVWFSTSIITMVIGVSKVEDKKDYFLSLLKENINVGVFLIFVLELYSFSFLIEFIMIPFSTFLFLYIKCNSLNENNKKISCFIYIILSLWIVIYFLHSIYLSVLLFDANSLWGNILELFLPSILSLICIPFLYFLSIYMEYERVFASLKIYFNDNGLFEYAKKLSLKYFKFNVDYLRRWNRNIRIYQIRDKEDLERSVCNIKKLKGVESNPPFVPSKKGWSPYLARNFLKNDKIIMTDYHPGYDNRWWAYSRPLLIDQENSFSDMITYYIYGDEKIVGNLKLKVYINNVSISESTKEVILKVFSGLLLNSIKCDSIKINNWLKKTPFSMEKDNYIISFTKENFTNNRGYTLELNISIKLE","1689085","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide
tmhmm\"[10-24]?\"[45-63]?\"[77-92]?\"[102-117]?\"[123-143]?\"[158-180]?\"[194-214]?transmembrane_regions


","No hits to the COGs database.","","Residues 15 to 434 match (3e-77) PD:PD574099 which is described as INNER PROTEOME COMPLETE MEMBRANE ","","","","","","","","","","","","Wed Jan 15 09:40:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02453 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02454","1694493","1690447","4047","ATGAATAAAAGAACGATAAAACAAGAACTTAATCCTTTACAACAATCCCTTTTCACACAACTGAATGACGTCATGCTTTCGGATAAACGCCGTTTATCCGAAAGCATTCACGGCATTGGCAAAATAAAAAGCACTGATGCGCAACAGGCGGTGATAGCGGAGATTGAACAGCAAATTCACCTCGCCAAATTGCGCGTAGAACAACGCAAAAGTGCGGTCAAAAATTTGATTGTTTTTCCGGAAAGTCTGCCTGTTAGCCAACGCAAAGCGGAAATCGAAAAATTATTGTCCGAACATCAAGTGATTGTGGTGGCGGGGGAAACCGGTTCAGGCAAAACCACTCAGTTGCCGAAAATGTGCCTGGAGTTGGGGTTAGGCAATCTTGGCATGATTGGGCATACTCAACCACGCCGTATTGCCGCCCGCTCCGTCGCCGCGCGTATTGCGGAAGAATTGCAAACGGAACTGGGCGATTTGGTCGGTTACAAAGTGCGTTTTAACGACCAAATCAGCGACAACACCCAAATCAAGTTAATGACTGACGGGATTTTGCTGGCGGAAATTCAAACGGATCGTTTTCTCAACCAATATGCCTGCCTGATTATCGACGAAGCCCACGAACGCAGTCTGAATAACGATTTTATTCTCGGCTATTTGAAACAGCTCCTGCCGCGTCGCCCTGATCTTAAATTGATTATCACGTCCGCAACCATTGATGTGGAGCGTTTTTCCAAGCATTTCGATAATGCGCCGATTATTGAAGTCTCCGGCAGAACTTATCCTGTGGAAGTGCGTTATCGTCCTATTGCGGAAGAAGACGATCAAGACCAGCTACAAGGCATTTTAAATGCGGTGGACGAGCTACAAGCGGAAGGGCGCGGTGATATTTTGATTTTTATGAACGGCGAACGGGAAATCCGCGACACCGCTGAAGCCCTGCAAAAGCAAAATTTAAAACACACGGAAATCCTACCGCTCTTTGCGCGCCTTTCTGCGCAAGAACAAAACAAAATTTTCCACCCGAGCGGACTTAATCGCATCGTGCTTGCCACCAACGTGGCGGAAACTTCCCTCACCGTGCCGGGCATTAAATACGTCATCGACCCCGGCACTGCGCGCATTTCCCGTTACAGTTACCGCACCAAAGTGCAACGTCTTCCCATTGAACCCATTTCACAAGCCTCCGCCAATCAGCGTAAAGGGCGTTGCGGGCGTGTGAGCGAAGGCATTTGTATTCGTCTTTATTCGGAAGACGATTTCAACAATCGCCCGGAATTTACCGATCCGGAAATCCTGCGAACCAATTTGGCGTCGGTGATTTTGCAAATGACGGTGTTGGGTTTGGATGATATTGAAGCCTTCCCGTTCGTGGATGCACCGGATAAACGGCATATTCAGGATGGCGTGAAATTGTTGGAAGAATTGGGGGCGTTGGAATGGAAGGCTATTCGCAAATCTCCCCCCTCCGCCTTCGGTACTTCCCCCCGTAAACAGGGGGAGGGAAAGGGTATTTTATCAGAAGAAGGATCTTCGCTCCCTCCGTTTACAGGGGGATCTGCCCGTAGGGCTGAGGGGGGGAATACTCCAACTTTCAAAGAAAAACGTGTTCTCACACACCTCGGTCGCCAACTCGCCCAGCTCCCAGTCGATCCATGCTTGGCAAAAATGCTACTAAGTGCGGTCAATTTTTGCAGCGTTTATGAAGTAATGATCATCGTTTCGGCGTTATCCATTCAGGATCTGCGCGAACGTCCGACGGAAAAACAACAGGCAGCGGACGAAAAACATCGTCGTTTTGCCGATAAAAAATCGGATTTCTTGGCGTTCTTGAACCTGTGGAATTATCTGCAAGAACAACAAAAAGCGCTGAGCAAAAACCAATTCCGTCGCCAATGTCAAAAAGATTTCCTCAATTACCTGCGCATTCGCGAATGGCAGGATATTTATCAGCAAATTCGTCTGGCGGTGCGTGAAATGGGCTTGCCGATTAATTCCGAAAAAGCCGAATATCAGCAAATTCATACCGCACTTTTAAGTGGCTTGTTGTCCCATATCGGGCTGAAAGAAGCGGAAAAACAACAATATCTCGGCGCGCGCAACGCCCATTTCGCCATTTTCCCCAATTCCGTGCTTTTCAAAAAACAACCGAAATGGGTAATGGCGGCGGAGCTGGTGGAAACTTCCAAACTTTGGGGGCGCATGGTAGCGGAAATTGAGCCGGAATGGATTGAGCCTTTGGCTGAACATCTGGTGAAAAAATCCTATTCCGAACCGCGTTGGTCGAAATCTCGCGGGGCGGTGATTGCCGATGAGAAAGTGAGCTTGTACGGCGTGCCGATTGTGGCGGGGCGCCCTGTGAATTACGGCGCTATCGATCCTGTGGTGAGCCGTGAGATCTTTATTCAATCGGCGTTGGTAGAAGGCGATTGGAATACGAAGCACCCATTCTTCAAGCAAAATCAACAGCTGATTCGTGAAGTGGAAGAACTGGAACACAAAAGCCGCCGTCGTGATATTTTGGTGGATGAGCGCACGTTGTTTGAATTTTACGACCAACGCATCGGCACAGACGTGGTGTCTCAAAAGCATTTTGATACCTGGTGGAAAAAAGCCTCAAAACAGGATCCGGAACTGCTGAATTTCGAGCGTTCCTTCCTGATTAATGATGACGTGGAACAGGTCAGCAAGCTGGATTTCCCGAATTTCTGGCATCAAGGTAATTTAAAACTCAAGCTCACGTATCAATTTGAACCGGGCACCGACGCAGATGGCGTGACGGTGCATATTCCGTTGCCGTTGCTCAATCAGGTGGAAATGACGGGCTTTGACTGGCAAATTCCGGGCTTGCGTGAAGAACTGGTGATTGCGCTGATTAAATCTTTGTCGAAATCCTACCGTCGTAATTTTGTGCCCGCGCCGAATTACGCTCAAGCCTTTTTAGGGCGAGCCGTACCATTGGAAAAACCGCTGTTAGATACGCTGATTTATGAATTGCGCCGTATGACGGGTGTGACCGTGGAAGCGGAACATTGGAACTGGGCACAAATTCCAAGCCATTTGAAAATGACCTTCCGCGTGGTGGATGAAAAAGGCAAGAAAATTGCCGAATCGATGGATTTGGACGCGCTGAAATTTGAGCTGAAAGACCGTGTGCAGGAAAGCATTTCTGCGGTGGCAGACGACGGCATTGAACAAAGCGGTGCGCACATTTGGAATTTCGCCGACCTGCCGCAATTTTATGAGCAGAAAAAACAGGGTTTCAGCGTCAAAGCCTTCCCGGCAATCGTCGATGAAAAAGATGCCGTGGGTGTGAAACTCTTTGAAACGGAATTTGAGCAAGCGGTGGCAATGCAACAAGGTCTGCGTCGATTATTACTGCTCAACGTGCCGTCGCCGATTAAATACCTGCACGAAAAATTGCCGAATAAATCCAAACTCGGGCTTTATTTCACGCCGTTTGGTCGCGTAATGGATTTGATTGACGATTGCATCGCCTGCGCCGTGGATAAACTTATTGCGGATTTCGGCGGTTTTGTGTGGAACGAAGAAGGCTTTGAAAAACTGCGCGATTTTGTGCGGGAAAACCTCAATGATGTCACCGTGGATATTGCACAAAAAGTAGAGCAAATCCTCACGCTCACCCATCAATTAAACCAACGGCTGAAAGGCAAAATGGATTTCACCATGGCGTTTGCCTTATCGGACATTAAGTCTCAATTAAGCGGCTTGGTGTATCAAGGTTTTGTGCAAAAGAGCGGTTACCATCGCCTACCGGATTTACTGCGTTATTTACAAGCCATTGATAAACGCATCGACAAACTTTCGCAAGATGTGAATCGCGATCGTGCGGCAATGTTACGCGTGGAACAGGTTCAACAGGCTTATCAACAGTTGCTCGCCAAACTCCCGAAATCTAAACCGATTTCTGATGAAGTGGCAGAGATTCGGTACATGATCGAAGAATTGCGTGTGAGTTTATTTGCACAGCAGTTGGGGACGAAGTATCAGGTTTCGGAGAAGAGGGTTTTGAATACGATTGGAACATTC","","","153910","MNKRTIKQELNPLQQSLFTQLNDVMLSDKRRLSESIHGIGKIKSTDAQQAVIAEIEQQIHLAKLRVEQRKSAVKNLIVFPESLPVSQRKAEIEKLLSEHQVIVVAGETGSGKTTQLPKMCLELGLGNLGMIGHTQPRRIAARSVAARIAEELQTELGDLVGYKVRFNDQISDNTQIKLMTDGILLAEIQTDRFLNQYACLIIDEAHERSLNNDFILGYLKQLLPRRPDLKLIITSATIDVERFSKHFDNAPIIEVSGRTYPVEVRYRPIAEEDDQDQLQGILNAVDELQAEGRGDILIFMNGEREIRDTAEALQKQNLKHTEILPLFARLSAQEQNKIFHPSGLNRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFNNRPEFTDPEILRTNLASVILQMTVLGLDDIEAFPFVDAPDKRHIQDGVKLLEELGALEWKAIRKSPPSAFGTSPRKQGEGKGILSEEGSSLPPFTGGSARRAEGGNTPTFKEKRVLTHLGRQLAQLPVDPCLAKMLLSAVNFCSVYEVMIIVSALSIQDLRERPTEKQQAADEKHRRFADKKSDFLAFLNLWNYLQEQQKALSKNQFRRQCQKDFLNYLRIREWQDIYQQIRLAVREMGLPINSEKAEYQQIHTALLSGLLSHIGLKEAEKQQYLGARNAHFAIFPNSVLFKKQPKWVMAAELVETSKLWGRMVAEIEPEWIEPLAEHLVKKSYSEPRWSKSRGAVIADEKVSLYGVPIVAGRPVNYGAIDPVVSREIFIQSALVEGDWNTKHPFFKQNQQLIREVEELEHKSRRRDILVDERTLFEFYDQRIGTDVVSQKHFDTWWKKASKQDPELLNFERSFLINDDVEQVSKLDFPNFWHQGNLKLKLTYQFEPGTDADGVTVHIPLPLLNQVEMTGFDWQIPGLREELVIALIKSLSKSYRRNFVPAPNYAQAFLGRAVPLEKPLLDTLIYELRRMTGVTVEAEHWNWAQIPSHLKMTFRVVDEKGKKIAESMDLDALKFELKDRVQESISAVADDGIEQSGAHIWNFADLPQFYEQKKQGFSVKAFPAIVDEKDAVGVKLFETEFEQAVAMQQGLRRLLLLNVPSPIKYLHEKLPNKSKLGLYFTPFGRVMDLIDDCIACAVDKLIADFGGFVWNEEGFEKLRDFVRENLNDVTVDIAQKVEQILTLTHQLNQRLKGKMDFTMAFALSDIKSQLSGLVYQGFVQKSGYHRLPDLLRYLQAIDKRIDKLSQDVNRDRAAMLRVEQVQQAYQQLLAKLPKSKPISDEVAEIRYMIEELRVSLFAQQLGTKYQVSEKRVLNTIGTF","1690445","","ATP-dependent helicase","Cytoplasm, Inner membrane","","
InterPro
IPR001650
Domain
Helicase, C-terminal
PF00271\"[315-407]THelicase_C
SM00490\"[307-407]THELICc
PS51194\"[280-447]THELICASE_CTER
InterPro
IPR002464
Family
ATP-dependent helicase, DEAH-box
PS00690\"[198-207]TDEAH_ATP_HELICASE
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[98-387]TAAA
InterPro
IPR007502
Domain
Helicase-associated region
PF04408\"[467-610]THA2
InterPro
IPR010222
Family
ATP-dependent helicase HrpA
TIGR01967\"[17-1348]TDEAH_box_HrpA: ATP-dependent helicase HrpA
InterPro
IPR011709
Domain
Domain of unknown function DUF1605
PF07717\"[650-750]TDUF1605
InterPro
IPR013173
Domain
DNA primase DnaG, DnaB-binding
SM00766\"[1117-1299]Tno description
InterPro
IPR014001
Domain
DEAD-like helicases, N-terminal
SM00487\"[40-265]TDEXDc
InterPro
IPR014021
Domain
Helicase superfamily 1 and 2 ATP-binding
PS51192\"[93-256]THELICASE_ATP_BIND_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[257-419]Tno description
PTHR18934\"[50-477]T\"[531-752]TATP-DEPENDENT RNA HELICASE


","No hits to the COGs database.","Significant hit ( 8e-15) to 2/3 blocks of the IPB002464 family, which is described as \"ATP-dependent helicase, DEAH-box\". Interpro entry for IP:IPR002464. IPB002464A 106-120 1.6e-05 IPB002464B 196-209 1.3e-07Significant hit ( 2.4e-05) to 1/5 blocks of the IPB001482 family, which is described as \"Bacterial type II secretion system protein E\". Interpro entry for IP:IPR001482. IPB001482B 98-120 2.4e-05","Residues 25 to 81 match (8e-07) PD:PD076023 which is described as HELICASE ATP-DEPENDENT PROTEOME COMPLETE HRPA ATP-BINDING HELICASE HOMOLOG ","","","","","","","","","","","","Wed Jan 15 09:44:25 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02454 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 467 to 611 (E-value = 7.2e-31) place AA02454 in the HA2 family which is described as Helicase associated domain (HA2) (PF04408)","","","","","Moriya,H., Kasai,H. and Isono,K.Cloning and characterization of the hrpA gene in the terC region of Escherichia coli that is highly similar to the DEAH family RNAhelicase genes of Saccharomyces cerevisiaeNucleic Acids Res. 23 (4), 595-598 (1995)PubMed: 7899078","","Wed Jan 15 09:44:25 2003","1","","","" "AA02455","1694879","1694493","387","ATGAAAAACAAATGGTTATTGATTGCCGCCGTGAGCGGTTTTTTATGTGTGACTATCGGTGCGTTTGCGGCGCACGGTTTAAGCCAAGTGTTGGACGCGAAAGCCTTAGCGTGGATTGACACCGGCGTGAAATATCAAATGTTCCACACCCTCGCCATCATGGGAATCGGCATCGCACAATTATGTCGCGAACCATTTGCCGCCAACAAAAGCGCCAATGTTGCCGCCGGCGCGTGGTCATTCGGAATCCTTCTCTTTAGCGGCAGTTTATACGCCCTCGCACTTGGCTCAGGTAAATTTATGGTTTGGCTCACGCCCATCGGCGGCACGCTATTTTTAATCGGCTGGCTTGGTTTAGCTTACGGCGCTTTCAAAAGTAAATCAGAA","","","13617","MKNKWLLIAAVSGFLCVTIGAFAAHGLSQVLDAKALAWIDTGVKYQMFHTLAIMGIGIAQLCREPFAANKSANVAAGAWSFGILLFSGSLYALALGSGKFMVWLTPIGGTLFLIGWLGLAYGAFKSKSE","1694491","","conserved hypothetical protein","Inner membrane, Extracellular","","
InterPro
IPR006696
Family
Protein of unknown function DUF423
PF04241\"[5-121]TDUF423
noIPR
unintegrated
unintegrated
PTHR10584\"[82-111]TSUGAR KINASE RELATED
signalp\"[1-23]?signal-peptide
tmhmm\"[5-23]?\"[42-62]?\"[74-94]?\"[100-120]?transmembrane_regions


","No hits to the COGs database.","","Residues 17 to 121 match (3e-21) PD:PD015683 which is described as COMPLETE PROTEOME TRANSMEMBRANE LIN0671 BACTERIAL-LIKE HYDROXYLATION CG2996 DR1864 BH3828 STY3121 ","","","","","","","","","","","","Wed Jan 15 09:49:54 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02455 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 121 (E-value = 3.6e-49) place AA02455 in the DUF423 family which is described as Protein of unknown function (DUF423) (PF04241)","","","","","","","","1","","","" "AA02456","1695482","1694883","600","TTGCCGCAAGACATCCGCAAGCGTAAAAACGCGTTTCAAAATGACCGTACTTTGGTTTCCGGAGTGCGGTTTTTTGCTGCTTGGCGCAGGGAAAAACAGGCGGTTTGTGCTATAATTCTCCGCAAATTTTTACCGCACTTTAGGATCAATATGTCGTTTCAATTCAACGCGATCGCCTTACTTTTGGTGATTTTAATTTTATTAGGTGTACTCAGCCACAACAGTTCCATCACCATTTCCGCTGCCGTATTGCTCATCATGCAACAAACCTTGCTCGCAAAATATATTCCTTACTTGGAAAAATACGGCTTGAGCATCGGTATCGTAATTTTAACCATCGGCGTACTAAGCCCGTTGGTTTCCGGCAGAATTCAACTGCCTGGCTTGTCGGCATTTTTTAGCTGGCGAATGTTTGTTGCCATTGGCGTCGGCGTATTAGTGGCGTGGCTTGCCGGCAAAGGCGTTCCGCTCATGGGGGAAGAGCCTGTTCTGGTAACCGGCTTGGTTATCGGCACCATTATCGGCGTTTCTTTTCTCGGTGGTATTCCCGTTGGTCCCCTTATTGCGGCAGGGATTTTGGCATTATTAATAGGAAAATTT","","","28566","LPQDIRKRKNAFQNDRTLVSGVRFFAAWRREKQAVCAIILRKFLPHFRINMSFQFNAIALLLVILILLGVLSHNSSITISAAVLLIMQQTLLAKYIPYLEKYGLSIGIVILTIGVLSPLVSGRIQLPGLSAFFSWRMFVAIGVGVLVAWLAGKGVPLMGEEPVLVTGLVIGTIIGVSFLGGIPVGPLIAAGILALLIGKF","1694881","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR007382
Family
Protein of unknown function DUF441
PF04284\"[54-200]TDUF441
noIPR
unintegrated
unintegrated
PD021096\"[72-182]TYEAL_HAEIN_P44110;
tmhmm\"[51-71]?\"[77-97]?\"[102-122]?\"[132-152]?\"[162-196]?transmembrane_regions


","No hits to the COGs database.","","Residues 72 to 182 match (1e-36) PD:PD021096 which is described as COMPLETE PROTEOME MEMBRANE TRANSMEMBRANE YTWI INNER PREDICTED ORTHOLOG YEAL PROTEIN ","","","","","","","","","","","","Wed Jan 15 09:52:18 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02456 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 54 to 200 (E-value = 2.1e-80) place AA02456 in the DUF441 family which is described as Protein of unknown function (DUF441) (PF04284)","","","","","","","","1","","","" "AA02457","1695834","1695460","375","GTGATACAATACGCGCGTTTTTTTCCTTCAATGAACACAAGGAATGTTATGGAAACTTTAGATAAAATCAAAAAACAAATTAGCGAAAACCCCATTCTTATTTACATGAAAGGTTCGCCGAAATTCCCGTCTTGCGGTTTTTCCGCCCGCGCGGTTGAAGCCTTAATTAACTGCGGTGTGCCGTTCGGTTATGTGGATATTTTACAACACCCGGACATTCGTGCCGAATTACCGGCTTATGCCAACTGGCCGACATTCCCGCAATTATGGGTGGAAGGCGAGCTCATCGGTGGTTGCGACATCGTGTTGGAAATGTACCAACAAGGTGAGCTTAAAACCTTGTTACAAGAGGTTGCCGCAAGACATCCGCAAGCG","","","14357","VIQYARFFPSMNTRNVMETLDKIKKQISENPILIYMKGSPKFPSCGFSARAVEALINCGVPFGYVDILQHPDIRAELPAYANWPTFPQLWVEGELIGGCDIVLEMYQQGELKTLLQEVAARHPQA","1695458","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR002109
Domain
Glutaredoxin
PF00462\"[32-96]TGlutaredoxin
InterPro
IPR004480
Family
Glutaredoxin-related protein
PTHR10293\"[6-118]TGLUTAREDOXIN
TIGR00365\"[20-118]TTIGR00365: glutaredoxin homolog
InterPro
IPR012335
Domain
Thioredoxin fold
G3DSA:3.40.30.10\"[19-122]Tno description
InterPro
IPR014434
Family
Monothiol glutaredoxin
PIRSF005894\"[17-123]TMonothiol glutaredoxin


","No hits to the COGs database.","","Residues 33 to 120 match (8e-43) PD:PD001458 which is described as PROTEOME COMPLETE THIOREDOXIN-LIKE PICOT PKCQ-INTERACTING GLUTAREDOXIN-LIKE THIOREDOXIN AT4G04950/T1J1_6 GRLA T1J1.6 ","","","","","","","","","","","","Wed Jan 15 09:54:20 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02457 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 31 to 115 (E-value = 4.7e-05) place AA02457 in the Glutaredoxin family which is described as Glutaredoxin (PF00462)","","","","","","","","1","","","" "AA02458","1697168","1696131","1038","ATGAAAAGAACTGCAATCGCATTAGCTATCGCTGGTTTAGCAGCAGCAACAGTAGCACAGGCAGCACCACAAGCAAACACTTTCTATGCTGGTGCAAAAGCCGGTTGGGCTTCGTCTCATCACGGATTAAATCAATTTAAACAGAAAGGAGTTTCTATAAATCGTAATTCTGAGGCTTACGGCGTTTTCGGTGGTTATCAAATTACAGATAACTTCGCTGTTGAAGCAGGTTATGAATATTTTGGACGTTCTAAGGCTAAAGTTAATGGTGCTCAACGCTTTAGACATACTGCTCATGGTACAACTTTAGCCCTTAAGGCAAGTTATCCTGTATTGGACAACTTAGATGTTTATGGACGTGTTGGCGCCGCTTTAATTCGTAGTGATTATAAAGTTGGTCAAGCCAATAAACCTGATAGATATCACAATTTGAAAGTATCTCCGGTTTTTGCCGGTGGTGTTGAGTATGCCATTCTTCCTGAACTGGCATTACGAGCAGAATATCAATGGGTTAGCCGTGTAGGTAACTTAGGCCGTGCAGAAGAAAAAGCCGACCGTTCTGCACGTACAATTGATTATTCACCGGACATCGGTTCTGTAGCAGTTGGCTTGTCTTACCGTTTCGGTCAAGGTGTAGCGCCTGCTCCGGCTCCTGAAGTTGTAAGAAAGACATTCAGTTTGAACTCTGATGTAACTTTCGCATTCGGTAAAGCTAACTTAAAACCACAAGCACAAAACACATTAGATGGCATCTACGGCGAAATCGCTCAAGTGAACAATGCTAATGTTCAAGTTGCAGGTTATACAGACCGTATCGGTTCCGACGCTTACAACCAAAAATTATCTCAAAGACGTGCTGAAACTGTAGCAAACTACCTTGTATCTAAAGGTGTTTCTCAACAAGCCATCTCTGCTACCGGTCACGGTAAAGCAAATCCGGTTACCGGTAACAAATGCGACGTAGTTAAAGGTCGTAAAGCGCTTATCGCTTGTTTGGCTGATGACCGTCGCGTAGAAATCGCTGTTAACGGTACTAAA","","","36920","MKRTAIALAIAGLAAATVAQAAPQANTFYAGAKAGWASSHHGLNQFKQKGVSINRNSEAYGVFGGYQITDNFAVEAGYEYFGRSKAKVNGAQRFRHTAHGTTLALKASYPVLDNLDVYGRVGAALIRSDYKVGQANKPDRYHNLKVSPVFAGGVEYAILPELALRAEYQWVSRVGNLGRAEEKADRSARTIDYSPDIGSVAVGLSYRFGQGVAPAPAPEVVRKTFSLNSDVTFAFGKANLKPQAQNTLDGIYGEIAQVNNANVQVAGYTDRIGSDAYNQKLSQRRAETVANYLVSKGVSQQAISATGHGKANPVTGNKCDVVKGRKALIACLADDRRVEIAVNGTK","1696129","","outer membrane protein 34","Outer membrane, Extracellular","","
InterPro
IPR000498
Domain
OmpA-like transmembrane region
PF01389\"[6-212]TOmpA_membrane
InterPro
IPR002368
Family
OmpA outer membrane protein
PR01022\"[110-126]T\"[221-236]T\"[287-306]T\"[321-334]TOUTRMMBRANEA
InterPro
IPR006664
Domain
Bacterial outer membrane protein
PR01021\"[233-255]T\"[263-278]T\"[278-294]TOMPADOMAIN
InterPro
IPR006665
Domain
OmpA/MotB
PD000930\"[221-289]TOmpA/MotB
PF00691\"[232-327]TOmpA
PS51123\"[220-346]TOMPA_2
InterPro
IPR006690
Domain
OmpA-like
PS01068\"[265-309]TOMPA_1
noIPR
unintegrated
unintegrated
G3DSA:2.40.160.20\"[22-209]TG3DSA:2.40.160.20
G3DSA:3.30.1330.60\"[215-346]TG3DSA:3.30.1330.60
SSF103088\"[218-342]TSSF103088
SSF56925\"[22-214]TSSF56925


","BeTs to 13 clades of COG2885COG name: Outer membrane protein and related peptidoglycan-associated (lipo)proteinsFunctional Class: MThe phylogenetic pattern of COG2885 is -------q--r---efghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.9e-57) to 4/4 blocks of the IPB001145 family, which is described as \"Bacterial outer membrane protein\". Interpro entry for IP:IPR001145. IPB001145A 103-131 3.2e-07 IPB001145B 229-256 1.3e-11 IPB001145C 263-309 4.2e-30 IPB001145D 331-342 0.00027Significant hit ( 9.9e-20) to 5/7 blocks of the PR01022 family, which is described as \"Outer membrane protein A signature\". Prints database entry for PR:PR01022. PR01022A 110-126 0.19 PR01022C 196-210 0.00054 PR01022D 221-236 0.12 PR01022F 287-306 0.02 PR01022G 321-334 0.0099","Residues 26 to 93 match (1e-09) PD:PD525046 which is described as OMPA2 ","","","","","","","","","","","","Wed Jan 15 10:02:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02458 is paralogously related to AA02479 (1e-145), AA02027 (7e-19) and AA02829 (4e-09).","","","","","","Residues 232 to 327 (E-value = 1.6e-41) place AA02458 in the OmpA family which is described as OmpA family (PF00691)","","","","White,P.A., Nair,S.P., Kim,M.J., Wilson,M. and Henderson,B.Molecular characterization of an outer membrane protein ofActinobacillus actinomycetemcomitans belonging to the OmpA familyInfect. Immun. 66 (1), 369-372 (1998)PubMed: 98084499Wilson,M.E.The heat-modifiable outer membrane protein of Actinobacillusactinomycetemcomitans: relationship to OmpA proteinsInfect. Immun. 59 (7), 2505-2507 (1991)PubMed: 91267635","Klesney-Tait,J., Hiltke,T.J., Maciver,I., Spinola,S.M., Radolf,J.D. and Hansen,E.J. The major outer membrane protein of Haemophilus ducreyi consists of two OmpA homologs. J. Bacteriol. 179 (5), 1764-1773 (1997) PubMed: 9045839.","Tue Feb 11 17:00:53 2003","Wed Jan 15 10:02:29 2003","1","","","" "AA02459","1697608","1700703","3096","ATGCAAATACTACCTCGTTTAAAAAATGTTCCCCAGTGTTCTCCTTTGGTTAAAAATTATTTGAATGCTCTGTACCGACAACACTTTGAAGGCGATATTTCGTCTAATTATGCCGATCGTTTGAGCTTAGCCACCGACAACAGTGTTTATCAGCAACTGCCACAAGCCATTTTGTTCCCTAAAACCGTCGCCGATGTGGTACGTCTGACCAAATTGGCACAACAGGAAAAATACCTTCCGCTGACCTTTACCCCGCGCGGCGGTGGCACAGGAACCAATGGGCAATCCATCAATAACAATATTATTGTGGACTTATCCCGCCACATGACGAAAATTTTAGAACTCAACGTCAAAGAACGTTGGGTGCGCGTGCAAGCGGGCGTGGTGAAAGATCAGCTTAATCAGTTCCTCAAACCGCACGGTTTATTTTTCTCGCCGGAGCTTTCTACCAGCAACCGTGCCACTTTGGGCGGTATGATCAATACGGATGCTTCCGGGCAAGGCTCCTTGCAATACGGCAAAACCTCCGACCATGTTTTGGGATTGCGTGCCGTATTAATGAATGGCGAAATTCTGGACACAAGTGCGGTCAAATCTGACGACGTTTTTCATGCGATAGAAGAAAGTCATTTATCTGCCAACGGGAAAAAAATCCATCAGGAAATTTTCCAACGTTGCAAAGAAAACCGTGAACAAATCATTAATGATTTACCGCAATTGAACCGTTTTCTCACCGGTTATGATTTGAAGAATGTTTTTAACGATGATTTAAGCGAATTCAATTTAACCCGCATTCTCACCGGCTCGGAAGGTTCCCTCGCCTTTATTTGTGAAGCAGTGCTGGATTTAACGCCGATTCCGCAATATCGTACCTTAATTAACATTAAATACAGTTCCTTTGACGCGGCGTTGCGTAATGCGCCGTTTATGGTGAAAGCCAATGCCCTTTCCGTGGAAACCGTGGATTCCAAGGTGTTGAATCTGGCGAAGCAGGACATTATTTGGCACTCGGTGAAAGCACTCTTAACAGAAGAAGAGCAAAATCCGATTCTCGGCTTAAATATAGTGGAATATGCCGGCAATAACCAGGCGCTCATTGAAAATCAAGTGTCTCAATTATGTGCGACATTAGATCAAAAAATCGCCGACGGGCAGGATCATATCATCGGCTATCAAGTGTGTTCCGATTTGCCTTCTATCGAACGAATTTACGCCATGCGCAAAAAAGCTGTGGGCTTGTTGGGTAATGCCAAAGGCGTAGCGAAACCTATCCCTTTTGTGGAAGACACCTGCGTGCCGCCGGAGAATCTGGCGGACTATATTAGTGAATTCCGCGCCTTGTTGGATAGCCATAAGCTGCAATACGGTATGTTCGGACACGTGGACGCGGGCGTGTTACACGTACGCCCGGCGTTAGATTTATGCGCTCCGGAACAAGTGAAACTGTTCAAACGAATTTCCGACCAAGTGGCGGACTTAACCCGCAAATACGGCGGTTTAATTTGGGGTGAACACGGCAAAGGTATGCGTTCGCAATACGGCGAAAAATTCTTCACACCGGCACTATGGCGTGAGTTACGTTACATCAAATTCCTGTTCGATCCGCAAAACCGCTTAAATCCGGGGAAAATCTGCACCCCGCTGGGCAGCGAGCAAGAACCCTACACCATTTTATCGCCGATGCGCGCCGATTTGGATCGTCAAATTCCTATTCAAATGAAACAAGAATTTATCGGCGCCATGAATTGTAATGGCAACGGATTATGCTTTAACTTTGACGTGCACAGCGCCATGTGCCCGTCCATGAAAGTGAGCAAAAACCGTATTTTTTCACCGAAAGGACGCGCTGCGATGATTCGCGAATGGTTGCGTTTATTGGCAAATGAACAAATTCGCCCGGAACAACTGGATTTCAGACAATCCACAATGAAACTCACGAATATCGTGAAAAAAATCCAAAACAGCCGCAAAAAACGTCGTGGCGAATATGATTTTTCCCATGAAGTGAAAGCCGCCATGGATACTTGCCTTGCCTGTAAAGCCTGCGCCAGTCAATGTCCGATTAAAATTGATGTGCCGAATTTCCGTTCTAAATTCTTCCATTTTTATCACCAACGCTACTTGCGCCCGATAAAAGATTATGTGGTGTCCAATGTAGAATTTATTGCGCCGCTGATGGCAAAACAGGCGAAATTCTTCAATTATTTTACCACGGCAAAAGTGAGCCAAAAGGCGGCGGAAAAATATTTAGGCATGACGGATTTGCCGTTGTTGTCCACGCCGAATTTGCAGCAGCAACTCATTCAAATCGGACATAAAAATGATTCCTTGGAAACACTGGAACGCCTAAGTGCGGTGGAAAAACAAAATGTTTTACTCATCGTGCAGGATCCTTTTACCTCTTATTATGATGCCAAAGTGGTTGTCGATTTTGTGGCGCTGACCGAAAAATTAGGATTTAAAGCAGTGTTATTGCCATTCAAACCGAATGGTAAAGCACAACACATCAAAGGCTTTTTAACCCGTTTTGCGAAAACCGCGAAAAATCAGGCGGACTTTCTTAATCGCATGGCGAAGCTAGGCTTGCCATTGGTAGGCGTGGATCCGGCGATTGTGTTATCTTATCGCGATGAGTATAAAGAAATCCTAGGGACAGAACGGGGGGATTTCCATGTGCTGACTGCACACGAATGGCTAAAACAACAGCTTGATAACGGCACGTTGTTGCAGCACATGAAAAACGCCGGGAAAAATGACCGCACTTTTGAGCCGCATCAGTGGTATTTATTCCCGCATTGCACGGAAATCACCGCAATGCCGAACAGCGCAAAAGAATGGCAGCAAATTTTTGCCGCGTTCACTCAACAGTTACAGGTCGAAAGCGTGGGTCGTTGCGGTATGGCGGGCACTTTCGGGCATGAAACCCAACACATCGACATGTCGAAAGCTATTTATGTATCTTCGTGGGAGCAAAAACTGCAAAATAGAAAGCCTGACTATTGTTTGGCCACCGGTTATTCCTGTCGCAGTCAAGTTAAACGTTTCGCCCATTATCAGCCAAAACACCCTGTGCAAGCCTTATTAACTTTATTTAAA","","","116871","MQILPRLKNVPQCSPLVKNYLNALYRQHFEGDISSNYADRLSLATDNSVYQQLPQAILFPKTVADVVRLTKLAQQEKYLPLTFTPRGGGTGTNGQSINNNIIVDLSRHMTKILELNVKERWVRVQAGVVKDQLNQFLKPHGLFFSPELSTSNRATLGGMINTDASGQGSLQYGKTSDHVLGLRAVLMNGEILDTSAVKSDDVFHAIEESHLSANGKKIHQEIFQRCKENREQIINDLPQLNRFLTGYDLKNVFNDDLSEFNLTRILTGSEGSLAFICEAVLDLTPIPQYRTLINIKYSSFDAALRNAPFMVKANALSVETVDSKVLNLAKQDIIWHSVKALLTEEEQNPILGLNIVEYAGNNQALIENQVSQLCATLDQKIADGQDHIIGYQVCSDLPSIERIYAMRKKAVGLLGNAKGVAKPIPFVEDTCVPPENLADYISEFRALLDSHKLQYGMFGHVDAGVLHVRPALDLCAPEQVKLFKRISDQVADLTRKYGGLIWGEHGKGMRSQYGEKFFTPALWRELRYIKFLFDPQNRLNPGKICTPLGSEQEPYTILSPMRADLDRQIPIQMKQEFIGAMNCNGNGLCFNFDVHSAMCPSMKVSKNRIFSPKGRAAMIREWLRLLANEQIRPEQLDFRQSTMKLTNIVKKIQNSRKKRRGEYDFSHEVKAAMDTCLACKACASQCPIKIDVPNFRSKFFHFYHQRYLRPIKDYVVSNVEFIAPLMAKQAKFFNYFTTAKVSQKAAEKYLGMTDLPLLSTPNLQQQLIQIGHKNDSLETLERLSAVEKQNVLLIVQDPFTSYYDAKVVVDFVALTEKLGFKAVLLPFKPNGKAQHIKGFLTRFAKTAKNQADFLNRMAKLGLPLVGVDPAIVLSYRDEYKEILGTERGDFHVLTAHEWLKQQLDNGTLLQHMKNAGKNDRTFEPHQWYLFPHCTEITAMPNSAKEWQQIFAAFTQQLQVESVGRCGMAGTFGHETQHIDMSKAIYVSSWEQKLQNRKPDYCLATGYSCRSQVKRFAHYQPKHPVQALLTLFK","1700701","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR001450
Domain
4Fe-4S ferredoxin, iron-sulfur binding
PS00198\"[676-687]T4FE4S_FERREDOXIN
InterPro
IPR004113
Domain
FAD linked oxidase, C-terminal
PF02913\"[286-544]TFAD-oxidase_C
InterPro
IPR006094
Domain
FAD linked oxidase, N-terminal
PF01565\"[54-195]TFAD_binding_4
noIPR
unintegrated
unintegrated
G3DSA:3.30.465.20\"[111-194]Tno description
PTHR11748\"[26-194]T\"[248-593]TD-LACTATE DEHYDROGENASE
PTHR11748:SF4\"[26-194]T\"[248-593]TOXIDOREDUCTASE


","No hits to the COGs database.","","Residues 546 to 589 match (4e-13) PD:PD590370 which is described as PROTEOME COMPLETE HI1163 VC1198 PM0787 ","","","","","","","","","","","","Wed Jan 15 10:31:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02459 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 286 to 544 (E-value = 1.5e-61) place AA02459 in the FAD-oxidase_C family which is described as FAD linked oxidases, C-terminal domain (PF02913)","","","","","","","","1","","","" "AA02460","1700716","1701135","420","ATGAGCATCTGGAAAAAAAATCTTACGTTGGAACAACTGAATGCGTTTTGTAAAAACTGCGCAGTAGAACATTTAGGCATTGAATTTATCGCCAAAGGTGATGATTGGCTGGAAGCACGAATGCCGGTAGATCGACGCACTACGCAACCCATGGGGTTATTGCACGGTGGCATTTCTGCGGCATTGGCGGAAACTATCGCTTCAACAGCCGGGTTTTGTTGTGTGGCGGAAAATCAGGTGGTGGTCGGGCTGGAAATTAACGCCAATCACTTGCGCGCCGTGCGTCAAGGCAATGTGTATGCCAAAACCATGCCCATTCACTTGGGCAAAAATGTGCAGGTTTGGCAAATTGACATTCGTGACGAGCAAGATAAACTATGCTGCGTTTCACGTTTAACTCTTTCTGTAATCACTCATGAA","","","15526","MSIWKKNLTLEQLNAFCKNCAVEHLGIEFIAKGDDWLEARMPVDRRTTQPMGLLHGGISAALAETIASTAGFCCVAENQVVVGLEINANHLRAVRQGNVYAKTMPIHLGKNVQVWQIDIRDEQDKLCCVSRLTLSVITHE","1701133","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003736
Domain
Phenylacetic acid degradation-related protein
TIGR00369\"[20-136]Tunchar_dom_1: uncharacterized domain
InterPro
IPR006683
Domain
Thioesterase superfamily
PF03061\"[51-128]T4HBT
noIPR
unintegrated
unintegrated
G3DSA:3.10.129.10\"[3-137]Tno description


","No hits to the COGs database.","Significant hit ( 2.1e-05) to 1/1 blocks of the IPB003736 family, which is described as \"DUF157\". Interpro entry for IP:IPR003736. IPB003736 52-65 2.3e-05","Residues 25 to 134 match (2e-11) PD:PD485347 which is described as AAD49765.1 F11A17.13 ","","","","","","","","","","","","Wed Jan 15 10:33:21 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02460 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 51 to 129 (E-value = 9.6e-18) place AA02460 in the 4HBT family which is described as Thioesterase superfamily (PF03061)","","","","","","","","1","","","" "AA02461","1701131","1702192","1062","ATGAATAAAGCAGCAAAAATCGGCGTCATCCTTGCCAATTTAGGTACACCGGACTCGCCCAATCCTAAGGATATTTCCCGCTACTTATGGCAATTTTTAACGGATCCGCGCGTAGTAGATTTGCCACGCTATAAATGGTTTCCGCTGCTCAAAGCCATTATTTTGCCCTTGCGCTCCAAACGTATTGCAAAAAACTACCGTGCCATTTGGACCAAACAAGGTTCGCCGCTACTTGCCATAACTCAACAACAAAAAGAAGCGTTAGCGATTTTTCTGCAACAACAAAACCTTAATATGGAAATCGAAATCGGCATGACTTACGGCAATCCGTCAATACCCGACGCGGTACAAAAATTAATAGATAAAAAAGTGGATCACATTATTGTATTGCCGCTTTATCCGCAATACAGTAGCACCACCACAGGCGCTGTGTTTGACTCCTTCGCTGCGGCGCTGAAACAACAGCGTGGCATCGTGCCGTTCGATTTCATTCATTCTTATCAATTAAACCAAGGTTATATTACAGCCCTGATTGAATCCTGCAAAGTGCGGTTGAAATCCGAAGAGTTTTTACTGTTCTCTTTCCATGGCATTCCGTTACGTTACGAAAACACCGGCGATTATTACCGCACCCACTGTCAACAAACTGCCACTGCTGTGGCGCAAGGCTTGGGTTTAAATGAAAAGCAGTGGGGGGTGACTTTCCAATCCCGTTTCGGTAAAGAAGAATGGTTGCAGCCTTACACCGACGACTTTCTTGCCGGTGCGGCACAACAAGGCATCAAAAATATTGCCGTACTCTGCCCGGGCTTTGCCGCCGATTGTTTGGAAACCTTGGAAGAAATCGCCGAAGAAAACCGCGAACTATTTTTAGCCAACGGCGGACAAAGCTATCACTACATCCCGGCGCTCAATGCCGAACCGGCGCATATCGAAGCGCTTGGTAAACTATTACTGAATATGATCGGCAAAATGAAATGCAATAATTGCAATGTGCCGAATATCAACGAAGTTCCGATCATTGAAGTGCAAACTTCAGGTCAATTAAGCAGCCGTTGCCAT","","","39763","MNKAAKIGVILANLGTPDSPNPKDISRYLWQFLTDPRVVDLPRYKWFPLLKAIILPLRSKRIAKNYRAIWTKQGSPLLAITQQQKEALAIFLQQQNLNMEIEIGMTYGNPSIPDAVQKLIDKKVDHIIVLPLYPQYSSTTTGAVFDSFAAALKQQRGIVPFDFIHSYQLNQGYITALIESCKVRLKSEEFLLFSFHGIPLRYENTGDYYRTHCQQTATAVAQGLGLNEKQWGVTFQSRFGKEEWLQPYTDDFLAGAAQQGIKNIAVLCPGFAADCLETLEEIAEENRELFLANGGQSYHYIPALNAEPAHIEALGKLLLNMIGKMKCNNCNVPNINEVPIIEVQTSGQLSSRCH","1702190","From PF00762: Ferrochelatase.This enzyme catalyzes the last step in heme biosynthesis: thechelation of a ferrous ion to proto-porphyrin IX, to form protoheme.","ferrochelatase","Cytoplasm","","
InterPro
IPR001015
Family
Ferrochelatase
PD002792\"[11-322]THEMZ_PASMU_P57874;
PTHR11108\"[1-323]TFERROCHELATASE
PF00762\"[6-322]TFerrochelatase
TIGR00109\"[2-323]ThemH: ferrochelatase
PS00534\"[191-209]TFERROCHELATASE
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1400\"[3-214]Tno description


","BeTs to 17 clades of COG0276COG name: Protoheme ferro-lyase (ferrochelatase)Functional Class: HThe phylogenetic pattern of COG0276 is ---p--yq-drlbcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 2.7e-68) to 7/7 blocks of the IPB001015 family, which is described as \"Ferrochelatase\". Interpro entry for IP:IPR001015. IPB001015A 8-18 0.0024 IPB001015B 71-77 28 IPB001015C 112-144 3.7e-14 IPB001015D 191-204 1.8e-06 IPB001015E 206-225 5.1e-06 IPB001015F 235-251 1.4e-10 IPB001015G 260-294 4.1e-19","Residues 6 to 72 match (4e-12) PD:PD523531 which is described as HEME BIOSYNTHESIS PROTEOME FERROCHELATASE PORPHYRIN SYNTHETASE COMPLETE IRON LYASE PROTOHEME ","","","","","Sat Jan 25 14:37:50 2003","","","","","","Wed Jan 15 10:47:27 2003","Wed Jan 15 10:43:30 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02461 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 6 to 322 (E-value = 3.4e-140) place AA02461 in the Ferrochelatase family which is described as Ferrochelatase (PF00762)","","","","","Miyamoto,K., Kanaya,S., Morikawa,K. and Inokuchi,H.Overproduction, purification, and characterization offerrochelatase from Escherichia coliJ. Biochem. 115 (3), 545-551 (1994)PubMed: 8056770Dailey TA, Dailey HA.Identification of [2Fe-2S] clusters in microbial ferrochelatases.J Bacteriol. 2002 May;184(9):2460-4.PMID: 11948160Qi Z, O'Brian MR.Interaction between the bacterial iron response regulator and ferrochelatase mediates genetic control of heme biosynthesis.Mol Cell. 2002 Jan;9(1):155-62.PMID: 11804594Schlor S, Herbert M, Rodenburg M, Blass J, Reidl J.Characterization of ferrochelatase (hemH) mutations in Haemophilus influenzae.Infect Immun. 2000 May;68(5):3007-9.PMID: 10769004","","Sat Jan 25 14:37:50 2003","1","","","" "AA02462","1702236","1702733","498","ATGAGTAAAGTCACTTTAACAGGCACCCCTATTGATGTTGCTGGCACTTTTCCTGCAACAGATACGCAAATCGCCAATTTCACTTTAGTCAACAATGAATTGGCAGATGTGGCACTTAATAGCTTTGCCGGTAAACGCAAAGTCTTAAATATTTTCCCAAGTATCGACACCGGTGTTTGCGCCACATCGGTACGCAAATTCAATGAAAAAGCGGCAAATTTGGCAAATACCGTAGTGCTTTGCATTTCCGCCGATTTACCGTTCGCCCAAGCCCGTTTCTGTGGCGCGGAAGGCGTTGAAAATGTCAAAACCCTTTCCACCTTCCGTAACCACGCCCTACACAACACCTTAGGCGTTGACATCACCTCCGGTCCGCTTGCCGGCTTAACGGCACGCGCGGTTATTGTGTTGGATGAAAATAACAACGTGTTACACAGCGAGTTAGTTTCTGAAATTAAGAATGAACCCAATTACGACGCGGCACTTGCAGTATTGGCA","","","17496","MSKVTLTGTPIDVAGTFPATDTQIANFTLVNNELADVALNSFAGKRKVLNIFPSIDTGVCATSVRKFNEKAANLANTVVLCISADLPFAQARFCGAEGVENVKTLSTFRNHALHNTLGVDITSGPLAGLTARAVIVLDENNNVLHSELVSEIKNEPNYDAALAVLA","1702731","From Genbank:[gi:1171956].This protein has antioxidant activity.It could remove peroxides or H(2)O(2)","thiol peroxidase (scavengase)","Cytoplasm, Periplasm","","
InterPro
IPR002065
Family
Antioxidant Tpx
PTHR10681:SF3\"[10-165]TPEROXIREDOXIN RELATED
PS01265\"[83-94]TTPX
InterPro
IPR012335
Domain
Thioredoxin fold
G3DSA:3.40.30.10\"[2-166]Tno description
InterPro
IPR013740
Domain
Redoxin
PF08534\"[19-165]TRedoxin
noIPR
unintegrated
unintegrated
PTHR10681\"[10-165]TPEROXIREDOXIN


","BeTs to 9 clades of COG2077COG name: PeroxiredoxinFunctional Class: OThe phylogenetic pattern of COG2077 is -------q--rlb-efgh--u-----Number of proteins in this genome belonging to this COG is","Significant hit ( 3e-85) to 3/3 blocks of the IPB002065 family, which is described as \"Tpx family\". Interpro entry for IP:IPR002065. IPB002065A 4-54 2.6e-18 IPB002065B 60-108 3.8e-40 IPB002065C 129-162 1.4e-24Significant hit ( 5.2e-10) to 3/3 blocks of the IPB000866 family, which is described as \"AhpC/TSA family\". Interpro entry for IP:IPR000866. IPB000866A 48-63 6.4e-05 IPB000866B 79-93 0.0082 IPB000866C 123-132 2.3e+02","Residues 76 to 159 match (9e-13) PD:PD480789 which is described as COMPLETE PROTEOME PEROXIDASE COMIGRATORY BACTERIOFERRITIN THIOL PROBABLE OXIDOREDUCTASE 1.11.1.- HOMOLOG ","","","","","","","","","","","Tue Jan 7 09:55:29 2003","Wed Jan 29 14:34:31 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02462 is paralogously related to AA02348 (3e-04).","","","","","","Residues 13 to 162 (E-value = 6.3e-26) place AA02462 in the AhpC-TSA family which is described as AhpC/TSA family (PF00578)","","","","","Cha,M.K., Kim,H.K. and Kim,I.H.Thioredoxin-linked 'thiol peroxidase' from periplasmic space ofEscherichia coliJ. Biol. Chem. 270 (48), 28635-28641 (1995)PubMed: 7499381Jakubovics NS, Smith AW, Jenkinson HF.Oxidative stress tolerance is manganese (Mn(2+)) regulated in Streptococcus gordonii.Microbiology. 2002 Oct;148(Pt 10):3255-63.PMID: 12368459 Spatafora G, Van Hoeven N, Wagner K, Fives-Taylor P.Evidence that ORF3 at the Streptococcus parasanguis fimA locus encodes a thiol-specific antioxidant.Microbiology. 2002 Mar;148(Pt 3):755-62.PMID: 11882710","","Wed Jan 29 14:34:31 2003","1","","","" "AA02463","1704023","1702944","1080","GTGGTGATTGAAGGCGAACATATTCAAGCCGTGGTTCTGCAAAGTGAATTGGAGCGCGGTATTAAAGCCATTGATTTACAAGGACATAACCTCACGGCAGGGTTTATTGATTTGCAACTTAACGGCTGCGGCGGCGTGATGTTTAACGATCAAACCAGCGTAGAAACCTTGGAAATCATGCAAGCTACCAATTTGAAATCGGGCTGCACCAGTTTCTTACCGACCTTTATCACCGCACCTGATGAAGGCATTAAAAGTGCGGTTAAAATTATGCGTGAATATTTAGCCAAGCATAAAAACCAAGCGCTGGGCTTGCACATTGAAGGACCGTATTTAAGCGTTGAGAAAAAAGGCGTGCACCGCCCGGAATATATCCGCGAAATTTCGCCGGAAATGAAAGATTTCCTTTGTGAAAATGCCGACGTGATCACCAAACTCACGATCGCCGCAGAAAATCCGACCGCCAATTATATTCCGGATTTCGTGAAAAGTGGCATTGTGGTTTCCATCGGGCATTCCAACGCCACCTATGAAGTGGCAAAAGCGGCGTTCCATAAAGGCGCCACCTTCGCCACCCACTTGCACAACGCCATGTCACCGATCAGTTCCGGACGCGCTATGGGCGTGGTCGGCGCGGTGTTGGATTCTGATGTTTACACTGGCATTATCGTGGACGGCGTGCATGTGAATTTCGGCAACGTACGCCTTGATAAAAAAGTGAAAGGCGACAAACTCTGTATTGTCACCGACTCCCTTGCCGCTGCCGGCGCAGGTCCGGAATTGGAAAGTTTCACCTTCGTGGGTAAAACCATTTATGTGAAAGATGGTCGTTGCTACGATGGCAACGGCACCATTGCCGGTGCGTCCATTACCATGATGGAATCCATCAAAAACGCCGTAGAATATGTGGAAATCCCGCTCGCCGAAGCGGTTCGCATGAGTAACCTTTATCCCGCACGCGCCATCGGCGTGGACGATCGTTTAGGTTCCGTGGAAACCGGCAAAATTGCCAACCTCGCCGTATTCTCCAATGATTACGAAGTTATTGGCACCGTGCTGAACGGCGAGTGGAAAGTGAAT","","","41161","VVIEGEHIQAVVLQSELERGIKAIDLQGHNLTAGFIDLQLNGCGGVMFNDQTSVETLEIMQATNLKSGCTSFLPTFITAPDEGIKSAVKIMREYLAKHKNQALGLHIEGPYLSVEKKGVHRPEYIREISPEMKDFLCENADVITKLTIAAENPTANYIPDFVKSGIVVSIGHSNATYEVAKAAFHKGATFATHLHNAMSPISSGRAMGVVGAVLDSDVYTGIIVDGVHVNFGNVRLDKKVKGDKLCIVTDSLAAAGAGPELESFTFVGKTIYVKDGRCYDGNGTIAGASITMMESIKNAVEYVEIPLAEAVRMSNLYPARAIGVDDRLGSVETGKIANLAVFSNDYEVIGTVLNGEWKVN","1702942","","N-acetylglucosamine-6-phosphate deacetylase","Cytoplasm","","
InterPro
IPR003764
Family
N-acetylglucosamine-6-phosphate deacetylase
TIGR00221\"[1-356]TnagA: N-acetylglucosamine-6-phosphate deace
InterPro
IPR006680
Domain
Amidohydrolase 1
PF01979\"[30-343]TAmidohydro_1
InterPro
IPR011550
Domain
Amidohydrolase-like
PD001248\"[305-339]TQ6D7K0_BBBBB_Q6D7K0;
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.140\"[35-323]Tno description
PTHR11113\"[23-360]TN-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE


","BeTs to 10 clades of COG1820COG name: N-acetylglucosamine-6-phosphate deacetylaseFunctional Class: GThe phylogenetic pattern of COG1820 is --------vdrlb-efghs--j--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 2.7e-38) to 4/4 blocks of the IPB003764 family, which is described as \"N-acetylglucosamine-6-phosphate deacetylase\". Interpro entry for IP:IPR003764. IPB003764A 192-206 7.2e-05 IPB003764B 221-237 2e-05 IPB003764C 244-256 0.0001 IPB003764D 313-355 1.4e-18","Residues 104 to 189 match (2e-08) PD:PD561636 which is described as PROTEOME N-ACETYLGLUCOSAMINE-6-PHOSPHATE COMPLETE DEACETYLASE NAGA SIMILAR PROBABLE CGI-14 CG17065 ","","","","","","","","","","","","Wed Jan 15 10:57:27 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02463 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 30 to 343 (E-value = 1.1e-49) place AA02463 in the Amidohydro_1 family which is described as Amidohydrolase family (PF01979)","","","","","Plumbridge,J.A.Sequence of the nagBACD operon in Escherichia coli K12 and patternof transcription within the nag regulonMol. Microbiol. 3 (4), 505-515 (1989)PubMed: 2668691Peri,K.G., Goldie,H. and Waygood,E.B.Cloning and characterization of the N-acetylglucosamine operon ofEscherichia coliBiochem. Cell Biol. 68 (1), 123-137 (1990)PubMed: 2190615Ferreira FM, Mendoza-Hernandez G, Calcagno ML, Minauro F, Delboni LF, Oliva G.Crystallization and preliminary crystallographic analysis of N-acetylglucosamine 6-phosphate deacetylase fromEscherichia coli.Acta Crystallogr D Biol Crystallogr. 2000 May;56 ( Pt 5):670-2.PMID: 10771446","","Wed Jan 15 11:01:56 2003","1","","","" "AA02464","1704050","1704154","105","TTGTGTAAATCACAGAGTTTGTTAATGCATATTTCATTCTTACCTTCCCAAATTTATCGAAAAAAACAACCGCACTTTCGTGCGGCGTTTAACTATAACACACTG","","","4164","LCKSQSLLMHISFLPSQIYRKKQPHFRAAFNYNTL","1704154","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 10:00:00 2004","Wed Feb 25 10:00:00 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02464 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 10:00:00 2004","","","","","","","","","","","","","1","","","" "AA02465","1704945","1704145","801","ATGCGTCTTATCCCACTCACTACAGAACAACAAGTCAGCCGCTGGGCAGCACGTCATATCGTGGATCGAATCAATCAATTCAAACCCACTGAAAATCGTCCTTTCGTATTGGGCTTGCCGACCGGCAGCACCCCGTTAAAAACCTATCAGGAATTAATTAAACTTTATCAAGCGGGCGAAGTGAGCTTTAAACATGTGGTGACATTTAACATGGATGAATATGTCGGTTTGCCGAAAGAACATCCGGAAAGTTATCACAGCTTTATGTATAACAATTTCTTCAATCATGTGGATATTCAACCGCAAAATATCAATATTTTAAACGGTAATACGGAAGATCATGATGAAGAATGCCGTTGTTACGAAGAAAAAATCAAATCCTATGGCAAAATCAATTTATTCATGGGCGGTGTGGGCGTTGACGGGCATATCGCCTTTAACGAACCGGCATCTTCTTTAAGCTCCCGCACCCGTATTAAAACCTTGACGAAAGACACCTTAATCGCCAATTCCCGCTTCTTTGATAATGATGTTAAAAAAGTGCCGAAATATGCCTTAACCATCGGTGTGGCAACGTTATTGGATGCGGAAGAAGTGATGATCTTAGCCACCGGACACCAAAAAGCCCTTGCAGTACAAGCAGCGGTGGAAGGTTCGGTGAACCATCTCTGGACGGTCAGCGCGTTGCAATTACATCGCCACTTTATTTTGGTGACGGATGAAGCCGCGTTGCAAGAGCTTAAAGTGAAAACCGTGAAATATTTCACCGAATTGGAAGAAAGAGCCATTCACAGTGTGTTA","","","30327","MRLIPLTTEQQVSRWAARHIVDRINQFKPTENRPFVLGLPTGSTPLKTYQELIKLYQAGEVSFKHVVTFNMDEYVGLPKEHPESYHSFMYNNFFNHVDIQPQNINILNGNTEDHDEECRCYEEKIKSYGKINLFMGGVGVDGHIAFNEPASSLSSRTRIKTLTKDTLIANSRFFDNDVKKVPKYALTIGVATLLDAEEVMILATGHQKALAVQAAVEGSVNHLWTVSALQLHRHFILVTDEAALQELKVKTVKYFTELEERAIHSVL","1704143","From PF01182:This enzyme is responsible for the conversion of D-glucosamine 6-phosphate into D-fructose 6-phosphate.It is the last specific step in the pathway for N-acetylglucosamine (GlcNAC) utilization in bacteria such as Escherichia coli (nagB). A region located in the central part of Glucosamine-6-phosphate isomerase contains a conserved histidine which has been shown in nagB, to be important for the pyranose ring-opening step of the catalytic mechanism.","glucosamine-6-phosphate isomerase","Cytoplasm","","
InterPro
IPR004547
Family
Glucosamine-6-phosphate isomerase
PTHR11280\"[24-255]TGLUCOSAMINE-6-PHOSPHATE ISOMERASE
TIGR00502\"[1-259]TnagB: glucosamine-6-phosphate isomerase
PS01161\"[125-143]TGLC_GALNAC_ISOMERASE
InterPro
IPR006148
Domain
Glucosamine/galactosamine-6-phosphate isomerase
PF01182\"[15-250]TGlucosamine_iso
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1360\"[1-266]Tno description


","BeTs to 7 clades of COG0363COG name: 6-phosphogluconolactonase/Glucosamine-6-phosphate isomerase/deaminaseFunctional Class: GThe phylogenetic pattern of COG0363 is ------y-v-rlbcefghsnuj-it-Number of proteins in this genome belonging to this COG is","Significant hit ( 2.6e-73) to 3/3 blocks of the IPB000457 family, which is described as \"Glucosamine/galactosamine-6-phosphate isomerase\". Interpro entry for IP:IPR000457. IPB000457A 36-78 1.4e-23 IPB000457B 121-173 2.5e-24 IPB000457C 189-243 4.8e-23","Residues 1 to 259 match (1e-131) PD:PD006132 which is described as ISOMERASE COMPLETE PROTEOME DEAMINASE GLUCOSAMINE-6-PHOSPHATE HYDROLASE 6-PHOSPHOGLUCONOLACTONASE 6PGL METABOLISM GNPDA ","","","","","","","","","","","Wed Jan 15 14:12:06 2003","Wed Jan 15 12:55:57 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02465 is paralogously related to AA01168 (7e-08).","","","","","","Residues 15 to 250 (E-value = 3e-185) place AA02465 in the Glucosamine_iso family which is described as Glucosamine-6-phosphate isomerases/6-phosphogluconolactonase (PF01182)","","","","","Rogers,M.J., Ohgi,T., Plumbridge,J. and Soll,D.Nucleotide sequences of the Escherichia coli nagE and nagB genes:the structural genes for the N-acetylglucosamine transport proteinof the bacterial phosphoenolpyruvate: sugar phosphotransferasesystem and for glucosamine-6-phosphate deaminaseGene 62 (2), 197-207 (1988)PubMed: 3284790Peri,K.G., Goldie,H. and Waygood,E.B.Cloning and characterization of the N-acetylglucosamine operon ofEscherichia coliBiochem. Cell Biol. 68 (1), 123-137 (1990)PubMed: 2190615Altamirano,M.M., Plumbridge,J.A. and Calcagno,M.L.Identification of two cysteine residues forming a pair of vicinalthiols in glucosamine-6-phosphate deaminase from Escherichia coliand a study of their functional role by site-directed mutagenesisBiochemistry 31 (4), 1153-1158 (1992)PubMed: 1734962Oliva,G., Fontes,M.R., Garratt,R.C., Altamirano,M.M., Calcagno,M.L. and Horjales,E.Structure and catalytic mechanism of glucosamine 6-phosphatedeaminase from Escherichia coli at 2.1 A resolutionStructure 3 (12), 1323-1332 (1995)PubMed: 8747459","","Wed Jan 15 14:12:06 2003","1","","","" "AA02466","1705978","1705103","876","ATGCGGGATTTAAAAGGAATTTTCAGTGCATTATTAGTATCATTCAACGAAGACGGCTCTGTGAATGAAAAAGGTTTGCGCGAAATTATTCGTTACAACATCGACAAAATGAAAGTGGACGGCTTGTATGTGGGCGGTTCCACCGGTGAAAACTTCATGCTTTCCACGGACGAGAAAAAACAAATCTTCCGTATTGCCAAAGATGAAGCCAAAGACCAAGTGGCGTTAATTGCCCAAGTGGGTAGCGTGAATTTACAGGAAGCCGTTGAATTGGGTAAATACGCCACCGAATTAGGCTATGACAGCTTGTCTGCGGTCACCCCGTTCTATTACAAATTCAGCTTCCCTGAAATCAAACATTACTATGATACTATCATTGCCGAAACTGGCAACAACATGATCGTGTATTCCATCCCGTTCTTAACCGGTGTGAACATGGGGATCGAACAATTCGGCGAACTTTACAAAAACCCGAAAGTGCTTGGCGTGAAATTCACCGCAGGCGATTTCTATCTGTTGGAACGTTTGAAAAAAGCCTATCCGAACCACTTAATCTGGGCAGGTTTCGACGAAATGATGTTACCGGCAGCCTCTTTAGGGGTGGATGGCGCTATCGGTTCAACCTTTAACGTGAACGGTATCCGCGCCCGTCAAATTTTTGAGTTAACCAAAGCGGGCAAACTCAAAGAAGCGCTTGAAATCCAGCACGTCACTAACGATTTAATCGAAGGCATTTTGGCGAACGGTTTATATTTAACCATCAAAGAATTGTTGAAATTGGAAGGCGTTCACGCCGGCTACTGCCGTGAACCGATGACCGCCAAAGCCACTCCGGAACAACTCGCGAAAGCGAAAGAATTAAAAGCGAAGTATTTA","","","32493","MRDLKGIFSALLVSFNEDGSVNEKGLREIIRYNIDKMKVDGLYVGGSTGENFMLSTDEKKQIFRIAKDEAKDQVALIAQVGSVNLQEAVELGKYATELGYDSLSAVTPFYYKFSFPEIKHYYDTIIAETGNNMIVYSIPFLTGVNMGIEQFGELYKNPKVLGVKFTAGDFYLLERLKKAYPNHLIWAGFDEMMLPAASLGVDGAIGSTFNVNGIRARQIFELTKAGKLKEALEIQHVTNDLIEGILANGLYLTIKELLKLEGVHAGYCREPMTAKATPEQLAKAKELKAKYL","1705101","From PF00701This enzyme catalyzes the condensation of N-acetyl-D-mannosamine and pyruvate to form N-acetylneuraminate.","N-acetylneuraminate lyase","Cytoplasm","","
InterPro
IPR002220
Family
Dihydrodipicolinate synthetase
PD001859\"[2-71]TNANA_HAEIN_P44539;
PR00146\"[38-59]T\"[74-92]T\"[106-122]T\"[131-148]TDHPICSNTHASE
PIRSF001365\"[4-290]TDihydrodipicolinate synthase
PTHR12128\"[1-272]TDIHYDRODIPICOLINATE SYNTHASE
PF00701\"[3-291]TDHDPS
PS00665\"[41-58]TDHDPS_1
PS00666\"[136-166]TDHDPS_2
InterPro
IPR005264
Family
N-acetylneuraminate lyase
TIGR00683\"[4-292]TnanA: N-acetylneuraminate lyase
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[1-288]Tno description
InterPro
IPR013838
Binding_site
Beta tubulin, autoregulation binding site
PS00228\"[1-4]?TUBULIN_B_AUTOREG


","BeTs to 22 clades of COG0329COG name: Dihydrodipicolinate synthase/N-acetylneuraminate lyaseFunctional Class: E,MThe phylogenetic pattern of COG0329 is aompkz-qv-rlbcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 2.1e-53) to 7/7 blocks of the IPB002220 family, which is described as \"Dihydrodipicolinate synthetase\". Interpro entry for IP:IPR002220. IPB002220A 10-22 0.028 IPB002220B 38-59 1.3e-10 IPB002220C 78-125 2.4e-19 IPB002220D 132-143 0.0074 IPB002220E 181-195 0.0018 IPB002220F 200-213 0.0098 IPB002220G 238-262 0.031","","","","","","","","","","","","Wed Jan 15 14:22:36 2003","Wed Jan 15 14:18:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02466 is paralogously related to AA02349 (4e-22).","","","","","","Residues 3 to 291 (E-value = 6.8e-141) place AA02466 in the DHDPS family which is described as Dihydrodipicolinate synthetase family (PF00701)","","","","","Meysick,K.C., Dimock,K. and Garber,G.E.Molecular characterization and expression of a N-acetylneuraminatelyase gene from Trichomonas vaginalisMol. Biochem. Parasitol. 76 (1-2), 289-292 (1996)PubMed: 8920014Izard T, Lawrence MC, Malby RL, Lilley GG, Colman PM.The three-dimensional structure of N-acetylneuraminate lyase fromEscherichia coli.Structure 1994 May 15;2(5):361-9PMID: 8081752","","Wed Jan 15 14:22:36 2003","1","","","" "AA02468","1706857","1705991","867","ATGGCAACGAATGGCAATGTGCTTAACACCGTTAGCGCGTTATATCAGAGTTTAACTAAAACGGAAAAGAAAATTGCCGATGTGATTTCGCAATCACCGGAAATGGTCATGCAATATTCTCTTTCCGAGCTTGCATCGAATTTGAATGTGGGCGAAGCGACCTTTGTACGTTTTTGTCGAACCTTGGGGTTCAAAGGCTTCAGCGATTTCAAACTGGCGTTTTCCATTGAGCTGGCAACCGCCAGAGAAAGCCGTGACGACACCGTGCTGGAAACGGAGATCATGCCTGACGACGATTCATTGAAAATCGCTCACAAATTACAGGCAGCGATCTCCAAAGTGATGGACGAAACGGTGAATTTGCTGGATTTCCAACAACTTGAAAGCGTGGTGCGGGCGATTCAAAAAGCTAAACGGGTCTTTTTATTCGGCGTGGGATCTTCCGGTGTCACGGCGGAAGATGCGAAAAATAAATTTATGCGTATCGGTGTGCCGGTAGATGCTACCGGTAACAATCATTTTATGTATATGCAGGCGGCGCTGCTGAAAGAAACCGATGTGGCGATTGGGATCAGCCATTCGGGCTATTCACAGGAAACCGCCCACACGTTAAAAATCGCCAAACAAAACGGGGCGACGACAGTGGCGTTAACGCACAGTTTGCGTTCGCCTATTACCGAACACGCGGATTTTGTACTGGTCAACGGCAATAAACAAGGGAAACTCCAGGGAGATTCCATCGGTACGAAAATCGCTCAATTATTTGTATTGGATTTGATCTACGCTTTATTGGTACAAGCCGAACAGGACGCCGCGACCAAAACCAAACAGAAAACACTTAATGTTATTTTAGAACAACGTATTAAA","","","31619","MATNGNVLNTVSALYQSLTKTEKKIADVISQSPEMVMQYSLSELASNLNVGEATFVRFCRTLGFKGFSDFKLAFSIELATARESRDDTVLETEIMPDDDSLKIAHKLQAAISKVMDETVNLLDFQQLESVVRAIQKAKRVFLFGVGSSGVTAEDAKNKFMRIGVPVDATGNNHFMYMQAALLKETDVAIGISHSGYSQETAHTLKIAKQNGATTVALTHSLRSPITEHADFVLVNGNKQGKLQGDSIGTKIAQLFVLDLIYALLVQAEQDAATKTKQKTLNVILEQRIK","1705989","","conserved hypothetical protein","Cytoplasm, Outer membrane","","
InterPro
IPR000281
Domain
Helix-turn-helix protein RpiR
PF01418\"[5-115]THTH_6
PS51071\"[5-81]THTH_RPIR
InterPro
IPR001347
Domain
Sugar isomerase (SIS)
PF01380\"[133-266]TSIS
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.10490\"[91-264]Tno description


","BeTs to 7 clades of COG1737COG name: Transcriptional regulatorsFunctional Class: KThe phylogenetic pattern of COG1737 is --------v--lb-efgh-n-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 7e-45) to 3/3 blocks of the IPB000281 family, which is described as \"Helix-turn-helix domain, RpiR family\". Interpro entry for IP:IPR000281. IPB000281A 144-162 2.2e-09 IPB000281B 171-218 2.1e-25 IPB000281C 239-261 2.8e-07Significant hit ( 4.3e-08) to 1/2 blocks of the IPB001347 family, which is described as \"SIS domain\". Interpro entry for IP:IPR001347. IPB001347B 186-211 4.3e-08","Residues 7 to 107 match (1e-07) PD:PD467665 which is described as COMPLETE PROTEOME TRANSCRIPTIONAL REGULATOR FAMILY REGULATOR TRANSCRIPTION REGULATION PLASMID RPIR ","","","","","","","","","","","","Wed Jan 15 14:30:43 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02468 is paralogously related to AA02796 (3e-13), AA02171 (5e-07) and AA01537 (3e-04).","","","","","","Residues 131 to 266 (E-value = 4e-16) place AA02468 in the SIS family which is described as SIS domain (PF01380)","","","","","","","","1","","","" "AA02470","1707754","1706870","885","ATGATGCGTTGCTTAGCTTTAGATATTGGCGGAACCAAAATCGCCGCCGCCATTGTTGCTCAGAACCAAGTTACACAACGGAAACAAATCCATACGCCACAGGAAAATGTGGCGGCGGCAATGCATCAGACTCTCGCGCAATTACTCACGGATTATGCAGGGCAATTTGATTACGTTGCGGTTGCTTCAACGGGCATCATCAATAAAGGAATATTGACCGCATTGAATCCGAAAAACCTGGGCGGTCTTGCTTACTTCCCGTTAAAAGAAAGCCTTTCCAAGCATACGTCCAAGCCGGTGTATTTATTAAACGATGCACAGGCGGCGACTTATGCGGAATATCAACTGCAAGATAAAAATAACATTCAAAACTTTGCTTTTATTACCGTCTCCACCGGTGTGGGAGGTGGTTTAATTTTAAATCGCCGATTACTTACCGAACCAAACGGCATTGCCGGTCATATCGGACATACCGTCGCCGATCCGAACGGGCCTGTGTGCGGTTGCGGACGCGTGGGCTGTGTGGAAGCTATTGCGTCGGGGCGTGCCATTGAAGCGGTTTCCAAACAATGGGACGATCCTTGCGAACCGAAAGAGGTGTTCGCCCGTTTTCGAAAAACGGACGAAAAAGCCACCGTACTTGTGTCCCGTTCGGCAAAAGCCATCGCCAATCTGGTGGCGGATTTGGTTATCGGTATGGATATTCAAAAAGTGGTTATCGGCGGCAGCGTAGGACTGGCGGAAGGCTATTTGCCTTTGGTTCAAGCCTATTTGCAACAAATGCCGGAAGTGTATCGCGGCGCTATCGAATCGGCTCAACTAGGGCAAGATGCGGGGCTTATCGGTGCAGCTTCTTGGGCGCTGGCGCAAATTCAGGCTGCCGCG","","","32937","MMRCLALDIGGTKIAAAIVAQNQVTQRKQIHTPQENVAAAMHQTLAQLLTDYAGQFDYVAVASTGIINKGILTALNPKNLGGLAYFPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHIGHTVADPNGPVCGCGRVGCVEAIASGRAIEAVSKQWDDPCEPKEVFARFRKTDEKATVLVSRSAKAIANLVADLVIGMDIQKVVIGGSVGLAEGYLPLVQAYLQQMPEVYRGAIESAQLGQDAGLIGAASWALAQIQAAA","1706868","From PF00480: ROK family A family of bacterial proteins has been described which groups transcriptional repressors, sugar kinases and yet uncharacterized open reading frames. This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon repressor, xylR, from Bacillus subtilis, Lactobacillus pentosus and Staphylococcus xylosus; N-acetylglucosamine repressor, nagC, from E.coli; glucokinase from Streptomyces coelicolor; fructokinase from Pediococcus pentosaceus, Streptococcus mutans and Zymomonas mobilis; allokinase and mlc from E.coli; and E.coli hypothetical proteins yajF and yhcI and the corresponding Haemophilus influenzae proteins. The repressor proteins (xylR and nagC) from this family possess an N-terminal region not present in the sugar kinases and which contains an helix-turn-helix DNA-binding motif. ","glucose kinase","Cytoplasm","","
InterPro
IPR000600
Family
ROK
PF00480\"[6-184]TROK
noIPR
unintegrated
unintegrated
G3DSA:3.30.420.160\"[105-295]Tno description
G3DSA:3.30.420.40\"[3-104]Tno description
PTHR18964\"[62-286]TROK FAMILY
PTHR18964:SF19\"[62-286]TGLUCOSE KINASE


","No hits to the COGs database.","Significant hit ( 5e-20) to 5/5 blocks of the IPB000600 family, which is described as \"ROK family\". Interpro entry for IP:IPR000600. IPB000600A 6-13 1.9 IPB000600B 99-113 0.00013 IPB000600C 130-139 0.0068 IPB000600D 152-158 0.68 IPB000600E 167-176 0.0012","Residues 68 to 141 match (2e-07) PD:PD548544 which is described as KINASE RELATED PROTEOME COMPLETE GLUCOSE ","","","","","","","","","","","Wed Jan 15 14:45:59 2003","Wed Jan 15 14:44:48 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02470 is paralogously related to AA02616 (4e-17) and AA01880 (1e-14).","","","","","","Residues 6 to 184 (E-value = 2.8e-68) place AA02470 in the ROK family which is described as ROK family (PF00480)","","","","","Titgemeyer F, Reizer J, Reizer A, Saier MH Jr.Evolutionary relationships between sugar kinases and transcriptional repressors in bacteria.Microbiology 1994 Sep;140 ( Pt 9):2349-54PMID: 7952186","","Wed Jan 15 14:44:48 2003","1","","","" "AA02472","1708469","1707771","699","ATGTCACAGCTATCTCAAAAATTATCTCATCAAGCCGTTTTCGCCCAACTTCAGAACGGATTAATTGCCTCTTGTCAGCCGGTGGATGATGGTCCGATGGATAAACCGGAAATTGTCGCTGCTATGGCGCAGGCTTCCGTTATCGGCGGGGCGGCGGGGTTGCGCATTGAAGGTGTGGACAATTTAAAAGCCGTGCGCCCGACCGTAAATGTGCCGATCATCGGTATCGTCAAACGGGATATTCCCGACAGCCCGGTACGTATCACCCCGTTTTTACAGGACATTGAAGACTTGGCGCACGCCGGAGCGGACATTATCGCCGTGGATGGCACTCGTCGCCCGCGCCCGGTAGAGATTGAAAGTGCGGTTAAAAAAATTCATGAAATGGGCTGTCTTGCCATGGCGGATTGCTCCAATCTGGAAGAAGGGTTGTATTGCCAAAAACTCGGTTTTGACATCGTGGGTAGCACCATGTCGGGCTATACCGGCGGCACCGTACCGACCGAACCGGATTATCAGTTAGTGAAAGATCTGAAAGCGGCGGGTTGCAAAGTGATGGCGGAAGGGCGTTATAACACGCCGGAACTTGCCAAAACCGCTATTGAAATCGGCGCGGATTTCGTCACCGTCGGATCGGCATTAACCCGCCTGGAACACATCGTCAGCTGGTTTGCAAGTGCGGTCAAATCGGCGGACAAA","","","25713","MSQLSQKLSHQAVFAQLQNGLIASCQPVDDGPMDKPEIVAAMAQASVIGGAAGLRIEGVDNLKAVRPTVNVPIIGIVKRDIPDSPVRITPFLQDIEDLAHAGADIIAVDGTRRPRPVEIESAVKKIHEMGCLAMADCSNLEEGLYCQKLGFDIVGSTMSGYTGGTVPTEPDYQLVKDLKAAGCKVMAEGRYNTPELAKTAIEIGADFVTVGSALTRLEHIVSWFASAVKSADK","1707769","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR007260
Family
Putative N-acetylmannosamine-6-phosphate epimerase
PF04131\"[39-230]TNanE
noIPR
unintegrated
unintegrated
PS51257\"[1-25]TPROKAR_LIPOPROTEIN


","BeTs to 4 clades of COG3010COG name: Putative N-acetylmannosamine-6-phosphate epimeraseFunctional Class: GThe phylogenetic pattern of COG3010 is -----------l--e-gh------t-Number of proteins in this genome belonging to this COG is","","Residues 7 to 41 match (1e-08) PD:PD409375 which is described as PROTEOME COMPLETE HI0145 YHCJ ","","","","","","","","","","","","Wed Jan 15 15:04:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02472 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 39 to 230 (E-value = 3.1e-141) place AA02472 in the NanE family which is described as Putative N-acetylmannosamine-6-phosphate epimerase (PF04131)","","","","","","","","1","","","" "AA02473","1708711","1709694","984","ATGAAACTAGCCAAACTTTTCCTTGCCACTGCAATTGCACTAGGTGTGACCTCTGTTGCCAATGCCGCAGAATATGATTTGAAATTCGGTATGAATGCAGGCACTTCATCCAATGAATACAAAGCTGCCGAAATGTTTGCCAAAGAAGTGAAAGAAAAATCCAACGGCAAAATTGAAATTTCCCTTTATCCAAGTTCTCAATTAGGTGACGACCGCGCCATGTTAAAGCAATTAAAAGACGGCGCATTGGACTTCACCTTTGCGGAATCCGCCCGTTTCCAATTGTTCTATCCTGAAGCGGCGGTATTTGCCCTGCCTTATGTGATCACCAATTATGAAGTGGCACAAAAGGCGTTACATGACACCGCATTCGGTAAAGATTTAATCCAAAAAATGAACAAAGAATTGGGCTTAACCTTGTTATCCCAAGCCTATAACGGCACTCGCCAAACCACTTCAAACCGCGCCATCAACGGCATTGCCGATATGAAAGGCTTGAAACTGCGCGTACCGAATGCCGCAACCAATCTGGCTTACGCCAAATATGTGGGCGCGTCTCCAACACCGATGGCATTCTCCGAAGTGTATTTAGCACTACAAACCAATTCCGTGGACGGTCAGGAAAACCCGTTGGCAACCGTGCAGGCGCAAAAATTCTATGAGGTGCAAAAATACTTGGCGATAACCAACCACATTCTGAACGACCAACTTTATTTGGTCAGCAGTGAAACCTTCGCCGACTTGCCGGAAGATTTACAAAAAGTAGTAAAAGAAGCTGCACAAAAAGCAGCGGAATATCACACCAAACTCTTTGTTGACGGAGAAAAAGAGTTAGTAACTTTCTTTGAAAAACAAGGTGTCACCGTTACGCATCCTGATTTAACACCGTTTAAAGACGCTATGAAACCTTACTACGCCGAATTTGTAAAACAAACCGGCGCAAAAGGTGAAGAGGTCCTAAAACAGATTCAAGCAATCAATAAA","","","36225","MKLAKLFLATAIALGVTSVANAAEYDLKFGMNAGTSSNEYKAAEMFAKEVKEKSNGKIEISLYPSSQLGDDRAMLKQLKDGALDFTFAESARFQLFYPEAAVFALPYVITNYEVAQKALHDTAFGKDLIQKMNKELGLTLLSQAYNGTRQTTSNRAINGIADMKGLKLRVPNAATNLAYAKYVGASPTPMAFSEVYLALQTNSVDGQENPLATVQAQKFYEVQKYLAITNHILNDQLYLVSSETFADLPEDLQKVVKEAAQKAAEYHTKLFVDGEKELVTFFEKQGVTVTHPDLTPFKDAMKPYYAEFVKQTGAKGEEVLKQIQAINK","1709692","From PF03480: Bacterial extracellular solute-binding protein.This family of proteins are involved in binding extracellular solutes for transport across the bacterial cytoplasmic membrane.","conserved hypothetical protein","Periplasm","","
InterPro
IPR004682
Family
TRAP dicarboxylate transporter- DctP subunit
PF03480\"[29-312]TSBP_bac_7
TIGR00787\"[29-286]TdctP: TRAP transporter solute receptor, Dct
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide


","BeTs to 7 clades of COG1638COG name: Dicarboxylate-binding periplasmic proteinFunctional Class: GThe phylogenetic pattern of COG1638 is --------v---bcefgh---j----Number of proteins in this genome belonging to this COG is","","Residues 209 to 252 match (2e-12) PD:PD584580 which is described as COMPLETE PROTEOME PERIPLASMIC ABC PLASMID HI0146 SOLUTE-BINDING BINDING SIGNAL PRECURSOR ","","","","","","","","","","","Wed Jan 15 15:20:50 2003","Wed Jan 15 15:10:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02473 is paralogously related to AA02385 (1e-35).","","","","","","Residues 29 to 312 (E-value = 4e-127) place AA02473 in the SBP_bac_7 family which is described as Bacterial extracellular solute-binding protein, family 7 (PF03480)","","","","","","","","1","","","" "AA02474","1709761","1711608","1848","ATGAAAATCTTTAATAAACTTGAAGAATGGATCGGTGGTGTCTTGTTCCTCGTGATATTCTGCATTCTTGTTTTACAAATTCTGTTCAGACAAGTTTTCCAATCTCCATTAATTTGGAGTGAAGAACTGGCAAAACTGCTATTCGTTTATGTGGGTATGCTTGGTATCAGTGTCGCCATCAGAAAACAAGAACATGTTTATATCGACTTTCTCACCAACTTAATGCCGCCGACAATCAAAAAAATCGTCAATTCCTTTGTGCAATTGGTGATTTTCCTCGGTGTGATTTTCTTTATCCACTTCGGCATAAAAACCTTCACAGGTGCCGGTTTCCCCATTGATGCCTTAGGCGGTATTTCGGAAAAATGGATTTACGCCTCCCTGCCGATTATTTCCGTTTTAATGCTAATTCGCTTCTTTCAAGCGCAAGCAGATAATTTCAAAGACAATAAAAGCTATCTGCCGGCGACCTTTTTCATTATAAGTGCGGTTATTTTATTGGGTATTTTATTTACCACCCCTGAATGGTACAAAGCACTGCGCATCACGGAATATGTCAAATTCGGCTCCAATGCGGTTTATGTCGCACTGGTCTTCTGGTTGGTTATCATGTTCTTAGGCGTTCCGGTGGGCTGGTCACTATTCATCACTACCCTGCTTTATTTCTCTATGACCCGTTGGAACGTGGTGAATGCGGCTTCCGAAAAACTGACCTTGAGCTTGGACAGTTTTCCACTCCTTGCCGTACCATTTTATATTCTCACCGGAATTTTAATGAACACCGGCGGTATCACTACCCGTATCTTTGATTTCGCCAAAACTTTATTAGGTCACTATACCGGCGGAATGGGACACGTTAACATCGGCGCCAGCTTATTATTCTCCGGTATGTCGGGTTCTGCCCTTGCCGATGCCGGTGGTTTAGGTCAACTGGAAATCAAAGCCATGCGCGACGCAGGTTATGACGATGACGTTTGTGGTGGTATCACTGCGGCTTCCTGTATCATCGGCCCACTAGTGCCGCCAAGTATCGCCATGATCATTTACGGCGTTATCGCCAACGAATCCATTGCAAAACTATTTATTGCCGGCTTCATCCCGGGTGTCTTAGTCACCATCGCACTAATGGGTATGAACTATTACATTGCTAAAAAACGCGGATATCCAAGAACATCGAAAACCACCCGGGAGCAACTTTGCGCCTCTTTTAAAGGGGCATTCTGGGCGATTTTAACCCCGTTATTGATTATCGGTGGTATCTTCTCCGGTTTATTCAGCCCGACAGAATCTGCGGTAGTAGCGGCCTTCTATTCCATCATTATCGGTAAATTCGTGTATAAAGAACTTACCCTTAAAATGCTGTTCAACAGCTGTGTGGAAGCCATGGCAATTACCGGCGTGGTCGCCCTGATGATCATGACGGTAACTTTCTTCGGCGACATGATCGCCCGCGAACAAGTGGCAATGCGTATTGCCAATGTGTTCGTCGCCGTGGCGGATTCCCCGTTAATGGTGCTGGTGATGATCAACGCCTTGTTACTATTCCTCGGTATGTTTATTGACGCCCTTGCCTTGCAATTCTTGGTATTACCGATGCTCATTCCAATCGCTATGCAATTTGGTATCGACCTCGTGTTCTTCGGTGTCATGACCACCTTGAACATGATGATCGGTATCTTAACACCGCCGATGGGAATGGCGTTGTTCGTGGTAGCACGGGTAGGCAATATGTCCGTCTCCACCGTTACCAAAGGGGTATTACCATTCTTAGTGCCGATTTTTATTACTTTGGTATTAATCACCATCTTCCCGCAAATTATTACCTTTGTGCCGAATTTATTAATACCT","","","67790","MKIFNKLEEWIGGVLFLVIFCILVLQILFRQVFQSPLIWSEELAKLLFVYVGMLGISVAIRKQEHVYIDFLTNLMPPTIKKIVNSFVQLVIFLGVIFFIHFGIKTFTGAGFPIDALGGISEKWIYASLPIISVLMLIRFFQAQADNFKDNKSYLPATFFIISAVILLGILFTTPEWYKALRITEYVKFGSNAVYVALVFWLVIMFLGVPVGWSLFITTLLYFSMTRWNVVNAASEKLTLSLDSFPLLAVPFYILTGILMNTGGITTRIFDFAKTLLGHYTGGMGHVNIGASLLFSGMSGSALADAGGLGQLEIKAMRDAGYDDDVCGGITAASCIIGPLVPPSIAMIIYGVIANESIAKLFIAGFIPGVLVTIALMGMNYYIAKKRGYPRTSKTTREQLCASFKGAFWAILTPLLIIGGIFSGLFSPTESAVVAAFYSIIIGKFVYKELTLKMLFNSCVEAMAITGVVALMIMTVTFFGDMIAREQVAMRIANVFVAVADSPLMVLVMINALLLFLGMFIDALALQFLVLPMLIPIAMQFGIDLVFFGVMTTLNMMIGILTPPMGMALFVVARVGNMSVSTVTKGVLPFLVPIFITLVLITIFPQIITFVPNLLIP","1711606","","transmembrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR004681
Family
TRAP dicarboxylate transporter, DctM subunit
TIGR00786\"[207-611]TdctM: TRAP transporter, DctM subunit
InterPro
IPR007387
Family
Tripartite ATP-independent periplasmic transporter, DctQ component
PF04290\"[19-149]TDctQ
InterPro
IPR010656
Domain
TRAP C4-dicarboxylate transport system permease DctM subunit
PF06808\"[197-607]TDctM
noIPR
unintegrated
unintegrated
signalp\"[1-34]?signal-peptide
tmhmm\"[10-30]?\"[46-61]?\"[82-102]?\"[124-142]?\"[152-172]?\"[191-223]?\"[244-264]?\"[288-308]?\"[329-351]?\"[357-377]?\"[405-425]?\"[431-446]?\"[461-479]?\"[498-518]?\"[528-550]?\"[556-576]?\"[586-606]?transmembrane_regions


","No hits to the COGs database.","","Residues 382 to 442 match (7e-21) PD:PD009429 which is described as PROTEOME COMPLETE MEMBRANE C4-DICARBOXYLATE LARGE TRANSMEMBRANE PLASMID INNER PERMEASE INTEGRAL ","","","","","","","","","","","","Wed Jan 15 15:34:25 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02474 is paralogously related to AA02387 (2e-79) and AA02643 (0.001).","","","","","","Residues 322 to 479 (E-value = 1.3e-52) place AA02474 in the DedA family which is described as DedA family (PF00597)","","","","","","","","1","","","" "AA02475","1711620","1711718","99","GTGCGGTTGAAAAACGCTGTAAATTTTAACCGCACTTTAAACCCTAGGGTGCAACCGGTTGCGCCCTACCACAAAAAATCTATTCATGCCGTTTACGAA","","","3843","VRLKNAVNFNRTLNPRVQPVAPYHKKSIHAVYE","1711718","","hypothetical protein","Cytoplasm, Extracellular","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 09:55:38 2004","Wed Feb 25 09:55:38 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02475 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 09:55:38 2004","","","","","","","","","","","","","1","","","" "AA02476","1711750","1712877","1128","ATGACATTCAAAAAAACAACATTAGCGAATTTATTTTTTGCTGCAACGGCTTTTGCCACGACTGCGCAAGCAGCTTATCCCGATTTACCCGTGGCGATTAAAAGCGGCGCAGGCGCGTTAATCAACGATACGGTTTATGTGGGCTTAGGCTCGGGCGGAGATAAATTTTATGCCTTGGATTTAAAGACCCCGAACGCCCGATGGAAAGAAATTGCCGCGTTCCCGGGTGGCGAACGCAACCAACCTGTCGCGGCGGCAGTTGATGGCAAATTGTACATTTTCGGCGGCTTACAAAAAAATGAAAAAGGCGAATTACAACTGGTCAATGACGCTTACAGCTACAACCCTGCCGACAATACCTGGAACAAATTGCCAACCCGTTCACCGCGTGGTCTAGTAGGTTCCAGCGGTGCTTCTCACGGCGACAAAGTGTATATCATCGGCGGTTCTAATCTCTCTATTTTCAACGGCTTCTTCCAAGACACCGTCGCCGCCGGTGAAGACAAAGCGAAAAAAGACGACATTGCCAAAGCCTATTTTGAACAACGCCCTGAAGATTATTTCTTCACCACCGAACTGCTCAGCTATGAACCGTCCACCAACAAATGGCGCAACGAAGGTCGCGTGCCGTTCTCCGGACGTGCCGGTGCGGCGTTTACTATTCAAGGCAATGAGTTAATCGTTGTCAACGGCGAAATCAAACCGGGCTTGCGCACAGCGGAAACCCATCAAGGTAAATTCACCGACAAAGGCGTGCAATGGAAAAATCTACCTGATCTGCCGGCACCAAAAGGGCAAAGCCAAGACGGTTTAGCGGGTGCCATGGCGGGCTATAGCCACGGGCATTATTTAGTCACCGGTGGCGCAAACTTCCCGGGCTCCGTAAAACAATTCAAAGAAGGCATGCTTCACGCCCACAAAGGCTTAAGCAAGGCCTGGCACAAAGACATTTACACCTTAAACAACGGTAAATGGCAAATTATCGGTGAATTGCCTGCCGGTATCGGCTATGGTGTTGCGGTGTCTTACAACAATCAAGTGCTTTTAATCGGTGGTGAAACCAACGGCGGCAAAGCCTTAACTTCCGTACAAAGCATGAGCTACGACGGCAAAAAATTAAGTGTCGAA","","","40291","MTFKKTTLANLFFAATAFATTAQAAYPDLPVAIKSGAGALINDTVYVGLGSGGDKFYALDLKTPNARWKEIAAFPGGERNQPVAAAVDGKLYIFGGLQKNEKGELQLVNDAYSYNPADNTWNKLPTRSPRGLVGSSGASHGDKVYIIGGSNLSIFNGFFQDTVAAGEDKAKKDDIAKAYFEQRPEDYFFTTELLSYEPSTNKWRNEGRVPFSGRAGAAFTIQGNELIVVNGEIKPGLRTAETHQGKFTDKGVQWKNLPDLPAPKGQSQDGLAGAMAGYSHGHYLVTGGANFPGSVKQFKEGMLHAHKGLSKAWHKDIYTLNNGKWQIIGELPAGIGYGVAVSYNNQVLLIGGETNGGKALTSVQSMSYDGKKLSVE","1712875","","conserved hypothetical protein","Periplasm, Extracellular","","
InterPro
IPR006652
Repeat
Kelch repeat
PF01344\"[78-128]TKelch_1
noIPR
unintegrated
unintegrated
G3DSA:2.120.10.80\"[67-364]Tno description
PTHR23230\"[61-151]T\"[189-290]T\"[308-367]TKELCH-RELATED PROTEIN
PTHR23230:SF184\"[61-151]T\"[189-290]T\"[308-367]TKELCH-RELATED
signalp\"[1-24]?signal-peptide
tmhmm\"[9-27]?transmembrane_regions


","BeTs to 3 clades of COG3055COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3055 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 26 to 123 match (4e-13) PD:PD482642 which is described as COMPLETE PROTEOME BMEII0856 REPEAT SIGNAL PRECURSOR VC1774 ","","","","","","","","","","","","Wed Jan 15 16:30:38 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02476 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 78 to 128 (E-value = 8.2e-10) place AA02476 in the Kelch family which is described as Kelch motif (PF01344)","","","","","","","","1","","","" "AA02477","1713129","1713431","303","ATGAGTGTTTTAAGTTATGCCCAAAAAATCGGGCAAGCCTTAATGGTACCCGTTGCCGTTTTGCCGGCAGCCGCCGTATTAATGGGGATCGGCTATTGGCTTGACCCGGACGGCTGGGGCGCAAACAGCCAACTTGCCGCCTTATTAATCAAGTCCGGCGCGGCAATCATCGATAACATGGGCTTATTATTCGCCGTGGGCGTAGCATTCGGGTTGTCCAAAGACAAGCACGGTTCTGCTGCGCTTTCCGGTTTAGTGGGCTATTATGTGGTCACTACCCTACTCGCCCCTGGCGGCGTAGCG","","","10129","MSVLSYAQKIGQALMVPVAVLPAAAVLMGIGYWLDPDGWGANSQLAALLIKSGAAIIDNMGLLFAVGVAFGLSKDKHGSAALSGLVGYYVVTTLLAPGGVA","1713429","From Genbank:[gi:131500] This protein is a component of the phosphoenolpyruvate-dependent sugar system (PTS), a major carbohydrate active-transport system. The IICD domains contain the sugar binding site and the transmembrane channel.The IIA domain contains the primary phosphorylation site (the donor is phospho-HPR). The IIA transfers its phosphoryl group to the IIB domain which finally transfers it to the sugar. ","PTS system, N-acetylglucosamine-permease IIABC component","Inner membrane, Extracellular","","
InterPro
IPR003352
Domain
Phosphotransferase system, EIIC
PF02378\"[11-101]TPTS_EIIC
InterPro
IPR013013
Domain
Phosphotransferase system, EIIC component, type 1
PS51103\"[1-101]TPTS_EIIC_TYPE_1
noIPR
unintegrated
unintegrated
signalp\"[1-25]?signal-peptide
tmhmm\"[15-35]?\"[54-72]?transmembrane_regions


","No hits to the COGs database.","","Residues 52 to 101 match (4e-14) PD:PD001764 which is described as COMPONENT PTS SYSTEM PROTEOME COMPLETE PHOSPHOTRANSFERASE IIABC ENZYME TRANSFERASE SYSTEM ","","","","","","","","","","","Wed Jan 15 16:40:45 2003","Wed Jan 15 16:51:36 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02477 is paralogously related to AA01875 (1e-11).","","","","","","","","","","","Rogers,M.J., Ohgi,T., Plumbridge,J. and Soll,D.Nucleotide sequences of the Escherichia coli nagE and nagB genes:the structural genes for the N-acetylglucosamine transport proteinof the bacterial phosphoenolpyruvate: sugar phosphotransferasesystem and for glucosamine-6-phosphate deaminaseGene 62 (2), 197-207 (1988)PubMed: 3284790Peri,K.G. and Waygood,E.B.Sequence of cloned enzyme IIN-acetylglucosamine of thephosphoenolpyruvate:N-acetylglucosamine phosphotransferase systemof Escherichia coliBiochemistry 27 (16), 6054-6061 (1988)PubMed: 3056518","","Wed Jan 15 16:40:45 2003","1","","","" "AA02478","1713459","1714592","1134","GTGCCTGCTGCTTTCGGCAAAATCAACAACCAATTTATCGGTATTTTAATCGGTGTACTTTCCGCCGAACTTTACAACCGTTTTTACCAAGTGGAATTGCCGAAAGCCTTATCATTCTTCAGCGGAAAACGTTTAGTGCCGATTGTAGTGTCTTTCGCCATGATCGCCTTGTCTTTCGTTTTACTCTATGTATGGCCTTATATCTTCAATGCCTTGGTGTCCTTCGGGGAGTCCATCAAAGACCTCGGTGCAGTGGGCGCAGGGATTTACGGCTTCTTCAACCGTTTATTAATCCCGGTTGGCTTACACCACGCCTTAAACTCCGTATTCTGGTTTGACGTTGCGGGCATTAACGATATTCCGAATTTCTTAGGCGGCGCCAAATCCATTGCCGAAGGCACGGCAACCATGGGCATCACCGGGATGTATCAAGCGGGCTTTTTCCCGGTCATGATGTTCGGCTTACCGGGCGCGGCACTTGCCATTTACCAATGTGCGAAACCAAGCCAAAAAGTGAAAGTCGCCTCCATCATGCTCGCCGGTGCTTTTGCTTCCTTCTTCACCGGTATCACCGAACCGCTCGAATTTTCTTTCATGTTCGTGGCGCCGATTCTTTATGTATTGCACGCATTACTCACCGGGATTTCCGTATTTATCGCCGCCAGTATGCACTGGATCGCAGGCTTCGGTTTCAGTGCCGGTTTGGTGGATATGGTACTTTCCTCCCGCAACCCACTCGCCGTTGACTGGTATATGTTACCGGTGCAAGGTTTAGTGTTCTTCGCCATTTACTATTTGGTGTTCCGTTTTGCCATCCAAGCCTTTAACTTAAAAACCATCGGTCGCACGGAAGAAACGGAAGAATCCGTCCCTGCACCAAGCGTAAACAATCAATCCCGTGAAGAAAGGGCGATCAAATTTATCGACGCTTTAGGCGGTGCCGACAATTTCAAAACCATTGACGCCTGTATTACCCGCTTGCGCTTAACCTTGGTTGATCGAAATAAAATCAACGAGGAACAACTCAAATCCCTCGGTTCTAAAAGCAATGTCAAACTAGGTAATGACGGGTTACAAGTGATTCTTGGCCCCGAAGCAGAATTGATGGCGGAGGCGATTAAAGCAAAAGTGAAG","","","41138","VPAAFGKINNQFIGILIGVLSAELYNRFYQVELPKALSFFSGKRLVPIVVSFAMIALSFVLLYVWPYIFNALVSFGESIKDLGAVGAGIYGFFNRLLIPVGLHHALNSVFWFDVAGINDIPNFLGGAKSIAEGTATMGITGMYQAGFFPVMMFGLPGAALAIYQCAKPSQKVKVASIMLAGAFASFFTGITEPLEFSFMFVAPILYVLHALLTGISVFIAASMHWIAGFGFSAGLVDMVLSSRNPLAVDWYMLPVQGLVFFAIYYLVFRFAIQAFNLKTIGRTEETEESVPAPSVNNQSREERAIKFIDALGGADNFKTIDACITRLRLTLVDRNKINEEQLKSLGSKSNVKLGNDGLQVILGPEAELMAEAIKAKVK","1714590","From PF02378The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of avariety of metabolic and transcriptional processes. The PTS catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The general mechanism of the PTS is the following: a phosphoryl group from phosphoenolpyruvate (PEP) is transferred to enzyme-I (EI) of PTS which in turn transfers it to a phosphoryl carrier protein (HPr). Phospho-HPr then transfers the phosphoryl group to a sugar-specific permease which consists of at least three structurally distinct domains (IIA, IIB, and IIC) which can either be fused together in a single polypeptide chain or exist as two orthree interactive chains, formerly called enzymes II (EII) and III (EIII). The IIC domain catalyzes the transfer of a phosphoryl group from IIB to the sugar substrate. ","PTS system, N-acetylglucosamine-specific enzyme IIABC","Inner membrane, Cytoplasm","","
InterPro
IPR001996
Domain
Phosphotransferase system, EIIB
PF00367\"[304-338]TPTS_EIIB
PS51098\"[301-378]TPTS_EIIB_TYPE_1
PS01035\"[316-333]?PTS_EIIB_TYPE_1_CYS
InterPro
IPR003352
Domain
Phosphotransferase system, EIIC
PF02378\"[1-214]TPTS_EIIC
InterPro
IPR011535
Domain
Phosphotransferase system, glucose-like IIB component
TIGR00826\"[273-363]TEIIB_glc: PTS system, glucose-like IIB comp
InterPro
IPR013013
Domain
Phosphotransferase system, EIIC component, type 1
PS51103\"[1-284]TPTS_EIIC_TYPE_1
noIPR
unintegrated
unintegrated
G3DSA:3.30.1360.60\"[289-377]Tno description
tmhmm\"[45-65]?\"[145-163]?\"[178-200]?\"[206-226]?\"[247-267]?transmembrane_regions


","BeTs to 6 clades of COG1263COG name: Phosphotransferase system IIC components, glucose/maltose/N-acetylglucosamine-specificFunctional Class: GThe phylogenetic pattern of COG1263 is -----------lb-efgh---j--twNumber of proteins in this genome belonging to this COG is","Significant hit ( 3.2e-19) to 2/2 blocks of the IPB001996 family, which is described as \"PTS (phosphotransferase system) EIIB domain\". Interpro entry for IP:IPR001996. IPB001996A 304-338 1.8e-16 IPB001996B 354-366 0.38","Residues 250 to 316 match (9e-13) PD:PD149718 which is described as COMPONENT PTS COMPLETE PROTEOME SYSTEM PHOSPHOTRANSFERASE IIABC ENZYME TRANSFERASE SYSTEM ","","","","","","","","","","","Wed Jan 15 16:59:23 2003","Wed Jan 15 16:55:17 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02478 is paralogously related to AA01876 (5e-40) and AA01875 (7e-20).","","","","","","Residues 304 to 338 (E-value = 3.2e-12) place AA02478 in the PTS_EIIB family which is described as phosphotransferase system, EIIB (PF00367)","","","","","Saier MH Jr, Reizer J.Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.J Bacteriol 1992 Mar;174(5):1433-8PMID: 1537788","","Wed Jan 15 16:59:23 2003","1","","","" "AA02479","1716341","1715274","1068","ATGAAAAAAACTGTAATCGCATTAGCTACTACTGCGGCTTTAGCTGCATCAGTAGCGACAATTGTGCAGGCAGCATCGCAAGCAAATACCTTTTATGCGGGGGCAAAAGCCGGCTGGGCATCTGTCCGTCACGGTTTAAATCAATATCAGTATGAGCAGGACGGCACAGTAGTGGGTAAAGCCAAGAAAAACTCGGAATCCTATGGCATCTTTGCCGGCTACCAAATTACCGATAATTTCGCTGTTGAAGCAGGGTATGAATTCTTCGGTCGCGGTAAAGTAAAAGAAGCTACCGGAGAAAAACGAATTACCGCTCATGGTTCCAGCTTGTCTCTTAAAGCAAGCTATCCTGTATTGCATAATTTAGATCTTTATGCACGTGCAGGTGCAGCATTAATCCGTGTTGATTACAAAGATAACACTTTCGGAGAAACTCATAAATTCCATGATTTAAAAGTTTCTCCGGTATTTGCCGGGGGGCTTGAATATGCCATTCTTCCTGAATTGGCATTACGTTTGGAGTATCAATGGGTGAGCCGAGTAGGCAATTTCGGCAAAGCAGAAAGAAAAGCCAATTATTATGAAAATAACGAATCTGATGTTCGCTATTCTCCGGATATTGGTTCCGTAGCGCTAGGTTTATCTTACCGCTTTGGTCAGGGACCGGCGCCTGTTATTGCTCCTGAAGTAGTTAACAAAGTATTCAATTTGAATTCTGATGTGACTTTTGCGTTCAACAAAGCGAATTTAAAACCGCAGGCGCAAAAAACTTTGGATGGCATTTCCCACGAAATTGCACAAGTAAATAACGCTAACGTTCAAGTTGCAGGTTATACAGACCGTATCGGTTCCGACGCTTACAACCAAAAATTATCCCAAAGACGTGCTGAAACTGTAGCAAATTACCTTGTATCTAAAGGTGTTTCTCAACAGGCAATTTCCGCTACCGGTTACGGTAAAGCAAACCCGGTTACCGGCAATAAATGTGACACGGTTAAAGGTCGCAAAGCGCTGATTGCGTGCTTGGCTGATGACCGTCGTGTAGAAATTGCGGTAAACGGCACGAAA","","","38427","MKKTVIALATTAALAASVATIVQAASQANTFYAGAKAGWASVRHGLNQYQYEQDGTVVGKAKKNSESYGIFAGYQITDNFAVEAGYEFFGRGKVKEATGEKRITAHGSSLSLKASYPVLHNLDLYARAGAALIRVDYKDNTFGETHKFHDLKVSPVFAGGLEYAILPELALRLEYQWVSRVGNFGKAERKANYYENNESDVRYSPDIGSVALGLSYRFGQGPAPVIAPEVVNKVFNLNSDVTFAFNKANLKPQAQKTLDGISHEIAQVNNANVQVAGYTDRIGSDAYNQKLSQRRAETVANYLVSKGVSQQAISATGYGKANPVTGNKCDTVKGRKALIACLADDRRVEIAVNGTK","1715272","","outer membrane protein 34","Outer membrane, Extracellular","","
InterPro
IPR000498
Domain
OmpA-like transmembrane region
PF01389\"[11-222]TOmpA_membrane
InterPro
IPR002368
Family
OmpA outer membrane protein
PR01022\"[117-133]T\"[231-246]T\"[297-316]T\"[331-344]TOUTRMMBRANEA
InterPro
IPR006664
Domain
Bacterial outer membrane protein
PR01021\"[243-265]T\"[273-288]T\"[288-304]TOMPADOMAIN
InterPro
IPR006665
Domain
OmpA/MotB
PD000930\"[231-299]TQ9S5J9_ACTAC_Q9S5J9;
PF00691\"[242-337]TOmpA
PS51123\"[230-356]TOMPA_2
InterPro
IPR006690
Domain
OmpA-like
PS01068\"[275-319]TOMPA_1
noIPR
unintegrated
unintegrated
G3DSA:2.40.160.20\"[25-219]Tno description
G3DSA:3.30.1330.60\"[225-356]Tno description
signalp\"[1-24]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.3e-57) to 4/4 blocks of the IPB001145 family, which is described as \"Bacterial outer membrane protein\". Interpro entry for IP:IPR001145. IPB001145A 110-138 9.5e-08 IPB001145B 239-266 1.2e-09 IPB001145C 273-319 1e-31 IPB001145D 341-352 0.00028Significant hit ( 2e-19) to 5/7 blocks of the PR01022 family, which is described as \"Outer membrane protein A signature\". Prints database entry for PR:PR01022. PR01022A 117-133 7.4 PR01022C 206-220 0.0004 PR01022D 231-246 0.021 PR01022F 297-316 0.021 PR01022G 331-344 0.0042","Residues 29 to 101 match (6e-07) PD:PD525046 which is described as OMPA2 ","","","","","","","","","","","","Wed Jan 15 17:02:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02479 is paralogously related to AA02458 (1e-145), AA02027 (3e-20) and AA02829 (1e-09).","","","","","","Residues 242 to 337 (E-value = 6.7e-43) place AA02479 in the OmpA family which is described as OmpA family (PF00691)","","","","White,P.A., Nair,S.P., Kim,M.J., Wilson,M. and Henderson,B. Molecular characterization of an outer membrane protein of Actinobacillus actinomycetemcomitans belonging to the OmpA family Infect. Immun. 66 (1), 369-372 (1998) PubMed: 9423883","Klesney-Tait,J., Hiltke,T.J., Maciver,I., Spinola,S.M., Radolf,J.D. and Hansen,E.J. The major outer membrane protein of Haemophilus ducreyi consists of two OmpA homologs. J. Bacteriol. 179 (5), 1764-1773 (1997) PubMed: 9045839.","Wed Jan 15 17:02:44 2003","Wed Jan 15 17:02:44 2003","1","","","" "AA02480","1718502","1716571","1932","TTGGCACATCAAACCTTGCTTGGGGTAACAGGTTCAGGCAAAACCTTTACCATTGCCAATGTGATTGCGCAATTGAATCGCCCTGCGATGGTGTTGGCACCGAACAAAACCCTTGCCGCCCAGCTTTATGCCGAAATGAAGGATTTTTTCCCGGAAAATGCGGTGGAATATTTTGTTTCTTACTATGATTATTATCAGCCCGAAGCCTATGTGCCGAGTAGCGATACTTTTATTGAGAAAGACGCGTCTATTAATGATCAAATTGAACAAATGCGACTTTCCGCCACAAAATCTTTCTTAGAACGGCGCGATACTATTGTAGTGGCGTCCGTGTCCGCTATTTATGGTTTAGGAGACCCCGATTCCTATTTAAAAATGATGCTGCATTTGCAACAAGGCGCGATTATTAATCAGCGCCAAATCTTGGCAAAATTGGCAGAGTTGCAATATACCCGTAATGATCAGGCGTTTCAGCGCGGAACGTTCCGTGTACGGGGAGAAATTATTGATATTTTCCCGGCGGAATCGGACGATCGGGCGGTACGTATCGAATTATTTGATGATGAAATCGAACGCTTGAGTTTATTTGATCCGCTCACCGGCAGCAGCTTCGGCACGGTGCCGCGCTTTACCGTTTATCCGAAAACGCACTATGTCACACCGCGCGAGCGTATCTTGGATGCCATCGAAAAAATTAAACTGGAATTGGCGCAACGGCGGGAGTATTTCATTAAAGAAAATAAATTATTGGAAGAGCAGCGTATCAGCCAACGTACCCAATTTGATATTGAGATGATGAATGAACTCGGTTATTGCTCGGGCATTGAAAACTATTCCCGCTATTTATCGGGTAGAAATGAGGGCGAACCGCCACCGACCTTATTTGATTATATGCCGTCTGACGCAATTTTGATTATTGACGAATCCCACGTCACCGTGCCACAAATCGGTGGGATGTATCGCGGCGATCGCTCCCGTAAAGAAACCTTGGTGGAATATGGTTTTCGTCTGCCTTCTGCGTTGGATAACCGTCCGTTACGTTTTGAAGAATTTGAACGTTTGGCACCGCAAACCATTTATGTTTCCGCCACACCGGGACCGTATGAACTGGAAAAATCCGGTGGGGAAATTATCGACCAAGTAGTGCGTCCGACAGGTTTGCTTGATCCGCAAATTGAAATTCGCCCGGTATCTATTCAGGTGGATGATTTACTTTCCGAAGCACGCCACAGAGCGGATAAAAATGAACGCGTTTTAGTGACGACATTAACGAAGAAAATGGCGGAAGATCTTACCGACTATTTAGATGAACATGGTATTCGCGTACGTTATTTGCATTCTGATATTGATACTGTCGAACGGGTGGAAATTATTCGTGATTTGCGCTTGGGGGAATTTGATGTTTTAGTCGGCATTAACTTATTACGGGAAGGTTTAGATATTCCGGAAGTGTCTTTAGTGGCAATTTTAGATGCGGATAAAGAAGGTTTTTTACGTTCCGAGCGTTCATTAATTCAAACGATCGGACGTGCTGCGCGAAATTTACACGGAAAAGCCATTTTGTATGCGGATAATATAACCAAATCAATGGAGAAAGCTATTACCGAAACCAATCGTCGGCGTGAGAAACAAGCAAAATATAATGAAGCACAGGGCATTGTGCCGCAGGCATTAAATAAAAAGGTAGGCGAGTTGTTAGATATCGGTCAGGGTGCCAATCAGAAAGCCAAAGCCAATAAACAACGTGGAAAAACGGTGGCAGAACCGACCGCACTTTATACAACGCCGAAATCACCGAAAGAATATCAGCAACAGATTAAGAAACTTGAGCAGCAAATGTATAAATTTGCACAGGATTTGGAATTTGAGAAAGCTGCTGCAACGCGCGATCAGTTACAACAATTACGGGAAAGTTTTATGTTATCAAGTGAG","","","77503","LAHQTLLGVTGSGKTFTIANVIAQLNRPAMVLAPNKTLAAQLYAEMKDFFPENAVEYFVSYYDYYQPEAYVPSSDTFIEKDASINDQIEQMRLSATKSFLERRDTIVVASVSAIYGLGDPDSYLKMMLHLQQGAIINQRQILAKLAELQYTRNDQAFQRGTFRVRGEIIDIFPAESDDRAVRIELFDDEIERLSLFDPLTGSSFGTVPRFTVYPKTHYVTPRERILDAIEKIKLELAQRREYFIKENKLLEEQRISQRTQFDIEMMNELGYCSGIENYSRYLSGRNEGEPPPTLFDYMPSDAILIIDESHVTVPQIGGMYRGDRSRKETLVEYGFRLPSALDNRPLRFEEFERLAPQTIYVSATPGPYELEKSGGEIIDQVVRPTGLLDPQIEIRPVSIQVDDLLSEARHRADKNERVLVTTLTKKMAEDLTDYLDEHGIRVRYLHSDIDTVERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLVAILDADKEGFLRSERSLIQTIGRAARNLHGKAILYADNITKSMEKAITETNRRREKQAKYNEAQGIVPQALNKKVGELLDIGQGANQKAKANKQRGKTVAEPTALYTTPKSPKEYQQQIKKLEQQMYKFAQDLEFEKAAATRDQLQQLRESFMLSSE","1716569","From Genbank:[gi:1174918] The ABC excision nuclease is a DNA repair enzyme that catalyzes the excision reaction of uv-damaged nucleotide segments producing oligomers having the modified base(s).uvrB stimulates the ATPase activity of uvrA in the presence of uv-irradiated double-stranded DNA. It also enhances the ability of uvrA to bind to uv-irradiated duplex DNA. ","excinuclease ABC subunit B","Cytoplasm","","
InterPro
IPR001650
Domain
Helicase, C-terminal
PF00271\"[434-515]THelicase_C
SM00490\"[429-515]THELICc
PS51194\"[400-553]THELICASE_CTER
InterPro
IPR001943
Domain
UvrB/UvrC protein
PF02151\"[603-638]TUVR
PS50151\"[603-638]TUVR
InterPro
IPR004807
Family
Excinuclease ABC, B subunit
TIGR00631\"[1-636]Tuvrb: excinuclease ABC, B subunit
InterPro
IPR006935
Family
Type III restriction enzyme, res subunit
PF04851\"[10-53]TResIII
InterPro
IPR014001
Domain
DEAD-like helicases, N-terminal
SM00487\"[1-395]TDEXDc
InterPro
IPR014021
Domain
Helicase superfamily 1 and 2 ATP-binding
PS51192\"[1-166]THELICASE_ATP_BIND_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[1-142]T\"[256-379]T\"[381-548]Tno description
G3DSA:4.10.860.10\"[598-643]Tno description
PTHR10967\"[402-487]TDEAD BOX ATP-DEPENDENT RNA HELICASE
PTHR10967:SF8\"[402-487]TATP-DEPENDENT HELICASE DDX7


","BeTs to 20 clades of COG0556COG name: Helicase subunit of the DNA excision repair complexFunctional Class: LThe phylogenetic pattern of COG0556 is -om----qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 3.8e-21) to 3/3 blocks of the IPB001943 family, which is described as \"UvrB/uvrC motif\". Interpro entry for IP:IPR001943. IPB001943A 4-13 0.00067 IPB001943B 473-482 0.0083 IPB001943C 609-636 4.7e-11","Residues 424 to 470 match (1e-09) PD:PD527854 which is described as ATP-BINDING B EXCISION ABC NUCLEASE SUBUNIT EXCINUCLEASE SOS PROTEOME REPAIR ","","","","","","","","","","","Thu Jan 16 07:40:28 2003","Thu Jan 16 07:40:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02480 is paralogously related to AA00861 (5e-11), AA00148 (1e-08), AA00506 (6e-06), AA02303 (2e-05), AA01335 (5e-04) and AA00927 (8e-04).","","","","","","Residues 603 to 638 (E-value = 3.7e-11) place AA02480 in the UVR family which is described as UvrB/uvrC motif (PF02151)","","","","","Backendorf,C., Spaink,H., Barbeiro,A.P. and van de Putte,P. Structure of the uvrB gene of Escherichia coli. Homology with other DNA repair enzymes and characterization of the uvrB5 mutation Nucleic Acids Res. 14 (7), 2877-2890 (1986) PubMed: 3008099 Arikan,E., Kulkarni,M.S., Thomas,D.C. and Sancar,A. Sequences of the E. coli uvrB gene and protein Nucleic Acids Res. 14 (6), 2637-2650 (1986) PubMed: 3515321 Rivera,E., Vila,L. and Barbe,J. The uvrB gene of Pseudomonas aeruginosa is not DNA damage inducible J. Bacteriol. 178 (18), 5550-5554 (1996) PubMed: 8808952 Van Houten B, Snowden A.Mechanism of action of the Escherichia coli UvrABC nuclease: clues to the damage recognition problem.Bioessays 1993 Jan;15(1):51-9PMID: 8466476","","Thu Jan 16 07:40:28 2003","1","","","" "AA02481","1720163","1719225","939","GTGTGGCAGCGGGAATTTAATCAACTGATTTCCGGTTACTTGCACGAAATCAAGCAACAGCCCGTGTATGCCGGCAGCCTGCTGATTGCTGTTAGTTTTTTATACGGTGTGTTTCATGCGCTGGGTCCGGGACACGGTAAATTTATTATTGCCGGTTATTTAGCCACCCATCAAACCAAGCTCGGGCGCAGTATGCAAATCACGTTCTTTTCTTCTTTAACGCAGGGCGTGGTGGCAATTTCGGCGGTGTCAATCGTGGTTTTGCTGCTTCAGCTTTCTTCCGCTTATTTTAATTTAAGCCAATTATGGCTGGAGCGAACCGCTTATGCGTTAGTGATTTTATTGGGATTAAATTGGTGTTGGAAAAGCGGGAAAACGCTGTTGAAGCAACATCGACAAACGAAGCAGCAACTGCAAATCAAAAAAATTGAAGGCGGTTTGGTAAATGAAATGCGTGTCGGTTCATTGATCGCAGGAAAAAGTGCGGTCAGAATTTCAGGTGTTTTTAACGGGCATACGGAACACCACGAAAATTGCGGTTGCGGGCATCAACATGTGCCGAACCCCGAACGACTCAATCAAAGTACCAACATCAAAGAAAGTTTGCTGATTATTTTGAGTATCGGCATGCGCCCCTGTTCCGGCGCGATTTTCGTACTGTTTCTGGCGTATATGTTGGATCTCTATGCTTGGGGCGTGATAGCGACACTGGCAATGGCTCTCGGCACAGGAATGACATTATCGGCCTTTGCGTTGTTGGTGCGCTATGCCCGATCCACTGCCGTGAAAATGGCGCAGTGGTATCGCCTGCCGTTTGCCAATGTGAATACGGAAGCCTTAATGAAATGCCTTGCCGGCATCATATTGATTTTCTTTGCGATGAGTTTACTTTATGGCACCACATTGCCGATAAGTGGCGGGGCAGCATTATTTGTTCGA","","","38995","VWQREFNQLISGYLHEIKQQPVYAGSLLIAVSFLYGVFHALGPGHGKFIIAGYLATHQTKLGRSMQITFFSSLTQGVVAISAVSIVVLLLQLSSAYFNLSQLWLERTAYALVILLGLNWCWKSGKTLLKQHRQTKQQLQIKKIEGGLVNEMRVGSLIAGKSAVRISGVFNGHTEHHENCGCGHQHVPNPERLNQSTNIKESLLIILSIGMRPCSGAIFVLFLAYMLDLYAWGVIATLAMALGTGMTLSAFALLVRYARSTAVKMAQWYRLPFANVNTEALMKCLAGIILIFFAMSLLYGTTLPISGGAALFVR","1719223","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR011541
Family
Nickel/cobalt transporter, high-affinity
PF03824\"[25-303]TNicO
noIPR
unintegrated
unintegrated
tmhmm\"[22-42]?\"[69-89]?\"[103-121]?\"[202-224]?\"[234-254]?\"[279-299]?transmembrane_regions


","No hits to the COGs database.","","Residues 209 to 290 match (3e-20) PD:PD472652 which is described as COMPLETE PROTEOME MEMBRANE TRANSMEMBRANE SMC02986 HI1248 PLASMID PM0427 RA0898 MLR2980 ","","","","","","","","","","","","Thu Jan 16 07:58:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02481 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 25 to 303 (E-value = 1.4e-57) place AA02481 in the NicO family which is described as High-affinity nickel-transport protein (PF03824)","","","","","","","","1","","","" "AA02482","1720900","1720271","630","GTGAAGAAACTTTTTTTATTGCTATTGTCTTTGTTATCCGCTCAGTATGTTTTTGCCCATCCTCATGCTTTCATTGAGATAAAAACCAAAACCTTGGTAGAGAATCAACAATTAGTCGGTTTTTCAATGCAGTGGATTTTAGACGAACCCAGCTCCGCAGCGGTTTTATACGATTTAAGACAAACCAAAGGCGATAAAAACGCGCGACAAAAGCTCATTGATGAAGTCATGGGCAATGTGGTGAATGAGCATTATTTTAGTTATTTTTTTGACAAGCAGGGCAATAAAATTAAATACCGAGCCAAACCGCAAAACTACGGTATGAAATCCAATGGTTCACAAGTGATGTACTTTTTCGATTTCATGTTGTCTAAACCGCAGCCCTTGACAGATAACGAATATACTTTAAGTACTTACGATCCAACCTATTATGTGTCCATGTATTACGGCGAACCGACCAAAAGTGCGGTGGATTTTTCCGCGCTGCCGGCAAATTGCCGGGGACAGGTGCTTGAGCCGCAAGTGGATGAAAAAGTGAAACAATACGCCTCATCATTAGATCAAACGCAACGTGATGAGGACAATACATTGGGTGCGCTATTTGCACAAAAAGTGCGGTTGATTTGCCGT","","","26832","VKKLFLLLLSLLSAQYVFAHPHAFIEIKTKTLVENQQLVGFSMQWILDEPSSAAVLYDLRQTKGDKNARQKLIDEVMGNVVNEHYFSYFFDKQGNKIKYRAKPQNYGMKSNGSQVMYFFDFMLSKPQPLTDNEYTLSTYDPTYYVSMYYGEPTKSAVDFSALPANCRGQVLEPQVDEKVKQYASSLDQTQRDEDNTLGALFAQKVRLICR","1720269","","conserved hypothetical protein","Periplasm","","
InterPro
IPR010412
Family
Protein of unknown function DUF1007
PF06226\"[3-209]TDUF1007
noIPR
unintegrated
unintegrated
PD109898\"[65-186]TQ9CNK3_PASMU_Q9CNK3;
signalp\"[1-19]?signal-peptide


","BeTs to 3 clades of COG3683COG name: Predicted periplasmic metal-binding proteinFunctional Class: SThe phylogenetic pattern of COG3683 is -----------------h---j--t-Number of proteins in this genome belonging to this COG is","","Residues 20 to 209 match (5e-75) PD:PD109898 which is described as PROTEOME COMPLETE EXPORTED BMEII1136 HI1249 OR PERIPLASMIC PM0426 SIGNAL PRECURSOR ","","","","","","","","","","","","Thu Jan 16 08:00:26 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02482 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 209 (E-value = 1.2e-96) place AA02482 in the DUF1007 family which is described as Protein of unknown function (DUF1007) (PF06226)","","","","","","","","1","","","" "AA02483","1721121","1720954","168","ATGATTATTTTATTTAGGAACTTTATGAATATCAAGCAATCACTTGACGCGATTGAATGCTATAGATTTTTTCGTGTGAAGAAAAATACTAAATTAAGTTTTTTTGATATAGATCACAAAACTGAGCGTGTTTTTTTCTTTTTGCTGATTTTTTATACTTGTTCTGTG","","","6922","MIILFRNFMNIKQSLDAIECYRFFRVKKNTKLSFFDIDHKTERVFFFLLIFYTCSV","1720954","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 09:53:38 2004","Wed Feb 25 09:53:38 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02483 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 09:53:38 2004","","","","","","","","","","","","","1","","","" "AA02484","1721217","1722980","1764","ATGAACCCCCGAATGATTAAATTCCATCGGTCAATCAGGTGCCGAAAAAACGCCTTGAATTCCGACCGCACTTTTCCCTTAACCCAGAGAATAATTATGTCAATACAATTCGTTTATACGATGCACCGAGTAGGCAAAGTAGTTCCGCCGAAACGTCATATTCTGAAAAATATTTCACTCAGCTTTTTCCCGGGCGCCAAAATCGGCGTACTTGGCTTAAACGGTGCCGGTAAATCCACCCTGCTTCGCATTATGGCAGGCATCGATAAAGAAATCGAAGGGGAAGCCCGTCCGCAGCCGGGCATTAAAATCGGCTATCTTCCGCAGGAACCGAAACTCGATCCACAGCACACCGTGCGCGAAGCCATTGAAGAAGCCGTCGGCGAGGTGAAACGCGCTTTAACCCGCTTGGATGAAGTGTATGCGCTATATGCGAATCCCGATGCGGACTTTGACAAACTTGCCGCCGAACAAGCGGAGCTGGAAGCCGTTATCCAGGCTCACGGCGGGCATAACTTAGAAAATCAATTAGAACGCGCCGCCGATGCGCTACGTTTACCGGACTGGAATGCCAAAATCGAGCATTTATCCGGGGGGGAACGCCGCCGCGTTGCTTTGTGTCGTTTGTTGTTGGAAAAACCGGATATGTTGCTGTTAGACGAGCCGACCAACCACTTGGACGCGGAATCCGTGGCATGGTTGGAACGCTTCTTACACGACTACGAAGGCACTGTAGTGGCAATCACCCACGACCGTTACTTCTTGGATAACGTTGCCGGTTGGATTTTAGAACTTGACCGCGGTGAAGGCATTCCTTGGGAAGGCAATTACTCCTCTTGGTTGGAACAAAAAGAAAAACGTCTGGCGCAGGAACAGGCGCAGGAATCCGCCCGCCAAAAATCCATTGAGAAAGAATTGGAATGGGTGCGTCAAAATCCGAAAGGCCGCCAAGCGAAAAGCAAAGCCCGTATGGCGCGCTTCGAAGAACTTAATTCCGGCGAATATCAAAAACGTAACGAAACCAACGAACTCTTTATTCCACCCGGTCCACGCCTGGGCGAAAAAGTCATCGAGGTGCAACATTTAAGTAAGTCCTACGGCGACCGCACTTTAATCGACGATTTATCCTTCAGCATTCCGAAAGGTGCCATTGTCGGCATTATCGGTGCCAACGGCGCGGGTAAATCCACCCTCTTCCGTATGCTTTCCGGCAAAGAAAAACCAGATTCCGGTACCATTACCTTGGGCGAAACCGTCGTGTTAGCTTCCGTGTATCAATTCCGTGATGCTATGGACGAAAAAAAAACCGTGTGGGAAGAAGTGTCCAACGGACAAGATATTCTAACCATCGGTAACTTTGAAATCCCAAGCCGTGCTTATGTAGGACGCTTCAACTTCAAAGGCGTGGATCAACAAAAACGTGTGGGCGAACTCTCCGGCGGTGAACGTGGTCGTTTGCATTTGGCGAAATTATTACAAGCCGGCGGCAACATGCTGTTATTGGACGAGCCAACTAACGATCTTGATGTGGAAACCTTGCGCGCACTGGAAAATGCCATCTTGGAATTCCCGGGCTGTGCCATGGTAATTTCCCATGACCGCTGGTTCTTAGATCGTATCGCCACCCACATTTTAGATTACGGCGATGAAGGCAAAGTCACCTTCTACGAAGGCAATTTCTCCGATTATGAAGAATGGAAAAAGAAAACTTTCGGTGCTGAAGCCCTTAAACCGCACCGAATTAAATATAAACGCATTGCGAAA","","","66534","MNPRMIKFHRSIRCRKNALNSDRTFPLTQRIIMSIQFVYTMHRVGKVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKEIEGEARPQPGIKIGYLPQEPKLDPQHTVREAIEEAVGEVKRALTRLDEVYALYANPDADFDKLAAEQAELEAVIQAHGGHNLENQLERAADALRLPDWNAKIEHLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDYEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYSSWLEQKEKRLAQEQAQESARQKSIEKELEWVRQNPKGRQAKSKARMARFEELNSGEYQKRNETNELFIPPGPRLGEKVIEVQHLSKSYGDRTLIDDLSFSIPKGAIVGIIGANGAGKSTLFRMLSGKEKPDSGTITLGETVVLASVYQFRDAMDEKKTVWEEVSNGQDILTIGNFEIPSRAYVGRFNFKGVDQQKRVGELSGGERGRLHLAKLLQAGGNMLLLDEPTNDLDVETLRALENAILEFPGCAMVISHDRWFLDRIATHILDYGDEGKVTFYEGNFSDYEEWKKKTFGAEALKPHRIKYKRIAK","1722978","From PF00005: ABC transportersABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain ABC_membrane.","ABC transporter, ATP-binding protein","Cytoplasm, Inner membrane","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[195-238]T\"[477-520]TQ9CNK4_PASMU_Q9CNK4;
PF00005\"[65-268]T\"[382-551]TABC_tran
PS50893\"[39-293]T\"[357-575]TABC_TRANSPORTER_2
PS00211\"[196-210]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[64-269]T\"[381-551]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[2-325]T\"[341-545]Tno description
PTHR19211\"[168-569]TATP-BINDING TRANSPORT PROTEIN-RELATED
PTHR19211:SF7\"[168-569]TABC TRANSPORTER ABCF3, UUP


","BeTs to 16 clades of COG0488COG name: ATPase components of ABC transporters with duplicated ATPase domainsFunctional Class: RThe phylogenetic pattern of COG0488 is ------y--drlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 5.5e-22) to 2/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 371-417 1.3e-14 IPB001140B 475-513 7.4e-06","Residues 192 to 411 match (1e-06) PD:PD570993 which is described as ATP-BINDING ABC PROTEOME COMPLETE TRANSPORTER ","","","","","","","","","","","Thu Jan 16 08:11:16 2003","Thu Jan 16 08:11:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02484 is paralogously related to AA02573 (3e-83), AA01555 (6e-53), AA02140 (6e-25), AA02080 (9e-18), AA00700 (1e-16), AA01820 (1e-15), AA00207 (1e-15), AA01645 (5e-15), AA01656 (7e-15), AA02550 (1e-14), AA01824 (4e-14), AA00415 (4e-14), AA00751 (6e-14), AA01051 (8e-14), AA02718 (1e-13), AA02320 (1e-13), AA02786 (2e-13), AA01393 (4e-13), AA01684 (5e-13), AA02440 (6e-13), AA01524 (8e-13), AA01616 (1e-12), AA02324 (1e-12), AA01422 (5e-12), AA01961 (1e-11), AA02353 (4e-11), AA00858 (4e-11), AA00799 (6e-11), AA02898 (8e-11), AA02899 (1e-10), AA02805 (1e-10), AA01757 (1e-10), AA01456 (1e-10), AA01510 (2e-10), AA02331 (3e-10), AA02609 (5e-10), AA01867 (1e-09), AA01568 (1e-09), AA00061 (2e-09), AA00933 (4e-09), AA00591 (7e-09), AA01779 (1e-08), AA01947 (2e-08), AA02152 (3e-08), AA02606 (6e-08), AA01509 (6e-08), AA02225 (5e-07), AA02226 (3e-06), AA02642 (1e-05), AA02146 (8e-05), AA00934 (2e-04), A02145 (3e-04) and AA01569 (7e-04).","","","","","","Residues 382 to 550 (E-value = 4.6e-44) place AA02484 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Higgins CF, Hyde SC, Mimmack MM, Gileadi U, Gill DR, Gallagher MP.Binding protein-dependent transport systems.J Bioenerg Biomembr 1990 Aug;22(4):571-92PMID: 2229036Higgins CF, Gallagher MP, Mimmack ML, Pearce SR.A family of closely related ATP-binding subunits from prokaryotic and eukaryotic cells.Bioessays 1988 Apr;8(4):111-6PMID: 3288195","","Thu Jan 16 08:11:16 2003","1","","","" "AA02485","1723974","1723090","885","ATGACATATCAATTATTTAAACACCACCTCGTTGCTTTAATGGTCACTGGTGCAATTTCTGTCAATGCATTGGCTAAAGACTCTTTTCTGGAAAATCCTTCTGCTAATCTTCCACAACAAGTCTTTAAAAACAGGGTGGATATTTTTAATAATGAGACGAACATTAATGAAAATAAGAAAGATATTGCTATTAATAAAGCAAATATTGCTAGTATAGAAAAAGATGTTATGCGTAACACTGGGGGGATCGATAGATTAGCTAAGCAAGAGCTTGTTAACAGGGCAAGGATTACTAAAAATGAGTTAGATATTCAGAAAAATACTAAATCAATTGCAGAGAATACAGCTTCTATAGCCCGTATTGATGGAAATCTGGAAGGCGTTAATCGGGTGCTTCAAAATGTAGATGTGAGATCTACCGAAAATGCGGCAAGATCCCGTGCTAACGAGCAAAAAATCGCCGAGAATAAAAAAGCAATTGAAAATAAAGCGGATAAGGCTGATGTAGAGAAAAACAGAGCCGATATTGCAGCAAATTCCAGAGCGATTGCAACCTTTAGATCTTCAAGCCAAAACATCGCGGCATTAACGACCAAAGTTGATCGTAATACTGCGCGTATTGATCGATTAGATAGCCGAGTCAATGAATTAGACAAAGAAGTAAAAAACGGTTTGGCTTCCCAAGCGGCACTAAGCGGCTTATTCCAACCGTATAATGTCGGCAGCCTTAACTTGAGTGCAGCTGTTGGTGGTTATAAATCTAAAACAGCACTAGCGGTTGGTTCAGGTTATCGTTTCAATCAAAATGTAGCCGCGAAGGCCGGTGTGGCAGTAAGTACCAATGGTGGCAGCGCAACCTATAACGTCGGTTTAAACTTTGAGTGG","","","32020","MTYQLFKHHLVALMVTGAISVNALAKDSFLENPSANLPQQVFKNRVDIFNNETNINENKKDIAINKANIASIEKDVMRNTGGIDRLAKQELVNRARITKNELDIQKNTKSIAENTASIARIDGNLEGVNRVLQNVDVRSTENAARSRANEQKIAENKKAIENKADKADVEKNRADIAANSRAIATFRSSSQNIAALTTKVDRNTARIDRLDSRVNELDKEVKNGLASQAALSGLFQPYNVGSLNLSAAVGGYKSKTALAVGSGYRFNQNVAAKAGVAVSTNGGSATYNVGLNFEW","1723088","","outer membrane protein 100","Outer membrane, Extracellular","","
InterPro
IPR005594
Domain
YadA-like, C-terminal
PF03895\"[217-295]TYadA
InterPro
IPR008378
Family
Ubiquitous surface protein
PR01804\"[57-71]T\"[74-96]T\"[210-224]T\"[263-276]TUBIQUITOUSSP
noIPR
unintegrated
unintegrated
SSF101999\"[191-263]TSSF101999


","No hits to the COGs database.","","Residues 166 to 293 match (2e-22) PD:PD042012 which is described as MEMBRANE OUTER COMPLETE GNA992 PROTEOME NHHA ADHESIN IMMUNOGLOBULIN-BINDING PLASMID RESISTANCE ","","","","","","","","","","","","Thu Jan 16 09:05:20 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02485 is paralogously related to AA00234 (1e-11).","","","","","","Residues 217 to 295 (E-value = 6.6e-38) place AA02485 in the YadA family which is described as YadA-like C-terminal region (PF03895)","","","","Komatsuzawa,H., Asakawa,R., Kawai,T., Ochiai,K., Fujiwara,T.,Taubman,M.A., Ohara,M., Kurihara,H. and Sugai,M.Identification of six major outer membrane proteins fromActinobacillus actinomycetemcomitansGene 288 (1-2), 195-201 (2002)PubMed: 12034509","Comanducci,M., Bambini,S., Brunelli,B., Adu-Bobie,J., Arico,B.,Capecchi,B., Giuliani,M.M., Masignani,V., Santini,L., Savino,S.,Granoff,D.M., Caugant,D.A., Pizza,M., Rappuoli,R. and Mora,M.NadA, a novel vaccine candidate of Neisseria meningitidisJ. Exp. Med. 195 (11), 1445-1454 (2002)PubMed: 12045242","Thu Jan 16 09:05:20 2003","Thu Jan 16 09:07:36 2003","1","","","" "AA02486","1724477","1726372","1896","ATGACAACGAATTATTCCGCCAACGAAATTACCGTTTTAAAAGACCTCGAACCTGTCCAGCTGCGTCCCGGCATGTACACGGACACCACCCGCCCGAACCATCTTGCGCAAGAAGTTATCGATAACAGCGTGGACGAAGCTCTTGCCGGTTTTGCCACCAAAATTGAAGTGATTTTGCACAAAGACCAATCCATTGAAGTCATTGATAACGGACGCGGGATGCCGGTGGATATTCACCCGGTGGAAAAAGTTTCCGGTGTGGAAGTGATCATGAGTAAATTGCACGCCGGCGGTAAATTCTCCAATAAAAACTACACCTTCTCGGGCGGTTTGCACGGGGTCGGAATTTCTGTCGTAAACGCCTTATCGGAGCGGGTTGATGTTACCGTTAAACGCAATGGCGAAATCTATAAAATCGCTTTTGAAAACGGCAAAAAAGTAGAAGATCTTACTGTTATCGGCACCTGCGGTCGCCGCACGACCGGTACCACCGTGCATTTCAAACCGAATCCGAAATATTTCGACAGCGAAAAATTCTCCGTCAGCCGCCTACGCCATTTATTACGCGCCAAAGCCGTACTTTGTTCCGGCTTGGAAATCAAATTTATCGACAACGTCAACGACACCGAAGACACCTGGCTATATCAAGACGGCTTAAATGACTACTTAATGGAAGCGGTCAATGGCTTGGTCACATTGCCGGAACAGCCCTTTATCGGCGAATTTAACGGCGAAAAAGAAGCGGTATCTTGGGCATTATTGTGGCTGCCGGAAGGCGGTGAACTCATTGGTGAAAGCTATGTGAACCTGATTCCCACCGCACTTGGCGGCACCCATGTCAACGGTTTGCGTCAAGGTTTATTAGACGCCATGCGCGAATTCTGCGAGTTTCGCAATCTATTGCCGCGCGGCGTAAAACTGACCGCCGACGACCTATGGGATCGCTGCGCTTATGTGCTTTCCCTCAAAATGCAGGATCCACAGTTCGCCGGTCAAACCAAAGAACGACTTTCTTCCCGTCAAAGTGCGGTGTTTATCGGCGGCGTAGTCAAAGATGCCTTCAGTTTATGGCTCAACCAAAACATTCAGCAAGCGGAACTGTTGGCAGACATGGCAATCAGCTCCGCTCAACGTCGTCTGCGTGCGGCGAAAAAAGTGGTACGCAAAAAACTGGTAAGTGGCCCTGCGCTACCGGGTAAACTCGCCGATTGTAGCTCGCAAGACATCAATTTCACCGAATTATTCCTCGTAGAAGGCGATTCCGCCGGTGGTTCCGCCAAACAAGCGCGGGATCGTGAATATCAGGCGATCCTGCCGTTACGCGGCAAGATTTTGAATACGTGGGAAGTGTCTCCGGAACAAGTTTTGGCATCACAAGAGGTGCATGATATTGCGGTGGCGTTGGGCATTGATCCCGACAATAGCGATTTATCCCAACTACGTTACGGTAAAGTCTGCATCCTTGCCGATGCGGACTCCGACGGCTTACACATCGCCACCCTGCTTTGCGCCTTGTTCCTACGCCATTTCCCGAAACTGGTGGAACTGGGCCATGTGTATGTGGCAATGCCGCCGTTATACCGTATTGATTTAGGCAAAGACGTGTTTTACGCCTTGGATGAAAGCGAAAAAGACGCGATTTTAGATCGTCTTAAAGGGAAAAAAGGCAAACCGAACGTACAGCGTTTTAAAGGCTTGGGCGAAATGAACCCAATGCAACTGCGCGAAACCACCATGGACCCGAACACCCGCCGCTTAGTGCAGCTCACCTTTGAAGCCCAAAGCGAAGAAAAGCGGGAAACCATCGAAACCATGGATATGTTACTGGCTAAAAAGCGTGCCGAAGACCGTAAAAACTGGTTGCAGGCAAAAGGTGACCAGGTTGATTTGGCGGTG","","","70276","MTTNYSANEITVLKDLEPVQLRPGMYTDTTRPNHLAQEVIDNSVDEALAGFATKIEVILHKDQSIEVIDNGRGMPVDIHPVEKVSGVEVIMSKLHAGGKFSNKNYTFSGGLHGVGISVVNALSERVDVTVKRNGEIYKIAFENGKKVEDLTVIGTCGRRTTGTTVHFKPNPKYFDSEKFSVSRLRHLLRAKAVLCSGLEIKFIDNVNDTEDTWLYQDGLNDYLMEAVNGLVTLPEQPFIGEFNGEKEAVSWALLWLPEGGELIGESYVNLIPTALGGTHVNGLRQGLLDAMREFCEFRNLLPRGVKLTADDLWDRCAYVLSLKMQDPQFAGQTKERLSSRQSAVFIGGVVKDAFSLWLNQNIQQAELLADMAISSAQRRLRAAKKVVRKKLVSGPALPGKLADCSSQDINFTELFLVEGDSAGGSAKQARDREYQAILPLRGKILNTWEVSPEQVLASQEVHDIAVALGIDPDNSDLSQLRYGKVCILADADSDGLHIATLLCALFLRHFPKLVELGHVYVAMPPLYRIDLGKDVFYALDESEKDAILDRLKGKKGKPNVQRFKGLGEMNPMQLRETTMDPNTRRLVQLTFEAQSEEKRETIETMDMLLAKKRAEDRKNWLQAKGDQVDLAV","1726370","From Genbank:[gi:1172018] This enzyme is essential for chromosome segregation. It plays a role in the relaxation of supercoiled DNA activity. It performs the decatenation events required during the replication of a circular DNA molecule.","topoisomerase IV, subunit B","Cytoplasm","","
InterPro
IPR001241
Domain
DNA topoisomerase, type IIA, subunit B or N-terminal
PR00418\"[31-46]T\"[66-79]T\"[109-123]T\"[266-279]T\"[414-428]T\"[479-495]T\"[497-514]T\"[517-529]T\"[560-576]TTPI2FAMILY
SM00433\"[34-626]TTOP2c
PS00177\"[416-424]TTOPOISOMERASE_II
InterPro
IPR002288
Domain
DNA topoisomerase, type IIA, subunit B, C-terminal
PF00986\"[551-622]TDNA_gyraseB_C
InterPro
IPR003594
Domain
ATP-binding region, ATPase-like
G3DSA:3.30.565.10\"[2-217]Tno description
PF02518\"[27-172]THATPase_c
SM00387\"[27-173]THATPase_c
InterPro
IPR005737
Family
DNA topoisomerase IV, subunit B, Gram-negative
PR01098\"[26-39]T\"[135-149]T\"[149-164]T\"[174-191]T\"[192-213]T\"[238-261]T\"[294-310]T\"[311-326]T\"[338-361]T\"[362-387]T\"[448-469]T\"[469-481]T\"[503-519]T\"[537-559]T\"[582-596]TTOPISMRASE4B
TIGR01055\"[2-628]TparE_Gneg: DNA topoisomerase IV, B subunit
InterPro
IPR011558
Domain
DNA topoisomerase, type IIA, subunit B, conserved region
PD149633\"[419-540]TQ9CNQ7_PASMU_Q9CNQ7;
InterPro
IPR013173
Domain
DNA primase DnaG, DnaB-binding
SM00766\"[526-631]Tno description
InterPro
IPR013506
Domain
DNA topoisomerase, type IIA, subunit B, region 2
PF00204\"[218-386]TDNA_gyraseB
InterPro
IPR013759
Domain
DNA topoisomerase, type IIA, subunit B or N-terminal, alpha-beta
G3DSA:3.40.50.670\"[378-583]Tno description
noIPR
unintegrated
unintegrated
PTHR10169\"[24-622]TDNA TOPOISOMERASE/GYRASE
PTHR10169:SF3\"[24-622]TDNA GYRASE SUBUNIT B


","BeTs to 22 clades of COG0187COG name: DNA gyrase (topoisomerase II) B subunitFunctional Class: LThe phylogenetic pattern of COG0187 is ao-p--yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit (1.4e-117) to 8/8 blocks of the IPB001241 family, which is described as \"DNA topoisomerase II family\". Interpro entry for IP:IPR001241. IPB001241A 10-31 2.3e-10 IPB001241B 105-123 1.2e-11 IPB001241C 162-174 0.00011 IPB001241D 266-279 1.2e-05 IPB001241E 311-337 5.3e-12 IPB001241F 413-461 3.9e-32 IPB001241G 480-506 2.4e-16 IPB001241H 561-584 4.6e-15","Residues 217 to 263 match (7e-17) PD:PD460168 which is described as TOPOISOMERASE ISOMERASE PROTEOME COMPLETE B SUBUNIT IV ATP-BINDING 5.99.1.- PARE ","","","","","","","","","","","Thu Jan 16 09:56:13 2003","Thu Jan 16 09:46:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02486 is paralogously related to AA00929 (1e-108).","","","","","","Residues 551 to 622 (E-value = 3.5e-26) place AA02486 in the DNA_gyraseB_C family which is described as DNA gyrase B subunit, carboxyl terminus (PF00986)","","","","","Peng,H. and Marians,K.J.Escherichia coli topoisomerase IV. Purification, characterization,subunit structure, and subunit interactionsJ. Biol. Chem. 268 (32), 24481-24490 (1993)PubMed: 8227000Breines,D.M., Ouabdesselam,S., Ng,E.Y., Tankovic,J., Shah,S.,Soussy,C.J. and Hooper,D.C.Quinolone resistance locus nfxD of Escherichia coli is a mutantallele of the parE gene encoding a subunit of topoisomerase IVAntimicrob. Agents Chemother. 41 (1), 175-179 (1997)PubMed: 8980775Wigley DB, Davies GJ, Dodson EJ, Maxwell A, Dodson G.Crystal structure of an N-terminal fragment of the DNA gyrase B protein.Nature 1991 Jun 20;351(6328):624-9PMID: 1646964","","Thu Jan 16 09:57:54 2003","1","","","" "AA02487","1726578","1726417","162","TTGTTTGAATCACGTAGTGGCGAGTTCGAAAATTTCCGTAAAGCAAATTCAGTGGAACAAGGGAAACAAGGGAAAGCAGGGCGTGTTTTCTTTTTGCCTACTTTTGCTTTGCACGAGCAAAGAAAAAGTAGGTCGCCCATCGGGCGAAATCCGATATCAATT","","","6133","LFESRSGEFENFRKANSVEQGKQGKAGRVFFLPTFALHEQRKSRSPIGRNPISI","1726417","","hypothetical protein","Cytoplasm, Periplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 09:42:43 2004","Wed Feb 25 09:42:43 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02487 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 09:42:43 2004","","","","","","","","","","","","","1","","","" "AA02489","1726689","1726594","96","ATGTTTTTTTATTTAAAAAATGATTTTAAAATCGACCGCACTTTTAGAGCTATTTATTGGGTTCCCTTCTTTGCCGCCCTTGTGGAGTTGAATTTG","","","3972","MFFYLKNDFKIDRTFRAIYWVPFFAALVELNL","1726594","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-30]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 09:32:58 2004","Wed Feb 25 09:32:58 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02489 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 09:32:58 2004","","","","","","","","","","","","","1","","","" "AA02490","1726750","1726956","207","TTGCCCGAACGTGCGTTAATTTTTAGGAAAATTTTGCTTTGTTTGAACCACGTAGTGGCGAGTTCAAAATTTTCCGTGAAGAAAATTAATGCTAAGAGAGGAAAAGCAATTTATCCGGGGTCGCCTTTCTTTTGGTTACTTTTCTTTGGCGAAGCAAAGAAAAGTAACTCGCCCCATCAGGCGAAACCGATTAACACAACCAAAATA","","","7780","LPERALIFRKILLCLNHVVASSKFSVKKINAKRGKAIYPGSPFFWLLFFGEAKKSNSPHQAKPINTTKI","1726954","","hypothetical protein","Periplasm, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Jan 16 09:59:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02490 is paralogously related to AA00658 (3e-04).","","","","","","","","","","","","","","1","","","" "AA02491","1726967","1729219","2253","ATGACAACAGAATCCATCAACTACGAAGGCATCGAACAAATGCCACTCCGCCACTTCACTGAAAGTGCGTACCTCAACTATTCCATGTACGTCATCATGGATCGCGCGTTGCCGTTTATTGGTGACGGCTTAAAGCCGGTGCAGCGACGTATTATTTACGCCATGTCCGAACTCGGGCTGAACGCCACGGCGAAGTACAAAAAATCCGCCCGTACCGTGGGGGACGTGTTGGGTAAATTCCATCCGCACGGCGATAGCGCTTGTTATGAAGCCATGGTGCTGATGGCGCAACCGTTCTCTTACCGCTATCCGCTGGTTGACGGGCAAGGTAACTGGGGGGCGGTGGATGATCCGAAATCCTTCGCCGCCATGCGTTATACGGAGTCCCGTTTATCTAAAATTTCTGAGATTCTGTTAGCGGAACTTGGACAAGGCACAGTAGATTATCAGCCGAACTTCGACGGCACGCTGGAAGAGCCGCAATATTTACCGGCGCGCCTACCGCACATTTTACTCAACGGCACCACCGGCATTGCGGTGGGGATGGCGACAGATATTCCACCGCACAACATTAATGAAATCGCCGACGCGGCGGTGATGTTATTGGACAATCCGAAAACTACGCTGGACGAATTATTAACCGTAGTGCAAGGCCCCGATTTCCCGACGGAAGCAGAAATTATTTCGCCGAAAGAAGATATTCGGAAGATTTATCAACTGGGTCGCGGTTCCATTAAAATGCGCGCCACTTGGAAGAAAGAAGACGGTGAAATTGTTATCAGCGCCTTGCCGCATCAATCTTCACCGTCGAAAGTCATCGCGCAAATCGCCGAGCAGATGAATGCCAAAAAACTGCCGATGGTGGAAGATATTCGTGATGAAGCGGATCATGAAAATCCGGTGCGCATCGTGCTGGTGCCGCGTTCCAATCGGGTGGATATTGACGCCGTGATGGCACATTTATTCGCCACCACCGATTTGGAAAAAAGTTATCGCGTAAACATGAACATGATCGGTCTTGATCACAAGCCGGCGGTGAAAAATCTGTTGGAAATTCTCACCGAATGGCTCAGCTTCCGCCGCACTACAGTCACCCGTCGTTTGCAATATCATCTGAACAAAGTGCTCGCCCGTTTGCATATTTTGCAAGGCTTAATGATCGCCTTTTTAAACATTGATGAAGTGATCCACATCATTCGCTACGAAGACGAACCGAAAGCGGAATTGATGGCGCGTTTTAATTTAAGCGACGAGCAGGCAGAAGCTATTTTGAACTTACGTTTGCGCCATTTAGCCAAGTTAGAAGAGCATGAGCTGCAAGCGGAACAAGCGGAGTTGGAAAAAGAGCGGTCATCTTTGGAAGAGATTTTAGGCTCCGAGCGCCGTTTGAATACGCTCCTGAAAAAAGAAATTCAACAGGATGCCAAAATCTACGCCAGTCCGCGCCGTTCGCCGTTAGTGGAACGTGCAGAAGCCAAAGCCATTGCGGAAAACGAAATGCTGCCGACAGAACCGGTCACCGTGATTTTGTCGGAAATGGGCTGGGTGCGTTGTGCCAAAGGACACGATATTGATCCACAAGGCTTGAGTTATAAAGCGGGCGATAAATATTTGGCGCACGCCTACGGCAAAAGCAATCAAGCAGCGGTGTTTATCGACAGCACGGGGCGCAGTTACGCGCTGGATCCGTTGACGTTGCCATCCGCCCGTTCACAAGGCGAACCGCTCACCGGCAAACTCACTTTACCGGCGGGGGCGACTATCGATCAGTTACTGATTGAAAATGAAGATCAGCCGTTGCTCATGGCATCTGACGCAGGCTACGGTTTTATTTGTAAATTTGCCGATTTAATTGCCCGCAATAAAGCCGGCAAAGCGCTGATTTCCCTGCCGGAAAATGCCAAAGTCTTGCCGCCGTTAACGCTGAAAAATTCCACCGCACTTTTGGTAGCGCTCACTTCCGCCGGTCGCATGCTCATTTTCCCCGCGCAGGATTTGCCGGAATTATCCAAAGGCAAAGGCAACAAAATCGTTACCATTCCGTCCGCCAACGCCAAAGCCCGTTCTGAGCTGTTGGTGCACTTATTGCTGATTGAAGAAAATTCGAGTCTAGTGTTCCATTCCGGCAGACGCAAAATTGTACTGAAACCGGAAGATCTGCAGAAATTCCGCGCCGAACGCGGTCGTAAAGGCACGCAATTGCCACGGGGTTTACACAGTAATGTGGAAATTGAAGTGGTAACACCACAGCAG","","","89053","MTTESINYEGIEQMPLRHFTESAYLNYSMYVIMDRALPFIGDGLKPVQRRIIYAMSELGLNATAKYKKSARTVGDVLGKFHPHGDSACYEAMVLMAQPFSYRYPLVDGQGNWGAVDDPKSFAAMRYTESRLSKISEILLAELGQGTVDYQPNFDGTLEEPQYLPARLPHILLNGTTGIAVGMATDIPPHNINEIADAAVMLLDNPKTTLDELLTVVQGPDFPTEAEIISPKEDIRKIYQLGRGSIKMRATWKKEDGEIVISALPHQSSPSKVIAQIAEQMNAKKLPMVEDIRDEADHENPVRIVLVPRSNRVDIDAVMAHLFATTDLEKSYRVNMNMIGLDHKPAVKNLLEILTEWLSFRRTTVTRRLQYHLNKVLARLHILQGLMIAFLNIDEVIHIIRYEDEPKAELMARFNLSDEQAEAILNLRLRHLAKLEEHELQAEQAELEKERSSLEEILGSERRLNTLLKKEIQQDAKIYASPRRSPLVERAEAKAIAENEMLPTEPVTVILSEMGWVRCAKGHDIDPQGLSYKAGDKYLAHAYGKSNQAAVFIDSTGRSYALDPLTLPSARSQGEPLTGKLTLPAGATIDQLLIENEDQPLLMASDAGYGFICKFADLIARNKAGKALISLPENAKVLPPLTLKNSTALLVALTSAGRMLIFPAQDLPELSKGKGNKIVTIPSANAKARSELLVHLLLIEENSSLVFHSGRRKIVLKPEDLQKFRAERGRKGTQLPRGLHSNVEIEVVTPQQ","1729217","","topoisomerase IV, subunit A","Cytoplasm","","
InterPro
IPR002205
Domain
DNA topoisomerase, type IIA, subunit A or C-terminal
PD000742\"[50-126]TQ6LUY8_PHOPR_Q6LUY8;
PF00521\"[35-479]TDNA_topoisoIV
SM00434\"[14-464]TTOP4c
InterPro
IPR005742
Family
DNA topoisomerase IV, subunit A, Gram-negative
TIGR01062\"[11-745]TparC_Gneg: DNA topoisomerase IV, A subunit
InterPro
IPR006691
Repeat
DNA gyrase/topoisomerase IV, subunit A, C-terminal beta-pinwheel
PF03989\"[597-644]T\"[646-700]TDNA_gyraseA_C
InterPro
IPR013757
Domain
DNA topoisomerase, type IIA, subunit A, alpha-helical
G3DSA:1.10.268.10\"[372-458]Tno description
InterPro
IPR013758
Domain
DNA topoisomerase, type IIA, subunit A or C-terminal, alpha-beta
G3DSA:3.90.199.10\"[33-296]Tno description
noIPR
unintegrated
unintegrated
PTHR10169\"[122-194]TDNA TOPOISOMERASE/GYRASE
PTHR10169:SF2\"[122-194]TDNA TOPOISOMERASE II


","No hits to the COGs database.","Significant hit ( 2.4e-78) to 6/6 blocks of the IPB002205 family, which is described as \"DNA gyrase/topoisomerase IV, subunit A\". Interpro entry for IP:IPR002205. IPB002205A 35-53 3.1e-13 IPB002205B 68-103 3e-29 IPB002205C 117-131 2.4e-07 IPB002205D 173-194 1.1e-16 IPB002205E 216-225 0.0012 IPB002205F 236-245 0.57","Residues 199 to 246 match (1e-08) PD:PD581540 which is described as TOPOISOMERASE SUBUNIT A ISOMERASE IV PROTEOME COMPLETE 5.99.1.- IV PREDICTED ","","","","","","","","","","","","Thu Jan 16 10:04:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02491 is paralogously related to AA02519 (1e-104).","","","","","","Residues 646 to 700 (E-value = 1.6e-05) place AA02491 in the DNA_gyraseA_C family which is described as DNA gyrase C-terminal domain, beta-propeller (PF03989)","","","","","","","","1","","","" "AA02492","1729506","1730114","609","ATGAAACTATATTTTAAACCGGGTGCATGCTCATTCGTACCGCATTTCGCATTGGAAAAAATCAATCAGCCTTATGAAGCCGAAGCAGTGACACAAGAGTATATGAAGAGCCCGGAATACTTAGAGCTCAATCCACAAGGTGCAGTTCCTCTACTCGTTGACGGTAATCTTGTACTTTCCCAAAACTTGGCGATTTTAACTTATTTAGACGATCTTTACCCACAGGCAAAACTCTTTGGCAGCGACTCAGCCAAAGGCAAAGCTATAGCATTTCGCTGGTTGGCATTCTTGAATTCTGACGTACACAAAGCCTTTGTCCCACTCTTCCATGTACCGCCTTACGTTCAAGATGAATCCTTAAAACAAGCGATTCAAAAAACAGCGAAAGAAAATATTCTGGGTATGCTGGCGCAAGCTAATCACTGCTTATCAAAGCAGAATTACCTAGGCGAAGATGTATCCGTCGCCGATATTTATCTATTTACAATTTTAGGCTGGTGTAAATTTATCGATCTTGATTTTTCATCCCTAACACATTTAACCGAATTTGCGCAACGCATTGCAGCATTGGACATTGTAAAACGTGTACAAAAAGCCGAAGGGTTGATT","","","22770","MKLYFKPGACSFVPHFALEKINQPYEAEAVTQEYMKSPEYLELNPQGAVPLLVDGNLVLSQNLAILTYLDDLYPQAKLFGSDSAKGKAIAFRWLAFLNSDVHKAFVPLFHVPPYVQDESLKQAIQKTAKENILGMLAQANHCLSKQNYLGEDVSVADIYLFTILGWCKFIDLDFSSLTHLTEFAQRIAALDIVKRVQKAEGLI","1730112","From Genbank:[gi:1170122] This protein plays a role in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. ","glutathione S-transferase","Cytoplasm","","
InterPro
IPR004045
Domain
Glutathione S-transferase, N-terminal
PF02798\"[1-71]TGST_N
InterPro
IPR004046
Domain
Glutathione S-transferase, C-terminal
PF00043\"[109-191]TGST_C
InterPro
IPR010987
Domain
Glutathione S-transferase, C-terminal-like
G3DSA:1.20.1050.10\"[79-203]Tno description
InterPro
IPR012335
Domain
Thioredoxin fold
G3DSA:3.40.30.10\"[1-75]Tno description
noIPR
unintegrated
unintegrated
PTHR11260\"[1-197]TGLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING


","BeTs to 9 clades of COG0625COG name: Glutathione-S-transferasesFunctional Class: OThe phylogenetic pattern of COG0625 is ------y----l-cefghsn-jx---Number of proteins in this genome belonging to this COG is","","Residues 13 to 190 match (1e-08) PD:PD082590 which is described as PROTEOME COMPLETE GLUTATHIONE S-TRANSFERASE TRANSFERASE PROBABLE RSC0086 FAMILY PM1551 PLASMID ","","","","","","","","","","","Thu Jan 16 10:45:28 2003","Thu Jan 16 10:45:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02492 is paralogously related to AA02236 (6e-09).","","","","","","Residues 88 to 191 (E-value = 2.8e-05) place AA02492 in the GST_C family which is described as Glutathione S-transferase, C-terminal domain (PF00043)","","","","","Nishida,M., Kong,K.H., Inoue,H. and Takahashi,K.Molecular cloning and site-directed mutagenesis of glutathioneS-transferase from Escherichia coli. The conserved tyrosyl residuenear the N terminus is not essential for catalysisJ. Biol. Chem. 269 (51), 32536-32541 (1994)PubMed: 7798255Arca,P., Garcia,P., Hardisson,C. and Suarez,J.E.Purification and study of a bacterial glutathione S-transferaseFEBS Lett. 263 (1), 77-79 (1990)PubMed: 2185038","","Thu Jan 16 10:47:54 2003","1","","","" "AA02493","1730887","1730171","717","ATGAATATGATGAAAAAACAGTTAAAACATTTTGCGATAGTATTGGGATTATTGGGTTTTTCTGTACAAGCGGCGGAAAATGTGGCGTTTTCGGTCGCGGAACGTGTACAAGAAATGTCGGCGTTTGCACAGAATAAATTGAATAATGATGAATTGAGAAATCTGGCAAGATATTTCTATCAAAATGACGATGTCCGTTCGGCATTCAATGTGATGCGTATTTTGGCGCTACGTGGTGATAGTAACGCGCAACTGGATTTAGGGCGTTTGTATTTTGGCGGTAACGGCGTAGAGAAAAATTACGAAAAAGCCTATTGGTGGTTTAGTGAGGCGGCAGAAAAGGGGAGTGTGAAAGCGCTCACCAATTTGGGCATTCTTTATACAGGCGGCTACGGCGTTAAAAAGAATCTGGAATATGGCATTAATTTATTGGAGCAGGCCGCCGAAGTTAGCGATTCGCAAGCCATGTTGATTTTAGGCATGCTGTATTACAACGAGAACAAAATTAAGAATTTCAACAAAGCATTTCAGTGGTTGGAAAGAAGCGCACGACAAGGCAACGAAGAAGCGATCTTTCGTCTGGCACTAATGTATGAACATGGCGAAGGTACTCGACGCAATCGCCCGCTCGCTATTTCTATTTACAAGGATCTTATTGCACAACAAAGTTATTTTTCTGATGCCGCCCGTGAACGGTTAGAGATTCTGAACTATCAC","","","33301","MNMMKKQLKHFAIVLGLLGFSVQAAENVAFSVAERVQEMSAFAQNKLNNDELRNLARYFYQNDDVRSAFNVMRILALRGDSNAQLDLGRLYFGGNGVEKNYEKAYWWFSEAAEKGSVKALTNLGILYTGGYGVKKNLEYGINLLEQAAEVSDSQAMLILGMLYYNENKIKNFNKAFQWLERSARQGNEEAIFRLALMYEHGEGTRRNRPLAISIYKDLIAQQSYFSDAARERLEILNYH","1730169","","conserved hypothetical protein","Outer membrane, Cytoplasm, Extracellular","","
InterPro
IPR001531
Family
Phospholipase C zinc-binding, prokaryotic
SM00770\"[3-208]Tno description
InterPro
IPR006597
Repeat
Sel1-like
PF08238\"[81-116]T\"[117-152]T\"[153-187]T\"[188-223]TSel1
SM00671\"[81-116]T\"[117-152]T\"[153-187]T\"[188-223]TSEL1
InterPro
IPR011990
Domain
Tetratricopeptide-like helical
G3DSA:1.25.40.10\"[44-226]Tno description
noIPR
unintegrated
unintegrated
PTHR11102\"[33-238]TSEL-1-LIKE PROTEIN
PTHR11102:SF11\"[33-238]TSEL-1-LIKE PROTEIN, SEL-1L
signalp\"[1-24]?signal-peptide
tmhmm\"[10-30]?transmembrane_regions


","No hits to the COGs database.","","Residues 73 to 130 match (4e-07) PD:PD475496 which is described as SEL-1 SUPPRESSOR PRECURSOR TRANSMEMBRANE LIN-12-LIKE GLYCOPROTEIN HOMOLOG SEL-1L SIGNAL ALTERNATIVE ","","","","","","","","","","","","Thu Jan 16 13:14:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02493 is paralogously related to AA00022 (2e-11).","","","","","","","","","","","","","","1","","","" "AA02494","1731600","1730887","714","ATGACGCTATTGATTTCTAATCAGCACGGCGCAATCGTCATGGCACTCATGCCATTTCTGTACGGTATGTTACTTGCTCACCCTATTTGGCAGCACCTTTTCTTTTTATTGGCATGGTTTTCATTATATTTAATGACTTACCCGTTTCTGAATTTGTTCAAAGGCAGAAATTTAGAACTGTACATAAAATGGTCGTGGATTTATTTCTTTGCCACGGTGATTTTTGCCATTCCGGTGTTATTGCATAACTGGCGAACGGTGCTTTTTGTGGTCGCCATGATGCCGTTAGTGTTGGTAAATATTTATTATGTGAAAAAAAAGGATGAGCGTGCTTTTTTAAATGATCTGGTGGGAATCATTATTTTTGCCATTGCGGGCATGGGATCCTACTATTTTTCCGACCGCACTTTTGATGGCAAAATCTGGCTGGTAGCGCTGTATCCGAGCTTGTTTTTTATCGGTACCACCTTATATGTCAAATCCGTCATGCGTGAGCGAAAAAATCCGTTATATTTGAAGTTATCTATCGGTTTTCATGCGCTTTGTGTGCTAGGATTTATCTTGTTACAACAGTATTTAATGGCGCTGGCGTTTGTTCCGTCGTTAATTCGTGCAATTTGGCTACCGCACAAAAAAATGTCGGTAAAACAAGTGGGGCTGACCGAAATGGGCGTTTCGCTGCTGTTTTTTGCCAATTTGCTTTATGCAACGTTA","","","27667","MTLLISNQHGAIVMALMPFLYGMLLAHPIWQHLFFLLAWFSLYLMTYPFLNLFKGRNLELYIKWSWIYFFATVIFAIPVLLHNWRTVLFVVAMMPLVLVNIYYVKKKDERAFLNDLVGIIIFAIAGMGSYYFSDRTFDGKIWLVALYPSLFFIGTTLYVKSVMRERKNPLYLKLSIGFHALCVLGFILLQQYLMALAFVPSLIRAIWLPHKKMSVKQVGLTEMGVSLLFFANLLYATL","1730885","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-46]?signal-peptide
tmhmm\"[9-29]?\"[35-55]?\"[60-78]?\"[84-104]?\"[113-133]?\"[139-159]?\"[169-189]?\"[218-236]?transmembrane_regions


","No hits to the COGs database.","","Residues 1 to 222 match (4e-68) PD:PD038465 which is described as COMPLETE PROTEOME TRANSMEMBRANE PM0367 HI1626 YWIC BH0230 ","","","","","","","","","","","","Thu Jan 16 13:20:49 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02494 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02495","1731702","1732052","351","ATGACACAAATTCAACGTATCGATACTCACGCCCGCCTTGCCGAACTGGTGATTTATCATGGTGTCGCTTATTTGGCAGGACAAGTTCCGGAAACCACCTTAGCACAGGATGCTTACGCCCAAACGCAAGAAGTGCTAAATCTCATCGACAAATTACTTGCCAAAGCCAATTCCCACAAAAGCCAAATTTTAAACGCGCAGATCTATCTTGCCGACATGCAGGATTATGCCCTGATGAATCAGGCATGGGACGAATGGGTTGATCCACAAAATCCACCGGCGCGCGCCACTGTAGAAGCCAAACTGGCAGATCCTCGCTGGAAAGTGGAAATTGTGGTGACGTCGGCGGTT","","","13111","MTQIQRIDTHARLAELVIYHGVAYLAGQVPETTLAQDAYAQTQEVLNLIDKLLAKANSHKSQILNAQIYLADMQDYALMNQAWDEWVDPQNPPARATVEAKLADPRWKVEIVVTSAV","1732050","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR006056
Family
YjgF-like protein
PS01094\"[93-111]TUPF0076
InterPro
IPR006175
Domain
Endoribonuclease L-PSP
PF01042\"[3-117]TRibonuc_L-PSP
InterPro
IPR013813
Domain
Endoribonuclease L-PSP/chorismate mutase-like
G3DSA:3.30.1330.40\"[8-115]Tno description
noIPR
unintegrated
unintegrated
PTHR11803\"[17-117]TTRANSLATION INITIATION INHIBITOR


","No hits to the COGs database.","Significant hit ( 5.9e-29) to 3/3 blocks of the IPB000543 family, which is described as \"YER057c/YjgF/UK114 family\". Interpro entry for IP:IPR000543. IPB000543A 6-33 0.0083 IPB000543B 41-87 2.4e-15 IPB000543C 93-115 1e-07","Residues 14 to 116 match (7e-24) PD:PD002429 which is described as PROTEOME COMPLETE INHIBITOR TRANSLATION PLASMID INITIATION ORF TRANSLATIONAL PROBABLE LIPOPROTEIN ","","","","","","","","","","","","Thu Jan 16 13:27:22 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02495 is paralogously related to AA01561 (0.001).","","","","","","Residues 3 to 117 (E-value = 1.4e-26) place AA02495 in the Ribonuc_L-PSP family which is described as Endoribonuclease L-PSP (PF01042)","","","","","","","","1","","","" "AA02496","1732969","1732100","870","TTGGGTAAAACAGATTTACTACAATTTAAAGATTATTCTGAAAATTATGTATTCCTACCTTTTTGGTATAAAGTATTTACACTGATTTACTATCCTTGGAATATGGACTATGCCGTATTATATAATGTTGCTTGGATAGTTTTTTTTATTTTACCGAGTTATATGGGCTATACCTTAACTAAGGATATTAAACGTTATATTCCTTTTATCGGTTTTCTCATTCTTTGGTTTAGTTTACCTCATGCACTTAATCAAACAGCATTTATATATGAACGATTTTCCATTTTTATGCTTCCTTTTTATTATTTAATTTTTGAAAAAAGGTCAATCAAAAAGAATAACGGTAACATAATTTTCTTTAATTTAATGTTTTTTATATTTGTTTTCTTATTAATGGGAAAAGTCTATTATAATAATATTCAATTTAATAATGATCCAAATATGAGAGCATATTCGAAAATAATAGAGTCTATGCAGTCTCAAAAAAGAATATTAACTTTATTTAGTCAATCTTCAGAAACCAGTGGATTGCTTACTTCAAGTACAGAATATTTACATTTTGGTAGCTGGTATCAGGCGCAAAAACATGGGTGGTCCGATTTTAATTTTGCCGTTTATTCACCGCAAATAGTTAGATTCAAACCTAATAAAATGCCAAATATATCAAGTCGTTCAGGTGTGGTTAATAAAGATTGGATTATTAGCCTTGATAATTGTAAGGATTATGATTATTTATTGATGAAAACAAAAGAATCACCAACAATGATTTCGACATGGTTGGCAGAAAACCCTCGATGTAAAACATTCATTTTAGAGAATCAGCAACAGGATTGGTTACTGTTTAAAAAAATTAAAGAAAATGAAGCGTTA","","","34797","LGKTDLLQFKDYSENYVFLPFWYKVFTLIYYPWNMDYAVLYNVAWIVFFILPSYMGYTLTKDIKRYIPFIGFLILWFSLPHALNQTAFIYERFSIFMLPFYYLIFEKRSIKKNNGNIIFFNLMFFIFVFLLMGKVYYNNIQFNNDPNMRAYSKIIESMQSQKRILTLFSQSSETSGLLTSSTEYLHFGSWYQAQKHGWSDFNFAVYSPQIVRFKPNKMPNISSRSGVVNKDWIISLDNCKDYDYLLMKTKESPTMISTWLAENPRCKTFILENQQQDWLLFKKIKENEAL","1732098","","hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
tmhmm\"[15-33]?\"[37-57]?\"[62-80]?\"[86-105]?\"[117-137]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Jan 29 14:07:57 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02496 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02498","1733648","1732965","684","ATGAAAATATTTACCTTATTAACTAATAATGAAAGAAATTTATTTTATCTGGTTCTGCTTGTTACTGTTCTTTTTTTATTTTATCCACCATATTTACCCATGGTTGATTTGCCGCAGCATGCAGCCCAAGTAGTTATGTTAGATGATCTGTTTAAACAACAGAGTAAATGGTCTGATTTAGTTCAGCTGAATTGGGATACTCCTTATTTAACGGGCTATTTTGTTTGGTGGTTGCTATATCAATTCACGGATATTGTTACATCTTCTAAACTGTTGGTGGTTTTTATATTCCTATTTAATGTTTGGGCGGTTTTTCTTTTGAGAAAAAGCTTTCAAGCTGAAAGTATTCTGGAATGGGCTGCGATAATAAGCTTTTTTGGATTTGCTTTCCAATGGGGATTTGTTACATTTCTTTTAGCAATACCTATCGGTATTTTATTTTTTCTTTCTAATAAAAATTGGCTTGAAACTAAGAAATATCGTTATTTTATAGGTATAGTATTATTAGGTATTTTATCTTACTGTAGCCATGTTTTAATTTTTTCATTCTTCTGTTTTATTTCATATGGATATTTTTTAGCTATTCATTTTAGACAAGAATCTTATAAAGCGGGGGGGGGGGGGGGGGGTAATATTTACTCTCCCTTATCTGCTATTTGCAATAATATTAATTCGGTATTTGGG","","","26505","MKIFTLLTNNERNLFYLVLLVTVLFLFYPPYLPMVDLPQHAAQVVMLDDLFKQQSKWSDLVQLNWDTPYLTGYFVWWLLYQFTDIVTSSKLLVVFIFLFNVWAVFLLRKSFQAESILEWAAIISFFGFAFQWGFVTFLLAIPIGILFFLSNKNWLETKKYRYFIGIVLLGILSYCSHVLIFSFFCFISYGYFLAIHFRQESYKAGGGGGGNIYSPLSAICNNINSVFG","1732963","","hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-33]?signal-peptide
tmhmm\"[14-32]?\"[60-80]?\"[86-106]?\"[121-141]?\"[160-194]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Thu Jan 16 13:29:34 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02498 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02499","1734604","1733654","951","ATGTCGGAACCTATACTTACAATTGTTTTGCCTTGTTATAACGAACAGTCTGTTTTATCTAAATCCATACCGATTATTCTTAATCACTTATTAAATTTAATAAATAATAAGAGAATTAATAAGAATAGTAAGTTATTGCTGATTGATGATGGTTCAAAAGATAATACCTGGCTGGAAATAGAAATGCTGGTTAAGCAATATCAGCAAATCAAAGCATTAAAGTTAACCCGCAATTTTGGGCACCAAAATGCCTTGTTGGCAGGAATGATGTTTTCAGCTAAACAGTTAAAAACAGATATTTGTATTACTATGGACTGCGATTTACAAGATGATCCCGGTACTTTAGAGGAGATGTTAGAAAAATATTTTTCTGGTTATGAAATTGTATATGCTGTGAGAAATAGGCGTGCAAAAGACAGCTTATTAAAACGGAATTTTGCTTTATTATATTATAACATTTTAAAAAAGATGAATATTAACGTTGTTCCTAACCATGCAGATTATCGTCTAATGAGTGCTAGAGCTTTGTCTGCTTTGGAATGTTTTAGGGAAAGTAATTTATTTCTTCGCGGTATTGTTCCACTTTTAGGATTTTCAAGTACTACAGTTTATTATGCACGTGAAGAAAGGATCGCCGGATTTAGTAAATATAGCATTCCTCGTATGATGCGTTTAGCCATAGATGGGATATGTGGATTTAGTGCAATTCCTTTATTATTTATATTATGGTTAGGTATTATTGTTAGTTTAATTTCACTGGCAATGGGAGGATGGGCACTAATTATAAAAATTTTTGGCAGTGGTATAGTACCCGGATGGGCGTCTACTGTTGTGCCTATGTATTTTTTAGGCGGTGTGCAACTTTTTACTTTAGGTATTATAGGTATCTATATTAGTAAAATATTCGATGAAGTCAAAGATAGACCTAAATATATAATAGAGAAAGAATTA","","","36593","MSEPILTIVLPCYNEQSVLSKSIPIILNHLLNLINNKRINKNSKLLLIDDGSKDNTWLEIEMLVKQYQQIKALKLTRNFGHQNALLAGMMFSAKQLKTDICITMDCDLQDDPGTLEEMLEKYFSGYEIVYAVRNRRAKDSLLKRNFALLYYNILKKMNINVVPNHADYRLMSARALSALECFRESNLFLRGIVPLLGFSSTTVYYAREERIAGFSKYSIPRMMRLAIDGICGFSAIPLLFILWLGIIVSLISLAMGGWALIIKIFGSGIVPGWASTVVPMYFLGGVQLFTLGIIGIYISKIFDEVKDRPKYIIEKEL","1733652","From PF00535:Glycosyl transferaseThis is a diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine,GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids. ","dolichol phosphate mannose","Inner membrane, Cytoplasm","","
InterPro
IPR001173
Domain
Glycosyl transferase, family 2
PF00535\"[7-180]TGlycos_transf_2
noIPR
unintegrated
unintegrated
G3DSA:3.90.550.10\"[4-192]Tno description
PTHR10859\"[12-314]TGLYCOSYLTRANSFERASE RELATED
tmhmm\"[186-206]?\"[227-261]?\"[280-298]?transmembrane_regions


","BeTs to 13 clades of COG0463COG name: Glycosyltransferases involved in cell wall biogenesisFunctional Class: MThe phylogenetic pattern of COG0463 is aompkzyqvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is","","Residues 7 to 133 match (5e-13) PD:PD395383 which is described as TRANSFERASE COMPLETE PROTEOME SYNTHASE GLYCOSYLTRANSFERASE MANNOSYLTRANSFERASE DOLICHOL-PHOSPHATE MANNOSE GLYCOSYL DOLICHYL-PHOSPHATE ","","","","","","","","","","","Thu Jan 16 13:35:47 2003","Thu Jan 16 13:32:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02499 is paralogously related to AA02636 (5e-09) and AA00492 (4e-06).","","","","","","Residues 7 to 180 (E-value = 2.6e-20) place AA02499 in the Glycos_transf_2 family which is described as Glycosyl transferase (PF00535)","","","","","","","","1","","","" "AA02500","1735638","1734751","888","ATGGCAAAGAAAACGACGCATTTTATTCGCAAATTTCTCGCTTTATTTGGCATAGTCGCAGTAGGCGTTGCTGCCTATCTTTTTTACAGCATCGAGATTTTTTTGCCGGTCAAAATCCATTTTTCCGGTGCTTCCAAGCTGACTTACCAACCGCTCGCAAAACACGAAGATTTAACCTGTTACCAAGCGGCGCAAAAACCGCAAGAAATGACACAAAATAGATTCCGTTTACTCGTTTGGAATTTGCACAAAGGGCAGGATGCCGGTTGGCAGCAGGCGCTTTCCCGTTTTGCCAAAGGGCGCGACTTTGTGTTGCTGCAAGAGGTGTTAAATACGCAACATCTGGCGACGCAATATTCAGCGCAATTTCCGACCGCACTTTATGCCTCTGCCTTTGCTTATTTACAGCAGCAATCGGGCGTTGAAATTCTCTCAAAATTTCCACCGCACTTTTATTGCGCCGGTTCAAAACCGGAACCCTGGATCCGCATTCCGAAAGTCGGTGCTGCCATGAGTCTGCCTCTGGCGGGAGGAAAAAATCTCTTATTAGTCAACGTGCATTTAATTAATTTTGAATTAAACCCCACTGCATACGGCGAGCAACTACGCACGCTCATGCAACTTATTTCCCACCATCAGGGACCGTTAATTTTCGCCGGGGATTTTAATTCTTGGAGCAGTTACCGTATGTCGCGTATTCATGAGTTAATTACGGAATATGGTTTACAAGAGGTGACTTTTCCGCAAGATCATCGTCTGCGCTTTTTGGGTAACCCGCTGGATCATATTTTTATTCGCGGATTAAATGTCATCAACGCCACTACAGAACCAACGGAAAGCTCCGACCATGCGCCGTTGTTGCTGGAGGCGGAGCTAATAGCAGATAAA","","","33597","MAKKTTHFIRKFLALFGIVAVGVAAYLFYSIEIFLPVKIHFSGASKLTYQPLAKHEDLTCYQAAQKPQEMTQNRFRLLVWNLHKGQDAGWQQALSRFAKGRDFVLLQEVLNTQHLATQYSAQFPTALYASAFAYLQQQSGVEILSKFPPHFYCAGSKPEPWIRIPKVGAAMSLPLAGGKNLLLVNVHLINFELNPTAYGEQLRTLMQLISHHQGPLIFAGDFNSWSSYRMSRIHELITEYGLQEVTFPQDHRLRFLGNPLDHIFIRGLNVINATTEPTESSDHAPLLLEAELIADK","1734749","","conserved hypothetical protein","Cytoplasm, Periplasm, Inner membrane","","
InterPro
IPR005135
Domain
Endonuclease/exonuclease/phosphatase
PF03372\"[75-290]TExo_endo_phos
noIPR
unintegrated
unintegrated
G3DSA:3.60.10.10\"[68-289]Tno description
signalp\"[1-24]?signal-peptide
tmhmm\"[12-30]?transmembrane_regions


","BeTs to 3 clades of COG3021COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3021 is ---------d----e-g----j----Number of proteins in this genome belonging to this COG is","","Residues 71 to 254 match (4e-29) PD:PD359439 which is described as COMPLETE PROTEOME STY0279 CYTOPLASMIC ALR4222 PLASMID VC2238 YAFD YPO1077 ","","","","","","","","","","","","Thu Jan 16 13:38:46 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02500 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 75 to 290 (E-value = 3e-13) place AA02500 in the Exo_endo_phos family which is described as Endonuclease/Exonuclease/phosphatase family (PF03372)","","","","","","","","1","","","" "AA02501","1737686","1735644","2043","ATGAGTTATCAGGTATTAGCAAGAAAATGGCGTCCGAAAACCTTTGCTGACGTTGTGGGGCAGCAACATATTTTGACCGCACTTGCTAACGGTTTGCGTGAAAATCGTCTGCATCATGCCTATTTGTTTTCCGGCACGCGCGGCGTGGGGAAAACTTCCATCGCCCGTTTATTCGCCAAAGGGCTTAATTGTGTCAGCGGTGTCACCGCCGAACCCTGTGGCGTGTGCGAGCATTGCAACGCCATCGAAAAAGGCAACTTTATTGATTTGATCGAAATCGATGCGGCGTCCCGAACCAAAGTGGAAGACACCCGTGAATTGCTGGATAACGTGCAATATAAACCGGTGTTGGGGCGCTATAAAGTGTATCTTATCGATGAAGTACACATGCTTTCCCGCCATTCTTTCAATGCGTTGCTGAAAACCCTGGAAGAGCCGCCGGAATACGTCAAATTCCTGCTCGCCACCACGGATCCGCATAAATTGCCGGTAACGATTTTATCCCGTTGTATGCAGTTCCATTTGAAAGCCCTGGAGCAATCACAAATCGCTGACCATTTGGCGTATATTCTCAATCAGGAACAGATCCCTTTTGAATCCTTGGCGTTAGATAAACTTGCCAACGCCGCGCAGGGCAGTATTCGCGACAGTTTAAGCCTCACCGATCAAGCGATAGCCATGAGCAACGGCAATGTTACGCTCAATATCGTTAACGATATGCTCGGTTTACTGGATGAAAGTCAAGCCATTGAGATGATTTATGCGTTACAGCAAGGTAACGGCGAAAAACTGATGCAGGCAGTGAATGCTGTGGCGGATAAAGCCGGCGATTGGGATGAATTGCTACGTGAAGTGGCGGAAAACTTGCACAAAATCGCCATGCAACAACTCTTGCCGCAGGCTGCCTTGGATGAAAGCAGTCAAATCGGCTTTTTAGCCAAACATATTGCGCCTCAGGACGTTCAATTTTTCTACCAGGTCGTTGTCACCGGTCGTAAAGAATTAAGTGCCGCACCAACGGCGCGTATGGGCGCTGAAATGGTGTTATTGCGTGCGTTGGCGTTTCACCCGAAATTAATGGGGGATTTTGCGAATGCAGAACAGAACGAATTCAATCCTCCGTTAAGCCAACAAAGTGCGGTGGAAAATCCCGTTAAATCTCCATTGCAATCTACCGCCCCCGCGATTGAAATGCCGGTGGTTTCACAGGCGATCAAAGCCAATTATCAAAGCCGTAAAAAATCGGTGGCGGATAATGCGCCGACTCAAATGGAAAAAGCACAACCTGCGCAATCGACAGAGGCGTTAGTCAATTCCCCCGTGCTGGACGCCTTAAACGGGCTGGAGCAGCTGGATGCCATGCCGAGTACGCCCTCTCAAGAAAAAAAAAAGTCTGAACGCTTAGCACAACATTCATCGGAAAAACTGACCGCACTTTCCCATGCAACCACGCATTCTGACGCCCAAAGTGCGGTAGAAAATCAGAGTGAATCTGATAGCGACGAAACTGATGCGGATGTGTTGTTAGGCGAGGATTATCGTTGGGAGTGGAGCAACCCCGAGCTTGCCAATATTGAGCAAGGCCCTAAGCCCTCCGAAATCAAAGCCGCCATTTTGCAGGACATCACTCCTGAATTACAGCAAAAAATCGTCAATTTAACTCAAACGCAAGATCGCTGGGCGCAGCTGATTGAGCAAAGCGGTGTAGAAAATCTCACCAAAGAGTTCGCCTTAAATACCTTCATTTGGCAGGAAAATGACGCGGAGTTTAAACTTGGTGTGCGTTCCAGCCACGGGCATTTAAATCAGGATAAGCATCGGAAGCTGTTACAACAGGCACTTTCAGTGGTGTTACAGAAAGAAATTGCACTGACCGTGGAAATTAACGACGACGAACAATATCTGACGCCGACGGATTATCGCCGTAAAACCTATGCTCAATTGCGTGAGCAGGCGAAACAGGATTTGTTGCAAGATGAAAAGTTGCAACTATTGGAGCGTGAATTTGATTGTCAGGTTGATGTGAAAAGTATTCGTCCGGTG","","","75998","MSYQVLARKWRPKTFADVVGQQHILTALANGLRENRLHHAYLFSGTRGVGKTSIARLFAKGLNCVSGVTAEPCGVCEHCNAIEKGNFIDLIEIDAASRTKVEDTRELLDNVQYKPVLGRYKVYLIDEVHMLSRHSFNALLKTLEEPPEYVKFLLATTDPHKLPVTILSRCMQFHLKALEQSQIADHLAYILNQEQIPFESLALDKLANAAQGSIRDSLSLTDQAIAMSNGNVTLNIVNDMLGLLDESQAIEMIYALQQGNGEKLMQAVNAVADKAGDWDELLREVAENLHKIAMQQLLPQAALDESSQIGFLAKHIAPQDVQFFYQVVVTGRKELSAAPTARMGAEMVLLRALAFHPKLMGDFANAEQNEFNPPLSQQSAVENPVKSPLQSTAPAIEMPVVSQAIKANYQSRKKSVADNAPTQMEKAQPAQSTEALVNSPVLDALNGLEQLDAMPSTPSQEKKKSERLAQHSSEKLTALSHATTHSDAQSAVENQSESDSDETDADVLLGEDYRWEWSNPELANIEQGPKPSEIKAAILQDITPELQQKIVNLTQTQDRWAQLIEQSGVENLTKEFALNTFIWQENDAEFKLGVRSSHGHLNQDKHRKLLQQALSVVLQKEIALTVEINDDEQYLTPTDYRRKTYAQLREQAKQDLLQDEKLQLLEREFDCQVDVKSIRPV","1735642","From Genbank:[gi:118808] DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria.This DNA polymerase also exhibits 3' to 5' exonuclease activity.The tau chain serves as a scaffold to help in the dimerization of the core complex.The gamma chain seems to interact with the delta subunit to transfer the beta subunit on the DNA. ","DNA polymerase III, subunits gamma and tau","Cytoplasm","","
InterPro
IPR001270
Family
Chaperonin clpA/B
PR00300\"[41-59]T\"[124-142]TCLPPROTEASEA
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[37-178]TAAA
InterPro
IPR003959
Domain
AAA ATPase, core
PF00004\"[40-173]TAAA
InterPro
IPR012763
Domain
DNA polymerase III, subunits gamma and tau
TIGR02397\"[3-353]TdnaX_nterm: DNA polymerase III, subunits ga
InterPro
IPR013991
Domain
PhnA protein N-terminal, proteobacterial
SM00782\"[46-83]Tno description
noIPR
unintegrated
unintegrated
G3DSA:1.20.272.10\"[242-369]Tno description
G3DSA:3.40.50.300\"[1-177]Tno description
PTHR11669\"[97-554]TREPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT


","BeTs to 18 clades of COG2812COG name: DNA polymerase III, gamma/tau subunitsFunctional Class: LThe phylogenetic pattern of COG2812 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 3 to 229 match (1e-112) PD:PD001042 which is described as DECARBOXYLASE SYNTHASE PYRIMIDINE LYASE BIOSYNTHESIS OROTIDINE OMPDECASE 5'-PHOSPHATE OMP OMPDCASE ","","","","","","","","","","","Thu Jan 16 14:16:06 2003","Thu Jan 16 13:44:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02501 is paralogously related to AA00302 (2e-15), AA02728 (5e-10) and AA01211 (3e-04).","","","","","","Residues 40 to 229 (E-value = 1e-05) place AA02501 in the AAA family which is described as ATPase family associated with various cellular activities (AAA) (PF00004)","","","","","Bullard JM, Pritchard AE, Song MS, Glover BP, Wieczorek A, Chen J, Janjic N, McHenry CS. A three-domain structure for the delta subunit of the DNA polymerase III holoenzyme delta domain III binds delta' and assembles into the DnaX complex. J Biol Chem. 2002 Apr 12;277(15):13246-56. PMID: 11809766 Pritchard AE, McHenry CS. Assembly of DNA polymerase III holoenzyme: co-assembly of gamma and tau is inhibited by DnaX complex accessory proteins but stimulated by DNA polymerase III core. J Biol Chem. 2001 Sep 14;276(37):35217-22. PMID: 11463784 Flower,A.M. and McHenry,C.S. The adjacent dnaZ and dnaX genes of Escherichia coli are contained within one continuous open reading frame Nucleic Acids Res. 14 (20), 8091-8101 (1986) PubMed: 3534795 Blinkowa,A.L. and Walker,J.R. Programmed ribosomal frameshifting generates the Escherichia coli DNA polymerase III gamma subunit from within the tau subunit reading frame Nucleic Acids Res. 18 (7), 1725-1729 (1990) PubMed: 2186364 ","","Thu Jan 16 14:16:06 2003","1","","","" "AA02502","1738330","1737722","609","ATGATAATATGCGCGCCGATTTATAATTTTAATCCGTGCAAAAAAACAACCGCACTTTTAGGTAAAAAAATGGAAAAACAACTTGCACTTATCGCTTCTTCAATTAAATCCATTCCCGATTATCCGAAACCGGGCATCATTTTTCGTGACATTACCAGCCTGGTAGAAAACCCGGCGGCATTTCATGCGGCTATCGATCTCATCGTGCAACATTGCAAAGACAAAGGGATTAATAAAGTGATCGGTACCGAATCCCGCGGTTTTATTTTCGGCGCGCCGGTGGCGTTGGCGTTAAATGTGCCTTTCGTGTTGGTGCGCAAGCCGGGCAAATTACCCCGTGAGACCATCGCACAATCTTACGAATTGGAATATGGGCAAGACACTTTGGAAATTCACACGGATTCCATTCAACAACGTGATAATGTCTTAGTGATTGATGATTTGTTGGCGACCGGCGGCACTGTTGAGGCCACCGTTAAATTAGTGCAACGTCTTGGCGGTGAAGTGAAGCACGCCGCGTTCGTGATTAATTTATCGGAATTGGGTGGCGAACAGCGTTTACTTGGATTGGGCGTGGAACCTTATACCTTGGTTAATTTCGCCGGTCAT","","","22058","MIICAPIYNFNPCKKTTALLGKKMEKQLALIASSIKSIPDYPKPGIIFRDITSLVENPAAFHAAIDLIVQHCKDKGINKVIGTESRGFIFGAPVALALNVPFVLVRKPGKLPRETIAQSYELEYGQDTLEIHTDSIQQRDNVLVIDDLLATGGTVEATVKLVQRLGGEVKHAAFVINLSELGGEQRLLGLGVEPYTLVNFAGH","1737720","From Genbank:[gi:1168477] This enzyme catalyzes a salvage reaction resulting in the formation of AMP that is energetically less costly than de novo synthesis.","adenine phosphoribosyltransferase","Cytoplasm","","
InterPro
IPR000836
Domain
Phosphoribosyltransferase
PF00156\"[50-186]TPribosyltran
InterPro
IPR002375
Family
Purine/pyrimidine phosphoribosyl transferase
PS00103\"[142-154]TPUR_PYR_PR_TRANSFER
InterPro
IPR005764
Family
Adenine phosphoribosyl transferase
TIGR01090\"[31-200]Tapt: adenine phosphoribosyltransferase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2020\"[24-200]Tno description


","No hits to the COGs database.","Significant hit ( 2.8e-06) to 2/2 blocks of the IPB002375 family, which is described as \"Purine/pyrimidine phosphoribosyl transferase\". Interpro entry for IP:IPR002375. IPB002375A 106-110 69 IPB002375B 139-154 2.1e-05","Residues 42 to 165 match (6e-08) PD:PD546495 which is described as PHOSPHORIBOSYLTRANSFERASE PLASMID GLYCOSYLTRANSFERASE TRANSFERASE ADENINE ","","","","","","","","","","","Thu Jan 16 14:34:57 2003","Thu Jan 16 14:32:34 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02502 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 50 to 186 (E-value = 4.6e-47) place AA02502 in the Pribosyltran family which is described as Phosphoribosyl transferase domain (PF00156)","","","","","Hershey,H.V. and Taylor,M.W.Nucleotide sequence and deduced amino acid sequence of Escherichiacoli adenine phosphoribosyltransferase and comparison with otheranalogous enzymesGene 43 (3), 287-293 (1986)PubMed: 3527873","","Thu Jan 16 14:38:21 2003","1","","","" "AA02504","1739308","1738355","954","ATGACAGATTCTCAACAAAACGTCCGTTTAACGGCGCGTGTCGGCTATGAACCACGTTTCTCATGGTCGTATTTAAAGCCGAAATACTGGGGCATTTGGTGCGGTATTTTGGTACTGCTTTTGCTCGGCTTTATCCCTTTTCGCTTGCGCGATAAGCTGGCGGCGAAACTCGGTGTGTTTATCGGGCATAAAGCGAAAAAACAACGTAAACGGGCGCAAATTAATTTGCAATGTTGCTTTCCGCAATGGTCGGAACAGCATCGTGAGAAGGTGATTGATGAAATGTTCGCCGTGTTGGCGCAAGTGATGTTGGGCATCGGTGAAGTTGCCGTGCGTTCAAAAAAACATTTGCAAAAACGCAGTGAATTTATCGGCATTGAACATATTAAACAGGCAAAAGAACAGGGTAAAAACGTGATTTTGCTGGTGCCGCACGGTTGGGCGATTGATGCGTCGGGGATTATTTTGCACACCCACGGCATTCCCATGACGTCCATGTATAACCCGCACCGCAATCCTCTGGTGGACTGGCTTTGGACTATCACCCGACAGCGTTTCGGCGGCAAAATGCACGCCCGCCAAAATGGTATTAAACCGTTTTTGAACCACATTAAGCAGGGGCAAATGGGCTATTATTTGCCGGATGAAGATTTTGGCGAAGAGCAGAGTGTGTATGTGGATTTCTTCGCCACCTACAAAGCTACATTGCCGGGTATTAATAAAATGGCGAAACTGGCAAAAGCGGTGGTGATTCCCATGTTTCCGCGCTACAACGCAGAGGCCGGCAAATACCAGATGGAAATTCATCTCGCCATGGCATTAAGTGATGATCCGGAACAATGTGCACGCGCCATGAATGCAGAAATTGAAAGTTTTGTCACTGAAACGCCGGCGCAATATGTGTGGATTTTACAGCTGCTGCGCACCCGAAAAAATGGTGAAGATCTTTATGAT","","","36647","MTDSQQNVRLTARVGYEPRFSWSYLKPKYWGIWCGILVLLLLGFIPFRLRDKLAAKLGVFIGHKAKKQRKRAQINLQCCFPQWSEQHREKVIDEMFAVLAQVMLGIGEVAVRSKKHLQKRSEFIGIEHIKQAKEQGKNVILLVPHGWAIDASGIILHTHGIPMTSMYNPHRNPLVDWLWTITRQRFGGKMHARQNGIKPFLNHIKQGQMGYYLPDEDFGEEQSVYVDFFATYKATLPGINKMAKLAKAVVIPMFPRYNAEAGKYQMEIHLAMALSDDPEQCARAMNAEIESFVTETPAQYVWILQLLRTRKNGEDLYD","1738353","From Genbank:[gi:1171030] This protein transfers myristate or laurate, activated on ACP to (kdo)2-(lauroyl)-lipid IVa. ","lipid A biosynthesis (kdo)2-(lauroyl)-lipid IVA acyltransferase","Inner membrane, Cytoplasm","","
InterPro
IPR004960
Family
Bacterial lipid A biosynthesis acyltransferase
PIRSF026649\"[16-318]TLipid A biosynthesis acyltransferase
PF03279\"[17-309]TLip_A_acyltrans
InterPro
IPR011921
Family
Lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase
TIGR02208\"[16-317]Tlipid_A_msbB: lipid A biosynthesis (KDO)2-(
noIPR
unintegrated
unintegrated
signalp\"[1-43]?signal-peptide
tmhmm\"[29-47]?transmembrane_regions


","BeTs to 8 clades of COG1560COG name: Lauroyl/myristoyl acyltransferase involved in lipid A biosynthesisFunctional Class: NThe phylogenetic pattern of COG1560 is ----------r---efghsnujxi--Number of proteins in this genome belonging to this COG is","","Residues 1 to 35 match (2e-10) PD:PD474683 which is described as PROTEOME COMPLETE ACYLTRANSFERASE BIOSYNTHESIS A KDO2-LAUROYL-LIPID TRANSMEMBRANE LIPOPOLYSACCHARIDE IVA 2.3.1.- ","","","","","","","","","","","Fri Jan 10 14:15:32 2003","Fri Jan 10 14:15:32 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02504 is paralogously related to AA02586 (4e-18).","","","","","","Residues 17 to 309 (E-value = 9.6e-141) place AA02504 in the Lip_A_acyltrans family which is described as Bacterial lipid A biosynthesis acyltransferase (PF03279)","","","","","D'Hauteville H, Khan S, Maskell DJ, Kussak A, Weintraub A, Mathison J,Ulevitch RJ, Wuscher N, Parsot C, Sansonetti PJ. Two msbB genes encoding maximal acylation of lipid A are required for invasive Shigella flexneri to mediate inflammatory rupture and destruction of the intestinal epithelium. J Immunol. 2002 May 15;168(10):5240-51. PMID: 11994481 Murray SR, Bermudes D, de Felipe KS, Low KB. Extragenic suppressors of growth defects in msbB Salmonella. J Bacteriol. 2001 Oct;183(19):5554-61. PMID: 11544217 Somerville JE Jr, Cassiano L, Darveau RP. Escherichia coli msbB gene as a virulence factor and a therapeutic target.Infect Immun. 1999 Dec;67(12):6583-90. PMID: 10569778","","Tue Feb 4 17:26:41 2003","1","","","" "AA02506","1740191","1739427","765","ATGGAATTCGGACTTGATATTTTAGCCATTTTATTTGCTGTTGCCTTTATTGCCGGTTTTATTGACGCCATTGCCGGTGGCGGCGGTTTAATCACCATCCCCGCGTTACTGATGACAGGGCTTCCGCCGGCGGTTGCGCTCGGTACCAATAAACTACAAGCCTGTGGCGGTTCCTTTTCTGCCAGCCTTTATTTTCTGCGTCAAAGAGCGGTTAAATTTTCGGAAGTTTGGTTGATTTTGTTGATGATCTTCCTCGGATCTGTTGCCGGCACCATTTTAATTCAATTAATTGACGCGTCTTTGATCAAGAAAATTCTCCCGTTTTTGATTTTGGCTATCGGTATCTATTTTTTGGTCACCCCTAAACTCGGCGACGAAGATCGCAAACAGCGTCTTTCTTACCCGATTTTTGCATTTTGTATCGGTACGTTTATGGGCTTTTATGACGGCTTTTTCGGCCCCGGTACCGGTTCCATCATGAGCTTGGCTTGCGTGACATTACTTGGCTTTAATCTGGCAAAAGCCACTGCCCATGCCAAAGTGATGAATTTTACCTCTAATCTGGCTTCCTTGATTTTCTTCTTAATCGGCGGACAAATTTTATGGACAGTGGGCTTGATTATGCTGGCAGGGCAGTTCATCGGCGCCAACTTAGGCGCCAAAATGGTGATGACCAAAGGAAAAACGTTGATTCGCCCTATGGTGGTCGTAATGTCCTTTATCATGACGGTGAAAATGGCGTTTGATCAAGGTTGGTTTGACTTT","","","27398","MEFGLDILAILFAVAFIAGFIDAIAGGGGLITIPALLMTGLPPAVALGTNKLQACGGSFSASLYFLRQRAVKFSEVWLILLMIFLGSVAGTILIQLIDASLIKKILPFLILAIGIYFLVTPKLGDEDRKQRLSYPIFAFCIGTFMGFYDGFFGPGTGSIMSLACVTLLGFNLAKATAHAKVMNFTSNLASLIFFLIGGQILWTVGLIMLAGQFIGANLGAKMVMTKGKTLIRPMVVVMSFIMTVKMAFDQGWFDF","1739425","","possible transmembrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR002781
Family
Protein of unknown function DUF81
PF01925\"[9-247]TDUF81
noIPR
unintegrated
unintegrated
signalp\"[1-90]?signal-peptide
tmhmm\"[5-25]?\"[44-66]?\"[76-96]?\"[102-122]?\"[132-152]?\"[158-176]?\"[191-211]?\"[230-248]?transmembrane_regions


","No hits to the COGs database.","","Residues 34 to 118 match (4e-25) PD:PD001246 which is described as PROTEOME COMPLETE TRANSMEMBRANE MEMBRANE INTEGRAL PLASMID PROBABLE PERMEASE ORF YRKJ ","","","","","","","","","","","","Fri Jan 10 14:32:27 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02506 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 9 to 247 (E-value = 1.3e-41) place AA02506 in the DUF81 family which is described as Domain of unknown function DUF81 (PF01925)","","","","","","","","1","","","" "AA02507","1741067","1740198","870","ATGAATAAAACCTTTCTCCAATTCATCAAAAGTGCGGTCGTTTTCAGCAGCGTTTTTTACGCCGCCAACGCTTTTGCCGCGCCGCAAGATTGGCAACAAATTAAACGTCCGATTCCCGCAGAAGGCGGGAAATCGCAGGCTATCGGCAGTTATTCCAACGGTTGTATCATAGGCGCCCAGCCTTTGCCTTATAAAGGCGACGGCTATCAAGTGATTCGCATGAATAAAAACCGCTATTACGGACACCCTGACATGATTAGCTACTTGCAACGTTTGGGGCAACGCGCCAAGGCGGCGGGTTTGCCGACCATGTTGGTGGGCGATATTGCTATGCCGGGCGGCGGACGTTTTCTGACGGGACACGCCAGCCATCAAATGGGGCTGGATGCGGATATTTGGCTGCGCATGGGCAGTATGTCCGACAGCGACGCACTGAATTCCGACGGCAAAGGTTTGTTGGTGGTGAATCGCAAAGCGCAGCGGGTGGACGACAGTATTTGGAATGCCAACCACGCGAAACTAATTAAACTGGCGGCGGAAGATGTGAAAGTGACGCGTATTTTCGTTAATCCGGCGATCAAATTAAAACTCTGCGAAACCGCGGGCGCCGATCGCGCCTGGTTGCACAAAATCCGCCCGTGGTTTGGGCATGACTCCCATTTCCATGTGCGTCTGACTTGTCCGCAAGGGGCGCAGTATTGTGAGAATCAAGCGCCGGTGCCCGCCGGCGACGGTTGTGGGGAAGAACTCTATTCTTGGTTTAAACCGGCAAAACCGGGTTCAGCCCCGAGCAAACCGAAAGTTACACCGCCCGAACCGTTTTTGTGTCAGCAAGTCTTAAGCTCGCCGAATCGAAGCGAGTGGCTGGAG","","","31869","MNKTFLQFIKSAVVFSSVFYAANAFAAPQDWQQIKRPIPAEGGKSQAIGSYSNGCIIGAQPLPYKGDGYQVIRMNKNRYYGHPDMISYLQRLGQRAKAAGLPTMLVGDIAMPGGGRFLTGHASHQMGLDADIWLRMGSMSDSDALNSDGKGLLVVNRKAQRVDDSIWNANHAKLIKLAAEDVKVTRIFVNPAIKLKLCETAGADRAWLHKIRPWFGHDSHFHVRLTCPQGAQYCENQAPVPAGDGCGEELYSWFKPAKPGSAPSKPKVTPPEPFLCQQVLSSPNRSEWLE","1740196","From Genbank:[gi:1170923] This protein is involved in the removal of murein from the sacculus. It may also facilitate integration of nascent murein strands into the sacculus by cleaving the peptide bonds between neighboring strands in mature murein. ","penicillin-insensitive murein endopeptidase A","Periplasm","","
InterPro
IPR005073
Family
Peptidase M74, penicillin-insensitive murein endopeptidase
PD039139\"[31-285]TMEPA_HAEIN_P44566;
PIRSF018455\"[1-287]TPenicillin-insensitive murein endopeptidase
PF03411\"[46-285]TPeptidase_M74
noIPR
unintegrated
unintegrated
G3DSA:3.30.1380.10\"[28-285]Tno description
signalp\"[1-24]?signal-peptide


","No hits to the COGs database.","","Residues 31 to 281 match (3e-120) PD:PD039139 which is described as COMPLETE PROTEOME MUREIN PENICILLIN-INSENSITIVE ENDOPEPTIDASE HYDROLASE 3.4.99.- DD-ENDOPEPTIDASE MEPA PERIPLASMIC ","","","","","","","","","","","Fri Jan 10 14:37:30 2003","Fri Jan 10 14:37:30 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02507 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 46 to 285 (E-value = 2.3e-179) place AA02507 in the Peptidase_U6 family which is described as Penicillin-insensitive murein endopeptidase (PF03411)","","","","","Keck,W., van Leeuwen,A.M., Huber,M. and Goodell,E.W. Cloning and characterization of mepA, the structural gene of thepenicillin-insensitive murein endopeptidase from Escherichia coli. Mol.Microbiol. 4(2):209-219, 1990. PubMed: 2187143.","","Fri Jan 10 14:40:48 2003","1","","","" "AA02509","1742162","1741092","1071","ATGGCAGGAAATACCATCGGACAATTATTTCGCGTCACCACCTTCGGCGAGTCCCACGGCATTGCCTTGGGTTGCATTGTGGACGGCGTACCGCCGAACATGGCATTATCGGAAGCGGATATTCAACCGGATTTGGATCGTCGTAAACCCGGCACCTCGCGCTATACCACACCGCGCCGCGAAGACGATGAAGTGCAGATTTTATCCGGTGTCTTTGAAGGAAAAACCACCGGCACCAGTATTGGCATAATCATTAAGAACGGCGATCAACGCTCGCAGGACTATGGCGAAATTAAAGATCGCTTCCGTCCGGGACATGCAGATTTTACTTATCAACAAAAATACGGCATTCGTGATTATCGCGGCGGCGGTCGTTCTTCCGCCCGCGAAACTGCCATGCGCGTGGCGGCGGGTGCCATCGCGAAAAAATATTTACGCGAACAATTCGGCATTGAAGTGCGTGGTTTCTTAAGCCAAATCGGCGATGTCAAAATTGCGCCGCAATCCGTGGAACATATTGATTGGGCAGAAGTAAATAGCAATCTGTTTTTCTGCCCCGATAAAAGTGCGGTGGAAAAATTCGATGAATTAATTCGTGATCTGAAAAAACAAGGGGATTCTATCGGTGCTAAATTGACCGTGGTGGCGGAAAACGTCCCCGTCGGGTTGGGCGAACCGGTGTTTGATCGTTTGGATGCGGATTTAGCCCACGCATTAATGAGCATTAATGCGGTAAAAGGCGTGGAAATTGGTGACGGTTTCGCTGTGGTAGAACAAAAAGGTAGCCAACATCGTGACGAAATGATCCCGCAAGGATTTCTTTCCAACTATGCCGGCGGGATTTTGGGCGGCATCAGTTCAGGACAACCGATTATCGCCACGATTGCCCTCAAACCCACTTCCAGCATTACCATTCCGGGGCGCTCGGTGAATCTCGACAATGAATCTGTCGAAGTTGTTACTAAAGGTCGCCACGATCCTTGTGTCGGCATCCGCGCCGTGCCGATTGCGGAAGCTATGACGGCGATTGTATTGTTGGATCATTTGTTGCGTTTTAAAGCGCAATGCCGA","","","38651","MAGNTIGQLFRVTTFGESHGIALGCIVDGVPPNMALSEADIQPDLDRRKPGTSRYTTPRREDDEVQILSGVFEGKTTGTSIGIIIKNGDQRSQDYGEIKDRFRPGHADFTYQQKYGIRDYRGGGRSSARETAMRVAAGAIAKKYLREQFGIEVRGFLSQIGDVKIAPQSVEHIDWAEVNSNLFFCPDKSAVEKFDELIRDLKKQGDSIGAKLTVVAENVPVGLGEPVFDRLDADLAHALMSINAVKGVEIGDGFAVVEQKGSQHRDEMIPQGFLSNYAGGILGGISSGQPIIATIALKPTSSITIPGRSVNLDNESVEVVTKGRHDPCVGIRAVPIAEAMTAIVLLDHLLRFKAQCR","1741090","From PF01264Chorismate synthase catalyzes the last of the seven steps in the shikimate pathway which is used in prokaryotes, fungi and plants for the biosynthesis of aromatic amino acids. It catalyzes the 1,4-trans elimination of the phosphate group from5-enolpyruvylshikimate-3-phosphate (EPSP) to form chorismate which can then be used in phenylalanine, tyrosine or tryptophanbiosynthesis. Chorismate synthase requires the presence of a reduced flavin mononucleotide (FMNH2 or FADH2) for its activity.Chorismate synthase from various sources shows a high degree of sequence conservation. It is a protein of about 360 to 400 amino-acid residues. ","chorismate synthase","Cytoplasm","","
InterPro
IPR000453
Family
Chorismate synthase
PD002941\"[40-347]TAROC_HAEIN_P43875;
PTHR21085\"[3-351]TCHORISMATE SYNTHASE
PF01264\"[10-353]TChorismate_synt
TIGR00033\"[10-356]TaroC: chorismate synthase
PS00787\"[16-31]TCHORISMATE_SYNTHASE_1
PS00788\"[124-140]TCHORISMATE_SYNTHASE_2
PS00789\"[324-340]TCHORISMATE_SYNTHASE_3


","BeTs to 23 clades of COG0082COG name: Chorismate synthaseFunctional Class: EThe phylogenetic pattern of COG0082 is aompkzyqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is","Significant hit (6.2e-148) to 6/6 blocks of the IPB000453 family, which is described as \"Chorismate synthase\". Interpro entry for IP:IPR000453. IPB000453A 10-51 1e-32 IPB000453B 57-81 6.3e-19 IPB000453C 103-131 1.1e-24 IPB000453D 230-266 1.5e-28 IPB000453E 275-303 1e-17 IPB000453F 323-347 2.2e-19","Residues 3 to 37 match (1e-07) PD:PD520157 which is described as SYNTHASE COMPLETE CHORISMATE PROTEOME LYASE 5-ENOLPYRUVYLSHIKIMATE-3-PHOSPHATE PHOSPHOLYASE AMINO ACID AROMATIC ","","","","","","","","","","","Fri Jan 10 15:19:01 2003","Fri Jan 10 14:46:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02509 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 10 to 353 (E-value = 1.1e-240) place AA02509 in the Chorismate_synt family which is described as Chorismate synthase (PF01264)","","","","","Charles,I.G., Lamb,H.K., Pickard,D., Dougan,G. and Hawkins,A.R. Isolation, characterization and nucleotide sequences of the aroC genes encoding chorismate synthase from Salmonella typhi and Escherichia coli. J. Gen. Microbiol. 136(Pt 2):353-358,1990. PubMed: 2182772. White,P.J., Millar,G. and Coggins,J.R. The overexpression, purification and complete amino acid sequence of chorismate synthase from Escherichia coli K12 and its comparison with the enzyme from Neurospora crassa. Biochem. J. 251(2):313-322, 1988. PubMed: 2969724. Dmitrenko O, Wood HB Jr, Bach RD, Ganem B. A theoretical study of the chorismate synthase reaction. Org Lett. 2001 Dec 27;3(26):4137-40. PMID: 11784161Jones DG, Reusser U, Braus GH.Molecular cloning, characterization and analysis of the regulation of the ARO2 gene, encoding chorismate synthase, of Saccharomyces cerevisiae.Mol Microbiol 1991 Sep;5(9):2143-52PMID: 1837329","","Fri Jan 10 15:21:35 2003","1","","","" "AA02511","1745507","1742187","3321","ATGAAAATAAACGCTTTTTTGACCGCACTTTGTGTGGCATTGTTGCTAAACGTTGCCGTTTCGCAAAGTGCATTTGCCGATCAGAATAATGCGTTACCGACGGAAAAATCCTTAAAAGCCGATTTGGCGAATGCGCAGAAACTGCCCGATGGCGATGAGAAAAAAACATTGGTCGCCGACCTGCAAACGTCTTTGGATTTGTTACAGCAAATTCAGGCACAGCAAAAAGCCAATGATGAGCTACAGGCAACCATTAACGGCGCCGATGCGGAAATTCAAAAAGATAGCACGGATCTGCAAAATCTGAAAAAACAACTGAATACGGCAAGTGCCGATGACTATAAATCCGCCACCTTGACCTCGTTACAATCCGCTTTTGAAAAGCTAAATGCACAACAACAAGACACGCAAGCGGCATTAAATGTAGCGAATGGCTTGTTGGCGGGGCAAAGTTCCGTGTCCGAACGGGCGCAAACGGCGTTGGCGACGAATTTAAAACGCACGCAGGAACTCAATCAAAAACTTGCCGAGTCTTCTACAAGCAGCACGCTGAAACAGCAATATCAGTTAGAGTTACAACTGATCGAACTGCGCAATGCCAACAATCAATTTTTGTTGAAAAACAGCGATCAACTTACCGTATTGTATAAAAACCGTTACGATTTATTGAGCGTAAGAGTACAAGTGCAGCAGCAACAGCTTGCGCTGATTCAAGAAGTGATTAACCAAAAGAATTTGGTGCAATCGCAAAATCAGGTGGAGCAGGCGCAGCAGCAACAGCAAAGTGCGGTCAAAAATAATTTTATTCAGCAAGAACTGGAGCGTAATGCACAGTTGAGCCGCTTTTTACTTGAACAAACGGAAAAAACCAATACGCTGACTCAGGATGAATTGCGTATGCGCAACGTGTTGGAAAATTTAACCCAAACTCAGCGCACCATTGACGAGCAAATCAGCGCCTTGCAGGGCACGTTGGTGTTGTCACGAATTATCCAGCAACAAAAACAAAAACTGCCTACCAATCTAAATATTCAGGGTTTATCAAAACAAATTGCCGATTTGCGCGTGCAGATTTTTGATATTACCCAGCGCCGTAACGAGTTGTACGATTTAGATGCTTATATTACGAAGGTACAATCTGATGAAAATCAAACCTTCACCGATACGGAAAAAACGCAATTAACTAATTTGTTGACGGAACGCCGTAAAATCGCTTCCGATGTGATTAAATCATTAAATAATCAGCTGAATTTGGCGATTTCCTTAGAGTTGACCCAACAGCAGATTACGCAAATCAGTGATCGAATTCAGGCTAAACTGGATCAGCAAAGCTTCTGGGTAAAAAGTAACAACCCGCTCAACCTGGATTGGATTAAAACCTTGCCGATGTCATTGAGCACGCAATTTGACGGCATCGTTAAAAAATTAGGTTTCCCGAGTAATTTTGACAATCTGCCGTATTTATTGACTTATGTGTTTATTCTGGTAGTCATTGGCGGGATTATTTTTAAATTCAAACCGGCAATTAAACACCGCTTTGCGTTAATGAACGGTGAAATCAATACGTTGCGCTCCGACAGCCAGTGGCATACGCCGATTGCGTTGTTTTACACAGCAATTTTGTCCCTGTCAGGAACGTTATGGTTTTTGGCAATTTGTCAGCTTGTCGGCTTTTTCTTCTTCCGTAACCCGGCGGAATTCTGGCAGTGGTCGCTGAGTATGGCGGGCTATTGGTGGTTCTTTAGTTTCCTACTGGCGGTATTGCGCCCGAACGGTATTTTAGTGCGCCACTTCGGCTTTTCACAGGAAACGGCGGAGAAATTCCAATCCATTACCAAGCGGATTATTGTCGCCGTGGTTTTATTGTTGAATACTTCGATTTTCAGCAGCGTGATGGATAGCGGTTTAGCCAATGATGTGCTTGGTGAAATTAATACCATTATTGCGTTAGGGTTCTGTATCCTCATTATTGCGCCGCGCTTTAATCGCGCGGTGACGGCGTTTGGCGCAAACACGCAGGATAATCGCGATAAAATTATTCTGAAAATCGTACGCATTTTGCTACGTTTGGCGCCGGTCGGATTAATCGTATTGGTCGTGTTAGGCTACTATTACACCGCGTTAAATCTGATTTCACACATTATTAATACTTACATTGCCTGGGTGGTGTGGTCGCTTGCCCGCCATACCGTCTATCGTGCCATTACCGTGGCGTCCCGCCGTTTGGCGTATCGTCGTTTACAGGAAAAACGTCAGCAAAAACAAGCGGATTCTAACGACGGTTCTCCTTCTGACGATGTGGTAATGATTACTGAGCAGGAAGAAGGTTTGGCGTTAAATCAAGTGCGCAGCCAGTTATTGAGCTTTGCCGATTTATTCATTTGGACGGCGCTGTTTGCCATGTTCTATTATGTATGGTCGGATTTGGTCACTGTGGCAAGCTATTTGCGCGACATTACATTGTGGCAGCAAATTTCTACCACGGAAGCGGGCGTAGTAACGGAAAGTATTTCGTTATTTAACTTGCTGGTGGCGTTGGTTATCATCAGCATTACCTACATTCTGGTGCGCAATATTCCGGGGATTTTGGAAGTGATCGTATTTTCTCGGGTAAGATTGTCGCAAGGTACGCCTTATACCATCAACACCTTATTAACCTATATTTTAGTAGCTATCGGCGGCGCCTGGGCGTTTGCGACGCTGGGAATGTCGTGGTCGAAATTGCAGTGGTTATTCGCCGCACTTTCCGTCGGTCTTGGTTTCGGTATGCAGGAAATCTTTGCGAACTTCGTGTCGGGGATTATTTTATTATTTGAACGCCCGATTCGGGTCGGCGATACCGTCACTATTAATGATGTGAGCGGTACCGTAGCGAAAATTCGGATTCGTGCTATTACGTTGATAGATTTTGATCGTAAAGAAGTGATTGTGCCAAATAAATCCTTCGTGACCGGGCAGGTGATCAACTGGGCGTTATCCAATACGATGACACGTTTGGTAATTCGCGTTGGAGTTGCTTATGGTTCCAATCTTGAATTGGTGAAAAAATTATTGCTTCAAGCGGCAAATGAACAGCCGGCTGTGCTTAAAGATCCTGAACCGCGTGCATTATTTTTATCCTTTGGGGCAAGCACATTAGATCATGAATTGCGTGTTTATGTGGGGCAACTTTCCGAGCGAACAAATACCATCGACTCGCTCAATCGACGAATTAATGAATTATTTACAGAAAATAACATTGATATTGCCTTTAATCAGCTTGATGTGTTTATTAAAAATCAAGATACCGGTGCAGTCATGCCACTGATTGAAGTAAAATCT","","","125608","MKINAFLTALCVALLLNVAVSQSAFADQNNALPTEKSLKADLANAQKLPDGDEKKTLVADLQTSLDLLQQIQAQQKANDELQATINGADAEIQKDSTDLQNLKKQLNTASADDYKSATLTSLQSAFEKLNAQQQDTQAALNVANGLLAGQSSVSERAQTALATNLKRTQELNQKLAESSTSSTLKQQYQLELQLIELRNANNQFLLKNSDQLTVLYKNRYDLLSVRVQVQQQQLALIQEVINQKNLVQSQNQVEQAQQQQQSAVKNNFIQQELERNAQLSRFLLEQTEKTNTLTQDELRMRNVLENLTQTQRTIDEQISALQGTLVLSRIIQQQKQKLPTNLNIQGLSKQIADLRVQIFDITQRRNELYDLDAYITKVQSDENQTFTDTEKTQLTNLLTERRKIASDVIKSLNNQLNLAISLELTQQQITQISDRIQAKLDQQSFWVKSNNPLNLDWIKTLPMSLSTQFDGIVKKLGFPSNFDNLPYLLTYVFILVVIGGIIFKFKPAIKHRFALMNGEINTLRSDSQWHTPIALFYTAILSLSGTLWFLAICQLVGFFFFRNPAEFWQWSLSMAGYWWFFSFLLAVLRPNGILVRHFGFSQETAEKFQSITKRIIVAVVLLLNTSIFSSVMDSGLANDVLGEINTIIALGFCILIIAPRFNRAVTAFGANTQDNRDKIILKIVRILLRLAPVGLIVLVVLGYYYTALNLISHIINTYIAWVVWSLARHTVYRAITVASRRLAYRRLQEKRQQKQADSNDGSPSDDVVMITEQEEGLALNQVRSQLLSFADLFIWTALFAMFYYVWSDLVTVASYLRDITLWQQISTTEAGVVTESISLFNLLVALVIISITYILVRNIPGILEVIVFSRVRLSQGTPYTINTLLTYILVAIGGAWAFATLGMSWSKLQWLFAALSVGLGFGMQEIFANFVSGIILLFERPIRVGDTVTINDVSGTVAKIRIRAITLIDFDRKEVIVPNKSFVTGQVINWALSNTMTRLVIRVGVAYGSNLELVKKLLLQAANEQPAVLKDPEPRALFLSFGASTLDHELRVYVGQLSERTNTIDSLNRRINELFTENNIDIAFNQLDVFIKNQDTGAVMPLIEVKS","1742185","","transmembrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR000209
Domain
Peptidase S8 and S53, subtilisin, kexin, sedolisin
PS00136\"[629-639]?SUBTILASE_ASP
InterPro
IPR006685
Family
MscS Mechanosensitive ion channel
PF00924\"[882-1083]TMS_channel
InterPro
IPR006686
Domain
MscS Mechanosensitive ion channel, middle
PS01246\"[955-989]TUPF0003
noIPR
unintegrated
unintegrated
signalp\"[1-26]?signal-peptide
tmhmm\"[5-25]?\"[485-503]?\"[533-553]?\"[575-595]?\"[610-630]?\"[636-658]?\"[679-701]?\"[707-727]?\"[786-806]?\"[836-856]?\"[877-899]?\"[905-923]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 3.8e-29) to 2/2 blocks of the IPB001880 family, which is described as \"Uncharacterized protein family UPF0003\". Interpro entry for IP:IPR001880. IPB001880A 913-948 5.9e-17 IPB001880B 957-990 9.4e-11","Residues 458 to 512 match (8e-08) PD:PD438798 which is described as PROTEOME TRANSMEMBRANE COMPLETE HI0195.1 SIGNAL PRECURSOR ","","","","","","","","","","","","Fri Jan 10 15:59:39 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02511 is paralogously related to AA02100 (4e-05), AA00579 (3e-04) and AA02347 (8e-04).","","","","","","Residues 883 to 1083 (E-value = 2.5e-81) place AA02511 in the MS_channel family which is described as Mechanosensitive ion channel (PF00924)","","","","","","","","1","","","" "AA02512","1746931","1745519","1413","ATGGCTCTTGGTAGCAAATTCGCACAATCTTCTTTATTCTCCGAACGAATCGCCTTGCAAGTATTGCAAGGCGACGCTTTTACATGGCGCCAACTGGTTGAAAAAACGCTACAAATTTCCGCATATCTGCAGCAATTGGGTGTAGAAAAACAATGTGGTGTCGCGCTATGCGGAAAAAATAGTCTTGAACTGCTGCTATTTTATTTGGCGGCGATTCAGACGGGGGCGCGGGTGTTAATGCTTAATCCGATGTTCCCGTTGGAAAAACGCATTGCTCTTTGTCAATCTAATCATGCGGATTTTTACTTTACGGCAGAGCAGAAGGCATTTGCTAGCGAGCAACAAAAGTGCGGTCCAATTTTCAAGTGTTTTTTAACCCTGAACGACGCCATGGCACAGGCAAATCAAATTCACGCTTACTCGGATGTTGATATTGATTTTTCTCAACCTGCCACCATGACGCTCACTTCCGGTTCCACAGGCTTACCGAAAGCCGTAGTGCACAATGTACAAGCCCATTTGGATAACGCCCGAGGCGTGTGTGAGTTAATGAACTTTGACGCAGCGGATTCGTGGCTGCTTTCCTTGCCCTTATACCATGTCTCCGGACAGGGGATTGTGTGGCGTTGGTTGACCGGCGCTACCACCTTGGTGTTACCCGGTGAAGATTTTTATGCGGCAGTGAATCAAGTGACCCATGTCTCGTTGGTGCCGACGCAGGTTCAACGTTGGTTGCAATATTTGCAGGAAAACCCGGCGCCGTTACAAATCAAGGCGGTGCTGCTTGGCGGCGCGCATATTTCCTTAACGCTTACCCGGGCGTTGCAACAGTTGGGTATTAAAAGCTATTGCGGTTACGGTATGACGGAAATGGCATCCACAGTGTTTGCCAAAGAGAGTGACGAAAAAAATGGTGTGGGAAACGTCTTAGCCGGGCGTGAATATTGCCTGCAAAATGGCGAAATTTGGCTACGTGGCGCGGGATTGGCACTCGGTTATTGGCAGCAGGGGAGAATTGTTTCGCTACTGAATGAACAGGGTTGGTTTGCTACCAAAGATAAAGGGCAATGGCAGAATGGCGAGCTTGTGATTTCGGGGCGAATTGATAATATGTTCATTTCCGGTGGGGAAAATATTCAGCCGGAAGAGATTGAAAAGGTGATATTGCAGTCTGATTTAGTTAAGCAGGTTTTTGTGTTGCCTATGGCGGATTTGGAATTCGGTCAGCGACCGGTTGCAATCATTGAGTGGTTGGAAAAATCCAAAAGTGCGGTGGAAAATCTGCGCGAATTTTTACAAGGGCGGTTGGAACGATTTAAACAGCCTGTTGCCTGTTATGATCTGCCGTTAAATTTAACCGACGGCGCTATTAAGATTTCACGGAAAACGTTGGCGGATTGGCTGGCGCAGCAA","","","52287","MALGSKFAQSSLFSERIALQVLQGDAFTWRQLVEKTLQISAYLQQLGVEKQCGVALCGKNSLELLLFYLAAIQTGARVLMLNPMFPLEKRIALCQSNHADFYFTAEQKAFASEQQKCGPIFKCFLTLNDAMAQANQIHAYSDVDIDFSQPATMTLTSGSTGLPKAVVHNVQAHLDNARGVCELMNFDAADSWLLSLPLYHVSGQGIVWRWLTGATTLVLPGEDFYAAVNQVTHVSLVPTQVQRWLQYLQENPAPLQIKAVLLGGAHISLTLTRALQQLGIKSYCGYGMTEMASTVFAKESDEKNGVGNVLAGREYCLQNGEIWLRGAGLALGYWQQGRIVSLLNEQGWFATKDKGQWQNGELVISGRIDNMFISGGENIQPEEIEKVILQSDLVKQVFVLPMADLEFGQRPVAIIEWLEKSKSAVENLREFLQGRLERFKQPVACYDLPLNLTDGAIKISRKTLADWLAQQ","1745517","","O-succinylbenzoate--CoA ligase","Cytoplasm, Inner membrane","","
InterPro
IPR000873
Domain
AMP-dependent synthetase and ligase
PR00154\"[148-159]T\"[160-168]TAMPBINDING
PF00501\"[28-399]TAMP-binding
PS00455\"[153-164]TAMP_BINDING
InterPro
IPR010192
Family
O-succinylbenzoate-CoA ligase
TIGR01923\"[28-464]TmenE: O-succinylbenzoate-CoA ligase
noIPR
unintegrated
unintegrated
G3DSA:3.30.300.30\"[369-470]Tno description
G3DSA:3.40.50.980\"[7-106]T\"[146-309]Tno description
PTHR11968\"[15-106]T\"[122-470]TATP-DEPENDENT AMP-BINDING ENZYME FAMILY MEMBER
PTHR11968:SF14\"[15-106]T\"[122-470]TO-SUCCINYLBENZOIC ACID--COA LIGASE


","BeTs to 17 clades of COG0318COG name: Acyl-CoA synthetases (AMP-forming)/AMP-acid ligases IIFunctional Class: I,QThe phylogenetic pattern of COG0318 is aomp-zy--drlbcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 5.1e-08) to 2/2 blocks of the IPB000873 family, which is described as \"AMP-dependent synthetase and ligase\". Interpro entry for IP:IPR000873. IPB000873A 155-170 0.00023 IPB000873B 190-200 0.091","Residues 128 to 355 match (1e-07) PD:PD137166 which is described as LIGASE PROTEOME COMPLETE O-SUCCINYLBENZOIC ACID-COA O-SUCCINYLBENZOYL-COA SYNTHETASE MENE O-SUCCINYLBENZOATE--COA XCLB ","","","","","","","","","","","","Fri Jan 10 16:33:37 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02512 is paralogously related to AA02598 (1e-13), AA00231 (8e-11), AA02108 (1e-08) and AA01193 (1e-05).","","","","","","Residues 28 to 399 (E-value = 6.9e-61) place AA02512 in the AMP-binding family which is described as AMP-binding enzyme (PF00501)","","","","","Sharma,V., Hudspeth,M.E. and Meganathan,R.Menaquinone (vitamin K2) biosynthesis: localization andcharacterization of the menE gene from Escherichia coliGene 168 (1), 43-48 (1996)PubMed: 8626063Meganathan R, Bentley R. Biosynthesis of o-succinylbenzoic acid in a men- Escherichia coli mutant requires decarboxylation of L-glutamate at the C-1 position. Biochemistry. 1981 Sep 1;20(18):5336-40. PMID: 6117313","","Fri Jan 10 16:37:56 2003","1","","","" "AA02513","1747554","1746940","615","ATGAAAATTATCGAAGTGGACGAAGAACTTTATCAATATATTGCCGGTAACACGCAATCTATTGGCGAAAGTGCATCCGATATTTTACGGCGCTTATTAAACCTTTCCCCGCACAACACATATTTCAGTTTACCGGAAAATCAACCGACGATCGTCACCTCTCCATCAGACGCCAAAGCAGAAGCAACGGAACAAACCACGATTTTTGAAGAAGAAATCAATAAGCCGGTGACGAGAAAACAATCTGATAAAGTGATGCAGAAAACCATCAGTAAATTGGAAACCTTGTTACATTCCGAAGAATTCAAACAGGAAAACAAAGCGGTTATTCGTTTTTTAGCGATTTTGACCATTTTGTATCGCACCAATCCGGAAGGATTTGCGCTTGCCACCGAATCGTTACAAGGGCGCACCCGCGTGTATTTTGCCAGAGATGAAGGCACATTGCTGATGGCGGGCAATCACACCAAACCGAAACAAATTCCCGATACGCCGTATTGGGTGATCACCAATACCAACAGCGGTCGTAAAATGCTCATGCTGGAAGGTGCGATGCAATCCATGCACTTGCCGGAATCGTTAATTGATCAAGTGCGGTTATTTTTTACGGCAAAT","","","23296","MKIIEVDEELYQYIAGNTQSIGESASDILRRLLNLSPHNTYFSLPENQPTIVTSPSDAKAEATEQTTIFEEEINKPVTRKQSDKVMQKTISKLETLLHSEEFKQENKAVIRFLAILTILYRTNPEGFALATESLQGRTRVYFARDEGTLLMAGNHTKPKQIPDTPYWVITNTNSGRKMLMLEGAMQSMHLPESLIDQVRLFFTAN","1746938","From Genbank:[gi:1173426] This protein is a negative regulator of replication initiation.It is required for sequestration, a process that blocks secondary initiation events. It could block the allosteric transition of DNAA from an inactive form to an active form. ","seqA protein","Cytoplasm","","
InterPro
IPR005621
Family
SeqA protein
PD035808\"[96-182]TSEQA_HAEIN_P44564;
PF03925\"[1-202]TSeqA


","BeTs to 3 clades of COG3057COG name: Negative regulator of replication initiationRFunctional Class: LThe phylogenetic pattern of COG3057 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 1 to 198 match (3e-62) PD:PD035808 which is described as PROTEOME COMPLETE SEQA REPLICATION NEGATIVE INITIATION DNA MODULATOR INHIBITOR REPLICATION ","","","","","","","","","","","Thu Jan 16 14:52:03 2003","Thu Jan 16 14:52:03 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02513 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 202 (E-value = 1.8e-113) place AA02513 in the SeqA family which is described as SeqA protein (PF03925)","","","","","Lu,M., Campbell,J.L., Boye,E. and Kleckner,N. SeqA: a negative modulator of replication initiation in E. coli. Cell 77(3):413-426. PubMed: 8011018. Slater,S., Wold,S., Lu,M., Boye,E., Skarstad,K. and Kleckner,N. E.coli SeqA protein binds oriC in two different methyl-modulated reactions appropriate to its roles in DNA replication initiation and origin sequestration. Cell 82(6):927-936. PubMed: 7553853.","","Thu Jan 16 14:59:00 2003","1","","","" "AA02514","1747641","1748438","798","ATGCAAAAATTACTCAAATTTCAATTTAATGAATTAAAACAAGCAATTAACAAGCCGACTCTGGTTTTTATTCACGGTTTATTCGGCGATATGAATAATTTGGGTATTATTGCCCGCGCATTTAGTGAAGATTATGCCATTTTACGGGTAGATTTGCGCAATCACGGCGCGAGCTTTCACAGTGAAGAAATGAACTATGATTTGATGGCGGAAGATGTGTTTCATGTCATTCAATCCTTATCACTGCGCGAAGTGATTTTGGTGGGTCATTCTATGGGCGGCAAAACCGCCATGGTACTGGCGGCGAATTCTCCTGATTTGGTAAAAGGACTGGTGGTGATTGATATTGCGCCCATTGCCTACGGCGAACATGGGCATGATGCGATTTTCAACGGGTTATTTGCGGTGAAAAACACGCAGCCTCATACCCGTCAGGAAGCCAAACCAATTTTGGCACAACATATTTACGATGAAAGCGTGCAACAGTTTATGCTGAAGTCTTTTGATGCCACAAGCGTCGATTATTTTCGTTTTAATTTGACCGCACTTAAACGCAATTACCCTAACCTGATGGGATGGCAAACCCGCCACATTCAACAACCCTGCCTGTTCATTAAAGGTGGCAATTCGTCCTATATTCTGCCGGAATATGCCGATCGCATTTTGGCCCAATGCCCGCAGGCAAGTTCCTTCACCATTAACGGCAGCGATCACTGGGTACACGCCGAGAAACCACAATTTGTAATTCGTGCTATCACGAACTTTTTAAATAAAATTAATAGCGAATACAAGTCTAAA","","","30114","MQKLLKFQFNELKQAINKPTLVFIHGLFGDMNNLGIIARAFSEDYAILRVDLRNHGASFHSEEMNYDLMAEDVFHVIQSLSLREVILVGHSMGGKTAMVLAANSPDLVKGLVVIDIAPIAYGEHGHDAIFNGLFAVKNTQPHTRQEAKPILAQHIYDESVQQFMLKSFDATSVDYFRFNLTALKRNYPNLMGWQTRHIQQPCLFIKGGNSSYILPEYADRILAQCPQASSFTINGSDHWVHAEKPQFVIRAITNFLNKINSEYKSK","1748436","From PF00561: alpha/beta hydrolase foldThe alpha/beta hydrolase fold is common to a number of hydrolytic enzymes of widely differing phylogenetic origin and catalytic function. The core of each enzyme is an alpha/beta-sheet (rather than a barrel), containing 8 strands connected by helices. The enzymes are believed to have diverged from a common ancestor, preserving the arrangement of the catalytic residues. All have a catalytic triad, the elements of which are borne on loops, which are the best conserved structural features of the fold.","esterase/lipase","Cytoplasm","","
InterPro
IPR000073
Domain
Alpha/beta hydrolase fold-1
PF00561\"[45-254]TAbhydrolase_1
InterPro
IPR008262
Active_site
Lipase, active site
PS00120\"[85-94]TLIPASE_SER
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1820\"[17-256]Tno description
PTHR10992\"[17-262]TALPHA/BETA HYDROLASE RELATED
PTHR10992:SF17\"[17-262]TVALACYCLOVIR HYDROLASE
tmhmm\"[21-41]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 3.6e-06) to 3/4 blocks of the PR00111 family, which is described as \"Alpha/beta hydrolase fold signature\". Prints database entry for PR:PR00111. PR00111A 44-59 63 PR00111B 87-100 0.001 PR00111C 101-114 22","Residues 135 to 256 match (2e-38) PD:PD013191 which is described as COMPLETE PROTEOME 3.1.-.- ESTERASE/LIPASE HYDROLASE R05D7.4 YBFF PM0355 HI0193 C22H12.03 ","","","","","","","","","","","Thu Jan 16 15:06:39 2003","Thu Jan 16 15:12:22 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02514 is paralogously related to AA00087 (3e-05).","","","","","","Residues 45 to 254 (E-value = 2.1e-22) place AA02514 in the Abhydrolase_1 family which is described as alpha/beta hydrolase fold (PF00561)","","","","","Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Schrag J, et al.The alpha/beta hydrolase fold.Protein Eng 1992 Apr;5(3):197-211PMID: 1409539","","Thu Jan 16 15:06:39 2003","1","","","" "AA02515","1748861","1749382","522","ATGGCTGTTGTCGGCTTATTTTATGGTAGTGACACAGGCAATACGGAAAATATTGCCAAAATGATTCAAAAACAATTAGGTAGTGAATTAGTCGATATTCGCGACATCGCAAAAAGCAGCAAAGAAGATATTGAAGCTTACGACTTTCTGCTATTCGGTATCCCGACTTGGTATTATGGTGAAGCGCAATGCGACTGGGATGATTTCTTCCCGACATTGGAACAAATTGATTTTACGGATAAACTCGTAGCAATTTTCGGTTGTGGCGACCAAGAGGATTACGCAGATTATTTCTGTGATGCCATGGGAACAGTGCGCAACATTATTGAACCGCACGGCGCCATTATCGTAGGCAACTGGTCAACCGAAGGCTATAGTTTTGAATCTTCACAAGCATTAATCGACAATGATACCTTTGTCGGCTTGTGCATTGATGAAGATCGCCAGCCTGAATTAACATCCGAACGTGTAAATAAATGGGTTAAACAAGTCTATGAAGAGATGTGCTTAGCCGAATTAGCT","","","19681","MAVVGLFYGSDTGNTENIAKMIQKQLGSELVDIRDIAKSSKEDIEAYDFLLFGIPTWYYGEAQCDWDDFFPTLEQIDFTDKLVAIFGCGDQEDYADYFCDAMGTVRNIIEPHGAIIVGNWSTEGYSFESSQALIDNDTFVGLCIDEDRQPELTSERVNKWVKQVYEEMCLAELA","1749380","From Genbank:[gi:120278] This protein is a low-potential electron donor to a number of redox enzymes.","flavodoxin","Cytoplasm","","
InterPro
IPR001094
Domain
Flavodoxin-like
PR00369\"[5-18]T\"[51-62]T\"[80-90]TFLAVODOXIN
InterPro
IPR001226
Domain
Flavodoxin, N-terminal
PS00201\"[6-22]TFLAVODOXIN
InterPro
IPR008254
Domain
Flavodoxin/nitric oxide synthase
PF00258\"[6-160]TFlavodoxin_1
PS50902\"[4-165]TFLAVODOXIN_LIKE
InterPro
IPR010086
Family
Flavodoxin, long chain
TIGR01752\"[3-169]Tflav_long
InterPro
IPR014357
Family
Flavodoxin
PIRSF000088\"[1-171]TFlavodoxin
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.360\"[1-170]TG3DSA:3.40.50.360
SSF52218\"[2-168]TSSF52218


","No hits to the COGs database.","Significant hit ( 7.6e-39) to 4/4 blocks of the IPB001226 family, which is described as \"Flavodoxin\". Interpro entry for IP:IPR001226. IPB001226A 6-22 1.3e-11 IPB001226B 50-60 5e-05 IPB001226C 80-91 1e-06 IPB001226D 139-160 1.1e-10Significant hit ( 2.6e-11) to 3/4 blocks of the PR00369 family, which is described as \"Flavodoxin signature\". Prints database entry for PR:PR00369. PR00369A 5-18 3.2e-05 PR00369B 51-62 1.1 PR00369C 80-90 0.15","Residues 122 to 164 match (5e-14) PD:PD008246 which is described as FLAVODOXIN ELECTRON FMN FLAVOPROTEIN PROTEOME COMPLETE FIXATION NITROGEN 3D-STRUCTURE PLASMID ","","","","","","","","","","","Thu Jan 16 15:56:45 2003","Thu Jan 16 15:56:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02515 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 6 to 160 (E-value = 3.2e-53) place AA02515 in the Flavodoxin_1 family which is described as Flavodoxin (PF00258)","","","","","Ekins A, Niven DF. Identification of fur and fldA homologs and a Pasteurella multocida tbpA homolog in Histophilus ovis and effects of iron availability on their transcription. J Bacteriol. 2002 May;184(9):2539-42. PMID: 11948169 Gaudu P, Weiss B. Flavodoxin mutants of Escherichia coli K-12. J Bacteriol. 2000 Apr;182(7):1788-93. PMID: 1071498 Jenkins,C.M. and Waterman,M.R. Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities J. Biol. Chem. 269 (44), 27401-27408 (1994) PubMed: 7961651 Ponstingl,H. and Otting,G. NMR assignments, secondary structure and hydration of oxidized Escherichia coli flavodoxin Eur. J. Biochem. 244 (2), 384-399 (1997) PubMed: 9119004 Hoover,D.M. and Ludwig,M.L. A flavodoxin that is required for enzyme activation: the structure of oxidized flavodoxin from Escherichia coli at 1.8 A resolution Protein Sci. 6 (12), 2525-2537 (1997) PubMed: 9416602 ","","Thu Jan 16 15:56:45 2003","1","","","" "AA02516","1749404","1749841","438","ATGTCTGAAGAAAATATTAAATTATTAAAAAAAGTAGGATTAAAAATTACCGAACCCCGTTTAACCATTCTCGCTTTAATGCAAAAACACAGAGAACACCATTTTTCTGCTGAAGACGTTTACAAAATGTTATTGGAAAATGGCGAAGACATCGGTCTAGCAACAGTATACCGTGTATTAAACCAGTTTGATGAAGCAAAGATTCTTATTCGCCATAACTTTGAAGGCAATAAATCAGTTTTCGAACTGGCGCCAACCCAACATCATGACCACATTATCTGCACCGATTGCGGCAAAGTCTTTGAATTCAATGACGAGTTAATCGAAAGTCGCCAAAAAGAAATCAGTAAACAACACGGTATTGAGCTTTCCAGTCACAACCTGTACCTTTACGGCAAGTGTAGCGACATTAATCATTGCGCAGAAAATAACAAAAAA","","","16929","MSEENIKLLKKVGLKITEPRLTILALMQKHREHHFSAEDVYKMLLENGEDIGLATVYRVLNQFDEAKILIRHNFEGNKSVFELAPTQHHDHIICTDCGKVFEFNDELIESRQKEISKQHGIELSSHNLYLYGKCSDINHCAENNKK","1749839","From Genbank:[gi:3913694] This protein acts as a global negative controlling element employing Fe(2+) as a cofactor to bind the operator of the repressed genes. From PF01475: Ferric uptake regulator family. This family includes metal ion uptake regulator proteins, that bind to the operator DNA and controls transcription of metal ion-responsive genes. This family is also known as the FUR family.","ferric uptake regulation protein","Cytoplasm","","
InterPro
IPR002481
Family
Ferric-uptake regulator
PD002003\"[36-141]TFUR
PF01475\"[11-131]TFUR
noIPR
unintegrated
unintegrated
SSF46785\"[3-136]TSSF46785


","BeTs to 19 clades of COG0735COG name: Fe2+/Zn2+ uptake regulation proteinsFunctional Class: PThe phylogenetic pattern of COG0735 is a--p-z-qvdrlbcefghsnuj--twNumber of proteins in this genome belonging to this COG is","Significant hit ( 3.9e-39) to 3/3 blocks of the IPB002481 family, which is described as \"Ferric uptake regulator family\". Interpro entry for IP:IPR002481. IPB002481A 9-22 0.00015 IPB002481B 34-77 2.7e-25 IPB002481C 88-98 2.5e-06","Residues 7 to 93 match (5e-07) PD:PD575237 which is described as PROTEOME COMPLETE REGULATOR RESPONSE IRON UPTAKE REGULATION FERRIC TRANSCRIPTION REGULATOR ","","","","","","","","","","","Thu Jan 16 16:12:52 2003","Thu Jan 16 16:12:52 2003","","Thu Aug 4 11:22:52 2005","Thu Aug 4 11:31:06 2005","Thu Mar 18 09:33:18 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02516 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Mar 18 09:33:18 2004","","","","","Residues 11 to 131 (E-value = 5.8e-68) place AA02516 in the FUR family which is described as Ferric uptake regulator family (PF01475)","Thu Mar 18 09:33:18 2004","","","Jacobsen I, Gerstenberger J, Gruber AD, Boss JT, Langford PR, Hennig-Pauka I, Meens J, Gerlach GF.Deletion of the ferric uptake regulator Fur impairs the in vitro growth and virulence of Actinobacillus pleuropneumoniae.Infect Immun. 2005 Jun;73(6):3740-4.PMID: 15908404","Carson,S.D., Thomas,C.E. and Elkins,C., Cloning and sequencing of a Haemophilus ducreyi fur homolog.Gene 176 (1-2), 125-129 (1996), PubMed: 8918243Delany I, Spohn G, Pacheco AB, Ieva R, Alaimo C, Rappuoli R, Scarlato V. Autoregulation of Helicobacter pylori Fur revealed by functional analysis of the iron-binding site. Mol Microbiol. 2002 Nov;46(4):1107-22. PMID: 12421315 Colquhoun D, Sorum H. Cloning, characterisation and phylogenetic analysis of the fur gene in Vibrio salmonicida and Vibrio logei. Gene. 2002 Aug 21;296(1-2):213. PMID: 12383519 Baichoo N, Helmann JD. Recognition of DNA by fur: a reinterpretation of the fur box consensus sequence. J Bacteriol. 2002 Nov;184(21):5826-32. PMID: 12374814 Escolar L, Perez-Martin J, de Lorenzo V. Binding of the fur (ferric uptake regulator) repressor of Escherichia coli to arrays of the GATAAT sequence. J Mol Biol 1998 Oct 30;283(3):537-47 PMID: 9784364Bahrami F, Niven DF.Iron acquisition by Actinobacillus suis: Identification and characterization of a single-component haemoglobin receptor and encoding gene.Microb Pathog. 39(1-2):45-51.PMID: 15899574","Thu Aug 4 11:31:06 2005","Thu Aug 4 11:31:06 2005","1","","","" "AA02518","1749847","1750008","162","ATGCAAAAGGCGGTCTCAAAACCGCCCTTTCTATCTCTGAAAACATCTGAAAAATCAACCGCACTTTTCGCCTATAAACCGAGATTTTTCTTAGGGAAAAGTACCTCTCCGTGCTATAATCACGCCAATTTTTCACTATTAAATTCAATCATTAGGAAATTC","","","6125","MQKAVSKPPFLSLKTSEKSTALFAYKPRFFLGKSTSPCYNHANFSLLNSIIRKF","1750008","","hypothetical protein","Periplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 09:14:10 2004","Wed Feb 25 09:14:10 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02518 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 09:14:10 2004","","","","","","","","","","","","","1","","","" "AA02519","1750012","1752672","2661","ATGTCTGATTTAATCCAAGATATTACGCCGGTAAGCCTTGAAGAAGAATTGAAATCTTCATACCTTGATTACGCCATGTCCGTTATTGTGGGGCGCGCCCTGCCCGATGTGCGTGACGGCTTAAAACCGGTACACCGCCGCGTGTTATTTGCGATGCATGAAGGGGGCAATCTCTACAACAAACCTTATCGTAAATCCGCCCGTATCGTCGGTGACGTGATCGGTAAATACCACCCGCACGGCGACAGCGCGGTATATGACACGTTAGTACGTATGGCGCAGCCGTTCTCCTTACGTTATATGTTGGTGGACGGGCAAGGTAACTTTGGTTCGGTGGACGGCGACGCGCCGGCGGCAATGCGTTATACGGAAGCCCGTATGACCAAAATCGCCCACGAATTATTGGCTGATTTAGACAAAGAAACCGTCAATTTCGTGCCAAACTACGATGGTTCCGAAATGATTCCCGAAGTGCTGCCGACCAAAGTCCCGGCGCTATTGGTAAACGGTTCCTCCGGGATTGCAGTGGGGATGGCAACCAACATTCCGCCACACAACTTGGGCGAAGTGTTGGACGGCTGTCTGGCTTATATCGAAAATAACGACATTACCATTGATGAATTAATGAGCCACATTCCCGGCCCGGATTTCCCGACGGCGGCATTGATCAACGGACGTAAAGGCATTGAAGAAGCCTATAAAACCGGACGCGGAAAAATTTACGTACGCGCCCGCGCAGAAATCGAAACCGATGAAAAAGGCCGTGAAAGCATCATCGTGAACGAAATTCCGTATCAAGTGAACAAAGCGAAACTCATCGAAAAAATTGCCGATTTCGTCAAAGACAAAAAAATTGAGGGGATCAGCGGGTTGCGCGATGAATCCGACAAAGACGGTATGCGCATCGTCATCGAAATCAAACGTGATGCGGTCGGCGAAGTGGTGTTAAATAACCTGTATGCGTTGACACAAATGCAAGTCACTTTCGGGATTAATATTGTCGCACTTGACCACGGTCAGCCCAAACTATTGAATTTAAAACAGCTCATTGAGGCGTTCGTATTACACCGCCGCGAAGTGGTGACCCGTCGTACGATTTTTGAATTACGCAAAGCCCGTGAACGTACGCACATCTTAGAAGGCTTGGCGATTGCCTTGGCAAACGTCGATCCGATTATCGAATTAATCCGCAAAGCACCAAATCCGGAAAACGCCAAACGTGAATTGCTCACCCATCCATGGCAGCTGGGTCATGTCGCCGATATGTTGGCGGCAAGCGGTGTCGATGCCGCTCGTCCGGAAGATTTGGACGAACAATATGGCATTCGTGACGGTTTATATTATTTAACCGAAGTGCAAGCACAAGCCATTTTAGATTTACGTTTGCAAAAATTAACCAATTTAGGTCACGATGAAATCCTGGACGAATACAAAAAATTATTGGATGCCATCGGTAAATTATTGTACATCTTGCGTAGCCCTGAGCGTTTAATGGAAGTGATTCGTGAAGAATTGGAGCAAATCCGCGAGCAATTTAACGATCCGCGCAGAACCGAAATCACGGCGGCTTCCGGTGATATAAATCTGGAAGATTTGATTGCCCAAGAAGATGTGGTGGTGACCCTTTCCCACGAAGGTTATGTGAAATATCAACCGATTACCGACTACGAAGCACAGCGTCGTGGTGGTAAAGGTAAATCCGCAACCAAAATGAAAGAAGAAGATTTTATCGAAAAATTACTGGTTGCCAACACCCACGATACCATTCTCTGCTTCTCCAGCCGCGGACGTTTATACTGGCTGAAAGTATATCAACTACCGCAAGCCAGCCGTGGCGCGCGCGGACGACCAATCGTGAATATTTTGCCGTTAAATGAAAATGAACGGATCACCGCTATTCTACCGGTCGCCGCCTACGAGGAAGACAAATTCGTCGTCATGGCAACCGCCGGTGGGATTGTGAAGAAAATCGCATTAACAGAATTCAGCCGTCCGCGTTCCAGCGGGATTATCGCCCTTAACTTGCGTGATGAAGATGAGTTAATCGGCGTGGATATTACCGACGGCAGCAATGAAATCATGTTGTTCTCCTCTCAAGGTCGCGTGGTGCGCTTCAGCGAATCCGCCGTGCGTGCTATGGGGCGCTTGGCAACGGGTGTGCGCGGGATCAAACTCGCCTTAACCAATGATCTGAATGACGACGAAAGTGCGGTGGAAATTGAAGACGTTTCTGATGATAACGCAGAAGAAACCTTGGATTTAAATATCGACAAAGTCGTTTCTTTAGTCATTCCGAAAAACAACGGCGAAATTCTCACCGCAACGCAGAATGGCTACGGTAAACGGACGAAACTGGATGAGTATCCGACCAAATCCCGCAACACTAAAGGGGTGATTTCCATTAAAGTGAGTGAGCGTAACGGCAAAGTCGTGGCGGCGGCACAAGTGGAAGAAAACGACCAAATCATGTTAATCACCGATGCAGGCACCCTTGTTCGCACCCGAGTAAGCGAAGTCAGCATCGTTGGACGTAACACCCAAGGCGTTCGCTTAATCCGCACCAGCGAAGCAGAACACGTTGTGAGTTTAGAACGTATCTGCGAAGTGGATGACGAAGAAAGTGAAAATCCGACAGAAAGTGCGGTAGAAAATAACGAAGAA","","","98750","MSDLIQDITPVSLEEELKSSYLDYAMSVIVGRALPDVRDGLKPVHRRVLFAMHEGGNLYNKPYRKSARIVGDVIGKYHPHGDSAVYDTLVRMAQPFSLRYMLVDGQGNFGSVDGDAPAAMRYTEARMTKIAHELLADLDKETVNFVPNYDGSEMIPEVLPTKVPALLVNGSSGIAVGMATNIPPHNLGEVLDGCLAYIENNDITIDELMSHIPGPDFPTAALINGRKGIEEAYKTGRGKIYVRARAEIETDEKGRESIIVNEIPYQVNKAKLIEKIADFVKDKKIEGISGLRDESDKDGMRIVIEIKRDAVGEVVLNNLYALTQMQVTFGINIVALDHGQPKLLNLKQLIEAFVLHRREVVTRRTIFELRKARERTHILEGLAIALANVDPIIELIRKAPNPENAKRELLTHPWQLGHVADMLAASGVDAARPEDLDEQYGIRDGLYYLTEVQAQAILDLRLQKLTNLGHDEILDEYKKLLDAIGKLLYILRSPERLMEVIREELEQIREQFNDPRRTEITAASGDINLEDLIAQEDVVVTLSHEGYVKYQPITDYEAQRRGGKGKSATKMKEEDFIEKLLVANTHDTILCFSSRGRLYWLKVYQLPQASRGARGRPIVNILPLNENERITAILPVAAYEEDKFVVMATAGGIVKKIALTEFSRPRSSGIIALNLRDEDELIGVDITDGSNEIMLFSSQGRVVRFSESAVRAMGRLATGVRGIKLALTNDLNDDESAVEIEDVSDDNAEETLDLNIDKVVSLVIPKNNGEILTATQNGYGKRTKLDEYPTKSRNTKGVISIKVSERNGKVVAAAQVEENDQIMLITDAGTLVRTRVSEVSIVGRNTQGVRLIRTSEAEHVVSLERICEVDDEESENPTESAVENNEE","1752670","From Genbak:[gi:17865733] DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. ","DNA gyrase A","Cytoplasm","","
InterPro
IPR002205
Domain
DNA topoisomerase, type IIA, subunit A or C-terminal
PD000742\"[47-122]TQ8L3L8_ACTAC_Q8L3L8;
PF00521\"[32-513]TDNA_topoisoIV
SM00434\"[11-498]TTOP4c
InterPro
IPR005743
Family
DNA gyrase, subunit A
TIGR01063\"[8-868]TgyrA: DNA gyrase, A subunit
InterPro
IPR006691
Repeat
DNA gyrase/topoisomerase IV, subunit A, C-terminal beta-pinwheel
PF03989\"[536-585]T\"[586-638]T\"[642-689]T\"[690-745]T\"[768-818]T\"[819-868]TDNA_gyraseA_C
InterPro
IPR013757
Domain
DNA topoisomerase, type IIA, subunit A, alpha-helical
G3DSA:1.10.268.10\"[369-492]Tno description
InterPro
IPR013758
Domain
DNA topoisomerase, type IIA, subunit A or C-terminal, alpha-beta
G3DSA:3.90.199.10\"[30-296]Tno description
noIPR
unintegrated
unintegrated
PTHR10169\"[32-192]TDNA TOPOISOMERASE/GYRASE
PTHR10169:SF2\"[32-192]TDNA TOPOISOMERASE II


","BeTs to 22 clades of COG0188COG name: DNA gyrase (topoisomerase II) A subunitFunctional Class: LThe phylogenetic pattern of COG0188 is ao-p--yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 3.7e-96) to 6/6 blocks of the IPB002205 family, which is described as \"DNA gyrase/topoisomerase IV, subunit A\". Interpro entry for IP:IPR002205. IPB002205A 32-50 2.2e-15 IPB002205B 65-100 2.1e-33 IPB002205C 113-127 9.9e-11 IPB002205D 169-190 6.3e-21 IPB002205E 212-221 0.00025 IPB002205F 231-240 0.00015","Residues 490 to 622 match (4e-07) PD:PD568977 which is described as A PROTEOME CHAIN COMPLETE TOPOISOMERASE ISOMERASE DNA ","","","","","","","","","","","Thu Jan 16 10:26:00 2003","Thu Jan 16 10:22:54 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02519 is paralogously related to AA02491 (1e-104).","","","","","","Residues 819 to 868 (E-value = 3.5e-14) place AA02519 in the DNA_gyraseA_C family which is described as DNA gyrase C-terminal domain, beta-propeller (PF03989)","","","","","Griggs,D.J., Gensberg,K. and Piddock,L.J.Mutations in gyrA gene of quinolone-resistant Salmonella serotypesisolated from humans and animalsAntimicrob. Agents Chemother. 40 (4), 1009-1013 (1996)PubMed: 8849216","","Thu Jan 16 10:26:00 2003","1","","","" "AA02521","1752743","1753090","348","ATGGGTATTTATCTGGTTTATTTGCACATTGTTTGTGCTTTTCTAAGTTTAGGGTTGTTAATTGTGCGTGGGGCAATGCAGTTAACACAGAAAAACTGGCGCGCGGTAAAACTCTTGAAAATCCTACCGCACTTAACGGACACCCTGCTTATTTTGAGCGGTGTCGCCATGTTATTTGTGTTCAACTACGGCTTACCAATTTGGATCATAGTGAAAATTTTACTGCTTGCAGGCTACATTGTCTTCTCGGCAAAATTCTTCAGTAAAAAACAATCTCAAATTCGACCGCACTTTTTCTTCTTCGCCCTTGCGGCACTGACTGCCACGATGTTATTAGGCTACTTTCAC","","","13190","MGIYLVYLHIVCAFLSLGLLIVRGAMQLTQKNWRAVKLLKILPHLTDTLLILSGVAMLFVFNYGLPIWIIVKILLLAGYIVFSAKFFSKKQSQIRPHFFFFALAALTATMLLGYFH","1753088","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR007360
Family
Invasion gene expression up-regulator, SirB
PF04247\"[1-115]TSirB
noIPR
unintegrated
unintegrated
signalp\"[1-24]?signal-peptide
tmhmm\"[4-24]?\"[39-61]?\"[67-87]?\"[97-115]?transmembrane_regions


","BeTs to 4 clades of COG3094COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3094 is --------------e-gh-n------Number of proteins in this genome belonging to this COG is","","Residues 5 to 93 match (8e-19) PD:PD079611 which is described as COMPLETE PROTEOME REGULATOR TRANSMEMBRANE PM0842 YCHQ HI1253 REGULATION MEMBRANE INVASION ","","","","","","","","","","","","Thu Jan 16 16:19:37 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02521 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 115 (E-value = 1.2e-34) place AA02521 in the SirB family which is described as Invasion gene expression up-regulator, SirB (PF04247)","","","","","","","","1","","","" "AA02523","1753444","1753130","315","ATGACAAGTCATTTAGTGTATTCCACCGACGTCGGACGTATTCAAGCCGACAAACCGCAGGAACCAATTCCGCAGGGCGACGGTATTGTGCGTATTCAGCTGCAAAAAACTGGACGGAAAGGAAGTGGTGTAAGTATTATTAACGGGCTTGGACTGGCTGAGCCTGAGTTGAAAGCCTTGGCGGCGGAATTAAAAAAACGCTGTGGCTGCGGTGGTGCGGTGAAAAATCACACCATTGAAATTCAAGGCGAAAAGCGTGATTTGCTGAAACAACTACTGGAGCAAAAAGGCTTTAAAGTAAAGTTGGCGGGAGGT","","","11581","MTSHLVYSTDVGRIQADKPQEPIPQGDGIVRIQLQKTGRKGSGVSIINGLGLAEPELKALAAELKKRCGCGGAVKNHTIEIQGEKRDLLKQLLEQKGFKVKLAGG","1753128","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR001950
Domain
Translation initiation factor SUI1
PF01253\"[24-102]TSUI1
PS50296\"[39-97]TSUI1
InterPro
IPR005872
Family
Archaeal/bacterial translation initiation factor SUI1
TIGR01158\"[5-105]TSUI1_rel: translation initation factor SUI1
noIPR
unintegrated
unintegrated
G3DSA:3.30.780.10\"[25-105]Tno description


","BeTs to 12 clades of COG0023COG name: Translation initiation factor (SUI1)Functional Class: JThe phylogenetic pattern of COG0023 is aompkzy------cefgh--------Number of proteins in this genome belonging to this COG is","Significant hit ( 1.6e-18) to 2/2 blocks of the IPB001950 family, which is described as \"Translation initiation factor SUI1\". Interpro entry for IP:IPR001950. IPB001950A 31-50 0.028 IPB001950B 60-97 1.2e-14","Residues 67 to 98 match (5e-08) PD:PD501550 which is described as PROTEOME COMPLETE TRANSLATION BIOSYNTHESIS REGULATION FACTOR SUI1 HOMOLOG YCIH INITIATION ","","","","","","","","","","","","Thu Jan 16 16:21:37 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02523 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 24 to 102 (E-value = 5.6e-29) place AA02523 in the SUI1 family which is described as Translation initiation factor SUI1 (PF01253)","","","","","","","","1","","","" "AA02524","1754142","1753453","690","ATGACGAATAAAGTCATTATTGCATTGGATTATGAAAGGGAAGCTGAAGCCTTGGCTTTGGTTGACCAACTGGATCCGAATTCATGCCGTTTAAAAGTCGGAAAGGAAATGTTTACGACGCTTGGTACGAATTTTGTAAAGCAGTTACATAAGCGTCATTTTGATGTTTTCCTTGATTTAAAATTCCATGATATTCCGAACACGGTAGCAAGAGCGGTGCGTTCTGCGGCCGATTTAGGCGTTTGGATGGTGGATTTACATGCCAGCGGCGGTTTGCGTATGATGGAAGAAGCCAAGAAAATCCTCGAGCCTTATGGCAAAGATGCTCCGTTGCTAATTGGCGTTACCGTGCTGACCAGCATGGAAGATTTGGATTTATTGCAAATCGGCATTAACGCCTCACCCATGGAACAAGTTATTCGTTTGGCGCATTTGACCCAACGAGCCGGTCTGGACGGCGTGGTTTGTTCACCGCAAGAAGTGGAAATTTTGCGTCGTAATTGCGGTGAGAACTTCCTGCTGGTGACACCGGGAATTCGTCCGATTGGTACCGATTTGGGTGATCAACGCCGCGTGATGACACCGGCGGCAGCAATTCGTTCCGGTTCCGATTATTTAGTGATTGGTCGTCCAATTACCCAGGCGGAAAACCCGGCAGAAGTGTTAAACGCCATTAATGCGTCTATTGCG","","","26297","MTNKVIIALDYEREAEALALVDQLDPNSCRLKVGKEMFTTLGTNFVKQLHKRHFDVFLDLKFHDIPNTVARAVRSAADLGVWMVDLHASGGLRMMEEAKKILEPYGKDAPLLIGVTVLTSMEDLDLLQIGINASPMEQVIRLAHLTQRAGLDGVVCSPQEVEILRRNCGENFLLVTPGIRPIGTDLGDQRRVMTPAAAIRSGSDYLVIGRPITQAENPAEVLNAINASIA","1753451","From PF00215This enzyme catalyzes the last step in the de novo biosynthesis of pyrimidines, the decarboxylation of OMP into UMP.","orotidine 5'-phosphate decarboxylase","Cytoplasm","","
InterPro
IPR001754
Domain
Orotidine 5'-phosphate decarboxylase, core
PF00215\"[3-225]TOMPdecase
PS00156\"[56-69]TOMPDECASE
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[3-229]Tno description
InterPro
IPR014732
Domain
Orotidine 5'-phosphate decarboxylase, subfamily 1, core
TIGR01740\"[5-226]TpyrF: orotidine 5'-phosphate decarboxylase


","BeTs to 19 clades of COG0284COG name: Orotidine-5'-phosphate decarboxylaseFunctional Class: FThe phylogenetic pattern of COG0284 is aompkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 7.6e-07) to 4/6 blocks of the IPB001754 family, which is described as \"Orotidine 5'-phosphate decarboxylase\". Interpro entry for IP:IPR001754. IPB001754A 1-41 1.5 IPB001754B 51-66 0.2 IPB001754C 137-176 1.1e+02 IPB001754E 202-212 6.2","","","","","","","","","","","","Thu Jan 16 17:08:27 2003","Thu Jan 16 17:12:13 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02524 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 225 (E-value = 9.6e-89) place AA02524 in the OMPdecase family which is described as Orotidine 5'-phosphate decarboxylase / HUMPS family (PF00215)","","","","","Strych,U., Wohlfarth,S. and Winkler,U.K. Orotidine-5\"-monophosphate decarboxylase from Pseudomonas aeruginosa PAO1: cloning, overexpression, and enzyme characterization Curr. Microbiol. 29 (6), 353-359 (1994) PubMed: 7765522 Yaoi T, Laksanalamai P, Jiemjit A, Kagawa HK, Alton T, Trent JD. Cloning and characterization of ftsZ and pyrF from the archaeon Thermoplasma acidophilum. Biochem Biophys Res Commun. 2000 Sep 7;275(3):936-45. PMID: 10973825 Arraiano CM, Cruz AA, Kushner SR. Analysis of the in vivo decay of the Escherichia coli dicistronic pyrF-orfF transcript: evidence for multiple degradation pathways. J Mol Biol. 1997 May 2;268(2):261-72. PMID: 9159469 ","","Thu Jan 16 17:12:13 2003","1","","","" "AA02525","1755362","1754175","1188","ATGCTTGAACTCCTCTTCCTTCTTTTGCCGATAGCCACCGCGTACGGTTGGTATATGGGGCACCGTAGTGCTAAAAAAGATCAGGATGATGTCAGCAACAAGCTTTCTCGGGATTATGTCACCGGGGTGAATTTTTTACTTGCCAATCAAACGGAAAAAGCTGTTGATTTATTTTTGGATATGCTGCAAAAGCAGGAAACTGAGAATGAAATCGATAGCACCTCACAATTTGAAGCGGAATTAACTTTAGGGAATTTATTTCGCTCCCGTGGCGAAGTGGATCGTGCGTTGCGTATCCATCAAGCCCTCGATAACAGCCCTCATTATTCTTTTGAACAAAAACTGTTAGCCAAACAACAATTAGCCAAAGATTTTATGACCGTCGGTTTTTTTGATCGGGCGGAAAATCTGTATATTTTAATGGTAGATGAGCCGGAGTTTGCCGAAGGCGCGTTACAACAACTGACGGTGATCTACCAGAAAACCAAAGAGTGGAAAAAAGCCATTAATGTGGCGGAGAAACTGGCAAAAATAGCACCGAAAGCCAATAATGTGGAACTGGCGCAGTATTATTGTGAATATGTGCAACATTTGCCGGCAGACAGTAAAGAAAATCGGCAGCAAATCTTATTGCAAGCGCTTAAAGTCTCTCCGAATTGCGTTCGTGCTTCAATGATGTTGGCGGACTTGGCAATTCAACAAGAAAACTATAAAAGTGCGGTCGGTTTTTTAGAAGAAATTTTAAATCAGAGCCCGGCGTATATTAGTGAAGCCTTGCCGGCGTTGAAACATTGTTATCAAAAATTAAATCTGTTAGATAATTTTGAGCTATTCTTAATCAAAGCCAGCCGCCAAAATAACAACAGCGCAGTGGTGTTAATGCTTGCAGAACTGATTGAAGAAAAAGACGGTTATTCTGCCGCCCAATTGAAGTTATACCAACAATTGCAACAAAATCCGAGCACGCCGATTTTTCATCGGTTTATCCAATATCAAATTGATGATGCAGAGCAGGGCAGAGGCAAAGACAGCTTGATTTTATTGCATAAAATGGTAGGTGAGCGGATTAAACAGACTTTTGATTACCGCTGTAGCAATTGCGGCTTTCAAACCCATAAATTAATGTGGTGCTGTCCTTCCTGTCGTCAATGGGAAACCATTAAACCGGTTAATGCGATTGAACATAAT","","","45551","MLELLFLLLPIATAYGWYMGHRSAKKDQDDVSNKLSRDYVTGVNFLLANQTEKAVDLFLDMLQKQETENEIDSTSQFEAELTLGNLFRSRGEVDRALRIHQALDNSPHYSFEQKLLAKQQLAKDFMTVGFFDRAENLYILMVDEPEFAEGALQQLTVIYQKTKEWKKAINVAEKLAKIAPKANNVELAQYYCEYVQHLPADSKENRQQILLQALKVSPNCVRASMMLADLAIQQENYKSAVGFLEEILNQSPAYISEALPALKHCYQKLNLLDNFELFLIKASRQNNNSAVVLMLAELIEEKDGYSAAQLKLYQQLQQNPSTPIFHRFIQYQIDDAEQGRGKDSLILLHKMVGERIKQTFDYRCSNCGFQTHKLMWCCPSCRQWETIKPVNAIEHN","1754173","","conserved hypothetical protein","Cytoplasm, Periplasm","","
InterPro
IPR011990
Domain
Tetratricopeptide-like helical
G3DSA:1.25.40.10\"[120-326]Tno description
InterPro
IPR013026
Domain
Tetratricopeptide region
SM00028\"[149-182]T\"[221-254]TTPR
PS50293\"[149-254]TTPR_REGION
InterPro
IPR013253
Family
Kinetochore Spc7
SM00787\"[26-303]Tno description
noIPR
unintegrated
unintegrated
PTHR23083\"[212-340]TTETRATRICOPEPTIDE REPEAT PROTEIN, TPR
PTHR23083:SF18\"[212-340]TTETRATRICOPEPTIDE REPEAT PROTEIN, TPR
signalp\"[1-16]?signal-peptide


","No hits to the COGs database.","","Residues 1 to 87 match (3e-37) PD:PD468362 which is described as PROTEOME COMPLETE SIGNAL PRECURSOR TRANSFERASE ZINC-FINGER VC1912 N-ACETYLGLUCOSAMINYL TRANSMEMBRANE YPO2225 ","","","","","","","","","","","","Thu Jan 16 17:13:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02525 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02526","1755658","1755365","294","ATGATTAAATATATTTTGGGGTTGATCATTACCTTAGCCATTGTGCTGGTTGCCGTTACCATTGGTGCCAACAATGATCAAATCATTACCTTTAATTATATTGTGGCGCAAAGCCAATTCCAGCTTTCTACCTTAGTTGCTATTTTATTCGGCCTGGGATTAATTCTAGGGTGGTTTATCACCGGATTCTTCTATCTCAAATTAAAGTTAAAAAATATTGCGCTGAATCGCCAAATCAAACGCCAAACGCAACAAATCAACGAATTAACGACCAGCAGAGATAAGGTTTCTCAA","","","11041","MIKYILGLIITLAIVLVAVTIGANNDQIITFNYIVAQSQFQLSTLVAILFGLGLILGWFITGFFYLKLKLKNIALNRQIKRQTQQINELTTSRDKVSQ","1755363","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR010445
Family
Protein of unknown function DUF1049
PF06305\"[2-90]TDUF1049
noIPR
unintegrated
unintegrated
PD029620\"[5-88]TYCIS_HAEIN_P44129;
signalp\"[1-22]?signal-peptide
tmhmm\"[5-25]?\"[44-66]?transmembrane_regions


","No hits to the COGs database.","","Residues 5 to 80 match (4e-13) PD:PD029620 which is described as PROTEOME COMPLETE MEMBRANE TRANSMEMBRANE INNER YCIS HI1222 VC1913 STY1342 ORF ","","","","","","","","","","","","Thu Jan 16 17:15:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02526 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 90 (E-value = 1.8e-50) place AA02526 in the DUF1049 family which is described as Protein of unknown function (DUF1049) (PF06305)","","","","","","","","1","","","" "AA02527","1756044","1755760","285","ATGACAAAGTCAGAACTTATTGAACTTCTGGTGCAAAAAAACAGCAACATTCCTGTTAAGCATGTTGAAGAAGCGGTAAAAGCAATTTTAGAGCAAATGTCATATGTGTTAGAACATGGCGAACGTATAGAAGTGCGTGGTTTCGGTAGTTTTTCTTTGCATTGTCGCCAACCGCGCATCGGACGTAATCCTAAAACCGGCGAACAAGTAAAATTGGATGCCAAATGTGTGCCATATTTTAAGGCAGGCAAAGAATTAAGAGAACGTGTCGACGTTTATGCAGCA","","","10822","MTKSELIELLVQKNSNIPVKHVEEAVKAILEQMSYVLEHGERIEVRGFGSFSLHCRQPRIGRNPKTGEQVKLDAKCVPYFKAGKELRERVDVYAA","1755758","From Genbank:This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and transcriptional control. ","integration host factor,beta-subunit","Cytoplasm","","
InterPro
IPR000119
Family
Histone-like bacterial DNA-binding protein
PD000945\"[8-93]TIHFB_PASMU_Q9CML8;
PR01727\"[41-56]T\"[59-72]T\"[75-89]TDNABINDINGHU
G3DSA:4.10.520.10\"[1-94]Tno description
PF00216\"[1-91]TBac_DNA_binding
SM00411\"[1-91]TBHL
PS00045\"[47-66]THISTONE_LIKE
InterPro
IPR005685
Family
Integration host factor, beta subunit
TIGR00988\"[1-94]Thip: integration host factor, beta subunit


","BeTs to 19 clades of COG0776COG name: Bacterial nucleoid DNA-binding proteinFunctional Class: LThe phylogenetic pattern of COG0776 is ---p---qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-16) to 1/1 blocks of the IPB000119 family, which is described as \"Bacterial histone-like DNA-binding protein\". Interpro entry for IP:IPR000119. IPB000119 37-67 1.1e-16","Residues 43 to 92 match (6e-19) PD:PD404788 which is described as DNA-BINDING DNA PROTEOME COMPLETE REGULATION INTEGRATION HOST FACTOR CONDENSATION HU ","","","","","","","","","","","Thu Jan 16 17:55:20 2003","Thu Jan 16 17:56:47 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02527 is paralogously related to AA02163 (9e-15) and AA00972 (7e-14).","","","","","","Residues 1 to 91 (E-value = 9.7e-44) place AA02527 in the Bac_DNA_binding family which is described as Bacterial DNA-binding protein (PF00216)","","","","","Highlander,S.K., Garza,O., Brown,B.J., Koby,S. and Oppenheim,A.B. Isolation and characterization of the integration host factor genes of Pasteurella haemolytica FEMS Microbiol. Lett. 146 (2), 181-188 (1997) PubMed: 9011038 Haluzi,H., Goitein,D., Koby,S., Mendelson,I., Teff,D., Mengeritsky,G., Giladi,H. and Oppenheim,A.B. Genes coding for integration host factor are conserved in gram-negative bacteria J. Bacteriol. 173 (19), 6297-6299 (1991) PubMed: 1917861","","Thu Jan 16 17:57:12 2003","1","","","" "AA02528","1757752","1756109","1644","ATGACAGAATCTTTTGCTCAACTCTTTGAAGAATCATTGAAAGACCTTGAAACCCGTCAAGGTGCGGTCGTTAAAGGTACCATCGTTGCTATCCAAAAAGGCTTCGTACTTGTAGATACTGGATCTAAATCCGAATCAGCTATTCCTGCCGAAGAATTTTTTAATGCACAAGGTGAATTGGAAGTTCAAGTGGGTGATGTTGTTGATGTCGTGCTTAAAGTGGTGGATGACGGTTTCGGTGAAACTGTAGCTTCCCGTGCTGATGCAAAACGCAACGAAGCTTGGATTGTATTGGAAAAAGCATACGACGAACAAGCGACTGTTCTTGGTTTGGTTAACGGTAAAGTTAAAGGTGGCTTCACAGTTGAGTTAAACGGTGTTCGCGCATTCTTACCGGGTTCATTGGTTGATACCCGTCCTGTTCGTGATGCAGATCACTTACTTGGCAAAGAATTAGAATTCAAAGTAATCAAACTTGATCAAAAACGTAACAACGTTGTTGTTTCCCGCCGTGCCGTTATCGAATCCGAAAGCAGCCAAGATCGCGAAGAAGTATTGGCGAACTTGTCTGAAGGTGCAGAAGTTAAAGGTACCGTTAAAAACTTAACCGACTACGGTGCGTTCGTTGATTTAGGCGGTGTTGACGGTTTATTACACATTACCGACATGGCTTGGAAACGTGTTAAACACCCAAGTGAAATCGTTAATGTTGGTGATGAAATCACTGTTAAGGTATTGAAATTCGACAAAGATCGTACCCGTGTATCTTTAGGCTTAAAACAATTAGGTCAAGATCCTTGGGCGGCAATCGCTGAAAATCACCCGGTAAACAGCAAATTAACCGGTAAAGTGACTAACTTAACCGACTACGGCTGTTTCGTTGAAATTTTAGACGGTGTTGAAGGTTTGGTTCACGTTTCCGAAATGGATTGGACTAACAAAAACATTCACCCATCTAAAGTGGTTAGCTTAGGTGATGTTGTTGAAGTGATGGTACTGGAAATCGATGAAGAACGTCGTCGTATTTCTTTAGGTTTAAAACAATGCAAACCTAACCCATGGACACAATTCGCCGAAACCCACAACAAAGGTGACAAAGTTGTCGGTAAAATCAAATCCATCACCGACTTCGGTATCTTCATCGGCTTAGAAGGCGGTATCGACGGTTTGGTTCACTTGTCCGATATTTCTTGGAATGTTCAAGGCGAAGAAGCCGTACGCAACTACAAGAAAGGTGACGAAGTCGCTGCCGTTGTATTGCAAGTGGACGCAGTGAAAGAACGTATTTCTTTAGGTATCAAACAACTTGAAGAAGATCCGTTCAATAACTTCGTTGCAATCAACAAAAAAGGCGCAGTATTAAACGCTAAAGTTGTTGAAGCAGACGCTAAAGGCGCTAAAGTTGAATTAGACGGCGGTGTTGAAGGTTATATCCGCGCGGCTGATTTAACTAACGAAGTGGTTGCCGGCGATGTTGTTGAAGCGAAATACACAGGCGTAGATCGTAAAGCCCGTATCGTTCATTTATCTGTTCGTGCGAAAGATCAAGCTGAAGAAGCCGCGGCAGTTGCAAGCGTGAATAAGCAAGAAGATGTTGCTATTCCAAATGCAATGGCAGAAGCTTTCAAAGCCGCTAAAGGTGAA","","","59489","MTESFAQLFEESLKDLETRQGAVVKGTIVAIQKGFVLVDTGSKSESAIPAEEFFNAQGELEVQVGDVVDVVLKVVDDGFGETVASRADAKRNEAWIVLEKAYDEQATVLGLVNGKVKGGFTVELNGVRAFLPGSLVDTRPVRDADHLLGKELEFKVIKLDQKRNNVVVSRRAVIESESSQDREEVLANLSEGAEVKGTVKNLTDYGAFVDLGGVDGLLHITDMAWKRVKHPSEIVNVGDEITVKVLKFDKDRTRVSLGLKQLGQDPWAAIAENHPVNSKLTGKVTNLTDYGCFVEILDGVEGLVHVSEMDWTNKNIHPSKVVSLGDVVEVMVLEIDEERRRISLGLKQCKPNPWTQFAETHNKGDKVVGKIKSITDFGIFIGLEGGIDGLVHLSDISWNVQGEEAVRNYKKGDEVAAVVLQVDAVKERISLGIKQLEEDPFNNFVAINKKGAVLNAKVVEADAKGAKVELDGGVEGYIRAADLTNEVVAGDVVEAKYTGVDRKARIVHLSVRAKDQAEEAAAVASVNKQEDVAIPNAMAEAFKAAKGE","1756107","From Genbank:[gi:2500383] This protein binds mRNA thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence.","30S ribosomal protein S1","Cytoplasm","","
InterPro
IPR000110
Family
Ribosomal protein S1
PR00681\"[21-39]T\"[39-53]T\"[84-103]T\"[108-124]T\"[126-143]T\"[155-175]T\"[212-233]T\"[290-309]T\"[330-348]TRIBOSOMALS1
TIGR00717\"[3-512]TrpsA: ribosomal protein S1
InterPro
IPR003029
Domain
RNA binding S1
PF00575\"[17-87]T\"[101-171]T\"[188-260]T\"[273-347]T\"[360-434]T\"[447-512]TS1
SM00316\"[19-87]T\"[103-171]T\"[190-260]T\"[275-347]T\"[362-434]T\"[449-512]TS1
PS50126\"[21-87]T\"[105-171]T\"[192-260]T\"[277-347]T\"[364-434]T\"[451-512]TS1
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[90-173]T\"[187-262]T\"[272-349]T\"[364-442]T\"[448-514]Tno description
noIPR
unintegrated
unintegrated
PTHR10724\"[186-312]TTEX PROTEIN-RELATEDTRANSCRIPTION ACCESSORY PROTEIN (S1 RNA BINDING DOMAIN)


","BeTs to 18 clades of COG0539COG name: Ribosomal protein S1Functional Class: JThe phylogenetic pattern of COG0539 is ------yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit (1.1e-124) to 9/9 blocks of the PR00681 family, which is described as \"Ribosomal protein S1 signature\". Prints database entry for PR:PR00681. PR00681A 21-39 1.1e-10 PR00681B 39-53 1.5e-05 PR00681C 84-103 0.00057 PR00681D 108-124 5.8e-09 PR00681E 126-143 1.7e-13 PR00681F 155-175 4.1e-17 PR00681G 212-233 1.6e-21 PR00681H 290-309 2.3e-16 PR00681I 330-348 1e-15 PR00681G 385-406 0.0038 PR00681G 298-319 0.025 PR00681H 464-483 0.86Significant hit ( 5.4e-07) to 2/2 blocks of the IPB003029 family, which is described as \"S1 RNA binding domain\". Interpro entry for IP:IPR003029. IPB003029A 282-293 0.0052 IPB003029B 325-336 0.047 IPB003029A 369-380 0.047 IPB003029B 412-423 0.068 IPB003029B 238-249 0.11 IPB003029B 65-76 0.55","Residues 20 to 85 match (2e-08) PD:PD012792 which is described as RIBOSOMAL S1 COMPLETE PROTEOME 30S REPEAT RNA-BINDING CHLOROPLAST RPSA DNA-BINDING ","","","","","","","","","","","Thu Jan 16 18:02:20 2003","Thu Jan 16 18:02:20 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02528 is paralogously related to AA00939 (8e-13), AA00151 (1e-10) and AA01372 (0.001).","","","","","","Residues 447 to 512 (E-value = 7.8e-05) place AA02528 in the S1 family which is described as S1 RNA binding domain (PF00575)","","","","","","","","1","","","" "AA02529","1758527","1757853","675","ATGAATAAAATTATTACGGTGGACGGCCCGAGCGGCGCCGGTAAAGGCACATTATGTTATGCGTTGGCGGAAAAACTGGGCTTTGCCTTGTTGGATTCCGGTGCGATTTATCGTGTGACGGCGTTAGCGGCGCTAAAAAGTGCGGTGGATTTGGCGGATGAATCTGCGCTTGCCGAGTTGGCACAACATTTACACATTGAATTTGTGGCGCAAGACGGTGAAATACAAATTTTACTCAATGGTGAAAATGTCAGCGGCCAGATTCGTACGCAGGAGGTTGCCGATGCCGCCTCAAAAGTCGCGGTGTTCCCGCAGGTACGGGCGGCGTTACTGCAACGTCAGCGCGATTTTGCAACGGAAAAAGGCTTGATCGCGGACGGTCGGGATATGGGCACGGTGGTGTTCCCCGAAGCGCAAGTCAAATTATTTTTAGACGCCAGCGCGGAGGAACGTGCAAAAAGACGTTATAACCAGTTGCAAAATAAAGGGATTAGTGGTAACTTTGCACAGATTTTAGCCGAGATAAAAGCGCGTGATTTGCGCGATAGAAATCGTGCCGTCGCTCCTTTAAAACCTGCTGGTGATGCGTTTTTACTTGATAGCACCGCATTGAGTATTGATGAAGTGATTCGTCAGGCGCTCGATTATATTCAGCAACGTATTGATATTAAAGCT","","","24329","MNKIITVDGPSGAGKGTLCYALAEKLGFALLDSGAIYRVTALAALKSAVDLADESALAELAQHLHIEFVAQDGEIQILLNGENVSGQIRTQEVADAASKVAVFPQVRAALLQRQRDFATEKGLIADGRDMGTVVFPEAQVKLFLDASAEERAKRRYNQLQNKGISGNFAQILAEIKARDLRDRNRAVAPLKPAGDAFLLDSTALSIDEVIRQALDYIQQRIDIKA","1757851","","cytidylate kinase 1","Cytoplasm","","
InterPro
IPR003136
Family
Cytidylate kinase
PTHR21299:SF2\"[15-221]TCYTIDYLATE KINASE (CK) (CYTIDINE MONOPHOSPHATE KINASE) (CMP KINASE)
TIGR00017\"[1-217]Tcmk: cytidylate kinase
InterPro
IPR011769
Domain
Adenylate/cytidine kinase, N-terminal
PD000657\"[4-46]TKCY2_HAEIN_P43893;
InterPro
IPR011994
Domain
Cytidylate kinase region
PF02224\"[58-215]TCytidylate_kin
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[4-224]Tno description
PTHR21299\"[15-221]TCYTIDYLATE KINASE/PANTOATE-BETA-ALANINE LIGASE


","BeTs to 16 clades of COG0283COG name: Cytidylate kinaseFunctional Class: FThe phylogenetic pattern of COG0283 is -------qvdrlbcefghsn-jxitwNumber of proteins in this genome belonging to this COG is","Significant hit (4.5e-100) to 4/4 blocks of the IPB003136 family, which is described as \"Cytidylate kinase\". Interpro entry for IP:IPR003136. IPB003136A 5-38 2.2e-23 IPB003136B 83-117 1.3e-21 IPB003136C 126-163 1e-30 IPB003136D 171-202 8e-21","Residues 4 to 38 match (2e-12) PD:PD034497 which is described as KINASE COMPLETE PROTEOME CYTIDYLATE TRANSFERASE CMP MONOPHOSPHATE CYTIDINE CK ATP-BINDING ","","","","","","","","","","","","Tue Jan 21 08:20:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02529 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 58 to 215 (E-value = 5.7e-85) place AA02529 in the Cytidylate_kin family which is described as Cytidylate kinase (PF02224)","","","","","Fricke,J., Neuhard,J., Kelln,R.A. and Pedersen,S. The cmk gene encoding cytidine monophosphate kinase is located in the rpsA operon and is required for normal replication rate in Escherichia coli J. Bacteriol. 177 (3), 517-523 (1995) PubMed: 7836281 Schultz,C.P., Ylisastigui-Pons,L., Serina,L., Sakamoto,H., Mantsch,H.H., Neuhard,J., Barzu,O. and Gilles,A.M. Structural and catalytic properties of CMP kinase from Bacillus subtilis: a comparative analysis with the homologous enzyme from Escherichia coli Arch. Biochem. Biophys. 340 (1), 144-153 (1997) PubMed: 9126287 ","","Tue Jan 21 08:12:58 2003","1","","","" "AA02531","1759401","1758523","879","GTGGCAACGTTCCATTTTCCGACATTTCATGAAATGTTTCCCGTTGAAAAACGTAAATTAAAATTATTGCGGGAAGGGTTGCGCTATGGGGCGCGTCGTTTGTTTTTTGTCGGGCAATGTTCGGCGTTGGTCAAGTTTATTCACGACAATCCCTTGTGGCAGCCGATTTTTACGCAGCATCCTTATCGGGTGAATACGTTATTGAGCCAATATTGCGATAAAGGTTTTAACGTAACTCAGCGCTTACAGGCGATTGAAACCAATTTTGCCGTGGCGGAAAAACAATTCGGTAAGGCGTTATGCGAAACGTTAATCGCGCAACAGCCGGTATTGCTATCACAGTTAACCGATGAGTTAGCGTTAAATTTAACGCTGAATCATATCGACCCTTACGAAGGTTTTTTTGCCATGGGTTTAACAGATGCAAATCAACGCAGCATTTATTCTGCCGGTTTTACCTTTTTAGCGAATAATCGCGTATTGATCGCTTCCATTCAGGGACCAAAAGGCGATGAAGCGCAGGATTTGGTGCGTCAGGCAACAAAAGCATTGCATGGCGTGCGCCCGATGTTTATGTTGGTGAATGCGTTTAAGGTATTGGCGGAAGTATTACATTGTCGCTTGCAAGGCATTCCGCATAAGCGTCAGGCGAAATACCGTTGGAACGATTCGGCGAAATTGTTGTTTAACTATGATGAATTTTGGCAGGAAAACGAGGGCAAATTAGAGGAAAATTATTGGCAAATTCCGACCGCACTTGAACGTCGTCCGTTAGAAGAAATCCAGAGTAAAAAACGTTCTATGTATCGCAAACGTTACGATATGTTCGACAAAATGACGACAGAAATTCAATCCCTTTTTAATAGAGAAAATCATGAA","","","34752","VATFHFPTFHEMFPVEKRKLKLLREGLRYGARRLFFVGQCSALVKFIHDNPLWQPIFTQHPYRVNTLLSQYCDKGFNVTQRLQAIETNFAVAEKQFGKALCETLIAQQPVLLSQLTDELALNLTLNHIDPYEGFFAMGLTDANQRSIYSAGFTFLANNRVLIASIQGPKGDEAQDLVRQATKALHGVRPMFMLVNAFKVLAEVLHCRLQGIPHKRQAKYRWNDSAKLLFNYDEFWQENEGKLEENYWQIPTALERRPLEEIQSKKRSMYRKRYDMFDKMTTEIQSLFNRENHE","1758521","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR007488
Family
Protein of unknown function DUF535
PF04393\"[12-286]TDUF535


","No hits to the COGs database.","","Residues 42 to 285 match (2e-12) PD:PD017199 which is described as PROTEOME COMPLETE VIRULENCE VIRK PLASMID LOCALIZATION PROPER SURFACE AT REQUIRED ","","","","","","","","","","","","Tue Jan 21 09:03:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02531 is paralogously related to AA00422 (3e-33).","","","","","","Residues 12 to 286 (E-value = 3.2e-112) place AA02531 in the DUF535 family which is described as Protein of unknown function (DUF535) (PF04393)","","","","","","","","1","","","" "AA02532","1759706","1762069","2364","ATGTATAAAAAAACCAAGATCGCATTTTTCATTTGTACGGCGCTGTATGCACAGCATGTTCTTTCGGAAGAAAAATCAACAAATAAATCCAATATGTTACCGGAAATTATAGTATACGGAGATAGTAATAAATCCCTTTCCTCCACCCAGGCTGTTACTTCCAATGAAATGGAAAAAATACCGACAACCAATAATAACATCACCGATTATCTACGTTCCAACCCGCACATTCGTTATGAAGACAGCGACCAAGATGGTTTTCAACGTGGCGAAATTAAGCCGCAAAATATCTCAATTAATGGAGCCGATGCAAACCAAACTGCTTACTTTGTCGATAACGTAAACGTAAATAATGATTTAACCGTCGATAACGAAATCTTTGATGGAGCCATGCAGGTTGTTCCGGGTATTAGTAATACGCAAGCTTATTTTTTTGATGCATCTATGCTATCAAAAGTCGAAGTTCACGATAGCAACATTTCCGCAAGTTTAGGTGGTTTCATGGGAGGTGCAGTCGTAGCTAAAACCAAACAATATAATGGTAAAGACGGTGTTTCACTAAAATATCGCACCACCAACTCCGGTTGGGCAAAAATTAATGCAGATAGCTCAGCAAAAACTCTTTTAGATAAAATTAGGCCTGATGCAGGCGGTGTTGCCGAATTTCAACCTAAATACCATAAACAGACGTTCAGCATCATGGCAGAAAAAGGCTTAACGGAAAATTTGGGCATGGTGATCGGTTACAGTAAACGCCACGCCCGCATTCAACAGAATAGATTAATTGGTTATGCTCCCGACGCTAAATTAGACAAACAAAATCATAAACGCGATTCAGATAATTTATTGTTGAACTTCAATTTGGCGGCAAGTGAAAAAGATCGTTTTGAACTGGGCTTCCGTTATTCTAATTATAAAGAACAAAAATATTATGCTACTAATATTGATAGTAACGTCAGTGATTATCATCAAGCCCTCGGTTCAACATTAGCTTGGGTACATTCTTTTAATTCAGGCATTTTGACAAATACACTTGCTTACGATCACTTTAAAGACAAGCGGAAATCCTCCTCTGCCAATGTTGAAATCGTTTCTGTTTTCGATGAAAACTTTGATCCGCTTTATGATTATGAAAAAGGTGGTTATGGTAATAGTTCTCTTACGCAAGACAACATTCATTTCTCCACAGAATTTGCCGTAGATCCCTTTAATTTAGGTTTTGCCAACCATTCTATTTCTATAGGTGGAATTTATCAGGCAACCCATTATAAATTTAACCGCCCGCAGGATGTACATTCCAAAATTATTCAAAAATATCCTAACCTTAGCCCAATTGAGACAACAAATATTACCCACCAAGGTAATGCCCAAACCCGTTATCAAAACTTTGTTTTTTATACCGAAGATTTAATTAAGTGGAAAAAATTGGAGCTACGCCCGGGTGTACGTATTGAACGTGATGACTATCTACAAAACAATAATATCGCCCCGCGTTTTGTTGCACGCTATAAGCCGTGGGAGGAAACCGGGTTCACATTAGGTTTAAATCGCTATTATGGACGCTCTTTCGCTTCATTAAAACTAACGAATGAGATTTTAAAAATAAACCGTGATACCAGTCGTAAATACCAAGAATTTCATTCCTTAAAAACCCCTTACGCTGATGAACTTAGTATCGGTTTTGATCAAGAATTCAATAATCTGGCATTTAAACTTAATTATATTCATCGCAAAAATAAAAATCGTATTGTGCTAAAACGTGATGCCAATAAAGTTAATTTTTATCATAACGGCAGTGACTTCAGCGTCGACGTTTACACTTTCCAAATGAATAATATTGAACCTTGGCAATTGGGTAAAAGCTACTGGACAAGCTCTCTGGGATTTGATTGGTTAAAAACCAAACGGGCGGATATAGGTCGAGATCTTGATCCCAATGAATTAGTTTATCTCGATGGTAAATTACTTACCCGCAGAGAAATGCTGAACAAAGTCAATAGTTCTACAGAAGACTGGATTGCCCGCTTCGGCTTGGATATGGCAATCCCCGATTACAACATCACTTGGTCAAACAAATTGTATATAAAAGCACCGATTCGCAGTTATGACGTTTTGGAAGGTGATTTTAACGACGGAATTTCCCGTTATCGTTCTTATCACTACGGCCGACACACCCAATGGGACAGTAGTATTCGTTGGCAACCGACCATTACCGGTAATCACAGTATTTATTTGCAAGTTGACATACTAAATGTATTAAATAAAACCCGTAAATCAAAAACCGTAAAACCAATTTCAAGTAACGATGAATACGGTATTTACACGCCCGGCCGCGAGTTTTGGCTGGAAGTCGGCTACAAATTC","","","90559","MYKKTKIAFFICTALYAQHVLSEEKSTNKSNMLPEIIVYGDSNKSLSSTQAVTSNEMEKIPTTNNNITDYLRSNPHIRYEDSDQDGFQRGEIKPQNISINGADANQTAYFVDNVNVNNDLTVDNEIFDGAMQVVPGISNTQAYFFDASMLSKVEVHDSNISASLGGFMGGAVVAKTKQYNGKDGVSLKYRTTNSGWAKINADSSAKTLLDKIRPDAGGVAEFQPKYHKQTFSIMAEKGLTENLGMVIGYSKRHARIQQNRLIGYAPDAKLDKQNHKRDSDNLLLNFNLAASEKDRFELGFRYSNYKEQKYYATNIDSNVSDYHQALGSTLAWVHSFNSGILTNTLAYDHFKDKRKSSSANVEIVSVFDENFDPLYDYEKGGYGNSSLTQDNIHFSTEFAVDPFNLGFANHSISIGGIYQATHYKFNRPQDVHSKIIQKYPNLSPIETTNITHQGNAQTRYQNFVFYTEDLIKWKKLELRPGVRIERDDYLQNNNIAPRFVARYKPWEETGFTLGLNRYYGRSFASLKLTNEILKINRDTSRKYQEFHSLKTPYADELSIGFDQEFNNLAFKLNYIHRKNKNRIVLKRDANKVNFYHNGSDFSVDVYTFQMNNIEPWQLGKSYWTSSLGFDWLKTKRADIGRDLDPNELVYLDGKLLTRREMLNKVNSSTEDWIARFGLDMAIPDYNITWSNKLYIKAPIRSYDVLEGDFNDGISRYRSYHYGRHTQWDSSIRWQPTITGNHSIYLQVDILNVLNKTRKSKTVKPISSNDEYGIYTPGREFWLEVGYKF","1762067","","conserved hypothetical protein","Outer membrane, Extracellular","","
InterPro
IPR000531
Domain
TonB-dependent receptor
PF00593\"[496-788]TTonB_dep_Rec
InterPro
IPR012910
Domain
TonB-dependent receptor, plug
PF07715\"[41-172]TPlug
noIPR
unintegrated
unintegrated
G3DSA:2.40.170.20\"[276-788]Tno description
signalp\"[1-22]?signal-peptide


","No hits to the COGs database.","","Residues 35 to 788 match (1e-308) PD:PD044018 which is described as PROTEOME COMPLETE PM0803 YDDB HI1369 CDS103 ORF ","","","","","","","","","","","","Tue Jan 21 09:06:02 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02532 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 43 to 788 (E-value = 4.1e-05) place AA02532 in the TonB_dep_Rec family which is described as TonB dependent receptor (PF00593)","","","","","","","","1","","","" "AA02533","1762150","1764042","1893","ATGAAAAAACTGACCGCACTTTTCGTACTGCTCTGCTCTTTTCACTTACTCATTGCTTGTCGAACCGGAATAGATCCTGATGCCTTAGCTTTCGATCCCGATATTAAACACGGCAAACTGACAAACGGATTGCAATATTACATCTTGAATAATCGTGATCCCAAAGATCGGGTGTATATTCGTTTAGTGGTAAATGCCGGTTCAATGCACGAAGATGATGATCAAAAAGGCATCGCCCATTTAGTAGAACACATGGCGTTTAACGGTTCGAAAAAATATCCTGAAAATACCATCATTAATGCTCTTGAAAAATTGGGTATGAAATTTGCCCGCGATATTAATGCATTCACTGATTTTGAAAATACCGTTTATACTCTGAATTTAGACGGTAATAGCCCGCAAAAACTATCCCTTGCTTTTGATGTTATCAATGAATGGATGAATCATCTCACAATTTTACCCAAAGACCTTGATGGTGAACGCGGCGTGGTACAAGAAGAATGGCGACGTCGATTAAGCCCAATGTTACGTCTCGGAGATAAAAAAAGTGCAATTGAAATGGCAGGTTCGCGCTATGTGTTACGTGACCCGATTGGCGATATGAATATTATTCGTCACATCTCCCGTGATCGCGTAACCGATTTTTATCATAAATGGTATAGACCGGATAATATGTCCCTTATTGTCGTCGGTGATATCGATGCGCACAAAATTGCACAGTTAATATCACAACAACTAGATAAACCGAGTTCTCGCACACAACGCCCGTTAGATAAAATTGATTTTAGCATTCCGCTGATTCATCATTGGCGGGTAGCAAGTATTGCCGAACAAGGCACCAATATCCCGGCACTGGAGTTGAGCTTTTTTGAAGAAGATAAACAAAAAGAAACGGTCATTGGCTACAAACAAGATCTCATTCAACAAATTGTGACCCGTTTAGTCAATTTACGTCTGCAAAAATGGGAAAAAAGCCAAAACAACTGGTTGGATTCGGCGAATTTCTATCGTTCTCATCTTGGTAAACAAACCCTGCAAAGTGTCTTTTCCTTGCAATTAATCGATACCAATTATTTAAAAAATATCACCGCACTTTTTGCTTTTATCGCCGAAATTAAACAACATGGATTTACCGCCGACGAGCTTAACGGCGAAATTGCACGACTACATAATCTCAATGAAAAACAACAAAATATTCGTCCTGGCAGCTTAAAAATTGCTAATGATTTGATTGCAATCGCGGCAAATCATCAAATCATGTTAAGCGCTAAAGAACGCTATAATCTAAATCGACGTTTTTTGAATGAAATTAAAGTAACTGACTTAAATGCAACATTTAATCAAATGTTAGCGTTAAACGCTAAGCTATTACTGATAACACAACCGCTACCGGAGAAAAAACTTCCTTTTGATGCAGATTATATAGAACAGCGTTGGAACCAAGCAATGCATTCCGGTCAAAATCAATGGGAAAACAAAAAACACATCGTAAAACAACCGCACTTTGAATTCAAAGACGGTTCATTAGTATTAGAAAAACACTGGGATAAAGGCGATATTGATGAATTTCGCCTCAGTAACGGGGCAAAATTAATTTATCACTACAGCAATAAAACACCGAACCAAGTCCATTTTCGAGCAGTAACAAGCGGTGGATTACGATCTGTACCAAACCAAGATTATCATTTATTGCGAACGGCGATTACCTTAGTTGATGATACCGGCACAGGTGAACTAACGCAGGCAGATGTCAACAACCTCTTTGGTCAAAGCCCACTTGTGTTGGCAACGGTTATTGATGACGATAAGCAAGGTTTTACCGGTGTGGCAAAACCGCAAGATCTCAGTAGTTTGCTGACACTTTTCCGTCTGAAACTCCAATCCGCTCCCGTT","","","72250","MKKLTALFVLLCSFHLLIACRTGIDPDALAFDPDIKHGKLTNGLQYYILNNRDPKDRVYIRLVVNAGSMHEDDDQKGIAHLVEHMAFNGSKKYPENTIINALEKLGMKFARDINAFTDFENTVYTLNLDGNSPQKLSLAFDVINEWMNHLTILPKDLDGERGVVQEEWRRRLSPMLRLGDKKSAIEMAGSRYVLRDPIGDMNIIRHISRDRVTDFYHKWYRPDNMSLIVVGDIDAHKIAQLISQQLDKPSSRTQRPLDKIDFSIPLIHHWRVASIAEQGTNIPALELSFFEEDKQKETVIGYKQDLIQQIVTRLVNLRLQKWEKSQNNWLDSANFYRSHLGKQTLQSVFSLQLIDTNYLKNITALFAFIAEIKQHGFTADELNGEIARLHNLNEKQQNIRPGSLKIANDLIAIAANHQIMLSAKERYNLNRRFLNEIKVTDLNATFNQMLALNAKLLLITQPLPEKKLPFDADYIEQRWNQAMHSGQNQWENKKHIVKQPHFEFKDGSLVLEKHWDKGDIDEFRLSNGAKLIYHYSNKTPNQVHFRAVTSGGLRSVPNQDYHLLRTAITLVDDTGTGELTQADVNNLFGQSPLVLATVIDDDKQGFTGVAKPQDLSSLLTLFRLKLQSAPV","1764040","","zinc protease; peptidase","Cytoplasm, Outer membrane, Periplasm","","
InterPro
IPR001431
Binding_site
Peptidase M16, zinc-binding site
PS00143\"[67-90]TINSULINASE
InterPro
IPR007863
Domain
Peptidase M16, C-terminal
PF05193\"[206-389]TPeptidase_M16_C
InterPro
IPR011765
Domain
Peptidase M16, N-terminal
PF00675\"[47-189]TPeptidase_M16
noIPR
unintegrated
unintegrated
G3DSA:3.30.830.10\"[22-257]Tno description
PTHR11851\"[62-400]TMETALLOPROTEASE
PTHR11851:SF63\"[62-400]TZINC PROTEASE-RELATED
PS51257\"[1-20]TPROKAR_LIPOPROTEIN
signalp\"[1-19]?signal-peptide


","No hits to the COGs database.","Significant hit ( 5.3e-06) to 1/1 blocks of the IPB001431 family, which is described as \"Insulinase family (Peptidase family M16)\". Interpro entry for IP:IPR001431. IPB001431 77-90 5.4e-06","Residues 37 to 84 match (9e-07) PD:PD420926 which is described as PROTEASE PQQL-LIKE ZINC ","","","","","","","","","","","","Fri Feb 7 13:11:02 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02533 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 206 to 389 (E-value = 6.6e-21) place AA02533 in the Peptidase_M16_C family which is described as Peptidase M16 inactive domain (PF05193)","","","","","","","","1","","","" "AA02534","1764052","1764921","870","GTGTTACAAAAATATCATCGGGAAACACAGGATTATTTTAAACAAATTGATGCCGAAACAAAGTTTATGCAATCTATTTCCTATTTGCGCCGACCTAACACTGCTACAGTTTATACCCAAAATCAAAATGAACAGCTTAGCTTTACAGCTGCACAATTAAGTCAAATTTATCAAGAAAAGATTTTAGGTAAAACGGATTTCACTTATTTCATTATTGGTGATATTTCCCGATCCGAGGTCGAAAAATTGGCAAAGCGATATTTAGCGACAGTGGAAATAAAAACACAGGCCCGTGCTTATCAGCCCGGTTATATTCATACTCCTAAAAAAGCATTCATTATGCGCGGATTAAGTGAACCACGTGCTGATGTGGAAATTTATCTTACCGCTGAAAATCAATGGCATCCGGAACAGAAATATGCCTTAGAAATCCTTGCTGAAATTGTACAAGAAAAACTTCGCCTTGTTTTACGTGAAAAAGTATCGGGCATTTATTCCGTCAATAGTTGGTTCAGCCAAGATCCGCATACGCCGCAAATTGAAGGGAAAATTGCGTTCAGTTGCGCACCTAATCGTGCTGAAGAATTAATCAAATTGACCCATCAAATTTTGGATGAAATTATTGAAAACGGTATAGATGAAACACTACTTCGCAAAAAAAAAGCTGAGCAACAGCAATACATCAAACGTCAGTTTGATTCACTCGTCTCTGTGGCAGGCATGATTGAGGACAGTTATTGGCAGCAAAGCAACCCACAGTCGGTTTATTTGTATCAACGATTGGAACAGATTGCCGACAAACCTCACCTTGAGGCATTAGCAAGAAAAGTTTTAGTCAAAGCTGCCCGTTTTGAAGCAATTTTACGTCAA","","","33853","VLQKYHRETQDYFKQIDAETKFMQSISYLRRPNTATVYTQNQNEQLSFTAAQLSQIYQEKILGKTDFTYFIIGDISRSEVEKLAKRYLATVEIKTQARAYQPGYIHTPKKAFIMRGLSEPRADVEIYLTAENQWHPEQKYALEILAEIVQEKLRLVLREKVSGIYSVNSWFSQDPHTPQIEGKIAFSCAPNRAEELIKLTHQILDEIIENGIDETLLRKKKAEQQQYIKRQFDSLVSVAGMIEDSYWQQSNPQSVYLYQRLEQIADKPHLEALARKVLVKAARFEAILRQ","1764919","","zinc protease","Cytoplasm, Extracellular","","
InterPro
IPR007863
Domain
Peptidase M16, C-terminal
PF05193\"[47-224]TPeptidase_M16_C


","No hits to the COGs database.","","Residues 2 to 289 match (2e-99) PD:PD043014 which is described as ZINC COMPLETE PROTEASE PROTEOME PQQL PROBABLE PROTEASE METALLOPROTEASE 3.4.99.- HYDROLASE ","","","","","","","","","","","","Tue Jan 21 09:17:20 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02534 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 47 to 224 (E-value = 4.3e-22) place AA02534 in the Peptidase_M16_C family which is described as Peptidase M16 inactive domain (PF05193)","","","","","","","","1","","","" "AA02536","1765323","1764994","330","ATGAGCTTAACCGAACAGATTCTCACCATTGCTATCGCAGTATTGGCGGTGCAGTTTACCCGTTGGCTGCCGTTCTGGATTTTCCCCGCCAACCGCCCGATTCCCGAATATATCCGTTATTTGGGCAGAGTGTTACCTGCCGCCATGTTTGGTATGCTGGTGGTGTATTGCTATAAGAATATTGACGTATTGATCGGTTTTCACGGCTTGCCGGAATTTATCGCCGGTGCGGTGGTGTTGGCGCTGCATTTTTGGAAACGCAATATGTTCCTTTCTATCGCTGCCGGCACCATGCTGTATATGTTGCTGGTGCAACAGGTTTTCGTGACA","","","12566","MSLTEQILTIAIAVLAVQFTRWLPFWIFPANRPIPEYIRYLGRVLPAAMFGMLVVYCYKNIDVLIGFHGLPEFIAGAVVLALHFWKRNMFLSIAAGTMLYMLLVQQVFVT","1764992","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR008407
Family
Branched-chain amino acid transport
PIRSF003203\"[1-109]TBranched-chain amino acid transport protein, AzlD type
PF05437\"[6-105]TAzlD
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide
tmhmm\"[10-30]?\"[40-60]?\"[64-84]?\"[89-109]?transmembrane_regions


","BeTs to 4 clades of COG1687COG name: Predicted branched-chain amino acid permeases (azaleucine resistance)Functional Class: EThe phylogenetic pattern of COG1687 is ------------b----h--u-----Number of proteins in this genome belonging to this COG is","","Residues 1 to 109 match (4e-35) PD:PD020505 which is described as COMPLETE PROTEOME TRANSMEMBRANE JHP1250 HP1330 AMINO-ACID BRANCHED-CHAIN AMINO PM0423 ACID ","","","","","","","","","","","","Tue Jan 21 09:21:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02536 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 107 (E-value = 2.2e-67) place AA02536 in the AzlD family which is described as Branched-chain amino acid transport protein (AzlD) (PF05437)","","","","","","","","1","","","" "AA02538","1766052","1765327","726","ATGTCTGATGTTAAGACAACTCCTCATCCTATATTTGCTGCCGCCAAAGCAGCGTTACCGTACAGTTCACCGATGATTGCCGGTTTTTTATTCCTTGGTATGGCATATGGCATTTATATGAAATCCCTGGGATTTGGTGCGTGGTATCCGTTTTTTATGGCACTGTTGATCTACGGTGGTTCGGTGGAATTTATTATTGCCGGCGCGCTCACCTTACCGTTCGCTCCGCTTAATGTGTTATTGATTACACTGATGGTCAGCGGACGACAACTTTTTTACAGCATTTCCATGTTGGAAAAATACGGTAAATATTTGGGCAAGAAACGTCCATATCTCATCGCTGCCCTAGTGGATGAATCCTTCTCTCTCAATTATATGGTAAAAATTCCACCGCACTTGGATCGCGGCTGGTATATGTTTTTCGTCAGCTTTTATTTACAAGTTTATTGGGTGGCAGGCGCGGTACTCGGCAATTTGTTCGGCAACATTATTCCTTTTGATTTAAAGGGCATTGAATTTGCTATGACGGCATTATTCTTAGTGATTTTTGCCGAAAACTGGTCGCGGGAAAAATCCCATGAAAGTTCTGTGTTGGGGCTGGCAATTGCGTTTATTGCGTTGTTAATTTTCGGCAAAGATTACTTCCTGCTGCCGACGCTAATCGGTATTTGGACGGTGCTGACACTCCGTCGCCCGAAACCGAAATCAAAATTGGAGAGGGTGAAA","","","27192","MSDVKTTPHPIFAAAKAALPYSSPMIAGFLFLGMAYGIYMKSLGFGAWYPFFMALLIYGGSVEFIIAGALTLPFAPLNVLLITLMVSGRQLFYSISMLEKYGKYLGKKRPYLIAALVDESFSLNYMVKIPPHLDRGWYMFFVSFYLQVYWVAGAVLGNLFGNIIPFDLKGIEFAMTALFLVIFAENWSREKSHESSVLGLAIAFIALLIFGKDYFLLPTLIGIWTVLTLRRPKPKSKLERVK","1765325","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR004471
Family
AzlC
TIGR00346\"[14-235]TazlC: azaleucine resistance protein AzlC
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[120-235]Tno description
InterPro
IPR011606
Family
AzlC-like
PF03591\"[23-165]TAzlC
noIPR
unintegrated
unintegrated
signalp\"[1-37]?signal-peptide
tmhmm\"[19-39]?\"[54-74]?\"[80-98]?\"[136-154]?\"[160-182]?\"[197-217]?transmembrane_regions


","BeTs to 8 clades of COG1296COG name: Predicted branched-chain amino acid permease (azaleucine resistance)Functional Class: EThe phylogenetic pattern of COG1296 is a--------d-lb-efgh-nuj----Number of proteins in this genome belonging to this COG is","","Residues 149 to 242 match (6e-22) PD:PD021699 which is described as COMPLETE PROTEOME TRANSMEMBRANE JHP1251 HP1331 AMINO-ACID BRANCHED-CHAIN AMINO PM0422 ACID ","","","","","","","","","","","","Tue Jan 21 09:40:54 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02538 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 23 to 182 (E-value = 7.2e-65) place AA02538 in the AzlC family which is described as AzlC protein (PF03591)","","","","","","","","1","","","" "AA02539","1766989","1766060","930","ATGAAACCGATCTTCCTTGAACTCAGACATCTCAAAACTTTACTTGCCCTGAAAGAAACCGGTAGCGTTTCCTTAGCGGCAAAGCGGGTTTATCTCACCCAATCGGCGCTGTCCCATCAAATTAAATTATTGGAAGAACAATACGGCTTGCCGTTATTTGAGCGGAAAACCCAACCGTTGCATTTCACCGCGGCCGGGGAGCGCTTGATTCAGCTTGCCAATGAGATTCTGCCGAAAGTGATTGAAGCGGAGCGCGATCTGGCGCGGGTGAAGCAGGGCGATGCGGGCGAGTTGCGGATTGCCGTGGAGTGTCATACCTGTTTTGACTGGCTGATGCCGGCAATGGATTCTTTCCGCAAGCACTGGCCATTGGTGGAACTGGATATTGTGTCCGGATTCCACACCGATGCCGTCGGCTTATTGCTGAACCATCGCGCCGATTGGGCGGTGGTTCAAGAAGTGGAAGAAAATTCGGGTATTGTATATAAACCATTGTTTTCGTATGAAATGGTCGGCTTATGCGCGAAAGATCATCCCCTGGCGACGAAAGATATTTGGCAGGCGGAAGATTTTTCCGATCAAACTCTGATTACCTATCCTGTGCCGGACGATATGCTGGATTTACTGCGTAAAGTGTTGTATCCGAAAGGCATTAACCCGACCCGTCGCACCAGCGAACTCACCATTGCGATTATTCAACTGGTGGCAAGTAAACGTGGCGTGGCGGCTTTGCCGTTTTGGGCGGCAAAACCTTATTTGGATCGTGGTTATATTGTGGCGCGCAAAATCACTCATCAAGGTTTGCACAGTAATCTCTATGCGGCCTTTCGTGAAACAGACGCGCATATCGCCTTTGTTGATGATTTTTATGAAACCGTTAAAGTACAAAGTTTTTCAACTTTACCTGAATTATCTATATTAGAAGAGAGC","","","35080","MKPIFLELRHLKTLLALKETGSVSLAAKRVYLTQSALSHQIKLLEEQYGLPLFERKTQPLHFTAAGERLIQLANEILPKVIEAERDLARVKQGDAGELRIAVECHTCFDWLMPAMDSFRKHWPLVELDIVSGFHTDAVGLLLNHRADWAVVQEVEENSGIVYKPLFSYEMVGLCAKDHPLATKDIWQAEDFSDQTLITYPVPDDMLDLLRKVLYPKGINPTRRTSELTIAIIQLVASKRGVAALPFWAAKPYLDRGYIVARKITHQGLHSNLYAAFRETDAHIAFVDDFYETVKVQSFSTLPELSILEES","1766058","From PF00126: Bacterial regulatory helix-turn-helix protein,lysR family.Numerous bacterial transcription regulatory proteins bind DNA via a helix-turn-helix (HTH) motif. These proteins are very diverse, but for convenience may be grouped into subfamilies on the basis of sequence similarity. One such family, the lysR family, groups together a range of proteins, including ampR, catM, catR, cynR, cysB, gltC, iciA, ilvY, irgB, lysR, metR, mkaC, mleR, nahR, nhaR, nodD, nolR, oxyR, pssR, rbcR, syrM, tcbR, tfdS and trpI.The majority of these proteins appear to be transcription activators and most are known to negatively regulate their own expression. All possess a potential HTH DNA-binding motif towards their N-termini. ","transcriptional activator","Cytoplasm","","
InterPro
IPR000847
Domain
Bacterial regulatory protein, LysR
PR00039\"[23-34]T\"[34-44]T\"[44-55]THTHLYSR
PF00126\"[8-67]THTH_1
PS50931\"[6-63]THTH_LYSR
InterPro
IPR005119
Domain
LysR, substrate-binding
PF03466\"[91-297]TLysR_substrate
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[6-92]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[95-206]Tno description
signalp\"[1-16]?signal-peptide


","No hits to the COGs database.","Significant hit ( 2.7e-16) to 1/1 blocks of the IPB000847 family, which is described as \"Bacterial regulatory protein, LysR family\". Interpro entry for IP:IPR000847. IPB000847 22-55 2.7e-16Significant hit ( 4.9e-08) to 1/2 blocks of the IPB001583 family, which is described as \"NodD transcription activator carboxyl terminal region\". Interpro entry for IP:IPR001583. IPB001583A 10-60 4.6e-08","Residues 85 to 178 match (9e-23) PD:PD462572 which is described as TRANSCRIPTION TRANSCRIPTIONAL PROTEOME COMPLETE DNA-BINDING REGULATION REGULATOR ACTIVATOR PROBABLE LYSR ","","","","","","","","","","","Tue Jan 21 10:09:09 2003","Tue Jan 21 10:01:02 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02539 is paralogously related to AA01999 (5e-16), AA01513 (3e-12), AA01794 (4e-12), AA00985 (1e-11), AA00940 (2e-11), AA00977 (1e-06) and AA00371 (1e-04).","","","","","","Residues 91 to 297 (E-value = 2.3e-39) place AA02539 in the LysR_substrate family which is described as LysR substrate binding domain (PF03466)","","","","","","","","1","","","" "AA02540","1767289","1769559","2271","ATGACAACTTTTCATTTATCCGGCTTTCCGCGCGTGGGCGCAAAACGTGAACTTAAATTTGCACAAGAACGTTATTGGCGCGGTGAAATCGCAGAAGCCGATTTATTAGACATCGCCAAAGCCTTACGCGAAATCAACTGGAAACACCAAGCGGCAGCGAATGCGGATTACGTCGCCGTGGCGGATTTCACCTTCTACGATCACATTTTAGACTTGCAAGTGGCAACAGGCGCGATTCCGGCTCGTTTCGGCTTTGACAGCCAACATTTAACCCTTGATCAATATTTCCAACTGGCGCGCGGTAACAAAGCACAATTTGCCATTGAAATGACCAAATGGTTTGACACCAACTATCATTACCTCGTGCCGGAATTCCACGCGGATACCCAATTCAAAGCTAATCCGGCGCATTACGTGCAACAAATTCGCGAAGCCAAAGCCCTTGGCTTGAATGTTAAACCCACTATTGTTGGTCCATTAACGTTCTTGTGGTTAGGCAAAGAAAAAGGTGCGGCATTTAATCGCTTTGATTTATTAAATAAACTCATACCGGTTTATGTAGAAATCTTAAACGCATTGGCAGCAGAAGGCGTGGATTATATTCAAATTGACGAACCTGCTTTAACTGTCGATTTGCCGGCTAAATGGGTTGCGGCTTATAAAGACGTGTACGCCACATTAAGCACACAAGTAAACGCAAAATTACTGTTAGCCACTTATTTCGGTTCTGTCGCGGAACACGCTGCGTTATTAAAAGCCTTGCCGGTTGCGGGCTTACACATTGATTTAGTGCGTGCGCCTGACCAACTTTCCGCCTTTGCTGATTACGACAAGATTTTGTCTGTGGGCGTGATTGATGGTCGTAACATTTGGCGTGCGAACCTGAACCAAGTGTTGGATGTGGTGGAACCGTTAAAAGCGAAACTGGGCGATCGTTTGTGGATTGCGCCAAGCTGTTCTCTGCTTCACACCCCTTATGATTTATCGGTGGAAACACAGTTACAAGTAAACAAACCTAAACTTTACAGCTGGCTTGCATTCTGTTTACAAAAAATTCAAGAATTACGCGTCATTAAGACCGCACTTGAGCAAGGCAGAGCCGCCGTACAAGCGGAACTGGATGCCAGCCAAGTTGCCGCCGATGCCCGTGCGACCTCAAAAGATATTCATCGCCCTGAAGTGGCGGAACGTTTGGCGAACTTGCCAAAAGGCGCGGATCAACGTAAATCCTCGTTTGCGGAACGTATCAAATTACAAAATGCCTGGTTAAATCTACCGTTATTGCCAACCACGAATATCGGTTCTTTCCCGCAAACTACTGAAATTCGACACGCGCGCGCCGCCTTCAAAAAAGGCACATTGTCCCTTGCGGATTATGAAGCGGCAATGAAAAAAGAAATCGAATTGGTGGTGCGTGAGCAAGAAAAATTGGATTTAGACGTGCTGGTTCACGGCGAAGCGGAACGTAACGACATGGTGGAATATTTCGGCGAATTATTAGACGGTTTTGCCTTCACCAAATTCGGTTGGGTACAAAGCTACGGTTCCCGTTGTGTAAAACCGCCGGTGATTTACGGCGATGTGGTTCGCCCTGAGCCAATGACGGTACGCTGGTCGCAATATGCCCAAAGTTTAACGCAAAAAGTGATGAAAGGCATGTTGACCGGCCCGGTAACGATTTTACAATGGTCTTTCGTACGCAATGATATTCCGCGTTCAACCGTATGTAAACAAATCGCCGTGGCACTTTCCGATGAAGTGTTGGATTTGGAAAAAGCCGGCATTAAAGTGATTCAAATTGACGAACCGGCAATTCGCGAAGGCTTACCGCTCAAACGCGCCGATTGGGACGCTTATTTACAATGGGCAGGAGAAGCATTCCGTTTAAGTTCAATGGGTTGCCAAGATGATACGCAAATTCACACCCACATGTGTTATTCCGAATTTAACGACATTTTACCGGCAATCGCAGGCTTGGACGCAGATGTGATCACCATCGAAACCTCTCGTTCCGACATGGAATTATTAACGGCATTCGGCGATTTCAAATACCCGAACGACATTGGCCCGGGCGTGTACGACATCCACAGCCCACGCGTCCCAACCGCCGCCGAAATCGAACACTTGCTACGCAAAGCGTTACAAGTGGTACCGAAAGAACGCTTATGGGTCAACCCGGACTGTGGTTTAAAAACCCGCGGTTGGCCGGAAACCATCGCCGCATTAAAAGTGATGGTGGATGTAACGAAAAAATTACGCGTGGAATTAGCG","","","84888","MTTFHLSGFPRVGAKRELKFAQERYWRGEIAEADLLDIAKALREINWKHQAAANADYVAVADFTFYDHILDLQVATGAIPARFGFDSQHLTLDQYFQLARGNKAQFAIEMTKWFDTNYHYLVPEFHADTQFKANPAHYVQQIREAKALGLNVKPTIVGPLTFLWLGKEKGAAFNRFDLLNKLIPVYVEILNALAAEGVDYIQIDEPALTVDLPAKWVAAYKDVYATLSTQVNAKLLLATYFGSVAEHAALLKALPVAGLHIDLVRAPDQLSAFADYDKILSVGVIDGRNIWRANLNQVLDVVEPLKAKLGDRLWIAPSCSLLHTPYDLSVETQLQVNKPKLYSWLAFCLQKIQELRVIKTALEQGRAAVQAELDASQVAADARATSKDIHRPEVAERLANLPKGADQRKSSFAERIKLQNAWLNLPLLPTTNIGSFPQTTEIRHARAAFKKGTLSLADYEAAMKKEIELVVREQEKLDLDVLVHGEAERNDMVEYFGELLDGFAFTKFGWVQSYGSRCVKPPVIYGDVVRPEPMTVRWSQYAQSLTQKVMKGMLTGPVTILQWSFVRNDIPRSTVCKQIAVALSDEVLDLEKAGIKVIQIDEPAIREGLPLKRADWDAYLQWAGEAFRLSSMGCQDDTQIHTHMCYSEFNDILPAIAGLDADVITIETSRSDMELLTAFGDFKYPNDIGPGVYDIHSPRVPTAAEIEHLLRKALQVVPKERLWVNPDCGLKTRGWPETIAALKVMVDVTKKLRVELA","1769557","From Genbank:[gi:1170933]This protein catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.","5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferase","Cytoplasm","","
InterPro
IPR002629
Domain
Methionine synthase, vitamin-B12 independent
PD004692\"[650-746]TMETE_PASMU_P57843;
PF01717\"[428-751]TMeth_synt_2
InterPro
IPR006276
Family
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase
TIGR01371\"[7-755]Tmet_syn_B12ind: 5-methyltetrahydropteroyltr
InterPro
IPR013215
Domain
Cobalamin (vitamin B12)-independent methionine synthase MetE, N-terminal
PF08267\"[3-310]TMeth_synt_1
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.210\"[16-346]T\"[422-753]Tno description


","No hits to the COGs database.","Significant hit ( 1e-286) to 13/13 blocks of the IPB002629 family, which is described as \"Methionine synthase, vitamin-B12 independent\". Interpro entry for IP:IPR002629. IPB002629A 8-26 5.7e-14 IPB002629B 53-73 2e-10 IPB002629C 109-121 1e-11 IPB002629D 141-167 3.3e-15 IPB002629E 182-212 4e-16 IPB002629F 282-295 2.6e-08 IPB002629G 315-331 1.7e-10 IPB002629H 423-458 9.5e-26 IPB002629I 474-518 5.9e-45 IPB002629J 530-578 4.3e-45 IPB002629K 638-671 4e-31 IPB002629L 688-701 1.8e-11 IPB002629M 722-753 1.5e-27 IPB002629E 579-609 0.13","Residues 571 to 604 match (2e-10) PD:PD590929 which is described as METHIONINE METHYLTRANSFERASE TRANSFERASE SYNTHASE COBALAMIN-INDEPENDENT 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE ISOZYME B INDEPENDENT VITAMIN-B12 ","","","","","","","","","","","Tue Jan 21 10:13:42 2003","Tue Jan 21 10:13:42 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02540 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 428 to 751 (E-value = 2e-226) place AA02540 in the Methionine_synt family which is described as Methionine synthase, vitamin-B12 independent (PF01717)","","","","","Zhou,Z.S., Peariso,K., Penner-Hahn,J.E. and Matthews,R.G.Identification of the zinc ligands in cobalamin-independentmethionine synthase (MetE) from Escherichia coliBiochemistry 38 (48), 15915-15926 (1999)PubMed: 10625458Gonzalez,J.C., Peariso,K., Penner-Hahn,J.E. and Matthews,R.G.Cobalamin-independent methionine synthase from Escherichia coli: azinc metalloenzymeBiochemistry 35 (38), 12228-12234 (1996)PubMed: 8823155Maxon,M.E., Redfield,B., Cai,X.Y., Shoeman,R., Fujita,K.,Fisher,W., Stauffer,G., Weissbach,H. and Brot,N.Regulation of methionine synthesis in Escherichia coli: effect ofthe MetR protein on the expression of the metE and metR genesProc. Natl. Acad. Sci. U.S.A. 86 (1), 85-89 (1989)PubMed: 2643109Gonzalez,J.C., Banerjee,R.V., Huang,S., Sumner,J.S. andMatthews,R.G.Comparison of cobalamin-independent and cobalamin-dependentmethionine synthases from Escherichia coli: two solutions to thesame chemical problemBiochemistry 31 (26), 6045-6056 (1992)PubMed: 1339288","","Tue Jan 21 10:19:11 2003","1","","","" "AA02541","1772704","1769996","2709","ATGAGCATCAGAACTCAAAACTACATCAACGGGCGTCTGTCTTTGCGCCCGCCGCAAGCGGAGAGCTTGGCAAAATTAAAACAGGCATTGGATGCCGCGCCTGAAATGGCACAAAAAGAACGCGATGTGGCGGCGGTGTTGGCGACCTTAAAAGCCGAATTTCCGACCTTGCAGGATTTTGAGCGCGAATTTCCGTCCTTGTGTTTCGCCTTGGCAACGGGCGTAGGGAAAACCCGTCTGATGGGGGCGTTTATTGCTTATCTGCATTTGGCGCATGGGATTAACAATTTTTTTGTCCTTGCGCCGAATCTGACGATTTACAACAAATTAATTGCGGATTTCACGCCTAATACGCCCAAATATGTGTTTAAGGGAATTAGTGAGTTTGCGGTTACGTCGCCAAAATTGATTACCGGCGATAATTATGAAAGTCAGAATTTAAGTATGGGCATGGATAATCTCTTCGGCGATATTACCATCAATGTCTTCAACATTTCCAAAATCAATTCTGAAGTGCGCGGCGGCAAAGAACCCAAAATCAAGCGGATGCGCGAAGTATTGGGCGACAGTTATTTCAATTATCTGGCGAGCTTGCCCGATTTGGTGTTGCTGATGGACGAATCCCACCGCTATCGGGCGCAGGCGGGGATGCGGGCGATTAATGAATTAAATCCGCTGTTCGGTTTAGAGCTGACTGCCACACCCTTTGTGGAATCCACCAAAGCGCCGATTGCGTTTAAAAACGTGATTGTAGATTATCCGCTGGCGCGGGCGATGGAAGACGGTTTTGTGAAAATGCCGGCGGTGGTTACGCAGCGTAATTTTGATGCGAAAAATTACACGCCGGAAGAAATTGAAAAAATCAAGCTGGAAGACGGCGTGCGCGTGCATGAAAACACCAAAGTGGAGCTTTTGACTTATGCGCGGGAAAATAATGTTGCCGTTGTGAAACCCTTTATGCTGGTCATCGCCCGCGATACCACTCACGCAGCGCAGCTTCTGACCTTGCTGGAATCGGATGCGTTTTATAACGGACGTTATCAAGGCAAAGTTATTCAGGTGGATTCGAGCAAATCGGGCAAAGACGAAGAGGAAATGATCGAGCGGCTGTTGGCGGTGGAAATCGTAGATGAGCCGACGGAAATTGTAATTCACGTCAATATGCTCAAAGAAGGCTGGGACGTTACCAATCTTTACACCATCGTGCCGCTGCGCGCCGCCAATGCCAGAACGCTGATCGAGCAGTCCATCGGTCGCGGTTTGCGCCTGCCATACGGCAGCACGGGCGTGGAAATTGTAGATCGGCTCAATATCGTCGCGCACGACCGCTTTCAGGAAATCATCGATGAAGCCAATAAAGGCGATTCGGTATTGAAATTAAAGCAGGTGATTTTGGCTGCGCCGAGTGTGGACGACAAAAAGGTGAGCGTACAGGTGGCCAGCCAAACGGAAACGTTGTTGGGCTTGGCGGAGACGTCGTCTGAAAATCCGGAACAAAGCGTGTTGCAAGCTCATACTTCGGTGGATTATCAGCCTGTTTTTAAAACCGAAAACGAAAAACGTATCGCTCGGGCGGTGATGGAAACCGCCGCCAAATATTCCGCCCGTCCAAGCGAAGCGCTGACTTCTCAAGCGTTATTGAGCGATGAAATCCGCCAAAAAATCATCAAGGAAGTTCAGACGACCTTGCAACCGATGCAAGGCGAACTGCTGGCGGATCATGAGGTGGATATGGCACAAATTGTCGCCAAAACGACAGAAATCATGGCGGCGCAAACCATCGATATTCCGCGCATTACCGTTGTGCCAAGCGGCGAAGTCAGCAGCGGCTTTCACCCGTTTAAACTGGATGTCGGCGGTCTGCACCTGCAACCGGGCGTACGCGAAATCACCATTCACAATCTGCATACCAACGAGCAAAGCAGCCTTTCTGCCGAATTGGGTTTGAAGGAAAAACGCCCCGAAGACTATATCGTCTTTGCGCTGATTGATTTTGAAGATATTGATTATCTGACCCAAGCCGATTTGCTTTACGATTTGGCAGGACAGATGGTGGCGCATTTGCACAGTTATTTGTCGGAAAGCGAAGCCTTGGAAGTATTGGATAAAGACCGCCGTCTGATTGCCAAAGAAATCCATGCTCAAATGCAGGCGCATTTTGAGGAGACCCCCACCGATTACGAAGTCCGCGTTAGCCAAGGATTCAGCACACTCAAATCCTGCAACTATACTGTTTCTGCTGATGAACCGATCCATTCCGTTCGACAGACACCAAAAGATGTCAGCCGTATTAAGCAAATGCTGTTTGGCGGATTTACCAAGTGCCTGTATCCGCTTCAAAAATTCGATTCCGACACCGAACGCCGCTTTGCTGTAATTTTGGAGCGCGATGCACAAAAATGGTTCAAACCCGTACAAGGACAGTTTCAGATTTACTGGAAATCAGGGTTGGATTCAAAAGAATACGTTCCCGATTTTGTGGTGGAAACTGAAGACGGCGTTTGGCTTGCCGAAATCAAAGCCCGCACGGATTTGGAAAGCCCGGAAGTTGTCGCCAAAGCCGAAGCTGCCATCCAATGGTGCAAACACGCCTCCGAATATGCTTTAAAACACGGCGGCAAGCCTTGGCGCTATGTTTTGATTCCGCATGATGAAGTCAACGAATCGAAAAGATTGGCGGATTTTTTAAGATTTGAGAAAAAGATCGTC","","","101542","MSIRTQNYINGRLSLRPPQAESLAKLKQALDAAPEMAQKERDVAAVLATLKAEFPTLQDFEREFPSLCFALATGVGKTRLMGAFIAYLHLAHGINNFFVLAPNLTIYNKLIADFTPNTPKYVFKGISEFAVTSPKLITGDNYESQNLSMGMDNLFGDITINVFNISKINSEVRGGKEPKIKRMREVLGDSYFNYLASLPDLVLLMDESHRYRAQAGMRAINELNPLFGLELTATPFVESTKAPIAFKNVIVDYPLARAMEDGFVKMPAVVTQRNFDAKNYTPEEIEKIKLEDGVRVHENTKVELLTYARENNVAVVKPFMLVIARDTTHAAQLLTLLESDAFYNGRYQGKVIQVDSSKSGKDEEEMIERLLAVEIVDEPTEIVIHVNMLKEGWDVTNLYTIVPLRAANARTLIEQSIGRGLRLPYGSTGVEIVDRLNIVAHDRFQEIIDEANKGDSVLKLKQVILAAPSVDDKKVSVQVASQTETLLGLAETSSENPEQSVLQAHTSVDYQPVFKTENEKRIARAVMETAAKYSARPSEALTSQALLSDEIRQKIIKEVQTTLQPMQGELLADHEVDMAQIVAKTTEIMAAQTIDIPRITVVPSGEVSSGFHPFKLDVGGLHLQPGVREITIHNLHTNEQSSLSAELGLKEKRPEDYIVFALIDFEDIDYLTQADLLYDLAGQMVAHLHSYLSESEALEVLDKDRRLIAKEIHAQMQAHFEETPTDYEVRVSQGFSTLKSCNYTVSADEPIHSVRQTPKDVSRIKQMLFGGFTKCLYPLQKFDSDTERRFAVILERDAQKWFKPVQGQFQIYWKSGLDSKEYVPDFVVETEDGVWLAEIKARTDLESPEVVAKAEAAIQWCKHASEYALKHGGKPWRYVLIPHDEVNESKRLADFLRFEKKIV","1769994","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR006935
Family
Type III restriction enzyme, res subunit
PF04851\"[12-237]TResIII


","BeTs to 3 clades of COG1061COG name: DNA or RNA helicases of superfamily IIFunctional Class: LThe phylogenetic pattern of COG1061 is ao-pkzy--drl--e-g-------t-Number of proteins in this genome belonging to this COG is","","Residues 7 to 168 match (3e-69) PD:PD034991 which is described as COMPLETE PROTEOME SMR BU098 DOMAIN FAMILY HI1202 YDAL SMR/MUTS Z3594 ","","","","","","","","","","","","Tue Jan 21 10:28:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02541 is paralogously related to AA00028 (4e-10).","","","","","","","","","","","","","","1","","","" "AA02543","1773494","1772841","654","ATGTCTACCCACATTATTCCCCGCCTGCAAAAAGTCATTGATGGCGAAGACCAAGGCGGGATTTCCAAAGCGGTGAATTGGCAGGGCGGCGGCGGTTTCCGTTATTTCCGTTTGGCACCGACGTTGATTGTGAACGACAAATGGGGCAACCAAATCATCAACCCCGACTACAACCCCGAAATGCTGGCGGAAGCGCTTGCCAAGCTGGAAGGTTTACCCGATTTCTCTTGGATCTTGGAATTGGGCAGCGGCTTTGCCTTTGTTGGACGGCAGTATCGTTTGGAAGTGAACGGCGATGAATTTTTTATCGATTTGCTTTTCTACCACATCCGTCTGAAATGTTATGTGGTGGTGGAATTAAAAGCCGCCGCATTTAAGCCCGAACACGCGGGACAATTGAATTTCTATTTGGCAGCAGTCGATGCCCAAGTAAAAGCTCCTGACGATAATCCGACTATCGGTTTGCTGTTGTGCAAAACACAAAACCGATTGGTTGCCGAATACGCCTTGTCGGACATTGATAAGCCTATCGGTATTGCCGAATACGAATTGGTACGCGCCTTGCCGGAACCCTTGGTAACGAATCTGCCGACTGTGGAACAATTGGAAAGCGAATTGTCGGACTGGCAGGAAGACGGGGAATTTTTTGGCGTT","","","24403","MSTHIIPRLQKVIDGEDQGGISKAVNWQGGGGFRYFRLAPTLIVNDKWGNQIINPDYNPEMLAEALAKLEGLPDFSWILELGSGFAFVGRQYRLEVNGDEFFIDLLFYHIRLKCYVVVELKAAAFKPEHAGQLNFYLAAVDAQVKAPDDNPTIGLLLCKTQNRLVAEYALSDIDKPIGIAEYELVRALPEPLVTNLPTVEQLESELSDWQEDGEFFGV","1772839","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR009362
Family
Protein of unknown function DUF1016
PF06250\"[4-199]TDUF1016


","BeTs to 3 clades of COG2189COG name: Adenine specific DNA methylase ModFunctional Class: LThe phylogenetic pattern of COG2189 is a--p-------------hsnuj---wNumber of proteins in this genome belonging to this COG is","","Residues 115 to 171 match (2e-14) PD:PD352722 which is described as COMPLETE PROTEOME CYTOPLASMIC RSC2621 RC0365 YHCG ORF ORF3 STY3512 ","","","","","","","","","","","","Tue Jan 21 10:29:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02543 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 199 (E-value = 4.3e-14) place AA02543 in the DUF1016 family which is described as Protein of unknown function (DUF1016) (PF06250)","","","","","","","","1","","","" "AA02544","1774005","1773457","549","ATGCCCCATCACCAGCTTACTCCCTATCAAGCCCGATACTACTCCTGGTTACTTACCCGTCAAGCCGAGGGGAGCAACGTCGAATCTTTAGCAAGCACCTTAGTCGATGCCCAAGTCGATTTGAATCCGCACCAAGTGGATGCAGCTTTGTTTGCCTGCCAAAATCCCCTGTCAAAAGGCGTGATTCTGGCGGATGAGGTCGGTTTGGGTAAAACTATTGAAGCGGGCTTGGTGATTTTGCAGCGTTGGGCGGAGCGCAAACGCAAAATTCTGATTATTACGCCTGCCAACCTGCGCAAACAATGGCATCAGGAATTGCAAGAAAAATTCGGTTTGCAAGGCATGATTTTGGAAGCCAAAAGCTACAACGCTGACAAGAAAACGGGCAAAAACCCATTCCGTCAAGAAAGCCCCGTTATTTGTTCTTACCAGTTCGCCAAATCCAAAGCGGACGACATCAAACAAATCGGCTGGGATTTGGTCGTATTGGACGAGGCGCACCGCCTACGCAATGTCTACCCACATTATTCCCCGCCTGCAAAAAGTCAT","","","20769","MPHHQLTPYQARYYSWLLTRQAEGSNVESLASTLVDAQVDLNPHQVDAALFACQNPLSKGVILADEVGLGKTIEAGLVILQRWAERKRKILIITPANLRKQWHQELQEKFGLQGMILEAKSYNADKKTGKNPFRQESPVICSYQFAKSKADDIKQIGWDLVVLDEAHRLRNVYPHYSPPAKSH","1773455","","ATP-dependent RNA helicase","Cytoplasm, Periplasm","","
InterPro
IPR000330
Domain
SNF2-related
PF00176\"[44-171]TSNF2_N
InterPro
IPR014001
Domain
DEAD-like helicases, N-terminal
SM00487\"[37-183]TDEXDc
InterPro
IPR014021
Domain
Helicase superfamily 1 and 2 ATP-binding
PS51192\"[52-183]THELICASE_ATP_BIND_1
noIPR
unintegrated
unintegrated
PTHR10799\"[29-171]TATP-DEPENDENT HELICASE SMARCA (SWI/SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN A)-RELATED
PTHR10799:SF40\"[29-171]TATP-DEPENDENT HELICASE


","BeTs to 16 clades of COG0553COG name: Superfamily II DNA/RNA helicases, SNF2 familyFunctional Class: K,LThe phylogenetic pattern of COG0553 is ao-pkzy-vdrlbcefghs----i-wNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.8e-12) to 3/7 blocks of the IPB000330 family, which is described as \"SNF2 related domain\". Interpro entry for IP:IPR000330. IPB000330A 41-55 4 IPB000330B 62-76 2.5e-06 IPB000330C 89-102 0.031","Residues 43 to 110 match (1e-09) PD:PD334662 which is described as HELICASE ATP-BINDING PROTEOME COMPLETE DNA NUCLEAR REPAIR ZINC-FINGER DNA-BINDING TRANSCRIPTION ","","","","","","","","","","","","Tue Jan 21 10:32:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02544 is paralogously related to AA01928 (2e-19).","","","","","","","","","","","","","","1","","","" "AA02545","1774281","1774105","177","GTGCAAATCCCTGAAAAAGCGTTTGAGGCTTTATATAAGGCAGGACGCATTGAGCCGATAAACGAGAAAACCTTCGGTAGACAATTTTATACACTGATTGGGCTGGATTTGTATGACGAGGTGGCGGAGCTTTCTTCGGAAGATACGGAGTTTTTGAAGAAAGAAAACTTGGTGTTT","","","6840","VQIPEKAFEALYKAGRIEPINEKTFGRQFYTLIGLDLYDEVAELSSEDTEFLKKENLVF","1774105","","conserved hypothetical protein","Cytoplasm","This sequence is similar to gi|34496679, a predicted conserved hypothetical from Chromobacterium violaceum ATCC 12472. See also gi|21244561 from Xanthomonas axonopodis pv.citri str. 306.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 09:08:49 2004","Wed Feb 25 09:11:16 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02545 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 09:08:49 2004","","","","","","","","","","","","","1","","","" "AA02546","1774678","1774821","144","TTGAAGCATAAAAACACCTACTTTTTAGACCGCACTTTTCACTCCGCAAGCGCATCCATAAAAAATATTTACTGCCAAGAATTGACTTTTCCCTTCTCAACCCTTACTTTACACAAAGGTTTTAACCTGTTATTTTCTTTAATT","","","5590","LKHKNTYFLDRTFHSASASIKNIYCQELTFPFSTLTLHKGFNLLFSLI","1774821","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 09:01:44 2004","Wed Feb 25 09:01:44 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02546 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 09:01:44 2004","","","","","","","","","","","","","1","","","" "AA02547","1774835","1775494","660","ATGCAATCTCGTATTATTGTTAGCACGCAGGAAGAATCGTTGCTGAGCACACATAAAGTGTTGCGTAACACCTATTTCCTATTGGCTTTGACGTTAGCATTTTCTGCTGTGGTGGCCTATGTTTCCATGGCGATGAATTTACCAAGACCGGGGTTAATTCTGATGCTTGTGGGTTTCTACGGTTTACTTTTCTTAACCAATGCGTTGGCAAACAGTGCGTTGGGGATTTTGTCCGTTTTCGCCTTTACCGGCTTCTTGGGTTATACCGTCGGACCGATTTTAAATGCGTATGTGAGTGCCGGTTTGGGTGATGCTATCGTGTTGGCATTGGCGGGTACTGCGGCGACCTTCTTCGCATGCTCTGCCTATGTATTGACCACGAAGAAAGATATGTCTTTCTTGTCCGGCACCATTTTAGCCTTATTCGTGGTGTTGTTACTTGGCATGATCGCCAGTTTCTTCTTCCAATTCCCGGCGCTTTATGTAGGTATCAGTGCGTTGTTCGTGATTTTCTCCACCATGGGAATTCTGTATGAAACCAGCAACATCATTCACGGCGGCGAAACCAACTATATTCGTGCCACAGTAAGTTTATTCGTATCAATCTATAACTTATTTATCAGCTTGTTAAACTTACTTTCATTCTTCTCTTCCCGAGAT","","","23725","MQSRIIVSTQEESLLSTHKVLRNTYFLLALTLAFSAVVAYVSMAMNLPRPGLILMLVGFYGLLFLTNALANSALGILSVFAFTGFLGYTVGPILNAYVSAGLGDAIVLALAGTAATFFACSAYVLTTKKDMSFLSGTILALFVVLLLGMIASFFFQFPALYVGISALFVIFSTMGILYETSNIIHGGETNYIRATVSLFVSIYNLFISLLNLLSFFSSRD","1775492","","transmembrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR006214
Family
Protein of unknown function UPF0005
PTHR23291\"[21-213]TBAX INHIBITOR-RELATED
PF01027\"[13-217]TUPF0005
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[13-175]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-39]?signal-peptide
tmhmm\"[24-44]?\"[50-70]?\"[75-95]?\"[105-125]?\"[135-155]?\"[161-181]?\"[196-216]?transmembrane_regions


","BeTs to 10 clades of COG0670COG name: Integral membrane protein, interacts with FtsHFunctional Class: RThe phylogenetic pattern of COG0670 is ------y--d-lbcefgh-nujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-40) to 3/3 blocks of the IPB002199 family, which is described as \"Uncharacterized protein family UPF0005\". Interpro entry for IP:IPR002199. IPB002199A 16-38 8.1e-10 IPB002199B 103-139 4.8e-14 IPB002199C 166-209 5.6e-14","Residues 76 to 131 match (4e-08) PD:PD556540 which is described as PROTEOME COMPLETE TRANSMEMBRANE CARRIER/TRANSPORT YCCA PA2604 HI0044 MEMBRANE PM0402 FAMILY ","","","","","","","","","","","","Tue Jan 21 10:39:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02547 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 13 to 217 (E-value = 3.3e-48) place AA02547 in the UPF0005 family which is described as Uncharacterised protein family UPF0005 (PF01027)","","","","","","","","1","","","" "AA02548","1775517","1775909","393","ATGCAGCGCCCCTTTTTTGGGGCGTTTTTATATAACCAAATCCGTATAAATCATGAGGTCTTGCCGATGCTCGAAGTCAATAAAAAACGCATTGAAACCGATGCGTCGGGGTATTTACTAAATATAAATGATTGGACACCGGACGTCGCCTTAGCGATTGCAAAGTTAGAAAATCTGGAATTAACGGATGCCCATTGGGAAATTATCCATTTTGTGCGTGATTTTTATCAAGAATATAAAACCTCTCCTGCCATTCGTATGTTGGTGAAAGCCACCGCGCAAAAGCTGGGAGAAGATAAAGGCAATAGCCGTTATTTGCAACGTTTATTTCCCGATGGTCCGGCAAAACAGGCAACCAAGCTGGCGGGTCTCCCCAAACCGGTAAAATGTCTA","","","15041","MQRPFFGAFLYNQIRINHEVLPMLEVNKKRIETDASGYLLNINDWTPDVALAIAKLENLELTDAHWEIIHFVRDFYQEYKTSPAIRMLVKATAQKLGEDKGNSRYLQRLFPDGPAKQATKLAGLPKPVKCL","1775907","","desulfoviridin gamma subunit","Cytoplasm","","
InterPro
IPR007453
Family
DsrC-like protein
PF04358\"[23-131]TDsrC
noIPR
unintegrated
unintegrated
PD012617\"[42-131]TQ9CNM6_PASMU_Q9CNM6;
G3DSA:1.10.10.370\"[61-131]Tno description


","BeTs to 5 clades of COG2920COG name: Sulfite reductase, gamma subunitFunctional Class: PThe phylogenetic pattern of COG2920 is a-------------efgh--------Number of proteins in this genome belonging to this COG is","","Residues 29 to 131 match (6e-44) PD:PD012617 which is described as PROTEOME COMPLETE SUBUNIT GAMMA SULFITE REDUCTASE REDUCTASE DISSIMILATORY YCCK HOMOLOG ","","","","","","","","","","","","Tue Jan 21 10:45:05 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02548 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 23 to 131 (E-value = 3.3e-77) place AA02548 in the DsrC family which is described as DsrC like protein (PF04358)","","","","","Karkhoff-Schweizer RR, Bruschi M, Voordouw G. Expression of the gamma-subunit gene of desulfoviridin-type dissimilatory sulfite reductase and of the alpha- and beta-subunit genes is not coordinately regulated. Eur J Biochem. 1993 Feb 1;211(3):501-7. PMID: 8436111 ","","Tue Jan 21 10:45:48 2003","1","","","" "AA02549","1776010","1776888","879","ATGCGTTTATTAGCCACATTAGTCAGCGTACTTGCGTTAAGCTTAAGCAGTAGTCTTGCTTATGCGAAATTTAAAGTTGTCACTACGTTCACTATTATTCAAGATATGGCACAAAATGTCGCCGGTGATGCGGCAACCGTAGAGTCCATCACCAAGCCCGGAGCAGAAATCCATGATTACGAGCCAACCCCGAAAGATATTGTCAAGGCACAATCTGCCGATTTAGTGTTATGGAATGGTTTGAACCTTGAGCGTTGGTTTGAAAAATTCTTCCAAAACGTCAAAGATAAACCGGCGGTCGTTGTAACCGAAGGCATTGAGCCGATGTCAATTCATGAAGGTCCGTACACCGGCAACCCGAACCCGCATGCCTGGATGTCACCTTCCAATGCGTTAATCTATGTTGAAAATATTAAAAATGCGTTGATTAAATACGATCCGCAAAATAAAGAAACATACGAAAAAAATACCGCACTTTATATCCAAAAAATCAAAGAACTTGATCAACCGTTGCGTGAAAAATTAGCACAAGTGCCGGAAGCACAGCGTTGGTTGGTGACCAGCGAAGGCGCATTCAGTTATTTAGCACGTGATTACGGTTTTAAAGAGGCTTATTTGTGGCCGATTAACGCTGAGCAACAAGGCACGCCGCAACAAGTGCGTAAAGTAATTGAAACCGTCAAAGCCAACAATATTCCGGTCGTATTCAGTGAAAGCACCATCTCCCCGAAACCGGCAAAACAAGTAGCAAAAGAAACCGGTGCAAAATACGGTGGCGTGCTTTATGTTGACTCTCTTTCCGGTGCCAAGGGTCCTGTGCCGACTTATATTGATTTATTAAAAGTGACTGTTTCTACCATTGCTAAAGGATTTGAAAAA","","","35792","MRLLATLVSVLALSLSSSLAYAKFKVVTTFTIIQDMAQNVAGDAATVESITKPGAEIHDYEPTPKDIVKAQSADLVLWNGLNLERWFEKFFQNVKDKPAVVVTEGIEPMSIHEGPYTGNPNPHAWMSPSNALIYVENIKNALIKYDPQNKETYEKNTALYIQKIKELDQPLREKLAQVPEAQRWLVTSEGAFSYLARDYGFKEAYLWPINAEQQGTPQQVRKVIETVKANNIPVVFSESTISPKPAKQVAKETGAKYGGVLYVDSLSGAKGPVPTYIDLLKVTVSTIAKGFEK","1776886","","iron (chelated) ABC transporter, periplasmic-binding protein","Periplasm, Inner membrane","This sequence corresponds to AY762615 in GenBank.","
InterPro
IPR006127
Family
Periplasmic solute binding protein
PF01297\"[1-292]TSBP_bac_9
InterPro
IPR006128
Family
Adhesion lipoprotein
PR00690\"[23-41]T\"[54-67]T\"[67-84]T\"[178-199]T\"[231-249]T\"[257-276]TADHESNFAMILY
InterPro
IPR006129
Family
Adhesin B
PR00691\"[23-44]T\"[48-66]T\"[67-86]T\"[178-195]T\"[204-222]T\"[227-244]T\"[249-267]TADHESINB
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1980\"[22-164]T\"[167-291]Tno description
signalp\"[1-22]?signal-peptide


","No hits to the COGs database.","Significant hit ( 2e-68) to 6/6 blocks of the PR00690 family, which is described as \"Adhesin family signature\". Prints database entry for PR:PR00690. PR00690A 23-41 4.4e-12 PR00690B 54-67 1.5e-07 PR00690C 67-84 1e-10 PR00690D 178-199 4.1e-14 PR00690E 231-249 1.5e-07 PR00690F 257-276 7.1e-09Significant hit ( 2.2e-40) to 8/9 blocks of the PR00691 family, which is described as \"Adhesin B signature\". Prints database entry for PR:PR00691. PR00691A 23-44 3.5e-06 PR00691B 48-66 0.007 PR00691C 67-86 0.00073 PR00691D 120-139 0.00012 PR00691E 178-195 4.7e-05 PR00691F 204-222 1.6e-06 PR00691G 227-244 17 PR00691H 249-267 30","Residues 23 to 97 match (2e-07) PD:PD527904 which is described as PROTEOME COMPLETE SAV2406 ","","","","","","","","","","","","Tue Jan 21 11:07:35 2003","Thu Aug 4 11:19:57 2005","Thu Aug 4 11:17:46 2005","Thu Aug 4 11:19:57 2005","Thu Aug 4 11:17:46 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA02549 is paralogously related to AA02935 (2e-14).","Thu Aug 4 11:17:46 2005","","","","","Residues 1 to 292 (E-value = 2e-148) place AA02549 in the SBP_bac_9 family which is described as Periplasmic solute binding protein family (PF01297)","Thu Aug 4 11:17:46 2005","",""," Haraszthy VI, Jordan SF, Zambon JJ.,Identification of Fur-regulated genes in Actinobacillus actinomycetemcomitans.Microbiology. 2006 Mar;152(Pt 3):787-96.PMID: 16514158Rhodes ER, Tomaras AP, McGillivary G, Connerly PL, Actis LA.Genetic and functional analyses of the Actinobacillus actinomycetemcomitans AfeABCD siderophore-independent iron acquisition system.Infect Immun. 2005 Jun;73(6):3758-63.PMID: 15908408","","Thu Aug 4 11:19:57 2005","","1","","","" "AA02550","1776891","1777778","888","ATGTCATCAAATATTGCCTCTATTTGCGTTGAAGACGTAGTCGTTCGTTACAACAATGGTCATACCGCCATTCATGATGTTTCTTTTAAACTAGAAGGCGGTACGACCTGCGCTTTAGTCGGCGTGAACGGGAGCGGTAAGTCAACCCTGTTTAAAAGTCTGATGGGGTTAATTACACCGCAACGAGGTAATATTTCTCTTTGCAATCTCACAATTAAACAAGCCTTAAAACAAAATTTAGTGTCTTATGTGCCACAATCGGAAGACGTGGACTGGCAATTTCCGGTCTCTGTTTACGATGTGGTGCTGATGGGGCGCTATGGTTACATGAACTTCCTGCGCCGTCCGAGTGAAACGGACAAACAAAAGGTGCAGGAAGCCATGCAACGGGTGAACATTGAACACCTTGCCCATCGCCAAATCGGCGAGCTTTCCGGTGGGCAAAAAAAACGGGCATTTCTTGCTCGCGCGCTCGCACAACAAAGTAAGATTATTTTATTGGACGAACCTTTCACCGGCGTAGATGTACAAACGGAAAACGCCATTATTGATTTATTAGGTCAGTTACGCAGTGAAGGGCATTTAATTCTGGTTTCCACGCACAATTTAGGTTCCGTGCCGGATTTTTGTGATCGCGTGGTAATGATTAACCGCACGGTAATCGCTGCAGGTTTGACCGAAACTACTTTTAACCAGCATAACTTGGAATTGGTTTTTGGCGGTGTGTTGCGCCACATTAAGCTATTAGGCGAAGACTTGCATGATGACGAGGACCCACGCGCCGTTACGGTATTAACCGATGATGAGCGGGCAGCGGTATTCTATGGTAAAACTAAAATTGATCCACCGGCACCTACTGTCAGATATACCAAACCGAAGGAAGACGCA","","","32743","MSSNIASICVEDVVVRYNNGHTAIHDVSFKLEGGTTCALVGVNGSGKSTLFKSLMGLITPQRGNISLCNLTIKQALKQNLVSYVPQSEDVDWQFPVSVYDVVLMGRYGYMNFLRRPSETDKQKVQEAMQRVNIEHLAHRQIGELSGGQKKRAFLARALAQQSKIILLDEPFTGVDVQTENAIIDLLGQLRSEGHLILVSTHNLGSVPDFCDRVVMINRTVIAAGLTETTFNQHNLELVFGGVLRHIKLLGEDLHDDEDPRAVTVLTDDERAAVFYGKTKIDPPAPTVRYTKPKEDA","1777776","From PF00005:ABC transporterABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family ofproteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain ABC_membrane.","iron (chelated) ABC transporter, ATP-binding protein","Cytoplasm, Inner membrane","This sequence corresponds to AY762615 in GenBank.","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[143-186]TY361_HAEIN_P44662;
PF00005\"[34-219]TABC_tran
PS50893\"[8-243]TABC_TRANSPORTER_2
PS00211\"[144-158]?ABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[33-249]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[8-246]Tno description
PTHR19222\"[8-240]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF31\"[8-240]TMETAL ABC TRANSPORTER


","No hits to the COGs database.","Significant hit ( 3.1e-30) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 23-69 2.3e-16 IPB001140B 141-179 4.2e-11 IPB001140C 195-224 11","Residues 24 to 222 match (1e-07) PD:PD055535 which is described as ATP-BINDING ABC PROTEOME COMPLETE TRANSPORTER ","","","","","","","","","","","Tue Jan 21 11:17:42 2003","Tue Jan 21 11:14:52 2003","Thu Aug 4 11:19:18 2005","Thu Aug 4 11:19:18 2005","Thu Aug 4 11:19:18 2005","Thu Aug 4 11:19:18 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA02550 is paralogously related to AA02152 (6e-30), AA00799 (2e-27), AA01824 (9e-26), AA02320 (1e-23), AA01820 (4e-23), AA01616 (1e-19), AA01524 (2e-19), AA02899 (2e-19), AA01051 (3e-19), AA02140 (5e-19), AA02440 (1e-18), AA00415 (2e-18), AA02898 (4e-18), AA00858 (7e-18), AA00207 (7e-18), AA00700 (6e-17), AA01509 (3e-16), AA01510 (5e-16), AA01684 (6e-16), AA01779 (8e-16), AA01867 (1e-15), AA01456 (1e-15), AA02609 (2e-15), AA02718 (3e-15), AA02484 (5e-15), AA02080 (7e-15), AA01757 (7e-15), AA01568 (2e-14), AA02324 (3e-14), AA01645 (3e-14), AA01961 (4e-14), AA01422 (6e-14), AA00751 (4e-13), AA01656 (5e-13), AA02786 (2e-12), AA01569 (2e-12), AA02353 (3e-12), AA00933 (3e-12), AA02606 (4e-12), AA02331 (4e-12), AA02805 (7e-12), AA01393 (9e-12), AA02146 (2e-11), AA02225 (6e-11), AA02573 (8e-11), AA02642 (2e-10), AA01947 (2e-10), A02145 (3e-09), AA01555 (6e-09), AA00591 (7e-09), AA00934 (1e-08), AA00061 (7e-07) and AA01291 (2e-05).","Thu Aug 4 11:19:18 2005","","","","","Residues 34 to 219 (E-value = 3.3e-47) place AA02550 in the ABC_tran family which is described as ABC transporter (PF00005)","Thu Aug 4 11:19:18 2005","",""," Haraszthy VI, Jordan SF, Zambon JJ.,Identification of Fur-regulated genes in Actinobacillus actinomycetemcomitans.Microbiology. 2006 Mar;152(Pt 3):787-96.PMID: 16514158Wang Y, Liu A, Chen C.Genetic basis for conversion of rough-to-smooth colony morphology in Actinobacillus actinomycetemcomitans.Infect Immun. 2005 Jun;73(6):3749-53.PMID: 15908406","Bearden SW, Staggs TM, Perry RD. An ABC transporter system of Yersinia pestis allows utilization of chelated iron by Escherichia coli SAB11. J Bacteriol 1998 Mar;180(5):1135-47. PubMed: 9495751","Thu Aug 4 11:19:18 2005","Tue Jan 21 11:14:52 2003","1","","","" "AA02551","1777781","1778635","855","ATGTGGGACCTGTTATTAGAACCCTTTTCCTACGATTACATGGTGAAAGCCATTTTAATCAGCTCGGCGGTGGGTGGCATTTGTGCGTTTTTATCCGCTTATTTAATGCTGAAAGGTTGGTCACTGATTGGTGATGCCCTTTCTCATTCCGTCGTACCCGGCGTTGCCATTGCTTATGCCCTCTCCCTGCCCTACGCGCTTGGTGCATTTTTTTCCGGTATCCTCGCCGCCATCGCCATTCTTTGGATAAAATCCATTACCAAACTCCGTGAAGACGCAGTCATCGGCTTTATTTTTACCACTTTCTTTGCCCTTGGCCTACTGATTATTTCCCTTAACCCGACGTCGATTAACGTACAAGACATTATCTTAGGCAACATTCTGGGCATTGCCGATGAAGATATTCTGCAAGTCGGCATTATCATCGGCGTTTGTTTAGTATTACTGCTGATCTTTTGGAAAGATCTTTTGCTGATTTTCTTTGATGAAGTGCACGCCACTTCCGTCGGCTTTTCACCGATTTACTACAAAATCCTGTTTTTCACCTTGCTCAGCGCCTGCGTGGTTGCCGCGTTACAAACCGTCGGTGCCATTTTGGTTATCGCCATGGTTATCACACCGGGCGCAACCGCTTACCTGCTCACCGATCGTTTTAAAACTTTGGTCCTTATTGCCGTAGTTTTAGGCATTTCTTCCAGTTCCGTAGGCGTTTATATAAGCTATTTCTTAGACGGTGCAACAGGTGGTGTTATTGTTTGTATTCAGACCGCTCTTTTCTTGCTGGCATTCATTTTTTCACCGAAGTACGGTTTGCTCCATCAACATAAACCCATCGCACAAGAAGAGGTGCAAAAA","","","30694","MWDLLLEPFSYDYMVKAILISSAVGGICAFLSAYLMLKGWSLIGDALSHSVVPGVAIAYALSLPYALGAFFSGILAAIAILWIKSITKLREDAVIGFIFTTFFALGLLIISLNPTSINVQDIILGNILGIADEDILQVGIIIGVCLVLLLIFWKDLLLIFFDEVHATSVGFSPIYYKILFFTLLSACVVAALQTVGAILVIAMVITPGATAYLLTDRFKTLVLIAVVLGISSSSVGVYISYFLDGATGGVIVCIQTALFLLAFIFSPKYGLLHQHKPIAQEEVQK","1778633","","iron (chelated) ABC transporter, permease protein","Inner membrane, Cytoplasm","This sequence corresponds to AY762615 in GenBank.","
InterPro
IPR001626
Family
ABC-3
PF00950\"[10-266]TABC-3
noIPR
unintegrated
unintegrated
SSF81345\"[1-260]TSSF81345


","BeTs to 19 clades of COG1108COG name: ABC-type Mn2+/Zn2+ transport systems, permease componentsFunctional Class: PThe phylogenetic pattern of COG1108 is aom-kz-qvdrlbcefgh-nujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 7e-92) to 5/5 blocks of the IPB001626 family, which is described as \"ABC 3 transport family\". Interpro entry for IP:IPR001626. IPB001626A 24-70 5e-27 IPB001626B 77-111 4e-15 IPB001626C 118-135 0.00036 IPB001626D 185-230 1.3e-26 IPB001626E 231-263 9.2e-14","Residues 166 to 272 match (4e-25) PD:PD002769 which is described as COMPLETE PROTEOME MEMBRANE ABC SYSTEM TRANSMEMBRANE IRON ZINC TRANSPORTER MANGANESE ","","","","","","","","","","","","Tue Jan 21 11:20:26 2003","Thu Aug 4 11:20:56 2005","Thu Aug 4 11:20:56 2005","Thu Aug 4 11:20:56 2005","Thu Aug 4 11:20:56 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA02551 is paralogously related to AA02552 (2e-60), AA01818 (4e-23) and AA02153 (9e-07).","Thu Aug 4 11:20:56 2005","","","","","Residues 10 to 266 (E-value = 3e-125) place AA02551 in the ABC-3 family which is described as ABC 3 transport family (PF00950)","Thu Aug 4 11:20:56 2005","",""," Haraszthy VI, Jordan SF, Zambon JJ.,Identification of Fur-regulated genes in Actinobacillus actinomycetemcomitans.Microbiology. 2006 Mar;152(Pt 3):787-96.PMID: 16514158Wang Y, Liu A, Chen C.Genetic basis for conversion of rough-to-smooth colony morphology in Actinobacillus actinomycetemcomitans.Infect Immun. 2005 Jun;73(6):3749-53.PMID: 15908406","Bearden,S.W., Staggs,T.M. and Perry,R.D. An ABC transporter system of Yersinia pestis allows utilization of chelated iron by Escherichia coli SAB11 J. Bacteriol. 180 (5), 1135-1147 (1998) PubMed: 9495751 ","Thu Aug 4 11:20:56 2005","Tue Jan 21 11:20:26 2003","1","","","" "AA02552","1778635","1779480","846","ATGAACGCCATTTATCTTTGGATTACCGAACCTTTCAGCTACCCTTTCATGCAAAACGCGTTAATTACCGCGCTGTTGGTGTCCGTTATTTGTGCTATGCTGTCCTGCTATTTAGTGTTAAAAGGCTGGTCGTTAATGGGCGATGCCATTTCACACGCCGTGTTACCGGGAATTGTGGTCGCATTCTGGTTGGGATTACCGTTAAGTATCGGCGCTTTTATCGCGGGCTTGGTTTGTTCTATTAGTGTGGGCTATTTAAAAGAAAACAGCCGAATTAAAGAAGATACTGCAATGGGTATTGTATTTTCAGGGATGTTTGCCTTAGGGATTGTACTGTTTACCAAAATTGAAACAGAACAACATTTAACCCATATTTTATTCGGTAATTTACTTGGTGTCAGTGATGCCGAGGTTTGGCAAACCTTCTTTATGACTGCGCTGATTTTTCTTGTCATCTTTCTCCGTCGAAAAGATTTCCTACTTTATTGTTTCGATCCCAACCAAACCAAAATTGTTGGTTTATCGCCGCGTCTGCTACATTACAGCTTATTGATTTTACTTGCCTTAACCATCATTAGCGCCATGCAGGTGGTGGGGGTTATTTTAGTAGTCGCCATGCTCATTTCACCGGGTATTACCGCCTTTATTTTAACCAAGCGATTTGATTATATGATCGCCATTGCCCTAATAACTTCAGTCAGCACGAGCATTTTAGGCACGATCATCAGCTATTATATCGACGGCGCAACCGGTCCTTGCATTATCTTGCTACAAGCGACCGCATTTTTGACCGCACTTATTTACAGAAAAATCCGCCTGCGCTTTAATGCAACACTTGAAACGTCG","","","31040","MNAIYLWITEPFSYPFMQNALITALLVSVICAMLSCYLVLKGWSLMGDAISHAVLPGIVVAFWLGLPLSIGAFIAGLVCSISVGYLKENSRIKEDTAMGIVFSGMFALGIVLFTKIETEQHLTHILFGNLLGVSDAEVWQTFFMTALIFLVIFLRRKDFLLYCFDPNQTKIVGLSPRLLHYSLLILLALTIISAMQVVGVILVVAMLISPGITAFILTKRFDYMIAIALITSVSTSILGTIISYYIDGATGPCIILLQATAFLTALIYRKIRLRFNATLETS","1779478","From InterPro: IPR001626ABC transporter, family 3ATP-binding cassette (ABC) transporters are multidomain membrane proteins, responsible for the controlled efflux and influx of substances (allocrites) across cellular membranes. They are minimally composed of four domains, with two transmembrane domains (TMDs) responsible for allocrite binding and transport and two nucleotide-binding domains (NBDs) responsible for coupling the energy of ATP hydrolysis to conformational changes in the TMDs. Both NBDs are capable of ATP hydrolysis, and inhibition of hydrolysis at one NBD effectively abrogates hydrolysis at the other. Hydrolysis at the two NBDs may occur in an alternative fashion although they appear substantially functionally symmetrical in terms of their binding to diverse nucleotides.A number of bacterial transport systems have been found to contain integral membrane components that have similar sequences: these systems fit the characteristics of ATP-binding cassette transporters. The proteins form homo- or hetero-oligomeric channels, allowing ATP-mediated transport. Hydropathy analysis of the proteins has revealed the presence of 6 possible transmembrane regions. These proteins belong to family 3 of ABC transporters. ","iron (chelated) ABC transporter, permease protein","Inner membrane, Cytoplasm","This sequence corresponds to AY762615 in GenBank.","
InterPro
IPR001626
Family
ABC-3
PF00950\"[13-269]TABC-3
noIPR
unintegrated
unintegrated
signalp\"[1-32]?signal-peptide
tmhmm\"[20-40]?\"[59-81]?\"[96-114]?\"[133-153]?\"[174-194]?\"[200-218]?\"[223-242]?\"[248-268]?transmembrane_regions


","BeTs to 19 clades of COG1108COG name: ABC-type Mn2+/Zn2+ transport systems, permease componentsFunctional Class: PThe phylogenetic pattern of COG1108 is aom-kz-qvdrlbcefgh-nujxit-Number of proteins in this genome belonging to this COG is","Significant hit (6.9e-101) to 5/5 blocks of the IPB001626 family, which is described as \"ABC 3 transport family\". Interpro entry for IP:IPR001626. IPB001626A 27-73 1.3e-31 IPB001626B 80-114 2.4e-19 IPB001626C 121-138 1.6e-06 IPB001626D 188-233 1.8e-24 IPB001626E 234-266 6.9e-14","Residues 118 to 166 match (1e-09) PD:PD580935 which is described as PROTEOME COMPLETE MEMBRANE ABC IRON TRANSMEMBRANE SYSTEM PERMEASE TRANSPORTER INNER ","","","","","","","","","","","Wed Mar 17 09:24:38 2004","Tue Jan 21 11:33:35 2003","Thu Aug 4 11:21:43 2005","Thu Aug 4 11:21:43 2005","Thu Aug 4 11:21:43 2005","Wed Mar 17 09:24:38 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02552 is paralogously related to AA02551 (2e-60), AA01818 (4e-24) and AA02153 (5e-07).","Wed Mar 17 09:24:38 2004","","","","","Residues 13 to 269 (E-value = 5.5e-136) place AA02552 in the ABC-3 family which is described as ABC 3 transport family (PF00950)","Wed Mar 17 09:24:38 2004","",""," Haraszthy VI, Jordan SF, Zambon JJ.,Identification of Fur-regulated genes in Actinobacillus actinomycetemcomitans.Microbiology. 2006 Mar;152(Pt 3):787-96.PMID: 16514158Wang Y, Liu A, Chen C.Genetic basis for conversion of rough-to-smooth colony morphology in Actinobacillus actinomycetemcomitans.Infect Immun. 2005 Jun;73(6):3749-53.PMID: 15908406","Schmitt L, Tamp R.Structure and mechanism of ABC transporters.Curr Opin Struct Biol. 2002 Dec;12(6):754-60.PMID: 12504680Bearden SW, Staggs TM, Perry RD.An ABC transporter system of Yersinia pestis allows utilization of chelated iron by Escherichia coli SAB11.J Bacteriol. 1998 Mar;180(5):1135-47.PMID: 9495751","Thu Aug 4 11:21:43 2005","Thu Aug 4 11:21:43 2005","1","","","" "AA02553","1779730","1779461","270","ATGCTGAAAAAACGTTTTTTGGTTTATGGTTGCGTGCAGGGTGTCGGCTTCCGTTATTTCACTTGGCAACAGGCAACAAAAATCGGCGTGACGGGCTTTGTACGCAACCTTGCTGATGGCTCCGTGGAAGTGGTAGCCATCGGTTCTGAGGTGCAAATTCAGGCGTTAAGTGACTGGCTGCACCATGGTCCGCGCACGGCGACGGTGCAACAGGTTTTTGCGGAAGATTATCTCAGCAGTAAAGTATTTACGACGTTTCAAGTGTTGCAT","","","10092","MLKKRFLVYGCVQGVGFRYFTWQQATKIGVTGFVRNLADGSVEVVAIGSEVQIQALSDWLHHGPRTATVQQVFAEDYLSSKVFTTFQVLH","1779459","","acylphosphatase","Cytoplasm","","
InterPro
IPR001792
Domain
Acylphosphatase
PD001884\"[5-88]TQ9CNN1_PASMU_Q9CNN1;
PR00112\"[3-18]T\"[24-49]TACYLPHPHTASE
PF00708\"[8-60]TAcylphosphatase
PS51160\"[3-90]TACYLPHOSPHATASE_3
PS00150\"[8-18]TACYLPHOSPHATASE_1
PS00151\"[32-48]TACYLPHOSPHATASE_2
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.100\"[1-90]Tno description
PTHR10029\"[5-90]TACYLPHOSPHATASE


","No hits to the COGs database.","Significant hit ( 8.2e-21) to 1/2 blocks of the IPB001792 family, which is described as \"Acylphosphatase\". Interpro entry for IP:IPR001792. IPB001792A 4-41 7.5e-21","Residues 5 to 88 match (4e-21) PD:PD001884 which is described as PROTEOME COMPLETE HYDROLASE PHOSPHOHYDROLASE ACYLPHOSPHATE ACYLPHOSPHATASE ACYLPHOSPHATASE ISOZYME TYPE FAMILY ","","","","","","","","","","","","Tue Jan 21 11:39:25 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02553 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 85 (E-value = 2.5e-07) place AA02553 in the Acylphosphatase family which is described as Acylphosphatase (PF00708)","","","","","Rosano C, Zuccotti S, Stefani M, Bucciantini M, Ramponi G, Bolognesi M.Crystallization and preliminary X-ray characterization of the acylphosphatase-like domain from the Escherichia coli hydrogenase maturation factor HypF.Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):524-5.PMID: 11856843","","Tue Jan 21 11:43:49 2003","1","","","" "AA02554","1779875","1780546","672","ATGAAATTTCGTTTAGCTGCATTAGCTGCAACACTTTTAGCCAGTACCGCCAGCTTTGCAGGTATGATCACCAGTTCATCCAACATCGACTTCCTCGCCTTTGACGGTCAAAAACCGTCAAAATCCTTATTGAAGGAAGCCCGCAGTTTCAATATTAATGACACCCAAAAGCACCAAGTGGTAGTGCGCGTATCCGAGATTATAAAAACCAGTTCCGACAGCGCCTTACTTGAAACCGATCCAATTGTCGTTACCTTCCAAGGTTCAACACAAGACATCATCATTTCCGCCCCGAAATTATCTAACGAGCGTGATTTCAATGCCTTTAAAAAGGCCCCGGTGATCAGCGTAAAAACCGCTTCCGGCGCGAACATACAAACCCAACAAGAATACTTAAAACAGGAAGGTTTCTTCCCAACCGTTAGCCTGATTAAAGACTTAGGCGAATACAACGCTTCCGGTGCAGCCGCCGCCGTGCCTGCCTTTGCAACCGCTTCAACTGCCACGCCGACCACTACCGTGGTAGCCGGTGGTGCGGCCACAGGTAAAGTAGAAAAAGGCAAAGTCACCTTACAAGGCGAGAATGTTGCCGAGCAAATGCTCCAATACTGGTATCAACAAGCCGACAAAGAAACGCAAACCCGTTTCATTAATTGGGTGAAAAAACAAAAA","","","35674","MKFRLAALAATLLASTASFAGMITSSSNIDFLAFDGQKPSKSLLKEARSFNINDTQKHQVVVRVSEIIKTSSDSALLETDPIVVTFQGSTQDIIISAPKLSNERDFNAFKKAPVISVKTASGANIQTQQEYLKQEGFFPTVSLIKDLGEYNASGAAAAVPAFATASTATPTTTVVAGGAATGKVEKGKVTLQGENVAEQMLQYWYQQADKETQTRFINWVKKQK","1780544","","conserved hypothetical protein","Periplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-20]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","BeTs to 3 clades of COG3110COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3110 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 20 to 223 match (1e-62) PD:PD037725 which is described as COMPLETE PROTEOME SIGNAL PRECURSOR YCCT EXPORTED PM0395 PERIPLASMIC VCA0026 HI1681 ","","","","","","","","","","","","Tue Jan 21 11:35:46 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02554 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02556","1780612","1781067","456","ATGCAAACCACTTATCGTGCGCTACCTAAAAATAAACATATCACGTTAGTGGCACATGATCACTGTAAACAGGACCTCATAAACTGGTGTAAAAACCACCGCACTTTATTGGCAAATCACACCCTGTACGGCACGGGTACGACCGGCAATCTGATTCATCGGGAAACGGGCTTAACGGTAAACAACCTATTGAGCGGTCCGATGGGCGGCGATCAGCAACTAGGCGGATTGATCGCCGAAAACAAAATTGATTTAATGATTTTCTTTTGGGATCCGATGAATGCCGTGCCCCATGATCCGGACGTCAAAGCCTTAATGCGTATCGCAACGGTGTGGAATATTCCGGTAGCCATGAATATCGCCAGTGCAGACTTTTTAGTCACTTCTCCGTTATTTAATGAAACTGCCGACATTCGCATTCCAGATTACCAAGGCTATTTAACCGAGCGACTGAAA","","","17049","MQTTYRALPKNKHITLVAHDHCKQDLINWCKNHRTLLANHTLYGTGTTGNLIHRETGLTVNNLLSGPMGGDQQLGGLIAENKIDLMIFFWDPMNAVPHDPDVKALMRIATVWNIPVAMNIASADFLVTSPLFNETADIRIPDYQGYLTERLK","1781065","From PF02142: MGS-like domainMethylglyoxal synthase catalyzes the conversion of dihydroxyacetone phosphate to methylglyoxal and phosphate. It provides bacteria with an alternative to triosephosphate isomerase for metabolizing dihydroxyacetone phosphate.Methylglyoxal synthase contains a domain shared by other enzymes.Other proteins containing this domain include purine biosynthesis protein PurH and carbamoyl phosphate synthetase. ","methylglyoxal synthase","Cytoplasm","","
InterPro
IPR004363
Family
Methylglyoxal synthase
PD010761\"[12-150]TMGSA_PASMU_Q9CNN3;
PIRSF006614\"[12-150]TMethylglyoxal synthase
TIGR00160\"[10-152]TMGSA: methylglyoxal synthase
PS01335\"[65-73]TMETHYLGLYOXAL_SYNTH
InterPro
IPR011607
Domain
MGS-like
PF02142\"[25-118]TMGS
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1380\"[1-152]Tno description


","BeTs to 7 clades of COG1803COG name: Methylglyoxal synthaseFunctional Class: GThe phylogenetic pattern of COG1803 is --------v---bce-gh------t-Number of proteins in this genome belonging to this COG is","Significant hit ( 2e-36) to 2/2 blocks of the IPB000384 family, which is described as \"Methylglyoxal synthase active site\". Interpro entry for IP:IPR000384. IPB000384A 13-55 7.9e-17 IPB000384B 88-122 2.6e-18","Residues 1 to 152 match (1e-67) PD:PD010761 which is described as SYNTHASE METHYLGLYOXAL PROTEOME COMPLETE MGS LYASE SLL0036 3D-STRUCTURE ","","","","","","","","","","","Tue Jan 21 12:10:32 2003","Tue Jan 21 11:49:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02556 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 15 to 118 (E-value = 2.5e-25) place AA02556 in the MGS family which is described as MGS-like domain (PF02142)","","","","","","","","1","","","" "AA02558","1781070","1781540","471","ATGAACGGAAATAACGCAACACTTGCACTCGTTTTAAATATTCTGAATTTTGTCCTGGGTGGCTTCGCCGTCACCTTGGCATGGCTTTTGGCCACCGTGATGAGCGCCGTTTTGATCGTCACCTTGCCATACACCCGCAGCTGTTGGGAAATCACCAAAATGACATTCGTGCCTTTCGGCAATGACATTATTCATGTTAAGTATTTAGAACCGAAAAGTGCGGTGGAAAATTCCATCGGATCCGTACTTAACATTGTCTGGTTCATTTTGTTCGGCTGGTGGCTTTGTCTCAGCAATGTGTTTTGCGGTATCTCTCAATGTCTGACCATCATCGGTATTCCGACCGGCTTGGCGCATTTCAAAATCGCCGCCATCGCATTATATCCGGTGGGACAACGCGTGTTGCCGAAAGACACTGCCGACTTAATCCGCCAACAATTCACCGAACAACAATACAAGCAGTTTTATAAA","","","17529","MNGNNATLALVLNILNFVLGGFAVTLAWLLATVMSAVLIVTLPYTRSCWEITKMTFVPFGNDIIHVKYLEPKSAVENSIGSVLNIVWFILFGWWLCLSNVFCGISQCLTIIGIPTGLAHFKIAAIALYPVGQRVLPKDTADLIRQQFTEQQYKQFYK","1781538","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR005185
Family
Protein of unknown function DUF307
PIRSF028777\"[8-143]TUncharacterised conserved protein
PF03733\"[10-66]T\"[81-137]TDUF307
noIPR
unintegrated
unintegrated
signalp\"[1-35]?signal-peptide
tmhmm\"[10-44]?\"[77-97]?transmembrane_regions


","No hits to the COGs database.","","Residues 84 to 134 match (7e-15) PD:PD021079 which is described as COMPLETE PROTEOME MEMBRANE RV0870C CC2111 VCA1051 PM0393 INTEGRAL CPE0688 INNER ","","","","","","","","","","","","Tue Jan 21 12:15:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02558 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 81 to 137 (E-value = 4.3e-24) place AA02558 in the DUF307 family which is described as Domain of unknown function (DUF307) (PF03733)","","","","","","","","1","","","" "AA02560","1781552","1783690","2139","ATGAATCGCTGGTTTAACGCCAAAGTTATTGCGTCCATTCCGATTTTTATCGCCGTAAATCTCGCGGTGCTGGCAATTTGGTATTTTAATATTTCCGAACAAAGCATGCCTTTGGTGCTGGGCATTATTGCCGGCGGATTAGTGGATTTGGATAACCGGTTAACCGGCCGTATTAAAAACGTATTTTACACCCTGCTCGCTTTCTCCGTTTCAACCCTAAGCGTGCAACTGAGCATTGGGCATAACCTGCAATTTATGCTGTTAATGACGCTCATGACCTTTGCCTTCACCATGATCGGCGCTTTGGGGCAGCGTTACAGCACCATCGCTTTCGGCACCTTAGTAGTAGCGTTATACACCACGCTGGCCTATTTGCCCGATACCCTTTGGTACATCAATCCGCTGATGATCCTCTGCGGTACGCTGCTTTATAGCGTCACTACCCTATGCGTGCATTTATTTTTCCCTAATCGCCCGGTGCAGGAAAGCGTTGCCAAATCCTTTTTGGCATTAGCCAATTATCTGGATGCCAAATCCATGTTTTTCGATCCTGATGAAATCGATCAAATCGAAAATAAACACATTGCCATGGCGATGAAAAACAGCGAACTCATCAATGCCTTCAACGGCTCCCGCACCGCACTTTTTTACCGTATTCGCGGGCAACATCGCCACAGCCACACCACCCAAATGATTCGTTATTATTTTACCGCACAGGACATTCACGAGCGCATCAGTTCCAGCCATTTTAACTATCAAAAATTAGCGGAACATTTAAAAAACACCGATTTAATTTTCCGCATTCAACGTTTATTGGAACTGCAAGCCCAAGCCTGTCGCGACATTGCTTTAAGTTTACAGCGCAATAAAACCTATCACTACGACACTCGGGTAGAAAAAGCCATTCACGGTTTAAACCAATCCTTTGAGTTTTACAGCGCCGCTCATGGGGAAGAAAGCGAAACTCTGCTCAATCTGCAAACCTTACTGGATAACCTGAAAAGCGTGGATTATCAGCTACGCCACATTGATCAGGAAGCGGACAATACGGAACAAACTGAACGGGCACAAATTTACACAGAGCAAATCACCGGGTTAAAAAATATCCTATTGGCAATTCGTAGCCATTGTAGCTTTGAATCCCAACTCTTCCGCCATGCGGTGCGTCTGTCTATTGTAGTGTTTGTTTGTTGTGTAATCGGCGAATTTTTACCGTTAGATCGTGGTTATTGGGTTTTGCTTACTGCCGTGTTCGTCTGCCAGCCGAACTACACCGCCACCAAATTACGTCTCAAACAACGAATTATCGGCACCATTCTCGGTGTGGTTATCGGTTCATTATTGCCATACACCAACCCGACACTGGAATTGCAACTGGGCTTAATTGTGCTGACCAGCACCCTGTTCTTCTTTTTCCGCACCAATAATTACAGTTTCTCCACCTTTTTTATTACTTTACAAGTGATTTTCAGTTTTGATGTCATGGGGTTTGATGTGGAACAGGCGCTTTATTCGCGGGTCATTGATACCCTTATCGGCGCTACGATCTCTTGGTTTGCGGTGTCTTATTTTTGGCCGGACTGGAAATATTTACAACTGGATAAAGTAAGCCGACAGGCAGTAAAAAGCGATGCGCAATATTTGCTTTATGTGGTCAGCCAACTGCAATTCGGCAAAGGGGATAATCTGAAATACCGTATCGTGCGTCGTTACGCCCACGAATATGCGGCGGCGCTAAGTGCCACCATTTCCAATATGAATCATGAACCGAAGAAATATCAGGCGTATTTGCAAACAGGATTCGAGCTGCTAAAAATCAATTATTCTCTGCTCAGTTATATTTCGGCGCTCGGCGCGTATCGCAGTAAAATGAAAAAAATACAGCAAAGCACGGCATTTTTAGCGGAATTTTATCCGGCGGCGAAAAAGATTATTTATATTTTGGAACACCTGGAAAAACTGCCACCGGATATTTTTGAAAAGCTGCACGAGAACATTGAATTACGTTTAAAACAGGTGCAAGTCAATCTAAATACTAACGCCCAACCGGAACAGGTACAATTTAACATTCCGATTCAGCAGTTAAGCATGATCAGCCAAATTCTGCCGTCCCTTTACGGTGCATTTCAGAAAACCGTC","","","81913","MNRWFNAKVIASIPIFIAVNLAVLAIWYFNISEQSMPLVLGIIAGGLVDLDNRLTGRIKNVFYTLLAFSVSTLSVQLSIGHNLQFMLLMTLMTFAFTMIGALGQRYSTIAFGTLVVALYTTLAYLPDTLWYINPLMILCGTLLYSVTTLCVHLFFPNRPVQESVAKSFLALANYLDAKSMFFDPDEIDQIENKHIAMAMKNSELINAFNGSRTALFYRIRGQHRHSHTTQMIRYYFTAQDIHERISSSHFNYQKLAEHLKNTDLIFRIQRLLELQAQACRDIALSLQRNKTYHYDTRVEKAIHGLNQSFEFYSAAHGEESETLLNLQTLLDNLKSVDYQLRHIDQEADNTEQTERAQIYTEQITGLKNILLAIRSHCSFESQLFRHAVRLSIVVFVCCVIGEFLPLDRGYWVLLTAVFVCQPNYTATKLRLKQRIIGTILGVVIGSLLPYTNPTLELQLGLIVLTSTLFFFFRTNNYSFSTFFITLQVIFSFDVMGFDVEQALYSRVIDTLIGATISWFAVSYFWPDWKYLQLDKVSRQAVKSDAQYLLYVVSQLQFGKGDNLKYRIVRRYAHEYAAALSATISNMNHEPKKYQAYLQTGFELLKINYSLLSYISALGAYRSKMKKIQQSTAFLAEFYPAAKKIIYILEHLEKLPPDIFEKLHENIELRLKQVQVNLNTNAQPEQVQFNIPIQQLSMISQILPSLYGAFQKTV","1783688","","integral membrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR010019
Family
Intergral membrane protein, YccS
PIRSF004840\"[1-713]TPredicted transmembrane protein, slr1298 type
TIGR01666\"[2-712]TYCCS: hypothetical membrane protein, TIGR01
InterPro
IPR010020
Family
Integral membrane protein, YccS/YhfK
TIGR01667\"[2-712]TYCCS_YHJK: integral membrane protein, YccS/
InterPro
IPR010289
Family
Protein of unknown function DUF893, YccS/YhfK
PF05976\"[1-711]TDUF893
InterPro
IPR013253
Family
Kinetochore Spc7
SM00787\"[156-468]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-25]?signal-peptide
tmhmm\"[10-30]?\"[36-56]?\"[61-79]?\"[85-103]?\"[108-126]?\"[136-156]?\"[437-471]?\"[477-497]?\"[507-525]?transmembrane_regions


","No hits to the COGs database.","","Residues 294 to 362 match (1e-07) PD:PD492331 which is described as PROTEOME COMPLETE TRANSMEMBRANE PM0392 HI1680 ","","","","","","","","","","","","Tue Jan 21 15:59:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02560 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02561","1784196","1783693","504","ATGTTAGATGATGAAGCGATTTCGCTGTTCCGTGCCGAAATCAAAGGTGTGAAGCCGTTAAAGCAGGACAGATTCGTGCCGCCGCGCGCCACGAAGAAGAAAAATCAGATAGCGGTCAAAGAGGTGCGCGAGCAGCGGGACACGTTATTTTATTTTTCTGACGAATATGAACCGTTGTTGAACGACGAAAGTGCGGTCAAATATTTACGTGAAAATGAGGATTCCCATTTGCTGAAACAATTGCGGCGCGGGGATTTTTCGCCGGAAATTTTTTTGGATTTGCACGGCTTAACCCGCGAGCAAGCAAAGCTGGAATTGGCGGCACTGATTCAAGCCTGTGAGAAAGAACATATTTATTGCGCAAGTATTATGACCGGTTACGGCACTTACACCTTAAAACGTCAAATTCCCCGTTGGTTGGTGCAACACCCTAAAGTGCGCGCCTTACACCAAGCCCCGAAAGAATGGGGCGGTGATGCGGCAATCTTGATTTTAATCGACGTT","","","19473","MLDDEAISLFRAEIKGVKPLKQDRFVPPRATKKKNQIAVKEVREQRDTLFYFSDEYEPLLNDESAVKYLRENEDSHLLKQLRRGDFSPEIFLDLHGLTREQAKLELAALIQACEKEHIYCASIMTGYGTYTLKRQIPRWLVQHPKVRALHQAPKEWGGDAAILILIDV","1783691","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR002625
Domain
Smr protein/MutS2 C-terminal
PF01713\"[92-167]TSmr
SM00463\"[89-167]TSMR
PS50828\"[92-167]TSMR


","No hits to the COGs database.","Significant hit ( 4.4e-05) to 2/2 blocks of the IPB002625 family, which is described as \"Smr domain\". Interpro entry for IP:IPR002625. IPB002625A 93-106 0.0025 IPB002625B 123-130 11","","","","","","","","","","","","","Wed Jan 22 07:46:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02561 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 92 to 167 (E-value = 8.3e-28) place AA02561 in the Smr family which is described as Smr domain (PF01713)","","","","","","","","1","","","" "AA02562","1784259","1785206","948","ATGAACCAAATTACCTTTAATCAGGAATTGATCGACGATATTTATTCCGCCAACGTACATGACGAACTGCACAGTATCAAAGATTTTCTGCGCTGGACCTACAGCACCTTTAATCGCGCCGAATTATTTTACGGGCATGGCTATGACAATGCCTGGGACGAAGCGCACCAGCTGGTGCTTTCCTGCCTTCACCTGCCGCCCGATTTTCCCGCCGAATTATACAATGCCCGCTTAACCGTCGCAGAAAAATTGGAACTCATCCGTTTAGTGATGATTCGTCTTGAAAAACGCCTTCCTATCGCCTATTTAATTCACAGCGCCTGGTTTTGTGGATTGGAATTTTATGTAGACGAACGGGTCATCATCCCGCGCTCGCCGATCGGTGCGCTGATTCAGGATGGCTTTGCCGGCTTGTTGCCAAAAGCGCCGAAACGTATTTTGGATATGTGCACCGGTAGCGGTTGTATCGCTATCGCCTGTGCCGAGCAATTCCCCGAAGCGGATGTGGACGCCGTCGATCTTTCTCTTGATGCGCTGAACGTAGCGGAAATCAACATTGAACGCTACAACCTCAGCCGCCGCGTGTTTCCGATTCAATCGGATTTATTCTCTCAATTATTGGCAGAACAATATGACCTCATCGTCACCAACCCGCCTTATGTGGATTTAGACGATCGCTCAGATATGCCGGAAGAATTTCACTACGAACCGGAAATGGCACTCGGTTCAGGCGACGACGGCTTAACCATCACCAAACAAATCCTGCGCCAAGCGGCAAACTACCTCACCGACGACGGCGTATTGGTATGCGAAGTAGGCAACAGCATGGTGCATTTAATCGAACAATTCCCCAACGTCCCGTTCAATTGGCTTGAACTCAAAAACGGCGGTGTCGGCGTTTTCGCCTTAGCCAAAGCAGAACTCATCGCCCACCAGGCAACTTTTGCT","","","35666","MNQITFNQELIDDIYSANVHDELHSIKDFLRWTYSTFNRAELFYGHGYDNAWDEAHQLVLSCLHLPPDFPAELYNARLTVAEKLELIRLVMIRLEKRLPIAYLIHSAWFCGLEFYVDERVIIPRSPIGALIQDGFAGLLPKAPKRILDMCTGSGCIAIACAEQFPEADVDAVDLSLDALNVAEINIERYNLSRRVFPIQSDLFSQLLAEQYDLIVTNPPYVDLDDRSDMPEEFHYEPEMALGSGDDGLTITKQILRQAANYLTDDGVLVCEVGNSMVHLIEQFPNVPFNWLELKNGGVGVFALAKAELIAHQATFA","1785204","","adenine specific methylase","Cytoplasm","","
InterPro
IPR002052
Domain
N-6 Adenine-specific DNA methylase
PS00092\"[214-220]?N6_MTASE
InterPro
IPR004556
Family
Modification methylase HemK
TIGR00536\"[24-315]ThemK_fam: methyltransferase, HemK family
InterPro
IPR007848
Domain
Methyltransferase small
PF05175\"[135-302]TMTS
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[107-307]Tno description
PTHR18895\"[141-275]TMETHYLTRANSFERASE
PTHR18895:SF7\"[141-275]THEMK METHYLTRANSFERASE FAMILY MEMBER


","No hits to the COGs database.","Significant hit ( 3.6e-07) to 2/4 blocks of the PR00507 family, which is described as \"N12 class N6 adenine-specific DNA methyltransferase signature\". Prints database entry for PR:PR00507. PR00507B 146-160 0.24 PR00507C 211-223 0.00067Significant hit ( 2.7e-05) to 1/1 blocks of the IPB002052 family, which is described as \"N-6 Adenine-specific DNA methylase\". Interpro entry for IP:IPR002052. IPB002052 210-220 2.8e-05","Residues 207 to 274 match (2e-07) PD:PD596871 which is described as PAPM METHYLASE METHYLTRANSFERASE ","","","","","","","","","","","","Wed Jan 22 07:48:25 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02562 is paralogously related to AA00647 (8e-17) and AA00508 (3e-04).","","","","","","","","","","","","","","1","","","" "AA02563","1786320","1785379","942","ATGGCGCTTAAATTAGAACGTGATGCGCTGGAAATGCGCAAAATTTACGCCGGCACCTTGCAGGAATGTATGCGGGAAAATCCGCTGGTGATTGAACTGGACGCGGATTTAATGAGCTGCATGACCATGGATAAAGTGCAGAAAAATCTGCCGAATCAGGTGATTAACTGTGGCATTATGGAAGCCAATGTGGTGGGCATGGCGGCAGGGTTAGCCATTGCCGGGCACATTCCGTTCTTCCACTCGTTTACCGCCTTTGCCAGCCGTCGCTGTTTGGATCAGCTGTTTATGTCGGTGGATTATCAACAGGCGAACGTGAAAGTTATCGCCTCCGACGCGGGTGTCACGGCAGTGTATAACGGCGGCACGCATATGTCCTTTGAAGACATGGGCATTGTGCGCGGGCTGGCTCATGCCAAGGTGTTGGAAATCACCGACGGCGCCATGATGAAAAATCTCGTTCGGCAGTTGGTGGCGTTAAAAGGCTTTTATTGGGTGCGCACCATTCGTAAAAGTGCGGTCAAAATTTACGATGAAAATGAAACCTTCACTATCGGTAAAGCAAAAGTCCTGCATGAAGGCAAAGACATTACCCTGATCGCCAACGGCATTATGGTGGCGGAGGCCTTGAAAGCGGCGGATATGTTGGCAGAGCAGGGCATTGACGCCACGGTAGTGGATATGTTCACCCTCAAACCGCTTGATCGGGAATGCGTGATTCAATGTGCCAAACGCACCGGTAGAATCGTCACCTGTGAAAATCACAGCGTCCAAAATGGTTTAGGTTCCGCCGTGGCAGAAGTGCTGGTGGAACATTGCCCGGTGCCAATGCGTCGTATCGGCATTAAAGAGCGTTACGGGCAAGTGGGATCCTTGGAATTCTTGATGAATGAATACGAGCTCACTGCGAATCATATTGTGCAGCAGGCGTTGACGTTGTTT","","","36865","MALKLERDALEMRKIYAGTLQECMRENPLVIELDADLMSCMTMDKVQKNLPNQVINCGIMEANVVGMAAGLAIAGHIPFFHSFTAFASRRCLDQLFMSVDYQQANVKVIASDAGVTAVYNGGTHMSFEDMGIVRGLAHAKVLEITDGAMMKNLVRQLVALKGFYWVRTIRKSAVKIYDENETFTIGKAKVLHEGKDITLIANGIMVAEALKAADMLAEQGIDATVVDMFTLKPLDRECVIQCAKRTGRIVTCENHSVQNGLGSAVAEVLVEHCPVPMRRIGIKERYGQVGSLEFLMNEYELTANHIVQQALTLF","1785377","From PF02779: Transketolase, pyridine binding domainThis family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases. ","transketolase C-terminal section","Cytoplasm","","
InterPro
IPR005475
Domain
Transketolase, central region
PF02779\"[8-129]TTransket_pyr
InterPro
IPR005476
Domain
Transketolase, C-terminal
PF02780\"[186-306]TTransketolase_C
InterPro
IPR009014
Domain
Transketolase, C-terminal-like
G3DSA:3.40.50.920\"[185-314]Tno description
InterPro
IPR012068
Family
Transketolase, C-terminal region
PIRSF036564\"[5-314]TPredicted transketolase, C-terminal subunit
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.970\"[7-185]Tno description
PTHR11624\"[41-314]TDEHYDROGENASE RELATED
PTHR11624:SF20\"[41-314]T1-DEOXYXYLULOSE-5-PHOSPHATE SYNTHASE


","BeTs to 6 clades of COG0021COG name: TransketolaseFunctional Class: GThe phylogenetic pattern of COG0021 is --mpkzyqvdrlbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is","","Residues 101 to 181 match (3e-07) PD:PD443507 which is described as COMPLETE SYNTHASE PROTEOME TRANSKETOLASE THIAMINE PYROPHOSPHATE TRANSFERASE BIOSYNTHESIS 5-PHOSPHATE TK ","","","","","","","","","","","Wed Jan 22 08:03:34 2003","Wed Jan 22 07:57:57 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02563 is paralogously related to AA02050 (2e-24).","","","","","","Residues 186 to 306 (E-value = 9.9e-42) place AA02563 in the Transketolase_C family which is described as Transketolase, C-terminal domain (PF02780)","","","","","Lindqvist Y, Schneider G, Ermler U, Sundstrom M.Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution.EMBO J 1992 Jul;11(7):2373-9PMID: 1628611Sprenger,G.A. Nucleotide sequence of the Escherichia coli K-12 transketolase(tkt) gene. Biochim. Biophys. Acta 1216 (2): 307-310 (1993) PubMed: 8241274","","Wed Jan 22 08:08:23 2003","1","","","" "AA02564","1786843","1786313","531","TTGCCAAGTCACCCCGACCGTTTGAAAACCCCCGGCGTGGACGCCACAACAGGTTCGCTCGGGCAGGGCATTTCCATTGCGGCAGGCATCGCCTTGTCCCATCAATTACGCGGTATGCCGAACCGCACTTTTTGTATTGTGGGCGACGGCGAACTGAACGAAGGTCAATGTTGGGAGGCGTTTCAGTTTATTGCGCATCGCAATTTAACCAATCTTTGCGTCATCGTGGATTACAACAAATTGCAATTAGACGGATGCCTGACGGACATCATCAATCCGTTCAGCTTGCAGGACAAATTTGCCGCTTTCGGCTTCGTGGTGGAAACCGTCAACGGCGATGATATTGACGCCTTGTGTCGTGTGCTTTCCGCTACGCCGACCCGACCGTTGGCGGTGATTTTGGATTCCAAAAAAGGGCAGGGCGTGCCTTATATCGAAAACCTTGCCAATAATCACCATTTGCGTCTGAATGACGAAAGCCGCGCGCAAATTCAGTTATCAATCGACGAATTGGAGGCGGAGTATGGCGCT","4.70","-8.04","19229","LPSHPDRLKTPGVDATTGSLGQGISIAAGIALSHQLRGMPNRTFCIVGDGELNEGQCWEAFQFIAHRNLTNLCVIVDYNKLQLDGCLTDIINPFSLQDKFAAFGFVVETVNGDDIDALCRVLSATPTRPLAVILDSKKGQGVPYIENLANNHHLRLNDESRAQIQLSIDELEAEYGA","","","transketolase N-terminal section","Cytoplasm, Inner membrane","Matches in gapped BLAST to transketolase N-terminal sections.AA02564 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus ducreyi gene.AA02564 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus influenzae Rd gene.","
InterPro
IPR005474
Domain
Transketolase, N-terminal
PF00456\"[4-120]TTransketolase_N
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.970\"[1-169]Tno description
PTHR11624\"[12-164]TDEHYDROGENASE RELATED
PTHR11624:SF2\"[12-164]TTRANSKETOLASE


","No hits to the COGs database.","","Residues 21 to 133 match (2e-37) PD:PD000580 which is described as COMPLETE PROTEOME THIAMINE SYNTHASE PYROPHOSPHATE FLAVOPROTEIN SUBUNIT PYRUVATE DEHYDROGENASE TRANSKETOLASE ","Sat Feb 28 10:43:11 2004","Sat Feb 28 17:24:34 2004","Sat Feb 28 17:24:34 2004","Sat Feb 28 17:24:34 2004","Sat Feb 28 10:43:11 2004","Sat Feb 28 10:43:11 2004","Sat Feb 28 10:43:11 2004","Sat Feb 28 10:43:11 2004","Sat Feb 28 10:43:11 2004","Sat Feb 28 10:43:11 2004","Sat Feb 28 10:43:11 2004","Sat Feb 28 10:43:11 2004","Sat Feb 28 10:43:11 2004","Sat Feb 28 10:43:11 2004","Sat Feb 28 10:43:11 2004","Sat Feb 28 10:43:11 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02564 is paralogously related to AA01563, a transketolase isozyme 1 (1e-14) and AA1329, a 1-deoxy-D-xylulose 5-phosphate synthase (4e-04).AA02564 is paralogously related to AA01563 (1e-14) and AA02050 (3e-04).","Sat Feb 28 10:43:11 2004","Sat Feb 28 17:24:34 2004","pdb1GPU1GPU-A TRANSKETOLASE COMPLEX WITH REACTION INTERMEDIATE 66.3 3e-12pdb1AY01AY0-A IDENTIFICATION OF CATALYTICALLY IMPORTANT 66.3 3e-12pdb1TKA1TKA-A TRANSKETOLASE (E.C.2.2.1.1) COMPLEXED WITH 66.3 3e-12pdb1GPU1GPU-A TRANSKETOLASE COMPLEX WITH REACTION INTERMEDIATE 66.3 3e-12pdb1TKA1TKA-A TRANSKETOLASE (E.C.2.2.1.1) COMPLEXED WITH 66.3 3e-12pdb1AY01AY0-A IDENTIFICATION OF CATALYTICALLY IMPORTANT 66.3 3e-12","","","Residues 1 to 175 (E-value = 4.3e-07) place AA02564 in the Transketolase_N family which is described as Transketolase, thiamine diphosphate binding domain (PF00456)","Sat Feb 28 10:43:11 2004","","","","","","","1","Sat Feb 28 10:43:11 2004","","" "AA02565","1787135","1786506","630","ATGGATACTACAGAACTTCAACGGTTTGCTCAGAAAATTCGTCTTAACACATTAAAATCGCTGGTGCATTTAGACTTTGGTCACTTCGGTGGCAGCCTTTCTATCGTAGAAACCCTTGCCGTGTTATACGGCAAGGTGATGCGCCTCAAACCTGAAGATCCGCATTGGCAGGAACGCGATTATTTTGTGTTATCCAAAGGGTACGCAGGCCCCGCCCTGTATGCCACTCTCGCCTTAAAAGGCTATTTTTCCTCTCGAGCAACTTTTTACCTTAAATTCCGACCGCACTTTTTTGCCAAGTCACCCCGACCGTTTGAAAACCCCCGGCGTGGACGCCACAACAGGTTCGCTCGGGCAGGGCATTTCCATTGCGGCAGGCATCGCCTTGTCCCATCAATTACGCGGTATGCCGAACCGCACTTTTTGTATTGTGGGCGACGGCGAACTGAACGAAGGTCAATGTTGGGAGGCGTTTCAGTTTATTGCGCATCGCAATTTAACCAATCTTTGCGTCATCGTGGATTACAACAAATTGCAATTAGACGGATGCCTGACGGACATCATCAATCCGTTCAGCTTGCAGGACAAATTTGCCGCTTTCGGCTTCGTGGTGGAAACCGTCAACGGCGA","","","24842","MDTTELQRFAQKIRLNTLKSLVHLDFGHFGGSLSIVETLAVLYGKVMRLKPEDPHWQERDYFVLSKGYAGPALYATLALKGYFSSRATFYLKFRPHFFAKSPRPFENPRRGRHNRFARAGHFHCGRHRLVPSITRYAEPHFLYCGRRRTERRSMLGGVSVYCASQFNQSLRHRGLQQIAIRRMPDGHHQSVQLAGQICRFRLRGGNRQRR","1786504","","transketolase, N-terminal subunit","Cytoplasm, Extracellular","","
InterPro
IPR005474
Domain
Transketolase, N-terminal
PF00456\"[40-82]TTransketolase_N
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.970\"[1-84]Tno description
PTHR11624\"[31-84]TDEHYDROGENASE RELATED
PTHR11624:SF2\"[31-84]TTRANSKETOLASE
tmhmm\"[21-43]?transmembrane_regions


","BeTs to 20 clades of COG0021COG name: TransketolaseFunctional Class: GThe phylogenetic pattern of COG0021 is --mpkzyqvdrlbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.7e-14) to 2/3 blocks of the IPB000360 family, which is described as \"Transketolase\". Interpro entry for IP:IPR000360. IPB000360A 27-38 1.3 IPB000360B 40-79 5.6e-12","Residues 10 to 83 match (5e-26) PD:PD449569 which is described as TRANSKETOLASE COMPLETE PROTEOME TRANSFERASE PYROPHOSPHATE THIAMINE TK FAMILY MULTIGENE PROBABLE ","","","","","","","","","","","","Wed Jan 22 08:15:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02565 is paralogously related to AA01563 (5e-08).","","","","","","","","","","","Lindqvist Y, Schneider G, Ermler U, Sundstrom M. Three-dimensional structure of transketolase, a thiamine diphosphatedependent enzyme, at 2.5 A resolution. EMBO J 1992 Jul;11(7):2373-9 PMID: 1628611 Sprenger,G.A. Nucleotide sequence of the Escherichia coli K-12 transketolase (tkt) gene. Biochim. Biophys. Acta 1216 (2): 307-310 (1993) PubMed: 8241274","","Wed Jan 22 08:18:37 2003","1","","","" "AA02566","1788239","1787148","1092","ATGGCGGTAGAAAAATACGGCACGGCGACGGCACTGATTATGGCGTTCGGCATGGTGGCGAATATTTTGGTCGCGCGTTTTACCCGCTTAAAATTCATTTTCTTAACCGGTCACCACACCTTTTATATGGCGTGTATGATTGCGGTGATTTTAACCGTTGCCGGTTTGGAAGGCATGGAATTGATTGTTGCCGGATCCCTGACTTTAGGCTTGATTATGGCGTTTTTCCCGGCGTTGGCGCATTTTTATATGAAGAAAATCACAGGTAGTAATGATGTGGGTTTCGGGCATTTCGGTACTTTGGGTTATGTGCTTTCCGGCGCCATCGGTCAGGCGGTGGGTAAAGGATCCAAATCCACGGAAGAAATGGATTTGCCGAAAAATCTAAGCTTCCTGCGTGACAGTTCCATTTCCATTTCACTGACCATGATGGCGATTTATTTCATTCTTGCCATCGCTTCCGGCAGTGAATATGTGACGGCGCATTTCAGTAACGGACAACATTATTTGGTGTATGCGGCGATTCAAGCCATTACCTTCGCAGCTGGCGTGTTCATCATCTTGCAAGGGGTGCGTTTGATTTTGGCTGAAATCGTGCCGGCATTTACCGGGATTTCCGAGAAGCTCGTGCCGGATGCCAAACCTGCGCTGGATTGCCCGATCGTCTTCCCGTACGCACCGAATGCGGTGTTAATTGGTTTTCTTGCCAGTTTCGTGGGTGGGATCGTCGGCTTGGCGTTACTCAATCAATTACACTGGGTGTTAATTCTGCCCGGTGTTGTACCGCACTTTTTCTGTGGCGCCACAGCCGGGGTGTTCGGTAACGCCACCGGTGGTCGTCGCGGCGCAATTTTAGGCGCATTTGCACACGGCGTGTTGATTACCTTCTTGCCGGTATTCTTATTGCCGGTCTTGGGTTCTCTTGGTTTTGCCAATACCACCTTCTCCGATTCGGACTTCGGCGGTGTGGGTATTGTGCTGGGCTACATGGCGCAATATTTCTCCAAAGAGATGATTTTAATCTCCGTGGTGAGTGTTTTCCTGTTGCTGGTGGGCTATAACTACATTGCGAAAAAAACAACAGAGCAAAAA","","","42337","MAVEKYGTATALIMAFGMVANILVARFTRLKFIFLTGHHTFYMACMIAVILTVAGLEGMELIVAGSLTLGLIMAFFPALAHFYMKKITGSNDVGFGHFGTLGYVLSGAIGQAVGKGSKSTEEMDLPKNLSFLRDSSISISLTMMAIYFILAIASGSEYVTAHFSNGQHYLVYAAIQAITFAAGVFIILQGVRLILAEIVPAFTGISEKLVPDAKPALDCPIVFPYAPNAVLIGFLASFVGGIVGLALLNQLHWVLILPGVVPHFFCGATAGVFGNATGGRRGAILGAFAHGVLITFLPVFLLPVLGSLGFANTTFSDSDFGGVGIVLGYMAQYFSKEMILISVVSVFLLLVGYNYIAKKTTEQK","1787146","","PTS system, IIC component","Inner membrane, Cytoplasm","","
InterPro
IPR000719
Domain
Protein kinase
PS00107\"[93-115]?PROTEIN_KINASE_ATP
InterPro
IPR007333
Family
Putative sugar-specific permease, SgaT/UlaA
PF04215\"[2-323]TSgaT_UlaA
noIPR
unintegrated
unintegrated
signalp\"[1-25]?signal-peptide
tmhmm\"[10-28]?\"[38-56]?\"[61-83]?\"[93-113]?\"[134-154]?\"[168-188]?\"[228-248]?\"[254-274]?\"[283-303]?\"[309-329]?\"[339-357]?transmembrane_regions


","No hits to the COGs database.","","Residues 288 to 332 match (1e-08) PD:PD470380 which is described as PROTEOME COMPLETE MEMBRANE INNER IIC PTS INTEGRAL SYSTEM SAV0329 COMPONENT ","","","","","","","","","","","","Wed Jan 22 09:19:20 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02566 is paralogously related to AA01695 (3e-37).","","","","","","Residues 2 to 323 (E-value = 9.4e-49) place AA02566 in the SgaT_UlaA family which is described as Putative sugar-specific permease, SgaT/UlaA (PF04215)","","","","","","","","1","","","" "AA02567","1788499","1788365","135","ATGGATTCTATACTTTTCTTTATTTTAGACATTTTAAAAGTGCCTTCCATTCTGGTCGGTCTCATTGCGTTGGTCGGCTTGTTGGTGCAAAAGAAATCCTTCCCCGATGTGGTGAAGGGAACGATTAAAACCATT","","","4879","MDSILFFILDILKVPSILVGLIALVGLLVQKKSFPDVVKGTIKTI","1788365","","hypothetical protein (possible inner membrane protein)","Cytoplasm","This sequence is weakly similar to gi|16765669, a predicted inner membrane protein from Salmonella typhimurium LT2.","
InterPro
IPR007333
Family
Putative sugar-specific permease, SgaT/UlaA
PF04215\"[1-45]TSgaT_UlaA
noIPR
unintegrated
unintegrated
signalp\"[1-30]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 08:41:17 2004","Wed Feb 25 08:41:17 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA1107.AA02567 is paralogously related to AA01695 (4e-04).","Wed Feb 25 08:41:17 2004","","","","","","","","","","","","","1","","","" "AA02568","1788785","1788519","267","ATGAAAATTATGGCTGTTTGCGGTTCCGGTTTAGGGAGCAGTTTTATGATGGAAATGAATGCCAAAAAGGCGCTTGCTAAATTGGGGATTGATGCCGAGGTGAATCATACGGATTTGGAGTCGGTGACGGTGAATGATGCGGATGTGTTTATTATGGCGAGCGATATTGCCGAGAGCAGTTCCATTCCGGTGGAGAAAATCGTGGTGGTGAAAAATATCGTGAGTGTCGGTGAATTTGAAGAAAAATTGGCGGCGTATTTTAATCGG","","","9540","MKIMAVCGSGLGSSFMMEMNAKKALAKLGIDAEVNHTDLESVTVNDADVFIMASDIAESSSIPVEKIVVVKNIVSVGEFEEKLAAYFNR","1788517","","sugar phosphotransferase component II B","Cytoplasm","","
InterPro
IPR003501
Domain
Phosphotransferase system, lactose/cellobiose-specific IIB subunit
PF02302\"[2-88]TPTS_IIB
InterPro
IPR013011
Domain
Phosphotransferase system, EIIB component, type 2
PS51099\"[1-89]TPTS_EIIB_TYPE_2


","BeTs to 4 clades of COG3414COG name: Phosphotransferase system component IIB of unknown specificityFunctional Class: GThe phylogenetic pattern of COG3414 is -----------lb-e-gh-------wNumber of proteins in this genome belonging to this COG is","","Residues 1 to 83 match (2e-19) PD:PD068164 which is described as COMPLETE PROTEOME PHOSPHOTRANSFERASE PTS COMPONENT TRANSFERASE ENZYME B IIB SYSTEM ","","","","","","","","","","","","Wed Jan 22 08:49:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02568 is paralogously related to AA01695 (6e-08).","","","","","","Residues 2 to 88 (E-value = 4.9e-16) place AA02568 in the PTS_IIB family which is described as PTS system, Lactose/Cellobiose specific IIB subunit (PF02302)","","","","","Zinser ER, Kolter R.Mutations enhancing amino acid catabolism confer a growth advantage in stationary phase.J Bacteriol. 1999 Sep;181(18):5800-7.PMID: 10482523","","Wed Jan 29 13:47:08 2003","1","","","" "AA02569","1789152","1789244","93","TTGGAAGGAATAGAAAAAGTGCGGTCTGTTTTGAAAGCGTTTTTTAAGAACAGAACAATGATTCAATCCTCCACGCTTGGACCGGATAAGCAC","","","3513","LEGIEKVRSVLKAFFKNRTMIQSSTLGPDKH","1789244","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Feb 25 08:29:18 2004","Wed Feb 25 08:29:18 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02569 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Feb 25 08:29:18 2004","","","","","","","","","","","","","1","","","" "AA02570","1790285","1789290","996","ATGAACAATTTAAAAAAGAACTGGATCATTATTACTGCTGGGGTATTAGTAATCATTGCTTTTGGTATGTATGTTTGGAATTTCCGGAACTATGATATTTCCGATAATAGTGCAAAGTGGAATGATTTTGGAAGCTATATTGGTGGGATATTTTCTGCATTAGCATTTTTAGGTGTTGTATATCAGTTGCATACAACAAAACAAGAACAAAAAAAGCAAGAGTTTGAACGAACTTTCTTTATGATGTTGGAACAGCATAATTTGAAGTTGAATACTATTGGGCAAGAGGTAATAGATGAAATCTACGATAAAATTATATCAAATTATGGAAGTATGGATTCACTAAGAAATAAAATTGAGATTCAAGAAAAATCTAAAATTTATTCTGAAGTTAATAGTTACTTTTTACTTCTATATAGGATTTTGAAATTCATTTATGAAAATGGTGAGTTAAATAATAAAAATAATTATTCAAGTTTATTGAGAAGTTTTATATCTAATAAATTATTAGTTGTATTGTCTTATCATCTATCTAATAGAGATGACTCTTATAGGAATTATATTGAATATATTAATAGGTTCTCATTTTTGGAGCACGTAAATTTTATAGATCTAGAACTTGAATTTATACATCAAGTGAGTAGGGTAGAGAAAGAAGCTTTATACGATTTAGTTTTTAAGGGAGAAAGTTATCTATTTGATGCTCTTAAGAGTGGTGAATTAATTCCTGATGATATTGATAGCTATGATCGTGAAATGTTTTTAAAGGAAATTATCCAAAGTAAACAGGAAAATTGTCCTATAATATATAAAAAGTTTATGGGGTTAAATTTGGGATATGTCAAGGAAGGGAAATCTGTAAAAGCTGAATTAAAGTATGAGGATAATATTATTTTTCATATATTAAAAAACTTTTCTTTATCTGCTTTTGGAAAAAATAAAGAGTATGGGGAATTAATTGTGAGATATAAAAATATAGTAAACCCAGATAAGGAA","","","39231","MNNLKKNWIIITAGVLVIIAFGMYVWNFRNYDISDNSAKWNDFGSYIGGIFSALAFLGVVYQLHTTKQEQKKQEFERTFFMMLEQHNLKLNTIGQEVIDEIYDKIISNYGSMDSLRNKIEIQEKSKIYSEVNSYFLLLYRILKFIYENGELNNKNNYSSLLRSFISNKLLVVLSYHLSNRDDSYRNYIEYINRFSFLEHVNFIDLELEFIHQVSRVEKEALYDLVFKGESYLFDALKSGELIPDDIDSYDREMFLKEIIQSKQENCPIIYKKFMGLNLGYVKEGKSVKAELKYEDNIIFHILKNFSLSAFGKNKEYGELIVRYKNIVNPDKE","1789288","","conserved hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide
tmhmm\"[9-29]?\"[43-63]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Jan 22 09:26:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02570 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02573","1792489","1790549","1941","GTGGCACTCATCAGCTTAACCAACGGATATCTTTCTTTCAGTGATGCGCCTTTATTGGATCATGCGGATTTACATATTGAACCGAACGAACGCGTTTGTTTAGTGGGGCGTAATGGGGCGGGGAAATCCACCTTGCTCAAAATTATTGCCGGCGATGTGGTGATGGACGACGGCAAAGTGCAATACGAAAAAGACTTGGTGGTGTCCCGTTTGGAGCAGGATCCGCCGCGTCATGCGGAAGGCAATGTGTTTGATTATGTGGCGGAGGGCATTGAGCATCTGGCGGATTTATTGAAGGAATATCATCATATTTCCGTGCAATTGGAGCAAAATTACAGCGAGCAGGTGCTCAATCAGCTTGCGCAAATTCAAGCCAAATTAGAACATGCCAATGGCTGGCAATTTGAAAATAAAATTAACGAAGTGCTGGCAAAACTGGAACTTAATCCGAATACCAAACTCGCCGATTTATCCGGCGGTTGGTTGCGCAAAGCCGCTTTGGCGCGTGCGTTGGTGTGTAATCCTGATGTCTTGTTATTGGATGAGCCTACCAACCACCTAGACGTTGATGCTATCGAATGGCTGGAAAATTTCTTGATGGAATTCAGCGGCAGCATAGTCTTTATTTCCCACGACCGTTCCTTTATTCGCAAAATGGCGACCCGCATTGTGGATTTGGATCGCGGCAAATTGGTTTCTTATCCCGGCGATTATGATTTATATCTCACTACCAAGGAAGAAAATCTGCGGGTGGAAGCCTTACAAAACGACTTATTCGACAAACGCTTAGCGCAGGAAGAAGTGTGGATTCGCCAAGGTATCAAAGCCCGCCGCACCCGTAATGAAGGACGTGTGCGCGCCTTAAAAGCTATGCGGGAAGAACGCAGCCAACTCCGCGACGTATTAGGCACGGCAAAATTGCAATTAGACACGTCCAGCCGCTCGGGCAAAATCGTATTTGAAATGGAAAATGTCAGCTACGACATCGACGGCAAGCAACTTCTCAAGGATTTCAGTACCACCATTTTACGTGGCGACAAAATCGCCCTTGTCGGTCCGAACGGCTGCGGCAAAACCACCTTTATTAAATTGTTGCTCGGCGAGATTCAGCCCACAAGCGGTTCTATTCGCTGCGGCACAAAATTGGACATTGCCTATTTTGACCAATACCGCGCTGATCTCGAACCGGAAAAATCGGTGATAGATAACGTCGCCGACGGCAAACAGGATGTGGAAGTCAACGGCGTAAAACGTCATGTGTTGGGCTACTTGCAGGATTTCCTATTCCTGCCGAAACGTGCCATGACCCCGGTTAAAGCCCTTTCAGGCGGCGAACGTAACCGTCTGTTATTGGCGAAATTATTGTTAAAACCCAATAATTTGCTCATTCTGGATGAGCCGACTAATGACTTGGACGTAGAAACCTTGGAATTGTTGGAAGAAATTCTCACGGATTATCAAGGCACCTTGCTTATCGTCAGTCACGATCGTCAATTTATTGATAATACCGCCACCGAATGCTACATCTTTGAAGGCAACGGCGTGCTGAATAAATACGTCGGCGGCTTCTTCGACGCCAAACAGCAGCAAGCCAATTATTTTGCACAAAAAGCCGAACAAGGCGCGGTTAAAAATAAAAAAATCGAGCCGAAAAAAGAAGAAAGTGCGGTGGAAAATAAAAACGTTTCCAACAAACCGAAAACCGTCAAACTTTCCTATAAAGAACAACGCGAATTGGAACAGCTGCCGCAATTGCTGGAAGATTTAGAAGAAAAAATCACCGCACTTCAAAGCGAAATCGCCGACCCGAATTTTTTCCAACAATCCCACGACATCACTGATGCCAAATTGAAAGCGCTGGCAGACACCGAAACCGAACTGGAAACGGCATTTATGCGCTGGGAAGAATTGGAGGAAAAGAAAAATCTGGCGGAAGGGAAA","","","73185","VALISLTNGYLSFSDAPLLDHADLHIEPNERVCLVGRNGAGKSTLLKIIAGDVVMDDGKVQYEKDLVVSRLEQDPPRHAEGNVFDYVAEGIEHLADLLKEYHHISVQLEQNYSEQVLNQLAQIQAKLEHANGWQFENKINEVLAKLELNPNTKLADLSGGWLRKAALARALVCNPDVLLLDEPTNHLDVDAIEWLENFLMEFSGSIVFISHDRSFIRKMATRIVDLDRGKLVSYPGDYDLYLTTKEENLRVEALQNDLFDKRLAQEEVWIRQGIKARRTRNEGRVRALKAMREERSQLRDVLGTAKLQLDTSSRSGKIVFEMENVSYDIDGKQLLKDFSTTILRGDKIALVGPNGCGKTTFIKLLLGEIQPTSGSIRCGTKLDIAYFDQYRADLEPEKSVIDNVADGKQDVEVNGVKRHVLGYLQDFLFLPKRAMTPVKALSGGERNRLLLAKLLLKPNNLLILDEPTNDLDVETLELLEEILTDYQGTLLIVSHDRQFIDNTATECYIFEGNGVLNKYVGGFFDAKQQQANYFAQKAEQGAVKNKKIEPKKEESAVENKNVSNKPKTVKLSYKEQRELEQLPQLLEDLEEKITALQSEIADPNFFQQSHDITDAKLKALADTETELETAFMRWEELEEKKNLAEGK","1790547","From PF00005: ABC transportersABC transporters for a large family of proteins are responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain ABC_membrane.","ABC transporter, ATP-binding protein","Cytoplasm, Inner membrane","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[156-199]TQ9CMF2_PASMU_Q9CMF2;
PF00005\"[29-229]T\"[345-513]TABC_tran
PS50893\"[4-253]T\"[320-537]TABC_TRANSPORTER_2
PS00211\"[157-171]?\"[441-455]?ABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[28-230]T\"[344-515]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[1-241]T\"[282-571]Tno description
PTHR19211\"[130-606]TATP-BINDING TRANSPORT PROTEIN-RELATED
PTHR19211:SF7\"[130-606]TABC TRANSPORTER ABCF3, UUP


","No hits to the COGs database.","Significant hit ( 4.1e-29) to 2/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 334-380 1.2e-18 IPB001140B 438-476 4.8e-09 IPB001140B 154-192 6.4e-07","Residues 524 to 574 match (4e-07) PD:PD345653 which is described as ATP-BINDING COMPLETE ABC PROTEOME REPEAT TRANSPORTER UUP-2 UUP-1 ","","","","","","","","","","","Wed Jan 22 09:32:35 2003","Wed Jan 22 09:29:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02573 is paralogously related to AA02484 (4e-83), AA01555 (7e-61), AA02140 (2e-22), AA01820 (1e-17), AA01524 (1e-17), AA00207 (1e-16), AA00751 (1e-16), AA01645 (4e-16), AA00700 (3e-15), AA02786 (3e-15), AA00933 (4e-15), AA01656 (6e-15), AA01867 (8e-15), AA00415 (1e-14), AA02331 (4e-14), AA02718 (8e-14), AA01568 (8e-14), AA02899 (2e-13), AA01684 (2e-13), AA01509 (4e-13), AA01051 (4e-13), AA01393 (7e-13), AA01757 (1e-12), AA00858 (3e-12), AA01961 (4e-12), AA02440 (6e-12), AA01422 (6e-12), AA01824 (8e-12), AA01779 (1e-11), AA02080 (3e-11), AA01456 (3e-11), AA02805 (5e-11), AA02609 (5e-11), AA01616 (5e-11), AA02353 (7e-11), AA02320 (7e-11), AA02550 (2e-10), AA00799 (2e-10), AA00061 (3e-10), AA01510 (1e-09), AA01947 (2e-09), AA02324 (1e-08), AA02152 (3e-08), AA02606 (4e-08), AA02225 (9e-08), AA00591 (2e-07), AA02898 (2e-07), AA02642 (6e-07), AA02226 (5e-06), AA00934 (7e-06), A02145 (1e-05), AA01556 (1e-05) and AA02146 (8e-04).","","","","","","Residues 345 to 513 (E-value = 4.8e-40) place AA02573 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Reddy,M. and Gowrishankar,J. Identification and characterization of ssb and uup mutants with increased frequency of precise excision of transposon Tn10 derivatives: nucleotide sequence of uup in Escherichia coli J. Bacteriol. 179 (9), 2892-2899 (1997) PubMed: 9139905 Higgins CF, Hyde SC, Mimmack MM, Gileadi U, Gill DR, Gallagher MP.Binding protein-dependent transport systems.J Bioenerg Biomembr 1990 Aug;22(4):571-92PMID: 2229036 ","","Wed Jan 22 09:31:20 2003","1","","","" "AA02574","1793884","1792535","1350","ATGAAAAATCAGATTAATCCCCGTTGGCAGCAACGTTTTATTGACGATAAACCACGGGAAAAAGACCACCGTCCGCCGTTCCGTCGAGATCGCGGACGCATTCTCCATTCCGCCGCCTTTCGTTGTTTACAGGCAAAAACCCAAATTCACGCGGTGGGCGAAAATGATTTTTATCGCACTCGTTTGACCCATTCGCTGGAAGTGGCGCAAATCGGCAGCAGCCTTGTAGCACAAATGAAATTTGCCGAAGCCTTCAATGCCGTGGCACACCAGCTTTCCGTAGAAAAAAGCGAACTGCAAAAACAGCTGATTCCGTTGTTGCCTTCTAATGATCTGATTGAAAGTTTATGTTTTGCTCACGACATCGGTCATCCGCCTTTCGGGCATGGTGGCGAAGTGGCGCTTAACTATATGATGCGTAACAACGGCGGCTTTGAGGGCAATGCACAAACCTTCCGCCTGCTCACCAAACTTGAGCCTTATACGCCGAACGCCGGCATGAATTTAGCCCGACGTACGATCCTTGGTATCGTAAAATATCCTACCATTTTGGATGTGTCCTCCGCACAGTATGCGCAGTTAGACGAAACCCAACACAGCGATCCCCGTTATGTGAAAATCGCCGATTGGCGACCGGGCAAAGGGCTGTTTCGTGATGACATTGCCATGTTCGATTGGTTGCTGGAACCGCTTTCCGAAAGCGACCGCACGTTGTTCGGCGCACTACAAAAAGTGCGGTCAAATCCCAAAGAGATTTTAAAGACCCGCTTTAAATCCTTGGATTGCAGCATTATGGAGCTGGCAGACGACATCGCCTACGGCGTGCACGATTTGGAAGATGCTATCGTGGTGGGCGTGGTGAATGTGCAGCAATGGCAAGAAGCGCTGAACGCACTGAAAAATAGCCAATCGGAGTGGATGCGTCAACATATCGAACACATCAGCGAAAAACTGTTTTCCGATCAACATTACTTACGCAAAAATGCCATCGGCGCCTTGGTCAACTATTTCATCACCAGCGTACGTTGGAAAATTCAGCCGGAATTCAGCGATCCGCTGTTGCGTTATAACGCCGAATTACCGCAAGAAGTGGTGGACGTACTCAACGTGTTCAAAAAATTCGTGTTGAAGTATGTCATCAATAGTGTGGAAACCCAGCGCGTGGAATATAAAGGTCAACGCATTTTGACGGAAATGTTCCAAATTTTTGAATCGGATCCGCAACGCCTGCTCCCCACCAACACCGCCAACCGCTGGTTGAAAGCGGAAGAATCGGGCAAGAAGCGCGTCATTTGCGATTACATCGCCGGTATGTCCGATGCGTACGCGCTCAAGGTGTATCAGCAGCTT","","","51869","MKNQINPRWQQRFIDDKPREKDHRPPFRRDRGRILHSAAFRCLQAKTQIHAVGENDFYRTRLTHSLEVAQIGSSLVAQMKFAEAFNAVAHQLSVEKSELQKQLIPLLPSNDLIESLCFAHDIGHPPFGHGGEVALNYMMRNNGGFEGNAQTFRLLTKLEPYTPNAGMNLARRTILGIVKYPTILDVSSAQYAQLDETQHSDPRYVKIADWRPGKGLFRDDIAMFDWLLEPLSESDRTLFGALQKVRSNPKEILKTRFKSLDCSIMELADDIAYGVHDLEDAIVVGVVNVQQWQEALNALKNSQSEWMRQHIEHISEKLFSDQHYLRKNAIGALVNYFITSVRWKIQPEFSDPLLRYNAELPQEVVDVLNVFKKFVLKYVINSVETQRVEYKGQRILTEMFQIFESDPQRLLPTNTANRWLKAEESGKKRVICDYIAGMSDAYALKVYQQL","1792533","","dGTP triphosphohydrolase","Cytoplasm","","
InterPro
IPR003607
Domain
Metal-dependent phosphohydrolase, HD region
SM00471\"[57-283]THDc
InterPro
IPR006261
Family
Deoxyguanosinetriphosphate triphosphohydrolase
TIGR01353\"[23-450]TdGTP_triPase: deoxyguanosinetriphosphate tr


","No hits to the COGs database.","","Residues 33 to 136 match (3e-13) PD:PD005052 which is described as PROTEOME COMPLETE INDUCIBLE INTERFERON-GAMMA MG11 TRIPHOSPHOHYDROLASE HYDROLASE MG461 CHROMOSOME SIMILAR ","","","","","","","","","","","","Wed Jan 22 09:36:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02574 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","",""," Haraszthy VI, Jordan SF, Zambon JJ.,Identification of Fur-regulated genes in Actinobacillus actinomycetemcomitans.Microbiology. 2006 Mar;152(Pt 3):787-96.PMID: 16514158"," Wurgler SM, Richardson CC.DNA binding properties of the deoxyguanosine triphosphate triphosphohydrolase of Escherichia coli.J Biol Chem. 1993 Sep;268(27):20046-54.PMID: 8397198Quirk S, Bhatnagar SK, Bessman MJ.Primary structure of the deoxyguanosine triphosphate triphosphohydrolase-encoding gene (dgt) of Escherichia coli.Gene. 1990 Apr;89(1):13-8.PMID: 2165018Wurgler SM, Richardson CC.Structure and regulation of the gene for dGTP triphosphohydrolase from Escherichia coli.Proc Natl Acad Sci U S A. 1990 Apr;87(7):2740-4.PMID: 2157212","","Wed Jan 22 09:42:19 2003","1","","","" "AA02575","1794578","1793889","690","ATGTCTTATTTGGTTTATCTTTATACTTTGCTAACCATTGTTGCGTTTGCTTTGGCAGTAAAAATTAACAAACGCTGGAAATCCGTCGTACTGAACAGTTTTGTGCTGACGGTGCTGATTTTAGTGGCGGTGTTGCTGATTTTCAAATTGCCTTATGAAAGTTATATGGAAGGTAACGCGCCACTCAATAATTTATTGGGCGTAAGTATTGTTGCGTTGGCTATTCCGTTATATGAACAACTTCGCCAAATTCGCAACTACTGGCAAATTATTTTAATCACAACGGTGGCGGCTTCTGTGTTGTCTATGTTAAGCGGGGGGATCTTTGCTTTATTGCTTGGCGCACAGCCTGATATTGTGGCTACCGTGTTGCCGAAATCCGTGACGACGCCCATTGCCATGGCGGTGTCCGAAAATCTTGGCGGCATTCCTTCCGTGGCGGCGGTGGGCGTGGTGGTTGCCGGTTTACAGGGGTCTATTTTCGGCTATTTATTATTAACCAAAATCGGCTTGAAAAATAAAGAATCCATCGGATTATCCGTGGGCGCCGTTTCTCACGCGTTAGGCACGGTAAGCTGTATGGAAAACGATAAGAAAGCCGGCAGTTACAGTTCCATTTCCTTAGTATTGTGCGGTATCATTAGTTCAATTTTGGCACCTCTTATCTTCAAATTGATCTACACATTGGTA","","","24401","MSYLVYLYTLLTIVAFALAVKINKRWKSVVLNSFVLTVLILVAVLLIFKLPYESYMEGNAPLNNLLGVSIVALAIPLYEQLRQIRNYWQIILITTVAASVLSMLSGGIFALLLGAQPDIVATVLPKSVTTPIAMAVSENLGGIPSVAAVGVVVAGLQGSIFGYLLLTKIGLKNKESIGLSVGAVSHALGTVSCMENDKKAGSYSSISLVLCGIISSILAPLIFKLIYTLV","1793887","","transmembrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR005261
Family
Conserved hypothetical protein 659
TIGR00659\"[2-227]TTIGR00659: conserved hypothetical protein T
InterPro
IPR007300
Family
LrgB-like protein
PF04172\"[12-226]TLrgB
noIPR
unintegrated
unintegrated
signalp\"[1-19]?signal-peptide
tmhmm\"[4-19]?\"[28-48]?\"[58-78]?\"[88-108]?\"[146-166]?\"[203-223]?transmembrane_regions


","BeTs to 8 clades of COG1346COG name: Putative effector of murein hydrolaseFunctional Class: MThe phylogenetic pattern of COG1346 is ----k----d-lb-efgh-n------Number of proteins in this genome belonging to this COG is","","Residues 13 to 218 match (4e-53) PD:PD009617 which is described as PROTEOME COMPLETE TRANSMEMBRANE MEMBRANE LRGB INNER YOHK HOLIN-LIKE PREDICTED PROBABLE ","","","","","","","","","","","","Wed Jan 22 09:55:03 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02575 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 12 to 226 (E-value = 1.1e-100) place AA02575 in the LrgB family which is described as LrgB-like family (PF04172)","","","","","","","","1","","","" "AA02576","1794988","1794581","408","ATGTATCGGAAAGTTTTTGACTTAGCAAGATCGTTACTCCTGTTATATTTCATGCTGTATTTGGGCGGGCTTACCGCGCATTTTGTTCCCATTGGCATTCCCTCCAGTATTTGGGGATTATTGTTGCTCTTTACGTGCTTAATTACGCGCATTATCAAAATCGAATGGGTGATGTTTTTCTCTAATTTTCTGGTTCGTTATATGGCACTGTTGTTCGTGCCGGTCAGCGTTGGGATCATTAAATATTCCGGGCTGCTTATGGATCAAATGAAAGTATTATTGTTGCCGAATATCGTCAGCACCTGCATAACCCTTGTAGTGATCGGTTTGTTTTCCGATTATTTGTTCTCACTGAAATCCTTTAGCCGTTTAAAACGCAAAGTCATCAAAAAAAGAGCAAAGGGGGAA","","","15633","MYRKVFDLARSLLLLYFMLYLGGLTAHFVPIGIPSSIWGLLLLFTCLITRIIKIEWVMFFSNFLVRYMALLFVPVSVGIIKYSGLLMDQMKVLLLPNIVSTCITLVVIGLFSDYLFSLKSFSRLKRKVIKKRAKGE","1794579","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR005538
Family
LrgA
PD009239\"[40-116]TY880_PASMU_Q9CME9;
PF03788\"[8-117]TLrgA
noIPR
unintegrated
unintegrated
signalp\"[1-26]?signal-peptide
tmhmm\"[12-30]?\"[36-54]?\"[64-84]?\"[98-118]?transmembrane_regions


","No hits to the COGs database.","","Residues 26 to 107 match (9e-15) PD:PD009239 which is described as COMPLETE PROTEOME MEMBRANE TRANSMEMBRANE HYDROLASE LRGA MUREIN INNER HOLIN-LIKE YOHJ ","","","","","","","","","","","","Wed Jan 22 09:58:30 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02576 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 117 (E-value = 5e-40) place AA02576 in the LrgA family which is described as LrgA family (PF03788)","","","","","","","","1","","","" "AA02577","1795407","1795904","498","ATGACCGCACTTTTAGCGCCGTTATCAATTATGCGACAAGGATTTTTCTGCATTCTGCTGGTATTGCTCCCCTTCACCGTTCACGCCCACACGTTAGCCTGTCGCGTTGTCGGCATCAGTGATGGTGACAGTTTTACCTGCTTAACAGGCAATCATAAACAAATCAAAGTGCGTTTGGCGGAAATTGATGCGCCCGAACACAATCAGCCATTCGGCAAGAAATCCCGTCAAATGCTCGCGTCATTGATTCATCAACGTGAGATCAAACTGGAGATTTCCGGCGAGGATCGCTATCATCGCAAGTTAGCCATCGCGTATGATGCGCAAGGGCAAAACGTTAATTTAATCATGGTCCAACAGGGCATGGCGTGGGCCTATAAACAATATGTTCAGGATCCCGTTTATCGCGAAGCGGAACAACGGGCAAAAAAACGGCGTATCGGCTTATGGCAGGATCGTCATCCCATCGAACCGCACTTATGGCGTCAACAAAGAAGG","","","19279","MTALLAPLSIMRQGFFCILLVLLPFTVHAHTLACRVVGISDGDSFTCLTGNHKQIKVRLAEIDAPEHNQPFGKKSRQMLASLIHQREIKLEISGEDRYHRKLAIAYDAQGQNVNLIMVQQGMAWAYKQYVQDPVYREAEQRAKKRRIGLWQDRHPIEPHLWRQQRR","1795902","","nuclease","Periplasm, Inner membrane, Cytoplasm","","
InterPro
IPR006021
Domain
Staphylococcus nuclease (SNase-like)
PF00565\"[30-152]TSNase
SM00318\"[30-152]TSNc
PS50830\"[30-152]TTNASE_3
noIPR
unintegrated
unintegrated
G3DSA:2.40.50.90\"[23-159]Tno description
signalp\"[1-29]?signal-peptide
tmhmm\"[15-33]?transmembrane_regions


","BeTs to 11 clades of COG1525COG name: Micrococcal nuclease (thermonuclease) homologsFunctional Class: LThe phylogenetic pattern of COG1525 is -om-k-yq----b--f-h-nuj---wNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-15) to 4/4 blocks of the IPB002071 family, which is described as \"Thermonuclease family\". Interpro entry for IP:IPR002071. IPB002071A 36-47 1 IPB002071B 56-66 0.00043 IPB002071C 96-106 0.1 IPB002071D 139-151 0.0023","","","","","","","","","","","","","Wed Jan 22 10:03:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02577 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 30 to 152 (E-value = 2.4e-38) place AA02577 in the SNase family which is described as Staphylococcal nuclease homologue (PF00565)","","","","","","","","1","","","" "AA02579","1795913","1797106","1194","ATGAATTTTGATCCCGTGATATTTCGTCAATATTTTCCTTATCTCCATTCCGATGCTGTGGTCTATTTAGATAACGCGGCGACCACACTGAAACCGCGGTGTTTAATTGATGCAACGGTGGATTTTTATCAATCCGCCGGTTCTGTCCATCGTAGCCAATATGATGAAAAACAGACCGCACTTTACGAACAGGCACGTACGCGGGTGAAGCAGTTGATTAACGCAGAAGACGAACGGGCGGTGGTTTGGACATCCGGCACGACGCAGGCGATTAACACGGTGGCAAACGGTTTACTACCACATTTACAAGCCGGCGATGAAATCATTATTAGTGAAGCGGATCATCACGCCAATTTTGTGACCTGGCATGAAATTGCCGAAAAAAGCGGCGCTAAAATTCATGTTTTGCCCATTGGTGATGATTGGTTGATTGATGCCGAGGCGTTACGGGAAAAACTCAATTCACGCACAAAATTGGTGGCGTTAAATTTTGCGTCGAACGTTACCGGCACGCAGCAAGCGGTAAAACAACTGATTCAGCGCATTCGTGCCAACAGTTCGGCGTTGATCTTGCTTGACGCCGCGCAGGCGATTAGCCACATAAAAATCGATTTGGCAGAACTCGACGCGGATTTTATCGCGTTTTCCGCCCATAAAATTTATGGTCCGACGGGGCTTGGTGTGCTCAGTGGGAAGTTATCCGCACTGGATTTACTGCAACCGTTGCAATACGGCGGCAAAATGATCAATAAAGTCAGTAAACAACAAATTACCTTTGCCGAATTGCCTTATCGTTTGGAAGCCGGCACGCCGAATATTGCCGCCGTTATCGGTTTCAACGCGGTGTTGGAATGGCTGGCACAATGGGACATCGGCGACATGGAAGAAACCGCCGTGCATTTGGCGGAAATCACCCGCCGTCGTTTGAGCGGTTATGCGCAATGTAAACTGTTTAACTCCCCGCAACCGAGTTCCGTGGTCAGCTTTATTTTTGGAGACGTCAACGCGTCCGATTTAGCCACATTGCTGGCGGAACAAAATATCGCGCTACGGGTCGGCGAGCACTGTGCCCAGCCTTATTTGGCACGCTTAGGACAAACCGCCACCTTGCGCTTGTCTTTTGCGCCGTACAACATAGAAGCGGAAGTAGATACTTTCTTCAACGCGTTAGATAAAGCCTTGGCATTATTACGA","","","45972","MNFDPVIFRQYFPYLHSDAVVYLDNAATTLKPRCLIDATVDFYQSAGSVHRSQYDEKQTALYEQARTRVKQLINAEDERAVVWTSGTTQAINTVANGLLPHLQAGDEIIISEADHHANFVTWHEIAEKSGAKIHVLPIGDDWLIDAEALREKLNSRTKLVALNFASNVTGTQQAVKQLIQRIRANSSALILLDAAQAISHIKIDLAELDADFIAFSAHKIYGPTGLGVLSGKLSALDLLQPLQYGGKMINKVSKQQITFAELPYRLEAGTPNIAAVIGFNAVLEWLAQWDIGDMEETAVHLAEITRRRLSGYAQCKLFNSPQPSSVVSFIFGDVNASDLATLLAEQNIALRVGEHCAQPYLARLGQTATLRLSFAPYNIEAEVDTFFNALDKALALLR","1797104","From Genbank:[gi:13431395] This protein catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine and L-selenocystine to produce L-alanine. ","aminotransferase nifS protein","Cytoplasm","","
InterPro
IPR000192
Family
Aminotransferase, class V
PF00266\"[21-386]TAminotran_5
InterPro
IPR015421
Domain
Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10\"[19-289]Tno description
noIPR
unintegrated
unintegrated
PTHR11601\"[20-398]TCYSTEINE DESULFURYLASE


","BeTs to 17 clades of COG0520COG name: Selenocysteine lyaseFunctional Class: EThe phylogenetic pattern of COG0520 is -om-kz--vdrlbcefghs-uj-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 8.5e-12) to 2/2 blocks of the IPB000192 family, which is described as \"Aminotransferase class-V\". Interpro entry for IP:IPR000192. IPB000192A 21-29 6.8e-05 IPB000192B 218-227 4.1e-05","Residues 145 to 193 match (4e-08) PD:PD558816 which is described as PROTEOME COMPLETE LYASE PYRIDOXAL PHOSPHATE TRANSFERASE CYSTEINE 4.4.1.- SYNTHASE CYSTATHIONINE ","","","","","","","","","","","Wed Jan 22 11:12:31 2003","Wed Jan 22 10:15:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02579 is paralogously related to AA00708 (2e-21) and AA00084 (6e-04).","","","","","","Residues 30 to 386 (E-value = 2.3e-12) place AA02579 in the Aminotran_5 family which is described as Aminotransferase class-V (PF00266)","","","","","Ouzounis C, Sander C.Homology of the NifS family of proteins to a new class of pyridoxal phosphate-dependent enzymes.FEBS Lett. 1993 May;322(2):159-64.PMID: 8482384","","Wed Jan 22 10:19:40 2003","1","","","" "AA02581","1797106","1797483","378","ATGAATATCGAACAACAGTTAATCACCGCTAAGAATTGGGAAGATCGCTATCGCTTAATTATTCAGGCGGGGAAAAATCTTCCCGAACCCAGCGAAGAAGCCTTGGTAGCCATGGAAACCATTCCGGGCTGCGAACTGCAGGTGTGGTTTAAATCCATCGAAAAAAATGACCGCACTTTTCACTTTGAGGCTTACAGCGAAGCACGCATCATGAACGGCTTGCTGTGGATTTTATTGCAGCGTATTGACAATCAACCAGCGGAAGCCTTACACCAATTTGATTTGACGGCGTATTTCAAGGAATTAGGCATTGCGCAGCGGTTGAGCTCTACCCGTTTAAATGGCTTAAAACACATTGAAGGGATTTTGCACAATCTA","","","14632","MNIEQQLITAKNWEDRYRLIIQAGKNLPEPSEEALVAMETIPGCELQVWFKSIEKNDRTFHFEAYSEARIMNGLLWILLQRIDNQPAEALHQFDLTAYFKELGIAQRLSSTRLNGLKHIEGILHNL","1797481","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003808
Family
Fe-S metabolism associated SufE
PF02657\"[3-124]TSufE
noIPR
unintegrated
unintegrated
G3DSA:3.90.1010.10\"[1-124]Tno description


","BeTs to 8 clades of COG2166COG name: SufE protein probably involved in Fe-S center assemblyFunctional Class: RThe phylogenetic pattern of COG2166 is ---------dr--cefghs--j-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.5e-32) to 3/3 blocks of the IPB003808 family, which is described as \"UPF0050_DUF\". Interpro entry for IP:IPR003808. IPB003808A 13-50 2.5e-15 IPB003808B 62-79 6.2e-08 IPB003808C 98-119 3.3e-06","Residues 3 to 126 match (1e-41) PD:PD008198 which is described as PROTEOME COMPLETE SUFE CENTER ASSEMBLY FE-S PROBABLY INVOLVED HI1293 STY1749 ","","","","","","","","","","","","Wed Jan 22 11:16:01 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02581 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 124 (E-value = 1e-40) place AA02581 in the SufE family which is described as Fe-S metabolism associated domain (PF02657)","","","","","","","","1","","","" "AA02584","1798789","1797533","1257","ATGAACATCGCTTCGTTAAATGTGCCGGTGCAATTGCTGGGCTTAACCGGTCAGGATGAAGCGGGCGCGGCGTTAACCTCATTATTACAACAACAAAAAATCGCTTGCGACTTCGTACAGCTTGCTACCCACCCGACAATTACCAAATTGCGTATTTTGTCCCGCCATCAACAATTATTACGCCTTGATTTTGAAGAAGATTTCCAGAACATGACAAGTGCGGATTTGCTGAAAAAACTAGAAAGTGCGGTCAAAAATTACGGCGCTTTGATCTTGTCCGATTACGGCAAAGGCACATTAAATGAAGTACAAAAAATGATCCAAATTGCCCGTAACGCCAATGTGCCGGTGCTCATCGATCCGAAAGGGACGGATTTTGAACGCTATCGCGGTGCGACCTTATTAACGCCGAATATGTCCGAATTTGAAGCGGTTGTGGGTAAATGTCATTCTGAGCAGGAAATTATCGACAAAGGGTTGAAACTCATTTCGGAGATAAATTTGACCGCACTTTTAGTGACCCGTTCGGAAAAAGGTATGACGCTGTTGCGTCCGAACCAGCCTGTGTATCACCTGCCGACGGAGGCCAAAGAAGTTTTTGATGTGACAGGGGCGGGAGACACCGTGATTAGTGTGTTGGCGACAGCATTGGCGGACGGTCGCAGTTTTGAAGAAGCCTGTTACTTAGCCAATGTCGCCGCCGGTATCGTCGTGGGCAAATTGGGCACGTCAACGGTTTCAACCGTGGAACTGGAAAATGCCATTCATGGCAGAACCGGCACCGGCTTTGGCGTAATGACCGAAGCGGAACTGAAAGAGGCCGTTAAACTGGCGAAAGATCGTGGTGAAAAAATCGTCATGACTAACGGTTGTTTTGATATTTTGCATCCCGGTCATGTGTCGTATTTGGATAATGCCCGTAAATTTGGCGATCGCCTGATTGTTGCGGTGAATACGGACGATTCGGTAAAACGCCTAAAAGGCGAGGAGCGTCCGATCAATAATTTGGCTTCCCGCATGGCGGTGCTTGCCGGGCTTTCTTCTGTGGACTGGTTGGTGCCGTTCGGTGAAGATACGCCACAGCGTTTAATCGGTGAAGTGTTGCCGGATTTATTGGTGAAAGGCGGCGATTACAAGCCGGAAGAGATTGCCGGTAGCAAAGAAGTGTGGGCGAACGGCGGTGATGTAAAAGTGCTGAATTTTGAGAACGGTTTTTCCACCTCAAACGTCATCAAAAAAATTAAACACTTGGAAAAA","","","51794","MNIASLNVPVQLLGLTGQDEAGAALTSLLQQQKIACDFVQLATHPTITKLRILSRHQQLLRLDFEEDFQNMTSADLLKKLESAVKNYGALILSDYGKGTLNEVQKMIQIARNANVPVLIDPKGTDFERYRGATLLTPNMSEFEAVVGKCHSEQEIIDKGLKLISEINLTALLVTRSEKGMTLLRPNQPVYHLPTEAKEVFDVTGAGDTVISVLATALADGRSFEEACYLANVAAGIVVGKLGTSTVSTVELENAIHGRTGTGFGVMTEAELKEAVKLAKDRGEKIVMTNGCFDILHPGHVSYLDNARKFGDRLIVAVNTDDSVKRLKGEERPINNLASRMAVLAGLSSVDWLVPFGEDTPQRLIGEVLPDLLVKGGDYKPEEIAGSKEVWANGGDVKVLNFENGFSTSNVIKKIKHLEK","1797531","","ADP-heptose synthase","Cytoplasm","","
InterPro
IPR004820
Domain
Cytidylyltransferase
PF01467\"[287-413]TCTP_transf_2
InterPro
IPR004821
Domain
Cytidyltransferase-related
TIGR00125\"[285-352]Tcyt_tran_rel: cytidyltransferase-related do
InterPro
IPR011611
Domain
PfkB
PF00294\"[2-250]TPfkB
InterPro
IPR011913
Domain
RfaE bifunctional protein, domain I
TIGR02198\"[1-256]TrfaE_dom_I: rfaE bifunctional protein, doma
InterPro
IPR011914
Domain
RfaE bifunctional protein, domain II
TIGR02199\"[273-416]TrfaE_dom_II: rfaE bifunctional protein, dom
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620\"[283-417]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.40.1190.20\"[1-243]Tno description
PTHR10584\"[1-267]TSUGAR KINASE RELATED


","BeTs to 7 clades of COG2870COG name: ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferaseFunctional Class: MThe phylogenetic pattern of COG2870 is -------q------ef-h-nuj----Number of proteins in this genome belonging to this COG is","","Residues 355 to 414 match (2e-09) PD:PD268681 which is described as PROTEOME COMPLETE TRANSFERASE SYNTHASE AUT RFAE ADP-HEPTOSE BIOSYNTHESIS BLMC /TRANSFERASE ","","","","","","","","","","","","Wed Jan 22 11:18:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02584 is paralogously related to AA00212 (6e-07) and AA02797 (0.001).","","","","","","Residues 287 to 413 (E-value = 5e-22) place AA02584 in the CTP_transf_2 family which is described as Cytidylyltransferase (PF01467)","","","","","Valvano MA, Marolda CL, Bittner M, Glaskin-Clay M, Simon TL, Klena JD.The rfaE gene from Escherichia coli encodes a bifunctional protein involved in biosynthesis of the lipopolysaccharide core precursor ADP-L-glycero-D-manno-heptose.J Bacteriol. 2000 Jan;182(2):488-97.PMID: 10629197","","Wed Jan 22 11:22:36 2003","1","","","" "AA02585","1799153","1798938","216","ATGCCGAGTGCAAGCCAAAAGCCCCAATGTTTGGGATGGAGAAATTCAGTTTTAAAAGTCGGAAGAACGGATTTTGCCATAAAGGAATTACAGGATTATTTCAATTGGTTTAGTTTAGCGGAATTTTTAGGAAATAGCATTTCCCCTGTGGTAGTATTAGCGAAATTTTTTATTCTATATAAGAGAAAATCAAATGGCTCAATATTCTGCACAATT","","","8190","MPSASQKPQCLGWRNSVLKVGRTDFAIKELQDYFNWFSLAEFLGNSISPVVVLAKFFILYKRKSNGSIFCTI","1798938","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
tmhmm\"[42-60]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 16:27:19 2004","Mon Feb 23 16:27:19 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02585 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 16:27:19 2004","","","","","","","","","","","","","1","","","" "AA02586","1799347","1800006","660","ATGGCGATTATTGAAACCGGCATGGCGTGGTTTTGGTCTGATCATCGGATCAAAAAGTGGTCAAAAATTGAAGGTTTGGAATATTTAAAAACGAATTTGCAGGATGGCATTATTTTTGTCGGCGTACATTTTTTAACGCTGGAATTAGGCGCACGTATTGTCGGCATCCATCAACCGGGCATTGGCGTTTATCGCCCGAATGATAATCCGTTATTTGACTGGATACAAACCCAAGGGAGGTTGCGTTCCAACAAAGATATGCTAGATCGCAAAGATTTACGCGGCATGATTAAAGCCATTCGTCACGGTGATATTATCTGGTATGCGCCGGATCATGACTACGGCAGAAAAAATGCGGTCTTTGTGCCGTTTTTCGCCGTTCCTGGCGCAGCAACCACAACGGGCAGCTACTATTTATTGAAGTCTTCACCGAACAGTAAAGTGATTCCTTTTTCACCGTTAAGAAACAAAGATAATTCCGGCTACACGGTTAAAATTTCCCCTCCCGTGGATTTTTCCGATCTGCACACGGAAACGGAAATTGCGACCCGGATGAATCAAATCATTGAAAAAGAAATACTAAACGGTGTGGAACAATATATGTGGATCCATCGCCGCTTTAAAACCCAGCCGAATGAAGAAGATAATTTGTATAAAGAT","","","35752","MAIIETGMAWFWSDHRIKKWSKIEGLEYLKTNLQDGIIFVGVHFLTLELGARIVGIHQPGIGVYRPNDNPLFDWIQTQGRLRSNKDMLDRKDLRGMIKAIRHGDIIWYAPDHDYGRKNAVFVPFFAVPGAATTTGSYYLLKSSPNSKVIPFSPLRNKDNSGYTVKISPPVDFSDLHTETEIATRMNQIIEKEILNGVEQYMWIHRRFKTQPNEEDNLYKD","1800004","","lipid A biosynthesis lauroyl acyltransferase","Inner membrane, Cytoplasm","","
InterPro
IPR004960
Family
Bacterial lipid A biosynthesis acyltransferase
PF03279\"[1-209]TLip_A_acyltrans
InterPro
IPR011920
Family
Lipid A biosynthesis lauroyl (or palmitoleoyl) acyltransferase
TIGR02207\"[1-218]Tlipid_A_htrB: lipid A biosynthesis lauroyl
noIPR
unintegrated
unintegrated
tmhmm\"[120-140]?transmembrane_regions


","No hits to the COGs database.","","Residues 6 to 213 match (3e-104) PD:PD011612 which is described as ACYLTRANSFERASE TRANSFERASE PROTEOME COMPLETE A LIPID BIOSYNTHESIS LAUROYL SHOCK HEAT ","","","","","","","","","","","","Wed Jan 22 11:26:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02586 is paralogously related to AA02504 (3e-18).","","","","","","Residues 1 to 209 (E-value = 8.5e-62) place AA02586 in the Lip_A_acyltrans family which is described as Bacterial lipid A biosynthesis acyltransferase (PF03279)","","","","","Karow,M. and Georgopoulos,C. Sequencing, mutational analysis, and transcriptional regulation of the Escherichia coli htrB gene Molecular microbiology. 5 (9), 2285-2292 (1991) PubMed: 1840644 Karow,M., Fayet,O., Cegielska,A., Ziegelhoffer,T. and Georgopoulos,C. Isolation and characterization of the Escherichia coli htrB gene,whose product is essential for bacterial viability above 33 degrees C in rich media Journal of bacteriology. 173 (2), 741-750 (1991) PubMed: 1846149 Lee,N.G., Sunshine,M.G., Engstrom,J.J., Gibson,B.W. and Apicella,M.A. Mutation of the htrB locus of Haemophilus influenzae nontypable strain 2019 is associated with modifications of lipid A and phosphorylation of the lipo-oligosaccharide J. Biol. Chem. 270 (45), 27151-27159 (1995) PubMed: 7592970 ","","Wed Jan 22 11:27:07 2003","1","","","" "AA02587","1800630","1800070","561","ATGCAGGAAAGTGTGCAATTCAATAATTTTTCTTTGATTAGCCGTTTATTCGGTAATTTATTTTACCGCCAACCGACAGATCCCATTTTATCCGGCGTTTTTGCTTGGTTGCAGCAAGGTAATTTATCCCAAGTCTGGGCGTTAAACGAAGACAGCGACGGTAAAAGCGCATTAGATGCCTTGCAAAGACCTATTGATTTGACATTGTTGAATCAAGAATATCAAAAACTTTTCGGTCAGTCGGGAAGTGTGGCGACACAAATTTCTGCTTATGAGATTTCCATTGAAGATTTTAAGGGTTTTCGGAAAATGCGCAATTTGCCTGAAACGGAAAATATCGATCATTTTGCCATGTTGCTACTGACGGCTTCCTGGTTGGAAGATAACACCGATTCATTGAGCGCCCAACAGGAATTATTTGAGCATTTTCTTCTGCCTTGTGCGGCGAAGTTTTTAGTGAAAGTTGAAAAGCAGGCGACGTTGCCATTTTATCGCGCTCTGGCTTATTTAACCCGTGAAATGCTTTCTGCGATGGCTGATGAGTTGGATTCTGAAGAACTA","","","21328","MQESVQFNNFSLISRLFGNLFYRQPTDPILSGVFAWLQQGNLSQVWALNEDSDGKSALDALQRPIDLTLLNQEYQKLFGQSGSVATQISAYEISIEDFKGFRKMRNLPETENIDHFAMLLLTASWLEDNTDSLSAQQELFEHFLLPCAAKFLVKVEKQATLPFYRALAYLTREMLSAMADELDSEEL","1800068","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR000886
PTM
Endoplasmic reticulum targeting sequence
PS00014\"[184-187]?ER_TARGET


","No hits to the COGs database.","","Residues 8 to 185 match (8e-61) PD:PD016777 which is described as PROTEOME COMPLETE COMPONENT OXIDOREDUCTASE PM0886 YPO3322 YPO2038 STY1174 HI1543 PARAL ","","","","","","","","","","","","Wed Jan 22 11:29:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02587 is paralogously related to AA01141 (6e-07).","","","","","","Residues 33 to 155 (E-value = 1.8e-05) place AA02587 in the TorD family which is described as Cytoplasmic chaperone TorD (PF06192)","","","","","","","","1","","","" "AA02589","1801241","1800633","609","ATGAAGCATTTAATTATTTCTGCACATCCTAATCAACAAAGTTTTAACCGCGCCATCGTGGAACGTATTGTAAAAGCCTCTCATGAATTAGAGGCGGAAACCACTGTTCGGGATTTGTATACATTAAATTTCAATCCCGTTTTGTCTTGGAGTGAATTAAGTGCAGGGCCTGAAGGCATTGTGCCGGCAGAAATTAAATTTGAGCAAAATTTAATTAAAGAAGCGGATTTGATTACCTTGGTCTATCCCCTTTGGTGGATGGGCTTCCCTGCTGTTTTGAAAGGTTATTTGGATCGCGTTCTTAGCTATGGATTTGCATATCAAACGGAAAATGGCGGTTCGGTGGGATTGTTGGGTGATAAAAAAATGCAACATTTTATTACCATGGGCAATAATCTTGAACGCTATCAAAGCATTGCTTTTGATAAAGCACTACAAACCTGTTTAGTTGACGGTTTGTTTAATTTCTGCGGTATTACCGATATTCACCATGATATTTTCGGAGATATTCACTTTCTGGATGAAGCTGGGTATCAGCAGATTTTGAATAATACCGCACAAAAAACACAAGAAAATCTGACCGCACTTTTGGCAAAGGATGGCTCCAAA","","","22820","MKHLIISAHPNQQSFNRAIVERIVKASHELEAETTVRDLYTLNFNPVLSWSELSAGPEGIVPAEIKFEQNLIKEADLITLVYPLWWMGFPAVLKGYLDRVLSYGFAYQTENGGSVGLLGDKKMQHFITMGNNLERYQSIAFDKALQTCLVDGLFNFCGITDIHHDIFGDIHFLDEAGYQQILNNTAQKTQENLTALLAKDGSK","1800631","From PF02525: Flavodoxin-like foldThis family consists of a domain with a flavodoxin-like fold. It includes bacterial and eukaryotic NAD(P)H dehydrogenase. These enzymes catalyse the NAD(P)H-dependent two-electron reductions of quinones and protect cells against damage by free radicals and reactive oxygen species.This enzyme uses a FAD co-factor.","NAD(P)H oxidoreductase","Cytoplasm","","
InterPro
IPR003680
Family
Flavodoxin-like fold
PF02525\"[1-194]TFlavodoxin_2
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.360\"[2-187]Tno description


","No hits to the COGs database.","Significant hit ( 1.1e-20) to 1/1 blocks of the IPB003680 family, which is described as \"NAD(P)H dehydrogenase (quinone)\". Interpro entry for IP:IPR003680. IPB003680 76-107 1.1e-20","Residues 4 to 190 match (2e-71) PD:PD022346 which is described as COMPLETE PROTEOME OXIDOREDUCTASE NADPH PHOSPHODIESTERASE QUINONE DEHYDROGENASE REDUCTASE ACYL CARRIER ","","","","","","","","","","","Wed Jan 22 13:13:08 2003","Wed Jan 22 11:30:49 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02589 is paralogously related to AA02024 (0.001).","","","","","","Residues 1 to 194 (E-value = 7.9e-70) place AA02589 in the Flavodoxin_2 family which is described as Flavodoxin-like fold (PF02525)","","","","","Li R, Bianchet MA, Talalay P, Amzel LM.The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction.Proc Natl Acad Sci U S A. 1995 Sep;92(19):8846-50.PMID: 7568029","","Wed Jan 22 13:09:24 2003","1","","","" "AA02590","1801702","1801253","450","TTGGGTATGGAATGGTTAGCAGATTGGGGCGTTTGGCACTGGCTTATTCTTGGTTTTATCTTGCTCATTGCTGAAGTTGTCATTCCCGGTGTTTTTCTTCTATGGTGGGGATTAGCCGCCATCGTTGTTGCCGGTATCATGAAATTTATTCCCGCCTTACCACTTTCGGCATTGGCGGTAATTTATGCGGTTATCGCCATTATTCTTAGTATTATTTGGTGGCGCTATCAACACGGTAAGGATCAAATTGATCAATCGAAATCTGTCCTCAATCAACGGGATCATGCCATGATAGGGGTGCAGGGAAAAGTCTTAACTATTGCCGAAAACGGCATTGGTAGAGGCGCTTTCGGTGATACTACGTGGAGAATCCAGGGGCGTGATTTAGCAGTGAATGATATTGTTGAAGTTGTTTCTGTTGATAGCATCACATTGAAAGTTAAGAAAATT","","","16622","LGMEWLADWGVWHWLILGFILLIAEVVIPGVFLLWWGLAAIVVAGIMKFIPALPLSALAVIYAVIAIILSIIWWRYQHGKDQIDQSKSVLNQRDHAMIGVQGKVLTIAENGIGRGAFGDTTWRIQGRDLAVNDIVEVVSVDSITLKVKKI","1801251","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR002810
Family
Nodulation efficiency, NfeD
PF01957\"[13-150]TNfeD
noIPR
unintegrated
unintegrated
signalp\"[1-44]?signal-peptide
tmhmm\"[10-32]?\"[34-52]?\"[58-76]?transmembrane_regions


","BeTs to 10 clades of COG1585COG name: Membrane protein implicated in regulation of membrane protease activityFunctional Class: N,OThe phylogenetic pattern of COG1585 is --m-k---vdr--cefghs--j----Number of proteins in this genome belonging to this COG is","","Residues 90 to 150 match (6e-17) PD:PD332302 which is described as PROTEOME COMPLETE TRANSMEMBRANE MEMBRANE MLR3022 IMPLICATED PM0888 REGULATION PROTEASE PLASMID ","","","","","","","","","","","","Wed Jan 22 13:14:39 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02590 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02591","1802646","1801723","924","ATGTATTTTTTAGATGGCCTACCAATTGTTTCCATTATTTTTATCGTACTTGTCGGTGTTGTGCTTTATTCAACATTGAAAACGGTGCCACAAGGTTATAACTGGACGATTGAACGTTTTGGTCGTTATACCCGTACATTAATGCCGGGATTAAATTTTATCGTTCCATTTGTTGATCGTGTTGGTCGTAAAATCAATATGATGGAACAAGTGTTAGACATCCCATCCCAAGAAGTTATTTCAAAAGATAATGCGAATGTCGCTATTGATGCGGTATGTTTCGTTCAGGTTATTGATGCGCGTAATGCCGCTTATGAAGTGAATCACTTAGAACAAGCTATTATCAATCTTACTATGACAAACATTCGTACGGTTTTAGGTTCCATGGAGTTGGATGAGATGCTATCTCAGCGCGATTCCATTAATAGTCGTTTGTTATCTATTGTAGATGAAGCGACAAATCCTTGGGGGATTAAAGTGACCCGTATTGAAATCCGAGATGTGCGTCCGCCACATGAATTGATCGCCGCGATGAATGCTCAAATGAAAGCTGAACGTAATAAACGTGCAGATATTTTGGAGGCGGAAGGTGTGCGTCAGGCTGAAATTTTACGCGCAGAAGGTGAAAAACAATCCCGTATTTTAAAAGCGGAAGGGGAACGTCAGGAAGCCTTCTTACAAGCTGAAGCCCGCGAACGTGCCGCGGAAGCGGAAGCGAAGGCGACCCAAATGGTATCCGATGCGATCGCTAATGGTGACACGAAAGCTATTAATTACTTTATTGCGCAAAAATATACTGAAGCGCTAAAAGAAATTGGTGGTTCGGATAATAGTAAAGTCGTGCTGATGCCTTTAGAAGCCGGCAACTTAATCGGTTCCATTGCCGGTATTACCGAATTATTAAAAACCGATAAAAAAGTAAAT","","","34293","MYFLDGLPIVSIIFIVLVGVVLYSTLKTVPQGYNWTIERFGRYTRTLMPGLNFIVPFVDRVGRKINMMEQVLDIPSQEVISKDNANVAIDAVCFVQVIDARNAAYEVNHLEQAIINLTMTNIRTVLGSMELDEMLSQRDSINSRLLSIVDEATNPWGIKVTRIEIRDVRPPHELIAAMNAQMKAERNKRADILEAEGVRQAEILRAEGEKQSRILKAEGERQEAFLQAEARERAAEAEAKATQMVSDAIANGDTKAINYFIAQKYTEALKEIGGSDNSKVVLMPLEAGNLIGSIAGITELLKTDKKVN","1801721","","conserved hypothetical protein (possible membrane protein)","Inner membrane, Cytoplasm","","
InterPro
IPR001107
Family
Band 7 protein
PF01145\"[25-199]TBand_7
SM00244\"[24-182]TPHB
InterPro
IPR001972
Family
Stomatin
PR00721\"[79-100]T\"[114-131]T\"[134-157]T\"[158-176]T\"[177-198]TSTOMATIN
PS01270\"[138-166]TBAND_7
noIPR
unintegrated
unintegrated
PTHR10264\"[3-301]TSTOMATIN-RELATED
signalp\"[1-23]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","BeTs to 24 clades of COG0330COG name: Membrane protease subunits, stomatin/prohibitin homologsFunctional Class: OThe phylogenetic pattern of COG0330 is aompkzyqvdrlbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-81) to 5/5 blocks of the IPB001972 family, which is described as \"Band 7 protein family/Stomatin\". Interpro entry for IP:IPR001972. IPB001972A 26-42 1.1e-05 IPB001972B 65-95 1.1e-14 IPB001972C 103-152 1.3e-23 IPB001972D 153-198 1.1e-28 IPB001972E 209-224 0.0013 IPB001972E 198-213 0.0097","Residues 244 to 287 match (2e-10) PD:PD391641 which is described as PROTEOME COMPLETE MLR3021 LIKE YCAD XF0185 STOMATIN ","","","","","","","","","","","","Wed Jan 15 16:35:33 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02591 is paralogously related to AA02363 (3e-12) and AA02365 (8e-12).","","","","","","Residues 26 to 199 (E-value = 1.3e-75) place AA02591 in the Band_7 family which is described as SPFH domain / Band 7 family (PF01145)","","","","","","","","1","","","" "AA02592","1803989","1803171","819","ATGAGAAACAAGATTCAATTTTTGATGCTATTTAGCATATTTTTTCTTATATCTACATTTTTTTATAGAGTGGCCTTTGCAGTTCCTTCAAAAAATGGTAACTATGGCGTATTTCTTGGTATTAATGGAAATGAAGAAGATAAATTGCAAGGATACAATATTGTTGTAATCGATTCTGCTATGTTTCAACCTTCTCAAGTGGAGAAATTACATGCTTCAGGGAAAACTGTGTATGGGTATATTAATATTGGAGCAATTGAGAAACACCGCCCGTATTATAGTCATTTTCAGTCAGTCATGCTTGGTATCTATGAAACTTGGCCGGATGAGCGATGGGTTGATGTATCCTCTCCGGTATGGCAGCGTTTTATCGTTAATGAGCTAGGAAAAAAGTATGCTGATATGGGGTTGGATGGTTTTTTTCTTGATAATGCAGATGTTTATTATCATTATCAAACAAATGAGATATTTCAAGGGCTTGTAACAATTTTGACTGGGCTTCGATATTATAATATTCCACTTATTATTAATGGAGGGGATCTTTTTGTAAAAAAATGTATTAATCAAAATACCGTTTTAATTGATGGTATTAACCAAGAAAGTGTTTTTACCACTATTGATTTTAATAAAAAAAAATATGGAATCCAGCAGAAATCGGAAACAACCTATTTTCAAAAATATCTGGCATATGTTAAGGCTCATGGATTATCTGTCTATTTACTTGAATATAATGCAAGTAAGGAACTGTCAAAAAAAATTGACAAATATGCAAATGAAAATGGCTTTCTTTGGTATAACGCGAAGGGATTAGAGCTTCGG","","","31642","MRNKIQFLMLFSIFFLISTFFYRVAFAVPSKNGNYGVFLGINGNEEDKLQGYNIVVIDSAMFQPSQVEKLHASGKTVYGYINIGAIEKHRPYYSHFQSVMLGIYETWPDERWVDVSSPVWQRFIVNELGKKYADMGLDGFFLDNADVYYHYQTNEIFQGLVTILTGLRYYNIPLIINGGDLFVKKCINQNTVLIDGINQESVFTTIDFNKKKYGIQQKSETTYFQKYLAYVKAHGLSVYLLEYNASKELSKKIDKYANENGFLWYNAKGLELR","1803169","","conserved hypothetical protein","Outer membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-27]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 3.1e-05) to 2/10 blocks of the PR01545 family, which is described as \"Thermotoga maritima hypothetical protein TM1410 signature\". Prints database entry for PR:PR01545. PR01545C 74-93 0.0085 PR01545F 130-149 1.9","Residues 151 to 272 match (5e-12) PD:PD556339 which is described as RELATED POSSIBLE ENDO PROTEOME ALPHA-14 GLUCANOTRANSFERASE COMPLETE TRANSFERASE POLYGALACTOSAMINIDASE ","","","","","","","","","","","","Wed Jan 15 16:39:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02592 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02593","1804198","1804686","489","ATGAAATTAAAAGTTTTAGCGTTAGCAATAATTACTGCCTTATCAACGGGAAGCATTCAGGCTGCCTCCAATACTGACAGTGAGTCTAACCAATCAGTAAAAAATAGCAGTCTATATTTAAAAACATTTAAAAGTAAATATTCTGCAGAGAACACTATTTCAAAAATCCGGCAAGCTTTGAATGATAAGAACATAAAAATATTCACGATAATTGACCATCAAGCTGCAGCAAAAGAAGCTGGATTGAGCATGCCGTTTTCAAGTGTAATTGTTTTTGGAAAACCGCAACTAGGTACCCCAATGATGATTGAATCCCCAACCCTAGCTATTGATTTACCATTAAAAGCTTTAGTATGGGAGAATAGCCAAGGTGAAATATTCGTAAGTCTAAATAGAAATGAGATTATAGCAGAAAAACATAATGTCACGGCAGGGAATGTAGAAAAAATGAATAAACTGGTGAAGTTAATAACTGAAAGTGTTACTGAA","","","17749","MKLKVLALAIITALSTGSIQAASNTDSESNQSVKNSSLYLKTFKSKYSAENTISKIRQALNDKNIKIFTIIDHQAAAKEAGLSMPFSSVIVFGKPQLGTPMMIESPTLAIDLPLKALVWENSQGEIFVSLNRNEIIAEKHNVTAGNVEKMNKLVKLITESVTE","1804686","","conserved hypothetical protein (exported protein)","Periplasm, Cytoplasm","This sequence is similar to gi|33601378, a predicted exported protein from Bordetella bronchiseptica RB50. See also gi|33595992 from Bordetella parapertussis.","
InterPro
IPR005180
Domain
Protein of unknown function DUF302
PF03625\"[40-160]TDUF302
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide
tmhmm\"[5-23]?transmembrane_regions


","BeTs to 3 clades of COG3439COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG3439 is -o-p---q-----------n----t-Number of proteins in this genome belonging to this COG is","","Residues 44 to 142 match (1e-17) PD:PD332406 which is described as COMPLETE PROTEOME EXPORTED MEMBRANE INNER OR ST1815 INTEGRAL PERIPLASMIC SSO0995 ","","","","","","","","","","","","Mon Feb 23 16:25:10 2004","Mon Feb 23 16:25:36 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02593 is paralogously related to AA00696 (7e-04).","Mon Feb 23 16:24:57 2004","","","","","Residues 40 to 160 (E-value = 7.8e-20) place AA02593 in the DUF302 family which is described as Domain of unknown function DUF302 (PF03625)","","","","","","","","1","","","" "AA02594","1805184","1804765","420","ATGAAAGAAGTTCTTAGAAAGTTTTGCCTTTCTAATATTGATATTACCGTATTAAGATTTTCAGTTGTTTTTATTATCGCATTATTTGGTAACTATAAATGGTTTGATTTTGAGGTAGAGGCCTTAAAACCTTTAATATCTCCAACATGGCTAAGTTTTTTATATGAATTTTTGGGATTTCATGGGACTAGTTATTTGCTAGGCTTTATTGAAAGCGTTACTTATATTTTCTTAGTTGTTGGTATTTTTAAACCTAAGTTTGGCGTACTTGGTAGCTTGTTTACTATCGCTCTTGGCGTAGTAACACTTAGCCTTATACCTCAAATTGGTGTTAATGGTTTTATTATTAAAGATATTATACTTATTGGCTCCGGTCTTGTGTTGTTAAAACACGACCTAAATAAAATTCCATTTGTTAAA","","","17265","MKEVLRKFCLSNIDITVLRFSVVFIIALFGNYKWFDFEVEALKPLISPTWLSFLYEFLGFHGTSYLLGFIESVTYIFLVVGIFKPKFGVLGSLFTIALGVVTLSLIPQIGVNGFIIKDIILIGSGLVLLKHDLNKIPFVK","1804763","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR007339
Family
Protein of unknown function DUF417
PF04224\"[1-137]TDUF417
noIPR
unintegrated
unintegrated
tmhmm\"[15-35]?\"[62-82]?\"[87-107]?\"[113-128]?transmembrane_regions


","No hits to the COGs database.","","Residues 1 to 133 match (1e-27) PD:PD175813 which is described as PROTEOME COMPLETE F200 PM1931 ","","","","","","","","","","","","Wed Jan 15 16:57:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02594 is paralogously related to AA01162 (5e-05).","","","","","","Residues 1 to 137 (E-value = 1.1e-45) place AA02594 in the DUF417 family which is described as Protein of unknown function, DUF417 (PF04224)","","","","","McCormack EA, Rohman MJ, Willison KR.Mutational screen identifies critical amino acid residues of beta-actin mediating interaction between its folding intermediates and eukaryotic cytosolic chaperonin CCT.J Struct Biol. 2001 Aug;135(2):185-97.PMID: 11580268","","Wed Jan 15 16:57:15 2003","1","","","" "AA02595","1805881","1807170","1290","ATGGAAAAATTATTGGCTGAAGGTAGTTACTCTGCCGAGCAACAAAAAATCGCAAAAGTCTTTTTTAACAACGGCTGCCAGTACTGTCATACACCAAATGCAGAACTCCCCTTTTATGCCCATGTTCCGTTAGTTGGCTCCATGTTGCAAAATGACATCAAAGAAGGCAACCGCGTATTCCTGTTAAATGAGTTACTGAACGGCTTAAAAGATCCAAGCAAATTATCGGAAGTGGATTTGGCAAAACTTGAACGGGTTATTGAAAATGACGAAATGCCGATTGCCAAGTTTCTTCATATTCACTGGGGAAGCCGCCCTGATGAAGATGAAAAAACCGCATTGCTAAACTGGATTCGCGAACAACGGAAAGCCTTTTTACCGGTAAATACCGAAGGCACGGACAACCACCGTTTAGTTCAACCGATTCCTGATGAAATCATGACCGATGCGGCAAAAGTTGCTCTTGGGCATAAACTGTTTATGGATGGTCGTTTATCCGGCGATGGTACGATTAAATGTCACACCTGCCACCAACTGGACAAAGGCGGTGTTGACCGTTTAGATACATCCACCGGCATTGATGGCAAAAAAGGCGGCATTAACGCGCCGACTGTCTTCAACGCCGCATTTAACTTCGCACAATTCTGGGATGGGCGTGCCGTGGATTTAGCCGATCAAGCCGGCGGACCGCCATTAAATCCGGTAGAAATGGGTTCCCATTCCTGGGAAGAAATTGTGGCACGATTTGAGCAGGATGAAGATTTTAAACAAGCGTTCTTACAAGTCTATCCGCAAATCAGCAAAGAAACCCTCACCAATGCTATCGGTGAATATGAAAAAACCTTAATTACGCCGAACAGCGATTTTGACCGCTATCTGAAAGGCGAAAACACATTAACCGCGCAACAACTTAAAGGTTACGAGCTATTTAAACAGTACAAATGCGACACCTGCCACACTGGCGTGAACATGGGCGGACAATCTTACGAATACATGGGTATCTACGGCGATTATTTCAAAGATCGCGGCACACCGCTCACTGATGCCGACCAAGGTCGTTTCGCACAAACTCAAGATCCGTATGATATGCACCGTTTCAAAGTGCCATCACTGCGCAATATTGCGTTAACGGCGCCTTATATGCACGATGCGTCGGCAAAAGATCTGAAAGAAGCCGTTCGTATCATGTTGAAATATCAAAGCAATGCTAAACCGCAGCAACAAGACATTGATGACATTACGTCCTTCTTGGAAAGTCTCACCGGCGAGTTTGAAGGCAAAAAATTACAA","","","51719","MEKLLAEGSYSAEQQKIAKVFFNNGCQYCHTPNAELPFYAHVPLVGSMLQNDIKEGNRVFLLNELLNGLKDPSKLSEVDLAKLERVIENDEMPIAKFLHIHWGSRPDEDEKTALLNWIREQRKAFLPVNTEGTDNHRLVQPIPDEIMTDAAKVALGHKLFMDGRLSGDGTIKCHTCHQLDKGGVDRLDTSTGIDGKKGGINAPTVFNAAFNFAQFWDGRAVDLADQAGGPPLNPVEMGSHSWEEIVARFEQDEDFKQAFLQVYPQISKETLTNAIGEYEKTLITPNSDFDRYLKGENTLTAQQLKGYELFKQYKCDTCHTGVNMGGQSYEYMGIYGDYFKDRGTPLTDADQGRFAQTQDPYDMHRFKVPSLRNIALTAPYMHDASAKDLKEAVRIMLKYQSNAKPQQQDIDDITSFLESLTGEFEGKKLQ","1807168","","cytochrome c peroxidase","Periplasm, Cytoplasm","","
InterPro
IPR004852
Domain
Di-haem cytochrome c peroxidase
PF03150\"[121-300]TCCP_MauG
InterPro
IPR009056
Domain
Cytochrome c, monohaem
PS51007\"[12-122]T\"[151-253]T\"[301-421]TCYTC
InterPro
IPR012282
Domain
Cytochrome c region
G3DSA:1.10.760.10\"[139-303]Tno description


","No hits to the COGs database.","","Residues 271 to 398 match (2e-09) PD:PD579584 which is described as COMPLETE PROTEOME PROBABLE PLASMID LIPOPROTEIN UTILIZATION METHYLAMINE TRANSMEMBRANE ATU2792 PEPTIDE ","","","","","","","","","","","","Wed Jan 15 16:56:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02595 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 121 to 300 (E-value = 3.5e-91) place AA02595 in the CCP_MauG family which is described as Di-haem cytochrome c peroxidase (PF03150)","","","","","Wilming M, Iffland A, Tafelmeyer P, Arrivoli C, Saudan C,Johnsson K. Examining Reactivity and Specificity of Cytochrome cPeroxidase by using Combinatorial Mutagenesis. Chembiochem. 2002 Nov 4;3(11):1097-104. PMID: 12404635 Rosenfeld RJ, Hays AM, Musah RA, Goodin DB. Excision of a proposed electron transfer pathway incytochrome c peroxidase and its replacement by aligand-binding channel. Protein Sci. 2002 May;11(5):1251-9. PMID: 11967381","","Wed Jan 15 16:56:44 2003","1","","","" "AA02597","1808418","1807264","1155","ATGCCTCAACTTAAAAAAGAAGTTCAAAATCCACCGCACTTTTCGGTGGTGACCGATGATGCTGAATTGGCGCGGGTATGTCAGGCGGCACGACAGCAAAGTGCGGTCGCGTTAGACACTGAATTTGTGCGGGTACGAACCCTGTATCCGAAACTCGGTTTAATTCAGATGTATTTCGGCGATCGGGTGGCGTTAATCGATCCCTTACCGATTCAGGATTTTTCGCCGTTCATTAAATTGCTTGCAGATACTAATTTGGTCAAAATTCTGCATGCTTGTAGCGAAGATTTAGACGTATTCCAGCATTATTTTCAGCAGCTGCCGCGCCCGATGTGTGATACACAAGTGATGGCGCATTTTCTCGGCTTTGCCGGCTCCACCGGTTTCGCTACCTTGGTGCAACATTATTTCCAAATTGAAATCGACAAAGGCGCCTCCCGTACCGATTGGCTGGCACGCCCGTTATCGGATACGCAGCTGCAATATGCGGCGGCGGATGTATGGTATTTGTTGCCGTTATATGAACAAATGCAACAACAGCTTACGCAAACCGAGTGGCAAAGTGTGGTGGAAAATGAATGTGAATTTTTATTGAACAAGCGGGCGCAGACAACCAAAGATCCCGATAGCGCTTATTTCGCTATTCCCAACGCATGGAAATTGAACCGATTGGAATTAATGCGCCTAAAACTGCTGGCTAAATGGCGTATGGAAGAGGCGATGAAGCGCGATCTTGCACTAAATTTTGTGGTGCGCGCAGAAAATTTATGGCAGGTGGCAAAAAGCAATCCGAAGCATATTTCTACATTGCCGGAACTGGGTTTAAGCACAGCGGAAGTGCGTATTCACGGTAAGAAATTGCTACAAATTATCGATCAGGTTAAACGTATCGTGCCCGAAGATTACCCGCCGCCGATTCAACGGCTCGCCGATGATCCGCGTTACAAAGCCATATTGAAAGCCTTGCAACAACATTTAATCCAAATTACCCCGCCGAATTTAGCGAAGGAACTTATCGCCGGCAAACGTCATTTGGAAAGTCTGATGAAATGGCATTGGTTAAAAAATAGTGAAGATGATTTGCCAGAGCTGCTGACGGGGTGGCGTAAGCCTTTTGGTGAGAAGTTGCTGGCGGCATTGAAAGCCTTTGATGAA","","","44405","MPQLKKEVQNPPHFSVVTDDAELARVCQAARQQSAVALDTEFVRVRTLYPKLGLIQMYFGDRVALIDPLPIQDFSPFIKLLADTNLVKILHACSEDLDVFQHYFQQLPRPMCDTQVMAHFLGFAGSTGFATLVQHYFQIEIDKGASRTDWLARPLSDTQLQYAAADVWYLLPLYEQMQQQLTQTEWQSVVENECEFLLNKRAQTTKDPDSAYFAIPNAWKLNRLELMRLKLLAKWRMEEAMKRDLALNFVVRAENLWQVAKSNPKHISTLPELGLSTAEVRIHGKKLLQIIDQVKRIVPEDYPPPIQRLADDPRYKAILKALQQHLIQITPPNLAKELIAGKRHLESLMKWHWLKNSEDDLPELLTGWRKPFGEKLLAALKAFDE","1807262","","ribonuclease D","Cytoplasm","","
InterPro
IPR002121
Domain
HRDC
PF00570\"[222-301]THRDC
PS50967\"[222-301]THRDC
InterPro
IPR002562
Domain
3'-5' exonuclease
PF01612\"[14-182]T3_5_exonuc
SM00474\"[14-182]T35EXOc
InterPro
IPR006292
Family
Ribonuclease D
TIGR01388\"[16-383]Trnd: ribonuclease D
noIPR
unintegrated
unintegrated
G3DSA:3.30.420.10\"[8-192]Tno description
PTHR12124\"[14-369]TPOLYMYOSITIS/SCLERODERMA AUTOANTIGEN-RELATED
PTHR12124:SF3\"[14-369]TRIBONUCLEASE D


","BeTs to 9 clades of COG0349COG name: Ribonuclease DFunctional Class: JThe phylogenetic pattern of COG0349 is ------y---r--cefghs--jx---Number of proteins in this genome belonging to this COG is","","Residues 16 to 173 match (8e-08) PD:PD023226 which is described as PROTEOME COMPLETE U1764U D RIBONUCLEASE ML1040 ","","","","","","","","","","","","Wed Jan 15 17:00:01 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02597 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 222 to 301 (E-value = 1.5e-10) place AA02597 in the HRDC family which is described as HRDC domain (PF00570)","","","","","Zhang,J.R. and Deutscher,M.P.Escherichia coli RNase D: sequencing of the rnd structural gene and purification of the overexpressed proteinNucleic Acids Res. 16 (14A), 6265-6278 (1988)PubMed: 3041371","","Wed Jan 15 17:01:52 2003","1","","","" "AA02598","1810177","1808504","1674","ATGGAAAAACTTTGGTTTAAAAATTATCCGGAAGGTGCGGAGCGCCAATTAGACACCTCGGAATACGATTCGATTTTAGATATGTTTGAAAAAGCGGTGCGCGAACATCCCGATCGTGCCGCTTATATTAATATGGGCAAGGTGTTGACGTTTCGCAAATTGGAAGAACGTAGCCGTGCTTTCGCTGCCTATTTGCAAAATGAATTGAAATTGGAGCGCGGCGATCGCGTGGCATTAATGATGCCGAATTTGCTGCAATATCCCATTGCGTTGTTCGGGGTGTTGCGTGCTGGGTTGGTGGTGGTCAATGTGAACCCGCTTTATACGCCGCGCGAGTTGGAGCATCAGCTGCAGGACAGCGGAGCGAAGGCCATTGTGGTGGTGTTAAATTTTGCTTCTACTTTGGAAAAAGTGGTGTTTAACACCGCCGTCAAGCACGTGATTTTAACCCGTATGGGCGATCAGCTTTCTTTCGGCAAACGCACTTTGGTGAATTTCGTGGTGAAATATGTGAAAAAGCTGGTGCCGAAATATAAACTGCCGAATGCGGTAACTTTCCGTGAAGTGCTGAGTGTGGGGAAATATCGCCAATATGTGCGCCCGCAAATGGAACGGGACGATTTGGCCCTCCTGCAATATACCGGCGGCACTACAGGCGTAGCGAAAGGGGCGATGTTATCCCACGGTAATATTATCGTGAACGTGTTCCAAGCCAAATGGATTGCTTACCCGTTTGTAGGCGATCGTGGACGCGAACGCTTGGCGATCCTCGCTTTGCCGCTTTATCATGTTTTTGCGCTAACGGTAAATTGCTTATTATTCATTGAGTTAGGTGTAACCGCTGTGTTAATCACCAATCCGCGTGATATTGAAGGCTTTGTGAAAGAAATGAGAAAGCACCGCTTTGTGGCGATTACCGGTGTGAATACCTTATTCAATGCCTTGTTAAACAACGAGAATTTCAAAGAAGTGAATTTCTCCGCATTGAAACTTTCCGTCGGCGGCGGCATGGCGATTCAACAAGCCGTAGCCACCCGCTGGCATGAATTGACCGGTTGTAACATCATTGAAGGCTATGGCATGACGGAATGTTCTCCATTGATTGCCGCCTGTCCGGTTAATGTGGTGAAACATAACGGCAGTATCGGTGTGCCGGTGCCGAATACGGACATTAAAATTATTAAAGAAGATGACACGGAAGCGGCTATCGGCGAAGCGGGCGAGTTATGGGTGAAAGGCGAGCAGGTTATGCAAGGTTATTGGCAGCGCCCGGAAGCCACTGCGGAAGTGATTAAAGACGGCTGGATGGCGACCGGCGACATTGTGGTTATGGACGAGGATTACAGTTTACGCATTGTGGATCGCAAAAAGGATATGATTCTGGTATCCGGTTTTAATGTGTATCCAAATGAAATCGAAGATGTGGTGATGTTGAATAACAAGGTTTCCGAAGTGGTTGCCATCGGCGTGCCTCATGAGGTTTCCGGCGAAACCATTAAGCTTTTTGTGGTGAAAAAAGACGAAAGCCTGACCCGCGATGAACTGCGTACGCATTGCCGCGAACACCTAACGGGTTACAAAATACCGAAAGATATTGAGTTCCGCGAGGAATTGCCGAAAAGCAATGTGGGCAAAATTTTGCGTCGCGTGTTGCGTGATGAAGAACTTGCGAAG","","","62933","MEKLWFKNYPEGAERQLDTSEYDSILDMFEKAVREHPDRAAYINMGKVLTFRKLEERSRAFAAYLQNELKLERGDRVALMMPNLLQYPIALFGVLRAGLVVVNVNPLYTPRELEHQLQDSGAKAIVVVLNFASTLEKVVFNTAVKHVILTRMGDQLSFGKRTLVNFVVKYVKKLVPKYKLPNAVTFREVLSVGKYRQYVRPQMERDDLALLQYTGGTTGVAKGAMLSHGNIIVNVFQAKWIAYPFVGDRGRERLAILALPLYHVFALTVNCLLFIELGVTAVLITNPRDIEGFVKEMRKHRFVAITGVNTLFNALLNNENFKEVNFSALKLSVGGGMAIQQAVATRWHELTGCNIIEGYGMTECSPLIAACPVNVVKHNGSIGVPVPNTDIKIIKEDDTEAAIGEAGELWVKGEQVMQGYWQRPEATAEVIKDGWMATGDIVVMDEDYSLRIVDRKKDMILVSGFNVYPNEIEDVVMLNNKVSEVVAIGVPHEVSGETIKLFVVKKDESLTRDELRTHCREHLTGYKIPKDIEFREELPKSNVGKILRRVLRDEELAK","1808502","","long-chain-fatty-acid-CoA ligase","Cytoplasm, Inner membrane","","
InterPro
IPR000873
Domain
AMP-dependent synthetase and ligase
PR00154\"[206-217]T\"[218-226]TAMPBINDING
PF00501\"[50-487]TAMP-binding
PS00455\"[211-222]?AMP_BINDING
noIPR
unintegrated
unintegrated
G3DSA:2.30.38.10\"[378-455]Tno description
G3DSA:3.30.300.30\"[457-553]Tno description
G3DSA:3.40.50.980\"[24-228]T\"[232-374]Tno description
PTHR11968\"[3-155]T\"[173-555]TATP-DEPENDENT AMP-BINDING ENZYME FAMILY MEMBER
PTHR11968:SF44\"[3-155]T\"[173-555]TLONG-CHAIN-FATTY-ACID--COA LIGASE
tmhmm\"[89-109]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 8.7e-07) to 2/2 blocks of the IPB000873 family, which is described as \"AMP-dependent synthetase and ligase\". Interpro entry for IP:IPR000873. IPB000873A 213-228 2.5e-05 IPB000873B 253-263 15","Residues 93 to 148 match (9e-07) PD:PD021813 which is described as LIGASE PROTEOME COMPLETE ACYL-COA AMP-BINDING SYNTHETASE PROBABLE MEDIUM-CHAIN MEDIUM-CHAIN-FATTY-ACID--COA FATTY ","","","","","","","","","","","","Wed Jan 15 17:03:59 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02598 is paralogously related to AA02108 (7e-28), AA00231 (1e-18), AA02512 (1e-13) and AA01193 (9e-06).","","","","","","Residues 50 to 487 (E-value = 4.6e-126) place AA02598 in the AMP-binding family which is described as AMP-binding enzyme (PF00501)","","","","","Weimar,J.D., DiRusso,C.C., Delio,R. and Black,P.N. Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous long-chainfatty acids. Amino acid residues within the ATP/AMP signaturemotif of Escherichia coli FadD are required for enzymeactivity and fatty acid transport J. Biol. Chem. 277 (33), 29369-29376 (2002) PubMed: 12034706 ","","Wed Jan 15 17:03:59 2003","1","","","" "AA02599","1810777","1810223","555","ATGAACAAAAAAATACTTTTATTTTGCACCGCACTTTCCCTTGTGTTAACCGGCTGCGTATCCGCGCCGCAGGGTTTGGAAGCCAAACAGTTCGAAATGTTAAATCTGAAAAATGTGCAGGCGCAGGATTACGATTGCCGCTGCCTGAAAGTGCGCTTGGGCGGCAAAGTGGTTTCCGCACAGGCGTTGAAAGATAAAACCAAAATTGAAGTATTGAATCAAACGGTGGCGTATTTTTCCGCGAAACCTATCGTGGATAGCTATAGCAACGGACGTTTTATCGCCTATTTAAACGGCTTTGTGGATCCGGAAAATCTGAAAGACCTGTATGTGACAGTCGGCGGAGTGCTGAGCGGCAAAGAGCAGGGCAAAATTGATCAGGCGGATTACAATTATCCCGTGGTTCAAGCCGATCAATACCGTATTTGGAAGCTGGTGAAAGAATATTATTACGACCCTGACGACATTTATGACTACGCACCGTTTTACCCTTACGGCTGGGGATTTTCGTCCCGCTTCTTTTGGGCTGAACCGCGCGTGCGCTATAATTTATAT","","","21248","MNKKILLFCTALSLVLTGCVSAPQGLEAKQFEMLNLKNVQAQDYDCRCLKVRLGGKVVSAQALKDKTKIEVLNQTVAYFSAKPIVDSYSNGRFIAYLNGFVDPENLKDLYVTVGGVLSGKEQGKIDQADYNYPVVQADQYRIWKLVKEYYYDPDDIYDYAPFYPYGWGFSSRFFWAEPRVRYNLY","1810221","From GenBank (gi:20140528):This protein is attached to the membrane by a lipid anchor","outer membrane protein, Slp family","Outer membrane, Periplasm, Cytoplasm","","
InterPro
IPR004658
Family
Outer membrane lipoprotein Slp
PF03843\"[16-172]TSlp
TIGR00752\"[2-184]Tslp: outer membrane lipoprotein, Slp family
noIPR
unintegrated
unintegrated
PS51257\"[1-19]TPROKAR_LIPOPROTEIN
signalp\"[1-21]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","","Residues 15 to 148 match (4e-14) PD:PD022571 which is described as MEMBRANE LIPOPROTEIN COMPLETE PROTEOME OUTER SLP PRECURSOR SIGNAL YEAY STARVATION ","","","","","Tue Feb 18 10:43:08 2003","","","","","","Wed Jan 15 17:15:27 2003","Tue Feb 18 10:43:08 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02599 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 16 to 172 (E-value = 2.9e-65) place AA02599 in the Slp family which is described as Outer membrane lipoprotein Slp family (PF03843)","","","","","","","","1","","","" "AA02600","1811531","1810812","720","ATGAAAAATGTCACATTACTTGCTTTAGATACGGCTACAGAAGCTTGTTCTGTTGCATTGTTACGCGGTGGAGAGAAAGCGCATTTGGAACGATTCGCACAACGTGAACATACCAAACATATTTTGCCCATGGTGGATGAAATTCTGGCGCAGGCGGGAATTAAACTTTATCAAGTGGATGCTTTGGTTTTCGGGCGCGGCCCGGGCAGTTTTACCGGTGTTCGAATCGGTGCCGGCATTGCGCAAGGGTTGGCGTTCGGCGCCAATTTGCCGGTGATTCCCGTGTCAAATTTAGCCGCCATGGCGCAAGCCGCTTATGTGCAATATCAGTCGGAAAATGTGCTGACCGCCATCGATGCGCGCATGAATGAAGTGTATTTTGCCCAATGGAAAGCGCGGAAAGTGCGGTCGGATTTCGGTACGTTTTTAGCTTGGCAGCCTATTATTGCCGAGCAGGTGTGCAGCGCGTCGAGAGTGCTTGAACAGGTGGTGCAGCACCAACACGATAATGCAGTGTTAGCCGGCACAGGTTGGACGGCATACCCGCAACTTACCGAGGCGAACCTTGGTAAAAGCACCGATATTACCCTGCCTTCCGCGTTATATATGCTGGATTTGGCGCTGCCGAAGTGGTTTGCCGGCGAGACCATCAGCCCGCTGGAAATTGAGCCGATTTACTTACGTAACGAAGTCACTTGGAAGAAATTACCGGGACGGGAA","","","26276","MKNVTLLALDTATEACSVALLRGGEKAHLERFAQREHTKHILPMVDEILAQAGIKLYQVDALVFGRGPGSFTGVRIGAGIAQGLAFGANLPVIPVSNLAAMAQAAYVQYQSENVLTAIDARMNEVYFAQWKARKVRSDFGTFLAWQPIIAEQVCSASRVLEQVVQHQHDNAVLAGTGWTAYPQLTEANLGKSTDITLPSALYMLDLALPKWFAGETISPLEIEPIYLRNEVTWKKLPGRE","1810810","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR000905
Domain
Peptidase M22, glycoprotease
PF00814\"[25-236]TPeptidase_M22


","BeTs to 15 clades of COG1214COG name: Inactive homologs of metal-dependent proteases, putative molecular chaperonesFunctional Class: OThe phylogenetic pattern of COG1214 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.4e-06) to 1/8 blocks of the IPB000905 family, which is described as \"Glycoprotease, (M22) metallo-protease family\". Interpro entry for IP:IPR000905. IPB000905C 58-98 2.2e-06","Residues 4 to 56 match (5e-14) PD:PD535552 which is described as COMPLETE PROTEOME 3.4.-.- PROTEASE METALLOPROTEASE HYDROLASE MOLECULAR VC1989 YEAZ YPO2072 ","","","","","","","","","","","","Thu Jan 16 08:17:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02600 is paralogously related to AA02402 (1e-05).","","","","","","Residues 5 to 230 (E-value = 1.5e-31) place AA02600 in the Peptidase_M22 family which is described as Glycoprotease family (PF00814)","","","","","","","","1","","","" "AA02601","1813369","1811537","1833","ATGGCGGTGGGCAAAGCCATTGAACAGCATGGCGCGTTGGTGGTGGAAGCCGGCACCGGCACGGGCAAAACCTTTGCCTATTTGGCGCCGGCATTATTGGCGAAGAAGAAAACCATTATTTCCACCGGTTCCAAAAACTTGCAGGATCAGCTATTTAATCGCGACCTACCCGCCATTCAAAAAGCCCTAGGTTACAGCGGTAAAATCGCGTTATTAAAAGGGCGCGCCAATTATTTATGTCTGGAACGGCTGGAGCAGGTGATTGCGCAGGGCGTGCTGGGCGATCGTAGTGTGTTGCATGATTTGTCCAAAGTGCGTAAATGGCGCAATGCCACGAAAACCGGCGATTTGTCCGAATGTATCGAAATTGCCGAAGACAGCCCGATCCTGACGCAATTAACCAGCACTGCCGAAAGCTGCCTTGGCAGCGATTGCCCGAATTATGCCGATTGTTACGTGGCATTGGCGCGGAAAAAAGCGCTCAATGCGGATTTGGTGGTGGTCAATCATCATTTATTTTTTGCCGACATGGCGGTGAAAGAAAACGGCTTCGGCGAATTGATTCCCAATGCGGAAGTGATCGTGTTTGACGAAGCCCATCAGCTCCCTGATATTGCCAGTCAATATTTCGGACAATCGGTCACCTCGCGCCAGCTGTTTGATTTGTGCAAAGATATTCAAATTACTTATCGCACCGAAGTGAAAGACATGAAACAGCTTGGCGTAGCGGCGGATCAGCTGGTAAAAATTGTGCAGGATTTCCGGTTGATGTTGGGCGAAGGCAATCTGCGTGGCAATTGGCGACAAATATTGCAGCAAAGTGCGGTCAAAAAATCCTTTGGTTTTTTATTGGAAAAACTCAATTTTACGGCGGACGTGGTGAAGCTCGGCTTGGGGCGTTCGCAAACTCTGGATAGCATTTTTGAGCGCATCGCCCAGCTACAAAATTTGCTTAAGCGCCTCACGGAAACGGAAATTACCGGCTATTGCTATTGGTTTGAATGTATCGGCCGCCAGTTCGGCTTGCACATTACGCCACTGACCGTGGCGGATAAATTCGGTGAGCAAATGGCGAAGCAAAAATGCGCCTGGATTTTTACCTCGGCGACCTTGGAAGTGGGCGGGACTTTCGAGCATATCTGCCACCGTTTAGGCATTCAAAACGCGGCGCAGAAAATTCTGCCGAGCCCGTTTAATTACGCAGAACAATCCCTGCTTTGTGTGCCGCGTTATCTGCCGGCAACCAATCACAGTAGCACCTTCAGTCAATTAGGCAAAATGCTGCTGCCGATTATCGAAGCCAACCAAGGGCGTTGTTTTGTGCTTTGTACGTCCTATGCCATGATGCGCAGTTTGGCGGAATATTTCCGTGAGAACAGTAAATTGATCATTTTGTTACAGGGTGAAACGGCGAAAGGCACTTTGTTGGAACAATTCATTTCGCAATCCCATAGCGTGTTGGTGGCGACCTCCAGTTTCTGGGAAGGTGTGGATGTGCGCGGTGACGCGTTGTCCTTGGTGATTATCGATAAACTACCATTTACCGCGCCGGATGAGCCCTTGTTGAAAGCACGCATTGAAGATTGCCGTTTACAAGGCGGCGAGCCTTTTAATGATATTCAGATTCCTGAAGCGGTGATTACTTTAAAACAGGGCGTCGGGCGTTTAATTCGTGACGTCACCGATCGCGGCGTGGTGATTATTTGCGATAATCGTTTGGTGATGCGCCCTTACGGTGAAACCTTTTTGCGCAGTTTGCCGAATTTTAAACGTACGCGGGATTTGCACAAAGTGGTACAATTCCTCACAACAATCAATAAAGAAGAATCAGAA","","","72458","MAVGKAIEQHGALVVEAGTGTGKTFAYLAPALLAKKKTIISTGSKNLQDQLFNRDLPAIQKALGYSGKIALLKGRANYLCLERLEQVIAQGVLGDRSVLHDLSKVRKWRNATKTGDLSECIEIAEDSPILTQLTSTAESCLGSDCPNYADCYVALARKKALNADLVVVNHHLFFADMAVKENGFGELIPNAEVIVFDEAHQLPDIASQYFGQSVTSRQLFDLCKDIQITYRTEVKDMKQLGVAADQLVKIVQDFRLMLGEGNLRGNWRQILQQSAVKKSFGFLLEKLNFTADVVKLGLGRSQTLDSIFERIAQLQNLLKRLTETEITGYCYWFECIGRQFGLHITPLTVADKFGEQMAKQKCAWIFTSATLEVGGTFEHICHRLGIQNAAQKILPSPFNYAEQSLLCVPRYLPATNHSSTFSQLGKMLLPIIEANQGRCFVLCTSYAMMRSLAEYFRENSKLIILLQGETAKGTLLEQFISQSHSVLVATSSFWEGVDVRGDALSLVIIDKLPFTAPDEPLLKARIEDCRLQGGEPFNDIQIPEAVITLKQGVGRLIRDVTDRGVVIICDNRLVMRPYGETFLRSLPNFKRTRDLHKVVQFLTTINKEESE","1811535","","ATP-dependent helicase","Cytoplasm","","
InterPro
IPR002345
Domain
Lipocalin
PS00213\"[259-270]?LIPOCALIN
InterPro
IPR006555
Domain
Helicase c2
SM00491\"[446-575]THELICc2
InterPro
IPR014013
Domain
Helicase superfamily 1 and 2 ATP-binding, DinG/Rad3-type
PS51193\"[1-244]THELICASE_ATP_BIND_2
noIPR
unintegrated
unintegrated
PTHR10967\"[6-54]TDEAD BOX ATP-DEPENDENT RNA HELICASE
PTHR10967:SF39\"[6-54]TMUTATOR PROTEIN 14


","BeTs to 16 clades of COG1199COG name: Rad3-related DNA helicasesFunctional Class: LThe phylogenetic pattern of COG1199 is -ompkzyq--rlb-efghsn-j----Number of proteins in this genome belonging to this COG is","","Residues 569 to 602 match (2e-09) PD:PD428541 which is described as HELICASE COMPLETE PROTEOME ATP-DEPENDENT ATP-BINDING DNA-BINDING PROBABLE FAMILY HYDROLASE BOX ","","","","","","","","","","","","Thu Jan 16 09:20:03 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02601 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02602","1813547","1814362","816","ATGATCAATATTCAACGACAACAACAAATCACGCCCGAACTGAGCTTATATACCTATAACGAAATTCCCGTTTTACATTTACAACACGCCATAGGCACGGCAAAAATCGCCTTACAAGGGGCGCATTTATTCAGCTGGCAGCCGGCGCACAGTAAACAGGACGTGCTGTGGCTAAGTGAAATCGAACCCTTTGAAACCAGCACGGCAATTCGCGGCGGCATTCCTATTTGTTATCCGTGGTTTAATAACGCCGGCACACCTGCCCACGGGTTCGCCCGTATCAGCCTGTGGCAGTTGAGCGATTACGCAATTAATGCCGATAAAGTGCGGTTGGTTTTTTCGTTGTTTTCCGCGCACAATGTGATTTTAGCGAAAGTAGAAATGATTTTCGGCAAACATTGTGACTTGCGCTTTACCCATTACGGTGAAGCAGGAATGGAAAAAGTGCAGCTGGCGTTACACAGTTATTTCAACATCGGTAATATCACCCATACCGACATCGCCAACCTGCCGACGGAATGCTTCAACGCCCTCACCCGCCAACAAGAAAGCGTGCCGTCACCACGCCATATTGCGGAAAATGTGGATTGTGTTTACACCACCCAACAACCGACGGAAATTCGCGACTATGACAATCAACGCACAATCATTGTGGAACATCACAATGCCGGCGATGTGGTACTGTGGAACCCATGGCACAAACCTACCGGTAACATGACAGAAAACGGCTATCAAACTATGGTCTGCGTGGAAACGGCACGAATCAATCGCTATCTTGATGCAGGGGAAACGGTGGCGGTGAGATTGCGTGTGGAA","","","31053","MINIQRQQQITPELSLYTYNEIPVLHLQHAIGTAKIALQGAHLFSWQPAHSKQDVLWLSEIEPFETSTAIRGGIPICYPWFNNAGTPAHGFARISLWQLSDYAINADKVRLVFSLFSAHNVILAKVEMIFGKHCDLRFTHYGEAGMEKVQLALHSYFNIGNITHTDIANLPTECFNALTRQQESVPSPRHIAENVDCVYTTQQPTEIRDYDNQRTIIVEHHNAGDVVLWNPWHKPTGNMTENGYQTMVCVETARINRYLDAGETVAVRLRVE","1814360","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR008183
Family
Aldose 1-epimerase
PF01263\"[23-272]TAldose_epim
InterPro
IPR014718
Domain
Glycoside hydrolase-type carbohydrate-binding, subgroup
G3DSA:2.70.98.10\"[2-268]Tno description
noIPR
unintegrated
unintegrated
PTHR11122\"[33-255]TAPOSPORY-ASSOCIATED PROTEIN C-RELATED


","BeTs to 7 clades of COG0676COG name: Uncharacterized enzymes related to aldose 1-epimeraseFunctional Class: GThe phylogenetic pattern of COG0676 is ------y----l-cefghs--j----Number of proteins in this genome belonging to this COG is","Significant hit ( 9.7e-40) to 5/6 blocks of the IPB003843 family, which is described as \"UPF0010_DUF\". Interpro entry for IP:IPR003843. IPB003843A 53-82 8.9e-15 IPB003843B 87-97 2.4e-05 IPB003843C 146-170 0.00034 IPB003843E 227-239 0.0001 IPB003843F 240-253 0.00039","Residues 223 to 272 match (4e-12) PD:PD590031 which is described as PROTEOME COMPLETE HI1317 PM0601 PM0711 ","","","","","","","","","","","","Thu Jan 16 09:26:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02602 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 24 to 272 (E-value = 2.2e-34) place AA02602 in the Aldose_epim family which is described as Aldose 1-epimerase (PF01263)","","","","","","","","1","","","" "AA02603","1814775","1815629","855","ATGACCGACTTTCCCTATATTCGTGACCTCAACGAACATAACCTTAATGAAACTCTGCAGCTTTCCCAAAATTATCCGTTAGTCATTATCTTTTATGCACCCAGCCATACCGATTCCGTGGCGTTTGTTAAAACGTTGGAAAACTACGCCAATCAATACCAAGGGCAGTTTGTGTTAGCCAAAGTGGATTGTGAAAAAGAACAAATGGTGGCGGCGCAATTCCACGTTCAGGCGTTGCCGACCACCTATTTATTCAGAGACGGGCAAGCCTTGGATGCGTTTCAAGGGGCATTGGATAATGCCACATTGCAACAGCGTTTGAATGCGATTTTACCGAAAGAGGAAGAAATTAAGTTTAATCAAGCGTTGGAATTGCTCGCCGTCGAAAATTACGAACAGGCATTGCCGTTGTTAAAAGATGCCTGGGAGTTGTCCGACCAGAAAAACAGTGAAATTGCGCTGCTCTATGCGGAAACCTATATCGCTATGAAGAAAACCGAGCCTGCGCAACAGATTTTAAATAAGATCCCGCTACAGGATCGCGACAGCCGCTGGCAGGGCTTGCAGGCGCAAATTGAATTATTGATTAAAGCCGCCGACACGCCGGAAATCCAGCAATTACAAGAAGAATTTGCCCAAGGGCCGACAAATGATCTTGCCTTAAAACTGGCGTTGCAATTACATCAAGCCAACCGCAATGAAGAAGCACTGGATCTGTTATTTAGGATTTTGCGTCAGGATTTAAGTGCGGAAGAAGGTAAAATCAAACAGGAATTTTTATCTATTTTAGCCGCTATCGGTAACAATGATCCCGTGGCTAATAAATACCGCCGATTGATCTATTCGTTGTTGTAC","","","32626","MTDFPYIRDLNEHNLNETLQLSQNYPLVIIFYAPSHTDSVAFVKTLENYANQYQGQFVLAKVDCEKEQMVAAQFHVQALPTTYLFRDGQALDAFQGALDNATLQQRLNAILPKEEEIKFNQALELLAVENYEQALPLLKDAWELSDQKNSEIALLYAETYIAMKKTEPAQQILNKIPLQDRDSRWQGLQAQIELLIKAADTPEIQQLQEEFAQGPTNDLALKLALQLHQANRNEEALDLLFRILRQDLSAEEGKIKQEFLSILAAIGNNDPVANKYRRLIYSLLY","1815627","","possible thioredoxin trxA homolog","Cytoplasm, Periplasm","","
InterPro
IPR012335
Domain
Thioredoxin fold
G3DSA:3.40.30.10\"[4-112]Tno description
InterPro
IPR013766
Domain
Thioredoxin domain
PF00085\"[50-110]TThioredoxin
InterPro
IPR015467
Domain
Thioredoxin family
PTHR10438\"[17-141]TTHIOREDOXIN-RELATED


","BeTs to 5 clades of COG3118COG name: Thioredoxin domain-containing proteinFunctional Class: OThe phylogenetic pattern of COG3118 is ----------r---efghs--j----Number of proteins in this genome belonging to this COG is","","Residues 69 to 110 match (4e-07) PD:PD236640 which is described as PROTEOME COMPLETE HI1159 PM0574 ","","","","","","","","","","","","Thu Jan 16 09:29:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02603 is paralogously related to AA02915 (4e-06).","","","","","","Residues 28 to 112 (E-value = 5.7e-07) place AA02603 in the Thioredoxin family which is described as Thioredoxin (PF00085)","","","","","Lim CJ, Geraghty D, Fuchs JA. Cloning and nucleotide sequence of the trxA gene ofEscherichia coli K-12. J Bacteriol 1985 Jul;163(1):311-6. PubMed: 3891733. ","","Thu Jan 16 09:29:51 2003","1","","","" "AA02604","1815692","1816642","951","ATGTCTGAAATTAAACACGCTCAATTACTCATTTTAGGCTCCGGCCCTGCCGGCTATACTGCTGCGATTTATGCGGCACGCGCTAATTTGAAACCGTTATTAGTAACCGGTTTACAACAAGGCGGTCAACTAACTACCACCAATGAAATTGAAAACTGGCCGGGCGATTTCGGTGAAACTACCGGTCCGGAACTGATGCAAAGAATGCTACAACACGCAGAAAAATTCGAGACGGAAATTGTCTTCGATCATATTAACCGTGTTGATCTTTCCTCCCGCCCATTCAAATTATACGGTGATGCTCAAACCTTTAGCTGTGATGCGTTAATTATCGCCACCGGTGCCTCCGCCCGCTATTTGGGATTACCGACCGAAGAAAGCTACAAAGGTCGTGGCGTTTCTGCCTGTGCCACCTGTGACGGATTCTTTTATCGCAATAAGCCTGTTGCAGTGATCGGCGGTGGCAATACGGCGGTCGAAGAAGCTTTGTATTTAGCCAATATTGCCAGCGAAGTGCATTTGATTCACCGTCGCGACAGCTTCCGCGCGGAAAAAATCCTTATTGATCGCCTATACAAAAAAGTAGAAGAAGGCAAAATCATTCTACATACCCACCGCACTTTAGACGAAGTATTAGGTGATAACATGGGCGTGACCGGAGTACGATTAAAAGACGTGCAGTCCGATGCCACCGAGGACGTCATGTTAGACGGCGTATTCGTCGCCATCGGTCATGCGCCGAACACGGAAATTTTCCAAGGTCAGCTTGAATTAAACAACGGCTATATCGTGGTGAAATCAGGCTTAGAAGGTAATGCCACCGCCACTTCCGTGGAGGGTGTCTTCGCCGCCGGTGATGTGATGGATCACAATTATCGCCAGGCAATTACCTCTGCCGGCACCGGTTGTATGGCAGCATTGGATGCCGAGCGTTATTTAGACGCGCAAAAA","","","34331","MSEIKHAQLLILGSGPAGYTAAIYAARANLKPLLVTGLQQGGQLTTTNEIENWPGDFGETTGPELMQRMLQHAEKFETEIVFDHINRVDLSSRPFKLYGDAQTFSCDALIIATGASARYLGLPTEESYKGRGVSACATCDGFFYRNKPVAVIGGGNTAVEEALYLANIASEVHLIHRRDSFRAEKILIDRLYKKVEEGKIILHTHRTLDEVLGDNMGVTGVRLKDVQSDATEDVMLDGVFVAIGHAPNTEIFQGQLELNNGYIVVKSGLEGNATATSVEGVFAAGDVMDHNYRQAITSAGTGCMAALDAERYLDAQK","1816640","","thioredoxin reductase","Cytoplasm","","
InterPro
IPR000103
Domain
Pyridine nucleotide-disulphide oxidoreductase, class-II
PR00469\"[8-30]T\"[41-56]T\"[62-72]T\"[107-115]T\"[129-141]T\"[144-168]T\"[199-215]T\"[238-259]T\"[276-294]TPNDRDTASEII
InterPro
IPR000759
Family
Adrenodoxin reductase
PR00419\"[8-30]T\"[149-163]TADXRDTASE
InterPro
IPR001327
Domain
Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PD000139\"[113-179]TQ9CN66_PASMU_Q9CN66;
PF00070\"[148-244]TPyr_redox
InterPro
IPR005982
Domain
Thioredoxin reductase
TIGR01292\"[7-313]TTRX_reduct: thioredoxin-disulfide reductase
InterPro
IPR008255
Active_site
Pyridine nucleotide-disulphide oxidoreductase, class-II, active site
PS00573\"[136-156]TPYRIDINE_REDOX_2
InterPro
IPR013027
Domain
FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PR00368\"[8-30]T\"[109-118]T\"[148-173]T\"[237-251]T\"[281-288]TFADPNR
PF07992\"[8-292]TPyr_redox_2
noIPR
unintegrated
unintegrated
G3DSA:3.50.50.60\"[2-117]T\"[118-244]Tno description
PTHR22912\"[10-291]TDISULFIDE OXIDOREDUCTASE


","BeTs to 25 clades of COG0492COG name: Thioredoxin reductaseFunctional Class: OThe phylogenetic pattern of COG0492 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 7.5e-94) to 5/5 blocks of the IPB000103 family, which is described as \"Pyridine nucleotide-disulphide oxidoreductase class-II\". Interpro entry for IP:IPR000103. IPB000103A 8-28 4.4e-13 IPB000103B 41-55 2.4e-08 IPB000103C 114-162 1.6e-33 IPB000103D 238-249 1.2e-07 IPB000103E 276-313 4.6e-26Significant hit ( 2.9e-39) to 5/5 blocks of the PR00368 family, which is described as \"FAD-dependent pyridine nucleotide reductase signature\". Prints database entry for PR:PR00368. PR00368A 8-30 7e-11 PR00368B 109-118 0.0017 PR00368C 148-173 1.7e-09 PR00368D 237-251 2.1e-07 PR00368E 281-288 0.22Significant hit ( 2.2e-05) to 2/5 blocks of the PR00419 family, which is described as \"Adrenodoxin reductase family signature\". Prints database entry for PR:PR00419. PR00419A 8-30 0.032 PR00419D 149-163 0.34","Residues 173 to 302 match (5e-07) PD:PD536467 which is described as PROTEOME COMPLETE THIOREDOXIN REDUCTASE FLAVOPROTEIN FAD OXIDOREDUCTASE ","","","","","","","","","","","","Thu Jan 16 09:33:11 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02604 is paralogously related to AA01306 (2e-11) and AA01988 (7e-05).","","","","","","Residues 8 to 297 (E-value = 8.8e-74) place AA02604 in the Pyr_redox family which is described as Pyridine nucleotide-disulphide oxidoreductase (PF00070)","","","","","Tong Q, Yang YG, Zhang HT, Chen Y, Yang SL, Gong Y. The Thioredoxin Reductase-deficient E.coli Mutant EnhancesExpression into Solution of Recombinant Proteins ContainingCys Residues. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2001;33(1):30-34. PMID: 12053185 Lee JH, Kim MS, Cho JH, Kim SC. Enhanced expression of tandem multimers of the antimicrobialpeptide buforin II in Escherichia coli by the DEAD-boxprotein and trxB mutant. Appl Microbiol Biotechnol. 2002 May;58(6):790-6. PMID: 12021800","","Thu Jan 16 09:33:11 2003","1","","","" "AA02605","1816695","1816820","126","GTGGGCTTTAAAGCCCGCCTTATGTTTTTTCTATCTTTTGTAAAAAACCGCAACTTATGGACAAATCCCGTCAAAAGTATTTGCAACAATGGTTACGCACGCAGCAAAAGCCAATTAAAGAATATT","","","4874","VGFKARLMFFLSFVKNRNLWTNPVKSICNNGYARSKSQLKNI","1816820","","hypothetical protein","Cytoplasm, Extracellular","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 16:21:13 2004","Mon Feb 23 16:21:13 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02605 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 16:21:13 2004","","","","","","","","","","","","","1","","","" "AA02606","1816865","1818511","1647","GTGGCGCAAACCTATTTACTGGCGTCATTGCTGTATAAAATCATTATTGTTAATAAAGCAATTAGTGGTCTTATACCTTATTTTATCGGCTTGATTGTGGGATTTGCATTGCGCGCTCTGATTTTATGGTTACGGGAAAAAATCGGCTTTAAGTGCGGTCAATTATTACGAAATAGTATTCGCCGGCAAATTCTGGATAAAATTCATCAGGTCGGTCCTGCCACCATTAACAACAAACCGGCGGGTAGCTGGGCGACGATCATGTTGGAACAGGTAGAAAACCTGCACAATTTCTACGCCCGTTATTTGCCGCAACAAGCGCTTTCCGCCATTGTACCGATCATTATTCTAATTGCGGTTTTCCCACTGAATTGGGCGGCAGGTTTGATTTTAATAGGCACCGCACCGCTGATCCCGATTTTCATGATTTTAGTGGGCAAAGCAGCAGCAGACAGCAGCCAAAAGAACATGGACACCCTCGCCCGTTTAAGCGGGCAATTTTTAGATCGGCTGCGTGGCTTGGAAACCTTACGTTTATTTGACCGCACTTTGGAACAAACCCGCTACATTGAAGAAAGCACGGAAGACTTCCGTGAAACTACTATGGACGTGCTGAAAATGGCGTTCCTCTCCTCTGCCGTGCTGGAATTTTTCACCTCCATCTCTATAGCATTAATGGCGGTATATTTCGGTTTTAGTTATTTAGGGCAAATCGAATTCGGTACTTACGGCACGCCAATCACCCTGTTTATCGGTTTCTTCTGCTTGATTCTCGCACCGGAATTTTATCAACCATTACGCGATCTCGGCACCTATTATCACGACCGCGCCGCAGGTATCGGGGCGGCAGATGCCATTGTGGATTTTCTGGAAGCCGATTATTTAACTGCCCAAGGCGATAAAAAAGCGGCATTTGAAGGAAAAAGTGCGGTAGAAATTTCAGGTGAAAATCTGGTGGTCTTATCGCCGCAAGGTAAACCGCTGACGGAAGTCCTGAATTTTTCTATTCCACCACACAGCCATATTGCCATCGTCGGGCAAAGCGGTGCCGGCAAAACTTCGCTCATCAACGCCATGTTAGGTTTTCTGCCGTATCAAGGCAGCCTGAAAATTAACGGACAAGAATTGCGCGATTTGGATTTAATGCAATGGCGTAAACATATTGCCTGGGTAGGGCAAAACCCGCTGCTGCTACAAGGCACCATTAAAGAAAATTTATTGCTGGGTGATATTCAAGCCGACGAACAGGAAATTGATCATGCCTTGCGCTTGGCACAAGCAAAAGAGTTTACCGATCGGCTTGGTCTGGAAGCAGAAATTAAAGAAGGCGGCATCGGTGTTTCCGTGGGGCAGGCGCAACGTTTGGCAGTGGCACGTGCACTGCTGCACAAAGGTGATTTGCTGTTGTTGGACGAACCTACCGCCAGCCTGGATGCCCAATCGGAAAATCAGGTGTTGCAGGCATTGCAACAAATTAGTCAACAGCAAACCACGGTAATGATCACTCACCGTATTGAAGATCTGAAACAATGCGAAAATATTTTGGTCATGCGCCATGGGCAAATTATTCAACAAGGGCATTTTGACCAACTACAACACCAAGGTTTCTTCGCCGAATTATTGGCACAACGACAACAGGATATTCAC","","","65507","VAQTYLLASLLYKIIIVNKAISGLIPYFIGLIVGFALRALILWLREKIGFKCGQLLRNSIRRQILDKIHQVGPATINNKPAGSWATIMLEQVENLHNFYARYLPQQALSAIVPIIILIAVFPLNWAAGLILIGTAPLIPIFMILVGKAAADSSQKNMDTLARLSGQFLDRLRGLETLRLFDRTLEQTRYIEESTEDFRETTMDVLKMAFLSSAVLEFFTSISIALMAVYFGFSYLGQIEFGTYGTPITLFIGFFCLILAPEFYQPLRDLGTYYHDRAAGIGAADAIVDFLEADYLTAQGDKKAAFEGKSAVEISGENLVVLSPQGKPLTEVLNFSIPPHSHIAIVGQSGAGKTSLINAMLGFLPYQGSLKINGQELRDLDLMQWRKHIAWVGQNPLLLQGTIKENLLLGDIQADEQEIDHALRLAQAKEFTDRLGLEAEIKEGGIGVSVGQAQRLAVARALLHKGDLLLLDEPTASLDAQSENQVLQALQQISQQQTTVMITHRIEDLKQCENILVMRHGQIIQQGHFDQLQHQGFFAELLAQRQQDIH","1818509","From GenBank (gi:1169169):This protein is somehow involved in the cytochrome D branch of aerobic repiration and seems to be a component of a transport system.","ABC transporter, ATP-binding protein/permease","Inner membrane, Cytoplasm","","
InterPro
IPR001140
Domain
ABC transporter, transmembrane region
PF00664\"[24-257]TABC_membrane
InterPro
IPR003439
Domain
ABC transporter related
PF00005\"[339-520]TABC_tran
PS50893\"[313-544]TABC_TRANSPORTER_2
PS00211\"[447-461]?ABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[338-529]TAAA
InterPro
IPR011527
Domain
ABC transporter, transmembrane region, type 1
PS50929\"[1-278]TABC_TM1F
InterPro
IPR014216
Family
ABC transporter, CydDC cysteine exporter (CydDC-E) family, permease/ATP-binding protein CydD
TIGR02857\"[1-517]TCydD: ABC transporter, CydDC cysteine expor
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[276-535]Tno description
PTHR19242\"[1-531]TATP-BINDING CASSETTE TRANSPORTER
PTHR19242:SF55\"[1-531]TABC TRANSPORTER (CYDD)
signalp\"[1-39]?signal-peptide
tmhmm\"[24-44]?\"[102-122]?\"[128-148]?\"[208-230]?\"[240-260]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 2.4e-44) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 328-374 8.9e-12 IPB001140B 444-482 1.6e-18 IPB001140C 497-526 3.2e-11","Residues 383 to 437 match (5e-08) PD:PD054667 which is described as ATP-BINDING COMPLETE PROTEOME ABC TRANSPORTER CYDC TRANSMEMBRANE TRANSPORTER PLASMID MEMBRANE ","","","","","","","","","","","Thu May 13 16:49:02 2004","Thu May 13 16:49:19 2004","","","Thu May 13 16:49:19 2004","Thu May 13 16:49:02 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02606 is paralogously related to AA01509 (1e-62), AA01961 (1e-41), AA01510 (3e-39), AA01393 (4e-39), AA02609 (3e-33), AA02805 (2e-32), AA02080 (2e-20), AA01684 (1e-19), AA01616 (4e-18), AA00591 (5e-18), AA02440 (8e-18), AA00415 (3e-17), AA00858 (4e-17), AA02899 (7e-17), AA01779 (7e-17), AA02331 (9e-17), AA01867 (9e-17), AA01422 (9e-17), AA01524 (1e-16), AA01645 (2e-16), AA00751 (3e-16), AA02718 (2e-15), AA00799 (2e-14), AA00700 (3e-14), AA02898 (9e-14), AA02140 (9e-14), AA00207 (3e-13), AA02353 (1e-12), AA02152 (2e-12), AA01568 (3e-12), AA01051 (3e-12), AA02786 (7e-12), AA02550 (9e-12), AA01656 (9e-12), AA01456 (1e-11), AA01947 (3e-11), AA01824 (4e-11), AA02320 (4e-10), AA02324 (5e-10), AA01757 (2e-09), AA00933 (2e-08), AA02573 (3e-08), AA01820 (3e-08), AA02642 (4e-08), AA02484 (6e-08), AA01555 (1e-07), AA02225 (4e-07), AA00061 (5e-07), AA00934 (6e-05), A02145 (8e-05), AA02146 (1e-04) and AA01291 (0.001).","Thu May 13 16:49:02 2004","","","","","Residues 339 to 520 (E-value = 1.6e-58) place AA02606 in the ABC_tran family which is described as ABC transporter (PF00005)","Thu May 13 16:49:02 2004","","","","Winstedt L, Yoshida K, Fujita Y, von Wachenfeldt C. Cytochrome bd biosynthesis in Bacillus subtilis: characterization of the cydABCD operon. J Bacteriol. 180(24):6571-80, 1998. PubMed: NOT_FOUND. Cook GM, Membrillo-Hernandez J, Poole RK. Transcriptional regulation of the cydDC operon, encoding aheterodimeric ABC transporter required for assembly of cytochromes c and bd in Escherichia coli K-12: regulation by oxygen and alternative electron acceptors. J Bacteriol. 179(20):6525-30, 1997. PubMed: NOT_FOUND. Poole,R.K., Hatch,L., Cleeter,M.W., Gibson,F., Cox,G.B. and Wu,G. Cytochrome bd biosynthesis in Escherichia coli: the sequences of the cydC and cydD genes suggest that they encode the components of an ABC membrane transporter. Mol. Microbiol. 10(2): 421-430, 1993. PubMed: 7934832. Pittman MS, Corker H, Wu G, Binet MB, Moir AJ, Poole RK. Cysteine is exported from the Escherichia coli cytoplasm by CydDC, an ABC-type transporter required for cytochrome assembly. J Biol Chem. 2002 Oct 21 PubMed: NOT_FOUND ","","Thu Jan 16 12:27:45 2003","1","","","" "AA02609","1818586","1820244","1659","ATGATTTTAGGGCTGGCGTCCAGTATCGGGTTGCTCACCCTTTCCGGCTGGTTTCTTGCCGCCACCGCCATCGCCGGTTTCGGCTCGCTATTTAACTTTTTCTACCCATCCGCCAGCGTACGCGGTTTGGCAATCGGGCGTACCGTGGCGCGCTACCTTGAAAAAGTGGTCACCCATGACGCCACCTTCCGCGTATTGGCAAAACTGCGTGTGCAGGTGTTTGACAAAATCATTCCGTTAAGCCCTGCGCTGCTCAACCGTTATCGTAACAGCGATTTATTAAACCGCTTGGTTGCCGATGTGGACACCCTCGACAGCCTATATCTTCGCCTCATTGCGCCCTTTATCAGCGCCATAGTGGTGATTGCGTTCATTACCTTTGGCTTGAGTTTTATTAATGCCCCGCTCGCGCTGTTTATCGGTTTCACATTACTGGCGCTCTTGCTGGTTATCCCGACGATTTTTTACCATTTGGGTAACAAATTCGGCGCCAAACTTACCCAATCCCGCGCCCTTTACCGCACGCAATTTATCGAATTTATTCAGGCGCAAGCGGAATTATTGCTGTTTAACGGCGAGGACAAGGTCAAAGAAAAACTGAACCAAACGGAACAACAATGGCAGGCTTACCAACAACGGGAAGCCAATTTATCGGGATTTTCCACCGCACTTTTATTGTTCGCCAACGGTTTGCTGTTATGTGTCACCTTGTGGTTTGCCGCCCAAGCGGATTTAGGCAACGATGAATACCGCATGGCGTTTATCGGCTTATTTGCCTTTGCCGCCCTTGCCTCGTTTGAAATCCTGATGCCTATCGGCGCAGCATTTTTACACATCGGGCAAGTGGTTACCTCTGCCGAGCGGGTAACGGACATTATTGAACAACAGCCGTTATTGGATTTTTCCGGTACGCAAGAAGTGGAACCCGATGAACAACAGCCGTTATTGCAAATGACAAATCTGCATTTTACTTACCCGCAACGCACTAATCCGGCGCTGGTGGATTTAACCCTCAACATTCAAGCCGGCGAAAAAGTTGCCATTTTAGGCAAAACCGGTAGCGGAAAATCCACGTTGTTGCAATTATTAGTTCGTAACTATGATGCCAACCAAGGTGAAATTCTGCTGGCAGGCAAACCGATTCAAACGTATAGCGAAACTGCCCTGCGCCAACAATTTTGCTTCTTGACCCAACGGGTGCACGTGTTCAGCGACACATTGCGCAATAACCTGCAACTTGCCAATCATGCTCCGTTGAGCGATGAAAAAATGCTTGCCGTGCTACAACAAGTGGGCTTGGAAAAACTCGTGAATCAGGAACAAGGCTTGGATTTATGGTTCGGTGACGGCGGTCGTCCGTTATCCGGCGGTGAACAACGCCGTTTGGGCTTGGCTCGGGTGCTATTAAATGACGCACCGATTTTACTGTTAGATGAGCCAACGGAAGGTTTGGATCGTGAAACGGAACGCCACATTCTGCAGGCAATTTTGGCACACAGCCGTGGAAAAACATTAATTATGGTGACGCACCGCTTAACCGCTATTGAACAATTTGATCAGTTGGTCATGATTGATAACAATCAATTAATTGAACAAGGTGCTTATCTGGATTTAATCAGTAAAGAAAATGGCTTTTTCAAGCAATTGACACAACGCATT","","","64295","MILGLASSIGLLTLSGWFLAATAIAGFGSLFNFFYPSASVRGLAIGRTVARYLEKVVTHDATFRVLAKLRVQVFDKIIPLSPALLNRYRNSDLLNRLVADVDTLDSLYLRLIAPFISAIVVIAFITFGLSFINAPLALFIGFTLLALLLVIPTIFYHLGNKFGAKLTQSRALYRTQFIEFIQAQAELLLFNGEDKVKEKLNQTEQQWQAYQQREANLSGFSTALLLFANGLLLCVTLWFAAQADLGNDEYRMAFIGLFAFAALASFEILMPIGAAFLHIGQVVTSAERVTDIIEQQPLLDFSGTQEVEPDEQQPLLQMTNLHFTYPQRTNPALVDLTLNIQAGEKVAILGKTGSGKSTLLQLLVRNYDANQGEILLAGKPIQTYSETALRQQFCFLTQRVHVFSDTLRNNLQLANHAPLSDEKMLAVLQQVGLEKLVNQEQGLDLWFGDGGRPLSGGEQRRLGLARVLLNDAPILLLDEPTEGLDRETERHILQAILAHSRGKTLIMVTHRLTAIEQFDQLVMIDNNQLIEQGAYLDLISKENGFFKQLTQRI","1820242","From GenBank (gi:1169169) This protein is somehow involved in the cytochrome D branchof aerobic repiration and seems to be a component of atransport system. ","ABC transporter, ATP-binding protein/permease","Inner membrane, Cytoplasm","","
InterPro
IPR001140
Domain
ABC transporter, transmembrane region
PF00664\"[64-272]TABC_membrane
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[454-496]TQ9CN68_PASMU_Q9CN68;
PF00005\"[343-527]TABC_tran
PS50893\"[316-551]TABC_TRANSPORTER_2
PS00211\"[454-468]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[342-534]TAAA
InterPro
IPR011527
Domain
ABC transporter, transmembrane region, type 1
PS50929\"[1-284]TABC_TM1F
InterPro
IPR014223
Family
ABC transporter, CydDC cysteine exporter (CydDC-E) family, permease/ATP-binding protein CydC
TIGR02868\"[2-512]TCydC: ABC transporter, CydDC cysteine expor
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[281-549]Tno description
PTHR19242\"[11-552]TATP-BINDING CASSETTE TRANSPORTER
PTHR19242:SF55\"[11-552]TABC TRANSPORTER (CYDD)
signalp\"[1-23]?signal-peptide
tmhmm\"[15-35]?\"[111-131]?\"[136-156]?\"[220-240]?\"[255-275]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.3e-47) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 332-378 1.8e-19 IPB001140B 451-489 7.7e-16 IPB001140C 504-533 1.6e-09","Residues 502 to 549 match (3e-08) PD:PD006957 which is described as ATP-BINDING TRANSMEMBRANE PROTEOME COMPLETE TRANSPORTER ABC MULTIDRUG GLYCOPROTEIN RESISTANCE REPEAT ","","","","","","","","","","","Wed Mar 17 09:30:21 2004","Thu May 13 16:51:26 2004","","","Thu May 13 16:51:26 2004","Wed Mar 17 09:30:21 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02609 is paralogously related to AA01510 (5e-55), AA01961 (2e-48), AA01509 (1e-44), AA01393 (4e-40), AA02805 (5e-37), AA02606 (3e-33), AA02440 (1e-22), AA01684 (2e-21), AA02080 (1e-20), AA01524 (3e-19), AA01867 (4e-19), AA02331 (1e-18), AA01616 (1e-18), AA01422 (2e-16), AA00415 (2e-16), AA02353 (3e-16), AA02718 (6e-16), AA00700 (1e-15), AA02550 (4e-15), AA00858 (1e-14), AA02899 (4e-14), AA00799 (5e-14), AA02140 (2e-13), AA01820 (2e-13), AA02786 (3e-13), AA01656 (4e-13), AA02152 (8e-13), AA01051 (1e-12), AA02324 (1e-12), AA00207 (2e-12), AA01824 (3e-12), AA00591 (7e-12), AA02320 (1e-11), AA00751 (1e-11), AA01645 (2e-11), AA02573 (4e-11), AA00933 (6e-11), AA01555 (1e-10), AA02898 (2e-10), AA01779 (2e-10), AA02484 (5e-10), AA01757 (5e-09), AA02225 (7e-09), AA01568 (3e-08), A02145 (3e-08), AA00061 (3e-08), AA01456 (4e-07), AA00934 (9e-06), AA01947 (2e-05), AA01291 (2e-04), AA02146 (5e-04) and AA02642 (0.001).","Wed Mar 17 09:30:21 2004","","","","","Residues 343 to 527 (E-value = 9.7e-47) place AA02609 in the ABC_tran family which is described as ABC transporter (PF00005)","Wed Mar 17 09:30:21 2004","","","","Winstedt L, Yoshida K, Fujita Y, von Wachenfeldt C.Cytochrome bd biosynthesis in Bacillus subtilis: characterization of the cydABCD operon.J Bacteriol. 1998 Dec;180(24):6571-80.PMID: 9852001Cook GM, Membrillo-Hernndez J, Poole RK.Transcriptional regulation of the cydDC operon, encoding a heterodimeric ABC transporter required for assembly of cytochromes c and bd in Escherichia coli K-12: regulation by oxygen and alternative electron acceptors.J Bacteriol. 1997 Oct;179(20):6525-30.PMID: 9335308Poole RK, Hatch L, Cleeter MW, Gibson F, Cox GB, Wu G.Cytochrome bd biosynthesis in Escherichia coli: the sequences of the cydC and cydD genes suggest that they encode the components of an ABC membrane transporter.Mol Microbiol. 1993 Oct;10(2):421-30.PMID: 7934832Le Douarin NM, Rival JM.A biological nuclear marker in cell culture: recognition of nuclei in single cells and in heterokaryons.Dev Biol. 1975 Nov;47(1):215-21.PMID: 1239389","","Thu May 13 16:51:26 2004","1","","","" "AA02610","1820511","1821374","864","ATGACCGCACTTCATCAACTTATCGACCTGTTAAAACTGGAAAAAATCGACGATTTACTCTTTCGCGGCGAAAGTCAGGATTTAGGCTTTCGTCAGGTTTTCGGCGGACAAGTCGTGGCGCAAGCCCTTTCTGCCGCCATTCAGGTGGCGCCGACAGATCGCTTTTTACATTCTTGCCATGCGTATTTTTTAGCCCCGGGCGACAGCCAATATCCGATCATTTATGATGTGGAAATTCTACGCGAAGGCAGAAATTTCACCGCCATGCGCGTCAAAGCCATTCAGCACAAATCACCGATTTACCACATCACCGCCTCTTTCCAAACCTTGGAGCAAGGCTTTGAGCATCAAAGTGAGATGCCAAAAGTGGAGGCCCCCGATGCACTCATGTCGGAAAGCTCGGTGATCCAGCAAATGGCGCAAATGATTCCGGAAGCGGTGCGCGATAAATTTACGGCGGAACGCCCCTTTGATATTCGCACCAAATACCTGAATAACCCATTCCACGGGCGCAAACTGCCGCCACAGCAATTTTCTTGGGTGCGTACCAACGGAAAAGCGCCGACGGATTATCGCATTCAACAATACCTGCTCGCCTATTTTTCGGATTTTCACTGCATTTTGACTGCACTTCATCCGCACGAAAAAGGCTTTTTACAAAAAGGCATGAAAGTCGCCACCATCGACCATTCAATTTGGTTCCATCGTCCTTTCGATATGAACGACTGGCTGCTATACGCCATTGAAAGCAACAACGCCTACGCCGCCCGTGGTTTGGCGCGCGGTCAGTTCTTCTCCGCTGACAGCAGACTAATTGCCACCACGCAGCAGGAAGGGCTGATTCGTTATCTTCCGGAAGAACAA","","","33080","MTALHQLIDLLKLEKIDDLLFRGESQDLGFRQVFGGQVVAQALSAAIQVAPTDRFLHSCHAYFLAPGDSQYPIIYDVEILREGRNFTAMRVKAIQHKSPIYHITASFQTLEQGFEHQSEMPKVEAPDALMSESSVIQQMAQMIPEAVRDKFTAERPFDIRTKYLNNPFHGRKLPPQQFSWVRTNGKAPTDYRIQQYLLAYFSDFHCILTALHPHEKGFLQKGMKVATIDHSIWFHRPFDMNDWLLYAIESNNAYAARGLARGQFFSADSRLIATTQQEGLIRYLPEEQ","1821372","From GenBank (gi:135612):TesB can hydrolyze a broad range of acyl-coa thioesters. Its physiological function is not known.","acyl-CoA thioesterase II","Cytoplasm","","
InterPro
IPR003703
Family
Acyl-CoA thioesterase
PIRSF004843\"[1-287]TAcyl-CoA thioesterase II, TesB type
PTHR11066\"[9-286]TACYL-COA THIOESTERASE
PF02551\"[16-114]T\"[146-280]TAcyl_CoA_thio
TIGR00189\"[11-282]TtesB: acyl-CoA thioesterase II
noIPR
unintegrated
unintegrated
G3DSA:3.10.129.10\"[1-115]T\"[130-282]Tno description
PTHR11066:SF10\"[9-286]TACYL-COA THIOESTERASE II


","No hits to the COGs database.","Significant hit ( 3.5e-63) to 7/7 blocks of the IPB003703 family, which is described as \"Acyl-CoA thioesterase\". Interpro entry for IP:IPR003703. IPB003703A 48-74 3.1e-16 IPB003703B 79-111 4.2e-16 IPB003703C 113-123 0.00024 IPB003703D 149-156 17 IPB003703E 159-174 0.12 IPB003703F 227-243 2.2e-13 IPB003703G 266-279 0.018","Residues 21 to 95 match (5e-08) PD:PD482003 which is described as PROTEOME II COMPLETE ACYL-COA THIOESTERASE TESB ","","","","","","","","","","","Thu Jan 16 12:36:44 2003","Thu Jan 16 12:36:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02610 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 146 to 280 (E-value = 6.7e-67) place AA02610 in the Acyl_CoA_thio family which is described as Acyl-CoA thioesterase (PF02551)","","","",""," Li,J., Derewenda,U., Dauter,Z., Smith,S. and Derewenda,Z.S.Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzymeNat. Struct. Biol. 7 (7), 555-559 (2000)PubMed: 10876240Swenson,L., Green,R., Smith,S. and Derewenda,Z.S.Crystallization of thioesterase II from Escherichia coliJ. Mol. Biol. 236 (2), 660-662 (1994)PubMed: 8107148Naggert,J., Narasimhan,M.L., DeVeaux,L., Cho,H., Randhawa,Z.I.,Cronan,J.E. Jr., Green,B.N. and Smith,S.Cloning, sequencing, and characterization of Escherichia coli thioesterase IIJ. Biol. Chem. 266 (17), 11044-11050 (1991)PubMed: 1645722","","Thu Jan 16 12:36:44 2003","1","","","" "AA02611","1821654","1821529","126","ATGAAAAAAATTATCCTGGCAGTATTTATTCTATTTAGCCTGGCAGCGTGTTCCGTAGGTGTCGGTGCAAGTGGCGGTTCCAATGGCGTTGGTGTAGGGTTCGGTGTTGGCACCGGTGTACGTTTA","","","3993","MKKIILAVFILFSLAACSVGVGASGGSNGVGVGFGVGTGVRL","1821529","","hypothetical protein","Outer membrane, Cytoplasm, Extracellular","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
PS51257\"[1-17]TPROKAR_LIPOPROTEIN
signalp\"[1-20]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 16:19:47 2004","Mon Feb 23 16:19:47 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02611 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 16:19:47 2004","","","","","","","","","","","","","1","","","" "AA02613","1822391","1821654","738","ATGTCAGACTCAGTGACGTTTTCTTTTGCGCAATATGTTCAGCGGCTCTTAGCAGAACATAAAGGGGAGCGGGTCTATTATTTTACCTACGGGAACAAAAATTATTGGCTGAAACAACCGGAACAATTGAAAGGCGTGTGGCATTTGCTAAAACCGCATCCGCAGCAGGCATTTCAAAACGAGCTCCGGAGTTTGCAGTATCTTGCACAACGAAAAGCACCGGTGCCGAAATTAGTCGCTTTCGGTAAAGATTATCTGGTGCTGGAAGATGGTGGCAAAAGCGTAGCAAATTGGGTTGACGATAATATCCCAACGCAAACCAAACAACAGATTCTGCTGGATTGTGCTAAAGCCTTGGCGCAGTTACATCAACAGGGATTGGTGCATGGGCGCCCGGCGATTCGGGATATTTTATGGCATGACGGCAGGGTGTTATTTATTGACTTTGAAGTGGACGCAACAAAACGGAACTTACCTCGTCAGAAAGTGCGCGATTTGATTTTGTTTATTTATAATTTATGTCGTGAGGAAAATATTTCCGATGAAACTGTCCGCACGGTTATGCGCGGTTATGAACAGGATTGTGAACCTCAAGAGTGGCAGGATATGATGTCTTCCGTATGCCATTATCGTTTTTTGTATTATTTATTATTGCCGTTTAAATATATTGCTAAAAAAGATTTAATCGGGGTGTATCGTTTATTTAGAAATGTGGAAAAAGTGAAAAGAGGCGAAGTA","","","30882","MSDSVTFSFAQYVQRLLAEHKGERVYYFTYGNKNYWLKQPEQLKGVWHLLKPHPQQAFQNELRSLQYLAQRKAPVPKLVAFGKDYLVLEDGGKSVANWVDDNIPTQTKQQILLDCAKALAQLHQQGLVHGRPAIRDILWHDGRVLFIDFEVDATKRNLPRQKVRDLILFIYNLCREENISDETVRTVMRGYEQDCEPQEWQDMMSSVCHYRFLYYLLLPFKYIAKKDLIGVYRLFRNVEKVKRGEV","1821652","","conserved hypothetical protein","Cytoplasm","","No hits reported.","BeTs to 4 clades of COG3642COG name: Mn2+-dependent serine/threonine protein kinaseFunctional Class: TThe phylogenetic pattern of COG3642 is aompkzy-------------------Number of proteins in this genome belonging to this COG is","","Residues 9 to 235 match (2e-61) PD:PD118736 which is described as COMPLETE PROTEOME HI1326 BMEI2006 ATU0257 CYTOSOLIC PM0673 ","","","","","","","","","","","","Thu Jan 16 12:41:08 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02613 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 191 (E-value = 3.2e-05) place AA02613 in the Kdo family which is described as Lipopolysaccharide kinase (Kdo/WaaP) family (PF06293)","","","","","","","","1","","","" "AA02614","1823092","1822460","633","ATGCAGAAATATATCACCAGGGTGGTCTTATGCTCATCAATTTTACTGTTATCGGCGTGTGGTTCGTTATCTGAAATGAAAACCGCCGGTACGTCGGGTTCCGTCACTGAGGTGATGCAGGCAAATGCCGATGTGAAAGCGTTACTGCAAAAAGCGGAAACCTTGCCGACATTTGAATATGTCGACAACAATACGCAATATACAGCTTACTTAAATGGACAACCGGAATTGATTAAAGTTAGCAACGGTAGTGACAATAAATTATTTTTCTATAAAGGCGGGAAAGTTTCCGTCGTGCAGGAAAATGGCAAAGTTCACAACATTGACGCGGCAAACCAAGCACAAAAAGCCTTAGTCGCCGAAGCCATGAAACTGTACAAAATGTTGGGTTCAAACAATGCGGATAAAGGCGTGGTTAACGTGAAAACCGGTAACGATGCTAAATTAAATTACCTTTGTATTGCAAAAATTCAACAGGTGGCACAAACTTCACGCGTATTTCGTAGTTCTGCTAACCACGCTAACAGCAATTCCCGCTTAACTGCTGATGTGCGTTTAAACGGTAATCGGTTCTATAAAATGGATTGCCGGTTGGCCGGCAACCGGGTTGCAAAATTAAGTTTAATTAAGAAA","","","22992","MQKYITRVVLCSSILLLSACGSLSEMKTAGTSGSVTEVMQANADVKALLQKAETLPTFEYVDNNTQYTAYLNGQPELIKVSNGSDNKLFFYKGGKVSVVQENGKVHNIDAANQAQKALVAEAMKLYKMLGSNNADKGVVNVKTGNDAKLNYLCIAKIQQVAQTSRVFRSSANHANSNSRLTADVRLNGNRFYKMDCRLAGNRVAKLSLIKK","1822458","","conserved hypothetical protein","Extracellular, Outer membrane","","
noIPR
unintegrated
unintegrated
PS51257\"[1-20]TPROKAR_LIPOPROTEIN
signalp\"[1-24]?signal-peptide


","No hits to the COGs database.","","Residues 1 to 211 match (1e-39) PD:PD400710 which is described as PROTEOME COMPLETE PM0674 ","","","","","","","","","","","","Thu Jan 16 12:42:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02614 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02615","1823180","1823761","582","ATGTTTGCTTGGTTAAAACCAAAATTTGTGACATTACTTTGTGCACTTTTGCTGACCTCAACATTATCAACATCCGCATTTGCCCTTGCCATCGGCGAAAATGAAATCAACCAATTGCTGGCTCGGCACAATAATTATAAAAATAATTATGGCATCCCCGGTCTTGCCAGCGTGGATTACAGTCTGCACGATTTCAGTGCCAGAATCGGACAATCCGCGGGAAAACGCTTGGAATTGAGCGGCATTATCGACGGCTTATTCAAACTGCCTACCGATCAGTTTTCCGCCAAATTGAATCTCACCTTCGACACTGTGCCTTATTATGATGCGCCAAAAGGTGCGATTTATTTGAAGGATATTCGCGTACTACGCTGGTCCGGCTCGCCTGAACAATACATGGGGCAAATTCAAAGTCTGGTGCCGTTACTCACCAACAATATCGCCACCTATCTGAGCAACACGCCGGTTTATACCCTAGACGAAAAAAATCCACGGGATATGATGATTAAACAAGCCGCTAAAGGCATTCGGGTAGAACAAGGCAGATTGGAAGTGGACACCTTTGATAATTTGCTAAAACCA","","","24391","MFAWLKPKFVTLLCALLLTSTLSTSAFALAIGENEINQLLARHNNYKNNYGIPGLASVDYSLHDFSARIGQSAGKRLELSGIIDGLFKLPTDQFSAKLNLTFDTVPYYDAPKGAIYLKDIRVLRWSGSPEQYMGQIQSLVPLLTNNIATYLSNTPVYTLDEKNPRDMMIKQAAKGIRVEQGRLEVDTFDNLLKP","1823759","","conserved hypothetical protein","Periplasm, Cytoplasm","","
InterPro
IPR010835
Family
Protein of unknown function DUF1439
PF07273\"[8-189]TDUF1439
noIPR
unintegrated
unintegrated
PD103888\"[31-183]TQ7VLQ5_HAEDU_Q7VLQ5;
signalp\"[1-28]?signal-peptide
tmhmm\"[9-31]?transmembrane_regions


","No hits to the COGs database.","","Residues 31 to 189 match (8e-20) PD:PD103888 which is described as LIPOPROTEIN PROTEOME COMPLETE YCEB MEMBRANE SIGNAL PRECURSOR STY1202 ORF ","","","","","","","","","","","","Thu Jan 16 12:43:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02615 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 189 (E-value = 1.1e-23) place AA02615 in the DUF1439 family which is described as Protein of unknown function (DUF1439) (PF07273)","","","","","","","","1","","","" "AA02616","1824735","1823824","912","ATGTTATACGGATTGGATATTGGCGGAACCAAAATTGAGTTGGCGGTGTTTAACTCGCAGTTGGAGAAGCAATATCGCGAACGGGTGGAAACGCCGAAAACCAGCTATGAAGATTGGCTGAATACTATTGCCGATTTGGTGAAAAAAGCCGACGAAAAATTCGGCGGTAAAGGTTCCGTCGGCTTAGGCATTCCGGGCTTTGTGAATCAAACCACCGGCATTGCGGAAATCACTAATATCCGCGTGGCGGATAACAAACCCATTTTGTGCGACTTATCCGCTATTTTAGAACGCGAAGTACGCGCCGAAAACGATGCTAACTGCTTTGCCTTGTCGGAAGCCTGGGATGCGGAAAACGCCGAATATCCTTCCGTATTAGGTCTAATTTTAGGCACCGGATTTGGCGGCGGTTTTGTGTTAAACGGCAAGATTCATTCCGGGCAAACCGGCATGGCGGGCGAATTAGGGCATTTGCAATTGAACTACCATGCGTTGAAATTACTCGGCTGGGACAAGGCACCGATTTACGACTGCGGTTGCGGCAATAAAGCCTGTTTGGACACCTATTTATCCGGTCGCGGTTTTGAAATGTTATACCGCGATTTAAAAGGCGAATCCTTATCGGCCAAAGAAATTATTCAACGTTTCTACGCCAGCGATAAAAGTGCGGTGGATTTTGTCGGCGTTTTTGTGGAGCTTGCCGTGATTTCCATCGGCAATATCATTACCGCCTTTGACCCGCATTTGATCGTACTCGGCGGCGGATTGTCCAATTTCGATTATTTATACGGTGCCTTACCGAAAGCTTTACCGCCGCATTTAATGCGCAGCGCCAAAGTGCCGGTGATTAAAAAAGCCAAATATGGCGACTCCGGCGGCGTGCGTGGCGCCGCGGCGTTGTTTTTATCCCGT","","","32761","MLYGLDIGGTKIELAVFNSQLEKQYRERVETPKTSYEDWLNTIADLVKKADEKFGGKGSVGLGIPGFVNQTTGIAEITNIRVADNKPILCDLSAILEREVRAENDANCFALSEAWDAENAEYPSVLGLILGTGFGGGFVLNGKIHSGQTGMAGELGHLQLNYHALKLLGWDKAPIYDCGCGNKACLDTYLSGRGFEMLYRDLKGESLSAKEIIQRFYASDKSAVDFVGVFVELAVISIGNIITAFDPHLIVLGGGLSNFDYLYGALPKALPPHLMRSAKVPVIKKAKYGDSGGVRGAAALFLSR","1823822","There is a reference in the A.a. hit, but it does not seem related to this gene (20435309).*****","transcriptional regulator","Cytoplasm, Inner membrane","","
InterPro
IPR000169
Active_site
Peptidase, cysteine peptidase active site
PS00639\"[161-171]?THIOL_PROTEASE_HIS
InterPro
IPR000600
Family
ROK
PF00480\"[4-195]TROK
PS01125\"[130-157]TROK
noIPR
unintegrated
unintegrated
G3DSA:3.30.420.160\"[105-298]Tno description
PTHR18964\"[63-304]TROK FAMILY
PTHR18964:SF13\"[63-304]TGLUCOSE KINASE


","No hits to the COGs database.","Significant hit ( 1.1e-21) to 5/5 blocks of the IPB000600 family, which is described as \"ROK family\". Interpro entry for IP:IPR000600. IPB000600A 4-11 0.12 IPB000600B 99-113 1.2e-05 IPB000600C 130-139 0.015 IPB000600D 152-158 0.27 IPB000600E 178-187 0.0045Significant hit ( 2.5e-05) to 3/7 blocks of the IPB003836 family, which is described as \"Glucokinase\". Interpro entry for IP:IPR003836. IPB003836A 6-16 0.095 IPB003836D 129-162 8.2 IPB003836E 184-199 13","Residues 1 to 66 match (3e-09) PD:PD222994 which is described as KINASE PROTEOME COMPLETE GLUCOKINASE SUGAR GLUCOSE TRANSCRIPTIONAL TRANSFERASE FAMILY ROK ","","","","","","","","","","","Thu Jan 16 13:03:27 2003","Thu Jan 16 12:53:36 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02616 is paralogously related to AA02470 (4e-17) and AA01880 (1e-11).","","","","","","Residues 4 to 195 (E-value = 6.5e-79) place AA02616 in the ROK family which is described as ROK family (PF00480)","","","","","","","","1","","","" "AA02618","1825547","1824789","759","ATGGCAGTCCGATTCTTATTTATGGTTATGAATATGTTAAAAAGATTGTCATTATATACGCTATTGCTTTGTCTTGTCCCTGTTTTTGTCTGGTTGTCTGCATGGCAGTGGAGCGGAAATCTGGTTTTTGAGGATTACGAACATCCTTTATATTGGCTAACGGAAACCGGCAGTGTGCCTTATGCCATTATCACTTGCGGCGTTTTTGCGCTGCTCTTTTTACCATTATTTTCTAATCGTAAACAATGGATTTTAGCTGTTGCTGTAATGGCTTTTTCGATGGTGGTGACACAGGGATTAAAATCCGGTTTAAAAAATGTATTTGCCGAACCGCGCCCTTTCGTTACTTACATCGCCGAACAAACCGGCACAGGCACCGACGCTTTTTATGCGCAAGATCGTAAAGCGCGGGCGCAAATCGTTGACCGATTCTATCAAACCCAGTCTTCGGTGCCTGAATGGATTAAAGGGCATTATGCCGATGAAGTGGGCTATTCTTTTCCTTCCGGACACACCATTTTCGCCGCCAGCTGGCTGATGTTAACCGTGGGCTTTGTGCAATTACTCGGCAACAGAAAAGGGAACGCGAAATTATTACTTGGCTTTATGAGCATTTGGGCGCTATTGATGTTGGTCAGTCGCCTGCGTTTCGGTATGCATTATCCGATAGATTTATTGATTTCCGTTTTAATGGCGTGGCTGGTGCATTGGGTGATGTTCGCATTTTTAGCCAAAAAGCGGTATTTCCAAAAAGCGGAA","","","29074","MAVRFLFMVMNMLKRLSLYTLLLCLVPVFVWLSAWQWSGNLVFEDYEHPLYWLTETGSVPYAIITCGVFALLFLPLFSNRKQWILAVAVMAFSMVVTQGLKSGLKNVFAEPRPFVTYIAEQTGTGTDAFYAQDRKARAQIVDRFYQTQSSVPEWIKGHYADEVGYSFPSGHTIFAASWLMLTVGFVQLLGNRKGNAKLLLGFMSIWALLMLVSRLRFGMHYPIDLLISVLMAWLVHWVMFAFLAKKRYFQKAE","1824787","From GenBank (gi:1172464):This protein hydrolizes phosphatidylglycerophosphare, phosphaditic acid, and lysophosphaditic acid; the pattern of activities varies according to subcellular location.****There is a primary reference in the A.a. hit, however, it does not seem to be related to this gene. (PMID: 10978535) **","phosphatidylglycerophosphatase B","Inner membrane, Cytoplasm","","
InterPro
IPR000326
Family
Phosphoesterase, PA-phosphatase related
PF01569\"[86-248]TPAP2
SM00014\"[85-240]TacidPPc
noIPR
unintegrated
unintegrated
G3DSA:1.20.144.10\"[104-253]Tno description
PTHR14969\"[164-244]TSPHINGOSINE-1-PHOSPHATE PHOSPHOHYDROLASE
signalp\"[1-32]?signal-peptide
tmhmm\"[15-35]?\"[57-77]?\"[82-100]?\"[169-189]?\"[194-214]?\"[220-240]?transmembrane_regions


","No hits to the COGs database.","","Residues 154 to 183 match (7e-09) PD:PD247748 which is described as PROTEOME COMPLETE PDPB ORF16 ","","","","","","","","","","","Thu Jan 16 13:00:20 2003","Thu Jan 16 12:57:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02618 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 72 to 248 (E-value = 2.7e-15) place AA02618 in the PAP2 family which is described as PAP2 superfamily (PF01569)","","","","","Filiatrault,M.J., Gibson,B.W., Schilling,B., Sun,S., Munson,R.S. Jr. and Campagnari,A.A. Construction and Characterization of Haemophilus ducreyiLipooligosaccharide (LOS) Mutants Defective in Expression ofHeptosyltransferase III and beta 1,4-Glucosyltransferase:Identification of LOS Glycoforms Containing Lactosamine Repeats.Infect. Immun. 68(6): 3352-3361, 2000. PubMed: 10816485 cho,T. Membrane-bound phosphatases in Escherichia coli: sequence of the pgpB gene and dual subcellular localization of the pgpB product. J.Bacteriol. 170(11): 5117-5124, 1998. PubMed: 2846511. Dillon DA, Wu WI, Riedel B, Wissing JB, Dowhan W, Carman GM. The Escherichia coli pgpB gene encodes for a diacylglycerolpyrophosphate phosphatase activity. J Biol Chem. 1996 Nov 29;271(48):30548-53. PubMed: NOT_FOUND ","","Thu Jan 16 14:26:35 2003","1","","","" "AA02619","1825603","1826253","651","ATGACAAAAATTGAATTAGTTGCCCAAGCGAATTTACCGACAGAATTCGGTCTGTTTAAAATCGTGGGCTTTGAATTTCCCGACACCAAAAAAGAACACGTTGCGTTGGTTTTAGGCGACATCCGCAATTCGGACGAACCGGTATTAGCGCGTATTCATTCCGAATGCTTAACCGGCGACGCATTACACAGCCTAAAATGCGACTGCGGTTTCCAACTGGCGGCGGCGTTACGTCAAATTCAACAGGAAGGGCGCGGCGTATTAATTTACCACCGCGAAGAAGGCAGAGGCATCGGCTTAATTAACAAAATCCGCGCGTATTCCCTACAAGATCAGGGCATGGACACCATTGAAGCCAACCTGGCTTTAGGCTTTGCCGCCGATGAACGCAATTTTGGCGTATGTGCGGATATTTTTGATTTATTGGGCGTAAAACAAATTCGTCTGCTCACCAATAATCCGGACAAAATCGAAACTATGAAACAGGCAGGAATCAACGTAGTTGCGCGGGTGCCGTTAAATGTGGGTGAGAATCGCTATAACACCGCCTATTTGGACACCAAAGCAAAAAAAATGGGGCATTTTATCGTGCATAACGGCGAACAGCATTTAATGGAATGCCCGTATTGTCAGGAAGAAGTGCCGAAAAAA","","","24178","MTKIELVAQANLPTEFGLFKIVGFEFPDTKKEHVALVLGDIRNSDEPVLARIHSECLTGDALHSLKCDCGFQLAAALRQIQQEGRGVLIYHREEGRGIGLINKIRAYSLQDQGMDTIEANLALGFAADERNFGVCADIFDLLGVKQIRLLTNNPDKIETMKQAGINVVARVPLNVGENRYNTAYLDTKAKKMGHFIVHNGEQHLMECPYCQEEVPKK","1826251","There is a reference in the A.a. hit that does not seem related to this protein (PMID: 10978535)******","GTP cyclohydrolase II","Cytoplasm","","
InterPro
IPR000926
Domain
GTP cyclohydrolase II
PF00925\"[4-173]TGTP_cyclohydro2
TIGR00505\"[5-196]TribA: GTP cyclohydrolase II
noIPR
unintegrated
unintegrated
PTHR21327\"[11-163]TGTP CYCLOHYDROLASE II-RELATED
PTHR21327:SF1\"[11-163]TGTP CYCLOHYDROLASE II


","BeTs to 18 clades of COG0807COG name: GTP cyclohydrolase IIFunctional Class: HThe phylogenetic pattern of COG0807 is a--p--yqvdrlbcefghsnuj-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-90) to 5/5 blocks of the IPB000926 family, which is described as \"GTP cyclohydrolase II\". Interpro entry for IP:IPR000926. IPB000926A 13-40 3.7e-13 IPB000926B 51-73 2.6e-20 IPB000926C 93-127 3.4e-28 IPB000926D 128-156 7.9e-18 IPB000926E 184-194 7.1e-06","Residues 41 to 173 match (1e-07) PD:PD323418 which is described as GTP RIBOFLAVIN CYCLOHYDROLASE BIOSYNTHESIS HYDROLASE ","","","","","","","","","","","Thu Jan 16 13:04:55 2003","Thu Jan 16 13:13:50 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02619 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 173 (E-value = 3.7e-115) place AA02619 in the GTP_cyclohydro2 family which is described as GTP cyclohydrolase II (PF00925)","","","","","Bereswill S, Fassbinder F, Volzing C, Covacci A, Haas R, Kist M.Hemolytic properties and riboflavin synthesis of Helicobacter pylori: cloning and functional characterization of the ribA gene encoding GTP-cyclohydrolase II that confers hemolytic activity to Escherichia coli.Med Microbiol Immunol (Berl). 1998 Mar;186(4):177-87.PMID: 9574900Fuller,T.E. and Mulks,M.H. Characterization of Actinobacillus pleuropneumoniae riboflavin biosynthesis genes J. Bacteriol. 177 (24), 7265-7270 (1995) PubMed: 8522537 ","","Thu Jan 16 13:17:11 2003","1","","","" "AA02620","1826535","1827272","738","ATGTTTAAAACCTTAAGTAAACTTATTTCATCTTCCATTTCTATGGCATTTTTAGTTGTTTTAGGCTGGTCCACTGCTTATGCCTATGGTTGGGGACAATCTTATTTTTACGGCTTTCCATGGTGGTATGTAGATGTAGGCACGGGCAATGTAGCTCGTAGTTTCGGCTATGTGATCTGGGTTAGCATTATTCTTCTCAGCACCTATTTAATCGGTTTATTCGGACTGAAGAAAACCCAGCCTTACATGACAGATGCTTGCCTTAGTCTGCTAAGAACCTATATTTTATGTACCGTTTTCCTTATCCCCGGCGTTATTGGTTACATTTTGACTGTTGGGAAAATAAGTTATCTTTTTATACTCACTTACATCATCATAACGTTTATTGTTACCCTGCTGTTTAAGCATTACATTCGGAAACACATAAACACAATCTCGCTCAATACCACAATTACGTTTCTGTATCGAAATAAAAGCTATGTGATGTTGTCCACTTATTGCTATTTTGTAATCTGTGCCTTCATTGTCGGCTACAGCCGCCCCCACTTCAAAACAGTGTTTGATTCCTTGGAAATTGAAGGTAGAGCCTATTACGTTTTAGCAAAATATAGCGATACCTTTATTTTAGCTAAAAGCATTCACGCGACTAATGGTAACTTTTATCTATACAAAATCGATCCTAATTCCTTATGTCACGTTCAAGTAATCAACATGGAAAGCATACCGAAACAACCTGAA","","","28273","MFKTLSKLISSSISMAFLVVLGWSTAYAYGWGQSYFYGFPWWYVDVGTGNVARSFGYVIWVSIILLSTYLIGLFGLKKTQPYMTDACLSLLRTYILCTVFLIPGVIGYILTVGKISYLFILTYIIITFIVTLLFKHYIRKHINTISLNTTITFLYRNKSYVMLSTYCYFVICAFIVGYSRPHFKTVFDSLEIEGRAYYVLAKYSDTFILAKSIHATNGNFYLYKIDPNSLCHVQVINMESIPKQPE","1827270","THERE IS A REFERENCE IN THE HIT TO THE AA GENE (gi:7592819) THAT DOES NOT SEEM RELATED TO THIS GENE (PubMed: 10978535)******","orf14; possible membrane protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-28]?signal-peptide
tmhmm\"[15-37]?\"[56-76]?\"[88-108]?\"[114-134]?\"[159-179]?transmembrane_regions


","No hits to the COGs database.","","Residues 189 to 246 match (2e-25) PD:PD256794 which is described as ORF14 ","","","","","","","","","","","Thu Jan 16 14:29:00 2003","Thu Jan 16 14:29:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02620 is paralogously related to AA01799 (1e-117).","","","","","","","","","","","","","","1","","4","" "AA02621","1827348","1827244","105","TTGGTTTTTTTCACCGCACTTTTTGAGCGGAGCATTATTTTTTATTCACAAAGTACGCCCAAAAAACAGCTGTTTATTCAGGTTGTTTCGGTATGCTTTCCATGT","","","4070","LVFFTALFERSIIFYSQSTPKKQLFIQVVSVCFPC","1827244","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 16:18:05 2004","Mon Feb 23 16:18:05 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02621 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 16:18:05 2004","","","","","","","","","","","","","1","","4","" "AA02623","1828039","1827440","600","GTGTATGGCGATGTGGCGGAAAATCACGCCTTATCCAAGGAAGATGCTGCGTATGCGCCAAGTAGTCCGTATTCCGCTTCAAAAGCCTCTGCCGATCATTTGGCTCACGCTTGGCACCGCACTTATGGCTTGCCGATAATAATCACTAATTGCGCCAATAATTACGGCCCTTATCAATATCCTGAAAAGCTGATTCCGTTTATGATCTCCAATGCATTGAATGGCAACGGGCAGCAGATTCGTGATTTGCTTTATGTGGAAGACCATGTTCGCGCCTTGTATTTGGTGCTTATGAAAGGCAATGTAGGCGAAAGCTACAATATCAGCAGCCATTGCGAAAAAACAAATTTGGCTGTGATTTGTGCCATTTGTGAGCTCTTGGAAGAATTGGCGCCCAATAAACCGATGGGCGTAAAATATTATGCTGATTTAATTGTTCATGTCACCGATCGTCCCGGCCACGATCGCCGCTACGCCCTTGATGCCACAAAAATTCAACAAGAATTAAGCTGGCAGCCACAAGAAAATTTCTTCTCCGGAATACGAAAAACCGTGCAATGGTACATAGATAACCGGAATTGCTCAGATAAAGTGCGGTCG","","","22592","VYGDVAENHALSKEDAAYAPSSPYSASKASADHLAHAWHRTYGLPIIITNCANNYGPYQYPEKLIPFMISNALNGNGQQIRDLLYVEDHVRALYLVLMKGNVGESYNISSHCEKTNLAVICAICELLEELAPNKPMGVKYYADLIVHVTDRPGHDRRYALDATKIQQELSWQPQENFFSGIRKTVQWYIDNRNCSDKVRS","1827438","","dTDP-D-glucose 4,6-dehydratase","Cytoplasm, Extracellular","","
InterPro
IPR001509
Family
NAD-dependent epimerase/dehydratase
PF01370\"[1-109]TEpimerase
InterPro
IPR002198
Family
Short-chain dehydrogenase/reductase SDR
PS00061\"[11-39]?ADH_SHORT
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[1-129]Tno description
PTHR10366\"[1-193]TNAD DEPENDENT EPIMERASE/DEHYDRATASE
PTHR10366:SF41\"[1-193]TDTDP-GLUCOSE 4,6-DEHYDRATASE


","BeTs to 13 clades of COG1088COG name: dTDP-D-glucose 4,6-dehydrataseFunctional Class: MThe phylogenetic pattern of COG1088 is a-mpkz---drlbcef-hsn-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 9.6e-09) to 3/5 blocks of the IPB001509 family, which is described as \"NAD dependent epimerase/dehydratase family\". Interpro entry for IP:IPR001509. IPB001509C 52-58 0.045 IPB001509D 81-88 0.27 IPB001509E 178-188 0.23","Residues 153 to 188 match (8e-10) PD:PD576531 which is described as 46-DEHYDRATASE DTDP-GLUCOSE PROTEOME COMPLETE DTDP-GLUCOSE-46-DEHYDRATASE LYASE DTDP-D-GLUCOSE DEHYDRATASE 6-DEHYDRATASE RMLB ","","","","","","","","","","","","Thu Jan 16 13:41:33 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02623 is paralogously related to AA02647 (5e-72).","","","","","","Residues 2 to 192 (E-value = 3.7e-38) place AA02623 in the Epimerase family which is described as NAD dependent epimerase/dehydratase family (PF01370)","","","","Yoshida,Y., Nakano,Y., Nezu,T., Yamashita,Y. and Koga,T.A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidine diphosphate-D-fucoseJ. Biol. Chem. 274 (24), 16933-16939 (1999)PubMed: 99287888Yoshida,Y., Nakano,Y., Yamashita,Y. and Koga,T.Identification of a genetic locus essential for serotype b-specific antigen synthesis in Actinobacillus actinomycetemcomitansInfect. Immun. 66 (1), 107-114 (1998)PubMed: 9423846","Allard ST, Giraud MF, Whitfield C, Graninger M, Messner P, Naismith JH. The crystal structure of dTDP-D-Glucose 4,6-dehydratase (RmlB) from Salmonella enterica serovar Typhimurium, the second enzyme in the dTDP-l-rhamnose pathway. J Mol Biol. 2001 Mar 16;307(1):283-95. PMID: 11243820 Bozue,J.A., Tullius,M.V., Wang,J., Gibson,B.W. and Munson,R.S. Jr. Haemophilus ducreyi produces a novel sialyltransferase. Identification of the sialyltransferase gene and construction of mutants deficient in the production of the sialic acid-containing glycoform of the lipooligosaccharide J. Biol. Chem. 274 (7), 4106-4114 (1999) PubMed: 9933604 Marolda,C.L. and Valvano,M.A. Genetic analysis of the dTDP-rhamnose biosynthesis region of the Escherichia coli VW187 (O7:K1) rfb gene cluster: identification of functional homologs of rfbB and rfbA in the rff cluster and correctlocation of the rffE gene Journal of bacteriology. 177 (19), 5539-5546 (1995) PubMed: 7559340 ","Tue Feb 11 14:21:23 2003","Thu Jan 16 13:41:33 2003","1","","4","" "AA02626","1829262","1828471","792","ATGCCGTTGAAAAATCCCGAACAGAATTGGCAAAATTACCGCACATTAATTAACGGTAAAATCGCCAGTTGCACGGTTAATTTGGATATTTTTGAGGCATTTTCTCCACAAAAATACAATAAAGTCGTGCAGGTTTCTCTACCTTATGAGCCTGATGAAAATGCTATGCCGACCTTGGATGAACATCATCGTGTTATCACGGAATTGTTCAAAATTCTGATTCAGGTTTCGGCACTATCCGATGTGCTTTATGCCGGGCATATCATTGGTGACGGGCATTTGCAGTTGCATTTTTATTGCGATAAACCGACCGCACTTTTTGATGTGCTTGACCAATTCAAGGAACATATTGATCATACGGGCGTGCAGGATGATCCGAATTGGGACACTTATTTTGACTTTTTGCTGCCGTCGCCATTGGAAATGAAGCTTAACGTTACGGAAGAAATTCTCGATATGTTATTGCAAAACGGCAGAAATTTGGCGGATAACTATCTCATCGAACATACCTTTCAATTTGCCGATGAACAGCTGATGTATCAATTCATGGAAGAAACCAATCTCAGTGACATTTATTTCAACACCATGAGTTACAGCAATGCACCTATTATCTTTTCTGCTTCTGACGAGGAAGACAAAGAAAGTTTTTATATCGTTAAAATTGAACAGGAAATGTCTTTGGATACGGATGAAATTTTTGCTTATGTTGAACAGTTTGAGCGTTTGGCGGAAAAATTTTCCGGTGAATATGTGGGCTGGGAGAGTGACACGATTAATCAGGTGAAAGCGAAT","","","30759","MPLKNPEQNWQNYRTLINGKIASCTVNLDIFEAFSPQKYNKVVQVSLPYEPDENAMPTLDEHHRVITELFKILIQVSALSDVLYAGHIIGDGHLQLHFYCDKPTALFDVLDQFKEHIDHTGVQDDPNWDTYFDFLLPSPLEMKLNVTEEILDMLLQNGRNLADNYLIEHTFQFADEQLMYQFMEETNLSDIYFNTMSYSNAPIIFSASDEEDKESFYIVKIEQEMSLDTDEIFAYVEQFERLAEKFSGEYVGWESDTINQVKAN","1828469","Thre are several hits to previously sequenced genes. References in these records do not seem to refer to this gene, but only a gene region (PubMed: 9805002, 99287888, 98084462, 20135606, 20435309).*****","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR006506
Family
Conserved hypothetical protein 1619
PD023891\"[8-258]TCons_hypoth1619
PF05117\"[6-136]TDUF695
TIGR01619\"[5-258]Thyp_HI0040
InterPro
IPR009671
Family
Protein of unknown function DUF1260
PF06877\"[142-257]TDUF1260
InterPro
IPR014489
Family
Uncharacterised conserved protein UCP017962
PIRSF017962\"[5-264]TUCP017962
noIPR
unintegrated
unintegrated
SSF89946\"[127-255]TSSF89946


","No hits to the COGs database.","","Residues 8 to 258 match (5e-135) PD:PD023891 which is described as PROTEOME COMPLETE GLYCOSYLTRANSFERASE HI0040 TRANSGLYCOSYLASE LYTIC REDUCTASE ORF17 ORF19 DNA ","","","","","","","","","","","Thu Jan 16 14:36:42 2003","Thu Jan 16 13:46:25 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02626 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 6 to 258 (E-value = 2.3e-209) place AA02626 in the DUF695 family which is described as Family of unknown function (DUF695) (PF05117)","","","","Nakano,Y., Yoshida,Y., Yamashita,Y. and Koga,T.A gene cluster for 6-deoxy-L-talan synthesis in ActinobacillusactinomycetemcomitansBiochim. Biophys. Acta 1442 (2-3), 409-414 (1998)PubMed: 99023768","","Tue Feb 11 16:17:11 2003","","1","","4","" "AA02628","1830065","1829265","801","ATGAAAATCATGTCGTTTAACATAAACGGATTAAGAGCCAGACCACATCAATTAGAAGAAATTATTAATAAATATCAACCGGATGTGCTGGGATTACAGGAAATCAAAGTGTCGGATGAGGTCTTTCCGTATGATTTGGTGGATCATCTTGGCTACCACGTCAATCATTTCGGGCAAAAGGGGCATTACGGCGTTGCGTTATTGAGTAAGCAGGTGCCATTGTCGGTGAGAAAAGGGTTTCCGACAGATGATGAGGAAGCGCAAAAGCGGATCATCATGATTGATTTAGAGACGAAATTCGGTCAACTGACTGTTATTAATGGCTATTTCCCGCAGGGGGAAAGCCGTGAACACCCGACTAAATTCCCGGCGAAACAAAAATTTTATGCAGATTTACAGCGTTATTTGGAGCAAGATCATAACGCGCAAAACCCGGTCATTATCATGGGCGATATGAATATCAGTCCTTCCGATTTAGACATTGGTATCGGCGAGGAAAATCGTAAACGTTGGTTGCGGACCGGCAAATGCTCTTTCCTGCCGGAAGAACGCGAATGGTATCAGCGTTTATATGCGTACGGCTTGGAAGATACCTTCCGCCACATGAATCCGACGGTTAATGATAAATTCTCCTGGTTTGATTATCGTTCCAAAGGGTTTGATGATAATCGCGGTTTGCGTATTGACCACATTTTGGCAAATAAAGCCTTGGTGGCACATTGTGTGGATACCGGTATTGCCTTGGATATTCGCGCCATGAATAAGCCTTCTGATCACGCACCGATTTGGGCGGAGTTTAAA","","","32932","MKIMSFNINGLRARPHQLEEIINKYQPDVLGLQEIKVSDEVFPYDLVDHLGYHVNHFGQKGHYGVALLSKQVPLSVRKGFPTDDEEAQKRIIMIDLETKFGQLTVINGYFPQGESREHPTKFPAKQKFYADLQRYLEQDHNAQNPVIIMGDMNISPSDLDIGIGEENRKRWLRTGKCSFLPEEREWYQRLYAYGLEDTFRHMNPTVNDKFSWFDYRSKGFDDNRGLRIDHILANKALVAHCVDTGIALDIRAMNKPSDHAPIWAEFK","1829263","THERE ARE REFERENCES IN THE HITS TO PREVIOUSLY SEQUENCED A.a.GENES THAT DO NOT SEEM RELATED TO THIS GENE IN PARTICULAR BUT MAY REFER TO THE ENTIRE REGION (PubMed: 10673051, 98084462, 99023768, 20435309)****** ","exodeoxyribonuclease III","Cytoplasm","","
InterPro
IPR000097
Family
AP endonuclease, family 1
TIGR00195\"[1-266]TexoDNase_III
PS00726\"[27-36]?AP_NUCLEASE_F1_1
PS00727\"[197-213]TAP_NUCLEASE_F1_2
InterPro
IPR004808
Family
Exodeoxyribonuclease III xth
PTHR22748\"[52-267]TExoIII_xth
TIGR00633\"[1-267]Txth
InterPro
IPR005135
Domain
Endonuclease/exonuclease/phosphatase
PF03372\"[1-266]TExo_endo_phos
noIPR
unintegrated
unintegrated
G3DSA:3.60.10.10\"[1-266]TG3DSA:3.60.10.10
SSF56219\"[1-267]TSSF56219


","No hits to the COGs database.","Significant hit ( 4.5e-74) to 5/5 blocks of the IPB000097 family, which is described as \"AP endonucleases family 1\". Interpro entry for IP:IPR000097. IPB000097A 1-13 2.6e-07 IPB000097B 27-36 0.0016 IPB000097C 59-96 4e-17 IPB000097D 144-178 1.3e-17 IPB000097E 210-257 6.7e-23","Residues 1 to 160 match (1e-07) PD:PD120671 which is described as LYASE ENDONUCLEASE DNA APYRIMIDINIC NUCLEAR AP LYASE-LIKE OR APURINIC-APYRIMIDINIC SITE ","","","","","","","","","","","Thu Jan 16 14:59:31 2003","Thu Jan 16 14:56:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02628 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 266 (E-value = 6.7e-59) place AA02628 in the Exo_endo_phos family which is described as Endonuclease/Exonuclease/phosphatase family (PF03372)","","","","Yoshida,Y., Nakano,Y., Yamashita,Y. and Koga,T.Identification of a genetic locus essential for serotype b-specific antigen synthesis in Actinobacillus actinomycetemcomitansInfect. Immun. 66 (1), 107-114 (1998)PubMed: 98084462Yoshida,Y., Nakano,Y., Nezu,T., Yamashita,Y. and Koga,T.A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidine diphosphate-D-fucoseJ. Biol. Chem. 274 (24), 16933-16939 (1999)PubMed: 99287888","Galhardo RS, Almeida CE, Leitao AC, Cabral-Neto JB.Repair of DNA lesions induced by hydrogen peroxide in the presence of iron chelators in Escherichia coli: participation of endonuclease IV and Fpg.J Bacteriol. 2000 Apr;182(7):1964-8.PMID: 10715004Asad NR, Asad LM, Silva AB, Felzenszwalb I, Leitao AC.Hydrogen peroxide effects in Escherichia coli cells.Acta Biochim Pol. 1998;45(3):677-90.PMID: 991849","Fri Feb 7 15:38:22 2003","Fri Feb 7 15:38:22 2003","1","","4","" "AA02629","1830334","1830212","123","ATGTTTACCCATAAAAAGCTGCACCTTAACTGGTTAGGTGTGGTATCCAATTTTTGGGTGGCAGATCATCAATGTCGGTATGTTAAAAATTGGTCTTTGTGGAATGATTTTGCCATTTTATGC","","","5004","MFTHKKLHLNWLGVVSNFWVADHQCRYVKNWSLWNDFAILC","1830212","","hypothetical protein","Cytoplasm, Extracellular","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 16:16:46 2004","Mon Feb 23 16:16:46 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02629 is paralogously related to AA01176 (2e-05).","Mon Feb 23 16:16:46 2004","","","","","","","","","","","","","1","","4","" "AA02630","1830436","1830534","99","TTGGTTGCAACGCTTGAAAAATACGGAACCAATGAGCTACATCGTCAACATATCAAAGTGAGAAAAATACTCGCCTTTAAGAATGTAGCAGTGAGTAAA","","","3788","LVATLEKYGTNELHRQHIKVRKILAFKNVAVSK","1830534","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 16:15:03 2004","Mon Feb 23 16:15:03 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02630 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 16:15:03 2004","","","","","","","","","","","","","1","","4","" "AA02631","1832024","1830609","1416","ATGAGAAAAACAGAAGGCTCCGCGCCCCTCATCAATAAGATCAGTTTGATTTTCACCGATATGATTTCGTATGTTTTTGCGATTGCGGTGGGCTACTGGCTTTCACCTTTAGATGATTTTTCTCGCGATATTTTGGAACTGAAAGGTTCTATCTATCGGGCGGGTTCCTTTTTCTTGGCGATGTTAGCAAGCATTGGGATTTTGTGGGTATTTTATCGTCATTACACTTACCGTAAGCCATTTTGGGACGAATTGAAAGACACCTATTTTTCACTCTTTGTGATTGCCTTTGTTAATTTGGCGCTATTGGTGTTTGCCAAAGTACCCGATCCTATGGAAACGTGGATTTATGTCTATGGCGTGCTTTTTCTCTGTTTTCCTCTTTTTCGGATCATTTGCAAAAAAGTCCTCAAATTTAACTGTTTGTGGGATATGCCAAGCGTGATCATCGGCACGGGGCGCAATGCTTTTCGTGCATACAAGGCGATTCAAGCTGAGTCTAACCTTGGTTATAAAGTGCAAACCTTTGTTTCTCAACAAGAAAGTTGTGTGCTGGCAAAACACCTAGATTTTATATCTGAGCAGGAATTTTTAAAACATTTGCACCGTTATGAAAAAGTATTTATTGCCTTAGAACACGATCAGGCAGATTTATTGGCATATTGGGTGAAAAAACTCTCGGCGCTGAATTTTCGCAATGTATCTATTATTCCGTCGTTGCAAGGCATCCCACTTTATGGGGCGGAAATTTCGCATTTCTTTAGCTCTGAAACCATTGTGCTGCGGATCCCCAATAAGCTCGCTAAGCGCTCAACCCGTTTGATGAAACGTACTTTTGATATTGTGGTTTCCAGCCTATTGTTGATTCTGCTTGCCCCGCTTTTCTTGGTGCTATTTTTGATGATTCGTAAAGATGGTGGAAAAGCAGTGTATAGCCAAGTTCGTGTCGGGCGAAATCGCAAAGTCTTCAAATGCTATAAACTCCGTACGATGGTGGTTAATTCTCAACAAGTGCTGCGTGAATTATTGGCGAAAGATGAGGAAGCCCGCGAGCAGTGGAATAAAGAGTTTAAACTCAAGAATGACCCTAGAATCACGCCAATCGGCAAAATTTTGCGTAAAACCAGCCTTGATGAGCTGCCGCAGTTATGGAACGTCTTTAAAGGTGAAATGAGCCTTGTTGGCCCTCGCCCTGTAACGAGGCAAGAGTTGAAATACTATGGCGATGACTTAATTTACTACGAAATGGTTCGCCCTGGGCTTTCAGGCTTATGGCAAGTGAGCGGGCGTAATGACATTGGCTACGCCACCCGCGTATATTTAGATGCATGGTATGTGAAAAACTGGTCGTTGTGGAATGATATTGTGATCTTGGCAAAAACCGTCAACATTGTGTTGAGAAGAAAAGGGGCATAT","","","54924","MRKTEGSAPLINKISLIFTDMISYVFAIAVGYWLSPLDDFSRDILELKGSIYRAGSFFLAMLASIGILWVFYRHYTYRKPFWDELKDTYFSLFVIAFVNLALLVFAKVPDPMETWIYVYGVLFLCFPLFRIICKKVLKFNCLWDMPSVIIGTGRNAFRAYKAIQAESNLGYKVQTFVSQQESCVLAKHLDFISEQEFLKHLHRYEKVFIALEHDQADLLAYWVKKLSALNFRNVSIIPSLQGIPLYGAEISHFFSSETIVLRIPNKLAKRSTRLMKRTFDIVVSSLLLILLAPLFLVLFLMIRKDGGKAVYSQVRVGRNRKVFKCYKLRTMVVNSQQVLRELLAKDEEAREQWNKEFKLKNDPRITPIGKILRKTSLDELPQLWNVFKGEMSLVGPRPVTRQELKYYGDDLIYYEMVRPGLSGLWQVSGRNDIGYATRVYLDAWYVKNWSLWNDIVILAKTVNIVLRRKGAY","1830607","THE HITS TO A.a. gene RECORDS HAVE REFERENCES TO REGIONS OF THE A.a. GENOME, BUT DO NOT SEEM TO REFER TO THIS PARTICULAR GENE(98084462, 99287888, 21391794).*******In Salmonella typhimurium a protein with 44% similarity to AA02631 is responsible for transfering galactose-1-phosphate to the lipid precursor undecaprenol phosphate in the first steps of O-polysaccharide biosynthesis [gi:20141709]. ******* ","undecaprenyl-phosphate galactosephosphotransferase homolog","Inner membrane, Cytoplasm","","
InterPro
IPR003362
Family
Bacterial sugar transferase
PF02397\"[276-472]TBac_transf
noIPR
unintegrated
unintegrated
signalp\"[1-27]?signal-peptide
tmhmm\"[15-35]?\"[54-72]?\"[87-109]?\"[115-133]?\"[279-299]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.6e-91) to 5/5 blocks of the IPB003362 family, which is described as \"Bacterial sugar transferase\". Interpro entry for IP:IPR003362. IPB003362A 275-305 1.6e-15 IPB003362B 307-331 1.5e-13 IPB003362C 360-398 1e-36 IPB003362D 418-429 1.2e-05 IPB003362E 438-461 8.1e-15","Residues 301 to 432 match (2e-71) PD:PD001742 which is described as TRANSFERASE COMPLETE PROTEOME GLYCOSYLTRANSFERASE CPSE EXOPOLYSACCHARIDE BIOSYNTHESIS UNDECAPRENYL-PHOSPHATE SYNTHESIS TRANSMEMBRANE ","","","","","","","","","","","Fri Jan 7 18:13:43 2005","Thu Jan 16 15:15:01 2003","","Fri Jan 7 18:13:43 2005","Fri Jan 7 18:13:43 2005","Fri Jan 7 18:13:43 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA02631 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Fri Jan 7 18:13:43 2005","","","","","Residues 276 to 472 (E-value = 1.4e-162) place AA02631 in the Bac_transf family which is described as Bacterial sugar transferase (PF02397)","Fri Jan 7 18:13:43 2005","","","Yoshida,Y., Nakano,Y., Yamashita,Y. and Koga,T.Identification of a genetic locus essential for serotype b-specific antigen synthesis in Actinobacillus actinomycetemcomitansInfect. Immun. 66 (1), 107-114 (1998)PubMed: 98084462Yoshida,Y., Nakano,Y., Nezu,T., Yamashita,Y. and Koga,T.A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidine diphosphate-D-fucoseJ. Biol. Chem. 274 (24), 16933-16939 (1999)PubMed: 99287888","Jiang,X.M., Neal,B., Santiago,F., Lee,S.J., Romana,L.K. and Reeves,P.R.Structure and sequence of the rfb (O antigen) gene cluster of Salmonella serovar typhimurium (strain LT2)Mol. Microbiol. 5 (3), 695-713 (1991)PubMed: 1710759Liu,D., Haase,A.M., Lindqvist,L., Lindberg,A.A. and Reeves,P.R.Glycosyl transferases of O-antigen biosynthesis in Salmonella enterica: identification and characterization of transferase genes of groups B, C2, and E1J. Bacteriol. 175 (11), 3408-3413 (1993)PubMed: 7684736","Fri Feb 7 15:41:42 2003","Thu Jan 16 15:20:44 2003","1","","4","" "AA02632","1832754","1831990","765","ATGGAATTTAATCATGGTGGCACGCGCAATCAAGCTGTTAAATTTGCTAAAAGTTTTGCAGATATTGTTGTGTTTATGACACAAGATGCGATTTTAGCTTCGCCTGATTCATTGGCAAATTTATTAGCGCCTTTTGCGGATCCTGAGGTAACGACGGTGTATGGTAAACAGTTGCCACACGCTAATTCCACGCCTGTTGCCGCTCACGCACGCTATTTTAATTACCCGGCGCAATCGAAATTAAAATCAAAAGCAGATATTCCCTCTTTAGGCATTAAAACGGCTTTTATGTCGAACTCTTTTGCGGCGTATCGTCGCTCGGTGTTTGAAGAACTTGGGGGCTTTCCTGATAATACAATTTTAGCGGAAGATATGTACTTAACCGCCAAAATGGTGTTAGCAGGTTATAAAGTTGCCTATTGTGCGGAAGCAACGGTATTTCATAGCCACAACTATACCTTAAGCCAGGAATTACAACGCTATTTTGACACAGGCGTGTTTCAGCAAGAACAAGGGTGGATTCAGCAAACCTTTGGAAAAATGGCTTCAGAAGGAAAGAAGTTTGTGCTTTCTGAACTCAAATTTCTTGTAAAAAATGCACCGCACTTGTTACCCAAAGCCTTGCTATCAACCTTTGCCAAATGGATTGGCTTTCAACTGGGGTATCATTATCAAAAATTGCCTTATGCGTGGTGTAAGGCATTAAGTATGCACAAAGGATATTGGAAAGATGAGAAAAACAGAAGGCTCCGCGCCCCTCATCAA","","","35920","MEFNHGGTRNQAVKFAKSFADIVVFMTQDAILASPDSLANLLAPFADPEVTTVYGKQLPHANSTPVAAHARYFNYPAQSKLKSKADIPSLGIKTAFMSNSFAAYRRSVFEELGGFPDNTILAEDMYLTAKMVLAGYKVAYCAEATVFHSHNYTLSQELQRYFDTGVFQQEQGWIQQTFGKMASEGKKFVLSELKFLVKNAPHLLPKALLSTFAKWIGFQLGYHYQKLPYAWCKALSMHKGYWKDEKNRRLRAPHQ","1831988"," ","rhamnosyltransferase","Periplasm","","
InterPro
IPR001173
Domain
Glycosyl transferase, family 2
PF00535\"[3-113]TGlycos_transf_2
noIPR
unintegrated
unintegrated
G3DSA:3.90.550.10\"[3-155]Tno description


","BeTs to 6 clades of COG0463COG name: Glycosyltransferases involved in cell wall biogenesisFunctional Class: MThe phylogenetic pattern of COG0463 is aompkzyqvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is","","Residues 96 to 147 match (4e-21) PD:PD007872 which is described as CELLULOSE TRANSFERASE PROTEOME COMPLETE SYNTHASE CATALYTIC SUBUNIT GLYCOSYLTRANSFERASE GLYCOSYL SYNTHASE-LIKE ","","","","","Wed Feb 19 08:54:18 2003","","","","","","Thu Jan 16 15:28:38 2003","Thu Jan 16 14:00:21 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02632 is paralogously related to AA02640 (1e-15) and AA02649 (3e-04).","","","","","","","","","","Yoshida,Y., Nakano,Y., Yamashita,Y. and Koga,T. Identification of a genetic locus essential for serotype b-specific antigen synthesis in Actinobacillusactinomycetemcomitans Infect. Immun. 66 (1), 107-114 (1998) PubMed: 9423846 Yoshida,Y., Nakano,Y., Nezu,T., Yamashita,Y. and Koga,T. A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidinediphosphate-D-fucose J. Biol. Chem. 274 (24), 16933-16939 (1999) PubMed: 10358040","Jiang,X.M., Neal,B., Santiago,F., Lee,S.J., Romana,L.K. and Reeves,P.R.Structure and sequence of the rfb (O antigen) gene cluster of Salmonella serovar typhimurium (strain LT2)Mol. Microbiol. 5 (3), 695-713 (1991)PubMed: 1710759Morona R, Stroeher UH, Karageorgos LE, Brown MH, Manning PA.A putative pathway for biosynthesis of the O-antigen component, 3-deoxy-L-glycero-tetronic acid, based on the sequence of the Vibrio cholerae O1 rfb region.Gene. 1995 Dec 1;166(1):19-31.PMID: 8529890 ","Fri Feb 7 15:45:30 2003","Thu Jan 16 15:40:56 2003","1","","4","" "AA02634","1833822","1832956","867","ATGCCTAAATTTAGTTATTCTGTCATCGTATGCACCCTCAACGGTGCATCTTTTATATCTGCACAGTTAAAAAGTATTTTGACTCAATCAATTTTGCCACAAAAAATTATTGTGTCTGATGATGGTTCAACTGATGGCACATTGGATGTTGTTCAACAGACTTTTTTAGAAGCAAATTTTACTGATTATGAAATTGTTCAAGGTCCGAAAAAAGGTGTGATTGCTAATTTTTTATCGGCATTGGCTTATAGTTCAGCAGACTTTACTTTTTTAGCCGATCAAGATGATATTTGGCATCATAAAAAAGCTGTAACATTTTCAAAAATGGCACAAACACAATCGCCTGATGTACCAACACTCACTTTCAGCGATGCACGTTTGATTGATGAATATAATCAAGAAATTACATCGAGTTTTTTTGTTTATCAAGCTTTAACAGCAGATTGTTTGGTAGATGACTCTATTTTGTATAAAAATTGTGTGCAAGGCGCAGCTTGTATGATTAATCGTGCATTGCGAAACTTAGCATTGGATTCCTTACCTTATATTAATTTATCTGAACTTTATATGCACGATTGGTGGCTGGCGTTGTTGGCACGTTATTACGGCAACACGCAATTTATTGATTTACCTTTGTTAGATTATCGTCAACATAGCCGCAATCAAGTAGGCGTGTTTAATTATAAATGGCGTTTATTTCGTTTCCATGCTTATTGGAAAAACTTTCAGCAAGCTATTCGGCAAGTAAAAATGTTTGAACAATTTGTCAAACAATATGGAAAGCCACATAACTTGCTAATTCGTTCAAAACGACAATACCTTTCAGTGCCAAAATTAAAGCGAGTTTTATTATTGCTATTCGCAAAA","","","33338","MPKFSYSVIVCTLNGASFISAQLKSILTQSILPQKIIVSDDGSTDGTLDVVQQTFLEANFTDYEIVQGPKKGVIANFLSALAYSSADFTFLADQDDIWHHKKAVTFSKMAQTQSPDVPTLTFSDARLIDEYNQEITSSFFVYQALTADCLVDDSILYKNCVQGAACMINRALRNLALDSLPYINLSELYMHDWWLALLARYYGNTQFIDLPLLDYRQHSRNQVGVFNYKWRLFRFHAYWKNFQQAIRQVKMFEQFVKQYGKPHNLLIRSKRQYLSVPKLKRVLLLLFAK","1832954","","rhamnosyltransferase; glycosyltransferase homolog 2","Cytoplasm","","
InterPro
IPR001173
Domain
Glycosyl transferase, family 2
PF00535\"[7-176]TGlycos_transf_2
noIPR
unintegrated
unintegrated
G3DSA:3.90.550.10\"[7-223]TG3DSA:3.90.550.10
PTHR22916\"[12-255]TPTHR22916
SSF53448\"[6-257]TSSF53448


","No hits to the COGs database.","","Residues 7 to 102 match (1e-08) PD:PD023980 which is described as TRANSFERASE PROTEOME COMPLETE GLYCOSYLTRANSFERASE GLYCOSYL BIOSYNTHESIS POLYSACCHARIDE SPORE SUGAR COAT ","","","","","","","","","","","Thu Jan 16 16:00:29 2003","Thu Jan 16 15:57:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02634 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 176 (E-value = 3.3e-20) place AA02634 in the Glycos_transf_2 family which is described as Glycosyl transferase (PF00535)","","","","Nakano,Y., Yoshida,Y., Yamashita,Y. and Koga,T.A gene cluster for 6-deoxy-L-talan synthesis in ActinobacillusactinomycetemcomitansBiochim. Biophys. Acta 1442 (2-3), 409-414 (1998)PubMed: 99023768","","Tue Feb 11 16:24:14 2003","","1","","4","" "AA02635","1834195","1833818","378","ATGACTGCTACTTTACAAGTTTTGCTAGTTATATTTAGTGTTTTATTATTGATTTTAATTATTCGTGATGTCAGCCGCTCAAAAATTATTTTCTCAGATTTTAGTTATTGGCTTCTTTTCTCTATATTTCTAATATTAATTGCTATTTTCCCAAAAATAACAGAATGGCTCGCATTGTTAATGGGTATTAAAACCGTTGCATTCTCAGTTTTTTTAATGGTTGTTACTATGTTGATTATGTTAACATTGAGTTTATCTTTTAGAATATCTATTTTGAATCGCCGTTTTATACAATTAACTCAGAACTTAGCATTGTTAGAAAATGAGAATGCTAGACGATTAGATAAATTAGAAAAAAATTTAAAAATCATTAATGCC","","","14574","MTATLQVLLVIFSVLLLILIIRDVSRSKIIFSDFSYWLLFSIFLILIAIFPKITEWLALLMGIKTVAFSVFLMVVTMLIMLTLSLSFRISILNRRFIQLTQNLALLENENARRLDKLEKNLKIINA","1833816","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR011187
Family
Uncharacterised conserved protein UCP006511
PIRSF006511\"[1-119]TUCP006511


","No hits to the COGs database.","","Residues 1 to 120 match (3e-23) PD:PD472653 which is described as YCBC GLYCOSYLTRANSFERASE PROTEOME TRANSGLYCOSYLASE COMPLETE LYTIC REDUCTASE DNA DTDP-4-RHAMNOSE FOR ","","","","","","","","","","","Thu Jan 16 16:01:33 2003","Thu Jan 16 16:03:08 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02635 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","4","" "AA02636","1834899","1834198","702","ATGAAAATATTGTTGATAATACCTTGTTATAATGAATCTGAGTCTATAATTTCATTATTAGATGAACTAAAAGATTATCCTGAATATGATTATATTGTTATTAATGACTGTTCTAAGGATAATACATCGAAAATTGTAAGAAATTATGGAGCTAACGTTATTGATCTTCCTATAAATTTAGGTTTATCTGGTGGTGTTCAAACTGGAATGATGTACGCAACTAAAAATGATTATGATATTTGTATACAGATTGATGGTGATGGACAACATATGCCATCAGAAATCTATAAACTAGTTGACAAAATTAAAGATGGTGTTGATATTGCAATTAGTTCAAGATTTTTAGAATCTAAAGATAGCTATTCTCAAACGTTTCTAAGAGCCTTAGGTGCAAAACATATTCAATTTTGCATTAAACTTTTCTCAGGGCTTACTCTTACAGATCCAACTAGCGGAATGAGAGCATTTACTAAAAATGTATTTCAACAGATGGCTTATGCAACTAATGAAAGACCTGAACCAGATACAATGCTATATTTTGCTCGATTGGGTTATAGGATAGAAGAAGTTCAAGTAACAATGAGGGAGCGCTTTGCTGGAGAATCTTATTTAACGCCTATTAAAGCAGCTAAGTATATGATTGAAAATACAGTATCATTTTTGTTTGTCGTATTTAAAACTTTAGGAAAAAGAGGTAAAAAG","","","26566","MKILLIIPCYNESESIISLLDELKDYPEYDYIVINDCSKDNTSKIVRNYGANVIDLPINLGLSGGVQTGMMYATKNDYDICIQIDGDGQHMPSEIYKLVDKIKDGVDIAISSRFLESKDSYSQTFLRALGAKHIQFCIKLFSGLTLTDPTSGMRAFTKNVFQQMAYATNERPEPDTMLYFARLGYRIEEVQVTMRERFAGESYLTPIKAAKYMIENTVSFLFVVFKTLGKRGKK","1834196","","glycosyl transferase","Cytoplasm","","
InterPro
IPR001173
Domain
Glycosyl transferase, family 2
PF00535\"[4-165]TGlycos_transf_2
noIPR
unintegrated
unintegrated
G3DSA:3.90.550.10\"[1-217]Tno description
PTHR10859\"[9-225]TGLYCOSYLTRANSFERASE RELATED


","BeTs to 22 clades of COG0463COG name: Glycosyltransferases involved in cell wall biogenesisFunctional Class: MThe phylogenetic pattern of COG0463 is aompkzyqvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is","","Residues 3 to 117 match (8e-13) PD:PD395383 which is described as TRANSFERASE COMPLETE PROTEOME SYNTHASE GLYCOSYLTRANSFERASE MANNOSYLTRANSFERASE DOLICHOL-PHOSPHATE MANNOSE GLYCOSYL DOLICHYL-PHOSPHATE ","","","","","Tue Feb 18 16:38:24 2003","","","","","","Thu Jan 16 16:09:05 2003","Thu Jan 16 16:09:05 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02636 is paralogously related to AA02499 (3e-09), AA01190 (3e-08), AA00492 (8e-08), AA01593 (2e-07) and AA02651 (5e-07).","","","","","","Residues 4 to 165 (E-value = 4.2e-34) place AA02636 in the Glycos_transf_2 family which is described as Glycosyl transferase (PF00535)","","","","","","","","1","","4","" "AA02636.1","1835294","1834911","384","ATACTATATGGGATAGTTATGAAAATCTGGCAGCTAGTTAAATTTTTTTCTGTAGGCGGTATATCAGCTTTAGTTGATATAGGATGCTTATATTTATTTAGTAAGATTTTGCTATGGAATAATGAGTTATCTATTTCATTAGCATTTATATTAGGATTGGTATTTAACTATTTTTCACATACATACTTCACTTTCCAAGAAAAAGCAAATGTTGGAAATCTAGTAAAATATCTTATTCTTTTTTTATTAAATTATATTAATACAATCGTATTAATGTATCTTCTAATAGAGCTTTTACATATTGACATCATTGTAGCAAAAGTAATTACACTTCCAATTATTGCAGTTACTACTTTTGTTATTTCTAAAGTCTGGGTTTATAAA","9.70","3.41","14713","ILYGIVMKIWQLVKFFSVGGISALVDIGCLYLFSKILLWNNELSISLAFILGLVFNYFSHTYFTFQEKANVGNLVKYLILFLLNYINTIVLMYLLIELLHIDIIVAKVITLPIIAVTTFVISKVWVYK","","","possible dTDP-glucose-4-keto-6-deoxy-D-glucose reductase","Inner membrane, Cytoplasm","AA02636.1 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus ducreyi gene.AA02636.1 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus influenzae Rd gene.AA02636.1 has significant similarity to the previously sequenced Actinobacillus actinomycetemcomitans genes 1944169 unnamed protein product (4e-67) and 12232615 dTDP-glucose-4-keto-6-deoxy-D-glucose reductase (1e-52).","
InterPro
IPR007267
Family
GtrA-like protein
PF04138\"[14-127]TGtrA
noIPR
unintegrated
unintegrated
signalp\"[1-23]?signal-peptide
tmhmm\"[15-33]?\"[43-63]?\"[73-93]?\"[99-121]?transmembrane_regions


","BeTs to 6 clades of COG2246COG name: Uncharacterized membrane proteinFunctional Class: SThe phylogenetic pattern of COG2246 is ao-pkz----r-bce------j----Number of proteins in this genome belonging to this COG is","","Residues 15 to 128 match (5e-29) PD:PD303371 which is described as PROTEOME COMPLETE TEICHOIC GTCA ACID GLYCOSYLATION TRANSMEMBRANE WALL CELL MESH ","Sat Feb 28 10:48:22 2004","Sat Feb 28 17:30:51 2004","Sat Feb 28 17:30:51 2004","Sat Feb 28 17:30:51 2004","Sat Feb 28 10:48:22 2004","Sat Feb 28 10:48:22 2004","Sat Feb 28 10:48:22 2004","Sat Feb 28 10:48:22 2004","Sat Feb 28 10:48:22 2004","Sat Feb 28 10:48:22 2004","Sat Feb 28 10:48:22 2004","Sat Feb 28 10:48:22 2004","Sat Feb 28 10:48:22 2004","Sat Feb 28 10:48:22 2004","Sat Feb 28 10:49:48 2004","Sat Feb 28 10:48:22 2004","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA02636.1 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sat Feb 28 10:49:48 2004","Sat Feb 28 10:49:48 2004","No hits to the PDB database.","","","Residues 14 to 127 (E-value = 5.4e-35) place AA02636.1 in the GtrA family which is described as GtrA-like protein (PF04138)","Sat Feb 28 10:48:22 2004","","","Yoshida Y, Nakano Y, Nezu T, Yamashita Y, Koga T.A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidine diphosphate-D-fucose.J Biol Chem. 1999 Jun 11;274(24):16933-9.PMID: 10358040Kaplan,J.B., Perry,M.B., MacLean,L.L., Furgang,D., Wilson,M.E. andFine,D.H.Structural and genetic analyses of O polysaccharide from Actinobacillus actinomycetemcomitans serotype fInfect. Immun. 69 (9), 5375-5384 (2001)PubMed: 11500407","","Sat Feb 28 10:50:22 2004","","1","Sat Feb 28 10:48:22 2004","4","" "AA02637","1836619","1835282","1338","ATGCTATTAAATAAATTTTATTCTAAATTATTTATTTTATTTTATTTTATTTTGACTTTTATTATTGGCGTTATTATAACGCCTCCATATCAGTCACCAGATGAGTTTTATCACTTTCAGAGAGGTTATGCTATATCAAATGGCCAAATAATACCCTCATCTACAGAAAAATTAGATAAAGCTATGATGAAGATGTTATCGATATATGAGGGAATCCCTTATCGAAGTGAAAATAAAGTAACTCATTTTTTAGAAAATGAAGCACAAAATGTAGCTTGGGAGAAGGAATATATTCTTGATGAATCTGCAAATACCAATGTCTATTTCCCTTTGATTTATTTACCTCAGGCATTGGGGAGTTTTCTAGGAAGCACATTAGATTTATCACTATATAATATGTACTATCTAGCCAAGATTTTTACTTTATTAGTATCGATAGCTATTTTATATTTTGCTAGTGTTCAATATAGATTAAGTATTCCTGTATTATTAATCCTTTCTTTACCCATGACAATGTTTCAGATGGGGTCAACAAATCCAGATAGTATTATATTTTCTCTGTCAGTGTTTATTGGTTCCTTACTAGCCAGAGGATTAGATTCAAACTATAATTTTACTCATAAGGATTTCTGTAAATTACTATTTTCTATATTTTTATGTGTGACAGTTAAATTTAATATGCTCGTATTGTTACTACTACCATTCTTTATTTCAAAAAGAAGAGAAATTAGACATGGTTCTATGTATTCTATTTTTATAATCATTCTATCAATTTTGTGGATAGTTTTGGCTATGAAATTAACTGAGGCTCAATCTCACTTCAAAGAAGGCGCATTACATAATTTCTCTTATTATATTTTTCATATGGATGACTTATTTGAAATTTTTAAAAATACTTTAAATCTTACTTATTTAAAATCTTTGCTGAGAATGTTTTTAGGCGTTCTTGGATGGGTTGATACGAAATTTACTATAAATGAGTATCTATTTTTCGGTTCTACTTTATTATTGGCTTATATTTTTCTATTCATTCACAACTTGTATAAACTAAAATATGTTATAGTAAGTGTTCTTTTAGTAGGAGTTGTATTTTTATTTACCCATTTTATTCTCTTGATTACTTATAATGAAATTGGCACAACACAAATAGTAGGAGTTCAAGGACGCTATTTTATTCCGATCATGCTTATTATTTTTTCTTCTTTTATTTTAAAAAAATCAGAAAAGACCAGTAATAATAAAACTATTTCTAAATATTTTATAATTGTACCTTTCTTGTTCTTATTTATATCTAGTTTTATTACAATTAACACTCTTGTTTCTAGATACTATATGGGA","","","51868","MLLNKFYSKLFILFYFILTFIIGVIITPPYQSPDEFYHFQRGYAISNGQIIPSSTEKLDKAMMKMLSIYEGIPYRSENKVTHFLENEAQNVAWEKEYILDESANTNVYFPLIYLPQALGSFLGSTLDLSLYNMYYLAKIFTLLVSIAILYFASVQYRLSIPVLLILSLPMTMFQMGSTNPDSIIFSLSVFIGSLLARGLDSNYNFTHKDFCKLLFSIFLCVTVKFNMLVLLLLPFFISKRREIRHGSMYSIFIIILSILWIVLAMKLTEAQSHFKEGALHNFSYYIFHMDDLFEIFKNTLNLTYLKSLLRMFLGVLGWVDTKFTINEYLFFGSTLLLAYIFLFIHNLYKLKYVIVSVLLVGVVFLFTHFILLITYNEIGTTQIVGVQGRYFIPIMLIIFSSFILKKSEKTSNNKTISKYFIIVPFLFLFISSFITINTLVSRYYMG","1835280","","conserved hypothetical protein (possible membrane protein)","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-27]?signal-peptide
tmhmm\"[10-30]?\"[131-151]?\"[153-173]?\"[179-199]?\"[214-236]?\"[246-264]?\"[299-319]?\"[329-347]?\"[352-372]?\"[386-404]?\"[419-441]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","Thu Jan 16 16:14:16 2003","Thu Jan 16 16:14:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02637 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","4","" "AA02638","1837298","1836609","690","ATGATAATCGGAAATGGAATGCTTGCTAAAGCATTTGAGAGTTTTCATAAGCGTACTTATAATTATATTATTTTTGCCAGTGGTGTATCTAATTCTAATGAAACGTCTTTTGAAAATTTTAATAGAGAAAAAGAACTTTTATTAGAAGTATTGGAGCAGTATAAAGATAAAACAATTGTTTATTTTAGTAGCTGTAGCATTTATGATTCTAGTTTAACTAATTCATTATACGTTTATCATAAAATGTGTATGGAAAGATTGGTTCGAGAAAATTCTAAAAACTATTTAATTGCTAGGCTTCCTCAGGTTATAGGAAAAACTTATTCTCCTACAATAGTCAATTTTTTATTTAATAAAATAAAGAATAGAGAATGTTTTTCTATTTTTGGTAAAGCACATAGAAATTTTATAGATGTAGATGATGTTGTAAAAGTTACTAATTACCTGCTTAAGGAAGGGCTGTTTATTAATTCTATTGTTAATTTAGCATCTACACATCATACGTCAATGTATGAACTTATTCTTTATCTTGAAAAAATTTCTAACCAAAGAGCTTTTTATAATGTGGAAAATAAAGGAAGTAGATATTTTATAGATGTTTCTATATTACAGGATGTTTATCAAAAATTAGGTATCAAATTTGATAAAGACTATGTTGAAAAGGTAATTAATAAATATTATGCTATTAAA","","","27516","MIIGNGMLAKAFESFHKRTYNYIIFASGVSNSNETSFENFNREKELLLEVLEQYKDKTIVYFSSCSIYDSSLTNSLYVYHKMCMERLVRENSKNYLIARLPQVIGKTYSPTIVNFLFNKIKNRECFSIFGKAHRNFIDVDDVVKVTNYLLKEGLFINSIVNLASTHHTSMYELILYLEKISNQRAFYNVENKGSRYFIDVSILQDVYQKLGIKFDKDYVEKVINKYYAIK","1836607","","conserved hypothetical protein (possible reductase)","Cytoplasm","","
InterPro
IPR001509
Family
NAD-dependent epimerase/dehydratase
PF01370\"[1-163]TEpimerase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[47-187]TG3DSA:3.40.50.720
SSF51735\"[47-228]TSSF51735


","BeTs to 7 clades of COG0451COG name: Nucleoside-diphosphate-sugar epimerasesFunctional Class: M,GThe phylogenetic pattern of COG0451 is aompk-yqvdrlbcefghsnuj--t-Number of proteins in this genome belonging to this COG is","","Residues 2 to 226 match (2e-96) PD:PD194689 which is described as REDUCTASE URDR GLYCOSYLTRANSFERASE 4-KETO 4-KETOREDUCTASE TRANSGLYCOSYLASE NDP-HEXOSE LYTIC HOMOLOG DNA ","","","","","","","","","","","Thu Jan 16 16:16:55 2003","Thu Jan 16 16:16:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02638 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","4","" "AA02639","1838526","1837273","1254","ATGAATAAAATTAAAAAGACATTTTCAGTCTTAAATGAGCATGGACTTTTTAGAGGTTCTTTAATTATCTTAAGAAAAATATTGAAGAAATCCCCAGATAATATTATTTTAGGTAAAACTGATATTTTAAAATTCTACAATTTTATTAATTATTCAGCAAACCCACCTAAATTAAAACAATCAATTAATATAAGCTCTCCTAAAATAATTTGGTTTATTCCTGATTTTGGGATAGGTTCTGGAGGGCACCTTAATATCTTTAGAATGATTTATAATTTAGAAAAATTAGATATTCATTCAGATATTACTGTATGTGGTTCTAGCCAGTGGGGAACAGAGGAAGTGATCAAAGACATACTATCGAAACATTTCTTTCCTTTGAATTCTAGAATTTTTATTCTAGAAGATGACTCTGATTTTGAACAATTAACAAGCTATGATATTGCTATGGCGACTTCTTGGCAAACAGCATATTATGTAAATAAATTTAATAATTGCTATAAGAAAGCATACTTTGTGCAAGATTACGAACCATATTTTACTGCCTTAGGAAGTGTTTATTCTTTTGCTGAAGAAACATATAAATTTGGATTTTTTGGAATTACCGCTGGAAACTGGTTATCTGAGAAACTTGAAAAAAAGTATTCGATGCCTTGTAAGCCATTTTCTTTTTCTTACGATAGAGAATTATACGGAATACATAAAAGAAATGAGCCGAGTAAAAAACATATTTTCTTCTATGCTAGACCACCGACAGAAAGGAGAGCTTTTGAACTAGGTTTGTTAGTTTTAGATAAGGTAACAAAGAAAAGACCTGATATTAGTATTATTTTTGCAGGATGGGATGTTTCTAGTTATGAAATCCCATTTCATCATTTAAATGCAGGTATTGTGAAACTAGATGAGTTATCTAACTTATACTCTCAATGTGACGCAGCTCTTGTTTTATCTTTTACTAATTTATCTTTACTTCCTCTAGAATTACTAGCGAGTGGTTGCCCTGTCGTGATGAACAAAGGGAATAATAATGATTGGATTGATATCGATAAAAAATTATTTATCTATTCTAATAATATAGATGAACTAGCCAATACATTAATTGATGTTGTAGATAAAAAAATAAATGTAGATTTTGATTATGTAAATCAGTTTTTGTCTAGCACATCTTGGGAAAATGAAGCAAGAAAAGTTAAATCAATTATTCATTCTATTCTAAATGAGGAAACTGATGATAATCGGAAATGGAATGCTTGC","","","48258","MNKIKKTFSVLNEHGLFRGSLIILRKILKKSPDNIILGKTDILKFYNFINYSANPPKLKQSINISSPKIIWFIPDFGIGSGGHLNIFRMIYNLEKLDIHSDITVCGSSQWGTEEVIKDILSKHFFPLNSRIFILEDDSDFEQLTSYDIAMATSWQTAYYVNKFNNCYKKAYFVQDYEPYFTALGSVYSFAEETYKFGFFGITAGNWLSEKLEKKYSMPCKPFSFSYDRELYGIHKRNEPSKKHIFFYARPPTERRAFELGLLVLDKVTKKRPDISIIFAGWDVSSYEIPFHHLNAGIVKLDELSNLYSQCDAALVLSFTNLSLLPLELLASGCPVVMNKGNNNDWIDIDKKLFIYSNNIDELANTLIDVVDKKINVDFDYVNQFLSSTSWENEARKVKSIIHSILNEETDDNRKWNAC","1837271","","conserved hypothetical protein","Outer membrane, Cytoplasm","","
InterPro
IPR001296
Domain
Glycosyl transferase, group 1
PF00534\"[228-397]TGlycos_transf_1
noIPR
unintegrated
unintegrated
SSF53756\"[295-407]TSSF53756


","No hits to the COGs database.","","Residues 289 to 345 match (2e-15) PD:PD590923 which is described as GLYCOSYLTRANSFERASE PROTEOME TRANSGLYCOSYLASE COMPLETE LYTIC REDUCTASE ALR4488 DNA DTDP-4-RHAMNOSE WBBX ","","","","","","","","","","","Thu Jan 16 16:26:34 2003","Thu Jan 16 16:24:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02639 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 228 to 397 (E-value = 5.4e-05) place AA02639 in the Glycos_transf_1 family which is described as Glycosyl transferases group 1 (PF00534)","","","","","","","","1","","4","" "AA02640","1839497","1838529","969","ATGAAAGCCTCAATAATTATTCCACTCAAAAATGGTGGAGATATTTTTAAGCAAGTTTTATCTAGTGTTTTATTACAAAAATTAGACGCTCCATTTGAGGTTATTGTAATTGATTCTGGTTCTAAAGATGGTTCTGTTGAATATTTAAATAATATTATAAAAAACCATGATAATGTTAGATTATATCAAATTAAACCTTATGAATTTGGGCATGGAAAAACAAGAAATTATGGAGCAAGCTTATCCAAAGGTGAATTTTTAGTTTTCATCACTCAAGATGCCCTTCCTGCAAATGAATTTTGGCTAGAAGAAATGATTAAACCATTTTCCTTAGACGAAAACATTCAAGGAGTATTTGGTAAGCATCTGCCATATGAAGATTGTGATATATTTGAAAAAAACAATCTCTATACGCATTTTAATAATTTTGGTAAAGGAATTGTAGTTTATAAAATAGAAGATAAAGCACGCTATGACTCAGATGAAGGATATAGACATCTGCTTTGTTTCTATTCTGATAATTCTTCGGCAATGAGAAAATGTATTTGGGACAAGTATCCATATGATGATGTCGATTTTGCTGAAGATCAAATCTGGGCTAAACGAATAATCGAATTAGGATATTTTAAAGCATATAATGAAAATGCCATTGTATTTCACTCACATAATTATTCTTTTAAAGAAATGCTGATGAGATCTTTTGACGATCACAAAGGATTGTATAAGATTTATGGATATAAATCTGTTAAAAATATTTTTTATCTACCTATTTATATCATAAAACATACAATTAATGATATGAGATTTCTAAAAACAAAAAAATTATCTAAGAAAGAAAAATTGTATTGGTCATATTTTTCTCTAATAAAAAATACTGTTAAATATACAGGTGCATATTTTGGACCAAAAGGCACAAATAATAAATTAATTACTAAGTTATTCTCTCGTGAATTAATTCTAAGGAATAAA","","","37946","MKASIIIPLKNGGDIFKQVLSSVLLQKLDAPFEVIVIDSGSKDGSVEYLNNIIKNHDNVRLYQIKPYEFGHGKTRNYGASLSKGEFLVFITQDALPANEFWLEEMIKPFSLDENIQGVFGKHLPYEDCDIFEKNNLYTHFNNFGKGIVVYKIEDKARYDSDEGYRHLLCFYSDNSSAMRKCIWDKYPYDDVDFAEDQIWAKRIIELGYFKAYNENAIVFHSHNYSFKEMLMRSFDDHKGLYKIYGYKSVKNIFYLPIYIIKHTINDMRFLKTKKLSKKEKLYWSYFSLIKNTVKYTGAYFGPKGTNNKLITKLFSRELILRNK","1838527","","rhamnosyltrasferase","Cytoplasm","","
InterPro
IPR001173
Domain
Glycosyl transferase, family 2
PF00535\"[4-187]TGlycos_transf_2
noIPR
unintegrated
unintegrated
G3DSA:3.90.550.10\"[1-226]TG3DSA:3.90.550.10
PTHR22916\"[9-145]T\"[164-285]TPTHR22916
SSF53448\"[2-220]TSSF53448


","BeTs to 20 clades of COG0463COG name: Glycosyltransferases involved in cell wall biogenesisFunctional Class: MThe phylogenetic pattern of COG0463 is aompkzyqvdrlbcefghsnujx-twNumber of proteins in this genome belonging to this COG is","","Residues 4 to 97 match (4e-07) PD:PD023980 which is described as TRANSFERASE PROTEOME COMPLETE GLYCOSYLTRANSFERASE GLYCOSYL BIOSYNTHESIS POLYSACCHARIDE SPORE SUGAR COAT ","","","","","","","","","","","Thu Feb 6 10:17:29 2003","Thu Jan 16 16:32:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02640 is paralogously related to AA02632 (2e-15) and AA00492 (5e-04).","","","","","","Residues 4 to 187 (E-value = 8.3e-29) place AA02640 in the Glycos_transf_2 family which is described as Glycosyl transferase (PF00535)","","","","","Jiang,X.M., Neal,B., Santiago,F., Lee,S.J., Romana,L.K. and Reeves,P.R.Structure and sequence of the rfb (O antigen) gene cluster of Salmonella serovar typhimurium (strain LT2)Mol. Microbiol. 5 (3), 695-713 (1991)PubMed: 1710759","","Thu Jan 16 16:32:24 2003","1","","4","" "AA02642","1840120","1839497","624","ATGTTCCAAGAATTTTTATCATTAAATGATGTTTCTTTTAAAGTTAAAAAGGGTGAATCTTGGGGATTGATTGGTACTAATGGCTCAGGAAAATCTACACTACTAAAACTTATCTGTGGAATTCTAAAACCATATAAAGGAAAACTTGAAGTTCATGGAAAGATTTCTCCTCTTATAGAGCTAGGAGCTGGATTTGATGGAGAATTAACGGCAAGAGAAAACATATATTTAAATGGGGCATTGTTAGGATATGATAAATCTTTAATGGATACTCATTTTGAAGAAATAATTGAATTTGCTGAATTAAACGAGTTTATTGATGTTCCTATTAAAAACTTTTCTTCGGGAATGTCTGCTAGATTAGGTTTTTCCATTGCTACAATAGTTAAACCTGAAATCCTTATCATTGACGAGGTGCTAGCTGTTGGTGATGCGGCATTTCAGGAAAAATGTAAAAAGAGAATGACCGAAATGTTAGAAAGTGGGACAACTTTATTATTTGTATCTCACTCTGTCGATCAGGTAAAAGAGCTTTGCCAAAAAGCTATATGGTTAGATAAAGGAAATGTCAAAGCTATTGGTGATGTTGAAGAAATTACAAATTTATACATGGGAAAAAATGCA","","","27172","MFQEFLSLNDVSFKVKKGESWGLIGTNGSGKSTLLKLICGILKPYKGKLEVHGKISPLIELGAGFDGELTARENIYLNGALLGYDKSLMDTHFEEIIEFAELNEFIDVPIKNFSSGMSARLGFSIATIVKPEILIIDEVLAVGDAAFQEKCKKRMTEMLESGTTLLFVSHSVDQVKELCQKAIWLDKGNVKAIGDVEEITNLYMGKNA","1839495","From GenBank (gi:2492555):This protein may form an ATP-driven O-antigen export apparatus, in association with RfbA. ","ABC transporter, ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[113-155]TQ8PCV1_XANCP_Q8PCV1;
PF00005\"[18-188]TABC_tran
PS50893\"[1-208]TABC_TRANSPORTER_2
PS00211\"[113-127]?ABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[17-205]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[2-201]Tno description
PTHR19222\"[1-204]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF2\"[1-204]TSIALIC ACID ABC TRANSPORTER


","BeTs to 12 clades of COG1134COG name: ABC-type polysaccharide/polyol phosphate transport system, ATPase componentFunctional Class: GThe phylogenetic pattern of COG1134 is a------q--rlbc-fghsnujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 2.6e-19) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 7-53 9e-16 IPB001140B 110-148 0.14 IPB001140C 165-194 1.3e+02","Residues 8 to 203 match (1e-08) PD:PD416480 which is described as VI POLYSACCHARIDE ATP-BINDING VEXC INNER EXPORT PROTEOME MEMBRANE COMPLETE BIOSYNTHESIS ","","","","","","","","","","","Wed Jan 29 12:08:51 2003","Thu Jan 16 16:41:10 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02642 is paralogously related to AA02140 (3e-17), AA00415 (7e-16), AA02320 (7e-15), AA01645 (7e-15), AA01656 (1e-14), AA00700 (2e-14), AA00858 (4e-14), AA01051 (5e-14), AA00799 (6e-14), AA02899 (1e-13), AA02353 (1e-12), AA01568 (2e-12), AA02805 (8e-12), AA02718 (8e-12), AA01779 (8e-12), AA02786 (3e-11), AA01524 (6e-11), AA02898 (1e-10), AA02550 (1e-10), AA00933 (1e-10), AA02440 (5e-10), AA02080 (7e-10), AA01961 (3e-09), AA01456 (3e-09), AA00207 (3e-09), AA01616 (6e-09), AA01555 (6e-09), AA01867 (1e-08), AA02606 (1e-08), AA01510 (3e-08), AA01422 (4e-08), AA02324 (7e-08), AA02573 (1e-07), AA01820 (4e-07), AA02331 (7e-07), A02145 (7e-07), AA00751 (1e-06), AA02226 (2e-06), AA02152 (2e-06), AA02484 (3e-06), AA01947 (3e-06), AA01684 (3e-06), AA01393 (4e-06), AA00061 (6e-06), AA01509 (1e-05), AA01569 (2e-05), AA02225 (5e-05), AA01824 (1e-04) and AA02609 (3e-04).","","","","","","Residues 18 to 188 (E-value = 3.5e-39) place AA02642 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","Yoshida Y, Nakano Y, Yamashita Y, Koga T.Identification of a genetic locus essential for serotype b-specific antigen synthesis in Actinobacillus actinomycetemcomitans.Infect Immun. 1998 Jan;66(1):107-14.PMID: 9423846Nakano,Y., Yoshida,Y., Yamashita,Y. and Koga,T.A gene cluster for 6-deoxy-L-talan synthesis in ActinobacillusactinomycetemcomitansBiochim. Biophys. Acta 1442 (2-3), 409-414 (1998)PubMed: 99023768","Kelly,R.F. and Whitfield,C.Clonally diverse rfb gene clusters are involved in expression of afamily of related D-galactan O antigens in Klebsiella speciesJ. Bacteriol. 178 (17), 5205-5214 (1996)PubMed: 8752339","Tue Feb 11 16:39:22 2003","Thu Jan 16 16:41:10 2003","1","","4","" "AA02643","1841025","1840237","789","ATGATTAAATTCTTATTAGATAAAACAAATAATTTTTTTTCCTACAGAGAGCTATTTAAACAACTAATTTATAGAGATATTAAATTAAAATATAGACGTAGCTATCTAGGGTATCTATGGAGCATTTTAAATCCATTAATGGTAATGTTTGTTTTATTAATTGTTTTCTCTAATTTATTTAAATTTGATATTCCGAATTTTTCCTTATATCTTTTATCTGGACAAATACTATTTAACTTTATGGTTGAAGCAACCACACTATCTGTAAGTTCCATAACAGGTAACGGTTCATTGCTAAAAAAGATATATGTACCAAAATATATTTTCACCATATCTAAAGTTGGAAGTTCATTAGTAAATCTAATTTTTTCATTTGGCGCATTGCTAATTGTAATGCTGTTTACTGACGCAAATTTCTCAATAAATATTCTTTTTATACCTTTTATTCTATTGCAAATATTTATTTTTAGTTTAGGATTAGGATTATGGTTAGCCTCTATTTCTGTTTTTTTTAGGGATATTCAGTATCTCTGGGGAGTTTTCTTAACAATGTGGATGTATCTTACGCCTATATTTTATCCTGTTTCAATTATATCAGAGAGCTATCAAGCTATTTATAAAAATCTTAACCCTATGTTTTCATACATAGAACAATTTAGACAAATTGTTTTATTTTCAAAATTTCCAGAAACAAATTTTATTTTATTAGGCATATTTTTTTCTTTGATAACATTGTTTTTAGGTACTTGGTATTTTAACAAGAAACAAGATGAATTTATATTGTACATA","","","31043","MIKFLLDKTNNFFSYRELFKQLIYRDIKLKYRRSYLGYLWSILNPLMVMFVLLIVFSNLFKFDIPNFSLYLLSGQILFNFMVEATTLSVSSITGNGSLLKKIYVPKYIFTISKVGSSLVNLIFSFGALLIVMLFTDANFSINILFIPFILLQIFIFSLGLGLWLASISVFFRDIQYLWGVFLTMWMYLTPIFYPVSIISESYQAIYKNLNPMFSYIEQFRQIVLFSKFPETNFILLGIFFSLITLFLGTWYFNKKQDEFILYI","1840235","From GenBank (gi:2501363):This protein may form an ATP-driven O-antigen export apparatus, in association with RfbB.","ABC transporter, membrane spanning permease","Inner membrane, Cytoplasm","","
InterPro
IPR000412
Family
ABC-2
PS51012\"[36-255]TABC_TM2
InterPro
IPR013525
Domain
ABC-2 type transporter
PF01061\"[17-224]TABC2_membrane
InterPro
IPR013526
Family
ABC-2 transporter
PR00164\"[38-59]T\"[143-167]T\"[180-199]TABC2TRNSPORT


","BeTs to 12 clades of COG1682COG name: ABC-type polysaccharide/polyol phosphate export systems, permease componentFunctional Class: MThe phylogenetic pattern of COG1682 is a------q--rlbc-fghsnujx---Number of proteins in this genome belonging to this COG is","","Residues 11 to 133 match (2e-09) PD:PD392625 which is described as ABC PROTEOME COMPLETE POLYSACCHARIDE PERMEASE TRANSPORTER ABC-TRANSPORTER ABC-2 RFBA-1 RFBA-2 ","","","","","","","","","","","Tue Feb 11 16:27:03 2003","Thu Jan 16 16:51:10 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02643 is paralogously related to AA02474 (5e-04).","","","","","","Residues 9 to 260 (E-value = 2.4e-110) place AA02643 in the ABC2_membrane family which is described as ABC-2 type transporter (PF01061)","","","","Kaplan JB, Perry MB, MacLean LL, Furgang D, Wilson ME, Fine DH.Structural and genetic analyses of O polysaccharide from Actinobacillus actinomycetemcomitans serotype f.Infect Immun. 2001 Sep;69(9):5375-84.PMID: 11500407Yoshida Y, Nakano Y, Yamashita Y, Koga T.Identification of a genetic locus essential for serotype b-specific antigen synthesis in Actinobacillus actinomycetemcomitans.Infect Immun. 1998 Jan;66(1):107-14.PMID: 9423846Nakano,Y., Yoshida,Y., Yamashita,Y. and Koga,T.A gene cluster for 6-deoxy-L-talan synthesis in ActinobacillusactinomycetemcomitansBiochim. Biophys. Acta 1442 (2-3), 409-414 (1998)PubMed: 99023768","Guo,D., Bowden,M.G., Pershad,R. and Kaplan,H.B.The Myxococcus xanthus rfbABC operon encodes an ATP-binding cassette transporter homolog required for O-antigen biosynthesisand multicellular developmentJ. Bacteriol. 178 (6), 1631-1639 (1996)PubMed: 8626291","Tue Feb 11 16:27:03 2003","Thu Jan 16 16:51:10 2003","1","","4","" "AA02644","1841598","1841062","537","ATGAAAGTTATTGATACTAAAATTCCCGATGTAAAACTATTAGAACCACAAGTGTTCGGTGATGAACGCGGTTTCTTTATGGAAACTTTCCGTGATGAATGGTTTAGAAAAAATGTAGCAGATCGCATATTTGTACAAGAAAATCATTCAAAATCCATCAAAGGCGTGTTACGCGGTTTACATTATCAAACAGAAAATACACAAGGCAAATTAGTTCGTGTTATTTCTGGTGCGGTATTTGATGTGGCTGTGGATATGCGTGGAAACTCGTTAACTTTTGGGCAATGGGTAGGTGAAATCTTATCTGCCGAGAATAAGCACCAACTATGGGTGCCGGAAGGTTTTGCTCACGGTTTTTATGTGTTGACAGATGAAGCTGAATTTACTTATAAATGTACGGATTACTACAATCCAAAAGCCGAACATTCACTGATTTGGAATGATGAAACGATTGGTATTGAATGGCCGCTTTATGGTGAACCGAGTTTATCGGCTAAGGACTTAGCAGGTAAAGTATTGGCAGAAACGGTAAAATTT","","","20509","MKVIDTKIPDVKLLEPQVFGDERGFFMETFRDEWFRKNVADRIFVQENHSKSIKGVLRGLHYQTENTQGKLVRVISGAVFDVAVDMRGNSLTFGQWVGEILSAENKHQLWVPEGFAHGFYVLTDEAEFTYKCTDYYNPKAEHSLIWNDETIGIEWPLYGEPSLSAKDLAGKVLAETVKF","1841060","","dTDP-4-keto-6-deoxy-D-glucose-3,5-epimerase","Cytoplasm","","
InterPro
IPR000888
Family
dTDP-4-dehydrorhamnose 3,5-epimerase related
PD001462\"[1-175]TdTDP_sugar_isom
PF00908\"[3-176]TdTDP_sugar_isom
TIGR01221\"[2-177]TrmlC
InterPro
IPR011051
Domain
Cupin, RmlC-type
SSF51182\"[1-176]TRmlC_like_cupin
InterPro
IPR014710
Domain
RmlC-like jelly roll fold
G3DSA:2.60.120.10\"[1-176]TRmlC-like_jellyroll
noIPR
unintegrated
unintegrated
PTHR21047\"[1-157]TPTHR21047


","No hits to the COGs database.","Significant hit ( 5.6e-59) to 4/4 blocks of the IPB000888 family, which is described as \"dTDP-4-dehydrorhamnose 3,5-epimerase\". Interpro entry for IP:IPR000888. IPB000888A 13-26 4.3e-09 IPB000888B 52-63 3.1e-06 IPB000888C 68-96 7.9e-19 IPB000888D 130-164 1.5e-20","Residues 1 to 173 match (2e-98) PD:PD001462 which is described as 35-EPIMERASE PROTEOME DTDP-4-DEHYDRORHAMNOSE COMPLETE ISOMERASE EPIMERASE DTDP-6-DEOXY-D-GLUCOSE-35-EPIMERASE RMLC DTDP-4-KETO-6-DEOXYGLUCOSE-35-EPIMERASE DTDP-L-RHAMNOSE ","","","","","Mon Feb 17 07:38:41 2003","","","","","","Thu Jan 16 17:19:07 2003","Thu Jan 16 17:22:53 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02644 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 176 (E-value = 6.4e-112) place AA02644 in the dTDP_sugar_isom family which is described as dTDP-4-dehydrorhamnose 3,5-epimerase (PF00908)","","","","Yoshida,Y., Nakano,Y., Nezu,T., Yamashita,Y. and Koga,T.A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidine diphosphate-D-fucoseJ. Biol. Chem. 274 (24), 16933-16939 (1999)PubMed: 10358040","Graninger M, Kneidinger B, Bruno K, Scheberl A, Messner P.Homologs of the Rml enzymes from Salmonella enterica are responsible for dTDP-beta-L-rhamnose biosynthesis in the gram-positive thermophile Aneurinibacillus thermoaerophilus DSM 10155.Appl Environ Microbiol. 2002 Aug;68(8):3708-15.PMID: 12147463 Wang L, Qu W, Reeves PR.Sequence analysis of four Shigella boydii O-antigen loci: implication for Escherichia coli and Shigella relationships.Infect Immun. 2001 Nov;69(11):6923-30.PMID: 11598067Giraud MF, Leonard GA, Field RA, Berlind C, Naismith JH.RmlC, the third enzyme of dTDP-L-rhamnose pathway, is a new class of epimerase.Nat Struct Biol. 2000 May;7(5):398-402.PMID: 1080273Tsuda H, Yamashita Y, Shibata Y, Nakano Y, Koga T.Genes Involved in Bacitracin Resistance in Streptococcus mutans.Antimicrob Agents Chemother. 2002 Dec;46(12):3756-64.PMID: 1243567","Thu Jan 16 17:19:07 2003","Mon Feb 17 07:38:41 2003","1","","4","" "AA02645","1842479","1841604","876","ATGGCAAAATTTCTGATTACAGGCGCAAACGGGCAAGTGGGCTACTGTTTAACCCAACAATTGCAAGGCAAACACGAAATTTTAGCCGTCGATCATGATGAGCTTGATATTACAAACCAAAATGCGGTGAAAAAAACGGTCGAAAATTTTCGTCCTGATGTAGTTATCAACGCCGCAGCACACACTGCGGTAGATCGTGCAGAAACTGAAATTGAGCTTTCCGAGGCCATTAATGTAAAAGGTCCGCAATACTTGGCGGAAACCGCGAAAAGTGTTGGTGCAGCAATTTTACATATTTCAACAGACTATGTTTTTGACGGGCGGCGTGCAGGTAAATACAAAGAAACTGATGCAGTCGATCCGCAAGGTATTTACGGCAAAACCAAACTAGCGGGCGAACAAGCCGTTGTAGAAGCAAACGATAAATTTATCGTATTGCGTACCGCTTGGGTATTCTGCGAGCACGGCAGCAATTTCGTTAAAACAATGCTGCGTTTAGCCAAAACTCGTGACACTTTAGGCGTAGTTGCTGATCAGATCGGCGGACCGACCTATGCAGGAGATATTGCCGCTGCGTTAATTCAAATTGCAGAAAAAATCATTGCAGGCGAATCTGTTGAATATGGTATTTATCATTTTACGGGGGAACCTTATGTCAGCTGGTGTGATTTTGCCAGAGCAATTTTTGATGAAGCTGTTTCGCAAAATATGTTAGAAAAAGCACCGCTTGTCAATGCAATTATCACGGCGGATTATCCAACACCAGCCAAACGCCCTGCGAATTCTTGCTTAGATTTGACCAAAATTCAACAAGCATTCGGTATCCAACCAAGTGATTGGCAAAGAGCTTTGAAAAATATTAAAGCGTATGCGGAG","","","31865","MAKFLITGANGQVGYCLTQQLQGKHEILAVDHDELDITNQNAVKKTVENFRPDVVINAAAHTAVDRAETEIELSEAINVKGPQYLAETAKSVGAAILHISTDYVFDGRRAGKYKETDAVDPQGIYGKTKLAGEQAVVEANDKFIVLRTAWVFCEHGSNFVKTMLRLAKTRDTLGVVADQIGGPTYAGDIAAALIQIAEKIIAGESVEYGIYHFTGEPYVSWCDFARAIFDEAVSQNMLEKAPLVNAIITADYPTPAKRPANSCLDLTKIQQAFGIQPSDWQRALKNIKAYAE","1841602","","dTDP-4-rhamnose reductase","Cytoplasm","","
InterPro
IPR005913
Family
dTDP-4-dehydrorhamnose reductase
PF04321\"[3-292]TRmlD_sub_bind
TIGR01214\"[3-290]TrmlD
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[3-215]TG3DSA:3.40.50.720
PTHR10491\"[1-292]TPTHR10491
SSF51735\"[2-287]TSSF51735


","BeTs to 14 clades of COG1091COG name: dTDP-4-dehydrorhamnose reductaseFunctional Class: MThe phylogenetic pattern of COG1091 is aompkz-q-drlbcef--sn-jx---Number of proteins in this genome belonging to this COG is","Significant hit ( 3.4e-08) to 3/4 blocks of the IPB002225 family, which is described as \"3-Beta hydroxysteroid dehydrogenase/isomerase family\". Interpro entry for IP:IPR002225. IPB002225A 1-31 0.39 IPB002225B 99-153 0.038 IPB002225C 177-219 0.48Significant hit ( 1.3e-06) to 2/5 blocks of the IPB001509 family, which is described as \"NAD dependent epimerase/dehydratase family\". Interpro entry for IP:IPR001509. IPB001509A 4-25 0.054 IPB001509B 53-87 0.011","Residues 3 to 203 match (8e-08) PD:PD123737 which is described as F6N23.17 DTDP-6-DEOXY-L-MANNOSE-DEHYDROGENASE ","","","","","Mon Feb 17 07:38:04 2003","","","","","","Thu Jan 16 17:40:19 2003","Thu Jan 16 17:40:19 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02645 is paralogously related to AA02647 (2e-05).","","","","","","Residues 140 to 284 (E-value = 1.1e-86) place AA02645 in the RmlD_sub_bind family which is described as RmlD substrate binding domain (PF04321)","","","","Nakano,Y., Yoshida,Y., Yamashita,Y. and Koga,T.A gene cluster for 6-deoxy-L-talan synthesis in ActinobacillusactinomycetemcomitansBiochim. Biophys. Acta 1442 (2-3), 409-414 (1998)PubMed: 99023768Yoshida,Y., Nakano,Y., Nezu,T., Yamashita,Y. and Koga,T.A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidine diphosphate-D-fucoseJ. Biol. Chem. 274 (24), 16933-16939 (1999)PubMed: 10358040Kaplan,J.B., Perry,M.B., MacLean,L.L., Furgang,D., Wilson,M.E. andFine,D.H.Structural and genetic analyses of O polysaccharide from Actinobacillus actinomycetemcomitans serotype fInfect. Immun. 69 (9), 5375-5384 (2001)PubMed: 11500407","Tsuda H, Yamashita Y, Shibata Y, Nakano Y, Koga T.Genes Involved in Bacitracin Resistance in Streptococcus mutans.Antimicrob Agents Chemother. 2002 Dec;46(12):3756-64.PMID: 12435673","Thu Feb 20 09:28:40 2003","Mon Feb 17 07:38:04 2003","1","","4","" "AA02646","1843379","1842483","897","ATGACTGTACTTTTTGAAGGTCTTTTTATGAAGGGTATTATTCTTGCAGGTGGTTCTGGAACTCGCCTTTATCCTATTACTCGTGGTGTATCAAAGCAGCTTTTACCTGTCTATGACAAACCAATGATTTACTACCCCCTTTCTGTGCTGATGTTAGCGGGGGTCCGTGACATTCTTATTATTACTACGCCAGAAGATAACGAAAGTTTCAAACGTTTGTTAGGTGATGGTTCTGAATTTGGTGTGAATTTACAATATGCTATTCAACCTAGCCCGGATGGCTTAGCACAAGCATTTCTCATTGGGGAAGGGTTTATCAATGGCGATAGCTGTTGTTTAGTATTAGGAGATAACATTTTCTATGGTCAGAATTTTACCCAAATGTTGCAGCAAGCTGTTGCTGGACCTTACGGTGCAACAGTGTTTGGATATTTAGTAAAAGATCCTGGGCGTTTCGGTGTGGTGGAATTTGACGAAAATTTCAAAGCTGTTTCTATTGAAGAAAAACCTGTTCAACCTAAATCTAACTATGCTGTAACAGGTTTATATTTCTACGATAATCGTGTGGTCGATTTCGCGAAACAGGTGAAACCATCTGCGCGCGGTGAGCTTGAAATCACCACATTAAATGAAATGTATCTAAAAGATGGTTCATTAAATGTGCAATTACTCGGTCGTGGTTTTGCGTGGTTAGACACAGGAACGCACGAAAGCCTACACGAAGCGGCATCTTTCGTTCGCACTGTTGAAAGCGTACAAGGTTTGCAAGTTGCATGTTTGGAAGAAATTGCCTGGCGTAATGGTTGGCTAACTTCTGAGCAAGTAGAAACATTAGCGAGACCAATGGTAAAAAATGAATACGGTCAATACTTGCTACGTTTAATCAACGAGGAGAAA","","","33200","MTVLFEGLFMKGIILAGGSGTRLYPITRGVSKQLLPVYDKPMIYYPLSVLMLAGVRDILIITTPEDNESFKRLLGDGSEFGVNLQYAIQPSPDGLAQAFLIGEGFINGDSCCLVLGDNIFYGQNFTQMLQQAVAGPYGATVFGYLVKDPGRFGVVEFDENFKAVSIEEKPVQPKSNYAVTGLYFYDNRVVDFAKQVKPSARGELEITTLNEMYLKDGSLNVQLLGRGFAWLDTGTHESLHEAASFVRTVESVQGLQVACLEEIAWRNGWLTSEQVETLARPMVKNEYGQYLLRLINEEK","1842481","","D-glucose-1-phosphate thymidylyltransferase","Cytoplasm","","
InterPro
IPR005835
Domain
Nucleotidyl transferase
PF00483\"[11-249]TNTP_transferase
InterPro
IPR005907
Family
Glucose-1-phosphate thymidylyltransferase, long form
TIGR01207\"[11-296]TrmlA: glucose-1-phosphate thymidylyltransfe
noIPR
unintegrated
unintegrated
G3DSA:3.90.550.10\"[8-297]Tno description
PTHR22572\"[18-295]TSUGAR-1-PHOSPHATE GUANYL TRANSFERASE
PTHR22572:SF13\"[18-295]TGLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE
signalp\"[1-16]?signal-peptide


","No hits to the COGs database.","","Residues 219 to 297 match (3e-40) PD:PD002767 which is described as TRANSFERASE GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE DTDP-GLUCOSE COMPLETE PROTEOME NUCLEOTIDYLTRANSFERASE SYNTHASE PYROPHOSPHORYLASE KINASE ","","","","","Mon Feb 17 07:40:28 2003","","","","","","","Tue Jan 21 09:06:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02646 is paralogously related to AA01014 (4e-12) and AA02090 (3e-06).","","","","","","Residues 11 to 249 (E-value = 6.3e-116) place AA02646 in the NTP_transferase family which is described as Nucleotidyl transferase (PF00483)","","","","Yoshida,Y., Nakano,Y., Yamashita,Y. and Koga,T.Identification of a genetic locus essential for serotype b-specific antigen synthesis in Actinobacillus actinomycetemcomitansInfect. Immun. 66 (1), 107-114 (1998)PubMed: 9423846Yoshida,Y., Nakano,Y., Nezu,T., Yamashita,Y. and Koga,T.A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidine diphosphate-D-fucoseJ. Biol. Chem. 274 (24), 16933-16939 (1999)PubMed: 10358040Nakano,Y., Yoshida,Y., Suzuki,N., Yamashita,Y. and Koga,T.A gene cluster for the synthesis of serotype d-specific polysaccharide antigen in Actinobacillus actinomycetemcomitansBiochim. Biophys. Acta 1493 (1-2), 259-263 (2000)PubMed: NOT_FOUND","Bozue,J.A., Tullius,M.V., Wang,J., Gibson,B.W. andMunson,R.S. Jr. Haemophilus ducreyi produces a novel sialyltransferase. Identification of the sialyltransferase gene andconstruction of mutants deficient in the production of the sialicacid-containing glycoform of the lipooligosaccharide J. Biol. Chem. 274 (7), 4106-4114 (1999) PubMed: 9933604 Marolda,C.L. and Valvano,M.A. Genetic analysis of the dTDP-rhamnose biosynthesis regionof the Escherichia coli VW187 (O7:K1) rfb gene cluster:identification of functional homologs of rfbB and rfbA in the rff cluster and correct location of the rffE gene J. Bacteriol. 177 (19), 5539-5546 (1995) PubMed: 7559340 Sivaraman J, Sauve V, Matte A, Cygler M. Crystal Structure of Escherichia coli Glucose-1-PhosphateThymidylyltransferase (RffH) Complexed with dTTP and Mg2+ J Biol Chem. 2002 Nov 15;277(46):44214-44219. PubMed: NOT_FOUND Graninger M, Kneidinger B, Bruno K, Scheberl A, Messner P. Homologs of the Rml enzymes from Salmonella enterica areresponsible for dTDP-beta-L-rhamnose biosynthesis in the gram-positive thermophile Aneurinibacillus thermoaerophilusDSM 10155. Appl Environ Microbiol. 2002 Aug;68(8):3708-15. PubMed: NOT_FOUND","Mon Feb 17 07:40:28 2003","Mon Feb 17 07:40:28 2003","1","","4","" "AA02647","1844497","1843433","1065","ATGTTGAAAACTATTTTAGTTACAGGCGGTGCAGGTTTTATAGGTTCTGCAGTAGTTCGCTATATTATTGAGAATACGCAAGACAGCGTAGTTAACGTTGATAAATTGACCTATGCAGGAAATTTAGAATCTCTTGAAGCAGTGAAAAATAATCCACGTTATATATTTGAACAAGTGGATATTTGCGATGCAAAAGCACTTGCTCGCATATTTGAACAGCACCAGCCTGATGCAGTAATGCACTTAGCCGCAGAAAGCCACGTTGACCGTTCTATTGATGGACCTGCTACTTTTATTGAAACTAATATCGTGGGTACTTACATTTTATTAGAAGCCGCCCGTGCTTATTGGAGTAGTTTAAACGATGAGAAAAAAGCAGGATTCCGTTTCCATCATATTTCGACCGATGAAGTTTATGGCGATTTAGATGGGACGAACAATCTTTTTACTGAAACCACGCCTTATTCCCCAAGTAGTCCTTATTCTGCATCAAAAGCCTCCAGCGATCATCTTGTTCGTGCGTGGTTGCGTACTTACAGCTTGCCAACGATTGTGACCAACTGCTCAAACAACTATGGGCCGTTTCACTTTCCGGAAAAATTGATTCCATTGATAATTTTAAACGCCTTAGATGGCAAACCGCTTCCTGTGTATGGTAACGGCCAGCAAATTCGTGACTGGCTATTTGTAGAGGATCATGCTCGTGCTTTATACAAAGTTGTGACAGAAGGCAAAATTGGAGAAACCTACAATATCGGTGGTCACAATGAAAAAGCGAACATTGATGTAGTTCGCACCATCTGTGCTTTATTAGAAGAACTGGTTCCAGATAAACCTGCTGGCGTTACCAAATACGAAGATTTAATCACTTACGTTAAAGACCGCCCTGGTCATGATGTGCGTTATGCCATTGATGCAACCAAAATCAGTCGTGAATTAGGCTGGAAACCGCAAGAAACCTTTGAATCAGGCATTCGTAAAACGGTGGAGTGGTATCTAAATAACCGAAAATGGTGGAGCCGTGTGTTAGATGGTTCTTACAATCGTGAGCGTTTAGGCAGTCAA","","","39962","MLKTILVTGGAGFIGSAVVRYIIENTQDSVVNVDKLTYAGNLESLEAVKNNPRYIFEQVDICDAKALARIFEQHQPDAVMHLAAESHVDRSIDGPATFIETNIVGTYILLEAARAYWSSLNDEKKAGFRFHHISTDEVYGDLDGTNNLFTETTPYSPSSPYSASKASSDHLVRAWLRTYSLPTIVTNCSNNYGPFHFPEKLIPLIILNALDGKPLPVYGNGQQIRDWLFVEDHARALYKVVTEGKIGETYNIGGHNEKANIDVVRTICALLEELVPDKPAGVTKYEDLITYVKDRPGHDVRYAIDATKISRELGWKPQETFESGIRKTVEWYLNNRKWWSRVLDGSYNRERLGSQ","1843431","","dTDP-D-glucose-4,6-dehydratase","Cytoplasm","","
InterPro
IPR001509
Family
NAD-dependent epimerase/dehydratase
PF01370\"[5-253]TEpimerase
InterPro
IPR002347
Family
Glucose/ribitol dehydrogenase
PR00081\"[4-21]T\"[161-180]TGDHRDH
InterPro
IPR005888
Family
dTDP-glucose 4,6-dehydratase
TIGR01181\"[4-342]TdTDP_gluc_dehyt
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[2-273]TG3DSA:3.40.50.720
PTHR10366\"[7-348]TPTHR10366
PTHR10366:SF41\"[7-348]TPTHR10366:SF41
SSF51735\"[3-347]TSSF51735


","No hits to the COGs database.","Significant hit ( 1.3e-47) to 5/5 blocks of the IPB001509 family, which is described as \"NAD dependent epimerase/dehydratase family\". Interpro entry for IP:IPR001509. IPB001509A 5-26 2.3e-12 IPB001509B 77-111 1.6e-21 IPB001509C 189-195 0.034 IPB001509D 225-232 0.028 IPB001509E 306-316 0.0057 IPB001509E 322-332 0.16Significant hit ( 4.3e-08) to 4/4 blocks of the IPB002225 family, which is described as \"3-Beta hydroxysteroid dehydrogenase/isomerase family\". Interpro entry for IP:IPR002225. IPB002225A 2-32 0.00013 IPB002225B 135-189 4.6e+02 IPB002225C 221-263 6.9e+02 IPB002225D 295-339 0.18Significant hit ( 5e-05) to 1/1 blocks of the IPB000558 family, which is described as \"Histone H2B\". Interpro entry for IP:IPR000558. IPB000558 84-128 4.8e-05","Residues 60 to 134 match (4e-08) PD:PD507032 which is described as DTDP-GLUCOSE-46-DEHYDRATASE ","","","","","Mon Feb 17 07:40:57 2003","","","","","","","Tue Jan 21 09:26:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02647 is paralogously related to AA02623 (1e-71), AA01886 (1e-18), AA02645 (3e-05) and AA00539 (6e-05).","","","","","","Residues 5 to 336 (E-value = 2.4e-212) place AA02647 in the Epimerase family which is described as NAD dependent epimerase/dehydratase family (PF01370)","","","","Kaplan,J.B., Perry,M.B., MacLean,L.L., Furgang,D., Wilson,M.E. andFine,D.H.Structural and genetic analyses of O polysaccharide from Actinobacillus actinomycetemcomitans serotype fInfect. Immun. 69 (9), 5375-5384 (2001)PubMed: 21391794Yoshida,Y., Nakano,Y., Nezu,T., Yamashita,Y. and Koga,T.A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidine diphosphate-D-fucoseJ. Biol. Chem. 274 (24), 16933-16939 (1999)PubMed: 10358040Nakano,Y., Yoshida,Y., Yamashita,Y. and Koga,T.A gene cluster for 6-deoxy-L-talan synthesis in Actinobacillus actinomycetemcomitansBiochim. Biophys. Acta 1442 (2-3), 409-414 (1998)PubMed: 9805002Yoshida,Y., Nakano,Y., Yamashita,Y. and Koga,T.Identification of a genetic locus essential for serotype b-specific antigen synthesis in Actinobacillus actinomycetemcomitansInfect. Immun. 66 (1), 107-114 (1998)PubMed: 9423846","Allard ST, Giraud MF, Whitfield C, Graninger M, Messner P, Naismith JH. The crystal structure of dTDP-D-Glucose 4,6-dehydratase (RmlB) from Salmonella enterica serovar Typhimurium, the second enzyme in the dTDP-l-rhamnose pathway. J Mol Biol. 2001 Mar 16;307(1):283-95. PMID: 11243820 Bozue,J.A., Tullius,M.V., Wang,J., Gibson,B.W. and Munson,R.S. Jr. Haemophilus ducreyi produces a novel sialyltransferase. Identification of the sialyltransferase gene and construction of mutants deficient in the production of the sialic acid-containing glycoform of the lipooligosaccharide J. Biol. Chem. 274 (7), 4106-4114 (1999) PubMed: 9933604 Marolda,C.L. and Valvano,M.A. Genetic analysis of the dTDP-rhamnose biosynthesis region of the Escherichia coli VW187 (O7:K1) rfb gene cluster: identification of functional homologs of rfbB and rfbA in the rff cluster and correct location of the rffE gene Journal of bacteriology. 177 (19), 5539-5546 (1995) PubMed: 7559340","Tue Dec 2 12:41:24 2003","Mon Feb 17 07:40:57 2003","1","","4","" "AA02648","1845697","1844570","1128","ATGATGAAATTAAACTGTATTTTAAAAATATCCGGAATTTCCACCGCACTTTTTCTAGCGGGTTGTTCCTCAAATTCAAGTGCGCCGACGCAATCCTCTGAGCAGGCGAATTCTGTTACGGCTGTGAATCCCACTGCGGTGTACAGTAAGCCCCGCACTTTGGATAACTTCAACGATTATGTGAATTTCTTAAAAGGTAAAGCAGCGGCAGAAGGCGTTTCTGCCGACGTATTGAATGCACAAAATAATATTAATTATATTCAAAAATCCGTGGATTTGGACGATCAGCAAGCGGGCAGAATTCGCAAGCGTGATCCAAATGCCCCGCCGATCATCAATCCGAACGGCACGACCAATTACTTAAATCGTGTATTAACCAAGAATAAAGTAGACACGGCAGAAGCACGTTATTGGGAACAATTGCCGCAGCTTGAAAATGCTTCAAAGAAATTCAGCGTACCGAAAAATTATCTGTTAGCCTTGTGGGGCATGGAGAGTAGCTTTGGCTATTATCAGGGCAATTACGATGTGTTATCCACCTTAGCCACTCTTGCTTTTGACGGACGCCGTGAAGCCTTATTCAGCAAAGAATTCATCGCCGCCATGAAAATGCTACAGCGCGATCATATTCAACGCTATAAAATGCTGGGTTCATGGGCAGGCGCCATGGGACAGACCCAATTCATGCCAAGCTCTTACCTCAGCTACGCCGCAGATGGCAACAATGATGGCGAGAAAAATATCTGGACCGATCATTATGATGTTTTCGCCTCCATCGCTAATTATTTACACACCGTCGGCTGGAACGAAAACCTGCCATGGGGTGTAGAAGTTGCACTAACCCAACCGTTAGACATGGCGCTTGCTGGCACAGAGGAAAATAAAAAACGTTCTTTAAGCGACTGGCAAAATATGGGTGTCACCCTAAAATACCAAACTCCACAAACACAACAAAAACTGACCGCACTTTCCGGCGCACAAGACTTATGGCTGGTAAGGCCGGATCGTGAATTAGGGCGTGCATTTTTGGTCTCTAATAATTACAGAACCTTGCTACATTGGAATAAATCCAACTATTTTGCTGTGAGTATTGGAATGTTTGCTGATAGGATTGAGCAAAGAGTCAAA","","","42199","MMKLNCILKISGISTALFLAGCSSNSSAPTQSSEQANSVTAVNPTAVYSKPRTLDNFNDYVNFLKGKAAAEGVSADVLNAQNNINYIQKSVDLDDQQAGRIRKRDPNAPPIINPNGTTNYLNRVLTKNKVDTAEARYWEQLPQLENASKKFSVPKNYLLALWGMESSFGYYQGNYDVLSTLATLAFDGRREALFSKEFIAAMKMLQRDHIQRYKMLGSWAGAMGQTQFMPSSYLSYAADGNNDGEKNIWTDHYDVFASIANYLHTVGWNENLPWGVEVALTQPLDMALAGTEENKKRSLSDWQNMGVTLKYQTPQTQQKLTALSGAQDLWLVRPDRELGRAFLVSNNYRTLLHWNKSNYFAVSIGMFADRIEQRVK","1844568","","lytic transglycosylase","Periplasm, Outer membrane","","
InterPro
IPR011970
Domain
Lytic murein transglycosylase
TIGR02283\"[56-373]TMltB_2
noIPR
unintegrated
unintegrated
G3DSA:1.10.530.10\"[112-371]TG3DSA:1.10.530.10
PS51257\"[1-22]TPROKAR_LIPOPROTEIN
SSF53955\"[40-375]TSSF53955


","BeTs to 5 clades of COG2951COG name: Membrane-bound lytic murein transglycosylase BFunctional Class: MThe phylogenetic pattern of COG2951 is --------------efghsn-j----Number of proteins in this genome belonging to this COG is","","Residues 102 to 222 match (5e-09) PD:PD548666 which is described as LYTIC TRANSGLYCOSYLASE MEMBRANE-BOUND B COMPLETE PROTEOME MUREIN HYDROLASE 3.2.1.- GLYCOSIDASE ","","","","","","","","","","","","Tue Jan 21 09:31:50 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02648 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","",""," Yoshida,Y., Nakano,Y., Yamashita,Y. and Koga,T.Identification of a genetic locus essential for serotype b-specific antigen synthesis in Actinobacillus actinomycetemcomitansInfect. Immun. 66 (1), 107-114 (1998)PubMed: 9423846","","Tue Jan 21 09:31:50 2003","","1","","4","" "AA02649","1846484","1845702","783","ATGTCCTTATATATTAAGGAAAATCCACAATATTTAAGAGAATGTTTGGAAAGTTTGGTGGCACAAACCTGCCCTGCCGATGAAGTCGTACTGGTGTTTGATGGCGCGGTGACGCCTGAATTGGAAGCGGTGGTTGCCGAGTTTGAATCGAAGCTGCCGTTTAATTTGGTGAAATTACCGAACAATTTAGGTTTAGGCAAAGCTCTCAACGAAGGTTTAAAATATTGCTCGCGCGATTGGGTTCTGCGCATGGATACCGATGATATTTGCGTGCCGGAACGTTTTGCCAAACAGGTGGCGTTTATTGAACAACATCCTGATACTATAGTGTTCGGTGGGCAAATTGCCGAATTCGGTGAAAATATCCATGACATAGTGGCATATCGAAATGTGCCGACTTCTGCGCAAGACATCGTTACATTTACCCAAAAACGCTGCCCGTTTAATCACATGACGGTGGCGTATCAAAAAAGTGCGGTCATAAATTGCGGCGGATATGAGGATTTACAGGAAGATTATTATTTGTGGATCAAACTGGTGGCGCAAGGGCAGCGCGTAGCAAATTTACCCGATATTTTGGTCTATGCGCGCGTCGGCAACGGCATGGTAGGGCGACGCCGTGGTTTAAACCAAGCCAAAGCGGAATGGCGCTTATTTAAGCTAAAACACCATCTTGGCATTCAGGGATTTTTATCCGGGCTATTCACTTTTGTCCTGCGTTCCGGTGCCAGATTATTGCCGACATCATTACTGAAAAACATCTATCAAACCTTTTTAAGAAAA","","","30432","MSLYIKENPQYLRECLESLVAQTCPADEVVLVFDGAVTPELEAVVAEFESKLPFNLVKLPNNLGLGKALNEGLKYCSRDWVLRMDTDDICVPERFAKQVAFIEQHPDTIVFGGQIAEFGENIHDIVAYRNVPTSAQDIVTFTQKRCPFNHMTVAYQKSAVINCGGYEDLQEDYYLWIKLVAQGQRVANLPDILVYARVGNGMVGRRRGLNQAKAEWRLFKLKHHLGIQGFLSGLFTFVLRSGARLLPTSLLKNIYQTFLRK","1845700","","possible glycosyltransferase","Cytoplasm","","
InterPro
IPR001173
Domain
Glycosyl transferase, family 2
PF00535\"[9-170]TGlycos_transf_2
noIPR
unintegrated
unintegrated
G3DSA:3.90.550.10\"[9-206]Tno description
PTHR22916\"[5-222]TGLYCOSYLTRANSFERASE


","No hits to the COGs database.","","Residues 1 to 160 match (3e-15) PD:PD023980 which is described as TRANSFERASE PROTEOME COMPLETE GLYCOSYLTRANSFERASE GLYCOSYL BIOSYNTHESIS POLYSACCHARIDE SPORE SUGAR COAT ","","","","","","","","","","","","Tue Jan 21 09:40:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02649 is paralogously related to AA02651 (5e-06), AA02632 (4e-04) and AA01402 (0.001).","","","","","","Residues 1 to 170 (E-value = 4.3e-26) place AA02649 in the Glycos_transf_2 family which is described as Glycosyl transferase (PF00535)","","","","Yoshida,Y., Nakano,Y., Yamashita,Y. and Koga,T.Identification of a genetic locus essential for serotype b-specific antigen synthesis in Actinobacillus actinomycetemcomitansInfect. Immun. 66 (1), 107-114 (1998)PubMed: 98084462 Yoshida,Y., Nakano,Y., Nezu,T., Yamashita,Y. and Koga,T.A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidine diphosphate-D-fucoseJ. Biol. Chem. 274 (24), 16933-16939 (1999)PubMed: 99287888Nakano,Y., Yoshida,Y., Yamashita,Y. and Koga,T.A gene cluster for 6-deoxy-L-talan synthesis in ActinobacillusactinomycetemcomitansBiochim. Biophys. Acta 1442 (2-3), 409-414 (1998)PubMed: 99023768","","Tue Feb 11 15:09:59 2003","","1","","4","" "AA02651","1847458","1846580","879","ATGTTCAGTATCATCGTTCCTTCTTATAATCGCAAAGAGGAAATGCCCGCGCTGTTGGAAAGTTTAAGCCAACAAACTGCGCATGATTTTGAAGTGGTGGTTGTGGACGATTGCTCGAAAGAACCTGTTACAGTGGTGCAAAATTATCCTTTCCCCGTGCGGGTGATTCGCAACGAAATCAATCAGGGCGCGGCGGAAAGTCGCAATATCGGTGCGCGCCATGCACAACATGACTGGTTATTGTTTTTAGACGATGACGATCGTTTCGCTAATGATAAATGTGAAAAATTGGCAGCGATGATTGCCGATCATGCCGACATTAACTTTATCTATCACCCGGCGAAATGCGAAATGGTGAATGAAGGCTTTACTTATGTCACGCATCCCATTGATCCGCAACATATCAGCATTGAAAGCATTTTGTTGGCGAATAAAATCGGCGGTATGCCGATGATCGGCGTGAAGAAAGATTTGTTCTTAAAAATAGGCGGATTATCCACCGCACTTCGTTCTTTGGAAGATTATGATTTTCTGTTGAAATTGTTGCAGGAGCCCGAATTCACGCCTTGCAAGGTAAATGAACCGCTGACCTATTGCACCTTCCACACCAAACGGGCAAGCGTTTCCACAGATACCACCAATACGCAAAAAGCCATTGATTATATTCGTGAGCATTATGTAAAAACGCCGGAACAGGCGCGCAATTTCAAGATTAACGCCAGTTATATTCTGGCTTATCCGCATATCATGAATTTATCCCGCAAAGCGGCGAAATATTATTTTGATATTTTTAAACAGACCAGAAGTCTGAAACAATTAATTATTGCCTTGGTAGTGCTGATTTCGCCTAAATTGGCGATTAATTTGAAGCGGTTTATG","","","33529","MFSIIVPSYNRKEEMPALLESLSQQTAHDFEVVVVDDCSKEPVTVVQNYPFPVRVIRNEINQGAAESRNIGARHAQHDWLLFLDDDDRFANDKCEKLAAMIADHADINFIYHPAKCEMVNEGFTYVTHPIDPQHISIESILLANKIGGMPMIGVKKDLFLKIGGLSTALRSLEDYDFLLKLLQEPEFTPCKVNEPLTYCTFHTKRASVSTDTTNTQKAIDYIREHYVKTPEQARNFKINASYILAYPHIMNLSRKAAKYYFDIFKQTRSLKQLIIALVVLISPKLAINLKRFM","1846578","","glycosyltransferase","Cytoplasm","","
InterPro
IPR001173
Domain
Glycosyl transferase, family 2
PF00535\"[3-163]TGlycos_transf_2
noIPR
unintegrated
unintegrated
G3DSA:3.90.550.10\"[1-241]TG3DSA:3.90.550.10
PTHR22916\"[8-184]TPTHR22916
SSF53448\"[1-226]TSSF53448


","No hits to the COGs database.","","Residues 3 to 132 match (4e-42) PD:PD023980 which is described as TRANSFERASE PROTEOME COMPLETE GLYCOSYLTRANSFERASE GLYCOSYL BIOSYNTHESIS POLYSACCHARIDE SPORE SUGAR COAT ","","","","","","","","","","","","Tue Jan 21 14:23:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02651 is paralogously related to AA02636 (7e-07) and AA02649 (6e-06).","","","","","","Residues 3 to 163 (E-value = 1.8e-36) place AA02651 in the Glycos_transf_2 family which is described as Glycosyl transferase (PF00535)","","","","Yoshida,Y., Nakano,Y., Suzuki,N., Nakao,H., Yamashita,Y. andKoga,T. 1999. Genetic analysis of the gene cluster responsible forsynthesis of serotype e-specific polysaccharide antigen inActinobacillus actinomycetemcomitans. Biochim. Biophys. Acta 1489:457-461. PubMed: . Yoshida,Y., Nakano,Y., Yamashita,Y. and Koga,T. 1998.Identification of a genetic locus essential for serotype b-specific antigen synthesis in Actinobacillus actinomycetemcomitans. Infect.Immun. 66(1): 107-114. PubMed: 9423846.","","Tue Feb 11 14:52:55 2003","","1","","4","" "AA02652","1848651","1847461","1191","ATGACCGCACTTTTTAATCTGTTTTACCTTTATGATCCTTGGTTCTTCCATTTTTTGCGAATGTCGCTCATTGCCGGGCTGATTGCGCTGGCAGTGTTGGCGTATCGGTTAGTAAAAAAACGGCAAACCAACGGCATTATCGTGCCGTTAGACAGCCTTGCCGTATTATGCGGCTTGATTCTGTTCAGTGTGATCCCCTTGTTGGTTAACGGCACGCGGGATCTTTCCGTCATCATGATGTACGTGAAGGGCTTTGTGTTATTTGTTTTGGGCATCGGCATCTATAACGTTTTTTATGCAGATGCCCACGGTCAGCAAAGAATGGTGCGGGATCTGCAAATCGGCGTGGTGACGCAGTTCGTTCTGGGCTTATTGGCGCTTTTCGGCGTGTCTTTTATAATTGATTTCCTGCTTGCCACGAACGCGCTGCTGCCGGCGCGGTTTTATGGTTCCGAACAGGAATATCGCTTATATAACGTGACATCGGCGGCTTTTTTCCAGCTAAGTTTGTTCTATTTAATGCTGTTTCATTTTCTGCTTGCCTACAACGCGAAACATAACCGCATTCCAAGTTTGATTATCTTCTTTATGTTGTGCATCGGTTTGATTTCCGGCAGAACCTTTTTGCTGCTTTCGGCGGTGAGCATTTTGTTGTACTTCAAAGTGCGGTATATTCCGGTAGTGATTTCGTTTGCCGTTTTGCTGCTATTGTTGGCGTATTTCCTGCCGGGTAATAAATATGTGGCGCACGCCTTGGAGCCGGTGATTAATGTGTTACATGGTGCGGGCTTTGTCAGTTCTTCGACAGATACGTTAGTGGAAAAACATTTATTTATGCCGACATTAAAACAATTTATTTCCGGCGACGGGCTTTATATGACGGGGCAAACGGAAGTGGGACGTTATTACGGTCACACAGATTCCGGGTTCTTGCGTCAGATTTTGTACGGCGGCGTGACTTATGCGCTGGTGTGTTTTTTAGTGACTTTCTATTTTGTGCGTAAAGTGGCGATAAATTGGTTTGACGGCAGTTGGAAATTCATGCTTTCCGCCTTTGTGATTCTCGCCGCCTGCAACGTGAAAGCCGACACTTTCGCTTTCCCGGGCATTATGTTTGTAATGTTGATGTTCTTCTCTTTATTTGGTTCACATGGCAAACAACTTGTGTTATTTAAACAAAAGGAGGCGAAA","","","44839","MTALFNLFYLYDPWFFHFLRMSLIAGLIALAVLAYRLVKKRQTNGIIVPLDSLAVLCGLILFSVIPLLVNGTRDLSVIMMYVKGFVLFVLGIGIYNVFYADAHGQQRMVRDLQIGVVTQFVLGLLALFGVSFIIDFLLATNALLPARFYGSEQEYRLYNVTSAAFFQLSLFYLMLFHFLLAYNAKHNRIPSLIIFFMLCIGLISGRTFLLLSAVSILLYFKVRYIPVVISFAVLLLLLAYFLPGNKYVAHALEPVINVLHGAGFVSSSTDTLVEKHLFMPTLKQFISGDGLYMTGQTEVGRYYGHTDSGFLRQILYGGVTYALVCFLVTFYFVRKVAINWFDGSWKFMLSAFVILAACNVKADTFAFPGIMFVMLMFFSLFGSHGKQLVLFKQKEAK","1847459","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-34]?signal-peptide
tmhmm\"[14-34]?\"[49-69]?\"[79-99]?\"[120-138]?\"[157-177]?\"[192-212]?\"[222-242]?\"[313-333]?\"[347-381]?transmembrane_regions


","No hits to the COGs database.","","Residues 1 to 395 match (2e-174) PD:PD042278 which is described as FOR GLYCOSYLTRANSFERASE CLUSTER PROTEOME TRANSGLYCOSYLASE COMPLETE 6-DEOXY-L-TALAN LYTIC SYNTHESIS REDUCTASE ","","","","","","","","","","","","Tue Jan 21 09:46:05 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02652 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","Yoshida,Y., Nakano,Y., Suzuki,N., Nakao,H., Yamashita,Y. and Koga,T. 1999. Genetic analysis of the gene cluster responsible for synthesis of serotype e-specific polysaccharide antigen in Actinobacillus actinomycetemcomitans. Biochim. Biophys. Acta 1489: 457-461. PubMed: . Nakano,Y., Yoshida,Y., Yamashita,Y. and Koga,T.A gene cluster for 6-deoxy-L-talan synthesis in ActinobacillusactinomycetemcomitansBiochim. Biophys. Acta 1442 (2-3), 409-414 (1998)PubMed: 99023768","","Tue Feb 11 16:06:31 2003","","1","","4","" "AA02654","1849307","1848663","645","GTGCTGTCGGCGGTGTTTAATCCGGTCAAATTTGAACAGCACTACGGGCGTAAAGTAACCAAAGGTGAAATCGGTTGTACTCTGAGTCATCTTGAGGTTTACCGCCAAATTGTCGCTGATGAAAAGGTGGCGGAAAAGGATTATGCCTTGGTGTGTGAAGACGATGCCCTGTTCAATAAAAATTTACCTGAAAATCTGACCGCACTTTTGGCGCAACATTGTACGGCGGACATCATCCTTATCGGGCAATCCAAAATTGCCGGATTTGATGACATGGAACTGGAAATCAATTATCCGACCACGTTTGCCTTTTTACGCGCCAATGTGGGTGCCGCCACTTATGCCTATCCGTATAAAAGCTATTTTGCCGGCACCGTGGCGTATTTAATCAAAAAATCCGCTGCACGGACGTTTCTTGCCATTTTGGAACAGGAAAAACCGTTTTGGCTCGCTGACGATTTTCTGTTATTTGAAACCCAATTTAAGCTGAACAATAACGTGGTGCGCCCGTTGATGGTAATTGAAAACCCACAACTGGTGAGTAATTTGGAAGCCGTGCGCGGGTCGAAGTCCAATAATTTAGCGAAAAAACTGCTGAAATACCCGTTGAAAAAACTGTTAGCCGTGAAGAAGAACTTAGGAAAA","","","29234","VLSAVFNPVKFEQHYGRKVTKGEIGCTLSHLEVYRQIVADEKVAEKDYALVCEDDALFNKNLPENLTALLAQHCTADIILIGQSKIAGFDDMELEINYPTTFAFLRANVGAATYAYPYKSYFAGTVAYLIKKSAARTFLAILEQEKPFWLADDFLLFETQFKLNNNVVRPLMVIENPQLVSNLEAVRGSKSNNLAKKLLKYPLKKLLAVKKNLGK","1848661","","probable lipopolysaccharide biosynthesis protein","Cytoplasm","","
InterPro
IPR002654
Family
Glycosyl transferase, family 25
PTHR10730:SF2\"[9-82]TCEREBRAL CELL ADHESION MOLECULE RELATED
PF01755\"[1-156]TGlyco_transf_25
noIPR
unintegrated
unintegrated
PTHR10730\"[9-82]TPROCOLLAGEN/CELL ADHESION MOLECULE RELATED


","BeTs to 4 clades of COG3306COG name: Glycosyltransferase involved in LPS biosynthesisFunctional Class: MThe phylogenetic pattern of COG3306 is -----------------h-nuj----Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Tue Jan 21 09:50:47 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02654 is paralogously related to AA01330 (4e-07) and AA01332 (1e-06).","","","","","","Residues 1 to 156 (E-value = 5.9e-18) place AA02654 in the Glyco_transf_25 family which is described as Glycosyltransferase family 25 (LPS biosynthesis protein) (PF01755)","","","","Yoshida,Y., Nakano,Y., Suzuki,N., Nakao,H., Yamashita,Y. and Koga,T. 1999. Genetic analysis of the gene cluster responsible for synthesis of serotype e-specific polysaccharide antigen in Actinobacillus actinomycetemcomitans. Biochim. Biophys. Acta 1489: 457-461. PubMed: . Yoshida,Y., Nakano,Y., Yamashita,Y. and Koga,T. 1998. Identification of a genetic locus essential for serotype b-specific antigen synthesis in Actinobacillus actinomycetemcomitans. Infect. Immun. 66(1): 107-114. PubMed: 9423846.Nakano,Y., Yoshida,Y., Yamashita,Y. and Koga,T. A gene cluster for 6-deoxy-L-talan synthesis in Actinobacillus actinomycetemcomitans Biochim. Biophys. Acta 1442 (2-3), 409-414 (1998) PubMed: 99023768","","Tue Feb 11 16:21:01 2003","","1","","4","" "AA02655","1849495","1851087","1593","TTGCTGATTATACTAAAGAAAACTATAATCCCCCACCTATTTTACGGAAAAAGGTCAAGATTAATTCTCATCATGTCCAACAAAACCATCGCAAAAAACACCCTGTTTCTTTATATCCGAATGCTCTTCAATATGGGCGCCATGCTGTATATTTCACGCGTGGTGCTACGGGTGCTCGGCGTAGAAGATTTCGGGATTTACACCATTGTGATGGGCGTGGTGATTTTGTTTTCGTTTTTCAACGGCACTATGACGGCAACCACCCAGCGTTTTATTAACGTGGAAAAAGCCTCAAACGACTCAAGCAGAGTAAATCAGGTTTTTAACATCAGCATCTTGAATCACCTGTTTATTATGCTGGTCGTGGTGATTCTGGCGGAAACGGCAGGATTATGGTTTTTAAATCATAAATTGAACATTCCCGCCCCGCGTATGAACGCCGCCAACATTGTGTACCAGGTAGCATTGCTCATTGCGTTGGTGGAAATCATTAAAGTACCCTTTAACGCTATGATCGTGGCGCATGAGCGAATGTCCTTTTATGCCTGGCTCGGGTTGGCGGAAACCGGCTTAAAACTGGGCGCAATTTTTATTCTCACGCAAATAGAAAACCACGATAAATTGATTTCTTACAGTTTACTGCTGCTGTGCGTAAGTTTATTGGTTTTCACCCTGTATTTTCGTTTCACCCGCAACGCCTTTCACGCAGAAACCCGCTTTCAGTTTCAAAAAGATCTCGGCAAAATCAAAGAAATGATGCGTTTTTCCGGCTGGATGTTGGTGGGGCAGGTAGCTTATGTGGGTTCCACCCAAGGCTTAAATATGGTGACCAATCTCTTCTTCGGCGTCACCGCCAATGCCGCCGTGGGCATTGCCACACAAGTCGATACGGCGGTGTACAGTTTCGTCAATAATTTCCAGGTGGCGTTCAATCCGCAACTGGTACAGTCTTACGCCGCGAAAGACTACGATCGCAACAAAAAGTTAATTTTAGGCACGTCAAAATATTCCTTCTATTTAATCGCCATTTTATCGGCGCCGGTGTTGTATTTCAGCCATACATTGCTCACCCTTTGGCTGGGCGATCATGTGCCGCAATATTCCGATAAACTGGTGCAAGCCACCATTGTTTGTTCCTTAATCAGCGCCATGGCGGGTTCCTTCTGGATGACGGCGCTTGCCATCGGTTCGCACACCATCAAACGATACAACGTCGTTTTGGCAACCATTGACCTGTGCACCGTACCGCTCGCCTATTATTTATTCACACTGGGCTACAATCCGGTGTTTGCGTTCATCGGCAAATTCTGCACCGCCTCACTCATGCAAATTTACCGTCTGTATTTTATTAACAACAAAATTAAATTTAATCGAAAAGAATTTGTCTCATACTTACTGAATATCGGCATTATTTTTGCCTTTTTATTGGGTTTAATTTATTTATCGAACACGCAACGCACGTATTCCCTCGTGGAATTTATCGGCGAAGCCATCCTTATTGAAATCGTTCTGTTTGCACTCATCCTGCTCATCGGATTAAACAAAGCAGAAAAAAACGTCTTATTTAGCTATTTACTGAAAAGAGTGAGAAAA","","","60217","LLIILKKTIIPHLFYGKRSRLILIMSNKTIAKNTLFLYIRMLFNMGAMLYISRVVLRVLGVEDFGIYTIVMGVVILFSFFNGTMTATTQRFINVEKASNDSSRVNQVFNISILNHLFIMLVVVILAETAGLWFLNHKLNIPAPRMNAANIVYQVALLIALVEIIKVPFNAMIVAHERMSFYAWLGLAETGLKLGAIFILTQIENHDKLISYSLLLLCVSLLVFTLYFRFTRNAFHAETRFQFQKDLGKIKEMMRFSGWMLVGQVAYVGSTQGLNMVTNLFFGVTANAAVGIATQVDTAVYSFVNNFQVAFNPQLVQSYAAKDYDRNKKLILGTSKYSFYLIAILSAPVLYFSHTLLTLWLGDHVPQYSDKLVQATIVCSLISAMAGSFWMTALAIGSHTIKRYNVVLATIDLCTVPLAYYLFTLGYNPVFAFIGKFCTASLMQIYRLYFINNKIKFNRKEFVSYLLNIGIIFAFLLGLIYLSNTQRTYSLVEFIGEAILIEIVLFALILLIGLNKAEKNVLFSYLLKRVRK","1851085","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR002797
Family
Polysaccharide biosynthesis protein
PF01943\"[30-318]TPolysacc_synt
noIPR
unintegrated
unintegrated
signalp\"[1-16]?signal-peptide
tmhmm\"[34-54]?\"[64-82]?\"[115-135]?\"[149-169]?\"[179-199]?\"[209-229]?\"[337-357]?\"[376-396]?\"[406-426]?\"[432-450]?\"[465-483]?\"[493-513]?transmembrane_regions


","BeTs to 4 clades of COG0534COG name: Na+-driven multidrug efflux pumpFunctional Class: QThe phylogenetic pattern of COG0534 is aom-kzyqvdrlbcefghsnuj--twNumber of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Tue Jan 21 10:02:42 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02655 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","4","" "AA02656","1851087","1852040","954","ATGAATCAACAACTTATTGATTTAAAACATAAGCTGGCGCCCATTGCGGATTTAATCAAAGATAAAAATGACGTGTTTTATCTGGATTATCCGTTACATTTAAATGTGGGCGATTTATTGATTTATCACGGAACGGAACAATTTTTTACCGATCACAACATTCATGTGAGGTTAAAACGTAGCGAATACGATACGAATATTGACGAAATCAAACAAAAAATCACACCGAATACCACGATTTTACTGCATGGCGGCGGTAATTTCGGCGATCTTTACCCGCAACATCAAAATCTGCGCGAAGCCATTGTGCAAACATTCCCGAACAACCGCATCATTGTTTTGCCACAAACCCTGTTCTATAAAAACCCAAAAACACTGGAAAAATCCACCGCACTTTTCCGCCAGCATCCCGATTGCCATTTGTTGGCGCGGGACGAACGCACGGCAAAAGCCTTTGAAGCGTTTTCCCCAAATGTGTATTTATCGCCGGACATGGCTCACGAACTGTATGGTACCTTGCCTACCAAAAACACACACACCGGAAAAGCTCTGTATTTTCTCCGCAAAGACATTGAAGCCAGCGACATTGAAAAAAACATCACCGCACAATTACCTGCCGGTAGCCATATTAAAGACTGGGATGACATCTTATCCAAACGCGACAGCCTGGTTCTCGCGCTAAGCTGGCGTTTAGCCAAATTTGCCAACAAATATCGACTATGCTGGTTAAAAGATCTCGTCCAGTTCGTCTGGAAAAATTACACCCTGCGCATTGTAAAACGCGTGGCGCAGGATTTTCTCGGCTACGACAACATCACCACCACCCGCCTGCACGGACATATATTCTCCAGCCTGTTGGAAATCCCTAATGTCGTCTGCGATAACACCTACGGCAAAAATACGGGCTACGCCAATTTATGGACCAAAGGGTTGGATTTTGTGACGTTTTATAAA","","","36865","MNQQLIDLKHKLAPIADLIKDKNDVFYLDYPLHLNVGDLLIYHGTEQFFTDHNIHVRLKRSEYDTNIDEIKQKITPNTTILLHGGGNFGDLYPQHQNLREAIVQTFPNNRIIVLPQTLFYKNPKTLEKSTALFRQHPDCHLLARDERTAKAFEAFSPNVYLSPDMAHELYGTLPTKNTHTGKALYFLRKDIEASDIEKNITAQLPAGSHIKDWDDILSKRDSLVLALSWRLAKFANKYRLCWLKDLVQFVWKNYTLRIVKRVAQDFLGYDNITTTRLHGHIFSSLLEIPNVVCDNTYGKNTGYANLWTKGLDFVTFYK","1852038","","possible polysaccharide polymerization protein","Cytoplasm","","
InterPro
IPR007345
Family
Polysaccharide pyruvyl transferase
PF04230\"[24-318]TPS_pyruv_trans


","No hits to the COGs database.","","Residues 166 to 311 match (2e-14) PD:PD129904 which is described as PROTEOME COMPLETE YVFF ","","","","","","","","","","","","Tue Jan 21 14:37:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02656 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 24 to 318 (E-value = 1.8e-09) place AA02656 in the PS_pyruv_trans family which is described as Polysaccharide pyruvyl transferase (PF04230)","","","","","","","","1","","4","" "AA02657","1852152","1852400","249","ATGAATGTAATAAGTTATTCTGCGTTTCGTGCAGAATTGGCAACCACACTTGATCAGGTGGTAGCAGATCATAGCCCAGTCATGATTACCAGACAAAATGGCAAACACGCTGTTGTAATGAGTTTAGAAGATTTCGCAGCTTACGAAGAAACGGCTTATTTATTACGCAGCCCCAAAAATAGAGAGCGTTTATTAGCCTCTATTGACCAGCTCAATTCAGGTAAAATCATCGAACGGGAACTCCAGGAA","","","12307","MNVISYSAFRAELATTLDQVVADHSPVMITRQNGKHAVVMSLEDFAAYEETAYLLRSPKNRERLLASIDQLNSGKIIERELQE","1852398","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003756
Family
Protein of unknown function DUF172
PF02604\"[1-74]TPhdYeFM
InterPro
IPR006442
Family
Prevent-host-death protein
TIGR01552\"[3-56]Tphd_fam: prevent-host-death family protein


","BeTs to 3 clades of COG2161COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG2161 is ----------r--ce-----------Number of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-11) to 1/1 blocks of the IPB003756 family, which is described as \"DUF172\". Interpro entry for IP:IPR003756. IPB003756 2-36 1.3e-11","Residues 1 to 57 match (1e-10) PD:PD029069 which is described as PROTEOME COMPLETE SP1741 SSR0761 SSR2754 PHD PLASMID RC0121 ATU2018 ALL0172 ","","","","","","","","","","","","Tue Jan 21 10:05:20 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02657 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 78 (E-value = 5.6e-28) place AA02657 in the DUF172 family which is described as Uncharacterized ACR, COG2161 (PF02604)","","","","","","","","1","","4","" "AA02658","1852400","1852651","252","ATGATTTTAGCTTGGACGGAAACCGCCTGGGAAGATTATCTTTATTGGCAGCAAGTTGATAAAAAGACGTTGTTGCGCATTAATAAACTTATCCAAAATATTACCAGATCACCTTTCGAAGGCTTAGGCAATCCTAAACCTTTAAAACATCAGTTATCCGGGTTTTGGTCTAGAAGAATAGATAAAGAGCATCGTCTTGTATACCAAGTATCGGATAGCCATTTAACGATTATTCAATGCCGCTATCACTAC","","","10200","MILAWTETAWEDYLYWQQVDKKTLLRINKLIQNITRSPFEGLGNPKPLKHQLSGFWSRRIDKEHRLVYQVSDSHLTIIQCRYHY","1852649","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR009614
Family
Addiction module toxin, Txe/YoeB
PF06769\"[5-84]TPlasmid_Txe
TIGR02116\"[5-84]Ttoxin_Txe_YoeB: addiction module toxin, Txe


","No hits to the COGs database.","","Residues 1 to 64 match (3e-19) PD:PD028652 which is described as PROTEOME COMPLETE SP1740 AVIX3 ASL0171 ATU2017 PLASMID DOC RV3358 YOEB ","","","","","","","","","","","","Tue Jan 21 10:06:43 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02658 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 84 (E-value = 8.3e-55) place AA02658 in the DUF1224 family which is described as Protein of unknown function (DUF1224) (PF06769)","","","","","","","","1","","4","" "AA02659","1852667","1853407","741","ATGTTCGAACTCAAAAAACTCATCACCACTATGCTGTTGCCACCATTTAATGTATTGATTTTATGGTTGCTTTCCTTATTTTTTTCATTAATCAGATGCAAAGCCGTAGGGCGTTTATGCGCTTTGCTTGGCATTTTGATTCTTTATGTGGTCAGCATTCCTTACACGGCGCAAATCCTTAAAGACAGCTTGGTGACGGAAGATCATTTAACCTTAGAGGATTACAAGCAGGCGCAAGCTATTGTGTTACTGGGCGGCGGTGTGCGTGACAGCAAAGAATTATATGCGCCTCTCGCCTCTTCCGCCACGCAATTAGAACGTTTGCGTTACGCTGCTTATTTGCAAAAAGAAACGCAGTTACCGTTATTAATCAGCGGTGTCAGCCCGACGGGTGCTTCGGAAGCCAAGGTATCCGCACAGGAACTGCTGGATTTCTTTCATGTGCCGACCAAGTGGCTGGAAGAAAAATCCCTAACCACCAAAGAAAATGCGTTATATACCCGTCAATTGCTGGAAAAAGAAGGCATCAATAAAATCATCTTAGTGACAAATGAATGGCATATGCAACGCGCCAAACTGTTATTTGAAGGACAGGGATTTCAAGTGTTGCCGGCAAGTGTCGGTGAAGGCATTACCCCTGAGGCTTATTCGTTAAATATGATGCACTTTATCCCACAAGCCGGCGCCATAGCAAAAAATATGCAATTACTGAAAGAATGGATGGGGTATTTGAAAGAAAAA","","","27785","MFELKKLITTMLLPPFNVLILWLLSLFFSLIRCKAVGRLCALLGILILYVVSIPYTAQILKDSLVTEDHLTLEDYKQAQAIVLLGGGVRDSKELYAPLASSATQLERLRYAAYLQKETQLPLLISGVSPTGASEAKVSAQELLDFFHVPTKWLEEKSLTTKENALYTRQLLEKEGINKIILVTNEWHMQRAKLLFEGQGFQVLPASVGEGITPEAYSLNMMHFIPQAGAIAKNMQLLKEWMGYLKEK","1853405","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR003848
Domain
Protein of unknown function DUF218
PF02698\"[77-243]TDUF218
noIPR
unintegrated
unintegrated
signalp\"[1-33]?signal-peptide
tmhmm\"[10-30]?\"[39-57]?transmembrane_regions


","BeTs to 9 clades of COG1434COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG1434 is -------qvd-l-cefghsn-jx---Number of proteins in this genome belonging to this COG is","","Residues 1 to 56 match (8e-07) PD:PD096330 which is described as PROTEOME COMPLETE TRANSMEMBRANE PM0506 HI1701 ","","","","","","","","","","","","Tue Jan 21 10:07:33 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02659 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 6 to 246 (E-value = 5.3e-67) place AA02659 in the DUF218 family which is described as Uncharacterized ACR, COG1434 (PF02698)","","","","","","","","1","","4","" "AA02662","1853423","1853656","234","TTGACCGCACTTTACCGCGAAAACAATCGAAGAATGCGCCAAGACAAAGCGCATTTTTTCGTGTTTTCATTTTTGATTTGGGATCGCCGTCGCAAAAATTCACAGGCATTGTTTATCTATAGCGCGCCTTTACCTATGCTCCTTTTTTATTTAAAGGAACTCGTATGCGTCATTTTAAACTGCTTCTCACCCTCTACTTTTTCAGCCTTTTTTGTTACGCAGAAAAACCGGATT","","","9413","LTALYRENNRRMRQDKAHFFVFSFLIWDRRRKNSQALFIYSAPLPMLLFYLKELVCVILNCFSPSTFSAFFVTQKNRI","1853656","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
tmhmm\"[32-50]?\"[56-74]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 16:13:42 2004","Mon Feb 23 16:13:42 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02662 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 16:13:42 2004","","","","","","","","","","","","","1","","4","" "AA02663","1853704","1854411","708","ATGAGCGAAAAATTAGATGGTGTACGCGGTTACTGGGACGGCAAACAAATGTTTACCCGCGGTGGCGTGCAACTGAGTCCGCCTACTTACTTTCTGGAAAAATTCCCGCCTTTTGCCATTGATGGCGAATTATTTAGTCAACGTGATCAATTTGCCGACATTTCTTCTATTGTTCGCGCTTATCAGGACAAAGGCTGGAATAAATTAAAGCTGTATGTCTTTGATGTGCCTGACGCTGAAGGAGACTTATTTGCCCGCTTGGCACAATTAAAAACCTATTTGGCGCAAAACCCAAGCGACTATATTGAAATTATTGAACAGATTCCTATTGAGAGCCCACAACATATTCAGCAATTTTTGCAGCAGGTGGAACAGCTCAAAGGTGAAGGCATTGTCATTCGCAATCCTAATGCGCCCTACGAAAGAAAACGCAGTTCGCAAATACTCAAATTAAAGACCGCACTTGACGAAGAATGCACCGTTGTCGCCCACCACAAAGGCAAAGGGCAGTTTGAAAGTGTGATGGGATCGCTCACTTGCGAAAACCATCGAGGGCAATTCAAAATCGGTTCGGGTTTCAAGTTGGATGATCGCATTAACCCGCCCCCGATCGGCGCCGTCATTACGTATAAATATCGCGGTTTAACCAATAAAGGTAAACCCAGATTTGCAACCTTTTGGCGGACAACCGAGCAAATACAGATACCC","","","31701","MSEKLDGVRGYWDGKQMFTRGGVQLSPPTYFLEKFPPFAIDGELFSQRDQFADISSIVRAYQDKGWNKLKLYVFDVPDAEGDLFARLAQLKTYLAQNPSDYIEIIEQIPIESPQHIQQFLQQVEQLKGEGIVIRNPNAPYERKRSSQILKLKTALDEECTVVAHHKGKGQFESVMGSLTCENHRGQFKIGSGFKLDDRINPPPIGAVITYKYRGLTNKGKPRFATFWRTTEQIQIP","1854409","","DNA ligase","Cytoplasm, Periplasm","","
InterPro
IPR000977
Family
ATP-dependent DNA ligase
PS00333\"[129-152]TDNA_LIGASE_A2
InterPro
IPR012310
Domain
ATP dependent DNA ligase, central
PF01068\"[1-152]TDNA_ligase_A_M
PS50160\"[71-152]TDNA_LIGASE_A3
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[152-235]Tno description
noIPR
unintegrated
unintegrated
PTHR10459\"[71-180]TATP-DEPENDENT DNA LIGASE FAMILY


","No hits to the COGs database.","","Residues 1 to 228 match (1e-93) PD:PD451817 which is described as DNA LIGASE PROTEOME COMPLETE SYNTHASE REPLICATION REPAIR RECOMBINATION ATP POLYDEOXYRIBONUCLEOTIDE ","","","","","","","","","","","","Wed Jan 22 08:53:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02663 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 152 (E-value = 2.6e-14) place AA02663 in the DNA_ligase_A_M family which is described as ATP dependent DNA ligase domain (PF01068)","","","","","Cheng C, Shuman S.Characterization of an ATP-dependent DNA ligase encoded by Haemophilus influenzae.Nucleic Acids Res. 1997 Apr;25(7):1369-74.PMID: 9060431Sriskanda V, Shuman S.A second NAD(+)-dependent DNA ligase (LigB) in Escherichia coli.Nucleic Acids Res. 2001 Dec;29(24):4930-4.PMID: 11812821Sriskanda V, Shuman S.Conserved residues in domain Ia are required for the reaction of Escherichia coli DNA ligase with NAD+.J Biol Chem. 2002 Mar;277(12):9695-700.PMID: 11781321Kaczmarek FS, Zaniewski RP, Gootz TD, Danley DE, Mansour MN, Griffor M, Kamath AV, Cronan M, Mueller J, Sun D, Martin PK, Benton B, McDowell L, Biek D, Schmid MB.Cloning and functional characterization of an NAD(+)-dependent DNA ligase from Staphylococcus aureus.J Bacteriol. 2001 May;183(10):3016-24.PMID: 11325928","","Wed Jan 22 09:06:14 2003","1","","","" "AA02666","1856643","1854550","2094","GTGCTGGCGGGGGCGGGGAGCGGTAAGACCCGTGTACTGACACATCGCATTGCGTGGTTGATCGGTGTTGAAGGTATTTCCGAAGGCAGTATTATGGCGGTGACCTTTACCAACAAAGCCGCCGCAGAAATGCGTCATCGTATTGAATCCGTGTTATCTGATGGCAATCAACGCCTGTTTGGTATGTGGGTCGGCACCTTTCATAGCACTGCCCATCGATTGCTACGCGCCCATCACCTTGATGCGGATCTGCCGCAAGATTTCCAGATTTTGGATTCGGAAGATCAGTTGCGTTTAATCAAACGCTTAATGAAACTGCACAATTTCGACGAAAAAAGTTTTCCACCGAAACAAGCCTGTTGGTACATCAATAATAAGAAAGATGAAGGGCTGCGTCCGAATCACATTGACGATCACAACGATCGTCAGGAACGTGAATGGATCAAAATTTATCAAATTTATCAAGATGCCTGCGATCGTGCAGGGTTGGTGGATTTTGCCGAAATTTTATTACGTTCTTACGAACTGTTTTTACACAAACCGCTGATTTTGCAACGTTATCAACAACGTTTTCAGCATATTTTGGTGGATGAGTTCCAAGATACCAACAAAATTCAATATGAATGGATTCGCTTGCTGGCGGGCAAAACCGGCAAAGTGATGATTGTGGGCGATGACGACCAGTCTATTTACGGCTGGCGCGGTGCAAAAATTGAAAATATTCAGTTATTTTTAAAAGATTTTGCCAACGCACAAACTATTCGTCTGGAACAAAATTACCGTTCCACCATGAACATTTTGCAAGCTGCCAATGAATTGATCGCCAACAACAGCAATCGTTTGGGGAAAAATTTGTGGTCGGAAGGCAATCAGGGCGAACCGGTGGGCATTTACGCCGCCTTCAATGAATTGGATGAAGCATTGTTTGTGGCTTCACAAATCAAGACTTGGATTGAAGACGGCGGTAAATTAAACGATTGTGCCATTTTATACCGTAGTAACAGCCAGTCACGAGTGATTGAAGAAGCGCTGATTCGTTCGCAAATTCCGTATCGCATTTATGGTGGGATGCGCTTCTTTGAACGGCAGGAAATTAAAGATGCCTTGGCTTATTTACGGTTAATCGCCAATCGACAGGACGATGCTGCCTTTGAGCGGGTCATTAATACGCCACCGCGCGGCATTGGCGATCGCACGTTGGATACCTTGCGCAATCTTACCCGTGAACATCAAATCACCTTATGGCAAGCCACCAATCTGGCGCTTCAGGAAAACAAACTCGCCGGGCGCGCCGCTACGGCATTGTTACGCTTTATGGAGTTAATTAATTCTTTGCAGCGGGACACGGAAGAAATGCCGTTGTTTGCGCAAACGGATTTTGTGATTAAGCATTCCGGGTTGTATCAAATGTACAAACAGGAAAAGGGCGAAAAAGGGGAGGTGCGTATTGAAAACCTGGAAGAATTGGTGTCTGCCGCCCGTGAATTTATCAAACCTGAAGACGCGGAAGATATGACGGATCTGACGGCATTTTTAACTCACGCTTCATTGGAGGCGGGCGAGGAGCAGGCTGCGCCACATCAGGCTTGCGTCGAAATGATGACGCTGCATTCGGTAAAAGGCTTGGAGTTTCCGCGTGTTTTCATGATTGGCGTGGAAGAAGGATTATTCCCGAGTTTCCGTTCTTTTGAAGAAGCGGGGCGTCTGGAAGAAGAGCGCCGTTTGGCATACGTCGGGATTACCCGCGCCAAGCAGAAACTCACCATTTCTTATGCGGAAAGCCGCCGTTTATATGGCAAGGAAGAACGTCATTTGCCTTCCCGTTTTATCACCGAATTACCCCAGCAATGTTTGCAGGAAATCCGTTTACGCGGTACCGTTACCCGTGCGTTAAATCAAGCGAAAATCGGAAGTGTTGCGCCGGTTGTGGGGGGAAGCGAATGGAAAATGGGGCAGAAAGTGAAACACGAAAAATTCGGTTTCGGTACGGTGATCAATGTGGAAGGTGCAGACAACAATTTACGCCTGCAAATTGCTTTCCAGAATCAGGGCATTAAATGGTTGATTGCCCATTTGGCGAAGTTGGAGAAAGTA","","","82942","VLAGAGSGKTRVLTHRIAWLIGVEGISEGSIMAVTFTNKAAAEMRHRIESVLSDGNQRLFGMWVGTFHSTAHRLLRAHHLDADLPQDFQILDSEDQLRLIKRLMKLHNFDEKSFPPKQACWYINNKKDEGLRPNHIDDHNDRQEREWIKIYQIYQDACDRAGLVDFAEILLRSYELFLHKPLILQRYQQRFQHILVDEFQDTNKIQYEWIRLLAGKTGKVMIVGDDDQSIYGWRGAKIENIQLFLKDFANAQTIRLEQNYRSTMNILQAANELIANNSNRLGKNLWSEGNQGEPVGIYAAFNELDEALFVASQIKTWIEDGGKLNDCAILYRSNSQSRVIEEALIRSQIPYRIYGGMRFFERQEIKDALAYLRLIANRQDDAAFERVINTPPRGIGDRTLDTLRNLTREHQITLWQATNLALQENKLAGRAATALLRFMELINSLQRDTEEMPLFAQTDFVIKHSGLYQMYKQEKGEKGEVRIENLEELVSAAREFIKPEDAEDMTDLTAFLTHASLEAGEEQAAPHQACVEMMTLHSVKGLEFPRVFMIGVEEGLFPSFRSFEEAGRLEEERRLAYVGITRAKQKLTISYAESRRLYGKEERHLPSRFITELPQQCLQEIRLRGTVTRALNQAKIGSVAPVVGGSEWKMGQKVKHEKFGFGTVINVEGADNNLRLQIAFQNQGIKWLIAHLAKLEKV","1854548","From HD1032 record:This protein may process damage occurring in nonreplicating regions of DNA to produce recombinational intermediates for sister strand recombinational exchange.","DNA helicase II","Cytoplasm","","
InterPro
IPR000212
Family
UvrD/REP helicase
PTHR11070\"[1-448]T\"[465-624]TUVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER
PF00580\"[1-467]TUvrD-helicase
InterPro
IPR005753
Family
ATP-dependent DNA helicase UvrD
TIGR01075\"[1-696]TuvrD: DNA helicase II
InterPro
IPR014016
Domain
Helicase superfamily 1, UvrD-related
PS51198\"[1-263]TUVRD_HELICASE_ATP_BIND
InterPro
IPR014017
Domain
UvrD-like DNA helicase, C terminal
PS51217\"[264-541]TUVRD_HELICASE_CTER
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[1-254]T\"[257-622]Tno description


","BeTs to 22 clades of COG0210COG name: Superfamily I DNA and RNA helicasesFunctional Class: LThe phylogenetic pattern of COG0210 is -omp--yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.3e-70) to 7/7 blocks of the IPB000212 family, which is described as \"UvrD/REP helicase\". Interpro entry for IP:IPR000212. IPB000212A 3-13 3.2e-06 IPB000212B 31-48 3e-12 IPB000212C 196-207 4.2e-07 IPB000212D 223-236 2e-10 IPB000212E 256-274 3.2e-09 IPB000212F 531-549 7.9e-09 IPB000212G 571-583 2.4e-07","Residues 144 to 284 match (4e-07) PD:PD285216 which is described as PROTEOME COMPLETE UVRD/REP HELICASE FAMILY ","","","","","","","","","","","Wed Jan 22 09:10:38 2003","Wed Jan 22 09:10:38 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02666 is paralogously related to AA00527 (1e-106), AA00021 (1e-10) and AA02266 (3e-06).","","","","","","Residues 1 to 467 (E-value = 7.7e-209) place AA02666 in the UvrD-helicase family which is described as UvrD/REP helicase (PF00580)","","","","","Walter RB, Morton KA, Stuy JH.The sequence of the Haemophilus influenzae mutB gene indicates it encodes a DNA helicase II-like protein.Gene. 1993 Dec;136(1-2):35-40.PMID: 8294031Yamamoto Y, Ogawa T, Shinagawa H, Nakayama T, Matsuo H, Ogawa H.Determination of the initiation sites of transcription and translation of the uvrD gene of Escherichia coli.J Biochem (Tokyo). 1986 Jun;99(6):1579-90.PMID: 2943729Easton AM, Kushner SR.Transcription of the uvrD gene of Escherichia coli is controlled by the lexA repressor and by attenuation.Nucleic Acids Res. 1983 Dec;11(24):8625-40.PMID: 6324092","","Tue Dec 2 12:44:44 2003","1","","","" "AA02667","1856749","1856874","126","TTGTACAGGCTAAATTATAGCAATTTCTATTCAAAATACAATGAAAGAAAAGGACGGGGAAAAGTGCGGTGGTTTTTCACGATGGTTTTTTATATGGAAAAGCGCACCATCATGATGCGCTTTAAA","","","5470","LYRLNYSNFYSKYNERKGRGKVRWFFTMVFYMEKRTIMMRFK","1856874","","hypothetical protein","Cytoplasm, Extracellular","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 16:12:08 2004","Mon Feb 23 16:12:08 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02667 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 16:12:08 2004","","","","","","","","","","","","","1","","","" "AA02668","1858181","1856898","1284","ATGCATGCCTTTGTGGCGTTAATTTTAGTCAGTTTATTGACCGCACTTGCCGCAGGAATTGCCGTGGATAAAATCCTGCCGACCATGTTAACCGGCTTCGGTAACACCTTGGCGTCCGTGGCGTTATTAGTCGGTTTGGGTACCATGATCGGGCGTTTATTGGAAGTCACCGGCGGGGCAAAAGTGCTTGCGGATACGTTGATTAATAAATTCGGCGAAAAGAAAGCGCCTTTTGCGCTGGGGATTGCCGCGTTGCTGTTCGGCTTCCCGATTTTCTTTGATGCCGGTCTGGTGGTCATGTTGCCTATCGTCTTTAGTGTCGCAAAACGTTTCGGTGGTTCCGTCTTGCGTTATGCCTTCCCGGTTGCCGGTGCTTTTGCGGTCATGCACGCGTTTTTACCGCCGCATCCGGGTCCGGTGGCTTCCGGTGATTTACTCGGCGTGAATATGGGCTTGATGGTGATTGTTGGCTTAATTTGCGCGATCCCGACCTGGTACATCGGTACTTATTTGTTCAGTATGTACATCAGTAAAAAATTTTTTGTGGAACTGCCGAAAACCTTTTTGAACACCGCCGCCATCAGCGAAACCTCCGTGCAAAATCCACCGGCGTTTGGGCGCGTTCTGTTTATTTTGGTTTTACCGATTTTCCTTATTTTGTTTGATACCGGGTTAAATACCCTCAGCGTGGCAAAAGTGATTGACGGTTCTTCCTTGTGGGTCGAAAGCCTGCGCCTCATCGGCAAAACCCCGATCGCGTTATTAATCACATTATTAATTGCCATTGCCTTATTGCGCGGAGAACGCAGTTATGAACAAATCGAAAGCCTTTGTAACAGTGCGCTGGGACCGATTTGCTCCATTATTTTAGTGACCGGTGCGGGCGGTATGTTCGGTGGCGTATTGCGCGCCAGCGGCATCGGCGATGAGTTATCCGCCATGTTGTCAAATACCGGTATGCCGATTATCATCGCCGCCTTTATTATTTCTATGGCATTGCGTGTGGCACAAGGTTCGGCAACGGTAGCCCTGACTACTGCAGCCGCATTAATCGCCCCGACCGTTGCCGCCGCAACCGATCTCAGCCAATTGGATTTATGTTTTATCGTGATTGCCATTGCCTCCGGCGCCACCGTATTCTCCCATGTGAACGACAGCGGTTTCTGGTTAATAAGCCGTTTCTTGGAAATGGACACCAAAACCACGTTAAAAACCTGGACCATGTTGGAAACCTCCATCGGTTTTGTCGGTTTTATTATCGCTTTAATCGGTAGCATTATTTTC","","","47283","MHAFVALILVSLLTALAAGIAVDKILPTMLTGFGNTLASVALLVGLGTMIGRLLEVTGGAKVLADTLINKFGEKKAPFALGIAALLFGFPIFFDAGLVVMLPIVFSVAKRFGGSVLRYAFPVAGAFAVMHAFLPPHPGPVASGDLLGVNMGLMVIVGLICAIPTWYIGTYLFSMYISKKFFVELPKTFLNTAAISETSVQNPPAFGRVLFILVLPIFLILFDTGLNTLSVAKVIDGSSLWVESLRLIGKTPIALLITLLIAIALLRGERSYEQIESLCNSALGPICSIILVTGAGGMFGGVLRASGIGDELSAMLSNTGMPIIIAAFIISMALRVAQGSATVALTTAAALIAPTVAAATDLSQLDLCFIVIAIASGATVFSHVNDSGFWLISRFLEMDTKTTLKTWTMLETSIGFVGFIIALIGSIIF","1856896","","gluconate permease","Inner membrane, Cytoplasm","","
InterPro
IPR003474
Family
Gluconate transporter
PF02447\"[1-427]TGntP_permease
TIGR00791\"[1-428]TgntP: transporter, gluconate:H+ symporter (
noIPR
unintegrated
unintegrated
signalp\"[1-19]?signal-peptide
tmhmm\"[4-22]?\"[37-57]?\"[76-105]?\"[115-133]?\"[152-172]?\"[208-230]?\"[244-264]?\"[285-307]?\"[313-333]?\"[338-358]?\"[364-384]?\"[405-427]?transmembrane_regions


","No hits to the COGs database.","Significant hit (2.6e-100) to 4/4 blocks of the IPB003474 family, which is described as \"GntP family permease\". Interpro entry for IP:IPR003474. IPB003474A 32-72 2.3e-24 IPB003474B 120-171 1e-27 IPB003474C 320-355 4.2e-19 IPB003474D 368-407 1.4e-25 IPB003474A 280-320 0.12 IPB003474A 293-333 0.74","Residues 270 to 339 match (3e-09) PD:PD014325 which is described as PROTEOME COMPLETE TRANSMEMBRANE MEMBRANE PERMEASE TRANSPORTER GLUCONATE INNER C4-DICARBOXYLATE PLASMID ","","","","","","","","","","","","Wed Jan 22 09:20:41 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02668 is paralogously related to AA00143 (8e-18).","","","","","","Residues 1 to 427 (E-value = 7.8e-115) place AA02668 in the GntP_permease family which is described as GntP family permease (PF02447)","","","","","Peekhaus N, Tong S, Reizer J, Saier MH, Murray E, Conway T.Characterization of a novel transporter family that includes multiple Escherichia coli gluconate transporters and their homologues.FEMS Microbiol Lett. 1997 Feb;147(2):233-8.PMID: 9119199Sweeney NJ, Klemm P, McCormick BA, Moller-Nielsen E, Utley M, Schembri MA, Laux DC, Cohen PS.The Escherichia coli K-12 gntP gene allows E. coli F-18 to occupy a distinct nutritional niche in the streptomycin-treated mouse large intestine.Infect Immun. 1996 Sep;64(9):3497-503.PMID: 8751890Klemm P, Tong S, Nielsen H, Conway T.The gntP gene of Escherichia coli involved in gluconate uptake.J Bacteriol. 1996 Jan;178(1):61-7.PMID: 8550444Reizer A, Deutscher J, Saier MH, Reizer J.Analysis of the gluconate (gnt) operon of Bacillus subtilis.Mol Microbiol. 1991 May;5(5):1081-9.PMID: 1659648","","Wed Jan 22 09:20:41 2003","1","","","" "AA02670","1858189","1858323","135","TTGATAATTAATAGCAGAAGTAAAAGCACTGCTGCGATCATAATAAAAATTAACATAATAATTCCTTATGTTGATAATGTTATCGGTAACATACCTTTTTGCCGACTTTTGGTAAATAAACAGCATTTAAAAATG","","","5071","LIINSRSKSTAAIIIKINIIIPYVDNVIGNIPFCRLLVNKQHLKM","1858323","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 16:10:30 2004","Mon Feb 23 16:10:30 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02670 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 16:10:30 2004","","","","","","","","","","","","","1","","","" "AA02671","1858462","1858977","516","ATGGCAACAGGCAAAAGCATTATTTTAATGGGAGTTTCCAGTACAGGAAAAACATCAGTGGGGACGGAAGTAGCACGTCGTTTGGAGATAAAACTGATTGATGGCGATGATCTGCACCCGCGCGCCAATATCATAAAAATGGGCGAAGGACATCCGCTCAATGATGAAGATCGGGCGCCTTGGTTGGAGCGTATTCGCGATGCAGCATTTAGCCTGGAGCAAAAAAGCGAGATGGGCATTATCGTTTGTTCCGCCCTCAAGAAGAAATACCGTGACCAAATCCGTCACGGCAACCGCAATGTGAAGTTCCTCTTTTTACAAGGATCTTATGATGTGATTCTGGAACGTATGCGCCAACGCAAAGGGCATTATATGAAAGAATCCATGTTGAAAAGTCAGTTTGATACGCTGGAAGTGCCGGGGGCGGATGAACCGGATGTGATCGCCATCGATATTGACGCCTCTTTTGAAGAGGTTGTAGCGCGTTGCGTTCAGGCACTGAAACCTTATCTTTCC","","","19390","MATGKSIILMGVSSTGKTSVGTEVARRLEIKLIDGDDLHPRANIIKMGEGHPLNDEDRAPWLERIRDAAFSLEQKSEMGIIVCSALKKKYRDQIRHGNRNVKFLFLQGSYDVILERMRQRKGHYMKESMLKSQFDTLEVPGADEPDVIAIDIDASFEEVVARCVQALKPYLS","1858975","","gluconokinase","Cytoplasm","","
InterPro
IPR000623
Domain
Shikimate kinase
PF01202\"[13-168]TSKI
InterPro
IPR002891
Domain
Adenylylsulfate kinase, C-terminal
PD002350\"[4-167]TQ7NN99_GLOVI_Q7NN99;
InterPro
IPR006001
Family
Carbohydrate kinase, thermoresistant glucokinase
TIGR01313\"[7-169]Ttherm_gnt_kin: carbohydrate kinase, thermor
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[7-171]Tno description


","No hits to the COGs database.","Significant hit ( 1.3e-05) to 1/5 blocks of the IPB000623 family, which is described as \"Shikimate kinase\". Interpro entry for IP:IPR000623. IPB000623A 7-36 1.3e-05","Residues 4 to 66 match (2e-25) PD:PD011135 which is described as KINASE GLUCONOKINASE COMPLETE PROTEOME TRANSFERASE THERMORESISTANT GLUCONATE THERMOSENSITIVE ATP-BINDING UTILIZATION ","","","","","","","","","","","","Wed Jan 22 09:30:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02671 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Izu H, Adachi O, Yamada M.Gene organization and transcriptional regulation of the gntRKU operon involved in gluconate uptake and catabolism of Escherichia coli.J Mol Biol. 1997 Apr;267(4):778-93.PMID: 9135111Tong S, Porco A, Isturiz T, Conway T.Cloning and molecular genetic characterization of the Escherichia coli gntR, gntK, and gntU genes of GntI, the main system for gluconate metabolism.J Bacteriol. 1996 Jun;178(11):3260-9.PMID: 8655507","","Wed Jan 22 09:30:24 2003","1","","","" "AA02673","1860048","1859053","996","ATGAATAAAAATAAACGTCCTACCTTACAAGACATTGCCGATTATCTTGGCATCACGAAAATGACCATCAGCCGCTATTTGCGCAATCCCGATTCCGTGGCGAACGGCACGCAGGCGCGCATTGCGGAAGCCATTGAACGTTTCGGCTATATTCCTAATCGCGCGCCGGATATTTTGTCGAATGCTAAGAGTCGGGCAATCGGTGTGTTGGTACCGTCGCTGACCAACCAAGTATTCGCCAATGTGATTCGTGGTATTGAACAGGTGACCGATAAAGCGGGCTATCAAACTATGTTAGCGCACTATGGCTACAGCGAAGAAAAAGAAGAGCAGCGCATTGAAAGCCTGCTTTCCTATAACGTAGACGGCATTATTTTGTCGGAAAGTCATCATTCCGAAAGAACCAAAAAAATGCTGAAAATAGCGAATATTCCAGTGATTGAAATTATGGATACGACCGAAGTGGGCATTCAGCAAGTCGTCGGCTTTGATAATATTGCGGCGGCACAGGCCATGGTGGAAACCATGATTAATCGCGGACATCGCAATGTGGCATATTTTGCTGCCCGTCAGGACAAACGCACCCGATTACGTCAACAGGGCTATGAAAATGCCATGACAAAGCATCAATTAACGCCACAGGTGATCGCCACCAAAGCGCATTCTTCTTTTACCTTGGGCGGAGAATTGTTACATCAGGCGCTCGCCAAATTTCCACCGTTGGACGGCATTTTTTGCACCAATGATGACATCGCCATCGGCGCGATTTTCGAATGCCGGCGTTTAGGTATTAAGGTTCCTGCACAAATCGCCGTGGCAGGCTTTCACGGACACGACGTGGGGCAATCCATCACGCCGCAACTTGCCACGGTCATCACGCCGCGTCTGGAAATCGGGCGAATTGCCGCGCAGGAATTACTGGCGCGCATTAACGACATCCCGGCGCAAAGTGCGATTATTAACTTGGGTTATCAGATTCATTTGGGCGAAAGCATT","","","36636","MNKNKRPTLQDIADYLGITKMTISRYLRNPDSVANGTQARIAEAIERFGYIPNRAPDILSNAKSRAIGVLVPSLTNQVFANVIRGIEQVTDKAGYQTMLAHYGYSEEKEEQRIESLLSYNVDGIILSESHHSERTKKMLKIANIPVIEIMDTTEVGIQQVVGFDNIAAAQAMVETMINRGHRNVAYFAARQDKRTRLRQQGYENAMTKHQLTPQVIATKAHSSFTLGGELLHQALAKFPPLDGIFCTNDDIAIGAIFECRRLGIKVPAQIAVAGFHGHDVGQSITPQLATVITPRLEIGRIAAQELLARINDIPAQSAIINLGYQIHLGESI","1859051","functional class from Y. pestis, gi:22127744].*****","gluconate utilization operon repressor","Cytoplasm","","
InterPro
IPR000843
Domain
Bacterial regulatory protein, LacI
PF00356\"[7-32]TLacI
SM00354\"[6-76]THTH_LACI
PS50932\"[7-61]THTH_LACI_2
InterPro
IPR001761
Domain
Periplasmic binding protein/LacI transcriptional regulator
PF00532\"[64-314]TPeripla_BP_1
noIPR
unintegrated
unintegrated
G3DSA:1.10.260.40\"[7-64]Tno description
G3DSA:3.40.50.2300\"[65-203]Tno description


","No hits to the COGs database.","Significant hit ( 1.8e-18) to 2/2 blocks of the IPB000843 family, which is described as \"Bacterial regulatory protein, LacI family\". Interpro entry for IP:IPR000843. IPB000843A 8-28 7.6e-06 IPB000843B 33-71 4.9e-11","Residues 276 to 332 match (2e-07) PD:PD485071 which is described as PROTEOME COMPLETE GALR/LACI REGULATORY REGULATOR L-IDONATE FAMILY ","","","","","","","","","","","Wed Jan 22 09:41:33 2003","Wed Jan 22 09:41:33 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02673 is paralogously related to AA02003 (2e-25), AA00749 (5e-23), AA02006 (2e-11), AA00209 (2e-09), AA00932 (5e-06), AA02787 (8e-04) and AA01462 (8e-04).","","","","","","Residues 64 to 332 (E-value = 3.9e-19) place AA02673 in the Peripla_BP_1 family which is described as Periplasmic binding proteins and sugar binding domain of the LacI family (PF00532)","","","","","Izu H, Adachi O, Yamada M.Gene organization and transcriptional regulation of the gntRKU operon involved in gluconate uptake and catabolism of Escherichia coli.J Mol Biol. 1997 Apr;267(4):778-93.PMID: 9135111Tong S, Porco A, Isturiz T, Conway T.Cloning and molecular genetic characterization of the Escherichia coli gntR, gntK, and gntU genes of GntI, the main system for gluconate metabolism.J Bacteriol. 1996 Jun;178(11):3260-9.PMID: 8655507","","Wed Jan 22 09:41:48 2003","1","","","" "AA02674","1860792","1860100","693","GTGGCGCTGGTTTATAATGATATTTCCCATACGGTAATGATGTGTTCGCCCCGTGATTTAGAGGATTTCGCTATGGGATTTTCGCTATCGGAAGGCATTATTGAAAAACCGAGTGATATTTATAGTATTGATATTGAAGAAGTTTGTAATGGTATTGAAGCCAGAGTCGAATTAGCCACCCGCTGTTTTGTGGCGCTGAAAGATCATCGCCGCACCTTAACCGGGCGAACCGGTTGCGGCATTTGCGGCGCAGAGCAGTTGCAACAGGTTTATAAAAACGTCGCCAAATTAGACCGCACTTTAACCTTCGATGTGGCGCAGCTGGACGATTGTTTAGAGCAATTGCAGAAATCGCAGGAACTGGGCAAACAAACGGGTTCCACACACGCCGCCGGTTTCTTTTCTTTGGAAGGGAGCTTGCTTGCTATTCGGGAAGATGTGGGGCGTCATGTGGCGTTGGATAAATTATTGGGCTGGCACGCCAAAGCAGGGAAGCCGCAAGGTTTTATCGTCGTCACCAGCCGTGCCAGTTATGAAATGGTGCAAAAAACCGTGTCTGTCGGAGTAGAAATATTGGTGGCGATTTCGGCTTCCACGGATTTGGCGGTGCAATATAACTTAACCCTGATCGGTTTTGCCAGAGCAGGGCGCGCCACAGTTTACAGCGGCAGAGAACGGTTACGGATTTGTGAT","","","29876","VALVYNDISHTVMMCSPRDLEDFAMGFSLSEGIIEKPSDIYSIDIEEVCNGIEARVELATRCFVALKDHRRTLTGRTGCGICGAEQLQQVYKNVAKLDRTLTFDVAQLDDCLEQLQKSQELGKQTGSTHAAGFFSLEGSLLAIREDVGRHVALDKLLGWHAKAGKPQGFIVVTSRASYEMVQKTVSVGVEILVAISASTDLAVQYNLTLIGFARAGRATVYSGRERLRICD","1860098","From GenBank (gi:1343152):FdhD is necessary for formate dehydrogenase activity and belongs to the FdhD family.","formate dehydrogenase-related protein","Cytoplasm","","
InterPro
IPR003786
Family
Formate dehydrogenase, subunit FdhD
PIRSF015626\"[1-229]TFormate dehydrogenase accessory protein FdhD
PF02634\"[1-225]TFdhD-NarQ
TIGR00129\"[1-229]TfdhD_narQ: formate dehydrogenase family acc


","No hits to the COGs database.","Significant hit ( 1.6e-46) to 4/4 blocks of the IPB003786 family, which is described as \"Formate dehydrogenase subunit FdhD\". Interpro entry for IP:IPR003786. IPB003786A -2-40 1.4e-19 IPB003786B 125-134 0.035 IPB003786C 145-164 5.9e-12 IPB003786D 193-226 2.6e-08","Residues 50 to 92 match (4e-07) PD:PD589991 which is described as PROTEOME FDHD COMPLETE PROBABLE DEHYDROGENASE PA5180 PLASMID FDSC ASSOCIATED FORMATE ","","","","","","","","","","","Wed Jan 22 09:53:53 2003","Wed Jan 22 09:53:53 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02674 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 225 (E-value = 5.6e-104) place AA02674 in the FdhD-NarQ family which is described as FdhD/NarQ family (PF02634)","","","","","Stewart V, Lin JT, Berg BL.Genetic evidence that genes fdhD and fdhE do not control synthesis of formate dehydrogenase-N in Escherichia coli K-12.J Bacteriol. 1991 Jul;173(14):4417-23.PMID: 1648557Bokranz M, Gutmann M, Körtner C, Kojro E, Fahrenholz F, Lauterbach F, Kröger A.Cloning and nucleotide sequence of the structural genes encoding the formate dehydrogenase of Wolinella succinogenes.Arch Microbiol. 1991;156(2):119-28.PMID: 1781728Schlindwein C, Giordano G, Santini CL, Mandrand MA.Identification and expression of the Escherichia coli fdhD and fdhE genes, which are involved in the formation of respiratory formate dehydrogenase.J Bacteriol. 1990 Oct;172(10):6112-21.PMID: 2170340","","Wed Jan 22 09:54:59 2003","1","","","" "AA02675","1861151","1861759","609","ATGCAGATCAGTAGAAGAAAATTCTTTAAGGTCTGTGCCGGAGGAATGGCGGGAACATCCGTTGCGATGTTAGGCTTTGCGCCATCAACGGCCTTGGCGGCACCACGCGAATATAAATTATTGCGTGCCAAAGAATCACGCCAAACCTGTACTTACTGTGCCGTAAGCTGCGGTATGTTGATGTACAGTACAGGGACACCATCCAATACATTAAGTAGTCATACGAGTACCAATACCCGTTCTAAATTATTCCATATTGAAGGTGACCCGGATCACCCGATCAGTCGTGGCGCATTGTGCCCTAAAGGTGCCGGCGCATTAGACTTTGTCAATAGTGAAAGCCGCGCCTTATATCCGCAATATCGCGCACCAGGTTCCGACAAATGGGAACGCCTTTCCTGGCATGATGCGGTTAAGCGCATCGCCCGCCTGATGAAAGATGACCGCGATGCCAACTTTGTCGAGAAAAATGAAGCGGGCAATATCGTTAACCGTTGGACCACTACGGGTATCATGACTGCATCGGCAATCAGTAATGAAGCCGCGCTGCTAACTCATAAGTGGATTCGAATGTTGGGGATGCTACCGGTATGTAACCAAGCGAATACT","","","23115","MQISRRKFFKVCAGGMAGTSVAMLGFAPSTALAAPREYKLLRAKESRQTCTYCAVSCGMLMYSTGTPSNTLSSHTSTNTRSKLFHIEGDPDHPISRGALCPKGAGALDFVNSESRALYPQYRAPGSDKWERLSWHDAVKRIARLMKDDRDANFVEKNEAGNIVNRWTTTGIMTASAISNEAALLTHKWIRMLGMLPVCNQANT","1861757","From GenBank (gi|1169659):FdxG allows formate to be used as a major electron donor during anaerobic respiration. Subunit alpha possibly forms the active site. fdxG is an ortholog of both E. coli fdnG and fdoG.","formate dehydrogenase alpha subunit","Periplasm","","
InterPro
IPR006311
Domain
Twin-arginine translocation pathway signal
TIGR01409\"[3-33]TTAT_signal_seq: Tat (twin-arginine transloc
InterPro
IPR006963
Domain
Molybdopterin oxidoreductase Fe4S4 region
PF04879\"[43-112]TMolybdop_Fe4S4
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.740\"[112-203]Tno description
PTHR11615\"[45-145]T\"[161-202]TNITRATE, FROMATE, IRON DEHYDROGENASE
signalp\"[1-33]?signal-peptide
tmhmm\"[12-32]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 8.3e-11) to 2/3 blocks of the IPB001467 family, which is described as \"Prokaryotic molybdopterin oxidoreductases\". Interpro entry for IP:IPR001467. IPB001467A 100-122 2e-06 IPB001467B 126-148 0.013","Residues 32 to 113 match (5e-29) PD:PD001047 which is described as COMPLETE PROTEOME SUBUNIT OXIDOREDUCTASE FORMATE DEHYDROGENASE NITRATE REDUCTASE ALPHA IRON-SULFUR ","","","","","","","","","","","Wed Jan 22 10:23:12 2003","Wed Jan 22 10:09:42 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02675 is paralogously related to AA00552 (2e-05) and AA01137 (4e-05).","","","","","","Residues 43 to 112 (E-value = 4.4e-16) place AA02675 in the Molybdop_Fe4S4 family which is described as Molybdopterin oxidoreductase Fe4S4 domain (PF04879)","","","","","Berg BL, Li J, Heider J, Stewart V.Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. I. Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA) encodes selenocysteine.J Biol Chem. 1991 Nov;266(33):22380-5.PMID: 1834669Jormakka M, Törnroth S, Byrne B, Iwata S.Molecular basis of proton motive force generation: structure of formate dehydrogenase-N.Science. 2002 Mar;295(5561):1863-8.PMID: 11884747","","Wed Jan 22 10:11:26 2003","1","","","" "AA02676","1861811","1864237","2427","ATGACAAATAACTGGGTTGATATCAAAAACGCCAACCTTATTCTTGTTCAGGGCGGTAACCCTGCCGAAGCCCACCCTGTTGGCTTCCGTTGGGCAATTGAAGCGAAGAAAAACGGTGCGAAAATCATCGTTGTGGATCCGCGCTTCAACCGTACGGCTTCTGTTGCCGATTTACATGCACCAATTCGTTCCGGCTCCGATATTGCATTCTTAATGGGTGTAATTCGTTACTTGCTGGAAACCAATCAGATTCAGCATGAATATGTAAAACATTACACTAACGCCTCTTATTTGGTAAACGAAGGTTACAAATTTGAAGACGGTTTATTCTCAGGCTTTAACGAGGAAAAACACAGTTACGACAAATCGACTTGGAATTATCAATTTGATGAAAACGGCCATCCGAAACGTGATATGACGTTGCAGGATCCGCGTTGCGTGATTAATGTCTTGAAAGAACACGTAGCCCGTTATACGCCCGAAGTGGTTGAAAATATTACCGGTGTAAAACAAAAACTGTTCTTACAAATTTGTGAAGAAATCGGTAAAACCTCTGCACCAAATAAAACCATGACGCATTTGTACGCGTTAGGCTTTACCGAACACACTATCGGTACGCAAAATATTCGCTCCATGGCGATGATCCAATTGTTATTGGGCAATATCGGTATGCCGGGGGGCGGAATTAACGCCTTGCGCGGTCACTCTAACGTACAGGGTACTACCGATATGGGCTTATTACCGACCATGCTGCCGGGCTATATGCGTTTACCGACAGAAAAAGAAAGCTCATTCGATCAGTTTATTAATGCGATTACGCCGAAAGACATCGTGCCGAATCAAATTAACTACTATCGTAATACGCCGAAATTCTTCATTAGTATGATGAAAACCTTCTATGGCGATAAAGCGACCAAAGAAAACAGCTGGGGCTTTGATTATCTTCCAAAAGTGGATCGCGTATATGATCCGATTACCCATGTGAAAATGATGCACGATGGCGAAATGCACGGTTGGATTTTACAAGGTTTCAACGTATTGAACTCCTTGCCGAACAAAAACAAAACCGTTGCCGGTATGAGTAAGTTGAAATACTTGATCGTGTTGGATCCGCTACAAACCGAAAGTTCCGAATTCTGGAGAAACTTCGGCGAATCCAACGAGGTAGATTCTTCCAAAATTCAAACGGAAGTCTTCCGTTTGCCGACCACCTGTTTCGCAGAAGAAGACGGTTCCATCGCGAACTCCGGTCGTTGGGCGCAATGGCACCAAAAATCCTGTGACCAACCGGGTGAAGCCTTACCGGATGCGGATATTTTCTCCATGATTCGTGAAGAAATGCATAAGCTTTACAAGAGCGAAGGTGGTCACGGTATTGAGTCATTTGAAGCAATGACTTGGAACTATGACATTCCGCATTCTCCGTCACCGACAGAATTAGCCAAAGAACTGAACGGTTATGCGTTGGAAGATTTATACGATGCCAACGGCAATCTGATGTACAAAAAAGGGCAATTGCTGAACGCTTTTGCCCACTTGCGAGATGACGGTACGACAACCTCCGGGAACTGGTTATATGTCGGTCAATGGACGGAGAAAGGTAACCAAACGGAAAATCGCGATAATTCCGATCCGTCCGGTTTAGGTTGTACTCTTGGTTGGGGCTTTGCATGGCCAGCAAACCGCCGCGTGCTTTATAGCCGCGCCTCTTTGGATATTAACGGTAATCCTTGGGATAAACACCGTCAACTGATCAAATGGAACGGTAAAAACTGGAACTGGTTTGATATTGCCGACTACGGCACTCAACCACCAGGTTCCGATACCAGACCATTTATGATGTCAGCCGAAGGTGTTGGACGCTTATTTGCCGTTGATAAAATTAATAGCGGACCGTTCCCGGAACACTATGAACCGATTGAAAGTCCGATTGATACGAATCCGCTTCATCCGAATGTGGTATCAGATCCGACGGTGCGTATTTACAAAGAAGATCGCGAGTTTATCGGCTCAAATAAAGAATATCCGTTTGTGGCAACAACTTATCGTCTAACCGAACATTTCCACAGTTGGACCGCGCAATCTGCCATTAACATCATCGCACAACCGCAACAATTTGTGGAAATCGGTGAAAAATTGGCAGAAGAAAAAGGTATCCAAAAAGGCGATATGGTACGTATTACCTCCAAACGGGGCTATATTAAAGCTGTTGCTGTGGTCACCAAACGCCTGAGAGCATTGGAAGTTAACGGAAAAACGGTACACCATGTAGGCATTCCGATTCACTGGAATATGAAAGTATTAAATGGCAAAGGTAACAGAGGTTTCTCAACCAACACGTTGACGCCATCTTGGGGTGAATCAGTGACACAAACCCCTGAATATAAGACTTTCCTGGTGAATGTCGAAAAAATAGCGGAGGCCGCA","","","91513","MTNNWVDIKNANLILVQGGNPAEAHPVGFRWAIEAKKNGAKIIVVDPRFNRTASVADLHAPIRSGSDIAFLMGVIRYLLETNQIQHEYVKHYTNASYLVNEGYKFEDGLFSGFNEEKHSYDKSTWNYQFDENGHPKRDMTLQDPRCVINVLKEHVARYTPEVVENITGVKQKLFLQICEEIGKTSAPNKTMTHLYALGFTEHTIGTQNIRSMAMIQLLLGNIGMPGGGINALRGHSNVQGTTDMGLLPTMLPGYMRLPTEKESSFDQFINAITPKDIVPNQINYYRNTPKFFISMMKTFYGDKATKENSWGFDYLPKVDRVYDPITHVKMMHDGEMHGWILQGFNVLNSLPNKNKTVAGMSKLKYLIVLDPLQTESSEFWRNFGESNEVDSSKIQTEVFRLPTTCFAEEDGSIANSGRWAQWHQKSCDQPGEALPDADIFSMIREEMHKLYKSEGGHGIESFEAMTWNYDIPHSPSPTELAKELNGYALEDLYDANGNLMYKKGQLLNAFAHLRDDGTTTSGNWLYVGQWTEKGNQTENRDNSDPSGLGCTLGWGFAWPANRRVLYSRASLDINGNPWDKHRQLIKWNGKNWNWFDIADYGTQPPGSDTRPFMMSAEGVGRLFAVDKINSGPFPEHYEPIESPIDTNPLHPNVVSDPTVRIYKEDREFIGSNKEYPFVATTYRLTEHFHSWTAQSAINIIAQPQQFVEIGEKLAEEKGIQKGDMVRITSKRGYIKAVAVVTKRLRALEVNGKTVHHVGIPIHWNMKVLNGKGNRGFSTNTLTPSWGESVTQTPEYKTFLVNVEKIAEAA","1864235","From GenBank (gi|1169659): FdxG allows formate to be used as a major electron donor duringanaerobic respiration. Subunit alpha possibly forms the active site. fdxG is an ortholog of both E. coli fdnG and fdoG.","formate dehydrogenase alpha subunit","Periplasm, Cytoplasm","","
InterPro
IPR006443
Family
Formate dehydrogenase, alpha subunit, anaerobic
TIGR01553\"[1-804]Tformate-DH-alph: formate dehydrogenase, alp
InterPro
IPR006655
Family
Prokaryotic molybdopterin oxidoreductase
PS00932\"[714-741]TMOLYBDOPTERIN_PROK_3
InterPro
IPR006656
Domain
Molybdopterin oxidoreductase
PF00384\"[6-256]TMolybdopterin
InterPro
IPR006657
Domain
Molydopterin dinucleotide-binding region
PF01568\"[677-799]TMolydop_binding
noIPR
unintegrated
unintegrated
G3DSA:2.40.40.20\"[637-804]Tno description
G3DSA:3.40.228.10\"[1-267]Tno description
G3DSA:3.40.50.740\"[285-467]Tno description
PTHR11615\"[1-106]T\"[141-277]T\"[325-381]T\"[399-508]T\"[667-805]TNITRATE, FROMATE, IRON DEHYDROGENASE


","BeTs to 16 clades of COG0243COG name: Anaerobic dehydrogenases, typically selenocysteine-containingFunctional Class: CThe phylogenetic pattern of COG0243 is aompkz-q-dr-bcefgh--uj----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.9e-08) to 1/3 blocks of the IPB001467 family, which is described as \"Prokaryotic molybdopterin oxidoreductases\". Interpro entry for IP:IPR001467. IPB001467C 42-67 1.9e-08","Residues 2 to 57 match (4e-26) PD:PD405664 which is described as TRANSFERASE PROTEOME GLYCOSYLTRANSFERASE COMPLETE BIOSYNTHESIS CLUSTER 2.-.-.- LBGA HI0765 6-DEOXY-L-TALAN ","","","","","","","","","","","Wed Jan 22 10:28:35 2003","Wed Jan 22 10:28:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02676 is paralogously related to AA02699 (8e-33), AA00552 (2e-16), AA01137 (2e-12) and AA02251 (1e-07).","","","","","","Residues 677 to 799 (E-value = 7.1e-43) place AA02676 in the Molydop_binding family which is described as Molydopterin dinucleotide binding domain (PF01568)","","","","","Berg BL, Li J, Heider J, Stewart V.Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. I. Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA) encodes selenocysteine.J Biol Chem. 1991 Nov;266(33):22380-5.PMID: 1834669Jormakka M, Törnroth S, Byrne B, Iwata S.Molecular basis of proton motive force generation: structure of formate dehydrogenase-N.Science. 2002 Mar;295(5561):1863-8.PMID: 11884747","","Wed Jan 22 10:28:35 2003","1","","","" "AA02677","1864242","1865165","924","ATGAGAGCAATGGATGTACAAACACAGGATGTTATTAAGATCTCCGCAACTTCAGGGTTAACTCCGGCACCACGTGCACGTGATCACAAGGTAGAAGTGGCCAAACTGATTGACGTCACCACCTGTATCGGTTGTAAAGCCTGCCAGGTAGGCTGTTCGGAGTGGAACGATATTCGTTCCGATGTCAATGCACAATGTGTCGGTATCTATGATAACCCGGTAGATCTTAACGCAAAAGCATGGACGGTCATGCGCTTTAATGAAGTGGAAGAAAATGATCGTTTAGAATGGTTAATTCGTAAAGACGGTTGTATGCACTGCACCGAGCCGGGTTGCTTAAAAGCCTGTCCGTCGCCGGGGGCGATTATTCAGTACGCCAACGGAATTGTGGACTTCCAATCCGATAAATGTATCGGTTGCGGCTACTGCATTGCCGGCTGTCCGTTTAACATTCCACGCATGAATCCGGAAGATAACCGTGTCTATAAATGCACTCTTTGTGTAGATCGTGTTTCCGTCGGTCAAGAACCGGCTTGCGTGAAAACCTGCCCGACCGGTGCGATTCGTTTCGGTTCCAAAGAAGAAATGAAAGTGTATGCAGAGCAACGCATTGCCGATTTAAAATCCCGTGGCTACAAAAACGCCGGACTTTATGACCCTGAAGGGGTTGGTGGGACGCATGTCATGTATGTATTACACCACGCCGACAAACCGGAGTTGTATAACGGTCTGCCGAAGGATCCACACATCGACCCGACAGTCACCTTATGGAAAGACATTCTGAAACCGATCGCAGCGGTTGCCATGGGAGGCTTGGCGCTTGCTGAAATCGGTCACTACCTCGTCGTAGGTCCGAATATTGAGGAAGATGTGGAAGATCATCATGAAGAATGTGAAGATGAGCGCGGGGGCACTCAAGATGAA","","","33873","MRAMDVQTQDVIKISATSGLTPAPRARDHKVEVAKLIDVTTCIGCKACQVGCSEWNDIRSDVNAQCVGIYDNPVDLNAKAWTVMRFNEVEENDRLEWLIRKDGCMHCTEPGCLKACPSPGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDNRVYKCTLCVDRVSVGQEPACVKTCPTGAIRFGSKEEMKVYAEQRIADLKSRGYKNAGLYDPEGVGGTHVMYVLHHADKPELYNGLPKDPHIDPTVTLWKDILKPIAAVAMGGLALAEIGHYLVVGPNIEEDVEDHHEECEDERGGTQDE","1865163","","formate dehydrogenase, beta subunit","Inner membrane, Cytoplasm","","
InterPro
IPR001450
Domain
4Fe-4S ferredoxin, iron-sulfur binding
PR00353\"[130-141]T\"[178-189]T4FE4SFRDOXIN
PF00037\"[130-153]TFer4
PS00198\"[137-148]T4FE4S_FERREDOXIN
InterPro
IPR006470
Family
Formate dehydrogenase, beta subunit
TIGR01582\"[10-294]TFDH-beta: formate dehydrogenase, beta subun
InterPro
IPR015246
Domain
Formate dehydrogenase, transmembrane
PF09163\"[250-293]TForm-deh_trans
noIPR
unintegrated
unintegrated
G3DSA:1.20.5.480\"[251-298]Tno description
G3DSA:3.30.70.20\"[33-117]T\"[128-244]Tno description
PTHR11938\"[36-57]T\"[85-261]TFAD NADPH DEHYDROGENASE/OXIDOREDUCTASE
PTHR11938:SF10\"[36-57]T\"[85-261]TMOLYBDOPTERIN OXIDOREDUCTASE


","No hits to the COGs database.","Significant hit ( 5.5e-10) to 2/2 blocks of the PR00353 family, which is described as \"4Fe-4S ferredoxin signature\". Prints database entry for PR:PR00353. PR00353A 130-141 0.0073 PR00353B 178-189 2.8e-05 PR00353A 35-46 0.038","Residues 104 to 149 match (3e-14) PD:PD010600 which is described as COMPLETE PROTEOME IRON-SULFUR REDUCTASE NITRATE SUBUNIT ELECTRON BETA 4FE-4S CHAIN ","","","","","","","","","","","","Wed Jan 22 10:42:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02677 is paralogously related to AA01138 (1e-24), AA00044 (2e-24) and AA02683 (1e-07).","","","","","","Residues 130 to 153 (E-value = 1.2e-05) place AA02677 in the Fer4 family which is described as 4Fe-4S binding domain (PF00037)","","","","","","","","1","","","" "AA02678","1865161","1865583","423","ATGAATAAGAGTAAAATTGAAATCACCAATAATACCCGTATCATTCGCCATCGAGTCCCTGCGCGTCTAAGTCACTGGTTCTTGGTGATCAGTTTCTTTTTAACCACATTTACCGGGGTGGCGTTCTTCTTCCCCGATTTTGCCTGGTTAACGGAAATTCTCGGTACGCCGCAACTGGCACGTGCCATTCACCCGTTCACCGGTATTTTGATGTTTATTGCATTCGTGTTCTTATGTTCACTATATTGGCATCACAATATTCCGGAGAAAAACGATATTCGCTGGATGAAAGGCATTGTTGAAGTGTTGAAAGGTAATGAACATGCCGTTGCCGATAACGGAAAATATAACCTGGGTCAAAAAATGTTGTTTTGGACACTGATCCTTGCCATGTTTACCTTAATGGGTTCCGGTATCATCATG","","","18662","MNKSKIEITNNTRIIRHRVPARLSHWFLVISFFLTTFTGVAFFFPDFAWLTEILGTPQLARAIHPFTGILMFIAFVFLCSLYWHHNIPEKNDIRWMKGIVEVLKGNEHAVADNGKYNLGQKMLFWTLILAMFTLMGSGIIM","1865581","","formate dehydrogenase, gamma subunit","Inner membrane, Cytoplasm","","
InterPro
IPR006471
Family
Formate dehydrogenase, gamma subunit
TIGR01583\"[13-141]Tformate-DH-gamm: formate dehydrogenase, gam
noIPR
unintegrated
unintegrated
signalp\"[1-41]?signal-peptide
tmhmm\"[23-43]?\"[62-82]?\"[122-140]?transmembrane_regions


","BeTs to 6 clades of COG2864COG name: Cytochrome b subunit of formate dehydrogenaseFunctional Class: CThe phylogenetic pattern of COG2864 is a------q------efgh--u-----Number of proteins in this genome belonging to this COG is","","Residues 14 to 141 match (6e-52) PD:PD013589 which is described as SUBUNIT FORMATE COMPLETE PROTEOME CYTOCHROME GAMMA DEHYDROGENASE B556 DEHYDROGENASE HEME ","","","","","","","","","","","","Wed Jan 22 10:46:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02678 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Benoit S, Abaibou H, Mandrand-Berthelot MA.Topological analysis of the aerobic membrane-bound formate dehydrogenase of Escherichia coli.J Bacteriol. 1998 Dec;180(24):6625-34.PMID: 9852007","","Wed Jan 22 10:46:15 2003","1","","","" "AA02679","1865620","1865871","252","GTGCTACGCATTGCCATCTTGCTGCATTCTGCCTGTGCTTTTATGCTGTTTACCGGTATTTTGGTACACATGTACATGGCGTTCTGGGTAAAAGGTTCCATCACCGGTATCGTGGAAGGTTGGGTAACTGTTCGCTGGGCGAAAAAACACCATCCGAAATGGTATCGTGAAGAAGTGCTTCCTGAACTGGAAAAAGATGTTGAGCGGGAAGAGAAAGGTGAGCAGACCAAAGCAATATTCAAGAAATTTAGC","","","9873","VLRIAILLHSACAFMLFTGILVHMYMAFWVKGSITGIVEGWVTVRWAKKHHPKWYREEVLPELEKDVEREEKGEQTKAIFKKFS","1865869","","formate dehydrogenase, gamma subunit","Inner membrane, Cytoplasm, Periplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-27]?signal-peptide
tmhmm\"[5-23]?\"[29-47]?transmembrane_regions


","BeTs to 6 clades of COG2864COG name: Cytochrome b subunit of formate dehydrogenaseFunctional Class: CThe phylogenetic pattern of COG2864 is a------q------efgh--u-----Number of proteins in this genome belonging to this COG is","","Residues 1 to 57 match (2e-23) PD:PD013589 which is described as SUBUNIT FORMATE COMPLETE PROTEOME CYTOCHROME GAMMA DEHYDROGENASE B556 DEHYDROGENASE HEME ","","","","","","","","","","","","Wed Jan 22 10:47:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02679 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Benoit S, Abaibou H, Mandrand-Berthelot MA.Topological analysis of the aerobic membrane-bound formate dehydrogenase of Escherichia coli.J Bacteriol. 1998 Dec;180(24):6625-34.PMID: 9852007","","Wed Jan 22 10:47:15 2003","1","","","" "AA02681","1865889","1866011","123","GTGAAAAATAACCGCACTTTGATCTGCACCCCAAAAGTTGGACACTACGACCAACTAATTAAAGTGCAGATTTTCATGGGTAAACATTATTCAACGGGTTCAAACATCGAACCATCTACATAC","","","4665","VKNNRTLICTPKVGHYDQLIKVQIFMGKHYSTGSNIEPSTY","1866011","","hypothetical protein","Cytoplasm, Extracellular","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 16:09:00 2004","Mon Feb 23 16:09:00 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02681 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 16:09:00 2004","","","","","","","","","","","","","1","","","" "AA02682","1868726","1866444","2283","ATGGAAGGCATTGAATTACGCATCAAAGGCAAAGTGCAGGGCGTAGGATTTCGCCCCTTCGTCTGGCTATTGGCGAACCGACATAACCTGCGCGGCGATGTGAACAACGACGGACAAGGCGTATTAATCCGCCTTCTTGCGCCGACGGAACAGCAGCTTAAACACTTCCTGCACGACTTACAAACCCAACTGCCGCTCCTTGCCCTCATCACCGACATTCAACAGCATGAAAAACGCTGGGAAAATCCACCGCACTTTACAGGCTTTGAAATCCGCGAAAGCGAAAACAACGCCATGGACACCCAAATCGTGCCCGATGCTGCCACCTGCCCCGCCTGCTTGAACGACTTATTCGACCGGAACAATCGGCGCTATCACTACCCATTCACTAACTGTACCCACTGCGGTCCGCGCTTTACCATTATTAAAGCCATTCCTTACGATCGCAAAAATACTTCCATGGTGAGTTTCCCGCTGTGCGCCGATTGTGCCGCCGAATATAAAAACCCCGCCGACCGCCGTTTTCACGCCCAACCCAACGCCTGCCCCGTCTGCGGCCCGCACGTTTGGCTGGTGGACAAGCGCGGCAATCTTGCCGATGAAAAAACACCGATAAAAACCACCGCACTTTTATTACAACGAGGCAGGATCGTCGCCGTCAAAGGCATCGGCGGTTTCCACCTGGCTTGCGATGCCACCAACGCCAACGCCGTGCAATTACTGCGCGAACGCAAACGCCGCCCGACCAAACCGCTGGCGGTGATGGTGCCGGATTTGTCTTTTTTAACGGATTTAACGGAAGCGGAAACCACATTGCTGACAAGCACCGCCGCGCCTATTGTCTTGCTGGCAAAACACAAAGTGCCGTTGCTGGCGGAACAGATCGCGCCGAAACTCAACGAAATCGGCGTGATGTTGCCAAGCAACCCGCTGCAACATTTACTGTTACGGGAAGCCAACCGCCCGCTGGTGATGACCTCCGCTAACCCAAGCGCACAACCGCCGATTTTGGGTAACGAAAGTGCGGTCCAAAATTTAAGTGATTTGGCGGATTATTTTCTTTGTCATAACCGCGACATTTTGCAGCGCGCCGACGATTCCTTAGTTCGCGCCGCTTTCGACGGTACGGAAACCCTGCGTCGCGCACGCGGTTATGTACCTGACGAAACCCTGTTGGACCACCACAGTCCGCGCAATGTGCTGGCGCTCGGTTCCGATTTAAAAAACACCTTCTGTCTGTTGCGCCAAAATAAAGCCATCGTCAGCCAACACATTGGCGACACCGCCAACGAAAAAGTGCGGTCACAATTGGAAGCGAATATCGCCCTGTTTTGCCAAATCTACCAATTCAAGCCGGAACTTATCGCCATCGACGCACACCGCGGTTATTTCACCCACGAAGTAGGCAAACAACTGGCGGCGCAATACCAAATTCCTTATGTGGAAGTGTTACACCACCACGCCCACATCGTCAGCGTCATGGCGGAACACCATTGTCATGAACAAGTCATCGGGCTGGCGCTGGACGGCATCGGCATGGGCGAAAACGGGCAACTTTGGGGTGGCGAATGTCTGCTGGCAGATGAAAAAGCCTCGCGCTATTTAGGCGGCTTACCTGCCGTCGCTCTGCCCGGCGGCGATCTTGCCGCCAAACAGCCTTGGCGCAACTGGCTGGCGCATTTACAACAATTTGTGCCAAATTGGCGGGAGCTCGTCGCCGAAACCTGCGCCGATCACGACTGGCAACTTCTCGCCACCGCCATTGAACGCAAAATCAACAGCCCGTTGATTTCTTCCGCCGGACGCTTCTTCGACGCCGTGGCGTTCGGCTTAGGCATCACCCCGCCACAACTCAGCTGGGAAGGCGAAGCCGCCTGCCAATTAGAAGTGCTCGCCGAACAGTCGACACTCGCCCGTTTGCCATTAAACGAAATCGACCTTCCAATCTTAATGCCGTTGAACAATGAAAATAAATTAGATCTCGCCGTCTTCTGGCAAACCTGGCTCGCCCTCAACGCCTCCGCGGCCGACAAAGCCTTTATCTTCCATTACGCGTTGGCTGAAGGCTTCGCCATTCTCGCCTGCCAACAAGCCGAACGCCACGGTTGCAAAACCATCGTGTTATCGGGTGGCGTATGGCATAACCGATTATTACGCCGATTGGTAAGAGAAAATTTAGCAGAATTTAACGTGTTAAGCGCCCACCAATTCCCCATGGGCGATGGCGGCTTGAGTTTGGGGCAGGTAGTGATTGCCGGTCAATTCAGCGAATCAAAAACAGAA","","","84566","MEGIELRIKGKVQGVGFRPFVWLLANRHNLRGDVNNDGQGVLIRLLAPTEQQLKHFLHDLQTQLPLLALITDIQQHEKRWENPPHFTGFEIRESENNAMDTQIVPDAATCPACLNDLFDRNNRRYHYPFTNCTHCGPRFTIIKAIPYDRKNTSMVSFPLCADCAAEYKNPADRRFHAQPNACPVCGPHVWLVDKRGNLADEKTPIKTTALLLQRGRIVAVKGIGGFHLACDATNANAVQLLRERKRRPTKPLAVMVPDLSFLTDLTEAETTLLTSTAAPIVLLAKHKVPLLAEQIAPKLNEIGVMLPSNPLQHLLLREANRPLVMTSANPSAQPPILGNESAVQNLSDLADYFLCHNRDILQRADDSLVRAAFDGTETLRRARGYVPDETLLDHHSPRNVLALGSDLKNTFCLLRQNKAIVSQHIGDTANEKVRSQLEANIALFCQIYQFKPELIAIDAHRGYFTHEVGKQLAAQYQIPYVEVLHHHAHIVSVMAEHHCHEQVIGLALDGIGMGENGQLWGGECLLADEKASRYLGGLPAVALPGGDLAAKQPWRNWLAHLQQFVPNWRELVAETCADHDWQLLATAIERKINSPLISSAGRFFDAVAFGLGITPPQLSWEGEAACQLEVLAEQSTLARLPLNEIDLPILMPLNNENKLDLAVFWQTWLALNASAADKAFIFHYALAEGFAILACQQAERHGCKTIVLSGGVWHNRLLRRLVRENLAEFNVLSAHQFPMGDGGLSLGQVVIAGQFSESKTE","1866442","","hydrogenase maturation protein","Cytoplasm","","
InterPro
IPR001792
Domain
Acylphosphatase
PD001884\"[4-92]TQ8ZMJ5_SALTY_Q8ZMJ5;
PF00708\"[1-88]TAcylphosphatase
PS51160\"[3-93]TACYLPHOSPHATASE_3
PS00150\"[8-18]TACYLPHOSPHATASE_1
InterPro
IPR004421
Family
Hydrogenase maturation factor, HypF-type
PIRSF006256\"[1-761]TCarbamoyl phosphate-converting enzyme ([NiFe]-hydrogenase maturation factor)
TIGR00143\"[6-753]ThypF: [NiFe] hydrogenase maturation protein
InterPro
IPR006070
Domain
SUA5/yciO/yrdC, N-terminal
PF01300\"[209-382]TSua5_yciO_yrdC
PS51163\"[202-384]TYRDC
InterPro
IPR006071
Domain
SUA5/yciO/yrdC
PD002209\"[400-460]TQ6D7S4_BBBBB_Q6D7S4;
InterPro
IPR011125
Domain
Zinc finger, HypF
PF07503\"[109-143]T\"[159-193]Tzf-HYPF
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.100\"[4-93]Tno description
G3DSA:3.90.870.10\"[205-399]Tno description
PTHR17490\"[215-354]TSUA5


","BeTs to 9 clades of COG0068COG name: Hydrogenase maturation factorFunctional Class: OThe phylogenetic pattern of COG0068 is a-m-k--q-----ce-----u-----Number of proteins in this genome belonging to this COG is","Significant hit ( 2.2e-17) to 2/2 blocks of the IPB001792 family, which is described as \"Acylphosphatase\". Interpro entry for IP:IPR001792. IPB001792A 4-41 3.3e-16 IPB001792B 588-608 15Significant hit ( 8.2e-11) to 1/2 blocks of the IPB000666 family, which is described as \"SUA5/yciO/yrdC family\". Interpro entry for IP:IPR000666. IPB000666A 217-245 8.1e-11","Residues 159 to 245 match (5e-07) PD:PD572526 which is described as PROTEOME HYPF PLASMID COMPLETE HOMOLOG ","","","","","","","","","","","","Wed Jan 22 10:54:31 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02682 is paralogously related to AA00576 (1e-05).","","","","","","Residues 209 to 382 (E-value = 1.7e-66) place AA02682 in the Sua5_yciO_yrdC family which is described as yrdC domain (PF01300)","","","","","Paschos A, Bauer A, Zimmermann A, Zehelein E, Bock A.HypF, a carbamoyl phosphate-converting enzyme involved in [NiFe] hydrogenase maturation.J Biol Chem. 2002 Dec 20;277(51):49945-51.PMID: 12377778Maier T, Binder U, Böck A.Analysis of the hydA locus of Escherichia coli: two genes (hydN and hypF) involved in formate and hydrogen metabolism.Arch Microbiol. 1996 May;165(5):333-41.PMID: 8661925Rosano C, Zuccotti S, Bucciantini M, Stefani M, Ramponi G, Bolognesi M.Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domain.J Mol Biol. 2002 Aug;321(5):785-96.PMID: 12206761Hansel A, Axelsson R, Lindberg P, Troshina OY, Wünschiers R, Lindblad P.Cloning and characterisation of a hyp gene cluster in the filamentous cyanobacterium Nostoc sp. strain PCC 73102.FEMS Microbiol Lett. 2001 Jul;201(1):59-64.PMID: 11445168Olson JW, Maier RJ.The sequences of hypF, hypC and hypD complete the hyp gene cluster required for hydrogenase activity in Bradyrhizobium japonicum.Gene. 1997 Oct;199(1-2):93-9.PMID: 9358044","","Mon Feb 17 13:44:05 2003","1","","","" "AA02683","1869022","1869618","597","ATGAATCGTTTTGTTATCGGTGATCCGAAAGATTGCATTGGATGCAACACCTGTATGGCCGCTTGTAGCGAAGTGCACAAAGCCTTCGGATTACAATCTTATCCTCGGTTACAAGTCATGCGTAATGATGATATAACCGTTCCAATCCTTTGTCGTCACTGTGATGACTCGCCGTGTGCCACCGTTTGCCCGGTACACGCGATTACACATGAAGGCGACACCATTCAACTCAACGAAAGTTTGTGTATCGGTTGTAAACTGTGCGGTATCGCCTGTCCGTTCGGCGCGATTACCCAACACGGCAGCGCACCGATCGATGCGCCTGCATACTACGAAAGTTTCACTTTCACTGATGCGGTAAAACGTGACATTCGCACCGCGCCGGATAATTCGGAATTGCATAATATGCTAGCATGGCAACCGGGCGTGAAAGCCATTGCGGTGAAATGCGACCTGTGCTATTTCCGTGAACAAGGACCGGCGTGCGTTCAAACCTGTCCGACCAAAACCCTGTTTATCATCAGTGATGAGAGTATTCAAGAAGCTAACCGCAAAAAACGTCAAATGGCAATGATGTCTTCACCTGCTATTCCAAGA","","","21845","MNRFVIGDPKDCIGCNTCMAACSEVHKAFGLQSYPRLQVMRNDDITVPILCRHCDDSPCATVCPVHAITHEGDTIQLNESLCIGCKLCGIACPFGAITQHGSAPIDAPAYYESFTFTDAVKRDIRTAPDNSELHNMLAWQPGVKAIAVKCDLCYFREQGPACVQTCPTKTLFIISDESIQEANRKKRQMAMMSSPAIPR","1869616","","hydrogenase 4 Fe-S subunit","Periplasm, Cytoplasm","","
InterPro
IPR001450
Domain
4Fe-4S ferredoxin, iron-sulfur binding
PR00353\"[75-86]T\"[161-172]T4FE4SFRDOXIN
PF00037\"[75-98]TFer4
PS00198\"[82-93]T4FE4S_FERREDOXIN
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.20\"[44-149]Tno description
PTHR11938\"[6-95]T\"[140-192]TFAD NADPH DEHYDROGENASE/OXIDOREDUCTASE
PTHR11938:SF10\"[6-95]T\"[140-192]TMOLYBDOPTERIN OXIDOREDUCTASE


","BeTs to 6 clades of COG1142COG name: Fe-S-cluster-containing hydrogenase components 2Functional Class: CThe phylogenetic pattern of COG1142 is a-m-k---v----ce-----------Number of proteins in this genome belonging to this COG is","Significant hit ( 2.9e-06) to 2/2 blocks of the PR00353 family, which is described as \"4Fe-4S ferredoxin signature\". Prints database entry for PR:PR00353. PR00353A 5-16 1.1 PR00353B 58-69 0.0014","Residues 144 to 187 match (3e-07) PD:PD051382 which is described as PROTEOME COMPLETE SUBUNIT IRON-SULFUR OXIDOREDUCTASE FORMATE HYDROGENLYASE FHL COMPONENT 4FE-4S ","","","","","","","","","","","","Wed Jan 22 10:59:47 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02683 is paralogously related to AA00044 (1e-13), AA01138 (1e-12) and AA02677 (6e-08).","","","","","","Residues 75 to 98 (E-value = 3e-08) place AA02683 in the Fer4 family which is described as 4Fe-4S binding domain (PF00037)","","","","","Skibinski DA, Golby P, Chang YS, Sargent F, Hoffman R, Harper R, Guest JR, Attwood MM, Berks BC, Andrews SC.Regulation of the hydrogenase-4 operon of Escherichia coli by the sigma(54)-dependent transcriptional activators FhlA and HyfR.J Bacteriol. 2002 Dec;184(23):6642-53.PMID: 12426353","","Wed Jan 22 10:59:47 2003","1","","","" "AA02684","1869654","1871672","2019","ATGAGTTATTCAATCAGTTTACTCATCACGACCCTGTTGATTTATGTCGTCGGTGCGTTTATTTCGCTAATTTTGAGTCGGAATGAACAACTTTCAATCAATATATCCGGCGTGACCGGTGTACTTGGTGGAGCTTTAGGCATTGTTGCCTGCATCCCCGTTCTTATCAGCAGCGACCCTGTCGTTGATGTTTTCCAAACCCCGTTTGAATTTGCCAATTTTTCAACCCGCATTGACGGATTGGCGGCGTTTATGGTGTGTGTGATTTCTTTGTTGGTTGTGGTGAGCGCACTCTACTCTTTCTCTTATGTCAAAGAGTATAAAGGCAAAGGCGCAGGTTCGATGGGTTTCTTTATGAATTTGTTTATCGCCTCAATGGTTGCCTTGGTGACCTGCGATAATGCGTTCTACTTCCTGGTCTTTTTTGAAATGATGTCGTTGGCGTCTTATTTCCTTGTGTTGACGGAACAAGACGACAACGCGGTGAATGCCGGTTTATTGTATTTCTTCATTGCTCATGCCGGTTCCGTATTAATTATGATCGCCTTCTTCATTTTCTACTGCTATGCAGGCAGTTTTGAATTCGGCGATTTCCGTCAAACCACTCTTTCCGAACCTCTTGCGTTTACCGTGTTTATTTTGGCTCTCCTCGGTTTCGGTGCGAAAGCGGGGATGATTCCGTTACACAGCTGGTTACCGAAAGCCCACCCGGCGGCACCTTCTCATGCGTCCGCCTTAATGTCCGGCGTGATGGTGAAAATCGGTATTTTCGGGATCGTGAAAGTGGGGATCGATCTGTTAGGTGCCACCAATATGTGGTACGGCGTGATTGTGTTAGGCTTCGGTGCGGTGTCTTCGGTGCTTGGCGTACTTTACGCCCTTGCCGAACATGATATTAAAAAATTATTGGCATACCACACCGTCGAAAATATCGGCATCATCATGATGGGCGTGGGTGTTGGCATGATCGGTATCGCCACACACCATCCGGTGCTTGCCACTGTGGGCTTACTCGGCGGTTTGTATCACTTATTGAACCATGCGGTATTTAAAGGCTTATTGTTCTTAGGTGCCGGCTCCATGATGTATCGGTTACATACCAAAGACATGGATTTAATGGGCGGTTTAGGTAAATTAATGCCATATACCGCCTTTTGTTTCTTAATCGGTACCATGGCGATTTCCGCATTGCCACCGTTTAACGGTTTCGTCAGTGAATGGTTTACTTATCAATCCTTGTTCAGCTTAAGCCAAAGCGATGATTTCGTGTTAAAACTTGCCGGTCCGATTGCCATTATCATGCTTGCCTTAACCGGTGCGCTTGCCGCGCTCTGTTTCGTGAAAGTGTACGGTATCAGCTTCGGCGGCGCGCCGCGTAGCGAAAAAGCGGCGAATGCACGGGAAGTGCCGAAACCGATGGTGATTGCCATGGCGATTTTGGCGTTATGTTGCGTGTTGTTGGGCGTGGGCGCTTCCGTGGTTACTCCAATCATTGCGAAAATTTCCACCGCACTTGCCAATACCGAAACCATGACCTTGGCACACAACGGCATTGTGGTTGCGCAAGCCGAACCGAATACGGCGCTTTCTACCCCGATGGTGACCATCATGCTGTTGGCGTTCTTCTTCCTGCCGTTTACCTATTACGCTTTTACCAAAAATCAACGATTATCGGATCGTGCCAAAGGCAATCCGTGGGCTTGCGGTTATGCCTATGAAGCGGATATGGCGGCATCTGCCGGCAGCTTTACCCGTCCGTTGCGCACTATCTTCAAACCGCTTTATACCTTGCGTGAAGTGTTGGATCCTGCGCCGTTAGGCAACAAAGGCGTTCAGGCGTTAATCAAAGGCGCAACCAAAACCGAACCGTTCTGGGAAGAAAAAGTCACCATGCCGATTGCGCATTTCATCCCTTGGCTGGGGACCAAAATTCAATGGCTGCAACAAGGCGACTTCCGCGTGTATTGCGTGTATTTCGTCATTGCCTTGGCGGCGTTACTGCTTTCCATTGCGTTGATG","","","72467","MSYSISLLITTLLIYVVGAFISLILSRNEQLSINISGVTGVLGGALGIVACIPVLISSDPVVDVFQTPFEFANFSTRIDGLAAFMVCVISLLVVVSALYSFSYVKEYKGKGAGSMGFFMNLFIASMVALVTCDNAFYFLVFFEMMSLASYFLVLTEQDDNAVNAGLLYFFIAHAGSVLIMIAFFIFYCYAGSFEFGDFRQTTLSEPLAFTVFILALLGFGAKAGMIPLHSWLPKAHPAAPSHASALMSGVMVKIGIFGIVKVGIDLLGATNMWYGVIVLGFGAVSSVLGVLYALAEHDIKKLLAYHTVENIGIIMMGVGVGMIGIATHHPVLATVGLLGGLYHLLNHAVFKGLLFLGAGSMMYRLHTKDMDLMGGLGKLMPYTAFCFLIGTMAISALPPFNGFVSEWFTYQSLFSLSQSDDFVLKLAGPIAIIMLALTGALAALCFVKVYGISFGGAPRSEKAANAREVPKPMVIAMAILALCCVLLGVGASVVTPIIAKISTALANTETMTLAHNGIVVAQAEPNTALSTPMVTIMLLAFFFLPFTYYAFTKNQRLSDRAKGNPWACGYAYEADMAASAGSFTRPLRTIFKPLYTLREVLDPAPLGNKGVQALIKGATKTEPFWEEKVTMPIAHFIPWLGTKIQWLQQGDFRVYCVYFVIALAALLLSIALM","1871670","","hydrogenase 4 membrane subunit","Inner membrane, Cytoplasm","","
InterPro
IPR001750
Domain
NADH/Ubiquinone/plastoquinone (complex I)
PF00361\"[132-413]TOxidored_q1
InterPro
IPR003918
Family
NADH-ubiquinone oxidoreductase, chain 4
PR01437\"[168-192]T\"[237-261]T\"[388-414]TNUOXDRDTASE4
noIPR
unintegrated
unintegrated
PTHR22773\"[99-488]T\"[546-670]TNADH DEHYDROGENASE
PTHR22773:SF13\"[99-488]T\"[546-670]TFORMATE DEHYDROGENLYASE SUBUNIT 3 (HYDROGENASE-3, SUBUNIT C)
signalp\"[1-19]?signal-peptide
tmhmm\"[5-27]?\"[33-55]?\"[81-101]?\"[111-131]?\"[136-154]?\"[164-186]?\"[207-227]?\"[273-295]?\"[310-328]?\"[338-358]?\"[379-399]?\"[430-452]?\"[473-493]?\"[532-552]?\"[654-672]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 8.4e-21) to 4/7 blocks of the IPB000260 family, which is described as \"NADH-ubiquinone oxidoreductase chain 4, amino terminus\". Interpro entry for IP:IPR000260. IPB000260A 9-42 70 IPB000260D 215-261 1.1e-09 IPB000260E 276-329 0.87 IPB000260F 356-405 3.6e-06Significant hit ( 7.6e-12) to 4/5 blocks of the PR01437 family, which is described as \"NADH-ubiquinone oxidoreductase subunit 4 signature\". Prints database entry for PR:PR01437. PR01437B 168-192 0.79 PR01437C 237-261 0.061 PR01437D 336-355 28 PR01437E 388-414 0.00059Significant hit ( 7.7e-12) to 5/10 blocks of the IPB002128 family, which is described as \"NADH-Ubiquinone oxidoreductase (complex I), chain 5 from chloroplast\". Interpro entry for IP:IPR002128. IPB002128B 66-120 1.4e+02 IPB002128C 149-203 7.9 IPB002128D 216-270 0.02 IPB002128E 314-368 0.015 IPB002128F 379-433 1.7Significant hit ( 3.6e-10) to 2/2 blocks of the IPB001750 family, which is described as \"NADH-Ubiquinone/plastoquinone (complex I), various chains\". Interpro entry for IP:IPR001750. IPB001750A 222-233 0.00016 IPB001750B 296-314 0.00078Significant hit ( 1.9e-07) to 4/7 blocks of the PR01434 family, which is described as \"NADH-ubiquinone oxidoreductase chain 5 signature\". Prints database entry for PR:PR01434. PR01434A 79-104 3.2 PR01434B 109-129 25 PR01434D 218-239 0.011 PR01434F 310-322 53","Residues 608 to 660 match (5e-07) PD:PD445840 which is described as PROTEOME COMPLETE MEMBRANE B HYDROGENASE HYDROGENASE-4 SUBUNIT TRANSMEMBRANE COMPONENT INNER ","","","","","","","","","","","","Wed Jan 22 11:10:50 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02684 is paralogously related to AA02689 (6e-45) and AA02687 (5e-36).","","","","","","Residues 132 to 434 (E-value = 1.4e-57) place AA02684 in the Oxidored_q1 family which is described as NADH-Ubiquinone/plastoquinone (complex I), various chains (PF00361)","","","","","","","","1","","","" "AA02686","1871686","1872645","960","ATGATTACTTTACCTTCAGAAATTGCAACATCCGCCGGAATGTTTGTATTAGCCATCGTGCAAGCCTTGATTTTGCTTGCCCTTGCCCCGTTATTCTCCGGTATTTCACGTATGATCCGCGCACGGATTCAATCCCGTCGCGGTCCGGGCGTGTTACAGGATTATCGCGACATTGCGAAATTAATGAAACGGCAAAATATTTGGCCGGATAATGCCGGTGCGGTGTCCCGTATCATGCCTTATGTGCTGATCAGCACCGTAATGGTGGTGGCGATGAGTTTGCCGTTGTTTACCCGCGTTTCACCTTTCGGGGCGGGCAGCGATTTAATCACCGTGATTTATTTATTCGCGTTGTTCCGTTTCTTCTTCTCCATCGCCGGGTTGGATTCCAACAGCACCTTCTCAAGTTTGGGCGCAAGCCGTGAAGTGACTTTAGGCGTGTTGGTTGAGCCGATTTTAATGTTGGCGTTTTTGGTCATCGCGTTAATCGCCGGTTCCACCAATTTTGCCGTGATCGGCACACAACTGGCGGATCAAAGCTGGCAATACCCGATAGCCACCGTGGTTGCCTTGGTTGCCGCGTTCTTCGCCGTGTTTATTGAAATGGGTAAAATCCCGTTCGACTTGGCGGAAGCGGAACAAGAATTACAAGAAGGTCCGTTGACCGAATATTCCGGTCCATCCCTTGCCTTATTGAAAATCGGCTTGAGCTTAAAATCCATGGTGGTTGCCGCCATCTTTGTGAGCGTGTTATTGCCATTCGGCGCGGCTCAGGATTTCAGTATAAGTGCGGTCGTTTTCGGCGCCGTTTTCTTCTTCGTGAAATTGTTGGTGGTGTTCGTGTTAGCTTGTGTGTTTGAAAACACGCTTTCCCGTACCCGCTTCATGTTAACAGGACGTTTAACCGTTGTCGGCTTCGGCATTTCTGTGTTGGCGTTTGTGTTTTACTTCACAGGATTG","","","34759","MITLPSEIATSAGMFVLAIVQALILLALAPLFSGISRMIRARIQSRRGPGVLQDYRDIAKLMKRQNIWPDNAGAVSRIMPYVLISTVMVVAMSLPLFTRVSPFGAGSDLITVIYLFALFRFFFSIAGLDSNSTFSSLGASREVTLGVLVEPILMLAFLVIALIAGSTNFAVIGTQLADQSWQYPIATVVALVAAFFAVFIEMGKIPFDLAEAEQELQEGPLTEYSGPSLALLKIGLSLKSMVVAAIFVSVLLPFGAAQDFSISAVVFGAVFFFVKLLVVFVLACVFENTLSRTRFMLTGRLTVVGFGISVLAFVFYFTGL","1872643","","hydrogenase 4 component C","Inner membrane, Cytoplasm","","
InterPro
IPR001694
Family
Respiratory-chain NADH dehydrogenase, subunit 1
PTHR11432\"[44-320]TNADH DEHYDROGENASE SUBUNIT 1
PF00146\"[14-312]TNADHdh
PS00667\"[50-65]?COMPLEX1_ND1_1
PS00668\"[206-219]TCOMPLEX1_ND1_2
noIPR
unintegrated
unintegrated
signalp\"[1-34]?signal-peptide
tmhmm\"[10-32]?\"[78-98]?\"[108-128]?\"[143-163]?\"[182-200]?\"[236-256]?\"[262-282]?\"[297-317]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 3.3e-50) to 4/4 blocks of the IPB001694 family, which is described as \"Respiratory-chain NADH dehydrogenase subunit 1\". Interpro entry for IP:IPR001694. IPB001694A 28-81 1.8e-12 IPB001694B 107-161 8.9e-15 IPB001694C 182-236 1.8e-19 IPB001694D 283-311 34","Residues 32 to 100 match (5e-16) PD:PD411630 which is described as SUBUNIT PROTEOME COMPLETE FORMATE MEMBRANE HYDROGENASE HYDROGENLYASE LYASE FHL INNER ","","","","","","","","","","","","Wed Jan 22 11:17:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02686 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 14 to 320 (E-value = 1.5e-34) place AA02686 in the NADHdh family which is described as NADH dehydrogenase (PF00146)","","","","","Andrews SC, Berks BC, McClay J, Ambler A, Quail MA, Golby P, Guest JR.A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system.Microbiology. 1997 Nov;143 ( Pt 11):3633-47.PMID: 9387241","","Wed Jan 22 11:18:42 2003","1","","","" "AA02687","1872661","1874103","1443","ATGGAACGTTTAGCTCTGATTACAATCATTTTGCCGTTTGTGGGCATCTTTATTGTAGGCTTAAATAAAACGCATTTTGCCAAATTAGCCACAATTTTCTCCGCCTTAACCACTGCCTGTATCAGCGCCTTGGCGGGGCAGTGGTATTTAAGCGGTCATCAAAGCGTGACTTACGAGTTGGTGGCATTTGATCAAACCGTGATCTTCGGTGTGACGCTGGATGCGGTCAGTACCTTAATAGGCTTTGCCGTAGTTAGCCTCGGTTTCTTGATTTGCTTATATTCCTGCGGCTATTTAACCGATAAAAACCGCGAACATCCGCACAACGGCTTACCGCGTTTTTACGCCTTCCTGCTCATCTTTATCGGCGCCATGGCGGGCTTGGTGTTATCCTCCACCTTGGCGGGACAATTATTGTTCTTTGAAATCACCGGTGGCTGTTCTTGGGCGTTAATTAGCTATTATCAAAGCCCGAAAGCCATGGCGGCGGCAATGAAAGCCTTGATTATCACCCATGTGGGTGCTATCGGCTTATACATTGCGGCGGCCTATTTATTTAGCAAATCCGGTACCTTCTCCATTACGGCGTTGGAACAGTTGGATCCGAGTGCGAAAACCATCGTGTTATTCGGTGTGATGTTCGCCGCTTGGGGTAAATCTGCGCAACTGCCGATGCAAATTTGGTTGCCGAACGCCATGGAAGCACCGACACCGGTGAGTGCCTATTTGCACGCAGCGTCTATGGTGAAAGTGGGTGTGTATATTTTCGCCCGTGCAGTCATGTCTGCCGGTGAAATTCCGTCTATTGTGGGCGAAGTGGGCATCATCATGGCGATGATTACCTTAATTTACGGCTTCCCGATGTACTTGCCGCAAACGGATTTAAAACGCTTGCTGGCGTATTCCACCATCACCCAGCTGTCTTACATTTTTATCGGTATTTCTCTTGCCGCGCTAGGTTCTAAATTAGCCTTCGTCGCCGCCATTGCCTATATCTTCAACCATGCCTTTGCAAAAAGCTTGTTCTTCTTGGTTGCCGGTTCCTTAAGTTATGCCACCGGAACCCGTTCAATGCCGTTATTACAAGGGATCATGCGTACCATGCCGGTAGTCGGTGCGGGATTTGGCGTTGCCGCCTTAGCAATTGCCGGGGTGCCGCCGTTTAACGGATTTTTCAGTAAATTCCCGTTATTTGCCGCCGGGTTTGAGTTAGGTAATGAATATAGCTGGATCACGACATTGATGGTTATCGCTTTGATCGAATCCACCGCAACCTTCGTTTGGTTGTTGTATAAATTCGGACAATGCGTTATCGGACAACCGTCAGAAGCCGTTGCCAAAGCACAACCGATTACGCTTTCTATGAGCGTCGTGTTGGCGATGCTGATGGTAATGTCTGTTTGTTCTGGTTTTATCGCCGCCTATTGGCTGGGTTTGGCAGGT","","","51420","MERLALITIILPFVGIFIVGLNKTHFAKLATIFSALTTACISALAGQWYLSGHQSVTYELVAFDQTVIFGVTLDAVSTLIGFAVVSLGFLICLYSCGYLTDKNREHPHNGLPRFYAFLLIFIGAMAGLVLSSTLAGQLLFFEITGGCSWALISYYQSPKAMAAAMKALIITHVGAIGLYIAAAYLFSKSGTFSITALEQLDPSAKTIVLFGVMFAAWGKSAQLPMQIWLPNAMEAPTPVSAYLHAASMVKVGVYIFARAVMSAGEIPSIVGEVGIIMAMITLIYGFPMYLPQTDLKRLLAYSTITQLSYIFIGISLAALGSKLAFVAAIAYIFNHAFAKSLFFLVAGSLSYATGTRSMPLLQGIMRTMPVVGAGFGVAALAIAGVPPFNGFFSKFPLFAAGFELGNEYSWITTLMVIALIESTATFVWLLYKFGQCVIGQPSEAVAKAQPITLSMSVVLAMLMVMSVCSGFIAAYWLGLAG","1874101","","hydrogenase-4 component D","Inner membrane, Cytoplasm","","
InterPro
IPR001750
Domain
NADH/Ubiquinone/plastoquinone (complex I)
PF00361\"[131-401]TOxidored_q1
InterPro
IPR003916
Family
NADH-ubiquinone oxidoreductase, chain 5
PR01434\"[74-99]T\"[108-128]T\"[154-175]T\"[215-236]T\"[237-263]T\"[306-318]TNADHDHGNASE5
noIPR
unintegrated
unintegrated
PTHR22773\"[58-478]TNADH DEHYDROGENASE
PTHR22773:SF39\"[58-478]TNADH DEHYDROGENASE SUBUNIT 5
signalp\"[1-21]?signal-peptide
tmhmm\"[4-22]?\"[32-52]?\"[71-93]?\"[114-132]?\"[138-158]?\"[167-187]?\"[266-286]?\"[298-318]?\"[324-346]?\"[367-389]?\"[408-430]?\"[457-477]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 8.9e-39) to 6/7 blocks of the PR01434 family, which is described as \"NADH-ubiquinone oxidoreductase chain 5 signature\". Prints database entry for PR:PR01434. PR01434A 74-99 0.055 PR01434B 108-128 0.00023 PR01434C 154-175 0.00051 PR01434D 215-236 2.1e-12 PR01434E 237-263 1e-07 PR01434F 306-318 8.1Significant hit ( 9.8e-24) to 4/10 blocks of the IPB002128 family, which is described as \"NADH-Ubiquinone oxidoreductase (complex I), chain 5 from chloroplast\". Interpro entry for IP:IPR002128. IPB002128C 148-202 0.82 IPB002128D 213-267 1.3e-16 IPB002128E 296-350 0.086 IPB002128F 367-421 21Significant hit ( 8.7e-14) to 2/2 blocks of the IPB001750 family, which is described as \"NADH-Ubiquinone/plastoquinone (complex I), various chains\". Interpro entry for IP:IPR001750. IPB001750A 219-230 0.018 IPB001750B 292-310 1.4e-09Significant hit ( 1.5e-12) to 3/7 blocks of the IPB000260 family, which is described as \"NADH-ubiquinone oxidoreductase chain 4, amino terminus\". Interpro entry for IP:IPR000260. IPB000260D 212-258 0.11 IPB000260E 272-325 0.025 IPB000260F 344-393 7.1e-05Significant hit ( 7.2e-07) to 4/5 blocks of the PR01437 family, which is described as \"NADH-ubiquinone oxidoreductase subunit 4 signature\". Prints database entry for PR:PR01437. PR01437B 167-191 24 PR01437C 234-258 50 PR01437D 324-343 1.7 PR01437E 376-402 0.097","Residues 212 to 258 match (3e-07) PD:PD239665 which is described as OXIDOREDUCTASE NAD PROTEOME COMPLETE NADH SUBUNIT DEHYDROGENASE TRANSMEMBRANE UBIQUINONE MITOCHONDRION ","","","","","","","","","","","","Wed Jan 22 11:24:24 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02687 is paralogously related to AA02684 (3e-36) and AA02689 (6e-33).","","","","","","Residues 131 to 418 (E-value = 5.8e-50) place AA02687 in the Oxidored_q1 family which is described as NADH-Ubiquinone/plastoquinone (complex I), various chains (PF00361)","","","","","Andrews SC, Berks BC, McClay J, Ambler A, Quail MA, Golby P, Guest JR.A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system.Microbiology. 1997 Nov;143 ( Pt 11):3633-47.PMID: 9387241","","Wed Jan 22 11:24:24 2003","1","","","" "AA02688","1874117","1874752","636","ATGTTAATGATAAATGCCCTTGCAAGTTTACTCATTATTACCTCCCTCTGCGTAATTATGGTACGAACCGCCAAAAAATCGGCATTGTTTTATAGCTTGCAATCTTTCGTATTAGTGTTGTTGTTTGTGTATCTTGCCTATGAAATGCAGGCGCACGAACTTTATATGTGGTCAATCAGCGCGTTTATCACCAAAGTGATTTTGGTGCCGGCGATTTTGATTTACGCCATGCGGAATATTGACGAAAGTCAAACGCCCGGCGGAATGAATATCGCTTGGTTGATCCCGATCACAGCAGTGATTGTTTCATTGTGCTACTTTGTTGTCATCCCGATCGATTTACCGTTGGTAGAACATCTCAAACCGGCGCTTTCCGTGTCCTTAAGTCACTTCTTGCTCGGTTTGGTTTGTATCGTCAGCCAACGTAATATCGTAAAACAAGTGTTCGGTTATTGTTTGATGGAAAACGGTTCTCATCTCACCTTAGCCTTATTAGCGAATAAAGCACCAGAATTAGTGGAAATCGGAATTGCCACCGATGCGATATTTGCGGTCATCATAATGGTGGTGCTGGTCAATAAAATTTACCGCACGTTCCATTCATTAGATGCAAAACAACTTATGAGTTTGAAGGGG","","","23502","MLMINALASLLIITSLCVIMVRTAKKSALFYSLQSFVLVLLFVYLAYEMQAHELYMWSISAFITKVILVPAILIYAMRNIDESQTPGGMNIAWLIPITAVIVSLCYFVVIPIDLPLVEHLKPALSVSLSHFLLGLVCIVSQRNIVKQVFGYCLMENGSHLTLALLANKAPELVEIGIATDAIFAVIIMVVLVNKIYRTFHSLDAKQLMSLKG","1874750","","hydrogenase 4 component E","Inner membrane, Cytoplasm","","
InterPro
IPR001133
Family
NADH-ubiquinone oxidoreductase, chain 4L
PF00420\"[122-212]TOxidored_q2
noIPR
unintegrated
unintegrated
signalp\"[1-17]?signal-peptide
tmhmm\"[2-22]?\"[28-46]?\"[56-76]?\"[90-110]?\"[125-145]?\"[172-192]?transmembrane_regions


","BeTs to 3 clades of COG0713COG name: NADH:ubiquinone oxidoreductase subunit 11 or 4L (chain K)Functional Class: CThe phylogenetic pattern of COG0713 is -o-p-z-q-dr--cef--snujx---Number of proteins in this genome belonging to this COG is","","Residues 2 to 211 match (4e-40) PD:PD037531 which is described as COMPLETE PROTEOME TRANSMEMBRANE INNER E HYDROGENASE-4 COMPONENT MEMBRANE 1.-.-.- RV0085 ","","","","","","","","","","","","Wed Jan 22 11:29:14 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02688 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 122 to 212 (E-value = 8e-07) place AA02688 in the Oxidored_q2 family which is described as NADH-ubiquinone/plastoquinone oxidoreductase chain 4L (PF00420)","","","","","Andrews SC, Berks BC, McClay J, Ambler A, Quail MA, Golby P, Guest JR.A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system.Microbiology. 1997 Nov;143 ( Pt 11):3633-47.PMID: 9387241","","Wed Jan 22 11:29:14 2003","1","","","" "AA02689","1874760","1876295","1536","ATGTATGAACAATGGATAATCGCGTTATTGACCGCACCTTTAGCCGTGGCTTTGGCATGCTTTGCCTGTCGCTCGACAAAAAATCGGACAATTTGCACAGCACTTCATGTAACAGGCTTAATCTTGATGGTGGGATTCGCCTTACAAATTATTAACGGTGTACTTACTCAAGGTGACATCAGTGCATTAAATAATTGGGTCTATATCGACAGTCTTTCCGCCATTTTCTTAGGATTAATTGCGGTTGTCGGTACCTTAGCCGGTATTTATTCCATCGGTTATATCGGCACCGAATTACAAGAGGGACATCTGAGCCTTAAGGATTTCTGCAATTATCACGGATTTTTGCACTTATTCTTTTTCACTATGATTATTTCCGTGATTACCAATAATGTGATTCTTATGTGGGTCGCCATTGAAGCGACAACCTTGAGTTCCGCATTTTTGGTGGGAACCTATAAACAAAAAACCTCTCTTGAAGCGGCATGGAAATACATCATCACTTGTTCCGTAGGGGTGGCGTTCGGCTTATACGGCACGATCTTAACCTTTGCGAACGGAAATAATCTGTTGGCGGATCCAAGCCAAGCGATTTTCTGGTCTGCGTTGAATCAACAAGCTGCCGGGTTAAATCCGATGCTCATGTATATCGCTTTTGCGTTCATTCTCATCGGTTTCGGCACAAAGTGCGGTCTGTTTCCGATGCATACTTGGTTATCCGACGCGCACAGTGAAGCCCCAAGCCCGGTAAGTGCGATTTTATCCGCCGTGTTATTGAATTGTGCCATGTTGGTGGTGTTGCGTTACTACATTTTGGTTTCAAAAGCCGTCGGTTCCTCCTATCCGCAAACCTTGTTGTTGGTATTCGGATTACTTTCCGTTTTGGTTGCCGCGTTATTTATCATCGTGCAATTCGACATCAAACGGTTACTGGCGTACTCCAGTATCGAAAACATGGGGCTAATCAGCTTTGCTTTCGGTTTGGGTGGACCTATCGGCGTGTTTGCGGGACTGCTGCACACCATTAACCACAGCTTGGCAAAAACCTTGTTATTCTGTGCTTCCGGTAACATTTTATTGAAATACAAAACCCGTGATATGAACCAAGTCCGCGGCTTATGGCGGGTCGCACCGGTAAGTGCGGTGCTTTTTGCCGGCGGTGCATTGGCATTGGGCGGATTACCGCCGTTTAACGTATTCGTCAGTGAATTTAGTATTGCGGTTGCAGGTATTTATGCGGGAAAAACCTGGTTGGTTATTTTCTGCTTAATCTTGCTCACCATTGTGTTGGCAGGATTAGCGTTAATGATTCTGAAAACCGTTTTAGGAAAACAACCGGATAATATTGAAACGGGAGACGTTAATAAAATCTCATTAGTAGCAATGGCGGTTCTCTTGTTATTAATGTTTGTAATGGGCATTCATATTGCCGAACCCATCTTGCAGTTATTAAAAAGTGCGGTCGGAATCGTACTCGGATCCGAACAAGTATCCTTTGGCGATATGTTAGTTTTACCTTGGCAAAGTTTAGCGAAA","","","55028","MYEQWIIALLTAPLAVALACFACRSTKNRTICTALHVTGLILMVGFALQIINGVLTQGDISALNNWVYIDSLSAIFLGLIAVVGTLAGIYSIGYIGTELQEGHLSLKDFCNYHGFLHLFFFTMIISVITNNVILMWVAIEATTLSSAFLVGTYKQKTSLEAAWKYIITCSVGVAFGLYGTILTFANGNNLLADPSQAIFWSALNQQAAGLNPMLMYIAFAFILIGFGTKCGLFPMHTWLSDAHSEAPSPVSAILSAVLLNCAMLVVLRYYILVSKAVGSSYPQTLLLVFGLLSVLVAALFIIVQFDIKRLLAYSSIENMGLISFAFGLGGPIGVFAGLLHTINHSLAKTLLFCASGNILLKYKTRDMNQVRGLWRVAPVSAVLFAGGALALGGLPPFNVFVSEFSIAVAGIYAGKTWLVIFCLILLTIVLAGLALMILKTVLGKQPDNIETGDVNKISLVAMAVLLLLMFVMGIHIAEPILQLLKSAVGIVLGSEQVSFGDMLVLPWQSLAK","1876293","","hydrogenase-4 component F","Inner membrane, Cytoplasm","","
InterPro
IPR001750
Domain
NADH/Ubiquinone/plastoquinone (complex I)
PF00361\"[129-410]TOxidored_q1
InterPro
IPR002345
Domain
Lipocalin
PS00213\"[366-377]?LIPOCALIN
InterPro
IPR003916
Family
NADH-ubiquinone oxidoreductase, chain 5
PR01434\"[70-95]T\"[225-246]T\"[318-330]TNADHDHGNASE5
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[54-192]Tno description
noIPR
unintegrated
unintegrated
PTHR22773\"[89-491]TNADH DEHYDROGENASE
PTHR22773:SF40\"[89-491]TNADH DEHYDROGENASE SUBUNIT 4
signalp\"[1-17]?signal-peptide
tmhmm\"[4-22]?\"[31-51]?\"[74-94]?\"[109-129]?\"[135-155]?\"[165-185]?\"[214-234]?\"[249-271]?\"[285-305]?\"[320-338]?\"[344-364]?\"[379-399]?\"[418-438]?\"[459-477]?transmembrane_regions


","BeTs to 10 clades of COG0651COG name: Formate hydrogenlyase subunit 3/Multisubunit Na+/H+ antiporter, MnhD subunitFunctional Class: C,PThe phylogenetic pattern of COG0651 is aompkz--vdr-bcefg-----x---Number of proteins in this genome belonging to this COG is","Significant hit ( 4.4e-17) to 3/7 blocks of the IPB000260 family, which is described as \"NADH-ubiquinone oxidoreductase chain 4, amino terminus\". Interpro entry for IP:IPR000260. IPB000260D 222-268 8.7e-07 IPB000260E 284-337 6.5e-05 IPB000260F 353-402 0.062Significant hit ( 1e-12) to 2/2 blocks of the IPB001750 family, which is described as \"NADH-Ubiquinone/plastoquinone (complex I), various chains\". Interpro entry for IP:IPR001750. IPB001750A 229-240 0.0029 IPB001750B 304-322 1e-07Significant hit ( 1.5e-10) to 4/10 blocks of the IPB002128 family, which is described as \"NADH-Ubiquinone oxidoreductase (complex I), chain 5 from chloroplast\". Interpro entry for IP:IPR002128. IPB002128B 53-107 0.16 IPB002128D 223-277 0.3 IPB002128E 311-365 0.96 IPB002128F 376-430 0.34Significant hit ( 9e-10) to 4/7 blocks of the PR01434 family, which is described as \"NADH-ubiquinone oxidoreductase chain 5 signature\". Prints database entry for PR:PR01434. PR01434A 70-95 0.00055 PR01434D 225-246 0.32 PR01434E 248-274 27 PR01434F 318-330 29Significant hit ( 2.6e-09) to 4/5 blocks of the PR01437 family, which is described as \"NADH-ubiquinone oxidoreductase subunit 4 signature\". Prints database entry for PR:PR01437. PR01437B 118-142 10 PR01437C 244-268 0.014 PR01437D 333-352 2.9 PR01437E 385-411 1","Residues 68 to 184 match (9e-11) PD:PD459137 which is described as PROTEOME COMPLETE HYDROGENLYASE RELATED SUBUNIT NADH-UBIQUINONE/PLASTOQUINONE FORMATE LYASE ","","","","","","","","","","","","Wed Jan 22 11:32:53 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02689 is paralogously related to AA02684 (4e-45) and AA02687 (6e-33).","","","","","","Residues 129 to 425 (E-value = 4.4e-54) place AA02689 in the Oxidored_q1 family which is described as NADH-Ubiquinone/plastoquinone (complex I), various chains (PF00361)","","","","","Skibinski DA, Golby P, Chang YS, Sargent F, Hoffman R, Harper R, Guest JR, Attwood MM, Berks BC, Andrews SC.Regulation of the hydrogenase-4 operon of Escherichia coli by the sigma(54)-dependent transcriptional activators FhlA and HyfR.J Bacteriol. 2002 Dec;184(23):6642-53.PMID: 12426353Johansson BW.[Model for evaluation of antiarrhythmic drugs in ambulatory patients].Lakartidningen. 1975 Nov;72(46):4517-8.PMID: 1195912Bagramyan K, Vassilian A, Mnatsakanyan N, Trchounian A.Participation of hyf-encoded hydrogenase 4 in molecular hydrogen release coupled with proton-potassium exchange in Escherichia coli.Membr Cell Biol. 2001;14(6):749-63.PMID: 11817571Andrews SC, Berks BC, McClay J, Ambler A, Quail MA, Golby P, Guest JR.A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system.Microbiology. 1997 Nov;143 ( Pt 11):3633-47.PMID: 9387241","","Wed Jan 22 11:32:53 2003","1","","","" "AA02691","1876277","1876375","99","TTGGCAAAGTTTAGCGAAATGATCGACAAGAGGGGGAAAAATGGAATTAACGAAAAATACATCCGTCGATCCGGGCAAAATGCTTGGCAAAAATTATAT","","","3926","LAKFSEMIDKRGKNGINEKYIRRSGQNAWQKLY","1876375","","hypothetical protein","Cytoplasm, Extracellular","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 16:06:39 2004","Mon Feb 23 16:06:39 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02691 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 16:06:39 2004","","","","","","","","","","","","","1","","","" "AA02692","1876464","1878044","1581","ATGCTGCCTGATGTGGTGGAGTACCTTTACTATCAACATGAAGGTTGGTTGCCGTTGGTGTTTGGTAATGACGAACGGACGATTCACGGCAATTATGCGGTGTACTATGTGCTTTCCATGGAAGGGGAAGTGAAAACCTTCATCACCATTAAAGCCTTGGTGGATCCCGTTACCTTAGAATTTCCTTCCGTCACGCCGAAAGTGAAAGCGGCGGTGTGGGGCGAACGTGAATTGTTCGATATGTACGGTTTGAAAGCTGTCGGGTTGCCCGATCAACGCCGTTTGGTGTTGCCGGACGACTGGCCGGACGATCTTTACCCATTACGTAAAGACTCTATGGACTATCGCTTGCGCCCCGATCCGACAACAGCGACGGAAACTTACGAATTTATCAATGAAAAAGGCGAGGCGCGTATCGTGCCGATCGGTCCGTTACATATTACGTCCGATGAACCGGGACATTTCCGTTTATTCGTGGACGGCGAAGACATTATTGACGCCGATTACCGTTTGTTCTATGTACATCGCGGCATGGAAAAACTGGCGGAAACCCGCATGGATTACGACCAAGTGAATTTCCTCGCCGACCGTGTGTGCGGTATTTGTGGGTTTACCCACAGCGTCGCCTACGCCAATTCCGTAGAAAGCGCGCTAGGCATTCAAATTCCAAAACGGGCGCAGTGGATCCGCGCGATTTTGCTTGAAGTGGAACGCTTGCACAGCCATTTGTTGAATTTAGGGCTTTCCAGCCACTTTACCGGTTTTGATACGGGCTTTATGCAGTTCTTCCGTGTACGGGAAAAATCCATGACCTTGGCGGAAGTGTTGACCGGCGCTCGTAAAACTTACGGTATCAACCTCATCGGCGGGGTGCGTCGCGATATGCTGAAACACCAACGTGAGCAATGTATCAAGCTGATTGCGGAAATGCGTGCGGAAATTAAAACCTTGTCGGAAATTCTGCTTTCCACGCCGAACATGGAACAACGCACCGTAGGCGTGGGCATTTTGGCAAAAGACATTGCCCGTGATTTCAGCCCGGTGGGACCGATGATTCGCGGTTCCGGTTTTGCCCGCGATGTGCGCAAAGTGCATCCGTTCTCCGGCTACAGCGATGTGCCTTTTGAATTGTTCACCGAACAGAACGGCGACGTGTTATCCCGTGTGAAAGTGCGGATCAACGAAGTGTTTAAATCCATGAATATCATCGATTACATGGTGGATAACTTGCCGAGTGGCGAAATCCTGAAAGAAGGCTTCAATTACACGCCGGGCCGTTTCGCTTTGGGCATTACCGAAGCGCCGCGCGGTGAAGATATTCACTGGTCAATGCTGGGCGACAACCAAAAATTGTTCCGTTGGCGTTGTCGTGCGGCAACCTATGCCAACTGGCCGACATTGCGTTATATGTTGCGTGGTAATACGGTTTCCGACGCGCCGTTGATTATTGGTAGCCTCGACCCTTGCTATTCCTGTACCGACCGCGTCACCGTGGTTGATGTGCGTAAGCGCAAAGCGAAAACCGTGGATTACAAAGAAATCGAACGCTACGGCATCGAACGTAAAAACTCACCATTGAAA","","","65777","MLPDVVEYLYYQHEGWLPLVFGNDERTIHGNYAVYYVLSMEGEVKTFITIKALVDPVTLEFPSVTPKVKAAVWGERELFDMYGLKAVGLPDQRRLVLPDDWPDDLYPLRKDSMDYRLRPDPTTATETYEFINEKGEARIVPIGPLHITSDEPGHFRLFVDGEDIIDADYRLFYVHRGMEKLAETRMDYDQVNFLADRVCGICGFTHSVAYANSVESALGIQIPKRAQWIRAILLEVERLHSHLLNLGLSSHFTGFDTGFMQFFRVREKSMTLAEVLTGARKTYGINLIGGVRRDMLKHQREQCIKLIAEMRAEIKTLSEILLSTPNMEQRTVGVGILAKDIARDFSPVGPMIRGSGFARDVRKVHPFSGYSDVPFELFTEQNGDVLSRVKVRINEVFKSMNIIDYMVDNLPSGEILKEGFNYTPGRFALGITEAPRGEDIHWSMLGDNQKLFRWRCRAATYANWPTLRYMLRGNTVSDAPLIIGSLDPCYSCTDRVTVVDVRKRKAKTVDYKEIERYGIERKNSPLK","1878042","","hydrogenase 4 subunit; hydrogenase 3 subunit","Cytoplasm, Periplasm","","
InterPro
IPR001135
Domain
NADH-ubiquinone oxidoreductase, chain 49kDa
PF00346\"[263-426]TComplex1_49kDa
InterPro
IPR001268
Domain
NADH dehydrogenase (ubiquinone), 30 kDa subunit
PD001581\"[70-92]TQ821A8_SHIFL_Q821A8;
PF00329\"[50-118]TComplex1_30kDa
InterPro
IPR001501
Domain
Nickel-dependent hydrogenase, large subunit
PF00374\"[197-244]TNiFeSe_Hases
InterPro
IPR014029
Domain
NADH-ubiquinone oxidoreductase, chain 49kDa, conserved region
PS00535\"[174-185]TCOMPLEX1_49K
InterPro
IPR014364
Family
[NiFe]-hydrogenase-3-type complex, fused large subunit/NADH:quinone oxidoreductase, subunit NuoCD
PIRSF000231\"[2-495]T[NiFe]-hydrogenase-3-type complex, fused large subunit/NADH:quinone oxidoreductase (complex I), subunit NuoCD
InterPro
IPR014656
Family
[NiFe]-hydrogenase-3-type complex, fused large subunit
PIRSF500032\"[1-526]T[NiFe]-hydrogenase-3-type complex, fused large subunit
noIPR
unintegrated
unintegrated
G3DSA:1.10.645.10\"[156-493]Tno description
PTHR11993\"[26-495]TNADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT


","BeTs to 5 clades of COG3261COG name: Ni,Fe-hydrogenase III large subunitFunctional Class: CThe phylogenetic pattern of COG3261 is --mpk-----r---e-----------Number of proteins in this genome belonging to this COG is","Significant hit ( 1.8e-98) to 6/6 blocks of the IPB001135 family, which is described as \"NADH-ubiquinone oxidoreductase 49Kd chain\". Interpro entry for IP:IPR001135. IPB001135A 141-162 1.1e-07 IPB001135B 164-216 6.3e-16 IPB001135C 222-272 6.5e-26 IPB001135D 333-385 1.8e-20 IPB001135E 418-465 2e-13 IPB001135F 477-495 2.2e-08 IPB001135D 317-369 0.92Significant hit ( 2.4e-20) to 1/1 blocks of the IPB001268 family, which is described as \"Respiratory-chain NADH dehydrogenase 30 Kd subunit\". Interpro entry for IP:IPR001268. IPB001268 61-111 2.3e-20Significant hit ( 1.8e-14) to 3/5 blocks of the IPB001501 family, which is described as \"Nickel-dependent hydrogenases large subunit\". Interpro entry for IP:IPR001501. IPB001501B 174-218 0.0019 IPB001501D 428-466 1.3e-05 IPB001501E 481-496 0.08","Residues 153 to 233 match (1e-07) PD:PD000353 which is described as HYDROGENASE SUBUNIT LARGE OXIDOREDUCTASE COMPLETE PROTEOME NICKEL ALPHA NIFE UPTAKE ","","","","","","","","","","","","Wed Jan 22 11:42:02 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02692 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 256 to 495 (E-value = 1.5e-15) place AA02692 in the Complex1_49kDa family which is described as Respiratory-chain NADH dehydrogenase, 49 Kd subunit (PF00346)","","","","","Skibinski DA, Golby P, Chang YS, Sargent F, Hoffman R, Harper R, Guest JR, Attwood MM, Berks BC, Andrews SC.Regulation of the hydrogenase-4 operon of Escherichia coli by the sigma(54)-dependent transcriptional activators FhlA and HyfR.J Bacteriol. 2002 Dec;184(23):6642-53.PMID: 12426353Bagramyan K, Mnatsakanyan N, Poladian A, Vassilian A, Trchounian A.The roles of hydrogenases 3 and 4, and the F0F1-ATPase, in H2 production by Escherichia coli at alkaline and acidic pH.FEBS Lett. 2002 Apr;516(1-3):172-8.PMID: 11959127Bagramyan K, Vassilian A, Mnatsakanyan N, Trchounian A.Participation of hyf-encoded hydrogenase 4 in molecular hydrogen release coupled with proton-potassium exchange in Escherichia coli.Membr Cell Biol. 2001;14(6):749-63.PMID: 11817571Andrews SC, Berks BC, McClay J, Ambler A, Quail MA, Golby P, Guest JR.A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system.Microbiology. 1997 Nov;143 ( Pt 11):3633-47.PMID: 9387241","","Wed Jan 22 11:42:21 2003","1","","","" "AA02693","1878061","1878705","645","ATGTTTAAGTTACTTAAAACCGTATTTAAAGCCGGCGACGTTACCACCAAATACCCGTTCCAACCTTATGAAGTGGATGATGATTTCAGAGGTAAACCGGAACTTAATTCCGATCAATGTATCGTATGCGCCGCCTGCACAATGGCTTGCCCGGCGAACGCTTTAACCATGCGCACCGACCCGGTGACCGGCGACCGCACTTGGTCTTTATTCCTGGGGCGCTGTATTTTCTGCGGTCGTTGTGAAGAAGTGTGCCCGACCAAAGCCATTCGCTTAACGCAGGATTTTGAATTATCGGTAACCAACAAACAGGATCTTTATCAGGAAACCACCTTTGCGACCGTTGCCTGTCAGGAATGCGGTCAACCATTCATTTCCTATAAAGAGCTGAATTACACCATTGATTTATTCAAACAAACTTTGGATGACCCGAATTTGGTTAAACAAAAACTGGCGGTGTTGCATACTTGCCCGGTATGCAAACGCCAAGGTAGCTTAGAAAAAACCGCAAACATGGAATCCAATATGCGGCTGAAACTCATCGACTTCAAAGAACCGGTGCGCCTGAATTTCAAACAAATGATCGAGCAACGGGAAGAAAGTGCGGTGGAAAATTCAAGAGTTTTAGCAGGAGGCGAAAGACGA","","","24509","MFKLLKTVFKAGDVTTKYPFQPYEVDDDFRGKPELNSDQCIVCAACTMACPANALTMRTDPVTGDRTWSLFLGRCIFCGRCEEVCPTKAIRLTQDFELSVTNKQDLYQETTFATVACQECGQPFISYKELNYTIDLFKQTLDDPNLVKQKLAVLHTCPVCKRQGSLEKTANMESNMRLKLIDFKEPVRLNFKQMIEQREESAVENSRVLAGGERR","1878703","","hydrogenase-4 component H","Cytoplasm, Periplasm","","
InterPro
IPR001450
Domain
4Fe-4S ferredoxin, iron-sulfur binding
PR00353\"[33-44]T\"[80-91]T4FE4SFRDOXIN
PF00037\"[33-56]T\"[68-91]TFer4
PS00198\"[40-51]T\"[75-86]T4FE4S_FERREDOXIN
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.20\"[24-95]Tno description
PTHR10849\"[1-166]TNADH-UBIQUINONE OXIDOREDUCTASE 1, CHAIN 1


","BeTs to 17 clades of COG1143COG name: Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I)Functional Class: CThe phylogenetic pattern of COG1143 is aompkz-qvdr--cef--snujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-05) to 2/2 blocks of the PR00353 family, which is described as \"4Fe-4S ferredoxin signature\". Prints database entry for PR:PR00353. PR00353A 33-44 15 PR00353B 80-91 0.00051Significant hit ( 8.1e-05) to 1/3 blocks of the PR00354 family, which is described as \"7Fe ferredoxin signature\". Prints database entry for PR:PR00354. PR00354C 35-52 8.3e-05 PR00354C 70-87 0.014","","","","","","","","","","","","","Wed Jan 22 11:45:54 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02693 is paralogously related to AA01808 (4e-05).","","","","","","Residues 68 to 91 (E-value = 6.7e-07) place AA02693 in the Fer4 family which is described as 4Fe-4S binding domain (PF00037)","","","","","Skibinski DA, Golby P, Chang YS, Sargent F, Hoffman R, Harper R, Guest JR, Attwood MM, Berks BC, Andrews SC.Regulation of the hydrogenase-4 operon of Escherichia coli by the sigma(54)-dependent transcriptional activators FhlA and HyfR.J Bacteriol. 2002 Dec;184(23):6642-53.PMID: 12426353Bagramyan K, Mnatsakanyan N, Poladian A, Vassilian A, Trchounian A.The roles of hydrogenases 3 and 4, and the F0F1-ATPase, in H2 production by Escherichia coli at alkaline and acidic pH.FEBS Lett. 2002 Apr;516(1-3):172-8.PMID: 11959127Bagramyan K, Vassilian A, Mnatsakanyan N, Trchounian A.Participation of hyf-encoded hydrogenase 4 in molecular hydrogen release coupled with proton-potassium exchange in Escherichia coli.Membr Cell Biol. 2001;14(6):749-63.PMID: 11817571Andrews SC, Berks BC, McClay J, Ambler A, Quail MA, Golby P, Guest JR.A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system.Microbiology. 1997 Nov;143 ( Pt 11):3633-47.PMID: 9387241","","Wed Jan 22 11:45:54 2003","1","","","" "AA02695","1878705","1879478","774","ATGAACACACAAATTCCAATGCCGGTCAATGGCATTTCAACGCCATTCAGCATAGATGAAAATATCGCCAAAATGAAACAAACCCTGTTGAAGAATATTCAACGTTCGGCGTATGTCTATCGTGTGGACTGCGGTGGTTGCAACGGCTGCGAAATCGAAATTTTCAGCACCATCACGCCGACCTTCGACGCGGAGCGTTTCGGGATTAAAGTGGTGGCATCGCCCCGCCATGCGGATATTTTGTTGTTCACCGGCGCGGTGACCCGTGCTATGCGCACCCCTGCAATGCGTGCCTACCAAGCGGCGCCCGATCCGAAAATCTGTATTTCTTACGGCGCTTGCGGTTGTGGCGGCGGGATTTTCCATGATCTTTATTGCGTCTGGGGCGGTAGCGATCAAATCGTGCCGATTGACGTGTATATCCCGGGCTGCCCGCCAACCCCAGCGGCAACCATTTACGGCTTCGCCATGGCGTTAGGGTTACTCGATCAAAAACTGAAAGGCAAACAGGAAAAAGCCGATCCGAATGCCGACGCCAAATTGCGTTTTCCGGGCATTCCGCTGGATTTGCGTATCAGCTTAGAACGGGAGGCTCGTCGTCTTGCCGGTTATCGCCAGGGTGGCAATATCGCCAATCAATTTATGGCGATGATGTCGGAAGATGACAGCGTGCCGTTCGGTGTGCGTTTAGGGGAATACCTGGAACGGGAAGCGGATCCGCGCCTGAGAGAAATCGTCAACCGTCTGCATGCCATTAGTATGCAGTTTTCGGGG","","","28271","MNTQIPMPVNGISTPFSIDENIAKMKQTLLKNIQRSAYVYRVDCGGCNGCEIEIFSTITPTFDAERFGIKVVASPRHADILLFTGAVTRAMRTPAMRAYQAAPDPKICISYGACGCGGGIFHDLYCVWGGSDQIVPIDVYIPGCPPTPAATIYGFAMALGLLDQKLKGKQEKADPNADAKLRFPGIPLDLRISLEREARRLAGYRQGGNIANQFMAMMSEDDSVPFGVRLGEYLEREADPRLREIVNRLHAISMQFSG","1879476","","hydrogenase-3 component G","Cytoplasm, Inner membrane","","
InterPro
IPR006137
Domain
NADH ubiquinone oxidoreductase, 20 kDa subunit
PF01058\"[52-159]TOxidored_q6
InterPro
IPR014406
Family
[NiFe]-hydrogenase-3-type complex, small subunit/NADH:quinone oxidoreductase, subunit PSST/NdhK/NuoB
PIRSF002913\"[24-177]T[NiFe]-hydrogenase-3-type complex, small subunit/NADH:quinone oxidoreductase (complex I), subunit PSST/NdhK/NuoB
PTHR11995\"[10-224]TNADH DEHYDROGENASE
InterPro
IPR014658
Family
[NiFe]-hydrogenase-3-type complex, small subunit
PIRSF500034\"[1-168]T[NiFe]-hydrogenase-3-type complex, small subunit
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.700\"[31-148]Tno description
PTHR11995:SF3\"[10-224]TFORMATE HYDROGENLYASE 7


","BeTs to 5 clades of COG3260COG name: Ni,Fe-hydrogenase III small subunitFunctional Class: CThe phylogenetic pattern of COG3260 is --mpk-----r---e-----------Number of proteins in this genome belonging to this COG is","Significant hit ( 2.1e-36) to 2/2 blocks of the IPB002096 family, which is described as \"Respiratory-chain NADH dehydrogenase 20 Kd subunit\". Interpro entry for IP:IPR002096. IPB002096A 34-84 2.1e-15 IPB002096B 117-162 1.1e-19","Residues 130 to 158 match (2e-07) PD:PD517181 which is described as OXIDOREDUCTASE SUBUNIT COMPLETE PROTEOME NADH CHAIN IRON-SULFUR 4FE-4S NAD DEHYDROGENASE ","","","","","","","","","","","","Wed Jan 22 11:52:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02695 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 52 to 159 (E-value = 2.9e-48) place AA02695 in the Oxidored_q6 family which is described as NADH ubiquinone oxidoreductase, 20 Kd subunit (PF01058)","","","","","Bagramian KA.[Electrochemical study of proton translocation function of hydrogenase 3].Biofizika. 47(5):847-51.PMID: 12397955Bagramyan K, Mnatsakanyan N, Poladian A, Vassilian A, Trchounian A.The roles of hydrogenases 3 and 4, and the F0F1-ATPase, in H2 production by Escherichia coli at alkaline and acidic pH.FEBS Lett. 2002 Apr;516(1-3):172-8.PMID: 11959127","","Wed Jan 22 11:52:45 2003","1","","","" "AA02696","1879616","1880017","402","ATGACCACCGTAATCTTCTATCTTCTCAACGAACGCTTTGTCGAAAACGAAGAACAAGTGCAGGAGCAGGCGCAGCAAGTAATGTATTACTCTTTGGCAATCGGTCACCATGTGGGTGTGATTGATTGCTTCAAAAAATTGCTGATTTGCGACTACGAGGATTATCAACAATTTGTCGCCGCCTTCCCGGAAGGGGAAGCAAAGCGTAAATTTACAGGGTTAATGAAATTCGGCGAAATCGTGATTGATTCCAGTCATGTGAATTTATTGGCGAAAGCGCTGGACGAAAATAAAGCCCATTTCACCCCGCAACATCAGCAATGGTCCGAAATTTTAATGGACACCTTGGCTTCCATTCAGCGCGAGCCGGTGATGTATATCATGGTGAAACGTCGTGACGAA","","","15691","MTTVIFYLLNERFVENEEQVQEQAQQVMYYSLAIGHHVGVIDCFKKLLICDYEDYQQFVAAFPEGEAKRKFTGLMKFGEIVIDSSHVNLLAKALDENKAHFTPQHQQWSEILMDTLASIQREPVMYIMVKRRDE","1880015","","formate hydrogenlyase maturation protein","Cytoplasm","","
InterPro
IPR010005
Family
Formate hydrogenlyase maturation HycH
PF07450\"[2-132]THycH
noIPR
unintegrated
unintegrated
PD021295\"[28-131]TQ8ZMJ2_SALTY_Q8ZMJ2;


","No hits to the COGs database.","","Residues 28 to 131 match (1e-24) PD:PD021295 which is described as PROTEOME COMPLETE HYDROGENLYASE MATURATION FORMATE HYDROGENASE-4 PART HYCE HYCH COMPONENT ","","","","","","","","","","","","Wed Jan 22 11:59:56 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02696 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 132 (E-value = 3.4e-54) place AA02696 in the HycH family which is described as Formate hydrogenlyase maturation protein HycH (PF07450)","","","","","Sauter M, Böhm R, Böck A.Mutational analysis of the operon (hyc) determining hydrogenase 3 formation in Escherichia coli.Mol Microbiol. 1992 Jun;6(11):1523-32.PMID: 1625581Rossmann R, Maier T, Lottspeich F, Böck A.Characterisation of a protease from Escherichia coli involved in hydrogenase maturation.Eur J Biochem. 1995 Jan;227(1-2):545-50.PMID: 7851435","","Wed Jan 22 11:59:56 2003","1","","","" "AA02697","1880010","1880468","459","GTGACGAATAACAATATCATTCTCACCGTCGGCAACAGCATGATGGGCGACGACGGCGCCGGTCCGTACCTGTATCAGCTGTTAAATGAAAATCCGTTGGAAAATTGGACCGCACTTGATGGCGGATCCGCGCCGGAAAATGTGGCGCATATCGTGCGGGAACTCAAACCCGAACTTTTGCTGATTTTCGATGCCGCCGATATGGAACTGGCGCCGGGCAAAATCCGCATTATCGAAAAAGAAGCCATCGCCGAAATGTTCTTCATGAGCACGCATAATATGCCGCTTAATTTTTTAATCGAACAATTAGAACAAGACATTAAAAAAATCATCTTTGTGGGCATTCAACCGGATCTGGTTTCCTTCGGTTTTCCCATGACCGATGCCGTCAAAGAATCCGTGCAGTTTATGTATGATTTTTTAAAAGACGGACGGACGCTTGCGGAGATTCCGGTGTTG","","","17085","VTNNNIILTVGNSMMGDDGAGPYLYQLLNENPLENWTALDGGSAPENVAHIVRELKPELLLIFDAADMELAPGKIRIIEKEAIAEMFFMSTHNMPLNFLIEQLEQDIKKIIFVGIQPDLVSFGFPMTDAVKESVQFMYDFLKDGRTLAEIPVL","1880466","","hydrogenase 3 maturation protease","Cytoplasm","","
InterPro
IPR000671
Family
Peptidase A31, hydrogen uptake protein
PR00446\"[5-17]T\"[17-28]T\"[35-52]T\"[58-68]T\"[69-85]THYDRGNUPTAKE
G3DSA:3.40.50.1450\"[3-143]Tno description
PIRSF005756\"[5-149]T[NiFe]-hydrogenase maturation protease
PF01750\"[22-144]THycI
TIGR00072\"[2-134]Thydrog_prot: hydrogenase maturation proteas
InterPro
IPR004420
Family
Peptidase A31, hydrogenase maturation protease HycI
TIGR00142\"[5-149]ThycI: hydrogenase maturation peptidase HycI


","No hits to the COGs database.","Significant hit ( 8.6e-15) to 5/5 blocks of the PR00446 family, which is described as \"Hydrogen uptake protein signature\". Prints database entry for PR:PR00446. PR00446A 5-17 0.064 PR00446B 17-28 5.4 PR00446C 35-52 0.053 PR00446D 58-68 0.13 PR00446E 69-85 0.27","Residues 6 to 134 match (1e-15) PD:PD002187 which is described as HYDROGENASE PROTEOME COMPLETE PROTEASE HYDROLASE METALLOPROTEASE NICKEL MATURATION EXPRESSION/FORMATION HUPD ","","","","","","","","","","","","Wed Jan 22 12:08:59 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02697 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 22 to 144 (E-value = 9e-25) place AA02697 in the HycI family which is described as Hydrogenase maturation protease (PF01750)","","","","","","","","1","","","" "AA02698","1881000","1881485","486","ATGGCTTTGGACAATAACAATAATTTATCCATATCGTGTTGTAGCTCAAATAAGGACATTACTATGGCAATTAAAAAAGTGATTACTGTATGTCCGTATTGTGCCTCAGGTTGTAAAATCAATCTTTTGGTTGAAAACAACAAAATTGTGGGAGCTGAGGGCGCAAACGGCAAGACCAACGAAGGGGAGTTGTGTCTAAAAGGATATTATGGCTGGGATTTCGTACATGACACTAAAATTCTGACTCCTCGCCTGACTCAACCGATGATCCGCTACAAACGTGGCGAACCATTCACCCCGGTAAGCTGGGAAGAAGCGATTTCTTACTCCGCTAACCGTCTCAAAGAAATCTGTGAAAAATACGGTAACGAATCCATTATGGTAACAGGGTCCTCCCGCGGTCCGGGTAACGAAGTGAACTTCGTTATGCAAAAATTCGCCCGTGCGGTATTAGGAAATAACAATGTTGACTGTTGTGCGCGCGTA","","","18476","MALDNNNNLSISCCSSNKDITMAIKKVITVCPYCASGCKINLLVENNKIVGAEGANGKTNEGELCLKGYYGWDFVHDTKILTPRLTQPMIRYKRGEPFTPVSWEEAISYSANRLKEICEKYGNESIMVTGSSRGPGNEVNFVMQKFARAVLGNNNVDCCARV","1881483","","formate dehydrogenase H, selenopolypeptide subunit","Periplasm, Extracellular","","
InterPro
IPR006655
Family
Prokaryotic molybdopterin oxidoreductase
PS00551\"[29-47]TMOLYBDOPTERIN_PROK_1
InterPro
IPR006656
Domain
Molybdopterin oxidoreductase
PF00384\"[84-162]TMolybdopterin
InterPro
IPR006963
Domain
Molybdopterin oxidoreductase Fe4S4 region
PF04879\"[24-77]TMolybdop_Fe4S4
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.740\"[84-162]Tno description
PTHR11615\"[26-161]TNITRATE, FROMATE, IRON DEHYDROGENASE


","No hits to the COGs database.","Significant hit ( 8.4e-10) to 2/3 blocks of the IPB001467 family, which is described as \"Prokaryotic molybdopterin oxidoreductases\". Interpro entry for IP:IPR001467. IPB001467A 65-87 0.049 IPB001467B 95-117 6e-06","Residues 25 to 77 match (4e-19) PD:PD001047 which is described as COMPLETE PROTEOME SUBUNIT OXIDOREDUCTASE FORMATE DEHYDROGENASE NITRATE REDUCTASE ALPHA IRON-SULFUR ","","","","","","","","","","","","Wed Jan 22 12:15:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02698 is paralogously related to AA00552 (1e-12) and AA01137 (1e-07).","","","","","","Residues 24 to 77 (E-value = 3.9e-19) place AA02698 in the Molybdop_Fe4S4 family which is described as Molybdopterin oxidoreductase Fe4S4 domain (PF04879)","","","","","Boyington JC, Gladyshev VN, Khangulov SV, Stadtman TC, Sun PD.Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster.Science. 1997 Feb;275(5304):1305-8.PMID: 9036855Chenier I, Dube F, Hallenbeck PC.Mutations permitting fdhF (Formate dehydrogenase H) expression in a selD mutant of salmonella typhimurium.Curr Microbiol. 2000 Jul;41(1):39-44.PMID: 0010821909","","Wed Jan 22 12:23:31 2003","1","","","" "AA02699","1881537","1883219","1683","ATGTCCAACTCAATCGTTGAGATTGAAGACACCAAATGTGTATTTATCTTCGGCTATAATGCCTCCACTTCACACCCAATCGTGGCGCGTCGAATTAATCACGCCAAAGAAAAAGGTGCGAAAATCATTGTTTGTGACCCTCCTAAAATCGAGACTGCGCGTATTGCTGATATTTATGCACCACTTGCCAACGGTAGTAACGTGGCATTCTTAAATGCCATGATGAATGTGATTTTGGAAGAGGGGTTACAAGATCAAAAATTTATTGATGAACACACCGAAAACTTCGATGCGTTCTATGAAACCGTAAAAGCCTATACACCGGAATCCACGCAACACATCACCGGCATTGACCCTGAAATGTTGCGTGAAATCGCCCGCACTTATGCGAAAGCGGAAACCGCGACGATCTTGTGGGGTATGGGTGTATGTCAATTCCGCCAAGGGGTGGAAACTGTTCGTGCGTTGGCAAGTTTGGCAATGTTGACGGGTAATCTTGGTAAACCGAATGTAGGTGTAAACCCGGTACGTGGTCAAAATAACGTACAGGGCGCGTGCGATATGGGCGCGTTATTCAACACCTTGCCGGGCTATCAAAGTTTTGCTGATCCTGAAACCAATGCGAAATTCGCCAAAGCCTGGGGAGTACCGTCCATTCCGACCAAACCGGGCGTGCCGTTAAGTGAAGTGCCGCACGCAGTGAAAGAAGGCAAACTCAAAGCGTTTTACATCATGGGTGAGGACACCTTACAAACCGAACCTGATATTAACGCTATGAAACAAACCTTCAAGGATTTGGAATTCATTATCGTACAGGATATTTTCATGACCCAAACCGCCGCGGAAGCGGATGTGATTTTACCGGCAACCTCCTGTGCCGAACATGAAGGTGTGTACAGTGCCGCCGACCGTGGTTTCCAACGCTTCTATAAGGCCGTTGAACCGGTAGGCAATGTCAAGGACGACTGGGAAATCATCAGTTTAATAGCGCAAGCCTTAGGCTATCCAATGCATTACAACAACACCAAAGAAATTTGGGACGAATTACGTGAACTTTGCCCGATTTACAAAGGCGCGACCTACGAAAAAATGGAAGGTTTGGGCTACATTCAATGGCCTTGTACCGACGAAGGACCGGAAGACCAAGGTACGCAGTATTTGTATGAAGGACAAATCTTCGACCGCAAAGGCGGCAAAGCCGAATTCTTTGCCTGCGACTGGGAACCGCCGATGGAAGATCTTTCCGAAGAATTCCCGTTGGTACTTTCCACCGTGCGTGAAGTGGGACACTATTCCTGCCGTTCTATGACAGGTAACTGTCGCGCCCTCGCCGCCCTTGCCGACGAACCGGGATTCGTTCAAATGAACGACCAAGACGCCAAAGCACTGGGTATTAAAAACAACGACTTGGTTTGGATTGCTTCTTCACGGGGTAAAGTTATTTCCCACGCCGATGTGAGCACCCGTACCAACAAAGGCGCTTGTTATATGACCTACCAATGGTGGATCGGTAAATGTAACGAACTCACCGCCGAACATTTGAACCCGGGTTCAAGAACGCCGGAATACAAATACAGCGCGGTGCGTATTGATAAAATTGAGGATCAAGCTTGGGCAGAGCACTATGTAGTGGCGGAATATACCAAACTGAAAAACCGCTTAAAACAAACTGCGTTAGTAGCA","","","62503","MSNSIVEIEDTKCVFIFGYNASTSHPIVARRINHAKEKGAKIIVCDPPKIETARIADIYAPLANGSNVAFLNAMMNVILEEGLQDQKFIDEHTENFDAFYETVKAYTPESTQHITGIDPEMLREIARTYAKAETATILWGMGVCQFRQGVETVRALASLAMLTGNLGKPNVGVNPVRGQNNVQGACDMGALFNTLPGYQSFADPETNAKFAKAWGVPSIPTKPGVPLSEVPHAVKEGKLKAFYIMGEDTLQTEPDINAMKQTFKDLEFIIVQDIFMTQTAAEADVILPATSCAEHEGVYSAADRGFQRFYKAVEPVGNVKDDWEIISLIAQALGYPMHYNNTKEIWDELRELCPIYKGATYEKMEGLGYIQWPCTDEGPEDQGTQYLYEGQIFDRKGGKAEFFACDWEPPMEDLSEEFPLVLSTVREVGHYSCRSMTGNCRALAALADEPGFVQMNDQDAKALGIKNNDLVWIASSRGKVISHADVSTRTNKGACYMTYQWWIGKCNELTAEHLNPGSRTPEYKYSAVRIDKIEDQAWAEHYVVAEYTKLKNRLKQTALVA","1883217","","formate dehydrogenase H, selenopolypeptide subunit","Cytoplasm, Periplasm","","
InterPro
IPR006478
Family
Formate dehydrogenase, alpha subunit
TIGR01591\"[1-530]TFdh-alpha: formate dehydrogenase, alpha sub
InterPro
IPR006655
Family
Prokaryotic molybdopterin oxidoreductase
PS00490\"[277-294]TMOLYBDOPTERIN_PROK_2
PS00932\"[460-487]TMOLYBDOPTERIN_PROK_3
InterPro
IPR006656
Domain
Molybdopterin oxidoreductase
PF00384\"[1-332]TMolybdopterin
InterPro
IPR006657
Domain
Molydopterin dinucleotide-binding region
PF01568\"[420-527]TMolydop_binding
noIPR
unintegrated
unintegrated
G3DSA:2.40.40.20\"[417-533]Tno description
G3DSA:3.40.228.10\"[1-211]Tno description
G3DSA:3.90.55.10\"[286-382]Tno description
PTHR11615\"[7-546]TNITRATE, FROMATE, IRON DEHYDROGENASE


","BeTs to 16 clades of COG0243COG name: Anaerobic dehydrogenases, typically selenocysteine-containingFunctional Class: CThe phylogenetic pattern of COG0243 is aompkz-q-dr-bcefgh--uj----Number of proteins in this genome belonging to this COG is","Significant hit ( 5.8e-09) to 1/3 blocks of the IPB001467 family, which is described as \"Prokaryotic molybdopterin oxidoreductases\". Interpro entry for IP:IPR001467. IPB001467C 269-294 5.8e-09 IPB001467C 42-67 0.00061","Residues 348 to 443 match (7e-07) PD:PD589010 which is described as PROTEOME COMPLETE FORMATE SUBUNIT ALPHA DEHYDROGENASE RELATED DEHYDROGENEASE 679AA LONG ","","","","","","","","","","","","Wed Jan 22 12:22:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02699 is paralogously related to AA00552 (2e-37), AA02676 (5e-33), AA02251 (2e-25) and AA01137 (2e-19).","","","","","","Residues 420 to 527 (E-value = 1.1e-27) place AA02699 in the Molydop_binding family which is described as Molydopterin dinucleotide binding domain (PF01568)","","","","","Boyington JC, Gladyshev VN, Khangulov SV, Stadtman TC, Sun PD.Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster.Science. 1997 Feb;275(5304):1305-8.PMID: 9036855Chenier I, Dube F, Hallenbeck PC.Mutations permitting fdhF (Formate dehydrogenase H) expression in a selD mutant of salmonella typhimurium.Curr Microbiol. 2000 Jul;41(1):39-44.PMID: 0010821909","","Wed Jan 22 12:23:53 2003","1","","","" "AA02700","1884265","1883396","870","ATGTCAATTTTAATCGATAATAACACCAAAGTAATTTGCCAAGGTTTCACCGGAGGACAAGGCACATTCCACTCCCAACAAGCATTGGCTTACGGCACCAAATTAGTCGGTGGCGTGTCCCCCGGCAAGGGCGGCACAACCCATCTGGGGCTGCCGGTGTTCAATACTGTGCGGGATGCCGTGGAAGCGACCGGCGCCACCGCAACAGTGATTTATGTCCCTGCACCGGGCTGCAAAGACGCCATTTTAGAAGCTATCGACGCGGGCATTCAGTTAATCGTGTGTATTACCGAAGGGATCCCAACGCTAGATATGTTAGTGGTCAAACAGCGTTTAAATCAAACCGGCGTAAGTATGATCGGCCCGAACTGCCCGGGCGTGATTACACCGGAAGAATGCAAAATCGGCATTATGCCGGGCGATATTCACAAGAAAGGCAAAATCGGCATCGTTTCCCGCTCCGGCACGCTCACTTATGAAGCGGTCAAACAAACCACCGACGAAGGTTTCGGGCAATCCACTTGTGTCGGCATCGGCGGCGATCCGATTCCCGGCTCCAACTTTGTGGATATTCTTAAATTATTCCAAGAAGATCCGCAAACAGAAGCTATTGTCATGATCGGCGAAATCGGCGGTTCGGCGGAAGAAGAAGCGGCGGCGTTCATTAAACAACACGTCACCAAGCCGGTAGTCAGCTACATCGCCGGCGTTACTGCCCCGAAAGACAAACGCATGGGGCACGCCGGCGCCATCATCAGCGGCGGCAAAGGCACCGCCGATGAAAAGTTTGTCGCCCTCGAAGCGGCCGGCGTGAAAACCGTCAGAAGCCTGGTAGGCATCGGTGCAGTATTGCGGGACGTGCTGAAGAAA","","","33179","MSILIDNNTKVICQGFTGGQGTFHSQQALAYGTKLVGGVSPGKGGTTHLGLPVFNTVRDAVEATGATATVIYVPAPGCKDAILEAIDAGIQLIVCITEGIPTLDMLVVKQRLNQTGVSMIGPNCPGVITPEECKIGIMPGDIHKKGKIGIVSRSGTLTYEAVKQTTDEGFGQSTCVGIGGDPIPGSNFVDILKLFQEDPQTEAIVMIGEIGGSAEEEAAAFIKQHVTKPVVSYIAGVTAPKDKRMGHAGAIISGGKGTADEKFVALEAAGVKTVRSLVGIGAVLRDVLKK","1883394","","succinyl-CoA synthase, alpha subunit","Cytoplasm","","
InterPro
IPR003781
Domain
CoA-binding
PF02629\"[4-100]TCoA_binding
InterPro
IPR005810
Family
Succinyl-CoA ligase, alpha subunit
PR01798\"[82-99]T\"[177-195]T\"[208-221]T\"[240-257]TSCOASYNTHASE
PIRSF001553\"[3-289]TSuccinyl-CoA synthetase, alpha subunit
PTHR11117\"[1-290]TSUCCINYL-COA SYNTHETASE-RELATED
TIGR01019\"[3-288]TsucCoAalpha: succinyl-CoA synthetase, alpha
PS00399\"[236-249]TSUCCINYL_COA_LIG_2
PS01216\"[152-181]TSUCCINYL_COA_LIG_1
InterPro
IPR005811
Domain
ATP-citrate lyase/succinyl-CoA ligase
PF00549\"[133-274]TLigase_CoA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.261\"[124-289]Tno description
G3DSA:3.40.50.720\"[2-123]Tno description


","BeTs to 21 clades of COG0074COG name: Succinyl-CoA synthetase alpha subunitFunctional Class: CThe phylogenetic pattern of COG0074 is aomp-zyq-dr-bcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 6.3e-67) to 4/4 blocks of the IPB000303 family, which is described as \"ATP-citrate lyase/succinyl-CoA ligases\". Interpro entry for IP:IPR000303. IPB000303A 23-69 5.4e-22 IPB000303B 92-101 3.6e-05 IPB000303C 119-162 1.5e-24 IPB000303D 228-251 3.7e-11Significant hit ( 4.1e-26) to 4/4 blocks of the IPB003781 family, which is described as \"DUF184\". Interpro entry for IP:IPR003781. IPB003781A 119-128 9.4e-05 IPB003781B 152-180 3.4e-08 IPB003781C 190-209 4.8e-07 IPB003781D 242-269 0.54","Residues 2 to 122 match (6e-53) PD:PD337294 which is described as SUCCINYL-COA LIGASE ALPHA PROTEOME COMPLETE CYCLE ACID TRICARBOXYLIC CHAIN SYNTHETASE ","","","","","","","","","","","","Wed Jan 22 12:32:52 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02700 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 133 to 274 (E-value = 2.9e-63) place AA02700 in the Ligase_CoA family which is described as CoA-ligase (PF00549)","","","","","","","Wed Jan 22 12:32:52 2003","1","","","" "AA02702","1885445","1884279","1167","ATGAATCTACACGAATACCAAAGTAAGCAGGTTTTTGCCGAATATGATTTACCGATATGCCGAGGCATCGCTTGTAAAACCGCAGACGAAGCGGCAGAGGCGATCAAACAGCTGAAGGGCGATGTTTGGGTTACCAAGTGCCAAGTGCATGCGGGTGGGCGCGGAAAAGCCGGTGGCGTGAAATTGGTGCGTAATGAAGCGGAAGTGCGTGCCTTTGTGGATAAATGGCTGGGGCAGCGTTTGGTGACCTTTCAAACCGATGCCAATGGGCAACCGATTAACATTATTTATGTGGAAGAAACGGTCAATATCGACCGAGAGTTATATTTGGGCGCGGTGATCGATCGCGCTTCACAAAAAGTGGTCTTTATGGCATCTGCCGCCGGCGGTATGGATATTGAAGAGGTGGCGGCGAAAACCCCGGAATTATTGCATAAAGTAGCGTTGGATCCGCTGGTGGGCGGAATGCCTTATCAAGGGCGCGAATTGGCGTTTAAACTGGGGTTGAAGGGCGATCAAATCAACCAATTTACCCATATTTTCACCCAACTGGCGAAAATGTTTGTAGAGCGGGATTTATCTCTGTTGGAAATTAATCCGCTTGTAGTAACCAAAGAAGGCAAGCTGTCTTGTCTGGATGCCAAGATCGTGGTGGACAGTAATGCACTATATCGCCAGCTGGATTTAGCCACTATGCACGATATTACCCAAAGCGATGCGCGTGAAGCCTTGGCGGAATTGCACCAGCTGAATTACGTAGCACTGGACGGCAACATCGGCTGTATGGTCAATGGCGCCGGGCTTGCCATGGGCACGATGGATATTGTGAAACTGCACGGCGGGCAGCCTGCAAATTTCCTTGATGTGGGCGGTGGCACAACCAAAGAACGGGTGGCGGAAGCCTTCAAAATCATTCTTTCCGATAAAAACGTCAAAGCCATATTGGTGAATATTTTCGGCGGCATTGTGCGTTGCGATCTGATCGCCGAAGGCATTGTGGCGGCGGTGAACCAAGTGGGCGTACATGTGCCGGTAGTGGTGCGTTTGGAAGGCAACAACGCGCCTTTAGGACGGGAAATTTTAGCCAACAGCGGTTTGAATATTATTGCGGCGAAAACCCTCACGGACGCGGCGGTGGAATCCATTAAAGCGGCAAATGGTAATTTA","","","41836","MNLHEYQSKQVFAEYDLPICRGIACKTADEAAEAIKQLKGDVWVTKCQVHAGGRGKAGGVKLVRNEAEVRAFVDKWLGQRLVTFQTDANGQPINIIYVEETVNIDRELYLGAVIDRASQKVVFMASAAGGMDIEEVAAKTPELLHKVALDPLVGGMPYQGRELAFKLGLKGDQINQFTHIFTQLAKMFVERDLSLLEINPLVVTKEGKLSCLDAKIVVDSNALYRQLDLATMHDITQSDAREALAELHQLNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGQPANFLDVGGGTTKERVAEAFKIILSDKNVKAILVNIFGGIVRCDLIAEGIVAAVNQVGVHVPVVVRLEGNNAPLGREILANSGLNIIAAKTLTDAAVESIKAANGNL","1884277","","succinyl-CoA synthetase, beta chain","Cytoplasm","","
InterPro
IPR005809
Family
Succinyl-CoA synthetase, beta subunit
PIRSF001554\"[1-388]TSuccinyl-CoA synthetase, beta subunit
PTHR11815\"[1-386]TSUCCINYL-COA SYNTHETASE BETA CHAIN
TIGR01016\"[1-386]TsucCoAbeta: succinyl-CoA synthetase, beta s
PS01217\"[257-281]TSUCCINYL_COA_LIG_3
InterPro
IPR005811
Domain
ATP-citrate lyase/succinyl-CoA ligase
PF00549\"[246-385]TLigase_CoA
InterPro
IPR013650
Domain
ATP-grasp fold, succinyl-CoA synthetase-type
PF08442\"[2-203]TATP-grasp_2
InterPro
IPR013816
Domain
ATP-grasp fold, subdomain 2
G3DSA:3.30.470.20\"[85-239]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.261\"[240-388]Tno description


","BeTs to 21 clades of COG0045COG name: Succinyl-CoA synthetase beta subunitFunctional Class: CThe phylogenetic pattern of COG0045 is aomp-zyq-dr-bcefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 2.9e-57) to 4/4 blocks of the IPB000303 family, which is described as \"ATP-citrate lyase/succinyl-CoA ligases\". Interpro entry for IP:IPR000303. IPB000303A 26-72 1.3e-18 IPB000303B 191-200 5.5 IPB000303C 263-306 1.1e-22 IPB000303D 343-366 9.5e-12Significant hit ( 1e-08) to 2/3 blocks of the IPB003135 family, which is described as \"ATP-grasp domain\". Interpro entry for IP:IPR003135. IPB003135B 44-56 0.00011 IPB003135C 274-284 0.039","Residues 236 to 385 match (2e-58) PD:PD002034 which is described as SUCCINYL-COA LIGASE COMPLETE PROTEOME SYNTHETASE CHAIN ALPHA ACID CYCLE TRICARBOXYLIC ","","","","","","","","","","","","Wed Jan 22 12:40:56 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02702 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 246 to 385 (E-value = 7.9e-74) place AA02702 in the Ligase_CoA family which is described as CoA-ligase (PF00549)","","","","","Kapatral V, Bina X, Chakrabarty AM.Succinyl coenzyme A synthetase of Pseudomonas aeruginosa with a broad specificity for nucleoside triphosphate (NTP) synthesis modulates specificity for NTP synthesis by the 12-kilodalton form of nucleoside diphosphate kinase.J Bacteriol. 2000 Mar;182(5):1333-9.PMID: 10671455Buck D, Spencer ME, Guest JR.Primary structure of the succinyl-CoA synthetase of Escherichia coli.Biochemistry. 1985 Oct;24(22):6245-52.PMID: 3002435Joyce MA, Fraser ME, James MN, Bridger WA, Wolodko WT.ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by x-ray crystallography.Biochemistry. 2000 Jan;39(1):17-25.PMID: 10625475Joyce MA, Fraser ME, Brownie ER, James MN, Bridger WA, Wolodko WT.Probing the nucleotide-binding site of Escherichia coli succinyl-CoA synthetase.Biochemistry. 1999 Jun;38(22):7273-83.PMID: 10353839","","Wed Jan 22 12:40:56 2003","1","","","" "AA02703","1885642","1885505","138","TTGAAATTTAATAAGAAAACCGCTTGTTTCTTGCTTGCAAGACAAGCGGTTTCGGTTTATAAAAACGCCTTAAGAAAAAAACGTTGTTTATTCTTCGCAGGTAAGTTTGCTTACTTGCTCACGCCAACAGTCAAAAAA","","","5308","LKFNKKTACFLLARQAVSVYKNALRKKRCLFFAGKFAYLLTPTVKK","1885505","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 16:05:19 2004","Mon Feb 23 16:05:19 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02703 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 16:05:19 2004","","","","","","","","","","","","","1","","","" "AA02704","1886855","1885635","1221","ATGACGATTGAAATTCTTGTCCCCGATTTACCCGAATCCGTAGCCGATGCCACCGTGGCAACTTGGCACAAAAAAGCGGGCGACGCAGTGAAACGTGATGAAGTGATTGTGGAAATCGAGACCGACAAAGTGGTGCTTGAAGTGCCGGCACAGGCGGACGGCGTGCTTGCCCAGATTTTGCAGGAAGAAGGGGCAACAGTAGTCAGCAAACAGTTGCTTGGCACTCTGGAAGATTCGGTGACGGCGGCAGCCATTGCAACGGAAAAAACGGCGGAGCCGACACCGAAAGATCGTCGCACGGAAGTGCCTGATGAACCGCATGTCACCGATGCGCAAGGACCTGCGGTACGCCGTTTATTAGCCGAGCACGGTTTACAGCCTTCCGATGTTGCCGATGTAAAAGGCACCGGCGTGGGCGGCAGAATTACCCGTGAAGATGTGGAAGCGATCCTTGCCCAACGCACGGCTGCAGCGGCACAACCGCAAGTGGCGGAAGATACCCTCAGCACCGTGGCATATGCCGCACGTAGTGAAAAACGCGTGCCGATGACCCGTTTACGCAAACGTATTGCGGAACGTCTGTTGGAAGCCAAAAACACCACCGCGATGTTGACTACGTTCAATGAAGTGGATATGCAGCCGATCATGAACCTGCGTAAACAATACGGTGAAAAATTTGAAAAACAACACGGCGTGCGTTTAGGCTTCATGTCTTTTTATATCAAAGCCGTGGTGGAAGCCTTAAAACGTTATCCGGAAGTGAATGCCTCCATTGACGGCGACGATGTGATTTATCACAACTATTTTGACGTGAGCATTGCGGTTTCGACTCCACGCGGTTTAGTGACGCCGGTATTGCGCGATTGTGATAATCTTTCCATGGCGGACATTGAAAAATCTATCAAAGCCCTGGCGGAAAAAGGGCGTGACGGCAAATTGACAGTAGAAGATTTAACCGGCGGTAACTTCACCATTACCAACGGCGGCGTGTTCGGTTCGCTAATGTCCACTCCGATTATCAACCCGCCGCAAAGTGCCATTTTAGGTATGCACGCCATTAAAGAACGCCCGGTGGCGCTAAACGGTCAAGTGGTGATTCGCCCGATGATGTATTTGGCATTGAGTTACGACCACCGCTTAATTGACGGGCGGGAATCCGTCGGTTTCTTAGTGACGATAAAAGAGCTGCTGGAAGACCCGACAAGATTATTACTTGAAATT","","","44426","MTIEILVPDLPESVADATVATWHKKAGDAVKRDEVIVEIETDKVVLEVPAQADGVLAQILQEEGATVVSKQLLGTLEDSVTAAAIATEKTAEPTPKDRRTEVPDEPHVTDAQGPAVRRLLAEHGLQPSDVADVKGTGVGGRITREDVEAILAQRTAAAAQPQVAEDTLSTVAYAARSEKRVPMTRLRKRIAERLLEAKNTTAMLTTFNEVDMQPIMNLRKQYGEKFEKQHGVRLGFMSFYIKAVVEALKRYPEVNASIDGDDVIYHNYFDVSIAVSTPRGLVTPVLRDCDNLSMADIEKSIKALAEKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKERPVALNGQVVIRPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLLLEI","1885633","","dihydrolipoamide succinyltransferase","Cytoplasm","","
InterPro
IPR000089
Domain
Biotin/lipoyl attachment
PF00364\"[3-76]TBiotin_lipoyl
PS50968\"[3-76]TBIOTINYL_LIPOYL
InterPro
IPR001078
Domain
Catalytic domain of components of various dehydrogenase complexes
PD001115\"[325-400]TODO2_HAEIN_P45302;
PF00198\"[175-405]T2-oxoacid_dh
InterPro
IPR003016
Binding_site
2-oxo acid dehydrogenase, lipoyl-binding site
PS00189\"[27-56]TLIPOYL
InterPro
IPR004167
Domain
E3 binding
PF02817\"[112-151]TE3_binding
InterPro
IPR006255
Family
Dihydrolipoamide succinyltransferase
TIGR01347\"[3-407]TsucB: 2-oxoglutarate dehydrogenase, E2 comp
noIPR
unintegrated
unintegrated
G3DSA:2.40.50.100\"[4-98]Tno description
G3DSA:3.30.559.10\"[175-407]Tno description
G3DSA:4.10.320.10\"[101-154]Tno description
PTHR23151\"[2-378]TDIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED
PTHR23151:SF8\"[2-378]TDIHYDROLIPOAMIDE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX


","BeTs to 17 clades of COG0508COG name: Dihydrolipoamide acyltransferasesFunctional Class: CThe phylogenetic pattern of COG0508 is -o-p-zy--drlbcefghsn-jxi-wNumber of proteins in this genome belonging to this COG is","Significant hit ( 5e-90) to 5/5 blocks of the IPB001078 family, which is described as \"2-Oxo acid dehydrogenase acyltransferase catalytic domain\". Interpro entry for IP:IPR001078. IPB001078A 22-54 5.2e-21 IPB001078B 117-147 3.1 IPB001078C 233-254 1.2e-10 IPB001078D 308-350 1.1e-29 IPB001078E 369-405 3.2e-23Significant hit ( 1.2e-21) to 2/2 blocks of the IPB000089 family, which is described as \"Biotin / Lipoyl attachment\". Interpro entry for IP:IPR000089. IPB000089A 270-289 4e-09 IPB000089B 324-343 5.9e-11Significant hit ( 6.4e-15) to 1/1 blocks of the IPB003016 family, which is described as \"2-oxo acid dehydrogenases acyltransferase component lipoyl binding site\". Interpro entry for IP:IPR003016. IPB003016 25-59 6.3e-15","Residues 309 to 369 match (2e-09) PD:PD510107 which is described as TRANSFERASE SUCCINYL DIHYDROLIPOAMIDE ","","","","","","","","","","","","Wed Jan 22 12:44:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02704 is paralogously related to AA01986 (1e-46).","","","","","","Residues 175 to 405 (E-value = 2.8e-146) place AA02704 in the 2-oxoacid_dh family which is described as 2-oxoacid dehydrogenases acyltransferase (catalytic domain) (PF00198)","","","","","Spencer ME, Darlison MG, Stephens PE, Duckenfield IK, Guest JR.Nucleotide sequence of the sucB gene encoding the dihydrolipoamide succinyltransferase of Escherichia coli K12 and homology with the corresponding acetyltransferase.Eur J Biochem. 1984 Jun;141(2):361-74.PMID: 6376124Zygmunt MS, Díaz MA, Teixeira-Gomes AP, Cloeckaert A.Cloning, nucleotide sequence, and expression of the Brucella melitensis sucB gene coding for an immunogenic dihydrolipoamide succinyltransferase homologous protein.Infect Immun. 2001 Oct;69(10):6537-40.PMID: 11553602Nguyen SV, To H, Yamaguchi T, Fukushi H, Hirai K.Characterization of the Coxiella burnetti sucB gene encoding an immunogenic dihydrolipoamide succinyltransferase.Microbiol Immunol. 1999;43(8):743-9.PMID: 10524791Spencer ME, Guest JR.Transcription analysis of the sucAB, aceEF and lpd genes of Escherichia coli.Mol Gen Genet. 1985;200(1):145-54.PMID: 3897791","","Wed Jan 22 12:44:00 2003","1","","","" "AA02705","1886857","1886988","132","ATGTTTATTCCTTTTTATGTTCGTTTAGCTAAGTCTTATATTTTGATGAAAAGTGCGGTCGGTTTTCGCCGCGTTTTTTTCGCACAAAAACGCTGTGAAAAATCACCGCACTTTATCGCCTCATTAACGTGT","","","5172","MFIPFYVRLAKSYILMKSAVGFRRVFFAQKRCEKSPHFIASLTC","1886988","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 16:03:57 2004","Mon Feb 23 16:03:57 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02705 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 16:03:57 2004","","","","","","","","","","","","","1","","","" "AA02706","1889787","1886983","2805","ATGCAGCATAATTCTTTACAGGAATGGCTTGCCTCCAGTGCGTTGGGTGGCGCGAATCAAGCGTATATCGAAGAGCTTTATGAAAGTTATCTTGAGGATCCGGGCAGTGTGGATAGCAGCTGGCAGGCGATTTTTAAAACGCTGCCAAAATCCACCGCACTTGAGCAACCCCATTCGATCGTGCGTGATTATTTCCGCCGTTTAGCCCGAGAGAATCATTCGCAGAGTACTGCCGTTATCGACCCCGAAGCGAGTGCGAAATTAGTCAAAGTACTCCAGTTTATCAATGCTTATCGCTCCCGTGGTTATATTGAAGCCACCCTTGACCCCCTCAATTACTACCGTTGGAAAACCTCCTCTGTTCCAGAGCTAGATTATCATCAACATGGCTTAACCGATGCCGATTTGGACGAAAGTTTCAATATTGACTATGCCGTTTACGGCAAAGAAACCATTAAACTCAGCGACTTAGCCCGTGATTTAAAAGCCACTTATTGCGGCAATATCGGCTTGGAGTTTATGCATATTCACGATATGGAACAGCGTAACTGGTTACAAAATAAACAGGAAAAATGGATTCAACAGCCGCTTTTTACGAAAGACGAAAAAGTGAATTTGCTTAAAGAATTGACGGCGGCGGACGGCTTAGAACGTTATTTAGGGGCAAAATTCCCGGGAGCAAAACGTTTTTCGTTAGAGGGTAGCGATGCCTTTATTCCGATGATGAAAGAGATCATTCGTCATGCCGGACGTAACGACATCGATGACATTGTTATTGGTATGGCGCACCGTGGGCGTTTAAATATGTTGGTGAACGTGCTGGGTAAAAAACCGGCGGAGTTATTCGATGAATTTGCCGGTAAACACGCGGAAACCAATCGCACCGGTGATGTGAAGTATCACCAAGGGTTTTCTTCCGATTTTGCGGTGGATGACAAACGGGTGCATTTAACCCTAGCGTTTAACCCGTCCCATTTGGAAATCGTCAGCCCGGTGGTTATCGGTTCCGTGCGCGCCAGACAAACTCGCAAACAGGATTTGGAACATAACCAAGTGCTTGCCGTTACCGTGCATGGGGATTCCGCCGTGGCAGGGCAGGGCATCGTGCAGGAAACTTTGAATATGTCCAATGCGCGCGGTTACAAAGTGGGCGGCACAATTCGTATCGTCATTAATAACCAAATCGGTTTCACCACCTCCAACCCAAACGACACCCGTTCCACCGAATTTTGTACCGACATTGCGAAAATGATCCAGGCGCCGATTATTCATGTGAACGGTGACGATCCGGAAGCGGTGGTTTTCGCCGCGCGTATGGCGGTGGAATATCGCAACGCCTTCAAACGGGATATTTTCATTGATTTAATTTCCTATCGTCGTCACGGACACAATGAGGCGGACGAACCTTTGGCCACCCAGCCGATGATGTACGGTATCATCAAAAAACACCCGACACCGCCGAAAGTCTATGCTGCCCGTTTAATTCAGGAAGGCACCATCAGCGAAGAAGATGCCACCGAAATTACCAATTTATATCGCGATGCGCTGGATAACGGCGAATGCGTCGTGCCGGAATGGCGGGCTATGGATATGGCGAAAGTGGATTGGTTGCAATACCTCAATTATGACTGGACGGCGCCATACGAAAGCCATTTCCCGTTGGATCGTTTCCAAACCTTGGCGAAACGGGTTTCCCATTATCCTGATTACGTGCAGCCGCATCCGCGTGTGGAAAAAATCTATGCAGATCGGAAAGAAATGGCACAAGGCGATAAATTATTGGATTGGGGCATGGCGGAAACCATGGCGTACGCCACCTTGTTGGATGAAGGCACTAATGTACGTTTGTCCGGTGAGGATGCGGGACGCAGTACGTTCTTCCATCGTCATGCGGTCGTGCACAACCAAAAAGACGGCACCGGTTATGTGCCGTTGACCCAATTACACGCCAACCAAGGGCGCTTTGAAGTGTGGGATTCCGTGCTGACCGAGGAAGGTGTGCTTGCCTTTGAATACGGCTATGCCACAACGGATCCGAAAACGTTGACCATCTGGGAAGCACAGTTCGGTGATTTCGCCAACGGTGCGCAAATCGTGATTGACCAATTCATTAGCTCCGGTGAACAAAAATGGGGCAGAATGTGCGGCTTGGTGATGTTGCTGCCGCACGGTTATGAAGGGCAAGGCCCGGAACACTCTTCCGCCCGCCTGGAACGCTATTTGCAACTCTGCGCGGAACAAAATATGCAGGTGTGTATCCCGTCAACGCCAGCGCAGGTTTATCACATGTTGCGCCGTCAAGCGATCCGCAAAATGCGTCGTCCGCTCATCGGTATTTCGCCTAAATCCCTATTGCGTCACCCGCTTGCGGTGTCCACGATGGACGAACTGGTGAACGGTACTTTCCAAACCGTCATCGGCGAAATTGATGAACTCGATCCGAAACAGGTCAAGCGCGTGGTGATGTGTTCGGGCAAAGTGTATTACGATTTGTTGGAACAACGCCGTAAAAACGAGCAAACAGACGTCGCGATTATCCGTATCGAACAACTTTATCCGTTCCCGCACGATGATGTGAAAGCGGTGCTTGCGCCTTATGCTCATGTGACGGATTTTGTGTGGTGTCAGGAAGAACCGCTGAACCAAGGCGCGTGGTATTCCAGCAAACACAATTTTGAAGCGGTTATTCCGGAAGGGGCGAAATTAACCTATGCCGGTCGCCCGGCCTCTGCCTCTCCAGCGGTGGGCTATATATCATTGCACACCAAACAACAAAAACAATTGGTGGAAGACGCGTTAACACGT","","","109131","MQHNSLQEWLASSALGGANQAYIEELYESYLEDPGSVDSSWQAIFKTLPKSTALEQPHSIVRDYFRRLARENHSQSTAVIDPEASAKLVKVLQFINAYRSRGYIEATLDPLNYYRWKTSSVPELDYHQHGLTDADLDESFNIDYAVYGKETIKLSDLARDLKATYCGNIGLEFMHIHDMEQRNWLQNKQEKWIQQPLFTKDEKVNLLKELTAADGLERYLGAKFPGAKRFSLEGSDAFIPMMKEIIRHAGRNDIDDIVIGMAHRGRLNMLVNVLGKKPAELFDEFAGKHAETNRTGDVKYHQGFSSDFAVDDKRVHLTLAFNPSHLEIVSPVVIGSVRARQTRKQDLEHNQVLAVTVHGDSAVAGQGIVQETLNMSNARGYKVGGTIRIVINNQIGFTTSNPNDTRSTEFCTDIAKMIQAPIIHVNGDDPEAVVFAARMAVEYRNAFKRDIFIDLISYRRHGHNEADEPLATQPMMYGIIKKHPTPPKVYAARLIQEGTISEEDATEITNLYRDALDNGECVVPEWRAMDMAKVDWLQYLNYDWTAPYESHFPLDRFQTLAKRVSHYPDYVQPHPRVEKIYADRKEMAQGDKLLDWGMAETMAYATLLDEGTNVRLSGEDAGRSTFFHRHAVVHNQKDGTGYVPLTQLHANQGRFEVWDSVLTEEGVLAFEYGYATTDPKTLTIWEAQFGDFANGAQIVIDQFISSGEQKWGRMCGLVMLLPHGYEGQGPEHSSARLERYLQLCAEQNMQVCIPSTPAQVYHMLRRQAIRKMRRPLIGISPKSLLRHPLAVSTMDELVNGTFQTVIGEIDELDPKQVKRVVMCSGKVYYDLLEQRRKNEQTDVAIIRIEQLYPFPHDDVKAVLAPYAHVTDFVWCQEEPLNQGAWYSSKHNFEAVIPEGAKLTYAGRPASASPAVGYISLHTKQQKQLVEDALTR","1886981","","2-oxoglutarate dehydrogenase E1 component (decarboxylase component)","Cytoplasm","","
InterPro
IPR001017
Domain
Dehydrogenase, E1 component
PF00676\"[208-535]TE1_dh
InterPro
IPR005475
Domain
Transketolase, central region
PF02779\"[592-788]TTransket_pyr
InterPro
IPR011603
Family
2-oxoglutarate dehydrogenase, E1 component
PIRSF000157\"[1-934]T2-oxoglutarate dehydrogenase, E1 component
PTHR23152\"[348-933]T2-OXOGLUTARATE DEHYDROGENASE
TIGR00239\"[14-933]T2oxo_dh_E1: 2-oxoglutarate dehydrogenase, E
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.970\"[168-539]Tno description


","BeTs to 12 clades of COG0567COG name: Pyruvate and 2-oxoglutarate dehydrogenases, E1 componentFunctional Class: CThe phylogenetic pattern of COG0567 is ------y--dr-b-efghsn-jxi--Number of proteins in this genome belonging to this COG is","","Residues 353 to 445 match (7e-21) PD:PD000580 which is described as COMPLETE PROTEOME THIAMINE SYNTHASE PYROPHOSPHATE FLAVOPROTEIN SUBUNIT PYRUVATE DEHYDROGENASE TRANSKETOLASE ","","","","","","","","","","","","Wed Jan 22 12:47:28 2003","","Thu Sep 23 15:09:14 2004","","Thu Sep 23 15:09:14 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02706 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Sep 23 15:09:14 2004","","","","","Residues 594 to 788 (E-value = 1.1e-72) place AA02706 in the Transket_pyr family which is described as Transketolase, pyridine binding domain (PF02779)","Thu Sep 23 15:09:14 2004","","","","Darlison MG, Spencer ME, Guest JR.Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate dehydrogenase of Escherichia coli K12.Eur J Biochem. 1984 Jun;141(2):351-9.PMID: 6376123The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 2. Molecular cloning and sequence analysis of the gene encoding the succinyltransferase component.Eur J Biochem. 1990 Jan;187(1):235-9.PMID: 2404760Park SJ, Chao G, Gunsalus RP.Aerobic regulation of the sucABCD genes of Escherichia coli, which encode alpha-ketoglutarate dehydrogenase and succinyl coenzyme A synthetase: roles of ArcA, Fnr, and the upstream sdhCDAB promoter.J Bacteriol. 1997 Jul;179(13):4138-42.PMID: 9209026","","Thu Sep 23 15:09:14 2004","1","","","" "AA02707","1889779","1889991","213","ATGCTGCATAAATACCACCTTAAAAATGAACACACTAACAAACAACGTCATGGCAACGACATAAAAAATACCGTTACATTTGAAAGGCATATTATGCCCGAGAAATTCAATTTATATTGTGATCCAAGTCAGAATTTTTACAAAAATTTAACGTATTCACGCCATAAAGTGCGGTCAAAAAAATCAGCGATTTTCAATTTCAATTTTACTAAC","","","8685","MLHKYHLKNEHTNKQRHGNDIKNTVTFERHIMPEKFNLYCDPSQNFYKNLTYSRHKVRSKKSAIFNFNFTN","1889991","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 16:02:27 2004","Mon Feb 23 16:02:27 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02707 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 16:02:27 2004","","","","","","","","","","","","","1","","","" "AA02708","1890701","1890066","636","ATGAATATTGAAATTATTCCCGTCACCGCATTTCAACAAAATTGTTCGTTAATTTGGGATGATAAGAAAAATGCGGCAATTATTGATCCCGGCGGCGAAGCGGATAAATTAATCAAACGAATTGAAGAATTAGGCTTGAATTTACAGGCGATTTTACTCACTCATGGGCATTTGGATCATGTGGGCGCGGCGGAAAAAGTCAAACAACAGTTTAATGTGCCCATCCTCGGTTCAAATTCCAAAGATGATTATTGGTTTAAGGGCTTGCCGCAACAATCGGAAAAATTCGGGATGTTGTTTGAAGTCGCCGCCTTTGAACCGGATCGTTGGTTGGATAAAGAAGGCGAAATTTTAACTATCGGCGATTTTACCTTTGAAGTTCTGCATTTACCGGGACACACGCCGGGGCATATCGGTTTTATCGAACATCAAAAACGTGTGGCGTTTACCGGTGATGTGTTATTTAAAAGTGGCATCGGGCGCACGGATTTTCCGGGCGGCAGTTATGACGAGATTATTGCTTCTATTCGGGAAAAATTATATCGGTTGGGTGATGATATGATTATTGTTCCGGGACACGGACCTTACACAACCATCGGTATAGAAAAACAAATCAATCCTTATGTGAAGCAGGAA","","","23725","MNIEIIPVTAFQQNCSLIWDDKKNAAIIDPGGEADKLIKRIEELGLNLQAILLTHGHLDHVGAAEKVKQQFNVPILGSNSKDDYWFKGLPQQSEKFGMLFEVAAFEPDRWLDKEGEILTIGDFTFEVLHLPGHTPGHIGFIEHQKRVAFTGDVLFKSGIGRTDFPGGSYDEIIASIREKLYRLGDDMIIVPGHGPYTTIGIEKQINPYVKQE","1890064","","probable glyoxalase II family protein","Cytoplasm","","
InterPro
IPR001279
Domain
Beta-lactamase-like
PF00753\"[12-193]TLactamase_B
noIPR
unintegrated
unintegrated
G3DSA:3.60.15.10\"[8-212]Tno description
PTHR11935\"[106-212]TBETA LACTAMASE DOMAIN
PTHR11935:SF8\"[106-212]TBETA LACTAMASE DOMAIN


","BeTs to 22 clades of COG0491COG name: Zn-dependent hydrolases, including glyoxylasesFunctional Class: RThe phylogenetic pattern of COG0491 is aompkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 2.6e-05) to 1/6 blocks of the IPB001587 family, which is described as \"Uncharacterized protein family UPF0036\". Interpro entry for IP:IPR001587. IPB001587B 31-79 2.4e-05","Residues 27 to 75 match (6e-07) PD:PD364615 which is described as COMPLETE PROTEOME HYDROLASE METALLO-BETA-LACTAMASE SUPERFAMILY DEPENDENT YCBL METAL VICX FUNCTION ","","","","","","","","","","","","Wed Jan 22 12:56:37 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02708 is paralogously related to AA01878 (2e-11).","","","","","","Residues 12 to 193 (E-value = 7.6e-39) place AA02708 in the Lactamase_B family which is described as Metallo-beta-lactamase superfamily (PF00753)","","","","","","","","1","","","" "AA02710","1891339","1890782","558","ATGAGCAATATTAACCATAGTCGTCGCAAATGGTTATCTTTAGGGGGAATTGTATTGGGTGCAACTTTGTTGCCTGATACGGTTTTAGCTGTGGTTTCAACGCCAAGGCCCCGTATGTTGAGCTTTCGCAATATTAATACCCAAGAGAAATTAAGCGCGGAATTCGTGCTTGGTCGCGGGTTTTCCAATACGACATTACGACTGTTAGATCATTTACTGCGTGATAAGCGCAATAATCAAGTACATAAAATGGACCCGCAGCTTTTTACTAAGTTTTATCGGGTTCAGCAAAATCTCGGTTTACGCAACACCGAAATCCAAATTATCTGCGGTTATCGTTCCGCTGCCAGCAATGCGGCAATGCACCGTCGCAGCCGTGGTGTCGCCAGCAATAGTTATCATATCCGTGGTCAAGCCATTGACTTCCGCATTGACGGCGTTCCGTTAGCGAAGTTACGCAACGCGGTGGAAGCGTTAAATGACGGTGGCGTCGGTTTCTATCCGCGCAGTAACTTCATTCACATGGATACCGGCCCTGTCCGTACCTGGAGAGGAAGT","","","20971","MSNINHSRRKWLSLGGIVLGATLLPDTVLAVVSTPRPRMLSFRNINTQEKLSAEFVLGRGFSNTTLRLLDHLLRDKRNNQVHKMDPQLFTKFYRVQQNLGLRNTEIQIICGYRSAASNAAMHRRSRGVASNSYHIRGQAIDFRIDGVPLAKLRNAVEALNDGGVGFYPRSNFIHMDTGPVRTWRGS","1890780","","conserved hypothetical protein","Periplasm, Extracellular","","
InterPro
IPR010275
Family
Protein of unknown function DUF882, bacterial
PF05951\"[32-183]TPeptidase_M15_2
noIPR
unintegrated
unintegrated
signalp\"[1-30]?signal-peptide
tmhmm\"[12-32]?transmembrane_regions


","BeTs to 3 clades of COG3108COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3108 is --------------e-gh---j----Number of proteins in this genome belonging to this COG is","","Residues 1 to 35 match (3e-08) PD:PD587362 which is described as PROTEOME COMPLETE TRANSMEMBRANE PM0271 EXPORTED HI1666 ","","","","","","","","","","","","Wed Jan 22 12:57:52 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02710 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 32 to 183 (E-value = 7.1e-91) place AA02710 in the DUF882 family which is described as Bacterial protein of unknown function (DUF882) (PF05951)","","","","","","","","1","","","" "AA02711","1892912","1891407","1506","ATGAATACGAAATCTTTTAAGTTGACCGCATGGACGTTAGCTATGGCGTTCTATGTGGGGAATGCGGTTGCGGAAGAAACGAAGCCTTCGGAGGCTGCCACGGAGCAAACTCAGGCACAAACTGATTTAGGTTTGGTGCAGCAACTGGCTTTAGAAAATAAAGCGGAAGAAGAGCGTCTTGCCGTCGAGAAAAAAAACGAAGAGGTACGTTTGGCAGCAGAGAAACAAGTACTGGCGGAGCAAGGTTTAGCTGAACGCATCGGTGAAACGGAACTGCAATTTAAACCGTTAATCGCAAAAATTTATGCGGAAAATAATTTTATGCCGCTGTGGCAGGATGAAGAAGCCAAACAACAGTTCTTGCGTGATTATGCGTTAATGGTGGCAAGCGGCATTTCCAAGCGTTCTGCCAACGTCTTAAATGCAGTAAGCCAGTCTGCCGATAAAGAAGCATTTGTGCAAGATGTTATCTTGACCGATGTGTTTTTAGATTATCTGTTTTATGCCAATAATGTGAAGAAATTTGCGCAAAAATGGTTATATTCGGAAAATAGCTACAAAGCAGGTAAACCGGACGAAAACCAGGTCGATTCCTGGCTAAGTGCGGTCAAAAATAATGATGTTTTTGCTTTCGTGAATAACTTATCCGGTGAAAATCCATTATTTAAGCAGACGTTAGCCAAGGTAGAAAATTTAATCCTAAACGGCAAATTAGATAAAAACGGTATTAATGAATTGTATCGTTTAGCGATCAACGCACAGCGTTTGCGTATTTTGCCTGAACTCGATAACGGGATTTTCGTGAATATTCCGAGTTATCAATTGAATTACTACCGTGACGGCAAACTGGTTTTGAATTCCCGCGTGATTGTGGGTACCGATAAACGCAAAACGCCGGTTATGTTCAGCCGTCTGAGCAATGTGGTGGTTAATCCGCCTTGGAATGCGCCAACCCGTTTAATTAACGAGGACATCATTCCGAAAGTGCGCCGGGATCCAAGTTACATTTATCGTAATGGTTATACGATCATCGACGGCAAAGGCAATACCATTGACCCTTATACCATTGACTGGGAAAACATGACGGCGAAGAAGTTCCCATATCGTTTGCGTCAGGTACCAAGCGACAATAGCGCATTGGGCAACTATAAATTTAATATGCCGAGTTCCGACGCTATTTATTTGCACGATACACCAAAACGTAGCTTATTCGGTAATAAAAGACGTGATTTAAGCTCCGGTTGTGTGCGTGTTGAAAAATCCGAAGAATTGGCAACAGTTTTGTTAAAGGAAGCGGGTTGGACGGCGGAAAGAAAACAAAGTGTACTGAAAAGCAGAAAAACGACGTCTGTAACTGTTAAATCCAATAACCCGGTTTTCTTATATTACGTCACTGCATGGGTTGATAAAGAGCAAGTACACACCTTGCCGGATGTTTATGGCTATGACAAAGCACCCAATCTGAGCTATATTGACTGGGACATTTTGAAAAAATATATTCAGCCT","","","57243","MNTKSFKLTAWTLAMAFYVGNAVAEETKPSEAATEQTQAQTDLGLVQQLALENKAEEERLAVEKKNEEVRLAAEKQVLAEQGLAERIGETELQFKPLIAKIYAENNFMPLWQDEEAKQQFLRDYALMVASGISKRSANVLNAVSQSADKEAFVQDVILTDVFLDYLFYANNVKKFAQKWLYSENSYKAGKPDENQVDSWLSAVKNNDVFAFVNNLSGENPLFKQTLAKVENLILNGKLDKNGINELYRLAINAQRLRILPELDNGIFVNIPSYQLNYYRDGKLVLNSRVIVGTDKRKTPVMFSRLSNVVVNPPWNAPTRLINEDIIPKVRRDPSYIYRNGYTIIDGKGNTIDPYTIDWENMTAKKFPYRLRQVPSDNSALGNYKFNMPSSDAIYLHDTPKRSLFGNKRRDLSSGCVRVEKSEELATVLLKEAGWTAERKQSVLKSRKTTSVTVKSNNPVFLYYVTAWVDKEQVHTLPDVYGYDKAPNLSYIDWDILKKYIQP","1891405","","conserved hypothetical protein","Periplasm, Outer membrane","","
InterPro
IPR002052
Domain
N-6 Adenine-specific DNA methylase
PS00092\"[308-314]?N6_MTASE
noIPR
unintegrated
unintegrated
signalp\"[1-24]?signal-peptide


","BeTs to 3 clades of COG2989COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG2989 is --------------e-gh---j----Number of proteins in this genome belonging to this COG is","","Residues 60 to 229 match (7e-45) PD:PD043098 which is described as PROTEOME COMPLETE TRANSMEMBRANE EXPORTED YCBB PM0270 VC1268 PERIPLASMIC HI1667 AMIDASE ","","","","","","","","","","","","Wed Jan 22 13:02:35 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02711 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02712","1895047","1892993","2055","ATGAAATTTATGAAAACAAAAAGCTATCTGACCGCACTTGTATTAACTTCCTTTTTGCTTAATGTCAATATTGCGGACGCGGTACAACCGAAATTAAAACAAAGTGATCTGGTCTCTTTACAGCCGTCGGAATCCAACATGTTTGCCACGAAACGTGCGACAACCCGCCTAACTCAGTCTCATTACCGTAGATTTCAGCTGGATGATGAATTTTCGAAAAAGATTTTTGATCGTTACCTTAAAGCGTTGGATTTTAACCGTACGACGTTTTTGCAATCCGATATTGATGAAATGTTCACTAAATATGGCAATAAAATTGATGACGAGTTGAATGCAGGTAATTTAGATATTGCTTTTAATATGTATGAGTTAATGATGAAACGCCGTTATGAACGTTATCGTTATGCCTTGTCTTTGCTGGATAAAGAACCGCATTTGAACGATGATGATCAAATTGAAATTGATCGTGAAAAAGCAGCCTGGCCGAAAACCGAAAAAGAAGCGAATAAGTTATGGGAAGCGCGCGTTAAAAACGACATCATCAGCTTGAAATTAAAAGATAAAAAATGGTCGGAAATTAAAGATAAATTAGTTAAGCGTTATAATTTGGCGATTCGTCGCTTAACCCAAACTAAAGCGGATGATGTGGTACAAACCTATTTAAACGCTTTTGCCCGTGAAATTGATCCACATACCAGTTATTTAGCCCCACGTACGGCAAAAAGTTTCAATGAAAGCATGAATTTATCTTTAGAAGGGGTCGGTGCCACATTGCAAACCGAGGATGGTGAAACCAGTATTAAATCTTTAGTTCCGGGAGCGCCTGCCGAACGCAGTAAAAAATTAAAAGCAGGTGATAAAATTATCGGTGTTGGTCAGGAGAAAGGCGAAATCGAGGATGTTGTCGGTTGGCGTCTGGAAGACATCGTTGACAAAATCAAAGGGAAAAAAGGCTCTAAAGTCCGTTTGGAAGTGGAACCGGCAAAAGGCGGAAAATCCCGTATTGTGACATTGGTTCGCGATAAAATTCGTATTGAAGATCAAGCGGCGAAATTAACCGTTGAAAAAGTTGACGGCATCAATGTTGCCGTGATTAAAATTCCAAGCTTCTACCTCGGTTTAACGGAAGACGTGAAAAAATTATTGGTAGAAATGAAGAACAAAAAAACCGCTGCGTTAATCGTGGATTTACGGGAAAACGGTGGCGGTGCGTTGACCGAAGCGGTCGGTTTAAGCGGCTTATTCATTAGCGATGGGTCTGTAGTGCAAGTGCGAGACGCCTATCAACGTATTCGTGTACACGAAGATCCGGACAATATGCAACAATATACCGGTCCGTTATTGGTGATGATTAACCGTTTCAGTGCTTCCGCGTCGGAAATTTTTGCCGCCGCGATTCAGGATTACAACCGCGGCATTATTATCGGACAAAATACCTATGGAAAAGGCACGGTCCAACAAAGTCGTTCACTCAATTTTGTGTATGACTTGGATCAAACTCCGCTCGGCTTAATTCAATATACCATTCAAAAATTCTATCGTATTAATGGCGGAAGCACCCAATTAAAAGGCGTTGCACCGGATATTAAATTCCCGTATGTGATCGATGCGCAAGAATATGGTGAAGAAAAAGAGGATAACGCCTTGCCTTGGGATAAAATTCCGTCGGTCAATTATTCCGAAGTGATGACGGCGCGTGATTTTGTTTCCGAGTTGACTAAAAAACACAAAGAAAGAATCGCGAAAAATCCGGAATTTATTGCTTTAAACGAGGATTTAAAGATTCGTGACGAGCGCCGTGATCGTAAGTTCTTATCTTTGAATTATCAAAAACGCAAAGCGGAAAACGATAAGGACGACGAAAAACGTTTGAAAGATATTAATGAGCGCTTTAAACGTGAAGGTAAGAAACCGTTAAAAGACATTAATGACTTACCGAAAGATTACGAAGCCCCGGATTTCTTTCTGAAAGAAGCAGAATTCATTGCTGCAGATGTCGTAAAATTTGATGCGGAAAAAACCGGACTGAAAGACGCGGATACCTCTGCAAAGCCG","","","78225","MKFMKTKSYLTALVLTSFLLNVNIADAVQPKLKQSDLVSLQPSESNMFATKRATTRLTQSHYRRFQLDDEFSKKIFDRYLKALDFNRTTFLQSDIDEMFTKYGNKIDDELNAGNLDIAFNMYELMMKRRYERYRYALSLLDKEPHLNDDDQIEIDREKAAWPKTEKEANKLWEARVKNDIISLKLKDKKWSEIKDKLVKRYNLAIRRLTQTKADDVVQTYLNAFAREIDPHTSYLAPRTAKSFNESMNLSLEGVGATLQTEDGETSIKSLVPGAPAERSKKLKAGDKIIGVGQEKGEIEDVVGWRLEDIVDKIKGKKGSKVRLEVEPAKGGKSRIVTLVRDKIRIEDQAAKLTVEKVDGINVAVIKIPSFYLGLTEDVKKLLVEMKNKKTAALIVDLRENGGGALTEAVGLSGLFISDGSVVQVRDAYQRIRVHEDPDNMQQYTGPLLVMINRFSASASEIFAAAIQDYNRGIIIGQNTYGKGTVQQSRSLNFVYDLDQTPLGLIQYTIQKFYRINGGSTQLKGVAPDIKFPYVIDAQEYGEEKEDNALPWDKIPSVNYSEVMTARDFVSELTKKHKERIAKNPEFIALNEDLKIRDERRDRKFLSLNYQKRKAENDKDDEKRLKDINERFKREGKKPLKDINDLPKDYEAPDFFLKEAEFIAADVVKFDAEKTGLKDADTSAKP","1892991","Tsp is said to attack C-termini bearing nonpolar residues (Beebe et al., 2000).","tail specific protease precursor","Periplasm, Cytoplasm","","
InterPro
IPR001478
Domain
PDZ/DHR/GLGF
PF00595\"[242-326]TPDZ
SM00228\"[252-329]TPDZ
PS50106\"[254-314]TPDZ
InterPro
IPR004447
Family
Peptidase S41A, C-terminal protease
TIGR00225\"[200-552]Tprc: C-terminal processing peptidase
InterPro
IPR005151
Domain
Peptidase S41
PF03572\"[361-531]TPeptidase_S41
SM00245\"[331-532]TTSPc
noIPR
unintegrated
unintegrated
G3DSA:2.30.42.10\"[252-329]Tno description
G3DSA:3.90.226.10\"[338-557]Tno description
PTHR11261\"[390-533]TINTERPHOTORECEPTOR RETINOID-BINDING PROTEIN
signalp\"[1-27]?signal-peptide
tmhmm\"[9-27]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 3.2e-19) to 2/3 blocks of the IPB003581 family, which is described as \"Tail specific protease\". Interpro entry for IP:IPR003581. IPB003581B 394-403 0.0044 IPB003581C 452-481 1.6e-14","Residues 92 to 179 match (2e-07) PD:PD062829 which is described as PROTEOME COMPLETE SUBUNIT FORMATE IRON-SULFUR COMPONENT HYDROGENASE HYDROGENLYASE F ELECTRON ","","","","","","","","","","","Wed Jan 22 13:05:41 2003","Wed Jan 22 13:05:41 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02712 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 359 to 533 (E-value = 8.2e-36) place AA02712 in the Peptidase_S41 family which is described as Peptidase family S41B (PF03572)","","","","","Beebe KD, Shin J, Peng J, Chaudhury C, Khera J, Pei D.Substrate recognition through a PDZ domain in tail-specific protease.Biochemistry. 2000 Mar;39(11):3149-55.PMID: 10715137","","Wed Jan 22 13:05:41 2003","1","","","" "AA02713","1895729","1895124","606","ATGACAGAAATACAAAAGTTAACAAATAATAAAGAGATTATTGCTTATTTAGCGGAAAAATTTCCGCTATGTTTTTCTATTGAGGGGGAAGCCAAACCGTTAAAAATCGGTTTGTTTCAGGATTTAAGCGAAGCGCTGAAAGATGACGAGCGCGTAAGCAAAACCCAACTCCGTCACGCCTTGCGTCAATATACTTCAAACTGGCGTTACCTACACGGCTGCAAAGCCGGTGCAATGCGCGTGGATTTACAGGGTAATCCGGTGGGGGAACTGGAGCAAGAACATGCTGATCATGCCGCGCAACAATTAGCGGAAGCTAAAGCCTTAATTGCCCAAAAACGTGCGGCGGAAAAAGCGGCAAAAGGCGAAAATGAGAAAAAACGCTCTGTCCGTCGCAATCAGAAGCAAGGTGAAAAGCATGCCCGTAAACCTAATTTTAATTTCAATAACGTGGATATGGCGATGTTGCAGGTCGGTCAGCAGGTAAAAGTCAAAGCAGCTGACCATGCGAAAAACGCCACCATTTTGGAAATTTCCGGCGATGCCGCCAGGGTGGAATTGGAAAACGGTTTGGTGATTACTGTCACGGCAGATCGTTTATTTGCC","","","23164","MTEIQKLTNNKEIIAYLAEKFPLCFSIEGEAKPLKIGLFQDLSEALKDDERVSKTQLRHALRQYTSNWRYLHGCKAGAMRVDLQGNPVGELEQEHADHAAQQLAEAKALIAQKRAAEKAAKGENEKKRSVRRNQKQGEKHARKPNFNFNNVDMAMLQVGQQVKVKAADHAKNATILEISGDAARVELENGLVITVTADRLFA","1895122","From H. ducreyi record HD1009:The function of this protein is not exactly known.It may be astructural element that influences the osmotic activation of propat a posttranslational level.","possible prop effector homolog","Cytoplasm","","
InterPro
IPR007447
Family
ProQ activator of osmoprotectant transporter ProP
PF04352\"[1-156]TProQ


","BeTs to 4 clades of COG3109COG name: Activator of osmoprotectant transporter ProPFunctional Class: TThe phylogenetic pattern of COG3109 is --------------efgh--------Number of proteins in this genome belonging to this COG is","","Residues 142 to 202 match (1e-10) PD:PD349785 which is described as PROP COMPLETE PROTEOME EFFECTOR PROQ ACTIVATOR INFLUENCES ACTIVATION OSMOTIC HOMOLOG ","","","","","","","","","","","Wed Jan 22 13:07:49 2003","Wed Jan 22 13:07:49 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02713 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 169 (E-value = 5.9e-77) place AA02713 in the ProQ family which is described as ProQ activator of osmoprotectant transporter ProP (PF04352)","","","","","Kunte HJ, Crane RA, Culham DE, Richmond D, Wood JM.Protein ProQ influences osmotic activation of compatible solute transporter ProP in Escherichia coli K-12.J Bacteriol. 1999 Mar;181(5):1537-43.PMID: 10049386","","Wed Jan 22 13:10:10 2003","1","","","" "AA02714","1895947","1897227","1281","ATGACAGCACATTCCAAGTTAAATTTGGCCGACGCTACTTTTCATCGCCTCGTTCGTTGCGGTGAATGCAATGCCGTGGTTAAAATTTCTGCATTACAACGAGGGCAACGTGCCCTTTGTCCGCGCTGCCAGAATGTGTTATATGCCACCAGCCGCTGGAGTTTAAAACGCTGTTCGATTATCGCCATCTCTATTTTAATCCTGATGCCTTTCGCTTTAACTTACCCGCTTTTAAGCATAGATTTATTAGGCGAAAAAATTGACGCCTCGGTCTGGCTGGGCGTGTGGAAAATGGCGACACAAGGTTTTTCTTACACTGCATTTTTAGTGTTTCTTTGCGCCGTGTTTATGCCCATTGCCTTTGCGCTGCTGGTTATTCTGCTGCGGCTGTCACAGATCATGCACATAAAACCACGCAATTTGTTGATTTCCCTCAGTTATATTAAACCCTGGGTGATGTTTGACGTGTATTTGGTGGCATTGGGCGTGAGCATTTTCAAAGTGCAGGAGTACGCCACATTAGAACTGAATATTTACTTAATCGCTTTTATTTTTACCGCACTTTTAACCACGCTCTTGTTTATTAAAATTAACCCCGACGAAGTGTGGAACGATTTTTACCCGCAAAGCAAAGCGGTCAATAATCTCACGCATACGGAAGATTTACGTTATTGTCATTCCTGCCAATATAGCTTTATTAATCCGCTCACCGATCGCAAAGGGCGCGAAATCTGTCCGCGTTGCTATTCGCAAATTGATTTGCCAAACGCCATTAAATTACAACGCACCTGGGCGCTATTAATTGCGGGTATTATCATGCTGTTTCCGGCAAATTTATTGCCGATGTCGGTGATTTATTTAAACGGTGCGCCAAGTACGGACACCTTAATGTCGGGCGTGATCAGCTTTATTGATATGGGCAGTTACTTCATTGCTTTTGTGGTATTTACCGCCAGTATTTTCGTGCCCATTAGCAAAGTGTTGATTATGTTGTACCTGCTCACCTGCATACACTTTAAACTGAAACATTCTATTCGCTGGCAAATGCGTTTGTTGCATATCGTGCATTTCGTCGGACGCTGGTCAATGCTTGATTTATTCGTATTGGCACTGATGATGTCTTTGGTTACCCGAGGGCAGATTATCGACTTTTCTGTAGGTACAGCGGCGCTCTATTTCGGCGCGGCGGTATTTTTGACAATGATTGCAGCGGAGCAATTTGACAGCCGCTTAATTTGGGAAATCTATGACAGACAACAAGCAAAACACGCAACATCAAAA","","","48608","MTAHSKLNLADATFHRLVRCGECNAVVKISALQRGQRALCPRCQNVLYATSRWSLKRCSIIAISILILMPFALTYPLLSIDLLGEKIDASVWLGVWKMATQGFSYTAFLVFLCAVFMPIAFALLVILLRLSQIMHIKPRNLLISLSYIKPWVMFDVYLVALGVSIFKVQEYATLELNIYLIAFIFTALLTTLLFIKINPDEVWNDFYPQSKAVNNLTHTEDLRYCHSCQYSFINPLTDRKGREICPRCYSQIDLPNAIKLQRTWALLIAGIIMLFPANLLPMSVIYLNGAPSTDTLMSGVISFIDMGSYFIAFVVFTASIFVPISKVLIMLYLLTCIHFKLKHSIRWQMRLLHIVHFVGRWSMLDLFVLALMMSLVTRGQIIDFSVGTAALYFGAAVFLTMIAAEQFDSRLIWEIYDRQQAKHATSK","1897225","","paraquat-inducible protein PqiA homolog","Inner membrane, Cytoplasm","","
InterPro
IPR005219
Family
Conserved hypothetical protein 155
TIGR00155\"[5-415]TpqiA_fam: integral membrane protein, PqiA f
InterPro
IPR007498
Family
Paraquat-inducible protein A
PF04403\"[9-210]T\"[214-420]TPqiA
noIPR
unintegrated
unintegrated
signalp\"[1-74]?signal-peptide
tmhmm\"[58-78]?\"[105-127]?\"[148-166]?\"[172-194]?\"[265-287]?\"[306-337]?\"[358-378]?\"[384-404]?transmembrane_regions


","BeTs to 4 clades of COG2995COG name: Uncharacterized paraquat-inducible protein AFunctional Class: SThe phylogenetic pattern of COG2995 is --------------e-gh-n------Number of proteins in this genome belonging to this COG is","","Residues 20 to 174 match (4e-10) PD:PD353661 which is described as PROTEOME COMPLETE PARAQUAT-INDUCIBLE A MEMBRANE PQIA INNER FAMILY TRANSMEMBRANE INTEGRAL ","","","","","","","","","","","","Wed Jan 22 13:09:47 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02714 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 214 to 420 (E-value = 2.1e-98) place AA02714 in the PqiA family which is described as Paraquat-inducible protein A (PF04403)","","","","","","","","1","","","" "AA02715","1897193","1899847","2655","ATGACAGACAACAAGCAAAACACGCAACATCAAAATAATGAAACGGAAGTCAACGCGCAGGTGCGTCAAAACCGGCGTATTTCGCCATTTTGGTTGTTACCTTTCATCGCCCTGTGTATCAGTGCCATTTTGTTCTTCCAAATTGTGCAGGAACAGGGTATCAGCGTAAAAATCACTTTTACCAACGGTGACGGTATCGTTGCCGGCAAAACACAAATTCGCTACCAAGGTTTGCAAATCGGGGTAGTAAAGAAGGTGAATTTCACCGATGATCTGCAAAAAGTGGAAGTGGTAGCCAATATTTACCCTGAGGCCAAAACCGTCTTACGGGAAAACACCAAATTCTGGCTGGTGAAACCAAGTGCATCCCTTGCCGGGATTTCAGGCTTAGATGCATTGGTTTCAGGTAATTACATCACCTTACAACCGGGCGGGGGGGACACCGAACATGAATTCATGGCAGAAACGAAAGGCCCTATAGCACAGCTTACTCCGGGTGATTTACTGATTCATTTAATTGCCGATGATTTGGGCTCTATTTCAATCGGTGCATCTATCTATTACAAAAAGATACCCGTGGGTCGAATCTATGATTTCCATTTCACCGAAGACGGCAAAAAAGTGGAAATTGATGTGGTCATCAATAAGCCTTACGCCAAATTTGTCAAAAAAGACAGCCATTTCTGGAATATCAGCGGCATCAGCGCCAGCATTGACGTTTCCGGTTTAAACGTTAACGTAGACAGCCTTAATTCTGTGGTGCAAGGTGCTGCTGCTTTTGATTCGCCAAACAACAGCCCGGCAGCGGAAATGAACGAAAGCTACACACTTTATTCCAACCTGCAAGCGGCAAAACGCGGTATCAACATTAATGTCAACCTTCCGAACACTGTCGGTTTGGTAGCAGGGAAAACCCACGTTTATTACCAAAATACCGAAATCGGCGTGTTATCCGAATTAAGTGCGGTAGAAAATAACGATGAAATGTTAAGTGGTACGTTATTAATTGATCCGAATCTTGCCAATTTGTTCAAAGCCAACAGCAACATTGTATTGCGCGTGAAAAAACCGGGTCTGGCAGATTTAACCGATGTACAAAAACTGCTACGCGGCAAATATTTTGAGGTGTTGCCGGGCGACGGTGAAAACCGAACGGATTTCGATGTGATTAAAGAAAGCGAGTTATTACTGAAACAGCCGAACACCTTAGTGCTGAATTTAACCGCACCGGAAACTTACGGTATCAACGAAGGACAACCGTTGATTTATAACAACATTCAAATCGGCGAAATTGTGTCTCAGCAAATTGATACCGGCGGCGTCAAATTCAAAGTCGCAATCGCCGGCGAGTATCGCCATTTAATTCACGGCGATACCCTATTTATCGCCGCCTCCAATTTTGAAGTGAGTTTGGGTGTTGACGGCTTACGTTTTGAAGCCGCCACACCGGAAAAATGGCTGCAAGGCGGCATTCGCGTGGTGGCGGGTAAAAATCAGGGCAAAGCAAAAGAAAGCTATACCCTTTACAGCGATTTAACCAACGCGGAAGCCGGCATTACCGACAACCGACCGCAACCTACCATCACGCTGACCACGTCCAATTTACCAAGTATTAACAAAGGCTCATTGGTGCTTTACCGCCAATATGAAGTGGGTAAAATTTTGGATATCCGTCCGCAAACCCAACATTTTGCCGTGGATGTGTTTATTTATCCGAAATACCGCTATTTATTGACGGACAAAAGCGTCTTCTGGGTGGAAAGTGCGGCGCAAATTGACATTACCCCGAAAGGCATCAGCATTCAGGCAACGCCCGCAGCACGTTCGTTAAAAGGCGCTATCAGCTTTGATAATAGCGGCGGTAAAGGCAACCATACCCTTTATCCGAACGAACTGCGCGCCAAGTCTGCAGAGCAACAAATCACCCTGACTGCCGAGGACGCCACTAACCTCAGCAAAGGCATGGCGTTACGTTATTTAGGCTTAACCATTGGTGAAATCGACAGCATTCAGCTTAATCAAAAGAGCAATAAAATCATCGCTAAAGCATTAATTAACCCGAATTACATGGCGCTAATCGCCAAAGAAGGCTCGCGCTTCAAAGTGATTTCACCGCAAATTTCCGCCGGCGGTATTGAAAATATCGACAGCTTATTGCAACCGTACATTGATGTGGAAGTGGGTTCCGGCAAAAGCAAAACACAATTTGCCTTAAGCCAATCCGTCAACAATAACATTAAATATACCAATGGGTTACCGCTTGTGCTGGAAACCAACGACGCGCTAAATATTACCGCGGGATCGCCGATTATGTATCGTGGCGTGGAAGTGGGAACCATTAAAAACTTAGAGCTGAATTCGTTGGGCGATCGGGTATTTATCAACATTCTTATCGCCCCGAAATATCAGCACCTCGTGCGCCAAAATTCCGAATTCTGGATCGCCTCCGGTTACGATTTCAACCTCGGCTGGTCCGGCGCCCAATTCAACACCGGCAGCGTACAACAGCTGTTAAAAGGCGGCATTTCCTTCTCTACGCCGTCAGGCACGGTGGTGCAAGGGCAGGTAAAAGCAAATCAGCATTTCTTATTGCAAGCCAAACGCCCGGAAAATGCACAGAAATGGAATCAAGGCGCGTTACCGGCAGCCAAAAAT","","","96692","MTDNKQNTQHQNNETEVNAQVRQNRRISPFWLLPFIALCISAILFFQIVQEQGISVKITFTNGDGIVAGKTQIRYQGLQIGVVKKVNFTDDLQKVEVVANIYPEAKTVLRENTKFWLVKPSASLAGISGLDALVSGNYITLQPGGGDTEHEFMAETKGPIAQLTPGDLLIHLIADDLGSISIGASIYYKKIPVGRIYDFHFTEDGKKVEIDVVINKPYAKFVKKDSHFWNISGISASIDVSGLNVNVDSLNSVVQGAAAFDSPNNSPAAEMNESYTLYSNLQAAKRGININVNLPNTVGLVAGKTHVYYQNTEIGVLSELSAVENNDEMLSGTLLIDPNLANLFKANSNIVLRVKKPGLADLTDVQKLLRGKYFEVLPGDGENRTDFDVIKESELLLKQPNTLVLNLTAPETYGINEGQPLIYNNIQIGEIVSQQIDTGGVKFKVAIAGEYRHLIHGDTLFIAASNFEVSLGVDGLRFEAATPEKWLQGGIRVVAGKNQGKAKESYTLYSDLTNAEAGITDNRPQPTITLTTSNLPSINKGSLVLYRQYEVGKILDIRPQTQHFAVDVFIYPKYRYLLTDKSVFWVESAAQIDITPKGISIQATPAARSLKGAISFDNSGGKGNHTLYPNELRAKSAEQQITLTAEDATNLSKGMALRYLGLTIGEIDSIQLNQKSNKIIAKALINPNYMALIAKEGSRFKVISPQISAGGIENIDSLLQPYIDVEVGSGKSKTQFALSQSVNNNIKYTNGLPLVLETNDALNITAGSPIMYRGVEVGTIKNLELNSLGDRVFINILIAPKYQHLVRQNSEFWIASGYDFNLGWSGAQFNTGSVQQLLKGGISFSTPSGTVVQGQVKANQHFLLQAKRPENAQKWNQGALPAAKN","1899845","","paraquat-inducible protein pqiB homolog","Outer membrane, Periplasm","","
InterPro
IPR001574
Family
Ribosome-inactivating protein
PS00275\"[691-707]?SHIGA_RICIN
InterPro
IPR003399
Domain
Mammalian cell entry related
PF02470\"[52-144]T\"[166-256]T\"[286-379]T\"[401-484]T\"[524-606]T\"[637-728]T\"[750-840]TMCE
noIPR
unintegrated
unintegrated
signalp\"[1-41]?signal-peptide
tmhmm\"[29-49]?transmembrane_regions


","BeTs to 5 clades of COG3008COG name: Paraquat-inducible protein BFunctional Class: RThe phylogenetic pattern of COG3008 is --------------efgh-n------Number of proteins in this genome belonging to this COG is","Significant hit ( 5e-06) to 1/4 blocks of the IPB003399 family, which is described as \"mce related protein\". Interpro entry for IP:IPR003399. IPB003399B 751-795 4.9e-06 IPB003399B 638-682 0.00086 IPB003399B 525-569 0.0072 IPB003399B 402-446 0.0091 IPB003399B 167-211 0.11","Residues 336 to 509 match (4e-11) PD:PD576521 which is described as PROTEOME COMPLETE VC1501 ","","","","","","","","","","","","Wed Jan 22 13:11:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02715 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02716","1901170","1899929","1242","ATGCAGGATTTATTATCTCAAGAACCCGTATTGGAGCGTTTTTTCAACTATGTGAGTTACGACACGCAATCCAAGCCCGGCGCCAAAGTTTCGCCCAGTACGGCAGGGCAGCTGGCATTAGCCAAACATTTGCAGCAGGAGCTTATCGCATTGGGTTTGCAAAATATTGAATTAAGCAAGCACGCCGTGCTTACCGCATTTTTGCCCTCCAATGTGGATCCTGATTCGCCGACCATCGGTTTGATTTCTCATTTAGACACCTCGCCCGAATGTAGCGGCAAGAACGTTCAGCCGGAATTGATTGAAAATTATCGCGGCGGTGACATCGCCCTTGGCATCGGCGAAGAGTTTATCAGCCCCGTGTATTATTCCTTCCTGCACCAATTAACGGGTAAAACCCTGATTGTGACCGACGGCAACACCTTATTAGGCGCGGATAACAAAGCAGGAATAGCGGAAATTATGACCGCACTTTATCGCCTAAAAACGGAAAATCTGCCCCATTGTAATATCCGTGTCGCTTTCACGCCCGATGAAGAAATCGGCTTAGGGATGCAGTTTTTCCCTTTTGAAGATTTCCCTTGCGATTGGGCCTACACTATTGATGGCGGCGCGGTGGGCGAGCTGGAATACGAAAACTTTAATGCCGCTTCCGCCAAAATCACATTTCACGGGCGCAATATTCACCCCGGCGCCGCTAAGAAAAAAATGGTGAATGCGCTGACCTTGGCGTGTGAGTTTCAAAATGCGTTTTCATCGGCGGAAACACCGGAAAATACCGAACAGCGCGAAGGTTTTTTCCATTTAAATCATTTTGCCGGCGACATTGAAAAAGTGGAATTGCATTACCTGATTCGTGATTTTGAATGGAATACCTTTGAACAGCGTAAACAATTCATCACGGCATTGGTGGAAAAATTCAATCGCGAAAAACGTTTACCGAAACCCATTGAGTTAATGATTTCCGACAGCTACAAAAATATGAACGAAACGGTGAAGAAAGTCCCTCAATCCATTGAATTGGCGGATTTGGCGATGCAACAATGCGGCGTTACCCCCAACCATAAATTGATTCGTGGCGGCACCGACGGCGCTTGGTTGGCGGAAAAAGGATTGGCTTGCCCGAACATTTTCACCGGCGGCTATAATTTTCACAGCAAACACGAATTGATTACCCTGGAGGGCATGAAAAACGCGGTGAACGTGATTGTCAAACTGGTCGAGCTGGCGGCTAAGGCGTCA","","","45940","MQDLLSQEPVLERFFNYVSYDTQSKPGAKVSPSTAGQLALAKHLQQELIALGLQNIELSKHAVLTAFLPSNVDPDSPTIGLISHLDTSPECSGKNVQPELIENYRGGDIALGIGEEFISPVYYSFLHQLTGKTLIVTDGNTLLGADNKAGIAEIMTALYRLKTENLPHCNIRVAFTPDEEIGLGMQFFPFEDFPCDWAYTIDGGAVGELEYENFNAASAKITFHGRNIHPGAAKKKMVNALTLACEFQNAFSSAETPENTEQREGFFHLNHFAGDIEKVELHYLIRDFEWNTFEQRKQFITALVEKFNREKRLPKPIELMISDSYKNMNETVKKVPQSIELADLAMQQCGVTPNHKLIRGGTDGAWLAEKGLACPNIFTGGYNFHSKHELITLEGMKNAVNVIVKLVELAAKAS","1899927","","peptidase T","Cytoplasm","","
InterPro
IPR001261
Family
ArgE/dapE/ACY1/CPG2/yscS
PS00758\"[79-88]TARGE_DAPE_CPG2_1
PS00759\"[144-182]TARGE_DAPE_CPG2_2
InterPro
IPR002355
Binding_site
Multicopper oxidase, copper-binding site
PS00079\"[380-400]?MULTICOPPER_OXIDASE1
InterPro
IPR002933
Family
Peptidase M20
PF01546\"[145-409]TPeptidase_M20
InterPro
IPR010161
Family
Peptidase M20B, tripeptide aminopeptidase
TIGR01882\"[7-413]Tpeptidase-T: peptidase T
InterPro
IPR011650
Domain
Peptidase M20, dimerisation
PF07687\"[211-315]TM20_dimer
noIPR
unintegrated
unintegrated
G3DSA:3.40.630.10\"[7-412]Tno description
PTHR11014\"[5-97]T\"[123-412]TPEPTIDASE M20 FAMILY MEMBER
PTHR11014:SF3\"[5-97]T\"[123-412]TPEPTIDASE T


","BeTs to 6 clades of COG2195COG name: Di- and tripeptidasesFunctional Class: EThe phylogenetic pattern of COG2195 is ---------d-lb-e-gh--uj--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 4.2e-12) to 3/3 blocks of the IPB001261 family, which is described as \"ArgE/dapE/ACY1/CPG2/yscS family\". Interpro entry for IP:IPR001261. IPB001261A 145-157 0.052 IPB001261B 171-180 0.0055 IPB001261C 371-387 0.0024","Residues 145 to 208 match (1e-13) PD:PD293379 which is described as PROTEOME COMPLETE SUCCINYL-DIAMINOPIMELATE DESUCCINYLASE HYDROLASE DEACETYLASE ACETYLORNITHINE DIPEPTIDASE BIOSYNTHESIS ZINC ","","","","","Tue Feb 18 14:07:39 2003","","","","","","","Wed Jan 22 13:23:04 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02716 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 14 to 412 (E-value = 1.3e-55) place AA02716 in the Peptidase_M20 family which is described as Peptidase family M20/M25/M40 (PF01546)","","","","","Savijoki K, Palva A.Purification and molecular characterization of a tripeptidase (PepT) from Lactobacillus helveticus.Appl Environ Microbiol. 2000 Feb;66(2):794-800.PMID: 10653753Lombardo,M.J., Miller,C.G. and Rudd,K.E.Physical mapping of the Escherichia coli pepT and potABCD genesJ. Bacteriol. 175 (23), 7745-7746 (1993)PubMed: 8244951Hakansson K, Broder D, Wang AH, Miller CG.Crystallization of peptidase T from Salmonella typhimurium.Acta Crystallogr D Biol Crystallogr. 2000 Jul;56 ( Pt 7):924-6.PMID: 10930847","","Tue Feb 18 14:07:39 2003","1","","","" "AA02717","1901259","1901372","114","TTGATATATAACAAATATCCGACTTTTTATGAAAAATCACTATTAATTGCTTTTCATTATGCCCTGATCGCTATATCATTAGCGTTCATTTTTACAGTCGCCGCCTGCATTTTG","","","4338","LIYNKYPTFYEKSLLIAFHYALIAISLAFIFTVAACIL","1901372","","hypothetical protein","Periplasm, Cytoplasm, Extracellular","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-36]?signal-peptide
tmhmm\"[15-37]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 16:00:56 2004","Mon Feb 23 16:00:56 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02717 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 16:00:56 2004","","","","","","","","","","","","","1","","","" "AA02718","1901434","1902549","1116","GTGGAAAATACAGTTCAAAACAAGCCAATTATCGAGCTTCGTTCCATTACTAAATCCTACGGTTCCAACACCATTATTAAAGCCTTCAATTTAACCATTAATAACGGTGAATTTTTGACAATTCTCGGCCCCTCCGGCTGCGGCAAAACAACGGTATTGCGTTTGCTTGCAGGCTTGGAAGAATTAGATTCGGGCAACATCATTTTAGACGGTGAAGACATCACCAACGTGCCGGCAGAGAAACGCCACGTTAACACCGTATTCCAAAGCTACGCACTTTTTCCGCACATGACCATCTTTGAAAACGTCGCTTTCGGTTTGCGTATGCAAAAAGTGCCGGAGGCGGAAATTAAACCGCGCGTGTTAGAAGCCCTACGCATGGTGCAATTAGAAGAAATGGCGGATCGTAAGCCGACCCAGCTTTCCGGTGGCCAGCAACAACGTATTGCCATTGCCCGGGCGGTTGTAAATAAACCTAAAGTGTTATTACTCGACGAATCCCTCTCCGCGTTGGACTACAAATTGCGTAAACAAATGCAATACGAACTGAAAGTGTTGCAGCGCCAGTTAGGTATCACATTTATTTTTGTAACCCACGATCAGGAAGAAGCGATTACCATGTCCGACCGTATTGTGTTGTTACGTAAAGGTAAAATCGCACAAGACGGTTCGCCGCGTGAAATTTACGAAGAACCTGCAAACCTGTTCGTCGCACGTTTTATCGGCGAAATTAATGTGTTTGATGCCACTGTGATTGAACGTAAATCGGAAAATGTGGTGTTGGCGAACGTGGAAGGTCGCGTTTGTGATATTTATACGGACATTCCGGTGAAAAAAGATCAGCAGCTTCAAGTGTTGCTTCGTCCCGAAGATATTGTAATTAAAGAACTTGACGAGCATGAACATTCCAAAGCCATTATCGGTCATATTATCGACCGCACTTATAAAGGCATGACCTTAGAATCCACCGTGGAATTTGAACAAAACGGCAAACGCGTGCTGGTCAGCGAATTCTTTAACGAAGATGATCCTCACATGGATCACAGTATTGGTCAACGTGTAGGCATTACATGGCACGAAGGTTGGGAGGTTGTACTCAACGATGAAGATAATCAA","","","42230","VENTVQNKPIIELRSITKSYGSNTIIKAFNLTINNGEFLTILGPSGCGKTTVLRLLAGLEELDSGNIILDGEDITNVPAEKRHVNTVFQSYALFPHMTIFENVAFGLRMQKVPEAEIKPRVLEALRMVQLEEMADRKPTQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQYELKVLQRQLGITFIFVTHDQEEAITMSDRIVLLRKGKIAQDGSPREIYEEPANLFVARFIGEINVFDATVIERKSENVVLANVEGRVCDIYTDIPVKKDQQLQVLLRPEDIVIKELDEHEHSKAIIGHIIDRTYKGMTLESTVEFEQNGKRVLVSEFFNEDDPHMDHSIGQRVGITWHEGWEVVLNDEDNQ","1902547","","spermidine/putrescine ABC transporter, ATP-binding protein","Cytoplasm, Inner membrane","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[140-183]TO85818_ACTAC_O85818;
PF00005\"[36-217]TABC_tran
PS50893\"[11-241]TABC_TRANSPORTER_2
PS00211\"[141-155]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[35-218]TAAA
InterPro
IPR005893
Family
Spermidine/putrescine ABC transporter ATP-binding subunit
TIGR01187\"[41-366]TpotA: polyamine ABC transporter, ATP-bindin
InterPro
IPR013611
Domain
Transport-associated OB
PF08402\"[285-366]TTOBE_2
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[5-250]Tno description
PTHR19222\"[11-313]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF43\"[11-313]TSPERMIDINE/PUTRESCINE ABC TRANSPORTER


","No hits to the COGs database.","Significant hit ( 1.5e-39) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 25-71 4.3e-19 IPB001140B 138-176 4.5e-16 IPB001140C 194-223 0.17","Residues 92 to 228 match (7e-07) PD:PD387048 which is described as ATP-BINDING 250AA PROTEOME COMPLETE III DICITRATE IRON LONG ","","","","","","","","","","","","Wed Jan 22 13:36:21 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02718 is paralogously related to AA00700 (5e-71), AA01645 (7e-65), AA01656 (3e-63), AA01051 (4e-55), AA01947 (3e-49), AA02353 (9e-44), AA01524 (7e-39), AA00415 (4e-38), AA00858 (8e-38), AA02440 (4e-33), AA01867 (1e-30), AA02899 (8e-30), AA02324 (1e-29), AA01779 (2e-29), AA02080 (7e-29), AA02140 (1e-28), AA01824 (2e-28), AA01684 (6e-28), AA01422 (7e-28), AA01616 (5e-27), AA02320 (6e-27), AA02805 (2e-24), AA00933 (2e-22), AA01820 (5e-22), AA01393 (8e-22), AA02152 (1e-21), AA02898 (3e-21), AA00799 (3e-21), AA01568 (2e-20), AA01961 (6e-20), AA02331 (2e-19), AA01456 (3e-19), AA02786 (2e-18), AA01510 (9e-18), AA00751 (2e-17), AA01509 (1e-16), AA00207 (2e-16), AA02609 (4e-16), AA02606 (1e-15), AA02225 (1e-15), AA02550 (4e-15), AA01757 (1e-14), AA00061 (1e-14), AA00591 (2e-14), AA02573 (5e-14), AA02484 (6e-14), AA01569 (6e-12), AA02642 (2e-11), AA00934 (6e-09), AA02146 (8e-08), AA02226 (1e-07), AA01555 (2e-07), A02145 (6e-06) and AA01291 (2e-04).","","","","","","Residues 36 to 217 (E-value = 7.2e-67) place AA02718 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Furuchi T, Kashiwagi K, Kobayashi H, Igarashi K.Characteristics of the gene for a spermidine and putrescine transport system that maps at 15 min on the Escherichia coli chromosome.J Biol Chem. 1991 Nov;266(31):20928-33.PMID: 1939142Kashiwagi K, Innami A, Zenda R, Tomitori H, Igarashi K.The ATPase activity and the functional domain of PotA, a component of the sermidine-preferential uptake system in Escherichia coli.J Biol Chem. 2002 Jul;277(27):24212-9.PMID: 11976340Kashiwagi K, Endo H, Kobayashi H, Takio K, Igarashi K.Spermidine-preferential uptake system in Escherichia coli. ATP hydrolysis by PotA protein and its association with membrane.J Biol Chem. 1995 Oct;270(43):25377-82.PMID: 7592703","","Wed Jan 22 13:36:21 2003","1","","","" "AA02719","1902536","1903393","858","ATGAAGATAATCAATAATAAATTCCAGAAAATTACTGTTGCGATTATCTTCAGCTGGCTAATCTTCTTCGTGCTGATCCCAAACTTATTGGTATTAGTCGTAAGTTTTTTAACCCGAGATGGTAGCAACTTTTATACCTTGCCATTTAACTTTGAAAACTACATCAACCTGTTTAATCCGCTTTATGCGCAGGTAGTGTGGAACTCATTGTATATGTCAATCATTGCCACCATTATTTGTTTACTAATCGGTTATCCGTTTGCCTTTATGGTCAGTAAAATTCACCCGAAATATCGACCGCTCTTATTGTTCCTTGTGGTGTTGCCGTTCTGGACAAACTCGCTTATTCGTATTTACGGCATGAAAGTGTTCCTCGGCGTGAAAGGCGTATTGAACACCATGTTATTGGAAATGGGTATTTTGAGTGAACCGATTCGGATTCTGAACACCGAAGTGGCGGTGATTATCGGTTTGGTGTATTTGCTTCTGCCGTTCATGATTCTGCCGCTCTACTCCGCCATTGAAAAGTTAGACGGACGCTTATTGGAAGCGGCAAAAGACTTGGGGGCAAACGCGTTCCAACGATTCTTCCGCGTGATTCTGCCGTTGACCATGCCGGGCATCGTTGCAGGCTGCTTGTTGGTATTATTGCCGGCAATGGGAATGTTTTATGTAGCGGACTTACTCGGCGGCGCGAAAGTGTTGCTTGTGGGTAACGTGATTAAGAGCGAATTCTTAATTTCCCGCAACTGGCCGTTCGGTTCCGCAATCAGTATCGGATTGACCATTTTGATGGCATTACTCATCTTCGTGTATTACCGCGCGAATAAATTATTGAACAAAAAAGTGGAGTTGGAA","","","32794","MKIINNKFQKITVAIIFSWLIFFVLIPNLLVLVVSFLTRDGSNFYTLPFNFENYINLFNPLYAQVVWNSLYMSIIATIICLLIGYPFAFMVSKIHPKYRPLLLFLVVLPFWTNSLIRIYGMKVFLGVKGVLNTMLLEMGILSEPIRILNTEVAVIIGLVYLLLPFMILPLYSAIEKLDGRLLEAAKDLGANAFQRFFRVILPLTMPGIVAGCLLVLLPAMGMFYVADLLGGAKVLLVGNVIKSEFLISRNWPFGSAISIGLTILMALLIFVYYRANKLLNKKVELE","1903391","","ABC-related spermidine/putrescine transport system permease","Inner membrane, Cytoplasm","","
InterPro
IPR000515
Family
Binding-protein-dependent transport systems inner membrane component
PF00528\"[66-285]TBPD_transp_1
PS50928\"[66-274]TABC_TM1
noIPR
unintegrated
unintegrated
signalp\"[1-35]?signal-peptide
tmhmm\"[15-37]?\"[69-89]?\"[101-121]?\"[152-172]?\"[199-219]?\"[253-273]?transmembrane_regions


","BeTs to 13 clades of COG1176COG name: ABC-type spermidine/putrescine transport system, permease component IFunctional Class: EThe phylogenetic pattern of COG1176 is ao---z--vd-l--efgh-nuj--twNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.4e-08) to 1/1 blocks of the IPB000515 family, which is described as \"Binding-protein-dependent transport systems inner membrane component\". Interpro entry for IP:IPR000515. IPB000515 183-202 2.4e-08","Residues 21 to 182 match (2e-07) PD:PD433883 which is described as COMPLETE PERMEASE SPERMIDINE/PUTRESCINE PROTEOME POTB SYSTEM TRANSMEMBRANE HOMOLOG ABC TRANSPORTER ","","","","","","","","","","","","Wed Feb 5 15:24:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02719 is paralogously related to AA01948 (5e-17), AA00699 (4e-13), AA01950 (8e-13), AA02720 (4e-11), AA01644 (1e-10), AA01780 (2e-09), AA00416 (3e-08), AA01650 (2e-07), AA02352 (3e-07), AA01050 (1e-06), AA01682 (1e-05) and AA01649 (1e-04).","","","","","","Residues 66 to 285 (E-value = 1.8e-18) place AA02719 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component (PF00528)","","","","","Furuchi T, Kashiwagi K, Kobayashi H, Igarashi K.Characteristics of the gene for a spermidine and putrescine transport system that maps at 15 min on the Escherichia coli chromosome.J Biol Chem. 1991 Nov;266(31):20928-33.PMID: 1939142","","Wed Jan 22 13:39:09 2003","1","","","" "AA02720","1903396","1904166","771","ATGAGCCGTTTACTACGCAATATTTTTATGTTTGTGGTATACGCTTATTTGTATATCCCGATTGTTATTTTAGTGACGAACTCTTTCAATTCAGACCGCTACGGTTTAAGTTGGAAAGGCTTCAGTTGGAACTGGTACGAGCGTTTATTTAACAACGACACCTTAATTCAGGCGGCGATTCACTCCGTTACCATAGCTTTTTTTGCAGCAACACTTGCGACCATCGTTGGCGGCTTAACGGCTATCGCGCTTTATCGTTATCGTTTCCGTGGCAAACAGGCGGTAAGCGGTATGTTGTTTATCGTGATGATGTCGCCGGATATCGTAATGGCGGTATCCTTACTCGCCTTATTTATGGTGGTGGGGATTTCCTTAGGTTTCTGGTCATTGCTTTTGGCACACGTAACTTTTTGTCTGCCTTACGTTACCGTCACCATTTTCTCCCGCTTAAACGGTTTTGACGCCAGAATGCTGGAAGCGGCGAAAGATTTGGGTGCAAGCGAAATCACCATTTTACGTAAAATCATCCTGCCGCTTGCCTTACCGGCGGTGGTGTCCGGTTGGTTGTTAAGTTTCACCATTTCACTGGATGACGTTGTGGTGTCCTCCTTTGTGAGCGGTGTCAGCTACGAAATCCTGCCGTTGCGTATCTTCTCCTTGGTGAAAACCGGAGTGACGCCGGAAGTGAATGCCCTTGCAACCATCATGATTGTGTTGTCATTATTACTAGTCATTGCCAGTCAATTTATTGGCAAGAAACACAAAGACATC","","","28508","MSRLLRNIFMFVVYAYLYIPIVILVTNSFNSDRYGLSWKGFSWNWYERLFNNDTLIQAAIHSVTIAFFAATLATIVGGLTAIALYRYRFRGKQAVSGMLFIVMMSPDIVMAVSLLALFMVVGISLGFWSLLLAHVTFCLPYVTVTIFSRLNGFDARMLEAAKDLGASEITILRKIILPLALPAVVSGWLLSFTISLDDVVVSSFVSGVSYEILPLRIFSLVKTGVTPEVNALATIMIVLSLLLVIASQFIGKKHKDI","1904164","","ABC-related spermidine/putrescine transport system permease","Inner membrane, Cytoplasm","","
InterPro
IPR000515
Family
Binding-protein-dependent transport systems inner membrane component
PF00528\"[55-257]TBPD_transp_1
PS50928\"[59-247]TABC_TM1
noIPR
unintegrated
unintegrated
signalp\"[1-28]?signal-peptide
tmhmm\"[10-30]?\"[65-85]?\"[95-127]?\"[133-153]?\"[174-192]?\"[198-218]?\"[230-250]?transmembrane_regions


","BeTs to 13 clades of COG1177COG name: ABC-type spermidine/putrescine transport system, permease component IIFunctional Class: EThe phylogenetic pattern of COG1177 is ao---z--vd-l--efgh-nuj--twNumber of proteins in this genome belonging to this COG is","Significant hit ( 6.3e-07) to 1/1 blocks of the IPB000515 family, which is described as \"Binding-protein-dependent transport systems inner membrane component\". Interpro entry for IP:IPR000515. IPB000515 159-178 6.4e-07","Residues 21 to 63 match (5e-07) PD:PD493771 which is described as COMPLETE PROTEOME PERMEASE PUTRESCINE ABC SYSTEM TRANSMEMBRANE TRANSPORTER POTI MEMBRANE ","","","","","","","","","","","","Wed Feb 5 15:24:53 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02720 is paralogously related to AA01950 (7e-18), AA01780 (3e-17), AA02719 (4e-11), AA01644 (9e-11), AA00699 (8e-09), AA01649 (1e-08), AA01948 (4e-07), AA01050 (1e-06), AA00416 (5e-06), AA01682 (9e-05) and AA02352 (8e-04).","","","","","","Residues 55 to 257 (E-value = 3.4e-10) place AA02720 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component (PF00528)","","","","","Pistocchi R, Kashiwagi K, Miyamoto S, Nukui E, Sadakata Y, Kobayashi H, Igarashi K.Characteristics of the operon for a putrescine transport system that maps at 19 minutes on the Escherichia coli chromosome.J Biol Chem. 1993 Jan;268(1):146-52.PMID: 8416922","","Wed Feb 5 15:24:53 2003","1","","","" "AA02721","1904261","1905394","1134","GTGGTTTTTTACCCCCTCTTTTACGGAGAACAAACAAAAATGAAAAAATTTGCCGGTTTATTCACCGCAAGTATGATCGCTGTTGCACTTACCGGTTGTAACGATAAAGACAACAAGCAAGCGCAAGCAACGCCGGAAGCCCCTAAAGCTGAAGCACCCGCAAATGATACCGTGTATCTTTACACTTGGACTGAATATGTACCGGATGGTCTTCTCGATGAATTCACCAAAGAAACCGGTATTAAAGTGATTGTTTCCAGTCTCGAATCCAACGAAACCATGTATGCAAAAATCAAAACCCAAGGTGCTGCCGGCGGTTATGATGTTATTGCGCCTTCCAACTACTTCGTGTCCAAAATGGCGCGCGAAGGCATGTTAAAAGAACTTGATCACAGCAAATTACCCGTCATTAAAGAATTAGACCCTGATTGGCTCGACAAACCTTACGACAAAGGCAACAAATATTCCCTTCCGCAATTATTAGGCGCTCCGGGCATTGCCTTTAACACTAACACTTACAAAGGCAGCGATTTCACCTCCTGGGGCGATTTATGGAAACCTGAATTTGCCAATAAAGTACAATTATTAGACGATGCCCGCGAAGTATTCAATATCGCGTTATTGAAAATCGGCCAGGATCCGAACACACAAGATCCGGCGATTATCAAACAGGCTTATGAAGAATTACTGAAATTACGTCCAAACGTGCTTTCTTTCAATTCCGACAACCCGGCAAACTCTTTCATTTCCGGTGAAGTGGAAGTCGGTCAATTATGGAATGGTTCCGTACGTATTGCGAAAAAAGAACAGGCACCTTTAGACATGGTGTTCCCGAAAGAAGGTCCGGTCCTTTGGGTAGATACCCTCGCGATTCCGGTTACTTCTAAAAACCCGGACGGCGCACACAAATTAATTAACTATATGTTGGGCGCAAAAGCGGCGGAAAAATTAACCTTAGCTATCGGCTATCCAACCGCTAACCTTGAAGCGAAAAAAGCCTTACCGAAAGAAATCACTGAAGATTCGGCGATTTACCCATCTGCCGACGTGCTACAAAAAAGCTACTGGCAAGATGATGTGGGCGACGCGATTCAATACTACGAGCAATATTATCAAGAGCTGAAAGCAGCGAAA","","","43777","VVFYPLFYGEQTKMKKFAGLFTASMIAVALTGCNDKDNKQAQATPEAPKAEAPANDTVYLYTWTEYVPDGLLDEFTKETGIKVIVSSLESNETMYAKIKTQGAAGGYDVIAPSNYFVSKMAREGMLKELDHSKLPVIKELDPDWLDKPYDKGNKYSLPQLLGAPGIAFNTNTYKGSDFTSWGDLWKPEFANKVQLLDDAREVFNIALLKIGQDPNTQDPAIIKQAYEELLKLRPNVLSFNSDNPANSFISGEVEVGQLWNGSVRIAKKEQAPLDMVFPKEGPVLWVDTLAIPVTSKNPDGAHKLINYMLGAKAAEKLTLAIGYPTANLEAKKALPKEITEDSAIYPSADVLQKSYWQDDVGDAIQYYEQYYQELKAAK","1905392","","spermidine/putrescine ABC transporter, periplasmic-binding protein","Periplasm","","
InterPro
IPR001188
Family
Bacterial periplasmic spermidine/putrescine-binding protein
PR00909\"[61-77]T\"[77-98]T\"[106-120]T\"[122-135]T\"[153-169]T\"[179-193]T\"[197-216]T\"[234-253]T\"[278-297]T\"[323-349]TSPERMDNBNDNG
InterPro
IPR006059
Family
Bacterial extracellular solute-binding protein, family 1
PF01547\"[17-315]TSBP_bac_1
InterPro
IPR011587
Domain
Prokaryotic extracellular metal-binding protein
PD008688\"[247-309]TQ98FT6_RHILO_Q98FT6;
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[162-302]Tno description
signalp\"[1-29]?signal-peptide


","BeTs to 13 clades of COG0687COG name: Spermidine/putrescine-binding periplasmic proteinFunctional Class: EThe phylogenetic pattern of COG0687 is ao---z--vd-l-cefgh-n-j--twNumber of proteins in this genome belonging to this COG is","Significant hit (2.2e-146) to 10/10 blocks of the PR00909 family, which is described as \"Bacterial periplasmic spermidine/putrescine-binding protein signature\". Prints database entry for PR:PR00909. PR00909A 61-77 3.8e-12 PR00909B 77-98 3.6e-17 PR00909C 106-120 3.9e-11 PR00909D 122-135 2.3e-09 PR00909E 153-169 9.4e-11 PR00909F 179-193 2.1e-11 PR00909G 197-216 1.4e-15 PR00909H 234-253 5.3e-14 PR00909I 278-297 1.4e-13 PR00909J 323-349 9.1e-19","Residues 190 to 240 match (2e-21) PD:PD402955 which is described as PROTEOME COMPLETE PERIPLASMIC ABC SPERMIDINE/PUTRESCINE-BINDING SPERMIDINE/PUTRESCINE TRANSPORTER POLYAMINE POTD PUTRESCINE-BINDING ","","","","","","","","","","","","Wed Jan 22 13:45:26 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02721 is paralogously related to AA01479 (3e-84), AA00698 (1e-07), AA01642 (1e-06) and AA00696 (1e-06).","","","","","","Residues 17 to 315 (E-value = 8.6e-28) place AA02721 in the SBP_bac_1 family which is described as Bacterial extracellular solute-binding protein (PF01547)","","","","","Furuchi T, Kashiwagi K, Kobayashi H, Igarashi K.Characteristics of the gene for a spermidine and putrescine transport system that maps at 15 min on the Escherichia coli chromosome.J Biol Chem. 1991 Nov;266(31):20928-33.PMID: 1939142Matsuo Y, Nishikawa K.Prediction of the structural similarity between spermidine/putrescine-binding protein and maltose-binding protein.FEBS Lett. 1994 May;345(1):23-6.PMID: 8194593","","Wed Jan 22 13:45:26 2003","1","","","" "AA02722","1905519","1906412","894","ATGTCATCCCACATTTCAGACAAGATTCAAGATGCTTTAGGCAAGATAGAACATTCCGTCTTGGCACAAGATATTTGGCATATTTTGCAAGAACAAAAATACCTCGGATTTCTACCGCACTTTGCCGTGCAACACCTGTGCAACAAACATCAACTCACGCCTAAACAGCTCGCGCTGAAACTCCTGCCTATCGCTGCCTGTTATGCCACCACGCCGATTTCACATTTTAATGTGGGTGCGGTTGTACATGGCATCGGTGGCGATTTTTATTTCGGTGCCAATCAGGAATTTTGCCAAACGGACATTCAACAAACTATTCATGCGGAACAAAGTGCCATTAGCCACGCTTGGATGCGCGGTGAAAAACAACTGACCGATGTCACGGTAAACTACACTCCGTGCGGGCATTGTCGCCAGTTTATGAATGAATTGAACAGTGCGGAAACGCTGCAAATTCACTTGCCGCATAGCCAAAATAATTTGTTGCACCAGTATTTGCCCGATGCGTTCGGTCCGAAAGATTTAAATATTCAGCTGAGTTTGCTGGATCAACACGATAACCAATTATCCCTAAATAACGACAATCCGTTGGTATTGCAAGCGCTCGCCATGGCAAATCAAGCCCATGCGCCCTATTCCAATTCTTTCCACGGCATTGCCATTCAAACCCGAAATCAGCAAATTTATCACGGCAGTTATGCGGAAAATGCCGCCTTCAATCCAAGCCTGCCGGCAATGCAGGTGGCATTAAATCATCTGATTTTAAGCGGTGAGGAGGTTGAGAATATCGTTCGCGTTGTGATGGTGGAAAAATCCAATACGCTCCATTACAAAGCCATGGCGGAAGAATTGCTCGGCACATTGAGCGACGTGAAATTAGACTATTTTGCCGTA","","","33302","MSSHISDKIQDALGKIEHSVLAQDIWHILQEQKYLGFLPHFAVQHLCNKHQLTPKQLALKLLPIAACYATTPISHFNVGAVVHGIGGDFYFGANQEFCQTDIQQTIHAEQSAISHAWMRGEKQLTDVTVNYTPCGHCRQFMNELNSAETLQIHLPHSQNNLLHQYLPDAFGPKDLNIQLSLLDQHDNQLSLNNDNPLVLQALAMANQAHAPYSNSFHGIAIQTRNQQIYHGSYAENAAFNPSLPAMQVALNHLILSGEEVENIVRVVMVEKSNTLHYKAMAEELLGTLSDVKLDYFAV","1906410","","cytidine deaminase","Cytoplasm","","
InterPro
IPR002125
Domain
CMP/dCMP deaminase, zinc-binding
PF00383\"[52-154]TdCMP_cyt_deam_1
PS00903\"[107-141]TCYT_DCMP_DEAMINASES
InterPro
IPR006263
Family
Cytidine deaminase, homodimeric
TIGR01355\"[34-298]Tcyt_deam_dimer: cytidine deaminase
InterPro
IPR013171
Domain
Cytidine and deoxycytidylate deaminase, zinc-binding region
PF08211\"[162-284]TdCMP_cyt_deam_2
noIPR
unintegrated
unintegrated
G3DSA:3.40.140.10\"[34-184]T\"[186-298]Tno description
PTHR11644\"[57-273]TCYTIDINE DEAMINASE


","BeTs to 12 clades of COG0295COG name: Cytidine deaminaseFunctional Class: FThe phylogenetic pattern of COG0295 is -o---zy-vdrlb-e-gh---j--twNumber of proteins in this genome belonging to this COG is","","Residues 162 to 272 match (2e-35) PD:PD021108 which is described as CYTIDINE DEAMINASE HYDROLASE PROTEOME COMPLETE AMINOHYDROLASE ZINC CDA CYTIDINE/DEOXYCYTIDINE CDD ","","","","","","","","","","","","Wed Jan 22 13:47:54 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02722 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 53 to 154 (E-value = 2.8e-20) place AA02722 in the dCMP_cyt_deam family which is described as Cytidine and deoxycytidylate deaminase zinc-binding region (PF00383)","","","","","Petersen-Mahrt SK, Harris RS, Neuberger MS.AID mutates E. coli suggesting a DNA deamination mechanism for antibody diversification.Nature. 2002 Jul;418(6893):99-103.PMID: 12097915Betts L, Xiang S, Short SA, Wolfenden R, Carter CW.Cytidine deaminase. The 2.3 A crystal structure of an enzyme: transition-state analog complex.J Mol Biol. 1994 Jan;235(2):635-56.PMID: 8289286Xiang S, Short SA, Wolfenden R, Carter CW.Cytidine deaminase complexed to 3-deazacytidine: a \"valence buffer\" in zinc enzyme catalysis.Biochemistry. 1996 Feb;35(5):1335-41.PMID: 8634261","","Wed Jan 22 13:47:54 2003","1","","","" "AA02723","1906513","1906403","111","TTGGCAAATCCGCGAAATAATCTGAAATATTTGTGGGTGCGTTGGCACCCACATTTTCTATCCACCCTTAAAAAAATGTCGTCAAAATCCACCGCACTTTATACGGCAAAA","","","4384","LANPRNNLKYLWVRWHPHFLSTLKKMSSKSTALYTAK","1906403","","hypothetical protein","Cytoplasm, Extracellular","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:58:49 2004","Mon Feb 23 15:58:49 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02723 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:58:49 2004","","","","","","","","","","","","","1","","","" "AA02724","1907810","1906497","1314","ATGATCGATCCGAATTTATTACGCAATAATCCGGCGGACGTCGCTGAAAAATTAAAAATTAAACGCGGTTTCGTGTTGGATACGGCAAAAATTACCCAATTAGAAGAACAACGCAAAGCGTTACAAGTTAAAACCGAAAATTTACAGGCGGAGCGTAATGCCCGTTCCAAAGCCATCGGTGCGGCAAAAGCCCGTGGTGAAGACATCGCCCCTTTATTGGCGGAAGTAGATCACATGGCGGAAGAATTGGAGCAGGGTAAAATTGAATTAGATAAAGTACAAAACGCTTTAAATGACATCGCTTTAAACATTCCGAATATTCCCGCCGATGAAGTGCCGTTAGGCAAAGACGATAGTGAAAATCTTGAAGTGTCCCGCTGGGGCGAACCGCGTAAATTCGATTTTGAAGTGAAAGATCATGTGACCCTAGGTGAAAATCTACAAGGCTTGGATTTTGCCGCAGCGGTGAAATTAACCGGTTCCCGTTTTGTGGTGATGAAAGGGCAAATTGCCAAATTACACCGCGCCATTGCGCAATTTATGTTGGATTTGCACACCGAACAACATGGTTACACTGAAGCCTACGTGCCTTATTTGGTCAACCATGACACCCTTTACGGCACAGGTCAGTTGCCGAAATTCGGCGAAGATTTATTCCACACTAAACCGTTGGAAGGACAAGATCCGAACGAAGTACAACGCACTTACGGCTTAATTCCGACGGCAGAAGTGCCTGTGACCAATTTGGTGCGTGGTGAAATTTTGGACGCGGAAAATTTACCGTTAAAAATGACCACACATACGCCGTGTTTCCGTTCCGAGGCGGGCTCTTATGGGCGTGATACGCGCGGCTTAATTCGTATGCACCAATTTGATAAAGTGGAATTGGTGCAAATCGTTGAACCGGAAAAATCCATGGAGGCGTTGGAAGAGTTAACCGGTCATGCGGAAAAAGTGTTGCAATTGCTCGGTTTGCCGTATCGTAAAGTGTTGCTTTGCACCGGTGACATGGGCTTCGGTTCCTGCAAAACCTACGATTTGGAAGTGTGGGTGCCTGCGCAAAACACCTATCGTGAAATTTCTTCCTGCTCCAATATGTGGGATTTCCAAGCCCGTCGTATGCAAGCCCGTTGCCGTTCAAAAGGCGACAAGAAAACCCGTTTGGTGCACACCTTAAATGGCTCGGGTTTGGCTGTGGGACGTACTTTGGTGGCGGTGTTGGAAAACTACCAAAACGCCGACGGTTCCATTACCGTACCGGAAGTCTTGCGTCCTTACATGGGCGGATTGGATGTGATTGGCAAATCCGCGAAA","","","48844","MIDPNLLRNNPADVAEKLKIKRGFVLDTAKITQLEEQRKALQVKTENLQAERNARSKAIGAAKARGEDIAPLLAEVDHMAEELEQGKIELDKVQNALNDIALNIPNIPADEVPLGKDDSENLEVSRWGEPRKFDFEVKDHVTLGENLQGLDFAAAVKLTGSRFVVMKGQIAKLHRAIAQFMLDLHTEQHGYTEAYVPYLVNHDTLYGTGQLPKFGEDLFHTKPLEGQDPNEVQRTYGLIPTAEVPVTNLVRGEILDAENLPLKMTTHTPCFRSEAGSYGRDTRGLIRMHQFDKVELVQIVEPEKSMEALEELTGHAEKVLQLLGLPYRKVLLCTGDMGFGSCKTYDLEVWVPAQNTYREISSCSNMWDFQARRMQARCRSKGDKKTRLVHTLNGSGLAVGRTLVAVLENYQNADGSITVPEVLRPYMGGLDVIGKSAK","1906495","","seryl-tRNA ligase","Cytoplasm","","
InterPro
IPR002314
Domain
tRNA synthetase, class II (G, H, P and S)
PF00587\"[173-354]TtRNA-synt_2b
InterPro
IPR002317
Family
Seryl-tRNA synthetase, class IIa
PR00981\"[274-286]T\"[286-299]T\"[326-339]T\"[343-359]T\"[361-377]TTRNASYNTHSER
PTHR11778\"[100-433]TSERYL-TRNA SYNTHETASE
PF02403\"[1-108]TSeryl_tRNA_N
TIGR00414\"[1-427]TserS: seryl-tRNA synthetase
InterPro
IPR006195
Domain
Aminoacyl-transfer RNA synthetase, class II
PS50862\"[172-420]TAA_TRNA_LIGASE_II
noIPR
unintegrated
unintegrated
G3DSA:1.10.287.40\"[1-105]Tno description
G3DSA:3.30.930.10\"[106-429]Tno description


","BeTs to 26 clades of COG0172COG name: Seryl-tRNA synthetaseFunctional Class: JThe phylogenetic pattern of COG0172 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit (6.2e-161) to 9/9 blocks of the IPB003364 family, which is described as \"Seryl-tRNA synthetase N-terminal domain\". Interpro entry for IP:IPR003364. IPB003364A 1-10 0.0027 IPB003364B 104-128 6.2e-13 IPB003364C 140-177 1.5e-20 IPB003364D 190-221 2.8e-19 IPB003364E 234-261 1.2e-13 IPB003364F 270-295 3.4e-24 IPB003364G 341-378 1e-29 IPB003364H 388-415 8.9e-21 IPB003364I 419-428 4.1e-06","Residues 169 to 322 match (4e-07) PD:PD023780 which is described as LIGASE SYNTHETASE AMINOACYL-TRNA BIOSYNTHESIS SERINE--TRNA ATP-BINDING SERRS SERYL-TRNA PROTEOME COMPLETE ","","","","","","","","","","","","Wed Jan 22 13:50:03 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02724 is paralogously related to AA00896 (7e-04).","","","","","","Residues 162 to 327 (E-value = 1.6e-57) place AA02724 in the tRNA-synt_2b family which is described as tRNA synthetase class II core domain (G, H, P, S and T) (PF00587)","","","","","Hartlein,M., Madern,D. and Leberman,R. Cloning and characterization of the gene for Escherichia coli seryl-tRNA synthetase Nucleic Acids Res. 15 (3), 1005-1017 (1987) PubMed: 3029694 Vincent,C., Borel,F., Willison,J.C., Leberman,R. and Hartlein,M. Seryl-tRNA synthetase from Escherichia coli: functional evidence for cross-dimer tRNA binding during aminoacylation Nucleic Acids Res. 23 (7), 1113-1118 (1995) PubMed: 7537870 Leberman,R.,Hartlein,M. and Cusack,S. Escherichia coli seryl-tRNA synthetase: the structure of a class 2 aminoacyl-tRNA synthetase Biochim. Biophys. Acta 1089 (3), 287-298 (1991) PubMed: 1859832 ","","Wed Jan 22 13:51:15 2003","1","","","" "AA02726","1908118","1909782","1665","ATGGAGTTTTTATCTAACCTCAGCGAAGGCACGCAATTTGCTATTCAGCTTGCCATCGTCTTAATCTGTTTGTTCTACGGCGCGAAAAAAGGCGGTATTGCACTGGGTTTACTGGGCGGTATCGGTCTGATCGTATTGGTCTTCGGCTTTGGCATCGAACCGGGTAAACCGGCAATCGACGTTATGCTTACCATCCTCGCCGTGGTAGTCACATCCGCAACATTACAAGCCAGTGGCGGTTTGGACGTGATGTTGCAAATTGCAGAAAAACTACTGCGTAAAAATCCGAAATATGTGAGTATCCTCGCACCGTTCGTTACCTGTACCCTCACCATTCTTTGCGGTACCGGTCATGTGGTTTATACCATGCTGCCGATTATTTACGACATCGCCATCAAAAATAACATTCGTCCGGAACGTCCGATGGCGGCTAGTTCCATCGCTTCCCAAATGGGGATCATCGCGTCTCCGGTGTCCGTTGCGGTAGTGACCTTAACCGCGTTCTTGGTGAATGCACAAAATCACTTAGCCGGTTTCGACGGGTATTTGGATTTATTAAAAATCACCGTGCCATCTACGCTCTGCGGTGTGTTAGCCATCGGTATTTTCAGCTGGTTCCGTGGCAAAGATTTAGATAAAGACCAAGAGTTCCAAGAGAAGTTAAAAGATCCGGAATTCAAAAAATACGTGTACGGCGACAGCACTTCCCTACTCGACAAAAAATTACCGCAATCCAGCTGGAACGCCATGTGGATCTTCTTCGGTGCCATTCTTATCGTTGCTTTGCTGGGTTACTTTAAAGACTTGCGTCCGTCCTTTGAGAAAAGCGCACCGGCACAAGTGGTTGAAGTGGTTTCCGACAATAAAGCGGTACAAAGTTTCAACGTGAAAGAAGGCAAAATCGTTGCTATTGCAAAAGACAGCAAAGTGGCGCTTGATGTGAAAGACAGCAAAGCCAAAGCGCAAACTGCTTATGACAGTGTTGAAATTTACGACAACAAAGGCGTGTTGACACAAACTTTATCCGCACAAAATAACAATGTGGTTATCACCACCAGCGATAAAACAGACAGCATTGCCAACGCCACTATCGCGTTAAAAGATACCGCGAAGAAAAAAGTGACGTTAGGCATGGTTCACGTTATCCAAATTTTCATGTTGTTAGCCGGTTCATTAATCATCATCTTTACCAAAACCGATGCAAGCAAAATCAGTAAAAATGAAATCTTCCGTTCCGGTATGATTGCATTAGTTGCCGTCTTCGGAATCTCCTGGATGGCAGAAACCATGTTCACCGTCCATACCCCGATGATGAAAGCGGCATTAGGCGACATCGTGAAAGCCCACCCTTGGACTTACGCCGTGATGTTGTTATTAATCTCCAAATTCGTAAACTCACAAGCCGCCGCCTTGGTTGCCTTCGTGCCGTTGGCATTAAACATCGGCGTTGACCCGGCAATCATCCTTGCCTTCGCTGCCGCTTGTTACGGCTACTACATCTTACCGACCTACCCAAGTGACTTAGCAGCAATCCAATTCGACCGCTCTGGCACCACCCACATCGGTAAATTCGTTATCAACCACAGCTTTATCCTACCGGGCTTAATCGGTGTGATTACGTCCTGTATTTTCGGATATATCTTTACGGGAATGTTTGGGTATTTG","","","60646","MEFLSNLSEGTQFAIQLAIVLICLFYGAKKGGIALGLLGGIGLIVLVFGFGIEPGKPAIDVMLTILAVVVTSATLQASGGLDVMLQIAEKLLRKNPKYVSILAPFVTCTLTILCGTGHVVYTMLPIIYDIAIKNNIRPERPMAASSIASQMGIIASPVSVAVVTLTAFLVNAQNHLAGFDGYLDLLKITVPSTLCGVLAIGIFSWFRGKDLDKDQEFQEKLKDPEFKKYVYGDSTSLLDKKLPQSSWNAMWIFFGAILIVALLGYFKDLRPSFEKSAPAQVVEVVSDNKAVQSFNVKEGKIVAIAKDSKVALDVKDSKAKAQTAYDSVEIYDNKGVLTQTLSAQNNNVVITTSDKTDSIANATIALKDTAKKKVTLGMVHVIQIFMLLAGSLIIIFTKTDASKISKNEIFRSGMIALVAVFGISWMAETMFTVHTPMMKAALGDIVKAHPWTYAVMLLLISKFVNSQAAALVAFVPLALNIGVDPAIILAFAAACYGYYILPTYPSDLAAIQFDRSGTTHIGKFVINHSFILPGLIGVITSCIFGYIFTGMFGYL","1909780","From GenBank (gi:1169253): This protein is responsible for thetransport of C4-dicarboxylates from the periplasm accross the inner membrane. Belongs to the DcuA/DcuB family of transporters.","anaerobic C4-dicarboxylate transporter","Inner membrane, Cytoplasm","","
InterPro
IPR004668
Family
Anaerobic c4-dicarboxylate membrane transporter
PD014334\"[381-546]TQ9PPN0_CAMJE_Q9PPN0;
PF03605\"[16-485]TDcuA_DcuB
TIGR00770\"[16-553]TDcu: transporter, anaerobic C4-dicarboxylat
noIPR
unintegrated
unintegrated
signalp\"[1-31]?signal-peptide
tmhmm\"[10-28]?\"[33-51]?\"[61-81]?\"[101-121]?\"[153-173]?\"[188-208]?\"[246-266]?\"[376-396]?\"[415-437]?\"[458-476]?\"[482-502]?\"[530-550]?transmembrane_regions


","No hits to the COGs database.","","Residues 372 to 546 match (3e-72) PD:PD014334 which is described as COMPLETE PROTEOME ANAEROBIC C4-DICARBOXYLATE TRANSPORTER MEMBRANE INNER TRANSMEMBRANE DCUA DCUB ","","","","","","","","","","","Wed Jan 22 13:54:38 2003","Wed Jan 22 13:54:38 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02726 is paralogously related to AA01508 (4e-61).","","","","","","Residues 16 to 485 (E-value = 4.5e-225) place AA02726 in the DcuA_DcuB family which is described as Anaerobic c4-dicarboxylate membrane transporter (PF03605)","","","","","Six S, Andrews SC, Unden G, Guest JR.Escherichia coli possesses two homologous anaerobic C4-dicarboxylate membrane transporters (DcuA and DcuB) distinct from the aerobic dicarboxylate transport system (Dct).J Bacteriol. 1994 Nov;176(21):6470-8.PMID: 7961398Six S, Andrews SC, Roberts RE, Unden G, Guest JR.Construction and properties of Escherichia coli mutants defective in two genes encoding homologous membrane proteins with putative roles in anaerobic C4-dicarboxylic acid transport.Biochem Soc Trans. 1993 Nov;21(4):342S.PMID: 8131924","","Wed Jan 22 13:55:23 2003","1","","","" "AA02727","1909875","1909985","111","TTGGAGCGCTTTTTTCTGTTTATTGTTGAATTAATATCGCATTTCGCCGATGGCGACCTTCTTTCTTTTGCTTACCCAAAAGAAAGAAGGCAAAGAAAAAGGCACCCCGGA","","","4472","LERFFLFIVELISHFADGDLLSFAYPKERRQRKRHPG","1909985","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:57:20 2004","Mon Feb 23 15:57:20 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02727 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:57:20 2004","","","","","","","","","","","","","1","","","" "AA02728","1911622","1910285","1338","ATGTCTAACTTCAGCTTTGATTTCAACGAAAATGACTTTCGCCCGCTTGCTGCAAGAATGCGCCCCACCACCTTGGCGCAATATTGCGGTCAGTCTCATTTATTGGGCGAAGGAAAACCGTTGCGCAAAGCTATTGAAGCGGGATATGTTCATTCCATGATTTTCTGGGGCCCGCCCGGCACCGGTAAAACCACCTTGGCGGAAATTATCGCCCATCGCATTAATGTGGAAGTAGAGCGCATTTCCGCCGTCACCAGCGGCATTAAAGAAATCCGTGAAGCCATCGACAAAGCCAAACAAAACAAACTGGCAGGTTTGCGCACCATTTTGTTTGTAGATGAAGTGCATCGTTTCAACAAAAGCCAGCAAGACGCTTTCCTGCCGCATATTGAAGACGGCACCATTATTTTTATCGGCGCTACCACGGAAAATCCCTCTTTTGAACTCAATAACGCGTTGCTTTCCCGCGCGCGGGTTTATATTCTAAAACCGCTTTCCGCGCAGGAAATCGAACAGGTTTTACAACAAGCCATAGATGACCCCGAAAACGGTTTGGGTAAAGTGCGGTTAAATTTACAAGAGAATTTATTGTCCCTGTTGGCAGAATACGTCAATGGCGACGCCCGTCTTGCTTTGAACTGCCTGGAAATGATGGTGGACATGGCGGGCGAATCGGAAAACGGCAAAATTTTAGACCGCACTTTACTCACGGAAGTGTTGGGCGAACGGCAGGCGCGTTTTGATAAACAAGGTGACCTTTTCTACGATTTCATTTCCGCACTGCACAAATCCATTCGCGGATCCGCCCCTGATGCGGCGTTATACTGGTACGCGCGCATTATCACTGCCGGCGGGGATCCTCTTTATGTGGCACGTCGATTATTGGCAATTGCTTCCGAAGATGTGGGCAACGCCGACCCGCGCGCCATGCAGGTGGCACTTGCCGCCTGGGATTGTTTCACCCGCGTCGGCGCTGCCGAAGGCGAACGCGCTATTGCGCAAGCCATTGTGTATTTAGCCGTCGCACCGAAAAGCAACGCCGTTTATCTCGCTTTCAAAGCCGCCAAAAAATTGGCAACCGAATCCGCCGATTTCGACGTCCCTGAACATCTCCGCAACGCCCCGACCAGCTTCATGAAAGACCTCGGCTTCGGCGCCGAATACCGCTACGCCCACAATGAACCTAACGCCTACGCTGCCGGCGAAAACTACTTCCCGCCACAACTGAAAGACACCCAATTCTATTTCCCGACCACCAGAGGCATGGAAATTAAGATTAAGGAGAAGTTGGAATGGCTGCGGGGGTTAGATCAGGAAAGTGGTAAGAAGCGATATAAA","","","49716","MSNFSFDFNENDFRPLAARMRPTTLAQYCGQSHLLGEGKPLRKAIEAGYVHSMIFWGPPGTGKTTLAEIIAHRINVEVERISAVTSGIKEIREAIDKAKQNKLAGLRTILFVDEVHRFNKSQQDAFLPHIEDGTIIFIGATTENPSFELNNALLSRARVYILKPLSAQEIEQVLQQAIDDPENGLGKVRLNLQENLLSLLAEYVNGDARLALNCLEMMVDMAGESENGKILDRTLLTEVLGERQARFDKQGDLFYDFISALHKSIRGSAPDAALYWYARIITAGGDPLYVARRLLAIASEDVGNADPRAMQVALAAWDCFTRVGAAEGERAIAQAIVYLAVAPKSNAVYLAFKAAKKLATESADFDVPEHLRNAPTSFMKDLGFGAEYRYAHNEPNAYAAGENYFPPQLKDTQFYFPTTRGMEIKIKEKLEWLRGLDQESGKKRYK","1910283","","conserved hypothetical protein (possible ATPase)","Cytoplasm","","
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[49-165]TAAA
InterPro
IPR003959
Domain
AAA ATPase, core
PF00004\"[52-221]TAAA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[6-165]Tno description
PTHR13779\"[24-442]THOLLIDAY JUNCTION DNA HELICASE RUVB-RELATED
PTHR13779:SF1\"[24-442]TWERNER HELICASE INTERACTING PROTEIN


","No hits to the COGs database.","Significant hit ( 8.4e-09) to 2/8 blocks of the PR00819 family, which is described as \"CbxX/CfqX superfamily signature\". Prints database entry for PR:PR00819. PR00819B 52-67 2.4e-07 PR00819D 97-116 13","Residues 69 to 118 match (7e-07) PD:PD487017 which is described as PROTEOME COMPLETE NMA1433 NMB1258 ","","","","","","","","","","","","Wed Jan 22 14:03:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02728 is paralogously related to AA02501 (3e-10), AA02844 (4e-08), AA02289 (1e-04), AA00425 (9e-04) and AA01211 (0.001).","","","","","","Residues 52 to 221 (E-value = 1.1e-21) place AA02728 in the AAA family which is described as ATPase family associated with various cellular activities (AAA) (PF00004)","","","","","","","","1","","","" "AA02731","1912252","1911638","615","ATGAAAAAAACACTGCTAAAACTGACCGCACTTTCTTTGCTCGGGCTCTCTTCTGTGGTTTGGGCGAATGCCGATATTGAGCTGCAAAACCGCTTAAATAAAGTAGATGTGTTAAGTGCGGATTTCGCGCAAACCGTGAGTTCGGCGAACGGTAAAAACGTGCAACAGGGCAACGGAAAATTGCAAATCAAACGCCCGAATTTGTTCCGTATGGACACCAAAGCACCACAGGAAACCCAAATCATTGCCGACGGGCAAACCCTGTGGTTCTACGATCCTTTTGTGGAACAAGTCACCGCCAACTGGGTGAAAGATGCGGTGAATAATACCCCGTTCGTGTTGTTGACCAGCGGTGATAAAAGCCATTGGTCGCAATATACCGTGCAACAAAAAGACGACACGTTTGTGTTAACCCCGAAAGCGAAGAATAGCAACGTCAAACAATTTGATATTCGCATTGATTCAAACGGCGTATTAAAAGGCTTTAGTACCATTGAAAAAGACGGGCAGTCCAATCAGTATGTGCTGCGCAATATCACCAATCAAAATTTAGACGACGGATTGTTTAAATTCAGCGTACCGAAAGGTGTCGAATTGGACGACCAACGGAAAAAA","","","23022","MKKTLLKLTALSLLGLSSVVWANADIELQNRLNKVDVLSADFAQTVSSANGKNVQQGNGKLQIKRPNLFRMDTKAPQETQIIADGQTLWFYDPFVEQVTANWVKDAVNNTPFVLLTSGDKSHWSQYTVQQKDDTFVLTPKAKNSNVKQFDIRIDSNGVLKGFSTIEKDGQSNQYVLRNITNQNLDDGLFKFSVPKGVELDDQRKK","1911636","","outer membrane lipoprotein carrier precursor","Periplasm","","
InterPro
IPR004564
Family
Outer membrane lipoprotein carrier protein LolA
PF03548\"[33-192]TLolA
TIGR00547\"[1-204]TlolA: outer membrane lipoprotein carrier pr
noIPR
unintegrated
unintegrated
signalp\"[1-24]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","BeTs to 8 clades of COG2834COG name: Outer membrane lipoprotein-sorting proteinFunctional Class: MThe phylogenetic pattern of COG2834 is --------------efghsnujx-t-Number of proteins in this genome belonging to this COG is","","Residues 40 to 203 match (2e-41) PD:PD577925 which is described as PROTEOME COMPLETE LIPOPROTEINS PERIPLASMIC CARRIER OUTER-MEMBRANE SIGNAL PRECURSOR LIPOPROTEIN CHAPERONE ","","","","","","","","","","","","Wed Jan 22 14:06:32 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02731 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 202 (E-value = 7.7e-105) place AA02731 in the LolA family which is described as Outer membrane lipoprotein carrier protein LolA (PF03548)","","","","","Matsuyama S, Tajima T, Tokuda H.A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane.EMBO J. 1995 Jul;14(14):3365-72.PMID: 7628437","","Wed Jan 22 14:06:45 2003","1","","","" "AA02733","1915089","1912348","2742","ATGATTAAACATATTACCGAACATTTTTCGCCGAAGTATTACCTATTACATTTGCTGTTAGGATTGACCGCACTTTTCGGTTTGTATTTGATAATCGCCTGGTCGGGCTATACGCCGCTGGACAATTCTTGGGCGACCTCCGGCTTCGCGCCGGAAACCATCAACAAAGCGGGTGCGTTCGGTGCGTGGTTTGTGGATTTGTTTTTTGTATTTTTCGGTTATATCGGCAACCTGATCCCTTTCATTTTATTTTTTATCCCCATTTATTTAATTCGTTCCAAGCGGGTGGAAAATCTCACTTGGACTAAATTCGCATTGCGTTCATTCGGTTTCATTTTGTTGCTTTGCGGTTTAACCGTGCTTGCTACACTTTCACTGAATAACCCGCCCTCTTACCTTGCGGGAGGCGTGCTGGGCGGTAGTTTAACCCTGAATTTATACCCGAGTTTAGGCAAATTCGGCGTATCCTTACTGGCTGTGATTTTTGTGGCGGTGGGCTTTATTTTCTGTTCGGGCGCGTTTTTTATTCGTCTATTAATGAAATTCTACCGCTGGCTGACCATGCAAAATCCGCCTGAAGACCCGGAAAAAACCGACGAAACTGAAAGTGAGGAAACGCACATGGCAGAACCGCCGGAAGAGATCGTGATTGGGAAAACTCCGGCGCAGGAAGCGGTGGAGCAGCTTACGGAATTTGTCAATCCTGCGGATCGCATTAATATTTCCGGCTTATCAAAAGCGCAGGATATGTTTTATGTGCCGATGAATAATGGGAACGAGGTCAATGCTTTTGCACCGGAAAACCCTGAATTCGTTAAATACGATTTTGAGCAACAGGAAACCTTGCCGAATGTGAGTATTTCTATGCAGCGCGGTCAGACAGAATTGTCGACGCAACATGATTTCACTCCGGTATGGCAACAGACAAATGTCTTCGGTGAAGAGAAAAGTGCGGTTGATTTTGGCAGTAAATTTACGACGTCAGAAGACATGCCGAGCGTATCACTGGCTGAACCGGAAGTAAACGTGGCGGAGGAAGATCCTGAACAAAGCGAACTTGCCCGCCAATTTGCCGCGCAAGAGCAACAACGTTTGCGGGAAATGGAACGGCGCGCGAAAGACATGGGCGTGCAGGACGTCTATCAGCAAATTGTGCAGGGACCAACGGCGGAAACCGCACCTAAGACAGCTAATTATCGCCAGTATGGCGATTCCTTGATTCATCCGGCATTTCAGCAACATAAAAAGAACATCGAAAAACCGAAGACGCCGTTGCCGAGCCTGGATTTATTGGAACATCGTCCGACCCGCGAACAGGATATTACCCAAGCGGAAATTGTCGAAACCTCACAACGTATTGAACAACAATTGCGCAATTTCAATGTGAAAGCGAAAGTCAAAGATGTTTTAGTGGGGCCGGTGGTGACACGCTATGAATTGGAATTGGATCCGGGTGTGAAAGCCTCCAAAGTCACGGGATTGGATACGGATCTGGCACGCGCCCTGATGTTCCGTTCCATTCGTGTGGCGGAAGTGATTCCGGGCAAACCTTATATTGGTATCGAAACACCGAACGATCACCGTCAAATAGTACCATTGCGTGATGTGTTGGACAGCGATGAATTCCGCAATTCCAAAGCCTTACTTTCCATGGCGTTAGGTAAAGACATTAGCGGCAAACCAATGGTGGTGGATCTTGCTAAAATGCCGCATTTATTGGTGGCGGGCACCACGGGTTCCGGTAAATCCGTCGGCGTAAATACCATGATTTTAAGCCTGCTTTACCGCGTTAAACCGGAAGAAGTGAAATTCATCATGATTGACCCGAAAGTGGTGGAATTGTCTATTTATAATGATATTCCGCATCTTTTAACGGAAGTGGTCACGGACATGAAAAAAGCGGCAAACGCGTTGCGCTGGTGTGTAGACGAAATGGAGCGCCGTTATCAATTATTGTCTGCTTTGCGGGTGCGTAATATTGAAGGATTTAACGAGAAAGTTGATGAATATGAGGCCTTAAATATGCCGATTCCGAACCCGTTATGGAAGCCGGGCGATTCCATGGATACTTTGCCGCCACCATTAGAAAAACTGAGTTACATTGTGGTGATTGTGGATGAATTCGCCGATTTGATGATGGTGGCAGGCAAACAGGTGGAAGAGCTTATCGCACGTTTGGCGCAAAAAGCCCGTGCGGTGGGGATTCACTTAATTTTGGCAACCCAACGCCCTTCCGTAGATGTGATTACCGGTTTGATTAAAGCGAACGTACCGAGTCGAATTGCGTTTACTGTGGCGACTAAAATTGACTCGCGTACTATTCTTGATGCAGGCGGTGCGGAATCCTTATTGGGTAAAGGTGATATGCTGTATTCCCCACAGGGTTCTACCGAATTAGTCCGTATTCACGGTGCCTTTATGACTGATGACGAAGTCGTGCGCGTGGTAGATGATTGGAAAGCACGCGGTAAACCGAATTACATTGATGGTATTTTAGAGGGTGATGAAGAAGATGCCGGTGCGGAACGCTTAAGTGAGCGTGGCGGCGAAACCGACGGGTTGTTTGATGAAGTGGTAGAGTTTGTGGTCAGCACAGGCACCACGTCTATTTCTGCGATTCAACGCCGTTTCCGAGTAGGCTTTAACCGTGCCGCCAATATTATGGATCAGCTGGAAGAGCAGGGCATTGTTTCGCCGGTGCAAAACGGTAAACGTGAAGTGTTGGCGCGCAGTGCGGATTAT","","","102039","MIKHITEHFSPKYYLLHLLLGLTALFGLYLIIAWSGYTPLDNSWATSGFAPETINKAGAFGAWFVDLFFVFFGYIGNLIPFILFFIPIYLIRSKRVENLTWTKFALRSFGFILLLCGLTVLATLSLNNPPSYLAGGVLGGSLTLNLYPSLGKFGVSLLAVIFVAVGFIFCSGAFFIRLLMKFYRWLTMQNPPEDPEKTDETESEETHMAEPPEEIVIGKTPAQEAVEQLTEFVNPADRINISGLSKAQDMFYVPMNNGNEVNAFAPENPEFVKYDFEQQETLPNVSISMQRGQTELSTQHDFTPVWQQTNVFGEEKSAVDFGSKFTTSEDMPSVSLAEPEVNVAEEDPEQSELARQFAAQEQQRLREMERRAKDMGVQDVYQQIVQGPTAETAPKTANYRQYGDSLIHPAFQQHKKNIEKPKTPLPSLDLLEHRPTREQDITQAEIVETSQRIEQQLRNFNVKAKVKDVLVGPVVTRYELELDPGVKASKVTGLDTDLARALMFRSIRVAEVIPGKPYIGIETPNDHRQIVPLRDVLDSDEFRNSKALLSMALGKDISGKPMVVDLAKMPHLLVAGTTGSGKSVGVNTMILSLLYRVKPEEVKFIMIDPKVVELSIYNDIPHLLTEVVTDMKKAANALRWCVDEMERRYQLLSALRVRNIEGFNEKVDEYEALNMPIPNPLWKPGDSMDTLPPPLEKLSYIVVIVDEFADLMMVAGKQVEELIARLAQKARAVGIHLILATQRPSVDVITGLIKANVPSRIAFTVATKIDSRTILDAGGAESLLGKGDMLYSPQGSTELVRIHGAFMTDDEVVRVVDDWKARGKPNYIDGILEGDEEDAGAERLSERGGETDGLFDEVVEFVVSTGTTSISAIQRRFRVGFNRAANIMDQLEEQGIVSPVQNGKREVLARSADY","1912346","","cell division protein K; sporulation protein spoIIIE","Inner membrane, Cytoplasm","","
InterPro
IPR002543
Domain
Cell divisionFtsK/SpoIIIE
PF01580\"[532-746]TFtsK_SpoIIIE
PS50901\"[559-772]TFTSK
noIPR
unintegrated
unintegrated
PD039762\"[1-77]TFTSK_PASMU_Q9CP13;
PTHR22683\"[340-675]T\"[693-874]TSPORULATION PROTEIN RELATED
PTHR22683:SF1\"[340-675]T\"[693-874]TDNA TRANSLOCASE FTSK
signalp\"[1-35]?signal-peptide
tmhmm\"[15-35]?\"[70-90]?\"[105-125]?\"[131-151]?\"[156-176]?transmembrane_regions


","No hits to the COGs database.","","Residues 398 to 442 match (4e-08) PD:PD486403 which is described as CELL DIVISION PROTEOME COMPLETE FTSK HOMOLOG ATP-BINDING ","","","","","","","","","","","","Tue Jan 28 14:38:19 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02733 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 532 to 746 (E-value = 6e-99) place AA02733 in the FtsK_SpoIIIE family which is described as FtsK/SpoIIIE family (PF01580)","","","","","Corre J, Louarn JM.Evidence from terminal recombination gradients that FtsK uses replichore polarity to control chromosome terminus positioning at division in Escherichia coli.J Bacteriol. 2002 Jul;184(14):3801-7.PMID: 12081949Capiaux H, Lesterlin C, Pérals K, Louarn JM, Cornet F.A dual role for the FtsK protein in Escherichia coli chromosome segregation.EMBO Rep. 2002 Jun;3(6):532-6.PMID: 12034757","","Tue Jan 28 14:38:19 2003","1","","","" "AA02734","1915752","1915096","657","TTGGGCAAACAAAAGAAAGAAGGTCGCCTTGGCGAAAATAGGAACTCGCCATCGGCGAAACCCTATCTTAACAATGAAATACAAAGCCCCAAAACAACATTCCTCACTTTATTACTGAATTTTCCCTCAAATTACGTTAAAATCTCCTCCCCTAAATTTTCAAACTCAACTCAAAACCTCATGGAAAAAAAGCTACCCAAAGCTCTTGATGCTATTGACATAAAAATTCTCAATGAATTGCAACGGAACGGAAAAATTTCCAATATTGATTTGTCCAAGAAAGTAGGGTTATCGCCGACACCTTGCCTGGAACGGGTGAAACGGTTGGAGAAGCAAGGGGTGATTATGGGGTATCGTGCTTTGCTGAATCCCGCATTATTGGATTCGCCGTTGTTGGTGATCGTGGAAATTACGCTGGTACGTGGCAAGCCCGATGTGTTTGAAGAATTTAACGCGGCGGTGCAGCAGTTAGATGAAATTCAGGAATGCCATTTGGTTTCCGGTGATTTCGATTATTTATTGAAAACACGGGTGGCGGATATGGCGGCGTATCGTAAATTGCTGGGGACCACCTTGCTGCGCCTGCCCGGGGTGAACGACACGCGCACTTATGTGGTGATGGAAGAAGTGAAACAAACGAATTTTTTACAGTTAAAA","","","27016","LGKQKKEGRLGENRNSPSAKPYLNNEIQSPKTTFLTLLLNFPSNYVKISSPKFSNSTQNLMEKKLPKALDAIDIKILNELQRNGKISNIDLSKKVGLSPTPCLERVKRLEKQGVIMGYRALLNPALLDSPLLVIVEITLVRGKPDVFEEFNAAVQQLDEIQECHLVSGDFDYLLKTRVADMAAYRKLLGTTLLRLPGVNDTRTYVVMEEVKQTNFLQLK","1915094","","leucine-responsive regulatory protein","Cytoplasm","","
InterPro
IPR000485
Family
Bacterial regulatory proteins, AsnC/Lrp
PR00033\"[69-85]T\"[85-96]T\"[96-115]THTHASNC
PF01037\"[133-209]TAsnC_trans_reg
SM00344\"[69-178]THTH_ASNC
PS50956\"[69-130]THTH_ASNC_2
PS00519\"[87-113]THTH_ASNC_1
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[69-120]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.30.70.920\"[122-219]Tno description


","BeTs to 15 clades of COG1522COG name: Transcriptional regulatorsFunctional Class: KThe phylogenetic pattern of COG1522 is aompkz---dr-b-efgh-n-j----Number of proteins in this genome belonging to this COG is","Significant hit ( 3.4e-50) to 3/3 blocks of the IPB000485 family, which is described as \"Bacterial regulatory proteins, AsnC family\". Interpro entry for IP:IPR000485. IPB000485A 69-90 1.2e-08 IPB000485B 97-137 9e-19 IPB000485C 147-188 4.5e-20","Residues 69 to 119 match (2e-20) PD:PD000857 which is described as PROTEOME COMPLETE TRANSCRIPTION TRANSCRIPTIONAL DNA-BINDING REGULATION REGULATOR REGULATORY FAMILY ASNC ","","","","","","","","","","","","Wed Jan 22 14:11:04 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02734 is paralogously related to AA00378 (6e-28) and AA00387 (6e-09).","","","","","","Residues 93 to 196 (E-value = 1.2e-49) place AA02734 in the AsnC_trans_reg family which is described as AsnC family (PF01037)","","","","","Willins DA, Ryan CW, Platko JV, Calvo JM.Characterization of Lrp, and Escherichia coli regulatory protein that mediates a global response to leucine.J Biol Chem. 1991 Jun;266(17):10768-74.PMID: 2040596Friedberg D, Platko JV, Tyler B, Calvo JM.The amino acid sequence of Lrp is highly conserved in four enteric microorganisms.J Bacteriol. 1995 Mar;177(6):1624-6.PMID: 7883720Haney SA, Platko JV, Oxender DL, Calvo JM.Lrp, a leucine-responsive protein, regulates branched-chain amino acid transport genes in Escherichia coli.J Bacteriol. 1992 Jan;174(1):108-15.PMID: 1729203D'Ari R, Lin RT, Newman EB.The leucine-responsive regulatory protein: more than a regulator?.Trends Biochem Sci. 1993 Jul;18(7):260-3.PMID: 8212136","","Wed Jan 22 14:11:04 2003","1","","","" "AA02735","1917484","1916114","1371","ATGGCAAAAGCAAAAACGGCTTATGTATGTAACGACTGCGGCGCGGAATATTCCCGCTGGCAGGGGCAATGTTCCGCCTGTAAAGCCTGGAACACCATCACCGAAGTGCGGTTGGTTTCTACGTCAAATAATAAAGCGGATCGATTTAGCGGCTACGCGGGTGAAACACGTGCGAAAATTCAAACCTTAAGTGAAATCAGCCTGCAGGAAACACCGCGTTTCAGCAGTGGATTTTTTGAGCTGGATCGTGTGTTGGGTGGCGGTGTCGTACCGGGCAGTGCGATCCTCATCGGCGGTCACCCGGGGGCGGGGAAAAGTACCCTGTTGTTGCAGGTGATGTGTAATTTATCGCAAAAAATGACCGCACTTTATGTCACCGGCGAAGAATCCTTACAACAAGTGGCGATGCGTGCCAAACGCCTTGGCCTGCCGCCGGAAAAATTGAATATGCTGTCGGAAACTTCTGTAGAGCAAATTTGTAACCTGGCGGATCAGCTCAAACCGCAGATTATCGTCATCGACTCCATTCAGGTTATGCACTTGGCGGATATTCAATCTTCCCCCGGCAGCGTGGCACAAGTGCGCGAATGTGCTTCTTTTTTAACCCGTTACGCGAAAACCCGTCAAGTGGCAATTGTGATGGTTGGGCATGTTACCAAAGACGGTACTCTTGCCGGGCCAAAAGTGTTGGAGCACGCTATTGACTGTTCCTTATTATTGGAAGGAGAAACGGACTCGCGCTTTCGCACCTTACGCAGCCATAAAAACCGTTTCGGCGCAGTGAACGAATTAGGCGTGTTCGCCATGACGGAACAAGGGCTGCGCGAAGTGAAAAACCCGTCGGCGATCTTTTTAAGTCGCGGCGACGAACAAACCTCCGGCAGTTCCGTGATGGTGTTATGGGAAGGCACGCGCCCGCTGTTGGTGGAAATTCAAGCCTTAGTGGATCATTCCATGCTCGCTAACCCGCGCCGTGTCGCTGTGGGGCTGGAACAAAACCGTCTTGCCTTATTACTTGCCGTATTACACCGCCACGGTGGCTTGCAAATGGCGGATCAGGATGTCTTCGTGAACGTGGTCGGCGGCGTCAAAGTGACCGAAACCGGCGCAGATTTAGCCTTACTCCTCGCACTCATCTCCAGCTTCCGCAACCGCCCGCTGCCACAGGATTTAGTGATCTTCGGCGAAGTGGGCTTGGCAGGCGAAATCCGCCCCGTACCAAGCGGTCAGGAACGTATCAGCGAAGCTGCAAAACACGGCTTCAAACGCGCCATCGTGCCTTTTGGCAATAAACCGAAACATAAAGTGGAGAATATGGAAGTGTTTACGGTACGGAAGTTAGGTGATGCGATTGAGGTGTTGGATCGGTTT","","","49717","MAKAKTAYVCNDCGAEYSRWQGQCSACKAWNTITEVRLVSTSNNKADRFSGYAGETRAKIQTLSEISLQETPRFSSGFFELDRVLGGGVVPGSAILIGGHPGAGKSTLLLQVMCNLSQKMTALYVTGEESLQQVAMRAKRLGLPPEKLNMLSETSVEQICNLADQLKPQIIVIDSIQVMHLADIQSSPGSVAQVRECASFLTRYAKTRQVAIVMVGHVTKDGTLAGPKVLEHAIDCSLLLEGETDSRFRTLRSHKNRFGAVNELGVFAMTEQGLREVKNPSAIFLSRGDEQTSGSSVMVLWEGTRPLLVEIQALVDHSMLANPRRVAVGLEQNRLALLLAVLHRHGGLQMADQDVFVNVVGGVKVTETGADLALLLALISSFRNRPLPQDLVIFGEVGLAGEIRPVPSGQERISEAAKHGFKRAIVPFGNKPKHKVENMEVFTVRKLGDAIEVLDRF","1916112","","DNA repair protein","Cytoplasm","","
InterPro
IPR001553
Family
RecA bacterial DNA recombination
PS50162\"[70-206]TRECA_2
InterPro
IPR001984
Family
Peptidase S16, Lon protease
PR00830\"[99-118]T\"[363-382]T\"[393-412]T\"[416-434]TENDOLAPTASE
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[91-244]TAAA
InterPro
IPR004504
Family
DNA repair protein RadA
PR01874\"[10-34]T\"[83-111]T\"[124-141]T\"[174-198]T\"[213-241]T\"[248-274]T\"[322-345]TDNAREPAIRADA
TIGR00416\"[1-451]Tsms: DNA repair protein RadA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[54-275]Tno description
PTHR10046\"[370-454]TATP DEPENDENT LON PROTEASE FAMILY MEMBER


","BeTs to 17 clades of COG1066COG name: Predicted ATP-dependent serine proteaseFunctional Class: OThe phylogenetic pattern of COG1066 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 2.9e-05) to 2/7 blocks of the IPB001198 family, which is described as \"DnaB helicase\". Interpro entry for IP:IPR001198. IPB001198C 77-115 0.0011 IPB001198E 167-180 13Significant hit ( 5.9e-05) to 1/10 blocks of the IPB003111 family, which is described as \"ATP-dependent protease La (LON) domain\". Interpro entry for IP:IPR003111. IPB003111J 374-420 5.7e-05","Residues 366 to 451 match (6e-07) PD:PD488852 which is described as DNA REPAIR RADA PROTEOME COMPLETE ","","","","","","","","","","","","Wed Jan 22 14:13:13 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02735 is paralogously related to AA02395 (1e-05) and AA01557 (3e-05).","","","","","","","","","","","Song Y, Sargentini NJ.Escherichia coli DNA repair genes radA and sms are the same gene.J Bacteriol. 1996 Aug;178(16):5045-8.PMID: 8759876","","Tue Dec 2 13:48:39 2003","1","","","" "AA02736","1918641","1917490","1152","ATGCAGGATGAAATTGAATTAAAGTTAGCGGTGGATTTTGTCGATGTAGCACAATTAGACAAAATTTTGAATCATTTCAAAGTGGTTGAAAAACAATGCGATTTTTTAGCCAATACCTATTACGACACCTCCGATCAGTTTTTTACCCGACATAAAATGGGCTTGCGGGTTCGCCGTCAGCAGGATAATTACACCTTAACGCTAAAAACCGACGGCAATTTTTCCGGCGGGTTGCACATGCGCCCCGAGTATAATGTGACGTTGCCCGATGCCAAACCTGATCTGAATGCCTTAATCGAAGAACATGGCTTACAGCTCGGCAATCTAAAAAATGAATTGCATCCTATTTTCAGCACAGATTTCGAACGCCAAAGCTGGTTGGTACAATATGCGCCCAATTGCCAAATTGAAGTGGCGTTCGACCAAGGCAATGTGATAGCAGGCGATAAACGGCAACCTATCCGTGAAATAGAATTTGAAATCAAATCCGGCGAATTGGCACCATTTTTTGCCTTCGTCATGGATTTCTTAACCCGTTATGAGGGCAGCGTACATTTTTATTCTGTGAGCAAAGCCAAACGCGGTTATCAATTGGTGCAGGGCAAATGTGCTAAATCAAGTGATTGGATCGAACATTGGCGCGGCGTTTTACAGACGGAAAAACGGGCACAAAAAACATCGGAAAAATTACTCACAATCGAATCAAGTTCGATTGTTCGCCCTGATGAGGCCGTTGGCAAAGCCAACGTTCAAAATCCGTTGGATTTTGTGACCGCACTTTTGGCTTACGAGCAGCCTTTAATTGAAGAAACCTTGGCGTTAGGGGCAAATTTCTTTGCTTCTGATTTCATCAAAAGCGTTGAACGGGTAGGAGCGTTTTTCAATTTGTATCATTATTACGAAGACAATAAATCCCTGTTGGAAACAGCATTGAACGAGCAATTAGCAGGCAATAGGCATTATGCGCAGGACGATGTATTGACGGCGTTGACCGAAGAAAATGATCGCATATTGGCGCAACTTCATGACATTATTCGTCTGCACAGCGAAAGCAAAGATAACGCGTCGGCGATGAATAAATTGCTTGAACTGATTCAAACGCCGCAATACGCCCAACGTATGCTCTACCTCATCACTTTAACCATCGGCGGG","","","43960","MQDEIELKLAVDFVDVAQLDKILNHFKVVEKQCDFLANTYYDTSDQFFTRHKMGLRVRRQQDNYTLTLKTDGNFSGGLHMRPEYNVTLPDAKPDLNALIEEHGLQLGNLKNELHPIFSTDFERQSWLVQYAPNCQIEVAFDQGNVIAGDKRQPIREIEFEIKSGELAPFFAFVMDFLTRYEGSVHFYSVSKAKRGYQLVQGKCAKSSDWIEHWRGVLQTEKRAQKTSEKLLTIESSSIVRPDEAVGKANVQNPLDFVTALLAYEQPLIEETLALGANFFASDFIKSVERVGAFFNLYHYYEDNKSLLETALNEQLAGNRHYAQDDVLTALTEENDRILAQLHDIIRLHSESKDNASAMNKLLELIQTPQYAQRMLYLITLTIGG","1917488","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR008172
Domain
Adenylate cyclase
PF01928\"[2-202]TCYTH
InterPro
IPR012207
Family
Uncharacterised conserved protein UCP036566, CYTH region, YgiF-related
PIRSF036566\"[1-384]TUncharacterised stand-alone CYTH domain protein, YgiF type


","No hits to the COGs database.","","Residues 40 to 199 match (2e-10) PD:PD589933 which is described as COMPLETE PROTEOME PA5209 PLASMID RSC2886 MLL9114 ","","","","","","","","","","","","Wed Jan 22 14:15:19 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02736 is paralogously related to AA02106 (2e-05).","","","","","","Residues 2 to 202 (E-value = 8.4e-31) place AA02736 in the CYTH family which is described as CYTH domain (PF01928)","","","","","","","","1","","","" "AA02737","1918806","1919483","678","ATGGCAATGAATAATATCCTCGGATTATTTGCCCACTCCCCTTTAAAGCCTCTGCAAAAACACTCTAATAAAGTTACCGAATGTTGTGAATTATTAATCCCTTTTTTTGAAGCAACATTTAATACCGACTGGGTAAAAGCGGAGCAAATTCGTTTAGATATTTCTGCACACGAACGTCAGGCTGACGCGTTAAAACGTGAGATTCGTTTAAAATTACCGCGCGGTTTATTCATGCCTATCGATCGTACGGATTTGTTGGAATTAGTGACTCAACAAGATAAATTGGCAAACTACACCAAAGACATTGCCGGCCGTATGATTGGTCGTCAGTTAAGTATTCCGGAGGAAATGAAAAACGAATTTATGAGCTATGTACGTCGCAGTTTGGACGCTACCGAACAAGCCCATAAAGTGATTGAAGAAATGGATCAACTACTGGAAACCGGTTTCAAAGGTCGCGAATTGAATTTCGTCAATCAAATGATTAACGAACTGGATATCATTGAAGACGATACCGACCAAATACAAATTAAATTGCGAAGAATGTTATTTGATATTGAAGATCGCTTTAACCCGATTGATGTAATGTTCTTATACAAAGTCATTGAATGGGTCGGTGTACTTGCCGATCAGGCACAACGTGTCGGAGCACGCATTGAGCTGATGTTAGCACGTTCA","","","26367","MAMNNILGLFAHSPLKPLQKHSNKVTECCELLIPFFEATFNTDWVKAEQIRLDISAHERQADALKREIRLKLPRGLFMPIDRTDLLELVTQQDKLANYTKDIAGRMIGRQLSIPEEMKNEFMSYVRRSLDATEQAHKVIEEMDQLLETGFKGRELNFVNQMINELDIIEDDTDQIQIKLRRMLFDIEDRFNPIDVMFLYKVIEWVGVLADQAQRVGARIELMLARS","1919481","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR002727
Family
Protein of unknown function DUF47
PF01865\"[6-225]TPhoU_div
TIGR00153\"[2-226]TTIGR00153: conserved hypothetical protein T


","No hits to the COGs database.","Significant hit ( 5.6e-24) to 1/1 blocks of the IPB002727 family, which is described as \"Protein of unknown function DUF47\". Interpro entry for IP:IPR002727. IPB002727 61-103 5.2e-24","Residues 1 to 37 match (1e-12) PD:PD476267 which is described as PROTEOME COMPLETE HI1603 ","","","","","","","","","","","","Wed Jan 22 14:15:57 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02737 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 6 to 225 (E-value = 9.1e-100) place AA02737 in the PhoU_div family which is described as Protein of unknown function DUF47 (PF01865)","","","","","","","","1","","","" "AA02738","1919512","1920774","1263","ATGGAATTACTCAATCAATATGGTTCCTTATTAATCATAATTACCGCAATTTTCGGCTTTTTTATGGCCTTTGGTGTGGGAGCTAACGATGTTTCAAATGCTATGGGAACATCTGTTGGTTCAGGGGCAGTCACAGCAAAACAAGCTATTTTTATTGCAATAATTTTTGAAGCCGCCGGTGCTTATTTAGCCGGTGGTGAAGTCACAGAAACTATCAAAAGCGGCATCATCGACACCATGGAATTCGTCAATGAACCGGAAGTTTTAGTTTTCGGGATGATGGCTGCCCTCTTCGCTTCAGGGGCCTGGTTATTAATCGCTTCCAAAATGGGCTGGCCGGTGTCCACCACTCACTCCATCATCGGTGCTGTTATTGGTTTTGCGTGCGTTACGGCAGGTCCTCATTCGGTGGATTGGAGCAATATCCGAAATATTGTCGGCAGTTGGTTTGTTACACCGGTAATTGCCGGAGTGTTGGCTTACGCCATTTTTATCAGCACGCAAAAACTGATTTTTGACACAGAAAACCCGCTTAAAAACGCACAAAAATATGGCCCTTACTATATGGGTATTACTATTTTCATCTTGTGCATTGTTACCCTGACCAAAGGGTTAAAGCATGTAGGGTTAAATTTAAGCAGTCAGGAAAACTTCCTGATTTCTTTTATTATCAGCGCAGTAGCCGTTATTTACTGCTATTTCTACTTTCGTAGTAAAAAATTCAAACAAAGAATGCTCCATGGCGGTACGTTTAGCGGCGTAGAAAAGATCTTCAGTATTTTAATGCTAATGACCGCTTGTGCTATGGCATTTGCCCATGGTTCTAACGATGTTGCGAACGCTATCGGTCCGCTTTCTGCGGTGGTCGCTATTATCAAAAGTGGCGGTCAAATCGCAAACAACACTCCTCTCGCTTGGTGGATTTTACCCCTGGGCGCATCCGGTATCATGGTCGGTTTGATCGTCATGGGTTACAAAGTGATGGCAACTATCGGTACGGGCATTACCGATTTAACGCCAAGTCGTGGCTTCGCCGCCCAATTCGCCACCGCAATGACTGTGGTCGTGGCATCCGGTACAGGCTTGCCGATTTCTACGACACAAACCTTAGTGGGTGCTGTATTAGGCATCGGTTTCGCGCGTGGAATTGCGGCAATTAACCTGACCGTAATTCGCAACATCGTGGTTTCATGGGTTGTTACTCTGCCTGCCGGCGCATTGTTCTCTATTATTATTTACTATTTGCTCAAAGCAATTTTTCAT","","","44472","MELLNQYGSLLIIITAIFGFFMAFGVGANDVSNAMGTSVGSGAVTAKQAIFIAIIFEAAGAYLAGGEVTETIKSGIIDTMEFVNEPEVLVFGMMAALFASGAWLLIASKMGWPVSTTHSIIGAVIGFACVTAGPHSVDWSNIRNIVGSWFVTPVIAGVLAYAIFISTQKLIFDTENPLKNAQKYGPYYMGITIFILCIVTLTKGLKHVGLNLSSQENFLISFIISAVAVIYCYFYFRSKKFKQRMLHGGTFSGVEKIFSILMLMTACAMAFAHGSNDVANAIGPLSAVVAIIKSGGQIANNTPLAWWILPLGASGIMVGLIVMGYKVMATIGTGITDLTPSRGFAAQFATAMTVVVASGTGLPISTTQTLVGAVLGIGFARGIAAINLTVIRNIVVSWVVTLPAGALFSIIIYYLLKAIFH","1920772","","phosphate permease","Inner membrane, Cytoplasm","","
InterPro
IPR001204
Family
Phosphate transporter
PTHR11101\"[16-420]TPHOSPHATE TRANSPORTER
PF01384\"[26-409]TPHO4
InterPro
IPR002345
Domain
Lipocalin
PS00213\"[141-152]?LIPOCALIN
noIPR
unintegrated
unintegrated
PTHR11101:SF8\"[16-420]TCHLOROPLAST PHOSPHATE TRANSPORTER
signalp\"[1-28]?signal-peptide
tmhmm\"[10-28]?\"[49-69]?\"[88-106]?\"[111-131]?\"[145-165]?\"[186-204]?\"[218-236]?\"[257-275]?\"[303-323]?\"[344-364]?\"[370-390]?\"[395-415]?transmembrane_regions


","BeTs to 19 clades of COG0306COG name: Phosphate/sulphate permeasesFunctional Class: PThe phylogenetic pattern of COG0306 is aompk-y-vdr-b-efgh-nuj-i--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.3e-41) to 3/3 blocks of the IPB001204 family, which is described as \"Phosphate transporter family\". Interpro entry for IP:IPR001204. IPB001204A 95-126 3.5e-21 IPB001204B 270-283 1.1e-09 IPB001204C 394-409 7.8e-08 IPB001204A 345-376 1.2e-07 IPB001204B 23-36 2.8e-05 IPB001204C 145-160 0.0003","Residues 163 to 254 match (7e-25) PD:PD127453 which is described as PROTEOME COMPLETE PHOSPHATE INNER PERMEASE PROBABLE PHO4 TRANSMEMBRANE PM0249 MEMBRANE ","","","","","","","","","","","","Wed Jan 22 14:17:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02738 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 26 to 409 (E-value = 4.6e-176) place AA02738 in the PHO4 family which is described as Phosphate transporter family (PF01384)","","","","","","","","1","","","" "AA02740","1920846","1921454","609","ATGCAAAAAACCATTAAATACCTTCTCACACTAACCTTTCTGGGCTTAGGTATCACTACTGCACAAGCAGAAACCAAATATGTAACAGAAAACCTTTCCACCTACTTACGTAAAGGTGCAGGTGACCAATATAAAATTGCCGGTGCTATTAAATCAGGTGAACCGGTAACCGTATTGGATCAAAAAGATCGATATACTCTAATCCGCGATGGCAAAGATCGCGAGGCCTGGATTTTAAGCAGTGAGCTAAGTAATGAAGCCAGCAGCAAACTGGAAAATCCGAAATTAAAACACCAAATTCAGGAATTAAGCATGAAGCTAGGCCGTATAGACAGCGACTGGCAACAACGTACTATTGAAATGCAACGACGTGCCAAACAAGCGGAACAACAAAGTAGCGAACTCTTAGAACAAAATTCACAGCTAAAACGCGAATTGGAAATCACCAAAAACAAAAACCGCGATTTGGAAGCCATGTTAGATGCGGGCAAACGCGAAATTGCCATTCAATGGTTCATTTATGGCGGTTCCGTGCTTGGGGTCGGCTTATTAATCGGGTTGATTTTACCGTTAATCATGCCGAAACGCCGTCGTCGCGATGGTTGGGCA","","","23163","MQKTIKYLLTLTFLGLGITTAQAETKYVTENLSTYLRKGAGDQYKIAGAIKSGEPVTVLDQKDRYTLIRDGKDREAWILSSELSNEASSKLENPKLKHQIQELSMKLGRIDSDWQQRTIEMQRRAKQAEQQSSELLEQNSQLKRELEITKNKNRDLEAMLDAGKREIAIQWFIYGGSVLGVGLLIGLILPLIMPKRRRRDGWA","1921452","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003646
Domain
Bacterial SH3-like region
SM00287\"[23-87]TSH3b
InterPro
IPR010466
Family
Protein of unknown function DUF1058
PF06347\"[30-85]TSH3_4
noIPR
unintegrated
unintegrated
signalp\"[1-23]?signal-peptide
tmhmm\"[171-191]?transmembrane_regions


","BeTs to 4 clades of COG3103COG name: SH3 domain proteinFunctional Class: TThe phylogenetic pattern of COG3103 is --------------efgh--------Number of proteins in this genome belonging to this COG is","","Residues 21 to 203 match (8e-57) PD:PD035607 which is described as COMPLETE PROTEOME TRANSMEMBRANE SIGNAL PRECURSOR PM0248 EXPORTED MEMBRANE DOMAIN YGIM ","","","","","","","","","","","","Wed Jan 22 14:17:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02740 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02742","1921448","1922758","1311","TTGGGCATAATGTCCGAAAATCATTTTCAAATTTATTTGGTTGGCGGGGCTGTGCGCGATCAGCTCCTCAACCTACCTGTTCAAGATCGCGATTGGGTCATTGTAGGTGCGACGCCGGAAGCACTACTCCAACAAGGCTATCATCAAGTGGGAAAAGATTTCCCCGTTTTTTTGCACCCACAAACCAAAGAAGAATACGCACTCGCCCGCACGGAACGTAAATCCGGTACGGGCTACACCGGCTTTATTTGCGATTTTTCTCCCGATATTAATCTGGAACAGGATTTAATCCGCCGCGATCTCACCATCAACGCCATGGCACAGGATTTGCAGGGCAATCTGTTCGACCCTTATGGCGGCGCACAGGATTTAGCCAACCTTGTGTTACGCCACGTCTCCCCCGCATTCGTTGAAGATCCCTTGCGCGTATTACGCGTGGCGCGCTTTGCCGCCCGTTATCATTATTTAGGATTCAAGATTGCCGAAGAAACCCTGCAATTAATGAAAGATCTCACTGCCCAAGGGGAGCTGCAACATTTAACCGCCGAGCGGGTATGGGCGGAAACGGAAAAAGCGTTAAACGAGAAAAATCCTGAAATTTATTTTGAAACCTTACGCCTGGTGGGCGCACTCAAGGTGTTATTTCCTGAATTGGACGCTCTATATGGCGTGCCGAACCCGGCGAAGTATCATCCGGAAATTGACAGCTTCGTGCACACTATGATGGTGTTACAACAGGCGACGTTGCTTTCTGAGCAAGTGGATTGCCACAAAAGTGCGGTGCGTTTTGCCGCCATTTGCCATGACTTGGGCAAAGCCAAAACGCCTAAACAAAGCTGGCCTCATCATCACGGTCATGAAAAGCTCGGCATGGCGCCGACCCAAAGCCTATGCAAGCGCTTAAAAGTACCCGGTTATTATCAACAACTGGCGGAACTCACCTGTGAATATCACACCCACATTCACAAAATTTTTGAATTACGCCCGGAAACTATCGTCAAACTGTTCAATACCTTTGATGTTTGGCGCAAACCGTTACGTTTCATGGAATTTTTGTTGGTGTGTTTTGCCGATACGCGCGGACGCAAAGGCTTCTCGCACATTGCGTACCCGCAACAGGAATTTACTATCGCCCTATATCGGGCGGCATTAAAAGTGGATATTCAATCCATCATCGCGGCAGGCTTTGAAAATAAAGCCATTCGCGATCAGTTAAACCGCGGACGGATTTTCGCCGTGAAGCAAAAACGCACGGAAATCCTACCGCACTTTAAACCATCGACATCAGATTGCCGCCCTCGTTGCGAACCG","","","53813","LGIMSENHFQIYLVGGAVRDQLLNLPVQDRDWVIVGATPEALLQQGYHQVGKDFPVFLHPQTKEEYALARTERKSGTGYTGFICDFSPDINLEQDLIRRDLTINAMAQDLQGNLFDPYGGAQDLANLVLRHVSPAFVEDPLRVLRVARFAARYHYLGFKIAEETLQLMKDLTAQGELQHLTAERVWAETEKALNEKNPEIYFETLRLVGALKVLFPELDALYGVPNPAKYHPEIDSFVHTMMVLQQATLLSEQVDCHKSAVRFAAICHDLGKAKTPKQSWPHHHGHEKLGMAPTQSLCKRLKVPGYYQQLAELTCEYHTHIHKIFELRPETIVKLFNTFDVWRKPLRFMEFLLVCFADTRGRKGFSHIAYPQQEFTIALYRAALKVDIQSIIAAGFENKAIRDQLNRGRIFAVKQKRTEILPHFKPSTSDCRPRCEP","1922756","From H. ducreyi record HD1091:This enzyme carries out synthesis of the tRNA CCA terminus withoutthe direction of a template using multiple accepting and donatingsubsites within its active site.","tRNA nucleotidyltransferase","Cytoplasm","","
InterPro
IPR002646
Domain
Polynucleotide adenylyltransferase region
PF01743\"[11-130]TPolyA_pol
InterPro
IPR003607
Domain
Metal-dependent phosphohydrolase, HD region
SM00471\"[232-372]THDc
InterPro
IPR006674
Domain
Metal-dependent phosphohydrolase, HD region, subdomain
PF01966\"[236-342]THD
InterPro
IPR012006
Family
tRNA nucleotidyltransferase, proteobacteria
PIRSF000813\"[9-421]TtRNA nucleotidyltransferase (CCA-adding enzyme), Proteobacteria type
noIPR
unintegrated
unintegrated
G3DSA:1.10.3090.10\"[138-332]Tno description
G3DSA:3.30.460.10\"[1-127]Tno description
PTHR13734\"[89-418]TTRNA-NUCLEOTIDYLTRANSFERASE/POLY(A) POLYMERASE FAMILY MEMBER
PTHR13734:SF6\"[89-418]Tgb def: tRNA nucleotidyltransferase (EC 2.7.7.25) (tRNA adenylyltransferase) (tRNA CCA-p


","No hits to the COGs database.","Significant hit ( 1.1e-39) to 4/4 blocks of the IPB002646 family, which is described as \"Poly A polymerase family\". Interpro entry for IP:IPR002646. IPB002646A 12-31 1.7e-10 IPB002646B 91-106 3.2e-08 IPB002646C 127-153 3.3e-12 IPB002646D 180-193 0.00046","Residues 200 to 423 match (3e-09) PD:PD300446 which is described as TRNA NUCLEOTIDYLTRANSFERASE RNA-BINDING PROTEOME ADENYLYLTRANSFERASE CCA-PYROPHOSPHORYLASE COMPLETE ATP-BINDING PROCESSING CCA-ADDING ","","","","","","","","","","","Wed Jan 22 14:20:34 2003","Wed Jan 22 14:19:58 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02742 is paralogously related to AA01965 (4e-14).","","","","","","Residues 236 to 342 (E-value = 2.3e-05) place AA02742 in the HD family which is described as HD domain (PF01966)","","","","","Cudny H, Lupski JR, Godson GN, Deutscher MP.Cloning, sequencing, and species relatedness of the Escherichia coli cca gene encoding the enzyme tRNA nucleotidyltransferase.J Biol Chem. 1986 May;261(14):6444-9.PMID: 3009457Seth M, Thurlow DL, Hou YM.Poly(C) synthesis by class I and class II CCA-adding enzymes.Biochemistry. 2002 Apr;41(14):4521-32.PMID: 11926813Schürer H, Schiffer S, Marchfelder A, Mörl M.This is the end: processing, editing and repair at the tRNA 3'-terminus.Biol Chem. 2001 Aug;382(8):1147-56.PMID: 11592395","","Wed Jan 22 14:20:34 2003","1","","","" "AA02743","1922790","1923416","627","TTGTTTATGAAAAAATTAAAATCCTACGTTTTACTTGTGTTAGCCGTGTTATTTTTAACCGCTTGCGTCACCGATCAGGAACGTCCGACTAACGTAAAATACATCGAAAAAACCGACCGCACTTGGCAGCAGCATTTCACCCAATTAAAACAAATTCAAGGTTATCAGGCGCTTGGGCAGTTAGGTTATATCAGCAGCAAAGAACGCTTTTCCACGCGCTTCGACTGGCAATATAACAACCCACGCGATTACACCCTGCAACTGTATTCCACCATCAGCAGCGAAACCCTGCAGATTCAAATGCACGCGCAAGGCATGACCATTTCCGACAACAAAGGGCGCCAACGCTCCGCCGCCGACGCAAAAATGCTGCTACGTGAAATTATCGGCATGGATTTCCCGTTGGAACAATTCGCTTTCTGGCTGAAAGGTCAACCGGAAGATAACGCCGATTATCAAGTGGGAGAAAACCATTTGTTAGCCACCTTCAGTCGCACTATCGACGGTAAACCCTGGACGGCGGACTATTTGTCATACCATGTCAATCGCCGTCCGCCGATGCCGGAAAATATTTTGCTGAAAACGGAAGGACAAACTTTGAAAATCCGTGTAGATGAATGGCTGTTT","","","24496","LFMKKLKSYVLLVLAVLFLTACVTDQERPTNVKYIEKTDRTWQQHFTQLKQIQGYQALGQLGYISSKERFSTRFDWQYNNPRDYTLQLYSTISSETLQIQMHAQGMTISDNKGRQRSAADAKMLLREIIGMDFPLEQFAFWLKGQPEDNADYQVGENHLLATFSRTIDGKPWTADYLSYHVNRRPPMPENILLKTEGQTLKIRVDEWLF","1923414","","outer membrane lipoprotein precursor/glutamyl-tRNA reductase subunit","Outer membrane, Periplasm, Cytoplasm","","
InterPro
IPR004565
Family
Outer membrane lipoprotein LolB
PF03550\"[51-207]TLolB
TIGR00548\"[5-209]TlolB: outer membrane lipoprotein LolB
noIPR
unintegrated
unintegrated
signalp\"[1-26]?signal-peptide
tmhmm\"[9-24]?transmembrane_regions


","No hits to the COGs database.","","Residues 168 to 209 match (3e-18) PD:PD344813 which is described as LIPOPROTEIN PRECURSOR OUTER-MEMBRANE LOLB OUTER MEMBRANE CHAPERONE SIGNAL PROTEOME COMPLETE ","","","","","","","","","","","","Wed Jan 22 14:24:49 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02743 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 197 (E-value = 5e-116) place AA02743 in the LolB family which is described as Outer membrane lipoprotein LolB (PF03550)","","","","","Matsuyama S, Yokota N, Tokuda H.A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli.EMBO J. 1997 Dec;16(23):6947-55.PMID: 9384574Masuda K, Matsuyama S, Tokuda H.Elucidation of the function of lipoprotein-sorting signals that determine membrane localization.Proc Natl Acad Sci U S A. 2002 May;99(11):7390-5.PMID: 12032293","","Wed Jan 22 14:24:49 2003","1","","","" "AA02745","1923419","1924327","909","ATGAAAACTTATCAATTTTCCACCGCACTTTTCACGCCCGAAACCTTGCAAAGCGAACAGGGTGTACGCTTCCCCTGCCCGGCGAAGCTGAATCTTTTTTTGTACATTAACGGCAAGCGGGCGGACGGTTACCACGAATTACAAACCCTGTTTCAGTTTGTTGATTTCGGCGATTGGCTACACATCAAAGTGCGCCCGGACGGCAAGATTCGTTTAACCTCCGTCATCGCCGATTTAAAAGCAGAAGATAATTTAATTTATCGCGCGGCAAAATTGCTGCAACAGTACACCGGCTGCACGCTGGGCACCGAGTTAACCTTAGATAAAATCCTGCCGATCGGTGGCGGCGTGGGTGGCGGTTCATCCAATGCGGCAACGACATTGGTCGCCTTAAATCATTTATGGAAAACCGGCTTGAGCACCGGGCAACTTGCCGAACTGGGCTTAACCCTTGGCGCGGATGTACCGATTTTCGTGCACGGCAAAGCGGCGTTTGCGGAAGGCATAGGCGAAAAAATCACATACTGCGAACCGCCGGAAAAATGGTATCTGGTGCTCAAGCCGAATGTGTCTATTTCCACTGCCGTTGTGTTCTCTGACCCGCACTTGCCACGTAATACACCGAAAAAATCGCTGGCACAATTATTGGCGGGAAAATACGCAAACGATTGTGAAAAAGTTGTGCGAGATCATTATTCAGAGGTTGAAGAGTCACTGAACTGGTTGGTAAAATATGCACCGGCCAGATTAACCGGGACTGGTGCTTGCGTTTTTGCGGAATTTGATGATAAAAAATCTGCCCAATCAGTTCTCCAAGCCAAACCAAAAAATTGTTTTGGTTTCGTCGCAAAAGGATTAAATCATTCTCCCTTGCATGAAATGTTGAAAAACGTGCCTGATTCAACGAAT","","","33602","MKTYQFSTALFTPETLQSEQGVRFPCPAKLNLFLYINGKRADGYHELQTLFQFVDFGDWLHIKVRPDGKIRLTSVIADLKAEDNLIYRAAKLLQQYTGCTLGTELTLDKILPIGGGVGGGSSNAATTLVALNHLWKTGLSTGQLAELGLTLGADVPIFVHGKAAFAEGIGEKITYCEPPEKWYLVLKPNVSISTAVVFSDPHLPRNTPKKSLAQLLAGKYANDCEKVVRDHYSEVEESLNWLVKYAPARLTGTGACVFAEFDDKKSAQSVLQAKPKNCFGFVAKGLNHSPLHEMLKNVPDSTN","1924325","","isopentenyl monophosphate kinase","Cytoplasm, Periplasm","","
InterPro
IPR004424
Family
4-diphosphocytidyl-2C-methyl-D-erythritol kinase
PIRSF010376\"[25-294]T4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate synthase
PTHR20861:SF2\"[67-277]T4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE
TIGR00154\"[19-297]TispE: 4-diphosphocytidyl-2C-methyl-D-erythr
InterPro
IPR006204
Domain
GHMP kinase
PF00288\"[104-162]TGHMP_kinases_N
InterPro
IPR013750
Domain
GHMP kinase, C-terminal
PF08544\"[212-277]TGHMP_kinases_C
InterPro
IPR014721
Domain
Ribosomal protein S5 domain 2-type fold
G3DSA:3.30.230.10\"[22-178]Tno description
noIPR
unintegrated
unintegrated
PTHR20861\"[67-277]THOMOSERINE/4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE


","No hits to the COGs database.","","Residues 161 to 245 match (1e-09) PD:PD534524 which is described as KINASE ISOPRENE PROTEOME COMPLETE 4-CYTIDINE-5'-DIPHOSPHO-2-C-METHYL-D-ERYTHRITOL ATP-BINDING CMK 4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL TRANSFERASE BIOSYNTHESIS ","","","","","","","","","","","","Wed Jan 22 14:29:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02745 is paralogously related to AA02358 (3e-04).","","","","","","Residues 102 to 265 (E-value = 2.7e-32) place AA02745 in the GHMP_kinases family which is described as GHMP kinases putative ATP-binding protein (PF00288)","","","","","Lange BM, Croteau R.Isopentenyl diphosphate biosynthesis via a mevalonate-independent pathway: isopentenyl monophosphate kinase catalyzes the terminal enzymatic step.Proc Natl Acad Sci U S A. 1999 Nov;96(24):13714-9.PMID: 10570138","","Wed Jan 22 14:29:46 2003","1","","","" "AA02747","1924464","1925318","855","GTGGGCCGTTTCAGCGATGGTGAAGTACAAGTCCAAATTAACGAAAACGTGCGTGGCAGCGATGTATTCATTATCCAATCCACCTGCGCACCGACTAACGATAATTTAATGGAATTATTAGTGATGGTTGACGCATTGCGCCGCGCTTCCGCCGGGCGTATTACTGCTGTCATCCCTTATTTCGGCTATGCCCGTCAGGATCGTCGGGTACGTTCCGCGCGCGTACCGATTACCGCTAAAGTGGTGGCAGACTTCCTCTCCGGTGTCGGTGTTGACCGTGTATTAACCTGTGATTTGCACGCCGAACAAATTCAAGGCTTCTTTGATGTGCCGGTAGATAATGTATTCGGTTCACCGGTATTACTTGACGATATCCGCAAAAAAACCGACCTTACCAACCCAATTGTGGTTTCCCCGGATATTGGTGGTGTGGTTCGTGCCCGTGCCGTTGCCAAATTATTGAACGACACCGACATGGCGATTATAGACAAACGCCGCCCGCGCGCTAATGTATCCAAAGTCATGCACATTATTGGCGATGTCGCGGATCGTGACTGTATCTTGGTTGACGACATGATCGACACAGGCGGCACCTTATGCAAAGCAGCGGAAGCCCTGAAAGAACGTGGTGCAAGACGGGTATTCGCCTATGCCACCCACGCCGTATTCTCAGGCTCTGCGGCAAAAAATATTGCCAGCGATGCCCTTGACGAAGTAGTCGTCACTGACACCATCCCACTTTCTCCGGAAATCCGCGTATTAGGCAAAGTCCGCACCTTAACCTTATCCGGTATGCTTGCCGAAGCTATTCGTCGCATCAGCAACGAAGAGTCCATTTCCGCAATGTTTAACGAA","","","34268","VGRFSDGEVQVQINENVRGSDVFIIQSTCAPTNDNLMELLVMVDALRRASAGRITAVIPYFGYARQDRRVRSARVPITAKVVADFLSGVGVDRVLTCDLHAEQIQGFFDVPVDNVFGSPVLLDDIRKKTDLTNPIVVSPDIGGVVRARAVAKLLNDTDMAIIDKRRPRANVSKVMHIIGDVADRDCILVDDMIDTGGTLCKAAEALKERGARRVFAYATHAVFSGSAAKNIASDALDEVVVTDTIPLSPEIRVLGKVRTLTLSGMLAEAIRRISNEESISAMFNE","1925316","[PATHWAY] Utilized by both the de novo and the salvage pathways bywhich endogenously formed or exogenously added pyrimidine, purine, or pyridine bases are converted to the corresponding ribonucleoside monophosphates.","ribose-phosphate pyrophosphokinase; phosphoribosylpyrophosphate synthase","Cytoplasm","","
InterPro
IPR000836
Domain
Phosphoribosyltransferase
PF00156\"[109-241]TPribosyltran
InterPro
IPR000842
Family
Phosphoribosyl pyrophosphate synthetase
PS00114\"[98-113]TPRPP_SYNTHETASE
InterPro
IPR002375
Family
Purine/pyrimidine phosphoribosyl transferase
PS00103\"[186-198]?PUR_PYR_PR_TRANSFER
InterPro
IPR005946
Family
Ribose-phosphate pyrophosphokinase
TIGR01251\"[1-284]TribP_PPkin: ribose-phosphate pyrophosphokin
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2020\"[1-140]Tno description
PTHR10210\"[1-284]TRIBOSE-PHOSPHATE PYROPHOSPHOKINASE
PTHR10210:SF14\"[1-284]TRIBOSE-PHOSPHATE PYROPHOSPHOKINASE 1,2,3,4


","BeTs to 24 clades of COG0462COG name: Phosphoribosylpyrophosphate synthetaseFunctional Class: F,EThe phylogenetic pattern of COG0462 is aompkzyqvdrlbcefghsnuj--twNumber of proteins in this genome belonging to this COG is","Significant hit (1.1e-166) to 6/6 blocks of the IPB000842 family, which is described as \"Phosphoribosyl pyrophosphate synthetase\". Interpro entry for IP:IPR000842. IPB000842A 3-45 6.9e-37 IPB000842B 74-119 4.3e-37 IPB000842C 133-160 8.8e-17 IPB000842D 162-216 1.3e-43 IPB000842E 219-246 7.4e-15 IPB000842F 260-283 8.4e-12Significant hit ( 1.8e-05) to 1/2 blocks of the IPB002375 family, which is described as \"Purine/pyrimidine phosphoribosyl transferase\". Interpro entry for IP:IPR002375. IPB002375B 183-198 1.9e-05","Residues 120 to 280 match (2e-08) PD:PD488578 which is described as PROTEOME SYNTHETASE COMPLETE PHOSPHORIBOSYL PROBABLE PYROPHOSPHATE PHOSPHORIBOSYLPYROPHOSPHATE ","","","","","","","","","","","Wed Jan 22 16:05:54 2003","Wed Jan 22 16:05:54 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02747 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 109 to 241 (E-value = 1.3e-35) place AA02747 in the Pribosyltran family which is described as Phosphoribosyl transferase domain (PF00156)","","","","","Hyyryläinen HL, Bolhuis A, Darmon E, Muukkonen L, Koski P, Vitikainen M, Sarvas M, Prágai Z, Bron S, van Dijl JM, Kontinen VP.A novel two-component regulatory system in Bacillus subtilis for the survival of severe secretion stress.Mol Microbiol. 2001 Sep;41(5):1159-72.PMID: 11555295He B, Choi KY, Zalkin H.Regulation of Escherichia coli glnB, prsA, and speA by the purine repressor.J Bacteriol. 1993 Jun;175(11):3598-606.PMID: 8388874Hove-Jensen B, Harlow KW, King CJ, Switzer RL.Phosphoribosylpyrophosphate synthetase of Escherichia coli. Properties of the purified enzyme and primary structure of the prs gene.J Biol Chem. 1986 May;261(15):6765-71.PMID: 3009477Bower SG, Harlow KW, Switzer RL, Hove-Jensen B.Characterization of the Escherichia coli prsA1-encoded mutant phosphoribosylpyrophosphate synthetase identifies a divalent cation-nucleotide binding site.J Biol Chem. 1989 Jun;264(17):10287-91.PMID: 2542328","","Wed Jan 22 16:05:54 2003","1","","","" "AA02748","1925499","1925642","144","ATGAAAAAATTACTTTTTGTCCTCGCCGGCATTTTAACCATCGCCGCCTGCTCCCAGCCAAAAGACATCTATTTTAACGGTTCCGAAGGTTCCCACTCCGGTTTGAAATACGACAAAAGTACTAAGACTTTTGGTGTTAATAAC","","","5176","MKKLLFVLAGILTIAACSQPKDIYFNGSEGSHSGLKYDKSTKTFGVNN","1925642","","conserved hypothetical protein","Outer membrane, Periplasm, Extracellular","This sequence is similar to gi|16273114, a predicted hypothetical protein from Haemophilus influenzae Rd KW20.","
noIPR
unintegrated
unintegrated
PS51257\"[1-17]TPROKAR_LIPOPROTEIN
signalp\"[1-20]?signal-peptide


","No hits to the COGs database.","","Residues 1 to 47 match (6e-10) PD:PD049903 which is described as HI1192 PROTEOME COMPLETE SIGNAL PRECURSOR ","","","","","","","","","","","","Mon Feb 23 15:55:39 2004","Mon Feb 23 15:55:39 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02748 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:55:39 2004","","","","","","","","","","","","","1","","","" "AA02749","1925954","1927096","1143","ATGATTATTTCGTCCGCTAACGATTATCGTGAAGCCGCACGTCGCAAAGTTCCACCTTTCATGTTTCATTATGCTGACGGTGGTTCTTATGCAGAACAAACCCTAAAACGTAATGTAAACGATCTGGAAAATATCGCGCTTAGGCAACGTGTATTAAAAGACATGTCACAACTGGACACTCAAATTGAGCTGTTTGGAGAAAAATTATCCATACCTGCAATTCTTGCGCCCGTGGGAGCGCTGGGTATGTATGCGCGCCGCGGTGAAGTACAAGCCGCTAAAGCTGCTGCAAGCAGAAATATTCCATTTACTCTTTCGACAGTTTCAATCTGCTCTATTGAAGAAGTTGCTCCAAAGATTGATCGTCCGATGTGGTTTCAGCTTTATGTGTTGAAAGACAGAGGGTTTATGCGTAATGCTCTTGAGCGGGCAAAAGCCGCCGGTTGTTCAACTTTAGTATTTACTGTTGACATGCCAACTCCCGGTGCACGTTATCGGGATATGCACTCAGGTATGAGTGGTCCTTATAAGGAAATCCGTCGTATCATTCAAGGGATAACCCATCCCTTTTGGGCATGGGATGTCGGAGTTAAAGGTAAACCTCATACATTAGGCAATGTGTCTCACTATATGGGTAAGCAAATTGGTTTAGATGACTACATTGGTTGGCTTACAGAAAACTTTGATCCCTCTATCTCGTGGAAAGATTTGGAGTGGATCCGTGAATTCTGGGATGGTCCGATGATTATTAAGGGGATCTTAGATCCAAAAGACGCTAAAGACGCCGTACTTTTCGGTGCAGATGGTATTGTGGTGTCAAATCACGGTGGTCGTCAATTAGATGGTGTATTATCCAGTGCACGCGCCCTTCCACCGATTGCAGAAGCTGTAAAAGGTGAAATTAAAATTCTGGCAGATTCGGGTATTCGTAACGGGTTAGATATTGTCAGAATGATTGCGCTGGGGGCAGATGCCTGCATGATCGGACGCTCTTTTGTATATGCACTTGGTGCGGCAGGTCAGTTGGGCGTGGAAAATATGCTGGATATTTTCAAAAAGGAAATGCATGTTGCCATGACACTTACCAGCAATCAAAAAATTAGTGACATTACTAAAGACGCATTAGTAGATTTAAGTAAGCTA","","","42032","MIISSANDYREAARRKVPPFMFHYADGGSYAEQTLKRNVNDLENIALRQRVLKDMSQLDTQIELFGEKLSIPAILAPVGALGMYARRGEVQAAKAAASRNIPFTLSTVSICSIEEVAPKIDRPMWFQLYVLKDRGFMRNALERAKAAGCSTLVFTVDMPTPGARYRDMHSGMSGPYKEIRRIIQGITHPFWAWDVGVKGKPHTLGNVSHYMGKQIGLDDYIGWLTENFDPSISWKDLEWIREFWDGPMIIKGILDPKDAKDAVLFGADGIVVSNHGGRQLDGVLSSARALPPIAEAVKGEIKILADSGIRNGLDIVRMIALGADACMIGRSFVYALGAAGQLGVENMLDIFKKEMHVAMTLTSNQKISDITKDALVDLSKL","1927094","","L-lactate dehydrogenase","Cytoplasm","","
InterPro
IPR000262
Domain
FMN-dependent alpha-hydroxy acid dehydrogenase
PF01070\"[13-377]TFMN_dh
InterPro
IPR008259
Active_site
FMN-dependent alpha-hydroxy acid dehydrogenase, active site
PS00557\"[273-279]TFMN_HYDROXY_ACID_DH
InterPro
IPR012133
Family
Alpha-hydroxy acid dehydrogenase, FMN-dependent
PIRSF000138\"[1-381]TAlpha-hydroxy acid dehydrogenase, FMN-dependent
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[3-378]Tno description
noIPR
unintegrated
unintegrated
PTHR10578\"[24-200]T\"[221-376]T(S)-2-HYDROXY-ACID OXIDASE-RELATED
PTHR10578:SF8\"[24-200]T\"[221-376]TL-LACTATE DEHYDROGENASE


","BeTs to 14 clades of COG1304COG name: L-lactate dehydrogenase (FMN-dependent) and related alpha-hydroxy acid dehydrogenasesFunctional Class: CThe phylogenetic pattern of COG1304 is aompkzy--drlbcefgh-n-jx-t-Number of proteins in this genome belonging to this COG is","Significant hit (2.4e-148) to 6/6 blocks of the IPB000262 family, which is described as \"FMN-dependent alpha-hydroxy acid dehydrogenases\". Interpro entry for IP:IPR000262. IPB000262A 17-65 1.2e-20 IPB000262B 66-113 5.2e-21 IPB000262C 125-170 4.7e-29 IPB000262D 229-257 1.2e-17 IPB000262E 258-294 3.3e-24 IPB000262F 299-351 6.2e-30Significant hit ( 2.4e-07) to 1/6 blocks of the IPB001093 family, which is described as \"IMP dehydrogenase / GMP reductase\". Interpro entry for IP:IPR001093. IPB001093D 302-341 2.4e-07Significant hit ( 9.7e-05) to 2/8 blocks of the IPB001295 family, which is described as \"Dihydroorotate dehydrogenase\". Interpro entry for IP:IPR001295. IPB001295F 258-276 6.9 IPB001295H 301-331 0.0074","Residues 333 to 376 match (6e-12) PD:PD529437 which is described as L-LACTATE PROTEOME DEHYDROGENASE COMPLETE OXIDOREDUCTASE FLAVOPROTEIN CYTOCHROME FMN ","","","","","","","","","","","","Wed Jan 22 11:52:41 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02749 is paralogously related to AA00629 (3e-04).","","","","","","Residues 13 to 377 (E-value = 4e-220) place AA02749 in the FMN_dh family which is described as FMN-dependent dehydrogenase (PF01070)","","","","","Dong JM, Taylor JS, Latour DJ, Iuchi S, Lin EC.Three overlapping lct genes involved in L-lactate utilization by Escherichia coli.J Bacteriol. 1993 Oct;175(20):6671-8.PMID: 8407843Dong JM, Taylor JS, Latour DJ, Iuchi S, Lin EC.Three overlapping lct genes involved in L-lactate utilization by Escherichia coli.J Bacteriol. 1993 Oct;175(20):6671-8.PMID: 8407843Sofia HJ, Burland V, Daniels DL, Plunkett G, Blattner FR.Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes.Nucleic Acids Res. 1994 Jul;22(13):2576-86.PMID: 8041620","","Wed Jan 22 11:52:41 2003","1","","","" "AA02750","1927229","1927122","108","TTGGTTAACAGGGTGATTTTTTATGCTTATTTTTTAGGCGTGAATTCTTGGTTTTTGATTATTATGGTTTCACTCAAATTAAAGGCGGCGTATATAAAATACGCCGTT","","","4210","LVNRVIFYAYFLGVNSWFLIIMVSLKLKAAYIKYAV","1927122","","hypothetical protein","Periplasm, Cytoplasm, Extracellular","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-29]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:52:45 2004","Mon Feb 23 15:52:45 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02750 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:52:45 2004","","","","","","","","","","","","","1","","","" "AA02751","1927342","1928928","1587","ATGGCTCTTTTCTTAAGTGTCTTTCCAATAATTCTATTAATTTATTTAATGGTTAACCGCAATGCTTTACCATCTTATATAGCGCTCCCTTGGATTGCTGCCGTGGTATTTATTATCCAACTAGTATTCTTCGGTACCGATATTACTATTGTTAGTGCAAACATCGCTTCAGCATTAGTTGCAGTACAGACACCGGTTACAGTAATCTTTGGTGCAATTTTATTTAACCGCTTTTCAGAAATCTCCGGAGCCACAAATACACTGCGCAAATGGTTAGGAAATATTAATCCTAATCCTGTTGCTCAGATTATGATTATCGGCTGGTCTTTCACTTTCATGATTGAAGGTGCCAGTGGTTTTGGTACACCAGCAGCGATTGCCGCACCTATTTTAGTAGGGCTAGGCTTTCCTGCACTAAAAGTAGCAATGTTAACGCTGGTAATGAATTCCGTACCGGTTTCTTTCGGTGCAGTGGGCACGCCAACATGGTTCGGTTTTGGTCCGTTAAATCTAACAGAAAATCAAATTCTTGAAATTGGTTCTATGTCGGCTCTAATTCATAGTATAGCGGCACTTATTATTCCACTTATTGCATTGCGCTTTATCGTCAGTAGCAAAGAAATCATCAAAAATATTCGATATATTTATCTGTCAATTTTCTCTTGTACCGTACCCTACTTTTTACTGGCGCAAGTTAATTATGAATTTCCGGCACTGGTAGGAGGCGCTATCGGTCTGTTTATTTCAATTTTTCTAGCTAATAGAGGTATTGGTTTGGAAAAAACCGAGAATGCATTAAATGGTCCTGTGGTTAATTTCCCAAATGTAGTTAAAGCGTTATTCCCTACCGGATTATTAATCATAATCTTAATCATAACCCGCCTACAGCAACTTCCATTTAAATCTATAATGAACGACACTACGTCATGGTTCAGTGTTCAGCTGGGTTCATTAGGAACTTTCGACATAAGCAGAGGGTTAATTCTCAGCTTAAAAGATATTTTCTCAACTCAAATCAGCGCAAGCTATAAATTACTCTATGTACCGGCATTACTGCCATTTATTGTCACTGTATTGATTGCAATTCCGATATTTTCTATTACTAAAACCCAAGCTAAAGATATTTTTGCCAGTAGTTTCAAACAAACAAAGAACCCATTCTTTGCGCTTGTCGGGGCATTAATCATGGTAAATCTGATGTTAGTCGGTGGCGATAATTCAATGGTAAAAATCATCGGTAAAAGTTTTGCAGAAGCAACCGGTCAGTATTGGACTATATTTTCTTCATACTTAGGGGCAGTAGGGGCTTTCTTCTCCGGTTCAAATACAGTGTCTAATCTAACTTTCGGTAGCGTACAGCTTTCTACTGCTGAACTGACCGGATTGTCCTCTACTTTGATACTTGCATTACAATCTGTAGGCGGTTCAATGGGTAATATGGTATGCATCAACAACATCGTTGCCGTTAGCTCAGTACTGAACATTAACAATGTAGAAGGCGTAATAATCAAGCGTACCGTGTTACCGATGATCATTTACGGTATTATCGCGGCCATTGTTGCCATTACAATTGTCCCTCTTATCTAT","","","56670","MALFLSVFPIILLIYLMVNRNALPSYIALPWIAAVVFIIQLVFFGTDITIVSANIASALVAVQTPVTVIFGAILFNRFSEISGATNTLRKWLGNINPNPVAQIMIIGWSFTFMIEGASGFGTPAAIAAPILVGLGFPALKVAMLTLVMNSVPVSFGAVGTPTWFGFGPLNLTENQILEIGSMSALIHSIAALIIPLIALRFIVSSKEIIKNIRYIYLSIFSCTVPYFLLAQVNYEFPALVGGAIGLFISIFLANRGIGLEKTENALNGPVVNFPNVVKALFPTGLLIIILIITRLQQLPFKSIMNDTTSWFSVQLGSLGTFDISRGLILSLKDIFSTQISASYKLLYVPALLPFIVTVLIAIPIFSITKTQAKDIFASSFKQTKNPFFALVGALIMVNLMLVGGDNSMVKIIGKSFAEATGQYWTIFSSYLGAVGAFFSGSNTVSNLTFGSVQLSTAELTGLSSTLILALQSVGGSMGNMVCINNIVAVSSVLNINNVEGVIIKRTVLPMIIYGIIAAIVAITIVPLIY","1928926","[FUNCTION] Transports L-lactate across the membrane. Can also transport D-lactate and glycolate. Seems to be driven by a proton motive force (By similarity).","L-lactate permease","Inner membrane, Cytoplasm","","
InterPro
IPR003804
Family
L-lactate permease
PF02652\"[1-524]TLactate_perm
TIGR00795\"[1-526]TlctP: transporter, lactate permease (LctP)
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide
tmhmm\"[21-41]?\"[55-75]?\"[90-110]?\"[116-136]?\"[145-165]?\"[179-199]?\"[214-232]?\"[238-258]?\"[273-293]?\"[345-365]?\"[386-404]?\"[423-441]?\"[451-469]?\"[475-495]?\"[510-528]?transmembrane_regions


","No hits to the COGs database.","Significant hit (5.8e-106) to 7/8 blocks of the IPB003804 family, which is described as \"L-lactate permease\". Interpro entry for IP:IPR003804. IPB003804A 67-101 8.4e-16 IPB003804B 103-129 1e-15 IPB003804C 130-159 2.7e-16 IPB003804D 164-201 5.1e-05 IPB003804E 296-310 3.5 IPB003804G 420-468 1.2e-24 IPB003804H 469-511 4.5e-20","Residues 5 to 67 match (5e-13) PD:PD349728 which is described as PROTEOME TRANSMEMBRANE COMPLETE L-LACTATE INNER PERMEASE LCTP PERMEASE MEMBRANE ","","","","","","","","","","","Wed Jan 22 11:48:52 2003","Wed Jan 22 14:31:02 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02751 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 524 (E-value = 1.8e-197) place AA02751 in the Lactate_perm family which is described as L-lactate permease (PF02652)","","","","","Dong JM, Taylor JS, Latour DJ, Iuchi S, Lin EC.Three overlapping lct genes involved in L-lactate utilization by Escherichia coli.J Bacteriol. 1993 Oct;175(20):6671-8.PMID: 8407843Sofia HJ, Burland V, Daniels DL, Plunkett G, Blattner FR.Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes.Nucleic Acids Res. 1994 Jul;22(13):2576-86.PMID: 8041620Núñez MF, Pellicer MT, Badía J, Aguilar J, Baldomà L.The gene yghK linked to the glc operon of Escherichia coli encodes a permease for glycolate that is structurally and functionally similar to L-lactate permease.Microbiology. 2001 Apr;147(Pt 4):1069-77.PMID: 11283302Núñez MF, Kwon O, Wilson TH, Aguilar J, Baldoma L, Lin EC.Transport of L-Lactate, D-Lactate, and glycolate by the LldP and GlcA membrane carriers of Escherichia coli.Biochem Biophys Res Commun. 2002 Jan;290(2):824-9.PMID: 11785976","","Wed Jan 22 14:31:02 2003","1","","","" "AA02754","1929418","1929089","330","ATGGACAATGTGAATAAATCTTTTCAGGATGTTTTGGAGTATGTGCGTATGTATCGCTTAAAAAATAAACTATTGCGCGATATGGACGATAATAATCGTAAAATCCGTGATAACCAGAAACGCGTATTGTTGTTACAAAACTTAGATCAGTACATTCGTGACGATATGTCAATTCGTGATGTGCGCACGATTATCGAAAATATGCGCGATGACTACGAAAACCGCGTGGACGACTATGTTATCCGCAATGCCGAATTGTCTAAACAACGTCGCGAAATCAGCAGCAAAATGAAGTCACAACAGAAATCCCATGGGGAATCCGCGAAAAAA","","","13524","MDNVNKSFQDVLEYVRMYRLKNKLLRDMDDNNRKIRDNQKRVLLLQNLDQYIRDDMSIRDVRTIIENMRDDYENRVDDYVIRNAELSKQRREISSKMKSQQKSHGESAKK","1929087","","conserved hypothetical protein","Periplasm, Cytoplasm","","
InterPro
IPR007458
Family
Protein of unknown function DUF496
PIRSF028773\"[1-109]TUncharacterised conserved protein
PF04363\"[8-102]TDUF496
noIPR
unintegrated
unintegrated
PD030876\"[11-103]TY836_PASMU_Q9CMI8;


","No hits to the COGs database.","","Residues 6 to 98 match (4e-21) PD:PD030876 which is described as PROTEOME COMPLETE HI1168 STY2264 CYTOPLASMIC PM0836 BU556 YEEX YPO1560 VCA0741 ","","","","","","","","","","","","Wed Jan 22 11:44:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02754 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 102 (E-value = 5.9e-60) place AA02754 in the DUF496 family which is described as Protein of unknown function (DUF496) (PF04363)","","","","","","","","1","","","" "AA02755","1929443","1929541","99","ATGAATGGCGATAATGTAGCCTTTTTTGTGAATTTCGTCAAAAAATTCGCACTTTTACAGGGGATTATTTTTCTTTCCCGCAAATTAAAAAAATTTCCG","","","3814","MNGDNVAFFVNFVKKFALLQGIIFLSRKLKKFP","1929541","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:51:27 2004","Mon Feb 23 15:51:27 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02755 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:51:27 2004","","","","","","","","","","","","","1","","","" "AA02756","1929617","1930696","1080","ATGGCGAACGTATTTAATTTCAGTGCCGGTCCGGCGATGATGCCGCAAGCGGTGTTAGAACAGGCGCAACAAGAATTACTGAACTGGCAAGGGCAAGGCACTTCGGTGATGGAAGTTAGCCACCGTGGCAAATTGTTCATGGAATTAATCACCCAATCCCAAGCGGATTTTCGTAAGCTCTATAACGTTCCTGAAAACTACCAAATCCTGTTTTTGCAAGGCGGTGCGCGCGGTCAATTCGCCGCCATTCCGATGAATTTATTACGTGAAAACTGCAAAGCCCTGTATTTAAACAGCGGTCACTGGTCTGCCACCGCCGCCAAAGAAGCCCGTTCCTTCGGCGAAATTGACGAAATCAATATTCTGGAACCGGGTGACGAATTAAAAGTAAAACCTTTAGATTTCAGCGACATCGCCGAACAATACGATTATGTGCATTACTGCCCGAACGAAACCATCAGCGGCGTAGAAATTTTTGATGTGCCGAATGTAGGCAACGGCGTGTTGGTAGGCGATTTCTCTTCCACCATTCTCTCCCGCAAAGTGGATGTCAGCAAATTCGGCTTAATTTATGCCGGTGCACAAAAAAACCTCGGTCCGGCAGGGATTACCATCGTGATCGTACGTGACGATCTCATCGGTAAGGCACGTAAAGCCACACCGTCCATTTGGAATTACGAAATTCAGAAAAACAGCGATTCCATGATCAACACCCCGCCGACTTTCGCATGGTATTTATGTGCCTTGGTATTCAAACATTTATCGGCTATCGGCGGCTTGCCGGAAATCGAAAAACGCAACCTGGTAAAAGCGAAACTGCTTTACGATTATTTGGACGGCAGCGATTTCTACCGCAATAATGTGGCGAAAGCCAACCGCTCTTTAATGAATGTCACCTTTACCACCGGCGATGATGAACTGAACGCCAAATTCATCGCCGAAGCCACCGCCGCAGGTTTACAGGCGTTAAAAGGGCACAAAGTGCTTGGCGGTATGCGCGCGTCCATTTATAACGCCATGCCGATTGAAGGCGTACAAGCATTGATTGCCTTCATGCAAAAATTCGCGGAAGAAAACGCG","","","39697","MANVFNFSAGPAMMPQAVLEQAQQELLNWQGQGTSVMEVSHRGKLFMELITQSQADFRKLYNVPENYQILFLQGGARGQFAAIPMNLLRENCKALYLNSGHWSATAAKEARSFGEIDEINILEPGDELKVKPLDFSDIAEQYDYVHYCPNETISGVEIFDVPNVGNGVLVGDFSSTILSRKVDVSKFGLIYAGAQKNLGPAGITIVIVRDDLIGKARKATPSIWNYEIQKNSDSMINTPPTFAWYLCALVFKHLSAIGGLPEIEKRNLVKAKLLYDYLDGSDFYRNNVAKANRSLMNVTFTTGDDELNAKFIAEATAAGLQALKGHKVLGGMRASIYNAMPIEGVQALIAFMQKFAEENA","1930694","[PATHWAY] Required both in major phosphorylated pathway of serine biosynthesis and in the biosynthesis of pyridoxine. ","phosphoserine aminotransferase","Cytoplasm","","
InterPro
IPR000192
Family
Aminotransferase, class V
PF00266\"[4-348]TAminotran_5
PS00595\"[187-206]TAA_TRANSFER_CLASS_5
InterPro
IPR003248
Family
Phosphoserine aminotransferase
PD001544\"[240-355]TSERC_PASMU_P57881;
TIGR01364\"[4-359]TserC_1: phosphoserine aminotransferase
InterPro
IPR015421
Domain
Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10\"[3-256]Tno description
InterPro
IPR015422
Domain
Pyridoxal phosphate-dependent transferase, major region, subdomain 2
G3DSA:3.90.1150.10\"[257-360]Tno description
noIPR
unintegrated
unintegrated
PTHR21152\"[1-359]TAMINOTRANSFERASE CLASS V
PTHR21152:SF1\"[1-359]TPHOSPHOSERINE AMINOTRANSFERASE


","BeTs to 10 clades of COG1932COG name: Phosphoserine aminotransferaseFunctional Class: H,EThe phylogenetic pattern of COG1932 is ------y---rlb-efghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit (7.1e-181) to 8/8 blocks of the IPB003248 family, which is described as \"Phosphoserine aminotransferase\". Interpro entry for IP:IPR003248. IPB003248A 6-39 2.6e-27 IPB003248B 57-87 1.4e-24 IPB003248C 94-110 2.7e-07 IPB003248D 144-156 2.7e-09 IPB003248E 172-214 3.8e-38 IPB003248F 237-284 1.2e-30 IPB003248G 293-308 2.2e-08 IPB003248H 323-355 9.6e-27","Residues 33 to 348 match (2e-07) PD:PD107690 which is described as AMINOTRANSFERASE TRANSFERASE PHOSPHOSERINE COMPLETE PROTEOME BIOSYNTHESIS PYRIDOXINE PSAT SERINE PYRIDOXAL ","","","","","","","","","","","Wed Jan 22 11:43:06 2003","Wed Jan 22 11:43:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02756 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 14 to 348 (E-value = 6.4e-113) place AA02756 in the Aminotran_5 family which is described as Aminotransferase class-V (PF00266)","","","","","O\"Gaora,P., Maskel,D., Coleman,D., Cafferkey,M. and Dougan,GCloning and characterisation of the serC and aroA genes of Yersinia enterocolitica, and construction of an aroA mutant. Gene 84(1): 23-30, 1989. PubMed: 2691337. Duncan,K. and Coggins,J.R. The serC-aro A operon of Escherichia coli. A mixed function operon encoding enzymes from two different amino acid biosynthetic pathways. Biochem. J. 234 (1): 49-57 (1986) [PubMed: 3518706].Link,A.J., Robison,K. and Church,G.M. Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis 18 (8): 1259-1313 (1997) [PubMed: 9298646].van der Zel,A., Lam,H.M. and Winkler,M.E. Extensive homology between the Escherichia coli K-12 SerC(PdxF) aminotransferase and a protein encoded by a progesterone-induced mRNA in rabbit and human endometria. Nucleic Acids Res. 17 (20): 8379 (1989) [PubMed: 2682527].","","Wed Jan 22 11:43:06 2003","1","","","" "AA02757","1930774","1931868","1095","ATGCAATATATCGATCGCGCCAATGAAGGCGTCAAAACCCTTTTGCCTTATCAAGCCGGCAAACCCATTGAAGAATTGGAACGCGAATTAGGCATTGAAAACATCATCAAACTCGCCTCTAACGAAAACCCTTTCGGCTTGCCGCCAAGTGCGAAAAAAGCCATTCAAGCGCAATTAGACAACCTCAACCTTTATCCCGATTCCAACGGATTTTATTTCAAACAGGCGGTTGCCGAGAAATTCGGTTTACAACCGGAGCAAATCACACTCGGCAACGGCTCCAACGATTTAATCGAGCTCATCGCCCACACCTTTGCCTCCGAACAAGATGAAGTGATTTATTCCCAATACGGCTTCATTGTTTACCCGCTGATCAGCCAGGCTTTGAACGCCAAGCGCGTGGAAATTCCGGCGAAAAATTATGGCAATGATTTGAAAGAATTTCTGAACGCCATCACGCCAAAAACCAAATTGATCTACATTGCCAACCCGAATAACCCGACGGGCAGCTTTGCAAATGCGACAGAGATTACCGACTTTTTAGCGCAAGTGCCACCGCAAGTGATTGTGGCATTGGACGAAGCCTATGTGGAATTTACCGAGCCGAGCGAACGGGTGGATTCTTTCGGTTTGTTGGCAAAATACCCGAACCTTATCGTGTGCCGCACCCTTTCTAAAGCCTACGGATTAGCCGGCTTGCGTATCGGTTATGCGGCTTCCTCAGTGGAAATCGCAGGGCTGTTAAATCGCGTACGTCAGCCCTTTAACTGCAACAGTCTGGCACTTGCCGCCGCCACAGCCGCCATTAAAGATGACGAATTTGTGGCAAAAGTTGCCGAAAATAACCGAATCGGTTTGCAATTGCTGCAAAACTTCTTTGACGAAAAAGGACTGCGCTATGTGCCGTCCAAGGGAAATTTCGTCATGTTGGATTTGCAACAGCCTGCCGTCCCCATTTATCAGGCGTTACTGCGTAAAGGCGTGATCGTGCGCCCGCTTGCAGGATATGGTTTGCCGAATCACTTGCGCATCAGCATCGGCTTGCCGGAAGAAAATCAACTTTTTTTAACCGCACTTAGCGAAATTTTAGGCTTA","","","42537","MQYIDRANEGVKTLLPYQAGKPIEELERELGIENIIKLASNENPFGLPPSAKKAIQAQLDNLNLYPDSNGFYFKQAVAEKFGLQPEQITLGNGSNDLIELIAHTFASEQDEVIYSQYGFIVYPLISQALNAKRVEIPAKNYGNDLKEFLNAITPKTKLIYIANPNNPTGSFANATEITDFLAQVPPQVIVALDEAYVEFTEPSERVDSFGLLAKYPNLIVCRTLSKAYGLAGLRIGYAASSVEIAGLLNRVRQPFNCNSLALAAATAAIKDDEFVAKVAENNRIGLQLLQNFFDEKGLRYVPSKGNFVMLDLQQPAVPIYQALLRKGVIVRPLAGYGLPNHLRISIGLPEENQLFLTALSEILGL","1931866","[PATHWAY] Histidine biosynthesis; seventh step.","histidinol-phosphate aminotransferase 2","Cytoplasm, Periplasm","Its nearest neighbor in the NR database is gi:21759205 from Pasteurella multocida.","
InterPro
IPR001176
Family
1-aminocyclopropane-1-carboxylate synthase
PR00753\"[87-107]T\"[153-177]T\"[217-241]TACCSYNTHASE
InterPro
IPR001917
Binding_site
Aminotransferase, class-II
PS00599\"[223-232]TAA_TRANSFER_CLASS_2
InterPro
IPR004839
Domain
Aminotransferase, class I and II
PF00155\"[33-359]TAminotran_1_2
InterPro
IPR005861
Family
Histidinol-phosphate aminotransferase
TIGR01141\"[8-362]ThisC: histidinol-phosphate aminotransferase
InterPro
IPR015421
Domain
Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10\"[47-271]Tno description
noIPR
unintegrated
unintegrated
PTHR11751\"[49-363]TSUBGROUP I AMINOTRANSFERASE RELATED
PTHR11751:SF3\"[49-363]THISTIDINOL-PHOSPHATE AMINOTRANSFERASE


","No hits to the COGs database.","Significant hit ( 3.1e-09) to 3/3 blocks of the IPB001511 family, which is described as \"Aminotransferases class-I\". Interpro entry for IP:IPR001511. IPB001511A 65-75 1.9e+02 IPB001511B 159-173 0.0041 IPB001511C 223-236 0.00094","Residues 54 to 124 match (4e-07) PD:PD587830 which is described as AMINOTRANSFERASE PHOSPHATE HISTIDINOL-PHOSPHATE TRANSFERASE HISTIDINE ACETOL- COMPLETE TRANSAMINASE PROTEOME IMIDAZOLE ","","","","","","","","","","","Wed Jan 22 11:34:31 2003","Wed Jan 22 11:34:31 2003","Tue May 24 09:23:48 2005","Tue May 24 09:23:48 2005","Tue May 24 09:23:48 2005","Tue May 24 09:23:48 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA02757 is paralogously related to AA02776 (4e-36), AA00084 (9e-12) and AA01458 (7e-04).","Tue May 24 09:23:48 2005","","","","","Residues 79 to 363 (E-value = 2.5e-30) place AA02757 in the Aminotran_1_2 family which is described as Aminotransferase class I and II (PF00155)","Tue May 24 09:23:48 2005","","","","Henner DJ, Band L, Flaggs G, Chen E.The organization and nucleotide sequence of the Bacillus subtilis hisH, tyrA and aroE genes.Gene. 1986;49(1):147-52.PMID: 3106153","","Tue May 24 09:23:48 2005","1","","","" "AA02758","1931942","1933210","1269","TTGCCGGGCTCGAAAAGCCTGTCCAACCGCGCCTTATTGTTGGCGGCATTGGCGCACGGCACCACCAAAGTGACCAACCTGCTGGACAGTGACGACATCCGCCATATGCTCAACGCCTTAAAACAGCTCGGTGTGCAATATACGTTGTCTGAAGACAAATCCGTATGCGAAGTACAAGGCTTGGGTGGCGCCTTTCAGTGGCACGACGGCTTGGCATTATTTTTAGGCAATGCCGGCACCGCCATGCGCCCGTTGGCGGCAGCACTTTGTTTGGCGCGTGCAGGCGATTCCGCGCAAAATGAAGTGATTTTAACGGGTGAACCGCGCATGAAAGAACGCCCGATTCGACACTTAGTGGATGCGTTGTTACAAGCGGGCGCCGATATTCGTTATTTAGAAAATGAAGGCTACCCGCCTATCGCCATTCGTAACACGGGATTACGCGGCGGTTTAATTAAAATCGACGGTTCCATTTCATCGCAATTTTTGACCGCACTTTTAATGGCGGCGCCCCTTGCGGAGAGTGACAGCGAAATCGAAATTATCGGTGAATTGGTGTCCAAACCGTACATCGACATCACACTCAACATGATGAAAATCTTCGGCGTGAGCGTGGAAAATCAACATTACCAACGCTTCATCGTAAAAGGCAAACAATCCTATCAATCACCCGGCTCATTTTTAGTGGAAGGTGATGCTTCCTCCGCCTCTTATTTCTTAGCGGCAGGCGCCATTAAGGGCAAAGTGAAAGTGACAGGCATCGGCAAAAACAGCATTCAGGGCGATCGTCTGTTTGCCGACGTCTTAGAAAAAATGGGCGCGCACATCACTTGGGGCGAGGATTTCATTCAAGCGGAACAAGCGCCGTTACATGGTGTGGATATGGACATGAACCACATTCCCGACGCCGCCATGACTATCGCCACCACCGCCCTTTTTGCGGAAGGCGAAACCGTGATTCGTAACATTTACAACTGGCGCGTGAAAGAAACGGATCGTTTAACCGCCATGGCGACGGAACTGCGCAAAGTGGGCGCGGAGGTGGAGGAAGGCGAAGATTTTATTCGCATTCAACCGTTAAAACCGACGGAATTTAAAGTGGCGGAAATCGAAACCTATAACGATCACCGCATGGCAATGTGCTTTGCGCTCATCGCCCTTTCCGACACGCCGGTAACGATTTTGGATCCGAATTGCACGGCAAAAACCTTCCCGACCTTTTTCAAGGAGTTTTTAGCCATCGCGCAACAACCGACCGGCGAAACGAAC","","","48167","LPGSKSLSNRALLLAALAHGTTKVTNLLDSDDIRHMLNALKQLGVQYTLSEDKSVCEVQGLGGAFQWHDGLALFLGNAGTAMRPLAAALCLARAGDSAQNEVILTGEPRMKERPIRHLVDALLQAGADIRYLENEGYPPIAIRNTGLRGGLIKIDGSISSQFLTALLMAAPLAESDSEIEIIGELVSKPYIDITLNMMKIFGVSVENQHYQRFIVKGKQSYQSPGSFLVEGDASSASYFLAAGAIKGKVKVTGIGKNSIQGDRLFADVLEKMGAHITWGEDFIQAEQAPLHGVDMDMNHIPDAAMTIATTALFAEGETVIRNIYNWRVKETDRLTAMATELRKVGAEVEEGEDFIRIQPLKPTEFKVAEIETYNDHRMAMCFALIALSDTPVTILDPNCTAKTFPTFFKEFLAIAQQPTGETN","1933208","From PF00275EPSP synthase (3-phosphoshikimate 1- carboxyvinyltransferase) catalyzes the sixth step in the biosynthesis from chorismate of the aromatic amino acids (the shikimate pathway) in bacteria (gene aroA).","3-phosphoshikimate 1-carboxyvinyltransferase","Cytoplasm","","
InterPro
IPR001986
Domain
3-phosphoshikimate 1-carboxyvinyltransferase
PD001867\"[1-414]TAROA_PASMU_Q04570;
G3DSA:3.65.10.10\"[8-230]Tno description
PF00275\"[1-411]TEPSP_synthase
PS00104\"[73-87]TEPSP_SYNTHASE_1
PS00885\"[327-345]TEPSP_SYNTHASE_2
InterPro
IPR006264
Domain
3-phosphoshikimate 1-carboxyvinyltransferase, subgroup
TIGR01356\"[1-417]TaroA: 3-phosphoshikimate 1-carboxyvinyltran
noIPR
unintegrated
unintegrated
PIRSF000505\"[1-421]T3-phosphoshikimate 1-carboxyvinyltransferase
PTHR21090\"[1-351]TAROM/DEHYDROQUINATE SYNTHASE
PTHR21090:SF5\"[1-351]T3-PHOSPHOSHIKIMATE 1-CARBOXYVINYLTRANSFERASE
signalp\"[1-23]?signal-peptide


","No hits to the COGs database.","Significant hit (1.1e-141) to 9/9 blocks of the IPB001986 family, which is described as \"EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase)\". Interpro entry for IP:IPR001986. IPB001986A -3-37 1.4e-21 IPB001986B 73-83 7.9e-06 IPB001986C 103-129 5e-15 IPB001986D 159-171 4.8e-10 IPB001986E 187-203 1.7e-10 IPB001986F 229-241 4.1e-09 IPB001986G 260-274 9.9e-09 IPB001986H 307-359 8.7e-39 IPB001986I 372-384 3.1e-11","Residues 321 to 386 match (2e-08) PD:PD538726 which is described as SYNTHASE AROMATIC 5- EPSP AMINO ACID EPSPS 1-CARBOXYVINYLTRANSFERASE TRANSFERASE ENOLPYRUVYLSHIKIMATE-3-PHOSPHATE ","","","","","","","","","","","Mon Jan 6 14:27:06 2003","Mon Jan 6 14:21:08 2003","","Thu Aug 4 11:06:18 2005","Thu Aug 4 11:06:18 2005","Thu Aug 4 11:06:18 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA02758 is paralogously related to AA02330 (2e-05).","Thu Aug 4 11:06:18 2005","","","","","Residues 1 to 411 (E-value = 3e-208) place AA02758 in the EPSP_synthase family which is described as EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase) (PF00275)","Thu Aug 4 11:06:18 2005","","","Del Río ML, Martín CB, Navas J, Gutiérrez-Muñiz B, Rodríguez-Barbosa JI, Rodríguez Ferri EF.aroA gene PCR-RFLP diversity patterns in Haemophilus parasuis and Actinobacillus species.Res Vet Sci. 2005 Jun.PMID: 15936788","Tatum,F.M., Briggs,R.E. and Halling,S.M. Molecular gene cloning and nucleotide sequencing and construction of an aroA mutant of Pasteurella haemolytica serotype A1 Appl. Environ. Microbiol. 60 (6), 2011-2016 (1994) PubMed: 8031095 Parish T, Stoker NG. The common aromatic amino acid biosynthesis pathway is essential in Mycobacterium tuberculosis. Microbiology. 2002 Oct;148(Pt 10):3069-77. PMID: 12368440 Padgette SR, Re DB, Gasser CS, Eichholtz DA, Frazier RB, Hironaka CM, Levine EB, Shah DM, Fraley RT, Kishore GM.Site-directed mutagenesis of a conserved region of the5-enolpyruvylshikimate-3-phosphate synthase active site.J Biol Chem 1991 Nov 25;266(33):22364-9PMID: 1939260 ","Thu Aug 4 11:06:18 2005","Mon Jan 6 14:25:53 2003","1","","","" "AA02762","1933768","1933304","465","ATGCGCAAACAAATCGAAATTTTTACCGACGGATCCTGCCTCGGCAACCCCGGTGCGGGCGGTATCGGCATTTTGTTACGTTACAAACAACACGAAAAAAAACTGTCCAAAGGCTTTTTTTTGACCACTAATAACCGCATGGAATTATTGGCGGTGGTGGAAGCCCTAAACAGCCTAAAAGAGCCCTGCGACATTCATTTATACAGCGACAGCCAATACATGAAAAACGGCATCACCCAGTGGATTTTTAACTGGAAGAAAAATCATTGGAAAGCGAGTAGCGGCAAACCGGTGAAAAATCAGGATTTGTGGATGGCGTTAGATCAGGCGATCGCCCGCCATAAGGTGGATTGGCGTTGGGTGAAAGGGCACGCGGGGCATCGTGAAAATGAAATTTGCGATCAACTGGCAAAGCAGGGCGCAGAGAACCCGACGTTAAACGATGAAGGTTATCAACCGGAAGCA","","","17720","MRKQIEIFTDGSCLGNPGAGGIGILLRYKQHEKKLSKGFFLTTNNRMELLAVVEALNSLKEPCDIHLYSDSQYMKNGITQWIFNWKKNHWKASSGKPVKNQDLWMALDQAIARHKVDWRWVKGHAGHRENEICDQLAKQGAENPTLNDEGYQPEA","1933302","","ribonuclease H","Cytoplasm, Extracellular","","
InterPro
IPR002156
Domain
Ribonuclease H
PF00075\"[2-142]TRnaseH
PS50879\"[1-142]TRNASE_H
noIPR
unintegrated
unintegrated
G3DSA:3.30.420.10\"[1-155]Tno description
PTHR10642\"[1-143]TRIBONUCLEASE H1


","BeTs to 16 clades of COG0328COG name: Ribonuclease HIFunctional Class: LThe phylogenetic pattern of COG0328 is -o----y--dr-bcefghsnujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 8.3e-12) to 3/3 blocks of the IPB002156 family, which is described as \"RNase H\". Interpro entry for IP:IPR002156. IPB002156A 7-17 0.0025 IPB002156B 64-74 0.0045 IPB002156C 129-138 0.15","Residues 113 to 141 match (2e-07) PD:PD590532 which is described as RIBONUCLEASE H COMPLETE PROTEOME HYDROLASE HI RNASE MAGNESIUM ENDONUCLEASE NUCLEASE ","","","","","","","","","","","","Tue Jan 14 15:34:18 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02762 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 142 (E-value = 4.8e-63) place AA02762 in the RnaseH family which is described as RNase H (PF00075)","","","","","Kanaya,S., Kimura,S., Katsuda,C. and Ikehara,M. Role of cysteine residues in ribonuclease H from Escherichia coli. Site-directed mutagenesis and chemical modification The Biochemical journal. 271 (1), 59-66 (1990) PubMed: 2171503 Katayanagi,K., Miyagawa,M., Matsushima,M., Ishikawa,M., Kanaya,S., Ikehara,M., Matsuzaki,T. and Morikawa,K. Three-dimensional structure of ribonuclease H from E. coli Nature. 347 (6290), 306-309 (1990) PubMed: 1698262 Katayanagi,K., Miyagawa,M., Matsushima,M., Ishikawa,M., Kanaya,S., Nakamura,H., Ikehara,M., Matsuzaki,T. and Morikawa,K. Structural details of ribonuclease H from Escherichia coli as refined to an atomic resolution Journal of molecular biology. 223 (4), 1029-1052 (1992) PubMed: 1311386 Yang,W., Hendrickson,W.A., Crouch,R.J. and Satow,Y. Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein Science. 249 (4975), 1398-1405 (1990) PubMed: 2169648 Ishikawa,K., Kimura,S., Kanaya,S., Morikawa,K. and Nakamura,H. Structural study of mutants of Escherichia coli ribonuclease HI with enhanced thermostability Protein engineering. 6 (1), 85-91 (1993) PubMed: 8381958 Katayanagi,K., Ishikawa,M., Okumura,M., Ariyoshi,M., Kanaya,S., Kawano,Y., Suzuki,M., Tanaka,I. and Morikawa,K. Crystal structures of ribonuclease HI active site mutants from Escherichia coli The Journal of biological chemistry. 268 (29), 22092-22099 (1993) PubMed: 8408067 Kashiwagi,T., Jeanteur,D., Haruki,M., Katayanagi,K., Kanaya,S. and Morikawa,K. Proposal for new catalytic roles for two invariant residues in Escherichia coli ribonuclease HI Protein engineering. 9 (10), 857-867 (1996) PubMed: 8931125 Yamazaki,T., Yoshida,M., Kanaya,S., Nakamura,H. and Nagayama,K. Assignments of backbone 1H, 13C, and 15N resonances and secondary structure of ribonuclease H from Escherichia coli by heteronuclear three-dimensional NMR spectroscopy Biochemistry. 30 (24), 6036-6047 (1991) PubMed: 1646006 Yamasaki,K., Ogasahara,K., Yutani,K., Oobatake,M. and Kanaya,S. Folding pathway of Escherichia coli ribonuclease HI: a circular dichroism, fluorescence, and NMR study Biochemistry. 34 (51), 16552-16562 (1995) PubMed: 8527428","","Tue Jan 14 15:34:18 2003","1","","","" "AA02763","1933836","1934537","702","ATGAGTATTCAAATTAACCCGAATCGCCAAATTGTACTGGATACGGAAACCACCGGTATGAACCAGTTAGGCGCCCATTATGAAGGTCATTGCATCATTGAAATCGGTGCGGTGGAAATGATTAACCGCCGTTATACCGGCAATAATTTTCACATTTATATTAAGCCGAATCGTCCGGTGGATCCCGATGCTATTAAGGTACACGGTATCACCGACGAAATGCTGGCGGACAAACCGGATTTCAGTCAGGCCGCCAATGAATTCATCGAATATATCAAAGGCGCCGAGTTGCTTATTCACAACGCGCCCTTCGACGTGGGCTTCATGGATTATGAATTCGCCAAGCTGAACCTGCCGATTAAAACCAACGACATTTGCCTGGTGACCGACACGCTGACCATGGCGCGTCAAATGTATCCCGGCAAGAAAAATAACTTGGATGCGCTCTGTAGCCGTTTGGGGATAGATAACAGTAAACGTACGCTACACGGCGCGTTACTGGATGCGGAGATTCTGGCGGATGTATATCTTGCCATGACGGGCGGGCAAACCAGCCTGTTTGATGAAAGTGAACCGGAAAATTATTCAGCACGCCGGCGAACAGCAAGTACAAAGTGCGGTCGTTTTTTCACACAATTTACGCCTGCTCACCCCGACGGAAGAAGAACTGCAGGCGCATTTGGAGTACCTCAAATTAATCAA","","","29364","MSIQINPNRQIVLDTETTGMNQLGAHYEGHCIIEIGAVEMINRRYTGNNFHIYIKPNRPVDPDAIKVHGITDEMLADKPDFSQAANEFIEYIKGAELLIHNAPFDVGFMDYEFAKLNLPIKTNDICLVTDTLTMARQMYPGKKNNLDALCSRLGIDNSKRTLHGALLDAEILADVYLAMTGGQTSLFDESEPENYSARRRTASTKCGRFFTQFTPAHPDGRRTAGAFGVPQINQ","1934592","","DNA polymerase III, epsilon subunit","Cytoplasm","","
InterPro
IPR006054
Domain
DNA polymerase III, epsilon subunit
TIGR00573\"[8-223]Tdnaq: exonuclease, DNA polymerase III, epsi
InterPro
IPR006055
Domain
Exonuclease
SM00479\"[9-185]TEXOIII
InterPro
IPR006309
Family
DNA polymerase 3, epsilon subunit
TIGR01406\"[9-230]TdnaQ_proteo: DNA polymerase III, epsilon su
InterPro
IPR013520
Domain
Exonuclease, RNase T and DNA polymerase III
PF00929\"[10-176]TExonuc_X-T
noIPR
unintegrated
unintegrated
G3DSA:3.30.420.10\"[3-187]Tno description


","BeTs to 16 clades of COG0847COG name: DNA polymerase III epsilon subunit and related 3'-5' exonucleasesFunctional Class: LThe phylogenetic pattern of COG0847 is a--p--yqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","","Residues 13 to 176 match (4e-07) PD:PD290303 which is described as COMPLETE PROTEOME DNA III EPSILON POLYMERASE SUBUNIT SIMILAR PROBABLE ARABIDOPSIS ","","","","","","","","","","","","Tue Jan 14 15:36:54 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02763 is paralogously related to AA02867 (2e-07).","","","","","","Residues 10 to 176 (E-value = 8.5e-53) place AA02763 in the Exonuc_X-T family which is described as Exonuclease (PF00929)","","","","","Cox,E.C. and Horner,D.L. DNA sequence and coding properties of mutD(dnaQ) a dominant Escherichia coli mutator gene J. Mol. Biol. 190 (1), 113-117 (1986) PubMed: 3023634 Maki,H., Horiuchi,T. and Sekiguchi,M. Structure and expression of the dnaQ mutator and the RNase H genes of Escherichia coli: overlap of the promoter regions Proc. Natl. Acad. Sci. U.S.A. 80 (23), 7137-7141 (1983) PubMed: 6316347 Takano,K., Nakabeppu,Y., Maki,H., Horiuchi,T. and Sekiguchi,M. Structure and function of dnaQ and mutD mutators of Escherichia coli Mol. Gen. Genet. 205 (1), 9-13 (1986) PubMed: 3540531 O'Donnell,M. Accessory protein function in the DNA polymerase III holoenzyme from E. coli Bioessays 14 (2), 105-111 (1992) PubMed: 1575709 ","","Tue Jan 14 15:36:54 2003","1","","","" "AA02766","1935205","1935071","135","GTGACGCANATAAAAGGCTGGTTGNNGTTACGGTTTAATANTGGCTACGGCACCATCTTGGNCTTGCGTACGCAANTGCCCATTGGGTCCNNNCGTTTTAAATCGGTAATGCTTGCGGCTTGTTGTGTCAAAATT","","","4338","VTXIKGWLXLRFNXGYGTILXLRTQXPIGSXRFKSVMLAACCVKI","1935071","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-17]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:49:49 2004","Mon Feb 23 15:49:49 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02766 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:49:49 2004","","","","","","","","","","","","","1","","","" "AA02767","1935341","1935517","177","TTGANTAAAAGGGCTTTAAAAGAGTGGCAAAAGTTAGGCGATACNCATACNGCCAACAATTCAAAAATAAACTTGCGGANACGCTTANGAAAATCCGAGNAGTANCCGGGCGACAAATTAAGAGGTTATCAAAACCTTTATAAAATCAAACTCCGCGCNAGCNCGGTNTATCNNGCT","","","6067","LXKRALKEWQKLGDTHTANNSKINLRXRLXKSEXXPGDKLRGYQNLYKIKLRASXVYXA","1935517","","conserved hypothetical protein (possible stability determinant)","Cytoplasm, Periplasm","This sequence is simnilar to gi3986434, a possible stability protein StbE from Morganella morganii.AA02767 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus ducreyi gene.AA02767 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus influenzae Rd gene.","No hits reported.","No hits to the COGs database.","Significant hit ( 2.9e-07) to 2/2 blocks of the IPB002776 family, which is described as \"Protein of unknown function DUF79\". Interpro entry for IP:IPR002776. IPB002776A 10-24 0.26 IPB002776B 44-56 0.00055","Residues 6 to 82 match (3e-21) PD:PD020125 which is described as COMPLETE PROTEOME PLASMID RELE INNER CYTOPLASMIC VLP VCA0478 STBE STABILITY ","","","","","Mon Jan 10 10:01:25 2005","","","Mon Jan 10 10:01:25 2005","Mon Jan 10 10:01:25 2005","","","Sat Feb 28 11:27:34 2004","Sat Feb 28 11:27:34 2004","Mon Jan 10 09:59:30 2005","Mon Jan 10 10:03:47 2005","Mon Jan 10 09:59:30 2005","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found to this sequence.AA02767 is paralogously related to AA02259 (3e-11).","Mon Jan 10 09:59:30 2005","Sat Feb 28 11:24:40 2004","No hits to the PDB database.","","","Residues 4 to 88 (E_value = 0.00021) place AA1817 in the DUF79 family which is described as Protein of unknown function DUF79.","Sat Feb 28 11:24:40 2004","","","","","","","1","","","" "AA02768","1935865","1935680","186","GTGNATGCTTTGGTGACAATATTGGAAGGCAAAGCCAGAATCNACTATNCGACANCAACCGACTACGAAGTCAATGCCGGCGAAAGTATCGTGCTGCCTGCGGACATTCCCCATGCTTTGTATNGCCTTGGAGAATTTCAAAATGTTCTTGACGGTGGTGTTCCCGAAAGAGGGGAGATAGTGAGG","","","6165","VXALVTILEGKARIXYXTXTDYEVNAGESIVLPADIPHALYXLGEFQNVLDGGVPERGEIVR","1935680","","conserved hypothetical protein","Cytoplasm","This sequence is similar to gi|15675470, a predicted conserved hypothetical protein from Streptococcus pyogenes. ","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:33:57 2004","Mon Feb 23 15:33:57 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA1818.AA02768 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:33:57 2004","","","","","","","","","","","","","1","","","" "AA02769","1935993","1935853","141","ATGATCTTCTGGCATNATCAAGACGGACAAGTTATCAGCAAANACATTTTCACAAAACCCTGCCGTGGGCTTAACNCATGTTTTNGTCTGCCGAAAGGCGAGGAAATCAGCGCCCATAANATCCCGTGGTGNATGCTTTGG","","","4841","MIFWHXQDGQVISKXIFTKPCRGLNXCFXLPKGEEISAHXIPWXMLW","1935853","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:30:03 2004","Mon Feb 23 15:30:03 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA1818.AA02769 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:30:03 2004","","","","","","","","","","","","","1","","","" "AA02770","1936087","1935980","108","TTGAGCGANCNANAGCAGTTTNNGATTTGNANCGATTTAAAAGGANGCAAAAATATGTTAAAAAACATTGAAAAAGCCACCGTTCTTAAATTGAATGATCTTCTGGCA","","","3254","LSXXXQFXIXXDLKGXKNMLKNIEKATVLKLNDLLA","1935980","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:27:37 2004","Mon Feb 23 15:27:37 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA1818.AA02770 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:27:59 2004","","","","","","","","","","","","","1","","","" "AA02772","1936384","1936836","453","ATGAAAATCTTAACTTGGCCTGTGGGTTGCAGGTGCTGCACTTGGTATCGTTGCTCCACTTCTAACCTACAATGGCAATCCCGGCAATATGGGCTTCTGCGCAGCCTGTTTCTTGCGCGACACAGCGGGCGCACTCGGTCTGCATCGCGCCACACCGTTACAATATTTACGCCCCGAACTTATCGGTTTGGTATTGGGCGCATTCTCCCATGGCACTTTGCGGACTTTGCTTCTTCGCTCGGTGGCGGTTGCCCGGGCAAAAAATTGGTGAACATCGGCGAAGGCAATAATGACGCCGCCCTCTTTGTATTAGGAATGGTGTTAGGTGCTACCGCCGCGCATAATTTTGCGCTCGCTGCTTCCCCTGCCGGCGTGACACAATTCACGCCTTATGTATTCGTCATCGGTTTTGTGGTCTGCCTTTATATCGGACTGACGAATAAATCCAAGATT","","","15662","MKILTWPVGCRCCTWYRCSTSNLQWQSRQYGLLRSLFLARHSGRTRSASRHTVTIFTPRTYRFGIGRILPWHFADFASSLGGGCPGKKLVNIGEGNNDAALFVLGMVLGATAAHNFALAASPAGVTQFTPYVFVIGFVVCLYIGLTNKSKI","1936670","","hypothetical protein","Extracellular, Inner membrane","","
noIPR
unintegrated
unintegrated
tmhmm\"[98-118]?\"[128-146]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Tue Jan 14 16:01:21 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02772 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02773","1936976","1936839","138","TTGCCCAAGGCAAATCGTAAGGACGGCTATTTTAGGCGGATTTTGGTTTTTGTAAAGGAAAAGTGCGGTGGGTTTTTTCGGTGTTTTTTAACGCAAAACGCCCGCTTGGTTTGCGGGCGTGGAAATTTCGGTAAAGGT","","","5251","LPKANRKDGYFRRILVFVKEKCGGFFRCFLTQNARLVCGRGNFGKG","1936839","","hypothetical protein","Cytoplasm, Extracellular","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:24:58 2004","Mon Feb 23 15:24:58 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02773 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:24:58 2004","","","","","","","","","","","","","1","","","" "AA02774","1937010","1938395","1386","ATGACAACCCCATTTAAACCTGAATTACTTTCTCCTGCCGGCTCGTTGAAAAATATGCGCTATGCCTTTGCTTACGGTGCAGATGCGGTTTATGCCGGTCAGCCACGTTACAGCCTGCGCGTGCGCAACAACGAGTTCAATCACGCCAATTTAAAAATCGGCATTGATGAAGCTCACGCCCTCGGCAAAAAATTCTATGTGGTGGTGAACATCGCGCCACATAATTCCAAGCTCAAAACCTTTATCAAAGATTTACAACCGGTCATCGACATGGGGCCGGATGCGTTAATTATGTCCGATCCGGGCTTGATCATGCTGGTACGCGAAAACTTCCCCAACATTGACATTCACCTTTCCGTGCAAGCCAACGCGGTAAACTGGGCGACGGTGAAATTCTGGAAACAAATGGGCTTAACCCGCGTGATTTTATCCCGCGAGCTTTCCCTTGATGAAATCGCCGAAATCCGCCAGCACGTGCCGGATATTGAACTTGAAATTTTCGTTCACGGCGCACTTTGCATGGCGTATTCCGGTCGTTGTCTGCTTTCCGGCTATATCAACAAACGCGACCCGAACCAAGGCACCTGTACCAACGCTTGCCGTTGGGAATATAAAATGGAAGAAGGCAAAGTGGATGACGTCGGCAACATCGTGCCGAAAATCGATCCGCGCCAACAAATTGAAGTGAAAAACGTCGCCCCGACGTTGGGCGAAGGCACCGTGACCGACAAAGTGTTCCTTTACACCGAAGCACAAAATCCCGACGAGCAAATGACCGCCTTTGAAGACGAGCACGGTACTTATTTCATGAACTCCAAAGATTTACGCGCCGTGCAACATGTGGAAAAATTGACCGCACTTGGCGTGTATTCCTTAAAAATTGAGGGGCGCACCAAATCCTTCTATTACTGCGCCCGTACTGCGCAAGTTTACCGCAAAGCGATCGACGATGCGGCTGCCGGCAAACCATTCGACGAAAGCCTGATGGATACGTTGGAATCTTTGGCGCACCGTGGCTACACCGAAGGCTTTCTGCGCCGCCACACCCATGATGAATACCAAAACTACGAATACGGCTATTCCATTTCCGAACGTCAACAATTCGTCGGTGAATTCACCGGCAAACGTAACGAACAAGGCATGGCGGAAGTGGCGGTGAAAAATAAATTCCTGCTTGGCGACGAAGTGGAAATAATGACACCGCAAGGCAATATCGTCTTCAAAATCAATAAAATGCTTAATCGCAAAAACGTCGAAGTAGATGCCGCATTAGGCGACGGACATTTTGTCTTCTTAGACGTGCCGCAAGACATCAACTTGGATTACGCGCTGTTAATGCGAAACCTGGTCAACACCAACACACGCAACCCTCACGAAAAGAAAAGT","","","53345","MTTPFKPELLSPAGSLKNMRYAFAYGADAVYAGQPRYSLRVRNNEFNHANLKIGIDEAHALGKKFYVVVNIAPHNSKLKTFIKDLQPVIDMGPDALIMSDPGLIMLVRENFPNIDIHLSVQANAVNWATVKFWKQMGLTRVILSRELSLDEIAEIRQHVPDIELEIFVHGALCMAYSGRCLLSGYINKRDPNQGTCTNACRWEYKMEEGKVDDVGNIVPKIDPRQQIEVKNVAPTLGEGTVTDKVFLYTEAQNPDEQMTAFEDEHGTYFMNSKDLRAVQHVEKLTALGVYSLKIEGRTKSFYYCARTAQVYRKAIDDAAAGKPFDESLMDTLESLAHRGYTEGFLRRHTHDEYQNYEYGYSISERQQFVGEFTGKRNEQGMAEVAVKNKFLLGDEVEIMTPQGNIVFKINKMLNRKNVEVDAALGDGHFVFLDVPQDINLDYALLMRNLVNTNTRNPHEKKS","1938229","","collagenase prtC homolog, possible protease","Cytoplasm","","
InterPro
IPR001539
Family
Peptidase U32
PD004398\"[93-317]TQ6MKQ7_BDEBA_Q6MKQ7;
PF01136\"[78-351]TPeptidase_U32
PS01276\"[165-183]TPEPTIDASE_U32


","No hits to the COGs database.","Significant hit ( 3.6e-67) to 3/3 blocks of the IPB001539 family, which is described as \"Peptidase family U32\". Interpro entry for IP:IPR001539. IPB001539A 8-33 1.9e-15 IPB001539B 161-201 1.3e-32 IPB001539C 291-316 1.3e-16","Residues 8 to 79 match (3e-10) PD:PD512036 which is described as PROTEOME COMPLETE PROTEASE PROBABLE YRRN LIN0959 LIN0960 SAV1613 SP0801 LMO0960 ","","","","","","","","","","","","Tue Jan 14 16:03:41 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02774 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 78 to 351 (E-value = 5.9e-143) place AA02774 in the Peptidase_U32 family which is described as Peptidase family U32 (PF01136)","","","","","","","","1","","","" "AA02775","1938695","1939783","1089","ATGCGTGTTGCCGATTTTTATTTTGATTTACCTGATGAGTTGATTGCCCGTTATCCGAAAACGGAGCGGACAGCCAGCCGATTGTTACAACTGGATGGTGAAAACGGGGAAATTTTTCACCGCACTTTTAGTGATGTGTTGGATCTGATTAACCCCGGCGATTTGATGATCTTCAATAATACCCGTGTGATTCCTGCACGGATGTTCGGGCGTAAAAGCAGTGGCGGGAAAATAGAGGTGTTGGTGGAGCGGGTGTTAAGCGAATCCCGTTTTTTAGCTCATGTTCGCGCCTCCAAAGCACCGAAGGAAGGCGCGGAATTGATCTTAGGCGAGGATAAACTGGGAGAAGGTCACGGCGTAAACGCCGTCATGGTGGGGCGTCAAGGCAGTTTGTTTGAGATCGAAATAGCCGAAAAACAGACCGCACTTTTTGATGTATTGCAGAAAATCGGGCACATGCCGTTGCCGCCGTATATCGATCGCCCCGATGAAGAAGCGGATCAGGAACGCTACCAAACCGTGTATAACAAAGTGCCCGGCGCGGTTGCCGCCCCAACGGCAGGGCTACATTTTGACGATGAATTGTTGACGAAACTCAAAGCCAAAGGGGTAAATTTTACCTTTGTTACGCTACACGTTGGGGCGGGAACATTTCAGCCGGTTCGCGTGGAAAATATTGAAGATCACGTGATGCACGCGGAATATGTGGAAGTGCCGCAAGAAGTGTGTGATGCCATTTTGGCGACCCAAAAAGCCGGTAAACGGGTGATTGCGGTAGGGACAACCTCCGTGCGTTCCATTGAAAGTGCGGCATTGGCAGCGGAAGAGAAGAAAAGTGCGGTGCTTATTGAGCCTTATTTTTCCGATACGTCCATTTTTATTTATCCGGGCAAATCGTTCCGCGTGGTGGATTGCCTGATTACCAATTTCCATTTGCCGGAAAGCACGTTAATTATGTTGGTTTCCGCCTTTGCGGGTTTTTCCTATACGATGAATGCCTATAAAAGTGCGGTAGAAAATCGCTATCGTTTTTTCAGTTACGGCGATGCAATGTTTATCAGTAAAAATCCTGATGTGAAGGGATTGAAA","","","40335","MRVADFYFDLPDELIARYPKTERTASRLLQLDGENGEIFHRTFSDVLDLINPGDLMIFNNTRVIPARMFGRKSSGGKIEVLVERVLSESRFLAHVRASKAPKEGAELILGEDKLGEGHGVNAVMVGRQGSLFEIEIAEKQTALFDVLQKIGHMPLPPYIDRPDEEADQERYQTVYNKVPGAVAAPTAGLHFDDELLTKLKAKGVNFTFVTLHVGAGTFQPVRVENIEDHVMHAEYVEVPQEVCDAILATQKAGKRVIAVGTTSVRSIESAALAAEEKKSAVLIEPYFSDTSIFIYPGKSFRVVDCLITNFHLPESTLIMLVSAFAGFSYTMNAYKSAVENRYRFFSYGDAMFISKNPDVKGLK","1939617","","S-adenosylmethionine:tRNA ribosyltransferase-isomerase (Queuosine biosynthesis protein queA)","Cytoplasm","","
InterPro
IPR003699
Family
Queuosine biosynthesis protein
PF02547\"[1-223]TQueuosine_synth
TIGR00113\"[1-354]TqueA: S-adenosylmethionine:tRNA ribosyltran


","BeTs to 15 clades of COG0809COG name: S-adenosylmethionine:tRNA-ribosyltransferase-isomerase (queuine synthetase)Functional Class: JThe phylogenetic pattern of COG0809 is -------qvd-lbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","Significant hit (9.4e-140) to 6/6 blocks of the IPB003699 family, which is described as \"Queuosine biosynthesis protein\". Interpro entry for IP:IPR003699. IPB003699A 1-31 5.8e-18 IPB003699B 43-72 5.3e-22 IPB003699C 145-161 1.3e-11 IPB003699D 167-204 9.1e-29 IPB003699E 253-268 4.3e-10 IPB003699F 303-353 2.7e-43","Residues 1 to 353 match (1e-170) PD:PD009740 which is described as PROTEOME COMPLETE TRANSFERASE ISOMERASE RIBOSYLTRANSFERASE-ISOMERASE BIOSYNTHESIS S-ADENOSYLMETHIONINE:TRNA QUEUOSINE QUEA 5.-.-.- ","","","","","","","","","","","","Tue Jan 14 16:05:59 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02775 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 223 (E-value = 2.4e-134) place AA02775 in the Queuosine_synth family which is described as Queuosine biosynthesis protein (PF02547)","","","","","Reuter,K., Slany,R., Ullrich,F. and Kersten,H. Structure and organization of Escherichia coli genes involved in biosynthesis of the deazaguanine derivative queuine, a nutrient factor for eukaryotes J. Bacteriol. 173 (7), 2256-2264 (1991) PubMed: 1706703 Slany,R.K., Bosl,M., Crain,P.F. and Kersten,H. A new function of S-adenosylmethionine: the ribosyl moiety of AdoMet is the precursor of the cyclopentenediol moiety of the tRNA wobble base queuine Biochemistry 32 (30), 7811-7817 (1993) PubMed: 8347586 ","","Tue Jan 14 16:05:59 2003","1","","","" "AA02776","1940966","1939833","1134","ATGCAACGGAGAAAACTTCTGAAATTAACCGGCGCCGCAGTTATCGGGATGACTATTGCGCCGGGGTTGATAGCAAAAAAGAAAGGCAGAGGTAGTGGTTCCGGTATTCTACATTTGAATTTCAATGAAAATTCATTGGGTATGTCGGAAAAAGCAAAACAGGCGATTATTAATAGCATTGGGATTGGTTCCCGTTATCCCGATGAGCATCGTAGTGAATTAATCCGTCAATTAGCTGAAAAATATAATCTGGAAGATAATTTCGTTTCCTTGGGGAATGGATCCTCTGAAAATATTCGTGGAATTATTCAGTCACAGGTATTTAAAGCCAGACAGGCGAAACAGACGGTTCAGCTGGTGGTGCCGGATCCGACGTTTAATTATGCCGAATTATATGCGCAAGCCATGAATGTGCCAGTTGTTAAGGTGCCGCTGACTAAAGATTTCCAATTTGATTTGGCAAAATTACAAGAAACCGCCGAGCAGTTTAGTGGCGTGAGTATTTTCTATTTGTGTAACCCGAATAATCCAACTTCAACCGTTACGCCGGCAAAAGAGTTATTCCGTTGGATTAAAAAAGCGCCGGAAAATTATTTCTTTTTACTGGATGAAGCCTACGCCGAATATGTACAGGATCCTGCTTTTGAAAGTGGCGTTAAGCTGATTAAACAGGGTTTTAAAAATGTTGCTGTCACCCGCACTTTCTCTAAATTTTATGCCATGGCAGGTTATCGCGTGGGGTATATGCTGGCGAATTCCGATGTGGTGGAAGAAGTGGATAAATTCATGTCCATTGACAATATCAACATTGCCGGTGCTGTTGCCGCGCTTGCTTCCTTGAAAGACAAAACTTTCTCCCAACTGAGCTTACAAAGCAACGAAGCCTCCCGTAAAATCGTGCAAAACGCATTGCGAGAACTGGGTTTAAAATTTGCACCGTCTAACGGCAACTTTATTTTTCATGAAATTAAAGGGGATGTCCAAACCTACCAGGAGCGTATGAAAGAAAATGGCATTTTGGTCGGACGTGAATTTTTACCGATTCAAAGCTGGAGCCGTTTAACCTTAGGAACGCCGGAAGAAATGCAACGTTTTGTTAAAGTCCTCAAAGAATTCAGACAAAACGGTTGGGTA","","","42380","MQRRKLLKLTGAAVIGMTIAPGLIAKKKGRGSGSGILHLNFNENSLGMSEKAKQAIINSIGIGSRYPDEHRSELIRQLAEKYNLEDNFVSLGNGSSENIRGIIQSQVFKARQAKQTVQLVVPDPTFNYAELYAQAMNVPVVKVPLTKDFQFDLAKLQETAEQFSGVSIFYLCNPNNPTSTVTPAKELFRWIKKAPENYFFLLDEAYAEYVQDPAFESGVKLIKQGFKNVAVTRTFSKFYAMAGYRVGYMLANSDVVEEVDKFMSIDNINIAGAVAALASLKDKTFSQLSLQSNEASRKIVQNALRELGLKFAPSNGNFIFHEIKGDVQTYQERMKENGILVGREFLPIQSWSRLTLGTPEEMQRFVKVLKEFRQNGWV","1939667","","conserved hypothetical protein","Cytoplasm, Outer membrane, Periplasm","","
InterPro
IPR004839
Domain
Aminotransferase, class I and II
PF00155\"[34-369]TAminotran_1_2
InterPro
IPR006311
Domain
Twin-arginine translocation pathway signal
TIGR01409\"[1-25]TTAT_signal_seq: Tat (twin-arginine transloc
InterPro
IPR015421
Domain
Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10\"[48-282]Tno description
noIPR
unintegrated
unintegrated
PTHR11751\"[47-375]TSUBGROUP I AMINOTRANSFERASE RELATED
PTHR11751:SF3\"[47-375]THISTIDINOL-PHOSPHATE AMINOTRANSFERASE
signalp\"[1-25]?signal-peptide


","No hits to the COGs database.","Significant hit ( 1.9e-07) to 3/3 blocks of the IPB001511 family, which is described as \"Aminotransferases class-I\". Interpro entry for IP:IPR001511. IPB001511A 66-76 1.5e+02 IPB001511B 169-183 0.019 IPB001511C 234-247 0.02","Residues 141 to 256 match (1e-17) PD:PD000087 which is described as AMINOTRANSFERASE PROTEOME COMPLETE TRANSFERASE PHOSPHATE PYRIDOXAL ASPARTATE SYNTHASE TRANSAMINASE LYASE ","","","","","","","","","","","","Tue Jan 14 16:06:58 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02776 is paralogously related to AA02757 (4e-36) and AA00084 (1e-04).","","","","","","Residues 80 to 373 (E-value = 1.6e-11) place AA02776 in the Aminotran_1_2 family which is described as Aminotransferase class I and II (PF00155)","","","","","","","","1","","","" "AA02777","1941439","1942587","1149","ATGAAGTATGAATTAGACAAAACCAGCGGCAATGCCCGTCGTGGTCGCTTGGTATTTGAACGCCCGCAAGGCACCTTTACCGTTGAAACGCCGGCATTTATGCCCGTAGGCACTTATGGCACAGTGAAAGGCATGACGCCGGAAGAAGTGCGCACCACCGGTGCGGAAATTTTGCTCGGTAATACCTTCCATTTGTGGTTGCGCCCGGGGCAGGAAGTCATGCGCAAGCACGGTGATTTACACGATTTTATGCAATGGCATCGTCCGATTTTGACGGATTCCGGCGGTTTCCAAGTGTTCAGTTTGGGCAAGTTACGCAAAATCACTGAAGAAGGCGTGAAATTTCAAAACCCGATTAATGGCGAACGTATTTTCTTATCGCCGGAAAAATCCATGGAAATTCAATATGATTTAGGTTCCGACATCGTGATGATTTTCGATGAATGTACGCCCTACCCCGCCACGTTTAATTATGCCAAGCAATCCATGGAAATGTCCCTGCGCTGGGCGCAACGCAGCCGCGCTCGTTTTGACGAATTAGGCAACAAAAACGCGCTGTTCGGCATTATCCAAGGCGGAACCTTTGAAGAATTGCGCAAAGTTTCACTGGAAGGCTTAATCAATATCGGCTTTGACGGCTATGCGGTGGGCGGTTTAGCCGTGGGCGAACCAAAAGAAGATATGCACCGCATTTTGGAGTACATCTGCCCGCAGATTCCCGCCGACAAACCGCGCTATTTAATGGGTGTAGGAAAACCGGAAGATTTAGTGGAAGGCGTACGTCGCGGCATTGATATGTTCGATTGCGTGATGCCAACCCGCAATGCGCGTAATGGGCATTTATTCGTCACCGACGGCATCGTTAAAATCCGTAATGCCAAATACAAAGACGACACCAGCCCGCCGGATCCGCACTGTGACTGTTACACCTGCAAACACTATACCAAAGCCTATTTGTATCACCTGGACAAATGTGGCGAAATTCTTGGTGCACGCCTTAATACCATCCACAATTTGCGTTATTACCAACGCTTAATGGCAGAAATTCGCCAGGCGATCGAAGCGGATCGTTTTGATGATTTCGTGGTGGAATTTTATGCCAGAATCGGCAAACCTGTTCCGCCGTTGCAATTAGCAGAAGCAAATCAG","","","43667","MKYELDKTSGNARRGRLVFERPQGTFTVETPAFMPVGTYGTVKGMTPEEVRTTGAEILLGNTFHLWLRPGQEVMRKHGDLHDFMQWHRPILTDSGGFQVFSLGKLRKITEEGVKFQNPINGERIFLSPEKSMEIQYDLGSDIVMIFDECTPYPATFNYAKQSMEMSLRWAQRSRARFDELGNKNALFGIIQGGTFEELRKVSLEGLINIGFDGYAVGGLAVGEPKEDMHRILEYICPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGIVKIRNAKYKDDTSPPDPHCDCYTCKHYTKAYLYHLDKCGEILGARLNTIHNLRYYQRLMAEIRQAIEADRFDDFVVEFYARIGKPVPPLQLAEANQ","1942421","","tRNA-guanine transglycosylase","Cytoplasm","","
InterPro
IPR002616
Family
Queuine/other tRNA-ribosyltransferase
G3DSA:3.20.20.105\"[1-374]Tno description
PTHR11962\"[21-369]TQUEUINE TRNA-RIBOSYLTRANSFERASE
PF01702\"[129-367]TTGT
TIGR00449\"[3-374]Ttgt_general: tRNA-guanine transglycosylases
InterPro
IPR004803
Family
Queuine tRNA-ribosyltransferase
TIGR00430\"[3-374]TQ_tRNA_tgt: queuine tRNA-ribosyltransferase


","No hits to the COGs database.","Significant hit (1.4e-136) to 6/6 blocks of the IPB002616 family, which is described as \"Queuine tRNA-ribosyltransferase\". Interpro entry for IP:IPR002616. IPB002616A 28-38 1.1e-07 IPB002616B 61-102 1.3e-33 IPB002616C 126-151 1.5e-23 IPB002616D 186-218 1.1e-19 IPB002616E 239-279 7e-36 IPB002616F 306-322 4.4e-10","Residues 3 to 368 match (5e-214) PD:PD004261 which is described as TRANSFERASE TRNA-RIBOSYLTRANSFERASE QUEUINE GLYCOSYLTRANSFERASE COMPLETE PROTEOME TRANSGLYCOSYLASE TRNA-GUANINE ZINC TRNA ","","","","","","","","","","","","Tue Jan 14 16:08:46 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02777 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 129 to 367 (E-value = 9.7e-156) place AA02777 in the TGT family which is described as Queuine tRNA-ribosyltransferase (PF01702)","","","","","Reuter,K., Slany,R., Ullrich,F. and Kersten,H. Structure and organization of Escherichia coli genes involved in biosynthesis of the deazaguanine derivative queuine, a nutrient factor for eukaryotes J. Bacteriol. 173 (7), 2256-2264 (1991) PubMed: 1706703","","Tue Jan 14 16:08:46 2003","1","","","" "AA02778","1942725","1942862","138","TTGCTCAATGCACAAAATCGTAGTCTTTTTTCACGGTATGCTTACAATATCATTTTCACATTCCAACAGATTTGTGGTATTTTAGGCGACGGTTTTTTTATCAGTTACGGACGCTTCACGGCCTCTTTATATTTTCAT","","","5357","LLNAQNRSLFSRYAYNIIFTFQQICGILGDGFFISYGRFTASLYFH","1942862","","hypothetical protein","Cytoplasm, Extracellular","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
tmhmm\"[15-35]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:23:02 2004","Mon Feb 23 15:23:02 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02778 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:23:02 2004","","","","","","","","","","","","","1","","","" "AA02779","1942882","1943178","297","ATGGAAACGCAACAAGGCAGCCCAATGTCAATGTTATTTATTTTCGTCATATTCGGATTGATTTTCTATTTCATGATTTATCGTCCGCAGGCAAAAAGAAATAAAGAACATAAAAAACTTATGTCTGAATTAGCCAAAGGCACTGAAGTGCTTACCGCCGGCGGTATCATCGGTAAAATCACCAAAATGGTTGAAAACAGTGACAACATTGTTATCGCATTAAACGACAGTACCGAAGTGACCATCAACCGCAATTACATTGCCGCGGTATTACCGAAAGGTACAATCAAAACCCTT","","","11067","METQQGSPMSMLFIFVIFGLIFYFMIYRPQAKRNKEHKKLMSELAKGTEVLTAGGIIGKITKMVENSDNIVIALNDSTEVTINRNYIAAVLPKGTIKTL","1943013","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003849
Family
YajC
PD374630\"[9-87]TY241_HAEIN_P44592;
PR01853\"[9-29]T\"[29-47]TYAJCTRNLCASE
PF02699\"[7-91]TYajC
TIGR00739\"[7-92]TyajC: preprotein translocase, YajC subunit
noIPR
unintegrated
unintegrated
signalp\"[1-23]?signal-peptide
tmhmm\"[10-28]?transmembrane_regions


","BeTs to 14 clades of COG1862COG name: Preprotein translocase subunit YajCFunctional Class: NThe phylogenetic pattern of COG1862 is -------qv-rlb-efghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 3.1e-23) to 1/1 blocks of the IPB003849 family, which is described as \"Domain of unknown function DUF219\". Interpro entry for IP:IPR003849. IPB003849 21-56 2.9e-23","Residues 12 to 87 match (1e-30) PD:PD374630 which is described as COMPLETE PROTEOME TRANSMEMBRANE YAJC MEMBRANE PREPROTEIN SUBUNIT TRANSLOCASE PROBABLE SIGNAL ","","","","","","","","","","","","Tue Jan 14 16:09:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02779 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 91 (E-value = 2e-45) place AA02779 in the YajC family which is described as Preprotein translocase subunit (PF02699)","","","","","","","","1","","","" "AA02780","1943212","1945059","1848","ATGTTAAATCGTTACCCTTTATGGAAGAATCTAATGGTGATCTTCGTGGTCGCCATTGGTATTTTATATGCTCTTCCAAATCTTTACGGTGAAGATCCTGCCGTACAAATTTCAGGAACTCGCGGTCAGGAAGCCAATTCTGCTGTACTTAGCGATGTTCAATCCGTGCTTAAAGATAATAATCTGACAACCAAATCCATCGTATTGGAAAGCGGCTCGATTTTAGTGCGTTTTAACAATACGGATACACAATTACTCGCCAAAGACAAAATTACCGAAAAATTAGGCACCAACTATTCCGTCGCGTTAAACCTTGCACCGGCAACCCCGAAATGGCTAAGTAGCATTGGCGGTAACCCGATGAAATGGGGTCTGGACTTACGTGGTGGCGTGCGCTTCCTGATGGAGGTGGACATGAATTCCGCACTGTCCAAACGTCAGGAACAGTTGCAGGATTCTTTGCGTACCGAACTGCGCAAAGAAAAATATCAATACAGCGCCATTAAATCCATTGATAATTTCAGCACCGGCGTAACCTTAACCAATTCTGAACAACTTTCTGACGTACAACGCTACTTACGCAAACAGCACCCGAATCTAGATGTTAGTGTCACATCCGAGAACACCTTGTCCCTAGGCTTATCTGATTCCGTATTGAATGAAGCCCGTGAGAGCGCTATTGAGCAAAACCTGAGTATTTTACGTAAACGTGTTACCGAATTGGGCGTCGCCGAAGCCGTTATTCAGCGTCAAGGGGCGGAACGCATTGTGGTTGAATTACCGGGGGTACAAGACACTGCCCGTGCGAAAGAAATTCTCGGTGCAACGGCTACCCTTGAATTTCGTATAGTTAATGCAAGCGCTAATTTAGAAGCGGCAGCGCGTGGTATGGTGCCTTCCGATTCCGAAGTCAAATACGACAGAAACAATCGTCCTGTGGTGTTATATAAACGCGCAGTACTCGGTGGCGAGCACATTACCAATGCCAGCTCCGGTGTCGATCAAAACACGTCGTTGCCGCAAGTGAGCGTGACCTTGGATAGCGAGGGCGGCGAAATCATGTCACAAACCACCCGTTTAAACCTGAAAAAACCGATGGCGACCTTATATGTAGAATATAAAGACAGCGGTAAAAAAGACGAAAACGGTAAAACCATTTTACAAAAACACGAAGAAGTCATTAACGTCGCGACTATTCAAGGTCGTTTCGGCAGTCAATTCCAAATTACCGGTATCGACTCCCCGGCAGAAGCACAAAACCTTGCCGTGCTACTCCGTTCCGGTGCGTTAATTGCGCCAATTCAAATTGTGGAAGAACGTACCATCGGTCCGTCTCTCGGGGCACAAAATGTAGAACAAGGCTTACAGGCCAGCTTCTGGGGCTTAATGATCGTGGTGGCATTTATGGTTATTTACTACCGTAAATTCGGCATCATCGCCAATATTGCTTTAATCGCCAATATCGTTTTATTGGTCAGTTTAATATCGTTATTGCCAGGCGCCACGCTCACCATGCCGGGCATTGCCGGTATCGTATTGGCAGTAGGGATGTCGGTGGATGCGAACGTATTGATTTTCGAGCGAATTAAAGAAGAAATCCGCAACGGTCGTCCAATCCAGCAAGCCATTAATGAAGGTTATAGCGGCGCATTCAGTTCCATCTTCGATGCCAACTTAACCACGATTTTAACCGCAGTCGCCCTCTACGCGGTGGGTACCGGTCCGATTAAAGGTTTCGCAATCACCCTATCTTTAGGTATTGCCATCTCAATGTTTACCGCAATCACCGGAACACGGGCAATCGTGAATTTCTTATACGGCGGCAAACGAATTGATAAATTATCAATT","","","66807","MLNRYPLWKNLMVIFVVAIGILYALPNLYGEDPAVQISGTRGQEANSAVLSDVQSVLKDNNLTTKSIVLESGSILVRFNNTDTQLLAKDKITEKLGTNYSVALNLAPATPKWLSSIGGNPMKWGLDLRGGVRFLMEVDMNSALSKRQEQLQDSLRTELRKEKYQYSAIKSIDNFSTGVTLTNSEQLSDVQRYLRKQHPNLDVSVTSENTLSLGLSDSVLNEARESAIEQNLSILRKRVTELGVAEAVIQRQGAERIVVELPGVQDTARAKEILGATATLEFRIVNASANLEAAARGMVPSDSEVKYDRNNRPVVLYKRAVLGGEHITNASSGVDQNTSLPQVSVTLDSEGGEIMSQTTRLNLKKPMATLYVEYKDSGKKDENGKTILQKHEEVINVATIQGRFGSQFQITGIDSPAEAQNLAVLLRSGALIAPIQIVEERTIGPSLGAQNVEQGLQASFWGLMIVVAFMVIYYRKFGIIANIALIANIVLLVSLISLLPGATLTMPGIAGIVLAVGMSVDANVLIFERIKEEIRNGRPIQQAINEGYSGAFSSIFDANLTTILTAVALYAVGTGPIKGFAITLSLGIAISMFTAITGTRAIVNFLYGGKRIDKLSI","1944894","","protein-export membrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR001036
Family
Acriflavin resistance protein
PR00702\"[450-473]T\"[504-528]T\"[579-602]TACRIFLAVINRP
InterPro
IPR003335
Family
SecD/SecF/SecDF export membrane protein
PF02355\"[423-608]TSecD_SecF
PF07549\"[112-143]TSec_GG
TIGR00916\"[346-595]T2A0604s01: protein-export membrane protein,
InterPro
IPR005791
Family
SecD export membrane protein
TIGR01129\"[123-602]TsecD: protein-export membrane protein SecD
noIPR
unintegrated
unintegrated
signalp\"[1-24]?signal-peptide
tmhmm\"[10-30]?\"[454-472]?\"[477-499]?\"[505-525]?\"[559-579]?\"[585-605]?transmembrane_regions


","BeTs to 20 clades of COG0342COG name: Preprotein translocase subunit SecDFunctional Class: NThe phylogenetic pattern of COG0342 is -om-k--qvdr-bcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 5.9e-48) to 4/4 blocks of the IPB003335 family, which is described as \"SecD/SecF/SecDF export membrane proteins\". Interpro entry for IP:IPR003335. IPB003335A 121-131 0.003 IPB003335B 442-473 1.2e-10 IPB003335C 508-531 7.3e-15 IPB003335D 559-587 1e-14Significant hit ( 3.4e-05) to 2/9 blocks of the PR00702 family, which is described as \"Acriflavin resistance protein family signature\". Prints database entry for PR:PR00702. PR00702E 504-528 9.9 PR00702G 579-602 0.0017","Residues 232 to 281 match (5e-17) PD:PD005230 which is described as MEMBRANE PROTEOME COMPLETE PROTEIN-EXPORT SECD TRANSMEMBRANE TRANSLOCATION TRANSLOCASE SUBUNIT INNER ","","","","","","","","","","","","Tue Jan 14 16:11:37 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02780 is paralogously related to AA02781 (1e-11) and AA01341 (2e-04).","","","","","","Residues 337 to 608 (E-value = 6.4e-08) place AA02780 in the SecD_SecF family which is described as Protein export membrane protein (PF02355)","","","","","Nouwen N, Driessen AJ. SecDFyajC forms a heterotetrameric complex with YidC. Mol Microbiol. 2002 Jun;44(5):1397-405. PMID: 12068816 Driessen AJ, Fekkes P, van der Wolk JP. The Sec system. Curr Opin Microbiol. 1998 Apr;1(2):216-22. Review. PMID: 10066476","","Tue Jan 14 16:11:37 2003","1","","","" "AA02781","1945079","1946041","963","GTGAATTTAGAAAACAGAAGTCAGTCAATTCGAGAAATTCAAGGCATTAAACTCCCTTTCCGTTTAGTTGAGTTTATGAAATACCGCATGTGGGGTTATCTTGCATCGGTGATCATCATTGCCGTTTCCCTGTTCTTTGTATTTACCAAAGGCTTCAACTGGGGTCTGGATTTTACCGGGGGTGTGGTGGTGGACACCCACTTTTCTCAACCGGCAGATTTGGAAAAAATCCGTTCTACTCTGGTCCAAAACGGGATTGAAAGTCCATTGGTACAAACCACCGGTGGTGTGCGTGATGTGATGATTCGCCTGCCCGCGACGGATAACGCACAAATCGGTGATAATGTTAAGAGAATGCTAAGTACGTTAGATAGCGATATTCAGATTCGCTCTACTGAGTTTGTTGGTCCGAATGTTGGAGAAGAACTGACTCAAGGCGCCATTTATGCCACGTTAACAACTCTTATCATGTTGTTACTTTATGTCGGTATACGTTTTGAATGGCGCTTAGCTGTTGGCGGCGTACTTTCCCTTGCGCACGATGTGATTGTTACCTTAGGTGCTTTCTCCTACTTGCAAATTGAAATGGATTTAACCTTTATCGCAGCGATTCTTTCCGTGGTGGGCTATTCCCTCAATGACAGTATCGTGGTATTCGATCGTGTGCGTGAGAACTTCCGTAAAATCAGACGGATTGCTTCTATCGACATTATTAACATTTCATTAACACAAACTCTCTCCCGAACTATTATGACTTCAGTGACGACGTTAATTGTGGTGATCGCCCTTTTTGTCTTCGGCGGCCCGACAATCCATAGTTTCTCGTTGGCCCTCTTAATAGGTATCGGATTCGGGACATACTCTTCTATCTTCGTTGCGATTGCTATTGCATATGACTTAGGTCTTGACCGTGAACACATGGTGCAACCCAAAGTGAACAAAGATGATATTGATGAGCTGCCT","","","37047","VNLENRSQSIREIQGIKLPFRLVEFMKYRMWGYLASVIIIAVSLFFVFTKGFNWGLDFTGGVVVDTHFSQPADLEKIRSTLVQNGIESPLVQTTGGVRDVMIRLPATDNAQIGDNVKRMLSTLDSDIQIRSTEFVGPNVGEELTQGAIYATLTTLIMLLLYVGIRFEWRLAVGGVLSLAHDVIVTLGAFSYLQIEMDLTFIAAILSVVGYSLNDSIVVFDRVRENFRKIRRIASIDIINISLTQTLSRTIMTSVTTLIVVIALFVFGGPTIHSFSLALLIGIGFGTYSSIFVAIAIAYDLGLDREHMVQPKVNKDDIDELP","1945876","","protein-export membrane protein","Inner membrane, Cytoplasm","","
InterPro
IPR003335
Family
SecD/SecF/SecDF export membrane protein
PR01755\"[50-65]T\"[161-175]T\"[209-227]T\"[241-256]TSECFTRNLCASE
PF02355\"[115-303]TSecD_SecF
PF07549\"[46-74]TSec_GG
TIGR00916\"[114-290]T2A0604s01: protein-export membrane protein,
InterPro
IPR005665
Family
SecF protein
TIGR00966\"[51-293]T3a0501s07: protein-export membrane protein
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[111-272]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-51]?signal-peptide
tmhmm\"[30-48]?\"[146-164]?\"[169-191]?\"[197-219]?\"[249-269]?\"[275-297]?transmembrane_regions


","BeTs to 20 clades of COG0341COG name: Preprotein translocase subunit SecFFunctional Class: NThe phylogenetic pattern of COG0341 is -om-k--qvdr-bcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 5.4e-51) to 4/4 blocks of the IPB003335 family, which is described as \"SecD/SecF/SecDF export membrane proteins\". Interpro entry for IP:IPR003335. IPB003335A 52-62 7.2e-07 IPB003335B 135-166 3.2e-12 IPB003335C 201-224 5.7e-13 IPB003335D 254-282 1.6e-14","Residues 95 to 136 match (6e-07) PD:PD542571 which is described as MEMBRANE INNER PROTEOME TRANSMEMBRANE SECF PROTEIN-EXPORT COMPLETE TRANSLOCATION ","","","","","","","","","","","","Tue Jan 14 16:13:53 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02781 is paralogously related to AA02780 (5e-12) and AA01341 (0.001).","","","","","","Residues 42 to 303 (E-value = 2.6e-121) place AA02781 in the SecD_SecF family which is described as Protein export membrane protein (PF02355)","","","","","Driessen AJ, Fekkes P, van der Wolk JP.The Sec system. Curr Opin Microbiol. 1998 Apr;1(2):216-22. Review. PMID: 10066476 Sagara K, Matsuyama S, Mizushima S. SecF stabilizes SecD and SecY, components of the protein translocation machinery of theEscherichia coli cytoplasmic membrane. J Bacteriol. 1994 Jul;176(13):4111-6. PMID: 8021192","","Tue Jan 14 16:13:53 2003","1","","","" "AA02782","1946264","1948888","2625","ATGAATTTTAAATTTAAAAAATCTCAAAAAAGTGACAAACGCAACCCTACACTACTCTTTTTGACCACTTTGATCTGCACGTCACAAAGTATCGATGCTGCCCCTCAAACTACGGTTCTACCGGACATAGTAGTTACCGGGCAAAGTAAAACTTCATATGAGGATGAACTGGAAAGCTATCTAAAATCCGGTTCGTACTCATATCTCAATGATACAAAAATTCAACGTTTTCGCGGCTCATCAGTAGGTGATTTTTTAAGCGGAATTCCGGGCGTTATGGTCGGCAACAAACGAAACAGCGGCGCTATAACCCCTATAATTAGAGGTATAGCCAACGAAAACAGAATTCCTGTTTTGATCGATGATTCGCTTCAGTCTATCCCTTCGTGGCAAGGCTATGCAGGTTCAAGTACCCGAACATATCTGGATCCTGATCTTATCTCGCGCGTAGAAATAGAAAAAGGCCCGTCACTCAAAGCAGATGCTACCGGCGCCACAGGTGGTGTAGTGAGAATGAATACCGTAGGCTACAAAGACATAATCCCCGAAAATAAGAACTGGGGACTTCGCTTGCGGTTCGGCACGATGTCTAATACTACAGACAAACCACCTCTTTATACACGCGGCGGATACCGCACTAAATGGATAGACGAATGTCGTACCAACCGTTCGGGTAAATGTCCGAAGCAAACCTACAACCCCAACGCGAAATACGCATCCAAAAATCCTTTTCAGAATTTAGGCAAAAGCTACAACTACTCGCTCGCATTTTCTAAAAAGTGGGAAAACGCCGACATTGTGTTGGCCTACGCCAAAAAGAAGCAGGGCAATTATTTCGTCGGACGCCATGGCGCCGTACCAGTGATAGAAGATATCGAATATAAAAATGAAGATGATTTTGAAGTACACAGAGACCCTACGAGAAAGGACAGATTCGGCAGACCTCTTGTGACTGAAGAAGATGTTAGGATCGGTAGGCTGAGATTTAAAGAGCAAAACGGTTATACCTACTTTCGTGGTGGCGAGGAAGTACTAAATACCAGCCAGGATAATAAGTCCTATCTGGCTAAGTTTAACACTTACAACGACACGCATGCTTTAAATTTGACCTACCGCGGCTATAGAAGCAAATTCGGCGAGCTGATGCCGTCCATTACGAGCTTTCGTGGAGACGGTGCGCTGCAGGGAGAAGGCACGGAAGTAAAGACCGATAGCTACAGCGCAAAATATATCTTCGATCCGACAAATCCATTTATCAAGCTAACTTTAAGCGGATATTACACTAAAAGTGACACTTCTAGCTTTACACCTTTCATCGAGGATCTGGTTGATTTCAGCTCTCGCCACGCGCACTTTACAATCTCCGAGCAGAAGGGACTAAATTTAAGCAACACCAGTGTAGCGCAAATTTTCGATAGACCACTAACGATAAACTACGGCATAAGTTACTCGCGCGAAAGAATTCATCCGCCTAAAGATATGGCTGCTAGAGTACGCGCAAAAGGCTATCCTGACAATGCTGTAGCACCGTTTTACATCAGAAACGCAAAGCGCAAAGAAAAAAGTGCCTTCATTTCGCTTAACTATCCAATCACGAACTGGCTTAAAATAGATCTAGGTCTGCGACACATCCGCACCGCAATTCATGATTTTCAGCCCAGAGTCGAAGATAAATTCGTACGCAAAAATATGCCCGATCCGAAGAATTCCGTCTGTGAACCGGTGCGCAACAACCCGTTTCAAAAAAGATGCCGGATTTATTCTTGGCCGCAACCTCCAAGCGTTAAGGCCACATCACCAATCGCGATGTTTACCTTCGAACCACATGAGAACGCGCAAATTTACATAAAATATGCCGAGGCTGTACGCTCAGCGAGTTTGTTTCAAGCATCACGCGGATTTAGCACACAAATAGTCGATTATCAAACCTACAAGTTAAAGCCTGAGAGACAAAAGAACTGGGAAATTGGCACAAATCTATTATTTGATGATATAGGCGGTGGAGATAATTTTTTAGGTTTTAAATTTGCTTATTTTAATAACTTCACGAAAGATTATCTCACCAGAACGAGTACGCAAGGCAGACTACAAACCGTCAATATTAGATCTGCCCTTTTTCGTGGGTATGAGACTTCGGCATATTTTGATATGAGAAGCTTCTATACACAGATAGGTATGACACACTATCTAAAAACGAAATTTTGCCGTAGGGACGATCAAGTCGGACGAATAAGAGATACACCGCAGTGCTTTGAGGGCGGTATCAGCGGAAGCAATCTCGCCAATACGTTGCCTCCTAAAACAACGATAACGACTACAGTCGGATTTAGATTCTGGGATGATAAACTTGAACTGGGTGCGCGCCACAATTACTACTCAAAACGCATAGTTTCGATATTTTCGCCAAACAATAGTACCGGGGAGACAAATTCTGCCGAATGGAAGCCATATGCAATAGTCGATCTTTTCGCAAATTATAAAATTTCAAAGGATCTAACAATATCTGCAACGCTGGATAATCTAACTAACAGATATTATTTAGACGCGAACAATATGGGATTAAATCCTGCACCGGGCAGAACCTTGAGGTTAAACCTGGATTATAAATTTGGGTCTATATTTGAT","","","99655","MNFKFKKSQKSDKRNPTLLFLTTLICTSQSIDAAPQTTVLPDIVVTGQSKTSYEDELESYLKSGSYSYLNDTKIQRFRGSSVGDFLSGIPGVMVGNKRNSGAITPIIRGIANENRIPVLIDDSLQSIPSWQGYAGSSTRTYLDPDLISRVEIEKGPSLKADATGATGGVVRMNTVGYKDIIPENKNWGLRLRFGTMSNTTDKPPLYTRGGYRTKWIDECRTNRSGKCPKQTYNPNAKYASKNPFQNLGKSYNYSLAFSKKWENADIVLAYAKKKQGNYFVGRHGAVPVIEDIEYKNEDDFEVHRDPTRKDRFGRPLVTEEDVRIGRLRFKEQNGYTYFRGGEEVLNTSQDNKSYLAKFNTYNDTHALNLTYRGYRSKFGELMPSITSFRGDGALQGEGTEVKTDSYSAKYIFDPTNPFIKLTLSGYYTKSDTSSFTPFIEDLVDFSSRHAHFTISEQKGLNLSNTSVAQIFDRPLTINYGISYSRERIHPPKDMAARVRAKGYPDNAVAPFYIRNAKRKEKSAFISLNYPITNWLKIDLGLRHIRTAIHDFQPRVEDKFVRKNMPDPKNSVCEPVRNNPFQKRCRIYSWPQPPSVKATSPIAMFTFEPHENAQIYIKYAEAVRSASLFQASRGFSTQIVDYQTYKLKPERQKNWEIGTNLLFDDIGGGDNFLGFKFAYFNNFTKDYLTRTSTQGRLQTVNIRSALFRGYETSAYFDMRSFYTQIGMTHYLKTKFCRRDDQVGRIRDTPQCFEGGISGSNLANTLPPKTTITTTVGFRFWDDKLELGARHNYYSKRIVSIFSPNNSTGETNSAEWKPYAIVDLFANYKISKDLTISATLDNLTNRYYLDANNMGLNPAPGRTLRLNLDYKFGSIFD","1948723","","outer membrane haemophore receptor (tonB related)","Outer membrane, Periplasm","","
InterPro
IPR000531
Domain
TonB-dependent receptor
PF00593\"[599-870]TTonB_dep_Rec
InterPro
IPR012910
Domain
TonB-dependent receptor, plug
PF07715\"[58-169]TPlug
noIPR
unintegrated
unintegrated
G3DSA:2.170.130.10\"[36-172]Tno description
G3DSA:2.40.170.20\"[311-870]Tno description
signalp\"[1-33]?signal-peptide
tmhmm\"[15-33]?transmembrane_regions


","BeTs to 8 clades of COG1629COG name: Outer membrane receptor proteins, mostly Fe transportFunctional Class: PThe phylogenetic pattern of COG1629 is -------q-----cefghsnuj----Number of proteins in this genome belonging to this COG is","","Residues 498 to 556 match (6e-15) PD:PD569616 which is described as PROTEOME COMPLETE HASR ","","","","","","","","","","","","Tue Jan 14 16:20:21 2003","","","","Thu Mar 18 09:33:43 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02782 is paralogously related to AA00590 (9e-17), AA02865 (9e-11), AA02202 (2e-07), AA00762 (1e-05) and AA00764 (0.001).","Thu Mar 18 09:33:43 2004","","","","","Residues 60 to 870 (E-value = 1.3e-28) place AA02782 in the TonB_dep_Rec family which is described as TonB dependent receptor (PF00593)","Thu Mar 18 09:33:43 2004","","","","Turner PC, Thomas CE, Stojiljkovic I, Elkins C, Kizel G, Ala'Aldeen DA, Sparling PF.Neisserial TonB-dependent outer-membrane proteins: detection, regulation and distribution of three putative candidates identified from the genome sequences.Microbiology. 2001 May;147(Pt 5):1277-90.PMID: 11320131Paquelin A, Ghigo JM, Bertin S, Wandersman C.Characterization of HasB, a Serratia marcescens TonB-like protein specifically involved in the haemophore-dependent haem acquisition system.Mol Microbiol. 2001 Nov;42(4):995-1005.PMID: 11737642","","Thu Mar 18 09:33:43 2004","1","","","" "AA02783","1949138","1948965","174","TTGATCTGGGTCAAAAAACAAACTGCTTTGACTACCGTTATTTATTTGGGGTTGATTGGATTGGCGCGGTTATGCTGGTCATATAAAAATAAAGGTAACGCATTGCAAACCAAAGAAATTGAGAAATATAACGGAATCGATAAAAAATCTTTTCCGTTATTTTTTGAAAGAATA","","","6745","LIWVKKQTALTTVIYLGLIGLARLCWSYKNKGNALQTKEIEKYNGIDKKSFPLFFERI","1948965","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-27]?signal-peptide
tmhmm\"[9-27]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:21:21 2004","Mon Feb 23 15:21:21 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02783 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:21:21 2004","","","","","","","","","","","","","1","","","" "AA02784","1949241","1951859","2619","ATGAGTAATGTTGAAAATGCAGTAAGTCCTGCACAAGCAGAAGTGAATGCTCTGGTTGAAAAAGGTTTGGTTGCGCTGGAAGAATTCCGCCAATTAAACCAAGAGCAGGTGAACTACATTGTGGCGAAAGCCTCTGTGGCGGCGCTGGATCAACATGGTGTGCTGGCAATGCACGCTTATGAAGAAACCGGGCGTGGCGTATTTGAGGATAAAGCGACCAAAAATTTATTCGCCTGTGAATATGTCGTGAACAATATGCGGCATTTAAAAACCGTCGGCATAATAAGTGAAAATGATGTAACAGGCATCACCGAAATCGCCGATCCTGTGGGCGTCATCTGTGGGATCACCCCGACAACCAACCCGACATCCACCGCCATTTTCAAGTCCCTCATTGCGCTAAAAACCCGTAACCCAATCATTTTTGCCTTCCATCCCTCCGCCCAACAATCTTCCGCGCACGCCGCCCGCATTGTGTATGAAGCTGCTATTGCCGCCGGTGCGCCGAAAAATTGTATTCAATGGATCGAAAAACCATCTATGGAAGGCACATCCGCATTAATGAAACACCCGGGCATCGCCACCATCCTTGCCACCGGCGGGAACGCCATGGTAGAAGCTGCTTATTCCTGCGGCAAACCGGCATTGGGCGTCGGTGCAGGTAACGTGCCGGCTTATGTGGAAAAATCCGCCAACTTAAAACAAGCAGTGCACGACATCGTGATGTCTAAATCCTTCGATAACGGCATGGTGTGCGCCTCCGAACAGGCGGCCATCGTCGATGAAGAAATCTATAACGATTTTGTAAAAGAAATGCTTTCTTACGGCGTTTATATGGTGAACAAGAAAGAAAAAGCCATGCTGGAAGAATTCATGTTCGGCACAAAAGCCAACAGCAAGAACTGTGGCGGCGCGAAACTGAATGCCAATGTGGTGGGTAAACCTGCCGCCTGGATTGCGGAACAGGCGGGCTTCAAAGTGCTACCGCGAACCAATATTCTGCTTGCCGAATGTAAAGAAGTGGGCGAAAAAGAGCCGCTAACCCGTGAAAAACTTTCTCCGGTACTGGCTTTAATTAAATCTACCTCCCGTGAAGACGGTCTTGAAAAAGCGGAACAAATGGTGGAATTCCATGGTTTGGGTCACTCCGCCGCCATTCACACCTCCGATGCGGAGCTTGCCAAAGAATTTGGTAAACGGGTGAAAGCCATTCGCGTTATCTGGAACTCGCCTTCCACCTTCGGCGGTATCGGTGATGTGTATAACGCCTTCCTGCCTTCCCTCACGTTAGGTTGTGGTTCTTATGGTAAAAATTCCGTGGGCAACAACGTAAGTGCGGTCAATTTAATTAACATTAAACGAGTAGGCAGACGGAGAAACAATATGCAATGGTTTAAAGTGCCGTCAAAAATCTATTTTGAACGGGATTCAATTCAATATCTTCAATCCATGGGCGGCATGGAACGCGTGGTCATCGTCACCGACCGTACCATGGTGGACTTAGGTTTCGTAGAAAAAATCGCCCACCAAATTACGGCTCGTGGCAATCACGTAACCTACCAATTATTTGCCGATGTAGAACCGGATCCGTCCATTGAAACCGTACGCCGTGGTACGGAGTTAATCCGTAACTACAAACCGGATACCATTATCGCCCTGGGTGGTGGTTCGGCAATGGATGCGGCAAAAGTGATGTGGTTATTCTATGAACAACCAGAAGTGGATTTCCGCGATTTGGTACAGAAATTCATGGATATACGTAAACGCGCGTTTAAATTCCCGCAACTAGGTCGTAAAGCCAGATTTATCGGTATTCCGACAACATCCGGTACCGGTTCTGAAGTGACACCGTTTGCGGTTATCACCGAAGGTAATAAAAAGTACCCGATTGCCGACTACTCGCTTACCCCGACCGTCGCCATTGTGGATCCGGCATTAGTGATCACTGTACCGGCACATGTCGCCGCCGACACCGGCTTGGACGTATTAACCCACGCCACCGAAGCTTATGTATCCATTCTTGCCAGCGACTTCACCGATGGTCTTGCCTTGCAAGCCATTAAACTGGTGTTTGAGTTCCTGGAAAAATCTGTGACCGAAAAAGATCAGGAAGCGCGCGAAAGAATGCATAACGCCTCCACCATGGCAGGTATGGCATTCGCCAATGCGTTTTTAGGGATGAACCACTCCCTTGCCCACAAAATCGGCGGTCGCTTCCATACACCACACGGACGCACCAACGCGATTTTAATGCCGCACGTGATTCGTTATAACGGTACCCGCCCGGAAAAAACCGCTACGTGGCCGAAATATAATTACTACAAAGCAGATGTAAAATACCAAGACATCGCCCGTATGCTCGGCTTGCCTTGCAGCACACCGGAAGAAGGCGTGCGTTCTTACGCACAAGCCTGCTACGATTTAGCTGTGCGTTGTGGCATTAAGATGTCTTTCAAAGAACAAGGCTTGGATGAAAAAGCGTGGATGGATGCCCGTCGTGATGTGGCACTGCTCGCCTTTGAAGACCAATGTTCCCCGGCAAACCCTCGTTTACCGATGGTTACCGATATGGAAGGCATCCTCACCCGCGCTTATTTTGGTTATGATCCAAAGGATTAT","","","95652","MSNVENAVSPAQAEVNALVEKGLVALEEFRQLNQEQVNYIVAKASVAALDQHGVLAMHAYEETGRGVFEDKATKNLFACEYVVNNMRHLKTVGIISENDVTGITEIADPVGVICGITPTTNPTSTAIFKSLIALKTRNPIIFAFHPSAQQSSAHAARIVYEAAIAAGAPKNCIQWIEKPSMEGTSALMKHPGIATILATGGNAMVEAAYSCGKPALGVGAGNVPAYVEKSANLKQAVHDIVMSKSFDNGMVCASEQAAIVDEEIYNDFVKEMLSYGVYMVNKKEKAMLEEFMFGTKANSKNCGGAKLNANVVGKPAAWIAEQAGFKVLPRTNILLAECKEVGEKEPLTREKLSPVLALIKSTSREDGLEKAEQMVEFHGLGHSAAIHTSDAELAKEFGKRVKAIRVIWNSPSTFGGIGDVYNAFLPSLTLGCGSYGKNSVGNNVSAVNLINIKRVGRRRNNMQWFKVPSKIYFERDSIQYLQSMGGMERVVIVTDRTMVDLGFVEKIAHQITARGNHVTYQLFADVEPDPSIETVRRGTELIRNYKPDTIIALGGGSAMDAAKVMWLFYEQPEVDFRDLVQKFMDIRKRAFKFPQLGRKARFIGIPTTSGTGSEVTPFAVITEGNKKYPIADYSLTPTVAIVDPALVITVPAHVAADTGLDVLTHATEAYVSILASDFTDGLALQAIKLVFEFLEKSVTEKDQEARERMHNASTMAGMAFANAFLGMNHSLAHKIGGRFHTPHGRTNAILMPHVIRYNGTRPEKTATWPKYNYYKADVKYQDIARMLGLPCSTPEEGVRSYAQACYDLAVRCGIKMSFKEQGLDEKAWMDARRDVALLAFEDQCSPANPRLPMVTDMEGILTRAYFGYDPKDY","1951694","","NAD+ dependent acetaldehyde-alcohol dehydrogenase, iron-containing","Cytoplasm","","
InterPro
IPR001670
Domain
Iron-containing alcohol dehydrogenase
PF00465\"[468-857]TFe-ADH
PS00913\"[640-668]TADH_IRON_1
InterPro
IPR012079
Family
Bifunctional aldehyde/alcohol dehydrogenase
PIRSF000111\"[7-869]TBifunctional aldehyde/alcohol dehydrogenase
noIPR
unintegrated
unintegrated
G3DSA:1.20.1090.10\"[652-868]Tno description
G3DSA:3.40.50.1970\"[460-651]Tno description
G3DSA:3.40.605.10\"[12-260]Tno description
PTHR11496\"[616-758]TALCOHOL DEHYDROGENASE


","BeTs to 12 clades of COG1454COG name: Alcohol dehydrogenase IVFunctional Class: CThe phylogenetic pattern of COG1454 is aompkzyqv--lb-efgh---j----Number of proteins in this genome belonging to this COG is","Significant hit ( 5.6e-39) to 4/4 blocks of the IPB001670 family, which is described as \"Iron-containing alcohol dehydrogenase\". Interpro entry for IP:IPR001670. IPB001670A 548-560 9.8e-07 IPB001670B 607-616 7.2e-05 IPB001670C 637-670 1.6e-16 IPB001670D 729-744 3.8e-06Significant hit ( 4.2e-16) to 4/6 blocks of the IPB002086 family, which is described as \"Aldehyde dehydrogenase family\". Interpro entry for IP:IPR002086. IPB002086A 109-122 2.2 IPB002086C 193-213 21 IPB002086D 223-266 4.1e-09 IPB002086E 635-688 0.12Significant hit ( 3.1e-08) to 2/5 blocks of the IPB000965 family, which is described as \"Gamma-glutamyl phosphate reductase\". Interpro entry for IP:IPR000965. IPB000965C 213-260 0.003 IPB000965D 354-400 0.0037","Residues 607 to 696 match (1e-08) PD:PD001437 which is described as OXIDOREDUCTASE DEHYDROGENASE PROTEOME COMPLETE ALCOHOL PROBABLE NAD-DEPENDENT 4-HYDROXYBUTYRATE IRON-CONTAINING LACTALDEHYDE ","","","","","","","","","","","","Tue Jan 14 16:25:59 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02784 is paralogously related to AA02922 (1e-08) and AA02790 (2e-05).","","","","","","Residues 468 to 857 (E-value = 6.2e-136) place AA02784 in the Fe-ADH family which is described as Iron-containing alcohol dehydrogenase (PF00465)","","","","","Bruchhaus,I. and Tannich,E.Purification and molecular characterization of the NAD(+)-dependent acetaldehyde/alcohol dehydrogenase from Entamoeba histolyticaBiochem. J. 303 (Pt 3), 743-748 (1994)PubMed: 7980441Xu,J. and Johnson,R.C.aldB, an RpoS-dependent gene in Escherichia coli encoding analdehyde dehydrogenase that is repressed by Fis and activated byCrpJ. Bacteriol. 177 (11), 3166-3175 (1995)PubMed: 7768815","","Mon Feb 17 15:44:00 2003","1","","","" "AA02785","1952898","1951948","951","ATGGAAAACGTGACATTGAAGAAAATTATCAATGCTTATGGAATGGTCCTAATTTTAATTCTTCTCTTTTTGGGCTTATCTGTTTCAATTGATGGTTTTTTCTCAGCAAGAACAGTGTGGAGTATTGTTGAACAAGTCTCTATGTTCGGTATTATTGCCATTGGGGTGACATTTATCATTATTACTACCGGTATTGATTTGTCATCAGGCTCAGTGGTCGCATTAACTGCTGTAGTTTCCGCGTCAGTGGTAACGGGCGGCGATACTTTTTCTGCCGCATTACTGGCTTTTGCAGTGTCTATTTTAATTGGTGCCGGATTGGGGTTAATTAACGGTGGGCTTACGGCAATTGGCAGCATTCCGCCGTTTATCGCCACATTGGGGATGATGATTATTGCACGTGGTGCAGCGCAACTTTATTCTGATGGTCGTCCGATTGACGCTTCTTCCGAAGCCTTTACCTGGATTGCCGATGTCAATATTTTAGGGTTGCCGGGATTGGTACTGTTATACATTTTAATTGTGATCGTCAGCCATATTTTACTCAGCCGTTCAACATTCGGTCGCCATGTTTATGCTGTTGGCGGAAACTTAAATGCAGCTAAAATTTGTGGTATTAACACCAATCGAACTTTAATCTGGGTTTATATCCTTGGAGGAGCGCTATCCGGTTTAGCCGGCGCATTGTTGGCGGCGCGTACTTATGCAGGTAACCCGTCTTATGGCTTGGCGTGGGAGCTTGATGCCATTGCGGCAGCCGTTATCGGCGGGGTTTCCTTAAGTGGTGGTTTCGGTACGATCCCAATGTGCGTTATCGGCGCATTGATTATCGGTACAACCAATAAAGGATTAAATATGCTCGGCGTTGACCCTTATTGGCAACAAATTGTTAAAGGGGCGATTATCGTTGTCGCCGTATTACTTGATACCTTAAAACGTCGTAAAAAAGGA","","","32665","MENVTLKKIINAYGMVLILILLFLGLSVSIDGFFSARTVWSIVEQVSMFGIIAIGVTFIIITTGIDLSSGSVVALTAVVSASVVTGGDTFSAALLAFAVSILIGAGLGLINGGLTAIGSIPPFIATLGMMIIARGAAQLYSDGRPIDASSEAFTWIADVNILGLPGLVLLYILIVIVSHILLSRSTFGRHVYAVGGNLNAAKICGINTNRTLIWVYILGGALSGLAGALLAARTYAGNPSYGLAWELDAIAAAVIGGVSLSGGFGTIPMCVIGALIIGTTNKGLNMLGVDPYWQQIVKGAIIVVAVLLDTLKRRKKG","1951783","","ribose ABC transporter, permease","Inner membrane, Cytoplasm","","
InterPro
IPR001851
Family
Bacterial inner-membrane translocator
PF02653\"[38-306]TBPD_transp_2
InterPro
IPR013209
Domain
LNS2, Lipin/Ned1/Smp2
SM00775\"[124-215]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-29]?signal-peptide
tmhmm\"[10-30]?\"[39-61]?\"[67-87]?\"[92-114]?\"[120-140]?\"[161-181]?\"[212-232]?\"[247-277]?\"[291-311]?transmembrane_regions


","BeTs to 7 clades of COG1172COG name: Ribose/xylose/arabinose/galactoside ABC-type transport systems, permease componentsFunctional Class: GThe phylogenetic pattern of COG1172 is --------v-rlb-efgh---j--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 5.9e-13) to 2/2 blocks of the IPB001851 family, which is described as \"Binding-system dependent bacterial transporters (araH, livH/limM families)\". Interpro entry for IP:IPR001851. IPB001851A 187-201 1.1e-05 IPB001851B 246-257 1.7e-05","Residues 274 to 316 match (9e-08) PD:PD409969 which is described as COMPLETE PROTEOME PERMEASE ABC SUGAR TRANSPORTER TRANSPORTER MEMBRANE SYSTEM PLASMID ","","","","","","","","","","","","Tue Jan 14 16:28:30 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02785 is paralogously related to AA00208 (3e-53), AA00753 (1e-51), AA01457 (2e-36), AA00936 (7e-34), AA02224 (2e-32), AA02220 (1e-27) and AA00935 (2e-22).","","","","","","Residues 38 to 306 (E-value = 8.6e-64) place AA02785 in the BPD_transp_2 family which is described as Branched-chain amino acid transport system / permease component (PF02653)","","","","","","","","1","","","" "AA02786","1954454","1952952","1503","ATGACTAACAGTTCAAATTCTCCGTATATTTTAGAAATGCGAAATGTGTCAAAAACATTTCCGGGGGTGAAGGCACTTGACGGCATTAATCTTCGCGTAAAACGTGGAAGCGTTCATGCCTTAATGGGGGAAAACGGTGCCGGGAAATCCACCTTGATGAAAGTGCTGTATGGCATCTATATCCCGGATGATGGCGGAGAATTAATTTTGGACGGCAAACCCTTTAAACCAAGTCGTCCTATTTATGCGATTCGTTGCGGCTTAACCATGGTGCCGCAGGAAATTTCCCCGGCTGCCAATTTGACCATCGCCGATAATTTTTACTTAGGGCGTGAAATTACCCAAGCCAAGTTTTTTCTCGATCAGAAAGCAATGGATGAGCAGGCTTCGGCGATATTAAAAGAGCTTGGCGTGCCGATGGACGTGACCGCCAAAATGTCCGATGTATCGGTGGCAAAAGCGCAGTTAGTTGCTATTGCTACGGCGGTTTCTAATGACGCCAAAGTCATCATTATGGACGAGCCGACCACGGCATTGACGGAAAATGAGGTCGAGCAGCTTTACCGCATTATTGAAACGGTAAAAGAAAGAGGCATCGCGATTATTTTTATTTCCCATAAATTAGATGAAGTTTTCCGTGTATCTGATGAGATTACCGTCATTCGTGACGGGCAATATGTAGATACCAAGCCAACCAAAGACGTTAGTAAAGAACAGCTTATTTCCATGATGGTGGGACGAGATATGTCGGAAATGTTCCAGCGTGAGCGTTTTGATTTATCCGATGAAATTGTGCTGGAAATTAAACATTTCACCCGCGCAGGAAAATATCAGGATATTAATTTCGCCGTGCGTAAAGGCGAAATTTTTGGTATTGCCGGATTGGTCGGTGCGGGACGTTCGGAAATCGTGGAAGGGTTATTCGGTTATAAACCGGCGGATAGCGGCGAAATTTATATTAAAGGCGAAAAAGCGATTATCAATAATCCGTTAGATGCCATGAAATATAAAATCGGTTTTGTGACGGAAGACCGGAAACTGACAGGGCTATTTTTAAATTTGAGCATTACAGACAACATGATTATGCCGAAAATGTCGCCATATCTGGAAAATTTCCTGGTGTCTGTCGTCAGAGCAAAAAGAACAGCAAATGAACAAAAAACAAAGCTCAAGATAAAAGCCCCGAATGTGGAAGTGATTACAAACAATCTTTCAGGGGGAAATCAGCAAAAAGTCTTACTTGCCCGCTGGCTATTGTTAGAGCCGGACATTCTGATTTTGGATGAACCGACAAAAGGGATTGATGTGGGGGCAAAAGCAGAATTGTATAAACTAATGGTTGAGCTATCAAAACAGGGCAAAACCATCATTATGATTACGTCGGATATGTTGGAGCTTTTATCGATGAGTGACCGCGTGATGGTAATGCATGAAGGATATCAAGTGGGTATTATTCCTCATACGGATCTGACACAAGAACGCATTCTTGAATTGGCTTCAGGC","","","55627","MTNSSNSPYILEMRNVSKTFPGVKALDGINLRVKRGSVHALMGENGAGKSTLMKVLYGIYIPDDGGELILDGKPFKPSRPIYAIRCGLTMVPQEISPAANLTIADNFYLGREITQAKFFLDQKAMDEQASAILKELGVPMDVTAKMSDVSVAKAQLVAIATAVSNDAKVIIMDEPTTALTENEVEQLYRIIETVKERGIAIIFISHKLDEVFRVSDEITVIRDGQYVDTKPTKDVSKEQLISMMVGRDMSEMFQRERFDLSDEIVLEIKHFTRAGKYQDINFAVRKGEIFGIAGLVGAGRSEIVEGLFGYKPADSGEIYIKGEKAIINNPLDAMKYKIGFVTEDRKLTGLFLNLSITDNMIMPKMSPYLENFLVSVVRAKRTANEQKTKLKIKAPNVEVITNNLSGGNQQKVLLARWLLLEPDILILDEPTKGIDVGAKAELYKLMVELSKQGKTIIMITSDMLELLSMSDRVMVMHEGYQVGIIPHTDLTQERILELASG","1952787","","ribose ABC transporter; ATP-binding","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[148-191]T\"[403-446]TQ6LK34_PHOPR_Q6LK34;
PF00005\"[36-224]T\"[401-479]TABC_tran
PS50893\"[11-248]T\"[260-498]TABC_TRANSPORTER_2
PS00211\"[404-418]?ABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[35-225]T\"[286-481]TAAA
InterPro
IPR012948
Domain
AARP2CN
SM00785\"[12-88]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[4-251]T\"[259-494]Tno description
PTHR19222\"[11-309]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF12\"[11-309]TSUGAR ABC TRANSPORTER


","BeTs to 7 clades of COG1129COG name: ABC-type sugar (aldose) transport system, ATPase componentFunctional Class: GThe phylogenetic pattern of COG1129 is -----z--v--lb-efgh---j--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 3.7e-26) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 25-71 5.5e-14 IPB001140B 401-439 1.8e-08 IPB001140C 456-485 1.7","Residues 148 to 191 match (1e-06) PD:PD000006 which is described as ATP-BINDING COMPLETE PROTEOME ABC TRANSPORTER TRANSPORTER PROBABLE TRANSMEMBRANE COMPONENT PLASMID ","","","","","","","","","","","","Tue Jan 14 16:29:41 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02786 is paralogously related to AA00751 (1e-120), AA00207 (1e-101), AA01456 (6e-97), AA02225 (5e-62), AA00933 (3e-48), AA00934 (3e-32), AA02140 (2e-31), AA01524 (3e-20), AA00415 (1e-19), AA02718 (3e-18), AA02320 (6e-18), AA00700 (2e-17), AA01656 (3e-17), AA02353 (5e-17), AA02898 (6e-17), AA01645 (6e-17), AA02080 (1e-16), AA02440 (2e-16), AA02152 (5e-16), AA01568 (5e-16), AA01051 (5e-16), AA00858 (5e-16), AA01393 (9e-16), AA01616 (2e-15), AA02573 (3e-15), AA01422 (3e-15), AA01820 (6e-15), AA01867 (8e-15), AA02899 (1e-14), AA01961 (1e-14), AA02805 (1e-14), AA00799 (2e-14), AA02324 (2e-14), AA01779 (4e-14), AA02484 (1e-13), AA02609 (2e-13), AA02226 (2e-12), AA01947 (3e-12), AA01510 (3e-12), AA02550 (3e-12), AA01509 (5e-12), AA02606 (6e-12), AA02642 (9e-11), AA01824 (9e-11), AA01684 (9e-11), AA01757 (1e-09), AA01569 (4e-09), AA02331 (8e-09), AA00061 (1e-06), AA01291 (6e-06), AA02146 (8e-06), AA00591 (8e-06), A02145 (3e-05) and AA01555 (4e-05).","","","","","","Residues 287 to 479 (E-value = 6.5e-27) place AA02786 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","","","","1","","","" "AA02787","1955455","1954526","930","ATGTTAAAAAAGATGTGCATCTTGGTTCTTGGTCTCTTTTTCACTCCGCTCATTCTTGCCAAATCCATAGTGGTTGGCGTTTCAATGTATAGTCTCGCTGATAAATACCCGACCTATTTGCAGGATTCAATGAATAAATTTGTGCGTTCGCAAACAGATCTTAAATTTAAATATGCGGATGCCAATGGTGATCCGGCAAAAATGCTGAATGACGTAGAGAATTTTATTGATTCCAATGTGGATGCGTTAATTATTATGCCAACGGATCAAAAAATTGTGAAAGCCATCGGCTTAAAAGCAAAAAAAGCCAAAATCCCTTTAATTGTCGTCACTGTAAAACCGAATGAAGAAGATATGCAATATGTAGCAAGTTATGTGGGATCCGAGGAAGTTAAAAGCGGGGAAATGCAAGGTGAATTTATTGTTAATTCGCTGAACGGTAAACCGGCGAAAGCGATTATTTTACTCGGTCCGTTGGGCTTGGAAGCGCAAATTAAACGTACGGAAGGCAATAAAAAGATTTTTGCGCAACATCCTGAAATTAAGGTGGTGGCGGAACAAGAGGCAAAATGGGACCGATCAAAAGGCATGGAAGTGGCGGAAAATCTGCTTTCGGCACATCGCGATGCCAATGTGATTTTGAGTAATAATGACGAAATGGCAATCGGCGCATTGCTCGCGGCGAGGAAACTGGGCTTTAAAGATGAAGATTTGCTTATTGTCGGCATTGACGCGACACCGGATGCGTTGGGGTATTTAGGTAACGGTCTTGACGCGACTGTTTATCAATCGGCATCAGGGCAGGGGCGTTTGAGTGCAGAAATGGCATACAAAGCTGCGTTAGGCGAAGACATTCCGAAATATAACTGGATTCCTTTTGAATTGGTGACACCCGATATGAAGGAGCAATATATCAACAAATATAAGGAG","","","34143","MLKKMCILVLGLFFTPLILAKSIVVGVSMYSLADKYPTYLQDSMNKFVRSQTDLKFKYADANGDPAKMLNDVENFIDSNVDALIIMPTDQKIVKAIGLKAKKAKIPLIVVTVKPNEEDMQYVASYVGSEEVKSGEMQGEFIVNSLNGKPAKAIILLGPLGLEAQIKRTEGNKKIFAQHPEIKVVAEQEAKWDRSKGMEVAENLLSAHRDANVILSNNDEMAIGALLAARKLGFKDEDLLIVGIDATPDALGYLGNGLDATVYQSASGQGRLSAEMAYKAALGEDIPKYNWIPFELVTPDMKEQYINKYKE","1954361","","ribose ABC transporter, sugar binding protein","Periplasm, Cytoplasm","","
InterPro
IPR001761
Domain
Periplasmic binding protein/LacI transcriptional regulator
PF00532\"[22-299]TPeripla_BP_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2300\"[129-278]Tno description
signalp\"[1-20]?signal-peptide
tmhmm\"[10-30]?transmembrane_regions


","No hits to the COGs database.","","Residues 181 to 261 match (2e-11) PD:PD280480 which is described as COMPLETE PROTEOME PERIPLASMIC ABC BINDING TRANSPORTER TRANSPORTER SUGAR PRECURSOR PLASMID ","","","","","","","","","","","","Tue Jan 14 16:32:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02787 is paralogously related to AA02788 (1e-111), AA00209 (2e-29), AA00932 (7e-29), AA01455 (8e-17), AA00750 (4e-16) and AA02673 (8e-04).","","","","","","","","","","","","","","1","","","" "AA02788","1956477","1955542","936","ATGAAAAAGACACTACTTGCGTTACTTTGTGGTGGAATCCTATTAACGTCTCAAGCTGTTATTGCTAAAAATGTTGTAATTGGCGCTCCGATGGTTGCCTTCTCCGATAAATGGCAAACCTATCTTCAAGATGCGATTCGTGAATTTGATAAAACTCACGATGATGTTGAAATCAAACTTGCCGATGCGAACGGTGACCCTGCCCGCTTATTAAATGATGCGGAAACCTTCATTGACCAAAAAGTCGATGCCTTACTGGTTGTGCCGACCGATCCGAATATTGTTAAGGTGATTGGCAGAAAAGCCAAACGCGCCGGCATTCCTCTCATTATTATTAATCGTAAACCGTTAGATGAAGATATGCAGTATGTCACCAGTTATGTGGGATCTGATGAAATTGAAGGGGGACGTATTCAAGCGGGCTTCATTGTGAATACATTGAAAGGTAATCCTGCCGAAGCCGCCATTTTAATGGGACCTTTAGGTCAGGATGCGCAAATTAAACGGACACAAGGTAACAAAGAAATTTTTGCACAGAATAAAAATATCAAAATCTTTACCGAACAAGAAGGTAAATGGGACAGAGCTAAGGGATTGGAAATTGCAGAAAACCTACTTGCGGCAAACAAAAATCTGAATGTTGTGGTAAGTAATAATGATGAAATGGCGATTGGTGCCGTATTGGCAGGTAGAAAGTTAGGACTTAAAGACGAAGATTTAATTATTGTGGGATTGGATGCGACACCGGATGCGTTGGATTACCTGGGTAAAGGTTTAGATGCGACCGTGTTCCAATCTGCTGCCGGTCAAGGTGCTGCAGGCGCGGAAATGGCATATCTCGCGGCTAAAGGTGAAAAAGTGCCGTCCGTGAAATGGGTACCTTTTGAACTTGTCACACCGGATAAAAAAGAGGAATACCAGGCGAAATATAAAAAA","","","33773","MKKTLLALLCGGILLTSQAVIAKNVVIGAPMVAFSDKWQTYLQDAIREFDKTHDDVEIKLADANGDPARLLNDAETFIDQKVDALLVVPTDPNIVKVIGRKAKRAGIPLIIINRKPLDEDMQYVTSYVGSDEIEGGRIQAGFIVNTLKGNPAEAAILMGPLGQDAQIKRTQGNKEIFAQNKNIKIFTEQEGKWDRAKGLEIAENLLAANKNLNVVVSNNDEMAIGAVLAGRKLGLKDEDLIIVGLDATPDALDYLGKGLDATVFQSAAGQGAAGAEMAYLAAKGEKVPSVKWVPFELVTPDKKEEYQAKYKK","1955377","","possible ABC-related substrate binding protein","Periplasm, Cytoplasm","","
InterPro
IPR001761
Domain
Periplasmic binding protein/LacI transcriptional regulator
PF00532\"[24-301]TPeripla_BP_1
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2300\"[131-280]Tno description
signalp\"[1-22]?signal-peptide


","No hits to the COGs database.","","","","","","","Mon Feb 17 06:19:56 2003","","","","","","","Wed Mar 17 09:38:37 2004","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02788 is paralogously related to AA02787 (1e-111), AA00932 (2e-29), AA00209 (1e-26), AA00750 (4e-20) and AA01455 (3e-18).","Wed Mar 17 09:38:37 2004","","","","","","","","","","Rossbach S, Kulpa DA, Rossbach U, de Bruijn FJ.Molecular and genetic characterization of the rhizopine catabolism (mocABRC) genes of Rhizobium meliloti L5-30.Mol Gen Genet. 1994 Oct;245(1):11-24.PMID: 7845353","","Mon Feb 17 06:19:56 2003","1","","","" "AA02789","1957917","1956781","1137","ATGAAACAAGTGCGTATAGGTTTAGTGGGAACGGGATATATTGGGCGTTGTCACGCAATTGCTTATGCTCAGGCGCCGACGGTGTTTCCTCTTGATGCCGAGTTGGTTTTAGAGTATTTGGCGGAAGTCACCCCCGAATTAGCGGAAAAAAAAGCAAAAGAATTTGGTTTTAAACGTTTTACCGGTGATTGGCGTGATATCGTGCAGGATCCGAATGTGGATGTGGTGGATATATGCACACCGAATTTTCTCCATAAAGACATTGCGTTGGCGGCCATTGCAAATGGCAAACACGTTTATTCCGAAAAACCGCTGGCATTGACGGCGGCAGATGCCAAGTTAATGTACAAAGCAGCAAAAAAAGCTGGGGTTAAGACTTTAGTCGGGTTTAACTACATCAAGAATCCGACAACCCAATTGGCACGGGAAATTATTGCCAAGGGCGAAATCGGTGAAGTTATTCATTTCTATGGCACACATAATGAAGATTATCTCGCTAATGAAAATACACCGTTGGATTGGCATTGTGTCAAAGAAAAGGCTGGTTTGGGCACATTAGGTGATCTTGCCGCACACATTGTGCAAATGTCTCAGTATTTGTTAGGACAAGAGATTCGCGTGGTTATCGGTGATATGCAAACGGTGATTCAAACCCGACCTAATCCTAACAGTCTGCAAGAGCGTCTGACGGTAGAAAATGAAGACCAGGCGAGCGCGTTGGTGCGTTTCGCCAATGGTTGTATGGGAACGATTGAAACCTCCCGTATCGCTTCCGGGCGTAAAATGGGGCTAAGTTATGTGATTACGGGAACAAAAGGCACAATTTCCTATACTCAGGAACGAATGGCTGAATTGAAGCTTTATCTGCATGATGAAGATCCTGCAAGACAAGGGTTTAAAACCATTCTCACCGGACCGTTACACCCTGATTACAAGCATTTTTGCGTAAGTGCCGGCCATGGTATCGGTTTTAATGACCAAAAAACGGTGGAGATCAGAGATTTGGTCAATGGTCTTGCGTCTTCTGAAAATACCTTATATCCGGATTTTGAAGAAGGTTACAAGGTTTCCCGCGTGTTGGATGCTATTGCGTTTTCATGTGAACAAAAGCGTTGGATAGACGTAGAAGAGGTTGCG","","","41969","MKQVRIGLVGTGYIGRCHAIAYAQAPTVFPLDAELVLEYLAEVTPELAEKKAKEFGFKRFTGDWRDIVQDPNVDVVDICTPNFLHKDIALAAIANGKHVYSEKPLALTAADAKLMYKAAKKAGVKTLVGFNYIKNPTTQLAREIIAKGEIGEVIHFYGTHNEDYLANENTPLDWHCVKEKAGLGTLGDLAAHIVQMSQYLLGQEIRVVIGDMQTVIQTRPNPNSLQERLTVENEDQASALVRFANGCMGTIETSRIASGRKMGLSYVITGTKGTISYTQERMAELKLYLHDEDPARQGFKTILTGPLHPDYKHFCVSAGHGIGFNDQKTVEIRDLVNGLASSENTLYPDFEEGYKVSRVLDAIAFSCEQKRWIDVEEVA","1956616","","oxidoreductase-dehydrogenase","Cytoplasm, Periplasm","","
InterPro
IPR000683
Domain
Oxidoreductase, N-terminal
PF01408\"[4-130]TGFO_IDH_MocA
InterPro
IPR004104
Domain
Oxidoreductase, C-terminal
PF02894\"[142-271]TGFO_IDH_MocA_C
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[2-165]Tno description
PTHR22604\"[61-379]TOXIDOREDUCTASES
PTHR22604:SF14\"[61-379]TOXIDOREDUCTASE


","No hits to the COGs database.","","Residues 122 to 254 match (2e-07) PD:PD040176 which is described as PROTEOME COMPLETE 2-DEHYDROGENASE MYO-INOSITOL MLL3104 TREHALOSE UTILIZATION-RELATED OXIDOREDUCTASE ","","","","","","","","","","","","Tue Jan 14 16:37:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02789 is paralogously related to AA02802 (9e-21).","","","","","","Residues 142 to 271 (E-value = 1.2e-08) place AA02789 in the GFO_IDH_MocA_C family which is described as Oxidoreductase family, C-terminal alpha/beta domain (PF02894)","","","","","","","","1","","","" "AA02790","1959516","1958011","1506","ATGGAAACCGTTTATAACTTTATTAATGGTAAACAAGTTCCAAGCAGAGGGACAAAAGCGCATCCGATTTATAACCCGGCAACCGGCGAGCAAATTCGTCAGGTGATCATGAGTTCGCCTGAGGATGTCAATGAAGCGATTGAAGTGGCGCATAAAGCCTTTGCCGATTGGTCGGCAACCGCTCCGCTACGTCGTGCCCGTATTATGTTTAAATTTAAGGAATTATTGGAAAGAGATTGGGATTCATTGGCTCGTTTGATTGTTGAAGAACATGGTAAAGTGTATTCCGATGCGTGCGGTGAATTGACGCGTGGCTTGGAAGTGGTGGAATTTTCATGCGGGATTCCTCATTTGTTAAAAGGTGAATTTTCAGAACAGGCGGGACGTGGTATCGATATTCACTCTTCATTGCAACCGTTAGGCGTAACTGTGGGAATCACGCCATTTAACTTCCCGGCAATGGTGCCGATGTGGATGTTCCCGATTGCCTTAGTTTGTGGTAATACCTTCATTTTGAAACCGGCAAAAGCCGATCCTTCTTTATCTATTCGTTTAGCCGAGCTGTTAAAAGAAGCCGGTTTGCCTGATGGAGTATTTAATGTGGTGCATGGCGATCGTAATGACAATGAAATTTTATTGCGCGATCTGCGTGTTCATGCGGTGAGTTTTGTGGGGTCAACACCGGCAGCGGCACATGTGTATAAAGTCGGTTCTGAATTCGGCAAACGCGTACAAACCTTTGGGGCTGCGAAAAATCATGCACTTATCATGCCTGATGCGGATATTGAATCCACGGCGAATGCTCTCTTGGGGGCGGCATTCGGTGCGGCCGGGGAACGTTGTATGGCGTTGGCACTGGCAGTGACGATTGATGATGAAACCACAGATAAATTGGTTGCCGCCTTAAAACCGAAAGTGGAAGCGCTTCGTTATGGTCCGGGCATTCCGAAACCGGGTGAAAAAGAAATGGACTTTGGTCCGCTCATTACGCAACAACACTTGAATAACGTGACCAATTACATTACAACCGGGGTAGAAGAAGGTGCTACTTTAGTGGTTGACGGACGTGGCAAAAAACCGGCAGATTATGAAAATGGCTTCTTTATCGGCGGTTCCTTATTTGACAATGTGACTTCCGATATGGTGATTTATAAAGAGGAAATCTTTGGCCCGGTACTCGGCATTGTCAGAGCGAAAAGCTTTGAAGAGGCGATGAAGCTGATTAATGAACATCCTTACGGAAACGGTACGGCAATCTTTACTTCCGACGGCGGCGCGGCGCGTGAATTCGCTTACCATGTTCAAGCCGGTATGGTGGGGATCAATGTGCCGATTCCGGTACCGATGTCATTCCACTGTTTCGGCGGCTGGAAACATTCTTCTTACAGCACCTTGAATGTTTATGGTCCGGATGGTGTTCGTTTTTATACGAAGATGAAAACGGTAACAACACGTTGGCCGAATAAATATGTGATTGAAAATGCGGCATTTAGTATGCCTACACTT","","","57947","METVYNFINGKQVPSRGTKAHPIYNPATGEQIRQVIMSSPEDVNEAIEVAHKAFADWSATAPLRRARIMFKFKELLERDWDSLARLIVEEHGKVYSDACGELTRGLEVVEFSCGIPHLLKGEFSEQAGRGIDIHSSLQPLGVTVGITPFNFPAMVPMWMFPIALVCGNTFILKPAKADPSLSIRLAELLKEAGLPDGVFNVVHGDRNDNEILLRDLRVHAVSFVGSTPAAAHVYKVGSEFGKRVQTFGAAKNHALIMPDADIESTANALLGAAFGAAGERCMALALAVTIDDETTDKLVAALKPKVEALRYGPGIPKPGEKEMDFGPLITQQHLNNVTNYITTGVEEGATLVVDGRGKKPADYENGFFIGGSLFDNVTSDMVIYKEEIFGPVLGIVRAKSFEEAMKLINEHPYGNGTAIFTSDGGAAREFAYHVQAGMVGINVPIPVPMSFHCFGGWKHSSYSTLNVYGPDGVRFYTKMKTVTTRWPNKYVIENAAFSMPTL","1957846","","NAD-dependent aldehyde dehydrogenase","Cytoplasm","","
InterPro
IPR002086
Domain
Aldehyde dehydrogenase
PF00171\"[13-482]TAldedh
PS00070\"[274-285]?ALDEHYDE_DEHYDR_CYS
InterPro
IPR010061
Family
Methylmalonate-semialdehyde dehydrogenase
PTHR11699:SF27\"[48-501]TMETHYLMALONATE-SEMIALDEHYDE DEHYDROGENASE
TIGR01722\"[4-486]TMMSDH: methylmalonate-semialdehyde dehydrog
InterPro
IPR012303
Family
NAD-dependent aldehyde dehydrogenase
PIRSF000147\"[20-490]TNAD-dependent aldehyde dehydrogenase
InterPro
IPR015590
Domain
Aldehyde Dehydrogenase_
PTHR11699\"[48-501]TALDEHYDE DEHYDROGENASE-RELATED
noIPR
unintegrated
unintegrated
G3DSA:3.40.605.10\"[3-284]Tno description


","No hits to the COGs database.","Significant hit ( 1.5e-48) to 6/6 blocks of the IPB002086 family, which is described as \"Aldehyde dehydrogenase family\". Interpro entry for IP:IPR002086. IPB002086A 139-152 5.6e-05 IPB002086B 193-210 0.00038 IPB002086C 218-238 0.00076 IPB002086D 252-295 1.6e-06 IPB002086E 368-421 1.7e-21 IPB002086F 438-462 18","Residues 381 to 421 match (7e-07) PD:PD506672 which is described as PROTEOME ALDEHYDE DEHYDROGENASE NAD-DEPENDENT COMPLETE OXIDOREDUCTASE ","","","","","","","","","","","","Tue Jan 14 16:38:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02790 is paralogously related to AA02784 (8e-06).","","","","","","Residues 13 to 486 (E-value = 3.2e-156) place AA02790 in the Aldedh family which is described as Aldehyde dehydrogenase family (PF00171)","","","","","Steele MI, Lorenz D, Hatter K, Park A, Sokatch JR.Characterization of the mmsAB operon of Pseudomonas aeruginosa PAO encoding methylmalonate-semialdehyde dehydrogenase and 3-hydroxyisobutyrate dehydrogenase.J Biol Chem. 1992 Jul;267(19):13585-92.PMID: 1339433","","Wed Jan 22 11:23:49 2003","1","","","" "AA02792","1961097","1959757","1341","ATGTCTGTTCTCAGCTTTTTTAAAGCCAGTTCGGCAATTCCGTTGAAGGATTACACGGAAAAAATGTTTAGAAGTACACGAATGAAAAACTTTTGGGCATTTTCATTCGCTTACGCCATTTATTATGTTTGTCGCTTATCTTTTAATGTGGCGAAGCCTGCGTTGGTCAATAACGGCATATTAAGCGCAACGGAATTGGGGGTTATCGGTTCCGCAACCTTTATTACTTATGCGGTCGGGAAATTCGTGAACAGTGCGTTGGCGGATCATTCCAACATCGTTCGTTTCTTTTCCGTCGGCTTGTTCTTTTCCGCGCTTGCCAATTTCGCCATGGGCATGAACACCAGCGCCATTGTGTTGACCATTATTTGGGGATTCAACGGTTGGGTGCAATCCATGGGGGTGGGACCTTGCGTCGTGGCGTTATCCCGTTGGTATGATGACAAAGACCGTGGTTCCTATTATGGTTTCTGGTCTGTTGCGCATAATGCGGGGGAAGCGATTACTTTTGTGGTGACAGCCGCCATTATTACCGCATTCGGTTGGCGCGCCGGGTTTAATTTTGCCGGTATCACCGGCTTGTTAGGTGTGCTTGTGACCATCATGTTCATGAAAGATTCGCCGGAATCCTGCGGATTTAAACCGATTATTAAAACCGAATCAAAAGAAGAAACTTTCGATAATAAAGAAGTATTAAAACACCAATGGGAAGTGATAAAAAATCCGGCGATTTGGATCCTGGCAGTCGCTTCTTGTTGTATGTATATTGCCCGTTATGGCGTGAACAGTTGGGGCGTATTTTTCCTGGAAAACGGCAAAGGCTACACCACCATTGAAGCAGCTTCTATTATTAGCGTAAACAGTATTGTCGGTATTCTGGGAACGGTGGCTTCAGGCTGGTTATCCGATCGTTTCTTACAGGGTAGACGGAATATCATGACCATCGGGGTCAGTTTGCTTAACGTCATTTCTTTGGCAGCCTTCTTATTCGCCCCGAACGGTAATACCTGGTTCTCCATTATTGCACTTTCCGTCTTTGGTATTACGCTCGGTATTCAATTATGTTTCTTAGGCGGTTTATTGGCGACGGACATTTCCCATAAATCCGCATCTGGTATCGCATTAGGCATGATGGGCGTATTCGGTTATGCCGGTGCGGCGGCAGGGGAGTTTCTCACCGGCTTTATGTTAGATAAAACCACGGTGATTAATGAAGCCGGTAAGAAAATTTATGATTTCGACAGCTTGTCCTATTTCTGGGTCGGCGCCGATGTGTGCTCCGTATTGGCATCCGTGCTGTTTGCTGTGGTTGTATACTATCAAACCCGACGGGTTACAAAT","","","48620","MSVLSFFKASSAIPLKDYTEKMFRSTRMKNFWAFSFAYAIYYVCRLSFNVAKPALVNNGILSATELGVIGSATFITYAVGKFVNSALADHSNIVRFFSVGLFFSALANFAMGMNTSAIVLTIIWGFNGWVQSMGVGPCVVALSRWYDDKDRGSYYGFWSVAHNAGEAITFVVTAAIITAFGWRAGFNFAGITGLLGVLVTIMFMKDSPESCGFKPIIKTESKEETFDNKEVLKHQWEVIKNPAIWILAVASCCMYIARYGVNSWGVFFLENGKGYTTIEAASIISVNSIVGILGTVASGWLSDRFLQGRRNIMTIGVSLLNVISLAAFLFAPNGNTWFSIIALSVFGITLGIQLCFLGGLLATDISHKSASGIALGMMGVFGYAGAAAGEFLTGFMLDKTTVINEAGKKIYDFDSLSYFWVGADVCSVLASVLFAVVVYYQTRRVTN","1959592","","GlpT/UhpT family transporter (hexosphosphate transport)","Inner membrane, Cytoplasm","","
InterPro
IPR007114
Family
Major facilitator superfamily
PS50850\"[25-441]TMFS
InterPro
IPR011701
Family
Major facilitator superfamily MFS_1
PF07690\"[34-398]TMFS_1
noIPR
unintegrated
unintegrated
PTHR11662\"[20-445]TSODIUM-DEPENDENT PHOSPHATE TRANSPORTERS
PTHR11662:SF13\"[20-445]TGLYCEROL-3-PHOSPHATE TRANSPORTER (HEXOSE TRANSPORTER)
tmhmm\"[31-49]?\"[59-79]?\"[99-119]?\"[125-145]?\"[160-180]?\"[184-204]?\"[243-261]?\"[280-302]?\"[312-332]?\"[338-360]?\"[369-389]?\"[418-438]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 4.9e-52) to 7/7 blocks of the IPB000849 family, which is described as \"GlpT family of transporters\". Interpro entry for IP:IPR000849. IPB000849A 23-55 4.6e-05 IPB000849B 65-105 9.4e-14 IPB000849C 131-166 1.3e-08 IPB000849D 186-222 0.0006 IPB000849E 232-269 3.2e-08 IPB000849F 286-303 0.049 IPB000849G 347-379 1.3Significant hit ( 1.3e-05) to 4/5 blocks of the IPB002897 family, which is described as \"Monocarboxylate transporter\". Interpro entry for IP:IPR002897. IPB002897B 75-129 26 IPB002897C 180-205 12 IPB002897D 247-299 4 IPB002897E 360-411 3.4","Residues 341 to 423 match (9e-07) PD:PD264499 which is described as REGULATORY PROTEOME COMPLETE UHPC ","","","","","","","","","","","","Tue Jan 14 16:43:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02792 is paralogously related to AA00497 (6e-59), AA01378 (6e-51) and AA02864 (2e-45).","","","","","","","","","","","Eiglmeier,K., Boos,W. and Cole,S.T. Nucleotide sequence and transcriptional startpoint of the glpT gene of Escherichia coli:extensive sequence homology of the glycerol-3-phosphate transport protein with components of the hexose-6-phosphate transport system Mol. Microbiol. 1 (3), 251-258 (1987) PubMed: 3329281 Gott,P. and Boos,W. The transmembrane topology of the sn-glycerol-3-phosphate permease of Escherichia coli analysed by phoA and lacZ protein fusions Mol. Microbiol. 2 (5), 655-663 (1988) PubMed: 3141744 Auer M, Kim MJ, Lemieux MJ, Villa A, Song J, Li XD, Wang DN. High-yield expression and functional analysis of Escherichia coli glycerol-3-phosphatetransporter. Biochemistry. 2001 Jun 5;40(22):6628-35. PMID: 11380257 ","","Tue Jan 14 16:42:23 2003","1","","","" "AA02793","1961918","1961118","801","ATGGACGTTGAACTACTAAATAGATATTTATTTTCTCAGGAGTTAGTCAAAGAAGTTGGGAAAATTGCACTGGATTTTTACCTTAAACGTAAGGAATTAAAAATTGAGTGTAAAAAAGGTGATTTACAGGATCAAGTCAGTATCGCGGATAAAACCGTTGAAGCGAAAATTAAAGAAGCATTAAAACAACATTTTCCGCAAGATGGTTTTTTAGGCGAAGAATCCGGTGCTGAAAACTTATCCTGTGAATATTGTTGGGTTGTGGATCCAATTGATGGCACCAGCCCGTTTTTATATGGGTTAAACGCATGGTGCGTGTCCATTGCAATTTTGCATAAAAATCAAATTGTCTCCGGTGTGATTTTTGATCCCGTCCACAATGAGTTGTTCAGAGCAATGAAAGGGGATGGCGCATTTCTGAATGATCAACCTATTCACGCTTCCTCTTCCACCTCTTTAAAAGAAGGATTAATGGGATTAGGCGTTTCCCACCGTGTTCACCCCGATACTTTTACTCCTGTGCTACACCAAATTTTATTGGACGGTGGGATGTTCATTCGTAACGGTTCCGGTGCGTTAATGTTGGTTTATGTGGCGGCAGGTCGCTTGATTGGCTATTTTGAACCGCATATTAACGCTTGGGATGTTTGCGCCGCGATCATTATTGTTCAGGAAGCGGGCGGGCATGTGAATAATTTCCTTGAAAATGAAGGACTCGGCAAAGGAAATTATATTTTAGGTTGCTGTACCGAAGCGCTGTTTACAGAACTCAATCACATCAAAAATTCACACGAAATACGC","","","29544","MDVELLNRYLFSQELVKEVGKIALDFYLKRKELKIECKKGDLQDQVSIADKTVEAKIKEALKQHFPQDGFLGEESGAENLSCEYCWVVDPIDGTSPFLYGLNAWCVSIAILHKNQIVSGVIFDPVHNELFRAMKGDGAFLNDQPIHASSSTSLKEGLMGLGVSHRVHPDTFTPVLHQILLDGGMFIRNGSGALMLVYVAAGRLIGYFEPHINAWDVCAAIIIVQEAGGHVNNFLENEGLGKGNYILGCCTEALFTELNHIKNSHEIR","1960953","","inositol-1-monophosphatase; extragenic suppressor protein","Cytoplasm","","
InterPro
IPR000760
Family
Inositol monophosphatase
PD023420\"[46-100]TQ8YCG2_BRUME_Q8YCG2;
PR00378\"[62-78]T\"[81-100]T\"[193-208]T\"[210-228]TINOSPHPHTASE
PTHR20854\"[66-230]TINOSITOL MONOPHOSPHATASE
PF00459\"[4-230]TInositol_P
PS00629\"[86-99]TIMP_1
PS00630\"[214-228]TIMP_2
noIPR
unintegrated
unintegrated
G3DSA:3.30.540.10\"[6-145]Tno description
G3DSA:3.40.190.80\"[146-262]Tno description
PTHR20854:SF4\"[66-230]TMYO INOSITOL MONOPHOSPHATASE


","No hits to the COGs database.","Significant hit ( 8.1e-30) to 3/3 blocks of the IPB000760 family, which is described as \"Inositol monophosphatase\". Interpro entry for IP:IPR000760. IPB000760A 44-74 1.2e-11 IPB000760B 86-97 6.4e-06 IPB000760C 214-232 4.3e-09","Residues 182 to 227 match (4e-13) PD:PD549415 which is described as MONOPHOSPHATASE INOSITOL PROTEOME PLASMID COMPLETE ","","","","","","","","","","","","Fri Jan 24 13:42:13 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02793 is paralogously related to AA00705 (8e-36) and AA01166 (2e-09).","","","","","","Residues 4 to 266 (E-value = 9.4e-60) place AA02793 in the Inositol_P family which is described as Inositol monophosphatase family (PF00459)","","","","","","","","1","","","" "AA02794","1962182","1963009","828","ATGAGTTACTTACTATCTAAATCCAAAAAAAATCATCCTGAAAAGAACGGTGAAGTCCAAAAAATCACACCGCAAACAGCCAATTGGGAATATGTCGGTTTTGAGATGTATCACCTGCAAAAAGACCAAGAGCTTACCTTCGATACGGAAAATACTGAGGTTTGCTTCGTGCTGATTGCTGGTCAAGCCACTGTTGCAACCGCTCAAGCCACATTTGAACATATCGGCAACCGCACTTCGCCTTTTGAGCGAATCCCCCCTTATTCCGTATACGTGCCGCATCATCAGCAGGTCCACATTAACGCGGAAAGCTATTTAGAACTGGCGGTTTGTCGTGCACCAAGCCAAGGGAATTTGCCGGTGCGTTTAATCGAACCAAAAGATGTGGGCGTAGAAAAACGCGGATACGGCAACAATAAACGTCTGGTGCACAATATCCTGCCGGAAACCGAAACCGCAGATGCGTTATTGGTGGTTGAAGTATTTACCGATGAAGGCAATACCAGTTCATTCCCCAGCCATAAACACGATGATAAAAACTCCCCAACCGAAACCTACCTGGAAGAAACCTATTATCACCGTTTCTTCCCGTCACAAGGCTTCGCATTACAACGCGTTTACACTGACGATCGATCACTAGATGAATGTATGGCGGTATATGACGGTGATGTAGTTCAGGTGCCAAGAGGTTATCATCCCGTTGCCACCATCGCCGGTTATGAAAATTATTACTTAAACGTGATGGCCGGTCCGGTGAGAAAATGGCGTTTTACCTGGGAACAGGATCACGCCTGGATTAACAGCGAAGAATACGCCGATAAATTCAAA","","","31747","MSYLLSKSKKNHPEKNGEVQKITPQTANWEYVGFEMYHLQKDQELTFDTENTEVCFVLIAGQATVATAQATFEHIGNRTSPFERIPPYSVYVPHHQQVHINAESYLELAVCRAPSQGNLPVRLIEPKDVGVEKRGYGNNKRLVHNILPETETADALLVVEVFTDEGNTSSFPSHKHDDKNSPTETYLEETYYHRFFPSQGFALQRVYTDDRSLDECMAVYDGDVVQVPRGYHPVATIAGYENYYLNVMAGPVRKWRFTWEQDHAWINSEEYADKFK","1962844","[PATHWAY] Myo-inositol catabolism.","myo-inositol catabolism protein","Cytoplasm","","
InterPro
IPR010669
Domain
Myo-inositol catabolism IolB region
PF06845\"[22-268]TIolB
InterPro
IPR012185
Family
Myo-inositol catabolism IolB
PIRSF036628\"[1-271]TMyo-inositol catabolism protein IolB
noIPR
unintegrated
unintegrated
PD550483\"[15-266]TQ8ZK62_SALTY_Q8ZK62;


","No hits to the COGs database.","","Residues 245 to 271 match (2e-07) PD:PD562891 which is described as INNER PROTEOME COMPLETE MEMBRANE ","","","","","","","","","","","Wed Jan 22 11:10:18 2003","Wed Jan 22 11:10:18 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02794 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 22 to 268 (E-value = 1.2e-158) place AA02794 in the IolB family which is described as Myo-inositol catabolism protein IolB (PF06845)","","","","","Yoshida K, Sano H, Miwa Y, Ogasawara N, Fujita Y.Cloning and nucleotide sequencing of a 15 kb region of the Bacillus subtilis genome containing the iol operon.Microbiology. 1994 Sep;140 ( Pt 9):2289-98.PMID: 7952181Yoshida K, Seki S, Fujimura M, Miwa Y, Fujita Y.Cloning and sequencing of a 36-kb region of the Bacillus subtilis genome between the gnt and iol operons.DNA Res. 1995;2(2):61-9.PMID: 7584049","","Wed Jan 22 11:10:18 2003","1","","","" "AA02796","1963141","1963977","837","ATGAAAGAAAAATCTCAATTAACCAATTTACAAACAGAAATACAAACCCGTTACGACAGCTTAAGTAAAAGGCTCAAACAGGTTGCTCAATATATTTTGGACAACAGCGACAGCATCGTTTTTGATACCGTTGCCACTATCGCCGAAAAAGCGGACGTACCGCCCTCTACATTAATCCGCTTTGCTGCCGAATTCGGTTTTTCCGGCTTTAACGAAATGAAACAAATTTTCCGTGAAAATCTCATGGAAAAAACCACAAACTACACGGAGCGACTACAGCTTTCACACAAAATCGCCCGATCGGAAGGAGAAGAATCCCCGGAAGACATTTTGACGATTTTCTCGCAAGCCAACAGTCAGGCATTGATTCAACTGGCAGAACAAACCACAAACGATCAAGTTTACGCCGCCGCCAAAATGTTAAAAGAAGCCAATAACATTTTTATTATCGGTCTAAAACGATCTTTTAGCGTTGCCTGTTATCTCAACTACGCTCTCCATCACTTAGATTGCAGTTCCTTTTTAATTAATGGCTTGGGCGGGATGTTTGATGAACAGCTCAATCAGGTTAAAGAAGGCGATGTGGTGGTTGCCATTAGTTTCTCGCCTTATGCGGCGGAAACCGTCAATATTATGAATACCAGTGCCAAAAAAGGCATTAAGCAAATTGCCATCACCGACAGCCAAATCAGCCCGCTACTTGCCTTCAGCGATATTGCTTTTGTGATAAAAGAAGCGCAGGTGTTGGGATTTCGTTCCCAATGCTCAACGATGACGTTGGTTCAAACACTGGCGATTGTGCTAGGGCTGGAAAAAGAAAAAGAGAAAACAAGCAAG","","","31064","MKEKSQLTNLQTEIQTRYDSLSKRLKQVAQYILDNSDSIVFDTVATIAEKADVPPSTLIRFAAEFGFSGFNEMKQIFRENLMEKTTNYTERLQLSHKIARSEGEESPEDILTIFSQANSQALIQLAEQTTNDQVYAAAKMLKEANNIFIIGLKRSFSVACYLNYALHHLDCSSFLINGLGGMFDEQLNQVKEGDVVVAISFSPYAAETVNIMNTSAKKGIKQIAITDSQISPLLAFSDIAFVIKEAQVLGFRSQCSTMTLVQTLAIVLGLEKEKEKTSK","1963812","","possible transcriptional regulator, RpiR family","Cytoplasm, Outer membrane","","
InterPro
IPR000281
Domain
Helix-turn-helix protein RpiR
PF01418\"[8-74]THTH_6
PS51071\"[8-84]THTH_RPIR
InterPro
IPR001347
Domain
Sugar isomerase (SIS)
PF01380\"[140-267]TSIS
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.10490\"[98-269]Tno description


","No hits to the COGs database.","Significant hit ( 1.1e-07) to 2/3 blocks of the IPB000281 family, which is described as \"Helix-turn-helix domain, RpiR family\". Interpro entry for IP:IPR000281. IPB000281A 151-169 15 IPB000281B 179-226 2.8e-06","Residues 14 to 87 match (2e-07) PD:PD246500 which is described as PROTEOME COMPLETE TRANSCRIPTIONAL REGULATOR TRANSCRIPTION REGULATION DNA-BINDING REPRESSOR REGULON RPIR ","","","","","","","","","","","","Fri Jan 31 14:03:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02796 is paralogously related to AA02468 (3e-13).","","","","","","Residues 8 to 122 (E-value = 5e-08) place AA02796 in the HTH_6 family which is described as Helix-turn-helix domain, rpiR family (PF01418)","","","","","Sorensen KI, Hove-Jensen B.Ribose catabolism of Escherichia coli: characterization of the rpiB gene encoding ribose phosphate isomerase B and of the rpiRgene, which is involved in regulation of rpiB expression.J Bacteriol. 1996 Feb;178(4):1003-11.PMID: 8576032","","Fri Jan 31 14:03:12 2003","1","","","" "AA02797","1965927","1964023","1905","ATGAAAACGGTGGAAAAAACATTAGACCTTATTTGTCTTGGTCGGGTTGCTGTTGATCTTTATGCCCAACAAATCGGCGCCAGATTGGAAGATGTCTCTTCTTTTTCCAAATATCTTGGCGGTTCGTCCGGTAACGTTGCTTATGGCACGGCGGTGCAGGGTGTGAAATCCTCCATGCTGGCGCGTGTCGGTGATGAACACATGGGGCGTTTTTTGCGTGAGGAATTACAACGTGTCGGCGTGGATACCAGCCATTTGATTACGGATAAAGAACGCCTGACTGCCCTTGTGATTCTAGGCATTAAAGATCAGGACACTTTCCCGTTGATTTTTTACCGTGAAAATTGTGCGGATATGGCAATTACCAAAGAGGATTTTGATGAAAGTTATATTGCTTCCGCCAAAGCGCTTGCCATTACCGGCACCCATTTGTCGCATCCGAAAACACGAGAAGCCGTGTTAACGGCGTTGGAATATGCGGGCAGAAATAATACGAAACGTTTGCTGGATATTGATTATCGTCCGGTGTTATGGGGGCTGACGTCCTTGGGTGATGGGGAAACCCGGTTTATTGATTCGGCGGCGGTAACTAAATCATTGCAAGAAGTGTTACACCATTTTGATGTGTTGGTGGGCACAGAAGAAGAATTCCACATTGCCGGCGGTTCGACAGATACTTTAACCGCACTTAAAAATGTGCGTAAATTCAGCCATGCCGTTTTGGTGTGTAAACGTGGTGCGCTGGGCTGTTCTGTGTTTGAAGGGGAAATCCCTGATGATTTGGACGGCGGGTTAAATGTTTATGGAGTCAGAGTCGAAGTGCTTAATGTATTGGGTGCCGGCGATGCCTTTATGTCGGGGCTGATTCGTGGTTACATTAATAATGAAGGCTGGGAACAGGCGTGTCGTTATGCCAATGCTTGCGGTGCGTTGGTGGTTTCCCGTCACGGTTGTGCACCGGCAATGCCGACCAAAGCGGAATTGGATAATTATCTTGCCCGCGCACAATCGGTGCCGCGCCCGGATTTAGATGAACAACTTAATCATTTGCACCGAGTGACAACCAGAAAAGCCAAATGGGATAACTTATGTATTTTTGCTTTTGACCACCGTAAACAATTGGTGGATATGGCGGAAAAATACGGTGCGGACGTCAAACGTATTCCTAAACTGAAACAGCTTCTCTTGCAGGCGGCGGAAAAAACGGCACAGGAAGAAGGTATTTATAACGGTCAGGCGGGGATTCTGGCGGATACGACTTTCGGACAAGCGGCATTGAATGAAATTACCGGCAAGAAATGGTGGATTGGTCGCCCGATTGAGCTGCCGTCCTCCCGTCCGTTGCGTTTGGAACACGGCGATTTAGGCAGCCAATTAGCCGGTTGGCCCCAAGAGCATGTAGTGAAATGTTTGGTCTTTTATCATCCGAAAGACCGCGCAGAGATGAAAGCGGAGCAGGATGTCACATTAAAACAAGTGTATCAAGCCTGCTGTCGAACCGGTCATGAGTTGCTGTTGGAAGTGATTTTGCCGGCGGATATGGAACAAAACGAACAATATTACGCGGACATTCTCGCACACTTCTATCAATTAGGTATTAAGCCGGATTGGTGGAAATTACCGGGCGTTTCAGCGCAGGATTGGGAACGTATCAGCGAAGTAATTCAGGCAAATGATCCATATTGTCGCGGCATTTTGATTCTCGGCTTGGATGCGCCGGAAGCGCAGTTTAAAGCAGTATTTGATGCGTCTGCCAATACGCCTTTAGTAAAAGGCTTTGCAGTGGGGCGGACAATTTTCGGGCAGCCGTCGGCGGATTGGTTTGCCGGAAAATTAACAGATGACGAACTGATCGCCGAAGTGGGTGAAAGATACAGAAGACTGATTAAACTTTGGAAATCCCGT","","","70558","MKTVEKTLDLICLGRVAVDLYAQQIGARLEDVSSFSKYLGGSSGNVAYGTAVQGVKSSMLARVGDEHMGRFLREELQRVGVDTSHLITDKERLTALVILGIKDQDTFPLIFYRENCADMAITKEDFDESYIASAKALAITGTHLSHPKTREAVLTALEYAGRNNTKRLLDIDYRPVLWGLTSLGDGETRFIDSAAVTKSLQEVLHHFDVLVGTEEEFHIAGGSTDTLTALKNVRKFSHAVLVCKRGALGCSVFEGEIPDDLDGGLNVYGVRVEVLNVLGAGDAFMSGLIRGYINNEGWEQACRYANACGALVVSRHGCAPAMPTKAELDNYLARAQSVPRPDLDEQLNHLHRVTTRKAKWDNLCIFAFDHRKQLVDMAEKYGADVKRIPKLKQLLLQAAEKTAQEEGIYNGQAGILADTTFGQAALNEITGKKWWIGRPIELPSSRPLRLEHGDLGSQLAGWPQEHVVKCLVFYHPKDRAEMKAEQDVTLKQVYQACCRTGHELLLEVILPADMEQNEQYYADILAHFYQLGIKPDWWKLPGVSAQDWERISEVIQANDPYCRGILILGLDAPEAQFKAVFDASANTPLVKGFAVGRTIFGQPSADWFAGKLTDDELIAEVGERYRRLIKLWKSR","1963858","[PATHWAY] Myo-inositol catabolism.","carbohydrate kinase; myo-inositol catabolism protein","Cytoplasm","","
InterPro
IPR002173
Family
Carbohydrate kinase, PfkB
PS00584\"[276-289]?PFKB_KINASES_2
InterPro
IPR011611
Domain
PfkB
PF00294\"[7-325]TPfkB
InterPro
IPR013983
Domain
Aldehyde ferredoxin oxidoreductase, N-terminal
SM00790\"[14-143]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.40.1190.20\"[9-326]Tno description
PTHR10584\"[11-330]TSUGAR KINASE RELATED
PTHR10584:SF34\"[11-330]TFRUCTOKINASE


","BeTs to 16 clades of COG0524COG name: Sugar kinases, ribokinase familyFunctional Class: GThe phylogenetic pattern of COG0524 is aompkzy-vdrlbcefghs--j----Number of proteins in this genome belonging to this COG is","Significant hit ( 4.3e-05) to 2/2 blocks of the IPB002173 family, which is described as \"PfkB family of carbohydrate kinases\". Interpro entry for IP:IPR002173. IPB002173A 39-54 5.1 IPB002173B 275-289 0.0043","Residues 321 to 373 match (9e-17) PD:PD590427 which is described as PROTEOME KINASE COMPLETE TRANSFERASE 2.7.-.- PROBABLE IOLC CARBOHYDRATE ","","","","","","","","","","","Wed Jan 22 11:01:08 2003","Wed Jan 22 11:01:08 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02797 is paralogously related to AA00212 (1e-09) and AA02384 (2e-08).","","","","","","Residues 9 to 325 (E-value = 6.8e-53) place AA02797 in the PfkB family which is described as pfkB family carbohydrate kinase (PF00294)","","","","","Yoshida K, Sano H, Miwa Y, Ogasawara N, Fujita Y.Cloning and nucleotide sequencing of a 15 kb region of the Bacillus subtilis genome containing the iol operon.Microbiology. 1994 Sep;140 ( Pt 9):2289-98.PMID: 7952181","","Wed Jan 22 11:01:08 2003","1","","","" "AA02798","1965929","1966093","165","ATGCAATTCCTTCTTATTTTAATGAAATTATTTTACCTGCATAAAATTGAAACATATATTTCAAAAAAATCAACATTGAAATTTGTTTTTTTAGACGTTAATCACAAAATCAGCCCCGTTAAATTTTCTTTTCTATATTTAATTCGCCAAGATTTAACAGGCTGT","","","6597","MQFLLILMKLFYLHKIETYISKKSTLKFVFLDVNHKISPVKFSFLYLIRQDLTGC","1966093","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:19:29 2004","Mon Feb 23 15:19:29 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02798 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:19:29 2004","","","","","","","","","","","","","1","","","" "AA02799","1966175","1966050","126","ATGCTTTTGAAACAAAAATTTCATTTTTGCGACATAGATCAAATTTTTCCGAATTTATGTTTTATCTTGCAAGATCAGGTTAACAGCCTGTTAAATCTTGGCGAATTAAATATAGAAAAGAAAATT","","","4960","MLLKQKFHFCDIDQIFPNLCFILQDQVNSLLNLGELNIEKKI","1966050","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:17:51 2004","Mon Feb 23 15:17:51 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02799 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:17:51 2004","","","","","","","","","","","","","1","","","" "AA02800","1966239","1968182","1944","ATGAAAACCGTAAGACTTACTGTTGCACAAGCACTTATAAAATTCCTTGATAATCAATATATCGAATTTGACGGCAAAGTAACAAAATTTGTTGAAGGTATCTTTGGTATTTTCGGTCATGGCAATGTGCTCGGCATTGGTCAGGCGCTGGAACAAGACAGCGGTAACCTGATTGTACGCCAAGGGCGCAATGAACAAGGCATGGCACATGTCGCCATCGGTTTTGCGAAACAAAATCTGCGTAAAAAAATTTACGCCTGCACCTCTTCCGTCGGTCCCGGCGCCGCCAACATGATTACTGCCGCCGCCACCGCAACCGCCAATCGCATTCCGCTTCTTCTTTTACCGGGTGATGTTTTCGCCACCCGCCAACCGGATCCGGTTTTACAACAAATCGAACAATTCCATGATTTAAGCATCAGCACAAACGACGCGTTCCGTGCCGTGAGCAAATATTGGGACAGAGTCAGCCGTCCGGAACAACTGATGACCGCTTGTATTAACGCCATGCTGGTGTTAACGGATCCGGCGGACACCGGCGCCGTCACCATCGCTCTGCCGCAAGACGTCCAAGCGGAAGCCTATGATTTCCCGGAATATTTCCTGCAAAAACGCATTCACCGCATTGAGCGCACGCTCCCTACCGAACCTATGTTGAAATCTGCCGTGGATTTGATTCTGAAGGCGAAAAAACCGTTAATTATTTGTGGTGGCGGGGTGCGTTATTCCGAAGCGGCGGAGCAATTAAAACAGTTCGCCGAAACCTTCCAGATTCCTTTTGCCGAAACCCAGGCGGGAAAAAGTGCGGTCGTTTCCGAGCACGTTTTGAATGTGGGCGGTGTGGGAGAAACCGGCTGTTTGAGCGCCAACCTGTTGGCAAAAGAAGCGGATCTGATTATCGGTATTGGCACGCGTTACACGGATTTCACCACCTCCTCAAAATGGATCTTCCAAAATCCGGATGTGAAATTCCTGAACATCAACGTTGCTCGTTTCGATGCCTATAAACTGGATGGCGTCCAAGTGGTTGCTGATGCCAAAGAAACGCTGGAAAAACTGACCGCACTTTTAGCACCGACGGGCTACCGTTACCGCGCTCAATGGGGCAACGCCGTTGCCGAAGCCAAAGCGCAATTTGCCCAAGAACTCCAACGGATTTATCACGCGGTTTACACCGAAACCGATTTCGTACCGGAAGTGGACGATGCTTTAGATCGCGAAAAAGTCTATGCGGAATTTATTAAATTGACCCAATCCCATCTGCCCCAAAGTCGCGTGTTAGGCATTCTCAATGAAACCTTGGGCGAAAACGACATTATCGTAGGCGCCGCGGGCAGCTTGCCGGGTGACTTGCAACGGGCATGGCAATCCAAGGTTGAAAACACTTACCATCTGGAATACGGCTATTCCTGCATGGGATATGAAGTGAACGCCGCATTGGGCGCGAAATTGGCGCAACCTGAAAAAGAAGTTTATGCCTTATTGGGCGACGGTTCTTACATGATGCTCCATTCCGAACTGGTGACCTCCGTTCAGGAACATAAAAAAATCAACGTAATTTTATTCGACAACATGACAAACGGCTGTATTAACAATCTGCAAATCGGCAATGGTATGGACAGCTTCGCCACCGAATTCCGCTTCAGAAATCCGCAAACCAATAAATTAGACGGCGGATTCGTGCCCGTTGACTTTGCCATGAATGCGGCATCTTACGGTTGTAAAACCTATAAAGTCACCACTGAAGAGGAATTACGCGCCGCCCTTGCCGATGCGAAAAAACAAACCGTCTCTACGTTGATTGACATAAAAGTCTTGCCAAAAACCATGATTCACGGCTACGGCAGCTGGTGGCACGTTGGCGTAGCAGAAGTGTCGGAAAAAGAAAAAATCCGCAAAGCGCATAAAAGCAGCGTGAAACACATTAACGAAGCAAGACGCTAT","","","75728","MKTVRLTVAQALIKFLDNQYIEFDGKVTKFVEGIFGIFGHGNVLGIGQALEQDSGNLIVRQGRNEQGMAHVAIGFAKQNLRKKIYACTSSVGPGAANMITAAATATANRIPLLLLPGDVFATRQPDPVLQQIEQFHDLSISTNDAFRAVSKYWDRVSRPEQLMTACINAMLVLTDPADTGAVTIALPQDVQAEAYDFPEYFLQKRIHRIERTLPTEPMLKSAVDLILKAKKPLIICGGGVRYSEAAEQLKQFAETFQIPFAETQAGKSAVVSEHVLNVGGVGETGCLSANLLAKEADLIIGIGTRYTDFTTSSKWIFQNPDVKFLNINVARFDAYKLDGVQVVADAKETLEKLTALLAPTGYRYRAQWGNAVAEAKAQFAQELQRIYHAVYTETDFVPEVDDALDREKVYAEFIKLTQSHLPQSRVLGILNETLGENDIIVGAAGSLPGDLQRAWQSKVENTYHLEYGYSCMGYEVNAALGAKLAQPEKEVYALLGDGSYMMLHSELVTSVQEHKKINVILFDNMTNGCINNLQIGNGMDSFATEFRFRNPQTNKLDGGFVPVDFAMNAASYGCKTYKVTTEEELRAALADAKKQTVSTLIDIKVLPKTMIHGYGSWWHVGVAEVSEKEKIRKAHKSSVKHINEARRY","1968017","","probable malonic semialdehyde oxidative decarboxylase","Cytoplasm","","
InterPro
IPR000399
Family
TPP-binding enzymes
PIRSF001370\"[8-620]TThiamine diphosphate-dependent enzyme, acetolactate synthase type
PS00187\"[480-499]TTPP_ENZYMES
InterPro
IPR011766
Domain
Thiamine pyrophosphate enzyme, C-terminal TPP-binding
PF02775\"[443-603]TTPP_enzyme_C
InterPro
IPR012000
Domain
Thiamine pyrophosphate enzyme, central region
PF00205\"[219-353]TTPP_enzyme_M
InterPro
IPR012001
Domain
Thiamine pyrophosphate enzyme, N-terminal TPP binding region
PF02776\"[6-199]TTPP_enzyme_N
InterPro
IPR012276
Family
Myo-inositol catabolism decarboxylase IolD
PIRSF500070\"[2-648]TMyo-inositol catabolism protein IolD
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1220\"[211-379]Tno description
G3DSA:3.40.50.970\"[4-210]T\"[406-619]Tno description
PTHR18968\"[259-392]T\"[418-546]T\"[562-641]TTHIAMINE PYROPHOSPHATE ENZYMES
PTHR18968:SF9\"[259-392]T\"[418-546]T\"[562-641]TMALONIC SEMIALDEHYDE OXIDATIVE DECARBOXYLASE


","BeTs to 20 clades of COG0028COG name: Thiamine pyrophosphate-requiring enzymes acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylaseFunctional Class: E,HThe phylogenetic pattern of COG0028 is a-mpkzyqvdrlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-28) to 4/5 blocks of the IPB000399 family, which is described as \"Thiamine pyrophosphate dependent enzyme\". Interpro entry for IP:IPR000399. IPB000399B 64-77 0.48 IPB000399C 90-113 3.5e-06 IPB000399D 282-311 1.9e-06 IPB000399E 470-509 5e-10","Residues 1 to 78 match (4e-32) PD:PD012304 which is described as ACTIVATOR LKTC/LTXC GENES LEUKOTOXIN GLYA PROMOTER BROGAN HAS ORF THIS ","","","","","","","","","","","","Wed Jan 22 10:57:56 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02800 is paralogously related to AA01428 (1e-09).","","","","","","Residues 218 to 363 (E-value = 3.6e-30) place AA02800 in the TPP_enzyme_M family which is described as Thiamine pyrophosphate enzyme, central domain (PF00205)","","","","","Yoshida K, Sano H, Miwa Y, Ogasawara N, Fujita Y.Cloning and nucleotide sequencing of a 15 kb region of the Bacillus subtilis genome containing the iol operon.Microbiology. 1994 Sep;140 ( Pt 9):2289-98.PMID: 7952181","","Wed Jan 22 10:57:56 2003","1","","","" "AA02801","1968240","1969133","894","ATGAAAGCTGAAAACGTGAAATTAGGTATCGCGCCAATCGGTTGGACTAACGATGATATGCCTGATCTTGGCAAAGAGAATACCTTTGAACAATGTGTCAGTGAAATGGCACTTGCGGGTTTTACCGGATGTGAAGTTGGAAATAAATATCCGCGCGACGTGGACGTGTTAAAACATAAGCTGGCGGTTCGCGGTATTCAAATTTGTAATGCGTGGTTCAGTACGTTTTTTGTCGACGGTAAAAAAGAAGAAACCATCAAAGAATTTATCAAACACCGCGATTTTCTCCATGCCATGGGCGCCAAAGTGATCGGCTGTTCCGAACAAAGCCGTAGTATTCAAGGCACCACCAAAGCCGTGTTCAAAGAGAAAACCGTATTCACCGAAGAAGAATGGCAACGCCTCGCCGAAGGTTACAACGAACTTGCCAAACTTGCCGCCGAAAAAGGCATGAAAGTTTGCCTGCACCACCACATGGGCACCGGCATTCAAACCCCGGCAGAAATTGATAAATATATGGCGGTGGTCAATGACGATGTGTATTTGTTATTCGATTCAGGTCACCTCTACTATTCCGAAGGCTCACAAAAAGCCATGCTGGATGTCTTGGAAAAATACATCGATCGCATTTGCCATGTGCATTTGAAAGACGTGCGCGATGAAGTGGTCGCCGACGTAAAAGCCAATAATCTGAGCTTCCTGGAAGGCGTGCGTAAAGGCACCTTTACCGTGCCGGGCGATGGCGTGATTGATTTCAGACCGATTTTCGACATTCTCGAAAAACACAATTACAAAGGCTGGATGGTTGTTGAAGCGGAACAGGATCCGGCAATCGCCAACCCATTTGAATATGCCGTCAAAGGCCGTAAATACATTAAAGAAACAGCGGGGATT","","","33594","MKAENVKLGIAPIGWTNDDMPDLGKENTFEQCVSEMALAGFTGCEVGNKYPRDVDVLKHKLAVRGIQICNAWFSTFFVDGKKEETIKEFIKHRDFLHAMGAKVIGCSEQSRSIQGTTKAVFKEKTVFTEEEWQRLAEGYNELAKLAAEKGMKVCLHHHMGTGIQTPAEIDKYMAVVNDDVYLLFDSGHLYYSEGSQKAMLDVLEKYIDRICHVHLKDVRDEVVADVKANNLSFLEGVRKGTFTVPGDGVIDFRPIFDILEKHNYKGWMVVEAEQDPAIANPFEYAVKGRKYIKETAGI","1968968","","myo-inositol catabolism protein","Cytoplasm","","
InterPro
IPR012307
Domain
Xylose isomerase-like TIM barrel
PF01261\"[33-250]TAP_endonuc_2
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.150\"[23-287]Tno description
PTHR12110\"[127-297]THYDROXYPYRUVATE ISOMERASE


","BeTs to 3 clades of COG1082COG name: Sugar phosphate isomerases/epimerasesFunctional Class: GThe phylogenetic pattern of COG1082 is a-m-k---v-r-bcef-----j----Number of proteins in this genome belonging to this COG is","","Residues 136 to 281 match (6e-09) PD:PD464560 which is described as PROTEOME MLR7228 COMPLETE ","","","","","","","","","","","","Wed Jan 22 10:53:46 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02801 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 6 to 111 (E-value = 3.6e-57) place AA02801 in the Myo-inos_cat_N family which is described as Myo-inositol catabolism protein N-terminus (PF06960)","","","","","Yoshida K, Sano H, Miwa Y, Ogasawara N, Fujita Y.Cloning and nucleotide sequencing of a 15 kb region of the Bacillus subtilis genome containing the iol operon.Microbiology. 1994 Sep;140 ( Pt 9):2289-98.PMID: 7952181Rossbach S, Kulpa DA, Rossbach U, de Bruijn FJ.Molecular and genetic characterization of the rhizopine catabolism (mocABRC) genes of Rhizobium meliloti L5-30.Mol Gen Genet. 1994 Oct;245(1):11-24.PMID: 7845353","","Wed Jan 29 15:59:37 2003","1","","","" "AA02802","1969139","1970146","1008","ATGATTAAAGTAGGTATTATCGGCGCCGGTCGTATCGGTCGCGTGCATTCCGAAAGCATTACAAAATATGTCAAAGGCGCTGAAATCAAAGCGATTTCCGATGTTCGCGTCACCGATGAGCTCACACAATGGGCGAAAGGCATGGGCATTCCACACGTTTATGAAGACTACAAACACATTCTGCAGGATCCTGAAATTGATGCTGTGTTGGTTTGTTCTTCCACCAACACCCACGCACCGATTTCCATTGAAGCCGCTCGTGCCGGCAAACACATTTTCTGTGAAAAACCGGTGGATGCCGATGTGAATCGCATTAAAGAAGTCTTAGTCGAAGTGGAAAAAGCGGGCGTGAAATTCCAGGTAGGATTCAACCGTCGTTTTGACCACAACTTTAAAGCCATCAAGACCCGCGTGGAAAACGGCGACATCGGTGAACCGCACTTAATCCGCGTTACCTCACGCGACCCTGACGCACCGCCGATTGAATACGTTAAAGTATCCAGCGGGATGTTCTTTGACATGACCATTCACGATTTCGACATGATCCGTTATTTATCCGGCAGCGAAGTGGTAGAAGTGTACGCGGCGGGCGGCGTGCTGGTGAATCCTGAAATCGGCAAAGCCGGCGATATTGACACCGCCGTCATCACCTTAAAACTGGCGAATGGCGCAATCGGTGTGATCGACAACAGCCGCAAAGCGGTTTACGGCTACGACCAACGGGCGGAAGTGTTCGGCTCGAAAGGCGCGGTACAAACCCGCAATGATACCGATTCCACCGCCGTGTATTCCTGTGAAGCGGGCGTGATTGCCGAAAAACCGAAATATTTCTTCCTAGAACGCTATATGCAATCTTTCGCCGATGAAATGGCGTGCTTTGTGGATTCCGTAGTAAACGACAAACCGACTTTAGTCAACGGCAACGACGGCTTGCAACCTGTGCTGATCGCGTTGGCGGCAAAACGTTCTCTTGATGAAGGACGCCCGGTGAAACTGGCGGAAATCGCC","","","36751","MIKVGIIGAGRIGRVHSESITKYVKGAEIKAISDVRVTDELTQWAKGMGIPHVYEDYKHILQDPEIDAVLVCSSTNTHAPISIEAARAGKHIFCEKPVDADVNRIKEVLVEVEKAGVKFQVGFNRRFDHNFKAIKTRVENGDIGEPHLIRVTSRDPDAPPIEYVKVSSGMFFDMTIHDFDMIRYLSGSEVVEVYAAGGVLVNPEIGKAGDIDTAVITLKLANGAIGVIDNSRKAVYGYDQRAEVFGSKGAVQTRNDTDSTAVYSCEAGVIAEKPKYFFLERYMQSFADEMACFVDSVVNDKPTLVNGNDGLQPVLIALAAKRSLDEGRPVKLAEIA","1969981","","probable myo-inositol 2-dehydrogenase","Cytoplasm","","
InterPro
IPR000683
Domain
Oxidoreductase, N-terminal
PF01408\"[2-123]TGFO_IDH_MocA
InterPro
IPR004104
Domain
Oxidoreductase, C-terminal
PF02894\"[135-243]TGFO_IDH_MocA_C
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[1-158]Tno description
PTHR22604\"[54-331]TOXIDOREDUCTASES
PTHR22604:SF14\"[54-331]TOXIDOREDUCTASE


","BeTs to 13 clades of COG0673COG name: Predicted dehydrogenases and related proteinsFunctional Class: RThe phylogenetic pattern of COG0673 is --mpk-yqvd-lbcefgh--uj----Number of proteins in this genome belonging to this COG is","Significant hit ( 7.4e-06) to 1/1 blocks of the IPB000683 family, which is described as \"Oxidoreductase family\". Interpro entry for IP:IPR000683. IPB000683 88-97 7.8e-06","Residues 25 to 108 match (8e-08) PD:PD336361 which is described as COMPLETE PROTEOME OXIDOREDUCTASE DEHYDROGENASE PLASMID 1.-.-.- GLUCOSE-FRUCTOSE MYO-INOSITOL OXIDOREDUCTASE GFO/IDH/MOCA ","","","","","","","","","","","","Wed Jan 29 13:51:32 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02802 is paralogously related to AA02789 (8e-21).","","","","","","Residues 135 to 243 (E-value = 8.6e-12) place AA02802 in the GFO_IDH_MocA_C family which is described as Oxidoreductase family, C-terminal alpha/beta domain (PF02894)","","","","","Finan TM, Weidner S, Wong K, Buhrmester J, Chain P, Vorhölter FJ, Hernandez-Lucas I, Becker A, Cowie A, Gouzy J, Golding B, Pühler A.The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing endosymbiont Sinorhizobium meliloti.Proc Natl Acad Sci U S A. 2001 Aug;98(17):9889-94.PMID: 11481431Bussey LB, Switzer RL.The degA gene product accelerates degradation of Bacillus subtilis phosphoribosylpyrophosphate amidotransferase in Escherichia coli.J Bacteriol. 1993 Oct;175(19):6348-53.PMID: 8407808","","Wed Jan 29 13:51:32 2003","1","","","" "AA02803","1971852","1970422","1431","ATGAAAACTTGGCTTTTGGCATTGTATGATGTGCTTTCCCGTTATAAAAACGTGTGGAATGAAACTTGGAAAATTCGTAAACAGCTTGATTCTCCGGTTAGAGAAAAAGATGAAAATGAATTTCTGCCCGCGCATTTGGAATTAATTGAAACACCTGTATCAAATGCACCACGATTCGTGTCTTATTCCATTATGCTCTTTTTAACTTTAGCGATTATTGTTTCTATCTTTAGCAATGTGGAAATTATCGCAACGGCTTCAGGAAAATTTGCACTAAGCGGGAGAAGCAAAGAAATTAAACCGATTGAAAATTCATTGGTTAAACATATTTTTGTGAAAGAGGGCGAATACGTGAAAAAGGGTGAACTATTGTTAAAACTGACCGCACTTGGTGCCGAAGCGGATACGTTAAAAACGAAGACATCGCTTTCTCAAGCTAAACTGGAGGAATTTCGTTATAAATCTTTATTGGAAGCTGTTGAAAAAGATCAATTACCAATATTAGATTTTTCTAAAATTGATTTACCTTTTATGACGGAAAACGATCAAAAAAGAGTGACTTTACTGATTGAAGAACAATTCTCTACTTGGCAAAAACAACGCCATCAGAAAACCTTGAATCTTAATAAAAAAGAAGCGGAAAAACTCAGTTATTTGGCACGAATAAAAAAATATGAAGGTCTGATTAATACAGAGCAAGTCCGATTGGATGATTTTAGAGCCTTATATAAGGAACATGCTATTGCAAAACATACAGTTTTAGATGAAGAGAATAAATATCAGGATGCAATCAATGAGCTTGAGGTATATAAGGCGAGTTTAATGCAAGTTGAAAACGAAGTTTTATTGGCCAAAGAAGAGCAGGAATTAGTCACACAATTGTTCAAAAATGATATTTTAGACAAGCTAAAACAGGCGACGGATAATGTGAATTTATTGACATTCGAACTGGACAAAAACAATCAACGCCAGCAAGTCTCTGAAATTCGAGCTCCTGTATCAGGTACTGTACAACAATTAAAAGTTCACACAATAGATGGCGTTGTTACTACGGCTGAAACATTAATGGTAGTTGTGCCGGAAGAAGATTCCCTTGAAGTCACTGCACTTATTCAAAATAAAGATATTGGTTTTGTGAAAGAAGGGCAAGAGGTTGTAATTAAGGTCGAAGCCTTCCCCTATACCCGTTATGGTTATTTAACGGGAAAAGTGAAAAATATTACTTTAGATGCGATTGAACATCCAAAGCTTGGACTTGTATTTAATACGATTATTGAATTGGATAAAAAAACACTTTCTACCGAAGAAAAAGAAATCCCACTTTCCGCAGGGATGGAAATTACTGCAGAAATTAAGACAGGCATGAGAAGCGTTATAAGCTATCTACTTAGCCCATTAGAAGAATCTATTGATAAAAGTTTAAGAGAACGT","","","54640","MKTWLLALYDVLSRYKNVWNETWKIRKQLDSPVREKDENEFLPAHLELIETPVSNAPRFVSYSIMLFLTLAIIVSIFSNVEIIATASGKFALSGRSKEIKPIENSLVKHIFVKEGEYVKKGELLLKLTALGAEADTLKTKTSLSQAKLEEFRYKSLLEAVEKDQLPILDFSKIDLPFMTENDQKRVTLLIEEQFSTWQKQRHQKTLNLNKKEAEKLSYLARIKKYEGLINTEQVRLDDFRALYKEHAIAKHTVLDEENKYQDAINELEVYKASLMQVENEVLLAKEEQELVTQLFKNDILDKLKQATDNVNLLTFELDKNNQRQQVSEIRAPVSGTVQQLKVHTIDGVVTTAETLMVVVPEEDSLEVTALIQNKDIGFVKEGQEVVIKVEAFPYTRYGYLTGKVKNITLDAIEHPKLGLVFNTIIELDKKTLSTEEKEIPLSAGMEITAEIKTGMRSVISYLLSPLEESIDKSLRER","1970257","[FUNCTION] Involved in the transport of the hemolysin/leukotoxin. ","leukotoxin secretion protein D; hemolysin export system membrane fusion protein","Cytoplasm, Inner membrane","","
InterPro
IPR003997
Family
Gram-negative bacterial RTX secretion protein D
PR01490\"[65-88]T\"[107-127]T\"[341-362]T\"[374-398]T\"[398-421]T\"[441-456]T\"[456-476]TRTXTOXIND
InterPro
IPR006143
Family
Secretion protein HlyD
PF00529\"[95-407]THlyD
InterPro
IPR006144
Domain
HlyD secretion protein, C-terminal
PS00543\"[441-463]THLYD_FAMILY
InterPro
IPR010129
Family
Type I secretion membrane fusion protein, HlyD
TIGR01843\"[54-477]Ttype_I_hlyD
noIPR
unintegrated
unintegrated
SSF111369\"[87-158]TSSF111369


","BeTs to 9 clades of COG0845COG name: Membrane-fusion proteinFunctional Class: QThe phylogenetic pattern of COG0845 is -------qvd-lbcefghsnujx-t-Number of proteins in this genome belonging to this COG is","Significant hit ( 2.4e-80) to 7/7 blocks of the PR01490 family, which is described as \"Gram-negative bacterial RTX secretion protein D signature\". Prints database entry for PR:PR01490. PR01490A 65-88 2.5e-06 PR01490B 107-127 2.2e-10 PR01490C 341-362 2e-11 PR01490D 374-398 1.4e-14 PR01490E 398-421 2.3e-11 PR01490F 441-456 1.7e-06 PR01490G 456-476 8e-11Significant hit ( 1.2e-45) to 3/3 blocks of the IPB002215 family, which is described as \"HlyD family secretion protein\". Interpro entry for IP:IPR002215. IPB002215A 93-129 3e-16 IPB002215B 329-363 3.1e-16 IPB002215C 444-466 2.4e-10","Residues 287 to 411 match (4e-09) PD:PD540961 which is described as PROBABLE PROTEOME COMPLETE SECRETION ","","","","","","","","","","","Wed Jan 22 10:45:59 2003","Wed Jan 22 10:45:59 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02803 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 95 to 407 (E-value = 8.8e-84) place AA02803 in the HlyD family which is described as HlyD family secretion protein (PF00529)","","","","Lally ET, Golub EE, Kieba IR, Taichman NS, Decker S, Berthold P, Gibson CW, Demuth DR, Rosenbloom J.Structure and function of the B and D genes of the Actinobacillus actinomycetemcomitans leukotoxin complex.Microb Pathog. 1991 Aug;11(2):111-21.PMID: 1961107Guthmiller JM, Kraig E, Cagle MP, Kolodrubetz D.Sequence of the lktD gene from Actinobacillus actinomycetemcomitans.Nucleic Acids Res. 1990 Sep;18(17):5292.PMID: 2402458","Lally ET, Golub EE, Kieba IR, Taichman NS, Decker S, Berthold P, Gibson CW, Demuth DR, Rosenbloom J.Structure and function of the B and D genes of the Actinobacillus actinomycetemcomitans leukotoxin complex.Microb Pathog. 1991 Aug;11(2):111-21.PMID: 1961107Guthmiller JM, Kraig E, Cagle MP, Kolodrubetz D.Sequence of the lktD gene from Actinobacillus actinomycetemcomitans.Nucleic Acids Res. 1990 Sep;18(17):5292.PMID: 2402458Felmlee T, Pellett S, Welch RA.Nucleotide sequence of an Escherichia coli chromosomal hemolysin.J Bacteriol. 1985 Jul;163(1):94-105.PMID: 3891743Schülein R, Gentschev I, Mollenkopf HJ, Goebel W.A topological model for the haemolysin translocator protein HlyD.Mol Gen Genet. 1992 Jul;234(1):155-63.PMID: 1495479Dobrindt U, Blum-Oehler G, Nagy G, Schneider G, Johann A, Gottschalk G, Hacker J.Genetic structure and distribution of four pathogenicity islands (PAI I(536) to PAI IV(536)) of uropathogenic Escherichia coli strain 536.Infect Immun. 2002 Nov;70(11):6365-72.PMID: 12379716","Mon Jan 27 15:43:22 2003","Mon Jan 27 15:43:22 2003","1","","5","" "AA02805","1973990","1971870","2121","ATGGACTCACAGAAAAATACTAATCTTGCCCTTCAGGCATTGGAAGTACTGGCTCAATATCATAATATTTCAATTAACCCGGAAGAAATAAAACATAAATTTGATATAGATGGGCATGGGCTGAACCAAACTAAATGGTTGCTTGCAGCAAAATCACTTGGATTAAAGGTAAGAACTGCGAACAAAACAGTTGACAGATTGCCTTTTTTACATTTACCGGCATTGGCTTGGCGTGATGATGGTGAACACTTTATTTTATTAAAAATAGATCAAGAAACCGATCGTTACCTCATTTTTGATCTAATTCAAAAAAATCCTATTGTTTTAGACAAAAATGAATTTGAAGAACGTTATCAAAGCAAGGTGATTTTAATTGCATCACGCGCATCTATTGTAGGAAATTTAGCAAAATTCGACTTTACCTGGTTTATTCCTGCCGTAATTAAATACCGCAAAATTTTTATAGAAACGTTAATCGTTTCTATATTTTTGCAAATTTTTGCACTGATTACACCACTCTTTTTTCAAGTCGTGATGGATAAAGTCCTGGTTCACCGTGGATTTTCAACATTGAATGTAATTACAGTGGCTCTTGCTATTGTAGTCTTATTTGAAATAATCTTGGGAGGCTTGAGAACCTATGTTTTTGCTCATAGTACAAGTCGTATTGATGTCGAATTGGGAGCAAGGCTTTTTCGTCATTTATTAGCTTTACCGATTTCTTATTTTGAAGCTCGTCGGGTCGGGGATACGGTGGCTCGTGTTCGTGAGTTAGATCAAATTCGGAATTTCTTAACAGGGCAGGCACTTACCTCTATTTTAGACTTGTTATTCTCTTTTATTTTCTTCGCTGTAATGTGGTATTACAGCCCAAAATTAACATTAGTTGTACTCGGTTCTTTACCTTGTTATGTCATTTGGTCTGTTTTTATTAGTCCTATTCTTAGGAGACGGCTTGATGATAAGTTCGCAAGAAATGCCGACAATCAGTCTTTTCTTGTTGAATCAGTGACTGCCATTAATACAATTAAAGCGATGGCTATTTCTCCTCAAATGACTAACATTTGGGATAAACAGTTAGCGAGTTATGTTGCTGTGAGTTTTAAAGTGACTGTACTTGCAACGATCGGACAGCAAGGTATCCAATTGATCCAGAAAGCCGTTATGGTGATCAACCTATGGCTTGGCGCACATTTAGTTATTTCCGGTGATTTAAGTATTGGTCAGCTAATTGCATTTAATATGCTTGCGGGACAAATTATTAGCCCTGTGATTCGTTTAGCCCAGATCTGGCAAGATTTCCAACAGGTCGGTATTTCTGTTACTCGTTTGGGTGATGTGCTTAATTCGCCTACAGAGAATAATACCGCCTCAGTATCATTACCGGAAATCCAGGGTGAGATTAGTTTTAGAAATATTAAGTTCCGCTATAAACCGGATTCCCCTATGATTTTAAACAATATTAACTTAGATATCAGTCAGGGAGAAGTGATTGGTATTGTTGGTCGTTCAGGTTCGGGGAAAAGTACGCTTACTAAACTCATCCAACGTTTTTATATTCCGGAGCAGGGGCAAGTCTTAATTGACGGTCACGATTTGGCGCTAGCCGATCCAAACTGGTTGCGCCGGCAAGTCGGTGTCGTCTTGCAAGATAATGTGTTGCTTAATCGAAGTATCAGAGAGAATATTGCGTTAACCAATCCGGGAATGCCAATGGAAAAGGTTATTGCCGCGGCAAAACTTGCGGGAGCGCACGATTTTATTTCTGAATTAAGAGAAGGTTATAACACGGTTGTGGGGGAACAGGGAGCCGGTTTGTCCGGAGGACAACGTCAACGGATCGCGATAGCAAGGGCACTAGTCAATAACCCAAGGATTTTGATTTTTGATGAAGCAACCAGTGCACTTGATTACGAATCTGAAAATATCATTATGCATAATATGCATAAAATTTGCCAAAATCGTACTGTGCTTATCATTGCTCACCGCCTTTCTACTGTAAAAAATGCTGATCGCATTATTGTGATGGACAAAGGTGAAATCATCGAACAAGGCAAGCATCAGGAATTACTGAAAGATGAAAAAGGTCTTTACTCTTATTTACACCAATTACAAGTAAAT","","","82303","MDSQKNTNLALQALEVLAQYHNISINPEEIKHKFDIDGHGLNQTKWLLAAKSLGLKVRTANKTVDRLPFLHLPALAWRDDGEHFILLKIDQETDRYLIFDLIQKNPIVLDKNEFEERYQSKVILIASRASIVGNLAKFDFTWFIPAVIKYRKIFIETLIVSIFLQIFALITPLFFQVVMDKVLVHRGFSTLNVITVALAIVVLFEIILGGLRTYVFAHSTSRIDVELGARLFRHLLALPISYFEARRVGDTVARVRELDQIRNFLTGQALTSILDLLFSFIFFAVMWYYSPKLTLVVLGSLPCYVIWSVFISPILRRRLDDKFARNADNQSFLVESVTAINTIKAMAISPQMTNIWDKQLASYVAVSFKVTVLATIGQQGIQLIQKAVMVINLWLGAHLVISGDLSIGQLIAFNMLAGQIISPVIRLAQIWQDFQQVGISVTRLGDVLNSPTENNTASVSLPEIQGEISFRNIKFRYKPDSPMILNNINLDISQGEVIGIVGRSGSGKSTLTKLIQRFYIPEQGQVLIDGHDLALADPNWLRRQVGVVLQDNVLLNRSIRENIALTNPGMPMEKVIAAAKLAGAHDFISELREGYNTVVGEQGAGLSGGQRQRIAIARALVNNPRILIFDEATSALDYESENIIMHNMHKICQNRTVLIIAHRLSTVKNADRIIVMDKGEIIEQGKHQELLKDEKGLYSYLHQLQVN","1971705","[FUNCTION] Involved in the export of leukotoxin (hemolysin). ","leukotoxin expression protein B; hemolysin secretion protein","Inner membrane, Cytoplasm","","
InterPro
IPR001140
Domain
ABC transporter, transmembrane region
PF00664\"[150-424]TABC_membrane
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[606-648]TABC_transporter
PF00005\"[495-679]TABC_tran
PS00211\"[606-620]TABC_TRANSPORTER_1
PS50893\"[468-703]TABC_TRANSPORTER_2
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[494-680]TAAA
InterPro
IPR005074
Domain
Peptidase C39, bacteriocin processing
PF03412\"[4-130]TPeptidase_C39
PS50990\"[4-125]TPEPTIDASE_C39
InterPro
IPR010132
Domain
Type I secretion system ATPase, HlyB
TIGR01846\"[10-707]Ttype_I_sec_HlyB
InterPro
IPR011527
Domain
ABC transporter, transmembrane region, type 1
PS50929\"[158-436]TABC_TM1F
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[449-705]TG3DSA:3.40.50.300
PIRSF002787\"[1-707]THemolysin_sec_B
PTHR19242\"[113-705]TPTHR19242
PTHR19242:SF87\"[113-705]TPTHR19242:SF87
SSF52540\"[468-707]TSSF52540
SSF90123\"[110-482]TSSF90123


","BeTs to 7 clades of COG2274COG name: ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domainFunctional Class: QThe phylogenetic pattern of COG2274 is -----------lbcefg-sn-j---wNumber of proteins in this genome belonging to this COG is","Significant hit ( 3e-80) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 484-530 6.2e-29 IPB001140B 603-641 3e-27 IPB001140C 656-685 1e-21Significant hit ( 2.2e-05) to 1/5 blocks of the IPB001324 family, which is described as \"Phosphoribulokinase family\". Interpro entry for IP:IPR001324. IPB001324A 494-515 2.2e-05","","","","","","","","","","","","Wed Jan 22 10:38:56 2003","Wed Jan 22 10:38:56 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02805 is paralogously related to AA01961 (6e-71), AA01393 (5e-62), AA01509 (2e-47), AA01510 (1e-44), AA02331 (3e-40), AA02609 (6e-37), AA02606 (2e-32), AA00415 (1e-30), AA02718 (4e-24), AA01616 (4e-23), AA01645 (2e-22), AA00858 (5e-22), AA02440 (5e-21), AA02899 (1e-20), AA01867 (1e-20), AA00700 (1e-20), AA01524 (2e-20), AA01422 (2e-20), AA02080 (4e-20), AA02353 (7e-20), AA01568 (4e-19), AA01684 (1e-18), AA01656 (5e-18), AA01051 (8e-18), AA01824 (5e-17), AA02324 (7e-17), AA02320 (9e-17), AA00799 (1e-16), AA00933 (8e-16), AA02140 (2e-15), AA00591 (3e-15), AA02786 (2e-14), AA01779 (2e-14), AA02898 (7e-14), AA01820 (7e-14), AA02152 (2e-13), AA00207 (3e-13), AA01456 (6e-13), AA02550 (2e-11), AA02642 (3e-11), AA02573 (6e-11), AA01569 (7e-11), AA02484 (1e-10), AA02225 (4e-10), AA01947 (4e-10), AA00751 (4e-09), AA01555 (1e-07), AA01757 (4e-07), AA00061 (5e-07), A02145 (1e-06), AA01291 (1e-06), AA00934 (4e-06) and AA02146 (2e-05).","","","","","","Residues 495 to 679 (E-value = 1.1e-68) place AA02805 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","Guthmiller JM, Kolodrubetz D, Cagle MP, Kraig E.Sequence of the lktB gene from Actinobacillus actinomycetemcomitans.Nucleic Acids Res. 1990 Sep;18(17):5291.PMID: 2402457Lally ET, Golub EE, Kieba IR, Taichman NS, Decker S, Berthold P, Gibson CW, Demuth DR, Rosenbloom J.Structure and function of the B and D genes of the Actinobacillus actinomycetemcomitans leukotoxin complex.Microb Pathog. 1991 Aug;11(2):111-21.PMID: 1961107","Guthmiller JM, Kolodrubetz D, Cagle MP, Kraig E.Sequence of the lktB gene from Actinobacillus actinomycetemcomitans.Nucleic Acids Res. 1990 Sep;18(17):5291.PMID: 2402457Lally ET, Golub EE, Kieba IR, Taichman NS, Decker S, Berthold P, Gibson CW, Demuth DR, Rosenbloom J.Structure and function of the B and D genes of the Actinobacillus actinomycetemcomitans leukotoxin complex.Microb Pathog. 1991 Aug;11(2):111-21.PMID: 1961107Koronakis V, Koronakis E, Hughes C.Comparison of the haemolysin secretion protein HlyB from Proteus vulgaris and Escherichia coli; site-directed mutagenesis causing impairment of export function.Mol Gen Genet. 1988 Aug;213(2-3):551-5.PMID: 3054490Felmlee T, Pellett S, Welch RA.Nucleotide sequence of an Escherichia coli chromosomal hemolysin.J Bacteriol. 1985 Jul;163(1):94-105.PMID: 3891743","Wed Jan 22 10:38:56 2003","Wed Jan 22 10:38:56 2003","1","","5","" "AA02806","1977226","1974062","3165","ATGGCAACTACTACACTGCCAAATACAAAACAGCAAGCTGCACAGTTTGCAAATTCAGTTGCAGATAGAGCTAAGGAAAATATTGATGCTGCAAAAGAACAATTGCAAAAGGCGTTAGATAAATTAGGGAAGACAGGTAAGAAATTAACTTTATATATCCCTAAGAATTACAAAAAAGGAAATGGTCTTACTGCGCTTATAAAAGCAGCACAGAAGTTAGGGATTGAAGTATATCATGAAGGGAAAGACGGCCCGGCATTAACTAATGGTATTTTAAATACTGGGAAAAAATTACTTGGTCTTACCGAACGAGGTTTAACTTTATTTGCTCCGGAATTAGATAAATGGATTCAAGGTAATAAACATTTAAGTAATTCTGTGGGTAGTACTGGAAATTTGACAAAAGCGATAGATAAGGTTCAGAGTGTTCTTGGTACGTTACAAGCGTTTTTGAACACCGCATTTTCGGGCATGGATTTAGATGCCTTAATTAAAGCCCGTCAAAATGGTAAAAATGTAACAGATGTACAGCTAGCAAAAGCCAGTCTTAACCTGATTAATGAATTGATTGGTACTATTTCTAGCATTACAAATAATGTAGATACTTTTTCTAAACAACTTAATAAGTTAGGTGAAGCACTAGGACAAGTAAAACATTTTGGTAGTTTTGGAGATAAATTAAAGAATTTACCTAAGTTAGGTAATCTTGGAAAAGGTTTAGGTGCATTATCCGGTGTATTGTCGGCTATATCAGCGGCTCTATTACTTGCAAATAAAGATGCTGATACTGCAACGAAAGCAGCGGCTGCAGCTGAATTGACAAATAAAGTGCTAGGTAACATCGGTAAAGCGATCACACAATACTTGATTGCTCAACGTGCTGCAGCGGGGCTTTCTACTACGGGACCTGTCGCAGGGTTAATTGCCTCTGTGGTCAGCTTGGCAATCAGCCCTTTGTCTTTCCTAGGTATTGCGAAACAATTTGATCGTGCGAGAATGCTTGAGGAATACTCGAAACGCTTTAAGAAATTTGGTTATAACGGCGATAGTTTACTTGGTCAATTCTACAAAAATACAGGGATCGCAGATGCTGCGATTACAACGATTAACACTGTATTAAGTGCTATTGCAGCAGGGGTTGGTGCAGCCTCCGCCGGTTCTTTAGTTGGTGCGCCAATCGGTTTGTTAGTGAGTGCGATTACCAGCTTAATTTCAGGAATTCTTGATGCTTCTAAACAAGCCGTTTTTGAACATATCGCGAATCAGCTCGCCGATAAAATTAAAGCATGGGAGAATAAGTACGGTAAGAATTACTTTGAAAATGGCTATGATGCCCGTCATTCCGCCTTCTTGGAAGATTCACTAAAATTATTTAATGAGTTACGTGAAAAATATAAAACCGAAAATATATTATCTATCACTCAACAAGGTTGGGATCAGCGCATTGGTGAATTAGCAGGTATCACTCGTAATGGAGATCGTATTCAAAGTGGTAAAGCTTATGTGGATTATTTGAAAAAGGGTGAGGAGCTTGCAAAGCATAGCGATAAATTCACTAAACAGATTTTAGATCCAATCAAAGGTAATATTGATCTTTCGGGTATAAAAGGTTCTACCACTCTAACTTTTTTAAATCCGTTGTTAACCGCAGGTAAGGAAGAACGGAAAACACGTCAGTCAGGTAAATATGAATTTATTACTGAATTAAAAGTAAAAGGACGTACCGATTGGAAGGTAAAAGGTGTTCCTAATTCTAATGGTGTATATGATTTTTCTAACTTAATTCAACATGCCGTTACACGTGATAATAAAGTTCTAGAAGCAAGATTAATTGCTAATTTGGGTGCTAAAGATGATTATGTTTTTGTCGGATCCGGTTCAACAATAGTTAATGCTGGAGACGGTTATGATGTGGTGGACTATAGTAAAGGTCGCACCGGTGCATTAACAATCGACGGTCGTAATGCTACTAAAGCCGGACAATATAAGGTTGAAAGAGATCTTAGCGGTACTCAAGTCTTGCAGGAAACCGTATCAAAGCAAGAAACTAAACGAGGGAAGGTTACCGATCTACTTGAATATCGTAACTATAAATTAGATTACTATTATACGAATAAGGGCTTTAAAGCTCATGATGAATTAAACTCAGTAGAGGAAATTATCGGCAGCACACTACGTGATAAATTTTATGGTTCTAAATTTAATGATGTTTTCCATGGTCACGATGGCGATGATTTGATTTATGGTTATGATGGCGATGATCGTTTGTATGGCGATAATGGGAATGACGAAATTCATGGCGGCCAAGGTAATGATAAGCTCTATGGTGGTGCCGGTAACGATAGGCTCTTTGGTGAATATGGCAACAACTATCTTGACGGTGGAGAAGGCGACGACCACTTAGAGGGAGGCAATGGTTCCGATATTCTAAGAGGTGGAAGTGGCAATGATAAGTTGTTTGGAAACCAAGGAGATGATTTACTTGACGGTGGAGAAGGCGATGACCAACTTGCCGGTGGAGAAGGAAATGATATTTATGTTTACCGTAAAGAATATGGGCACCACACTATTACGGAACATAGCGGTGATAAAGATAAATTATCATTAGCAAATATCAATCTCAAAGATGTGTCATTTGAGCGTAACGGCAATGATCTACTATTGAAAACAAATAATAGAACAGCAGTAACATTTAAAGGATGGTTTAGTAAACCTAATTCATCGGCAGGATTAGATGAGTATCAAAGAAAACTTCTTGAATACGCACCTGAAAAGGATCGTGCACGACTTAAGAGACAATTTGAGTTACAGCGAGGTAAAGTCGACAAATCACTCAATAATAAAGTTGAAGAAATTATCGGTAAAGATGGGGAGCGGATTACTTCGCAAGACATTGATAATCTTTTTGATAAGAGTGGGAACAAAAAGACAATTTCACCTCAAGAGCTTGCCGGACTTATTAAGAATAAAGGTAAGTCAAGTAGCCTTATGTCTTCTTCTCGTTCGTCAAGTATGCTTACACAAAAGTCCGGTTTGTCAAATGATATTAGTCGTATTATTTCAGCAACCAGTGGTTTTGGTTCATCCGGTAAAGCGTTATCCGCTTCGCCATTGCAGACCAATAATAACTTTAACTCTTACGCAAATTCGTTAGCAACTACTGCT","","","113851","MATTTLPNTKQQAAQFANSVADRAKENIDAAKEQLQKALDKLGKTGKKLTLYIPKNYKKGNGLTALIKAAQKLGIEVYHEGKDGPALTNGILNTGKKLLGLTERGLTLFAPELDKWIQGNKHLSNSVGSTGNLTKAIDKVQSVLGTLQAFLNTAFSGMDLDALIKARQNGKNVTDVQLAKASLNLINELIGTISSITNNVDTFSKQLNKLGEALGQVKHFGSFGDKLKNLPKLGNLGKGLGALSGVLSAISAALLLANKDADTATKAAAAAELTNKVLGNIGKAITQYLIAQRAAAGLSTTGPVAGLIASVVSLAISPLSFLGIAKQFDRARMLEEYSKRFKKFGYNGDSLLGQFYKNTGIADAAITTINTVLSAIAAGVGAASAGSLVGAPIGLLVSAITSLISGILDASKQAVFEHIANQLADKIKAWENKYGKNYFENGYDARHSAFLEDSLKLFNELREKYKTENILSITQQGWDQRIGELAGITRNGDRIQSGKAYVDYLKKGEELAKHSDKFTKQILDPIKGNIDLSGIKGSTTLTFLNPLLTAGKEERKTRQSGKYEFITELKVKGRTDWKVKGVPNSNGVYDFSNLIQHAVTRDNKVLEARLIANLGAKDDYVFVGSGSTIVNAGDGYDVVDYSKGRTGALTIDGRNATKAGQYKVERDLSGTQVLQETVSKQETKRGKVTDLLEYRNYKLDYYYTNKGFKAHDELNSVEEIIGSTLRDKFYGSKFNDVFHGHDGDDLIYGYDGDDRLYGDNGNDEIHGGQGNDKLYGGAGNDRLFGEYGNNYLDGGEGDDHLEGGNGSDILRGGSGNDKLFGNQGDDLLDGGEGDDQLAGGEGNDIYVYRKEYGHHTITEHSGDKDKLSLANINLKDVSFERNGNDLLLKTNNRTAVTFKGWFSKPNSSAGLDEYQRKLLEYAPEKDRARLKRQFELQRGKVDKSLNNKVEEIIGKDGERITSQDIDNLFDKSGNKKTISPQELAGLIKNKGKSSSLMSSSRSSSMLTQKSGLSNDISRIISATSGFGSSGKALSASPLQTNNNFNSYANSLATTA","1973897","[FUNCTION] One of the virulence factors of A.actinomycetemcomitans might be a cytotoxin, possibly the membrane-bound hemolysin.[FUNCTION] Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture by mechanisms not clearly defined.","leukotoxin A; hemolysin A","Extracellular","","
InterPro
IPR001343
Domain
Hemolysin-type calcium-binding region
PR00313\"[764-775]T\"[776-784]T\"[812-820]T\"[839-848]TCABNDNGRPT
PF00353\"[739-756]T\"[757-774]T\"[775-792]T\"[793-810]T\"[811-828]T\"[829-846]THemolysinCabind
InterPro
IPR003995
Family
Bacterial RTX cytolytic toxin, protein A
PR01488\"[279-300]T\"[345-363]T\"[401-421]T\"[436-452]T\"[489-510]T\"[543-567]T\"[740-761]TRTXTOXINA
PF02382\"[5-654]TRTX
InterPro
IPR011049
Domain
Serralysin-like metalloprotease, C-terminal
SSF51120\"[594-788]T\"[789-903]TSerralysn_like_C
InterPro
IPR013550
Domain
RTX C-terminal
PF08339\"[868-1055]TRTX_C
noIPR
unintegrated
unintegrated
G3DSA:2.150.10.10\"[618-784]T\"[785-898]TG3DSA:2.150.10.10


","BeTs to 6 clades of COG2931COG name: RTX toxins and related Ca2+-binding proteinsFunctional Class: QThe phylogenetic pattern of COG2931 is -------q-----c-fg-sn-j----Number of proteins in this genome belonging to this COG is","Significant hit (9.3e-108) to 7/7 blocks of the PR01488 family, which is described as \"Gram-negative bacterial RTX toxin determinant A family signature\". Prints database entry for PR:PR01488. PR01488A 279-300 2.8e-14 PR01488B 345-363 4.2e-11 PR01488C 401-421 4.7e-14 PR01488D 436-452 2.8e-14 PR01488E 489-510 1.5e-13 PR01488F 543-567 5.9e-16 PR01488G 740-761 2.6e-16 PR01488G 758-779 1e-08 PR01488G 767-788 5.3e-08 PR01488G 794-815 9.9e-07 PR01488G 812-833 2.1e-06 PR01488G 821-842 3e-06 PR01488G 803-824 4.9e-06 PR01488G 749-770 1e-05 PR01488G 785-806 2.1e-05 PR01488G 776-797 0.0001 PR01488G 731-752 0.0011 PR01488G 830-851 0.12Significant hit ( 3.2e-26) to 2/2 blocks of the IPB001343 family, which is described as \"Hemolysin-type calcium-binding region\". Interpro entry for IP:IPR001343. IPB001343A 294-306 1.2 IPB001343B 758-799 4.1e-24","Residues 719 to 873 match (7e-08) PD:PD534637 which is described as TOXIN RTX ","","","","","","","","","","","Wed Jan 22 10:29:09 2003","Wed Jan 22 10:29:09 2003","","Tue Feb 8 14:20:19 2005","Tue Feb 8 14:20:19 2005","Tue Feb 8 14:20:19 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA02806 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Tue Feb 8 14:20:19 2005","","","","","","","",""," Balashova NV, Diaz R, Balashov SV, Crosby JA, Kachlany SC.,Regulation of Aggregatibacter (Actinobacillus) actinomycetemcomitans leukotoxin secretion by iron.J Bacteriol. 2006 Dec;188(24):8658-61. Epub 2006 Oct 13.PMID: 17041062 Crosby JA, Kachlany SC.TdeA, a TolC-like protein required for toxin and drug export in Aggregatibacter (Actinobacillus) actinomycetemcomitans.Gene. 2007 Feb 15;388(1-2):83-92. Epub 2006 Oct 17.PMID: 17116373Kelk P, Claesson R, Hänström L, Lerner UH, Kalfas S, Johansson A.Abundant secretion of bioactive interleukin-1beta by human macrophages induced by Actinobacillus actinomycetemcomitans leukotoxin.Infect Immun. 2005 Jan;73(1):453-8.PMID: 15618184Lally ET, Golub EE, Kieba IR, Taichman NS, Rosenbloom J, Rosenbloom JC, Gibson CW, Demuth DR.Analysis of the Actinobacillus actinomycetemcomitans leukotoxin gene. Delineation of unique features and comparison to homologous toxins.J Biol Chem. 1989 Sep;264(26):15451-6.PMID: 2670940","Lally ET, Golub EE, Kieba IR, Taichman NS, Rosenbloom J, Rosenbloom JC, Gibson CW, Demuth DR.Analysis of the Actinobacillus actinomycetemcomitans leukotoxin gene. Delineation of unique features and comparison to homologous toxins.J Biol Chem. 1989 Sep;264(26):15451-6.PMID: 2670940Felmlee T, Pellett S, Welch RA.Nucleotide sequence of an Escherichia coli chromosomal hemolysin.J Bacteriol. 1985 Jul;163(1):94-105.PMID: 3891743Nicaud JM, Mackman N, Gray L, Holland IB.Characterisation of HlyC and mechanism of activation and secretion of haemolysin from E. coli 2001.FEBS Lett. 1985 Aug;187(2):339-44.PMID: 3894051","Tue Feb 8 14:20:19 2005","Tue Feb 8 14:20:19 2005","1","","5","" "AA02807","1977745","1977242","504","ATGGAGAAAAATAATAATTTTGAAGTGTTAGGGTATGTGGCTTGGTTATGGGCAAATTCTCCTTTGCATAGAAATTGGTCTTTATCATTACTTGCTATTAATGTACTGCCTGCAATTCAATATGGGCAATATACATTATTAATGAGAGATGGGGTTCCTATTGCTTTTTGTAGCTGGGCAAATTTAAGCCTTGAGAATGAGATAAAATATCTTGAAGATGTATCATCTCTTGTTTATGACGACTGGAATTCCGGTGATCGTAAATGGTTTATTGATTGGATTGCGCCATTTGGTCACAATTATGTGCTTTATAAACATATGCGTAAATCATTTCCCTATGATTTATTCAGATCAATTCGTGTTTATAAAGGTTCGTCAGAGGGCAAAATTACTGAATTCCATGGAGGTAAAGTCGATAAACAATTAGCTAATAAAATCTTTCAACAATATCATTTTGAGTTAATCAATGAATTAAAAAACAAATCTGAAGTTATATCTATTAAT","","","24378","MEKNNNFEVLGYVAWLWANSPLHRNWSLSLLAINVLPAIQYGQYTLLMRDGVPIAFCSWANLSLENEIKYLEDVSSLVYDDWNSGDRKWFIDWIAPFGHNYVLYKHMRKSFPYDLFRSIRVYKGSSEGKITEFHGGKVDKQLANKIFQQYHFELINELKNKSEVISIN","1977077","[FUNCTION] Involved in fatty acylation of the protoxin (lktA) at two internal lysine residues, thereby converting it to the active toxin. The acyl donor is ACP (by similarity). Related to the A.pleuropneumoniae ApxII.","leukotoxin activator (leukotoxin C)","Cytoplasm","","
InterPro
IPR003996
Family
Bacterial RTX toxin-activating protein C
PR01489\"[11-27]T\"[53-71]T\"[75-97]T\"[129-150]TRTXTOXINC
PF02794\"[2-159]THlyC
noIPR
unintegrated
unintegrated
signalp\"[1-42]?signal-peptide


","BeTs to 3 clades of COG2994COG name: ACP:hemolysine acyltransferase (hemolysin-activating protein)Functional Class: OThe phylogenetic pattern of COG2994 is -------------c--g--n------Number of proteins in this genome belonging to this COG is","Significant hit ( 2.2e-72) to 4/4 blocks of the PR01489 family, which is described as \"Gram-negative bacterial RTX toxin-activating protein C signature\". Prints database entry for PR:PR01489. PR01489A 11-27 1.2e-14 PR01489B 53-71 1.1e-15 PR01489C 75-97 1.3e-21 PR01489D 129-150 2.2e-16","Residues 128 to 161 match (2e-12) PD:PD009491 which is described as C HEMOLYSIN HEMOLYSIS ACYLTRANSFERASE TRANSFERASE LYSINE-ACYLTRANSFERASE ACTIVATING 2.3.1.- TOXIN- PLASMID ","","","","","","","","","","","Thu Aug 4 11:44:52 2005","Tue Feb 11 17:03:45 2003","","Thu Aug 4 11:44:52 2005","Thu Aug 4 11:44:52 2005","Thu Aug 4 11:44:52 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA02807 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Aug 4 11:44:52 2005","","","","","Residues 2 to 159 (E-value = 2.4e-136) place AA02807 in the HlyC family which is described as RTX toxin acyltransferase family (PF02794)","Thu Aug 4 11:44:52 2005","","","Lally ET, Golub EE, Kieba IR, Taichman NS, Rosenbloom J, Rosenbloom JC, Gibson CW, Demuth DR.Analysis of the Actinobacillus actinomycetemcomitans leukotoxin gene. Delineation of unique features and comparison to homologous toxins.J Biol Chem. 1989 Sep;264(26):15451-6.PMID: 2670940Kraig E, Dailey T, Kolodrubetz D.Nucleotide sequence of the leukotoxin gene from Actinobacillus actinomycetemcomitans: homology to the alpha-hemolysin/leukotoxin gene family.Infect Immun. 1990 Apr;58(4):920-9.PMID: 2318535","Felmlee T, Pellett S, Welch RA.Nucleotide sequence of an Escherichia coli chromosomal hemolysin.J Bacteriol. 1985 Jul;163(1):94-105.PMID: 3891743Nicaud JM, Mackman N, Gray L, Holland IB.Characterisation of HlyC and mechanism of activation and secretion of haemolysin from E. coli 2001.FEBS Lett. 1985 Aug;187(2):339-44.PMID: 3894051Stanley P, Packman LC, Koronakis V, Hughes C.Fatty acylation of two internal lysine residues required for the toxic activity of Escherichia coli hemolysin.Science. 1994 Dec;266(5193):1992-6.PMID: 7801126Juarez A, Hughes C, Vogel M, Goebel W.Expression and regulation of the plasmid-encoded hemolysin determinant of Escherichia coli.Mol Gen Genet. 1984;197(2):196-203.PMID: 6394952Goebel W, Hacker J, Knapp S, Then I, Wagner W, Hughes C, Juarez A.Structure, function, and regulation of the plasmid-encoded hemolysin determinant of Escherichia coli.Basic Life Sci. 1985;30:791-805.PMID: 2990440Trent MS, Worsham LM, Ernst-Fonberg ML.HlyC, the internal protein acyltransferase that activates hemolysin toxin: role of conserved histidine, serine, and cysteine residues in enzymatic activity as probed by chemical modification and site-directed mutagenesis.Biochemistry. 1999 Mar;38(11):3433-9.PMID: 10079090Jansen R, Briaire J, Kamp EM, Gielkens AL, Smits MA.Structural analysis of the Actinobacillus pleuropneumoniae-RTX-toxin I (ApxI) operon.Infect Immun. 1993 Sep;61(9):3688-95.PMID: 8359891Kuhnert P, Schlatter Y, Frey J.Characterization of the type I secretion system of the RTX toxin ApxII in \"Actinobacillus porcitonsillarum\".Vet Microbiol. 2005 May;107(3-4):225-32.PMID: 15863281","Tue Mar 25 13:20:35 2003","Thu Aug 4 11:44:52 2005","1","","5","" "AA02808","1978004","1977771","234","ATGTCCAGTACAGAATATGCTCCATTTTATCTCCGTTTTATTCAGTTCCCAAGTAATGAAGTTTTACTCTATGAATACTGGAAACTTGTTCAGAATTTTGTACAAAAGGTTAGTAAAATAACGGTAAGATTAGCACAAATCGTTGGCATTCTCGGCGAAAAAACTATTTGGAAATACCAAAGTACTTTTAATGATGGCATGCTGGATATTGTGGTTTGGTTATCTTATTCAAAA","","","9247","MSSTEYAPFYLRFIQFPSNEVLLYEYWKLVQNFVQKVSKITVRLAQIVGILGEKTIWKYQSTFNDGMLDIVVWLSYSK","1977606","","conserved hypothetical protein (possible serine hydroxymethyltransferase)","Cytoplasm","","
InterPro
IPR009369
Family
Actinobacillus actinomycetemcomitans leukotoxin activator LktC
PF06261\"[1-77]TLktC


","No hits to the COGs database.","","","","","","","","","","","","","","Fri Jan 31 15:00:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02808 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 77 (E-value = 4.2e-22) place AA02808 in the LktC family which is described as Actinobacillus actinomycetemcomitans leukotoxin activator LktC (PF06261)","","","","","Brogan JM, Lally ET, Poulsen K, Kilian M, Demuth DR.Regulation of Actinobacillus actinomycetemcomitans leukotoxin expression: analysis of the promoter regions of leukotoxic and minimally leukotoxic strains.Infect Immun. 1994 Feb;62(2):501-8.PMID: 8300209","","Tue Mar 25 13:10:31 2003","1","","5","" "AA02810","1979584","1978325","1260","ATGTTTAAAAAAAGTATGAACATCGCCGATTACGATCCCGTGTTATGGCAAGCTATTCAAAATGAAAACCGCCGCCAGGAAGAACATATCGAATTAATCGCTTCTGAAAACTATGCCAGCCCGCGCGTAATGCAAGCGCAAGGTTCCCAATTCACCAACAAATATGCGGAAGGCTACCCGGGCAAGCGTTATTATGGCGGTTGTGAATACGCGGACATTGTGGAACAGCTCGCTATTGAGCGTGCGAAAGAATTATTCGGCGCCGATTATGTGAACGTGCAACCGCACTCCGGTTCGCAAGCCAATGCGGCAGTTTACATGGGGTTACTCAATCCGGGCGATACCATTTTAGGCATGAGCTTAGCGCACGGCGGTCACTTAACCCACGGCGCGTCCGTGAGTTTCTCCGGCAAGATTTATCACGCGGAACAATACGGCATTACCGACGAAGGGTTAATCGACTATGATGCGTTACGCAAACAAGCCCATGACGTGAAACCGAAAATGATCGTGGGCGGATTCTCCGCGTATTCTCAAGTAGTGGATTGGAAAAAAATGCGTGAAATCGCCGATGAAGTGGGCGCATATTTATTCGTGGATATGGCGCACGTTGCGGGTTTAATCGCTGCAGGTATTTACCCGAATCCATTGCCGTACGCCCATGTGGTGACCACTACTACCCACAAAACCTTAGGCGGTCCGCGTGGCGGTTTGATTCTTTCTTCTTGCGGTGATGAAGAAATCTATAAAAAACTCAACAGCGCCGTTTTCCCTGCAGGTCAGGGCGGTCCGTTGGTGCACATTATCGCGGCGAAAGCGGTGTGCTTCAAAGAAGCCTTGGAGCCGGAATACAAAGTGTATCAACAAAATGTGTTGAAAAACGCCAAAGCCATGGTGGAAGTGTTCAAACAACGCGGTTATAAAGTCGTTTCCAACGGCACTGAAAACCACTTGTTCTTAGTGGACTTAGTCAGCCATGGATTGACCGGTAAAGCCGCCGATGCCGCATTAGGCAAGGCCAACATTACCGTGAATAAAAACTCTGTGCCGAACGATCCGCAAAAACCGTTCATCACTTCCGGTATCCGTGTGGGCACGCCTTCCGTCACCCGTCGCGGTTTCAACGAAGCGGACGTGAAAGAACTTGCCGGCTGGATGTGTGACGTATTAGACGCCATCGGCAAAGATAACGAAGCGGAAGTGATTGCCGACACCAAAGACAAAGTCTTGGCAATTTGTAAACGTCTTCCGGTTTACGCG","","","45746","MFKKSMNIADYDPVLWQAIQNENRRQEEHIELIASENYASPRVMQAQGSQFTNKYAEGYPGKRYYGGCEYADIVEQLAIERAKELFGADYVNVQPHSGSQANAAVYMGLLNPGDTILGMSLAHGGHLTHGASVSFSGKIYHAEQYGITDEGLIDYDALRKQAHDVKPKMIVGGFSAYSQVVDWKKMREIADEVGAYLFVDMAHVAGLIAAGIYPNPLPYAHVVTTTTHKTLGGPRGGLILSSCGDEEIYKKLNSAVFPAGQGGPLVHIIAAKAVCFKEALEPEYKVYQQNVLKNAKAMVEVFKQRGYKVVSNGTENHLFLVDLVSHGLTGKAADAALGKANITVNKNSVPNDPQKPFITSGIRVGTPSVTRRGFNEADVKELAGWMCDVLDAIGKDNEAEVIADTKDKVLAICKRLPVYA","1978160","[FUNCTION] Interconversion of serine and glycine. [PATHWAY] Key enzyme in the biosynthesis of purines, lipids, hormones and other components. ","glycine hydroxymethyltransferase; serine hydroxymethyltransferase","Cytoplasm","","
InterPro
IPR001085
Family
Glycine hydroxymethyltransferase
PIRSF000412\"[6-420]TSerine/glycine hydroxymethyltransferase
PTHR11680\"[10-393]TSERINE HYDROXYMETHYLTRANSFERASE
PF00464\"[8-386]TSHMT
PS00096\"[221-237]TSHMT
InterPro
IPR015421
Domain
Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10\"[37-289]Tno description
noIPR
unintegrated
unintegrated
tmhmm\"[193-213]?transmembrane_regions


","BeTs to 26 clades of COG0112COG name: Glycine hydroxymethyltransferaseFunctional Class: EThe phylogenetic pattern of COG0112 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit (1.5e-167) to 6/6 blocks of the IPB001085 family, which is described as \"Serine hydroxymethyltransferase (SHMT)\". Interpro entry for IP:IPR001085. IPB001085A 37-86 1e-43 IPB001085B 101-130 5.7e-23 IPB001085C 182-232 4e-44 IPB001085D 251-287 1.9e-25 IPB001085E 330-352 1e-11 IPB001085F 359-383 6.5e-14","Residues 19 to 173 match (1e-15) PD:PD489402 which is described as TRANSFERASE METHYLTRANSFERASE PROTEOME HYDROXYMETHYLTRANSFERASE COMPLETE RELATED GLYCINE SERINE ","","","","","","","","","","","Wed Jan 22 10:17:12 2003","Wed Jan 22 10:17:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02810 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 8 to 386 (E-value = 2.7e-284) place AA02810 in the SHMT family which is described as Serine hydroxymethyltransferase (PF00464)","","","","Brogan JM, Lally ET, Poulsen K, Kilian M, Demuth DR.Regulation of Actinobacillus actinomycetemcomitans leukotoxin expression: analysis of the promoter regions of leukotoxic and minimally leukotoxic strains.Infect Immun. 1994 Feb;62(2):501-8.PMID: 8300209","Plamann MD, Stauffer LT, Urbanowski ML, Stauffer GV.Complete nucleotide sequence of the E. coli glyA gene.Nucleic Acids Res. 1983 Apr;11(7):2065-75.PMID: 6300791Plamann MD, Stauffer GV.Characterization of the Escherichia coli gene for serine hydroxymethyltransferase.Gene. 1983 Apr;22(1):9-18.PMID: 6190704Scarsdale JN, Radaev S, Kazanina G, Schirch V, Wright HT.Crystal structure at 2.4 A resolution of E. coli serine hydroxymethyltransferase in complex with glycine substrate and 5-formyl tetrahydrofolate.J Mol Biol. 2000 Feb;296(1):155-68.PMID: 10656824","Tue Mar 25 12:58:31 2003","Tue Mar 25 12:58:31 2003","1","","","" "AA02811","1980165","1979722","444","GTGAGCGGGGAATGGCAATGTACCAGTATTTACCCTGAACACAATTTAACAACCGTAAATAATCTGCGCTTAAATCGGGATGGCACGTTGGTGAATAACCGCACCATTATTGAACCTATTGATAAGCCATTTTTTGTGTATGAAATCACGGGCACGGGAACATGGCAGCTAAGTGAACTTGATCACAAATTGACCTATACGTTTACCACTAATTGGGTACAACGTAGGCATACGGAAGAGGCTTTGGACGCCATTAAAAAGGATTCCAGATATAAACTTTATGAAGAAAATTTGTTTAAGAAATACAGTAAGCGCGTGAATAAATCGAACACGATTAATTTTGTGATTAGCTCACTGACACGCGATATGGAGCTTGGCAGAGATATGATGACTTTAACGCAAAAAACAGCACAAAAAAGCTACACCACAGCTTGCGTTCGCCAA","","","21190","VSGEWQCTSIYPEHNLTTVNNLRLNRDGTLVNNRTIIEPIDKPFFVYEITGTGTWQLSELDHKLTYTFTTNWVQRRHTEEALDAIKKDSRYKLYEENLFKKYSKRVNKSNTINFVISSLTRDMELGRDMMTLTQKTAQKSYTTACVRQ","1979557","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Wed Jan 22 10:13:05 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02811 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02813","1980358","1980185","174","ATGGATTACAATAAAAAATCCTTGTCGTATTTTGGACATTCCCTATTAGGAATAAAAAACACTGAAAAAATGCACCGCACTTTTAGAGGAGATGCAAATGAAAAAATTATTTTTACTCGGATTAACCCTGTCTTTTTTGAGCGGCTGTACGCTTACGGATTTAATAGACAATGG","","","7034","MDYNKKSLSYFGHSLLGIKNTEKMHRTFRGDANEKIIFTRINPVFFERLYAYGFNRQW","1980185","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:16:21 2004","Mon Feb 23 15:16:21 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02813 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:16:21 2004","","","","","","","","","","","","","1","","","" "AA02814","1980320","1980505","186","ATGTCCAAAATACGACAAGGATTTTTTATTGTAATCCATGTAATACGCTTATTTCTGAGTAAGTGCGGAAAAGAATTTACACCAAGTGCGGTCGTCTTACAAAACGTTTTTCATTATCAGAAAAGTACCAACCTGTTTGCAGATTCGCGCTTTAATGGAACAAATCTAAATCACATTTTTAGCATT","","","7144","MSKIRQGFFIVIHVIRLFLSKCGKEFTPSAVVLQNVFHYQKSTNLFADSRFNGTNLNHIFSI","1980505","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-24]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:14:53 2004","Mon Feb 23 15:14:53 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02814 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:14:53 2004","","","","","","","","","","","","","1","","","" "AA02816","1980572","1980820","249","GTGGACTTTATTCATCGTGCCGCAACCGAAAATAATCTGATATTGTCCTGCTACGGCAAACTGCACTTTTACACCCTCAATGTTGTCAATGCCTTGTCAACTTTGCTTTTGTTATTCAGAACAACGCGCCAACGCATGGCGCAGTGGGTAGCTGTCACAATATTTTCTTTGTCGCCAAGTTTTTCAATAACCTGTTGGGCGATTTTAAGAAGATTCATATTATTCGCCGGAAGTGTCTTAAATAATAAG","","","9491","VDFIHRAATENNLILSCYGKLHFYTLNVVNALSTLLLLFRTTRQRMAQWVAVTIFSLSPSFSITCWAILRRFILFAGSVLNNK","1980655","","hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-44]?signal-peptide
tmhmm\"[21-39]?\"[49-69]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Wed Jan 22 10:12:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02816 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02818","1981880","1980879","1002","GTGATTTGTGCAGAAAGCGAAGTGTTGGAACGGCATTTGGATTTTTTAAGCGGGAAGTCCCTGCTGCTCAGCGGGGCGGCGAACGATGATTTTCTCGCCGATTTACAACGTCAGGGATTCAACGCCCGCGCATGGAGCTGGTATTTTGACTATGCCAACAGACAACATCAAACGCCACAAAGTGCGGTGGATTTTTCCCTTGAATTTCATGGCAGCGCCGATGTGATCCTGTTTTATTGGACGAAGAATAAACAGGAATGCCATTTCCAGCTCATGCAGCTTCTCTCACAATGCACCGCCGGGCAGGAGGTTTTGCTGGTGGGCGAAAATCGTAGCGGCGTGCGTTCCGCCGAAAAAATGCTTGCCGATTACGGCGATATTCACAAAATCGACTCCGCCCGCCGTTGCAGTCTGTATCATTTTCAGTTAAAAAATCCACCGCACTTTGAACTGAAAACTTTCTGGAAATCCTATCAATCGCCACAAATTGCCGATTTAACTATCTATGCGTTGCCCGGCGTATTCAGCGCCGCCGAACTGGATGGCGGCACGGCATTATTGCTTTCTACGCTAAAAAACATCGCAGGCGGGGTGTTGGACGTGGGCTGCGGCGCGGGAGTGATCGGCAGTTATATTCAACGGCACAACCCGAACACCCGATTAATCATGACAGATATTCATGCCTTGGCGTTGGCTTCCGCAAAGCGCACTTTACAGGAAAATCGGCTACAGGGAACAGTGGTTGCCAGTGATGTGTTTTCCCATATTGACGGCAAATTTGATCTGATCATTTCCAACCCGCCGTTTCATGATGGCATTGACACCGCTTACACCGCCGTTAACGAACTGATAAAACAGGCAAAATGGCATTTGAAACCGGGCGGTGAGCTGCGCATCGTGGCAAATGCGTTTCTGCCTTACGCCGACTGGCTGAATCAACATTTCGGCAGTCATGACGTCCTGGCGAGAAATAACAAGTTTAAGGTTTATTCGGTGCACGGA","","","37237","VICAESEVLERHLDFLSGKSLLLSGAANDDFLADLQRQGFNARAWSWYFDYANRQHQTPQSAVDFSLEFHGSADVILFYWTKNKQECHFQLMQLLSQCTAGQEVLLVGENRSGVRSAEKMLADYGDIHKIDSARRCSLYHFQLKNPPHFELKTFWKSYQSPQIADLTIYALPGVFSAAELDGGTALLLSTLKNIAGGVLDVGCGAGVIGSYIQRHNPNTRLIMTDIHALALASAKRTLQENRLQGTVVASDVFSHIDGKFDLIISNPPFHDGIDTAYTAVNELIKQAKWHLKPGGELRIVANAFLPYADWLNQHFGSHDVLARNNKFKVYSVHG","1980714","[FUNCTION] Specifically methylates the guanosine in position 1207 of 16S rRNA in the 30S particle (by similarity). ","ribosomal RNA small subunit methyltransferase C","Cytoplasm","","
InterPro
IPR002052
Domain
N-6 Adenine-specific DNA methylase
PS00092\"[263-269]?N6_MTASE
InterPro
IPR007848
Domain
Methyltransferase small
PF05175\"[165-331]TMTS
InterPro
IPR013675
Domain
Methyltransferase small, N-terminal
PF08468\"[6-158]TMTS_N
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[164-334]Tno description
PTHR18895\"[183-326]TMETHYLTRANSFERASE
PTHR18895:SF6\"[183-326]TRIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE D (RRNA (GUANINE-N(2)-)-METHYLTRANSFERASE)


","No hits to the COGs database.","Significant hit ( 3.6e-06) to 3/4 blocks of the PR00507 family, which is described as \"N12 class N6 adenine-specific DNA methyltransferase signature\". Prints database entry for PR:PR00507. PR00507B 198-212 8.2 PR00507C 260-272 0.0046 PR00507D 278-302 34","Residues 194 to 254 match (2e-17) PD:PD016907 which is described as COMPLETE PROTEOME METHYLTRANSFERASE TRANSFERASE TRNA 2.1.1.- HEMK PROCESSING RNA RRNA ","","","","","","","","","","","Wed Jan 22 10:11:12 2003","Wed Jan 22 10:11:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02818 is paralogously related to AA00647 (4e-07) and AA00508 (6e-05).","","","","","","Residues 284 to 334 (E-value = 3.1e-19) place AA02818 in the MTS family which is described as Methyltransferase small domain (PF05175)","","","","","Tscherne JS, Nurse K, Popienick P, Ofengand J.Purification, cloning, and characterization of the 16 S RNA m2G1207 methyltransferase from Escherichia coli.J Biol Chem. 1999 Jan;274(2):924-9.PMID: 9873033","","Wed Jan 22 10:11:12 2003","1","","","" "AA02819","1981936","1982382","447","TTGATTTTAGATATGCAAAAAACGCGCCGACACACTTCCCGCCGAGATTTATTATTGCAGCAAATGGGCATCAGCCAATGGCAATTGGTGCGCCCTGAAGCCTTAAAAGGCGCGATTAATATCGTCGTGCCCGAATCGGTTCGTTTGGTTATCGTGAGCCATCAAAATCTGTTGCAACAACCCATCATACAGGATCTGTTGCGCAGTCTCACACTTGATAGCACGCAAGTGCTGAATATCACCTTTGAGCAGCTTGCCTATTTGCAAGTCAACCACACCGTCAATTATTGGCTACTCCATAAAAACGCCGATGAAATCCACCGCACTTTAAGCGGGCTGCAACAGCCGTTGAATGTCTGGCAATCCGTCGATCTCGCCGCGTTTAAACATGATCCGCAGGCGAAACGCCAACTCTGGCGGCAAATTCAGCAATCCGCACCGATAAAG","","","17332","LILDMQKTRRHTSRRDLLLQQMGISQWQLVRPEALKGAINIVVPESVRLVIVSHQNLLQQPIIQDLLRSLTLDSTQVLNITFEQLAYLQVNHTVNYWLLHKNADEIHRTLSGLQQPLNVWQSVDLAAFKHDPQAKRQLWRQIQQSAPIK","1982217","[FUNCTION] DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. the exact function of the PSI subunit is unknown. [SUBUNIT] DNA polymerase III contains a core (composed of alpha, epsilon and theta chains) that associates with a tau subunit. This core dimerizes to form the POLIII' complex. PolIII' associates with the gamma complex (composed of gamma, delta, delta', psi and chi chains) and with the beta chain to form the complete DNA polymerase III complex. The final composition of the complex is: (alpha,epsilon,theta)[2]-tau[2]-(gamma,delta,delta', psi,chi)[2]-beta[4].","DNA polymerase III, psi subunit","Cytoplasm","","
InterPro
IPR004615
Family
DNA polymerase III, psi subunit
PD032475\"[35-141]TQ9CM78_PASMU_Q9CM78;
PIRSF029225\"[12-149]TDNA polymerase III, psi subunit
PF03603\"[12-120]TDNA_III_psi


","No hits to the COGs database.","","Residues 13 to 143 match (5e-24) PD:PD032475 which is described as DNA POLYMERASE COMPLETE PROTEOME SUBUNIT PSI III TRANSFERASE NUCLEOTIDYLTRANSFERASE DNA-DIRECTED ","","","","","","","","","","","Tue Jan 28 16:01:23 2003","Wed Jan 22 16:19:10 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02819 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 12 to 120 (E-value = 6.6e-39) place AA02819 in the DNA_III_psi family which is described as DNA polymerase III psi subunit (PF03603)","","","","","Xiao,H., Dong,Z. and O'Donnell,M. DNA polymerase III accessory proteins. IV. Characterization of chi and psi. J. Biol. Chem. 268 (16): 11779-11784 (1993) PubMed: 8505305.O'Donnell,M. Accessory protein function in the DNA polymerase III holoenzyme from E. coli. Bioessays 14 (2): 105-111 (1992) PubMed: 1575709.Xiao,H., Crombie,R., Dong,Z., Onrust,R. and O'Donnell,M. DNA polymerase III accessory proteins. III. holC and holD encoding chi and psi. J. Biol. Chem. 268 (16): 11773-11778 (1993) PubMed: 8389364.Carter,J.R., Franden,M.A., Aebersold,R. and McHenry,C.S. Identification, isolation, and overexpression of the gene encoding the psi subunit of DNA polymerase III holoenzyme. J. Bacteriol. 175 (17): 5604-5610 (1993) PubMed: 8366044.Yoshikawa,A., Isono,S., Sheback,A. and Isono,K. Cloning and nucleotide sequencing of the genes rimI and rimJ which encode enzymes acetylating ribosomal proteins S18 and S5 ofEscherichia coli K12. Mol. Gen. Genet. 209 (3): 481-488 (1987) PubMed: 2828880.","","Tue Jan 28 16:01:23 2003","1","","","" "AA02821","1982395","1982835","441","GTGATACACATTTCTCCTATTGAACCCTCGGATTTTGATCGTCTTTATCTCATTGAGCAGGCGGCACACGCGGTGCCTTGGAGCTTAGGCACGCTGAAAAATAATCAGGGCAAACGTTACCTCAATTTGAAAATCGGCGAAGAAAGCCGAATCGACGGTTTTGCCATTTGCCAGACGGTGTTGGATGAAGCCACGCTGTTTAATATCGCCGTGGATCCGCAACAGCAGGGATTGGGGCTGGGGCGCCGCTTATTAAGCGAGCTGATGACACAATTAAAACAAAAAAGCATTCTGACCTTGTGGCTGGAAGTGCGCGAATCCAATAAAAAAGCCCAAGCGCTGTATGATTCGCTGGGCTTTAATCAGGTGGATATTCGCAAAAATTATTATCCCACCCCCGACGGCAAACGGGAAAATGCCGTGGTGATGGCGGCGTATTTA","","","16631","VIHISPIEPSDFDRLYLIEQAAHAVPWSLGTLKNNQGKRYLNLKIGEESRIDGFAICQTVLDEATLFNIAVDPQQQGLGLGRRLLSELMTQLKQKSILTLWLEVRESNKKAQALYDSLGFNQVDIRKNYYPTPDGKRENAVVMAAYL","1982670","[FUNCTION] This enzyme acetylates the N-terminal alanine of a ribosomal protein S18 (by similarity).","ribosomal-protein-alanine acetyltransferase","Cytoplasm","","
InterPro
IPR000182
Domain
GCN5-related N-acetyltransferase
PF00583\"[43-121]TAcetyltransf_1
PS51186\"[2-147]TGNAT
InterPro
IPR006464
Family
Ribosomal-protein-alanine acetyltransferase
TIGR01575\"[11-143]TrimI: ribosomal-protein-alanine acetyltrans
noIPR
unintegrated
unintegrated
G3DSA:3.40.630.30\"[2-147]Tno description
PTHR23091\"[7-143]TN-TERMINAL ACETYLTRANSFERASE
PTHR23091:SF1\"[7-143]TRIBOSOMAL-PROTEIN-ALANINE ACETYLTRANSFERASE


","No hits to the COGs database.","","Residues 69 to 135 match (4e-13) PD:PD258150 which is described as PROTEOME COMPLETE TRANSFERASE ACETYLTRANSFERASE ACYLTRANSFERASE 2.3.1.- RESISTANCE N-ACETYLTRANSFERASE PHOSPHINOTHRICIN RIBOSOMAL-PROTEIN-ALANINE ","","","","","","","","","","","Wed Jan 22 09:56:12 2003","Wed Jan 22 09:56:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02821 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 43 to 121 (E-value = 2e-15) place AA02821 in the Acetyltransf_1 family which is described as Acetyltransferase (GNAT) family (PF00583)","","","","","Yoshikawa A, Isono S, Sheback A, Isono K.Cloning and nucleotide sequencing of the genes rimI and rimJ which encode enzymes acetylating ribosomal proteins S18 and S5 of Escherichia coli K12.Mol Gen Genet. 1987 Oct;209(3):481-8.PMID: 2828880Carter JR, Franden MA, Aebersold R, McHenry CS.Identification, isolation, and overexpression of the gene encoding the psi subunit of DNA polymerase III holoenzyme.J Bacteriol. 1993 Sep;175(17):5604-10.PMID: 8366044","","Wed Jan 22 09:56:12 2003","1","","","" "AA02823","1986229","1982843","3387","GTGTTTACTGTTTATCATTCCAATCAACTTGAGGTGCAAAAAGACATTTTAGTTGAATTAATTCAACGTCAACCGCTGAACAACCCATTACAGCCGGAAATCGCGTTGGTGCAAAGCCCGGGCATGGCGCAATGGCTGCAACTGCAAATTGCCGGACAAAAAGGTATTGCGGCGAACTTCGCCTTTCCTATGCCCGCCAGTTTTATCTGGCAACTTTATGCGGAAAACCTGCTCGATGTAGCGCAAAGTAATCAATTTAACAAAAATGCCATGATGTGGCGTTTGGTTCGTTTGATTCCTCAATATTTACAACAGGATGCGCTGCGCCCTTTGCGTCATTACTTAGCCTATTCCGCCCAATCGGAGCAATTTAAACTTTATCAACTTGCCGGGAAAATCGCCGATTTATTCGACCAATATTTGGTTTATCGTCCGGACTGGATTGCCGCTTGGGAAAATCAGCAAGACGACGACATTCGCCGACAAATCGAGAGCCAATTAAGTCTAAATAATGAACGTTTACTGGCGCAGATTACGCAAAATATCGCATGGCAAGGCATTTTGTGGCGCGCCTTGGTGCGGGCGGTGAAAGCGGATACCGGGCTGGATTTGGTACAACACCGCGCCCATTTGCACCAACTGCTATTAGAAAAACTCCGTGAAAATCAACCGCTCTTTTTGCCGGAACGCCTGTTTATTTTCGGCATTCCCGCCTTGCCAAAGGCTTATTTGGAAATTTTTCAGGCAATCAGCCAATATTGCGATGTGCACTTGTTTTTTAATAATCCCTGCGAGGAATATTGGGGCGACATCGTTGATCCGAAATTCGTAGAAAAACTGGCGTTGCGTACTCGCACCGATTATTTTAATCACGCAGATAAGCCTTTATTATCGGCGGAACAGGCTGCACAGGCGCAGCAACATTGGGAGCTGACTTATGCGCAGGAAAAATTACAGGTGGGTAATTCCTTATTGGCATCTTGGGGTAAGCTGGGACGGGATTTTTCCTACTTATTGGCGCAGCTGGAACCCAATGACATTTCCGCCTATGTGGAAATCATGCCGCACAATTTATTAAGCCAGATCCAACATCGTATTTTGCATTTAACACCGAACGGCACCACGCCGTTAAACTATCGGGAAAATGACCGCACTTTAACTTTCCATTCCTGCCACAGCATGATGCGCGAAGTGGAAGTGTTGCAGGATTATTTGCTGCATTTGCTGCAACAGAATCCTGATTTAACGCCGAAAGACATTATTGTGATGGTGGCGGATATTGATAAATACACGCCCTATATCCGCGCCGTGTTCGGGCAAAATGCAACGCCGCAGACCGCTATTCCGTTTTCCATTTCCGATAACAAATTATCGGAGAATAATGTGATTATCGCCGGTTTTCTGACCTTATTGCAGCTGAAAGAAAGCACGTTTAGTGCCGAAGACGTGCTGGCATTGCTTGATGTGCCGGCAATTCGCCAACGCTTTAATATTGAATTGCAGGATTTGGCGCAAATTCGTGATTGGGTGAAAAATGCCGGCGTGCGTTTCGGCTTAGCAAAAAATGATGAGGCGGAAAGTAACTACAATTCATGGCAAGCCGGCTTGGAGCGAATGTTATTGGGTTATGCCTTGCGCGAAGAAAACGGCATTTGGCAGGATAGCCTCGGGCTGGATAACAGTTTCGGTTTGAAAGGGCAACTGGCAGGGCAATTGGCGGCATTTTTAGCGGCGTTATTCGACTGGTTCCAAACGCTGCAAAACCGTTATTCCGTGGAACAATGGCAACAGCATTTACTGGCGCTCACCGATAAATTCTTCGCCTCCTCGGCGGAAACCGATGAAACCCTGTTTTATATTAAAGAGGTAATCCGACAATTTGCCGAACAGTTAGCGGAGGTGCATTTTAGCGACGCGTTGGGCGTGGATGTGGTGGCGGATGTCATGAATAATGCGTTGGAGGAAAATCCGAACCATTATCGCTTCCTCGCCGGCAAAGTGAATTTTTGTACATTGTTGCCGATGCGCTCCATTCCGTTCAAAGTGGTTTGTCTGCTCGGTATGAACGACGGCGAATACCCGCGCCAACAAGCGCCGAACAGTTTCGATTTAATGCAATATCACCGCTTAAAAGGCGATCGCGCCCGTCGCGATGACGATCGTTATCTGTTCCTTGAAGCCTTGCTGTCGGCGCAGGATTATTTGTACATCAGCTACATCGGTCGTTCTATTGCCGATAATCAGGAGCGGGAGCCGTCGGTGCTGGTGAGTCAGTTGCTGGATTACATCGTGGAAAATCTGCCGGCGGAAAATACCCCATCGGGAAATCTCAAGTGGCGCGAACGACTGATTCAACAACATGGCATGACCGTGTTCAGTCGTAAAAACTTTGAAAAAAACGACTGCACTTTTATGCAATCTTTCGCGCAACAGTGGCTACCTTTGGCAAATTCGCAGGTAAATCAAACCTTGCAGGATTTTATTCAGCCGATGATGACGGATGCGGAGCCGGAAAATGAAATTGAGTTTTCCCGCTTGGTGGCGTTTGTGAAAAATCCGGTGAAATTTTTCTTTGAAAAACGCCTTGGCGTGAATTTCTCCGAACAGGAAGAAAGCATTGCCGACAGCGAAAATTTCGCCTTGGATAATGCCTTGGAAAAATACGCCATTCATGCGGATTTGGTGGAAGCGGACGAGCAGCAAACCGACGCGTTTTTTGCGCGTCTGAAAGTCAAAGGCGTGTTGCCGCGCGGGGAGTTCTCCGCCATTTATGCCAATCAGTTGCTGGCGGATGTGGCGGAATTCAAAGGCAAGATCGCCGATTATGTAAGCCAAACGCCGCAAAGCCGTTTTGTGCAATTCACCGTGCCGACCCAAGAGGGTGACATGACGTTGTCGGGCAACATTTCCCATTTATACGGTGACAATCTACAGCGCGTCACTTGGCGCATGGCGACGGTAAAAGATAAAGATCGTATTGAAGCTTGGCTTTATCACTTATTGTTGTGCGCCACGCAGGAACAGCCGACGGAATCGCTTTTCCAGGGGAAAGATCAGCGCGTGCGGTTTAATGTGTTGCCTCAACAGGACGCCGTTGCCCAACTGCAAATTTATGTGGAAAGTTATTTGGCGGGGCGGACGCAATTACAGCTGGTTCCGACCACAAACCTTGAAGCGTATTTGAAGTTGATTGCCGATGAAAGTGCGGTGGATATTGACAAGTGTTTTTCCCTGTTAAATAAAATCGCTATGAGCGATGAGCGTTCGCCTGGCGATTTATATTGGCGGCGAGTACTGGTGCAAACGCAGGAATTGGATTTGAATTGGATCAATCGGCAGGTAAACGCTTGGTTTGCGCCGATGTTGCAAGCTATCAAAAGGGAAAAA","","","130968","VFTVYHSNQLEVQKDILVELIQRQPLNNPLQPEIALVQSPGMAQWLQLQIAGQKGIAANFAFPMPASFIWQLYAENLLDVAQSNQFNKNAMMWRLVRLIPQYLQQDALRPLRHYLAYSAQSEQFKLYQLAGKIADLFDQYLVYRPDWIAAWENQQDDDIRRQIESQLSLNNERLLAQITQNIAWQGILWRALVRAVKADTGLDLVQHRAHLHQLLLEKLRENQPLFLPERLFIFGIPALPKAYLEIFQAISQYCDVHLFFNNPCEEYWGDIVDPKFVEKLALRTRTDYFNHADKPLLSAEQAAQAQQHWELTYAQEKLQVGNSLLASWGKLGRDFSYLLAQLEPNDISAYVEIMPHNLLSQIQHRILHLTPNGTTPLNYRENDRTLTFHSCHSMMREVEVLQDYLLHLLQQNPDLTPKDIIVMVADIDKYTPYIRAVFGQNATPQTAIPFSISDNKLSENNVIIAGFLTLLQLKESTFSAEDVLALLDVPAIRQRFNIELQDLAQIRDWVKNAGVRFGLAKNDEAESNYNSWQAGLERMLLGYALREENGIWQDSLGLDNSFGLKGQLAGQLAAFLAALFDWFQTLQNRYSVEQWQQHLLALTDKFFASSAETDETLFYIKEVIRQFAEQLAEVHFSDALGVDVVADVMNNALEENPNHYRFLAGKVNFCTLLPMRSIPFKVVCLLGMNDGEYPRQQAPNSFDLMQYHRLKGDRARRDDDRYLFLEALLSAQDYLYISYIGRSIADNQEREPSVLVSQLLDYIVENLPAENTPSGNLKWRERLIQQHGMTVFSRKNFEKNDCTFMQSFAQQWLPLANSQVNQTLQDFIQPMMTDAEPENEIEFSRLVAFVKNPVKFFFEKRLGVNFSEQEESIADSENFALDNALEKYAIHADLVEADEQQTDAFFARLKVKGVLPRGEFSAIYANQLLADVAEFKGKIADYVSQTPQSRFVQFTVPTQEGDMTLSGNISHLYGDNLQRVTWRMATVKDKDRIEAWLYHLLLCATQEQPTESLFQGKDQRVRFNVLPQQDAVAQLQIYVESYLAGRTQLQLVPTTNLEAYLKLIADESAVDIDKCFSLLNKIAMSDERSPGDLYWRRVLVQTQELDLNWINRQVNAWFAPMLQAIKREK","1982678","[FUNCTION] Exhibits a wide variety of catalytic activities including ATP-dependent exonuclease, ATP-stimulated endonuclease,ATP-dependent helicase and DNA-dependent ATPase activities (by similarity). ","exodeoxyribonuclease V gamma chain","Cytoplasm, Inner membrane","","
InterPro
IPR006697
Family
Exodeoxyribonuclease V, RecC subunit
PF04257\"[1-1127]TExonuc_V_gamma
TIGR01450\"[2-1094]TrecC: exodeoxyribonuclease V, gamma subunit


","BeTs to 9 clades of COG1330COG name: Exonuclease V gamma subunitFunctional Class: LThe phylogenetic pattern of COG1330 is ----------r---efghsn---it-Number of proteins in this genome belonging to this COG is","","Residues 869 to 1066 match (2e-07) PD:PD148857 which is described as COMPLETE PROTEOME V EXONUCLEASE EXODEOXYRIBONUCLEASE DNA HELICASE HYDROLASE ENDONUCLEASE SUBUNIT ","","","","","","","","","","","Wed Jan 22 09:53:01 2003","Wed Jan 22 09:53:01 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02823 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Finch PW, Wilson RE, Brown K, Hickson ID, Tomkinson AE, Emmerson PT.Complete nucleotide sequence of the Escherichia coli recC gene and of the thyA-recC intergenic region.Nucleic Acids Res. 1986 Jun;14(11):4437-51.PMID: 3520484Finch PW, Wilson RE, Brown K, Hickson ID, Emmerson PT.Complete nucleotide sequence of the Escherichia coli ptr gene encoding protease III.Nucleic Acids Res. 1986 Oct;14(19):7695-703.PMID: 3534791","","Wed Jan 22 09:53:01 2003","1","","","" "AA02824","1986459","1986271","189","GTGCAACGAAAAAGTGCGGTGGAAATTTATCAGCGTTTTCAAGCCATCCAAATTGCCGAAAATCAGCATCAACGCCGTTTTCTCGGGTTGCCTTGTGAATCACAGGTGCAGCAAAATCAAATTCGTTTTCAGGTGATTTGTTCGCAAAATCAGGTGTCGGTAAAATATCCTCGCGGTGAAATTAGTTTA","","","7400","VQRKSAVEIYQRFQAIQIAENQHQRRFLGLPCESQVQQNQIRFQVICSQNQVSVKYPRGEISL","1986106","","conserved hypothetical protein","Cytoplasm, Extracellular","","
noIPR
unintegrated
unintegrated
PD068240\"[2-61]TY941_HAEIN_P44082;


","No hits to the COGs database.","","Residues 2 to 61 match (3e-10) PD:PD068240 which is described as COMPLETE PROTEOME PM0962 HI0941 SIGNAL PRECURSOR ","","","","","","","","","","","","Wed Jan 22 09:49:51 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02824 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02826","1987168","1986476","693","ATGAAGAATAGAGCGTTTTTCCACGTGCCGCCTTATCACGGGCAAAGCCTTGTTGCGCTGATGATTTCCGTGGCGCTTTCGAGCTCTTTATTTCTCGTCATCATGCAGTTTTATAGCCAACATCAGCAACAAAATCGGGAAATGTTACTGCGTTTGCAGTTACAAATGGAATTACAACGCGTCATTCAATTAATGGGGAAAGATTTGGCAAGAAGCGGTTTTCGTGCCGTGAATAATAAATTAAAACAAAATAATATCGCCTTATTTGAGCAAGAAAATACACCATCGGCAGTGACCATCGCGCAAGTGAATGGCGAGAAAAATAACAGCTGCGTGTTGTTCTTTTATGACTTGGATGCCAATGGGTGTATCGGCGGAAATTATAAAGGCGATGCTTGTGTTGTGAACGGGCGTAACAATACAAGAGAAATTGAGCGCGAATTGTTCGGCTATCGACTTAACCAAAACATGCTGGAAACTCGTTTGACCTACAAAAGTGCGGTGAAGCAAAACTGCACACAAGAAGAATGCCGCCGTTATACGCAACAATCCGCGTGCCATTACGGTGGTTGGGCAGATTTACTGGACGAGAAAGAATATGAAATTTCGCAGTTGAGTTTTGATTGGCTGTCGGAACAAAAGGGGATTAAAATTCGCCTCAGTGGACGTTTTAAACGACATAAACAGATCGAA","","","27289","MKNRAFFHVPPYHGQSLVALMISVALSSSLFLVIMQFYSQHQQQNREMLLRLQLQMELQRVIQLMGKDLARSGFRAVNNKLKQNNIALFEQENTPSAVTIAQVNGEKNNSCVLFFYDLDANGCIGGNYKGDACVVNGRNNTREIERELFGYRLNQNMLETRLTYKSAVKQNCTQEECRRYTQQSACHYGGWADLLDEKEYEISQLSFDWLSEQKGIKIRLSGRFKRHKQIE","1986311","","conserved hypothetical protein","Outer membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
PD110566\"[61-231]TQ9CM73_PASMU_Q9CM73;
signalp\"[1-32]?signal-peptide
tmhmm\"[15-35]?transmembrane_regions


","No hits to the COGs database.","","Residues 61 to 231 match (1e-48) PD:PD110566 which is described as PROTEOME COMPLETE TRANSMEMBRANE PM0964 HI0939 ","","","","","","","","","","","","Wed Jan 22 09:49:19 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02826 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02827","1987679","1987161","519","ATGCAAAAGGGATTCACTTTGTTGGAAATGTTAATAGCATTATTTATTATCAGCCTGTTACTGACACTGGCTTTGCCGGCATGGCAACAGCATTCGCAACAAACTATTCTGCAAAAAGAACAACAAAAACTTTATGTCTTTCTTCGTCAAATTCAGGCGCGCGTGGAAAATTCTACGGACATCTGGTTGTTATTGGCAAATCGTGATCCTGTAGGAAAGCGCTGGTGTTTGACAGCGCAAATTAAAAATAGCCATTTGTGCGATTGCCTAAATCCTGTTGCTTGCCCGCAAAATGTTTCCGCCCATTTTTATTATCCCGCTTTTGCTGAAACTGTGTTGGTGAGCAAGCGTTATTATCCTTTGGAGTTTACCCGTTTAAGTGGTATTCGGAATACGGCTTCTACCACTTGTTTTGTGCTACAAGCCAATCAGCAGCGTACTTTGTTTTCGTTCTTTAATGTGGGCAGTTTGAAATTAAAGGATAACCAATCTTTGAGTGCTTGTGTCAATGATGAAGAA","","","23589","MQKGFTLLEMLIALFIISLLLTLALPAWQQHSQQTILQKEQQKLYVFLRQIQARVENSTDIWLLLANRDPVGKRWCLTAQIKNSHLCDCLNPVACPQNVSAHFYYPAFAETVLVSKRYYPLEFTRLSGIRNTASTTCFVLQANQQRTLFSFFNVGSLKLKDNQSLSACVNDEE","1986996","","conserved hypothetical protein","Inner membrane, Periplasm, Cytoplasm","","
InterPro
IPR001120
PTM
Prokaryotic N-terminal methylation site
PS00409\"[3-23]TPROKAR_NTER_METHYL
InterPro
IPR012902
PTM
Prepilin-type cleavage/methylation, N-terminal
PF07963\"[3-26]TN_methyl
TIGR02532\"[2-25]TIV_pilin_GFxxxE: prepilin-type N-terminal c
noIPR
unintegrated
unintegrated
G3DSA:3.30.700.10\"[4-31]Tno description
signalp\"[1-29]?signal-peptide
tmhmm\"[10-28]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 7e-10) to 1/1 blocks of the IPB001120 family, which is described as \"Prokaryotic N-terminal methylation site\". Interpro entry for IP:IPR001120. IPB001120 2-21 7.2e-10Significant hit ( 2.4e-05) to 1/2 blocks of the PR00813 family, which is described as \"Bacterial general secretion pathway protein G signature\". Prints database entry for PR:PR00813. PR00813A 4-29 2.5e-05","Residues 1 to 168 match (3e-46) PD:PD098181 which is described as PROTEOME COMPLETE TRANSMEMBRANE PM0965 HI0938 ","","","","","","","","","","","","Wed Jan 22 09:44:57 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02827 is paralogously related to AA00160 (9e-05).","","","","","","","","","","","","","","1","","","" "AA02828","1988381","1988277","105","TTGCTGGAATGTATAAAAACCGGGTATAAGCCCGGTTTTTTGTTGGTATCAATTCGCCTAATTAGTAGAAAAATGATAAAAAAACTGACCGCACTTTATTTTGTT","","","4039","LLECIKTGYKPGFLLVSIRLISRKMIKKLTALYFV","1988277","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:13:31 2004","Mon Feb 23 15:13:31 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02828 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:13:31 2004","","","","","","","","","","","","","1","","","" "AA02829","1988851","1988387","465","ATGAATAAATTTACGAAAGCATTGTTAGTTGCTGGTTCTGTGGCTGTGTTAGCGGCGTGTGGATCATCCAACAAAAACGAAAGCGGTAGTGGTAGCAATAATGGTCAAACATTTGGTGGCTATTCCGTTCAAGATTTACAACAACGCTACAACACCGTGTATTTCGGCTTTGATAAATATGATATTGAAGGTGAATACACTCAAATCTTAGATGCTCATGTAGCATACTTAAATGCAACACCTGCAACAAGCGTGCGTGTTGAAGGTAACACCGACGAGCGTGGTACACCGGAATATAATATGGCATTAGGTGAACGCCGTGCACGTGCAGTACAAAACTTTTTAACTGCTAAAGGTGTAAAAGCAGGTCAAATATCCACCGTTTCTTACGGTGAAGAAAAACCGGCAGTATTAGGTCATGACGAATCTGCTTATGCTAAAAACCGTCGTGCAGTATTAGCATAC","","","16701","MNKFTKALLVAGSVAVLAACGSSNKNESGSGSNNGQTFGGYSVQDLQQRYNTVYFGFDKYDIEGEYTQILDAHVAYLNATPATSVRVEGNTDERGTPEYNMALGERRARAVQNFLTAKGVKAGQISTVSYGEEKPAVLGHDESAYAKNRRAVLAY","1988222","[FUNCTION] Thought to play a role in bacterial envelope integrity. Very strongly associated with the peptidoglycan.","peptidoglycan-associated outer membrane","Outer membrane, Extracellular","","
InterPro
IPR006664
Domain
Bacterial outer membrane protein
PR01021\"[55-77]T\"[85-100]T\"[100-116]TOMPADOMAIN
InterPro
IPR006665
Domain
OmpA/MotB
PD000930\"[53-112]TPAL_PASMU_Q51886;
PF00691\"[54-149]TOmpA
PS51123\"[42-155]TOMPA_2
InterPro
IPR006690
Domain
OmpA-like
PS01068\"[87-131]TOMPA_1
InterPro
IPR014169
Family
Peptidoglycan-associated lipoprotein
TIGR02802\"[52-155]TPal_lipo: peptidoglycan-associated lipoprot
noIPR
unintegrated
unintegrated
G3DSA:3.30.1330.60\"[51-153]Tno description
PS51257\"[1-20]TPROKAR_LIPOPROTEIN
signalp\"[1-23]?signal-peptide


","BeTs to 13 clades of COG2885COG name: Outer membrane protein and related peptidoglycan-associated (lipo)proteinsFunctional Class: MThe phylogenetic pattern of COG2885 is -------q--r---efghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 5.6e-33) to 3/4 blocks of the IPB001145 family, which is described as \"Bacterial outer membrane protein\". Interpro entry for IP:IPR001145. IPB001145B 51-78 3e-06 IPB001145C 85-131 1e-22 IPB001145D 144-155 0.58","Residues 53 to 151 match (2e-20) PD:PD340072 which is described as COMPLETE PROTEOME MEMBRANE CHEMOTAXIS MOTB FLAGELLAR OUTER FLAGELLA TRANSMEMBRANE LIPOPROTEIN ","","","","","","","","","","","Wed Jan 22 09:44:06 2003","Wed Jan 22 09:44:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02829 is paralogously related to AA02479 (4e-10), AA02458 (1e-09) and AA02027 (6e-09).","","","","","","Residues 54 to 149 (E-value = 4.4e-45) place AA02829 in the OmpA family which is described as OmpA family (PF00691)","","","","","Spinola SM, Hiltke TJ, Fortney K, Shanks KL.The conserved 18,000-molecular-weight outer membrane protein of Haemophilus ducreyi has homology to PAL.Infect Immun. 1996 Jun;64(6):1950-5.PMID: 8675292Kasten RW, Hansen LM, Hinojoza J, Bieber D, Ruehl WW, Hirsh DC.Pasteurella multocida produces a protein with homology to the P6 outer membrane protein of Haemophilus influenzae.Infect Immun. 1995 Mar;63(3):989-93.PMID: 7868272Chen R, Henning U.Nucleotide sequence of the gene for the peptidoglycan-associated lipoprotein of Escherichia coli K12.Eur J Biochem. 1987 Feb;163(1):73-7.PMID: 3545827Lazzaroni JC, Portalier R.The excC gene of Escherichia coli K-12 required for cell envelope integrity encodes the peptidoglycan-associated lipoprotein (PAL).Mol Microbiol. 1992 Mar;6(6):735-42.PMID: 1574003","","Thu Sep 25 13:08:59 2003","1","","","" "AA02830","1990146","1988869","1278","ATGAAAGTAGTTATTCGAATTTTTGGCTTATTTATTATGCTGTTAGGGTTTGCCATGGTAGCCCGAGCAGAGGTGCGAATCGTGATTGATGAAGTCATGGATTCTGCCCGCCCTATTGCTGTCGTGCCATTTAAATGGAATGGACCTGGTAGTGCGCCGGCAAATATCGCTGAGATTATTTCCGCAGACTTGCGTAATAGCGGTAAATTTAATCCGTTGCCGGAAAGCAAGATGCCGCAACAGCCGACTTCGGCATCGGAAGTTAATCCGGAAGCTTGGTCGGCATTAGGCATTGAAGCCGTTATTGTTGGACAAGTTACTCCTTCCAATGGTGGTTTTGATATTGCTTACCAATTGGTTGATACCATGGGCAGCGTTGGTTCAATTTTGTCACAAAATCAATATACGGTAATGCAAAAATGGTTGCGTTATGGTGCACATACGATAAGTGATGAGACATTTGAAAAACTCACCGATATTCGTGGTGCGTTCAGAACCCGTATTGCTTATGTCGTGCAGAAAAATGGCGGTTCCCAGCCTTATGAAGTGCGCGTGGCAGATTATGACGGTTTTAATCAATTTATCGTGAATAGAAGTTCTCAACCGTTTATGTCACCGGCATGGTCACCGGACGGTAAAAAACTCGCTTATGTAACCTTTGAAAATAAGAAAGCACAGGTTGTCTTACAGGATCTTGTTTCTATGGCGCGTAAAGTGGTTGCTTCTTTCCCGGGACATAACGGCGCACCGGCATTTTCACCGGATGGTTCCAGACTTGCATTTGCGTCTTCAAAGGACGGTGTGTTAAATATTTATGTGACTAATTTGGGCAGTGGACAGGTTTCTCAGTTAACCAGCGGTGCGGGTAATAATACCGAACCGTCATGGTCGCCTGATGGTCAGTCCATCGTGTTCACTTCTGATAGAGGTGGCTCGCCTCAAGTTTATCGTATGAGTGCATCCGGCGGTGGTGCTTCTCTTATCGGTGGGCGCGGTAGCGGTCAAATCAGTTCAGATGGTAATTTATTAGTTATGGTTGATGTAAACAATAATATCGTTAAAAAAGATTTGACGTCAGGCAGTTCTGAGGTGTTAAGTTCCACCTTCTTGGATGAAAGTCCGAGTATTTCACCAAACGGTATCATGGTTATTTATAGTTCTACCCAAGGCTTAGGAAAGGTGCTACAATTAGTATCCACTGACGGTCGCTTTAAGGCACGTTTACCTGGGAATGATGGACAAGTTAAATTTCCGGCTTGGTCACCATACTTAACTAAA","","","45528","MKVVIRIFGLFIMLLGFAMVARAEVRIVIDEVMDSARPIAVVPFKWNGPGSAPANIAEIISADLRNSGKFNPLPESKMPQQPTSASEVNPEAWSALGIEAVIVGQVTPSNGGFDIAYQLVDTMGSVGSILSQNQYTVMQKWLRYGAHTISDETFEKLTDIRGAFRTRIAYVVQKNGGSQPYEVRVADYDGFNQFIVNRSSQPFMSPAWSPDGKKLAYVTFENKKAQVVLQDLVSMARKVVASFPGHNGAPAFSPDGSRLAFASSKDGVLNIYVTNLGSGQVSQLTSGAGNNTEPSWSPDGQSIVFTSDRGGSPQVYRMSASGGGASLIGGRGSGQISSDGNLLVMVDVNNNIVKKDLTSGSSEVLSSTFLDESPSISPNGIMVIYSSTQGLGKVLQLVSTDGRFKARLPGNDGQVKFPAWSPYLTK","1988704","[FUNCTION] Involved in the tonB-independent uptake of proteins. A group a colicins (colicins A, E1, E2, E3, and K). necessary for the colicins to reach their respective targets after initial binding to the bacteria. Also involved in the translocation of bacteriophage DNA. (by similarity).","colicin tolerance protein","Periplasm, Outer membrane","","
InterPro
IPR001680
Repeat
WD-40 repeat
SM00320\"[236-273]TWD40
InterPro
IPR007195
Domain
TolB, N-terminal
PF04052\"[8-174]TTolB_N
InterPro
IPR011659
Repeat
WD40-like Beta Propeller
PF07676\"[193-230]T\"[238-273]T\"[282-317]T\"[362-398]TPD40
InterPro
IPR014167
Family
Tol-Pal system beta propeller repeat, TolB
TIGR02800\"[15-421]Tpropeller_TolB: Tol-Pal system beta propell
noIPR
unintegrated
unintegrated
G3DSA:2.120.10.30\"[166-424]Tno description
G3DSA:3.40.50.10070\"[30-165]Tno description
signalp\"[1-23]?signal-peptide
tmhmm\"[5-23]?transmembrane_regions


","BeTs to 10 clades of COG0823COG name: Periplasmic component of the Tol biopolymer transport systemFunctional Class: NThe phylogenetic pattern of COG0823 is a------------cefghs-ujxi--Number of proteins in this genome belonging to this COG is","","Residues 265 to 318 match (7e-07) PD:PD476064 which is described as COMPLETE TOLB PROTEOME PRECURSOR SIGNAL PERIPLASMIC PROBABLE TOLB-RELATED COLICINS PHAGE ","","","","","","","","","","","Wed Jan 22 09:09:56 2003","Wed Jan 22 09:09:56 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02830 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 12 to 174 (E-value = 9.7e-70) place AA02830 in the TolB_N family which is described as TolB amino-terminal domain (PF04052)","","","","","Sen K, Sikkema DJ, Murphy TF.Isolation and characterization of the Haemophilus influenzae tolQ, tolR, tolA and tolB genes.Gene. 1996 Oct;178(1-2):75-81.PMID: 8921895Levengood SK, Webster RE.Nucleotide sequences of the tolA and tolB genes and localization of their products, components of a multistep translocation system in Escherichia coli.J Bacteriol. 1989 Dec;171(12):6600-9.PMID: 2687247Isnard M, Rigal A, Lazzaroni JC, Lazdunski C, Lloubes R.Maturation and localization of the TolB protein required for colicin import.J Bacteriol. 1994 Oct;176(20):6392-6.PMID: 7929011Lazzaroni JC, Portalier R.The excC gene of Escherichia coli K-12 required for cell envelope integrity encodes the peptidoglycan-associated lipoprotein (PAL).Mol Microbiol. 1992 Mar;6(6):735-42.PMID: 1574003","","Thu Sep 25 13:08:13 2003","1","","","" "AA02832","1991389","1990184","1206","GTGCAGAATAAGCGACAAAAAGGTGATGTTGATGCAGTTGTGATTTCCATCATAATGCACTTAGCGTTGTTCGGATTGTTAATTTTAAGCTCGCTCTACCATAATATTGACATTATGGGCGGCGGTGAAGGCGATAACGGTGAAGTTATCGGCGCCGTGATGGTTGATACGGGCTCGGCAGCGCAGGAATGGGGGCGAATTCAACAACAGAAAAAAGGTCAGGCGGACAGACAAAAGAAACAAGCCCTTGAAGACCAAAAACGTGAAGAGCAGAAACGGGAAGAAGAAAAACAACGGGAAGTGTTAAAAGAGCAACAACGTCAACAGGAAATTGCCCGTCAGAAAGAACTGGAACAGCAAAAAGAGCTGGAAAGACAAAGGTTCTTGGCTGAACAGAAAAAGCAACAGGAAGAAAAAGCCCGCTTAGAAGCCTTGGAAAAGCAAAAACAGGCAGAAGAGGCGAAAGCCAAACAGGCTGCTGAAGCCGCTAAGCTCAAAGCTGAAGCTGAGGCAAAACGTTTAGCAGATGCTGCAAAACAAGCGGAAGAAGAAGCAAAAGCCAAAGTGCAGGCAGACGAGAAAGCAAAACAAGAGGCAAAAGCCAAAGCAGAGGCGGAAGCTAAGGCAAAAGCAGAGGCGCAGGCTAAAGCGAAGGCGGAAGCTGATGCAAAAGCCAAAGCGGATGCTAAAGCGAAAGCTGACGCAGAAGCAAAAGCTAAGGCCGATGCTAAAGCGAAAGCTGACGCCAAGGCTAAGGCAGATGCGGAAGCCAAAGCGAAAGCGGATGCGCAACGTCGAGCTGATCAAAATGCATTAGATGATTTTTTTAATGGCGGTGATGTGGGCGGCGGCAGTGCTTTGCAAGGTAGTAACATAAATAAACAAGGCAGCCAGGGTTCAGGTGCTTCAGCGGGCGCAGGCGATGGCGGTAAGGCGGGTTCGAGGTATGCAGGTATTATCTATAAATCTGTGAAGCCATATTTTCGTGGTGATAGTCGTTTTTTTGGTAAGGTCTGTGATATTAGAATTGAGCTTTCTAGTGATGGCACTATTTTATCTTACCAAAAGGTCTCCGGGCCAAATGATTTATGTGGGGCGGCTTTAAATGCTATTGGTCAAACCAGAAAAATGAACGAACCGCCTACGCCGGAAGAATATGAAATATTTAAAAGGTCCATTGTAACCTTTGACCCAAGAAAAGTGCGG","","","43639","VQNKRQKGDVDAVVISIIMHLALFGLLILSSLYHNIDIMGGGEGDNGEVIGAVMVDTGSAAQEWGRIQQQKKGQADRQKKQALEDQKREEQKREEEKQREVLKEQQRQQEIARQKELEQQKELERQRFLAEQKKQQEEKARLEALEKQKQAEEAKAKQAAEAAKLKAEAEAKRLADAAKQAEEEAKAKVQADEKAKQEAKAKAEAEAKAKAEAQAKAKAEADAKAKADAKAKADAEAKAKADAKAKADAKAKADAEAKAKADAQRRADQNALDDFFNGGDVGGGSALQGSNINKQGSQGSGASAGAGDGGKAGSRYAGIIYKSVKPYFRGDSRFFGKVCDIRIELSSDGTILSYQKVSGPNDLCGAALNAIGQTRKMNEPPTPEEYEIFKRSIVTFDPRKVR","1990019","[FUNCTION] Involved in the tonB-independent uptake of proteins. A group a colicins (colicins A, E1, E2, E3, and K). necessary for the colicins to reach their respective targets after initialbinding to the bacteria. Also involved in the translocation of bacteriophage DNA. (by similarity). ","outer membrane integrity protein","Periplasm, Outer membrane, Inner membrane, Cytoplasm","","
InterPro
IPR010528
Family
TolA
PF06519\"[3-398]TTolA
InterPro
IPR014161
Family
Tol-Pal system, TolA
TIGR02794\"[10-398]TtolA_full: protein TolA
noIPR
unintegrated
unintegrated
G3DSA:3.30.1150.10\"[320-398]Tno description
signalp\"[1-32]?signal-peptide
tmhmm\"[10-30]?transmembrane_regions


","BeTs to 3 clades of COG3064COG name: Membrane protein involved in colicin uptakeFunctional Class: MThe phylogenetic pattern of COG3064 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","Significant hit ( 2.5e-07) to 2/26 blocks of the IPB001101 family, which is described as \"Plectin repeat\". Interpro entry for IP:IPR001101. IPB001101O 73-106 0.056 IPB001101P 107-161 0.0017 IPB001101N 122-176 0.48Significant hit ( 2.5e-05) to 1/8 blocks of the IPB003134 family, which is described as \"Repeat in HS1/Cortactin\". Interpro entry for IP:IPR003134. IPB003134F 178-226 2.4e-05 IPB003134F 156-204 0.00077 IPB003134F 192-240 0.0015 IPB003134F 69-117 0.0041 IPB003134F 170-218 0.02 IPB003134F 162-210 0.025 IPB003134F 90-138 0.049 IPB003134F 200-248 0.052 IPB003134F 131-179 0.073 IPB003134F 84-132 0.092 IPB003134F 149-197 0.098 IPB003134F 133-181 0.1 IPB003134F 124-172 0.17 IPB003134F 62-110 0.18 IPB003134F 222-270 0.26 IPB003134F 117-165 0.45 IPB003134F 74-122 0.69 IPB003134F 82-130 0.94 IPB003134F 104-152 0.94Significant hit ( 7.1e-05) to 1/5 blocks of the IPB001800 family, which is described as \"Lipoprotein, type 6\". Interpro entry for IP:IPR001800. IPB001800D 216-262 6.8e-05 IPB001800D 202-248 0.00024 IPB001800D 194-240 0.00063 IPB001800D 201-247 0.00086 IPB001800D 224-270 0.0011 IPB001800D 196-242 0.0016 IPB001800D 182-228 0.0028 IPB001800D 210-256 0.0038 IPB001800D 208-254 0.01 IPB001800D 214-260 0.01 IPB001800D 204-250 0.013 IPB001800D 209-255 0.027 IPB001800D 212-258 0.03 IPB001800D 198-244 0.04 IPB001800D 200-246 0.045 IPB001800D 206-252 0.053 IPB001800D 222-268 0.12 IPB001800D 190-236 0.14 IPB001800D 215-261 0.15 IPB001800D 217-263 0.15 IPB001800D 193-239 0.16 IPB001800D 149-195 0.18 IPB001800D 151-197 0.18 IPB001800D 192-238 0.18 IPB001800D 133-179 0.26 IPB001800D 172-218 0.32 IPB001800D 188-234 0.32 IPB001800D 180-226 0.34 IPB001800D 223-269 0.49 IPB001800D 187-233 0.59 IPB001800D 207-253 0.83 IPB001800D 228-274 0.83","Residues 265 to 399 match (1e-18) PD:PD031808 which is described as PROTEOME COMPLETE TOLA INNER TRANSMEMBRANE MEMBRANE REPEAT ","","","","","","","","","","","Wed Jan 22 09:06:22 2003","Thu Mar 20 17:20:09 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02832 is paralogously related to AA02347 (3e-16), AA01922 (5e-12), AA01808 (1e-10), AA00450 (6e-07), AA01337 (5e-06), AA01488 (9e-05), AA01213 (9e-05), AA01211 (2e-04), AA02591 (6e-04), AA00609 (6e-04) and AA02964 (8e-04).","","","","","","Residues 3 to 398 (E-value = 9.2e-136) place AA02832 in the TolA family which is described as TolA protein (PF06519)","","","","","Sen K, Sikkema DJ, Murphy TF.Isolation and characterization of the Haemophilus influenzae tolQ, tolR, tolA and tolB genes.Gene. 1996 Oct;178(1-2):75-81.PMID: 8921895Levengood SK, Webster RE.Nucleotide sequences of the tolA and tolB genes and localization of their products, components of a multistep translocation system in Escherichia coli.J Bacteriol. 1989 Dec;171(12):6600-9.PMID: 2687247Levengood SK, Beyer WF, Webster RE.TolA: a membrane protein involved in colicin uptake contains an extended helical region.Proc Natl Acad Sci U S A. 1991 Jul;88(14):5939-43.PMID: 2068069Derouiche R, Gavioli M, Bénédetti H, Prilipov A, Lazdunski C, Lloubès R.TolA central domain interacts with Escherichia coli porins.EMBO J. 1996 Dec;15(23):6408-15.PMID: 8978668","","Thu Mar 20 17:10:06 2003","1","","","" "AA02834","1991828","1991409","420","ATGTCCTATCGTCGCCAGCGCCGTGATATAAAATCCGAAATCAATATTGTTCCGTTTTTGGACGTGCTTTTAGTATTGGTTTTAATTTTTATGGCTACTGCGCCAATTATTAGTCAAAGCGTAGAAGTTGAACTGCCGGATGCGGTTCAAAGTCAAAATGTTTCTACGGAAGACAAAACACCGGTGATTTTAGAAGTGTCGGGAATCGGTCAGTACGCCATTTCAATCGGCGGCACCCGTACGGAAAATCTTACCGAAGAGATGGTTACCCAACTATCAAAACAAGAATTTGATAAAGATAACAATACAATGTTCTTAGTCGGCGGTGCCAAAGAAGTACCTTATGAAGAGGTCATTAAAGCACTCAATTTGCTTCATCTTGCCGGCATCAAATCCGTTGGTTTAATGACAAACCCAATT","","","15460","MSYRRQRRDIKSEINIVPFLDVLLVLVLIFMATAPIISQSVEVELPDAVQSQNVSTEDKTPVILEVSGIGQYAISIGGTRTENLTEEMVTQLSKQEFDKDNNTMFLVGGAKEVPYEEVIKALNLLHLAGIKSVGLMTNPI","1991244","","colicin transport protein","Inner membrane, Periplasm, Cytoplasm","","
InterPro
IPR003400
Family
Biopolymer transport protein ExbD/TolR
PF02472\"[7-140]TExbD
noIPR
unintegrated
unintegrated
signalp\"[1-38]?signal-peptide
tmhmm\"[15-37]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 6.9e-13) to 1/1 blocks of the IPB003400 family, which is described as \"Biopolymer transport protein ExbD/TolR\". Interpro entry for IP:IPR003400. IPB003400 13-35 7e-13","Residues 12 to 139 match (3e-50) PD:PD007356 which is described as COMPLETE PROTEOME BIOPOLYMER EXBD TRANSMEMBRANE MEMBRANE INNER TOLR FAMILY EXBD/TOLR ","","","","","","","","","","","","Tue Jan 21 18:26:21 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02834 is paralogously related to AA01124.1 (2e-07).","","","","","","Residues 7 to 140 (E-value = 1.3e-06) place AA02834 in the ExbD family which is described as Biopolymer transport protein ExbD/TolR (PF02472)","","","","","Sen K, Sikkema DJ, Murphy TF.Isolation and characterization of the Haemophilus influenzae tolQ, tolR, tolA and tolB genes.Gene. 1996 Oct;178(1-2):75-81.PMID: 8921895Sun TP, Webster RE.Nucleotide sequence of a gene cluster involved in entry of E colicins and single-stranded DNA of infecting filamentous bacteriophages into Escherichia coli.J Bacteriol. 1987 Jun;169(6):2667-74.PMID: 3294803Kampfenkel K, Braun V.Membrane topologies of the TolQ and TolR proteins of Escherichia coli: inactivation of TolQ by a missense mutation in the proposed first transmembrane segment.J Bacteriol. 1993 Jul;175(14):4485-91.PMID: 8331075","","Tue Mar 4 16:11:41 2003","1","","","" "AA02835","1991936","1991841","96","TTGGTAAAAACCATCACAATTAATTTACCGAAAATTCTTACCGCACTTTATGCTAAAAGTGCGGTCATTATTTTAAGCGTTTTTAGATTCCAGATT","","","3570","LVKTITINLPKILTALYAKSAVIILSVFRFQI","1991841","","hypothetical protein","Cytoplasm, Outer membrane","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-15]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:11:59 2004","Mon Feb 23 15:11:59 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02835 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:11:59 2004","","","","","","","","","","","","","1","","","" "AA02836","1992603","1991917","687","ATGGCAGCAGAGTTAAACTTTTTAGATTTATTTCTAAAAGCGAGTATCGTAGTTCAGCTCGTTATCTTAATCTTAATCATTTTCTCAATTACCTCTTGGGCTATCATCATTCAGCGTAGCCGTGTATTAACCAAAGCGTTGAAAGAATCCATGGCATTTGAAGATCGTTTTTGGTCCGGCGAAGATTTAAATAAACTTTATGAAGGTTTATCTAACCGTCGCGATGGGTTAACCGGCAGCGAACAGATTTTTTATGTAGGATTTAAAGAATTTTCCCGCTTAAAACAAGCTAATCCGGATGCGCCTGAAGCCATTATCCAAGGCAGCACCCGTGCTATGAATTTATCCATGAATCGTGAAATTGAAGATCTGGAAACCCGCGTACCGTTTTTGGCAACGGTGGCTTCCATCAGCCCGTATATCGGCTTATTCGGTACGGTTTGGGGGATTATGCACGCATTTCTGTCCTTAAGTGGCGCAAAACAAGCCACCTTACAGATGGTAGCACCGGGCATTGCGGAAGCATTGATTGCAACGGCTATCGGTTTGTTTGCTGCGATTCCTGCAGTAATGGCATATAACCGTTTGAGTTTACGTGTGAATAAACTTGAGCAAAATTACGGCAATTTCATCGATGAATTTACCACCATTTTGCACCGTCAAGTGTTTGGTAAAAACCATCACAAT","","","26282","MAAELNFLDLFLKASIVVQLVILILIIFSITSWAIIIQRSRVLTKALKESMAFEDRFWSGEDLNKLYEGLSNRRDGLTGSEQIFYVGFKEFSRLKQANPDAPEAIIQGSTRAMNLSMNREIEDLETRVPFLATVASISPYIGLFGTVWGIMHAFLSLSGAKQATLQMVAPGIAEALIATAIGLFAAIPAVMAYNRLSLRVNKLEQNYGNFIDEFTTILHRQVFGKNHHN","1991752","","colicin transport protein","Inner membrane, Cytoplasm","","
InterPro
IPR002898
Family
MotA/TolQ/ExbB proton channel
PF01618\"[74-212]TMotA_ExbB
InterPro
IPR014163
Family
Tol-Pal system, TolQ
TIGR02796\"[6-220]TtolQ: protein TolQ
noIPR
unintegrated
unintegrated
signalp\"[1-34]?signal-peptide
tmhmm\"[16-36]?\"[128-148]?\"[167-187]?transmembrane_regions


","BeTs to 14 clades of COG0811COG name: Biopolymer transport proteinsFunctional Class: NThe phylogenetic pattern of COG0811 is --m----q-d---cefghsnujxi--Number of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-21) to 2/2 blocks of the IPB002898 family, which is described as \"MotA/TolQ/ExbB proton channel family\". Interpro entry for IP:IPR002898. IPB002898A 138-154 6.3e-12 IPB002898B 172-186 4.4e-08","Residues 128 to 193 match (1e-08) PD:PD400673 which is described as PROTEOME COMPLETE BIOPOLYMER TRANSMEMBRANE EXBB-LIKE MEMBRANE INNER EXBB EXBB2 HOMOLOG ","","","","","","","","","","","","Tue Jan 21 18:23:13 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02836 is paralogously related to AA01124 (6e-08).","","","","","","Residues 74 to 212 (E-value = 1.1e-61) place AA02836 in the MotA_ExbB family which is described as MotA/TolQ/ExbB proton channel family (PF01618)","","","","","Sen K, Sikkema DJ, Murphy TF.Isolation and characterization of the Haemophilus influenzae tolQ, tolR, tolA and tolB genes.Gene. 1996 Oct;178(1-2):75-81.PMID: 8921895Sun TP, Webster RE.Nucleotide sequence of a gene cluster involved in entry of E colicins and single-stranded DNA of infecting filamentous bacteriophages into Escherichia coli.J Bacteriol. 1987 Jun;169(6):2667-74.PMID: 3294803Kampfenkel K, Braun V.Membrane topologies of the TolQ and TolR proteins of Escherichia coli: inactivation of TolQ by a missense mutation in the proposed first transmembrane segment.J Bacteriol. 1993 Jul;175(14):4485-91.PMID: 8331075Vianney A, Lewin TM, Beyer WF, Lazzaroni JC, Portalier R, Webster RE.Membrane topology and mutational analysis of the TolQ protein of Escherichia coli required for the uptake of macromolecules and cell envelope integrity.J Bacteriol. 1994 Feb;176(3):822-9.PMID: 8300535","","Tue Jan 21 18:23:13 2003","1","","","" "AA02837","1993037","1992636","402","TTGGAGCAAAAAGCTTTTTACTATTCCGCCCGTGTTTATTATGAAGATACCGATGCCGGTGGCGTAGTTTATCACGCACGCTATTTACATTTTTTGGAGCGTGCAAGAACAGAATGTTTAAGAGAATTTAATTTTTCCCAACAAACGTTGTTAAATGAGAATAAAGGCGCTTTCGTCGTTAAATCAATGAACATTGATTATTGTGTTGCGGCGAGATTAGACGATTTGTTACAAGTGGAAACTGCTGTAACCGAGCTAAAAGGCGCTTCAATTATTTTTTCTCAAACGATTAAGCGGGATGATGTCCTTTTATGTCGGGCTACCGTCAAGGTAGCCTATGTTGATCTTGGTAAGATGAAACCGGTGGCAATTCCGCAGAAAATCAAGACAATGTTAATCAAG","","","15319","LEQKAFYYSARVYYEDTDAGGVVYHARYLHFLERARTECLREFNFSQQTLLNENKGAFVVKSMNIDYCVAARLDDLLQVETAVTELKGASIIFSQTIKRDDVLLCRATVKVAYVDLGKMKPVAIPQKIKTMLIK","1992471","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR006683
Domain
Thioesterase superfamily
PF03061\"[20-106]T4HBT
InterPro
IPR006684
Family
4-hydroxybenzoyl-CoA thioesterase
TIGR00051\"[9-125]TTIGR00051: conserved hypothetical protein
InterPro
IPR008272
Active_site
4-hydroxybenzoyl-CoA thioesterase, active site
PS01328\"[11-28]T4HBCOA_THIOESTERASE
InterPro
IPR014166
Family
Pol-Pal system-associated acyl-CoA thioesterase
TIGR02799\"[6-131]Tthio_ybgC: tol-pal system-associated acyl-C
noIPR
unintegrated
unintegrated
G3DSA:3.10.129.10\"[6-132]Tno description


","BeTs to 15 clades of COG0824COG name: Predicted thioesteraseFunctional Class: RThe phylogenetic pattern of COG0824 is -omp-z-q-dr-bcefghsnuj--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 5.7e-24) to 1/1 blocks of the IPB000365 family, which is described as \"4-hydroxybenzoyl-CoA thioesterase family active site\". Interpro entry for IP:IPR000365. IPB000365 11-40 5.6e-24","Residues 76 to 125 match (1e-12) PD:PD474726 which is described as PROTEOME COMPLETE YBGC HYDROLASE PM0971 STY0790 PA0968 HI0386 ESTERASE ORF1 ","","","","","","","","","","","","Tue Jan 21 18:21:06 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02837 is paralogously related to AA01188 (2e-04).","","","","","","Residues 20 to 107 (E-value = 2e-17) place AA02837 in the 4HBT family which is described as Thioesterase superfamily (PF03061)","","","","","","","","1","","","" "AA02838","1993431","1993156","276","ATGATTAACTCATTGTACCAATCAGTAAATAAGGGTTCGTTTCGAACCCTTTCATTTATTTTAGCTCTAATACTCACGATATTTTTCTTTTTCAATGTCAATCAATTTGCCACACAACTAAGAGCGGTCGAATTTTATTACGTTTTTGGTTTGATTTGGGGAACGATAGTCCTATGGATTCACGGCATTGGATTTGAAATTCGGCTAAGCTTATGGCGTGTGATTTTCATGCCTTGGATTGGTTATATTGCGGGGATCGGTGCGCTCCTGCATAAT","","","10693","MINSLYQSVNKGSFRTLSFILALILTIFFFFNVNQFATQLRAVEFYYVFGLIWGTIVLWIHGIGFEIRLSLWRVIFMPWIGYIAGIGALLHN","","","conserved hypothetical protein","Inner membrane, Cytoplasm","This sequence is similar to gi15602837, a predicted unknown from Pasteurella multocida. Also see gi33152789 from Haemophilus ducreyi.","
InterPro
IPR005829
Family
Sugar transporter superfamily
PS00217\"[48-73]?SUGAR_TRANSPORT_2
noIPR
unintegrated
unintegrated
PD414257\"[11-83]TQ9CM66_PASMU_Q9CM66;
signalp\"[1-35]?signal-peptide
tmhmm\"[15-35]?\"[45-65]?\"[70-90]?transmembrane_regions


","No hits to the COGs database.","","Residues 5 to 90 match (1e-11) PD:PD414257 which is described as PROTEOME COMPLETE LIPOPROTEIN MEMBRANE YBGE PM0972 INNER VC1841 YPO1119 ","Mon Mar 24 15:26:46 2003","","","Mon Mar 24 16:14:51 2003","Mon Mar 24 16:14:51 2003","","","Mon Mar 24 16:14:51 2003","Mon Mar 24 16:14:51 2003","Mon Mar 24 15:26:46 2003","Mon Mar 24 15:26:46 2003","Thu Feb 26 17:14:59 2004","Thu Feb 26 17:15:57 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No sequence paralogous to this sequence was found.AA02838 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 26 17:15:57 2004","","","","","","","","","","","","Thu Feb 26 17:14:59 2004","1","","","" "AA02839","1993534","1993439","96","ATGTTCTATGTTATCTGGGTATTTGGTGTTTTGTTAGCCATTATGCTAAGTGTGGTTGTGACCATTAGTATTGAAAAGACAGGTAAATTTGACGAG","","","3632","MFYVIWVFGVLLAIMLSVVVTISIEKTGKFDE","1993439","","hypothetical protein","Cytoplasm, Periplasm","There are no significant similarities to the NR database.","
InterPro
IPR012994
Family
Membrane bound YbgT-like
PF08173\"[1-28]TYbgT_YccB
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide
tmhmm\"[4-24]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:10:04 2004","Mon Feb 23 15:10:04 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02839 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:10:04 2004","","","","","","","","","","","","","1","","","" "AA02840","1994682","1993549","1134","ATGTTTGATTATGAATTTCTACGTTTTGTATGGTGGATCCTAGTTTGCGTATTGCTTATTGGATTTGCCGTTACCGATGGTTTTGATATGGGCGTTTTAAGCCTATTACCTTTTACCGGTAAAAAAGAAGTTGAAAAGCGTATTATGATTAATACTATCGCGCCGCACTGGGATGGTAACCAAGTTTGGTTGCTAACTGCCGGTGGAGCAATGTTTGCTGCATGGCCGTTAGTCTATGCAACCTCATTCTCCGGTTTCTTTATTGCGATGATTTTAGTGTTAGCCGCCTTATTTTTCCGTCCTGTCGGTTTTGAATATCGTGCCAAAATTGATAATCCAACCTGGCGTAAGGCATGGGATTGGGGGTTGTTTATCGGTGGATTTGTTCCGTCCTTGGTATTCGGTGTAGCATTTGGTAACTTATTACAGGGTGTTCCGTTTGAATTCAATGAGTTACAACAGGTGCAATACACCGGTACATTCTTTGGGTTGTTAAATCCGTTTGCATTGCTTTGTGGTGTAATCAGTTTGGCAATGTTAACCACCCATGGTGCGAACTGGCTGCAAATGAAAACCACGTCAGAATTGCGTGCACGCGCTTGCGTGATTTCTCAGGTGGGTGCAACCGTGACATTAATCGCCTTTGTGTTGGCAGGTGTATGGTTATCTTTCAAAGATGGTTTTGTTGTCACCAGTGTGATTGATCACAACGCGCCTTCCAATCCGATTGGTAAAGAAGTGGCAGTACAAGCCGGTGCCTGGTTTAACAACTATAAAGAAATGCCGATTTTATGGTTATTCCCGGTATTGGCTGTAGGGGGAGCATTGCTTAACGCAATATTCTCGAAAGCAAATCGTTGTGGTTTTGCCTTCTTGTTCTCATCATTAACCATGGCCGGTGTGATTTTAACCGCTGCAATTGCTATGTTCCCATTTGTGATGCCATCCATTTCTCATCCGGAAATGAGTTTATTAATGTGGGATGCTACTTCAAGTAAATTAACCTTAACATTAATGTTCTTCTTGTCATTAATTTTTGTGGTGATTCTGCTTTCTTATACCATTTGGGCCTATTACAAAATGTTTGGTCGCATTGATAGCAGTTTCATTGAAGAAAACAAAAACTCACTATAT","","","42115","MFDYEFLRFVWWILVCVLLIGFAVTDGFDMGVLSLLPFTGKKEVEKRIMINTIAPHWDGNQVWLLTAGGAMFAAWPLVYATSFSGFFIAMILVLAALFFRPVGFEYRAKIDNPTWRKAWDWGLFIGGFVPSLVFGVAFGNLLQGVPFEFNELQQVQYTGTFFGLLNPFALLCGVISLAMLTTHGANWLQMKTTSELRARACVISQVGATVTLIAFVLAGVWLSFKDGFVVTSVIDHNAPSNPIGKEVAVQAGAWFNNYKEMPILWLFPVLAVGGALLNAIFSKANRCGFAFLFSSLTMAGVILTAAIAMFPFVMPSISHPEMSLLMWDATSSKLTLTLMFFLSLIFVVILLSYTIWAYYKMFGRIDSSFIEENKNSLY","1993384","[FUNCTION] Cytochrome D terminal oxidase complex is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. ","cytochrome D ubiquinol oxidase, subunit II","Inner membrane, Cytoplasm","","
InterPro
IPR003317
Family
Cytochrome bd ubiquinol oxidase, subunit II
PF02322\"[5-366]TCyto_ox_2
TIGR00203\"[1-378]TcydB: cytochrome d ubiquinol oxidase, subun
noIPR
unintegrated
unintegrated
signalp\"[1-27]?signal-peptide
tmhmm\"[10-28]?\"[79-99]?\"[120-142]?\"[161-181]?\"[202-222]?\"[263-281]?\"[291-313]?\"[336-356]?transmembrane_regions


","No hits to the COGs database.","Significant hit (6.6e-148) to 6/6 blocks of the IPB003317 family, which is described as \"Cytochrome bd ubiquinol oxidase, subunit II\". Interpro entry for IP:IPR003317. IPB003317A 3-42 4.1e-30 IPB003317B 43-60 5.8e-15 IPB003317C 72-106 8.4e-32 IPB003317D 112-143 1.2e-27 IPB003317E 158-174 1.4e-09 IPB003317F 323-365 6.8e-28","Residues 23 to 117 match (3e-44) PD:PD558660 which is described as PROTEOME COMPLETE CYTOPLASMIC YEBC MG332 ORF GLUCOSE-1-PHOSPHATE RC0681 SIMILAR VMA7-RPS31A ","","","","","","","","","","","Tue Jan 21 18:19:12 2003","Tue Jan 21 18:19:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02840 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 366 (E-value = 3.6e-195) place AA02840 in the Cyto_ox_2 family which is described as Cytochrome oxidase subunit II (PF02322)","","","","","Green GN, Fang H, Lin RJ, Newton G, Mather M, Georgiou CD, Gennis RB.The nucleotide sequence of the cyd locus encoding the two subunits of the cytochrome d terminal oxidase complex of Escherichia coli.J Biol Chem. 1988 Sep;263(26):13138-43.PMID: 2843510Bebbington KJ, Williams HD.A role for DNA supercoiling in the regulation of the cytochrome bd oxidase of Escherichia coli.Microbiology. 2001 Mar;147(Pt 3):591-8.PMID: 11238966Cotter PA, Melville SB, Albrecht JA, Gunsalus RP.Aerobic regulation of cytochrome d oxidase (cydAB) operon expression in Escherichia coli: roles of Fnr and ArcA in repression and activation.Mol Microbiol. 1997 Aug;25(3):605-15.PMID: 9302022Muller MM, Webster RE.Characterization of the tol-pal and cyd region of Escherichia coli K-12: transcript analysis and identification of two new proteins encoded by the cyd operon.J Bacteriol. 1997 Mar;179(6):2077-80.PMID: 9068659Muller MM, Webster RE.Characterization of the tol-pal and cyd region of Escherichia coli K-12: transcript analysis and identification of two new proteins encoded by the cyd operon.J Bacteriol. 1997 Mar;179(6):2077-80.PMID: 9068659","","Mon Mar 24 16:31:11 2003","1","","","" "AA02841","1996262","1994700","1563","ATGTTAGACGTTGTTGAACTCTCAAGACTGCAGTTTGCTTTGACTGCATTATATCACTTCATATTTGTGCCATTAACGTTAGGGATGACTTTTCTGTTGGCTATCATGGAAACACTTTATGTCGTCACAAATAAAGAAGTTTATAAAGATATGACCAAATTCTGGGGTAAGTTATTTGGTATTAACTTTGCGCTGGGCGTAACCACCGGCGTTACAATGGAATTTGAATTCGGCACTAACTGGTCATATTATTCTCATTATGTGGGAGATATTTTCGGCGCACCTCTTGCCATTGAAGCGTTGTTAGCCTTTTTCTTGGAATCTACTTTTGTCGGCCTTTTCTTTTTTGGATGGGATCGTTTAAGTAAAGGTAAACACCTTTTGGCAACTTACTGTGTTGCGTTCGGTTCAAATCTTTCCGCCATGTGGATTCTAGTGGCAAACGGCTGGATGCAATCTCCGGTCGGTTCCGAATTTAACTTTGAAACCATGCGGATGGAAATGACCAGTTTCATGGATTTGTGGTTGAATCCGATTGCGCAAAGTAAATTCTTACACACTTTATCCGCCGGTTATGTTTCCGCTGCATTCTTTGTATTAGCAATCAGCTCTTACTATTTACTGAAAGGTCGCGATATTGGTTTTGCCAAACGTTCGTTCTCTGTTGCTTCTACTTTCGGTATTATCTCTGTGGTTTCCTTGTTAATCATGGGGGACGAATCCGGTTATGAAATCGGCTACGCACAGCCGACTAAGTTGGCTGCAATGGAAGGCGAATGGCATACCCAGCCGGCTCCGGCAGCCTGGAATATGATTATTGTTCCAAATCAAGCAGAGCAGAAAAATGATTTCTCCTTGCAAATTCCATATATAGCAGGGGTTATTGTTACCCGTTCATTTGACAAACAATTCAGTGGTTTGATCGATTTGCAAGAACGTAATCTTGAACGTGTGCGTAGTGGTATCCAGGCCTATGCCTTATTGCAACAACTGAGAGAGGAGAAAAAGGCAAATGGTCAGGCAAGTGAAGAAACAAAAGCGAAATTTGATAAAGTACAAAAAGATTTAGGTTTCGGCTTATTGTTAAAACGTTATACCGATAACGTGGTTGATGCTACTGAAGAACAAATTAAACAGGCAGCAGCAGATACAATTCCTAAAGTAGCACCGACATTCTGGTCTTTCCGTGTGATGATGGCTACCGGTGGTGCGATTTTACTGCTAATGCTGCTTGCCTTTGTACAAAATGTTCGTAAAACCGTAGGCAGTCGTCCGTTATTATTAAAAGCATTATTGTGGGGGTTGCCACTGCCGTGGATTGGTATTGAGTGCGGTTGGTTTTTGGCGGAATATGGTCGTCAACCTTGGGCGATTTATGAAGTATTGCCGGTAGGTGTTTCTGCTTCCAAGCTTGCGCCGGGTGATTTGTGGTTCTCTATCGGTTTGATTTGTGCGTTATATACCTTATTCCTCGTCGTAGAAATGTACTTAACGTTTAAATACGGAAGATTAGGTCCAAGTGCATTAAAAACCGGCCGTTATTATTTCGAACAATCCTCTAAA","","","58462","MLDVVELSRLQFALTALYHFIFVPLTLGMTFLLAIMETLYVVTNKEVYKDMTKFWGKLFGINFALGVTTGVTMEFEFGTNWSYYSHYVGDIFGAPLAIEALLAFFLESTFVGLFFFGWDRLSKGKHLLATYCVAFGSNLSAMWILVANGWMQSPVGSEFNFETMRMEMTSFMDLWLNPIAQSKFLHTLSAGYVSAAFFVLAISSYYLLKGRDIGFAKRSFSVASTFGIISVVSLLIMGDESGYEIGYAQPTKLAAMEGEWHTQPAPAAWNMIIVPNQAEQKNDFSLQIPYIAGVIVTRSFDKQFSGLIDLQERNLERVRSGIQAYALLQQLREEKKANGQASEETKAKFDKVQKDLGFGLLLKRYTDNVVDATEEQIKQAAADTIPKVAPTFWSFRVMMATGGAILLLMLLAFVQNVRKTVGSRPLLLKALLWGLPLPWIGIECGWFLAEYGRQPWAIYEVLPVGVSASKLAPGDLWFSIGLICALYTLFLVVEMYLTFKYGRLGPSALKTGRYYFEQSSK","1994535","[FUNCTION] C.ytochrome d terminal oxidase complex is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration.[PATHWAY] Respiratory chain; terminal step.","cytochrome D ubiquinol oxidase, subunit I","Inner membrane, Cytoplasm","","
InterPro
IPR002585
Family
Cytochrome bd ubiquinol oxidase, subunit I
PF01654\"[7-516]TBac_Ubq_Cox
noIPR
unintegrated
unintegrated
signalp\"[1-28]?signal-peptide
tmhmm\"[14-34]?\"[55-77]?\"[83-117]?\"[127-147]?\"[188-208]?\"[220-238]?\"[392-414]?\"[429-449]?\"[475-493]?transmembrane_regions


","No hits to the COGs database.","Significant hit (8.4e-274) to 10/10 blocks of the IPB002585 family, which is described as \"Cytochrome bd ubiquinol oxidase, subunit I\". Interpro entry for IP:IPR002585. IPB002585A 5-41 9e-34 IPB002585B 42-66 6.7e-20 IPB002585C 70-99 6.2e-29 IPB002585D 100-145 1.1e-41 IPB002585E 149-187 1.4e-32 IPB002585F 193-234 3.8e-23 IPB002585G 237-286 3.6e-33 IPB002585H 287-317 6.9e-11 IPB002585I 380-402 3.6e-12 IPB002585J 426-464 1.8e-27","Residues 419 to 507 match (2e-28) PD:PD344108 which is described as SUBUNIT I CYTOCHROME PROTEOME COMPLETE OXIDASE D UBIQUINOL OXIDOREDUCTASE 1.10.3.- ","","","","","","","","","","","Tue Jan 21 18:13:13 2003","Tue Jan 21 18:13:13 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02841 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 7 to 516 (E-value = 2.2e-302) place AA02841 in the Bac_Ubq_Cox family which is described as Bacterial Cytochrome Ubiquinol Oxidase (PF01654)","","","","","Green GN, Fang H, Lin RJ, Newton G, Mather M, Georgiou CD, Gennis RB.The nucleotide sequence of the cyd locus encoding the two subunits of the cytochrome d terminal oxidase complex of Escherichia coli.J Biol Chem. 1988 Sep;263(26):13138-43.PMID: 2843510Bebbington KJ, Williams HD.A role for DNA supercoiling in the regulation of the cytochrome bd oxidase of Escherichia coli.Microbiology. 2001 Mar;147(Pt 3):591-8.PMID: 11238966Cotter PA, Melville SB, Albrecht JA, Gunsalus RP.Aerobic regulation of cytochrome d oxidase (cydAB) operon expression in Escherichia coli: roles of Fnr and ArcA in repression and activation.Mol Microbiol. 1997 Aug;25(3):605-15.PMID: 9302022Muller MM, Webster RE.Characterization of the tol-pal and cyd region of Escherichia coli K-12: transcript analysis and identification of two new proteins encoded by the cyd operon.J Bacteriol. 1997 Mar;179(6):2077-80.PMID: 9068659","","Tue Dec 2 13:58:16 2003","1","","","" "AA02842","1996714","1997022","309","ATGACAAACAAAATAACCGGAATTCTAACCGCACTTTGCATGGCAATCACTGTCAACAACGTTGCAAATGCTGCTCAAAACGATAAAAAAGCAGTAGAAATGCCAAAGCAGTGCAAAGATTTATTTAGTGAAGCCGAAAATTTAATTGCCGAAGCGGAAAGACAGCCCGGTACACATACCCAAGTAAATAAAATCAGGAGTAAGTTAAATCAAAGCAAAAAGCAAATCTTGGAAATGGAATTGGCAACACAAATCAAAAGTTGTAATGTGGCATTAGCTAAACTCACCAGCATGAAACAACAGCAACAG","","","11384","MTNKITGILTALCMAITVNNVANAAQNDKKAVEMPKQCKDLFSEAENLIAEAERQPGTHTQVNKIRSKLNQSKKQILEMELATQIKSCNVALAKLTSMKQQQQ","1996857","","conserved hypothetical protein","Periplasm, Extracellular","","
noIPR
unintegrated
unintegrated
PD065628\"[34-99]TY310_HAEIN_P43982;
signalp\"[1-24]?signal-peptide


","No hits to the COGs database.","","Residues 34 to 99 match (1e-14) PD:PD065628 which is described as COMPLETE PROTEOME PM0975 SIGNAL PRECURSOR HI0310 ","","","","","","","","","","","","Tue Jan 21 17:50:57 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02842 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02844","1997945","1997082","864","TTGCGTCAGGATGCGTTGGATCATTTGCTGATTTTTGGCCCGCCGGGTTTGGGAAAAACCACCTTGGCAAATATTGTTGCCAATGAAATGGGCGTAAATATTCGCACTACGTCAGGCCCCGTGCTGGAAAAAGCGGGGGATTTGGCGGCAATGTTGACCAATCTGGAGCCTCATGATGTGTTGTTTATTGATGAAATTCATCGTCTTTCTCCGGCGATTGAAGAAGTGCTTTATCCGGCAATGGAAGATTATCAGCTTGATATTATGATTGGCGAAGGGCCGGCAGCGCGTTCTATTAAATTGGATTTACCTCCTTTTACGCTTATCGGTGCAACCACCCGTGCGGGCTCTTTAACCTCTCCGTTGCGCGATCGTTTTGGTATTGTGCAGCGTTTGGAATTTTATTCCGTGTCGGATTTAACTTCTATTGTGTCCAGAAGTGCGGTCTGTTTACAGCTTAAAATTAACGATACAGCAGCTTATGAAATCGCCCGCCGTTCTCGCGGCACGCCACGGATTGCCAATCGGTTATTACGTCGGGTGCGTGATTATGCTGATGTGCGTAACAATGGCATGATTAGTGAAGAGATTGCTAAAGCAGCGCTATCCATGCTGGATATTGATGATGCGGGGTTTGACTACTTAGACAGAAAATTGCTTACGGCAGTTTTGGAGCGCTTTGACGGTGGTCCGGTCGGTTTGGATAATTTGGCGGCGGCAATTGGGGAAGAGCGGGATACCATTGAAGACGTATTGGAACCATACTTAATTCAACAGGGTTTTTTACAGCGAACCTCAAGGGGGCGAATTGCTACACTCACCACATATCGCCATTTTGGTATTGAGAAAATTACTCGCGAAGAT","","","37625","LRQDALDHLLIFGPPGLGKTTLANIVANEMGVNIRTTSGPVLEKAGDLAAMLTNLEPHDVLFIDEIHRLSPAIEEVLYPAMEDYQLDIMIGEGPAARSIKLDLPPFTLIGATTRAGSLTSPLRDRFGIVQRLEFYSVSDLTSIVSRSAVCLQLKINDTAAYEIARRSRGTPRIANRLLRRVRDYADVRNNGMISEEIAKAALSMLDIDDAGFDYLDRKLLTAVLERFDGGPVGLDNLAAAIGEERDTIEDVLEPYLIQQGFLQRTSRGRIATLTTYRHFGIEKITRED","1996917","[FUNCTION] The ruvA-ruvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is an helicase that mediates the holliday junction migration by localized denaturation and reanneling. RuvA stimulates, in the presence of DNA, the weak atpase activity of ruvB. Binds both single-and double-stranded DNA (dsDNA. Binds preferentially to supercoiled rather than to relaxeddsDNA. ","Holliday junction DNA helicase","Cytoplasm","","
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[5-132]TAAA
InterPro
IPR003959
Domain
AAA ATPase, core
PF00004\"[8-187]TAAA
InterPro
IPR004605
Family
Holliday junction DNA helicase RuvB
TIGR00635\"[1-281]TruvB: Holliday junction DNA helicase RuvB
InterPro
IPR008823
Domain
Holliday junction DNA helicase RuvB, C-terminal
PF05491\"[204-282]TRuvB_C
InterPro
IPR011991
Domain
Winged helix repressor DNA-binding
G3DSA:1.10.10.10\"[211-283]Tno description
noIPR
unintegrated
unintegrated
G3DSA:1.10.8.60\"[135-210]Tno description
G3DSA:3.40.50.300\"[1-135]Tno description
PTHR13779\"[2-288]THOLLIDAY JUNCTION DNA HELICASE RUVB-RELATED
PTHR13779:SF2\"[2-288]THOLLIDAY JUNCTION DNA HELICASE RUVB


","No hits to the COGs database.","Significant hit ( 1.1e-07) to 3/8 blocks of the PR00819 family, which is described as \"CbxX/CfqX superfamily signature\". Prints database entry for PR:PR00819. PR00819B 8-23 2.9e-05 PR00819D 48-67 51 PR00819G 121-140 21Significant hit ( 5.5e-05) to 2/3 blocks of the IPB002464 family, which is described as \"ATP-dependent helicase, DEAH-box\". Interpro entry for IP:IPR002464. IPB002464A 13-27 0.28 IPB002464B 57-70 0.11","Residues 29 to 71 match (4e-14) PD:PD582814 which is described as DNA HELICASE PROTEOME RECOMBINATION COMPLETE ATP-BINDING HOLLIDAY JUNCTION RESPONSE SOS ","","","","","","","","","","","Tue Jan 21 17:48:45 2003","Wed Feb 5 13:43:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02844 is paralogously related to AA02728 (2e-08) and AA02395 (3e-06).","","","","","","Residues 204 to 282 (E-value = 3.7e-51) place AA02844 in the RuvB_C family which is described as Holliday junction DNA helicase ruvB C-terminus (PF05491)","","","","","Tsaneva IR, Muller B, West SC.RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro.Proc Natl Acad Sci U S A. 1993 Feb;90(4):1315-9.PMID: 8433990West SC.Processing of recombination intermediates by the RuvABC proteins.Annu Rev Genet. 1997;31:213-44.PMID: 9442895Benson FE, Illing GT, Sharples GJ, Lloyd RG.Nucleotide sequencing of the ruv region of Escherichia coli K-12 reveals a LexA regulated operon encoding two genes.Nucleic Acids Res. 1988 Feb;16(4):1541-9.PMID: 3279394Shinagawa H, Makino K, Amemura M, Kimura S, Iwasaki H, Nakata A.Structure and regulation of the Escherichia coli ruv operon involved in DNA repair and recombination.J Bacteriol. 1988 Sep;170(9):4322-9.PMID: 2842314","","Tue Jan 21 17:50:06 2003","1","","","" "AA02845","1998721","1998110","612","ATGATTGGTCATCTCACCGGTATTTTAATGGAAAAACAGCCGCCGGAAATTTTGTTGGATGTGCAAGGTATCGGCTATGAGCTACTGCTGCCGATGACAAGTTTTTATAACTTGCCGGAAGTAGGCAAACAAACTTGTTTATTTACTCATCTGGTGGTACGTGAGGATGCCCATTTGTTGTTTGGATTTGCTCAAAAAGCCGACCGCACTTTATTCCGCGAACTGATAAAAACCAATGGTGTCGGGCCCAAATTGGCGCTGGCAATTTTATCGGCCATGTCGGTAGATGAATTTGCTTATGCTATTGAACGCGAGGAACTCTCCCGTTTGGTAAAAATTCCCGGTATCGGCAAGAAAACCGCCGAACGGTTATTGGTGGAGTTAAAAGGTAAATTTAAAGAAGTAAAAACAAACGACTTCTTCGTGCAGGCGGATCATTTACCTCGTTTTAGTACGGAAATATCGGCGACGGTTGAACCGTCCAACGAAGCGGTAGCGGCGCTCGTGGCATTAGGTTATAAACCGTTAGACGCGGAAAAAATGGTGAAGAAAGTTTCCAAACCTGAACTTTCCAGCGAACAGATCATTCGTGAAGCTCTGAAAGCGGCATTA","","","22619","MIGHLTGILMEKQPPEILLDVQGIGYELLLPMTSFYNLPEVGKQTCLFTHLVVREDAHLLFGFAQKADRTLFRELIKTNGVGPKLALAILSAMSVDEFAYAIEREELSRLVKIPGIGKKTAERLLVELKGKFKEVKTNDFFVQADHLPRFSTEISATVEPSNEAVAALVALGYKPLDAEKMVKKVSKPELSSEQIIREALKAAL","1997945","[FUNCTION] The ruvA-ruvB complex in the presence of ATP renatures cruciform structure in supercoiled dna with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is an helicase that mediates the holliday junction migration by localized denaturation and reanneling. RuvA stimulates, in the presence of DNA, the weak atpase activity of ruvB. Binds both single-and double-stranded DNA (dsDNA. Binds preferentially to supercoiled rather than to relaxed dsDNA. ","Holliday junction DNA helicase","Cytoplasm","","
InterPro
IPR000085
Family
Bacterial DNA recombination protein RuvA
TIGR00084\"[1-204]TruvA: Holliday junction DNA helicase RuvA
InterPro
IPR003583
Domain
Helix-hairpin-helix DNA-binding, class 1
SM00278\"[73-92]T\"[108-127]THhH1
InterPro
IPR011114
Domain
RuvA, domain III
PF07499\"[159-204]TRuvA_C
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[1-66]Tno description
InterPro
IPR013849
Domain
Bacterial DNA recombination protein RuvA, domain I
PF01330\"[1-62]TRuvA_N
InterPro
IPR013850
Domain
Bacterial DNA recombination protein, RuvA, central
PD006268\"[72-133]TRUVA_PASMU_P57893;
noIPR
unintegrated
unintegrated
G3DSA:1.10.150.20\"[67-158]Tno description


","BeTs to 17 clades of COG0632COG name: Holliday junction resolvasome DNA-binding subunitFunctional Class: LThe phylogenetic pattern of COG0632 is --------vdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 5.2e-59) to 5/5 blocks of the IPB000085 family, which is described as \"Bacterial DNA recombination protein, RuvA\". Interpro entry for IP:IPR000085. IPB000085A 1-10 0.052 IPB000085B 47-88 1.2e-30 IPB000085C 110-129 8.2e-14 IPB000085D 163-173 4.1e-05 IPB000085E 196-201 0.2","","","","","","","","","","","","Tue Jan 21 17:44:27 2003","Wed Feb 5 13:42:56 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02845 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 62 (E-value = 6.4e-27) place AA02845 in the RuvA family which is described as RuvA N terminal domain (PF01330)","","","","","Shinagawa H, Makino K, Amemura M, Kimura S, Iwasaki H, Nakata A.Structure and regulation of the Escherichia coli ruv operon involved in DNA repair and recombination.J Bacteriol. 1988 Sep;170(9):4322-9.PMID: 2842314Tsaneva IR, Müller B, West SC.RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro.Proc Natl Acad Sci U S A. 1993 Feb;90(4):1315-9.PMID: 8433990Rafferty JB, Sedelnikova SE, Hargreaves D, Artymiuk PJ, Baker PJ, Sharples GJ, Mahdi AA, Lloyd RG, Rice DW.Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction.Science. 1996 Oct;274(5286):415-21.PMID: 8832889Nishino T, Ariyoshi M, Iwasaki H, Shinagawa H, Morikawa K.Functional analyses of the domain structure in the Holliday junction binding protein RuvA.Structure. 1998 Jan;6(1):11-21.PMID: 9493263Benson FE, Illing GT, Sharples GJ, Lloyd RG.Nucleotide sequencing of the ruv region of Escherichia coli K-12 reveals a LexA regulated operon encoding two genes.Nucleic Acids Res. 1988 Feb;16(4):1541-9.PMID: 3279394Takahagi M, Iwasaki H, Nakata A, Shinagawa H.Molecular analysis of the Escherichia coli ruvC gene, which encodes a Holliday junction-specific endonuclease.J Bacteriol. 1991 Sep;173(18):5747-53.PMID: 1885548","","Fri Jan 24 13:43:03 2003","1","","","" "AA02846","1999357","1998788","570","ATGAGCATTATTTTAGGCATTGACCCCGGTTCCCGTGTCACCGGTTATGGTGTGATTGGGCAAAACGGACGGCATTTGGAATATCTTGGCAGCGGCGCAATTCGCACCCAAGTAGAAGATTTGCCTACGCGCTTAAAGCGTATTTATGCCAGTGTAACGGAAATTATCACGCAATTTCAGCCCGATATGTTTGCCATTGAGCAAGTTTTTATGGCGAAAAATGCCGATTCGGCATTAAAACTGGGACAAGCCCGCGGTACGGCAATTGTGGCGGCGGTGAATCATAATTTGCCGGTATTTGAATATGCGGCACGCTTAATCAAGCAAACGGTGGTCGGTATCGGTTCTGCGGATAAAGTTCAAGTGCAGGAGATGGTCACCCGCATTCTTAAACTTTCCGATAAACCGCAAGCCGATGCGGCAGATGCCTTGGCGATCGCCATTACGCATGCCCATTCCATACAGCATTCTTTCCATGTGGCAAGTTCGGCCGGTCAAAACGAAACGCAGGAAAAACTGACCGCACTTTTACGCACTCGATACAGCCGGGGACGCTTTCACTTAAAAATT","","","20703","MSIILGIDPGSRVTGYGVIGQNGRHLEYLGSGAIRTQVEDLPTRLKRIYASVTEIITQFQPDMFAIEQVFMAKNADSALKLGQARGTAIVAAVNHNLPVFEYAARLIKQTVVGIGSADKVQVQEMVTRILKLSDKPQADAADALAIAITHAHSIQHSFHVASSAGQNETQEKLTALLRTRYSRGRFHLKI","1998623","[FUNCTION] Nuclease that resolves holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'terminal phosphate and a 3'terminal hydroxyl group (by similarity).","crossover junction endodeoxyribonuclease","Cytoplasm","","
InterPro
IPR002176
Family
Crossover junction endodeoxyribonuclease RuvC
PD008333\"[10-137]TRUVC_HAEIN_P44633;
PR00696\"[5-18]T\"[61-77]T\"[83-99]T\"[107-126]T\"[138-150]TRSOLVASERUVC
PF02075\"[4-150]TRuvC
TIGR00228\"[4-159]TruvC: crossover junction endodeoxyribonucle
PS01321\"[113-147]TRUVC
noIPR
unintegrated
unintegrated
G3DSA:3.30.420.10\"[2-159]Tno description


","BeTs to 15 clades of COG0817COG name: Holliday junction resolvasome endonuclease subunitFunctional Class: LThe phylogenetic pattern of COG0817 is --------vdr--cefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 5.5e-73) to 4/4 blocks of the IPB002176 family, which is described as \"Crossover junction endodeoxyribonuclease RuvC\". Interpro entry for IP:IPR002176. IPB002176A 4-15 3.4e-07 IPB002176B 55-100 6.1e-31 IPB002176C 101-128 4.7e-17 IPB002176D 129-150 8.1e-14","Residues 2 to 157 match (3e-64) PD:PD008333 which is described as RUVC JUNCTION HOLLIDAY DNA NUCLEASE RESOLVASE CROSSOVER ENDODEOXYRIBONUCLEASE PROTEOME RECOMBINATION ","","","","","","","","","","","Wed Feb 5 13:43:18 2003","Tue Jan 21 17:38:26 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02846 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 150 (E-value = 3.5e-96) place AA02846 in the RuvC family which is described as Crossover junction endodeoxyribonuclease RuvC (PF02075)","","","","","Sharples GJ, Lloyd RG.Resolution of Holliday junctions in Escherichia coli: identification of the ruvC gene product as a 19-kilodalton protein.J Bacteriol. 1991 Dec;173(23):7711-5.PMID: 1657895Takahagi M, Iwasaki H, Nakata A, Shinagawa H.Molecular analysis of the Escherichia coli ruvC gene, which encodes a Holliday junction-specific endonuclease.J Bacteriol. 1991 Sep;173(18):5747-53.PMID: 1885548Dunderdale HJ, Benson FE, Parsons CA, Sharples GJ, Lloyd RG, West SC.Formation and resolution of recombination intermediates by E. coli RecA and RuvC proteins.Nature. 354(6354):506-10.PMID: 1758493Ariyoshi M, Vassylyev DG, Iwasaki H, Nakamura H, Shinagawa H, Morikawa K.Atomic structure of the RuvC resolvase: a holliday junction-specific endonuclease from E. coli.Cell. 1994 Sep;78(6):1063-72.PMID: 7923356","","Wed Feb 5 13:43:18 2003","1","","","" "AA02847","1999823","1999416","408","ATGAAATTAGTAAAAACATTATCTGCTGTTGCAGTCATTGCGGTACTGTCCGCGTGTTCTGCTTCTAAGAAAGAACCACAACCGGTTAAATCGGAGAAAACTGTGGTTTATTCTTGTAAGAAAAGAACCGTTACCGTGACTTACCAATTTGAAAACCAAGAAGCCACTGAAGCGAAAGTTGTGATGCGCAAAAAGGTGATTGCGGAATCTCTTCCGGTGAGTAACGTCGATAAAGATTTCCCTTCATTTATTTCCGACAAATACATCTGGAGCGTTGACAGCGGGTTTTCATTAAATACGGCAACAGCAACCGATGGCGTAATGTTGACTCAACGCGGTAAGAAAGTGGATAGAATCTTGGCTAAAAATTGTAAAGTCAATGCAAAAGCCACAGCAAGAGCTAACCAA","","","14860","MKLVKTLSAVAVIAVLSACSASKKEPQPVKSEKTVVYSCKKRTVTVTYQFENQEATEAKVVMRKKVIAESLPVSNVDKDFPSFISDKYIWSVDSGFSLNTATATDGVMLTQRGKKVDRILAKNCKVNAKATARANQ","1999251","","conserved hypothetical protein","Periplasm, Outer membrane","","
noIPR
unintegrated
unintegrated
PD089635\"[28-124]TY246_HAEIN_P43972;
PS51257\"[1-19]TPROKAR_LIPOPROTEIN
signalp\"[1-21]?signal-peptide


","No hits to the COGs database.","","Residues 28 to 124 match (9e-17) PD:PD089635 which is described as COMPLETE PROTEOME PM0979 HI0246 SIGNAL PRECURSOR ","","","","","","","","","","","","Tue Jan 21 17:35:16 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02847 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02848","2000575","1999838","738","ATGGCAGGCCATAGTAAGTGGGCAAATATTAAACACCGTAAAGCGGCACAAGATGCTCAGCGCGGGAAAATTTTTACCAAATTAATTCGTGAATTGGTGACTGCCGCTAAAATCGGTGGCGGTGATGTTAGTTCTAACCCGCGTCTGCGTGCGGCGGTAGATAAAGCATTAAGCAATAATATGACCCGTGATACCATTAACCGTGCGATTGAGCGCGGCGTCGGCGGTGGCGATGATACCAACATGGAAACCCGCGTGTATGAAGGTTACGGTCCGGGCGGTGCGGCAGTGATGGTGGAATGTTTAAGCGATAACGCCAATCGCACTATTTCCCAAGTGCGCCCGAGTTTTACCAAATGTGGCGGTAACTTAGGCACCGAGGGTTCCGTGGGCTATTTGTTTAGTAAAAAAGGCTTGATTTTAGTGAATCAGGCGGATGAAGACGCTTTGATGGAAGCAGCAATTGAAGGCGGCGCAGACGATGTTCAGCCACAAGAAGACGGTTCCTTCGAAATTTATACCGCTTGGGAAGATTTGGGTTCTGTACGTGATGCCATTGAAGCGGCAGGGTTTAACGTTGAAAACGCGGAAGTGACAATGATTCCTTCCACTACAGTAGATTTGGATGCAGAAACTGCGCCGAAGCTACTACGTTTAATCGATATGTTAGAAGACTGTGATGATGTACAAAACGTATATCATAACGGTGAAATTAGTGATGAAATCGCAGCAATGCTA","","","26356","MAGHSKWANIKHRKAAQDAQRGKIFTKLIRELVTAAKIGGGDVSSNPRLRAAVDKALSNNMTRDTINRAIERGVGGGDDTNMETRVYEGYGPGGAAVMVECLSDNANRTISQVRPSFTKCGGNLGTEGSVGYLFSKKGLILVNQADEDALMEAAIEGGADDVQPQEDGSFEIYTAWEDLGSVRDAIEAAGFNVENAEVTMIPSTTVDLDAETAPKLLRLIDMLEDCDDVQNVYHNGEISDEIAAML","1999673","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR002876
Family
Protein of unknown function DUF28
PD004323\"[11-243]TY315_HAEIN_P44634;
PTHR12532\"[1-246]TUNCHARACTERIZED
PF01709\"[5-237]TDUF28
TIGR01033\"[1-237]TTIGR01033: conserved hypothetical protein T
InterPro
IPR003308
Domain
Integrase, N-terminal zinc-binding
G3DSA:1.10.10.200\"[1-81]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.30.1270.10\"[82-246]Tno description


","BeTs to 19 clades of COG0217COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG0217 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.2e-81) to 3/3 blocks of the IPB002876 family, which is described as \"Domain of unknown function DUF28\". Interpro entry for IP:IPR002876. IPB002876A 24-75 5.8e-29 IPB002876B 87-132 7.2e-32 IPB002876C 209-235 3e-18","","","","","","","","","","","","","Tue Jan 21 17:34:42 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02848 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 237 (E-value = 5.9e-152) place AA02848 in the DUF28 family which is described as Domain of unknown function DUF28 (PF01709)","","","","","","","","1","","","" "AA02850","2001055","2000612","444","ATGACCATATTGAAATACAAAAGTAATGAGTCGGTTCTGGTTGTGATCTCCGCCCAAAATAGTGGCAGGGTATTAATGCTGCAACGCTGCGATGATCCTGATTTCTGGCAGTCTGTAACGGGATCTCTGGAAGAAAATGAAACACCGCGACAAGCCGCAATTCGTGAGTTATGGGAAGAAATCGGGTTAAAAACGCCGTCAAAAACAACCGCACTTTTTGATTGCAACGAAAGCATAGCGTTTGAAATTTTCCCGCATTTCCGCTATAAATACGCACCGAATATCACCCATTGTCGCGAACATTGGTTTTTATTGGCGGTTGAGCAGGAATTTACCCCTAAATTAACGGAACATTTAGCGTTTCAATGGGTACCTGCCGAACAAGCTGCTGAAATGACAAAGTCGCCGAATAATGCGGAAGCAATAAAAAAATATTTATTGAAA","","","17119","MTILKYKSNESVLVVISAQNSGRVLMLQRCDDPDFWQSVTGSLEENETPRQAAIRELWEEIGLKTPSKTTALFDCNESIAFEIFPHFRYKYAPNITHCREHWFLLAVEQEFTPKLTEHLAFQWVPAEQAAEMTKSPNNAEAIKKYLLK","2000447","[FUNCTION] Hydrolysis of nucleoside triphosphates with a preference for datP (by similarity). ","dATP pyrophosphohydrolase","Cytoplasm","","
InterPro
IPR000086
Domain
NUDIX hydrolase
PR00502\"[36-50]T\"[50-65]TNUDIXFAMILY
G3DSA:3.90.79.10\"[5-145]Tno description
PF00293\"[8-148]TNUDIX
PS00893\"[41-62]TNUDIX
InterPro
IPR003564
Family
DATP pyrophosphohydrolase
PR01404\"[6-23]T\"[23-44]T\"[74-93]T\"[102-123]T\"[129-142]TNPPPHYDRLASE
noIPR
unintegrated
unintegrated
PTHR22769\"[14-77]T\"[93-147]TMUTT/NUDIX HYDROLASE


","BeTs to 17 clades of COG0494COG name: NTP pyrophosphohydrolases including oxidative damage repair enzymesFunctional Class: L,RThe phylogenetic pattern of COG0494 is aomp-zyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 4.3e-63) to 5/5 blocks of the PR01404 family, which is described as \"DATP pyrophosphohydrolase signature\". Prints database entry for PR:PR01404. PR01404A 6-23 6e-05 PR01404B 23-44 4.4e-19 PR01404C 74-93 1.4e-15 PR01404D 102-123 7.3e-11 PR01404E 129-142 1.1e-06Significant hit ( 2.3e-09) to 1/1 blocks of the IPB000086 family, which is described as \"NUDIX hydrolase\". Interpro entry for IP:IPR000086. IPB000086 36-62 2.3e-09","Residues 6 to 61 match (2e-14) PD:PD000653 which is described as COMPLETE PROTEOME HYDROLASE MUTT FAMILY MUTT/NUDIX MUTATOR 3.6.1.- MAGNESIUM PYROPHOSPHOHYDROLASE ","","","","","","","","","","","Tue Jan 21 17:27:32 2003","Tue Jan 21 17:27:32 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02850 is paralogously related to AA00204 (2e-05) and AA01085 (7e-05).","","","","","","Residues 8 to 148 (E-value = 1.5e-24) place AA02850 in the NUDIX family which is described as NUDIX domain (PF00293)","","","","","","","","1","","","" "AA02851","2001036","2001128","93","TTGTATTTCAATATGGTCATTCGTGTTATTGGAAATGAATGGCATAATACCTTGTCTTTAAAAAACTTTCAAAAAAATTACCGCACTTTACGG","","","3852","LYFNMVIRVIGNEWHNTLSLKNFQKNYRTLR","2001128","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:08:21 2004","Mon Feb 23 15:08:21 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02851 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:08:21 2004","","","","","","","","","","","","","1","","","" "AA02853","2002429","2001164","1266","ATGAGTGAAGTTTCAAATCTGGTAGAAAAATTCACTTGGGCGAGTAAATTTTCTGCCTTAGGTCCGGGCATTGTCATGGCGTCAGCTGCTGTCGGTGGTTCGCATATTATCGCTTCAACCCAAGCCGGTGCAATTTATGGTTGGGAGTTGGTGAGCATTGTTATCCTGGTTAATTTATTCAAATATCCTTTTTTCCGATTTGGTGTGCAATATACCTTGGATACGGGCAATACCTTGTTGGAAGGGTATCGCCAAAAAGGGCGTTTCTATTTGTGGTTATTTCTTATTTTAAATGTCTTTGCAACAGTCGTTAATACGGCAGCGGTGGGGTTATTAACTGCTGCGATTCTGATATTTATTACACCAATCCCTTTGCCAATGCCGGTGTTAAGTTCATTAGTCATTGTTATTACAACAGGGATTCTATTGTTAGGTAAATATCGTCTTTTAGACAGATTATCAAAAATCATCATGATTGCTTTAACCGTCACGACGGTGAGTGCAGTGGTGATTGCCGTTATGCGTAACGGAATGCAAGGCGTCGCACCGGCAGATTTTGTTGCGCCTTCGCCATGGGAATTGAGCAAATTAGCATTCTTAGTTGCACTCATGGGCTGGATGCCTGCCCCGATTGAAATCTCGGCGATTAATTCCATGTGGGTGGTTGCTAAACGTCGTTTGACCAAAGTGTCTTATCAGGACGGTTTGTTTGACTTTAACGTGGGGTATATCGGCACGGCGATTTTAGCGGTGGTGTTCCTGGCACTAGGCGCCTTAGTGCAATTTGGTTTGCCTGAAACCGTTGAAATGGTCGGCGGAAAATATATTGCACAACTTATTAATATGTATGCAAGCACCATCGGTGAATGGGCGCGTTTACTGATCGCAGTGATCGCCTTTATGTGCATGTTCGGCACAACTATCACCGTGATTGACGGTTATTCCCGCACTAACGTGGAATCTTTGCGTTTATTGCTCGGTAAACATGAGTGTTCGGTCAGAACCTTAAACATTTCCATGGTTTTGGCGGCGTTATCCGGTTTGGTGATTATTTTCTGTTTTAATAACGCTGTGGGTCCGATGCTCAAATTCGCAATGATCGCCTCGTTTGTTTCTGCCCCGGTTTTTGCCTGGCTAAATTTATCCTTAACCAAGAAGTCTAAGCACAGCGTGAAAGGCGGGTTATTGTGGTTGTCTTTTATTGGATTATTCTATTTAACCGCATTCGCTGCGTTATTCATCGCTCAACAAGCAGGCTGGCTAAGT","","","47319","MSEVSNLVEKFTWASKFSALGPGIVMASAAVGGSHIIASTQAGAIYGWELVSIVILVNLFKYPFFRFGVQYTLDTGNTLLEGYRQKGRFYLWLFLILNVFATVVNTAAVGLLTAAILIFITPIPLPMPVLSSLVIVITTGILLLGKYRLLDRLSKIIMIALTVTTVSAVVIAVMRNGMQGVAPADFVAPSPWELSKLAFLVALMGWMPAPIEISAINSMWVVAKRRLTKVSYQDGLFDFNVGYIGTAILAVVFLALGALVQFGLPETVEMVGGKYIAQLINMYASTIGEWARLLIAVIAFMCMFGTTITVIDGYSRTNVESLRLLLGKHECSVRTLNISMVLAALSGLVIIFCFNNAVGPMLKFAMIASFVSAPVFAWLNLSLTKKSKHSVKGGLLWLSFIGLFYLTAFAALFIAQQAGWLS","2000999","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
tmhmm\"[20-38]?\"[44-64]?\"[89-123]?\"[129-147]?\"[156-178]?\"[197-219]?\"[240-260]?\"[293-315]?\"[336-358]?\"[364-384]?\"[394-414]?transmembrane_regions


","BeTs to 6 clades of COG1914COG name: Mn2+ and Fe2+ transporters of the NRAMP familyFunctional Class: PThe phylogenetic pattern of COG1914 is ---p--y--drlb-ef--sn-j----Number of proteins in this genome belonging to this COG is","","Residues 12 to 419 match (5e-129) PD:PD322908 which is described as COMPLETE PROTEOME TRANSMEMBRANE METAL ION PLASMID INTEGRAL MEMBRANE SP0159 MS111 ","","","","","","","","","","","","Tue Jan 21 17:24:05 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02853 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02854","2002738","2002553","186","TTGGTTTTTTGTAAAGAAAGTGGGGCAGGGTGCGTTGGCATACATAAAAGTGCGGTAAAAAACATCGGCGTTTTTGACCGCACTTTTTTCATCAGAAAAATTTTATTCTCTGAGATAAATCGATTTTTTGGTATTATTGCCGGTTATTTATTTTTTATCTTAATATTATTTCCTGAAATTATTAAA","","","7041","LVFCKESGAGCVGIHKSAVKNIGVFDRTFFIRKILFSEINRFFGIIAGYLFFILILFPEIIK","2002388","","hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
tmhmm\"[39-57]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Tue Jan 21 17:22:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02854 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02856","2004599","2002824","1776","ATGATGCGTTCACATTATTGCGGTGCGTTAAATCGTACCAATATTGGCCAAGAGATAACCTTAAGCGGATGGGTTCATCGTCGCCGTGATTTAGGCGGTTTAATTTTTATTGATATGCGCGATCGTGAAGGCATCGTGCAAGTGTGTTTTGATCCGAAATATCAAAAAGCCTTAACCGCCGCTGCGGGTTTGCGTAACGAATTTTGTATTCAAATTCAAGGCGAAGTCATTGCCCGTCCGGATAATCAAATCAACAAAAATATGGCGACCGGTGAAGTGGAAGTGTTGGCAAAAGTGTTGAAAATTTACAATGCTTCCGATGTGTTACCGCTCGATTTCAACCAAAACAATACTGAAGAACAACGCCTAAAATATCGTTATTTGGATTTACGTCGCCCTGAAATGGCGCAGCATTTGAAAACCCGCGCGAAAATCACTGGTTTTGTGCGCCGCTTTATGGACGACAACGGTTTCTTGGATATTGAAACGCCGATGCTCACTAAAGCCACCCCGGAAGGCGCGCGCGACTATCTTGTGCCAAGCCGTGTGCATAAAGGCAAATTCTACGCGCTTCCGCAATCACCGCAGCTTTTCAAACAGCTTTTGATGATGTCCGGTTTTGATCGTTATTATCAAATCGTGAAATGCTTCCGCGATGAAGATTTACGCGCGGATCGTCAGCCGGAATTCACGCAGATTGATGTGGAAACTTCGTTCTTAACCGCGCCGGAGGTACGTGAAATCATGGAACGTATGGTGCACGGTTTGTGGCAGCATACTTTAGGTGTCGATTTGGGCAAATTCCCGGTGATAACCTGGCAAGAAGCGATGCGCCGTTTTGGTTCCGATAAACCGGATTTGCGCAATCCGTTAGAACTGGTGGACGTGGCAGATATTGTCAAAAACGTAGATTTCAAGATATTCCAAGGTCCGGCAAATGACCCGAATGGTCGTGTCACCTTAATTCGTGTGCCGCAGGGGAATGAAATCACCCGTAAACAAATTGATGAATATACCCAATTTGTCGGCATTTATGGTGCTAAAGGCTTGGCTTGGTTAAAAGTGAATGACGTAAACGCCGGTCTTGAAGGCGTCCAAAGCCCTATTGCAAAATTCTTAAATGAAGACGTGCTAAAAGCCTTGTTTGAACGCGTGGGCGCGCAAACTGGCGATATTTTATTCTTCGGTGCCGACAAATGGCAAACCGCCACAGATTCAATGGGCGCGTTACGTTTGAAATTAGGACGCGATCTCGGTTTAACCCGTTTAGATGAATGGCAACCGCTTTGGGTTATTGATTTTCCCATGTTTGAACGTGATGATGAAGGCTGCTTGACGGCAATGCACCACCCATTCACCTCGCCAAAAGATTTCACACCTGAACAATTAGAAGCGGATCCGACAAGTGCGGTCGCCAATGCTTACGATATGGTCATCAATGGTTATGAAGTGGGTGGCGGTTCCGTGCGTATTTTTGATCCGAAAATGCAACAAACCGTGTTCCGCATTCTCGGTATTGACGAAGAACAACAACGCGAAAAATTCGGCTTCTTATTAGATGCGTTAAAATTCGGCACACCACCGCATGCCGGTCTTGCGTTCGGTTTAGACCGTTTGACTATGTTATTAACCGGCACGGAAAACATTCGCGACGTGATCGCCTTCCCGAAAACCACTGCAGCGGCGTGCTTAATGACGGAAGCGCCAAGTGTGGCAAATCCGCAGGCGTTGTCGGAATTAAGCATTCAAGTGGTAAAGACCAATAAAGCGGAGGGG","","","66957","MMRSHYCGALNRTNIGQEITLSGWVHRRRDLGGLIFIDMRDREGIVQVCFDPKYQKALTAAAGLRNEFCIQIQGEVIARPDNQINKNMATGEVEVLAKVLKIYNASDVLPLDFNQNNTEEQRLKYRYLDLRRPEMAQHLKTRAKITGFVRRFMDDNGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFLTAPEVREIMERMVHGLWQHTLGVDLGKFPVITWQEAMRRFGSDKPDLRNPLELVDVADIVKNVDFKIFQGPANDPNGRVTLIRVPQGNEITRKQIDEYTQFVGIYGAKGLAWLKVNDVNAGLEGVQSPIAKFLNEDVLKALFERVGAQTGDILFFGADKWQTATDSMGALRLKLGRDLGLTRLDEWQPLWVIDFPMFERDDEGCLTAMHHPFTSPKDFTPEQLEADPTSAVANAYDMVINGYEVGGGSVRIFDPKMQQTVFRILGIDEEQQREKFGFLLDALKFGTPPHAGLAFGLDRLTMLLTGTENIRDVIAFPKTTAAACLMTEAPSVANPQALSELSIQVVKTNKAEG","2002659","","aspartyl-tRNA synthetase","Cytoplasm","","
InterPro
IPR002312
Family
Aspartyl-tRNA synthetase, class IIb
PR01042\"[191-203]T\"[208-221]T\"[475-491]T\"[519-533]TTRNASYNTHASP
InterPro
IPR004115
Domain
GAD
PF02938\"[308-407]TGAD
InterPro
IPR004364
Domain
tRNA synthetase, class II (D, K and N)
PF00152\"[118-560]TtRNA-synt_2
InterPro
IPR004365
Domain
Nucleic acid binding, OB-fold, tRNA/helicase-type
PF01336\"[19-103]TtRNA_anti
InterPro
IPR004524
Family
Aspartyl-tRNA synthetase bacterial/mitochondrial type
PTHR22594:SF5\"[90-587]TASPARTYL-TRNA SYNTHETASE
TIGR00459\"[1-588]TaspS_bact: aspartyl-tRNA synthetase
InterPro
IPR006195
Domain
Aminoacyl-transfer RNA synthetase, class II
PS50862\"[139-556]TAA_TRNA_LIGASE_II
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[1-109]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.30.930.10\"[111-556]Tno description
PTHR22594\"[90-587]TASPARTYL/LYSYL-TRNA SYNTHETASE


","No hits to the COGs database.","Significant hit ( 1.4e-08) to 2/2 blocks of the IPB002106 family, which is described as \"Aminoacyl-transfer RNA synthetases class-II\". Interpro entry for IP:IPR002106. IPB002106A 152-164 0.0077 IPB002106B 535-549 0.00067","Residues 424 to 472 match (5e-08) PD:PD483841 which is described as LIGASE SYNTHETASE AMINOACYL-TRNA BIOSYNTHESIS ASPARTYL-TRNA ATP-BINDING ASPRS ASPARTATE--TRNA PROTEOME COMPLETE ","","","","","","","","","","","","Tue Jan 21 17:21:32 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02856 is paralogously related to AA01743 (7e-17), AA02233 (5e-08) and AA00801 (1e-07).","","","","","","Residues 308 to 407 (E-value = 1.4e-49) place AA02856 in the GAD family which is described as GAD domain (PF02938)","","","","","Eriani G, Dirheimer G, Gangloff J.Aspartyl-tRNA synthetase from Escherichia coli: cloning and characterisation of the gene, homologies of its translated amino acid sequence with asparaginyl- and lysyl-tRNA synthetases.Nucleic Acids Res. 1990 Dec;18(23):7109-18.PMID: 2129559Sharples GJ, Lloyd RG.Location of a mutation in the aspartyl-tRNA synthetase gene of Escherichia coli K12.Mutat Res. 1991 Nov;264(3):93-6.PMID: 1944398Eiler S, Dock-Bregeon A, Moulinier L, Thierry JC, Moras D.Synthesis of aspartyl-tRNA(Asp) in Escherichia coli--a snapshot of the second step.EMBO J. 1999 Nov;18(22):6532-41.PMID: 10562565Rees B, Webster G, Delarue M, Boeglin M, Moras D.Aspartyl tRNA-synthetase from Escherichia coli: flexibility and adaptability to the substrates.J Mol Biol. 2000 Jun;299(5):1157-64.PMID: 10873442Takahagi M, Iwasaki H, Nakata A, Shinagawa H.Molecular analysis of the Escherichia coli ruvC gene, which encodes a Holliday junction-specific endonuclease.J Bacteriol. 1991 Sep;173(18):5747-53.PMID: 1885548","","Tue Dec 2 14:04:59 2003","1","","","" "AA02857","2004807","2005331","525","ATGCTACTTATTAACATTTTCTTTGCGTTAGCTCTATTATTACGATTTTATACTTTATCTATTTCAATCAGAAATGAAAAAAATTTACTAAAAAAAGGCGCCATACAATATGGAAAGAAAAATTCAATTGCCTTATCAGTAGTACATATTTTATTCTATCTTTCATGTATTACTGAAGCCAATTACAATCAAGTTATTTTTAATAAAGAATCTCAGATTGGATTAATAATCTTGATTTTCTCTCTTATAATGCTGTTTTACGTAATCTATCAACTAAAAGAAATTTGGACTGTAAAAGTTTACATCTTGCCTAATCATAAGATAAATACTTCATTTATATTCAAATATTTTAGACATCCTAATTATTTTCTGAATATCATTCCCGAATTAATTGGTTTAAGCTTACTATGCCAAGCTAAACTAACTGCCATGTTTATATTACCTTTATACATGATCATCTTAGCTATCCGTATTATGCAAGAAGAAAAGGCGATGAAATGCTTGTTTAAAGAAAATCATAATATC","","","20561","MLLINIFFALALLLRFYTLSISIRNEKNLLKKGAIQYGKKNSIALSVVHILFYLSCITEANYNQVIFNKESQIGLIILIFSLIMLFYVIYQLKEIWTVKVYILPNHKINTSFIFKYFRHPNYFLNIIPELIGLSLLCQAKLTAMFILPLYMIILAIRIMQEEKAMKCLFKENHNI","2005166","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR007269
Family
Isoprenylcysteine carboxyl methyltransferase
PF04140\"[75-167]TICMT
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide
tmhmm\"[5-23]?\"[42-62]?\"[72-90]?\"[122-156]?transmembrane_regions


","BeTs to 6 clades of COG1755COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG1755 is ---------drlb----h-n------Number of proteins in this genome belonging to this COG is","","Residues 104 to 165 match (1e-07) PD:PD010871 which is described as STEROL COMPLETE PROTEOME REDUCTASE TRANSMEMBRANE METHYLTRANSFERASE BIOSYNTHESIS OXIDOREDUCTASE NADP CARBOXYL ","","","","","","","","","","","","Tue Jan 21 17:18:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02857 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 75 to 167 (E-value = 1.9e-44) place AA02857 in the ICMT family which is described as Isoprenylcysteine carboxyl methyltransferase (ICMT) family (PF04140)","","","","","","","","1","","","" "AA02858","2005406","2006128","723","ATGAACAAAGACACCATTTTCTCCGTCCCTATTGAAAAATTGGGTGATTTTACTTTCGATGAAAGTGTTGCGGAAGTTTTCCCCGACATGATCCAACGCTCCGTGCCGGGCTACTCCAACATCATCACCGCTATCGGTATGATTGCCGAACGCTTTGTCAGTGCCGACAGTAACGTTTACGATCTGGGCTGCTCCCGTGGCGCAGCAACCTTATCCGCCCGTCGTCATATTCAATGCAAAAATGTGAAAATCATCGGTGTGGATAATTCCCAACCGATGGTGGAACGCTGTCGTCAGCATATCGCCGCCTATCACAGCAACATCCCGGTGGAAATTTTATGTGATGACATTCGTCATATTGGGATCAAAAACGCATCCATGGTGATTTTAAATTTCACCCTGCAATTTTTACTGCCGCAGGATCGCATTGCGTTACTGGAGAAAATTTATCAAGGATTAAATCCCAATGGCGTGTTGGTGCTATCGGAAAAATTCCGTTTTGAAGATGGGAAAATTGACGAATTGCTGATCGACCTGCACCACCAATTCAAACGTGCCAACGGCTACAGTGAATTAGAAGTGAGCCAGAAACGCACTGCCTTGGAAAAGGTTATGCGTACGGACAGTATTGAAACCCATAAAGTGCGGTTAAAAAATGTGGGATTTTCCCATGTGGAACTGTGGTTCCAGTGCTTTAATTTCGGTTCGATGATCGCCATCAAA","","","27360","MNKDTIFSVPIEKLGDFTFDESVAEVFPDMIQRSVPGYSNIITAIGMIAERFVSADSNVYDLGCSRGAATLSARRHIQCKNVKIIGVDNSQPMVERCRQHIAAYHSNIPVEILCDDIRHIGIKNASMVILNFTLQFLLPQDRIALLEKIYQGLNPNGVLVLSEKFRFEDGKIDELLIDLHHQFKRANGYSELEVSQKRTALEKVMRTDSIETHKVRLKNVGFSHVELWFQCFNFGSMIAIK","2005963","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR005271
Family
Proteobacterial methyltransferase
TIGR00740\"[3-241]TTIGR00740: methyltransferase, putative
InterPro
IPR013216
Domain
Methyltransferase type 11
PF08241\"[60-161]TMethyltransf_11
noIPR
unintegrated
unintegrated
PD857035\"[3-38]TQ7VLX6_HAEDU_Q7VLX6;
G3DSA:3.40.50.150\"[17-241]Tno description
PTHR10108\"[19-163]TMETHYLTRANSFERASE
PTHR10108:SF11\"[19-163]TARSENITE METHYLTRANSFERASE


","BeTs to 16 clades of COG0500COG name: SAM-dependent methyltransferasesFunctional Class: Q,RThe phylogenetic pattern of COG0500 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 17 to 241 match (1e-113) PD:PD020676 which is described as COMPLETE PROTEOME METHYLTRANSFERASE TRANSFERASE VC1164 PH0545 PM0985 SAM-DEPENDENT CG13929 METHYLTRANSFERASES ","","","","","","","","","","","","Tue Jan 21 17:17:43 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02858 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02860","2007815","2006214","1602","GTGACTGCATTAATTTGGCTTTTTTTAACGTTAAATGTGTCTGAACCGAAAACCGGTTTGCTGATTTTAAACGTTATTGTGTTGTTTATTGCGCTGGGGTTGCATTTTGGCAATCCCCACGCGGAAAGTCATATGTCGATTATCATCGGGATTTTCTTCTTTATGGGCTACAATCTGCTTGCCGGTTATTTCCTTGCCGATGTATTTGATTCTTACGGTGAGGGCGCCTTAACCTGTGATGTACCGTTATTGTTTACTGCGATAATTTCTATGCTTTATTTTTTACGCAAAGAGAACTGGCTGAAAACTCTAACTCTCGTGATTGTTTTGGGCGTGTGGCATATTTATTTAACCGATTTTTCCACAGGTGATCTTAGCCATGCCAATCGCATCGAATACAGTTATGTGCCTTTGTATTTTGTCACGATGTTGGGTTGCGTTATTGCTTTCTTTGTGCAAAATATATACGGAGAAAACAGTAAAGTCAGAGTGCGGATCACGCCTGTTGCTTGGGCGTTTTTACTGTTCAGCATAGGCGGCTGGGCGTTTTCCACTGATAATTTCTTGTCTTTGTTTGTAGTCTACGTTCCCGGCACTGTGGATGCGCTACCGGAAATTGATACTTTCAGCGGCTTCTTTACGATGATCACCGCCGGGTTTTATTCTCGCGCTGTGCTCGGATTAGGTTGGACAATTCCTTTCTTAGTTTGTTTTACGCCGTTGGTCACGTATTTCGCCATCAGCCGTTTTTTCAGTTTAAAAACCGATGAAAAAATGTGCATTGCCGCGATCCTGGCACTATTTACTTTCCTCTTTGTCGGTCAGCCTTCCGTATTATTTTTCGTTACGTTGTTGCTGATTGCCTACTTTGTGCAAAGCCGCACGTTGTTTTTTATCGGTGTTTTATCTTTAGTCGGTAACTTGGCAATTTACTATTATTTGTTATTTATTCCACTGCTTTACAAGGCATTTTTACTGCTGTTCTTTGCTTTGCTATTCTCTGCGGTTGCTATTTATTTACACAGAAAACATCAACCGCAAACACAAAGCGCGGTTAGTTTTTACAACGTTTCTAAAGTGAAACCGATGGTTGCGCTCTGTACGGTGTTGCTTATTCTGATTCCGTTAAATTATAAAGTGTGGCAGTTTGAAAATGTGTTGATGACAGGTAAGCCGGTGGTGTTAAAAATTGCGCCCGTTGATCCGCGTTCCATCATACAAGGGGATTATATGTCTCTCAGTTATGCTATTTTGACGGATATTCGTGCACAATTAAATACTTCCGTAAATGATCAAGAAGCTGCCATTAGTGGACGAAAAACACGCCCCAAACGGGTTTACGCGTTAGTACACCAGGACGAACAGGGTGTCGCCACATTATGTCGTGTAGAGAATCGCATTCCGACGGATTTCTACGATTGTGTGCCTGATATGTATTTGCCGGTCAATAATGTCGGTTGGTTCCCGCAACTGCCAAGTCAGGAATATTTCTTTGCGGAAGGCAAAGGACAACATTATGCGCAGGCGAAATATGCCGAATATCGCTTTAAAGACGGCATCTTATTGCTTGCCCGTTTGCTGGATAAAGATTTGAAAGGCTTG","","","60442","VTALIWLFLTLNVSEPKTGLLILNVIVLFIALGLHFGNPHAESHMSIIIGIFFFMGYNLLAGYFLADVFDSYGEGALTCDVPLLFTAIISMLYFLRKENWLKTLTLVIVLGVWHIYLTDFSTGDLSHANRIEYSYVPLYFVTMLGCVIAFFVQNIYGENSKVRVRITPVAWAFLLFSIGGWAFSTDNFLSLFVVYVPGTVDALPEIDTFSGFFTMITAGFYSRAVLGLGWTIPFLVCFTPLVTYFAISRFFSLKTDEKMCIAAILALFTFLFVGQPSVLFFVTLLLIAYFVQSRTLFFIGVLSLVGNLAIYYYLLFIPLLYKAFLLLFFALLFSAVAIYLHRKHQPQTQSAVSFYNVSKVKPMVALCTVLLILIPLNYKVWQFENVLMTGKPVVLKIAPVDPRSIIQGDYMSLSYAILTDIRAQLNTSVNDQEAAISGRKTRPKRVYALVHQDEQGVATLCRVENRIPTDFYDCVPDMYLPVNNVGWFPQLPSQEYFFAEGKGQHYAQAKYAEYRFKDGILLLARLLDKDLKGL","2006049","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-35]?signal-peptide
tmhmm\"[19-37]?\"[46-66]?\"[76-94]?\"[99-117]?\"[136-156]?\"[166-184]?\"[190-210]?\"[225-247]?\"[261-290]?\"[295-315]?\"[319-339]?\"[360-378]?transmembrane_regions


","No hits to the COGs database.","","Residues 366 to 516 match (3e-38) PD:PD589088 which is described as PROTEOME COMPLETE PM0986 MEMBRANE BMEI1070 ","","","","","","","","","","","","Tue Jan 21 17:16:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02860 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02861","2008778","2007861","918","ATGATAAATCAATCTTCTCTGTTTAATTTATCTTGGCCACGTTATTTAAATTTATTGTTTTTAATCTTAAGTGCAGGATTTTTAGCCAGCGGTATCGTGACATTAATTGCCGCTAATTTAGATTATTTTTCCGATTTAGCCAAAATTTACGGCTTGCAACTGATTTTGGTCGCTTCGGTTTTATTAGGGAGTTATTTCTTTTTGCGTGAAAGCCAAAAAGTCGCAAAAGAGAAATTAAAACTGCTTTCCGCTACTTTTTTCTTTCTTACTGCCGTGCTTATAGGCGCGGTGTTTGCCCTAGTAGGGCAGACGTATCAAACGGGCGCGAATGCGTGGGAATTATTTGCACTGTGGTCGCTGTGCCAACTGCCGTTGTTATTGTTGCTGCCGAATATTGCTTCCGCTTTATTACTTATCGCCACGACCAATCTCACCTTGTATTTGTATTATGATGCTTGGTTTGATCACGGTGTGGTGAATTATGTTGTCCTGTTAAATTTTATTTTCTTGTTGTTAAGTGAAATTTTTATTCGCCAATTACACGATCAAAACTGGCGCATTCTGCCTAAAATTCTTACCTTTTTAGTGTTAAGTCATTTATTCGGCGTCCGTGTTATTACCGATAATTTACCTAACGATATTTACTCCGGTGTGTATTTTTTTCTTGTGTTTTTACAAGTGGTGATTCCATCGGGGATCGTGATTTATGTGTATAAAAAATACCGATTTGATTTTGTTAATTTAATTACTGCAACTATCTGTTCTATCGTTGCTTTTGGTATTTTCCTATTTTCCAATGTAAATTCCGGTGATTTTGCCGTATTGGCAGGCCTGTTGCTTTTTATTATTACGATCTTTGCCATTATGTTGTTGCATGGTTGGTATAAGCAGCATTATCCGCACCTTAAGAACATTTCT","","","34699","MINQSSLFNLSWPRYLNLLFLILSAGFLASGIVTLIAANLDYFSDLAKIYGLQLILVASVLLGSYFFLRESQKVAKEKLKLLSATFFFLTAVLIGAVFALVGQTYQTGANAWELFALWSLCQLPLLLLLPNIASALLLIATTNLTLYLYYDAWFDHGVVNYVVLLNFIFLLLSEIFIRQLHDQNWRILPKILTFLVLSHLFGVRVITDNLPNDIYSGVYFFLVFLQVVIPSGIVIYVYKKYRFDFVNLITATICSIVAFGIFLFSNVNSGDFAVLAGLLLFIITIFAIMLLHGWYKQHYPHLKNIS","2007696","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-31]?signal-peptide
tmhmm\"[15-35]?\"[49-67]?\"[82-102]?\"[108-128]?\"[133-153]?\"[157-177]?\"[187-207]?\"[217-237]?\"[246-266]?\"[272-294]?transmembrane_regions


","No hits to the COGs database.","","Residues 11 to 115 match (6e-14) PD:PD493794 which is described as PROTEOME COMPLETE PM0986 MEMBRANE ","","","","","","","","","","","","Tue Jan 21 17:15:52 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02861 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02862","2008807","2008908","102","ATGCGTAAAAAATCGAGGCTATTCTGCCAACTTCAACAGAAAAATGAAAGAAAAAGTGCGGTGGATTTTCGCCGCGAATTTCAACCGCACTTTAGTATTATT","","","4235","MRKKSRLFCQLQQKNERKSAVDFRREFQPHFSII","2008908","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:06:24 2004","Mon Feb 23 15:06:24 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02862 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:06:24 2004","","","","","","","","","","","","","1","","","" "AA02864","2010252","2008924","1329","ATGTTTTCATTTCTTAAGGCCTCTCCGCCGGCACCTCGAATTGAGTCTTCCCGAGTTGATGCGGAGTATAAGAAATTACGTTGGCAGGTATTTGCCGGTGTATTTATAGGCTATGCGGCGTATTATTTGATCCGCAAAAACTTTTCCCTCGCTATCCCTTACCTAATTGATGAATATGGTTTTACTAAAGCGGATTTAGGCACTGTGGGTGTTGCGTTGTCCCTCGCTTATGGTTTTAGTAAGTTCATTATGGGGAATTTTTCCGACCGTAGTAATCCTAAGTATTTTATCACTATAGGTTTGCTGGGTTCGGCAATCGTGAGTTTAATTTTCGGCTTAGTGCCCGGCGTGTTGGCTTCCATTCCGATCATGATCGTGCTAGCCGCTTTTAACGGCTGGTTCCAAGGAATGGGTTACCCACCGGGTGCAAAAACCATGACCAACTGGTTCTCCGTATCCGAACGGGGTGTGTGGTGGAGCTGGTGGAATGTGTCCCATAACTTGGGCGGCGGTTTAATCGGCCCGTTAGCCATTTTAGGTTTGGCGATTTTTGGTACATGGCAATCACTTTTCTATTTACCGGCATTAATTGCTATCGTGTTAGCGTTTATTATGTTTTGGTTAATGCGCGATACACCGGAATCACAAGGTTTACCGCCGGTGGATGAGTGGAAGGGCGAAAAAGTCGTACAGCAGGTTGAATCAGCCCATACCCTTTCTTCAAAAGATATTTTTATGAAATATATCTTAAATAACAAGTTCTTATGGGCAATTGCTATTGCCAATGTGTTTGTATATTTCATTCGTTACGGCATTATCGACTGGGCACCGACCTACTTAAAAGAAGTGAAACATTTTTCCGTAGATAAACAAAGCTGGGCATATTTCCTGTATGAGTATGCAGGGATTTTCGGCATGCTGACCAGTGGTTATTTGAGCGATAAAGTGTTCAAAGGTCACCGCGCCCCGCCAATGCTATTGTTCCTGACAGGTGTGCTTGTTGCGATTTTTGTTTATTGGAAAAATCCGGCGGGTAATCCGTTAGTCGATAATATCTGTTTGGTCGCAATTGGTTTCCTGATTTACGGACCGGTGATGATGATCGGCTTACAGGCAGCAGATTTGGTACCTCGTGTGGCGACCGGTACAGCAACAGGCTTAACCGGTTTATTTGGTTACTTGTTGGGATCTGCCAGTGCCGGTTATGTGATGGGTAAACTGGTGGATGTATTCGGTTGGGACGGCGGATTTTATGCGCTCATCCTTTCTTGTTTCCTCGGTTTTGCTTTTATTGCCGTCACTTTATTCCATAAACCGAATACCAAGAAA","","","49098","MFSFLKASPPAPRIESSRVDAEYKKLRWQVFAGVFIGYAAYYLIRKNFSLAIPYLIDEYGFTKADLGTVGVALSLAYGFSKFIMGNFSDRSNPKYFITIGLLGSAIVSLIFGLVPGVLASIPIMIVLAAFNGWFQGMGYPPGAKTMTNWFSVSERGVWWSWWNVSHNLGGGLIGPLAILGLAIFGTWQSLFYLPALIAIVLAFIMFWLMRDTPESQGLPPVDEWKGEKVVQQVESAHTLSSKDIFMKYILNNKFLWAIAIANVFVYFIRYGIIDWAPTYLKEVKHFSVDKQSWAYFLYEYAGIFGMLTSGYLSDKVFKGHRAPPMLLFLTGVLVAIFVYWKNPAGNPLVDNICLVAIGFLIYGPVMMIGLQAADLVPRVATGTATGLTGLFGYLLGSASAGYVMGKLVDVFGWDGGFYALILSCFLGFAFIAVTLFHKPNTKK","2008759","[FUNCTION] Responsible for glycerol-3-phosphate uptake (by similarity). ","glycerol-3-phosphate transport protein","Inner membrane, Cytoplasm","","
InterPro
IPR000849
Family
GlpT transporter
TIGR00881\"[35-417]T2A0104: phosphoglycerate transporter family
InterPro
IPR007114
Family
Major facilitator superfamily
PS50850\"[26-442]TMFS
InterPro
IPR011701
Family
Major facilitator superfamily MFS_1
PF07690\"[34-409]TMFS_1
noIPR
unintegrated
unintegrated
PTHR11662\"[12-435]TSODIUM-DEPENDENT PHOSPHATE TRANSPORTERS
PTHR11662:SF13\"[12-435]TGLYCEROL-3-PHOSPHATE TRANSPORTER (HEXOSE TRANSPORTER)
tmhmm\"[26-44]?\"[91-111]?\"[117-137]?\"[158-184]?\"[190-208]?\"[255-273]?\"[292-312]?\"[322-340]?\"[350-370]?\"[375-397]?\"[416-436]?transmembrane_regions


","BeTs to 8 clades of COG2271COG name: Sugar phosphate permeaseFunctional Class: GThe phylogenetic pattern of COG2271 is -----------lb-efgh--u-xi--Number of proteins in this genome belonging to this COG is","Significant hit (1.5e-142) to 7/7 blocks of the IPB000849 family, which is described as \"GlpT family of transporters\". Interpro entry for IP:IPR000849. IPB000849A 23-55 9.4e-25 IPB000849B 65-105 2.8e-21 IPB000849C 135-170 2.2e-18 IPB000849D 191-227 2.9e-20 IPB000849E 243-280 2.5e-24 IPB000849F 297-314 5.3e-07 IPB000849G 357-389 5e-19","Residues 73 to 127 match (5e-07) PD:PD003807 which is described as PROTEOME COMPLETE TRANSPORTER TRANSMEMBRANE GLYCEROL-3-PHOSPHATE REGULATORY SUGAR G-3-P INNER MEMBRANE ","","","","","","","","","","","Tue Jan 21 17:14:52 2003","Tue Jan 21 17:14:52 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02864 is paralogously related to AA01378 (1e-118), AA00497 (6e-82), AA02792 (2e-45) and AA00266 (2e-10).","","","","","","","","","","","Song XM, Forsgren A, Janson H.Glycerol-3-phosphate transport in Haemophilus influenzae: cloning, sequencing, and transcription analysis of the glpT gene.Gene. 1998 Jul;215(2):381-8.PMID: 9714837Eiglmeier K, Boos W, Cole ST.Nucleotide sequence and transcriptional startpoint of the glpT gene of Escherichia coli: extensive sequence homology of the glycerol-3-phosphate transport protein with components of the hexose-6-phosphate transport system.Mol Microbiol. 1987 Nov;1(3):251-8.PMID: 3329281Gött P, Boos W.The transmembrane topology of the sn-glycerol-3-phosphate permease of Escherichia coli analysed by phoA and lacZ protein fusions.Mol Microbiol. 1988 Sep;2(5):655-63.PMID: 3141744Auer M, Kim MJ, Lemieux MJ, Villa A, Song J, Li XD, Wang DN.High-yield expression and functional analysis of Escherichia coli glycerol-3-phosphate transporter.Biochemistry. 2001 Jun;40(22):6628-35.PMID: 11380257","","Tue Jan 21 17:14:52 2003","1","","","" "AA02865","2010653","2012602","1950","ATGCGTAAACATTTTTCATTGCTTCCTCTGGCAATATTAGTTGCCACCGCAGTTCAGGCTGAGGAATTAGATATCATCAATGTGGTGTCCGAAAATACCGGTGCCAAAAGCAAAACCAATGTAATTACTACAGAATCAGTTAATCGCAGTACTGAAACCGAGTTAAAAGGTTTACTCAAGGAAGAGCCCGCACTTAACTTCGGGGGAGGGCGCGGAACCTCTCAATGGTTTACCATTCGTGGTATGGGACAGGATCAGGTGGATGTTAAAATCGATGATGCCTACACTGATGCTCAACTGTTCCACCATCAAGGTCGCTTCGTTTTTGATCCGTCTTTGTTTAAAAAAGTTAGTGTACAAAAAGGTACAGGCTCCGCCAGCGCAGGCATTGGCGCCACCAGTGGTACAATTGTGGCGGAAACTGTCAGCGCAAAAGATTTGCTGAAAGAGGAACAAGACTTTGGTTTTAAAGTTAATGCCGGCGTAAGTTCGAATAGCGGTTGGAGCAAAGGCGCCACCATTTATTCCAAAGTCGGTGCATTCGATGCTTTAATTTCCGGTAACTGGGTAAAAGAACGTGATTACAAAGCGGGTAATGGCTATAAGATCAAAAATAGTGCACTGGGTCAGCGTGGTTTATTGGCTAAAATCGGTGTAGATCTAAACGAAGATCATCGTATTGAATTAAGCCGCCGCCAAGAACGCCATTATGGTGTCCGCGCATTACGTGAGGAGTTTGACTTTGCTCAGGACGGAAGAGAATCAGTTAATGCTCCACGCTATCGCGTCACCACTAATGATACCGGCAAGATTGAGTGGACCGGCAAAAACATTGGCTTTATCAGTACCGCAAAAGCCAATGTTTGGCGTACAGTTATTAGCCGAGAAGAACCTACCGAACGTTCCAAAATCCATTTGGTTGCCAATGGTGCAAACCTTAACTTAGATTCTCAAATCGGTGAGTCTCACTTAATCAAATATGGTGTCAATTACCGTGATCAAGAAGGCAGACCAAATTCTCTCACGGTACAAAACGGGGTACAAATAAGAAATCAAAAGAAACGTGATGTGGGCGTTTATGCAGAAGGTATCTGGGGTCTCGGTGCATTCACCTTAACCACAGGTTTACGTTACGATCACTTCTCATTCCGAGCTATGGATGGCAGAAAATCAAACAAAGGTAATTTAAACCCAAGTTTTGGTTTAATCTATGAAGTAACGAAGGATTTAAGTTTTAGTGCCAGCTTAAACTACGCAACCCGTAGTCCTCGTTTCCGGGAAATTCTATTGTCGTCAGGAACTACCAGAGGAAACCCCGCAGTCTATTCCATTGCCGGCAATATTAAACCTGAAAAGTCACGCAATACGGAAGTCGGCTTCAACTATAAATTAGCCGATAGCCTTTCATTAAACGGTAGCTATTTCTGGCAAACGATTCAGGATACTCACGCGTTCACTCAAATTAGACCGGGTTATTTTGAAATTCAAAATGCAGGTAAGTTGAGAAATAGCGGTTACGAATTAGGTGCGGCATATAAATATGAAGGTTTAACTTTACGTGCTGGTGTAGCCTATAGCAAGCCTGAATTAGATGGCAGAACCGTCGACAGTACGGTTACTGCCATTCCAATTGGTCGTACTTGGACCACCGGCGTATCTTACCGCTTTGAACAACCTGATGTGGAAATTGGCTGGAGAGGACGTTTCGTACAGCATACGAGTTATGATACCAGCACGAATAACCGTGGTGGCGGTTCAACCACCACTAAACGCCCTGGCTATGGTGTGAACGATTTCTACGTCACATGGAAACCGGTTGAAAACATCAACGTTAACTTGGCGTTAAATAATGCGTTTAATAAATATTATCGCAGCCACAGCCAACGTGCAGGTGTTTCCACCCTACCCGAACCGGGTCGCGATGTTCGCTTAAATGTCAATTACACCTTC","","","72006","MRKHFSLLPLAILVATAVQAEELDIINVVSENTGAKSKTNVITTESVNRSTETELKGLLKEEPALNFGGGRGTSQWFTIRGMGQDQVDVKIDDAYTDAQLFHHQGRFVFDPSLFKKVSVQKGTGSASAGIGATSGTIVAETVSAKDLLKEEQDFGFKVNAGVSSNSGWSKGATIYSKVGAFDALISGNWVKERDYKAGNGYKIKNSALGQRGLLAKIGVDLNEDHRIELSRRQERHYGVRALREEFDFAQDGRESVNAPRYRVTTNDTGKIEWTGKNIGFISTAKANVWRTVISREEPTERSKIHLVANGANLNLDSQIGESHLIKYGVNYRDQEGRPNSLTVQNGVQIRNQKKRDVGVYAEGIWGLGAFTLTTGLRYDHFSFRAMDGRKSNKGNLNPSFGLIYEVTKDLSFSASLNYATRSPRFREILLSSGTTRGNPAVYSIAGNIKPEKSRNTEVGFNYKLADSLSLNGSYFWQTIQDTHAFTQIRPGYFEIQNAGKLRNSGYELGAAYKYEGLTLRAGVAYSKPELDGRTVDSTVTAIPIGRTWTTGVSYRFEQPDVEIGWRGRFVQHTSYDTSTNNRGGGSTTTKRPGYGVNDFYVTWKPVENINVNLALNNAFNKYYRSHSQRAGVSTLPEPGRDVRLNVNYTF","2012437","","iron-regulated outer membrane protein (omp64)","Outer membrane, Extracellular","","
InterPro
IPR000531
Domain
TonB-dependent receptor
PF00593\"[397-650]TTonB_dep_Rec
InterPro
IPR010917
Domain
TonB-dependent receptor, C-terminal
PS01156\"[633-650]?TONB_DEPENDENT_REC_2
InterPro
IPR012910
Domain
TonB-dependent receptor, plug
PF07715\"[31-136]TPlug
noIPR
unintegrated
unintegrated
G3DSA:2.170.130.10\"[16-141]TG3DSA:2.170.130.10
G3DSA:2.40.170.20\"[149-650]TG3DSA:2.40.170.20
SSF56935\"[23-650]TSSF56935


","No hits to the COGs database.","","Residues 505 to 650 match (1e-11) PD:PD018313 which is described as IRON-REGULATED PROTEOME OUTER COMPLETE MEMBRANE FRPB ","","","","","","","","","","","","Tue Jan 28 13:36:52 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02865 is paralogously related to AA02782 (7e-11), AA02202 (1e-06), AA02158 (9e-06), AA00762 (2e-05), AA00590 (7e-05) and AA02151 (0.001).","","","","","","Residues 38 to 650 (E-value = 1.6e-36) place AA02865 in the TonB_dep_Rec family which is described as TonB dependent receptor (PF00593)","","","","Komatsuzawa H, Asakawa R, Kawai T, Ochiai K, Fujiwara T, Taubman MA, Ohara M, Kurihara H, Sugai M.Identification of six major outer membrane proteins from Actinobacillus actinomycetemcomitans.Gene. 2002 Apr;288(1-2):195-201.PMID: 12034509","","Tue Jan 28 13:36:52 2003","","1","","","" "AA02866","2012764","2013168","405","ATGCGAATTTTACACACCATGTTACGCGTCGGCGATTTACAACGTTCCATTCGATTTTATCAAGATGTGTTGGGTATGCGTTTATTGCGCACCGGCGAAAATCCCGAATACAAATATTCTCTGGCATTTTTAGGTTACGACGATGAAGACAAAACCTCCGTGTTGGAACTGACTTACAACTGGGGCGTGGATAAATACGAACTCGGCACCGCTTACGGGCATATCGCCATCGGCACGGACGATATTTACGCCACCTGCGAAGCGGTGCGCAAAGCCGGTGGCAATGTCACCCGTGAGCCCGGCCCGGTAAAAGGCGGCAAAACAGTGATTGCCTTTGTGGAAGATCCGGACGGTTATAAAATCGAATTTATCGAAAACAAAAACGCACAAGCCGGATTAGGCAAC","","","20489","MRILHTMLRVGDLQRSIRFYQDVLGMRLLRTGENPEYKYSLAFLGYDDEDKTSVLELTYNWGVDKYELGTAYGHIAIGTDDIYATCEAVRKAGGNVTREPGPVKGGKTVIAFVEDPDGYKIEFIENKNAQAGLGN","2013003","[FUNCTION] Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione (by similarity). ","lactoylglutathione lyase","Cytoplasm","","
InterPro
IPR004360
Domain
Glyoxalase/bleomycin resistance protein/dioxygenase
PF00903\"[2-123]TGlyoxalase
InterPro
IPR004361
Family
Glyoxalase I
TIGR00068\"[2-135]Tglyox_I: lactoylglutathione lyase
PS00934\"[5-26]TGLYOXALASE_I_1
PS00935\"[69-81]TGLYOXALASE_I_2
InterPro
IPR011588
Domain
Glyoxalase/extradiol ring-cleavage dioxygenase
PD002334\"[5-123]TQ52533_PSESP_Q52533;
noIPR
unintegrated
unintegrated
G3DSA:3.10.180.10\"[2-133]Tno description
PTHR10374\"[1-125]TLACTOYLGLUTATHIONE LYASE (GLYOXALASE I)


","BeTs to 16 clades of COG0346COG name: Lactoylglutathione lyase and related lyasesFunctional Class: EThe phylogenetic pattern of COG0346 is aom-kzy--drlbcefghsnuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 4.5e-62) to 4/4 blocks of the IPB000325 family, which is described as \"Glyoxalase I\". Interpro entry for IP:IPR000325. IPB000325A 5-43 2.8e-25 IPB000325B 55-64 0.00057 IPB000325C 70-104 4.1e-21 IPB000325D 110-122 1.6e-07Significant hit ( 9.1e-07) to 2/3 blocks of the IPB000486 family, which is described as \"Extradiol ring-cleavage dioxygenase\". Interpro entry for IP:IPR000486. IPB000486A -2-25 1.7e-05 IPB000486C 102-126 23","Residues 7 to 64 match (1e-08) PD:PD503291 which is described as LYASE I GLYOXALASE GLX METHYLGLYOXALASE METHYLGLYOXAL KETONE-ALDEHYDE ZINC LACTOYLGLUTATHIONE S-D-LACTOYLGLUTATHIONE ","","","","","","","","","","","Tue Jan 21 17:04:00 2003","Tue Jan 21 17:04:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02866 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 123 (E-value = 1.5e-44) place AA02866 in the Glyoxalase family which is described as Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily (PF00903)","","","","","Clugston SL, Daub E, Kinach R, Miedema D, Barnard JF, Honek JF.Isolation and sequencing of a gene coding for glyoxalase I activity from Salmonella typhimurium and comparison with other glyoxalase I sequences.Gene. 1997 Feb;186(1):103-11.PMID: 9047352Clugston SL, Barnard JF, Kinach R, Miedema D, Ruman R, Daub E, Honek JF.Overproduction and characterization of a dimeric non-zinc glyoxalase I from Escherichia coli: evidence for optimal activation by nickel ions.Biochemistry. 1998 Jun;37(24):8754-63.PMID: 9628737He MM, Clugston SL, Honek JF, Matthews BW.Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation.Biochemistry. 2000 Aug;39(30):8719-27.PMID: 10913283","","Tue Jan 21 17:04:00 2003","1","","","" "AA02867","2013258","2013908","651","ATGTCAGAAACCCAAGAAACCATTAATTACAATATATTAAAACATCGATTCCGAGGTTATTTGCCGGTGGTAATCGACGTGGAAACCGCCGGGTTAAACGCCAAAACCGATGCGTTGTTGGAGTTGGCAGCAATTACCCTCAAAATGGATGAAAACGGCAATTTGCTGCCGGATCAAAAATGCCATTTTCACATTCAAGCTTTTGAAGGGGCGAATATCGATCCCGAATCCCTTAAATTTAACGGCATTGATATTGATAACCCGTTGCGTGGTGCGGTGAGCGAAAATATCGCCATCAGCGAAATGTTCAAGATGGTACGTAAAGCGCAAAAAGATGCGGATTGCCAGCGATCCATTATCGTGGCGCATAATGCGGCGTTCGATCAGGGGTTTCTCATGGCGGCGGCACAACGTATGAATGTTAAACACAACCCATTCCACCCCTTTTCCACCTTTGACACGGCAACCTTGAGCGGTTTTATGTTCGGGCAAACCGTGTTGGTGAAAGCCTGCCAAGCAGCAAAAATCCCTTTTGACAGCCAGCAGGCACATTCAGCGTTATATGACACGGAACGCACTGCCGAATTGTTTTGTTATATGGTGAATCATTTGAAGCAATTGGGTGGGTTTCCGCATCTTGTAGCGAATGAT","","","24119","MSETQETINYNILKHRFRGYLPVVIDVETAGLNAKTDALLELAAITLKMDENGNLLPDQKCHFHIQAFEGANIDPESLKFNGIDIDNPLRGAVSENIAISEMFKMVRKAQKDADCQRSIIVAHNAAFDQGFLMAAAQRMNVKHNPFHPFSTFDTATLSGFMFGQTVLVKACQAAKIPFDSQQAHSALYDTERTAELFCYMVNHLKQLGGFPHLVAND","2013743","[FUNCTION] Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis (By similarity).","ribonuclease T","Cytoplasm","","
InterPro
IPR005987
Family
Ribonuclease T
TIGR01298\"[13-212]TRNaseT: ribonuclease T
InterPro
IPR006055
Domain
Exonuclease
SM00479\"[21-206]TEXOIII
InterPro
IPR013520
Domain
Exonuclease, RNase T and DNA polymerase III
PF00929\"[22-197]TExonuc_X-T
noIPR
unintegrated
unintegrated
G3DSA:3.30.420.10\"[15-208]Tno description


","No hits to the COGs database.","","Residues 127 to 202 match (3e-31) PD:PD384566 which is described as T RIBONUCLEASE RNASE HYDROLASE PROTEOME 3.1.13.- COMPLETE EXONUCLEASE TRNA EXORIBONUCLEASE ","","","","","","","","","","","Tue Jan 21 16:50:08 2003","Tue Jan 21 16:50:08 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02867 is paralogously related to AA02763 (2e-07).","","","","","","Residues 22 to 197 (E-value = 1.7e-34) place AA02867 in the Exonuc_X-T family which is described as Exonuclease (PF00929)","","","","","Huang S, Deutscher MP.Sequence and transcriptional analysis of the Escherichia coli rnt gene encoding RNase T.J Biol Chem. 1992 Dec;267(35):25609-13.PMID: 1460056Padmanabha KP, Deutscher MP.RNase T affects Escherichia coli growth and recovery from metabolic stress.J Bacteriol. 1991 Feb;173(4):1376-81.PMID: 1704882Padmanabha KP, Deutscher MP.RNase T affects Escherichia coli growth and recovery from metabolic stress.J Bacteriol. 1991 Feb;173(4):1376-81.PMID: 1704882","","Tue Jan 21 16:50:08 2003","1","","","" "AA02869","2014032","2013928","105","TTGCGAATAACGTTCATTTTGTTTCTCCTGTGTGAGTTGCTTTTTAAACTACTGGAAAAGTTTTTTCATCGCAAGTGGTTTTTTAAAAAATGTGAAAGTGCGGTC","","","4390","LRITFILFLLCELLFKLLEKFFHRKWFFKKCESAV","2013928","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-19]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:04:37 2004","Mon Feb 23 15:04:37 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02869 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:04:37 2004","","","","","","","","","","","","","1","","","" "AA02870","2014263","2015612","1350","ATGTTAACCAACCCTGTTGTCATTTCGATCATCGTATTGCTGGCACTTAGTTTGCTCCGCATTAACGTGGTCATCGCATTGGTGATTTCCGCCTTAACTGCCGGTTTAGTCGGTGATTTAGGCTTGACTAAAACCATCGAAGCCTTTACCGGCGGACTTGGCGGCGGTGCGGAAGTTGCTATGAACTATGCGATGCTCGGCGCTTTTGCTATTGCCATCTCCAAATCCGGCATTACCGATTTACTTGCCTACAAAATCATCACCCGCATGAATAAAGTGCCAACCGCAAACAGCCTTGCCATGTTCAAATATGCCATGCTCGGTATCCTAACGCTGTTCGCTATTTCTTCCCAAAACCTGCTGCCGGTACACATTGCCTTTATTCCTATCGTCATTCCGCCGATGCTCGCCATTTTCAACAAATTGAAAATTGACCGCCGTGCGGTGGCTTGTGTGCTGACCTTCGGTTTAACCGCCACCTATATGTTATTGCCGGTGGGTTTCGGAAAAATCTTTATCGAAAGCATTCTGGTGAAAAATATCAACACCGTAGGCAATTCATTAGGCTTACAAACCAGCGTGGGCGAAGTGTCACTGGCAATGACCATTCCCGTGATCGGCATGGTTTTGGGGTTGTTAACCGCCGTGTTTATCACTTATCGCAAACCGCGCGAATACGTGGTGATGAGCACCGAGCCGACAACCCAAGACATTGAACAACACATTGCCAACATCAAACCGAAACAAATTGTGGCAAGTTTAATCGCCATCGTCGCCACCTTCACAGTGCAATTAGTCACCAGTTCCACCATCATCGGCGGCTTGGTCGGTTTAATTATCTTCGCCGTATTTGGCATTTTTAAACTCAAAGAAAGCAACGATATTTTCCAACAAGGCTTGCGTTTAATGGCGATGATCGGCTTTGTGATGATCGCCGCCTCCGGTTTCGCCAACGTCATTAACACCACAACCGGCGTGAAAGAGCTAATAGACGTGTTAAGCACCAGTGTGATTCAAAGCAAAGGCGCCGCCGCATTCCTGATGTTGCTCGTGGGTTTGCTCATCACCATGGGTATCGGTTCTTCTTTCTCTACCGTACCGATTATTACTTCCATTTATGTGCCGTTGTGTTTATCTTTCGGCTTCTCGCCGCTTGCCACCGTGTCTATTGTCGGCGTAGCGGCTGCGCTGGGCGATTCAGGTTCACCGGCATCCGACTCGACGTTGGGGCCGACTTCCGGTTTGAATATGGACGGCAAACACGACCACATTTGGGATTCCGTGGTGCCGACCTTTATTCACTACAACATTCCGTTAATTATCTTCGGCTGGATTGCCGCGGTGTATCTG","","","47429","MLTNPVVISIIVLLALSLLRINVVIALVISALTAGLVGDLGLTKTIEAFTGGLGGGAEVAMNYAMLGAFAIAISKSGITDLLAYKIITRMNKVPTANSLAMFKYAMLGILTLFAISSQNLLPVHIAFIPIVIPPMLAIFNKLKIDRRAVACVLTFGLTATYMLLPVGFGKIFIESILVKNINTVGNSLGLQTSVGEVSLAMTIPVIGMVLGLLTAVFITYRKPREYVVMSTEPTTQDIEQHIANIKPKQIVASLIAIVATFTVQLVTSSTIIGGLVGLIIFAVFGIFKLKESNDIFQQGLRLMAMIGFVMIAASGFANVINTTTGVKELIDVLSTSVIQSKGAAAFLMLLVGLLITMGIGSSFSTVPIITSIYVPLCLSFGFSPLATVSIVGVAAALGDSGSPASDSTLGPTSGLNMDGKHDHIWDSVVPTFIHYNIPLIIFGWIAAVYL","2015447","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR004770
Family
Na+/H+ antiporter NhaC
PF03553\"[152-444]TNa_H_antiporter
noIPR
unintegrated
unintegrated
signalp\"[1-26]?signal-peptide
tmhmm\"[10-30]?\"[40-60]?\"[66-84]?\"[99-117]?\"[123-138]?\"[148-168]?\"[200-220]?\"[250-284]?\"[300-320]?\"[341-363]?\"[369-398]?\"[428-448]?transmembrane_regions


","No hits to the COGs database.","","Residues 392 to 450 match (3e-25) PD:PD421371 which is described as PROTEOME COMPLETE MEMBRANE INTEGRAL PROBABLE TRANSMEMBRANE PM0989 SAV0943 BH1986 YUIF ","","","","","","","","","","","","Tue Jan 21 16:46:56 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02870 is paralogously related to AA00143 (2e-16).","","","","","","Residues 152 to 444 (E-value = 9.3e-89) place AA02870 in the Na_H_antiporter family which is described as Na+/H+ antiporter family (PF03553)","","","","","","","","1","","","" "AA02872","2015679","2016242","564","ATGAACAGTATTTCCATCCAACGCCTTAAACAAAGCCTTCAGCATTTCTTCGCGCGTTATGACGCGCAAAAGGAAGGAACGGTGTATGCCAAATTTTCGGCAAATTTATTTACGGAAAACCGGCAAAAAGTAGCATTTTATTTTCAGCAAATCGAACAAACCTTTGCGCGTCTTGAGCAGGCGGATCCCAGCAATCTTGAAGCGTTGCAGTTTTACACGCAAAAACTGTCGGCGCAATGCACCGCACTTTCCGATGCCTTAACCCGACAACAGCAAAACGACCAACCCTTTCCGCGCAAAACCAAGGAAGAACCTAAACCCGCCGGTAAACGCCGTCATCCCGTACACAGTTTGCCGCCCCGTGAACGGTTAGCGAAATATTATGACTATCTGGCATCGTTCAATGAAAAAATTCAGGTTGAACAGGATACGTTGGAAAAAGCACAGCGTGAAGGTCGACTTGTTAATAAACAAATGCTGGAGCAATTAGAACAGCGCCGTGCCCGTTGTTTGGAAGCGATTGACGTGCTGGAAGAATATTTGGTTTTTGTCGAAAAGCAAAAA","","","22434","MNSISIQRLKQSLQHFFARYDAQKEGTVYAKFSANLFTENRQKVAFYFQQIEQTFARLEQADPSNLEALQFYTQKLSAQCTALSDALTRQQQNDQPFPRKTKEEPKPAGKRRHPVHSLPPRERLAKYYDYLASFNEKIQVEQDTLEKAQREGRLVNKQMLEQLEQRRARCLEAIDVLEEYLVFVEKQK","2016077","","conserved hypothetical protein","Cytoplasm","","
noIPR
unintegrated
unintegrated
PD099685\"[30-178]TQ8ZC93_YERPE_Q8ZC93;


","No hits to the COGs database.","","Residues 35 to 181 match (1e-17) PD:PD177636 which is described as PROTEOME PM0990 COMPLETE ","","","","","","","","","","","","Tue Jan 21 16:45:20 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02872 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02873","2017687","2016305","1383","ATGAATGAATACGATTCATCAAAAATGGCGGATTTATTACACAGTACGCATGGTTTGGAACTCACCGAAGTGCCGGAAGAAGCGGATGTTTTGCTATTGAATACCTGTTCCATTCGCGAAAAAGCACAGGAAAAAGTGTTCCATCAATTAGGTCGCTGGAAAGAATTAAAAAAGAGCAATCCGAATTTATTGATTGGCGTGGGCGGTTGTGTAGCATCGCAGGAAGGTGAACATATTCGCACCCGTGCCCCTTATGTGGATATTATTTTCGGGCCGCAAACCCTGCACCGTTTACCGGAAATGATTAACCAAATTCGCGGTGGCAAAAGTGCTGTGGTGGATATTAGTTTCCCGGAAATCGAAAAATTCGACCGGTTGCCGGAACCGCGCGCAGAAGGCCCGACTGCCTTTGTTTCTATCATGGAAGGCTGTAATAAATACTGTACTTACTGCGTGGTGCCTTATACCCGTGGCGAGGAAGTTAGCCGTCCGGTGGATGATATTTTATTTGAAATTGCCCAGTTGGCGGAGCAAGGCGTGCGCGAAGTGAATTTGCTCGGCCAGAACGTGAACGCCTATCGTGGTCCGACATTTGATGGCGATATTTGCACCTTCGCCGAATTGTTGCGTTTGGTAGCGGCCATTGACGGTATCGATCGTTTGCGTTTTACCACCAGCCATCCTATTGAATTCACCGATGATATTATCGATGTGTATCGTGATACGCCAGAATTGGTGAGTTTCCTGCATTTGCCGGTGCAATCCGGTTCCGATCATGTGTTGAACATGATGAAACGCGGACATACAGCGATTGAATATAAGTCTATTATTCGTAAGCTCAAAGCGGTGCGCCCGCATATTCAAGTCAGTTCTGACTTTATCGTGGGCTTCCCGGGCGAAACCAACGAAGATTTCGAGCAAACCATGAATTTGATTGCGCAAGTGAATTTCGATATGAGCTTCAGCTTCATTTATTCCGCACGTCCCGGCACGCCGGCGGCGGATTATCCTGACGATGTCAGCGAAGAAGAGAAAAAACAACGCCTTTATTTGTTGCAACAACGCATTAATAACCAAGCGGCGCAGTTCAGCCGCGCCATGTTGGGATCCGAGCAACGCGTGTTGGTGGAAGGTCCGTCGAAAAAAGACATTATGGAATTGACGGGACGTACGGAAACCAACCGCATCGTGAATTTCCAAGGCACACCGGATATGATCGGCAAGTTCGTAGATATTAAAATCACTGACGTGTTTACCAACTCCCTACGTGGTGAAGTGGTGCGCACCGAAGATCAAATGGGCTTGCGTGTGTTGCAATCGCCGCAAATGGTGATTAACCGCACCCGTAAGGAAGATGAACTTGGCGTAGGGCGCTATGTTGGT","","","53592","MNEYDSSKMADLLHSTHGLELTEVPEEADVLLLNTCSIREKAQEKVFHQLGRWKELKKSNPNLLIGVGGCVASQEGEHIRTRAPYVDIIFGPQTLHRLPEMINQIRGGKSAVVDISFPEIEKFDRLPEPRAEGPTAFVSIMEGCNKYCTYCVVPYTRGEEVSRPVDDILFEIAQLAEQGVREVNLLGQNVNAYRGPTFDGDICTFAELLRLVAAIDGIDRLRFTTSHPIEFTDDIIDVYRDTPELVSFLHLPVQSGSDHVLNMMKRGHTAIEYKSIIRKLKAVRPHIQVSSDFIVGFPGETNEDFEQTMNLIAQVNFDMSFSFIYSARPGTPAADYPDDVSEEEKKQRLYLLQQRINNQAAQFSRAMLGSEQRVLVEGPSKKDIMELTGRTETNRIVNFQGTPDMIGKFVDIKITDVFTNSLRGEVVRTEDQMGLRVLQSPQMVINRTRKEDELGVGRYVG","2016140","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR002792
Domain
Deoxyribonuclease/rho motif-related TRAM
PF01938\"[365-428]TTRAM
PS50926\"[365-428]TTRAM
InterPro
IPR005839
Family
Protein of unknown function UPF0004
PTHR11918\"[1-435]TRADICAL SAM PROTEINS
TIGR00089\"[1-424]TTIGR00089: RNA modification enzyme, MiaB fa
PS01278\"[138-158]TUPF0004
InterPro
IPR006463
Family
tRNA-i(6)A37 modification enzyme MiaB
TIGR01574\"[1-427]TmiaB-methiolase: tRNA-i(6)A37 thiotransfera
InterPro
IPR006638
Domain
Elongator protein 3/MiaB/NifB
SM00729\"[134-354]TElp3
InterPro
IPR007197
Domain
Radical SAM
PF04055\"[138-312]TRadical_SAM
InterPro
IPR013785
Domain
Aldolase-type TIM barrel
G3DSA:3.20.20.70\"[142-338]Tno description
InterPro
IPR013848
Domain
Protein of unknown function UPF0004, N-terminal
PF00919\"[1-91]TUPF0004


","BeTs to 24 clades of COG0621COG name: 2-methylthioadenine synthetaseFunctional Class: JThe phylogenetic pattern of COG0621 is aompkz-qvdr-bcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit (3.8e-114) to 6/7 blocks of the IPB001861 family, which is described as \"Uncharacterized protein family UPF0004\". Interpro entry for IP:IPR001861. IPB001861B 28-38 0.00023 IPB001861C 56-79 3.7e-09 IPB001861D 136-186 9.9e-38 IPB001861E 208-237 1.7e-15 IPB001861F 249-269 4.5e-13 IPB001861G 285-328 7.3e-28","Residues 352 to 427 match (3e-08) PD:PD315216 which is described as PROTEOME COMPLETE YQEV SAV1292 OXIDOREDUCTASES TM0653 BH2372 CPE2025 FE-S SAV1576 ","","","","","","","","","","","","Tue Jan 21 16:32:01 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02873 is paralogously related to AA00397 (2e-36).","","","","","","Residues 365 to 428 (E-value = 3.2e-23) place AA02873 in the TRAM family which is described as TRAM domain (PF01938)","","","","","","","","1","","","" "AA02874","2017834","2017959","126","TTGGAAGATAAAATAAATACCACTCAATATCGTCAGAGAAATGAAAAAGTGACGGGAATTTTAAAAGATATTATTGTTGTCAGCGGAGGCGTGATTGGTGCGGCCTCGCCTTCGGTTTTAAAGATG","","","4526","LEDKINTTQYRQRNEKVTGILKDIIVVSGGVIGAASPSVLKM","2017959","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
tmhmm\"[20-40]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 15:02:42 2004","Mon Feb 23 15:02:42 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02874 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 15:02:42 2004","","","","","","","","","","","","","1","","","" "AA02875","2018070","2018210","141","ATGCAATCGGGCATGGATCTGTTTTATAAGGCGTTTAAGGAAAAGATTTTACCATTGAAAATGCTACGAAATATCGCATTAGTAGCGGCAGATAAAACCCCGTTGTTGAAAAAACAAGCCTTGCGTTACGCCTTGGGATTA","","","5334","MQSGMDLFYKAFKEKILPLKMLRNIALVAADKTPLLKKQALRYALGL","2018210","","conserved hypothetical protein (2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase)","Cytoplasm, Periplasm","This sequence is similar to gi|33152863, a predicted 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol from Haemophilus ducreyi. See also gi|23466876 from Haemophilus somnus 129PT.","No hits reported.","BeTs to 4 clades of COG0654COG name: 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductasesFunctional Class: H,CThe phylogenetic pattern of COG0654 is ------y--dr-bcefghsn-jx---Number of proteins in this genome belonging to this COG is","","Residues 1 to 47 match (1e-07) PD:PD251540 which is described as PROTEOME COMPLETE MONOOXYGENASE OXIDOREDUCTASE 1.14.13.- FAD HYDROXYLASE 2-OCTAPRENYL-3-METHYL-6-METHOXY-14-BENZOQUINOL FLAVOPROTEIN PM1002 ","","","","","","","","","","","","Mon Feb 23 15:00:16 2004","Mon Feb 23 15:01:51 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02875 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 14:59:55 2004","","","","","","","","","","","","","1","","","" "AA02876","2018813","2018433","381","GTGATCTGTCTCAATTATTCTTTAACTTTTTTTGAATATAATCCGCTCGCCAATTTTATTATGGAGATTAATTATATGAAAAAATTATTATTTGTTGGGCTTGTTAGTTTTCTATTAACCGGATGCACTATTCATAAAGAACTGGTTGCCACTGGTGGTAGTAAGGCAGATGGTACTATCGAGTTATCTTATACTTATGGCGGAATGCAGGTACCAGTAATTAATGAAGAACAAGGATTGCAATTAGCAAAAAAACGTTGTGAGTCTTGGGGATATAAAAACGCAGAGAAATTCGGCGGACATAAACAAGTTTGTTCTATGTATGGTGGTCTCGGATGTACCGAGTTTACAGTTACAATTCAGTATCAGTGTTTAGATAAA","","","14175","VICLNYSLTFFEYNPLANFIMEINYMKKLLFVGLVSFLLTGCTIHKELVATGGSKADGTIELSYTYGGMQVPVINEEQGLQLAKKRCESWGYKNAEKFGGHKQVCSMYGGLGCTEFTVTIQYQCLDK","2018268","","conserved hypothetical protein","Cytoplasm, Extracellular","","
noIPR
unintegrated
unintegrated
PD070660\"[26-124]TQ8ZNU5_SALTY_Q8ZNU5;
signalp\"[1-41]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Tue Jan 21 16:30:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02876 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02878","2019658","2018930","729","ATGACAGAACAACATAACCCCAAAAGTGCGGTTAATTTTCAAAACAAAATTCGCAAGCAAAAACCGCGCAAAGATCCCAATGCCCCTTTTATTCGTGAAAAGCTGGAATTACCTGATGGGCATAATAAACTGCTGTTGCATTCCTGCTGTGCGCCTTGCTCGGGCGAGGTGATGGAAGCGATTTTGGCGTCCGGTATCGAATTTACCATTTATTTTTACAATCCGAATATCCACCCGTTAAAAGAATATTTAATTCGTAAAGAAGAGAATATTCGTTTTGCGCAGAAATTCGGCATTCCGTTTATTGACGCGGATTATGATCGTCAGGAATGGTTTGATCGCGCCAAAGGCATGGAATGGGAGCCGGAGCGCGGCATTCGTTGCACCATGTGTTTTGATATGCGCTTTGAAAAAGCCGCCGAATATGCGCATGAACATGGTTTTCCGGTTTTTACCAGCTGCCTTGGTATTTCCCGCTGGAAAGATATGGATCAAATTAACGGCTGCGGGCATCGCGCAGCAGAAAAATATGATGACGTGATTTATTGGGATTACAACTGGCGCAAAGAAGGCGGCTCGCAACGCATGATCGAAATCAGCAAACGCGAGCGTTTTTATCAGCAGGAATATTGCGGTTGCGTCTATTCTTTACGCGACAGCAATAAATGGCGTGAACAAACCGGTCGCCAAAAAATCGAAATCGGTAAGCTTTACTATTCGCCGAATCAA","","","28924","MTEQHNPKSAVNFQNKIRKQKPRKDPNAPFIREKLELPDGHNKLLLHSCCAPCSGEVMEAILASGIEFTIYFYNPNIHPLKEYLIRKEENIRFAQKFGIPFIDADYDRQEWFDRAKGMEWEPERGIRCTMCFDMRFEKAAEYAHEHGFPVFTSCLGISRWKDMDQINGCGHRAAEKYDDVIYWDYNWRKEGGSQRMIEISKRERFYQQEYCGCVYSLRDSNKWREQTGRQKIEIGKLYYSPNQ","2018765","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003828
Family
Protein of unknown function DUF208
PF02677\"[44-239]TDUF208


","BeTs to 9 clades of COG1636COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG1636 is -------qv--l-----hsnu-x---Number of proteins in this genome belonging to this COG is","","Residues 8 to 43 match (3e-10) PD:PD209608 which is described as PROTEOME COMPLETE HI0882 ","","","","","","","","","","","","Tue Jan 21 16:30:19 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02878 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 44 to 239 (E-value = 1.3e-147) place AA02878 in the DUF208 family which is described as Uncharacterized BCR, COG1636 (PF02677)","","","","","","","","1","","","" "AA02879","2020649","2019663","987","ATGAATACAACAAATTTAATGGATATGAAGGCAATCCAGGCGTTAAGCCATGGGGATATGCAAAAAGTAAACGAATCAATTTTAGCCCAACTGAACTCCGATGTGGCGTTAATTAATCAGTTGGGTTTCTACATTGTGCAAGGTGGCGGCAAGCGTATTCGTCCGCTTATCGCTGTGTTGGCGGCTCGTGCATTGGGTTTCGATGGGCAGCAAGCCATCACCTGTGCGACTTTTGTCGAGTTTATTCATACCGCGTCTTTATTACACGACGATGTCATCGATGAATCGGATATGCGTCGCGGGCGTGCCACGGCGAATGCGGAATTCGGTAATGCGGCAAGCGTGTTGGTGGGTGATTTCATTTATACCCGCGCGTTCCAATTGGTTGCGCAGCTGGAGTCTTTGAAAATTTTACGCATTATGGCGGATGCCACTAATGTGTTGGCGGAAGGAGAAGTGCAACAATTAATGAACGTAAATGATCCGCAAACCAGCGAAGAAAATTATATGCGGGTGATTTACAGTAAAACCGCTCGTTTATTTGAGGTGGCGGCGCAGGCAGCGGCAATTATTGCCGGCGCGGATGACACGCAGGAAAAAGCATTACAGAATTACGGTCGTTATCTCGGCACCGCATTTCAATTGGTGGATGACGTTCTGGATTACAGCGCCAACGCAAACGCCTTAGGGAAAAATGTTGGTGATGATTTAGCCGAAGGAAAACCAACCCTTCCTTTGTTACACGCCATGCACCACGGCAATGCGCAGCAAGCCGCCTTAATCCGCAAAGCCATTGAGCAAGGAGGAAGACGTGATGCTATTGATGACGTATTAGCCATTATGGCGGAACACAACTCTTTAGATTACGCCATGAACCGCGCCAAACAAGAAGCGCAAAAAGCCGTTGATGCCATTCAATGTTTGCCGGAAAGCGAATATAAACTGGCGTTGATTTCCTTGGCATATTTATCCGTAGATAGAACCTAT","","","35849","MNTTNLMDMKAIQALSHGDMQKVNESILAQLNSDVALINQLGFYIVQGGGKRIRPLIAVLAARALGFDGQQAITCATFVEFIHTASLLHDDVIDESDMRRGRATANAEFGNAASVLVGDFIYTRAFQLVAQLESLKILRIMADATNVLAEGEVQQLMNVNDPQTSEENYMRVIYSKTARLFEVAAQAAAIIAGADDTQEKALQNYGRYLGTAFQLVDDVLDYSANANALGKNVGDDLAEGKPTLPLLHAMHHGNAQQAALIRKAIEQGGRRDAIDDVLAIMAEHNSLDYAMNRAKQEAQKAVDAIQCLPESEYKLALISLAYLSVDRTY","2019498","[FUNCTION] Supplies octaprenyl diphosphate, the precursor for the side chain of the isoprenoid quinones ubiquinone andmenaquinone. ","octaprenyl-diphosphate synthase","Cytoplasm","","
InterPro
IPR000092
Family
Polyprenyl synthetase
PTHR12001\"[12-328]TGERANYLGERANYL PYROPHOSPHATE SYNTHASE
PF00348\"[37-291]Tpolyprenyl_synt
PS00444\"[209-221]TPOLYPRENYL_SYNTHET_2
PS00723\"[87-101]TPOLYPRENYL_SYNTHET_1
noIPR
unintegrated
unintegrated
G3DSA:1.10.600.10\"[23-327]Tno description


","BeTs to 25 clades of COG0142COG name: Geranylgeranyl pyrophosphate synthaseFunctional Class: HThe phylogenetic pattern of COG0142 is aompkzyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 3.6e-29) to 5/5 blocks of the IPB000092 family, which is described as \"Polyprenyl synthetase\". Interpro entry for IP:IPR000092. IPB000092A 49-58 0.026 IPB000092B 79-90 7.2e-06 IPB000092C 91-106 1.9e-06 IPB000092D 151-156 2e+02 IPB000092E 209-231 4.4e-09","Residues 163 to 317 match (1e-08) PD:PD237751 which is described as PYROPHOSPHATE MITOCHONDRIAL GH23839P MITOCHONDRION ISOPRENE HPS HEXAPRENYL CG10585 SYNTHETASE PEPTIDE ","","","","","","","","","","","Tue Jan 21 16:29:00 2003","Tue Jan 21 16:29:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02879 is paralogously related to AA02051 (1e-24).","","","","","","Residues 37 to 291 (E-value = 1.3e-122) place AA02879 in the polyprenyl_synt family which is described as Polyprenyl synthetase (PF00348)","","","","","Jeong JH, Kitakawa M, Isono S, Isono K.Cloning and nucleotide sequencing of the genes, rpIU and rpmA, for ribosomal proteins L21 and L27 of Escherichia coli.DNA Seq. 1993;4(1):59-67.PMID: 8312607Choi YL, Nishida T, Kawamukai M, Utsumi R, Sakai H, Komano T.Cloning and sequencing of an Escherichia coli gene, nlp, highly homologous to the ner genes of bacteriophages Mu and D108.J Bacteriol. 1989 Sep;171(9):5222-5.PMID: 2670911Asai K, Fujisaki S, Nishimura Y, Nishino T, Okada K, Nakagawa T, Kawamukai M, Matsuda H.The identification of Escherichia coli ispB (cel) gene encoding the octaprenyl diphosphate synthase.Biochem Biophys Res Commun. 1994 Jul;202(1):340-5.PMID: 8037730","","Tue Jan 21 16:29:00 2003","1","","","" "AA02880","2020897","2021205","309","ATGTACGCAGTTTTCCAAAGTGGCGGTAAACAACACCGAGTAAGCGAAGGTCAAGTGGTTCGTTTGGAAAAACTTGAACTTGCAGCCGGCGCAACAGTTGAGTTTGATTCGGTGTTGATGGTTGCTAATGGTGAAGATGTTAAAATCGGTGCACCGGTCGTTGCCGGCGCGAAAGTAGTGGCTGAAGTAGTTGCACAAGGTCGTGGCGAGAAAATTAAAATCGTTAAGTTCCGTCGTCGCAAACACAGCCGTAAACAACAAGGTCATCGTCAGTGGTTCACAGAAGTGAAAATCACTGGGATTCAAGCA","","","13058","MYAVFQSGGKQHRVSEGQVVRLEKLELAAGATVEFDSVLMVANGEDVKIGAPVVAGAKVVAEVVAQGRGEKIKIVKFRRRKHSRKQQGHRQWFTEVKITGIQA","2021040","[FUNCTION] This protein binds to 23S ribosomal RNA in the presence of protein L20. ","50S ribosomal protein L21","Cytoplasm","","
InterPro
IPR001787
Family
Ribosomal protein L21
PD003604\"[1-101]TRL21_HAEIN_P44359;
PTHR21349\"[1-103]T50S RIBOSOMAL PROTEIN L21
PF00829\"[1-96]TRibosomal_L21p
TIGR00061\"[2-102]TL21: ribosomal protein L21
PS01169\"[72-94]TRIBOSOMAL_L21


","BeTs to 18 clades of COG0261COG name: Ribosomal protein L21Functional Class: JThe phylogenetic pattern of COG0261 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 4.7e-39) to 2/2 blocks of the IPB001787 family, which is described as \"Ribosomal protein L21\". Interpro entry for IP:IPR001787. IPB001787A 2-17 1.7e-08 IPB001787B 59-101 3e-29","Residues 1 to 101 match (1e-29) PD:PD003604 which is described as RIBOSOMAL L21 50S COMPLETE PROTEOME RRNA-BINDING CHLOROPLAST SUBUNIT PROBABLE MITOCHONDRION ","","","","","","","","","","","Tue Jan 21 16:25:17 2003","Tue Jan 21 16:25:17 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02880 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 96 (E-value = 2.3e-59) place AA02880 in the Ribosomal_L21p family which is described as Ribosomal prokaryotic L21 protein (PF00829)","","","","","Heiland I, Wittmann-Liebold B.Amino acid sequence of the ribosomal protein L21 of Escherichia coli.Biochemistry. 1979 Oct;18(21):4605-12.PMID: 387076Jeong JH, Kitakawa M, Isono S, Isono K.Cloning and nucleotide sequencing of the genes, rpIU and rpmA, for ribosomal proteins L21 and L27 of Escherichia coli.DNA Seq. 1993;4(1):59-67.PMID: 8312607Arnold RJ, Reilly JP.Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry.Anal Biochem. 1999 Apr;269(1):105-12.PMID: 10094780","","Tue Jan 21 16:25:17 2003","1","","","" "AA02881","2021229","2021483","255","ATGGCAACTAAAAAAGCTGGTGGTTCAACTCGTAACGGTCGTGATTCTGAAGCTAAACGTCTTGGTGTTAAACGTTTCGGTGGTGAGTCTGTATTAGCAGGTAGTATCATCGTTCGCCAACGTGGTACTAAGTTCCACGCGGGCAACAACGTTGGAATGGGACGTGACCACACCTTATTCGCGACAGCCGATGGTAAAGTAAAATTTGAAGTAAAAGGCGAAAAAAGCCGTAAATACGTAAGTATCGTTACTGAG","","","9122","MATKKAGGSTRNGRDSEAKRLGVKRFGGESVLAGSIIVRQRGTKFHAGNNVGMGRDHTLFATADGKVKFEVKGEKSRKYVSIVTE","2021318","","50S ribosomal protein L27","Cytoplasm, Extracellular","","
InterPro
IPR001684
Family
Ribosomal protein L27
PD003114\"[2-75]TRibosomal_L27
PR00063\"[4-28]T\"[29-53]T\"[54-78]TRIBOSOMALL27
PTHR15893\"[8-83]TRibosomal_L27
PF01016\"[2-83]TRibosomal_L27
TIGR00062\"[1-83]TL27
PS00831\"[34-48]TRIBOSOMAL_L27
noIPR
unintegrated
unintegrated
SSF110324\"[20-84]TSSF110324


","BeTs to 19 clades of COG0211COG name: Ribosomal protein L27Functional Class: JThe phylogenetic pattern of COG0211 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.2e-50) to 2/2 blocks of the IPB001684 family, which is described as \"Ribosomal protein L27\". Interpro entry for IP:IPR001684. IPB001684A 8-37 6.7e-22 IPB001684B 38-69 1.4e-27","Residues 1 to 83 match (7e-29) PD:PD003114 which is described as RIBOSOMAL L27 50S PROTEOME COMPLETE CHLOROPLAST 60S MITOCHONDRIAL TRANSIT PRECURSOR ","","","","","","","","","","","","Tue Jan 21 16:22:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02881 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 83 (E-value = 5.2e-55) place AA02881 in the Ribosomal_L27 family which is described as Ribosomal L27 protein (PF01016)","","","","","Jeong JH, Kitakawa M, Isono S, Isono K.Cloning and nucleotide sequencing of the genes, rpIU and rpmA, for ribosomal proteins L21 and L27 of Escherichia coli.DNA Seq. 1993;4(1):59-67.PMID: 8312607Chen R, Mende L, Arfsten U.The primary structure of protein L27 from the peptidyl-tRNA binding site of Escherichia coli ribosomes.FEBS Lett. 1975 Nov;59(1):96-9.PMID: 1225626Urlaub H, Kruft V, Bischof O, Müller EC, Wittmann-Liebold B.Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies.EMBO J. 1995 Sep;14(18):4578-88.PMID: 7556101Arnold RJ, Reilly JP.Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry.Anal Biochem. 1999 Apr;269(1):105-12.PMID: 10094780","","Tue Jan 21 16:22:15 2003","1","","","" "AA02883","2021558","2022487","930","ATGCAACAACAACCTTTAGCCGGTTTTTTACTCGCGTTAACCGCCGTCTGTATGTGGGGTGCGTTGCCTATCGCCTTGCAACAGATCGTCGCAGTCATGGATGCCCAAACCATTGTGTGGTATCGCTTTATCACATCGGCGATCGGTTTATTTATTTTATTGGGATTACGTAAAACGCTGCCAAAACCCACCGCACTTCGTCAGCGTTATCTCCTTTTGATTATGCTGGGCATTCTTGGGCTATCGGCAAATTTCTTCTTATTTAATCTGGCGCTGAACTATATTCCACCGACCAGCAGCCAAGTGCTCAGTCCGTTATCCTCGTTTATCATGCTATTTGTCGGTGTGTTTGTGTTTAAAGAACACATCGGGCTCCATCAAAAAATCGGTTTGGTTATTTTAATTCTCGGCTTGGTCTTATTTTTCAACCAACGCTTTAGTGATTTCTTACAGCTCAATGATTATTTTAAAGGCGTTGTTATTGCCCTATGCGCCAGCTCCTGCTGGGTTGCCTATGGCATGGCGCAAAAGCTGATGTTGAGCCGTTTCAGTTCGCAACAAATTTTGCTCATAATTTATGTCGGCTGCACGATCATTTTTACGCCCTTTGCCAATATTCAGCAGGTGAGCGCGTTAAATTCCTTTCAGCTGGGCTGCTTGATTTTTTGTTGCCTTAATACCATTATTGCTTACGGCACTTACGGCGAAGCGCTAAATCGCTGGGATGTTTCAAAAGTCAGCGCCATCATGACGCAGATTCCGATTTTCACGATTATTTTCACAGAAATTTTAATTGCCGTTTATCCACAATTATTCGTTGATCAGGAACTCAATTGGATCAGCTACCTTGGTGCGATTGCCGTCGTTTCAGGTTCATTGCTCTCCGTGTTGGGACACAAACTTCCCGCGATTTTTCATCGTAAAAATTGT","","","34523","MQQQPLAGFLLALTAVCMWGALPIALQQIVAVMDAQTIVWYRFITSAIGLFILLGLRKTLPKPTALRQRYLLLIMLGILGLSANFFLFNLALNYIPPTSSQVLSPLSSFIMLFVGVFVFKEHIGLHQKIGLVILILGLVLFFNQRFSDFLQLNDYFKGVVIALCASSCWVAYGMAQKLMLSRFSSQQILLIIYVGCTIIFTPFANIQQVSALNSFQLGCLIFCCLNTIIAYGTYGEALNRWDVSKVSAIMTQIPIFTIIFTEILIAVYPQLFVDQELNWISYLGAIAVVSGSLLSVLGHKLPAIFHRKNC","2022322","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR000620
Domain
Protein of unknown function DUF6, transmembrane
PF00892\"[17-143]T\"[167-260]TDUF6
InterPro
IPR003439
Domain
ABC transporter related
PS00211\"[170-184]?ABC_TRANSPORTER_1
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[51-235]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-20]?signal-peptide
tmhmm\"[5-24]?\"[38-56]?\"[71-91]?\"[101-119]?\"[124-142]?\"[152-172]?\"[187-205]?\"[211-231]?\"[246-268]?\"[278-298]?transmembrane_regions


","BeTs to 11 clades of COG0697COG name: Permeases of the drug/metabolite transporter (DMT) superfamilyFunctional Class: G,E,RThe phylogenetic pattern of COG0697 is aompkzyqvd-lbcefghsnujxit-Number of proteins in this genome belonging to this COG is","","Residues 8 to 127 match (5e-24) PD:PD058316 which is described as PROTEOME COMPLETE TRANSMEMBRANE MEMBRANE INTEGRAL PLASMID PROBABLE PERMEASE FAMILY TRANSPORTER ","","","","","","","","","","","","Tue Jan 21 16:18:31 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02883 is paralogously related to AA02885 (2e-96) and AA02980 (2e-13).","","","","","","Residues 167 to 297 (E-value = 3.4e-09) place AA02883 in the DUF6 family which is described as Integral membrane protein DUF6 (PF00892)","","","","","","","","1","","","" "AA02885","2022568","2023482","915","ATGAAACAACAACCACTACTTGGTTTTCTTTTTGCACTCATTACCGCGATGGCGTGGGGCTCTTTACCCATCGCGCTGAAACAGGTGGTTACGGCAATGAACGTGCAAACCATCGTATGGTATCGTTTCGTTGTTGCCGGTTGCGCCCTTTTGTTATTACTCGGCTATAAAAAAACGCTGCCCGATTTATCCAAACTGGGTTATTTCTGGTTACTGGCAATCATTGGCATACTTGGCTTGGCTGGCAATTTCTTCTTATTTAACAGTTCATTAAATTATATTGAACCCTCCGTTGCACAAATTTTTATTCATTTATCCTCCTTCGGCATGCTCATTTGCGGCGTAGTGATTTTTAAGGAAAAATTAGGCTTGCATCAAAAAATCGGCTTGGTCTTATTGCTTATCGGTTTGGGACTCTTTTTCAACGATAAATTAGAGGTTTTCAACGGATTAAACACCTACACTACCGGCGTGCTTATCAGCGTGAGTGCTACGCTGGTATGGGTGGCCTACGGTATGGCGCAAAAATTAATGTTACGAAAATTCAGCGCCCAACAAATTTTATTAATGATTTATTTCGGCTGCGCCATCGTCTTTACGCCCTTCGCCGAATTTTCACAAGTTCAGGGATTAACCCCACTGGCGCTAGGCTGCTTCATTTATTGCTGCTTAAACACTCTATTCGGTTACGGCGCTTACGCGGAAGCCCTAAACCGCTGGGAAGTATCCAAAGTCAGCGTGGTAATTACGTTGGTTCCCTTGTTTACTATTCTATTTGCTCATATGGCGCACTATATTTCCCCGACGAATTTCTCCGCACTGAAATTAAATACCATTAGCTATATTGGTACGTTTATTGTAGTATGCGGAGCAATTTTATCCGCCATAGGACATAAGCTATTTCCTGCTAACCGG","","","33572","MKQQPLLGFLFALITAMAWGSLPIALKQVVTAMNVQTIVWYRFVVAGCALLLLLGYKKTLPDLSKLGYFWLLAIIGILGLAGNFFLFNSSLNYIEPSVAQIFIHLSSFGMLICGVVIFKEKLGLHQKIGLVLLLIGLGLFFNDKLEVFNGLNTYTTGVLISVSATLVWVAYGMAQKLMLRKFSAQQILLMIYFGCAIVFTPFAEFSQVQGLTPLALGCFIYCCLNTLFGYGAYAEALNRWEVSKVSVVITLVPLFTILFAHMAHYISPTNFSALKLNTISYIGTFIVVCGAILSAIGHKLFPANR","2023317","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR000620
Domain
Protein of unknown function DUF6, transmembrane
PF00892\"[17-142]T\"[166-261]TDUF6
noIPR
unintegrated
unintegrated
signalp\"[1-20]?signal-peptide
tmhmm\"[5-24]?\"[38-56]?\"[66-86]?\"[100-118]?\"[128-148]?\"[154-172]?\"[187-205]?\"[211-233]?\"[245-265]?\"[279-297]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Tue Jan 21 16:16:25 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02885 is paralogously related to AA02883 (2e-96).","","","","","","Residues 166 to 296 (E-value = 1.5e-13) place AA02885 in the DUF6 family which is described as Integral membrane protein DUF6 (PF00892)","","","","","","","","1","","","" "AA02886","2023522","2024694","1173","ATGAAATTTATTGATGAAGCTTTGATTCACGTTGAAGCCGGTGACGGCGGCAATGGTTGTGCCAGTTTCCGTCGTGAAAAATATATCCCAAAAGGCGGTCCCGACGGCGGTGACGGCGGTGACGGCGGTGATGTTTATTTAATCGCCGATGAAAACCTCAACACCCTCATTGACTACCGCTTTGAAAAACGTTTCGCCGCCGAACGCGGGGAAAACGGGTTCAGTGCAAACTGCACCGGCCATCGCGGCAAAGATATTACCTTACACGTGCCGGTGGGCACCCGCGCCATCGACAACGATACGCAGGAAGTCATCGGTGATTTAACCAAAAATGGTATGAAATTATTGGTGGCGAAAGGCGGCTATCACGGCTTGGGCAATACCCGTTTTAAATCTTCAGTCAACCGCGCACCGCGCCAAAAAACCATGGGTACGGCAGGGGAAAAACGTGATCTCTTGTTAGAATTAATGCTCCTCGCCGATGTGGGAATGCTCGGTTTACCGAATGCCGGCAAATCCACCTTTATCCGCGCTGTTTCCGCCGCCAAACCGAAAGTCGCCGATTATCCGTTTACCACCTTGGTACCAAGTTTAGGCGTGGTGAAAGTAGATGACAATCGCAGTTTTGTGATCGCCGACATTCCTGGCTTAATTGAAGGCGCATCGGAAGGAGCAGGCTTGGGTATCCGCTTCCTGAAACACTTGGAACGTTGCCGCGTGTTGATTCATTTGGTGGATATCAACCCAATTGATGATTCCAACCCGGCGGATAACGTGGCGATTATCGAATCGGAATTGTTCCAATACAGCGAGTCCTTGGCGGAAAAACCGCGCTGGCTGGTGTTCAACAAAATCGATACGCTCAGTGATGAAGAAGCCCATGCGCGAGCGAAAGAGATCACCGAACGTCTGGGCCGGGAGGAAGGTTATTATTTAATTTCCGCCGCCACCGGTAAAAACGCCCCGCAACTGTGCCGCGATATTATGGACTTCCTGGAAGCCCACCCGCGCAAAACAGAAAAAACGCCGGTAGAAAATGAAGAAGTCAAATTCAAATGGGAAGATTATCATCAGGAGCAATTGGAAAATGCCGATGTTGATGATGAAGAGGATAATGACTGGGATGACTGGTCGGAAGACGATGAAGAAGGCGTGGAAATTATCTATAAGCCT","","","43255","MKFIDEALIHVEAGDGGNGCASFRREKYIPKGGPDGGDGGDGGDVYLIADENLNTLIDYRFEKRFAAERGENGFSANCTGHRGKDITLHVPVGTRAIDNDTQEVIGDLTKNGMKLLVAKGGYHGLGNTRFKSSVNRAPRQKTMGTAGEKRDLLLELMLLADVGMLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVKVDDNRSFVIADIPGLIEGASEGAGLGIRFLKHLERCRVLIHLVDINPIDDSNPADNVAIIESELFQYSESLAEKPRWLVFNKIDTLSDEEAHARAKEITERLGREEGYYLISAATGKNAPQLCRDIMDFLEAHPRKTEKTPVENEEVKFKWEDYHQEQLENADVDDEEDNDWDDWSEDDEEGVEIIYKP","2024529","","OBG-related GTP-binding protein","Cytoplasm","","
InterPro
IPR002917
Domain
GTP-binding protein, HSR1-related
PF01926\"[160-286]TMMR_HSR1
InterPro
IPR006073
Domain
GTP1/OBG
PR00326\"[162-182]T\"[183-201]T\"[211-226]T\"[228-246]TGTP1OBG
InterPro
IPR006074
Domain
GTP1/OBG domain
PS00905\"[213-226]TGTP1_OBG
InterPro
IPR006169
Domain
GTP1/OBG subdomain
PF01018\"[3-158]TGTP1_OBG
InterPro
IPR014100
Family
GTP-binding protein Obg/CgtA
TIGR02729\"[3-289]TObg_CgtA: GTP-binding protein Obg/CgtA
noIPR
unintegrated
unintegrated
G3DSA:2.70.210.12\"[2-158]Tno description
G3DSA:3.40.50.300\"[158-365]Tno description
PTHR11702\"[1-345]TDEVELOPMENTALLY REGULATED GTP-BINDING PROTEIN-RELATED
PTHR11702:SF3\"[1-345]TMITOCHONDRIAL GTPASE 2(YEAST)/OBG-RELATED


","BeTs to 19 clades of COG0536COG name: Predicted GTPaseFunctional Class: RThe phylogenetic pattern of COG0536 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2e-19) to 1/1 blocks of the IPB000765 family, which is described as \"GTP1/OBG family\". Interpro entry for IP:IPR000765. IPB000765 160-203 1.9e-19","Residues 1 to 30 match (2e-09) PD:PD585178 which is described as COMPLETE PROTEOME GTP-BINDING GTP1/OBG FAMILY SPO0B-ASSOCIATED OBG PROTEIN BINDING GTP ","","","","","Wed Feb 19 07:01:57 2003","","","","","","","Tue Jan 21 16:15:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02886 is paralogously related to AA02417 (1e-13) and AA00689 (8e-06).","","","","","","Residues 16 to 288 (E-value = 3.9e-127) place AA02886 in the GTP1_OBG family which is described as GTP1/OBG family (PF01018)","","","","","Buglino J, Shen V, Hakimian P, Lima CD. Structural and biochemical analysis of the obg GTP binding protein. Structure (Camb). 2002 Nov;10(11):1581-92. PMID: 12429099 Dutkiewicz R, Slominska M, Wgrzyn G, Czy A. Overexpression of the cgtA ( yhbZ, obgE) Gene, Coding for anEssential GTP-Binding Protein, Impairs the Regulation of Chromosomal Functions in Escherichia coli. Curr Microbiol. 2002 Dec;45(6):440-5. PMID: 12402086Sikora-Borgula A, Slominska M, Trzonkowski P, Zielke R, Mysliwski A, Wegrzyn G, Czyz A.A role for the common GTP-binding protein in coupling of chromosome replication to cell growth and cell division.Biochem Biophys Res Commun. 2002 Mar 29;292(2):333-8.PMID: 11906166 Slominska M, Konopa G, Wegrzyn G, Czyz A.mpaired chromosome partitioning and synchronization of DNA replication initiation in aninsertional mutant in the Vibrio harveyi cgtA gene coding for a common GTP-binding protein.Biochem J. 2002 Mar 15;362(Pt 3):579-84.PMID: 11879184","","Wed Feb 19 07:01:57 2003","1","","","" "AA02888","2025121","2024768","354","ATGCGTGCCGGCAAAGTCAATTTGAGTGACAGCTATGTGATTTTTAAAAACGGTGAAGCTTTCTTATTCGGCGCAACCATTCAGCCTCTAAGCGTGGCATCAACGCACATTGTGTGCGACCCGACCCGCACCCGCAAATTATTGCTTAAACAGCGTGAACTGGATTCCTTATTCGGCAAAGCCAACCGCGACGGATTTACCCTGATTGCCCTTTCCCTCTCTTGGAAAGGCGCGTGGGCGAAAGTCAAAATTGGCTTGGCAAAAGGGAAAAAACAACAGGACAAGCGGGAAGACATTAAAGAACGTGAATGGAAAGTGGTAAAAGAGCGTATTATGAAAAACGCGCGAAAAGGG","","","18172","MRAGKVNLSDSYVIFKNGEAFLFGATIQPLSVASTHIVCDPTRTRKLLLKQRELDSLFGKANRDGFTLIALSLSWKGAWAKVKIGLAKGKKQQDKREDIKEREWKVVKERIMKNARKG","2024603","[FUNCTION] Binds specifically to the ssrA RNA (tmRNA) and is required for stable association of ssrA with ribosomes (by similarity). ","ssrA-binding protein, small protein B","Cytoplasm, Periplasm","","
InterPro
IPR000037
Family
SmpB protein
PD004488\"[1-95]TSSRP_HAEIN_P44967;
PF01668\"[1-37]TSmpB
TIGR00086\"[1-113]TsmpB: SsrA-binding protein
noIPR
unintegrated
unintegrated
G3DSA:2.40.280.10\"[1-92]Tno description


","No hits to the COGs database.","Significant hit ( 4.6e-42) to 2/3 blocks of the IPB000037 family, which is described as \"SmpB protein\". Interpro entry for IP:IPR000037. IPB000037B 38-75 3.1e-19 IPB000037C 81-113 1.4e-21","Residues 1 to 103 match (1e-44) PD:PD004488 which is described as COMPLETE PROTEOME SSRA-BINDING RNA-BINDING SMALL B SMPB HOMOLOG PROBABLE TMRNA-BINDING ","","","","","","","","","","","Tue Jan 21 15:51:18 2003","Tue Jan 21 15:51:18 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02888 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 37 (E-value = 2.2e-06) place AA02888 in the SmpB family which is described as SmpB protein (PF01668)","","","","","Karzai,A.W., Susskind,M.M. and Sauer,R.T. SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA) EMBO J. 18 (13), 3793-3799 (1999) PubMed: 10393194Williams KP.Traffic at the tmRNA Gene.J Bacteriol. 2003 Feb;185(3):1059-70.PMID: 12533482Wower J, Zwieb CW, Hoffman DW, Wower IK.SmpB: a protein that binds to double-stranded segments in tmRNA and tRNA.Biochemistry. 2002 Jul 16;41(28):8826-36.PMID: 12102625Dong G, Nowakowski J, Hoffman DW.Structure of small protein B: the protein component of the tmRNA-SmpB system for ribosome rescue.EMBO J. 2002 Apr 2;21(7):1845-54.PMID: 11927568 Hanawa-Suetsugu K, Takagi M, Inokuchi H, Himeno H, Muto A.SmpB functions in various steps of trans-translation.Nucleic Acids Res. 2002 Apr 1;30(7):1620-9.PMID: 11917023","","Wed Jan 29 15:48:59 2003","1","","","" "AA02889","2025185","2025331","147","GTGTCTGGCGCGTTTATTCAGCGCAATCGTGTTAGAACCGGGTTTTACTTTTTTCTTGGTCATAATCTGTTGGAAATGAAAAATAAATTAGCGCTCATTCTACCGAATCCGCACAAAGATAGCAAAACCCGCCGGATTGCTATAACA","","","5666","VSGAFIQRNRVRTGFYFFLGHNLLEMKNKLALILPNPHKDSKTRRIAIT","2025331","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 13:43:57 2004","Mon Feb 23 13:43:57 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02889 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 13:43:57 2004","","","","","","","","","","","","","1","","","" "AA02890","2025592","2025458","135","ATGAATTATCGTAAGAGTCAGAAAAATGATCTATCGCAAAATAGTTATTTTGTAAAGATCAATTCACAAAAAAGAACGATTTATTTACTCTTCTATAAAAAAGGAAAAAATAAAGGCGAAAAATTATGTTTTATT","","","5449","MNYRKSQKNDLSQNSYFVKINSQKRTIYLLFYKKGKNKGEKLCFI","2025458","","hypothetical protein","Cytoplasm, Extracellular","There are no significant similarities to the NR database.","
InterPro
IPR012317
Domain
PARP, catalytic
PS51059\"[1-41]TPARP_CATALYTIC


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 13:36:25 2004","Mon Feb 23 13:36:25 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02890 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 13:36:25 2004","","","","","","","","","","","","","1","","","" "AA02891","2025615","2026430","816","ATGCAACAAAAATTACTTGTCTCAACCATTGCGCTTGCCTTATCTTGCAGCGTTTATGCCGCCAAAGTACCTGAAGGAACACAGCTCGCAGAAACACAGAATATCGTGATCAACAACGGTTCCGAGCCACAAAGTTTTGACCCGCACAAAACCGACGGGATCCCAGAAGCAGAAGTCGCTTATCAATTATTTGAGGGTTTGGTGACTACTGATTCCGACGGCAATTTGATTACGGGTGTGGCAGAAAGCTGGGAAAACACGCCCGATTACAAAACCTGGACATTCCACCTGCGCAAAGATGCCAAATGGTCAAACGGTGAACCTATTACGGCAAATGATTTCGTCTTCGCCTGGCGTCGTTTAGTAACACCGGCAACCGCCTCACCTTACGCCAGTTTCCTGGATTATCTTCAAGTTGAAAACGCACAAGACATTATTGACGGCAAGAAAAAACCGGAAGAACTTGGCGTGGAAGCAAAAGACAATTACACTTTTGTCGTTCACACCACAAACCCGGTGCCTTATGCGGTGGGTTTGACGACCCACCAATCCTTGTTACCGTTACCGCAAAAAATCGTGGAAAAATTCGGTGACGATTGGGTGAAAAAAGACAATATCGTCGGTAACGGTGCCTATAAATTAAAAAATCACGTCATCAACGAAAAAATTGAATTTGAGCGCAACCCGCAATATTGGAATGACAAAGAAACGCAAATTAACAACGCCACCTTCTTAGCCATTGAGAATTCCAGCACCGACGTGGCACGTTATCGTGCAGGAGATTTGGACATCACCAGCCACGCCCTTCCGCCGGAG","","","30372","MQQKLLVSTIALALSCSVYAAKVPEGTQLAETQNIVINNGSEPQSFDPHKTDGIPEAEVAYQLFEGLVTTDSDGNLITGVAESWENTPDYKTWTFHLRKDAKWSNGEPITANDFVFAWRRLVTPATASPYASFLDYLQVENAQDIIDGKKKPEELGVEAKDNYTFVVHTTNPVPYAVGLTTHQSLLPLPQKIVEKFGDDWVKKDNIVGNGAYKLKNHVINEKIEFERNPQYWNDKETQINNATFLAIENSSTDVARYRAGDLDITSHALPPE","2026265","[FUNCTION] This protein is a component of the oligopeptide permease, a binding protein-dependent transport system, it binds peptides up to five amino acids long with high affinity. ","oligopeptide-binding protein precursor","Periplasm","","
InterPro
IPR000914
Family
Bacterial extracellular solute-binding protein, family 5
PF00496\"[75-271]TSBP_bac_5
PS01040\"[81-103]TSBP_BACTERIAL_5
noIPR
unintegrated
unintegrated
G3DSA:3.40.190.10\"[207-265]Tno description
G3DSA:3.90.76.10\"[33-199]Tno description
PS51257\"[1-16]TPROKAR_LIPOPROTEIN
signalp\"[1-20]?signal-peptide


","BeTs to 19 clades of COG0747COG name: ABC-type dipeptide/oligopeptide/nickel transport systems, periplasmic componentsFunctional Class: E,PThe phylogenetic pattern of COG0747 is ao-pkz-qvdrlbcefgh--uj-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 3.8e-13) to 2/3 blocks of the IPB000914 family, which is described as \"Bacterial extracellular solute-binding protein, family 5\". Interpro entry for IP:IPR000914. IPB000914A 78-85 5 IPB000914B 89-106 2.3e-11","Residues 35 to 81 match (1e-07) PD:PD578143 which is described as COMPLETE PROTEOME ABC PERIPLASMIC OLIGOPEPTIDE-BINDING OLIGOPEPTIDE TRANSPORTER PRECURSOR TRANSPORTER PEPTIDE-BINDING ","","","","","","","","","","","Tue Jan 21 15:47:52 2003","Wed Jan 22 11:29:30 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02891 is paralogously related to AA01607 (3e-30), AA00458 (4e-11) and AA01573 (1e-07).","","","","","","Residues 6 to 272 (E-value = 1.6e-06) place AA02891 in the SBP_bac_5 family which is described as Bacterial extracellular solute-binding proteins, family 5 (PF00496)","","","","","Hiles,I.D., Gallagher,M.P., Jamieson,D.J. and Higgins,C.F.Molecular characterization of the oligopeptide permease of Salmonella typhimurium. J. Mol. Biol. 195 (1): 125-142 (1987) PubMed: 2821267.Hiles,I.D. and Higgins,C.F. Peptide uptake by Salmonella typhimurium. The periplasmic oligopeptide-binding protein. Eur. J. Biochem. 158 (3): 561-567 (1986) PubMed: 3525163.Tame,J.R., Murshudov,G.N., Dodson,E.J., Neil,T.K., Dodson,G.G., Higgins,C.F. and Wilkinson,A.J. The structural basis of sequence-independent peptide binding by OppA protein. Science 264 (5165): 1578-1581 (1994) [PubMed: 8202710].","","Wed Feb 5 15:30:10 2003","1","","","" "AA02892","2026542","2027237","696","GTGAGAAAAGCATTAAATTTAGCCTTAGATCGTAATGTGATTACCGATAAAGTGCTGGGACAAGGTCAAACACCAACCTATGTGTTTACCCCGCCGTACATTAATGAAGGCGAGCTGATTCAACAACCGGCTTACAGCAAAGAACCGATGGCTCAACGCAATGAGGAAGCCATTAAACTGTTGGAAGAAGCCGGATTCAGCAAAGCGAATCCGCTGAAATTCACGATTCTTTACAACACCAATGAGAACCACAAAAAAGTGGCGATCGCCGCCGCCTCCATGTGGAAAGCCAATACAAAAGGTTTGGTGGATGTCAAGCTGGAAAATCAAGAATGGAAAACCTATATCGACAACCGTCGCGGACAGCGTTATGACGTCGCGCGCGCCGGCTGGAATGCAGACTACAACCAGGCCAGCACGTTCGGGAACTATTTCTTATCCAATTCCAGTAACAACACCGCCAAGTACAAGAATGTAGAATACGACAAAGCCATTGCCGATTCTTATCTTGCTACCGATGAGAAAGGTCGTGCGCAAGCCTATGCCAAAGCCGAAGAAATTCTGGCAAATGATTTCGCCGTGATTCCGGTATATAACTATGTGAATCCGCGTTTGGTGAAACCTTATGTGAAAGGCTACAGCGGCAAAGATCCGCAAGATAACGTTTTGTTACGCAACCTTTATATTATTAAACAT","","","26328","VRKALNLALDRNVITDKVLGQGQTPTYVFTPPYINEGELIQQPAYSKEPMAQRNEEAIKLLEEAGFSKANPLKFTILYNTNENHKKVAIAAASMWKANTKGLVDVKLENQEWKTYIDNRRGQRYDVARAGWNADYNQASTFGNYFLSNSSNNTAKYKNVEYDKAIADSYLATDEKGRAQAYAKAEEILANDFAVIPVYNYVNPRLVKPYVKGYSGKDPQDNVLLRNLYIIKH","2027072","[FUNCTION] Part of the binding-protein-dependent transport system for oligopeptides. Probably responsible for energy coupling to the transport system (by similarity). ","oligopeptide ABC transporter, periplasmic-binding protein","Periplasm","","
InterPro
IPR000914
Family
Bacterial extracellular solute-binding protein, family 5
PF00496\"[1-153]TSBP_bac_5
noIPR
unintegrated
unintegrated
G3DSA:3.10.105.10\"[1-201]Tno description


","BeTs to 16 clades of COG0747COG name: ABC-type dipeptide/oligopeptide/nickel transport systems, periplasmic componentsFunctional Class: E,PThe phylogenetic pattern of COG0747 is ao-pkz-qvdrlbcefgh--uj-itwNumber of proteins in this genome belonging to this COG is","","Residues 160 to 213 match (3e-16) PD:PD307168 which is described as COMPLETE PROTEOME ABC PERIPLASMIC BINDING TRANSPORTER TRANSPORTER OLIGOPEPTIDE OLIGOPEPTIDE-BINDING SUBSTRATE ","","","","","","","","","","","Tue Jan 21 15:17:42 2003","Tue Jan 21 15:17:42 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02892 is paralogously related to AA01607 (1e-17).","","","","","","","","","","","Kashiwagi,K., Yamaguchi,Y., Sakai,Y., Kobayashi,H. and Igarashi,K. Identification of the polyamine-induced protein as a periplasmic oligopeptide binding protein. J. Biol. Chem. 265 (15): 8387-8391 (1990) PubMed: 2187863.Abouhamad,W.N. and Manson,M.D. The dipeptide permease of Escherichia coli closely resembles other bacterial transport systems and shows growth-phase-dependent expression Molecular microbiology. 14 (5), 1077-1092 (1994) PubMed: 7536291 ","","Wed Feb 5 15:28:33 2003","1","","","" "AA02893","2027341","2027604","264","ATGTTTAAGTTCATCTTAAAACGCGTGTTGGAAGCGATACCTACATTATTTGTTCTGATTACGTTTTCTTTTTTCCTTATGCGCTTGGCGCCGGGCAGCCCGTTTACCTCGGAACGCGCTTATCCGCCTGAAGTGATGGCGAACATTGAAGCCAAATATCACCTAAACGAACCGCTGCATACACAGTATTTTTTATATTTAAAGAACTTGGTCAAGGGGGATTTTGGTCCGTCTTTTAAATATAAAGATCAGTCCGTAAGTAAA","","","10251","MFKFILKRVLEAIPTLFVLITFSFFLMRLAPGSPFTSERAYPPEVMANIEAKYHLNEPLHTQYFLYLKNLVKGDFGPSFKYKDQSVSK","2027439","[FUNCTION] Part of the binding-protein-dependent transport system for oligopeptides. Probably responsible for energy coupling to the transport system (by similarity). ","oligopeptide transport system permease protein, N-terminal","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-32]?signal-peptide
tmhmm\"[9-27]?transmembrane_regions


","BeTs to 20 clades of COG0601COG name: ABC-type dipeptide/oligopeptide/nickel transport systems, permease componentsFunctional Class: E,PThe phylogenetic pattern of COG0601 is ao-pkz-qvdrlbcefgh--uj-itwNumber of proteins in this genome belonging to this COG is","","Residues 26 to 87 match (1e-20) PD:PD001686 which is described as COMPLETE PROTEOME PERMEASE ABC OLIGOPEPTIDE TRANSPORTER TRANSPORTER SYSTEM MEMBRANE TRANSMEMBRANE ","","","","","","","","","","","Tue Jan 21 15:15:20 2003","Wed Mar 17 10:00:07 2004","","","","Wed Mar 17 09:59:49 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02893 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Wed Mar 17 09:59:49 2004","","","","","","","","","","Abouhamad,W.N. and Manson,M.D. The dipeptide permease of Escherichia coli closely resembles other bacterial transport systems and shows growth-phase-dependent expression Molecular microbiology. 14 (5), 1077-1092 (1994) PubMed: 7536291 ","","Wed Feb 5 15:26:32 2003","1","","","" "AA02895","2027624","2028262","639","TTGCCCGTTTCTCTGAAACTCGGCACCATTGCCTTTTTCTTTGCTGTAACCCTGGGTGTTGCCGCCGGCACGCTCGCCGCCCTGAACCAAAACAGCAGATGGGATTACATTCTGATGAGCTATTCCATGGTGGGCGTGATCATGCCGAGTTTTGTTTTTGCACCTTTACTGGTGCTGTTGTTTGCGATAACTCTGGGCTGGCTGCCGGCAGGCGGTTGGAATGAGGGGGCTTTGAGTTACATTCTGTTGCCGGTGGCATCCTTAACCATCGGATATGTGGCGGGCATTGCGCGGATTATGCGCGGTTCTATGATTGAAGTGTTGCACTCCAATTTTATTCGTACCGCCAAGGCAAAAGGCTTGTCCACCTCTCGCATTATCTTAAAGCACGCGCTGCGCCCCGCCCTGTTGCCGGTGATTACCTATTTAGGGCCGGCATTTGTGGGCATTATTACCGGTTCCATGGTGATCGAAACCGTATTCGGCTTACCGGGCATGGGCAAACTTTTCGTTAACGGCGCGCTTAACCGCGATTATTCCCTTGTATTGAGCCTCACGATTTTGGTCGGCACACTGACTATCGTTTTTAACGCCGTAGTGGATATTTTATACGCCGTGATTGATCCGAAAATTCGTTAT","","","22803","LPVSLKLGTIAFFFAVTLGVAAGTLAALNQNSRWDYILMSYSMVGVIMPSFVFAPLLVLLFAITLGWLPAGGWNEGALSYILLPVASLTIGYVAGIARIMRGSMIEVLHSNFIRTAKAKGLSTSRIILKHALRPALLPVITYLGPAFVGIITGSMVIETVFGLPGMGKLFVNGALNRDYSLVLSLTILVGTLTIVFNAVVDILYAVIDPKIRY","2028097","[FUNCTION] Part of the binding-protein-dependent transport system for oligopeptides. Probably responsible for energy coupling to the transport system (by similarity). ","oligopeptide transport system permease protein, C-terminal","Inner membrane, Cytoplasm","","
InterPro
IPR000515
Family
Binding-protein-dependent transport systems inner membrane component
PF00528\"[1-213]TBPD_transp_1
PS50928\"[1-200]TABC_TM1
noIPR
unintegrated
unintegrated
signalp\"[1-26]?signal-peptide
tmhmm\"[10-28]?\"[38-70]?\"[76-96]?\"[135-157]?\"[180-200]?transmembrane_regions


","BeTs to 20 clades of COG0601COG name: ABC-type dipeptide/oligopeptide/nickel transport systems, permease componentsFunctional Class: E,PThe phylogenetic pattern of COG0601 is ao-pkz-qvdrlbcefgh--uj-itwNumber of proteins in this genome belonging to this COG is","","Residues 96 to 212 match (6e-07) PD:PD318263 which is described as PERMEASE HOMOLOG OPPB OLIGOPEPTIDE ","","","","","","","","","","","Tue Jan 21 15:01:26 2003","Wed Mar 17 10:00:30 2004","","","","Thu Mar 11 14:26:55 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA02895 is paralogously related to AA01572 (1e-17) and AA02897 (1e-06).","Thu Mar 11 14:26:55 2004","","","","","Residues 1 to 213 (E-value = 1.8e-56) place AA02895 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component (PF00528)","Thu Mar 11 14:26:55 2004","","","","Abouhamad,W.N. and Manson,M.D. The dipeptide permease of Escherichia coli closely resembles other bacterial transport systems and shows growth-phase-dependent expression Molecular microbiology. 14 (5), 1077-1092 (1994) PubMed: 7536291 ","","Tue Jan 21 15:01:26 2003","1","","","" "AA02897","2028275","2029210","936","ATGACGAAAAATGATGGTGTAAAACCAATAAATCAAAAAAATACCGAATTTGTTGAACAACTTGCGGAACGCATGGATGAAATGCAACTGGAAGGGCGCAGCCTGTGGCAAGACGCCAAACGGCGTTTCTTCCGCAATAAAGCGGCGGTGGTCAGTTTAATCATGTTGGGTGTTATCGTGCTTTTCATTACTTTTGCGCCCCTCGCTTTCCCTTTTACTTATGAAGACACCGACTGGAACATGATGGGCGTGGCGCCGACGCTGGAAGGCTACCATTTCTTCGGTACGGATTCCTCCGGCCGCGATCTTTTGGTGCGTACCGCCATCGGCGGGCGAATTTCCTTAATGGTGGGCATTGCAGGCGCGCTGATTTCCGTGTTAATCGGCACGATTTACGGCGCCATTTCCGGTTATTTCGGCGGCAAAATCGACATGGTGATAATGCGCCTTCTGGAAATTTTAAGCTCTTTTCCGTTCATGTTTTTCGTCATCTTATTGGTGACCTTATTCGGACAAAATATTTTCCTGATTTTTGTAGCTATCGGTGCCATTGCCTGGCTCGGCTTGGCGCGTATCGTGCGCGGACAGACCCTCAGCCTGAAAAACAAAGAATTTGTAGAAGCGGCGATTGTGTGCGGCGTGCCTCGTCGTCAAATCATTTTTAAACACATCATTCCGAATGTGTTGGGGTTAGTGGCAGTTTATGCCTCTCTTGAAGTACCGGGCTTCATTTTGTTTGAATCCTTTCTGAGCTTTTTAGGCTTGGGTACGCAAGAACCCATGAGCAGCTGGGGCGCATTATTAAGCGACGGCGCCGCACAAATGGAAGTGTCCCCTTGGTTGCTGACTTTCCCGGCGTTCTTCCTCTGTTTAACCCTTTTTTGCTTTAACTTTATCGGTGACGGGTTGCGCGATGCACTCGATCCGAAAGACCGC","","","34570","MTKNDGVKPINQKNTEFVEQLAERMDEMQLEGRSLWQDAKRRFFRNKAAVVSLIMLGVIVLFITFAPLAFPFTYEDTDWNMMGVAPTLEGYHFFGTDSSGRDLLVRTAIGGRISLMVGIAGALISVLIGTIYGAISGYFGGKIDMVIMRLLEILSSFPFMFFVILLVTLFGQNIFLIFVAIGAIAWLGLARIVRGQTLSLKNKEFVEAAIVCGVPRRQIIFKHIIPNVLGLVAVYASLEVPGFILFESFLSFLGLGTQEPMSSWGALLSDGAAQMEVSPWLLTFPAFFLCLTLFCFNFIGDGLRDALDPKDR","2029045","[FUNCTION] Part of the binding-protein-dependent transport system for oligopeptides. Probably responsible for energy coupling to the transport system (by similarity). ","oligopeptide ABC transporter; permease protein","Inner membrane, Cytoplasm","","
InterPro
IPR000515
Family
Binding-protein-dependent transport systems inner membrane component
PF00528\"[111-312]TBPD_transp_1
PS50928\"[111-300]TABC_TM1
noIPR
unintegrated
unintegrated
tmhmm\"[50-72]?\"[113-135]?\"[150-170]?\"[174-193]?\"[225-245]?\"[280-300]?transmembrane_regions


","BeTs to 20 clades of COG1173COG name: ABC-type dipeptide/oligopeptide/nickel transport systems, permease componentsFunctional Class: E,PThe phylogenetic pattern of COG1173 is ao-pkz-qvdrlbcefgh--uj-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 8.6e-05) to 1/1 blocks of the IPB000515 family, which is described as \"Binding-protein-dependent transport systems inner membrane component\". Interpro entry for IP:IPR000515. IPB000515 207-226 8.8e-05","Residues 46 to 178 match (2e-07) PD:PD465326 which is described as PERMEASE OLIGO/DIPEPTIDE PROTEOME COMPLETE DPPC-2 TRANSPORT ","","","","","","","","","","","Tue Jan 21 14:59:23 2003","Tue Jan 21 14:59:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02897 is paralogously related to AA01571 (1e-20) and AA02895 (2e-06).","","","","","","Residues 111 to 312 (E-value = 3e-42) place AA02897 in the BPD_transp_1 family which is described as Binding-protein-dependent transport system inner membrane component (PF00528)","","","","","Abouhamad,W.N. and Manson,M.D. The dipeptide permease of Escherichia coli closely resembles other bacterial transport systems and shows growth-phase-dependent expression Mol. Microbiol. 14 (5), 1077-1092 (1994) PubMed: 7536291 ","","Wed Feb 5 15:34:10 2003","1","","","" "AA02898","2029223","2030203","981","ATGACAAACTCAACGCACTTATTGGATGTGCAAAATTTGCATGTCGGTTTTAAAACCCCGGACGGCATTGTGACCGCTGTCAACGATTTAAATTTCACTTTAGATGCCGGACACACTCTTGGCATCGTGGGCGAATCCGGTTCCGGCAAATCGCAAACCGCTTTTGCCCTCATGGGGTTGCTCGCACCCAACGGCGAAGTTTCGGGATCGGCATTATTTGATGAAGTCCAATTGGTCAATCTGCCAATAGAGAAACTGAACAAAATCCGCGCGGAACAAATTTCTATGATTTTCCAGGATCCCATGACGTCGCTGAATCCTTATATGAAAATCGGCGAGCAACTCATGGAAGTGTTAATATTGCACAAAGGCTACGACAAACAGACGGCATTTAACGAATCGGTGAAAATGTTGGATGCGGTAAAAATGCCGGAAGCCAAGAAACGCATGGGGATGTATCCACACGAATTCTCCGGCGGTATGCGCCAACGGGTGATGATCGCTATGGCACTGTTATGTCGTCCGAAGCTGTTAATTGCCGACGAACCGACCACCGCGCTGGACGTGACCGTGCAAGCGCAAATCATGACTTTGTTAAACGAGCTGAAACACGAGTTCAATACGGCGATTATTATGATCACCCACGATCTCGGCGTGGTGGCGGGCATTTGTGATCATGTGCTGGTGATGTATGCCGGTCGCACCATGGAATACGGCAATGCGGAACAGATTTTCTATCATCCGACTCATCCTTATTCTATCGGTTTAATGGACGCTATCCCGCGCCTGGATATGGATGAAGAACATTTGGTCACCATTCCCGGTAATCCGCCGAATCTGCTGCATTTACCGCAAGGTTGCCCGTTTTCACCGCGTTGCCGATTCGCTTCCGAGCAATGCCAAAAAACGCCGCCAAAACTGACCGCACTTCATGACGGACGGATCAGAAACTGTTGGCTACCTGCGGAGGAATTTGCCCTA","","","36223","MTNSTHLLDVQNLHVGFKTPDGIVTAVNDLNFTLDAGHTLGIVGESGSGKSQTAFALMGLLAPNGEVSGSALFDEVQLVNLPIEKLNKIRAEQISMIFQDPMTSLNPYMKIGEQLMEVLILHKGYDKQTAFNESVKMLDAVKMPEAKKRMGMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKHEFNTAIIMITHDLGVVAGICDHVLVMYAGRTMEYGNAEQIFYHPTHPYSIGLMDAIPRLDMDEEHLVTIPGNPPNLLHLPQGCPFSPRCRFASEQCQKTPPKLTALHDGRIRNCWLPAEEFAL","2030038","[FUNCTION] Part of the binding-protein-dependent transport system for oligopeptides. Probably responsible for energy coupling to the transport system (by similarity). ","oligopeptide transport ATP-binding protein","Inner membrane, Cytoplasm","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[156-199]TQ9CJT4_PASMU_Q9CJT4;
PF00005\"[37-233]TABC_tran
PS50893\"[8-257]TABC_TRANSPORTER_2
PS00211\"[157-171]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[36-242]TAAA
InterPro
IPR010066
Domain
Oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal
TIGR01727\"[234-320]Toligo_HPY: oligopeptide/dipeptide ABC trans
InterPro
IPR013563
Domain
Oligopeptide/dipeptide ABC transporter, C-terminal
PF08352\"[236-300]Toligo_HPY
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[2-266]Tno description
PTHR19222\"[8-324]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF28\"[8-324]TOLIGOPEPTIDE ABC TRANSPORTER


","BeTs to 18 clades of COG0444COG name: ABC-type dipeptide/oligopeptide/nickel transport system, ATPase componentFunctional Class: E,PThe phylogenetic pattern of COG0444 is ao-pkz-qvd-lb-efgh--uj-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.7e-23) to 3/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 26-72 4.1e-10 IPB001140B 154-192 3e-10 IPB001140C 210-239 11","Residues 84 to 122 match (2e-07) PD:PD000720 which is described as ATP-BINDING PROTEOME COMPLETE ABC TRANSPORTER OLIGOPEPTIDE TRANSPORTER PEPTIDE DIPEPTIDE PLASMID ","","","","","","","","","","","Tue Jan 21 14:56:08 2003","Tue Jan 21 14:56:08 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02898 is paralogously related to AA02899 (2e-55), AA01569 (5e-54), AA01568 (5e-33), AA00415 (2e-25), AA01524 (9e-24), AA00858 (2e-23), AA02718 (2e-21), AA02353 (6e-21), AA02440 (9e-21), AA01616 (2e-20), AA02080 (2e-19), AA01645 (5e-19), AA00700 (5e-19), AA01656 (2e-18), AA02550 (4e-18), AA01422 (1e-17), AA02786 (4e-17), AA01051 (5e-17), AA01684 (8e-17), AA02324 (1e-16), AA01779 (1e-16), AA02320 (2e-16), AA01820 (2e-16), AA02140 (3e-16), AA01456 (5e-16), AA01824 (9e-16), AA00207 (9e-16), AA01867 (2e-15), AA02225 (1e-14), AA01393 (2e-14), AA00799 (2e-14), AA02805 (3e-14), AA02606 (5e-14), AA01961 (3e-13), AA02152 (4e-13), AA01947 (1e-12), AA00751 (2e-12), AA01555 (1e-11), AA01509 (2e-11), AA01510 (3e-11), AA02484 (4e-11), AA01757 (4e-11), AA02609 (1e-10), AA02642 (2e-10), AA02331 (3e-10), AA00591 (3e-10), AA02573 (9e-08), AA02146 (2e-06), AA00934 (2e-06), AA00933 (3e-06), AA01291 (5e-06) and AA00061 (1e-04).","","","","","","Residues 37 to 233 (E-value = 1.4e-55) place AA02898 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Abouhamad,W.N. and Manson,M.D. The dipeptide permease of Escherichia coli closely resembles other bacterial transport systems and shows growth-phase-dependent expression Molecular microbiology. 14 (5), 1077-1092 (1994) PubMed: 7536291 ","","Tue Jan 21 14:56:08 2003","1","","","" "AA02899","2030203","2031198","996","ATGAATGAACAAGTAGAAAGAAAATTATTACTGGAAGTGAACCACCTCGGCGTGAGCTTCAAAATTAAGAACGACAAATCCCTGTTCTTTGCCAAACCGCAAACCTTGAAAGCAGTAAAAGACGTGTCCTTTAAACTCTACGCCGGTGAAACCCTCGGCGTGGTGGGCGAATCCGGTTGTGGTAAATCCACGCTGGCACGCGCCATTATCGGCTTGGTGGAAGCTTCTGAGGGGCAAATTCTATGGCTTGGCAAAGATTTGCGCAAACAATCGGCAAAACAATGGCACGATACCCGCAAAGATATTCAAATGATTTTTCAGGATCCGCTGGCATCTCTCAATCCTCGCATGAATATCGGTGAAATTATTGCCGAACCGTTGAAAATTTATCAACCGCACTTGAGTAAAGCACAAGTCAAAGAAAAAGTGCAAGCGATGATGTTAAAAGTGGGTTTGCTACCGAACCTGATTAACCGTTATCCGCATGAATTTTCCGGCGGACAATGTCAACGTATCGGTATTGCCCGTGCATTAATTATCGAACCGAAAATGATTATTTGCGATGAACCGGTTTCCGCCTTGGACGTTTCCATTCAGGCGCAAGTAGTGAATTTGCTAAAATCGCTGCAAAAAGAAATGGACTTGTCTCTCATTTTTATTGCGCACGATCTGGCGGTGGTGAAACACATTTCCGATCGCGTATTGGTTATGTATCTGGGAAATGCCATGGAGCTTGGCACCGATGATGAAGTGTACAAACACACAAAACACCCTTACACCAAAGCCCTGATGTCCGCCGTGCCGATTCCTGATCCGAAACTGGAGCGTAATAAATCTATCCAGCTGTTGGAAGGCGATCTGCCGTCACCGATTAATCCACCTTCCGGCTGTGTTTTCCGCACCCGTTGCCTGCTTGCCGATGACAGTTGCGCACAACAGAAACCGGTGTTCAACAGCGACAACAACAGCCATTTTGTCGCCTGCTTAAAGGTTTCT","","","37746","MNEQVERKLLLEVNHLGVSFKIKNDKSLFFAKPQTLKAVKDVSFKLYAGETLGVVGESGCGKSTLARAIIGLVEASEGQILWLGKDLRKQSAKQWHDTRKDIQMIFQDPLASLNPRMNIGEIIAEPLKIYQPHLSKAQVKEKVQAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALIIEPKMIICDEPVSALDVSIQAQVVNLLKSLQKEMDLSLIFIAHDLAVVKHISDRVLVMYLGNAMELGTDDEVYKHTKHPYTKALMSAVPIPDPKLERNKSIQLLEGDLPSPINPPSGCVFRTRCLLADDSCAQQKPVFNSDNNSHFVACLKVS","2031033","[FUNCTION] Part of the binding-protein-dependent transport system for oligopeptides. Probably responsible for energy coupling to the transport system (by similarity). ","oligopeptide ABC transporter, ATP-binding protein","Cytoplasm, Inner membrane","","
InterPro
IPR003439
Domain
ABC transporter related
PD000006\"[163-206]TOPPF_HAEIN_P45051;
PF00005\"[49-240]TABC_tran
PS50893\"[23-264]TABC_TRANSPORTER_2
PS00211\"[164-178]TABC_TRANSPORTER_1
InterPro
IPR003593
Domain
AAA+ ATPase, core
SM00382\"[48-241]TAAA
InterPro
IPR010066
Domain
Oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal
TIGR01727\"[241-330]Toligo_HPY: oligopeptide/dipeptide ABC trans
InterPro
IPR013194
Domain
Histone deacetylase interacting
SM00761\"[168-244]Tno description
InterPro
IPR013563
Domain
Oligopeptide/dipeptide ABC transporter, C-terminal
PF08352\"[243-310]Toligo_HPY
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[5-273]Tno description
PTHR19222\"[11-331]TATP BINDING CASSETE (ABC) TRANSPORTER
PTHR19222:SF28\"[11-331]TOLIGOPEPTIDE ABC TRANSPORTER


","BeTs to 14 clades of COG1124COG name: ABC-type dipeptide/oligopeptide/nickel transport system, ATPase componentFunctional Class: E,PThe phylogenetic pattern of COG1124 is ao-pkz-qvd-lb-efgh--uj-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.3e-31) to 2/3 blocks of the IPB001140 family, which is described as \"ABC transporter transmembrane region\". Interpro entry for IP:IPR001140. IPB001140A 38-84 1.5e-19 IPB001140B 161-199 1.1e-10Significant hit ( 9.8e-05) to 1/5 blocks of the IPB001324 family, which is described as \"Phosphoribulokinase family\". Interpro entry for IP:IPR001324. IPB001324A 48-69 1e-04","Residues 99 to 162 match (1e-07) PD:PD468041 which is described as ATP-BINDING COMPLETE PROTEOME ABC TRANSPORTER OLIGOPEPTIDE PLASMID TRANSPORTER DIPEPTIDE ATPASE ","","","","","","","","","","","Tue Jan 21 14:52:43 2003","Tue Jan 21 14:52:43 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02899 is paralogously related to AA02898 (2e-55), AA01568 (5e-41), AA00415 (3e-32), AA01569 (2e-31), AA02718 (7e-30), AA01645 (4e-29), AA00700 (6e-29), AA02353 (4e-28), AA01524 (4e-28), AA01656 (3e-26), AA00858 (2e-25), AA01051 (7e-24), AA01422 (1e-23), AA01616 (2e-22), AA02324 (5e-22), AA02805 (4e-21), AA01684 (1e-20), AA01867 (3e-20), AA00799 (1e-19), AA02550 (2e-19), AA02140 (3e-19), AA01779 (2e-18), AA02225 (2e-18), AA01947 (3e-18), AA02080 (1e-17), AA02440 (3e-17), AA02606 (4e-17), AA01509 (5e-17), AA02320 (4e-16), AA01961 (5e-16), AA01456 (9e-16), AA01820 (2e-15), AA01393 (2e-15), AA02152 (4e-15), AA00933 (5e-15), AA02786 (6e-15), AA02609 (2e-14), AA00207 (4e-14), AA01757 (7e-14), AA00751 (7e-14), AA02573 (1e-13), AA02642 (2e-13), AA01824 (3e-13), AA01510 (4e-13), AA02484 (5e-11), AA02331 (2e-10), AA00061 (9e-09), A02145 (1e-07), AA01555 (3e-07), AA00591 (5e-07), AA00934 (2e-06), AA02146 (5e-06) and AA02226 (3e-05).","","","","","","Residues 49 to 240 (E-value = 1.3e-61) place AA02899 in the ABC_tran family which is described as ABC transporter (PF00005)","","","","","Abouhamad,W.N. and Manson,M.D. The dipeptide permease of Escherichia coli closely resembles other bacterial transport systems and shows growth-phase-dependent expression Mol. Microbiol. 14 (5), 1077-1092 (1994) PubMed: 7536291 ","","Tue Jan 21 14:52:43 2003","1","","","" "AA02902","2032015","2031311","705","ATGCAAACACCACGAATTTTAATCGTTGAAGATGAAACGATCACCAGAAACACGCTAAAAAGTATTTTTGAAGCGGAAGGATATGAAGTATTTGAAGCGTCGGACGGTACGCAAATGCACCAAGTGCTGGATACCGAAGATATTCATTTAGTGATTATGGATATTAATTTGCCGGGCAAAAACGGCTTAATGCTTGCCCGTGAATTGCGTGAAAATGCGGACATTGCACTGATGTTTTTAACCGGTCGAGATAACGAAGTGGATAAAATTCTAGGCTTGGAAATTGGTGCCGATGATTACATCACCAAACCTTTCAACCCGCGTGAATTAACGATTCGCGCCAGAAACCTGTTGCAGCGTACCATGCAGGAGAATCAACGCACGCACCATGTGGAACAATATAAATTTAACGGCTGGACACTGGATTTAAACAGTCGCACGTTGGTTACGCCGGAAGGCGAGGAGCGCAAATTGCCGCGTAGTGAGTTCCGCGCCATGTTACATTTCTGCGAGAATCCGGGCAAAATTCAAACCCGTGAAGAATTATTGAAGAAAATGACCGGACGCGAGCTCAAACCGCAGGATCGTACGGTGGATGTGACCATTCGTCGAATTCGTAAACATTTTGAAGATCATCACGAGACACCGGAAATCATCGCCACCATTCACGGCGAAGGTTATCGCTTCTGTGGTGACTTGGAATCC","","","27593","MQTPRILIVEDETITRNTLKSIFEAEGYEVFEASDGTQMHQVLDTEDIHLVIMDINLPGKNGLMLARELRENADIALMFLTGRDNEVDKILGLEIGADDYITKPFNPRELTIRARNLLQRTMQENQRTHHVEQYKFNGWTLDLNSRTLVTPEGEERKLPRSEFRAMLHFCENPGKIQTREELLKKMTGRELKPQDRTVDVTIRRIRKHFEDHHETPEIIATIHGEGYRFCGDLES","2031146","[FUNCTION] Member of the two-component regulatory system arcB/arcA. Represses a wide variety of aerobic enzymes under anaerobic conditions. controls the resistance of E.coli to dyes; required for expression of the alkaline phosphatase and sex factor F genes; it also may be involved in the osmoregulation of envelope proteins. When activated by arcB, it negatively regulates the expression of genes of aerobic function. Activates the transcription of the plfB operon by binding to its promoter. ","aerobic respiration control protein","Cytoplasm","","
InterPro
IPR001789
Domain
Response regulator receiver
PD000039\"[6-118]TQ8XFN2_SALTI_Q8XFN2;
PF00072\"[4-115]TResponse_reg
SM00448\"[4-114]TREC
PS50110\"[5-118]TRESPONSE_REGULATORY
InterPro
IPR001867
Domain
Transcriptional regulatory protein, C-terminal
PD000329\"[134-228]TQ6LQ51_PHOPR_Q6LQ51;
PF00486\"[153-229]TTrans_reg_C
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.2300\"[1-154]Tno description
PTHR23283\"[1-120]TSENSOR HISTIDINE KINASE-RELATED
PTHR23283:SF21\"[1-120]TTWO-COMPONENT SYSTEM SENSOR HISTIDINE KINASE/RESPONSE REGULATOR (INTESTINAL BACTERIA - BACTEROIDES THETAIOTAOMICRON)


","No hits to the COGs database.","Significant hit ( 1.3e-43) to 4/4 blocks of the IPB001867 family, which is described as \"Transcriptional regulatory protein, C terminal\". Interpro entry for IP:IPR001867. IPB001867A 49-62 0.00055 IPB001867B 76-120 6.8e-24 IPB001867C 156-187 1e-07 IPB001867D 215-229 0.0019Significant hit ( 6.2e-14) to 3/3 blocks of the IPB001789 family, which is described as \"Response regulator receiver domain\". Interpro entry for IP:IPR001789. IPB001789A 6-12 15 IPB001789B 49-62 0.00076 IPB001789C 96-105 8.3e-07Significant hit ( 6.9e-06) to 3/6 blocks of the IPB000673 family, which is described as \"CheB methylesterase\". Interpro entry for IP:IPR000673. IPB000673A 6-16 17 IPB000673B 21-74 0.36 IPB000673C 74-104 0.38","Residues 134 to 231 match (2e-47) PD:PD000329 which is described as DNA-BINDING COMPLETE PROTEOME TRANSCRIPTION REGULATOR SENSORY TRANSDUCTION REGULATION PHOSPHORYLATION RESPONSE ","","","","","","","","","","","Tue Jan 21 14:49:15 2003","Tue Jan 21 14:49:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02902 is paralogously related to AA00997 (1e-33), AA01837 (3e-13), AA00959 (5e-09) and AA00757 (6e-06).","","","","","","Residues 153 to 229 (E-value = 2.3e-15) place AA02902 in the Trans_reg_C family which is described as Transcriptional regulatory protein, C terminal (PF00486)","","","","","Drapal,N. and Sawers,G. Purification of ArcA and analysis of its specific interaction with the pfl promoter-regulatory region. Mol. Microbiol. 16 (3): 597-607 (1995) PubMed: 7565118.Drury,L.S. and Buxton,R.S. DNA sequence analysis of the dye gene of Escherichia coli reveals amino acid homology between the dye and OmpR proteins. J. Biol. Chem. 260 (7): 4236-4242 (1985) PubMed: 2984198.Oshima T, Aiba H, Masuda Y, Kanaya S, Sugiura M, Wanner BL, Mori H, Mizuno T. Transcriptome analysis of all two-component regulatory system mutants of Escherichia coli K-12. Mol Microbiol. 2002 Oct;46(1):281-91. PMID: 12366850 ","","Tue Feb 4 15:33:12 2003","1","","","" "AA02903","2032417","2032280","138","ATGCAAGTATTATCTTCATTAAAAAATGCCAAGACCTGCCATCCGGGTTGTAAAGTCGTGCGTCGTCATGGTGTGGTTTATGTGATTTGTAAAGAAAATCCACGTTTTAAAGCGCGTCAGGGTGGCAAGAAAAAACGT","","","5220","MQVLSSLKNAKTCHPGCKVVRRHGVVYVICKENPRFKARQGGKKKR","2032280","","conserved hypothetical protein (ribosomal protein L36)","Cytoplasm, Extracellular","This sequence is similar to gi|16123297, a predicted ribosomal protein L36 from Yersinia pestis. See also gi|37524067 from Photorhabdus luminescens subsp.laumondii TTO1.","
InterPro
IPR000473
Family
Ribosomal protein L36
PD002101\"[1-40]TRL36_XANAC_Q8NL34;
PF00444\"[1-41]TRibosomal_L36
TIGR01022\"[1-41]TrpmJ_bact: ribosomal protein L36
PS00828\"[14-40]TRIBOSOMAL_L36


","BeTs to 19 clades of COG0257COG name: Ribosomal protein L36Functional Class: JThe phylogenetic pattern of COG0257 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.9e-14) to 1/1 blocks of the IPB000473 family, which is described as \"Ribosomal protein L36\". Interpro entry for IP:IPR000473. IPB000473 4-40 2.5e-14","Residues 1 to 41 match (3e-07) PD:PD579763 which is described as RIBOSOMAL PROTEOME COMPLETE L36 50S L36 COPY SECOND ","","","","","","","","","","","","Mon Feb 23 13:28:32 2004","Mon Feb 23 13:28:32 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02903 is paralogously related to AA01238 (3e-04).","Mon Feb 23 13:28:32 2004","","","","","Residues 1 to 41 (E-value = 5.9e-07) place AA02903 in the Ribosomal_L36 family which is described as Ribosomal protein L36 (PF00444)","","","","","","","","1","","","" "AA02904","2032693","2032430","264","ATGAAAAAAGGTATTCATCCGGAAAATTATCGCACCGTTCTTTTTTATGACTCCAATGCCAAACAAGGCTTTTTGATTCGTTCCTGCGCCAGAACCACCAACACTATGAAATGGGAAGATGGAAAAGAATATCCGGTCTTTATGTGTGATACATCTTCAGCTTCACATCCGTTTTACACCGGTAAAACCAGACAGGTTGTCAACGAAGGGCGCGCCAGTGATTTCGCCAACCGTTACGGCAAATTCAGTGCATTTAAATCAAAA","","","10116","MKKGIHPENYRTVLFYDSNAKQGFLIRSCARTTNTMKWEDGKEYPVFMCDTSSASHPFYTGKTRQVVNEGRASDFANRYGKFSAFKSK","2032265","","50S ribosomal protein L31","Periplasm, Extracellular","","
InterPro
IPR002150
Family
Ribosomal protein L31
PR01249\"[2-19]T\"[46-61]T\"[61-79]TRIBOSOMALL31
PS01143\"[50-71]?RIBOSOMAL_L31


","No hits to the COGs database.","Significant hit ( 5.4e-15) to 1/1 blocks of the IPB002150 family, which is described as \"Ribosomal protein L31\". Interpro entry for IP:IPR002150. IPB002150 49-79 5.2e-15","Residues 1 to 80 match (2e-14) PD:PD003785 which is described as RIBOSOMAL L31 50S PROTEOME COMPLETE CHLOROPLAST B TYPE SUBUNIT ","","","","","","","","","","","","Tue Jan 21 14:43:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02904 is paralogously related to AA01331 (6e-05).","","","","","","Residues 1 to 82 (E-value = 5.6e-06) place AA02904 in the Ribosomal_L31 family which is described as Ribosomal protein L31 (PF01197)","","","","","","","","1","","","" "AA02905","2033465","2032908","558","GTGGTTTATTGTGGCGCGGCACTCGACAATTTGCCGAGCTATCGCCAAGTGACTATTCAATTAGGCGAATGGATTACGCAACATCGACATACGTTAGTTTATGGCGGTGGAAAGGCGGGATTGATGGGCGTGTTGGCGGATACGGTACTTTCCAACGGCGGTACCGTTATCGGCGTGATCCCTGAATTTTTACAGGCGCGGGAATTGGTACACCAAGGTTGTACCGAAATTATCATTGTGGATTCCATGTCGGAGCGAAAAGCCAAAATGCTGGCATTAGCCGATGCTTGTATTGCTTTGTCGGGTGGGCCGGGCACGCTGGAAGAAATCAGCGAAGTCTATTCTTGGGCGCGAATCGGTAAAAATCCTCATCCTTGTATTCTATTTAACCAAGATGGTTTTTATGAACCGCTGAGAAGTCAATATCAAAGCATGGTCACTGCCGGTTTCTTGACGCAAAGTCATTTTGATAAGTTATTATTTAGTACAAATATTTTTGAAATAGAACGTTTTATTCTTGATTATCAAGTGCCTGAGATTCGTACTTATGAAGATGTG","","","20989","VVYCGAALDNLPSYRQVTIQLGEWITQHRHTLVYGGGKAGLMGVLADTVLSNGGTVIGVIPEFLQARELVHQGCTEIIIVDSMSERKAKMLALADACIALSGGPGTLEEISEVYSWARIGKNPHPCILFNQDGFYEPLRSQYQSMVTAGFLTQSHFDKLLFSTNIFEIERFILDYQVPEIRTYEDV","2032743","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR005269
Family
Conserved hypothetical protein 730
PF03641\"[42-175]TLysine_decarbox
TIGR00730\"[2-175]TTIGR00730: conserved hypothetical protein T
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.450\"[2-185]Tno description


","No hits to the COGs database.","","Residues 42 to 163 match (4e-25) PD:PD005712 which is described as COMPLETE PROTEOME LYSINE DECARBOXYLASE-LIKE PLASMID DECARBOXYLASE RIORF52 SAV0680 NMB0283 AQ_1884 ","","","","","","","","","","","","Tue Jan 21 14:40:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02905 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 42 to 175 (E-value = 9.4e-42) place AA02905 in the Lysine_decarbox family which is described as Possible lysine decarboxylase (PF03641)","","","","","","","","1","","","" "AA02906","2033444","2033542","99","GTGCCGCGCCACAATAAACCACAATGTTCATTTGATTGCCTCAGTTATTTTGCATTGATAAATTTTACGCCGAATTCCATATGGAATAAATCGCAACAA","","","3866","VPRHNKPQCSFDCLSYFALINFTPNSIWNKSQQ","2033542","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 13:18:51 2004","Mon Feb 23 13:18:51 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02906 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 13:19:26 2004","","","","","","","","","","","","","1","","","" "AA02907","2033617","2035404","1788","ATGGAAGATAACAACCGTTTTATGAAAAGATTTCTCCTCATTATCCTCTGCTTTTTCGTGACATTCAATGTGCAAGCCGTGGATCTGTTTAACCAAAAGCCAAAATTTTTACCGGTCGATCAAGCGTTTCAACTTCAGGCAGAACAATATGGCAACGACATTTCACTTAATTGGCAAATCGTCGAAAATTATTATCTCTATCAGGACAAACTGGAATTTGCCCTCAATGGACAGCCGATTGAAAGCCAACCGCAATTTTTAAGCCGGGCAGAACAATACGAAGATCCGTATTTTGGCACGGTACAAATCTTCAAGCACCAACTTCCTTTACGCCTGTCATTGCCAAATAGCAAACCGCAAGATATTCTGGAAGTCACTTATCAAGGTTGTACTCCCGGCTTTTGTTATCCGCCGAAAACTAAACAATTTATGCTTGGCGAACTGCCACACAATGCTGTAGAAACTTCACTAGTAGCTCAAGAAGAAACTAAAAGTGCGGTCAGAAATCCAAGTGTTTTTTCATCTCAACAAAATCAGCTTGCCGACAGTTTATTCCAAAGCAAATATGCCATGTTGTGGTTTTTTGTACTGGGCATCGGTTTAGCATTCACTCCTTGTGTGTTGCCGATGCTGCCGCTGTTATCGGCGATTGTCATCGGCAACAGAACGGAACATAGCCATACCTGGCGCGCCTTTACGCTGAGTTTCATGTATGTGCAAGGCATGGCGCTAACCTATACGCTCCTGGGCTTATTGGTCGTGCTTATCGGTTTACCGTTCCAAGTGGCGTTGCAAAGCCCCTATGTGTTAATCGGCTTATCGGTAGTGTTTACCTTGCTGGCACTTTCTATGTTCGGTGTGTTTACTTTGCAGTTGCCTCCATCTTTACAAACCAAGCTCACTCAATTAAGCCAACAACAAAAACGTGGCGCGTTTTTCGGTGTATTTGCCATGGGCGCCATCGCAGGTTTGGTCGCTTCCCCCTGCACATCCGCACCACTTTCCGGCGCACTGCTTTATGTAGCGCAATCAGGAGACCTTGTTATCGGCGCATTAACCCTTTATTTATTGGCACTTGGCATGGGCTTACCATTAATTCTGATTACTGTCTTCGGTAACAAAATTCTGCCGAAATCCGGTGCCTGGATGGAGAATGTAAAAACTGCCTTCGGCTTTGTGATGCTTGCCTTACCGGTCTTTCTACTTTCCCGCGTTCTTCCGTTGGACTGGGAACCGCGTTTATGGGCGCTGCTTGGCGTCAGCTTCTTTATTTGGCTCGCCACTCAAATGCACACCAACGGTATTGGCTTACTGTTCCGTATTCTTTTTCTGATTGCCGCCATCACACTAGCCCAGCCGCTCCAAAATTGGCTGTGGCAAAATAATACCGACCATGCAAGAACCCATAGTGCGGTCAAGAATTCCCTTGAATTTCAATCCGTGCAAAGCTACGAGGAGTTACAACTGGTATTAACGAAGAACCCGAAACCACTGGCGCTATTGGATCTTTACGCGGATTGGTGCGTCGCTTGTAAAGAATTTGAACATAAAACCTTTGCGGAACCACAAGTGCAAGACGCTTTAAAAGACGTTTTGCTGTTAAGAATCGACATGACAAACAACAGCGAAAACAACCGCACTTTAATGAAGCAATTGTCAATAACCGGCTTGCCGACGTTGATGCTTTTTAACCCGCAGGGAAAAGAAATTTCATCGCACCGCATTACCGGTTTTATGGAAGGAGAAGCATTTTTACAAACATTACAAGCAGCAAAAGCGTTAAATAAT","","","66870","MEDNNRFMKRFLLIILCFFVTFNVQAVDLFNQKPKFLPVDQAFQLQAEQYGNDISLNWQIVENYYLYQDKLEFALNGQPIESQPQFLSRAEQYEDPYFGTVQIFKHQLPLRLSLPNSKPQDILEVTYQGCTPGFCYPPKTKQFMLGELPHNAVETSLVAQEETKSAVRNPSVFSSQQNQLADSLFQSKYAMLWFFVLGIGLAFTPCVLPMLPLLSAIVIGNRTEHSHTWRAFTLSFMYVQGMALTYTLLGLLVVLIGLPFQVALQSPYVLIGLSVVFTLLALSMFGVFTLQLPPSLQTKLTQLSQQQKRGAFFGVFAMGAIAGLVASPCTSAPLSGALLYVAQSGDLVIGALTLYLLALGMGLPLILITVFGNKILPKSGAWMENVKTAFGFVMLALPVFLLSRVLPLDWEPRLWALLGVSFFIWLATQMHTNGIGLLFRILFLIAAITLAQPLQNWLWQNNTDHARTHSAVKNSLEFQSVQSYEELQLVLTKNPKPLALLDLYADWCVACKEFEHKTFAEPQVQDALKDVLLLRIDMTNNSENNRTLMKQLSITGLPTLMLFNPQGKEISSHRITGFMEGEAFLQTLQAAKALNN","2035239","[FUNCTION] Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps (By similarity).","thiol:disulfide interchange protein; inner membrane copper tolerance protein","Inner membrane, Cytoplasm","","
InterPro
IPR003834
Domain
Cytochrome c biogenesis protein, transmembrane region
PF02683\"[194-403]TDsbD
InterPro
IPR006662
Domain
Thioredoxin-related
PR00421\"[499-507]T\"[507-516]T\"[553-564]TTHIOREDOXIN
PS00194\"[500-518]TTHIOREDOXIN
InterPro
IPR012335
Domain
Thioredoxin fold
G3DSA:3.40.30.10\"[469-593]Tno description
InterPro
IPR013766
Domain
Thioredoxin domain
PF00085\"[480-591]TThioredoxin
noIPR
unintegrated
unintegrated
G3DSA:2.60.40.1250\"[26-151]Tno description
signalp\"[1-26]?signal-peptide
tmhmm\"[10-30]?\"[189-221]?\"[242-260]?\"[266-288]?\"[309-329]?\"[348-368]?\"[389-407]?\"[434-454]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.4e-07) to 2/2 blocks of the IPB003834 family, which is described as \"Cytochrome c biogenesis protein transmembrane region\". Interpro entry for IP:IPR003834. IPB003834A 195-209 4.4e-06 IPB003834B 317-326 13","Residues 37 to 155 match (7e-09) PD:PD256990 which is described as C-TYPE PROTEOME COMPLETE COPPER BIOGENESIS TOLERANCE CYTOCHROME ","","","","","","","","","","","Tue Jan 21 14:36:54 2003","Tue Jan 21 14:36:54 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02907 is paralogously related to AA02011 (9e-13).","","","","","","Residues 478 to 593 (E-value = 7.8e-05) place AA02907 in the Thioredoxin family which is described as Thioredoxin (PF00085)","","","","","Crooke,H. and Cole,J. The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain. Mol. Microbiol. 15 (6): 1139-1150 (1995) [PubMed: 7623667].Fong,S.T., Camakaris,J. and Lee,B.T. Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12. Mol. Microbiol. 15 (6): 1127-1137 (1995) [PubMed: 7623666]. Missiakas,D., Schwager,F. and Raina,S. Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. EMBO J. 14 (14): 3415-3424 (1995) [PubMed: 7628442]. Gordon,E.H., Page,M.D., Willis,A.C. and Ferguson,S.J. Escherichia coli DipZ: anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, onein each of three domains, contribute differentially to function. Mol. Microbiol. 35 (6): 1360-1374 (2000) [PubMed: 10760137].Chung,J., Chen,T. and Missiakas,D. Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and proteinfolding in the bacterial periplasm. Mol. Microbiol. 35 (5): 1099-1109 (2000) [PubMed: 10712691].","","Tue Jan 21 14:36:54 2003","1","","","" "AA02908","2035509","2035399","111","TTGCTGTATTTGTTTAAAAACATTTTTTCTTCCTTAAATAAAATAATGAAAATTGAAGGCGCGTATGCTAACAGTAAATTTAAAAGAAAAAAACAATATTGGTTAATTATT","","","4494","LLYLFKNIFSSLNKIMKIEGAYANSKFKRKKQYWLII","2035399","","hypothetical protein","Cytoplasm, Extracellular","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 13:11:06 2004","Mon Feb 23 13:11:06 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02908 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 13:11:58 2004","","","","","","","","","","","","","1","","","" "AA02909","2035487","2035873","387","ATGTTTTTAAACAAATACAGCAATTACTTTTTAGGCTTATTACGCATTACTTCAGGTTATGCATTCGTATTACATGCTACAGCAAAATTTTGGGAATTCCCAATTTCCGTGACCGGCGGCAACGGTTCCGTTCAACTGGCATCCTTAATGGGTGTTGGTGGTGTGATTGAACTGGTTTTCGGTATCCTACTGATTTTAGGTTTGTTTACCCGCGTATCTGCGTTCTTACTCAGCGGTCAAATGGCGATAGCTTATTTCATGTTCCATGCTTCCCCATACCCACTCTTGAAAGACGGTGAACCGGCATTTTTATACTGCTTCATTTTCTTATACTTTGTTTTCACAGGCGCCGGTGCATTTGCATTAGATAATAAAATCGGTAAAAAA","","","14147","MFLNKYSNYFLGLLRITSGYAFVLHATAKFWEFPISVTGGNGSVQLASLMGVGGVIELVFGILLILGLFTRVSAFLLSGQMAIAYFMFHASPYPLLKDGEPAFLYCFIFLYFVFTGAGAFALDNKIGKK","2035708","","conserved hypothetical protein","Inner membrane, Extracellular","","
InterPro
IPR011637
Family
DoxX
PF07681\"[10-90]TDoxX
noIPR
unintegrated
unintegrated
signalp\"[1-21]?signal-peptide
tmhmm\"[10-28]?\"[47-67]?\"[72-92]?\"[102-122]?transmembrane_regions


","BeTs to 4 clades of COG2259COG name: Predicted membrane proteinFunctional Class: SThe phylogenetic pattern of COG2259 is -o-------dr-b-efgh-n-j----Number of proteins in this genome belonging to this COG is","","Residues 3 to 44 match (3e-07) PD:PD508386 which is described as PROTEOME TRANSMEMBRANE COMPLETE HI0886 ","","","","","","","","","","","","Tue Jan 21 14:31:05 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02909 is paralogously related to AA02159 (8e-07).","","","","","","Residues 9 to 124 (E-value = 3.6e-25) place AA02909 in the DoxD family which is described as DoxD-like family (PF04173)","","","","","","","","1","","","" "AA02910","2039165","2036277","2889","ATGAAAAGAATGTTAATCAATGCGACTCAAAAAGAAGAGTTGCGCGTTGCGTTAGTCGATGGGCAACGCTTATTCGACCTGGACATTGAGAGTCTGGGGCATGAACAGAAAAAAGCCAATATTTACAAGGGAAAAATTACTCGGGTTGAGCCGAGTTTGGAAGCCGCTTTTGTGGATTACGGTGCAGAACGTCACGGTTTTTTACCGTTGAAAGAAATTGCACGTGAATATTTTCCGTCGGGTTATGTATATCAAGGCCGCCCGAATATTCGCGATATTATCTCGGAAGGGCAGGAAGTCATTGTTCAGGTCAACAAAGAAGAGCGCGGTAATAAAGGTGCGGCGCTGACCACCTTTGTTTCCTTGGCAGGGAGTTATTTGGTGATTATGCCGAATAATCCGCGCGCCGGCGGGATTTCCCGTCGTATTGAAGGCGATGAGCGTTTGGAGTTAAAAGATGCGTTGAGTTCTTTGGATGTGCCTGAAGGCGTGGGATTAATCGTACGCACCGCGGGCGTGGGAAAATCCCCGGAAGAATTGCAATGGGACTTGAAAGTGCTGTTGCATCATTGGGAAGCCATTAAACAAGCGTCTCAAAGCCGCCCGGCGCCTTTTTTAATTCATCAGGAAAGTGATGTTATCGTGCGTGCCATTCGCGATTATTTGCGTCGCGATATTGGTGAAATCCTGATTGATAGCCTGCAAGTTTATGAAAAAGCCAAGGCGCACATTAAATTGGTTCGTCCGGATTTCATTAATCGAGTGAAATTATACCAAGGTGAAGTGCCGTTATTTAGCCATTATCAAATTGAGTCGCAAATCGAATCGGCATTCCAACGTGAAGTGCGGTTGCCTTCCGGCGGTTCTATTGTTATTGATGTGACCGAAGCCTTAACAGCCATTGATATTAACTCCGCCCGTTCCACCCGTGGTGGCGACATTGAAGAAACCGCGTTAAACACCAACCTTGAAGCTGCCGATGAAATCGCCCGTCAATTGCGTTTGCGCGACTTGGGCGGTTTAATCGTGATTGACTTTATTGATATGACGCCGGTTCGTCATCAGCGTGAAGTGGAAAATCGGGTTCGTGATGCGGTGCGCCAGGATCGGGCGCGTATTCAAATTAGCCGAATTTCCCGTTTCGGGTTGTTGGAAATGTCCCGTCAGCGTTTGAGTCCGTCATTAGGCGAATCCTCTCACCACGTTTGCCCGCGCTGCCAAGGCACCGGCAAAATCCGTGATAACGAGTCACTTTCCCTTTCCATTTTGCGTTTATTGGAAGAAGAAGCGTTAAAAGAAAATACCAAACAGGTTCACACCATCGTTCCGGTACAAATCGCGTCTTACTTACTCAATGAAAAACGGAAAGCCATTCATAGCATCGAAAAACGCCACACTGTGGATATTCTCGTGGTGCCGAATGAAGCTATGGAAACACCGCACTTTAGTGTGTTCCGTGTGCGTGATGGGGAAGAGGTTAATGAATTAAGTTATAACTTAGCCAGATTACATCAGGGGCAAGATGAGACCCTTGTAGCTGAAGAATCCCTGATTTCCCGTAACATTGACACCACACCTGCGGAAACGCCGGTGGTGGAAAGTGCGGCGGTTTCTTTATCCATTCCAATGCCGGCACCGGAACCTGTTGAGCGTAAAGAACAAAGCGGTCCGTCTTTGTTGAGCCGTTTATTGGCGGCGTTAAAAGGCTTATTTGCTTCCGAACCGAAACAGGAAGAGCAAAATAAGAAAACGCGTAATAACAATAGAAACAGTAACAATAATCGCAATCGACGTAACCAGGAACGTCGTAATAATCGCCGTAACCGTAATGACAATGCGGAAAATGTGGTTGAAGAGCAAACTGCAGAAAAGGCTGAGAGAGTTGAAAGCAGAAATCGCAATCAAGAGCGTAATGCCAAACGTAATCGCAAACCTGAAGTAATTGAAGAGGTGATTAACTCTGAGGCTTCCACACCGGTTAGCGAAGAAAGGGTAGAACCGACACAACGTCGTCAACGTCGTGATTTGCGCAAAAAAGTGCGTCTTAATGAAGAGGAAATGAATGAGGTTCCGCCTTCTAAATCGACAGTAGCACAATTTGCAGAAAACACCGTTGTTGAGCCAAAAGCGGAAGAAGAGATTGTAGTAACGGACGTGATTGATCTTGATGATAATGCTGAAGTCGATAAAGGGCGCGATAATTCACGTCAACGTCGTTTGCCACGTCATTTGCGCGTCAATAATCAGCGCCGTCGTCGCAATACGCAAGAAAAATCGCCGATGCCATTATTTGCGGCAGTGGCTTCACCGGAATTAGCGAGCGGTAAAGTGTGGATCGACATGGGGCAGTCCGTTCAATCAAAAGAAAATAGCTTCTTATCTGTTGATGAACTTCTTGAGCAACAAAATCAATCTGATGCAGGCGAACCGGAGCAAAGTATCACTGTCACTATGCCGGCGTTGGATATGATTGTTGAAAAAAGTAAAAATGATGTTCAGCCATTAACGGAATTTATTATCCAACCGGCAAATGATTCCGTTAAGAAAAAAGTACAAGCATCGTTACAACGCTTAAATAACAATGTGGTATCCGCTCCAATGGAAGCGACAGCTGAAGTGATTGTAACGATGGATGTCTCTGATAATGTGAAATTCATGGATGAAACTGACCGCACTTATGTTTTTAACGGGCGTCTAGGGACATTCTCGGCAGTAACCCACACTAAAGCAGAAGCGACTTTGGCGAAGCCTTCCGATACACCGATTACGACTTATCCGGTGCAAGAATGGCAGGAATCCCGTTATTATTTCTACGGTAAAGGCGCGGCAGGGCACCACACCGCAATCAGCCATATTTATACCGAACCGACTAAAGCGGAAGCGGTGAAA","","","109013","MKRMLINATQKEELRVALVDGQRLFDLDIESLGHEQKKANIYKGKITRVEPSLEAAFVDYGAERHGFLPLKEIAREYFPSGYVYQGRPNIRDIISEGQEVIVQVNKEERGNKGAALTTFVSLAGSYLVIMPNNPRAGGISRRIEGDERLELKDALSSLDVPEGVGLIVRTAGVGKSPEELQWDLKVLLHHWEAIKQASQSRPAPFLIHQESDVIVRAIRDYLRRDIGEILIDSLQVYEKAKAHIKLVRPDFINRVKLYQGEVPLFSHYQIESQIESAFQREVRLPSGGSIVIDVTEALTAIDINSARSTRGGDIEETALNTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQREVENRVRDAVRQDRARIQISRISRFGLLEMSRQRLSPSLGESSHHVCPRCQGTGKIRDNESLSLSILRLLEEEALKENTKQVHTIVPVQIASYLLNEKRKAIHSIEKRHTVDILVVPNEAMETPHFSVFRVRDGEEVNELSYNLARLHQGQDETLVAEESLISRNIDTTPAETPVVESAAVSLSIPMPAPEPVERKEQSGPSLLSRLLAALKGLFASEPKQEEQNKKTRNNNRNSNNNRNRRNQERRNNRRNRNDNAENVVEEQTAEKAERVESRNRNQERNAKRNRKPEVIEEVINSEASTPVSEERVEPTQRRQRRDLRKKVRLNEEEMNEVPPSKSTVAQFAENTVVEPKAEEEIVVTDVIDLDDNAEVDKGRDNSRQRRLPRHLRVNNQRRRRNTQEKSPMPLFAAVASPELASGKVWIDMGQSVQSKENSFLSVDELLEQQNQSDAGEPEQSITVTMPALDMIVEKSKNDVQPLTEFIIQPANDSVKKKVQASLQRLNNNVVSAPMEATAEVIVTMDVSDNVKFMDETDRTYVFNGRLGTFSAVTHTKAEATLAKPSDTPITTYPVQEWQESRYYFYGKGAAGHHTAISHIYTEPTKAEAVK","2036112","[FUNCTION] Mutures 5S rRNA from its precursors from all the rRNA genes. Major endoribonuclease participating in mRNA turnover. It initiates the decay of RNAs by cutting them internally near their 5'-end. it is able to remove poly(A) tails by an endonucleolytic process (by similarity). ","ribonuclease E","Cytoplasm","","
InterPro
IPR003029
Domain
RNA binding S1
PF00575\"[35-119]TS1
SM00316\"[37-119]TS1
PS50126\"[39-119]TS1
InterPro
IPR004659
Domain
Ribonuclease E and G
TIGR00757\"[13-424]TRNaseEG: ribonuclease, Rne/Rng family
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[30-125]Tno description
InterPro
IPR013256
Family
Chromatin SPT2
SM00784\"[568-643]Tno description


","BeTs to 14 clades of COG1530COG name: Ribonucleases G and EFunctional Class: JThe phylogenetic pattern of COG1530 is -o--kz-qv-r-bcefghsnujxi--Number of proteins in this genome belonging to this COG is","","Residues 92 to 123 match (6e-08) PD:PD506522 which is described as E PROTEOME COMPLETE RIBONUCLEASE HYDROLASE 3.1.4.- RNASE RNA-BINDING ENDONUCLEASE NUCLEASE ","","","","","","","","","","","Tue Jan 21 14:20:54 2003","Tue Jan 21 14:20:54 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02910 is paralogously related to AA00679 (1e-71) and AA02347 (2e-04).","","","","","","Residues 35 to 119 (E-value = 2.1e-15) place AA02910 in the S1 family which is described as S1 RNA binding domain (PF00575)","","","","","Walsh,A.P., Tock,M.R., Mallen,M.H., Kaberdin,V.R., Gabain Av,A. and McDowall,K.J. Cleavage of poly(A) tails on the 3'-end of RNA by ribonuclease E of Escherichia coli Nucleic Acids Res. 29 (9), 1864-1871 (2001) Pubmed: 11328869 ","","Tue Jan 21 14:20:54 2003","1","","","" "AA02911","2039146","2039295","150","TTGATTAACATTCTTTTCATTCGTTTTCTCTTTTATAAAAAAGGGCGAACCCTAAAAAACTCCATCAAAATGGACCGCACTTTGCTTAGTAATCGACCTCGTGTCTGTCGCAGAATGTCCGTCTTCCCGACCGTCATCTGCTGGGTGCAT","","","6065","LINILFIRFLFYKKGRTLKNSIKMDRTLLSNRPRVCRRMSVFPTVICWVH","2039295","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-17]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 13:03:18 2004","Mon Feb 23 13:03:18 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02911 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 13:04:23 2004","","","","","","","","","","","","","1","","","" "AA02912","2039650","2039435","216","TTGATGGTTTTTTCACTCATATTTGTCTATTTATTGCCACGGTTACAAAATTCGGCACGCATCATAGCATATCGCGCCATGGGTTTGAATGTGGCGGAGAATATTCGTCGAATTATGATAACCACCTTGCTAAAAATCCCTATTCGGGCGATAATAACGAGCATTTTTAAGTTGCAAAAAACGCTTAAAAATAAATACGTTATCATTGACGGGATA","","","8302","LMVFSLIFVYLLPRLQNSARIIAYRAMGLNVAENIRRIMITTLLKIPIRAIITSIFKLQKTLKNKYVIIDGI","2039270","","hypothetical protein","Periplasm, Cytoplasm","","
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Tue Jan 21 14:14:21 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02912 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02913","2039631","2040587","957","ATGAGTGAAAAAACCATCAACCCAAGTGTACAATTTTTAACTGTTAGCGACGATGAAGCCGGTCAACGACTGGATAATTTCTTACTGGCACGTTTAAAAGGTGTGCCGAAAAGCCTGATTTATCGTATTGTGCGCAAGGGCGAAGTACGGGTAAATAAAGCCAGAAGCAAACCGGAATATAAGCTACTGGCGGATGATGTGGTGCGCATTCCGCCCGTTCGCGTAGCAGAAAAAGCACAGGATACGATTTCCAATAAGCTCACCAAAGTTGCCCAACTGGAACAACACATCATCTTTGAAGACAATTATTTATTGGTGCTCAACAAGCCGTCCGGAATTGCCGTACATGGCGGCAGCGGGTTAGATTTCGGCGTCATTGAAGCTTTGCGTGCACTGCGTCCGGCAGCTCGTTTTTTAGAACTGGTTCATCGTTTAGATCGCGATACGTCGGGCATTTTATTGGTAGCAAAAAAACGTTCTGCTTTACGCAATCTGCACGAACAGCTGCGCGAAAAAACCGTGCAAAAAGATTATTTGGCACTCGTGCGCGGACAGTGGCAATCGCACTGCAAAGTGGTACAAGCGCCATTGCTGAAAAATGAACTTGCCGGTGGTGAGCGGATTGTGAAAGTGAGTGAACAAGGCAAACCCTCAGAAACCCGTTTTTCTGTGGAAGAACGCTATACCAATGCCACGCTAATCAAAGCCTCACCTGTCACCGGACGCACTCACCAAATTCGGGTGCATACCCAATATGCCGGTCACCCTATCGCATTCGATAGCAAATACGGTGATAAAGAATTTGATCAACACATGGTGGAATTAGGATTAAATCGCTTATTTTTACACGCCTACACCATTCGTTTTGAACATCCGCACAGTGGCGAAACGTTACGTTTAACCGCGCCATTAGAGGAAAAAATGAAAGGCATTCTGAAGCGTTTGCGTGAGATGAAG","","","36215","MSEKTINPSVQFLTVSDDEAGQRLDNFLLARLKGVPKSLIYRIVRKGEVRVNKARSKPEYKLLADDVVRIPPVRVAEKAQDTISNKLTKVAQLEQHIIFEDNYLLVLNKPSGIAVHGGSGLDFGVIEALRALRPAARFLELVHRLDRDTSGILLVAKKRSALRNLHEQLREKTVQKDYLALVRGQWQSHCKVVQAPLLKNELAGGERIVKVSEQGKPSETRFSVEERYTNATLIKASPVTGRTHQIRVHTQYAGHPIAFDSKYGDKEFDQHMVELGLNRLFLHAYTIRFEHPHSGETLRLTAPLEEKMKGILKRLREMK","2040422","[FUNCTION] Responsible for synthesis of pseudouridine from uracil at positions 955, 2504 and 2580 in 23S ribosomal RNA (by similarity). ","ribosomal large subunit pseudouridine synthase","Cytoplasm","","
InterPro
IPR002942
Domain
RNA-binding S4
PF01479\"[22-68]TS4
SM00363\"[22-81]TS4
PS50889\"[22-94]TS4
InterPro
IPR006145
Domain
Pseudouridine synthase
PD001819\"[142-191]TRLUC_HAEIN_P44433;
PF00849\"[103-252]TPseudoU_synth_2
InterPro
IPR006224
Family
Pseudouridine synthase, Rlu
PS01129\"[142-156]TPSI_RLU
InterPro
IPR006225
Domain
Pseudouridine synthase, RluD
TIGR00005\"[17-316]TrluA_subfam: pseudouridine synthase, RluA f
noIPR
unintegrated
unintegrated
PTHR10436\"[3-306]TRIBOSOMAL PSEUDOURIDINE SYNTHASE


","BeTs to 19 clades of COG0564COG name: Pseudouridylate synthases, 23S RNA-specificFunctional Class: JThe phylogenetic pattern of COG0564 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1e-60) to 4/4 blocks of the IPB000613 family, which is described as \"Pseudouridine synthase\". Interpro entry for IP:IPR000613. IPB000613A 97-117 2.6e-09 IPB000613B 142-181 8.6e-26 IPB000613C 240-264 3.3e-15 IPB000613D 279-292 3.3e-06Significant hit ( 2.5e-54) to 3/3 blocks of the IPB002990 family, which is described as \"Pseudouridine synthase, Rlu family\". Interpro entry for IP:IPR002990. IPB002990A 97-117 1.6e-09 IPB002990B 142-180 8.9e-26 IPB002990C 240-264 2.5e-16","Residues 10 to 315 match (2e-09) PD:PD112947 which is described as L2759.7 ","","","","","","","","","","","Tue Jan 21 14:17:18 2003","Tue Jan 21 14:17:18 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02913 is paralogously related to AA01355 (2e-30), AA00513 (9e-29), AA02276 (1e-24) and AA02063 (3e-17).","","","","","","Residues 103 to 252 (E-value = 2.1e-56) place AA02913 in the PseudoU_synth_2 family which is described as RNA pseudouridylate synthase (PF00849)","","","","","Conrad,J., Sun,D., Englund,N. and Ofengand,J. The rluC gene of Escherichia coli codes for a pseudouridine synthase that is solely responsible for synthesis of pseudouridine at positions 955, 2504, and 2580 in 23 S ribosomal RNA J. Biol. Chem. 273 (29), 18562-18566 (1998) PubMed: 9660827 ","","Tue Jan 21 14:17:18 2003","1","","","" "AA02915","2041112","2040792","321","ATGAGCGAAGTATTACATTCCAGCGATGCAACATTCGTTGCAGACGTTTTAAATTCAGAGGTCCCTGTATTATTAGACTTTTGGGCTACATGGTGCGGACCGTGCAAAATGATTGCCCCGATCCTTGATGATTTGGCGGTGGAATTTGATGGTAAAGTGAAAATTGTGAAAATCAATATTGACGATAACCAGGCCACCCCTGCACAGTTCGGCGTGCGTAGTGTCCCGACACTATTATTATTTAAAGATGGCAAACCGGTAGCAACCCAAGTCGGCGCCTTACCGAAAAATCAATTGGCCGCATTTATCAACCAAAATATC","","","11579","MSEVLHSSDATFVADVLNSEVPVLLDFWATWCGPCKMIAPILDDLAVEFDGKVKIVKINIDDNQATPAQFGVRSVPTLLLFKDGKPVATQVGALPKNQLAAFINQNI","2040627","[FUNCTION] Component of the thioredoxin-thioredoxin reductase system. Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (By similarity).","thioredoxin m","Cytoplasm, Periplasm","","
InterPro
IPR005746
Family
Thioredoxin
TIGR01068\"[7-107]Tthioredoxin
InterPro
IPR006662
Domain
Thioredoxin-related
PR00421\"[23-31]T\"[31-40]T\"[71-82]TTHIOREDOXIN
PS00194\"[24-42]TTHIOREDOXIN
InterPro
IPR012335
Domain
Thioredoxin fold
G3DSA:3.40.30.10\"[2-107]TThioredoxin_fold
InterPro
IPR012336
Domain
Thioredoxin-like fold
SSF52833\"[2-107]TIPR012336
InterPro
IPR013766
Domain
Thioredoxin domain
PF00085\"[3-106]TThioredoxin
InterPro
IPR015467
Domain
Thioredoxin family
PTHR10438\"[14-107]TTrx
noIPR
unintegrated
unintegrated
PTHR10438:SF13\"[14-107]TPTHR10438:SF13


","No hits to the COGs database.","Significant hit ( 1.3e-08) to 1/1 blocks of the IPB000063 family, which is described as \"Thioredoxin\". Interpro entry for IP:IPR000063. IPB000063 23-36 1.4e-08","Residues 16 to 87 match (6e-07) PD:PD384488 which is described as M PROTEOME COMPLETE THIOREDOXIN ","","","","","","","","","","","Tue Jan 21 14:13:07 2003","Tue Jan 21 14:13:07 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02915 is paralogously related to AA02603 (9e-07), AA02442 (5e-05), AA00054 (2e-04) and AA00040 (0.001).","","","","","","Residues 3 to 107 (E-value = 2.3e-45) place AA02915 in the Thioredoxin family which is described as Thioredoxin (PF00085)","","","","","Lim CJ, Geraghty D, Fuchs JA. Cloning and nucleotide sequence of the trxA gene of Escherichia coli K-12. J Bacteriol 1985 Jul;163(1):311-6. PubMed: 3891733.Holmgren,A. Thioredoxin. 6. The amino acid sequence of the protein from escherichia coli B. Eur. J. Biochem. 6 (4): 475-484 (1968) [PubMed: 4883076].Kotani,H. and Nakajima,K. Cloning and sequence of thioredoxin gene of Salmonella typhimurium LT2. Nucleic Acids Res. 20 (6): 1424 (1992) [PubMed: 1561103]. ","","Tue Jan 21 14:13:07 2003","1","","","" "AA02916","2042207","2041215","993","ATGAAAGTTGCAGTATATAGCACCAAAAGTTATGACCGAAAATATTTAGAGTTAATTGATGCTAAATACGGCTTGGATTTGGAATTTTACGATTTCATGCTCAGTGAGCGCACGGCAAAAATGGCGGAACATTGTGAAGCCGTATGTATTTTCGTGAATGATGACGGAAGCAGAAAAGTGTTGGAAAAACTCGCCGCACTTGGAGTAAAAATTATTGCCTTGCGTTGCGCCGGTTTTAATAATGTAGATTTAAAAGCCGCCCAAGAACTCGGTTTGACGGTCGTTCGTGTGCCGGCATATTCACCGGAAGCGGTGGCAGAACATACGGTCGGCTTAATGATGACGTTAAACCGTCGTATTCATCGCGCTTACCAACGCACCCGTGAAGCTAACTTCTCCTTAGAAGGGCTGATCGGTTTCAATATGTATGGTCGCACCGTCGGTGTTATCGGCACAGGTAAAATAGGTGTTGCGGTCATGCGTATTCTAAAAGGCTTCGGTATGCACATTTTAGCCTTTGACCCATTCAAAAATCCGACAGCGGAAGAGTTAGGCGCAGAATATGTCAGCCTGGATGAGATTTATCGACGTTCTCATGTTATTACCTTGCATTGCCCGGCAACACCGGAAAACTATCATTTGCTGAATCGCGAAGCCTTTGCCAAAATGAAAGACGGCGTGATGATCATCAACACCAGTCGTGGTACGCTGATTGATACTAAAGCGGCAATTGATGCGTTGAAACAGCGTAAAATCGGTGCTTTAGGTATGGATGTATATGAAAACGAAAGGGATTTATTCTTTGAGGATAAATCCAATGAAGTGATTCTGGATGACGTATTCCGTCGTTTATCTTCCTGTCACAATGTGTTATTAACAGGCCATCAGGCATTTCTAACGGAAGAGGCGCTAACCAGCATTGCCGATGTTACCCTGTCTAATATTTATGCTATTGGGAAAGGCAAACCTTGCGATAATGTAGTTTTGTCTTCT","","","37301","MKVAVYSTKSYDRKYLELIDAKYGLDLEFYDFMLSERTAKMAEHCEAVCIFVNDDGSRKVLEKLAALGVKIIALRCAGFNNVDLKAAQELGLTVVRVPAYSPEAVAEHTVGLMMTLNRRIHRAYQRTREANFSLEGLIGFNMYGRTVGVIGTGKIGVAVMRILKGFGMHILAFDPFKNPTAEELGAEYVSLDEIYRRSHVITLHCPATPENYHLLNREAFAKMKDGVMIINTSRGTLIDTKAAIDALKQRKIGALGMDVYENERDLFFEDKSNEVILDDVFRRLSSCHNVLLTGHQAFLTEEALTSIADVTLSNIYAIGKGKPCDNVVLSS","2041050","[FUNCTION] Fermentative lactate dehydrogenase. ","2-hydroxyacid dehydrogenase; D-lactate dehydrogenase","Cytoplasm","","
InterPro
IPR006139
Domain
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic region
PF00389\"[3-329]T2-Hacid_dh
InterPro
IPR006140
Domain
D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding
PF02826\"[110-297]T2-Hacid_dh_C
PS00065\"[147-174]TD_2_HYDROXYACID_DH_1
PS00670\"[194-216]TD_2_HYDROXYACID_DH_2
PS00671\"[223-239]TD_2_HYDROXYACID_DH_3
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[102-297]Tno description
PTHR10996\"[1-331]T2-HYDROXYACID DEHYDROGENASE
PTHR10996:SF17\"[1-331]T2-HYDROXYACID DEHYDROGENASE


","No hits to the COGs database.","Significant hit ( 3.3e-65) to 5/5 blocks of the IPB002162 family, which is described as \"D-isomer specific 2-hydroxyacid dehydrogenase\". Interpro entry for IP:IPR002162. IPB002162A 81-118 1.3e-19 IPB002162B 144-156 4.8e-06 IPB002162C 191-204 0.13 IPB002162D 211-260 1.1e-26 IPB002162E 284-303 1.8e-05","Residues 105 to 216 match (3e-12) PD:PD349508 which is described as PROTEOME COMPLETE DEHYDROGENASE OXIDOREDUCTASE REDUCTASE 2-HYDROXYACID HYDROXYPYRUVATE PYRUVATE D-ISOMER SPECIFIC ","","","","","","","","","","","Tue Jan 21 14:06:23 2003","Tue Jan 21 14:06:23 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02916 is paralogously related to AA01614 (5e-30) and AA02375 (4e-23).","","","","","","Residues 105 to 295 (E-value = 1.3e-103) place AA02916 in the 2-Hacid_dh_C family which is described as D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain (PF02826)","","","","","Chuang,S.E. and Blattner,F.R. Characterization of twenty-six new heat shock genes of Escherichia coli. J. Bacteriol. 175 (16): 5242-5252 (1993) [PubMed: 8349564].Bunch,P.K., Mat-Jan,F., Lee,N. and Clark,D.P. The ldhA gene encoding the fermentative lactate dehydrogenase of Escherichia coli. Microbiology 143 (Pt 1): 187-195 (1997) [PubMed: 9025293].","","Tue Jan 21 14:06:23 2003","1","","","" "AA02917","2043340","2042234","1107","ATGACACAAAAATATGCGATTGATACCCTATTAGCCCAAGCCGGCAATCGCACCGACGAGCGCACCGGCGCCGTTTCCACCCCAATTTTCCTTTCTACCGCTTACGGGCACCATGGCATTGGTGAAAGTACCGGTTTTGATTATACCCGAACCAAAAATCCTACTCGCGCTGTGTTAGAAGAGACTATCGCCCAATTAGAAAAGGGCGAGCGCGGTTTTGCCTGCTCTTCCGGCATGGCGGCAATTCAATTATTGATGTCATTATTTACGTCACCCGATGAGTGGATTGTATCCAGTGATGTTTATGGTGGAACTTATCGTTTATTGGATTTTTGTTACAAAAACACCAACGGCGTCAAACCGGTTTATGTGAATACCGCTTCTGTTCAGGCGATTGAAGGGGCGATTACGTCGAACACCAAAGCAGTTTTTATTGAAACTCCCTCCAATCCGTTAATGGAAGAATGCGATGTGGATGCCATTGCCAAGGTGGCGAAAAAGCACAATTTATTACTTATTGTCGATAATACGTTCCTCACGCCGGTGTTATTCCGCCCGATGGAACATGGGGCTGATATTGTGATTCATAGCGGGACCAAATATATTGCCGGGCATAATGACGTTTTAGTCGGTTTGATTGTTGCTAAAGGGCAAGAACTGTGTGATCGCCTGTTTTACATCCAAAACGGTGCGGGCCCGGTGTTATCGCCGTTTGACTCCTGGTTAACCATTCGCGGTATGAAAACTTTGGCATTGCGTATGCAGCGTCATGAAGAAAATGCCAAAGCCATCGCCGAATTTTTGCGTCAACAACCGCAAGTGAAAGATGTGTTGTATCCTAATAAAGGCGGTATGTTATCTTTCCGCCTGCAGGATGAAAGTTGGGTTAATACGTTCTTGAAGGCGATTAAATTGATTACGTTCGCCGAAAGCCTTGGCGGTACCGAAAGTTTCATTACTTACCCGGCAACTCAAACCCACATGGATATTCCGGAAGCAGAGCGCATTGCGCGCGGTATCACCAATAATCTGCTGCGTTTCTCTGTCGGTTTGGAAAATGTGGAAGACATCAAAGCGGATCTGGTACAGGCGTTTGCACAGCTTAAA","","","42161","MTQKYAIDTLLAQAGNRTDERTGAVSTPIFLSTAYGHHGIGESTGFDYTRTKNPTRAVLEETIAQLEKGERGFACSSGMAAIQLLMSLFTSPDEWIVSSDVYGGTYRLLDFCYKNTNGVKPVYVNTASVQAIEGAITSNTKAVFIETPSNPLMEECDVDAIAKVAKKHNLLLIVDNTFLTPVLFRPMEHGADIVIHSGTKYIAGHNDVLVGLIVAKGQELCDRLFYIQNGAGPVLSPFDSWLTIRGMKTLALRMQRHEENAKAIAEFLRQQPQVKDVLYPNKGGMLSFRLQDESWVNTFLKAIKLITFAESLGGTESFITYPATQTHMDIPEAERIARGITNNLLRFSVGLENVEDIKADLVQAFAQLK","2042069","","cystathionine gamma-synthase","Cytoplasm","","
InterPro
IPR000277
Family
Cys/Met metabolism pyridoxal-phosphate-dependent enzymes
PTHR11808\"[85-368]TTRANS-SULFURATION ENZYME FAMILY MEMBER
PF01053\"[8-366]TCys_Met_Meta_PP
PS00868\"[192-206]TCYS_MET_METAB_PP
InterPro
IPR015421
Domain
Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10\"[3-250]Tno description
InterPro
IPR015422
Domain
Pyridoxal phosphate-dependent transferase, major region, subdomain 2
G3DSA:3.90.1150.10\"[251-369]Tno description
noIPR
unintegrated
unintegrated
PIRSF001434\"[9-369]TCystathionine gamma-synthase
PTHR11808:SF15\"[85-368]TCYSTATHIONINE GAMMA-LYASE (GAMMA-CYSTATHIONASE)


","No hits to the COGs database.","Significant hit ( 1e-103) to 6/6 blocks of the IPB000277 family, which is described as \"Cys/Met metabolism pyridoxal-phosphate-dependent enzymes\". Interpro entry for IP:IPR000277. IPB000277A 45-66 8.7e-10 IPB000277B 138-171 1.4e-17 IPB000277C 175-210 5.7e-25 IPB000277D 232-272 8e-29 IPB000277E 311-327 1.7e-06 IPB000277F 344-361 2.2e-09","Residues 142 to 357 match (4e-10) PD:PD024577 which is described as CYSTATHIONINE GAMMA-SYNTHASE PHOSPHATE METHIONINE LYASE PYRIDOXAL BIOSYNTHESIS THIOL-LYASE O-SUCCINYLHOMOSERINE CHROMOSOME ","","","","","","","","","","","Mon May 23 11:03:49 2005","Mon May 23 11:02:48 2005","","Mon May 23 11:02:48 2005","Mon May 23 11:03:49 2005","Mon May 23 11:02:48 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA02917 is paralogously related to AA00662 (2e-36) and AA00084 (0.001).","Mon May 23 11:02:48 2005","","","","","Residues 8 to 366 (E-value = 1.4e-214) place AA02917 in the Cys_Met_Meta_PP family which is described as Cys/Met metabolism PLP-dependent enzyme (PF01053)","Mon May 23 11:02:48 2005","","","","","","","1","","","" "AA02918","2043561","2043460","102","GTGCATTTTACTGACTTATCTAAAACTGTCAACAAACAATTAAAAAAAACGATGAGTTTGTCGAAAAAATACAAAAGGTTAAAAAATTCCGAGGTTAAATTT","","","4038","VHFTDLSKTVNKQLKKTMSLSKKYKRLKNSEVKF","2043460","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 11:47:13 2004","Mon Feb 23 11:47:13 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02918 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 11:47:55 2004","","","","","","","","","","","","","1","","","" "AA02919","2044342","2045361","1020","ATGGTCCCTGAAATTTTATTAGCTTGCTCAACAATAGTTCACATTGAAACACTTCACGCATTAATTCAAACAGAAAGCTCATATAATCCTTATGCTATCGCAGTAGTAAATGATATTCCTCTTGCTCAACAGCCTAAAACACTCCAAGAAGCAGAATTAGTCATAGATGAACTTGAAGCTAAAAAAATAAATTATTCGGTTGGATTGGGACAAGTGAACAAAGGGAATTTTGCAAAATATGGTGTAACAGGTAAACAACTATTAGATAGTTGCACTAATATCAAAGTGAGTGAAAAAATTCTGTCTGCATGCTATGCCAAATCACCAAATAAATCGGTTGCAGAGGCGTTGAGTTGTTATTACGCAGGGAATTTCTCTTATGGCTTTGTACGGGAGGGTAAATACGGCATTACCCGCTTACTTGAAAATATTCAGGAAGATACCGAAAACCCGAATTCCCTTTATAGCCGTTTAACAATTTGGAAAAAAGGCGGGATTTATGGATGGGTGTTTGACAACGAAAACGACCAACTCTCTTTTGATGACCGCATAATTTACGGCTTTGATGGTACAGAAATTCTAGATAATGCAGCGGTGATTAATGCTATTGCTTATTATCTCTTATATCGTGTACAACAAACGCTTGATGGTCGCCGAATGGTTGTTTTCCTTGATGAATTTTGGAAATGGTTACAAGGTGAAAGCTTTCGGGAATTTACCTTTGACGGCTTAAAAACAATGCGTAAGAAAAATGGTTTTGTTGTACCAATCACTCAGTCGCCAAGTGAGATTTTAAAAAGTGATATTGCACGAGCCATTATTGAACAGGTAGAAACATTTATCTATCTCCCAAATAGTAAAGCGGATAGAAATGAGTATATCAATCATTTCAGAGTATCGGAAAAAGAATTTGACCTTATCACCGGGCTTGAAGATGATAGCCGAATGTTCTTAGTCAAGAAAGGTAATGAAAACGATAATCGCGGCAACACTGGTATAAAAAAATGTTTAAAGGTCGTT","","","38610","MVPEILLACSTIVHIETLHALIQTESSYNPYAIAVVNDIPLAQQPKTLQEAELVIDELEAKKINYSVGLGQVNKGNFAKYGVTGKQLLDSCTNIKVSEKILSACYAKSPNKSVAEALSCYYAGNFSYGFVREGKYGITRLLENIQEDTENPNSLYSRLTIWKKGGIYGWVFDNENDQLSFDDRIIYGFDGTEILDNAAVINAIAYYLLYRVQQTLDGRRMVVFLDEFWKWLQGESFREFTFDGLKTMRKKNGFVVPITQSPSEILKSDIARAIIEQVETFIYLPNSKADRNEYINHFRVSEKEFDLITGLEDDSRMFLVKKGNENDNRGNTGIKKCLKVV","2045196","","CagE protein (tranport-associated)","Cytoplasm, Outer membrane","","
InterPro
IPR008258
Domain
Lytic transglycosylase, catalytic
PF01464\"[2-143]TSLT


","BeTs to 4 clades of COG3451COG name: Type IV secretory pathway, VirB4 componentsFunctional Class: NThe phylogenetic pattern of COG3451 is ------------------s-ujx---Number of proteins in this genome belonging to this COG is","Significant hit ( 4.2e-07) to 2/2 blocks of the IPB000189 family, which is described as \"SLT domain\". Interpro entry for IP:IPR000189. IPB000189A 25-49 0.0018 IPB000189B 87-101 0.1","Residues 170 to 221 match (8e-08) PD:PD567048 which is described as VIRB4 PLASMID ATPASE PROTEOME COMPLETE ASSOCIATED HOMOLOG ","","","","","","","","","","","","Fri Jan 31 15:25:20 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02919 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 143 (E-value = 1.4e-05) place AA02919 in the SLT family which is described as Transglycosylase SLT domain (PF01464)","","","","Novak,K.F., Dougherty,B. and Pelaez,M.Actinobacillus actinomycetemcomitans harbours type IV secretionsystem genes on a plasmid and in the chromosomeMicrobiology 147 (Pt 11), 3027-3035 (2001)PubMed: 21557162Galli,D.M., Chen,J., Novak,K.F. and Leblanc,D.J.Nucleotide Sequence and Analysis of Conjugative Plasmid pVT745J. Bacteriol. 183 (5), 1585-1594 (2001)PUBMED 11160089","","Fri Jan 31 15:25:20 2003","","1","","","" "AA02920","2045534","2045809","276","ATGGCAAAATACTATGAGCGCAATCCGAATAGCCCATTTTTCCACCTTATGCAAGATACATCCGTAGAAGACAAATTAAGTGAAGAAGAAAAAGAGCGTATTGTATGGATCACAAAAACAAACCTGATTTCAGTCGATCTTGAAACCGAAAAAAGTACTCCAGATGAAGAAGCCTATCTTCTTTATGTTGCACTAAATGATGTGCCAGCAGATGAAGCAACAAGAAATTTACTTATCAATGAACTAGGTAAAGAAGAAGTCGAGGCGTTAGGACTT","","","10588","MAKYYERNPNSPFFHLMQDTSVEDKLSEEEKERIVWITKTNLISVDLETEKSTPDEEAYLLYVALNDVPADEATRNLLINELGKEEVEALGL","2045644","","hypothetical protein","Cytoplasm","","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Tue Jan 21 11:53:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02920 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02921","2045814","2046134","321","ATGGATCCTTTTAAATTTATTAGAGAGAGTGAAGTCCCGCCCGAAAACAACATTGTTTCTTTTAAGGGGCTTACTGAAACTGAAAAATGGTATGCTTACTTCTACAAAGGAACGCAGGTGATGAAAAACCTTCTCAGTATTAGAGATGCTGAGAAGTTAGAAAAAGTGGAAAAGCAAATATCAAGAGTCAAAGCAGTAAGTGTTAATAAACTCAATATAGAAAGAGATTTTGATTTCAATAGACTAAAATCGATTCATAGATTTTATTTTGAAGAACTATATTCTTGGGCGGGTGAACCGAGACAAGTTAATATGTATAAA","","","12906","MDPFKFIRESEVPPENNIVSFKGLTETEKWYAYFYKGTQVMKNLLSIRDAEKLEKVEKQISRVKAVSVNKLNIERDFDFNRLKSIHRFYFEELYSWAGEPRQVNMYK","2046134","","conserved hypothetical protein (cell filamentation protein)","Cytoplasm","This sequence is similar to gi|28198904, a predicted cell filamentation protein from Xylella fastidiosa Temecula1. See also gi|23121605 from Desulfitobacterium hafniense.","No hits reported.","BeTs to 7 clades of COG2184COG name: Protein involved in cell divisionFunctional Class: DThe phylogenetic pattern of COG2184 is ----------r---ef-hsnuj----Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Mon Feb 23 11:36:19 2004","Mon Feb 23 11:38:38 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to AA0742, possible cell filamentation protein.AA02921 is paralogously related to AA01132 (5e-08).","Mon Feb 23 11:38:12 2004","","","","","","","","","","","","","1","","","" "AA02922","2047501","2046365","1137","TTGGAACAGGAGCGTATTTTAGCCGCCAACGCGCAGGATATTGATGCTGCAAAACAAAGCGGTTTGTCGGACGCGATCATCGACCGCTTATTATTAACGCCGGAACGTTTACAGGGCATTGCTAACGATGTGCATCATGTGATTTCCCTTGCGGATCCTGTGGGGCAAATTATTGATAGCGGTTTGTTGGACAGTGGTGTGAAAATTGAACGGGTACGCGTGCCTTTGGGTGTTATAGGTACCATTTATGAAGCCCGTCCGAACGTGACTATTGATGTTGTGGGTTTATGCTTAAAAACCGGCAATGCAGTGGTTTTGCGTGGCGGTAAAGAAACGCAGCATTCCAATAAAGTGTCGGTGGAGGTGGTGCAAAATGCCTTGGAACGCGCAGGGCTGCCGAAAACGGCGGTACAAGCGATTACCGATCCTTATCGTGCGTTGGTCATGGAATTATTAAAATTGGATCGCTATGTGGATATGATTATTCCGCGTGGTGGTGCGGCGTTACATCAATTGGCGAAGGAACATTCCACCATTCCGGTGATTGTCGGCGGCATCGGTGTTTGTCATATGTTTGTGGAAGAAAGTGCCGATTTAGAAAAAGCCTTGCCGATGATTTTAAACGCGAAAACCCAGCGAGCGAGTACGTGTAATACGTTGGAAACCCTTTTAGCGCAATGTAGCATTGCCGATGAATTTTTGCCGCGACTAGCAGATTATTTACAGGTGAAAAACGTAAAATTACATGCCGATCCGACCGCACTTTCACTCTTGCAAAAAGCCGGTGCAGAGGTTTATCCGCTAAAAGAAGAGTTGAAACAGGAATGGTTGTCTTTGGATTTGAATGTGGTGGTAGAGGATTTGGAGCAAGTGGTAGCTCATATTCGTCAATATGGCAGCCGGCACTCCGATAGCATTTTGACCGGTTCACAAAAATTGGCACAGCAATTTATTACCCAAGTGGATTCGGCGGCGGTGTATGTGAATGCAAGCACCCGTTTCACTGACGGCGGGCAATTCGGATTAGGCGCAGAAGTGGCGGTGAGTACACAGAAATTACACGCACGCGGTCCGATGGGATTAGAGGCCTTAACAACCTATAAATGGGTTTTTGTTGGCGATCATTCGATCCGATCT","","","41323","LEQERILAANAQDIDAAKQSGLSDAIIDRLLLTPERLQGIANDVHHVISLADPVGQIIDSGLLDSGVKIERVRVPLGVIGTIYEARPNVTIDVVGLCLKTGNAVVLRGGKETQHSNKVSVEVVQNALERAGLPKTAVQAITDPYRALVMELLKLDRYVDMIIPRGGAALHQLAKEHSTIPVIVGGIGVCHMFVEESADLEKALPMILNAKTQRASTCNTLETLLAQCSIADEFLPRLADYLQVKNVKLHADPTALSLLQKAGAEVYPLKEELKQEWLSLDLNVVVEDLEQVVAHIRQYGSRHSDSILTGSQKLAQQFITQVDSAAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARGPMGLEALTTYKWVFVGDHSIRS","2046200","[PATHWAY] Proline biosynthesis; second step.[FUNCTION] Catalyzes the NADPH into L-glutamate 5-semialdehyde andphosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. ","gamma-glutamylphosphate reductase","Cytoplasm","","
InterPro
IPR000965
Domain
Gamma-glutamyl phosphate reductase GPR
TIGR00407\"[1-368]TproA: gamma-glutamyl phosphate reductase
InterPro
IPR012134
Family
Glutamate-5-semialdehyde dehydrogenase
PTHR11063:SF1\"[2-379]TGLUTAMATE SEMIALDEHYDE DEHYDROGENASE
noIPR
unintegrated
unintegrated
G3DSA:3.40.309.10\"[182-359]Tno description
G3DSA:3.40.605.10\"[2-181]Tno description
PTHR11063\"[2-379]TGLUTAMATE SEMIALDEHYDE DEHYDROGENASE


","No hits to the COGs database.","Significant hit (2.9e-107) to 5/5 blocks of the IPB000965 family, which is described as \"Gamma-glutamyl phosphate reductase\". Interpro entry for IP:IPR000965. IPB000965A -20-32 15 IPB000965B 78-115 8.3e-27 IPB000965C 179-226 3.4e-29 IPB000965D 274-320 2.3e-10 IPB000965E 321-360 2e-36","Residues 3 to 239 match (3e-09) PD:PD011559 which is described as DEHYDROGENASE COMPLETE PROTEOME OXIDOREDUCTASE ALCOHOL ALDEHYDE-ALCOHOL ACETALDEHYDE MULTIFUNCTIONAL ALCOHOL-ACETALDEHYDE ETHANOLAMINE ","","","","","","","","","","","Tue Jan 21 11:52:18 2003","Tue Jan 21 11:52:18 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02922 is paralogously related to AA02784 (6e-09).","","","","","","Residues 1 to 374 (E-value = 9.2e-06) place AA02922 in the Aldedh family which is described as Aldehyde dehydrogenase family (PF00171)","","","","","Deutch,A.H., Rushlow,K.E. and Smith,C.J. Analysis of the Escherichia coli proBA locus by DNA and protein sequencing. Nucleic Acids Res. 12 (15): 6337-6355 (1984) PubMed: 6089111. ","","Mon Jan 27 15:08:19 2003","1","","","" "AA02925","2048211","2047633","579","ATGGATATTTTCGGCGTGATTATTATCGCCAGCATGACGGCAATTGGTGGCGGTTCGGTGCGCGATGTGTTGTTAGGGCATTATCCGCTGGGTTGGGTGAAGCACCCCGAATATTTTATTATTGTGGCATCTGCGGCGGTGTTGACCGTGGTTATTGCCCCTTTTATTCGGCATTTTATGCGTTATTTTCAAACTATTTTCTTGGTGCTGGATGCGGTCGGTTTAATTGTGTTTTCCATTATTGGCGCCCAAATCGCCTTGGATATGGGGCATGGCACGACAATTGCCATTATTGCGGCGATCATCACCGGCGCATTCGGCGGCGTATTGCGCGATTTACTGTGTAACCGCATTCCGCTCGTGTTCCAGAAAGAATTGTATGCCAGTGTCGCTTTATTGGCGACGGCGATTTATATTGGCTTGCAACACTTAAATATCGATCAGAATCTTGTCATTATTGTGACCTTAATCGTGGGATTTATCACCCGCTTATTGGCAATTCATTTTGAATGGGGACTGCCAATTTTTGATTATCAGGAACAGGATATTTCAAAGCACCATAAAGACGATAAATTACCG","","","23892","MDIFGVIIIASMTAIGGGSVRDVLLGHYPLGWVKHPEYFIIVASAAVLTVVIAPFIRHFMRYFQTIFLVLDAVGLIVFSIIGAQIALDMGHGTTIAIIAAIITGAFGGVLRDLLCNRIPLVFQKELYASVALLATAIYIGLQHLNIDQNLVIIVTLIVGFITRLLAIHFEWGLPIFDYQEQDISKHHKDDKLP","2047468","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR005115
Domain
Protein of unknown function UPF0126
PF03458\"[1-62]T\"[67-151]TUPF0126
noIPR
unintegrated
unintegrated
signalp\"[1-17]?signal-peptide
tmhmm\"[5-24]?\"[38-56]?\"[66-86]?\"[90-110]?\"[120-140]?\"[150-168]?transmembrane_regions


","BeTs to 8 clades of COG2860COG name: Predicted membrane proteinFunctional Class: SThe phylogenetic pattern of COG2860 is -o-------d-lb-efgh--uj----Number of proteins in this genome belonging to this COG is","","Residues 109 to 181 match (5e-07) PD:PD331360 which is described as PROTEOME TRANSMEMBRANE COMPLETE CJ0593C ","","","","","","","","","","","","Tue Jan 21 11:46:45 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02925 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 67 to 151 (E-value = 3.5e-35) place AA02925 in the UPF0126 family which is described as UPF0126 domain (PF03458)","","","","","","","","1","","","" "AA02926","2048276","2048407","132","ATGCTGAGCAGCATAAGGTTCCTTAAAAGTGCGGTTAGTTTTCACGTTATTTTAGAGAGAGAAACGGCAAAATGCTATGTTTTAGATCATAACTTTATGTGGCTTGGTGCAGATAAAAAACGCCCGGATTTT","","","5183","MLSSIRFLKSAVSFHVILERETAKCYVLDHNFMWLGADKKRPDF","2048407","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 11:25:09 2004","Mon Feb 23 11:25:09 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02926 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 11:26:28 2004","","","","","","","","","","","","","1","","","" "AA02927","2048465","2048373","93","GTGCATTATGCAAGAATTCCAACAGGCGGTCAAAAGTCAGACGTAAAAAGTGCGGTTAAAAATCCGGGCGTTTTTTATCTGCACCAAGCCACA","","","3352","VHYARIPTGGQKSDVKSAVKNPGVFYLHQAT","2048373","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 11:17:04 2004","Mon Feb 23 11:17:04 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02927 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 11:17:42 2004","","","","","","","","","","","","","1","","","" "AA02928","2048501","2049304","804","ATGTCCGAACAACAACCTAAATTTTTAACCGCACTTTCTTCTTTGGCGCCCATTCTATTTTTACTGGTTATTGATATATTCACCCTGTGGTTACAAGCGCAATCCAAGGCGGTTTCTCATTTAGCGCTCGGTGTGCTGACAGCGCAACTGATTTGTCTGGTGGTATTCATTAAAGGCGAAATTTGTAACGGGCAACGTTCCCGTTTAAGTCGGGCTAACCTTTATTTTACGCTTTTTTGGCTGGTTTGGTTTCTGCTTAGTTTTTGGTCGAATTATCACTATATCTTAACGGATTTTGTCAGTGTTTGTGGTTTGGCAATGGCACTGACTACCTGGAAACAACCGCAGGAAGACGAATTGCGTCACGGATTGTTAAAAATGGCGGGATTAATCGGCTTACTGGGCACAACCTGTTATGCCATTACGTTATTTAACGACGTAAACCTGATTCAATTTAACCCGTTGGCACAAATGCTGTTAGGCGTTATTTTAGCCAATCTGATGCTGGTTATTGCGCGCAACCGCTTACAACAATTTATTGCATTATTGATTTTATGTATGGTGGCATTCCTTGCGCTAAACGCCATTTTCGTCGCGACAGCTTTATTCCATTTATACCAACAAAGTGCGGTCGTTTTTGCCAATGAATTTGCGTTGCTGCTCTACTTTGCTTTGCATGTTGTTATGGCGTTAATTCTTGGGCTGCACGTTTTCAAAAAATGGACACTATCCTATAACACGCTGTTTATTTTATTTCTGATTGCCGCCAGTTTGCCGCTCTGGGTAAATTTTGCTTATGTGGCA","","","32548","MSEQQPKFLTALSSLAPILFLLVIDIFTLWLQAQSKAVSHLALGVLTAQLICLVVFIKGEICNGQRSRLSRANLYFTLFWLVWFLLSFWSNYHYILTDFVSVCGLAMALTTWKQPQEDELRHGLLKMAGLIGLLGTTCYAITLFNDVNLIQFNPLAQMLLGVILANLMLVIARNRLQQFIALLILCMVAFLALNAIFVATALFHLYQQSAVVFANEFALLLYFALHVVMALILGLHVFKKWTLSYNTLFILFLIAASLPLWVNFAYVA","2049139","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR002086
Domain
Aldehyde dehydrogenase
PS00070\"[55-66]?ALDEHYDE_DEHYDR_CYS
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[1-178]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-35]?signal-peptide
tmhmm\"[9-31]?\"[37-57]?\"[69-88]?\"[94-112]?\"[124-144]?\"[150-170]?\"[179-199]?\"[218-238]?\"[247-267]?transmembrane_regions


","No hits to the COGs database.","","Residues 205 to 264 match (8e-07) PD:PD123656 which is described as PROTEOME COMPLETE HI1241 TRANSMEMBRANE PM0934 ","","","","","","","","","","","","Tue Jan 21 11:45:12 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02928 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02929","2049430","2049329","102","TTGAGAGGGGATTTTTTTTATGAAATATTTTTATCCGAAATTATTTTTCATTCATATTATTTCACTCACTCCATTTTATTTAATTTACTGATAAATAAAAAA","","","4212","LRGDFFYEIFLSEIIFHSYYFTHSILFNLLINKK","2049329","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
tmhmm\"[14-32]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 11:09:39 2004","Mon Feb 23 11:09:39 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02929 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 11:10:15 2004","","","","","","","","","","","","","1","","","" "AA02930","2050578","2049574","1005","ATGAAAACATTAGGTCAATTTATCGTAGAAAAACAAGCGGAATACCCACATGCTAAAGGAGAATTGAGCGGGATTTTATCTTCTATTCGCCTCGTGGCAAAAGTGGTTCATCGTGACATTAATAAAGCGGGGTTAACCAATGACATTATCGGTAATTCAGGCGTGCAAAACGTGCAGGGTGAAGCGCAAATGAAATTGGATTTATTTGCTCATAATACGATGAAACAGGCCCTAATGAGCCGTGAGGAAGTGGCAGGCTTTGCGTCTGAAGAAGAGGAAAATTTCATTGCTTTTGATACGGAACGCGGTCGTAACGCGAAATATGTTATTTTAACGGATCCATTGGATGGTTCTTCTAACATTGATGTTAATGTGGCGGTCGGCACGATTTTTTCTATTTATCGCCGTGTATCGCCCGTTGGTACACCGGTTACCCTCGAAGATTTCATGCAACCGGGTAATCGCCAAGTGGCGGCGGGTTACATCGTGTATGGTTCCTCCACTATGTTGGTTTATACCACCGGGCACGGCGTAAATGGTTTTACCTACGATCCGTCCCTTGGTGTATTTTGTCTTTCCCACGAAAATATCCAAATTCCGCAAACCGGCAAAATTTATTCCATTAATGAAGGGCAATACCTCAAATTCCCGATGGGCGTGAAAAAATATCTAAAATACTGCCAAGAGGAAGACAAAGAAACCCAACGTCCTTATACTTCCCGTTATATAGGTTCCTTGGTTTCCGACTTCCATCGCAATATGTTAAAAGGTGGAATCTACATTTACCCAAGTGCCACCAACTACCCGAACGGTAAATTACGCTTGTTGTACGAAGGCAATCCAATGGCATTCCTGGCTGAACAGGCTGGTGGTGTGGCGAGTGACGGCTATAACCGAATTTTAGATATTCAGCCGACTGCATTACACCAACGGGTTCCGCTTTTTATTGGCTCCAAAGAAATGGTGAAAAAAGCTGAACAGTTAATGCGTGATTTTAAAGACCAA","","","37296","MKTLGQFIVEKQAEYPHAKGELSGILSSIRLVAKVVHRDINKAGLTNDIIGNSGVQNVQGEAQMKLDLFAHNTMKQALMSREEVAGFASEEEENFIAFDTERGRNAKYVILTDPLDGSSNIDVNVAVGTIFSIYRRVSPVGTPVTLEDFMQPGNRQVAAGYIVYGSSTMLVYTTGHGVNGFTYDPSLGVFCLSHENIQIPQTGKIYSINEGQYLKFPMGVKKYLKYCQEEDKETQRPYTSRYIGSLVSDFHRNMLKGGIYIYPSATNYPNGKLRLLYEGNPMAFLAEQAGGVASDGYNRILDIQPTALHQRVPLFIGSKEMVKKAEQLMRDFKDQ","2049409","[PATHWAY] Involved in several metabolic pathways. In E.coli and yeast it is necessary for growth on substances such as glycerol,succinate and acetate. ","fructose-1,6-bisphosphatase","Cytoplasm","","
InterPro
IPR000146
Family
Inositol phosphatase/fructose-1,6-bisphosphatase
PD001491\"[3-200]TQ9CMA4_PASMU_Q9CMA4;
PR00115\"[113-134]T\"[152-172]T\"[177-192]T\"[240-263]T\"[271-291]T\"[300-322]TFBPHPHTASE
PR00377\"[109-120]T\"[254-264]T\"[277-291]TINFBPHPHTASE
PIRSF000904\"[1-335]TFructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase
PTHR11556\"[1-335]TFRUCTOSE-1,6-BISPHOSPHATASE-RELATED
PF00316\"[2-332]TFBPase
PS00124\"[271-283]TFBPASE
noIPR
unintegrated
unintegrated
G3DSA:3.30.540.10\"[3-196]Tno description
G3DSA:3.40.190.80\"[197-335]Tno description
PTHR11556:SF1\"[1-335]TFRUCTOSE-1,6-BISPHOSPHATASE


","BeTs to 10 clades of COG0158COG name: Fructose-1,6-bisphosphataseFunctional Class: GThe phylogenetic pattern of COG0158 is -o----y------cefgh-nuj----Number of proteins in this genome belonging to this COG is","Significant hit ( 1.1e-80) to 4/4 blocks of the IPB000146 family, which is described as \"Inositol phosphatase/fructose-1,6-bisphosphatase\". Interpro entry for IP:IPR000146. IPB000146A 51-93 1.6e-16 IPB000146B 106-133 5.1e-19 IPB000146C 151-185 9.8e-27 IPB000146D 271-291 1.4e-14","Residues 1 to 54 match (7e-21) PD:PD477929 which is described as PROTEOME COMPLETE HYDROLASE FRUCTOSE-16-BISPHOSPHATASE METABOLISM CARBOHYDRATE FRUCTOSE-BISPHOSPHATASE FBPASE 1-PHOSPHOHYDROLASE D-FRUCTOSE-16-BISPHOSPHATE ","","","","","","","","","","","Tue Jan 21 11:18:42 2003","Tue Jan 21 11:18:42 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02930 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 332 (E-value = 1.1e-196) place AA02930 in the FBPase family which is described as Fructose-1-6-bisphosphatase (PF00316)","","","","","Hamilton,W.D., Harrison,D.A. and Dyer,T.A. Sequence of the Escherichia coli fructose-1,6-bisphosphatase gene Nucleic Acids Res. 16 (17), 8707 (1988) PubMed: 2843822 Marcus,F., Gontero,B., Harrsch,P.B. and Rittenhouse,J.Amino acid sequence homology among fructose-1,6-bisphosphatases Biochem. Biophys. Res. Commun. 135 (2), 374-381 (1986) PubMed: 3008716 Tang GL, Yang CS, Bao JS, Wang YF, Chen HB, Shi DJ,Liu FL. Co-expression of Triosephosphate Isomerase, Fructose-1, 6-bisphosphate Aldolase and Fructose-1, 6-bisphosphatase in E.coli. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2001;33(1):131-136. PMID: 12053203 ","","Wed Jan 29 13:11:10 2003","1","","","" "AA02931","2050736","2052106","1371","ATGACAACCAAACATCTTCATATTCTCGGCATTTGCGGCACATTTATGGGCGGCATTGCGATGATCGCCAAGCAAATGGGCTATCATGTAACAGGCTCCGACACCAACGTTTACCCACCAATGAGCACTTTTCTTGCCGAAAATCACATTGAAATCATACCGCACTTTGAGCCAAGCCAGTTACAACCAGCGCCGGATATGGTCATCGTGGGAAATGCCATGAAACGCGGCAATCCCTGCATCGAGTATATGTTAGCAAATAACATTCCTTACACGTCCGGCCCGCAATGGTTGCACGATCATTTATTACGGGATCGCTGGGTTTTGGCAGTTTCCGGCACACACGGCAAAACCACGACCACCGGCATGCTAACTTGGATTTTGGAACAAAACGGTTTGCAACCGGGCTTTTTAATTGGCGGTATTGCAGGCAATTTCGGTATTTCCGCACGCTTAGGGCAAAGCCCGTATTTTGTTATTGAAGCGGATGAATACGATACGGCGTTTTTTGATAAACGATCCAAATTTGTACATTACAATCCGCGTATACTGATTATTAATAATATCGGCTTCGATCACGCGGATATTTTCGACGATCTAAACGCGATTCAGCGCCAATTCCATCACATGATCCGCACCATTCCAAACAATGGACGCATTCTCTCCTTTGCCGGTGAAGAAAGCGTACAACAAACCTTGGCGATGGGCTGCTGGTCGGAATGTCAGTACGTAGGCAAAGATCAGGAATGGTATGCCGAACGCATTAAACATGATTGTACGGAGTTTGCCGTTTACCATAAAGGTGAAAAAATCACGGAAGTGCATTGGAATATCGTAGGTGAACACAATATGCGTAACGGTTTGATGGCAATTGCGGCAGCGAATCATGCCGGTGTGAGCATTGAAAATGCCTGCGCGACGTTAGGATCCTTTATTAATGCGAAACGCCGTTTGGAAGTGAAAGGCAATGTTCATGGCATCACCGTTTATGATGATTTCGCCCATCACCCCACCGAAATACAGGCAACATTGACCGCACTTCGCGATAAAGTCGGGCAAAATGCGCGTATTCTGGCGGTGTTAGAGCCGCGTTCCAACACCATGAAAATGGGGGTACATAAAGATGAAATCGCACCAGCGTTAAAGCTGGCCGATGCGGTATTTCTATTCCAACCGGAAACTATTCTATGGAAAGTGGCGGATATTGCCGCACAATTAACACAACCAGCGTATGACAGTGATAATTTGGACACCTTCGTCGATCTGATTGTCGCCGAAACTAAACCGACAGATCACATTTTAGTGATGTCAAACGGCAGTTTCGGTGGTATTCACCAAAAACTTTTAGAGGCGCTACAGAAGAAAAGCGTT","","","54140","MTTKHLHILGICGTFMGGIAMIAKQMGYHVTGSDTNVYPPMSTFLAENHIEIIPHFEPSQLQPAPDMVIVGNAMKRGNPCIEYMLANNIPYTSGPQWLHDHLLRDRWVLAVSGTHGKTTTTGMLTWILEQNGLQPGFLIGGIAGNFGISARLGQSPYFVIEADEYDTAFFDKRSKFVHYNPRILIINNIGFDHADIFDDLNAIQRQFHHMIRTIPNNGRILSFAGEESVQQTLAMGCWSECQYVGKDQEWYAERIKHDCTEFAVYHKGEKITEVHWNIVGEHNMRNGLMAIAAANHAGVSIENACATLGSFINAKRRLEVKGNVHGITVYDDFAHHPTEIQATLTALRDKVGQNARILAVLEPRSNTMKMGVHKDEIAPALKLADAVFLFQPETILWKVADIAAQLTQPAYDSDNLDTFVDLIVAETKPTDHILVMSNGSFGGIHQKLLEALQKKSV","2051941","[FUNCTION] Reutilizes the intact tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelate by linking it toUDP-N-acetylmuramic acid. [PATHWAY] Cell wall synthesis; murein tripeptide recycling pathway; last step.","UDP-N-acetylmuramate:L-alanyl-gamma-d-glutamayl-medo-diaminopimelate","Cytoplasm","","
InterPro
IPR000713
Domain
Cytoplasmic peptidoglycan synthetase, N-terminal
PF01225\"[5-106]TMur_ligase
InterPro
IPR004101
Domain
Cytoplasmic peptidoglycan synthetases, C-terminal
PF02875\"[314-396]TMur_ligase_C
InterPro
IPR005757
Family
UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase
TIGR01081\"[5-453]Tmpl: UDP-N-acetylmuramate:L-alanyl-gamma-D-
InterPro
IPR012237
Family
UDP-N-acetylmuramate-alanine ligase
PIRSF001562\"[4-449]TUDP-N-acetylmuramate-alanine ligase
InterPro
IPR013221
Domain
Mur ligase, middle region
PF08245\"[109-294]TMur_ligase_M
noIPR
unintegrated
unintegrated
G3DSA:3.40.1190.10\"[95-311]Tno description
G3DSA:3.40.50.720\"[4-93]Tno description
G3DSA:3.90.190.20\"[315-454]Tno description
PTHR23135\"[111-454]TMUR LIGASE FAMILY MEMBER
PTHR23135:SF5\"[111-454]TUDP-N-ACETYLMURAMATE--L-ALANINE LIGASE
signalp\"[1-20]?signal-peptide
tmhmm\"[5-23]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 8.2e-05) to 1/5 blocks of the IPB001645 family, which is described as \"Folylpolyglutamate synthetase\". Interpro entry for IP:IPR001645. IPB001645A 108-132 8.2e-05","Residues 315 to 386 match (1e-09) PD:PD039273 which is described as LIGASE CELL COMPLETE PROTEOME UDP-N-ACETYLMURAMATE--ALANINE SYNTHETASE UDP-N- DIVISION WALL ACETYLMURAMOYL-L-ALANINE ","","","","","","","","","","","Tue Jan 21 11:15:01 2003","Tue Jan 21 11:15:01 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02931 is paralogously related to AA00833 (2e-37), AA00838 (1e-07) and AA00840 (2e-07).","","","","","","Residues 314 to 404 (E-value = 9.1e-21) place AA02931 in the Mur_ligase_C family which is described as Mur ligase family, glutamate ligase domain (PF02875)","","","","","Mengin-Lecreulx,D., van Heijenoort,J. and Park,J.T. Identification of the mpl gene encoding UDP-N-acetylmuramate: L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase in Escherichia coli and its role in recycling of cell wall peptidoglycan J. Bacteriol. 178 (18), 5347-5352 (1996) PubMed: 8808921 ","","Tue Jan 21 11:15:01 2003","1","","","" "AA02932","2052489","2053604","1116","ATGCTATTCAACCGCACTTCTTTTTATAAATTTCTCACGCTTTCCGCTATTGCGGTATTAACGGCATGTTCCTCCAATTCTAATAAACCTGCAGCCGGACAAACAACAGCCCAAAATACATTGGACATCGATCCGCAAAAATTCGGCGCAATTTATAACGGACGGACTTATCAGCAATCCATTTTTATGCCGGTGAGCCAAATTGAAAACAAAAGTGCGGTGGTAAATCAGGGTGATTTTTTAACCCAACTGTCAAATATAAATAATTATTCCGCTAAATTGAGCAGCAGCTTCGCCCCGCTTTACAACAAAGTGACCGCTTGGGTACTCGCCGGTGCCAATACCGGTGAATTAACTAATTTCGGTATCCAAAGCCAAGTGATGAAAGGCTTCGACGGCTATCAAAATGTACTCATGACGGGCTATTATTCCCCGGTGATTCATGCCCGTCGCACCCAACAAGGCAAATTTAACCAACCGATTTATGCACTTCCTTCGAAAAAACGTTTCTCCCGTGCCGAAATTTATGCCGGTGCATTGAGAGGTAAAGGTTTGGAATTGGCGTACAGCGATTCTATGATCGACAACTTTCTGCTGGGCGTGCAAGGCAGTGGTTATGTGGATTTTGGTGAAGGCAATTTGAATTATTTCGCTTACGCGGGACAAAACGGCTACCAATATGCGGCGGTCGGTCGCCTGCTGGTGGAAGACGGTGAAATTCCGAAAGAAAAAATGTCTATTCAGGCAATTCGCGATTGGGCGAATGCCAACCCTTCACGGGTGCAAAGCCTGTTAGAGCGCAACCCCTCTTATGTTTTCTTTAAAAATGATCCGTACGGAAAAGTAAAAGGTGCGGCAGGCGTGCCTTTGGTGCCGATGGCGTCCGTGGCGTCCGACCGCGGTGTGATTCCATTGGGTAGCGTGTTGCTGGTGGAGGTGCCGCAAATAGATAATGACGGCAACTGGACAGGGCAACATCAGTTACACCTCATGGTTGCGCTGGATGTGGGCGGTGCCGTGAACGGACACCATTTCGATTTATATCGCGGTATCGGCGATCAGGCGGGACATATTGCCGGCTTGTCGAAACATTACGGTCGCGTTTGGGTGTTACGT","","","40639","MLFNRTSFYKFLTLSAIAVLTACSSNSNKPAAGQTTAQNTLDIDPQKFGAIYNGRTYQQSIFMPVSQIENKSAVVNQGDFLTQLSNINNYSAKLSSSFAPLYNKVTAWVLAGANTGELTNFGIQSQVMKGFDGYQNVLMTGYYSPVIHARRTQQGKFNQPIYALPSKKRFSRAEIYAGALRGKGLELAYSDSMIDNFLLGVQGSGYVDFGEGNLNYFAYAGQNGYQYAAVGRLLVEDGEIPKEKMSIQAIRDWANANPSRVQSLLERNPSYVFFKNDPYGKVKGAAGVPLVPMASVASDRGVIPLGSVLLVEVPQIDNDGNWTGQHQLHLMVALDVGGAVNGHHFDLYRGIGDQAGHIAGLSKHYGRVWVLR","2053439","[FUNCTION] Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. Optimal activity is between ph 4.0 and 4.5; loses its activity rapidly at temperatures above 30 degrees celsius. Degrades murein glycan strands and insoluble, high-molecular weight murein sacculi. ","lytic murein transglycosylase A","Outer membrane, Extracellular","","
InterPro
IPR005300
Domain
MltA
PF03562\"[146-275]TMltA
InterPro
IPR010611
Domain
3D
PF06725\"[294-372]T3D
noIPR
unintegrated
unintegrated
PS51257\"[1-23]TPROKAR_LIPOPROTEIN
signalp\"[1-23]?signal-peptide


","No hits to the COGs database.","","Residues 1 to 79 match (2e-12) PD:PD390923 which is described as PROTEOME PM0928 COMPLETE ","","","","","","","","","","","Tue Jan 21 11:07:40 2003","Tue Jan 21 11:07:40 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02932 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 294 to 372 (E-value = 1.7e-31) place AA02932 in the 3D family which is described as 3D domain (PF06725)","","","","","Lommatzsch,J., Templin,M.F., Kraft,A.R., Vollmer,W. and Holtje,J.V. Outer membrane localization of murein hydrolases: MltA, a third lipoprotein lytic transglycosylase in Escherichia coli. J. Bacteriol. 179(17): 5465-5470, 1997. PubMed: 9287002. Ursinus,A. and Holtje,J.V. Purification and properties of a membrane-bound lytic transglycosylase from Escherichia coli J. Bacteriol. 176 (2), 338-343 (1994) PubMed: 8288527 Vollmer,W., von Rechenberg,M. and Holtje,J.V. Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli J. Biol. Chem. 274 (10), 6726-6734 (1999) PubMed: 10037771 ","","Tue Jan 21 11:07:40 2003","1","","","" "AA02933","2053607","2054374","768","ATGGCGCACATTGACAACTATGAACAACGCTTTGGCGGTATCGGCCGTTTATATGGCGCCGATGCTTTAGCGCGCTTGCGTAAAACGCACATTTGCGTAATCGGTATCGGCGGCGTCGGTTCCTGGGCGGTGGAAGCTCTCGCCCGTTCCGGCATCGGCAAGATTACGATGATTGATATGGATGATATTTGTGTTACCAATATTAATCGCCAGATTCATGCCTTGAGCGGTAATATCGGGCAACTCAAAACCGACATTATGCGGCAGCGGATCAGATTGATTAATCCCGAATGTGCAGTCAATATCATTGATGACTTTCTTTCTAGCGAAAATCTAGCCCAATACCTTCACAATAATCACGATTATATCATTGACGCTATTGATCAAGTGAAAACCAAAGCGGCGTTAATCGCTTATTGTAAACGGCACAAAATCAATATTATTACCATTGGAGGGGCAGGCGGACAAACGGATCCGAGCCAAATTCAGATTGCCGATTTAAGCCGAACCATTCAAGATCCGTTGCTGGCAAAAGTGCGGTCGGTTTTACGCAAGGATTATCATTTCACGCAAAATCCGAAACGCAAATTTTCCATTGATGCGGTATTCTCTAGCCAACCGCTGATTTTCCCTCAGGTCGGCGATAGCTGTGCCACTTCCGCAACCATGAATTGCGCCAATGGTTTTGGTGCGGCGACCATGATTACCGCCACATTCGGCTTTTTTGCCGTTTCCCGTGTTATTGATAAATTATTACAGAAAAATAAT","","","28576","MAHIDNYEQRFGGIGRLYGADALARLRKTHICVIGIGGVGSWAVEALARSGIGKITMIDMDDICVTNINRQIHALSGNIGQLKTDIMRQRIRLINPECAVNIIDDFLSSENLAQYLHNNHDYIIDAIDQVKTKAALIAYCKRHKINIITIGGAGGQTDPSQIQIADLSRTIQDPLLAKVRSVLRKDYHFTQNPKRKFSIDAVFSSQPLIFPQVGDSCATSATMNCANGFGAATMITATFGFFAVSRVIDKLLQKNN","2054209","","conserved hypothetical protein (HesA/MoeB/ThiF family protein)","Cytoplasm","","
InterPro
IPR000594
Domain
UBA/THIF-type NAD/FAD binding fold
PF00899\"[27-162]TThiF
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[5-254]Tno description
PTHR10953\"[16-175]TUBIQUITIN-ACTIVATING ENZYME E1
tmhmm\"[228-248]?transmembrane_regions


","No hits to the COGs database.","","Residues 19 to 147 match (1e-10) PD:PD094752 which is described as RPL14B-GPA1 ","","","","","","","","","","","","Fri Jan 31 15:27:25 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02933 is paralogously related to AA01661 (4e-16).","","","","","","Residues 27 to 162 (E-value = 6.2e-47) place AA02933 in the ThiF family which is described as ThiF family (PF00899)","","","","","","","","1","","","" "AA02934","2054477","2054382","96","TTGTATTTCCTTCTATTATTGAAATATGAATTGAATAAAACCAAGCTAGATTACTCTTTTTTAAGCGGAATTGCTATCTTTTTTTATTTTAAAAAA","","","3923","LYFLLLLKYELNKTKLDYSFLSGIAIFFYFKK","2054382","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
tmhmm\"[16-30]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 11:03:04 2004","Mon Feb 23 11:03:04 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02934 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 10:56:46 2004","","","","","","","","","","","","","1","","","" "AA02935","2054483","2055493","1011","ATGTTAGTGCAAAGCTTAAAGAAAACGGCAATTGCCGCTGCCATTCTTTCTTTTTCCGCTGCGGCTTCCGCAACAATTGTCACCTCCATTAAACCCTTAGGCTTTATTGCGACAGCCGTTGCAAATGGCGTTACCAATGTGGATGTATTAGTGCCGACCGGGGCTTCCCCTCATGATTACAATCTAAAACCCTCCGACGCGCAAAAACTAAAATCTGCTGAAATGGTAGTTTGGATTGGGGAAGATGTGGATGCTTTCTTAGATAAATCCATTGACGATCTTGATTATAAGAAAGTGCTGACAATCAAAGACATCGCCGCCATTGAACCGTTTTTAATGAAAGGATCCCATCACCATCATCACCATGGCGAAGGCAACGCGCATGAAGAGCATGATCATTCACACGAGGGGCATAATCACACACATGAAGGTCATGATCACAAGCATGAACATGGACACGATCACGAAGGACATGCACATCATCACGACGACGATTCAAGCATTAACTGGCATGTATGGTATTCACCGGATATTAGTAAAGCGGTCGCGCAACGCATTGCTGTAAAACTCATCAAACAATATCCGGAGAAAAAAGCGTTGATTGAAAAAAACATCTCCGAATTTAACCGCACTTTAGATGACACAAGTGCAAAAATTAACGTGCAATTGGAAAGTGTAAAAGATAAAGGGTTCTATGTTTTCCACGACGCCTACGGCTATTTCAACCACGCTTACGGTTTAAAACAAATCGGCTATTTCACCATCAATCCGCTTGTTGCACCGGGCGCAAAAACCTTGGCAAAAATCAAAGAAGAAATTGCCGAACACAAAGTCAGCTGTTTATTTGCCGAACCTCAGTTTACACCTAAAATGATTGAAAGCTTAAGTAAAGGCGCACAGGTGAATGTAGGACGTCTTGACCCAATGAGCGATAGTGTGAAAATGGAAGGAAATCCTTACGCCGCGTTCTTGCAATTTACGGCGGATAGCTATATGCAATGTTTAGCAAAA","","","37576","MLVQSLKKTAIAAAILSFSAAASATIVTSIKPLGFIATAVANGVTNVDVLVPTGASPHDYNLKPSDAQKLKSAEMVVWIGEDVDAFLDKSIDDLDYKKVLTIKDIAAIEPFLMKGSHHHHHHGEGNAHEEHDHSHEGHNHTHEGHDHKHEHGHDHEGHAHHHDDDSSINWHVWYSPDISKAVAQRIAVKLIKQYPEKKALIEKNISEFNRTLDDTSAKINVQLESVKDKGFYVFHDAYGYFNHAYGLKQIGYFTINPLVAPGAKTLAKIKEEIAEHKVSCLFAEPQFTPKMIESLSKGAQVNVGRLDPMSDSVKMEGNPYAAFLQFTADSYMQCLAK","2055328","[FUNCTION] Involved in the high-affinity zinc uptake transport system (by similarity). ","high-affinity zinc uptake system periplasmic binding protein","Periplasm","","
InterPro
IPR006127
Family
Periplasmic solute binding protein
PF01297\"[11-336]TSBP_bac_9
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1980\"[15-208]T\"[225-331]Tno description
signalp\"[1-24]?signal-peptide
tmhmm\"[10-30]?transmembrane_regions


","BeTs to 19 clades of COG0803COG name: ABC-type Mn/Zn transport system, periplasmic Mn/Zn-binding (lipo)protein (surface adhesin A)Functional Class: PThe phylogenetic pattern of COG0803 is aom-kz-qvdrlbcefgh-nujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 8.1e-07) to 2/3 blocks of the PR00334 family, which is described as \"HMW kininogen signature\". Prints database entry for PR:PR00334. PR00334B 117-140 0.0054 PR00334C 144-166 0.066 PR00334B 115-138 0.15 PR00334B 128-151 0.22 PR00334B 137-160 0.71 PR00334B 132-155 0.94 PR00334C 146-168 0.23","Residues 210 to 316 match (5e-07) PD:PD404478 which is described as ABC PROTEOME METAL COMPLETE BINDING SUBSTRATE TRANSPORTER ","","","","","","","","","","","Tue Jan 21 11:03:15 2003","Tue Jan 21 11:03:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02935 is paralogously related to AA02549 (2e-14).","","","","","","Residues 11 to 336 (E-value = 9.2e-37) place AA02935 in the SBP_bac_9 family which is described as Periplasmic solute binding protein family (PF01297)","","","","","Patzer,S.I. and Hantke,K. The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli. Mol. Microbiol. 28 (6): 1199-1210 (1998) [PubMed: 9680209].Lewis,D.A., Klesney-Tait,J., Lumbley,S.R., Ward,C.K., Latimer,J.L.,Ison,C.A. and Hansen,E.J. Identification of the znuA-encoded periplasmic zinc transport protein of Haemophilus ducreyi Infect. Immun. 67 (10), 5060-5068 (1999) PubMed: 10496878 Lu,D., Boyd,B. and Lingwood,C.A. Identification of the key protein for zinc uptake in Hemophilus influenzae J. Biol. Chem. 272 (46), 29033-29038 (1997) PubMed: 9360976 Lu,D., Boyd,B. and Lingwood,C.A. The expression and characterization of a putative adhesin B from H. influenzae FEMS Microbiol. Lett. 165 (1), 129-137 (1998) PubMed: 9711849 ","","Tue Jan 21 11:03:15 2003","1","","","" "AA02936","2055750","2056433","684","ATGCAGGAATCCGGTGAATATGATGCGCTGGCTTATCAGGCATTTAACACGGCGAAAGTCGCATTTGATCATGCTAAAGTACAAAAAGGCAAGAAAAAAGCCGTAGTTGTGGACTTAGATGAAACCATGATCGATAACAGCGCATACGCCGGCTGGCAGATAAAAAATAACAAACCTTTTGACGGTAAAGACTGGACCCGTTGGGTCGATGCGAGAGAATCCGGAGCCATTGCCGGTGCAGTAGAATTTAACAATTATGTCAATTCTCATAAAGGCAAAATGTTCTATGTGTCAAATCGCAAAGACAGTAATGAAAAAGCAGGTACCATTGATGACATGAAACGTTTAGGCTTTACCGGTGTTGATGAATCATCCCTTTATCTGAAAAAAGATAAATCCGCCAAATCTGCCCGTTTTGCAGAAATTGAAAGTCAAGGCTATGACATCGTGCTTTATGTAGGCGACAACCTGGATGATTTCGGTGATGCAACACACGGTAAATTAAATGCGGATCGTCGAGACTTTGTTGCTAAAAACCAGGCGAAATTCGGTAAAACTTATATCGTTTTACCTAATCCGAATTACGGTGGTTGGGAAGGCGGTTTAGCCAAAGACTACTTTAAAGGTGATTCCCAAAGCAAAGTTGATGCCCGCTTAAATGTAATTAAGGCATGGAGTGGAAAA","","","29835","MQESGEYDALAYQAFNTAKVAFDHAKVQKGKKKAVVVDLDETMIDNSAYAGWQIKNNKPFDGKDWTRWVDARESGAIAGAVEFNNYVNSHKGKMFYVSNRKDSNEKAGTIDDMKRLGFTGVDESSLYLKKDKSAKSARFAEIESQGYDIVLYVGDNLDDFGDATHGKLNADRRDFVAKNQAKFGKTYIVLPNPNYGGWEGGLAKDYFKGDSQSKVDARLNVIKAWSGK","2056268","","lipoprotein E precursor; outer membrane protein P4 precursor; acid phosphatase","Periplasm, Outer membrane","","
InterPro
IPR005519
Family
Acid phosphatase (Class B)
PF03767\"[4-198]TAcid_phosphat_B
InterPro
IPR006423
Family
5-nucleotidase lipoprotein e(P4)
PIRSF019271\"[1-228]TAcid phosphatase, class C
TIGR01533\"[1-225]Tlipo_e_P4: 5'-nucleotidase, lipoprotein e(P


","BeTs to 4 clades of COG2503COG name: Predicted secreted acid phosphataseFunctional Class: NThe phylogenetic pattern of COG2503 is -----------l-----h--u----wNumber of proteins in this genome belonging to this COG is","","Residues 128 to 228 match (2e-34) PD:PD510927 which is described as COMPLETE PROTEOME PRECURSOR SIGNAL ACID PHOSPHATASE HYDROLASE OUTER P4 MEMBRANE ","","","","","","","","","","","","Tue Jan 21 10:58:46 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02936 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 198 (E-value = 6.2e-72) place AA02936 in the Acid_phosphat_B family which is described as HAD superfamily, subfamily IIIB (Acid phosphatase) (PF03767)","","","","","Green,B.A., Farley,J.E., Quinn-Dey,T., Deich,R.A. and Zlotnick,G.W. The e (P4) outer membrane protein of Haemophilus influenzae: biologic activity of anti-e serum and cloning and sequencing of the structural gene Infect. Immun. 59 (9), 3191-3198 (1991) PubMed: 1715322 ","","Tue Jan 21 10:58:46 2003","1","","","" "AA02937","2057007","2056519","489","ATGCCATCATTCGACATTGTTTCCGAAATCAGCGGACACGAAATCCGCAACGCCGTGGAAAACGCCAATCGCGAGCTGACCAACCGCTGGGACTTCCGCAACGTACAAGCCGCCATTGAATTTAATGAAAAAAACGAAACCATCAAAGTCAGCAGCGAATCGGATTTCCAGGTGGAACAACTTATCGATATTCTGCGTAACGCCTGCATTAAGCGCAACATTGAATCCAACTCCCTGGACATTCCCGCCGAATATGAACACAGCGGCAAAACCTACAGCAAAGAAATCAAGCTGAAACAGGGGATTGAAAGCGATATGGCGAAGAAAATAACCAAGTTAATCAAAGAGTCCAAAATCAAAGTCCAAAGCCAAATTCAAGGCGAACAAGTGCGCGTTACCGGCAAATCCCGTGACGATTTACAAGCGGTAATTCAACTGGTCAAAACCGCCGAACTGGGACAACCGTTCCAATTTAACAATTTCCGCGAT","","","18683","MPSFDIVSEISGHEIRNAVENANRELTNRWDFRNVQAAIEFNEKNETIKVSSESDFQVEQLIDILRNACIKRNIESNSLDIPAEYEHSGKTYSKEIKLKQGIESDMAKKITKLIKESKIKVQSQIQGEQVRVTGKSRDDLQAVIQLVKTAELGQPFQFNNFRD","2056354","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR007551
Family
Protein of unknown function DUF520
PF04461\"[1-162]TDUF520
noIPR
unintegrated
unintegrated
PD016517\"[14-162]TYG56_PASMU_Q9CKG2;
G3DSA:3.30.70.860\"[93-163]Tno description


","No hits to the COGs database.","","Residues 1 to 163 match (2e-69) PD:PD016517 which is described as PROTEOME COMPLETE HI1034 PA4395 YPO3170 CYTOPLASMIC RSC2549 ALL4662 BH2387 STY0474 ","","","","","","","","","","","","Tue Jan 21 10:55:01 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02937 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 162 (E-value = 7.2e-110) place AA02937 in the DUF520 family which is described as Protein of unknown function (DUF520) (PF04461)","","","","","","","","1","","","" "AA02939","2057962","2057021","942","ATGCAAACACAAAATCTGACCGCCATTATCGAACACTTTTCATCACTGCCCGCGCCGTTCATTGCCGATCAGCCTTATGAAACCACACAGGCGTTTATTCTCTATTCCGACAACGTAAACCTCACAAAGTTACAGGCTTTTCAGCAAAAGTGCGGTGAAAATTTTCTGTGTTTTGCGGCGTGGAATGTGTTGCATAACACCGTGGTGCTGCTCAAAGGCACATGGCGGGCAGAATGGGTGAATATCGCCCATGAATTGAAACTGGATATTGCGCCCTTAAACTTTCACGCGAGCCTGAGCCAAGCGGGACTATTGGTAATGGACATGGATTCCACCGCCATTCAAATTGAATGTATCGATGAAATCGCCAAACTTGCCGGCACCGGTGAGATGGTTTCCGCCATCACTGAGCGGGCCATGCGCGGTGAATTGGATTTCAGCCAAAGCCTGCGCCAACGGGTCGCCACCTTGAAAGATGCGCCGGAAGGCATTTTGCAGGAAGTGAAAAAACATCTGCCGCTCATGCCCGGCTTGACGGAAACGGTCAAAACATTAAAAGATCACGGCTGGAAAGTGGCGATTGCGTCAGGCGGCTTCACTTATTTCGCCGAAGTGTTACAGCAACAGCTCGGCTTGGATTTCATCGCTGCCAACCAATTTGAAATCATCGACGGCAAACTTACCGGCAACGTACAAGGTGCCATTGTAGACGCACAATACAAAGCGCAAATCTTACAACAACTTGCGCAACAATTTCACATTGCCGCCGAAAACACCGTTGCCATCGGCGACGGCGCCAACGATCTTGCCATGATGCAGGTCGCCGATTTGGGCGTTGCCTATCATGCCAAACCGAAAGTGCAACAATTAGCGCAAGTTATCATCAATTTCACCGATTTAACCGCACTTTTATGTATTTTAAGTGCTAACGACAAAATCAAA","","","35869","MQTQNLTAIIEHFSSLPAPFIADQPYETTQAFILYSDNVNLTKLQAFQQKCGENFLCFAAWNVLHNTVVLLKGTWRAEWVNIAHELKLDIAPLNFHASLSQAGLLVMDMDSTAIQIECIDEIAKLAGTGEMVSAITERAMRGELDFSQSLRQRVATLKDAPEGILQEVKKHLPLMPGLTETVKTLKDHGWKVAIASGGFTYFAEVLQQQLGLDFIAANQFEIIDGKLTGNVQGAIVDAQYKAQILQQLAQQFHIAAENTVAIGDGANDLAMMQVADLGVAYHAKPKVQQLAQVIINFTDLTALLCILSANDKIK","2056856","","phosphoserine phosphatase","Cytoplasm","","
InterPro
IPR004469
Domain
Phosphoserine phosphatase SerB
TIGR00338\"[89-307]TserB: phosphoserine phosphatase SerB
InterPro
IPR005834
Domain
Haloacid dehalogenase-like hydrolase
PF00702\"[102-285]THydrolase
InterPro
IPR006383
Domain
HAD-superfamily hydrolase, subfamily IB, PSPase-like
TIGR01488\"[104-275]THAD-SF-IB: HAD-superfamily hydrolase, subfa
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1000\"[159-308]Tno description
PTHR10000\"[76-311]TPHOSPHOSERINE PHOSPHATASE


","No hits to the COGs database.","Significant hit ( 4.3e-06) to 3/3 blocks of the IPB000150 family, which is described as \"Cof protein\". Interpro entry for IP:IPR000150. IPB000150A 101-115 1.5e+02 IPB000150B 189-198 1.6e+02 IPB000150C 260-292 6.6e-05","Residues 1 to 103 match (2e-25) PD:PD095689 which is described as COMPLETE PROTEOME SERB PSP PHOSPHOSERINE SERINE O-PHOSPHOSERINE PHOSPHATASE PSPASE BIOSYNTHESIS ","","","","","","","","","","","","Tue Jan 21 10:53:46 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02939 is paralogously related to AA00482 (3e-04).","","","","","","Residues 102 to 285 (E-value = 4.3e-27) place AA02939 in the Hydrolase family which is described as haloacid dehalogenase-like hydrolase (PF00702)","","","","","Neuwald,A.F. and Stauffer,G.V. DNA sequence and characterization of the Escherichia coli serB gene . Nucleic Acids Res. 13 (19): 7025-7039 (1985) [PubMed: 2997734].","","Tue Jan 21 10:53:46 2003","1","","","" "AA02940","2058062","2058712","651","ATGAAGTTTATGATGTTCTTCGGCATCGTGTTGTTATGTGTGGGGATCATGGCGATCATTTTGTTCGGGGTTAAACAATTTAAAATCGGTTCACAACTTGCCAGCGTCAATCAGGTGGCAAATTTGTCTCATTTGCTGGTGCGCCAGCAAGCCAATCTATTTTCTATGTTATTGATGAATAACGCGAAAACTGAACGTTTGGTGGAGAATCTGGATAATTTCGCCAAAGAAGAATTTGTGCTTGATGCCGCCGTGTATGCGCGCAACGGCGAGTTATTGGCGCAAAGCACCAATTCGTCCGATATGCGCAGTTTATTGGGGCTGGATAAAAAAGAAGAAAATGAAAAGGATTCCCAGCAAATTGTGGAACCCATTTATTCGCCGAACGGCGTGGAAGGTTTTCTGCGCGTGACCTTTGATGCCAAATACGGACAAACCACGCAAAGCAAAATCAATCATATTTTTCATCGTTTATACGGCGAGATTATTATCGTCTTCCTTGCCGGGATCCTGCTTGCCAGCAGCCTGCATTATTTCCTCAGCCATTATCGACGTAGCCGTATTCATGTGGTGGAAAAAACACCGGTATTGCGCAACAAAATTACGCAATCTATGAGTAAGTTGTTTCATCAGCGACGCAGAAGGGTGAAA","","","25882","MKFMMFFGIVLLCVGIMAIILFGVKQFKIGSQLASVNQVANLSHLLVRQQANLFSMLLMNNAKTERLVENLDNFAKEEFVLDAAVYARNGELLAQSTNSSDMRSLLGLDKKEENEKDSQQIVEPIYSPNGVEGFLRVTFDAKYGQTTQSKINHIFHRLYGEIIIVFLAGILLASSLHYFLSHYRRSRIHVVEKTPVLRNKITQSMSKLFHQRRRRVK","2058547","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
PD111923\"[9-171]TAHPA_PASMU_Q9L8J3;
signalp\"[1-18]?signal-peptide
tmhmm\"[5-23]?\"[162-180]?transmembrane_regions


","BeTs to 3 clades of COG3726COG name: Uncharacterized membrane protein affecting hemolysin expressionFunctional Class: TThe phylogenetic pattern of COG3726 is --------------efgh--------Number of proteins in this genome belonging to this COG is","","Residues 40 to 107 match (9e-07) PD:PD009618 which is described as PROTEOME COMPLETE FILAMENTATION CELL PLASMID NMA0004 HI0977 MOBILIZATION FIC-RELATED CAMP-INDUCED ","","","","","","","","","","","","Tue Jan 21 10:50:28 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02940 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02941","2058791","2058675","117","TTGGGCGGTTTTTTGTTTTTATCAATTGTGTTTATTTCCGATGAAAAAACGCCGGGAAAAACCACCGCACTTTTCCCTATTTCACCCTTCTGCGTCGCTGATGAAACAACTTACTCA","","","4196","LGGFLFLSIVFISDEKTPGKTTALFPISPFCVADETTYS","2058675","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 10:49:48 2004","Mon Feb 23 10:49:48 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02941 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 10:50:45 2004","","","","","","","","","","","","","1","","","" "AA02944","2059088","2058828","261","TTGGCTAATATCAAGTCAGCAAAAAAACGTGCGGTTCAATCTGAAAAACGCCGTCAACACAACGCAAGCCAACGCTCTATGATGCGTACTTACATCAAAAAAGTTTATGCACAAGTTGCCGCAGGCGAGAAAGCAGCTGCTGAAGCCGCATTCGTTGAAATGCAAAAAGTTGTGGACAGAATGGCATCTAAAGGTTTAATCCACGCGAACAAAGCAGCCAACCACAAATCTAAATTAGCTGCACAAATCAAAAAATTAGCA","","","9802","LANIKSAKKRAVQSEKRRQHNASQRSMMRTYIKKVYAQVAAGEKAAAEAAFVEMQKVVDRMASKGLIHANKAANHKSKLAAQIKKLA","2058663","[FUNCTION] Binds directly to 16S ribosomal RNA (By similarity).","30S ribosomal protein S20","Periplasm, Cytoplasm","","
InterPro
IPR002583
Family
Ribosomal protein S20
PD004231\"[13-86]TRS20_VIBVU_Q8DES4;
G3DSA:1.20.58.110\"[5-86]Tno description
PF01649\"[2-85]TRibosomal_S20p
TIGR00029\"[1-87]TS20: ribosomal protein S20


","BeTs to 18 clades of COG0268COG name: Ribosomal protein S20Functional Class: JThe phylogenetic pattern of COG0268 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.5e-38) to 2/2 blocks of the IPB002583 family, which is described as \"Ribosomal protein S20\". Interpro entry for IP:IPR002583. IPB002583A 1-34 1.4e-24 IPB002583B 58-79 1.2e-12","Residues 5 to 86 match (5e-11) PD:PD004231 which is described as RIBOSOMAL S20 30S RRNA-BINDING COMPLETE PROTEOME CHLOROPLAST CYANELLE AT3G15190/F4B12_10 RNA-BINDING ","","","","","","","","","","","Tue Jan 21 10:48:44 2003","Tue Jan 21 10:48:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02944 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 85 (E-value = 6.2e-47) place AA02944 in the Ribosomal_S20p family which is described as Ribosomal protein S20 (PF01649)","","","","","Mackie,G.A. 1981. Nucleotide sequence of the gene for ribosomal protein S20 and its flanking regions. J. Biol. Chem. 256(15): 8177-8182. PubMed: 6267039. Wittmann-Liebold,B., Marzinzig,E. and Lehmann,A. 1976.Primary structure of protein S20 from the small ribosomal subunit of Escherichia coli. FEBS Lett. 68(1): 110-114. PubMed: 786731.Mackie,G.A. Structure of the DNA distal to the gene for ribosomal protein S20 in Escherichia coli K12: presence of a strong terminator and an IS1element. Nucleic Acids Res. 14 (17): 6965-6981 (1986) [PubMed: 2429258].Arnold,R.J. and Reilly,J.P. Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry. Anal. Biochem. 269 (1): 105-112 (1999) [PubMed: 10094780].Tung,C.S., Joseph,S. and Sanbonmatsu,K.Y. All-atom homology model of the Escherichia coli 30S ribosomal subunit. Nat. Struct. Biol. 9 (10): 750-755 (2002) [PubMed: 12244297].","","Tue Jan 21 10:48:44 2003","1","","","" "AA02946","2059356","2060930","1575","TTGAGTAAAAGATTATTAAAATCCGGCATCGTCGTCAGCGCCATGACCTTAATTTCGCGTGTATTAGGCTTGGTGCGTGATGTGGTGATTGCCAATTTAATCGGCGCAGGCGCTGCCGCCGACGTATTTTTATTTGCCAATCGCATTCCGAATTTCCTCCGCCGCTTGTTTGCCGAAGGGGCGTTTTCACAAGCCTTCGTGCCTGTGTTGGCGGAATATCAGAAATCCGGCGATTTATCCAAAACCCGCGAATTTATCGGCAAGGTTTCCGGTACTTTGGGTGGGTTGGTTACCATCGTCACTTTGCTGGCGATGATCGGATCGCCCGTCGTGGCGGCGATTTTCGGGACGGGCTGGTTTGTGGATTGGCTTAATGACGGCCCTAACGCGGAAAAATTCACCCAAGCCTCGTTGTTGCTCAAAATCACCTTCCCTTATTTATGGTTCGTGACCTTTGTGGCGCTGTCCGGCGCGATTTTAAACACCCTCGGTAAGTTCGGCGTCATGTCCTTTTCGCCTGTGCTGCTCAATGTGGCGATGATTGCTACCGCACTTTGGTTGGCGCCGCAGCTGAAAAATCCTGATTTAGGCTTGGCAATCGGGATCTTTCTCGGCGGCTTGTTGCAATTTCTGTTCCAACTGCCGTTCTTATATAAAGCCAAATTATTGGTGAAGCCAAAGTGGGCATGGCATGACGAAGGCGTGAAGAAAATTCGCACATTGATGATCCCTGCGTTGTTCGGCGTGTCGGTCAGCCAACTCAACTTGTTACTGGATACTTTCATCGCCAGTTTCTTAATGACCGGTTCCATCAGCTGGCTTTATTATTCTGATCGCTTGCTGGAGTTTCCGCTCGGCTTGTTCGGTATCGCCATTTCCACGGTCATTTTACCAACCCTCGCCCGCCACCATGTGAACCGCGACGATAACGTCAAAAGTGCGGTAGATTTTTGCAACACAATGGACTGGGGCGTGCGCATGATTTTGCTGCTCGGCGTGCCGGCAATGATTGGCATCGCCGTGTTAGCACAGCCCATGTTGCTCGTGCTGTTCATGCGCGGCAGCTTTAATTTCAGCGATGTACAGGCGGCATCCTATTCTCTCTGGGGCTTTAATGCGGGGTTACTGAGCTTCATGTTAATCAAGATTTTGGCGAACGGTTACTACGCCCGCCAAGACACCAAAACGCCGGTGAAGATCGGTATCATTGCCATGGTGAGCAACATGGCGTTCAACCTGCTTGCGATTCCTTTCAGTTATGTGGGCTTGGCGATTGCCTCCGCCATGTCGGCGACACTCAACGCGTTTCTGCTTTATCGCGGCTTGGCGAAAGCCGATGTGTATCATTTCAGCCGACAAAGTGCGGTCTTTTTTCTGAAAGTTTTGTTTGCCGCCGTCATCATGGGATTGTTGGTTTGGTACAACAGCCCAAGCCTGACGGAATGGAACGATATGCGCTTTCTCACCCGTGTACATTGGCTGACGTGGCTCATCGTGTTGGCAGCGATGGTTTACGGTGGCATGTTGGTGCTGTTGGGGATTCGCAAACGTGATTTGACGGGCGCGCACTCCGCG","","","57570","LSKRLLKSGIVVSAMTLISRVLGLVRDVVIANLIGAGAAADVFLFANRIPNFLRRLFAEGAFSQAFVPVLAEYQKSGDLSKTREFIGKVSGTLGGLVTIVTLLAMIGSPVVAAIFGTGWFVDWLNDGPNAEKFTQASLLLKITFPYLWFVTFVALSGAILNTLGKFGVMSFSPVLLNVAMIATALWLAPQLKNPDLGLAIGIFLGGLLQFLFQLPFLYKAKLLVKPKWAWHDEGVKKIRTLMIPALFGVSVSQLNLLLDTFIASFLMTGSISWLYYSDRLLEFPLGLFGIAISTVILPTLARHHVNRDDNVKSAVDFCNTMDWGVRMILLLGVPAMIGIAVLAQPMLLVLFMRGSFNFSDVQAASYSLWGFNAGLLSFMLIKILANGYYARQDTKTPVKIGIIAMVSNMAFNLLAIPFSYVGLAIASAMSATLNAFLLYRGLAKADVYHFSRQSAVFFLKVLFAAVIMGLLVWYNSPSLTEWNDMRFLTRVHWLTWLIVLAAMVYGGMLVLLGIRKRDLTGAHSA","2060765","","virulence factor protein","Inner membrane, Cytoplasm","","
InterPro
IPR004268
Family
Virulence factor MVIN-like
PR01806\"[35-54]T\"[54-70]T\"[142-166]T\"[166-187]T\"[268-294]T\"[371-390]T\"[422-439]TVIRFACTRMVIN
PF03023\"[30-494]TMVIN
TIGR01695\"[4-522]TmviN: integral membrane protein MviN
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[117-282]Tno description
noIPR
unintegrated
unintegrated
signalp\"[1-23]?signal-peptide
tmhmm\"[5-20]?\"[26-46]?\"[89-123]?\"[142-162]?\"[171-191]?\"[197-219]?\"[240-274]?\"[280-300]?\"[327-347]?\"[366-386]?\"[396-411]?\"[417-439]?\"[454-474]?\"[493-513]?transmembrane_regions


","No hits to the COGs database.","","Residues 442 to 516 match (1e-18) PD:PD276887 which is described as COMPLETE PROTEOME VIRULENCE FACTOR MVIN TRANSMEMBRANE HOMOLOG MEMBRANE PA4562 INNER ","","","","","","","","","","","","Tue Jan 21 10:39:21 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02946 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 30 to 494 (E-value = 2.7e-192) place AA02946 in the MVIN family which is described as MviN-like protein (PF03023)","","","","","Rudnick PA, Arcondeguy T, Kennedy CK, Kahn D. glnD and mviN are genes of an essential operon in Sinorhizobium meliloti. J Bacteriol. 2001 Apr;183(8):2682-5. PMID: 11274131","","Tue Jan 28 13:42:29 2003","1","","","" "AA02947","2061011","2061934","924","ATGCAGCTGATTCGAGGCCTGGGAAATTTACCGCAAAATTTGCACGCTTGCGCGTTAACCATCGGTAATTTTGATGGCGTGCATCTGGGGCATCAAGCTATTTTGCGTCATTTGCGGGAAAAAGCCGACGAATTGCATTTGCCCATGGTGGTGATGCTGTTTGAACCGCAGCCGCGTGAATATTTTTGCGGTGAAGATGCGCCGGCGCGTTTAATGCACTTGCGCGATAAATTGCATTATCTTGAACAGGCGGGCGTGGACATCGTTATCGTAGCGAAATTCGACCGCACTTTTGCCGCATTGCCGGCGCAGCAATTTATCGAAGATTGGCTGGTGCGCAAATTAAAGGTGAAATTTTTAAGTATCGGCGATGATTTTAAATTTGGCGCCAAACGCCAAGGGAATTTCGCGATGTTACAACAAGCCGGCGAACAATTCGGTTTTACGGTGGAAGATAACCGCAGCTTTTGCCTGGATGAACTGCGTATCAGCAGCACTGCAATTCGCCTTGCGTTGGCGAACGATGATTTACCGCTGGCGGAAAAATTGCTCGGGCATCCATACCGCATTTTAGGACGCGTAATTCACGGTAATGAATTGGGTCGCACCATCGGCTTCCCGACGGCGAATATTCGCCTGCATCGTCAGGTGAACCCGGTGAAAGGGGTTTATGCCGTTAAAGTGCGGTTAAAATCCGGCGCGTTTTTTAACGGTGTGGCAAACATCGGCACCCGCCCGACCATCAACGGCGTGAATCAATTATTAGAAGCCCATTTATTTGATTTTCAAGGTGATCTTTACGGGCAATGGCTGGAAGTGGAACTGTGCCATAAAATCCGTAATGAAATGAAATTTCCGTCTTTTGACACACTAAAAGCGCAAATCGCGCAGGATGTGGAGACGGCGAAAAAGGTTTTTGAAGCG","","","34795","MQLIRGLGNLPQNLHACALTIGNFDGVHLGHQAILRHLREKADELHLPMVVMLFEPQPREYFCGEDAPARLMHLRDKLHYLEQAGVDIVIVAKFDRTFAALPAQQFIEDWLVRKLKVKFLSIGDDFKFGAKRQGNFAMLQQAGEQFGFTVEDNRSFCLDELRISSTAIRLALANDDLPLAEKLLGHPYRILGRVIHGNELGRTIGFPTANIRLHRQVNPVKGVYAVKVRLKSGAFFNGVANIGTRPTINGVNQLLEAHLFDFQGDLYGQWLEVELCHKIRNEMKFPSFDTLKAQIAQDVETAKKVFEA","2061769","[CATALYTIC ACTIVITY] ATP + riboflavin = ADP + FMN.[CATALYTIC ACTIVITY] ATP + FMN = diphosphate + FAD.","riboflavin biosynthesis protein","Cytoplasm","","
InterPro
IPR002345
Domain
Lipocalin
PS00213\"[261-273]?LIPOCALIN
InterPro
IPR002606
Family
Riboflavin kinase / FAD synthetase
PD003662\"[187-306]TRIBF_HAEIN_P44957;
PF01687\"[183-307]TFlavokinase
PF06574\"[15-167]TFAD_syn
TIGR00083\"[18-307]TribF: riboflavin biosynthesis protein RibF
InterPro
IPR004821
Domain
Cytidyltransferase-related
TIGR00125\"[17-83]Tcyt_tran_rel: cytidyltransferase-related do
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620\"[17-186]Tno description
noIPR
unintegrated
unintegrated
G3DSA:2.40.30.30\"[188-306]Tno description
PTHR22749\"[184-308]TRIBOFLAVIN KINASE/FMN ADENYLYLTRANSFERASE


","BeTs to 18 clades of COG0196COG name: FAD synthaseFunctional Class: HThe phylogenetic pattern of COG0196 is ------yqvdrlbcefghsnuj-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.5e-80) to 7/7 blocks of the IPB002606 family, which is described as \"Riboflavin kinase / FAD synthetase\". Interpro entry for IP:IPR002606. IPB002606A 22-31 4.3e-07 IPB002606B 54-68 2.1e-05 IPB002606C 115-129 8.8e-06 IPB002606D 192-213 1.9e-14 IPB002606E 221-228 0.087 IPB002606F 238-250 4e-07 IPB002606G 256-298 6.1e-30","Residues 19 to 107 match (6e-18) PD:PD175372 which is described as RIBOFLAVIN COMPLETE PROTEOME TRANSFERASE KINASE ADENYLYLTRANSFERASE KINASE/FMN NUCLEOTIDYLTRANSFERASE RIBF BIOSYNTHESIS ","","","","","","","","","","","Tue Jan 21 10:36:00 2003","Tue Jan 21 10:36:00 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02947 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 183 to 307 (E-value = 2.2e-69) place AA02947 in the FAD_Synth family which is described as Riboflavin kinase / FAD synthetase (PF01687)","","","","","Kamio,Y., Lin,C.K., Regue,M. and Wu,H.C. Characterization of the ileS-lsp operon in Escherichia coli. Identification of an open reading frame upstream of the ileS geneand potential promoter(s) for the ileS-lsp operon. J. Biol. Chem. 260 (9): 5616-5620 (1985) [PubMed: 2985604].","","Tue Jan 21 10:36:00 2003","1","","","" "AA02949","2062302","2062084","219","GTGGGTTATGTGTTACATCACCCCGACCGGCAAGTAATCCATCAATTGAAATATCTTCATCCAATGCATCCCAGTGAATGCCACGACGACTTAATTCATAATTTTCCAATTCCGTTTTTGTCGCCCGCAGCAATTTTGGAAACCAAACCAAAGGAATGCCTAAAATACGCGCATCATCAAGCTCAACCTACATTCTGTTTTCATCAAAACGTACATGTT","","","8534","VGYVLHHPDRQVIHQLKYLHPMHPSECHDDLIHNFPIPFLSPAAILETKPKECLKYAHHQAQPTFCFHQNVHV","2062084","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 10:46:41 2004","Mon Feb 23 10:46:41 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02949 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 10:47:24 2004","","","","","","","","","","","","","1","","","" "AA02950","2062435","2065173","2739","ATGTTGAAAAATTGGTATGAGAAAGATCTTTACCAAAAAATCCGTCAGGCGACCAAAGGCAAGAAATCCTTTATTTTGCACGACGGTCCTCCTTATGCCAACGGCACCATTCATATCGGTCATGCGGTGAATAAAATTCTTAAAGATATTATCGTGAAATCCAAAACCGCACTTGGGTTTGATTCCCCTTATATTCCGGGTTGGGACTGCCATGGCTTGCCGATTGAACTGAAAGTGGAAGGCTTGGTGGGCAAACCGAACGAGAAAATTTCAGCGGCGGAATTCCGCCAAAAATGCCGTGAATATGCGGCGGAACAGGTGGAAGGTCAGAAAAAAGACTTCGTGCGCCTCGGTGTGTTGGGCGATTGGGATAATCCGTACCTCACCATGAATTTCAACACCGAAGCCAACATTATTCGCACTTTGGGCAAAGTGATCGCCAACGGGCATTTATATAAAGGCTCCAAACCGGTGCATTGGTGTTTGGATTGTGGCTCCTCTTTGGCGGAAGCGGAAGTGGAATATGAAGACCGTGTGTCGCCGTCCATTTATGTACGTTTCCCGGCAGAAAGTGCGGTGGAAATTGAAGGTAAATTTAACGCCGTTGGCAAAGGCAGCGGCAAGTTGTCCGCCGTGATTTGGACCACAACCCCTTGGACCATGCCGTCCAACCGTGCTATTTCCGTGAATGCCGAGCTGGAATATCAGCTTGTGCAATTAGGCGACGAGCGCGTGATTTTAGCTGCCGATTTGGTGGAAGACATGGTGAAGGCGGTTGGCGTGGAAAAGGTGGAAATCTTAGGTTCCGCAAAAGGTAAAGATCTTGAGTTATTCCGCTTCCATCATCCGTTTTACAATTTCACCGTGCCGATTATTTTAGGCGATCATGTGACTACCGACGGTGGTACCGGTTTGGTACATACCGCGCCGAATCACGGTTTGGACGACTTTATCGTGGGTAAACAATATGACTTGCCGATGGCAGGCTTGGTAACGAATGACGGTAAATTTATTTCTTCCACCGAATTTTTTGCCGGCAAAGGCGTGTTTGAAGCCAATCCGTTAGTGATCGAAAAATTGCAAGAAACGGGTAACTTGTTGAAATTAGACAAGATTAAACACAGCTACCCACACTGCTGGCGTCATAAAACCCCGATTATTTTCCGCGCCACACCGCAATGGTTTATCGGCATGGAAGTGCAAGGTTTGCGTCCGCAAGCGCTTGGCGAAATCAAACAAGTGCGTTGGATCCCCGATTGGGGGCAGGCGCGTATTGAAAAAATGGTGGAAAATCGCCCTGACTGGTGTATTTCCCGTCAGCGTACCTGGGGCGTGCCGATGACCTTATTCGTGCACAAAGAAACCGAAGAGTTACACCCGCGCACCCTTGAATTGCTGGAAGAAGTGGCAAAACGCGTAGAAAAAGCCGGGATTCAGGCATGGTGGGATTTGGACGAAAAAGAACTGCTCGGTGCCGACGCGGAAACCTATCGTAAAGTGCCGGACACCCTTGATGTGTGGTTTGATTCCGGATCCACCTATTCTTCCGTAGTGGCGAATCGCCCTGAATTTGAAGGCAAAGCGGCGGATATGTATTTGGAAGGTTCCGACCAACATCGCGGCTGGTTTATGTCCTCATTAATGCTTTCCACCGCCACGGACAACAAAGCGCCTTATAAACAAGTGCTTACCCATGGTTTCACTGTGGACGGTCAAGGGCGCAAGATGTCGAAATCCATCGGCAATGTGGTGACCCCGCAAGAAGTGATGGATAAATTCGGCGGTGATATTTTGCGTTTGTGGGTGGCATCCACCGATTACACCGGCGAAATGACGGTTTCCGATGAAATCTTAAAACGTGCGGCGGACAGTTATCGTCGTATTCGTAACACGGCGCGTTTCCTGTTGGCGAACTTAAACGGCTTCGACCCGCAACGTGATGCGGTGAAACCGGAGGAAATGATTAGCCTGGATCGTTGGGCGGTGGCTTGTGCGTTAGAGGCGCAAAACGAAATCAAAGACGCCTACGATAACTATCAATTCCACGCCGTCGTGCAACGCTTAATGCGCTTCTGTTCCGTGGAAATGGGTTCTTTCTACCTTGATATTATCAAAGACCGCCAATACACCACCAAAGCGGACAGCCTCGCCCGTCGCAGCTGCCAAACCGCCTTGTGGCACATTGCGGAAGCCTTGGTTCGTTGGATGGCGCCGATTTTATCCTTCACGGCGGATGAAATCTGGGGCCACTTGCCGAAAACCACCGCACCGCGCGCCGAATTCGTGTTTACCGAAGAATTTTACGAAGGCTTATTCAGCTTAGGTGAAAACGAAAAATTAGACGACGCTTATTGGCAAACCTTGATTAAAGTGCGTTCCGAAGTAAACCGCGTGTTGGAAATCGCCCGTAACGATAAAGTGATCGGCGCCGGTTTGGAAGCGGAAGTGACCGTTTACACCAACGACGAATATCGTGCGTTATTGGAAAAACTCGGCGACGAACTCCGTTTCGTGTTGATTACCTCTAAAGCGGAAGTCAAACCATTGACAGACAAACCTGCCGATGTGGCGGAGGGCGAGTTGGAAGGCATCGCCGTGAGCATCGCCCGTTCCAACGGCGGGAAATGCCCGCGTTGCTGGCATTATTCCGACAAAATCGGCGTCAACCCGCAACATCCGAGCCTTTGTCCGCGTTGCGTGGAAAACGTGGCAGGTAACGGCGAAATCCGACATTTCGCT","","","106007","MLKNWYEKDLYQKIRQATKGKKSFILHDGPPYANGTIHIGHAVNKILKDIIVKSKTALGFDSPYIPGWDCHGLPIELKVEGLVGKPNEKISAAEFRQKCREYAAEQVEGQKKDFVRLGVLGDWDNPYLTMNFNTEANIIRTLGKVIANGHLYKGSKPVHWCLDCGSSLAEAEVEYEDRVSPSIYVRFPAESAVEIEGKFNAVGKGSGKLSAVIWTTTPWTMPSNRAISVNAELEYQLVQLGDERVILAADLVEDMVKAVGVEKVEILGSAKGKDLELFRFHHPFYNFTVPIILGDHVTTDGGTGLVHTAPNHGLDDFIVGKQYDLPMAGLVTNDGKFISSTEFFAGKGVFEANPLVIEKLQETGNLLKLDKIKHSYPHCWRHKTPIIFRATPQWFIGMEVQGLRPQALGEIKQVRWIPDWGQARIEKMVENRPDWCISRQRTWGVPMTLFVHKETEELHPRTLELLEEVAKRVEKAGIQAWWDLDEKELLGADAETYRKVPDTLDVWFDSGSTYSSVVANRPEFEGKAADMYLEGSDQHRGWFMSSLMLSTATDNKAPYKQVLTHGFTVDGQGRKMSKSIGNVVTPQEVMDKFGGDILRLWVASTDYTGEMTVSDEILKRAADSYRRIRNTARFLLANLNGFDPQRDAVKPEEMISLDRWAVACALEAQNEIKDAYDNYQFHAVVQRLMRFCSVEMGSFYLDIIKDRQYTTKADSLARRSCQTALWHIAEALVRWMAPILSFTADEIWGHLPKTTAPRAEFVFTEEFYEGLFSLGENEKLDDAYWQTLIKVRSEVNRVLEIARNDKVIGAGLEAEVTVYTNDEYRALLEKLGDELRFVLITSKAEVKPLTDKPADVAEGELEGIAVSIARSNGGKCPRCWHYSDKIGVNPQHPSLCPRCVENVAGNGEIRHFA","2065008","","isoleucyl-tRNA synthetase","Cytoplasm","","
InterPro
IPR001412
Family
Aminoacyl-tRNA synthetase, class I
PS00178\"[31-42]TAA_TRNA_LIGASE_I
InterPro
IPR002300
Domain
Aminoacyl-tRNA synthetase, class Ia
PF00133\"[1-614]TtRNA-synt_1
InterPro
IPR002301
Domain
Isoleucyl-tRNA synthetase, class Ia
PR00984\"[24-35]T\"[212-235]T\"[374-389]T\"[499-512]T\"[534-543]TTRNASYNTHILE
TIGR00392\"[1-820]TileS: isoleucyl-tRNA synthetase
InterPro
IPR010663
Domain
Zinc finger, Fpg-type
PF06827\"[873-902]Tzf-FPG_IleRS
InterPro
IPR013155
Domain
tRNA synthetase, valyl/leucyl, anticodon-binding
PF08264\"[658-819]TAnticodon_1
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620\"[1-604]Tno description
noIPR
unintegrated
unintegrated
G3DSA:1.10.730.10\"[617-751]Tno description
PTHR11946\"[1-842]TISOLEUCYL, LEUCYL, TYROSYL, VALYL AND METHIONYL-TRNA SYNTHETASES
PTHR11946:SF9\"[1-842]TISOLEUCYL TRNA SYNTHETASE


","No hits to the COGs database.","Significant hit ( 5.1e-09) to 2/2 blocks of the IPB001412 family, which is described as \"Aminoacyl-transfer RNA synthetases class-I\". Interpro entry for IP:IPR001412. IPB001412A 31-41 0.0088 IPB001412B 572-582 0.00021","Residues 377 to 420 match (8e-07) PD:PD588462 which is described as SYNTHETASE LIGASE AMINOACYL-TRNA ISOLEUCYL-TRNA PROTEOME ILERS BIOSYNTHESIS COMPLETE ATP-BINDING ISOLEUCINE--TRNA ","","","","","","","","","","","","Tue Jan 21 10:30:42 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02950 is paralogously related to AA01724 (5e-37), AA01090 (3e-12) and AA00717 (1e-06).","","","","","","Residues 873 to 902 (E-value = 5.8e-14) place AA02950 in the zf-FPG_IleRS family which is described as Zinc finger found in FPG and IleRS (PF06827)","","","","","Yanagisawa,T., Lee,J.T., Wu,H.C. and Kawakami,M. Relationship of protein structure of isoleucyl-tRNA synthetase with pseudomonic acid resistance of Escherichia coli. A proposed mode of action of pseudomonic acid as an inhibitor of isoleucyl-tRNA synthetase J. Biol. Chem. 269 (39), 24304-24309 (1994) PubMed: 7929087 Kamio,Y., Lin,C.K., Regue,M. and Wu,H.C. Characterization of the ileS-lsp operon in Escherichia coli. Identification of an open reading frame upstream of the ileS gene and potential promoter(s) for the ileS-lsp operon J. Biol. Chem. 260 (9), 5616-5620 (1985) PubMed: 2985604 Webster,T., Tsai,H., Kula,M., Mackie,G.A. and Schimmel,P. Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase. Science 226 (4680): 1315-1317 (1984) PubMed: 6390679.","","Wed Jan 29 15:04:32 2003","1","","","" "AA02952","2065256","2065747","492","ATGACGAACAAACCAAAATCCGGGCTCTCATTTTTGTGGTTAAGTACGCTGGCATTTATCGCCGATATTTTTACCAAATACTTAATCGTAAGCCATTTTGAATACGGCGAAAGCGTAAATATCCTGCCGATTTTTAATTTGACCTATGTGGGTAACTTTGGCGCCGCTTTTAGTTTCCTGGCGGATCATGACGGTTGGCAAAAATTCTTTTTCCTTGCGTTGGCAGTGGGGATTTCCGCCATGTTGGTTTATTTTTTAATGAAAAATCGCCATGAACAAAAACTGCTGAATGCCGCCTACGCTTTGATTATCGGCGGCGCTTTGGGCAATGCGGCGGATCGTCTGTATCACGGCTATGTGGTGGATTTTTTAGATTTCTATTGGCGGGATTGGCATTATCCCGTGTTTAACCTGGCGGATATTGCCATTTGTGTGGGTGCCGGTTTGATTGCCTTGGATGCGTTCAAAAACGGCAATAAACAGGAATGTAAA","","","18467","MTNKPKSGLSFLWLSTLAFIADIFTKYLIVSHFEYGESVNILPIFNLTYVGNFGAAFSFLADHDGWQKFFFLALAVGISAMLVYFLMKNRHEQKLLNAAYALIIGGALGNAADRLYHGYVVDFLDFYWRDWHYPVFNLADIAICVGAGLIALDAFKNGNKQECK","2065582","[FUNCTION] This protein specifically catalyzes the removal of signal peptides from prolipoproteins. ","lipoprotein signal peptidase","Inner membrane, Cytoplasm","","
InterPro
IPR001872
Family
Peptidase A8, signal peptidase II
PD004304\"[44-160]TLSPA_HAEIN_P44975;
PR00781\"[52-60]T\"[100-115]T\"[136-152]TLIPOSIGPTASE
PF01252\"[9-161]TPeptidase_A8
TIGR00077\"[1-164]TlspA: signal peptidase II
noIPR
unintegrated
unintegrated
signalp\"[1-25]?signal-peptide
tmhmm\"[10-30]?\"[39-59]?\"[69-87]?\"[96-116]?\"[135-155]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.6e-13) to 1/1 blocks of the IPB001872 family, which is described as \"Signal peptidase II/lipoprotein signal peptidase family (A8)\". Interpro entry for IP:IPR001872. IPB001872 100-123 1.6e-13","Residues 7 to 152 match (6e-13) PD:PD444317 which is described as PEPTIDASE SIGNAL II LIPOPROTEIN COMPLETE PROTEOME SPASE PROLIPOPROTEIN PROTEASE ASPARTYL ","","","","","","","","","","","Tue Jan 21 10:24:55 2003","Tue Jan 21 10:24:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02952 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 9 to 161 (E-value = 1.3e-71) place AA02952 in the Peptidase_A8 family which is described as Signal peptidase (SPase) II (PF01252)","","","","","Cavard D. Inhibition of colicin synthesis by the antibiotic globomycin. Arch Microbiol. 1998 Dec;171(1):50-8. PMID: 9871019 Yu F, Yamada H, Daishima K, Mizushima S. Nucleotide sequence of the lspA gene, the structural gene for lipoprotein signal peptidase of Escherichia coli. FEBS Lett. 1984 Jul 23;173(1):264-8. PMID: 6378662 Yamada H, Kitagawa M, Kawakami M, Mizushima S. The gene coding for lipoprotein signal peptidase (lspA) and that for isoleucyl-tRNA synthetase (ileS) constitute a cotranscriptional unit in Escherichia coli. FEBS Lett. 1984 Jun 11;171(2):245-8. PMID: 6373377 Yamagata H, Taguchi N, Daishima K, Mizushima S. Genetic characterization of a gene for prolipoprotein signal peptidase in Escherichia coli. Mol Gen Genet. 1983;192(1-2):10-4. PMID: 6227793Innis,M.A., Tokunaga,M., Williams,M.E., Loranger,J.M., Chang,S.Y., Chang,S. and Wu,H.C. Nucleotide sequence of the Escherichia coli prolipoprotein signal peptidase (lsp) gene. Proc. Natl. Acad. Sci. U.S.A. 81 (12): 3708-3712 (1984) [PubMed: 6374664].Bouvier,J. and Stragier,P. Nucleotide sequence of the lsp-dapB interval in Escherichia coli . Nucleic Acids Res. 19 (1): 180 (1991) [PubMed: 2011499].Munoa,F.J., Miller,K.W., Beers,R., Graham,M. and Wu,H.C. Membrane topology of Escherichia coli prolipoprotein signal peptidase (signal peptidase II). J. Biol. Chem. 266 (26): 17667-17672 (1991) [PubMed: 1894646].","","Tue Jan 21 10:24:55 2003","1","","","" "AA02954","2065750","2066691","942","ATGAAAATTATTTTAGCCAACCCGCGCGGGTTCTGTGCCGGCGTGGATCGTGCTATCAGCATCGTAGAACTGGCGTTGGAAATTCACGGTGCGCCCATTTATGTGCGGCATGAAGTGGTGCATAACCGTTTCGTGGTGAACGGCTTGCGTGAGCGCGGTGCCATTTTTGTGGAAGAATTAAGCGAAGTGCCGGACGGCGCCATTGTGATTTTCTCCGCTCATGGTGTGTCCCAAGCGGTGCGTCAGGAAGCAAAAGAGCGCAATTTGAAAGTGTTCGACGCCACGTGCCCGTTGGTGACCAAAGTGCATATGCAGGTGGCGCGTGCCAGCCGTAAAGGCACCAAAGCCATTTTAATCGGGCACAAAGGGCATCCCGAAGTGGAAGGCACCATGGGGCAATACGGCAATCAAGAGGGCGGCATTTATTTAATCGAAAGTGTGGAAGACATCGCCAACTTACCGGTGAAACAAAATGACGACCTCACATTTATGACGCAAACCACCTTATCTTTGGACGACACGGCGGAAACCATCAGCGCCCTGAAAGAAAAATATCCCGCCATTCAAGGCCCGCATAAAAACGACATTTGTTATGCCACCACCAATCGACAAGAAGCCGTACGTGAACTGGCGAAACAGTCGGATTTAGTGGTCGTGGTCGGATCCAAAAACTCCTCCAATTCCAATCGTTTGGCGGAGCTTGCCTCCCGCATGGGCGTCGCTTCTAAATTAATCGATGACCCGAACGACATTCACGCAAACTGGTTCGACGGCGTGCAAACTATCGGCGTCACCGCCGGTGCTTCCGCCCCGGAAGAATTGGTACAATCGGTTATCTCCCGCCTGAAAGAATTCGGCGTCACCACCGTAGAAGAACTGCAAGGCTTGGAAGAAAATATGTTCTTTGAAGTTCCGAAAGAGTTGCGGCTGAAAGAAGCAAAT","","","34339","MKIILANPRGFCAGVDRAISIVELALEIHGAPIYVRHEVVHNRFVVNGLRERGAIFVEELSEVPDGAIVIFSAHGVSQAVRQEAKERNLKVFDATCPLVTKVHMQVARASRKGTKAILIGHKGHPEVEGTMGQYGNQEGGIYLIESVEDIANLPVKQNDDLTFMTQTTLSLDDTAETISALKEKYPAIQGPHKNDICYATTNRQEAVRELAKQSDLVVVVGSKNSSNSNRLAELASRMGVASKLIDDPNDIHANWFDGVQTIGVTAGASAPEELVQSVISRLKEFGVTTVEELQGLEENMFFEVPKELRLKEAN","2066526","[FUNCTION] Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) (By similarity). Regulates the activity of guanosine 3',5'-bispyrophosphate synthetase I (RelA)[PATHWAY] Nonmevalonate terpenoid biosynthesis pathway; seventh (last) step.","penicillin tolerance protein; hydroxymethylbutenyl pyrophosphate reductase","Cytoplasm","","
InterPro
IPR003451
Family
LytB protein
PF02401\"[3-285]TLYTB
TIGR00216\"[2-285]TispH_lytB: 4-hydroxy-3-methylbut-2-enyl dip


","BeTs to 16 clades of COG0761COG name: Penicillin tolerance proteinFunctional Class: I,MThe phylogenetic pattern of COG0761 is -------qvdr-bcefghsnuj-it-Number of proteins in this genome belonging to this COG is","Significant hit (4.3e-145) to 6/6 blocks of the IPB003451 family, which is described as \"LytB protein\". Interpro entry for IP:IPR003451. IPB003451A 3-23 1.3e-17 IPB003451B 32-59 8e-21 IPB003451C 69-123 4.2e-42 IPB003451D 155-191 1.3e-18 IPB003451E 199-235 1.2e-27 IPB003451F 262-282 2.5e-12","Residues 1 to 282 match (3e-136) PD:PD005867 which is described as ISOPRENE BIOSYNTHESIS ISPH COMPLETE PROTEOME PEPTIDE TRANSIT PRECURSOR LYTB-LIKE LYTB ","","","","","","","","","","","Tue Jan 21 10:20:15 2003","Tue Jan 21 10:20:15 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02954 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 285 (E-value = 8.5e-190) place AA02954 in the LYTB family which is described as LytB protein (PF02401)","","","","","De Las Rivas B, Garcia JL, Lopez R, Garcia P Purification and polar localization of pneumococcal LytB, a putative endo-beta-N-acetylglucosaminidase: the chain-dispersing murein hydrolase. J Bacteriol. 2002 Sep;184(18):4988-5000. PMID: 12193614 McAteer S, Coulson A, McLennan N, Masters M. The lytB gene of Escherichia coli is essential and specifies a product needed for isoprenoid biosynthesis. J Bacteriol. 2001 Dec;183(24):7403-7. PMID: 11717301 Cunningham FX Jr, Lafond TP, Gantt E. Evidence of a role for LytB in the nonmevalonate pathway of isoprenoid biosynthesis. J Bacteriol. 2000 Oct;182(20):5841-8. PMID: 11004185 Rohdich,F., Hecht,S., Gartner,K., Adam,P., Krieger,C., Amslinger,S., Arigoni,D., Bacher,A. and Eisenreich,W. Studies on the nonmevalonate terpene biosynthetic pathway: metabolic role of IspH (LytB) protein. Proc. Natl. Acad. Sci. U.S.A. 99 (3): 1158-1163 (2002) [PubMed: 11818558].Gustafson,C.E., Kaul,S. and Ishiguro,E.E. Identification of the Escherichia coli lytB gene, which is involved in penicillin tolerance and control of the stringent response. J. Bacteriol. 175 (4): 1203-1205 (1993) [PubMed: 8432714].Altincicek,B., Kollas,A., Eberl,M., Wiesner,J., Sanderbrand,S., Hintz,M., Beck,E. and Jomaa,H. LytB, a novel gene of the 2-C-methyl-D-erythritol 4-phosphate pathway of isoprenoid biosynthesis in Escherichia coli. FEBS Lett. 499 (1-2): 37-40 (2001) [PubMed: 11418107].McAteer,S., Coulson,A., McLennan,N. and Masters,M. The lytB gene of Escherichia coli is essential and specifies a product needed for isoprenoid biosynthesis. J. Bacteriol. 183 (24): 7403-7407 (2001) [PubMed: 11717301].","","Tue Jan 21 10:20:15 2003","1","","","" "AA02955","2068457","2067162","1296","ATGTCATTAAATATTGAAACGACTCAAGGTTTAGAGCGTCGTGTAACCGTCACCGTTCCGGCTGAAACCGTTGATCAAGCAGTACGCGAAGAATTAAAACGCGTTGCCAAAAACGCACGTGTTGACGGTTTCCGTAAAGGTAAAGTCCCTCCGCAAATTATTGAAAAACGCTTCGGCGCTTCCGTTCGTCAAGATATTTTAGGCGATTTATTACAAAAACATTTCTTCCAAGCGGTTATCGAAAATAAAGTTAACTTAGCCGGTCGCCCAAGCTTCACCGTGGAACAATTTGAAGACGGCAAAGAATTAAAATTCAGCACAACTTTTGAAGTTTACCCTGAAGTTGAATTGAAAGGTTTAGAAAATATCAAAGTTGAAAAACCGGTTGTTGAAATCTCCGAAGCGGATGTTGACAAAATGGTTGACGTGTTACGCAAACAACAAGCCACTTGGTCTGAAACGCAAGAGGTAGCAAAAGCGGAAGATCGCGTTACTATCGATTTCGTCGGTTCCGTTGACGGTGAAGAATTTGAAGGCGGCAACGCGGAAGATTTCGTGTTATTCATGGGGCAAGGTCGTATGATTCCGGGCTTTGAAGATGGCATCGTAGGTCACAAAGCCGGTGATAAATTCACGATTGATGTGACCTTCCCGGAAGAATACCACTCCGAAAAATTAAAAGGCAAAGCGGCGAAATTCGACATTACCTTGAAGAAAGTCGAGGTTATGGTATTGCCTGAATTAACCGATGAATTCATCGCAAAATTTGGTCCGAACACCAAATCCGTAGCGGATTTACGCAGCGAAATTCGCAAAAATATGCAACGTGAATTGAAAAATGCATTGACTACCCGCGTGAAAAATCAAGTGATCGACGGTTTAGTTGAACAAAACCAAATTGATGTCCCAAGCGCCGCAGTTGAGCAAGAAATTGACGTGTTACGCCAACAAGCGGCACAACGTTTCGGCGGCAATGCACAACAAGTGGCACAATTACCACGTGAGTTATTTGAAGAACAAGCAAAACGCTGTGTACTAGTCGGTTTATTATTAGCGCAAGTTATCGCGTCAAACGAACTAAAAGCAGACGAAGAACGTGCCAAAGCCATGATTGAAGACATCGCTTCCGCTTACGAACAACCAGCGGATGTGGTTGAATACTACAGCAAAAATAATGAATTAATGAACAATATTCGTAACGTTGTATTGGAAGAACAAGCAGTTGATGCGGTACTGGCTAAAGCGCAAGTTACCGAAAAAGCGGCAACCTTCGATGAAATCATGAATCCGCAAGCT","","","48362","MSLNIETTQGLERRVTVTVPAETVDQAVREELKRVAKNARVDGFRKGKVPPQIIEKRFGASVRQDILGDLLQKHFFQAVIENKVNLAGRPSFTVEQFEDGKELKFSTTFEVYPEVELKGLENIKVEKPVVEISEADVDKMVDVLRKQQATWSETQEVAKAEDRVTIDFVGSVDGEEFEGGNAEDFVLFMGQGRMIPGFEDGIVGHKAGDKFTIDVTFPEEYHSEKLKGKAAKFDITLKKVEVMVLPELTDEFIAKFGPNTKSVADLRSEIRKNMQRELKNALTTRVKNQVIDGLVEQNQIDVPSAAVEQEIDVLRQQAAQRFGGNAQQVAQLPRELFEEQAKRCVLVGLLLAQVIASNELKADEERAKAMIEDIASAYEQPADVVEYYSKNNELMNNIRNVVLEEQAVDAVLAKAQVTEKAATFDEIMNPQA","2066997","From Genbank:[gi:1174696]This protein is involved in protein export. It acts as a chaperone by maintaining the newly synthesized protein in an open conformation.","trigger factor","Cytoplasm","","
InterPro
IPR001179
Domain
Peptidyl-prolyl cis-trans isomerase, FKBP-type
PTHR10516\"[172-221]TFK506 BINDING PROTEIN
PF00254\"[153-238]TFKBP_C
PS50059\"[161-246]TFKBP_PPIASE
InterPro
IPR005215
Family
Trigger factor
PIRSF003095\"[1-432]TFKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor)
TIGR00115\"[1-430]Ttig: trigger factor
InterPro
IPR008880
Domain
Bacterial trigger factor, C-terminal
PF05698\"[239-408]TTrigger_C
InterPro
IPR008881
Domain
Bacterial trigger factor, N-terminal
PF05697\"[1-145]TTrigger_N
noIPR
unintegrated
unintegrated
G3DSA:1.10.3120.10\"[237-389]Tno description
G3DSA:3.30.70.1050\"[1-112]Tno description
PTHR10516:SF3\"[172-221]Tgb def: Peptidyl-prolyl cis-trans isomerase


","BeTs to 18 clades of COG0544COG name: FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor)Functional Class: OThe phylogenetic pattern of COG0544 is -------qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.3e-09) to 1/1 blocks of the IPB001179 family, which is described as \"FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase)\". Interpro entry for IP:IPR001179. IPB001179 189-222 1.2e-09","Residues 119 to 153 match (5e-08) PD:PD579497 which is described as TRIGGER COMPLETE PROTEOME ISOMERASE CHAPERONE CELL DIVISION FACTOR ROTAMASE TF ","","","","","","","","","","","Tue Dec 24 09:14:32 2002","Tue Dec 24 09:08:48 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02955 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 239 to 408 (E-value = 2.4e-53) place AA02955 in the Trigger_C family which is described as Bacterial trigger factor protein (TF) C-terminus (PF05698)","","","","","Guthrie,B. and Wickner,W. Trigger factor depletion or overproduction causes defective cell division but does not block protein export Journal of bacteriology. 172 (10), 5555-5562 (1990) PubMed: 2211496 Aldea,M., Garrido,T., Hernandez-Chico,C., Vicente,M. and Kushner,S.R. Induction of a growth-phase-dependent promoter triggers transcription of bolA, an Escherichia coli morphogene The EMBO journal. 8 (12), 3923-3931 (1989) PubMed: 2684651 Stoller,G., Tradler,T., Rucknagel,K.P., Rahfeld,J.-U. and Fischer,G. An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents the domain carrying the peptidyl-prolyl cis/trans isomerase activity FEBS letters. 384 (2), 117-122 (1996) PubMed: 8612805 Valent,Q.A., Kendall,D.A., High,S., Kusters,R., Oudega,B. and Luirink,J. Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides The EMBO journal. 14 (22), 5494-5505 (1995) PubMed: 8521806 Huang GC, Chen JJ, Liu CP, Zhou JM. Chaperone and antichaperone activities of trigger factor. Eur J Biochem. 2002 Sep;269(18):4516-23. PMID: 12230563 ","","Tue Dec 24 09:13:06 2002","1","","","" "AA02956","2069514","2068624","891","ATGAATAACTCGGCATTATTGGATTTATTCCTGAACGAATTATGGATTGGCAAAGGCTTGTCACCCAATACGGTGGAGTCTTATCGCTTGGATCTGACCGCACTTTGCGATTGGTTGGAGGCGCGGCATTTGTCGTTGCTCGGTTTGGATGCCGTGGACTTGCAAGCCTTTTTGGGCGAACGGGTAGAGCAGGGCTACAAAGCCACCAGCACGGCGAGATTGCTCAGTGCTATGCGGAAGCTGTTTCAATATTTGTATCAGGAAAAATATCGCACCGATGACCCCAGCGCGGTGCTCAGTTCGCCTAAATTGCCGAGCCGTTTGCCGAAATATTTAACGGAGCAGCAAGTGACGGATCTGCTGAATGTACAGAGTTTGGAACAACCCATTGAGTTACGCGATAAAGCCATGCTGGAGCTGTTGTATGCCACGGGCTTGCGGGTGACGGAATTGGTTTCCCTGAACACCGACAGCATTAATCTGAATCAAGGCGTGGTGCGGGTTATCGGCAAAGGCAAGAAGGAACGTATTGTCCCCATGGGCGAGGAGGCGACCCATTGGGTGAAACAATTTATGTTGTTTGCCCGCCCGATGTTGCTGGACGGGCAAAGCTCCGATGTGCTATTTCCCAGCCGACGCGGTACGCAAATGACGCGGCAAACTTTTTGGCATCGGATTAAACATTATGCGGTGTTGGCGGAGATTGACAGCGAGATGTTGTCGCCGCACGTTTTACGCCATGCGTTCGCTACTCATTTGGTGAATCACGGGGCGGATTTGCGCGTGGTGCAAATGTTGTTGGGACACAGTGATTTATCCACGACGCAAATTTACACCCACGTGGCAAAAGAACGGCTAAAACGTTTACATGAACGCTATCATCCGCGCGGC","","","33987","MNNSALLDLFLNELWIGKGLSPNTVESYRLDLTALCDWLEARHLSLLGLDAVDLQAFLGERVEQGYKATSTARLLSAMRKLFQYLYQEKYRTDDPSAVLSSPKLPSRLPKYLTEQQVTDLLNVQSLEQPIELRDKAMLELLYATGLRVTELVSLNTDSINLNQGVVRVIGKGKKERIVPMGEEATHWVKQFMLFARPMLLDGQSSDVLFPSRRGTQMTRQTFWHRIKHYAVLAEIDSEMLSPHVLRHAFATHLVNHGADLRVVQMLLGHSDLSTTQIYTHVAKERLKRLHERYHPRG","2068459","A puzzling duality: the Primary Reference opts for one definition, disulfide oxidase, the comparison to other sequences and ancillary data point to another, integrase-recombinase.","integrase-recombinase","Cytoplasm","","
InterPro
IPR002104
Domain
Integrase, catalytic core, phage
PF00589\"[120-288]TPhage_integrase
InterPro
IPR004107
Domain
Integrase, N-terminal SAM-like, phage
PF02899\"[7-89]TPhage_integr_N
InterPro
IPR011932
Family
Tyrosine recombinase XerD
TIGR02225\"[8-297]Trecomb_XerD: tyrosine recombinase XerD
InterPro
IPR013762
Domain
Integrase-like, catalytic core, phage
G3DSA:1.10.443.10\"[110-291]Tno description
noIPR
unintegrated
unintegrated
G3DSA:1.10.150.130\"[2-99]Tno description


","BeTs to 25 clades of COG0582COG name: IntegraseFunctional Class: LThe phylogenetic pattern of COG0582 is aompkz-qvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 5.1e-13) to 2/2 blocks of the IPB002104 family, which is described as \"Phage integrase family\". Interpro entry for IP:IPR002104. IPB002104A 243-257 1.1e-06 IPB002104B 267-278 0.00014","Residues 99 to 183 match (9e-08) PD:PD582878 which is described as INTEGRASE PLASMID DNA RECOMBINASE SITE-SPECIFIC INTEGRASE/RECOMBINASE PROTEOME COMPLETE INTIA INTI1 ","","","","","","","","","","","Thu Dec 19 12:42:14 2002","Thu Dec 19 12:42:14 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02956 is paralogously related to AA01202 (1e-48).","","","","","","Residues 112 to 288 (E-value = 7.8e-66) place AA02956 in the Phage_integrase family which is described as Phage integrase family (PF00589)","","","","Kaplan,J.B. and Fine,D.H.Codon usage in Actinobacillus actinomycetemcomitansFEMS Microbiol. Lett. 163 (1), 31-36 (1998)PubMed: 98295003","Bregu M, Sherratt DJ, Colloms SD. Accessory factors determine the order of strand exchange in Xer recombination at psi. EMBO J. 2002 Jul 15;21(14):3888-97. PMID: 12110600 Huber KE, Waldor MK. Filamentous phage integration requires the host recombinases XerC and XerD. Nature. 2002 Jun 6;417(6889):656-9. PMID: 12050668 Blakely,G., May,G., McCulloch,R., Arciszewska,L.K., Burke,M., Lovett,S.T. and Sherratt,D.J. Two related recombinases are required for site-specific recombination at dif and cer in E. coliK12. Cell 75 (2), 351-361 (1993) PubMed: 8402918. Subramanya,H.S., Arciszewska,L.K., Baker,R.A., Bird,L.E., Sherratt, D.J. and Wigley,D.B. Crystalstructure of the site-specific recombinase, XerD. EMBO J. 16 (17), 5178-5187 (1997) PubMed: 9311978. ","Thu Dec 19 12:31:22 2002","Thu Dec 19 12:31:22 2002","1","","","" "AA02958","2070551","2069520","1032","ATGGTGCTGGCGAGTGCTTATGTGTTCCGTTTTGTGGGCGGTTTGTTCTTCTCCGGTTTAATTAAACGGGCGTCGCAGCTGATTAATTCCTTGCGCTTATTGGCGCTGGCAAGTGCCTTGATTATGGCGGGGCTCAGTTTTGTTGCCGAGAATTTTTGGCTGTTATTCTCCGCTATCGGTTTGTTTGCCATGGTAAACGCCGCCGGTATGCCGATTACGGATTCGCTGGCGAGCACCTGGCAGCGCCAGATTCAACTGGATTACGGCAAAGCGCGGTTAATCGGTTCTCTGGCGTTTGTGGTGGGCGTGACTTTGTTCGGCAATGTGATCGGCTTTTTCGGCGAGCAAAATATCGTTTGGATTTTGGCCGCACTTTTAGCCGCTTATACGCTCATGCAGTGCGTGAGCCCGACCATTCCGCCGCAGGATGAACAGTCGGCACATGCCGCCGTTGGGGTGTGTTATTGGGATTTATTGAAAAACAAAACCACGTTGCGCGTCTTGCTGGCATCGTCGCTGATTCAAGGATCGCACTCCGCTTATTATGTTTACAGCGTGTTGTATTGGACGGGACTTGGCATTTCCGTTTCGCAAACCAGTTTGCTTTGGGGCTTGGCGGTGGTCTCCGAAATTCTGTTATTTTTCTTCTCCCGTCGTTTACTGCAAAACTGGAAAGTCAGCACCATTTTTCATTTGGCAACCGTTGCCTGCATTGTTCGCTGGTTGGGGCTTGCCGCCACCGATGCGATTTGGCTTATCGCCATCTTGCAATTGTTGCACAGCCTGACTTATGCCTCTGCACATTATGCCATGGTGCGTTATATTACGACGCAACCGCAAACCCATATCTCCAAGTTACAAGCCTTGTATAACGGCGTTTCCAACAGCGCAATGGTGGCGATTTTGACCGCACTTTCCGGTGTCATTTATCCGTATTCGGCGTCGATGACGTTTATTCTCATGGCATTGGCTGCTGCCGTTGCTTTCGTCGTCACTCCGCGTAAAGTGGATGCCTTTTTGTTGAAACAGGGA","","","43926","MVLASAYVFRFVGGLFFSGLIKRASQLINSLRLLALASALIMAGLSFVAENFWLLFSAIGLFAMVNAAGMPITDSLASTWQRQIQLDYGKARLIGSLAFVVGVTLFGNVIGFFGEQNIVWILAALLAAYTLMQCVSPTIPPQDEQSAHAAVGVCYWDLLKNKTTLRVLLASSLIQGSHSAYYVYSVLYWTGLGISVSQTSLLWGLAVVSEILLFFFSRRLLQNWKVSTIFHLATVACIVRWLGLAATDAIWLIAILQLLHSLTYASAHYAMVRYITTQPQTHISKLQALYNGVSNSAMVAILTALSGVIYPYSASMTFILMALAAAVAFVVTPRKVDAFLLKQG","2069355","","3-phenylpropionic acid transporter","Inner membrane, Cytoplasm","","
InterPro
IPR011701
Family
Major facilitator superfamily MFS_1
PF07690\"[11-311]TMFS_1
noIPR
unintegrated
unintegrated
PTHR10074\"[1-332]TMAJOR FACILITATOR SUPERFAMILY MEMBER
signalp\"[1-67]?signal-peptide
tmhmm\"[28-46]?\"[52-72]?\"[93-113]?\"[119-141]?\"[162-180]?\"[186-208]?\"[223-243]?\"[249-267]?\"[288-306]?\"[312-332]?transmembrane_regions


","BeTs to 9 clades of COG0477COG name: Permeases of the major facilitator superfamilyFunctional Class: G,E,P,RThe phylogenetic pattern of COG0477 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","","Residues 259 to 334 match (3e-16) PD:PD477782 which is described as PROTEOME COMPLETE TRANSPORTER PROBABLE MFS PERMEASE ACID INNER SUPERFAMILY SYMPORT ","","","","","","","","","","","","Tue Dec 10 10:39:46 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02958 is paralogously related to AA00691 (8e-05).","","","","","","","","","","","Diaz E, Ferrandez A, Garcia JL.Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid inEscherichia coli K-12.J Bacteriol. 1998 Jun;180(11):2915-23.PMID: 9603882 ","","Tue Dec 10 10:39:46 2002","1","","","" "AA02959","2071036","2070680","357","GTGGGCAAAACCCTGTGGCTTGATTCGGAAGAAAAAATGCACGCCGTTACCGCCGCCTCAGGCAGCAGCCCGGTGTATTTTTTTCAGCTGTTGGAAGCCATGCAACAAGGTTTGATTCACATGGGATTAAACGATCAGCAGGTACGCGAATTGGTGCAGCAGGCAATGTTGGGTTCGGCAAAAATGGTGGTGGAAAATCCACAACTGGATTTAGCAACCTTGCGCCAAAATGTCACATCCAAAGGCGGCACCACGGCAGCAGCGCTGAATGTGTTCAATCAACGTCAATTTAACGACATCGTGCAGCAGGCAATGCAGGCTTGCATGGCACGTTCAAAAGAAATGGAAACCTTATTT","","","13515","VGKTLWLDSEEKMHAVTAASGSSPVYFFQLLEAMQQGLIHMGLNDQQVRELVQQAMLGSAKMVVENPQLDLATLRQNVTSKGGTTAAALNVFNQRQFNDIVQQAMQACMARSKEMETLF","2070515","","pyrroline-5-carboxylate (P5C) reductase","Periplasm, Cytoplasm","","
InterPro
IPR000304
Family
Delta 1-pyrroline-5-carboxylate reductase
PTHR11645\"[1-116]TPYRROLINE-5-CARBOXYLATE REDUCTASE
PS00521\"[71-93]TP5CR
InterPro
IPR004455
Family
NADP oxidoreductase, coenzyme F420-dependent
PF03807\"[1-100]TF420_oxidored


","BeTs to 18 clades of COG0345COG name: Pyrroline-5-carboxylate reductaseFunctional Class: EThe phylogenetic pattern of COG0345 is --mp-zyqvdrlbcefghsnuj--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 1.7e-28) to 2/5 blocks of the IPB000304 family, which is described as \"Delta 1-pyrroline-5-carboxylate reductase\". Interpro entry for IP:IPR000304. IPB000304D 10-45 4.9e-16 IPB000304E 70-98 4.7e-11","Residues 1 to 115 match (4e-36) PD:PD002555 which is described as REDUCTASE PYRROLINE-5-CARBOXYLATE PROTEOME COMPLETE OXIDOREDUCTASE P5CR P5C PROLINE BIOSYNTHESIS NADP ","","","","","","","","","","","","Tue Dec 10 10:36:08 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02959 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02961","2071380","2070925","456","ATGCAACATAAATTGGTGACTTTTATCGGTGGCGGCAATATGGCACAAGCCATCGTGTTCGGTTTGTTAAAACGTGGTTATCCTGCCGATAAAATCATTGTCTGTGATCCTAACGAAGAAAAACGGGATTTGTTTGCGCAAAAAGGTGTGCGCACGGCAACGGATAATGTTGCGGCAGCCATGCAGGCGGATGTGGTGTTGTTGGCGGTAAAGCCGCAGATGTTGGTGGCAGTTTGTGCGCCGTTAAGTGCGGTAGATTTTCAGGCTAAATTGGTGATTTCCATCGCCGCCGGGAGTTCGTTGGCAAGATTGACCGCACTTTTGCGCAGGATTTGTTGGCCGCCGTGGGCAAAACCCTGTGGCTTGATTCGGAAGAAAAAATGCACGCCGTTACCGCCGCCTCAGGCAGCAGCCCGGTGTATTTTTTTCAGCTGTTGGAAGCCATGCAACAAGGTT","","","16443","MQHKLVTFIGGGNMAQAIVFGLLKRGYPADKIIVCDPNEEKRDLFAQKGVRTATDNVAAAMQADVVLLAVKPQMLVAVCAPLSAVDFQAKLVISIAAGSSLARLTALLRRICWPPWAKPCGLIRKKKCTPLPPPQAAARCIFFSCWKPCNKV","2070760","[PATHWAY] Proline biosynthesis; third (last) step.","pyrroline-5-carboxylate reductase","Periplasm, Cytoplasm","","
InterPro
IPR000304
Family
Delta 1-pyrroline-5-carboxylate reductase
PTHR11645\"[1-108]TPYRROLINE-5-CARBOXYLATE REDUCTASE
InterPro
IPR004455
Family
NADP oxidoreductase, coenzyme F420-dependent
PF03807\"[5-108]TF420_oxidored
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.720\"[4-79]Tno description


","No hits to the COGs database.","Significant hit ( 8.5e-14) to 2/5 blocks of the IPB000304 family, which is described as \"Delta 1-pyrroline-5-carboxylate reductase\". Interpro entry for IP:IPR000304. IPB000304A 6-21 8.8e-07 IPB000304B 62-72 3e-05","Residues 1 to 75 match (8e-07) PD:PD462102 which is described as PROTEOME COMPLETE REDUCTASE PYRROLINE-5-CARBOXYLATE ","","","","","","","","","","","Tue Jan 21 10:06:29 2003","Tue Jan 21 10:06:29 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02961 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 4 to 146 (E-value = 2.6e-07) place AA02961 in the P5CR family which is described as Delta 1-pyrroline-5-carboxylate reductase (PF01089)","","","","","Deutch,A.H., Smith,C.J., Rushlow,K.E. and Kretschmer,P.J.Escherichia coli delta 1-pyrroline-5-carboxylate reductase: gene sequence, protein overproduction and purification. Nucleic Acids Res. 10 (23): 7701-7714 (1982) [PubMed: 6296787]. ","","Tue Jan 21 10:06:29 2003","1","","","" "AA02962","2071443","2072345","903","ATGTTTTGGTTCAAAAACGCCATGATTTACCGCCTGACCAAATCCCTCGATTGGTCGGAACAAACCCTTTCAGTCGCCCTCGCAAACCATCAATATCACCCTTGCCATCAATCGGAACAAAGCAAATTCGGTTGGTCACAACCGCTGAAAGGCAGTGAATTATTGTATTTCACCGTCGGCAAGCAGATTTTACTGCTCGCGCAAAAAGAAGAAAAAATCCTGCCTTCCCATGTGGTGAAACGGGAACTAGACGCCCGCATAGAAAAATTGGAGCAGGCGGAAAACCGCAAGCTGAAAAAAGTGGAAAAACAAACCTTAAAAGACGACGTGGTCGCCACCCTATTGCCACGGGCTTTCAGTAAATATCAACAAACGACAATTTGGATTGATGCGGAAAACCACTTGATTTATGTAAACGCCGCCTCCGCCAAACGCGCGGAAGAGGTGCTGGCGTTATTGCGGAAATCTTTAGGTTCGTTGCCTGTAGTGCCGCTGGCATTTACCAACGAACCGGCATTAATCATGCAAACCTGGATCGCGCAGGAAAACACACCGGAATGGCTGGTGCCGCTGGAAGAAGCGGAATTGCGCGATGTGCAAACCGACAGTGTGATTCGTTGCAAACAACAAGCCTTGGACAGCGAAGAAATTTTATCGTTGGTGCATTCTAAATTCGTCACAAAATTAGCCTTGGAATGGGAGGAGCGTTTATCCTTCGTGTTGAACGAAGATTGCAGTTTAAAACGCTTAAAATTCGCCGATCAAATTCGGGAGCAAAATGACGATATTTTAAAAGAAGATTTTGCCCAGCGTTTTGATGCGGATTTTGTGTTAATGACGGGTATTCTAAGCAAACTGACGGAAAATCTGTTGCACGATTTCGGTGGAGAGAAAGAACGGCTA","","","34838","MFWFKNAMIYRLTKSLDWSEQTLSVALANHQYHPCHQSEQSKFGWSQPLKGSELLYFTVGKQILLLAQKEEKILPSHVVKRELDARIEKLEQAENRKLKKVEKQTLKDDVVATLLPRAFSKYQQTTIWIDAENHLIYVNAASAKRAEEVLALLRKSLGSLPVVPLAFTNEPALIMQTWIAQENTPEWLVPLEEAELRDVQTDSVIRCKQQALDSEEILSLVHSKFVTKLALEWEERLSFVLNEDCSLKRLKFADQIREQNDDILKEDFAQRFDADFVLMTGILSKLTENLLHDFGGEKERL","2072180","","recombination associated protein","Cytoplasm","","
InterPro
IPR007476
Family
Putative exonuclease, RdgC
PF04381\"[2-299]TRdgC


","BeTs to 6 clades of COG2974COG name: DNA recombination-dependent growth factor CFunctional Class: LThe phylogenetic pattern of COG2974 is --------------efghsn------Number of proteins in this genome belonging to this COG is","","","","","","","","","","","","","","Tue Dec 10 10:25:54 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02962 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 299 (E-value = 7.7e-177) place AA02962 in the RdgC family which is described as Putative exonuclease, RdgC (PF04381)","","","","","Ryder,L., Sharples,G.J. and Lloyd,R.G. Recombination-dependent growth in exonuclease-depleted recBC sbcBC strains of Escherichia coliK-12 Genetics 143 (3), 1101-1114 (1996) PubMed: 8807285 Mehr IJ, Long CD, Serkin CD, Seifert HS.A homologue of the recombination-dependent growth gene, rdgC, is involved in gonococcal pilin antigenic variation.Genetics. 2000 Feb;154(2):523-32.PMID: 10655208","","Tue Dec 10 10:25:54 2002","1","","","" "AA02963","2072813","2072442","372","ATGTTAAGAGCGAGCTTCATCTTATTGACGCTAATGGGATTAACCGCTTGTATGGTAAAACCGGTAGAGCAAAAGGCCCCAGCCAAACCACGCACGCAGGTTCTGCAAAAAGCCACTCAAAAGGGTTCGGCGCAAGACTATCTTTGCAAAGATAATAAAACGGTTAGGGTTGTTCGCCACACCACTAAAAACAAGAAAAAATTGAATTCTATCAGCGTGACGTTTAACAACGTGACACACCGTCTGACCCCGACGATCGCCGAAAGCGGACGTAATTATTCCAACATTCATTGGCTTTGGTTGGAACGCAAGGAATTCTCCATTCTGAAAAGCAGCGTAGGTGAAATTCTTGCGGAGCAATGTGCCGCACAG","","","14226","MLRASFILLTLMGLTACMVKPVEQKAPAKPRTQVLQKATQKGSAQDYLCKDNKTVRVVRHTTKNKKKLNSISVTFNNVTHRLTPTIAESGRNYSNIHWLWLERKEFSILKSSVGEILAEQCAAQ","2072277","","opacity associated protein B","Outer membrane, Periplasm, Extracellular","","
noIPR
unintegrated
unintegrated
PS51257\"[1-17]TPROKAR_LIPOPROTEIN
signalp\"[1-17]?signal-peptide


","No hits to the COGs database.","","Residues 47 to 121 match (3e-17) PD:PD082755 which is described as OAPB PROTEOME OPACITY PROTEINS COMPLETE ASSOCIATED ","","","","","","","","","","","","Tue Dec 10 10:19:32 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02963 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Weiser JN, Chong ST, Greenberg D, Fong W.Identification and characterization of a cell envelope protein of Haemophilus influenzae contributing to phase variation in colonyopacity and nasopharyngeal colonization.Mol Microbiol. 1995 Aug;17(3):555-64.PMID: 8559074 ","","Tue Dec 10 10:19:32 2002","1","","","" "AA02964","2074188","2072878","1311","GTGGATTCTGAAAAAAGAACCCCGGAAAATGAAAATAATCCGGCACAAAATGAATTGGATTTGGGCTTTAGTCAAATGGAACCGATCACCCCGAAAAAAGTGATTAAACCGGAACCGTCTTTGTTTGAGAAGTTGCTTGGAAAAGGCAAAGATCTCCTTACGAAGAAAGAACAAAAGAATATGGAAAATCAATTTGCCGTTCGCAGAGAACCCGTATTCGGTGGTGCCGGTGCGACTGGAGAGAAAAGCATGACAAGCGAAAACCCGACCGAGAGATTTTCAATAGAAAACACAGAAAGCAACGAACCGCAGATTGCCGCCGACACGGCGACGGAAACCCCGTCAGAAGCCCCGGACGAACCTCTCGTTACCGTAGCGGAAGAAGCCGTTGAAGCAACACAACCGGAACCTGCCGAATTGAAAGAAAAACCGAAAGCCGGTTTTAAAAATCCTGAAAATTGGGCGATTTTAAGTATTCTCCCGCAAAAACATCGTCGCATTTTCGTCGCGCTATTCGGCGTGGTGTTGGTGCTGATTTTTATCTTGTGGATGAAACCAAGCTCCGATACGGTGCAATCTTACGAGCAGCAAAGTAATAACGGCGTGCCGATTCAATTCCAGCAGTTAGACCAATCACAAACCGTTGAACCGACCGTGTTGGATAATCTGACCCCGCAAACCGATAACACTGTCGCGCAACAACCTGCTGCGGAAACCAATACGCAAAATGTCAATGCCGGCGCCATAGAACCGCAAGCGGTGGAACAAGGGGCAACCACCTCCGTTGCTGAGCAAACGACAACTGCGGCGGTAGAAAATAAACCGGCAGAAGTCAAACCGGAAGAGGTCGAAACCGTTAAACCGAGTGAGCCTGCAAAAGCGCAAGAAGCCGTCAAACCGCGTCAACATCAGGAAAGCGTGAAAAAAGAGCCGGTGAAAACCGATAAAGTGAAACAGGCTGAAAAAGCGACTGCTAAAAATCAACCGACTAAATCGGCAAAAACCGAAAAAGAAGTACGGGATATTTTAGAAGGCAAAACAACGACTATCACCAAAGCAGCAGCCGGTAGCAAAACCTTAACCATTCCGCAAGGCGTGACCTTAATGCAGGTGTTCCGTGACAACCATCTACCTGTCGGTGATGTGAATGCCATGACCAAAGCCAAAGGCGTAGGCAAGGTGTTAAGCAGCTTCAAGCCGGGTGATAAGGTACAGGTTTCCCTGAATGCACAAGGTCGCGTGAGCGAATTGCGTTTGCCCAACGGCGCACGCTTTACCCGCCAATCCGACGGCAGTTATCAATTTAAGAAG","","","47725","VDSEKRTPENENNPAQNELDLGFSQMEPITPKKVIKPEPSLFEKLLGKGKDLLTKKEQKNMENQFAVRREPVFGGAGATGEKSMTSENPTERFSIENTESNEPQIAADTATETPSEAPDEPLVTVAEEAVEATQPEPAELKEKPKAGFKNPENWAILSILPQKHRRIFVALFGVVLVLIFILWMKPSSDTVQSYEQQSNNGVPIQFQQLDQSQTVEPTVLDNLTPQTDNTVAQQPAAETNTQNVNAGAIEPQAVEQGATTSVAEQTTTAAVENKPAEVKPEEVETVKPSEPAKAQEAVKPRQHQESVKKEPVKTDKVKQAEKATAKNQPTKSAKTEKEVRDILEGKTTTITKAAAGSKTLTIPQGVTLMQVFRDNHLPVGDVNAMTKAKGVGKVLSSFKPGDKVQVSLNAQGRVSELRLPNGARFTRQSDGSYQFKK","2072713","","opacity associated protein A","Periplasm, Extracellular, Inner membrane","","
InterPro
IPR007340
Family
Opacity-associated protein A
PF04225\"[356-437]TOapA
InterPro
IPR013731
Domain
Opacity-associated protein A, N-terminal
PF08525\"[155-188]TOapA_N
noIPR
unintegrated
unintegrated
tmhmm\"[167-187]?transmembrane_regions


","BeTs to 3 clades of COG3061COG name: Cell envelope opacity-associated protein AFunctional Class: MThe phylogenetic pattern of COG3061 is --------------e-gh--------Number of proteins in this genome belonging to this COG is","","Residues 15 to 327 match (1e-17) PD:PD415877 which is described as OAPA COMPLETE PROTEOME PROTEINS OPACITY ASSOCIATED ","","","","","","","","","","","","Tue Dec 10 10:16:10 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02964 is paralogously related to AA02832 (9e-04).","","","","","","Residues 228 to 437 (E-value = 7.4e-47) place AA02964 in the OapA family which is described as Opacity-associated protein A (PF04225)","","","","","Bauer,B.A., Lumbley,S.R. and Hansen,E.J. Characterization of a WaaF (RfaF) homolog expressed by Haemophilus ducreyi Infect. Immun. 67 (2), 899-907 (1999) PubMed: 9916106 Weiser,J.N., Chong,S.T., Greenberg,D. and Fong,W. Identification and characterization of a cell envelope protein of Haemophilus influenzae contributing to phase variation in colony opacity and nasopharyngeal colonization Mol. Microbiol. 17 (3), 555-564 (1995) PubMed: 8559074 ","","Tue Dec 10 10:16:10 2002","1","","","" "AA02965","2074209","2074346","138","ATGCCGATATGCCGTAAAAGTGCGGTCGTTTTTTTCTGCGTTTTTCATGAGAGGAATCAACACAGAAACCGAATCGCTCACAGCATAAAATTAATAAGTAAAAAAATCGCGCCTATTCTAAAACATCTTTTGCTTTTT","","","5437","MPICRKSAVVFFCVFHERNQHRNRIAHSIKLISKKIAPILKHLLLF","2074346","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
signalp\"[1-4]?signal-peptide


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 10:43:27 2004","Mon Feb 23 10:43:27 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02965 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 10:44:27 2004","","","","","","","","","","","","","1","","","" "AA02966","2075331","2074363","969","TTGGAACATCTGGCAAACGGGATTTCGGACCCGAAAATCTTATTACAACACCTGGAACTGCCCCTCGAACCGTTTAAACAAGACATTGAAGCCCGCAAATTGTTTGCCATACGCGTGCCTTTGCCTTTTGTGGCGAAAATGGAAAAAGGCAATGCGCGCGATCCCTTATTTTTACAAGTGATGTCTTTTGCTGACGAATTTCTGCAGGCAGAAGGGTTCAGCAAAGATCCGCTGGAAGAACAAGAAGATAAGAATGTGGTGCCGAATATTCTGCACAAATACCATAATCGCTTGTTATTTATGGTCAAAGGCGGCTGTGCGGTCAATTGCCGCTATTGTTTTCGCCGTCATTTTCCCTATGACCAAAACAAAGGCAATAAACAAAATTGGCAGAAGGCGCTGGACTATATTGCCACCCATCCGGAAATCGAAGAGGTGATTTTATCCGGCGGCGATCCGCTTATGGCGAAGGATCATGAAATCGCTTGGCTGATAAAACACCTGGAAAATCTACCGCACTTAACACGTCTGCGCATTCATTCACGTTTGCCGGTGGTGATTCCGCAACGCATTACCGACAAATTTTGCCATATTCTGACGCAAACCCGTTTACAGAAAATTCTGGTCACACACGTTAATCATGCCAATGAAATTGATGAAGATTTTTCCCATGCCATGGATAAATTAAAGAATTGCGGTGTCGTATTATTAAACCAATCGGTTTTACTGAAAAACGTGAATGACGATGCCCATATTCTGAAAGCATTGAGCGACCGTTTATTTTCAGTGGGGATTCTGCCTTATTATCTGCATTTGCTGGATAAGGTGGAAGGCGCGGCGCATTTTTATCTTGATGATGCGCAGGCGTTAAGAATTTACAAACAATTACAACGCATTACCTCCGGTTATTTAGTGCCGAAACTCGCCCGCGAAATTGGTGGCGAACCGAATAAAACCTTGTTTGCAACA","","","43907","LEHLANGISDPKILLQHLELPLEPFKQDIEARKLFAIRVPLPFVAKMEKGNARDPLFLQVMSFADEFLQAEGFSKDPLEEQEDKNVVPNILHKYHNRLLFMVKGGCAVNCRYCFRRHFPYDQNKGNKQNWQKALDYIATHPEIEEVILSGGDPLMAKDHEIAWLIKHLENLPHLTRLRIHSRLPVVIPQRITDKFCHILTQTRLQKILVTHVNHANEIDEDFSHAMDKLKNCGVVLLNQSVLLKNVNDDAHILKALSDRLFSVGILPYYLHLLDKVEGAAHFYLDDAQALRIYKQLQRITSGYLVPKLAREIGGEPNKTLFAT","2074198","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR003739
Family
Protein of unknown function DUF160
TIGR00238\"[1-314]TTIGR00238: lysine 2,3-aminomutase YodO fami
InterPro
IPR007197
Domain
Radical SAM
PF04055\"[100-256]TRadical_SAM


","BeTs to 10 clades of COG1509COG name: Lysine 2,3-aminomutaseFunctional Class: EThe phylogenetic pattern of COG1509 is --m----qvd--b-e-ghs--j--t-Number of proteins in this genome belonging to this COG is","Significant hit ( 4.6e-75) to 3/3 blocks of the IPB003739 family, which is described as \"DUF160\". Interpro entry for IP:IPR003739. IPB003739A 106-116 1.2e-07 IPB003739B 140-190 3.9e-34 IPB003739C 233-282 6.7e-31","Residues 47 to 165 match (1e-12) PD:PD183058 which is described as PROTEOME COMPLETE L-LYSINE 23-AMINOMUTASE BH2943 23-AMINOMUTASE TM0121 ISOMERASE YODO AQ_1632 ","","","","","","","","","","","","Tue Dec 10 10:14:09 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02966 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 100 to 256 (E-value = 4.4e-10) place AA02966 in the Radical_SAM family which is described as Radical SAM superfamily (PF04055)","","","","","","","","1","","","" "AA02967","2075372","2075974","603","ATGACCACTTTAAAAAACAATCTTTTTCTTGAGGATAATATGGCTACATATACTACCAGTGATTTCAAACCAGGTCTAAAATTTATGCAAGACGGCGAACCTTGCGTGATCGTTGAAAATGAATTCGTCAAACCCGGCAAAGGTCAGGCGTTCACCCGCACCCGTATTCGTAAATTAATTTCCGGCAAAGTATTGGATGTGAACTTCAAATCCGGTACCTCTGTTGAAGCCGCTGATGTTATGGATTTAAACTTAACCTATTCTTACAAAGACGATGCGTTCTGGTATTTCATGCACCCGGAAACGTTCGAACAATATTCCGCCGACGCCAAAGCCGTAGGCGATGCCGAAAAATGGTTATTAGACCAAGCCGATTGTATCGTGACCTTATGGAACGGCGCACCGATTACCGTGACCCCACCGAACTTCGTTGAGTTGGAAATCGTCGATACCGATCCTGGCTTAAAAGGTGATACCGCAGGTACCGGCGGCAAACCGGCAACCTTAAGCACCGGCGCCGTGGTGAAAGTGCCGTTATTCGTACAAATCGGTGAAGTGATCCGCGTAGATACCCGCTCCGGCGAATATGTTTCCCGCGTGAAG","","","22132","MTTLKNNLFLEDNMATYTTSDFKPGLKFMQDGEPCVIVENEFVKPGKGQAFTRTRIRKLISGKVLDVNFKSGTSVEAADVMDLNLTYSYKDDAFWYFMHPETFEQYSADAKAVGDAEKWLLDQADCIVTLWNGAPITVTPPNFVELEIVDTDPGLKGDTAGTGGKPATLSTGAVVKVPLFVQIGEVIRVDTRSGEYVSRVK","2075809","[FUNCTION] Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase (by similarity). [PATHWAY] Protein biosynthesis.","elongation factor P (EF-P)","Cytoplasm, Periplasm","","
InterPro
IPR001059
Domain
Translation elongation factor P/YeiP, central
PF01132\"[82-136]TEFP
InterPro
IPR011768
Family
Translation elongation factor P
PIRSF005901\"[16-201]TTranslation elongation factor P
TIGR00038\"[14-201]Tefp: translation elongation factor P
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[79-142]T\"[143-200]Tno description
InterPro
IPR013185
Domain
Translation elongation factor, KOW-like
PF08207\"[18-75]TEFP_N
InterPro
IPR013852
Domain
Translation elongation factor P/YeiP, C-terminal
PS01275\"[165-184]TEFP
InterPro
IPR014722
Domain
Translation protein SH3-like, subgroup
G3DSA:2.30.30.30\"[16-78]Tno description
InterPro
IPR015365
Domain
Elongation factor P, C-terminal
PF09285\"[144-199]TElong-fact-P_C


","BeTs to 20 clades of COG0231COG name: Translation elongation factor P/translation initiation factor eIF-5AFunctional Class: JThe phylogenetic pattern of COG0231 is aompkzyqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.4e-54) to 2/2 blocks of the IPB001059 family, which is described as \"Elongation factor P (EF-P)\". Interpro entry for IP:IPR001059. IPB001059A 37-76 1.1e-20 IPB001059B 156-199 1.6e-32","Residues 14 to 57 match (2e-07) PD:PD485492 which is described as FACTOR ELONGATION P PROTEOME COMPLETE EF-P BIOSYNTHESIS ","","","","","","","","","","","Tue Jan 21 10:00:53 2003","Tue Jan 21 10:00:53 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02967 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 16 to 200 (E-value = 3.2e-122) place AA02967 in the EFP family which is described as Elongation factor P (EF-P) (PF01132)","","","","","Aoki,H., Adams,S.L., Chung,D.G., Yaguchi,M., Chuang,S.E. and Ganoza,M.C. Cloning, sequencing and overexpression of the gene for prokaryotic factor EF-P involved in peptide bond synthesis Nucleic Acids Res. 19 (22), 6215-6220 (1991) PubMed: 1956781 Aoki,H., Adams,S.L., Turner,M.A. and Ganoza,M.C. Molecular characterization of the prokaryotic efp gene product involved in a peptidyltransferase reaction Biochimie 79 (1), 7-11 (1997) PubMed: 9195040 ","","Tue Jan 21 10:00:53 2003","1","","","" "AA02968","2076057","2076221","165","ATGGAAATTAATATTCTTTACAATAACACCTTTCAAAACTCAATAATTTATCTAAAAATCACGCTATTTTATATAAAAAATTATTTATTTTATAAAAATAAACTAAATTTTAATAATTTTTTATTATATGTGACATTCCTCACAGTAATGCTAAAAATTTTTTAT","","","6861","MEINILYNNTFQNSIIYLKITLFYIKNYLFYKNKLNFNNFLLYVTFLTVMLKIFY","2076221","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
tmhmm\"[36-54]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 09:52:22 2004","Mon Feb 23 09:52:22 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02968 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 10:15:31 2004","","","","","","","","","","","","","1","","","" "AA02969","2076247","2076477","231","ATGTTTGAGAAGCGAGTTACCAGCATGGACTTTAAACTCATCATAAACAGGAGACAAATTATGACATACTATCCAGCAGAGCCGTTCCGAATCAAAAGTGTTGAACCGGTTTCCATTTTACCGAAAGAAGAACGCGAAAAAGCCATGAAAGAAGCGGGATATAATACCTTCTTACTTGATTCTAAAGATGTATATATCGATCTCTTAACCGATAGCGGTACCAATGCCATG","","","23549","MFEKRVTSMDFKLIINRRQIMTYYPAEPFRIKSVEPVSILPKEEREKAMKEAGYNTFLLDSKDVYIDLLTDSGTNAM","2076693","","beta tyrosinase (tyrosine phenol-lyase)","Cytoplasm","","
InterPro
IPR001597
Domain
Aromatic amino acid beta-eliminating lyase/threonine aldolase
PD005927\"[30-77]TTPL_ESCIN_P31012;
InterPro
IPR015422
Domain
Pyridoxal phosphate-dependent transferase, major region, subdomain 2
G3DSA:3.90.1150.10\"[21-77]Tno description


","No hits to the COGs database.","Significant hit ( 4.4e-38) to 1/11 blocks of the IPB001597 family, which is described as \"Beta-eliminating lyase\". Interpro entry for IP:IPR001597. IPB001597A 27-72 3.7e-38","Residues 24 to 77 match (2e-20) PD:PD005927 which is described as PHOSPHATE PYRIDOXAL LYASE TNASE TRYPTOPHANASE CATABOLISM INDOLE-LYASE TRYPTOPHAN L-TRYPTOPHAN COMPLETE ","","","","","","","","","","","","Tue Dec 10 10:12:12 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02969 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Demidkina TV, Barbolina MV, Faleev NG, Sundararaju B, Gollnick PD, Phillips RS. Threonine-124 and phenylalanine-448 in Citrobacter freundii tyrosine phenol-lyase are necessaryfor activity with L-tyrosine. Biochem J. 2002 May 1;363(Pt 3):745-52. PMID: 11964175 Faleev NG, Zhukov YN, Khurs EN, Gogoleva OI, Barbolina MV, Bazhulina NP, Belikov VM, DemidkinaTV, Khomutov RM. Interaction of tyrosine phenol-lyase with phosphoroorganic analogues of substrate amino acids. Eur J Biochem. 2000 Dec;267(23):6897-902. PMID: 11082202 Katayama T, Suzuki H, Koyanagi T, Kumagai H. Cloning and random mutagenesis of the Erwinia herbicola tyrR gene for high-level expression oftyrosine phenol-lyase. Appl Environ Microbiol. 2000 Nov;66(11):4764-71. PMID: 11055921 ","","Tue Dec 10 10:12:58 2002","1","","","" "AA02970","2076513","2077451","939","ATGAAGCTTACGCCGGTAGTAGAAACTTCTATCATCTGCAAGAAACCGTACAAGAACTCTTCGGTTTCAAACATATCGTTCCAACCCACCAAGGACGTGGTAGCGGAAAACATCCTTTCCCGCATTGCCATCAAACCGGGACAATATGTGCCGGAGAATATGTATTTCACCACAACCCGTTATCACCGAGAAGCCAACGGCGGGATTTTCTACGATATTATCCGTGATGAAGCCCATGAGGCGACATTAGACATACCGTTCAAAGGCGATATTGACCTGAAAAAACTGGAAAACCTGATCAATGAAAAAGGGGCGGAAAATATCGCTTATGTGTGCTTGGCGGTTACTGTAAACCTCGCCGGCGGTCAACCGGTTTCCATCGCCAATATGAAAGCCGTGCGTGAACTTACCGCCAAACACGGCATTAAAGTGTTCTTCGATGCCACCCGTTGCGTTGAAAATGCTTACTTCATTAAAGAACAGGAAGAAGGCTACCAAGATCGCTCCATTAAATCCATCATTCACGAAATGTTCAGCTATGCCGACGGCTGTACCATGAGCGGTAAAAAAGACTGCTTAACCAATATCGGCGGCTTCTTATGTATGAACGATGAAGAATTGTTCATGAAAGCCAAAGAGTTAGTTGTGGTATTTGAAGGTATGCCGTCTTACGGCGGTATGGCTGGTCGTGATATGGAAGCCATGGCAATCGGTTTGAAAGAAGCCACCCAAGAAGAATACATTGAACACCGTGTAAAACAAGTGCGTTATCTCGGCGAAAAATTAAAAGCCGCCGGCGTACCGATTGTTGAACCGATTGGTGGTCATGCCGTATTCTTGGATGCCCGTCGTTTCTGCCCGCACTTGAAACAAGAAGAAGATTTCCCTGCTCAAGCCTTGGCGGCGGCAATCTACATCGAATGCGGTGTACGTACCATG","","","22439","MKLTPVVETSIICKKPYKNSSVSNISFQPTKDVVAENILSRIAIKPGQYVPENMYFTTTRYHREANGGIFYDIIRDEAHEATLDIPFKGDIDLKKLENLINEKGAENIAYVCLAVTVNLAGGQPVSIANMKAVRELTAKHGIKVFFDATRCVENAYFIKEQEEGYQDRSIKSIIHEMFSYADGCTMSGKKDCLTNIGGFLCMNDEELFMKAKELVVVFEGMPSYGGMAGRDMEAMAIGLKEATQEEYIEHRVKQVRYLGEKLKAAGVPIVEPIGGHAVFLDARRFCPHLKQEEDFPAQALAAAIYIECGVRTM","2077283","","tyrosine phenol-lyase","Cytoplasm","","
InterPro
IPR001597
Domain
Aromatic amino acid beta-eliminating lyase/threonine aldolase
PD005927\"[35-313]TQ7P6C8_BBBBB_Q7P6C8;
PF01212\"[35-313]TBeta_elim_lyase
InterPro
IPR011166
Family
Tryptophanase
PIRSF001386\"[15-313]TTryptophanase
InterPro
IPR015421
Domain
Pyridoxal phosphate-dependent transferase, major region, subdomain 1
G3DSA:3.40.640.10\"[35-243]Tno description


","BeTs to 4 clades of COG3033COG name: TryptophanaseFunctional Class: EThe phylogenetic pattern of COG3033 is -o---z--------e-gh--------Number of proteins in this genome belonging to this COG is","Significant hit (1.3e-136) to 7/11 blocks of the IPB001597 family, which is described as \"Beta-eliminating lyase\". Interpro entry for IP:IPR001597. IPB001597C 52-67 1e-07 IPB001597D 87-113 6.9e-16 IPB001597E 115-139 1.1e-16 IPB001597F 140-177 1.5e-29 IPB001597G 178-203 8.8e-23 IPB001597H 204-241 5.5e-28 IPB001597I 267-313 2.2e-08 IPB001597I 268-313 0.006","Residues 35 to 313 match (9e-136) PD:PD005927 which is described as PHOSPHATE PYRIDOXAL LYASE TNASE TRYPTOPHANASE CATABOLISM INDOLE-LYASE TRYPTOPHAN L-TRYPTOPHAN COMPLETE ","","","","","","","","","","","","Mon Jan 13 17:17:55 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02970 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 14 to 313 (E-value = 5.2e-133) place AA02970 in the Beta_elim_lyase family which is described as Beta-eliminating lyase (PF01212)","","","","","Demidkina TV, Barbolina MV, Faleev NG, Sundararaju B, Gollnick PD, Phillips RS.Threonine-124 and phenylalanine-448 in Citrobacter freundii tyrosine phenol-lyase are necessary for activity with L-tyrosine.Biochem J. 2002 May 1;363(Pt 3):745-52.PMID: 11964175 Faleev NG, Zhukov YN, Khurs EN, Gogoleva OI, Barbolina MV, Bazhulina NP, Belikov VM, Demidkina TV, Khomutov RM.Interaction of tyrosine phenol-lyase with phosphoroorganic analogues of substrate amino acids.Eur J Biochem. 2000 Dec;267(23):6897-902.PMID: 11082202 Katayama T, Suzuki H, Koyanagi T, Kumagai H.Cloning and random mutagenesis of the Erwinia herbicola tyrR gene for high-level expression of tyrosine phenol-lyase.Appl Environ Microbiol. 2000 Nov;66(11):4764-71.PMID: 11055921 ","","Tue Dec 10 10:09:57 2002","1","","","" "AA02972","2077521","2077682","162","GTGCGTATCACCATTCCTCGCCGTGTTTATACCTATGCCCACATGGATTTAGTGGCTGACGGTATTATCCACCTGTTTAAACATAAACAAGACATTAAAGGTCTTCGTTTCGTGTATGAACCGAAACAACTCCGTTTCTTCACTGCACGTTTTGAACAAAAA","","","6574","VRITIPRRVYTYAHMDLVADGIIHLFKHKQDIKGLRFVYEPKQLRFFTARFEQK","2077682","","conserved hypothetical protein (tyrosine phenol lyase-related protein)","Cytoplasm","This sequence is similar to gi|477613, a predicted tyrosine phenol-lyase from Citrobacter freundii. See also gi|401203 from Citrobacter intermedius.","
InterPro
IPR001597
Domain
Aromatic amino acid beta-eliminating lyase/threonine aldolase
PD005927\"[1-52]TTPL_ESCIN_P31012;
PF01212\"[1-21]TBeta_elim_lyase
InterPro
IPR015422
Domain
Pyridoxal phosphate-dependent transferase, major region, subdomain 2
G3DSA:3.90.1150.10\"[1-52]Tno description


","No hits to the COGs database.","Significant hit ( 9.6e-21) to 2/11 blocks of the IPB001597 family, which is described as \"Beta-eliminating lyase\". Interpro entry for IP:IPR001597. IPB001597J -20-20 0.074 IPB001597K 32-52 2.3e-17","Residues 1 to 52 match (9e-20) PD:PD005927 which is described as PHOSPHATE PYRIDOXAL LYASE TNASE TRYPTOPHANASE CATABOLISM INDOLE-LYASE TRYPTOPHAN L-TRYPTOPHAN COMPLETE ","","","","","","","","","","","","Mon Feb 23 11:36:50 2004","Mon Feb 23 15:32:35 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA02972 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 09:27:42 2004","","","","","","","","","","","","","1","","","" "AA02973","2077847","2079058","1212","ATGAACAAAACATTAGGCAGTACGCTGATTACATCGGGAACGATGATCGGCGCGGGGATGCTTGCCATGCCGCTCACTTCGGCAGGTATCGGTTTCACATTTACGGTGGGGCTACTTTGTATTTTATGGGTATTGCTCACCTACAGCGCGCTTCTTTTTGTAGAAGTCTATCAAACGGCAGAATATGATGCCGGCATAGGAACTCTCGCGGCACAATACTTCGGCAAACCGGGACGGGTTGTAGCAACCACCGTTCTCATGATTTTCCTGTATGCACTGCTCTCCGCTTATGTTACCGGCGGCGGCTCAATTCTTGCGTCAACCTTGCCGGACTTTTCCCCGCCGGACCTTAAAATGAAAGGCTCCATTCTGCTCTTTACCGTCTTTTTCGGCACTTTTATCGTTATCGGAACAAAAATTGTTGATGGCTTAAACCGAATCTTATTTTTCACCATGCTCATTGCCCTGTTCGTGGTACTTAGCTTAATGATTCCGGAAATTCATGTTGATAATTTAATGGCTATGCCCATAGATAATGCTTTATTGATTTCTGCCAGTCCGGTATTTTTTACTGCCTTCGGTTTTCACGGCTCCATTCCTTGCCTAAATAAATACCTCGAAGGTGATGTAAAAGCCCTGAGAATTTCCATTACTATCGGTTCGGCGATTACGCTTATCGGCTATATTCTTTGGCAATTTTCCACCCACGGCGTGTTAAGCCAAACCCGCTTCTTAGAGATTCTAAGTAAGGATCCGACATTAAACGGCTTGGTGAACGCAGTGAAAATCATTACAGGCAGCGATATGATTGCAGGCGTCGTCAAACTGTTCTCCGCCTTGGCATTGATTACCTCATTCCTCGGTGTTGCGTTAGGATTGTTTGAATGTATTGAAGATCTGCTCAAACGCGCCTTCAATATTGATGCCAACAGACCTTGCCTCGGCATATTAACTTTTTTCCCACCGTTGCTGTTTGCCTTCTTCTATCCGGAAGGCTTCATTTTAGCGCTAGGCTACGCCGGGCAAATGTTCGCGTTCTACGCGGTGTTTTTGCCGGCGGCATTGGTGTGGAAAGCCCGCCAACAACACCCGAATTTAGCATATCGCGTGCCCGGCGGCGCCGGCGTGCTACTGCTCGTTTCCATTCTGGGGATCATTATCGTCAGCATTCCATTCCTGATCAAACTCGGCTACCTGCCGATGGTGGTGGGG","","","43453","MNKTLGSTLITSGTMIGAGMLAMPLTSAGIGFTFTVGLLCILWVLLTYSALLFVEVYQTAEYDAGIGTLAAQYFGKPGRVVATTVLMIFLYALLSAYVTGGGSILASTLPDFSPPDLKMKGSILLFTVFFGTFIVIGTKIVDGLNRILFFTMLIALFVVLSLMIPEIHVDNLMAMPIDNALLISASPVFFTAFGFHGSIPCLNKYLEGDVKALRISITIGSAITLIGYILWQFSTHGVLSQTRFLEILSKDPTLNGLVNAVKIITGSDMIAGVVKLFSALALITSFLGVALGLFECIEDLLKRAFNIDANRPCLGILTFFPPLLFAFFYPEGFILALGYAGQMFAFYAVFLPAALVWKARQQHPNLAYRVPGGAGVLLLVSILGIIIVSIPFLIKLGYLPMVVG","2078890","","tyrosine-specific transport protein","Inner membrane, Cytoplasm","","
InterPro
IPR002091
Family
Aromatic amino acid permease
PR00166\"[9-32]T\"[36-55]T\"[81-101]T\"[147-167]T\"[181-203]T\"[220-239]T\"[281-300]T\"[316-334]T\"[337-356]TAROAAPRMEASE
PF03222\"[3-391]TTrp_Tyr_perm
InterPro
IPR013059
Family
Tryptophan/tyrosine transporter
TIGR00837\"[6-384]TaraaP: aromatic amino acid transport protei
InterPro
IPR013061
Family
Tryptophan/tryrosine permease
PS00594\"[16-32]TAROMATIC_AA_PERMEASE_1
noIPR
unintegrated
unintegrated
signalp\"[1-49]?signal-peptide
tmhmm\"[5-24]?\"[30-52]?\"[85-107]?\"[121-141]?\"[146-164]?\"[183-203]?\"[213-231]?\"[276-294]?\"[309-329]?\"[335-355]?\"[376-394]?transmembrane_regions


","BeTs to 9 clades of COG0814COG name: Amino acid permeasesFunctional Class: EThe phylogenetic pattern of COG0814 is ------y-------efgh-nu--i--Number of proteins in this genome belonging to this COG is","Significant hit (2.5e-117) to 6/6 blocks of the IPB002091 family, which is described as \"Aromatic amino acids permease\". Interpro entry for IP:IPR002091. IPB002091A 7-50 9.1e-22 IPB002091B 68-105 2.7e-17 IPB002091C 187-202 1.2e-08 IPB002091D 217-259 4.3e-20 IPB002091E 277-301 4.4e-14 IPB002091F 310-360 4.4e-29Significant hit ( 1.6e-07) to 2/2 blocks of the IPB002422 family, which is described as \"Permeases for amino acids and related compounds, family II\". Interpro entry for IP:IPR002422. IPB002422A 14-24 6.5e-06 IPB002422B 287-293 11","Residues 1 to 83 match (6e-21) PD:PD407890 which is described as PROTEOME COMPLETE TYROSINE-SPECIFIC TYROSINE PERMEASE AMINO-ACID INNER MEMBRANE TRANSMEMBRANE TYRP ","","","","","","","","","","","","Tue Dec 10 10:01:48 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02973 is paralogously related to AA01704 (1e-162), AA01245 (1e-124), AA00468 (1e-59) and AA00092 (4e-10).","","","","","","Residues 3 to 391 (E-value = 2e-165) place AA02973 in the Trp_Tyr_perm family which is described as Tryptophan/tyrosine permease family (PF03222)","","","","","Wookey,P.J. and Pittard,A.J. DNA sequence of the gene (tyrP) encoding the tyrosine-specific transport system of Escherichia coli. J. Bacteriol. 170(10): 4946-4949.1988. PubMed: 3049553. Sarsero,J.P., Wookey,P.J., Gollnick,P., Yanofsky,C. and Pittard,A.J. . A new family of integral membrane proteins involved in transport of aromatic amino acids in Escherichia coli. J. Bacteriol. 173(10): 3231-3234.1991 PubMed: 2022620.","","Tue Dec 10 10:01:48 2002","1","","","" "AA02974","2079804","2079130","675","ATGAACAGGTTACAAAAGAAATATTTTATTGGTTTAACCCATTTTTTAGGCAATGTATTAGGACCGAAATATGAGGTGGTGTTTCATTCCTTTGAAAAAAATAAAGCCTCAATGGAAGCCATCGTCAACAGCCATGTGAGCGGCAGAAATCTCTCTTCGCCACTGAGTTCTTTTGCATCGAATATGTTGCTGGAAAAGGTTTATTTAGATAAGGATTTTATCTTTAATTACAAAGCAGTTGCCGATTCCGATAAGACAATTCGAGGTTCAACATTTTTCATTAAAAACGGTAAGCGATTGGAAGGGATTTTGTGCATTAATCACGATACTTCCGAACTTATGGATGCCATGACGAAATTAATTTCCCTGGAAAATTTGGGTAATTTTATCAATGTGCTGGGGTTCGATCCGGCACTAGACCGCAGTGATGATGCCGGTATTCCTAATAAAGAAAGGTTGGAACATTCTATTGAAGATATTCTTTCGGAATATATCGACATTAATTTATTAAATTCGGAGAAAAACCTGACTTTAAGGCAGAAAGAAAACTCTATTCGGATTTTGTTCGATAAGGGCGTTTTTAATATAAAAGGTGCGATTCCCATGGTGGCAAAATATTTAAAAATATCGGTGCCAAGTGTTTATCGGTATTTAAAATTAATCAGAGGAAAAGCA","","","25499","MNRLQKKYFIGLTHFLGNVLGPKYEVVFHSFEKNKASMEAIVNSHVSGRNLSSPLSSFASNMLLEKVYLDKDFIFNYKAVADSDKTIRGSTFFIKNGKRLEGILCINHDTSELMDAMTKLISLENLGNFINVLGFDPALDRSDDAGIPNKERLEHSIEDILSEYIDINLLNSEKNLTLRQKENSIRILFDKGVFNIKGAIPMVAKYLKISVPSVYRYLKLIRGKA","2078962","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR013559
Domain
YheO-like
PF08348\"[5-123]TPAS_6


","No hits to the COGs database.","","Residues 151 to 219 match (2e-15) PD:PD312385 which is described as COMPLETE PROTEOME DNA-BINDING CONTAINING SPY0144 HELIX-TURN-HELIX ","","","","","","","","","","","","Tue Dec 10 09:59:39 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02974 is paralogously related to AA01519 (1e-12).","","","","","","","","","","","","","","1","","","" "AA02975","2080373","2079870","504","ATGGCTGATCCACATATTAAATCCCATATGGATGTTTGGGACTATGTTACCGTTATCATCTATCGTTCGGGTTTCACCCTTGCGGTGCCCATGTTATTGATGTTGCCATGGTATCCCGCAACGGCGCAAATCGGCTTATTAATTGCCGCCGCTTCTTGTGCCGCCTGCGTGCATTTATATATGAAAAATTTCCGTTATCTTTTTCAGTTCGCCATGTGGTTGGGGTTGTTATGCCAAATTCTGGGTTTTCCTCAGCTTGCTTTGGGCGCGGCGTTTTTAGTGCTGGGCGGGTTAAGTTATAAAGAATATTTTTGTTTTCGTGTTTTTGCGTTAAACCTGCAACCAATATTTTTTGCAATATTATGGTTTGCCTTATTATTTGATCTGACCTGGCTTAGCACCTTATTATCGCTTGTAACAGGCATTTTAATTTTATTATTAAGCATTCAAAAGTGGCGTATGCCGTTACATTTCGATATTGGAGATAAAAGAAAATATCAGGTT","","","19278","MADPHIKSHMDVWDYVTVIIYRSGFTLAVPMLLMLPWYPATAQIGLLIAAASCAACVHLYMKNFRYLFQFAMWLGLLCQILGFPQLALGAAFLVLGGLSYKEYFCFRVFALNLQPIFFAILWFALLFDLTWLSTLLSLVTGILILLLSIQKWRMPLHFDIGDKRKYQV","2079702","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
noIPR
unintegrated
unintegrated
PD092039\"[1-168]TQ9CPE4_PASMU_Q9CPE4;
signalp\"[1-42]?signal-peptide
tmhmm\"[19-39]?\"[44-64]?\"[70-99]?\"[109-129]?\"[135-155]?transmembrane_regions


","No hits to the COGs database.","","Residues 1 to 168 match (8e-34) PD:PD092039 which is described as PROTEOME COMPLETE PM0101 TRANSMEMBRANE HI0120 ","","","","","","","","","","","","Tue Dec 10 09:58:10 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02975 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02976","2081097","2080369","729","ATGCAAAAAACCTATTTTATTGCAGACTTACATCTGGCAGAAAGTCGACCGCACTTATTAGCGCTTTTTCGCCAATTTATGCAGGAACAGGCGCCACAAGCGGAAAAACTGTATATTCTGGGCGATTTATTTGATTTTTGGATTGGCGATGATGAACAATCCGGCTTAATTTTCGATGTACAACAGTTAATTAAAAACTTAACCCATCAAGGCGTGCAGTGTTACTTTCAACATGGCAATCGTGATTTTTTAATAGGCGAAACCTTTGCCGATGCTTGTGGTCTAACCCTCCTACCCACTTATAAATTGATTGATTTATACGGCGTACCGACACTGTTATGCCACGGCGACACCCTGTGTATTGATGACGTGAAATATCAGCAGTATCGTAAGAAAGTCCATCAAAAATGGCGTCAGTGGCTGTTCCTGCACTTGCCGTTAAAAGTGCGGTTAAAAATCGCAGAGAAAATTCGGGCGAAGAGCCGGCGGGATAAACAATTTAAACCGACAGAGATTATGGATGTGAATGCGGATTTTGTGTTGCAAACGTTCGCTAAATTTCAGGTGACACAAATTATTCACGGACATACGCACCGTCAAAAACACCATGAAATTCCACCGCACTTTCACCGTATCGTGCTCGGTGATTGGGGTGAAACTTCCTCTATTTTGGAAGTTACGCCCGATTCCATGCAGTTTATTAATGATAATCTAAGGAGTAAAAATGGC","","","28511","MQKTYFIADLHLAESRPHLLALFRQFMQEQAPQAEKLYILGDLFDFWIGDDEQSGLIFDVQQLIKNLTHQGVQCYFQHGNRDFLIGETFADACGLTLLPTYKLIDLYGVPTLLCHGDTLCIDDVKYQQYRKKVHQKWRQWLFLHLPLKVRLKIAEKIRAKSRRDKQFKPTEIMDVNADFVLQTFAKFQVTQIIHGHTHRQKHHEIPPHFHRIVLGDWGETSSILEVTPDSMQFINDNLRSKNG","2080201","From GenBank (gi:22095857):This protein catalyzes the hydrolysis of the pyrophosphate bond ofUDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP (By similarity). LpxA is the fourth step in lipid A biosynthesis.","UDP-2,3-diacylglucosamine hydrolase","Cytoplasm","","
InterPro
IPR004843
Domain
Metallophosphoesterase
PF00149\"[2-200]TMetallophos
InterPro
IPR010138
Family
UDP-2,3-diacylglucosamine hydrolase
TIGR01854\"[4-231]Tlipid_A_lpxH: UDP-2,3-diacylglucosamine hyd


","No hits to the COGs database.","","Residues 1 to 226 match (2e-95) PD:PD038423 which is described as COMPLETE PROTEOME HYDROLASE UDP-23-DIACYLGLUCOSAMINE SYNTHESIS LIPID 3.6.1.- VC1850 PM0102 STY0583 ","","","","","","","","","","","Fri Jan 24 11:49:44 2003","Fri Jan 24 11:49:44 2003","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02976 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 2 to 200 (E-value = 1.9e-07) place AA02976 in the Metallophos family which is described as Calcineurin-like phosphoesterase (PF00149)","","","","","Babinski KJ, Kanjilal SJ, Raetz CR.Accumulation of the lipid A precursor UDP-2,3-diacylglucosamine in an Escherichia coli mutant lacking the lpxH gene.J Biol Chem. 2002 Jul;277(29):25947-56.PMID: 12000771Babinski KJ, Ribeiro AA, Raetz CR.The Escherichia coli gene encoding the UDP-2,3-diacylglucosamine pyrophosphatase of lipid A biosynthesis.J Biol Chem. 2002 Jul;277(29):25937-46.PMID: 12000770","","Mon Jan 27 15:26:30 2003","1","","","" "AA02977","2081208","2081948","741","ATGTTAAAAATCGCCAGAATTTTCATTATTCTTCTTTGCTGCATTCTCATTTGCGTCCTCGGCACGCTCTATTCTTTCATTCGTTTTCGTAACCCAAGTAACGTGGGCATTTTCGCCCGTTGGTTCGGTCGGCTATATCCGCTTTTCGGGCTGAACGTCGAACATCGCTACCCGCCGAATACCGACAAAATCGGGCGCTGCATTTATATCGGCAACCACCAAAATAACTACGACATGGTGACCATTTCTTATATGGTGATGCCGCGCACCGTCAGCGTCGGTAAGAAAAGCCTGATTTGGGTGCCGTTTTTCGGCATTTTATATTGGGCGACGGGCAATATTTTTCTGGATCGCGACAATCGCTCCAAAGCCCACAACACCATGACGGAACTGGCACGCCGCATAAATCAGGACAATCTGTCTATTTGGATGTTCCCGGAAGGCACTCGCAGTCGCGGACGCGGATTATTGCCGTTTAAAACCGGCGCCTTTCATGCTGCCATTGCTGCCGACGTGCCTGTCGTGCCGGTGGTCTGCTCCACTACACACAATAAAATCGATTTAAACCGCTGGAACAACGGCAAGGTGATTTGTGAAATGCTGGAACCCATTGACGTTTCCGGCTATACCCGTGAAAACGTGCGCGAACTGGCGGAATATTGCCACGATATAATGCAAAAACGCATCAATGAATTAGATCAGGAAATTGCCCAATCCGCACAAACAACATCACCCGCAGGC","","","28249","MLKIARIFIILLCCILICVLGTLYSFIRFRNPSNVGIFARWFGRLYPLFGLNVEHRYPPNTDKIGRCIYIGNHQNNYDMVTISYMVMPRTVSVGKKSLIWVPFFGILYWATGNIFLDRDNRSKAHNTMTELARRINQDNLSIWMFPEGTRSRGRGLLPFKTGAFHAAIAADVPVVPVVCSTTHNKIDLNRWNNGKVICEMLEPIDVSGYTRENVRELAEYCHDIMQKRINELDQEIAQSAQTTSPAG","2081780","","1-acyl-sn-glycerol-3-phosphate acyltransferase","Inner membrane, Cytoplasm","","
InterPro
IPR002123
Domain
Phospholipid/glycerol acyltransferase
PF01553\"[52-180]TAcyltransferase
SM00563\"[67-182]TPlsC
InterPro
IPR004552
Domain
1-acyl-sn-glycerol-3-phosphate acyltransferase
TIGR00530\"[50-180]TAGP_acyltrn: 1-acyl-sn-glycerol-3-phosphate
noIPR
unintegrated
unintegrated
PTHR10434\"[4-237]T1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE
signalp\"[1-21]?signal-peptide
tmhmm\"[7-27]?\"[98-116]?transmembrane_regions


","BeTs to 15 clades of COG0204COG name: 1-acyl-sn-glycerol-3-phosphate acyltransferaseFunctional Class: IThe phylogenetic pattern of COG0204 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 2.4e-08) to 2/2 blocks of the IPB002123 family, which is described as \"Phospholipid and glycerol acyltransferase (from 'motifs_6.msf')\". Interpro entry for IP:IPR002123. IPB002123A 63-78 0.0079 IPB002123B 142-150 0.0012","Residues 86 to 155 match (6e-22) PD:PD546302 which is described as ACYLTRANSFERASE TRANSFERASE 1-ACYL-SN-GLYCEROL-3-PHOSPHATE LYSOPHOSPHATIDIC ACID BIOSYNTHESIS LPAAT PHOSPHOLIPID 1-AGPAT 1-AGP ","","","","","","","","","","","","Tue Dec 10 09:32:50 2002","","Thu Feb 10 10:16:05 2005","Fri Mar 25 08:45:29 2005","Thu Feb 10 10:16:05 2005","yes","Fri Feb 20 15:41:32 MST 1998","AA02977 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Thu Feb 10 10:16:05 2005","","","","","Residues 50 to 180 (E-value = 2.4e-50) place AA02977 in the Acyltransferase family which is described as Acyltransferase (PF01553)","Thu Feb 10 10:16:05 2005","","","","Swartley JS, Balthazar JT, Coleman J, Shafer WM, Stephens DS.Membrane glycerophospholipid biosynthesis in Neisseria meningitidis and Neisseria gonorrhoeae: identification, characterization, and mutagenesis of a lysophosphatidic acid acyltransferase.Mol Microbiol. 1995 Nov;18(3):401-12.PMID: 8748025Coleman J.Characterization of the Escherichia coli gene for 1-acyl-sn-glycerol-3-phosphate acyltransferase (plsC).Mol Gen Genet. 1992 Mar;232(2):295-303.PMID: 1557036","","Fri Mar 25 08:45:29 2005","1","","","" "AA02978","2081953","2083368","1416","ATGCAAATGAAACCGTGTTCCCGTCGTCAGCTCTTAAAAACAACATTATTTTCCACCGCACTTTTTGCGGTGCCTAAGCCTTTGTTGGCGGCGACCAATCCGCCGTTGTACGTTCCGCCGCTGCTTGAAACCCGTCGCGGCAAACCGATTTTCCTGAATATGCAAAACACCCAAACGTCCTTGTTGCCGGGGAAACGTACCGAAGTTTGGGGTTTCAACGGCGCTTATCTCGGGCCGACAATTAAAATCAAAAAAGGCGATTTTGCCAAATTGAACTGGAAAAACAATCTGCCGCAATTTGTCGCCATGAATATTCAGGGTTTACAGGCTTCCGGCGAATTAATGGGCGGTATCGCCAAAAATCTGCAAAAAGGCGAAACCTGGGCGCCAATCGTGCCGATTACCCAAGCACCCGCCACTTGCTGGTATCACGCCTGCACCCTTGCCAGTGCGGCGTATCAAACTTATCGCGGGCTTGTGGGGCTGTGGCTGATTGAAGATAAAAAAAGTGCCAAACCGGGCTTGCCGCAAAAATACGGCGTGGATGACATTCCGTTAATTTTGCAGGATATGCAACTCAACGGCGAAGGCGCGCAATTGTTTCAGCAAAATCAAACCTCGCTCATCGGCGATCGTTTATTTGTCAACGGGCGAGAAGCCCCTTATTTAACCGCACCGCGTGGTTTGGTGCGCTTACGTTTACTGAACGCTTCCCTTTCCCGTGCCTACGACATTCGCTTTGACGACGAACGCGAATTTACCCTTATCGCTCAAGATCTCGGCTTCCTACCGCAAGGCAAAAAAGTCAATGTTATCCATCTTGCGCCAAGCGAACGCGCAGAAATCCTGGTGGATTTAAACAACAGCGAAGCAGTCAGTTTAATTGCCGGTCATAAACGCGGCTTTTTCGATAAAATCGGCAATTTTTTCAGTTCGGACGGCGAACTGATTGACAACACCATTTTAGAACTACGCCCGGACGGTTTAGCCGGTGCCTTTGAACAAAAAGAAAAAAGCTGGCAATTTGACACCGATGCGCCTGCCACGCTCTCCGCACAAGTGCAACAAGAACGTCGTTTCCACATTGACACCACCAACGCCAGCATCAATCAGAACCGATTCGACCCGCGCCGTTTGGACATATACGCCAAATTAGACAGTGTTGAACGCTGGACGCTCACCGCCTCTTCCGCCGTAGGCTTTTCCGTGCGCGGGGCAAAATTTATCGTCGAATCTATTAATGATAAACCGTTAGAAGCGGCTGAAATCAGTTGGAAAGACAGCGTTTGGATCGATGGCAAAGTGACTATTTTGGTGAAATTTGAAAACACCTCGTCCAACAATTACCCCTTCACCTTCGGCGCGTCCGATCTTATGCTGGCGGATAAAGGCTGCATGGGGTTAATGATCGTGCAA","","","54018","MQMKPCSRRQLLKTTLFSTALFAVPKPLLAATNPPLYVPPLLETRRGKPIFLNMQNTQTSLLPGKRTEVWGFNGAYLGPTIKIKKGDFAKLNWKNNLPQFVAMNIQGLQASGELMGGIAKNLQKGETWAPIVPITQAPATCWYHACTLASAAYQTYRGLVGLWLIEDKKSAKPGLPQKYGVDDIPLILQDMQLNGEGAQLFQQNQTSLIGDRLFVNGREAPYLTAPRGLVRLRLLNASLSRAYDIRFDDEREFTLIAQDLGFLPQGKKVNVIHLAPSERAEILVDLNNSEAVSLIAGHKRGFFDKIGNFFSSDGELIDNTILELRPDGLAGAFEQKEKSWQFDTDAPATLSAQVQQERRFHIDTTNASINQNRFDPRRLDIYAKLDSVERWTLTASSAVGFSVRGAKFIVESINDKPLEAAEISWKDSVWIDGKVTILVKFENTSSNNYPFTFGASDLMLADKGCMGLMIVQ","2083200","","sufI protein precursor homolog","Periplasm","","
InterPro
IPR011707
Domain
Multicopper oxidase, type 3
PF07732\"[53-170]TCu-oxidase_3
noIPR
unintegrated
unintegrated
G3DSA:2.60.40.420\"[27-165]T\"[169-313]Tno description
PTHR11709\"[123-295]TMULTI-COPPER OXIDASE
PTHR11709:SF2\"[123-295]TSPORE COAT PROTEIN
signalp\"[1-30]?signal-peptide


","No hits to the COGs database.","","Residues 290 to 351 match (1e-09) PD:PD385703 which is described as PROTEOME SUFI COMPLETE ","","","","","","","","","","","","Tue Dec 10 09:30:12 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02978 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","Yahr TL, Wickner WT.Functional reconstitution of bacterial Tat translocation in vitro.EMBO J. 2001 May 15;20(10):2472-9.PMID: 11350936 ","","Tue Dec 10 09:30:12 2002","1","","","" "AA02980","2084305","2083445","861","ATGCAGTACATTCTCATCGCATTGTGTTTGTGGAGCAGTTCTTTTGTCGCCGGTAAATACACTTACACCATGCTCGATCCCGTGTTGATGGTGCAAATGCGCTTGTTTATTGCGACAGCGATTGTGCTGCCGATGTTTGTACGGGTTTGGAAACGCGTGCCGAAGGAGATTCGCCCGCAGGTGTGGTGGCTGGGTTTTTTAAATTATCCCGCGATTTTTTTATTGCAGTTTGTCGGCTTAAGTCATACTTCCGCGTCCAGCGCTTCCACCATGTTAGGACTGGAACCGTTTCTGGTGGTGCTGATCGGGCATTTTTTCTTTGGCGATAAAGCCAAAACCCATCATTGGATTTTCGGCTTAATTGCTTTTTTAGGTGTGGCATTATTGATTTCCGGCGGCGAAGAAACCGGCAATATCAGTATTTTCGGCTGTAGCCTGGTGTTGTTTGCCGGCGTGGTTTTTGCCTCTTGCTTGCGTTGGGCGCAAAAAATCATCGTGCAGCTCACCGCACAGGTTTATACCACCAGCAGTATCGTCCTCGGTACCATCACTTGTCTTCCTTTTACGTTATGGCTAACGCAAAGCTGGCAAATTCACTGGAATTGGCAAGGCATCGCAGGATTGTTGTATATCGGCATTGGTTGTAGCTGGCTGGCGTATTATCTCTGGAACAAAGGCATCAATAGCGTGGATTCCAATCTTGCCGGCATTTTGGTTTCATTGGAGCCGGTGTTTGCCATCATCTTGGCGGTGTTGTTACTGGGCGAAAATATCAGCCCGCTTTCTTGGCTGGGGATTTTGGCGGTGGTCAGCACCACATTGATTTCCAGCGTCTATCCGCGCTTGGTTCGGCGTGCGAAC","","","31883","MQYILIALCLWSSSFVAGKYTYTMLDPVLMVQMRLFIATAIVLPMFVRVWKRVPKEIRPQVWWLGFLNYPAIFLLQFVGLSHTSASSASTMLGLEPFLVVLIGHFFFGDKAKTHHWIFGLIAFLGVALLISGGEETGNISIFGCSLVLFAGVVFASCLRWAQKIIVQLTAQVYTTSSIVLGTITCLPFTLWLTQSWQIHWNWQGIAGLLYIGIGCSWLAYYLWNKGINSVDSNLAGILVSLEPVFAIILAVLLLGENISPLSWLGILAVVSTTLISSVYPRLVRRAN","2083277","","conserved hypothetical protein","Inner membrane, Cytoplasm","","
InterPro
IPR000620
Domain
Protein of unknown function DUF6, transmembrane
PF00892\"[9-131]T\"[152-278]TDUF6
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide
tmhmm\"[2-20]?\"[26-46]?\"[61-81]?\"[87-107]?\"[116-131]?\"[137-157]?\"[178-198]?\"[204-224]?\"[234-254]?\"[260-280]?transmembrane_regions


","No hits to the COGs database.","","Residues 205 to 272 match (3e-12) PD:PD111415 which is described as PROTEOME COMPLETE TRANSMEMBRANE MEMBRANE INTEGRAL PLASMID PROBABLE PERMEASE TRANSPORTER GENE ","","","","","","","","","","","","Tue Dec 10 09:26:34 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02980 is paralogously related to AA02883 (2e-13), AA02113 (3e-04) and AA00573 (4e-04).","","","","","","Residues 148 to 278 (E-value = 4.2e-20) place AA02980 in the DUF6 family which is described as Integral membrane protein DUF6 (PF00892)","","","","","","","","1","","","" "AA02982","2085187","2084450","738","ATGTCAGTCGTTGCAAGAATCCACTCTTATGAATCCTGCGGCACCGTTGACGGGCCGGGAATTCGTTTTATTCTGTTTTTACAAGGCTGTTTAATGCGCTGTAAGTATTGCCATAACCGTGATACTTGGGATTTGCACGGCGGCAAAGAAATCACCGTGGAAGAGTTGATGAAAGAAGTGGTCACTTATCGCCACTTTATGAACGCCAGCGGTGGTGGAGTGACGGCATCGGGCGGCGAGGCCATTTTACAGGCGGAATTCGTTCGCGATTGGTTCCGCGCCTGCAAAGCGGAAGGCATTCATACCTGCCTGGATACCAACGGATTCGTACGTCACTATGATCATGTTATTGATGAACTGATTGATGTCACCGATTTGGTGCTGTTGGATTTGAAAGAACTCAACGACAAAGTGCACCAAAACCTCATCGGCGTGCCGAATAAACGCACTCTTGAATTTGCCAAATACCTGCAAAAGCGGAATCAGCCCGTATGGATTCGTTATGTGGTGGTGCCGGGTTATACGGATTCCGACCACGACGTGCATTTGCTCGGGCAATTTATCGAAGGCATGACCAATATAGAAAAAGTAGAGCTACTGCCATATCACCGTTTAGGTGCGCACAAATGGGCGGCAATGGGCGAGAAATACGAATTGGAAGACGTAAAACCACCGACAAAAGAATCCTTAGAACACATTAAAACCATCTTGGAAGGCTATGGTCACATCGTTAAATAT","","","28140","MSVVARIHSYESCGTVDGPGIRFILFLQGCLMRCKYCHNRDTWDLHGGKEITVEELMKEVVTYRHFMNASGGGVTASGGEAILQAEFVRDWFRACKAEGIHTCLDTNGFVRHYDHVIDELIDVTDLVLLDLKELNDKVHQNLIGVPNKRTLEFAKYLQKRNQPVWIRYVVVPGYTDSDHDVHLLGQFIEGMTNIEKVELLPYHRLGAHKWAAMGEKYELEDVKPPTKESLEHIKTILEGYGHIVKY","2084282","","pyruvate formate-lyase activating enzyme","Cytoplasm","","
InterPro
IPR001989
Domain
Radical-activating enzyme
PS01087\"[18-39]TRADICAL_ACTIVATING
InterPro
IPR007197
Domain
Radical SAM
PF04055\"[24-185]TRadical_SAM
InterPro
IPR012838
Family
Pyruvate formate-lyase activating
TIGR02493\"[6-240]TPFLA: pyruvate formate-lyase 1-activating e


","BeTs to 11 clades of COG1180COG name: Pyruvate-formate lyase-activating enzymeFunctional Class: OThe phylogenetic pattern of COG1180 is a-mpkz-qv-rl--efgh--------Number of proteins in this genome belonging to this COG is","Significant hit ( 3.9e-27) to 3/3 blocks of the IPB001989 family, which is described as \"Radical activating enzymes\". Interpro entry for IP:IPR001989. IPB001989A 16-43 4.3e-20 IPB001989B 73-84 0.00084 IPB001989C 127-132 5.5","Residues 16 to 82 match (6e-07) PD:PD016381 which is described as ANAEROBIC REDUCTASE COMPLETE PROTEOME RIBONUCLEOSIDE-TRIPHOSPHATE ACTIVATING OXIDOREDUCTASE RIBONUCLEOTIDE SMALL CLASS ","","","","","","","","","","","","Tue Dec 10 09:23:39 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02982 is paralogously related to AA00241 (1e-05).","","","","","","Residues 24 to 185 (E-value = 8.9e-28) place AA02982 in the Radical_SAM family which is described as Radical SAM superfamily (PF04055)","","","","","Rodel,W., Plaga,W., Frank,R. and Knappe,J. Primary structures of Escherichia coli pyruvate formate-lyase and pyruvate-formate-lyase-activating enzyme deduced from the DNA nucleotide sequences Eur. J. Biochem. 177 (1), 153-158 (1988) M:89030680 Walsby CJ, Ortillo D, Broderick WE, Broderick JB, Hoffman BM.An Anchoring Role for FeS Clusters:Chelation of the Amino Acid Moiety of S-Adenosylmethionine to the Unique Iron Site of the[4Fe-4S] Cluster of Pyruvate Formate-Lyase Activating Enzyme. J Am Chem Soc. 2002 Sep 25;124(38):11270-1. PMID: 12236732 Becker A, Kabsch W X-ray Structure of Pyruvate Formate-Lyase in Complex with Pyruvate and CoA. HOW THE ENZYME USESTHE CYS-418 THIYL RADICAL FOR PYRUVATE CLEAVAGE. J Biol Chem. 2002 Oct 18;277(42):40036-42. PMID: 12163496 ","","Tue Dec 10 09:23:39 2002","1","","","" "AA02983","2087644","2085335","2310","ATGACTCAATTAACAGAAGCTCAACAAAAAGCCTGGGAAGGTTTTGTCGGTGGAGATTGGCAAAAAGAAGTCAACGTGCGTGACTTTATCCAAAAAAACTATACTCCGTATGAAGGCGACGAATCTTTCTTAGCCGATGCAACACCTGCGACCACGGAGTTGTGGGAAAAAGTGATGGAAGGGATTAAAATCGAAAATAAAACGCATGAGCCGTTAGATTTTGATACGGATAATCCATCTACAATCACTTCTCACAAACCGGGTTATATCAATAAAGAATTGGAAAAAATCGTCGGTTTACAAACCGATGCACCGTTAAAACGTGCAATTATGCCGTTCGGTGGTATCAAAATGGTGAAAGGATCTTGCGAAGTTTATGGTCGTCAATTAGATCCTGAAGTAGAACATATCTTTACCGAATATCGTAAAACCCACAACCAAGGTGTTTTCGACGTTTATACACCGGACATTCTTCGTTGCCGTAAATCCGGCGTGTTAACCGGTTTGCCGGATGCTTACGGTCGTGGTCGTATTATCGGTGACTATCGTCGTTTAGCGGTTTATGGTGTCGATTTCTTGATGGCGGATAAGAAAAAACAATTCGCTTCCTTACAACCTAAATTAGAACGTGGTGAAGACATTCAAGCCACCATTCAATTACGTGAAGAAATTGCCGAACAACATCGCGCATTGGGTAAATTAAAAGAAATGGCAGCCTCTTACGGTTACGACATTTCTAACCCGGCAACAAACGCACAGGAAGCCGTTCAATGGACTTACTTTGCTTATCTTGCCGCCGTGAAATCCCAAAACGGTGCGGCAATGTCATTTGGTCGCGTATCGACTTTCTTAGATATTTATATCGAACGTGATTTGAAAAACGGTAAAATCACCGAACAAGAAGCACAAGAATTAATCGACCACTTGGTGATGAAGCTTCGTATGGTTCGTTTCTTGCGTACGCCTGAATATGATCAATTGTTCTCCGGCGACCCAATGTGGGCAACTGAAACTTTAGCCGGTATGGGCTTAGATGGTCGTACTCTCGTGACCAAAAACAGCTTCCGTATCTTACACACCCTATACACCATGGGGCCTTCTCCGGAACCGAACTTAACCATTCTTTGGTCTGAACAATTACCTGATGCGTTCAAACGTTTCTGTGCCAAAGTGTCTATTGATACTTCTTCCGTACAATATGAAAACGATGACTTAATGCGTCCGGACTTCAACAGCGATGACTATGCTATTGCCTGCTGTGTATCCCCGATGGTGGTGGGTAAACAAATGCAGTTCTTCGGTGCCCGTGCGAACTTGGCGAAAACCTTGTTATACGCAATCAACGGCGGTATCGATGAGAAAAACGGTATGCAGGTTGGTCCGAAAACCGAAGCGATTAAAGACGAAGTGCTTGATTTCGACACTGTGATGACCCGCATGGACAGCTTCATGGATTGGTTGGCAACACAATATGTGACCGCTTTGAACATCATCCACTTCATGCACGATAAATATGCTTATGAAGCGGCGTTAATGGCGTTCCATGATCGTGACGTATTCCGTACCATGGCATGCGGTATCGCAGGACTTTCCGTTGCTGCTGACTCTTTATCTGCCATTAAATACGCGAAAGTTAAACCGATTCGTGGCGATATTAAAGACAAAGACGGCAATGTTGTGGCATCTAATGTGGCAACCGACTTCGAAATTGAAGGCGAATATCCGCAATTCGGTAACAACGATCCGCGTGTGGATGACATTGCGTGCGACTTGGTTGAACGTTTCATGAAGAAAATTCAAACTCACCATACTTACCGTAATGCAACACCAACGCAATCCGTGCTTACTATCACGTCTAACGTGGTATATGGTAAGAAAACCGGTAATACCCCGGACGGTCGTCGCGCAGGCGCACCATTCGGACCGGGTGCTAACCCAATGCACGGACGTGACCAAAAAGGTGCGGTGGCATCTTTAACTTCCGTGGCTAAATTGCCATTCGCTTACGCGAAAGACGGTATTTCTTATACCTTTTCCATCGTACCGAATGCGTTAGGTAAAGATTACGAAGCGCAAAAACGTAACTTAGCCGGCTTAATGGACGGTTACTTCCACCACGAAGCCACTGTTGAAGGCGGTCAACACTTGAACGTTAACGTGATGAACCGTGAAATGTTGTTAGACGCAATGGAAAATCCGGAAAAATATCCGCAATTAACCATCCGCGTTTCCGGTTATGCCGTACGTTTCAACTCGTTGACTAAAGAGCAACAACAAGACGTTATCACCCGTACATTTACCCAAACAATG","","","86414","MTQLTEAQQKAWEGFVGGDWQKEVNVRDFIQKNYTPYEGDESFLADATPATTELWEKVMEGIKIENKTHEPLDFDTDNPSTITSHKPGYINKELEKIVGLQTDAPLKRAIMPFGGIKMVKGSCEVYGRQLDPEVEHIFTEYRKTHNQGVFDVYTPDILRCRKSGVLTGLPDAYGRGRIIGDYRRLAVYGVDFLMADKKKQFASLQPKLERGEDIQATIQLREEIAEQHRALGKLKEMAASYGYDISNPATNAQEAVQWTYFAYLAAVKSQNGAAMSFGRVSTFLDIYIERDLKNGKITEQEAQELIDHLVMKLRMVRFLRTPEYDQLFSGDPMWATETLAGMGLDGRTLVTKNSFRILHTLYTMGPSPEPNLTILWSEQLPDAFKRFCAKVSIDTSSVQYENDDLMRPDFNSDDYAIACCVSPMVVGKQMQFFGARANLAKTLLYAINGGIDEKNGMQVGPKTEAIKDEVLDFDTVMTRMDSFMDWLATQYVTALNIIHFMHDKYAYEAALMAFHDRDVFRTMACGIAGLSVAADSLSAIKYAKVKPIRGDIKDKDGNVVASNVATDFEIEGEYPQFGNNDPRVDDIACDLVERFMKKIQTHHTYRNATPTQSVLTITSNVVYGKKTGNTPDGRRAGAPFGPGANPMHGRDQKGAVASLTSVAKLPFAYAKDGISYTFSIVPNALGKDYEAQKRNLAGLMDGYFHHEATVEGGQHLNVNVMNREMLLDAMENPEKYPQLTIRVSGYAVRFNSLTKEQQQDVITRTFTQTM","2085167","","formate acetyltransferase","Cytoplasm","","
InterPro
IPR001150
Domain
Formate C-acetyltransferase glycine radical
PF01228\"[640-751]TGly_radical
PS51149\"[642-770]TGLY_RADICAL_2
PS00850\"[740-748]TGLY_RADICAL_1
InterPro
IPR004184
Domain
Pyruvate formate-lyase, PFL
PF02901\"[11-624]TPFL
InterPro
IPR005949
Family
Formate acetyltransferase
PIRSF000379\"[9-770]TFormate acetyltransferase
TIGR01255\"[11-770]Tpyr_form_ly_1: formate acetyltransferase
noIPR
unintegrated
unintegrated
G3DSA:3.20.70.20\"[2-770]Tno description


","BeTs to 5 clades of COG1882COG name: Pyruvate-formate lyaseFunctional Class: CThe phylogenetic pattern of COG1882 is a-m--------l--e-gh--------Number of proteins in this genome belonging to this COG is","Significant hit ( 6.4e-37) to 2/2 blocks of the IPB001150 family, which is described as \"Pyruvate formate-lyase, glycine radical\". Interpro entry for IP:IPR001150. IPB001150A 613-623 0.56 IPB001150B 719-768 1.4e-34","Residues 605 to 704 match (3e-13) PD:PD552594 which is described as PYRUVATE FORMATE-LYASE PROTEOME COMPLETE FORMATE TRANSFERASE ACETYLTRANSFERASE GLUCOSE RADICAL ORGANIC ","","","","","","","","","","","","Tue Dec 10 09:21:25 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02983 is paralogously related to AA03001 (2e-23).","","","","","","Residues 640 to 751 (E-value = 6.5e-66) place AA02983 in the Gly_radical family which is described as Glycine radical (PF01228)","","","","","Sawers,G. and Bock,A. Novel transcriptional control of the pyruvate formate-lyase gene: upstream regulatory sequences and multiple promoters regulate anaerobic expression J. Bacteriol. 171 (5), 2485-2498 (1989) M:89213931 Wagner,A.F., Frey,M., Neugebauer,F.A., Schafer,W. and Knappe,J. The free radical in pyruvate formate-lyase is located on glycine-734 Proc. Natl. Acad. Sci. U.S.A. 89 (3), 996-1000 (1992) M:92141244 Molloy,M.P., Herbert,B.R., Walsh,B.J., Tyler,M.I., Traini,M., Sanchez,J.C., Hochstrasser,D.F., Williams,K.L. and Gooley,A.A. Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis Electrophoresis 19 (5), 837-844 (1998) M:98291876 Becker,A., Fritz-Wolf,K., Kabsch,W., Knappe,J., Schultz,S. and Volker Wagner,A.F. Structure and mechanism of the glycyl radical enzyme pyruvate formate-lyase Nat. Struct. Biol. 6 (10), 969-975 (1999) M:99436526 ","","Tue Dec 10 09:21:25 2002","1","","","" "AA02984","2088594","2087746","849","ATGGATACCGAAACTTCCAAAACGACTTGTATGGTGTCTCCGGCAGAAATGAGCCAAATCGGCGAGGACGTCGGTGTATACAAAGCTTCAAAAAGACAGATTTTATCGTTTTTTTCAGCTATTCCTGCCGGTGCGTTTATTGCATTGGCGTTTGTTTTTTATACCACTACGCAAACGGGAAGTGTGGGCGGTTCCTGGGGGTTGACGAAATTAGTCGGCGGGATCGTGTTCTCGTTAGGGGTCATTATGGTAGTGGTGTGCGGCTCCGAGTTATTTACTTCTTCTACAATGACGACAGTTGCCCGTGCCGGTGGTCGTATCAGTACGTTTCAAATGCTGCGAAATTGGGTTGTAGTTTATTGTGGTAATTTCGTCGGCGCAATTTTTATTGTTTTAGTCATTTGGTTTTCCGGTCAGACAATGGCTGCTCACGGGCAGTGGGGGCTCACCATTTTAAGTACGGCGCAACATAAGATTCACCATACATGGATTGAAGCGTTCTGCTTAGGTATTTTATGTAATATCATGGTGTGTATTGCCATTTGGATGACATACGCGGGAAAAACGTTAACAGATAAAGCCTTCATTATGATTTTACCGATTGCTTTGTTTGTGGCCTCAGGGTTTGAGCACAGTGTGGCGAATATGTTTATGATTCCGATGGGGATCATTACCGCACACTTTAGCTCACCTGAATTTTGGCAGGCAATTAATATGGATCCTCAGCAGTTTGCGGACTTGGATCTTTATCATTTTGTGGTGAAGAATTTAATTCCGGTCACGCTGGGTAATATTGTTGGTGGTGGTTGTTGTATTGCATTGACTTTATGGTCAATTAATAGACCGCAC","","","30765","MDTETSKTTCMVSPAEMSQIGEDVGVYKASKRQILSFFSAIPAGAFIALAFVFYTTTQTGSVGGSWGLTKLVGGIVFSLGVIMVVVCGSELFTSSTMTTVARAGGRISTFQMLRNWVVVYCGNFVGAIFIVLVIWFSGQTMAAHGQWGLTILSTAQHKIHHTWIEAFCLGILCNIMVCIAIWMTYAGKTLTDKAFIMILPIALFVASGFEHSVANMFMIPMGIITAHFSSPEFWQAINMDPQQFADLDLYHFVVKNLIPVTLGNIVGGGCCIALTLWSINRPH","2087578","","formate transporter","Inner membrane, Cytoplasm","","
InterPro
IPR000292
Family
Formate/nitrite transporter
PF01226\"[10-283]TForm_Nir_trans
TIGR00790\"[28-282]Tfnt: formate/nitrite transporter
PS01005\"[85-94]TFORMATE_NITRITE_TP_1
noIPR
unintegrated
unintegrated
signalp\"[1-45]?signal-peptide
tmhmm\"[34-56]?\"[75-95]?\"[116-138]?\"[166-186]?\"[195-215]?\"[257-277]?transmembrane_regions


","BeTs to 6 clades of COG2116COG name: Formate/nitrite family of transportersFunctional Class: PThe phylogenetic pattern of COG2116 is ------y----lb-efgh--------Number of proteins in this genome belonging to this COG is","Significant hit ( 2e-81) to 4/4 blocks of the IPB000292 family, which is described as \"Formate and nitrite transporters\". Interpro entry for IP:IPR000292. IPB000292A 71-97 1.5e-18 IPB000292B 116-134 7.8e-11 IPB000292C 177-224 2.1e-36 IPB000292D 256-277 8.4e-12 IPB000292D 115-136 0.4","Residues 11 to 102 match (3e-32) PD:PD386211 which is described as FORMATE PROTEOME COMPLETE TRANSPORTER PROBABLE CHANNEL TRANSMEMBRANE INNER MEMBRANE 1 ","","","","","","","","","","","","Tue Dec 10 09:19:07 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02984 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 10 to 283 (E-value = 1.3e-148) place AA02984 in the Form_Nir_trans family which is described as Formate/nitrite transporter (PF01226)","","","","","Suppmann,B. and Sawers,G. Isolation and characterization of hypophosphite--resistant mutants of Escherichia coli: identification of the FocA protein, encoded by the pfl operon, as aputative formate transporter Mol. Microbiol. 11 (5), 965-982 (1994) PubMed: 8022272 ","","Tue Dec 10 09:19:07 2002","1","","","" "AA02987","2088907","2089254","348","ATGACAGCCGAAACCATTTTCAGCAAAATTATCCGCAAAGAAATCCCCGCCAATATTGTATATCAAGATGAGCTTGTCACCGCCTTTCGCGATATTGCGCCACAAGCAAAAACCCACATTTTAATCATTCCGAATAAATTGATCCCGACCGTTAATGATGTGACCGAACAAGATGAAGTAACTCTTGGTCGCCTGTTCACCGTTGCCGCCAAACTTGCTGCCCAAGAAGGCATCGCACAAGACGGCTATCGTTTAATCGTCAATTGCAACAAACACGGCGGACAGGAAGTGTTCCACTTACATATGCACCTCGTCGGCGGCGAACCGTTGGGCAAAATGTTGGATAAA","","","12855","MTAETIFSKIIRKEIPANIVYQDELVTAFRDIAPQAKTHILIIPNKLIPTVNDVTEQDEVTLGRLFTVAAKLAAQEGIAQDGYRLIVNCNKHGGQEVFHLHMHLVGGEPLGKMLDK","2089086","","histidine triad protein homolog","Cytoplasm","","
InterPro
IPR001310
Family
Histidine triad (HIT) protein
PR00332\"[6-22]T\"[27-45]T\"[95-105]THISTRIAD
PIRSF000714\"[1-116]THistidine triad hydrolase
PTHR23089\"[20-106]THISTIDINE TRIAD (HIT) PROTEIN
PF01230\"[12-110]THIT
PS51084\"[6-116]THIT_2
PS00892\"[88-106]THIT_1
noIPR
unintegrated
unintegrated
G3DSA:3.30.428.10\"[4-115]Tno description


","BeTs to 24 clades of COG0537COG name: Diadenosine tetraphosphate (Ap4A) hydrolase and other HIT family hydrolasesFunctional Class: F,G,RThe phylogenetic pattern of COG0537 is aompkzyq-drlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 3.9e-34) to 2/2 blocks of the IPB001310 family, which is described as \"HIT (Histidine triad) family\". Interpro entry for IP:IPR001310. IPB001310A 15-45 4.5e-16 IPB001310B 82-108 1.1e-16","Residues 6 to 46 match (2e-15) PD:PD001840 which is described as PROTEOME COMPLETE HIT-LIKE KINASE HIT HISTIDINE TRIAD C FAMILY HYDROLASE ","","","","","","","","","","","","Tue Dec 10 09:17:06 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02987 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 5 to 110 (E-value = 1.9e-52) place AA02987 in the HIT family which is described as HIT domain (PF01230)","","","","","","","","1","","","" "AA02989","2089258","2089608","351","ATGAAAAAACCAATTTCACTGTTTTTTTTGACCGCACTTTTAGCGGCCTGTAGCGCCAAAGCGCCGAATTTATTGAACACCCAAAACCCGATTCTAAACATTGAAGCCCCTGCGGCGGCAAGAGTGGAAGCCGGTGTAAACAGCGATAACGCCTGGGTGAAAAACAAAACCGGACGCATCGTAGATTTGGCTTACAGCCTGTATTGGTACGACAAAAACGGCGTTACCATCCTTGCGGAAGAACAGCCTACATGGCACGCATTGACGTTACAACCGATGCAAAAACAAACGCTGACTTTCGCCCGCCCGAGCGCCGACAGCGTCAATTATCGCTTATATCTTCGCCTGAAA","","","13061","MKKPISLFFLTALLAACSAKAPNLLNTQNPILNIEAPAAARVEAGVNSDNAWVKNKTGRIVDLAYSLYWYDKNGVTILAEEQPTWHALTLQPMQKQTLTFARPSADSVNYRLYLRLK","2089440","","conserved hypothetical protein","Periplasm, Outer membrane","","
noIPR
unintegrated
unintegrated
PD074733\"[1-115]TQ9CPG9_PASMU_Q9CPG9;
PS51257\"[1-17]TPROKAR_LIPOPROTEIN
signalp\"[1-19]?signal-peptide
tmhmm\"[5-25]?transmembrane_regions


","No hits to the COGs database.","","Residues 1 to 115 match (1e-18) PD:PD074733 which is described as PROTEOME COMPLETE PM0072 HI0960 SIGNAL PRECURSOR ","","","","","","","","","","","","Sun Dec 8 10:28:16 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02989 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 116 (E-value = 5.3e-05) place AA02989 in the DUF1425 family which is described as Protein of unknown function (DUF1425) (PF07233)","","","","","","","","1","","","" "AA02990","2089613","2090656","1044","ATGTCCACATTACTCATTGACTTAGCCGGTTACGAACTTCAACAGGAAGAAATCGAACTGCTGGAACACCCGCTGGTGGCGGGTTTAATTCTCTTCACCCGCAACTTTCACGATCGCGCGCAACTTCAAGCGCTTATCCGATCCGTACGACAAAAAGTGAAAAAACCGTTGCTGATTACCGTGGATCAGGAAGGCGGTCGGGTACAGCGTTTTCGTGAAGGCTTCACTCAAATTCCCGCCATGCAGGCGTTTTCCGCGCTGATTAAAGATCCGGCGCAACAACAGAAAATGGCGCAGGAAGCCGGCTGGCAAATGGCGGCAGAAATGACCGCACTTGATATTGATCTGAGCTTCGCGCCGGTGCTGGATCTCGGTCACCAATGCAAAGCCATCGGCGATCGCAGTTTCGGTGACGACGTCAAAAGTGCGGTGGATTTGGCAGCCAATTTTATTCGCGGCATGCACCAGGCAGGCATGGCGGCAACGGGCAAACACTTTCCCGGGCATGGGCACGTTATCGCCGATTCCCATTTGGAAACGCCTTATGACGAACGAAGCAAAGACGAGATTTTCCGGCAAGACATTCAACCGTTTCAACAACTCATTGAACAACACCTTCTGCAAGCCATCATGCCCGCTCATGTGATTTACTCGCAATGCGATAACCAACCGGCGAGCGGTTCCGCCTATTGGCTGCAAGATGTTTTACGCCATCAGCTGCATTTTAACGGTGCCATTTTCTCCGACGATCTCGGCATGAAAGGTGCCGGATTTATGGGCGATTTTGTAGCTCGCAGTGAACAGGCACTGAATGCGGGCTGCGATTTATTATTGCTTTGCAACGAACGGGACGGCGTGATTCAAGTGTTGGACCAGTTAAAACTCACGGAAAAACAACCGCACTTTTTGCTACGCCAACAGCGCTTACGACGCCTCTTCAAACGTAAAAGTTTCACTTGGTCAGAGCTGGAATCCGCGCCACGTTGGTTGGAAAATCGCGAAAAACTGACCGCACTTCAACAGCAATGGCTGGCAACCAAAGGT","","","39393","MSTLLIDLAGYELQQEEIELLEHPLVAGLILFTRNFHDRAQLQALIRSVRQKVKKPLLITVDQEGGRVQRFREGFTQIPAMQAFSALIKDPAQQQKMAQEAGWQMAAEMTALDIDLSFAPVLDLGHQCKAIGDRSFGDDVKSAVDLAANFIRGMHQAGMAATGKHFPGHGHVIADSHLETPYDERSKDEIFRQDIQPFQQLIEQHLLQAIMPAHVIYSQCDNQPASGSAYWLQDVLRHQLHFNGAIFSDDLGMKGAGFMGDFVARSEQALNAGCDLLLLCNERDGVIQVLDQLKLTEKQPHFLLRQQRLRRLFKRKSFTWSELESAPRWLENREKLTALQQQWLATKG","2090488","","beta hexosaminadase","Cytoplasm","","
InterPro
IPR001764
Domain
Glycoside hydrolase, family 3, N-terminal
PF00933\"[52-279]TGlyco_hydro_3
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.300\"[1-346]Tno description


","No hits to the COGs database.","Significant hit ( 2.1e-18) to 3/3 blocks of the IPB001764 family, which is described as \"Glycoside hydrolase family 3, N terminal\". Interpro entry for IP:IPR001764. IPB001764A 158-172 1.1e-06 IPB001764B 235-250 0.0022 IPB001764C 264-287 7.7e-05","Residues 291 to 347 match (4e-07) PD:PD362932 which is described as CELL DIVISION BETA-N-ACETYLHEXOSAMINIDASE BETA-HEXOSAMINIDASE PROTEOME GLYCOSIDASE PEPTIDOGLYCAN COMPLETE SYNTHESIS N-ACETYL-BETA-GLUCOSAMINIDASE ","","","","","","","","","","","","Sun Dec 8 10:26:10 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02990 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 52 to 279 (E-value = 6.2e-73) place AA02990 in the Glyco_hydro_3 family which is described as Glycosyl hydrolase family 3 N terminal domain (PF00933)","","","","","Yem,D.W. and Wu,H.C.Purification and properties of beta-N-acetylglucosaminidase fromEscherichia coliJ. Bacteriol. 125 (1), 324-331 (1976)PubMed: 1377Cheng,Q., Li,H., Merdek,K. and Park,J.T.Molecular characterization of the beta-N-acetylglucosaminidase ofEscherichia coli and its role in cell wall recyclingJ. Bacteriol. 182 (17), 4836-4840 (2000)PubMed: 10940025","","Sun Dec 8 10:26:10 2002","1","","","" "AA02992","2090778","2091800","1023","TTGAATACCTCCCGTTTAACGTGGTTTAAGCCGTTTCAATCACAGCCGACCGCTTTTCGCAACAAAGCCAAAATGGTGATCAGCGGCGCGGTGGAACGCCCGATTCTCGGTATTCTGCCGAATCCGCAAGCGCCACAAAGTGCGGTAGATTTGTGCGATTGCCCGCTTTACCCGCAACGCTTTCAGGCGATTTTCCCCATTCTCAAAGACTTCATCGCCCGCGCGGGACTCGTGCCCTACAACGTAGCAAAACAAAAAGGGGAACTGAAACATATTCTGCTGACGGAAAGCCAACACAGTCATCAACTGATGTTGCGTTTTGTGTTGCGCTCGGAAAGCAAACTGCCGCTGATCCGGCGGGAATTGCCGGCGTTGCGTCAAAAGCTGCCGCAACTTGCCGCTATTTTAGAAGGGGAAAAAGAGATTTTCCTCACGGAACAACACACTTTACCGGAATCGTTTAACGGCATTCCGCTGTTCATCCGCCCGCAAGGTTTCTTCCAAACCAATCCGCTGGTTGCAGAAGGATTGTATGGCACGGCGCAACAATGGGTTCAAGATCTGCCGATTAACACCCTTTGGGATTTATTTTGCGGTGTGGGCGGCTTCGGATTATATTGTTTACAAGCGCTACAACAGCGACATACGCAGAAAACCCTTCGTCTCACCGGCATTGAAATCTCCGCCTCCGCCATTGCCGCCGCCACATTATCGGCACAACAGCTTGGGCTTGCCGAACAGTTGAGTTTTCAATCTCTGGATGCGGCAAATTTTGCCTTAACCCAGGCGGAAAAACCTGATTTGATTATCGTCAACCCGCCCCGCCGTGGCGTTGGCAAGACACTCGCCGAATTCCTCAATGCAATGCAACCGCACTTTATCCTCTATTCCAGCTGCAACGCCGAAACCATGGGCAAGGACTTGCAATCCCTCACTCATTACCAGTCGGAAAAAATCCAACTGTTCGATATGTTCCCGCATACTGCCCATTATGAGGTGTTGGTGTTGTTAAAATTGCATAAA","","","42877","LNTSRLTWFKPFQSQPTAFRNKAKMVISGAVERPILGILPNPQAPQSAVDLCDCPLYPQRFQAIFPILKDFIARAGLVPYNVAKQKGELKHILLTESQHSHQLMLRFVLRSESKLPLIRRELPALRQKLPQLAAILEGEKEIFLTEQHTLPESFNGIPLFIRPQGFFQTNPLVAEGLYGTAQQWVQDLPINTLWDLFCGVGGFGLYCLQALQQRHTQKTLRLTGIEISASAIAAATLSAQQLGLAEQLSFQSLDAANFALTQAEKPDLIIVNPPRRGVGKTLAEFLNAMQPHFILYSSCNAETMGKDLQSLTHYQSEKIQLFDMFPHTAHYEVLVLLKLHK","2091632","","RNA methyltransferase","Cytoplasm, Inner membrane","","
InterPro
IPR010280
Family
(Uracil-5)-methyltransferase
PF05958\"[22-340]TtRNA_U5-meth_tr
PS01230\"[272-303]TTRMA_1
PS01231\"[322-332]TTRMA_2
InterPro
IPR011825
Family
23S rRNA (uracil-5-)-methyltransferase RumB
TIGR02085\"[3-339]Tmeth_trns_rumB: 23S rRNA (uracil-5-)-methyl
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.150\"[153-274]Tno description
PTHR11061\"[15-338]TRNA M5U METHYLTRANSFERASE FAMILY
PTHR11061:SF2\"[15-338]TRNA M5U METHYLTRANSFERASE


","No hits to the COGs database.","Significant hit ( 8.6e-35) to 4/4 blocks of the IPB001566 family, which is described as \"RNA methyltransferase trmA family\". Interpro entry for IP:IPR001566. IPB001566A 193-234 1.1e-08 IPB001566B 269-279 0.002 IPB001566C 294-303 0.0012 IPB001566D 314-337 3.1e-14","Residues 248 to 294 match (2e-10) PD:PD155875 which is described as METHYLTRANSFERASE 2.1.1.- TRANSFERASE PROTEOME COMPLETE RRNA RNA PROCESSING YBJF PM0070 ","","","","","","","","","","","","Sun Dec 8 10:04:47 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02992 is paralogously related to AA01071 (3e-16) and AA00324 (1e-09).","","","","","","","","","","","Urbonavicius J, Durand JM, Bjork GR.Three modifications in the D and T arms of tRNA influence translation in Escherichia coli and expression of virulence genes in Shigella flexneri.J Bacteriol. 2002 Oct;184(19):5348-57.PMID: 12218021Frees D, Varmanen P, Ingmer H.Inactivation of a gene that is highly conserved in Gram-positive bacteria stimulates degradation of non-native proteins andconcomitantly increases stress tolerance in Lactococcus lactis.Mol Microbiol. 2001 Jul;41(1):93-103.PMID: 11454203","","Sun Dec 8 10:13:21 2002","1","","","" "AA02993","2092868","2091906","963","ATGATTAAAAAAATTGCAGTATTAACAAGTGGTGGCGATGCCCCGGGTATGAACGCCGCAATTCGCGGTGTGGTCCGTTCAGCATTAGCCGAAGGGTTGGAAGTGTATGGTATTTACGACGGGTATCATGGTTTATATAACAATAAAATCAAACAATTAACCCGTTATAGTGTGTCCGATATTATCAATCGCGGCGGTACATTCTTAGGGTCTGCCCGTTTCCCTGAATTTAAAAATCCTGACGTGCGGGCAAAATGTGCGGAGATTTTACGCTCTCACGGCATTAATGCTTTGGTAGTTATCGGCGGTGACGGTTCCTACATGGGCGCAAAATTATTAACGGAAGAACATGGTTTCCCTTGCGTCGGTATCCCGGGCACTATCGATAACGACGTTGCCGGCACCGACTATACCATCGGCTACCAAACCGCCCTTGAAACTGCCGTTGAGGCCATCGATCGCTTACGCGACACCTCAAGTTCCCATCAACGCATCTCTATCGTCGAAATCATGGGGCGCCATTGTAGCGATCTCACTATCTCCGCAGGGATTGCCGGCGGTTGCGAATACATCGTGGCGTCAGAAATCGAATTTAATCGTGAAGAGTTAATTCGCCAAATCGAAAGAAGCATTATCAAAGGCAAACGCCACGCGATTATCGCTATTACCGAGCTTATTTGCGACGTAAACGAGTTAGCGCGCGAAATTGAAGCCCGCGTGAAACACGAAACCCGCGCCACTATTTTGGGTCATATTCAACGTGGCGGCACACCTTGTGCTTTCGACCGTATTTTAGGTTCGCGCATGGGGGTTTATGCCGTTGATTTGCTGTTACAAGGCAAAGGCGGCTACTGCGTGGGTATCCAAAACGAACAATTGGTTCACCATGACATCATCGATGCGATCAACAATATGCGCCGTGAATTCAAAGCCGATTGGTTGAATATGTCCAAACGTTTGGAT","","","35145","MIKKIAVLTSGGDAPGMNAAIRGVVRSALAEGLEVYGIYDGYHGLYNNKIKQLTRYSVSDIINRGGTFLGSARFPEFKNPDVRAKCAEILRSHGINALVVIGGDGSYMGAKLLTEEHGFPCVGIPGTIDNDVAGTDYTIGYQTALETAVEAIDRLRDTSSSHQRISIVEIMGRHCSDLTISAGIAGGCEYIVASEIEFNREELIRQIERSIIKGKRHAIIAITELICDVNELAREIEARVKHETRATILGHIQRGGTPCAFDRILGSRMGVYAVDLLLQGKGGYCVGIQNEQLVHHDIIDAINNMRREFKADWLNMSKRLD","2091738","","6-phosphofructokinase","Cytoplasm","","
InterPro
IPR000023
Family
Phosphofructokinase
PD000707\"[116-178]TK6PF_PASMU_Q9CPH2;
PR00476\"[7-26]T\"[32-45]T\"[94-110]T\"[122-139]T\"[140-158]T\"[160-176]T\"[178-195]T\"[214-226]T\"[241-263]TPHFRCTKINASE
PTHR13697\"[119-302]TPHOSPHOFRUCTOKINASE
PF00365\"[3-279]TPFK
PS00433\"[245-263]TPHOSPHOFRUCTOKINASE
InterPro
IPR012003
Family
ATP-dependent phosphofructokinase, prokaryotic
PIRSF000532\"[3-321]TATP-dependent phosphofructokinase, prokaryotic type
InterPro
IPR012828
Family
6-phosphofructokinase
TIGR02482\"[4-302]TPFKA_ATP: 6-phosphofructokinase
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.450\"[3-206]Tno description


","BeTs to 14 clades of COG0205COG name: 6-phosphofructokinaseFunctional Class: GThe phylogenetic pattern of COG0205 is ------yqvdrlbce-ghs--j-itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.9e-84) to 4/4 blocks of the IPB000023 family, which is described as \"Phosphofructokinase\". Interpro entry for IP:IPR000023. IPB000023A 3-21 3.1e-15 IPB000023B 65-102 1.2e-17 IPB000023C 139-193 2e-27 IPB000023D 243-274 2.3e-20","Residues 1 to 320 match (3e-171) PD:PD000707 which is described as KINASE TRANSFERASE PHOSPHOFRUCTOKINASE GLYCOLYSIS 6-PHOSPHOFRUCTOKINASE PHOSPHOHEXOKINASE REPEAT COMPLETE PROTEOME SUBUNIT ","","","","","","","","","","","","Sun Dec 8 09:57:32 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02993 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 3 to 279 (E-value = 4.9e-189) place AA02993 in the PFK family which is described as Phosphofructokinase (PF00365)","","","","","Sun,S., Scheffler,N.K., Gibson,B.W., Wang,J. and Munson Jr,R.S. Jr. Identification and characterization of the N-acetylglucosamine glycosyltransferase gene of Haemophilus ducreyi Infect. Immun. 70 (10), 5887-5892 (2002) PUBMED: 12228324 Kornberg HL. Routes for fructose utilization by Escherichia coli. J Mol Microbiol Biotechnol. 2001 Jul;3(3):355-9. Review. PMID: 11361065 Wu LF, Reizer A, Reizer J, Cai B, Tomich JM, Saier MH Jr. Nucleotide sequence of the Rhodobacter capsulatus fruK gene, which encodes fructose-1-phosphate kinase: evidence for a kinase superfamily including both phosphofructokinases of Escherichia coli. J Bacteriol. 1991 May;173(10):3117-27. PMID: 1850730","","Wed Jan 29 13:03:06 2003","1","","","" "AA02994","2093376","2092933","444","ATGCTGATGAATGTGGCGATTTTGATTTCCCTTGGCTTAAGCGCTTACGGGGTGTTATTGGCGGACGCGGTTTTTGCTATTTTAACCGCCCTGTATATTTTGTTGAATGCCGCCAAAATGCTGTTTGATTCGGTGCAGTTATTGTTGGATCAAATGCTGCCGTCACAGGAAATTGAGCAAATCAACGCATTGCTTACCACCGAAATCGCGGAGGATCGGCGCATTCTTGGCTTTCACGCGTTACGCACCCGACGTTCCGGCGCCATTCGTTTTATTCAGTTTCATTTGGAGTTGGCGGATGAGCTGTCATTTATTGACGCCCATGACATCACCGAACACTTGGAACGTCAATTACAGAGATTATTTCCGCGCAGCGACATTGTGATTCACCCTGAACCCACAATTGTGGTGCAACGGGAAATGCAAGTAGATAAAAAAGTGATA","","","16829","MLMNVAILISLGLSAYGVLLADAVFAILTALYILLNAAKMLFDSVQLLLDQMLPSQEIEQINALLTTEIAEDRRILGFHALRTRRSGAIRFIQFHLELADELSFIDAHDITEHLERQLQRLFPRSDIVIHPEPTIVVQREMQVDKKVI","2092765","","probable cation transport protein","Inner membrane, Cytoplasm","","
InterPro
IPR002524
Family
Cation efflux protein
PF01545\"[1-138]TCation_efflux
noIPR
unintegrated
unintegrated
signalp\"[1-37]?signal-peptide
tmhmm\"[14-34]?transmembrane_regions


","BeTs to 16 clades of COG0053COG name: Predicted Co/Zn/Cd cation transportersFunctional Class: PThe phylogenetic pattern of COG0053 is aom-kzyqvdrlbcefgh--ujx-t-Number of proteins in this genome belonging to this COG is","","Residues 34 to 133 match (2e-21) PD:PD331770 which is described as COMPLETE PROTEOME EFFLUX CATION TRANSMEMBRANE SYSTEM P34 ZINC/CADMIUM FAMILY TRANSPORTER ","","","","","","","","","","","","Sun Dec 8 09:39:15 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02994 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02996","2093844","2093509","336","ATGCCCGCTGTCGCTTATTCCGCGCAGGTGAAAAAAGCCGCGCATTTTGCCATTATTACTGCGCTGATTTTAATCTTAGCAAAAGGCATTGCCTGGTGGCAAACGGGCTCGGTCGGTATGCTTGCCTCCATAACGGATTCCATGCTGGACTTGCTGGCGTCCTTTATGAGCATGTTGATTTTGCGCTTTGCGTTAATGCCGGCGGATCATAATCATTCTTTCGGTCACGGCAAGGCGGAATCGTTGGCGTCGCTGGTGCAAAGCGCGTTTATTTCCGGTTCGGCGATTTTCCTGTTATTGCAGGGCATTCATCGTTTTAATTCACCGCAGAGGCGC","","","12081","MPAVAYSAQVKKAAHFAIITALILILAKGIAWWQTGSVGMLASITDSMLDLLASFMSMLILRFALMPADHNHSFGHGKAESLASLVQSAFISGSAIFLLLQGIHRFNSPQRR","2093341","","probable cation transport protein","Inner membrane, Cytoplasm","","
InterPro
IPR002524
Family
Cation efflux protein
PF01545\"[14-110]TCation_efflux
noIPR
unintegrated
unintegrated
signalp\"[1-31]?signal-peptide
tmhmm\"[15-33]?\"[39-61]?\"[82-100]?transmembrane_regions


","No hits to the COGs database.","Significant hit ( 1.4e-26) to 2/3 blocks of the IPB002524 family, which is described as \"Cation efflux family\". Interpro entry for IP:IPR002524. IPB002524A 24-64 6.5e-10 IPB002524B 66-105 2.9e-15","Residues 32 to 88 match (4e-08) PD:PD016506 which is described as PROTEOME COMPLETE CATION TRANSPORTER TRANSMEMBRANE MEMBRANE EFFLUX SYSTEM INNER CG8632 ","","","","","","","","","","","","Sun Dec 8 09:37:25 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02996 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02998","2094410","2093847","564","ATGAAGATAAAAAAAACACTTGGATTTTTGACCGCACTTTTTCTGGCAGCCTGTGCCTCAAAACCGCAGCTACAGGTGCCGCAAAGCCTGCAACATAATCAGAAAACCTATGATTTGGCAAGCCGGCAGGATTTGGATTCCGTTACCCGTTATTTTTATGTGCTGCCGGGCGAACAAGCGTCGAAATGGCAAAGTGCGGTGGAAATTCTGCTCGATCGTGGTGAGCAACATCGCACGCTGGAAGAGCGTGCAGAGTGGCGCAAAAAGATTTACACCAACACCGGAGTGAAGTATTTCAAGCTGGATGTAAAAGATGACGCGCTGTATTCTTATGTGATTTATGAGCCGTCGGCACAAAGTAAAGACTGGCAGGTGAATGTGGCGAAAGGCAAGAATGTAGCGCCTTGCGGGTTCGTGCAATATCAATATTCCATGAAAATTCCGCGCACCCATAAATTACGCAATATGAGCAATAAAAAAATCATCAGCCACTTGAAGAAATTCTTCGTAGATAAAGAAATGAAAAAGCTAACGCAGGCGGATTGGGCGTTGGGATGTAGAAGA","","","24835","MKIKKTLGFLTALFLAACASKPQLQVPQSLQHNQKTYDLASRQDLDSVTRYFYVLPGEQASKWQSAVEILLDRGEQHRTLEERAEWRKKIYTNTGVKYFKLDVKDDALYSYVIYEPSAQSKDWQVNVAKGKNVAPCGFVQYQYSMKIPRTHKLRNMSNKKIISHLKKFFVDKEMKKLTQADWALGCRR","2093679","","conserved hypothetical protein","Periplasm, Outer membrane","","
noIPR
unintegrated
unintegrated
PD487572\"[20-186]TQ9CPH4_PASMU_Q9CPH4;
PS51257\"[1-18]TPROKAR_LIPOPROTEIN
signalp\"[1-19]?signal-peptide


","No hits to the COGs database.","","Residues 23 to 188 match (9e-33) PD:PD105806 which is described as PROTEOME COMPLETE HI0983 ","","","","","","","","","","","","Sun Dec 8 09:34:52 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02998 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","","","","","","","","","1","","","" "AA02999","2095191","2094415","777","ATGCTCGCGATTATTTCTCCGGCAAAAACCTTAGATTTTCAGTCCGCAGTGCCGGAAAAACTCCCGAAATTTCAACCGCACTTTTTGGCGCAAAGCCAACAATTAATCGACATTTGCCGCCGCCTGACACCGGCGGATATTGCTTCGCTCATGTCTATCAGCGACAAACTTGCCGGGTTGAATGCCGCACGTTTCGCCGAATGGCAGTTGGAACATAACGAACACAATGCCAAAGCGGCGGTGTATGCCTTTAGAGGCGATGTTTACACCGGCTTGGACGTGGATTCCTTAAGCAATGACGATATGTTGTTTGCACAACAGCATTTGCGCATTTTGTCCGGGTTATATGGGCTGTTAACGCCGCTGGATTTGATTCAGCCTTATCGTTTGGAAATGGGCACCAAATTAGCCAACGGCAAAGGCGCCGATTTGTATGCCTTTTGGCATGGTTTGGTGATGCAGGCGTTACAACAGGCGATTGATGAACAACAGGACGATGTTTTGGTGAATCTGGCGTCCGATGAATATTATAAATCGGTACAACCGTCGAATTTAACGGCGCAAATCATTAAACCGGTGTTCCTGGATAATAAAAACGGCAAATATAAAATTATCAGTTTCTACGCGAAAAAAGCCCGCGGTTTAATGTGTCGTTATATTATTCAAAATCGCGTAACGGAAGTAGAGCAGTTGAAAGATTTTGACTTCGGCGGTTATTGGTTTGACAGCGCGTCCTCAAGCAAAACGGAATTTGTCTTTAAACGGGATTTGGCGGAG","","","29268","MLAIISPAKTLDFQSAVPEKLPKFQPHFLAQSQQLIDICRRLTPADIASLMSISDKLAGLNAARFAEWQLEHNEHNAKAAVYAFRGDVYTGLDVDSLSNDDMLFAQQHLRILSGLYGLLTPLDLIQPYRLEMGTKLANGKGADLYAFWHGLVMQALQQAIDEQQDDVLVNLASDEYYKSVQPSNLTAQIIKPVFLDNKNGKYKIISFYAKKARGLMCRYIIQNRVTEVEQLKDFDFGGYWFDSASSSKTEFVFKRDLAE","2094247","","conserved hypothetical protein","Cytoplasm","","
InterPro
IPR005583
Family
Protein of unknown function DUF328
PF03883\"[1-257]TDUF328


","BeTs to 6 clades of COG3022COG name: Uncharacterized BCRFunctional Class: SThe phylogenetic pattern of COG3022 is -----------l--efgh-nuj----Number of proteins in this genome belonging to this COG is","","Residues 1 to 78 match (7e-14) PD:PD337211 which is described as PROTEOME COMPLETE NMA1114 VC2355 NMB0895 ","","","","","","","","","","","","Sat Dec 7 17:41:30 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA02999 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 257 (E-value = 8.2e-156) place AA02999 in the DUF328 family which is described as Protein of unknown function (DUF328) (PF03883)","","","","","","","","1","","","" "AA03000","2095881","2095216","666","ATGAGAACCTGGAAAGATGTGATTGGACAAGAAAAACAACAGCCTTATTTTCAGCAGGTGTTGGGACGGGTGCATGCGGAGCGCGAACAGGGCAAGATTATTTACCCGCCGGCGCCGGATGTGTTTAATGCCTTTAAATTAACCGAATTTGAACAAGTGAAAGTGGTGATTTTAGGGCAGGATCCGTATCATGGTCCGAATCAAGCGCACGGTTTGTCTTTTTCCGTAAAACATGGTGTGCGTCCGCCGCCCTCTTTAGTGAATATTTATCAGGAATTGTCTAAAGACATTGAGGGTTTTCAAATTCCCAATCATGGTTGTTTGCTGGAATGGGCGCAGCAAGGCGTGTTATTGCTGAATTCGGTGTTAACCGTGGAACAAGGTCTGGCGCATTCTCATGCCAATTGGGGCTGGGAAATTTTCACCGATAAAGTGATTGAAACCTTGAATTCACAACGGGAAAATCTGGTCTTTTTATTGTGGGGCAGTCCGGCGCAGAAAAAAGGGCGGTTTATTGACAGACAAAAACATTGCGTGCTGACATCCGTGCATCCTTCGCCGTTATCCGCCCATCGCGGTTTTTTCGGTTGCCGTCATTTCTCCCAAGCCAATGCTTATTTACAACAACACCATATTACGCCGATTAACTGGCAATTAACTTCAATT","","","26080","MRTWKDVIGQEKQQPYFQQVLGRVHAEREQGKIIYPPAPDVFNAFKLTEFEQVKVVILGQDPYHGPNQAHGLSFSVKHGVRPPPSLVNIYQELSKDIEGFQIPNHGCLLEWAQQGVLLLNSVLTVEQGLAHSHANWGWEIFTDKVIETLNSQRENLVFLLWGSPAQKKGRFIDRQKHCVLTSVHPSPLSAHRGFFGCRHFSQANAYLQQHHITPINWQLTSI","2095048","","uracil-DNA glycosylase (UDG)","Cytoplasm","","
InterPro
IPR002043
Family
Uracil-DNA glycosylase
PTHR11264\"[17-220]TURACIL-DNA GLYCOSYLASE
TIGR00628\"[1-212]Tung: uracil-DNA glycosylase
PS00130\"[54-63]TU_DNA_GLYCOSYLASE
InterPro
IPR003249
Family
Uracil-DNA glycosylase, not poxvirus
PD001589\"[3-217]TUNG_PASMU_P57807;
InterPro
IPR005122
Family
Uracil-DNA glycosylase superfamily
PF03167\"[46-208]TUDG
noIPR
unintegrated
unintegrated
G3DSA:3.40.470.10\"[2-217]Tno description


","BeTs to 15 clades of COG0692COG name: Uracil DNA glycosylaseFunctional Class: LThe phylogenetic pattern of COG0692 is ------y--drlb-efghsnu--itwNumber of proteins in this genome belonging to this COG is","Significant hit ( 9.4e-80) to 5/5 blocks of the IPB002043 family, which is described as \"Uracil-DNA glycosylase\". Interpro entry for IP:IPR002043. IPB002043A 52-76 1.4e-22 IPB002043B 106-139 3.3e-23 IPB002043C 157-167 4e-05 IPB002043D 177-189 3.2e-07 IPB002043E 194-217 4.3e-16","Residues 3 to 217 match (3e-90) PD:PD001589 which is described as GLYCOSYLASE URACIL-DNA GLYCOSIDASE DNA HYDROLASE 3.2.2.- COMPLETE PROTEOME UDG REPAIR ","","","","","","","","","","","","Sat Dec 7 17:38:52 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA03000 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 48 to 208 (E-value = 5.5e-79) place AA03000 in the UDG family which is described as Uracil DNA glycosylase superfamily (PF03167)","","","","","Varshney,U., Hutcheon,T. and van de Sande,J.H. Sequence analysis, expression, and conservation of Escherichia coli uracil DNA glycosylase andits gene (ung) J. Biol. Chem. 263 (16), 7776-7784 (1988) PubMed: 2836397 Lundquist,A.J., Beger,R.D., Bennett,S.E., Bolton,P.H. and Mosbaugh,D.W. Site-directed mutagenesis and characterization of uracil-DNA glycosylase inhibitor protein. Role of specific carboxylic amino acids in complex formation with Escherichia coli uracil-DNA glycosylase J. Biol. Chem. 272 (34), 21408-21419 (1997) PubMed: 9261156 Ravishankar,R., Bidya Sagar,M., Roy,S., Purnapatre,K., Handa,P., Varshney,U. and Vijayan,M. X-ray analysis of a complex of Escherichia coli uracil DNA glycosylase (EcUDG) with a proteinaceous inhibitor. The structure elucidation of a prokaryotic UDG Nucleic Acids Res. 26 (21), 4880-4887 (1998) PubMed: 9776748 Putnam,C.D., Shroyer,M.J., Lundquist,A.J., Mol,C.D., Arvai,A.S., Mosbaugh,D.W. and Tainer,J.A. Protein mimicry of DNA from crystal structures of the uracil-DNA glycosylase inhibitor protein and its complex with Escherichia coli uracil-DNA glycosylase J. Mol. Biol. 287 (2), 331-346 (1999) PubMed: 10080896 Xiao,G., Tordova,M., Jagadeesh,J., Drohat,A.C., Stivers,J.T. and Gilliland,G.L. Crystal structure of Escherichia coli uracil DNA glycosylase and its complexes with uracil and glycerol: structure and glycosylase mechanism revisited Proteins 35 (1), 13-24 (1999) PubMed: 10090282 ","","Sat Dec 7 17:38:52 2002","1","","","" "AA03001","2096167","2096547","381","ATGATTAAAGGTATTCAAATTACCCAAGCGGCTAACGACAATCTGTTAAACTCTTTCTGGTTGTTAGATAGCGAAAAAGGTGAAGCTCGTTGTTTATGTGCAAAAGGCGATTACGCTGAAGACCAAGTGGTTGCAGTAAGTGAACTTGGTAAAATCGAATATCGCGAATTGCCGGTAGATGTTGCACCAACCGTTAAAGTGGAAGGCGGTCAACACTTAAACGTTAACGTATTACGTCGTGAAACATTAGAAGATGCGGTGAAACACCCTGAAAAATATCCGCAATTAACCATCCGTGTTTCCGGTTATGCCGTACGTTTCAACTCTTTAACACCGGAACAACAACGCGACGTTATCACCCGTACTTTCACTGAAAGCCTA","","","14272","MIKGIQITQAANDNLLNSFWLLDSEKGEARCLCAKGDYAEDQVVAVSELGKIEYRELPVDVAPTVKVEGGQHLNVNVLRRETLEDAVKHPEKYPQLTIRVSGYAVRFNSLTPEQQRDVITRTFTESL","2096379","","probable glycyl radical protein/pyruvate-formate lyase","Cytoplasm","","
InterPro
IPR001150
Domain
Formate C-acetyltransferase glycine radical
PF01228\"[3-108]TGly_radical
PS51149\"[5-127]TGLY_RADICAL_2
PS00850\"[97-105]TGLY_RADICAL_1
InterPro
IPR011140
Family
Glycyl radical cofactor protein YfiD
PIRSF000378\"[2-127]TGlycyl radical cofactor protein YfiD
noIPR
unintegrated
unintegrated
G3DSA:3.20.70.20\"[66-127]Tno description


","No hits to the COGs database.","Significant hit ( 7.9e-38) to 2/2 blocks of the IPB001150 family, which is described as \"Pyruvate formate-lyase, glycine radical\". Interpro entry for IP:IPR001150. IPB001150A 28-38 5.2 IPB001150B 76-125 1.7e-36","Residues 1 to 26 match (5e-09) PD:PD076814 which is described as COMPLETE PROTEOME RADICAL FORMATE ORGANIC TRANSFERASE YFID ACETYLTRANSFERASE PM0064 ACETYL ","","","","","","","","","","","","Sat Dec 7 17:00:56 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA03001 is paralogously related to AA02983 (2e-24).","","","","","","Residues 3 to 108 (E-value = 6.3e-47) place AA03001 in the Gly_radical family which is described as Glycine radical (PF01228)","","","","","Lehtio L, Leppanen VM, Kozarich JW, Goldman A.Structure of Escherichia coli pyruvate formate-lyase with pyruvate.Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2209-12.PMID: 12454503","","Sat Dec 7 17:05:37 2002","1","","","" "AA03002","2096563","2096694","132","TTGAAAAGAAACCCCGAAGCGATTCGGGGTTTTATTTTTTCAAAACGCCGAAAAAAACGACCGCACTTTTCTTTTCTAGCGATTCCCATGCTTTTCAGGTACAATCCGCCAGTTAAATTTAATGACTTTTTA","","","5377","LKRNPEAIRGFIFSKRRKKRPHFSFLAIPMLFRYNPPVKFNDFL","2096694","","hypothetical protein","Periplasm, Cytoplasm","There are no significant similarities to the NR database.","
noIPR
unintegrated
unintegrated
tmhmm\"[21-36]?transmembrane_regions


","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 09:17:12 2004","Mon Feb 23 09:17:12 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA03002 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 09:18:05 2004","","","","","","","","","","","","","1","","","" "AA03003","2096684","2098507","1824","ATGACTTTTTATGAGAAAACTTACCTAGTTATGAAGAATATTCGCAACTTTTCCATTATTGCCCATATTGACCACGGTAAATCCACCTTATCGGATCGTTTAATCCAGACCTGCGGCGGGTTATCCGATCGCGAAATGGCGGAGCAGGTGCTGGATTCCATGGATCTTGAACGTGAGCGCGGGATCACCATTAAAGCGCAAAGCGTGACCTTAAATTACAACGCCAAAGACGGCGAAACTTATCAACTTAACTTTATCGACACCCCGGGGCACGTTGACTTTTCTTATGAAGTGTCCCGTTCCCTCGCCGCTTGTGAAGGTGCATTGTTAGTGGTGGATGCCGGGCAAGGTGTGGAAGCGCAAACTTTAGCGAACTGTTACACCGCCATTGAAATGAATTTGGAAGTGGTACCAATTTTAAACAAAATCGACCTGCCTGCCGCCGAACCTGAACGCGTGGCGGAAGAAATTGAAGACATTGTAGGTATTGATGCCATTGATGCGGTGCGCTGCTCCGCCAAAACCGGCGTGGGCATTGAAGACGTATTGGAAGAAATCGTGGCGAAAATCCCGGCACCCGAAGGAGATCCGAACGCACCGTTACAAGCCTTGATTATCGATTCCTGGTTTGACAATTATTTGGGCGTGGTGTCCTTGGTACGAATTAAAAACGGCACATTACGCAAAGGTGATAAAATCAAAGTGATGTCCACCGGGCAATCGTATAACGTGGATCGCTTGGGGATTTTCACCCCGAAACAAATGGATACCAACGTGTTAAATTGCGGCGAAGTGGGCTGGGTGGTATGTGCCATTAAAGACATCTTAGGTGCGCCGGTAGGCGATACGTTGACCCTACATAATCATCCTGCAAGTTCCGTACTACCGGGCTTTAAAAAAGTGAAGCCACAGGTTTACGCGGGGCTTTTCCCAATCAGTTCCGATGATTACGAAGCCTTCCGTGACGCGTTAGGTAAGTTAAGCCTTAACGATGCTTCTCTGTTCTATGAACCGGAAAATTCCACCGCACTTGGTTTCGGTTTCCGTTGTGGTTTCCTTGGGCTGTTGCACATGGAAATCATTCAGGAGCGCCTGGAACGAGAATATGATTTGGATTTAATCACCACCGCGCCGACCGTAGTCTATGAAGTCGAACTTACCAATGGCGAGGTAGTCTATGTAGATAGCCCGTCAAAACTGCCGCCGTTAAACAATATCGCGGAGATTCGCGAGCCGATTGCGGAATGTAATATGCTGTTACCGCAAACCTATTTAGGCAATGTGATTACCCTGTGCGTGGAAAAACGCGGGGTACAGACCCACATGGTGTATCACGGCAATCAAGTGGCGCTTACCTATGAAATCCCGATGGGCGAAGTAGTGCTGGATTTCTTCGACCGCTTAAAATCCACCTCACGCGGTTATGCGTCTTTGGATTACGGTTTCAAACGCTTCCAGGCGGCGGACATGGTTCGCGTGGATATTATGATCAATGGCGAACGCGTGGATGCCTTGGCGTTAATCGTACACAAAGACAACGCGCCGTATCGCGGTCGTGAATTGGTAGAAAAAATGCGTGAGTTAATCCCGCGCCAGCAATTTGATATTGCCATTCAGGCTGCCATCGGCAATCACATTATCGCCCGTTCTACAGTGAAACAATTGCGTAAAAACGTTTTGGCGAAGTGTTATGGCGGCGACGTGAGCCGTAAGAAGAAATTGTTGCAAAAACAAAAAGAAGGTAAGAAACGCATGAAACAACTGGGTAACGTGGAAGTGCCGCAAGAAGCCTTCTTAGCCATCTTGCACGTTGGAAAAGACAAG","","","67465","MTFYEKTYLVMKNIRNFSIIAHIDHGKSTLSDRLIQTCGGLSDREMAEQVLDSMDLERERGITIKAQSVTLNYNAKDGETYQLNFIDTPGHVDFSYEVSRSLAACEGALLVVDAGQGVEAQTLANCYTAIEMNLEVVPILNKIDLPAAEPERVAEEIEDIVGIDAIDAVRCSAKTGVGIEDVLEEIVAKIPAPEGDPNAPLQALIIDSWFDNYLGVVSLVRIKNGTLRKGDKIKVMSTGQSYNVDRLGIFTPKQMDTNVLNCGEVGWVVCAIKDILGAPVGDTLTLHNHPASSVLPGFKKVKPQVYAGLFPISSDDYEAFRDALGKLSLNDASLFYEPENSTALGFGFRCGFLGLLHMEIIQERLEREYDLDLITTAPTVVYEVELTNGEVVYVDSPSKLPPLNNIAEIREPIAECNMLLPQTYLGNVITLCVEKRGVQTHMVYHGNQVALTYEIPMGEVVLDFFDRLKSTSRGYASLDYGFKRFQAADMVRVDIMINGERVDALALIVHKDNAPYRGRELVEKMRELIPRQQFDIAIQAAIGNHIIARSTVKQLRKNVLAKCYGGDVSRKKKLLQKQKEGKKRMKQLGNVEVPQEAFLAILHVGKDK","2098339","","GTP-binding membrane protein","Cytoplasm","","
InterPro
IPR000178
Family
Initiation factor 2
PD186100\"[162-233]TQ72KE8_THET2_Q72KE8;
InterPro
IPR000640
Domain
Translation elongation factor EFG/EF2, C-terminal
G3DSA:3.30.70.240\"[411-500]Tno description
PF00679\"[408-496]TEFG_C
InterPro
IPR000795
Domain
Protein synthesis factor, GTP-binding
PR00315\"[16-29]T\"[59-67]T\"[84-94]T\"[100-111]T\"[136-145]TELONGATNFCT
PF00009\"[12-194]TGTP_EFTU
PS00301\"[52-67]TEFACTOR_GTP
InterPro
IPR004161
Domain
Translation elongation factor EFTu/EF1A, domain 2
PF03144\"[215-285]TGTP_EFTU_D2
InterPro
IPR005225
Domain
Small GTP-binding protein domain
TIGR00231\"[12-188]Tsmall_GTP: small GTP-binding protein domain
InterPro
IPR006297
Family
GTP-binding protein LepA
TIGR01393\"[12-605]TlepA: GTP-binding protein LepA
InterPro
IPR013842
Domain
GTP-binding protein LepA, C-terminal
PF06421\"[497-605]TLepA_C
noIPR
unintegrated
unintegrated
G3DSA:2.40.30.10\"[195-290]Tno description
G3DSA:3.40.50.300\"[7-195]Tno description
PTHR23115\"[11-318]TTRANSLATION FACTOR
PTHR23115:SF40\"[11-318]TGTP-BINDING PROTEIN LEPA


","BeTs to 19 clades of COG0481COG name: Membrane GTPase LepAFunctional Class: NThe phylogenetic pattern of COG0481 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.4e-48) to 6/6 blocks of the IPB000640 family, which is described as \"Elongation factor G, C-terminus\". Interpro entry for IP:IPR000640. IPB000640A 14-39 2.2e-14 IPB000640B 51-73 2.5e-08 IPB000640C 83-110 3.3e-15 IPB000640D 117-145 0.024 IPB000640E 182-193 2.9e+02 IPB000640F 405-439 0.057Significant hit ( 9.3e-27) to 3/3 blocks of the IPB000795 family, which is described as \"GTP-binding elongation factor\". Interpro entry for IP:IPR000795. IPB000795A 16-31 2.4e-07 IPB000795B 86-117 1.6e-15 IPB000795C 121-145 1.1Significant hit ( 8.3e-18) to 4/8 blocks of the IPB000178 family, which is described as \"Initiation factor 2\". Interpro entry for IP:IPR000178. IPB000178A 13-51 15 IPB000178B 83-115 3.2e-07 IPB000178C 116-155 0.00021 IPB000178E 215-267 0.33Significant hit ( 2e-05) to 3/5 blocks of the PR00449 family, which is described as \"Transforming protein P21 RAS signature\". Prints database entry for PR:PR00449. PR00449C 74-96 17 PR00449D 132-145 1.1e+02 PR00449E 168-190 0.0043","Residues 14 to 95 match (3e-09) PD:PD196535 which is described as GTP-BINDING NUCLEAR U5 BIOSYNTHESIS RIBONUCLEOPROTEIN SMALL SPLICING COMPONENT MRNA PROTEIN ","","","","","","","","","","","","Sat Dec 7 16:57:19 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA03003 is paralogously related to AA02344 (2e-39), AA01922 (4e-19), AA01852 (6e-19), AA00564 (1e-18), AA00931 (1e-13), AA00563 (1e-13) and AA00892 (2e-08).","","","","","","Residues 497 to 605 (E-value = 6.9e-81) place AA03003 in the LepA_C family which is described as GTP-binding protein LepA C-terminus (PF06421)","","","","","March,P.E. and Inouye,M. Characterization of the lep operon of Escherichia coli. Identification of the promoter and thegene upstream of the signal peptidase I gene. J. Biol. Chem. 260(12): 7206-7213, 1985. PubMed: 2987248. March,P.E. and Inouye,M. GTP-binding membrane protein of Escherichia coli with sequence homology to initiation factor 2and elongation factors Tu and G. Proc. Natl. Acad. Sci. U.S.A. 82(22): 7500-7504, 1985. PubMed: 2999765.","","Sat Dec 7 16:57:19 2002","1","","","" "AA03004","2098521","2099540","1020","ATGTCGAATTTATTTACAATTATTTTAATCGCTGTCGGATATGGTTTATGGAAGCTATTGGATCATTTCCAACTGCCTAACACCTTTTCAATTTTACTGATTATTTTCACCGCACTTTCCGGCGTGGTTTGGTGTTATCTGCGTTTTGGCGTATTGCCGAAACGCGCCAGACAAATAAGTCGGTTAGAACAACGCAGTGGAAAAACCTTAACGGATGAAGAAAAAGCGCAAATCGAACCGATTTCCGAAAGTGCCGAATTTACGGCGTCACTCTTTCCGGTGTTGGCGTTTGTGTTAATTATTCGCTCCTTTGTGTTCGAACCGTTCCAAATCCCTTCTTCGTCAATGGAACCGACCTTACGCATAGGCGATTTTATTGTGGTGAATAAATTTGACTATGGCATTAAAGATCCCGTCTTCCAAAACACTTTAATCAAAATGGGCAAACCGCAACGCGGTGACGTGATCGTGTTCAAAGCGCCGGAATCCCCAAGCGTAGACTACATTAAACGTGTTGTCGGCACGCCGGGCGATCGGGTCATTTATAATGATGTCAACCGTCACCTCACCATCATTTACGGTAAAGACGGCAAAGAATGCCTCACCGACTGCATCACCAAAGAGTTTAGTTACACCCAGCCGCAACCGAATGAAAATTTCCGTTTCATCTTAGGACGTGATTACGCAGGCAAGATTGTTTATGGCCCTTCCCCGTTGGAAACTATCGAAAGCGGCGATGTTTCCCATGCGATTCATTGGGCACCTGAAGTGAGAAATGAAAGTTTCCGCTATAAAGCCTTTGATAAACAGGACAATTACGTAACCGAATGGGTTGTGCCAGAAAATCACTATTTCGTGATGGGCGACAATCGCAACAACAGCGAAGACAGCCGTTTTTGGGGCTTTGTACCGGAACAAAATATCGTCGGCAAAGCCACCTACATTTGGCTGAGTTTGAAGAAAGAACAGGATGAATGGCCGACCGGCGTACGCACCGAACGGTTGTTCCAAAAAATCCAA","","","40149","MSNLFTIILIAVGYGLWKLLDHFQLPNTFSILLIIFTALSGVVWCYLRFGVLPKRARQISRLEQRSGKTLTDEEKAQIEPISESAEFTASLFPVLAFVLIIRSFVFEPFQIPSSSMEPTLRIGDFIVVNKFDYGIKDPVFQNTLIKMGKPQRGDVIVFKAPESPSVDYIKRVVGTPGDRVIYNDVNRHLTIIYGKDGKECLTDCITKEFSYTQPQPNENFRFILGRDYAGKIVYGPSPLETIESGDVSHAIHWAPEVRNESFRYKAFDKQDNYVTEWVVPENHYFVMGDNRNNSEDSRFWGFVPEQNIVGKATYIWLSLKKEQDEWPTGVRTERLFQKIQ","2099372","","signal peptidase I (SPase I)","Inner membrane, Cytoplasm","","
InterPro
IPR000223
Family
Peptidase S26A, signal peptidase I
PR00727\"[104-120]T\"[168-180]T\"[279-298]TLEADERPTASE
TIGR02227\"[87-320]Tsigpep_I_bact: signal peptidase I
PS00501\"[113-120]?SPASE_I_1
PS00760\"[170-182]TSPASE_I_2
PS00761\"[284-297]TSPASE_I_3
InterPro
IPR006198
Domain
Peptidase S24, S26A and S26B
PF00717\"[110-196]TPeptidase_S24
InterPro
IPR011056
Domain
Peptidase S24 and S26, C-terminal region
G3DSA:2.10.109.10\"[99-339]Tno description
InterPro
IPR014037
Family
Peptidase S26A
PTHR12383\"[94-198]T\"[277-321]TPROTEASE FAMILY S26 MITOCHONDRIAL INNER MEMBRANE PROTEASE-RELATED
noIPR
unintegrated
unintegrated
PTHR12383:SF1\"[94-198]T\"[277-321]TSIGNAL PEPTIDASE I
signalp\"[1-45]?signal-peptide
tmhmm\"[27-47]?transmembrane_regions


","BeTs to 20 clades of COG0681COG name: Signal peptidase IFunctional Class: NThe phylogenetic pattern of COG0681 is aompkzyqvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 2.5e-49) to 4/4 blocks of the IPB000508 family, which is described as \"Signal peptidase\". Interpro entry for IP:IPR000508. IPB000508A 98-128 4.4e-19 IPB000508B 148-159 1.3e-05 IPB000508C 168-178 1.6e-05 IPB000508D 279-298 1.2e-14","Residues 1 to 100 match (2e-38) PD:PD408686 which is described as I PROTEOME COMPLETE PEPTIDASE LEADER TRANSMEMBRANE SPASE PROTEASE MEMBRANE INNER ","","","","","","","","","","","","Sat Dec 7 16:47:32 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA03004 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 76 to 310 (E-value = 1.5e-60) place AA03004 in the Peptidase_S26 family which is described as Signal peptidase I (PF00461)","","","","","Black,M.T. Evidence that the catalytic activity of prokaryote leader peptidase depends upon the operationof a serine-lysine catalytic dyad. J. Bacteriol. 175(16): 4957-4961, 1993. PubMed: 8394311. Black,M.T., Munn,J.G. and Allsop,A.E. On the catalytic mechanism of prokaryotic leader peptidase 1. Biochem. J. 282(Pt 2): 539-543,1992. PubMed: 1546969. Paetzel,M., Dalbey,R.E. and Strynadka,N.C. Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor Nature 396 (6707), 186-190 (1998) PubMed: 9823901 Sung,M. and Dalbey,R.E.Identification of potential active-site residues in theEscherichia coli leader peptidase. J. Biol. Chem. 267(19): 13154-13159, 1992. PubMed: 1618816. Bilgin,N., Lee,J.I., Zhu,H.Y., Dalbey,R. and von Heijne,G. Mapping of catalytically important domains in Escherichia coli leader peptidase. EMBO J. 9(9): 2717-2722, 1990. PubMed: 2202591. van Dijl JM, van den Bergh R, Reversma T, Smith H, Bron S, Venema G. Molecular cloning of the Salmonella typhimurium lep gene in Escherichia coli. Mol. Gen. Genet. 223 (2), 233-240, 1990. PubMed: . Wolfe PB, Wickner W, Goodman JM. Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope. J. Biol. Chem. 258 (19) 12073-12080,, 1983. PubMed: .","","Sat Dec 7 16:55:30 2002","1","","","" "AA03006","2099550","2100227","678","ATGAAAGAAAATCAATTAGAACGTTTACAACGTCAAATTAACTACAGGTTCCAAAATATCGAGTTGCTTAAACAGGCTTTAACCCATCGTAGCGCCGGACATCAACACAATGAGCGGTTGGAATTTTTAGGCGATGCCATTTTGAATTTAACCATCGGCGAAGCCTTGTTCCATCAATTCCCGAAATGTAACGAAGGGGAATTGAGCCGTATGCGTGCCACCTTGGTGCGCGAACCGACCCTTGCCCTTCTGGCGCGGGATTTTAAGCTGGGTGATTATATTTTGCTCGGTCAAGGGGAATTAAAAAGTGGCGGTTTCCGCCGTGAATCTATTCTGGCGGATTGCGTGGAAGCCATTATCGGCGCGATTTCACTGGACAGCAATCTGACAAATGCCACACAAATTGTGTGTCAGTGGTATCAGAATTTATTGAAAGAAATTAAACCGGGCGACAATCAAAAAGATGCGAAAACCCGCTTGCAGGAATATTTACAAGGCAATCGCCTGCCTTTGCCGACATACAATATCGTGAATATTCAAGGAGAAGCCCATAATCAATTGTTCATCGTGGAATGTTCCATCCAAAATAGTGACCGCACTTTTATCGGTAAAGGCTCCAGTCGTCGTAAAGCGGAACAGGCGGCGGCAGAACAAATTTTACAAGAGTTGAATATCAAA","","","25713","MKENQLERLQRQINYRFQNIELLKQALTHRSAGHQHNERLEFLGDAILNLTIGEALFHQFPKCNEGELSRMRATLVREPTLALLARDFKLGDYILLGQGELKSGGFRRESILADCVEAIIGAISLDSNLTNATQIVCQWYQNLLKEIKPGDNQKDAKTRLQEYLQGNRLPLPTYNIVNIQGEAHNQLFIVECSIQNSDRTFIGKGSSRRKAEQAAAEQILQELNIK","2100059","","ribonuclease III","Cytoplasm","","
InterPro
IPR000999
Domain
Ribonuclease III
G3DSA:1.10.1520.10\"[4-147]Tno description
PF00636\"[38-128]TRibonuclease_3
SM00535\"[21-149]TRIBOc
PS50142\"[6-128]TRNASE_3_2
PS00517\"[38-46]TRNASE_3_1
InterPro
IPR001159
Domain
Double-stranded RNA binding
PF00035\"[156-223]Tdsrm
SM00358\"[156-224]TDSRM
PS50137\"[155-225]TDS_RBD
InterPro
IPR011907
Family
Ribonuclease III, bacterial
TIGR02191\"[9-223]TRNaseIII: ribonuclease III
InterPro
IPR014720
Domain
Double-stranded RNA-binding-like
G3DSA:3.30.160.20\"[154-226]Tno description
noIPR
unintegrated
unintegrated
PTHR11207\"[5-225]TRIBONUCLEASE III


","BeTs to 18 clades of COG0571COG name: dsRNA-specific ribonucleaseFunctional Class: KThe phylogenetic pattern of COG0571 is ------yqvdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 1.9e-71) to 6/6 blocks of the IPB000999 family, which is described as \"Ribonuclease III family\". Interpro entry for IP:IPR000999. IPB000999A 22-31 1.1e-05 IPB000999B 37-73 2e-29 IPB000999C 110-128 6.5e-11 IPB000999D 155-174 2.8e-10 IPB000999E 180-190 0.042 IPB000999F 205-216 1.4e-05","Residues 146 to 209 match (7e-10) PD:PD479860 which is described as III RIBONUCLEASE COMPLETE PROTEOME HYDROLASE ENDONUCLEASE NUCLEASE RNASE RNA-BINDING SLR0346 ","","","","","","","","","","","","Sat Dec 7 16:45:07 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA03006 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 156 to 223 (E-value = 6.1e-22) place AA03006 in the dsrm family which is described as Double-stranded RNA binding motif (PF00035)","","","","","Powell,B.S., Peters,H.K., Nakamura,Y. and Court,D.L. . Cloning and analysis of the rnc-era-recO operon from Pseudomonas aeruginosa. J. Bacteriol 181(16): 5111-3.1999 PubMed: . Binnie U, Wong K, McAteer S, Masters M. Absence of RNASE III alters the pathway by which RNAI, the antisense inhibitor of ColE1replication, decays. Microbiology 145 ( Pt 11):3089-100.1999 PubMed: . Franch T, Thisted T, Gerdes K.. Ribonuclease III processing of coaxially stacked RNA helices. J Biol Chem 274(37):26572-8. 1999 PubMed: . Takiff,H.E., Chen,S.M. and Court,D.L. Genetic analysis of the rnc operon of Escherichia coli. J.Bacteriol. 171(5): 2581-2590.1989. PubMed: 2540151. Nashimoto,H. and Uchida,H. . DNA sequencing of the Escherichia coli ribonuclease III gene and its mutations. Mol. Gen. Genet. 201(1): 25-29.1985 PubMed: . March,P.E., Ahnn,J. and Inouye,M. The DNA sequence of the gene (rnc) encoding ribonuclease III of Escherichia coli. Nucleic Acids Res. 13(13): 4677-4685.1985 PubMed: 3895158.","","Sat Dec 7 16:45:07 2002","1","","","" "AA03008","2100227","2101132","906","ATGAGCGAACAACAAAACCAAACTTACTGCGGCTTTATTGCTATCGTCGGTCGTCCGAATGTAGGCAAATCCACCCTGCTGAATAAAATCCTCGGACAAAAAATCTCCATCACCTCACGCAAAGCCCAAACCACCCGCCACCGCATTGTGGGCATTAAAACCGAAGGTGCGTATCAAGAAATTTACGTGGACACCCCGGGGTTGCATATTGAAGAAAAACGCGCCATCAATCGCCTGATGAACCGCGCCGCCAGCAGTGCTATCAGCGATGTGGAGTTGGTGATTTTCGTGGTGGACGGCACACACTGGAACGACGATGATGAAATGGTGCTAAACAAACTGCGCAAAACCAAAGCGCCGGTGGTGCTCGCCATTAATAAAATCGACAACATTAAAAACAAGGACGATTTGCTGCCGTTTATCACCGAAATCAGCAGCAAATTTAATTTCGCCGACGTCGTGCCGATTTCGGCTGAAAAAGGCAATAACATTAATGTGCTTGAACAAATCGTGCGCAAATCACTCCGCCCCGGCATACACCATTTCCCGGAAGATTACGTCACCGATCGTTCTCAACGTTTCATGGCATCGGAAATTATCCGCGAAAAACTCATGCGTTTTATGGGCGAGGAATTGCCTTATTCCGTCACGGTGGAAATTGAACAATTTAAAGTCAATGAACGCGGCACTTACGAAATTAACGGTTTAATTTTAGTGGAACGGGACGGTCAGAAAAAAATCGTCATCGGGCATAAAGGTGAAAAGCTGAAAAAAATCGGCACCGAAGCCCGCCTTGATATGGAACGCTTATTTGACAACAAAGTCCATCTGGAGCTTTGGGTGAAAGTGAAATCCGGCTGGGCGGATGATGAACGTGCCCTACGCAGTTTGGGCTATATGGAAGAT","","","34508","MSEQQNQTYCGFIAIVGRPNVGKSTLLNKILGQKISITSRKAQTTRHRIVGIKTEGAYQEIYVDTPGLHIEEKRAINRLMNRAASSAISDVELVIFVVDGTHWNDDDEMVLNKLRKTKAPVVLAINKIDNIKNKDDLLPFITEISSKFNFADVVPISAEKGNNINVLEQIVRKSLRPGIHHFPEDYVTDRSQRFMASEIIREKLMRFMGEELPYSVTVEIEQFKVNERGTYEINGLILVERDGQKKIVIGHKGEKLKKIGTEARLDMERLFDNKVHLELWVKVKSGWADDERALRSLGYMED","2100964","","GTP-binding protein era homolog (GTPase)","Cytoplasm","","
InterPro
IPR002917
Domain
GTP-binding protein, HSR1-related
PF01926\"[11-129]TMMR_HSR1
InterPro
IPR004044
Domain
KH, type 2
PF07650\"[235-299]TKH_2
PS50823\"[208-285]TKH_TYPE_2
InterPro
IPR005225
Domain
Small GTP-binding protein domain
TIGR00231\"[8-173]Tsmall_GTP: small GTP-binding protein domain
InterPro
IPR005289
Domain
GTP-binding
TIGR00650\"[16-49]TMG442: GTP-binding conserved hypothetical p
InterPro
IPR005662
Family
GTP-binding protein Era
TIGR00436\"[11-282]Tera: GTP-binding protein Era
InterPro
IPR006073
Domain
GTP1/OBG
PR00326\"[13-33]T\"[81-99]TGTP1OBG
InterPro
IPR009019
Domain
KH, prokaryotic type
G3DSA:3.30.300.20\"[191-299]Tno description
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[3-186]Tno description
PTHR11649\"[5-294]TMSS1/TRME-RELATED GTP-BINDING PROTEIN
PTHR11649:SF3\"[5-294]TGTP-BINDING PROTEIN ERA


","No hits to the COGs database.","Significant hit ( 9.2e-17) to 1/1 blocks of the IPB000765 family, which is described as \"GTP1/OBG family\". Interpro entry for IP:IPR000765. IPB000765 11-54 8.7e-17","Residues 149 to 279 match (6e-07) PD:PD260909 which is described as GTP-BINDING CG7488 II E02H1.2 CHROMOSOME ","","","","","","","","","","","","Sat Dec 7 16:36:58 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA03008 is paralogously related to AA00689 (2e-11), AA03010 (2e-06) and AA01922 (2e-05).","","","","","","Residues 13 to 195 (E-value = 8.5e-06) place AA03008 in the GTP_EFTU family which is described as Elongation factor Tu GTP binding domain (PF00009)","","","","","Anderson,P.E., Matsunaga,J., Simons,E.L. and Simons,R.W. Structure and regulation of theSalmonella typhimurium rnc-era-recO operon. Biochimie 78(11-12): 1025-1034, 1996. PubMed: 9150881. Lerner,C.G., Gulati,P.S. and Inouye,M. Cold-sensitive conditional mutations in Era, an essential Escherichia coli GTPase, isolated bylocalized random polymerase chain reaction mutagenesis. FEMS Microbiol. Lett. 126(3): 291-298, 1995. PubMed: 7729673. Sood,P., Lerner,C.G., Shimamoto,T., Lu,Q. and Inouye,M. Characterization of theautophosphorylation of Era, an essential Escherichia coli GTPase. Mol. Microbiol. 12(2): 201-208, 1994. PubMed: 8057845. Lerner,C.G., Sood,P., Ahnn,J. and Inouye,M. Cold-sensitive growth and decreased GTP-hydrolytic activity from substitution of Pro17 for Valin Era, an essential Escherichia coli GTPase. FEMS Microbiol. Lett. 74(2-3): 137-142,1992. PubMed: 1526446.","","Sat Dec 7 16:36:58 2002","1","","","" "AA03009","2101141","2101296","156","GTGGGCATAACGCTCACCTTTTTATATGCCGAATGGATACGCCGACACACCCAAAGTGCGGTAGAAAAAACACCTGAAATTTCGACCGCACTTTTGCCTTATTTGCCGATACAAAACGAACTGAAAATATTCGTCAGCAAATCGTCAGAGGTAAAT","","","5915","VGITLTFLYAEWIRRHTQSAVEKTPEISTALLPYLPIQNELKIFVSKSSEVN","2101296","","hypothetical protein","Cytoplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 09:13:49 2004","Mon Feb 23 09:13:49 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA03009 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 09:13:49 2004","","","","","","","","","","","","","1","","","" "AA03010","2102594","2101242","1353","ATGAAAGAAACAATCGTAGCACAAGCCACAGCCCCGGGGCGCGGCGGAATCGGCATTTTGCGTGTATCCGGTCCTAAAGCCATTGAGGTGGCGCAAGCGGTGTTGGGGAAATGCCCGAAACCGCGTATGGCGGATTATTTGCCTTTTAAAGAGGCGGACGGAACCGTTTTGGATCAGGGCATTGCACTGTATTTTAAAGGACCGAATTCCTTTACCGGCGAAGATGTGCTGGAACTTCAAGGACACGGCGGGCAGGTTGTGCTGGATTTGCTGTTAAAGCGGATTTTGCGCATTGAAGGCATTCGTTTGGCACGTCCGGGCGAGTTTTCCGAACAGGCATTTTTGAACGATAAACTGGATTTGGCGCAAGCGGAAGCTATCGCCGATTTAATTGATGCCAGTTCCGAGCAGGCAGCGCGTTCGGCGTTAAAATCCTTGCAGGGCGAATTTTCCAATAAGGTAAATCAGTTGGTGGATTCGGTGATTTACCTGCGCACGTATGTGGAGGCTGCGATTGACTTCCCCGATGAAGAAATCGATTTCCTCGCCGACGGCAAAATCGAAGGGCACTTGAATGATATTATCGCGCAGCTGGACAAGGTTCGCGCCGAAGCAAAACAAGGTTCGATTTTACGCGAAGGCATGAAAGTGGTGATCGCAGGTCGTCCGAATGCAGGCAAGTCCAGCTTGTTGAACACTCTTGCCGGGCGGGAAGCGGCGATTGTAACCGACATTGCGGGAACGACGCGCGACGTATTACGTGAGCACATTCATTTGGACGGAATGCCGTTGCATATTATTGATACTGCAGGGCTACGCGATGCCACCGATGAAGTGGAGCGCATCGGTATTTCCCGTGCATGGCATGAAATCGAGCAGGCGGATCGCATTTTGTTGATGTTGGATAGCAGCGATACGGAACAGGATTTGGCAAAAGTGCGGTCGGAATTTTTGGCAAAATTACCGAACAACATTCCGCTGACCATTATTCGTAATAAAGCGGATTTAAGCGGCGAAGCGGAACGTTTATATGAAGAAGATGGCTATACTGTGGTGAATTTGTCGGCGAAAACCCAGCAGGGCGTAGATTTATTACGTGATCATTTAAAACAGGCGATGGGCTATCAAACAGGTATGGAAGGCGGTTTCCTGGCGCGTCGTCGTCATTTGGAAGCGTTGGAATTGGCGGCGCGACATTTGCAAATGGGGCATGTTCAATTAACCCAATTCCATGCGGGTGAATTATTGGCGGAAGAACTACGTATGGTGCAAAGCGCGTTAAGTGAAATTACCGGTCAATTTACCTCTGACGATTTGCTGACGAATATTTTCAGTTCGTTTTGTATCGGCAAA","","","49337","MKETIVAQATAPGRGGIGILRVSGPKAIEVAQAVLGKCPKPRMADYLPFKEADGTVLDQGIALYFKGPNSFTGEDVLELQGHGGQVVLDLLLKRILRIEGIRLARPGEFSEQAFLNDKLDLAQAEAIADLIDASSEQAARSALKSLQGEFSNKVNQLVDSVIYLRTYVEAAIDFPDEEIDFLADGKIEGHLNDIIAQLDKVRAEAKQGSILREGMKVVIAGRPNAGKSSLLNTLAGREAAIVTDIAGTTRDVLREHIHLDGMPLHIIDTAGLRDATDEVERIGISRAWHEIEQADRILLMLDSSDTEQDLAKVRSEFLAKLPNNIPLTIIRNKADLSGEAERLYEEDGYTVVNLSAKTQQGVDLLRDHLKQAMGYQTGMEGGFLARRRHLEALELAARHLQMGHVQLTQFHAGELLAEELRMVQSALSEITGQFTSDDLLTNIFSSFCIGK","2101074","","thiophene and furan oxidation protein","Cytoplasm","","
InterPro
IPR001806
Family
Ras GTPase
PR00449\"[215-236]T\"[323-336]TRASTRNSFRMNG
InterPro
IPR002917
Domain
GTP-binding protein, HSR1-related
PF01926\"[215-335]TMMR_HSR1
InterPro
IPR004520
Family
tRNA modification GTPase TrmE
TIGR00450\"[9-451]TthdF: tRNA modification GTPase TrmE
InterPro
IPR005225
Domain
Small GTP-binding protein domain
TIGR00231\"[212-371]Tsmall_GTP: small GTP-binding protein domain
InterPro
IPR005289
Domain
GTP-binding
TIGR00650\"[220-271]TMG442: GTP-binding conserved hypothetical p
noIPR
unintegrated
unintegrated
G3DSA:3.30.1360.120\"[3-118]Tno description
G3DSA:3.40.50.300\"[208-378]Tno description
PTHR11649\"[39-451]TMSS1/TRME-RELATED GTP-BINDING PROTEIN
PTHR11649:SF14\"[39-451]TMITOCHONDRIAL GTP BINDING PROTEIN


","No hits to the COGs database.","Significant hit ( 2.6e-15) to 1/1 blocks of the IPB000765 family, which is described as \"GTP1/OBG family\". Interpro entry for IP:IPR000765. IPB000765 215-258 2.5e-15Significant hit ( 8.8e-07) to 3/5 blocks of the PR00449 family, which is described as \"Transforming protein P21 RAS signature\". Prints database entry for PR:PR00449. PR00449A 215-236 0.025 PR00449D 323-336 0.25 PR00449E 351-373 44","Residues 273 to 369 match (4e-08) PD:PD481065 which is described as TRNA GTP-BINDING PROTEOME GTPASE COMPLETE MODIFICATION PROCESSING MITOCHONDRIAL PROBABLE TRME ","","","","","","","","","","","","Sat Dec 7 16:34:48 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA03010 is paralogously related to AA00689 (7e-14) and AA03008 (3e-06).","","","","","","Residues 216 to 370 (E-value = 6.9e-05) place AA03010 in the Ras family which is described as Ras family (PF00071)","","","","","Zabel MD, Bunch PK, Clark DP. Regulation of the thdF gene, which is involved in thiophene oxidation by Escherichia coli K-12. Microbios. 2000;101(399):89-103. PMID: 10738982 Alam KY, Clark DP. Molecular cloning and sequence of the thdF gene, which is involved in thiophene and furanoxidation by Escherichia coli. J Bacteriol. 1991 Oct;173(19):6018-24. PMID: 1917835 ","","Sat Dec 7 16:34:48 2002","1","","","" "AA03011","2104353","2102725","1629","ATGGATTCAAGACGAGGCCTGCTGGTCATTGCACTACTCTTTATGTCTTTTATTGTTTATCAGCAATGGCAACTGGATTATCACACGCCAAAACCTGTAACAACCGAACAAACCGCCGCATCGGCATCCGATGTACCTGCCTCTTCCAATGCGGGTAATGCGGTTATTGCAACGGACACCCAAGCAAAAGGCAAAATCATCACCTTGGAAAATGATGTATTTTGTTTGAAAATTAATACATTGGGCGGTGATGTCGTCAGTTCCGAGTTATTGAAATATGACGCCGAGTTAGATTCAAATACCCCGTTCATGTTGCTACAAAATACACCACAACATGTGTATATCGCACAAAGCGGTTTAATCGGTAAAGACGGGATTGACACCAAATCAGGTCGCGCGGACTATCAAGCAGACGGTGATAATTTTAAATTGGCCGATGGGCAGAATGAATTGAGCGTACCTCTTGTTTATGTGAAAGACGGCGTAACCTATCGTAAAGTCTTCACATTAAAACGTGGTGAATATAACATTGCCGTCAATTACGAAATCAATAACCAAAGCGATAAAACCATTGAAGTGGAACCTTATGGTCAATTAAGACACACTTTAGTTGAAAGCTCCGGTAATGTGGCAATGCCGACTTATACCGGCGGCGCCTATTCTTCTTCCGAAACCAATTATAAAAAATACAGTTTCAGCGACATGGAAAATGCCAACTTGTCCATCAATACCAAAGCCGGTTGGGTGGCTGTGTTGCAACACTATTTCGTTTCTGCCTGGATTCCGAATCAGGATGCCGATAATCAGCTTTACACCTTAATCGACAAAGCCAATAACATCGGTTCAATCGGTTATCGCGGTCCGGTAACCAGCATTCAACCAAATACGACGGAAACCTTAACCAGCAAATTATGGACTGGTCCGAAGTTACAAAATGAAATGGCACAAGTGGCCAACCATTTGGATTTAACTGTTGACTACGGTTGGGCATGGTTTATTGCAAAACCGCTATTCTGGTTGTTGACCTTTATTCAAAAACTGGTGCATAACTGGGGTGTGGCGATTATCTGTGTCACCTTAGTGGTGAAAGCGATTTTGTATCCGCTCACCAAAGCACAATATACTTCTATGGCAAAAATGCGTATGTTGCAACCGAAATTGCAGGAAATGCGCGAACGTTTCGGTGAAGATCGTCAACGTATGAGCCAGGAAATGATGAAGCTGTATAAAGACGAGAAAGTCAATCCATTGGGCGGTTGCTTGCCGTTGTTATTACAAATGCCGATTTTCATCGCTTTATATTGGACTTTTTTGGAAGCCGTTGAATTGCGTCATGCACCGTTCTTCGGTTGGATTCAAGACTTATCTGCACAAGATCCGTATTATATCCTGCCGATCTTAATGGGCGCTTCCATGTTCCTGTTACAAAAAATGTCACCGACGCCGGTTGCCGATCCGATGCAGCAAAAAGTGATGACCTTCATGCCGTTAATCTTCATGGTGTTCTTCCTTTGGTTCCCGGCGGGTCTGGTGCTTTACTGGTTGGTGTCCAACTTAATCACGATTATCCAACAACAACTGATTTACCGTGGTTTAGAGAAAAAAGGGTTACATACCCGTCATAAAAAA","","","61449","MDSRRGLLVIALLFMSFIVYQQWQLDYHTPKPVTTEQTAASASDVPASSNAGNAVIATDTQAKGKIITLENDVFCLKINTLGGDVVSSELLKYDAELDSNTPFMLLQNTPQHVYIAQSGLIGKDGIDTKSGRADYQADGDNFKLADGQNELSVPLVYVKDGVTYRKVFTLKRGEYNIAVNYEINNQSDKTIEVEPYGQLRHTLVESSGNVAMPTYTGGAYSSSETNYKKYSFSDMENANLSINTKAGWVAVLQHYFVSAWIPNQDADNQLYTLIDKANNIGSIGYRGPVTSIQPNTTETLTSKLWTGPKLQNEMAQVANHLDLTVDYGWAWFIAKPLFWLLTFIQKLVHNWGVAIICVTLVVKAILYPLTKAQYTSMAKMRMLQPKLQEMRERFGEDRQRMSQEMMKLYKDEKVNPLGGCLPLLLQMPIFIALYWTFLEAVELRHAPFFGWIQDLSAQDPYYILPILMGASMFLLQKMSPTPVADPMQQKVMTFMPLIFMVFFLWFPAGLVLYWLVSNLITIIQQQLIYRGLEKKGLHTRHKK","2102557","","inner membrane protein, 60 kDa","Inner membrane, Cytoplasm","","
InterPro
IPR001708
Family
60 kDa inner membrane insertion protein
PR00701\"[2-23]T\"[72-93]T\"[161-181]T\"[214-232]T\"[247-262]T\"[321-341]T\"[412-435]T\"[459-481]T\"[496-519]T60KDINNERMP
PTHR12428\"[329-538]TOXA1
PF02096\"[349-533]T60KD_IMP
InterPro
IPR006741
Family
Accessory gene regulator B
SM00793\"[385-534]Tno description
InterPro
IPR013308
Family
YidC translocase/secretase
PR01900\"[336-352]T\"[465-480]T\"[485-509]TYIDCPROTEIN
noIPR
unintegrated
unintegrated
PTHR12428:SF11\"[329-538]TOXAA 1, 2
signalp\"[1-22]?signal-peptide
tmhmm\"[5-23]?\"[347-367]?\"[416-438]?\"[457-475]?\"[496-516]?transmembrane_regions


","No hits to the COGs database.","Significant hit (1.4e-149) to 9/9 blocks of the PR00701 family, which is described as \"60Kd inner membrane protein signature\". Prints database entry for PR:PR00701. PR00701A 2-23 2.3e-10 PR00701B 72-93 1.6e-11 PR00701C 161-181 2.5e-10 PR00701D 214-232 4.5e-12 PR00701E 247-262 1.7e-13 PR00701F 321-341 1.4e-18 PR00701G 412-435 4.6e-22 PR00701H 459-481 5.5e-19 PR00701I 496-519 1.7e-21","Residues 1 to 37 match (9e-12) PD:PD126150 which is described as PROTEOME COMPLETE INNER MEMBRANE TRANSMEMBRANE PROTEIN INNER-MEMBRANE HOMOLOG YIDC ","","","","","","","","","","","","Sat Dec 7 16:30:50 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA03011 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 349 to 533 (E-value = 2.5e-122) place AA03011 in the 60KD_IMP family which is described as 60Kd inner membrane protein (PF02096)","","","","","Saaf,A., Monne,M., de Gier,J.W. and von Heijne,G. Membrane topology of the 60-kDa Oxa1p homologue from Escherichia coli. J. Biol. Chem. 273 (46), 30415-30418 (1998) PubMed: 9804807 ","","Sat Dec 7 16:32:58 2002","1","","","" "AA03012","2104616","2104356","261","ATGGCAACGACACATTCGTTTAGCGCAAAAATCCTCATCGGATTAATTCGTTTTTATCAAATCGTTATCAGCCCGTTAATCGGTCCGCGTTGCCGTTTTACGCCCACGTGTTCCTGTTATGGCATTGAGGCGGTAAAAACGCACGGCACGCTAAAAGGTGGTTGGCTTACGCTTAAACGTATATTAAAATGTCATCCTTTAAATACGGGTGGGTACGATCCCGTTCCACCGAAGATCAATAATAACAAAACAGAGAATAAA","10.60","9.51","9624","MATTHSFSAKILIGLIRFYQIVISPLIGPRCRFTPTCSCYGIEAVKTHGTLKGGWLTLKRILKCHPLNTGGYDPVPPKINNNKTENK","","","conserved hypothetical protein","Periplasm","Residues 1-83 are 87% similar to 14286067 YB64_PASMU Hypothetical protein PM1164 and 80% similar to >23467795 hypothetical protein [Haemophilus somnus 129PT].AA03012 has no significant similarity (BLAST p-value < 1e-25) to a Haemophilus ducreyi gene.AA03012 has significant similarity to the Haemophilus influenzae Rd gene 16272936 (5e-38).","
InterPro
IPR002696
Family
Protein of unknown function DUF37
PD004225\"[16-76]TYB64_PASMU_Q9CLQ3;
PF01809\"[8-75]TDUF37
TIGR00278\"[12-86]TTIGR00278: conserved hypothetical protein T
noIPR
unintegrated
unintegrated
signalp\"[1-24]?signal-peptide


","BeTs to 17 clades of COG0759COG name: Uncharacterized ACRFunctional Class: SThe phylogenetic pattern of COG0759 is -------qvdrlbcefghsnujxit-Number of proteins in this genome belonging to this COG is","Significant hit ( 5.4e-42) to 1/1 blocks of the IPB002696 family, which is described as \"Domain of unknown function DUF37\". Interpro entry for IP:IPR002696. IPB002696 16-66 4.4e-42","Residues 11 to 73 match (1e-27) PD:PD004225 which is described as COMPLETE PROTEOME RNPA 3'REGION YIDD ALPHA-HEMOLYSIN AT3G09310 LMO1670 TOXIN BB0143 ","Sat Feb 28 11:34:28 2004","Sat Feb 28 17:44:05 2004","Sat Feb 28 17:44:05 2004","Sat Feb 28 17:44:05 2004","Sat Feb 28 11:34:28 2004","Sat Feb 28 11:34:28 2004","Sat Feb 28 11:34:28 2004","Sat Feb 28 11:34:28 2004","Sat Feb 28 11:34:28 2004","Sat Feb 28 11:34:28 2004","Sat Feb 28 11:34:28 2004","Sat Feb 28 11:34:28 2004","Sat Feb 28 11:34:28 2004","Sat Feb 28 11:34:28 2004","Sat Feb 28 11:34:28 2004","Sat Feb 28 11:34:28 2004","yes","Fri Feb 20 15:41:32 MST 1998","AA03012 has no significant similarity (blastp p-value < 1e-03) to any other gene in this genome. AA03012 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Sat Feb 28 11:34:28 2004","Sat Feb 28 11:34:28 2004","No hits to the PDB database.","","","Residues 8 to 75 (E-value = 1.3e-44) place AA03012 in the DUF37 family which is described as Domain of unknown function DUF37 (PF01809)","Sat Feb 28 11:34:28 2004","","","","","","","1","Sat Feb 28 11:34:28 2004","","" "AA03013","2104906","2104574","333","TTGTTAACTCCCGAACATTTTAAATATGTCTTCCAACAGCCGTCCCGCGCCGGTTCACCTGAAATCACCATTCTTGCCCGCCAAAATCACCTTGAGCATCCCCGCTTAGGCTTAACCGTAGCAAAAAAACACCTGAAACGTGCCCACGATCGTAATCGGATTAAACGATTATGCCGGGAATCTTTTCGTTTAGCGCAACATGATTTGCCGAACTATGATTTTGTGATTGTGGCAAAACAGGGAATCGGTGTTTTAAACAACCGCACTTTATGGCAAACGCTGGATAAATTATGGCAACGACACATTCGTTTAGCGCAAAAATCCTCATCGGAT","","","14407","LLTPEHFKYVFQQPSRAGSPEITILARQNHLEHPRLGLTVAKKHLKRAHDRNRIKRLCRESFRLAQHDLPNYDFVIVAKQGIGVLNNRTLWQTLDKLWQRHIRLAQKSSSD","2104406","","ribonuclease P protein component","Cytoplasm","","
InterPro
IPR000100
Family
Bacterial ribonuclease P protein
PD003629\"[6-87]TRNPA_PASMU_P57915;
PF00825\"[1-102]TRibonuclease_P
TIGR00188\"[1-105]TrnpA: ribonuclease P protein component
InterPro
IPR014721
Domain
Ribosomal protein S5 domain 2-type fold
G3DSA:3.30.230.10\"[1-103]Tno description
noIPR
unintegrated
unintegrated
PIRSF001011\"[1-110]TBacterial ribonuclease P, protein component


","BeTs to 14 clades of COG0594COG name: RNase P protein componentFunctional Class: JThe phylogenetic pattern of COG0594 is --------vdrlbcefghsnujxitwNumber of proteins in this genome belonging to this COG is","Significant hit ( 9.3e-10) to 1/1 blocks of the IPB000100 family, which is described as \"Bacterial ribonuclease P protein\". Interpro entry for IP:IPR000100. IPB000100 48-63 1e-09","Residues 1 to 100 match (2e-38) PD:PD003629 which is described as P RIBONUCLEASE COMPONENT PROTEOME COMPLETE HYDROLASE RNASE C5 RNA-BINDING TRNA ","","","","","","","","","","","","Sat Dec 7 16:13:52 2002","","","","","yes","Fri Feb 20 15:41:32 MST 1998","AA03013 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","","","","","","Residues 1 to 102 (E-value = 7.9e-43) place AA03013 in the Ribonuclease_P family which is described as Ribonuclease P (PF00825)","","","","","Park BH, Choi YN, Park JW, Sim S, Gil MC, Kim S, Kim M, Lee Y. Expression of C5 protein, the protein component of Escherichia coli RNase P, from the tac promoter. Mol Cells. 1998 Feb 28;8(1):96-100. PMID: 9571638 Hansen,F.G., Hansen,E.B. and Atlung,T. 1985. Physical mapping and nucleotide sequence of the rnpA gene that encodes the protein component of ribonuclease P in Escherichia coli. Gene 38(1-3):85-93. PubMed: 2415431. Hansen,F.G., Hansen,E.B. and Atlung,T. 1982. The nucleotide sequence of the dnaA gene promoter and of the adjacent rpmH gene, coding for the ribosomal protein L34, of Escherichia coli. EMBO J. 1(9):1043-1048. PubMed: 6329723. Skovgaard,O. 1990. Nucleotide sequence of a Proteus mirabilis DNA fragment homologous to the 60K-rnpA-rpmH-dnaA-dnaN-recF-gyrB region of Escherichia coli. Gene 93(1):27-34. PubMed: 2172087.","","Tue Dec 17 16:47:46 2002","1","","","" "AA03014","2105086","2104955","132","ATGAAACGCACATTTCAACCTTCTGTATTAAAACGCAGCCGTACTCACGGTTTCCGTGCCCGTATGGCGACTAAAAATGGCCGTCAAGTTTTAGCCCGTCGTCGTGCTAAAGGTCGCAAAAGTTTGTCTGCA","","","5080","MKRTFQPSVLKRSRTHGFRARMATKNGRQVLARRRAKGRKSLSA","2104955","","conserved hypothetical protein","Cytoplasm, Extracellular","Matches weakly in gapped BLAST to an unknown protein from Arabidopsis thaliana (gi|29824329|) and to ribosomal protein L34 from Haemophilus influenzae (gi|16272934|).","
InterPro
IPR000271
Family
Ribosomal protein L34
PD003101\"[1-40]TRL34_HAEIN_P44370;
PF00468\"[1-44]TRibosomal_L34
TIGR01030\"[1-44]TrpmH_bact: ribosomal protein L34
PS00784\"[2-21]TRIBOSOMAL_L34


","No hits to the COGs database.","Significant hit ( 1.8e-33) to 1/1 blocks of the IPB000271 family, which is described as \"Ribosomal protein L34\". Interpro entry for IP:IPR000271. IPB000271 2-39 1.5e-33","","","","","","","","","","","","","Mon Feb 23 09:06:57 2004","Mon Feb 23 09:10:56 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA03014 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 09:06:57 2004","","","","","Residues 1 to 44 (E-value = 6.2e-22) place AA03014 in the Ribosomal_L34 family which is described as Ribosomal protein L34 (PF00468)","","","","","","","","1","","","" "AA03015","2105311","2105222","90","TTGCTTGCCATTTTTAACCAAAACCGTATAATTCCTTCGCTTTTAAATGCTGTGAGTGGTGGAAAATTAAACGGATTGCCGGGTTTTTCC","","","3107","LLAIFNQNRIIPSLLNAVSGGKLNGLPGFS","2105222","","hypothetical protein","Cytoplasm, Extracellular","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 08:38:39 2004","Mon Feb 23 08:38:39 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA03015 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 08:38:39 2004","","","","","","","","","","","","","1","","","" "AA03016","2105418","2105284","135","ATGGTTTTTACTGACTTTTTCGCCATAAAGTGGGGTTGGAAGGGCGATCATTTTACAATAAAGGAAAAAAAAGATCTTCCACCCGCTTCTAAAAAAAGCAAAAAAGGTTGCTTGCCATTTTTAACCAAAACCGTA","","","5183","MVFTDFFAIKWGWKGDHFTIKEKKDLPPASKKSKKGCLPFLTKTV","2105284","","hypothetical protein","Cytoplasm, Periplasm","There are no significant similarities to the NR database.","No hits reported.","No hits to the COGs database.","","","","","","","","","","","","","","Mon Feb 23 08:28:34 2004","Mon Feb 23 08:28:34 2004","","","","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found to this sequence.AA03016 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.","Mon Feb 23 08:28:34 2004","","","","","","","","","","","","","1","","","" "pVT1","452","18","435","ATGGCTGGAGTTAATAAAGTCATTATCGTTGGTCGTTTAGGCAATGAGCCGGAAATGCGCGCCATGCCGAACGGTGAATCGGTTGCCAATCTTAGTGTTGCGACCAGTGAAAGTTGGACGGATAAAAATACCGGCGAACGCCGGGAAGTGACCGAATGGCACCGTATCGTATTTTATCGCCGTCAAGCGGAAGTGTGCGGTGAATACCTGCATAAAGGCTCACAAGTATACATTGAAGGGCGTTTAAAAACGCGCAAATGGCAAGACCAAAGCGGGCAAGACCGCTACACCACCGAAATTCAAGGTGATGTATTGCAAATGTTAGGTGATCCGAAACCAACACAGACACCGACACAAGCTCCGGCTAAATCGGTAACGCCGCCAAAACCGCAAGCGGAAACTCCGGCTGATAATTTTGATGATGATATTCCATTC","","","16302","MAGVNKVIIVGRLGNEPEMRAMPNGESVANLSVATSESWTDKNTGERREVTEWHRIVFYRRQAEVCGEYLHKGSQVYIEGRLKTRKWQDQSGQDRYTTEIQGDVLQMLGDPKPTQTPTQAPAKSVTPPKPQAETPADNFDDDIPF","","See AA01292 for the chromosomal version of this gene. Galli and colleagues report that \"sequences homologous to pVT745 have previously been detected in the chromosomes of numerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183 (5):1585-94)).Plasmid pVT745 is said to be a conjugative plasmid.","single-stranded DNA binding protein","Periplasm, Cytoplasm, Extracellular","This sequence corresponds to GI:10954410, a predicted single-strand DNA binding protein from pVT745 taken from A.actinomycetemcomitans.Nearest neighbor is GI:507347, a predicted ssb sequence from H.influenzae.","
InterPro
IPR000424
Family
Single-strand binding protein/Primosomal replication protein n
PF00436\"[4-108]TSSB
PS50935\"[4-109]TSSB
InterPro
IPR011344
Family
Single-strand binding protein
PTHR10302\"[39-145]TSingle_strand_bd
TIGR00621\"[2-145]Tssb
InterPro
IPR012340
Domain
Nucleic acid-binding, OB-fold
G3DSA:2.40.50.140\"[4-144]TOB_NA_bd_sub
noIPR
unintegrated
unintegrated
PIRSF002070\"[4-144]TSSB
SSF50249\"[1-145]TNucleic_acid_OB


","No hits to the COGs database.","***** IPB000424 (Single-strand binding protein family) with a combined E-value of 2.8e-45. IPB000424A 4-42 IPB000424B 68-90 IPB000424C 139-145","Residues 16-69 are 40% similar to a protein domain (PD446907) which is seen in SSB_RHOSH. Residues 4-64 are 40% similar to a protein domain (PD593367) which is seen in SSB_BACSU. Residues 4-69 are 34% similar to a protein domain (PD446013) which is seen in Q9EZL8_CYTJO. Residues 4-69 are 33% similar to a protein domain (PD186103) which is seen in Q932A8_STAAM. Residues 3-88 are 34% similar to a protein domain (PD299339) which is seen in Q9RY51_DEIRA. Residues 3-69 are identical to a protein domain (PD468010) which is seen in Q9F278_ACTAC. Residues 70-108 are 89% similar to a protein domain (PD187678) which is seen in SSB_HAEIN. Residues 77-145 are 81% similar to a protein domain (PD072908) which is seen in Q9F278_ACTAC. Residues 5-108 are 34% similar to a protein domain (PD186605) which is seen in Q95KK4_RABIT.","","Thu Jun 19 09:54:21 2003","Thu Jun 19 09:54:21 2003","Thu Jun 19 09:54:21 2003","Thu Jun 19 09:54:21 2003","","","Thu Jun 19 09:49:53 2003","","","Fri Jan 7 18:37:41 2005","Fri Jan 7 18:30:51 2005","Wed Jun 18 15:33:40 2003","Fri Jan 7 18:20:59 2005","Sat Aug 23 16:43:41 2003","Sat Aug 23 16:43:41 2003","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to the chromosomal AA01292.","Fri Jan 7 18:37:41 2005","Fri Jan 7 18:20:59 2005","pdb1KAW1KAW-A STRUCTURE OF SINGLE STRANDED DNA BINDING PROTEIN157.0 1e-39pdb1QVC1QVC-A CRYSTAL STRUCTURE ANALYSIS OF SINGLE STRANDED 157.0 1e-39pdb1EYG1EYG-A CRYSTAL STRUCTURE OF CHYMOTRYPTIC FRAGMENT OF E.157.0 1e-39pdb3ULL3ULL-A HUMAN MITOCHONDRIAL SINGLE-STRANDED DNA BINDING 66.0 4e-12pdb1KAW1KAW-A STRUCTURE OF SINGLE STRANDED DNA BINDING PROTEIN124.0 7e-30pdb1QVC1QVC-A CRYSTAL STRUCTURE ANALYSIS OF SINGLE STRANDED 124.0 7e-30","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160089Chen J, Leblanc DJ, Galli DM.DNA inversion on conjugative plasmid pVT745.J Bacteriol. 2002 Nov;184(21):5926-34.PMID: 12374826Novak KF, Dougherty B, Pelez M.Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid and in the chromosome.Microbiology. 2001 Nov;147(Pt 11):3027-35.PMID: 11700353","Jarosik GP, Hansen EJ.Cloning and sequencing of the Haemophilus influenzae ssb gene encoding single-strand DNA-binding protein.Gene. 1994 Aug;146(1):101-3.PMID: 8063092Meyer RR, Laine PS.The single-stranded DNA-binding protein of Escherichia coli.Microbiol Rev. 1990 Dec;54(4):342-80.PMID: 2087220","Fri Jan 7 18:20:59 2005","Wed Jun 18 15:33:40 2003","4","","","" "pVT10","6528","6701","174","ATGCTACTTTTCAAGAAGTATCAAATTGCCGTGCAAAATCCTAAACGAGATTTTTCTGATGAAAAAAATTCATTGGCATATTTGCGCGGGTGGATTATGGCGGGCAAACTGACAAATGATGATTTTAAAGACGCCATAAAAACAGCTGTAAAAGTATCAAATTACATTACATAA","","","6582","MLLFKKYQIAVQNPKRDFSDEKNSLAYLRGWIMAGKLTNDDFKDAIKTAVKVSNYIT$","","Galli and colleagues report that \"sequences homologous to pVT745 have previously been detected in the chromosomes of numerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183(5), 1585-1594 (2001)).Plasmid pVT745 is said to be a conjugative plasmid.","hypothetical protein from pVT745 taken from A.actinomycetemcomitans","Periplasm","This sequence corresponds to GI:10954419(labeled gene AA07), an unknown in GenBank.There are no near neighbors in GenBank at this time.","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-57 are identical to a protein domain (PD255974) which is seen in Q9F269_ACTAC. ","","","","Wed Jun 25 17:08:50 2003","Wed Jun 25 17:08:50 2003","","","Wed Jun 25 17:08:50 2003","Wed Jun 25 17:08:50 2003","","Thu Mar 18 16:43:33 2004","Tue Jun 17 15:27:07 2003","Tue Jun 17 15:27:07 2003","Sat Aug 23 16:49:08 2003","","Sat Aug 23 16:49:08 2003","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found in A.actinomycetemcomitans.","Tue Jun 17 16:08:43 2003","Sat Aug 23 16:49:08 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ. Nucleotide sequence and analysis of conjugative plasmidpVT745. J Bacteriol. 2001 Mar;183(5):1585-94. PMID: 11160089Chen J, Leblanc DJ, Galli DM.DNA inversion on conjugative plasmid pVT745.J Bacteriol. 2002 Nov;184(21):5926-34.PMID: 12374826Novak KF, Dougherty B, Pelez M.Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid andin the chromosome.Microbiology. 2001 Nov;147(Pt 11):3027-35.PMID: 11700353","","Thu Mar 18 16:43:33 2004","","4","","","" "pVT11","7101","6892","210","TTGCTACCACAAGGGCAAAATACACTCCGACCCAATATTTATTGGGTAACAGTATGCAACCAGTTTAAGAAATTTGCTCATGTGCTTATCAAGGTCAAGCCCTCCGGGTTGGCTACGCCAAACCTTGACAATCACCCGCAAATTCTTAATGGTTTAGCATACCGTTACCCCCTCATTTTGGCTAAAGCACGATATAAACAAAAACTGCGG","","","8085","MLPQGQNTLRPNIYWVTVCNQFKKFAHVLIKVKPSGLATPNLDNHPQILNGLAYRYPLILAKARYKQKLR","","Galli and colleagues report that \"sequences homologous topVT745 have previously been detected in the chromosomes ofnumerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183(5), 1585-1594 (2001)).Plasmid pVT745 is said to be a conjugative plasmid.","hypothetical protein from pVT745 taken from A.actinomycetemcomitans","Periplasm, Cytoplasm","This sequence corresponds to GI:10954420 (labeled gene AA08), an unknown in GenBank.There are no near neighbors in GenBank at this time.","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-70 are identical to a protein domain (PD267495) which is seen in Q9F268_ACTAC. ","","Wed Jun 25 17:09:34 2003","Wed Jun 25 17:09:34 2003","Wed Jun 25 17:09:34 2003","Wed Jun 25 17:09:34 2003","","","Wed Jun 25 17:09:14 2003","","","Thu Mar 18 16:44:01 2004","Thu Jun 19 14:32:38 2003","Tue Jun 17 16:21:56 2003","Sat Aug 23 16:49:38 2003","","Sat Aug 23 16:49:38 2003","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found in A.actinomycetemcomitans.","Tue Jun 17 16:25:46 2003","Sat Aug 23 16:49:38 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ. Nucleotide sequence and analysis of conjugative plasmidpVT745. J Bacteriol. 2001 Mar;183(5):1585-94. PMID: 11160089Chen J, Leblanc DJ, Galli DM.DNA inversion on conjugative plasmid pVT745.J Bacteriol. 2002 Nov;184(21):5926-34.PMID: 12374826Novak KF, Dougherty B, Pelez M.Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid andin the chromosome.Microbiology. 2001 Nov;147(Pt 11):3027-35.PMID: 11700353","","Thu Mar 18 16:44:01 2004","","4","","","" "pVT12","8415","7411","1005","ATGAAGATTAAACGTAAAAAAATCAACAGAACATTCGGCTTTAAGTCATCAAAACGAGCTGTCAACTATGAGAAGGCCGCGAAGAAAAAACATCGCAATCTTACTCCTTTCTTTACTCAAAATCTCCAGAGCCGGGAATTTGCTTATACAACGTGGTTTTTCCTGCAACGTTGTGAAACCCATAATTTCAATAAGAATCCTTACTTGAACGCTTTACGATTAAGTAAATATCAGCGTGAGACTATCCGCCGGGAACGTCGGGAAGTCCTTTCTGTTTTGTTGCCAACGCTTATTACTTACTGTGACTTTTCTCCGGCAAGCGATTATCTCTTTGAAGTCCGCGCAAACGTCGAACATATCGCTAATATGTGTAATCAGGCTTATGTATCGTGGGATAAGAACGGTAAAAATCGAGTGCGTTACGATACGGTACTCAATGCTATTCAAATGTTGGAAGACGCTGAATTGATTACTGTATTACGTGAGTATGACCGATTGGGACAAAAGCATAAACCAATGCGGATTTTCTTAAACGTTGAATTCTTTTTAATGTTCAACATTACAGAGAAAGAATTAAGAAAAATCCTGGTCGATTTCCATAAATATCAATTTGTGAACAATCGAGTAAATCAAACATTCGAGCGTTATAAAAAACATCTGGACAAACTGGAAAATAAAGGTGTGGCTGGTATTAAACAGCACCATTCATTAAAAAACTTACTCATCAAACGCCGAAAGGATTTGTTAGGCGAGCACGTCATTAAATTTGTTTCGCAACGTAAGCCGGTAAATTATCTTGATTTAGACATTGAAAGCGACGTTTTTAAACCGTGTTTTCGTTCGTTTACCGACTGTAACACAACGGAAGAAGTACAAAAACTCCGCAAGCGTCTATATGACAAGGAACGAATAAGACAACGAGCACGGGAAAAAGCGGCAAACGATATTTTGTACCGGAAAGCCCTCAAAGAAAGCTACATGACCGATTTACAACATTACGCCTCT","","","40419","MKIKRKKINRTFGFKSSKRAVNYEKAAKKKHRNLTPFFTQNLQSREFAYTTWFFLQRCETHNFNKNPYLNALRLSKYQRETIRRERREVLSVLLPTLITYCDFSPASDYLFEVRANVEHIANMCNQAYVSWDKNGKNRVRYDTVLNAIQMLEDAELITVLREYDRLGQKHKPMRIFLNVEFFLMFNITEKELRKILVDFHKYQFVNNRVNQTFERYKKHLDKLENKGVAGIKQHHSLKNLLIKRRKDLLGEHVIKFVSQRKPVNYLDLDIESDVFKPCFRSFTDCNTTEEVQKLRKRLYDKERIRQRAREKAANDILYRKALKESYMTDLQHYAS","","Galli and colleagues report that \"sequences homologous topVT745 have previously been detected in the chromosomes ofnumerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183(5), 1585-1594 (2001)).Plasmid pVT745 is said to be a conjugative plasmid.","conserved hypothetical protein from pVT745 taken from A.actinomycetemcomitans","Cytoplasm","This sequence corresponds to GI:10954421, an unknown (labeled gene AA09) from pVT745 taken from A. actinomycetemcomitans.Nearest neighbor is GI:21628931, an hypothetical from the H.influenzae \"3031\" plasmid. See also GI:2208979, a plasmid fragment from Y.enterocolitica. ","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 4-56 are identical to a protein domain (PD254412) which is seen in Q9F267_ACTAC. Residues 245-331 are identical to a protein domain (PD280119) which is seen in Q9F267_ACTAC. Residues 57-244 are 96% similar to a protein domain (PD131295) which is seen in Q9F267_ACTAC. ","","Wed Jun 25 17:10:11 2003","Wed Jun 25 17:10:11 2003","Wed Jun 25 17:10:11 2003","Sun Aug 24 13:39:34 2003","","","Wed Jun 25 17:09:56 2003","","","Sun Aug 24 13:39:34 2003","Thu Jun 19 14:45:33 2003","Sun Aug 24 13:39:34 2003","Sat Aug 23 16:50:12 2003","","Sat Aug 23 16:50:12 2003","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences in A.actinomycetemcomitans.","Thu Jun 19 14:44:01 2003","Sat Aug 23 16:50:12 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160089Chen J, Leblanc DJ, Galli DM.DNA inversion on conjugative plasmid pVT745.J Bacteriol. 2002 Nov;184(21):5926-34.PMID: 12374826Novak KF, Dougherty B, Peláez M.Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid andin the chromosome.Microbiology. 2001 Nov;147(Pt 11):3027-35.PMID: 11700353","Kroll,J.S., Farrant,J.L., Tyler,S., Coulthart,M.B. andLangford,P.R.Characterisation and genetic organisation of a 24-MDa plasmid from the Brazilian Purpuric Fever clone of Haemophilus influenzae biogroup aegyptiusPlasmid 48 (1), 38-48 (2002)PubMed: 12206754","Sat Aug 23 16:50:12 2003","Thu Jun 19 14:45:17 2003","4","","","" "pVT13","8796","8999","204","ATGACAGATTCAGATATTTCAATTAGAGTTCGCACAAACAGGGCACTGAAAAATCAAGCCGCTAAAGAACTACGAAAAATGGGATTAACCGTTTCTGACGCCATTAGGCTATATTTAAGCTATATAGCAAATGAAAAAAAATTACCAAATGAATTAACAAATTCTGCTGTATTGATAAGCATAGCGAAAGAAAGGAAGCTGTAA","","","7557","MTDSDISIRVRTNRALKNQAAKELRKMGLTVSDAIRLYLSYIANEKKLPNELTNSAVLISIAKERKL$","","Galli and colleagues report that \"sequences homologous topVT745 have previously been detected in the chromosomes ofnumerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183(5), 1585-1594 (2001)). The authors speculate that this protein may be involved in DNA repair.Plasmid pVT745 is said to be a conjugative plasmid.","hypothetical protein from pVT745 taken from A.actinomycetemcomitans","Cytoplasm, Periplasm","This sequence corresponds to GI:10954422 (labeled gene AA10), an unknown from pVT745 taken from A.actinomycetemcomitans.The nearest neighbor, distantly related at best, is GI:10955845, an unknown from plasmid pYC taken from Y.pestis.","
InterPro
IPR007337
Family
RelB antitoxin
PF04221\"[5-67]TRelB


","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-67 are identical to a protein domain (PD503630) which is seen in Q9F266_ACTAC. ","","","","Wed Jun 25 17:11:02 2003","Wed Jun 25 17:11:02 2003","","","Wed Jun 25 17:11:02 2003","Wed Jun 25 17:11:02 2003","","Thu Mar 18 16:44:58 2004","Thu Jun 19 14:52:05 2003","Thu Jun 19 14:50:22 2003","Sun Aug 24 13:40:49 2003","","Sun Aug 24 13:40:49 2003","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found in A.actinomycetemcomitans.","Thu Jun 19 14:52:05 2003","Sun Aug 24 13:40:49 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160089","","Thu Jun 19 14:50:22 2003","","4","","","" "pVT14","9160","9321","162","ATGAATATCGTTTTTCTACAATATATCCATAGCCGTAAAAACCAAAATCAATCACTCGAAGTACAACAGGAAATAATCCAAGCCATAATCATTCAACAATACCACGAAATCAGCGAGCAATTAACGACATTACAGAGTTTAATAAACAGCTTGAAACGGTAA","","","6307","MNIVFLQYIHSRKNQNQSLEVQQEIIQAIIIQQYHEISEQLTTLQSLINSLKR$","","Galli and colleagues report that \"sequences homologous to pVT745 have previously been detected in the chromosomes of numerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183 (5), 1585-1594 (2001)). Plasmid pVT745 is said to be a conjugative plasmid.","hypothetical protein from pVT745 taken from A. actinomycetemcomitans","Cytoplasm","This sequence corresponds to GI:10954423, an unknown (labeled gene AA11) from pVT745 taken from A.actinomycetemcomitans.There were no near neighbors found at this time in GenBank.","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-53 are 77% similar to a protein domain (PD251557) which is seen in Q9F265_ACTAC. ","","","","Wed Jun 25 17:11:18 2003","Wed Jun 25 17:11:18 2003","","","Wed Jun 25 17:11:18 2003","Wed Jun 25 17:11:18 2003","","Thu Mar 18 16:51:25 2004","Thu Jun 19 14:56:33 2003","Thu Jun 19 14:56:33 2003","Sat Aug 23 16:50:36 2003","","Sat Aug 23 16:50:36 2003","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found in A. actinomycetemcomitans.","Thu Jun 19 14:56:33 2003","Sat Aug 23 16:50:36 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160089Chen J, Leblanc DJ, Galli DM.DNA inversion on conjugative plasmid pVT745.J Bacteriol. 2002 Nov;184(21):5926-34.PMID: 12374826Novak KF, Dougherty B, Pelez M.Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid andin the chromosome.Microbiology. 2001 Nov;147(Pt 11):3027-35.PMID: 11700353","","Thu Mar 18 16:51:25 2004","","4","","","" "pVT15","10039","9410","630","TTGGGGCTAGGCGCCTCGCTTCAGGAAACCGTCGCTCCAAATCCAGAGACCATCAAGGCCGCCGAGTTTTCGGCAGCTTCTCCTAAGCAAGAATCCGGGACCCTSCGCTGGTTGCTCGGCATCAATGCACTTCTGTTCGTGGTGGAAATGACTGCAGGTCTGATCGCCCAGTCCACTGGCCTGATTGGAGAATCCCTGGACAATTTTTCCGATGCGGCGGTGTACGGGCTTGCCCTTTATGCGGTTGGACATAGCGTGAAAATGCAGGTACGTGCCGCGCATCTTGCTGGTGTACTGCAACTGATCTTGGCTATGGGCGTGCTCGTAGAGGTGGTGAGACGCTTTGTATTCGGTAGTGAGCCTGAATCGCTGGTGATGATGGCTATCGCATTCGTCGCATTGATTGCCAATACCAGTTGTCTGCTGCTCATATCCAAACATCGGGAAGGCGGGGCGCACATGAAGGCAAGCTGGATATTCTCGGCCAACGACGTGGTGATCAACCTGGGGGGCATCACCGCCGGCGCCCTGGTCGCGTGGACCGGTTCCAATTATCCGGATCTGATTATCGGCACCATCGCGGGGGGCATTGTACTTAACGGTGCCAGACGCATTTTGGCGTTGAAGGGT","","","31267","LGLGASLQETVAPNPETIKAAEFSAASPKQESGTLRWLLGINALLFVVEMTAGLIAQSTGLIGESLDNFSDAAVYGLALYAVGHSVKMQVRAAHLAGVLQLILAMGVLVEVVRRFVFGSEPESLVMMAIAFVALIANTSCLLLISKHREGGAHMKASWIFSANDVVINLGGITAGALVAWTGSNYPDLIIGTIAGGIVLNGARRILALKG","","Similar to putative transporter protein ofNeisseria meningitidis.Galli and colleagues report that \"sequences homologous to pVT745 have previously been detected in the chromosomes of numerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183 (5), 1585-1594 (2001)). Plasmid pVT745 is said to be a conjugative plasmid.","predicted metal/ion transport protein from pVT745 taken from A.actinomycetemcomitans","Inner membrane, Cytoplasm","This sequence corresponds to GI:10954425(labeled gene AA12), an unknown from pVT745 taken from A. actinomycetemcomitans. It is virtually identical to GI:13378322, a predicted pit1 gene from plasmid pLEM taken from Pasteurella multocida. See also GI:18150964, a predicted transporter from plasmid pWW0 taken from P. putida.","
InterPro
IPR002524
Family
Cation efflux protein
PF01545\"[123-170]TCation_efflux
InterPro
IPR006121
Domain
Heavy metal transport/detoxification protein
PS50846\"[32-95]THMA_2
SSF55008\"[27-98]THeavyMe_transpt


","No hits to the COGs database.","***** IPB002524 (Cation efflux family) with a combined E-value of 4e-08. IPB002524A 133-173 IPB002524B 197-236","Residues 129-293 are identical to a protein domain (PD107131) which is seen in Q9F264_ACTAC. Residues 33-98 are identical to a protein domain (PD349833) which is seen in Q9F264_ACTAC. Residues 1-32 are identical to a protein domain (PD226143) which is seen in Q9F264_ACTAC. Residues 37-148 are 34% similar to a protein domain (PD300486) which is seen in Q8XSZ8_RALSO. Residues 129-225 are 29% similar to a protein domain (PD001602) which is seen in Q9ZNF5_STAAU. Residues 99-128 are identical to a protein domain (PD589498) which is seen in Q9F264_ACTAC.","","Wed Jun 25 17:12:30 2003","Wed Jun 25 17:12:30 2003","Wed Jun 25 17:12:30 2003","Sun Aug 24 13:45:42 2003","","","Wed Jun 25 17:11:33 2003","","","Thu Oct 11 17:09:52 2007","Thu Jun 19 15:18:59 2003","Thu Jun 19 15:10:50 2003","Thu Oct 11 13:31:24 2007","Sat Aug 23 16:51:00 2003","Thu Oct 11 13:31:24 2007","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is a duplicate of GI:19568176, a predicted transport protein from chromosomal A. actinomycetemcomitans (gene Aa32-334-7).","Thu Jun 19 15:27:19 2003","Sat Aug 23 16:51:00 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160089Chen J, Leblanc DJ, Galli DM.DNA inversion on conjugative plasmid pVT745.J Bacteriol. 2002 Nov;184(21):5926-34.PMID: 12374826Novak KF, Dougherty B, Pelez M.Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid andin the chromosome.Microbiology. 2001 Nov;147(Pt 11):3027-35.PMID: 11700353","Greated,A., Lambertsen,L., Williams,P.A. and Thomas,C.M.Complete sequence of the IncP-9 TOL plasmid pWW0 from Pseudomonas putidaEnviron. Microbiol. 4 (12), 856-871 (2002)PubMed: 12534468","Thu Oct 11 13:31:24 2007","Thu Oct 11 13:31:24 2007","4","","","" "pVT16","9525","9803","279","ATGCCCCCCAGGTTGATCACCACGTCGTTGGCCGAGAATATCCAGCTTGCCTTCATGTGCGCCCCGCCTTCCCGATGTTTGGATATGAGCAGCAGACAACTGGTATTGGCAATCAATGCGACGAATGCGATAGCCATCATCACCAGCGATTCAGGCTCACTACCGAATACAAAGCGTCTCACCACCTCTACGAGCACGCCCATAGCCAAGATCAGTTGCAGTACACCAGCAAGATGCGCGGCACGTACCTGCATTTTCACGCTATGTCCAACCGCATAA","","","9668","MPPRLITTSLAENIQLAFMCAPPSRCLDMSSRQLVLAINATNAIAIITSDSGSLPNTKRLTTSTSTPIAKISCSTPARCAARTCIFTLCPTA$","","Galli and colleagues report that \"sequences homologous to pVT745 have previously been detected in the chromosomes of numerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183 (5), 1585-1594 (2001)). Plasmid pVT745 is said to be a conjugative plasmid.","hypothetical protein from pVT745 taken from A.actinomycetemcomitans","Periplasm","This sequence corresponds to GI:10954424 (labeled gene AA13), an unknown in GenBank.There are no near neighbors in GenBank at this time.","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-92 are 86% similar to a protein domain (PD280497) which is seen in Q9F263_ACTAC. ","","","","Wed Jun 25 17:13:02 2003","Wed Jun 25 17:13:02 2003","","","Wed Jun 25 17:13:02 2003","Wed Jun 25 17:13:02 2003","","Thu Mar 18 16:44:28 2004","Thu Jun 19 14:33:10 2003","Tue Jun 17 16:34:21 2003","Sat Aug 23 16:51:21 2003","","Sat Aug 23 16:51:21 2003","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found in A.actinomycetemcomitans.","Tue Jun 17 16:34:21 2003","Sat Aug 23 16:51:21 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160089Chen J, Leblanc DJ, Galli DM.DNA inversion on conjugative plasmid pVT745.J Bacteriol. 2002 Nov;184(21):5926-34.PMID: 12374826Novak KF, Dougherty B, Pelez M.Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid andin the chromosome.Microbiology. 2001 Nov;147(Pt 11):3027-35.PMID: 11700353","","Thu Mar 18 16:44:28 2004","","4","","","" "pVT17","11355","11239","117","ATGAATACTGTAAATGAACTAAAAAAAGTATTGGATTCGAAGCGTCCGCTTGACCCGGTTACGACMAAATCTTTACAAGATGATTTTATGTTGCGTTATAACCAAGCGTCTAGGCAA","","","4564","MNTVNELKKVLDSKRPLDPVTTKSLQDDFMLRYNQASRQ","","Galli and colleagues report that \"sequences homologous to pVT745 have previously been detected in the chromosomes of numerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183 (5), 1585-1594 (2001)). Plasmid pVT745 is said to be a conjugative plasmid.","conserved hypothetical protein from pVT745 taken from A.actinomycetemcomitans","Cytoplasm, Periplasm","This sequence corresponds to GI:10954426 (labeled gene AA14), an unknown from pVT745 taken from A.actinomycetemcomitans.","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-39 are identical to a protein domain (PD231768) which is seen in Q9F262_ACTAC. ","","Wed Jun 25 17:13:22 2003","Wed Jun 25 17:13:22 2003","Wed Jun 25 17:13:22 2003","Wed Jun 25 17:13:22 2003","","","Wed Jun 25 17:13:12 2003","","","Sun Aug 24 13:52:01 2003","Thu Jun 19 15:34:56 2003","Thu Jun 19 15:38:16 2003","Sat Aug 23 16:51:52 2003","","Sat Aug 23 16:51:52 2003","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is virtually identical to AA1260 from chromosomal A.actinomycetemcomitans, a hypothetical.","Sun Aug 24 13:52:01 2003","Sat Aug 23 16:51:52 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160089Chen J, Leblanc DJ, Galli DM.DNA inversion on conjugative plasmid pVT745.J Bacteriol. 2002 Nov;184(21):5926-34.PMID: 12374826Novak KF, Dougherty B, Peláez M.Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid andin the chromosome.Microbiology. 2001 Nov;147(Pt 11):3027-35.PMID: 11700353","","Sat Aug 23 16:51:52 2003","","4","","","" "pVT18","11647","11411","237","ATGAGTAAATTAACAAAAGGCACACTAAGCAAATCCGGGCTTTCTATGGGTAACATTGAAAAAACGGCTATGCCACAGCTCAAAGAGGAAGTAACTATTGCCGAACAACGAACTACCATCATGATTCCGGTGGATGTTTACAAAGCAGTGAAGAAATATGCGTTACTTAATGATATTAAGTTGAAAGAGTATTTTAATGACTTACTTAGTAAGGATTTAAAAGAAAAAGGCATGTTA","","","8906","MSKLTKGTLSKSGLSMGNIEKTAMPQLKEEVTIAEQRTTIMIPVDVYKAVKKYALLNDIKLKEYFNDLLSKDLKEKGML","","Galli and colleagues report that \"sequences homologous to pVT745 have previously been detected in the chromosomes of numerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183 (5), 1585-1594 (2001)). The authors speculate that this protein may be related to plasmid stability.Plasmid pVT745 is said to be a conjugative plasmid.","hypothetical protein from pVT745 taken from A.actinomycetemcomitans","Cytoplasm","This sequence corresponds to GI:10954427, an unknown (labeled gene AA15) from pVT745 taken from A.actinomycetemcomitans.No near neighbors were found in GenBank at this time.","
InterPro
IPR010985
Domain
Ribbon-helix-helix
SSF47598\"[34-77]TMet_repress_like


","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-79 are identical to a protein domain (PD273949) which is seen in Q9F261_ACTAC. ","","Wed Jun 25 17:14:27 2003","Wed Jun 25 17:14:27 2003","Wed Jun 25 17:14:27 2003","Wed Jun 25 17:14:27 2003","","","Wed Jun 25 17:13:39 2003","","","Thu Mar 18 16:52:05 2004","Thu Jun 19 15:47:00 2003","Thu Jun 19 15:47:00 2003","Sat Aug 23 16:52:14 2003","","Sat Aug 23 16:52:14 2003","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found in A.actinomycetemcomitans.","Thu Jun 19 15:47:00 2003","Sat Aug 23 16:52:14 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160089Chen J, Leblanc DJ, Galli DM.DNA inversion on conjugative plasmid pVT745.J Bacteriol. 2002 Nov;184(21):5926-34.PMID: 12374826Novak KF, Dougherty B, Pelez M.Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid andin the chromosome.Microbiology. 2001 Nov;147(Pt 11):3027-35.PMID: 11700353","","Thu Mar 18 16:52:05 2004","","4","","","" "pVT19","12281","11643","639","ATGAAAGTCATATCCGTATTAAGTCAGAAAGGCGGTAGCGGTAAAAGCACGCTTTCTATCAATATTGCCCGCAGCCTGCAACTTAAAGGTTTTGATGTCGCATTAATTGATACCGACCCGCAAGCGTCCGCGCGTGAATGGAATGCGCTTGCCGGTGATGATTTTTTCCCGGTGTTTGCTTGTGATAAAGGGCTCTCCGAAAAAGAAATCCGTGCGCTTGGTCGCCAAGCGGATTTTTTAATCATTGATGGTGCGCCACGTATTGAAAAAGCCATGACCGATTCGATTAAACTTGCCGATTACATTCTGATCCCACTGAAACCATCACAATTTGATATTTGGGCATGCAAAGATTCGATAGAGCTGGTGCAAGCACGTATGCAAATTGATGATAAGCTCAAAGCCGGGTTAGTCATCAGTCAAACGAATAAGCAGACAAATTTAGCTAAAGAAGTTATTGAATTTATCAACGAAAACTTTGAAATACCGTTATTAAAGGGTAGTRCGGCGGTACGCGTCAGCTATGCAGAAGTCTTAAGTTCCGGTAATACGGTTTKTGAAAGTCAATCTAAAGAAGCGAAAGCAGAGATTAATCAAATCACAAATGAAATTTTAACTGCACTAGGAGTTCAATATGAG","","","23105","MKIKRKKINRTFGFKSSKRAVNYEKAAKKKHRNLTPFFTQNLQSREFAYTTWFFLQRCETHNFNKNPYLNALRLSKYQRETIRRERREVLSVLLPTLITYCDFSPASDYLFEVRANVEHIANMCNQAYVSWDKNGKNRVRYDTVLNAIQMLEDAELITVLREYDRLGQKHKPMRIFLNVEFFLMFNITEKELRKILVDFHKYQFVNNRVNQTF","","Galli and colleagues report that \"sequences homologous to pVT745 have previously been detected in the chromosomes of numerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183 (5), 1585-1594 (2001)). Plasmid pVT745 is said to be a conjugative plasmid.","partition protein from pVT745 taken from A. actinomycetemcomitans","Cytoplasm","This sequence corresponds to GI:10954428, a predicted partitioning protein from pVT745 taken from A.actinomycetemcomitans.Nearest neighbor is GI:16902302 for plasmid pRA2 from S.marcescens (parA).","
InterPro
IPR000897
Domain
GTP-binding signal recognition particle SRP54, GTPase
PD000819\"[12-87]TSRP54
InterPro
IPR002586
Domain
Cobyrinic acid a,c-diamide synthase
PF01656\"[4-177]TCbiA
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[2-204]TG3DSA:3.40.50.300
SSF52540\"[1-206]TSSF52540


","BeTs to 18 clades of COG1192COG name: ATPases involved in chromosome partitioningFunctional Class: DThe phylogenetic pattern of COG1192 is -ompk--q-dr-bcefg-snujxitwNumber of proteins in this genome belonging to this COG is","***** IPB000808 (Mrp family) with a combined E-value of 4.6e-09. IPB000808A 0-44","Residues 163-213 are identical to a protein domain (PD451937) which is seen in Q9F260_ACTAC. Residues 43-208 are 24% similar to a protein domain (PD547562) which is seen in Q8XTV1_RALSO. Residues 33-210 are 22% similar to a protein domain (PD328296) which is seen in Q52325_ECOLI. Residues 68-152 are identical to a protein domain (PD336937) which is seen in Q9F260_ACTAC. Residues 2-41 are identical to a protein domain (PD000159) which is seen in Q9F260_ACTAC. Residues 121-204 are 34% similar to a protein domain (PD530901) which is seen in Q8VW79_SERMA. Residues 78-204 are 25% similar to a protein domain (PD309531) which is seen in O66424_AQUAE. Residues 3-209 are 25% similar to a protein domain (PD555115) which is seen in Q93KR1_YEREN.","","Wed Jun 25 17:14:52 2003","Wed Jun 25 17:14:52 2003","Wed Jun 25 17:14:52 2003","Sun Aug 24 13:53:52 2003","","","Wed Jun 25 17:14:39 2003","","","Sun Aug 24 13:53:52 2003","Thu Jun 19 15:49:41 2003","Thu Jun 19 15:57:31 2003","Sat Aug 23 16:52:35 2003","Sat Aug 23 16:52:35 2003","Sun Aug 24 13:53:52 2003","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is weakly related to AA0467 in chromosomal A.actinomycetemcomitans.","Thu Jun 19 15:49:41 2003","Sat Aug 23 16:52:35 2003","pdb|1HYQ|1HYQ-A MIND BACTERIAL CELL DIVISION REGULATOR FROM A. 38.3 0.001000pdb|1ION|1ION-A THE SEPTUM SITE-DETERMINING PROTEIN MIND 46.5 4e-06pdb|1G3Q|1G3Q-A CRYSTAL STRUCTURE ANALYSIS OF PYROCOCCUS 46.1 5e-06pdb|1F48|1F48-A CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI 39.1 7e-04pdb|1FP6|1FP6-A THE NITROGENASE FE PROTEIN FROM AZOTOBACTER 38.3 0.001000pdb|1G20|1G20-E MGATP-BOUND AND NUCLEOTIDE-FREE STRUCTURES OF 38.3 0.001000pdb|1DE0|1DE0-A MODULATING THE MIDPOINT POTENTIAL OF THE 38.3 0.001000pdb|1F48|1F48-A CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI 88.3 1e-18pdb|1HYQ|1HYQ-A MIND BACTERIAL CELL DIVISION REGULATOR FROM A. 61.8 1e-10pdb|1ION|1ION-A THE SEPTUM SITE-DETERMINING PROTEIN MIND 61.8 1e-10pdb|1G3Q|1G3Q-A CRYSTAL STRUCTURE ANALYSIS OF PYROCOCCUS 60.2 3e-10pdb|1FP6|1FP6-A THE NITROGENASE FE PROTEIN FROM AZOTOBACTER 57.1 3e-09pdb|1G20|1G20-E MGATP-BOUND AND NUCLEOTIDE-FREE STRUCTURES OF 57.1 3e-09pdb|1DE0|1DE0-A MODULATING THE MIDPOINT POTENTIAL OF THE 57.1 3e-09pdb|1CP2|1CP2-A NITROGENASE IRON PROTEIN FROM CLOSTRIDIUM 46.2 5e-06pdb|1FTS|1FTS SIGNAL RECOGNITION PARTICLE RECEPTOR FROM E. COLI 40.0 4e-04pdb|1F48|1F48-A CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI 86.5 4e-18pdb|1G20|1G20-E MGATP-BOUND AND NUCLEOTIDE-FREE STRUCTURES OF 71.3 1e-13pdb|1DE0|1DE0-A MODULATING THE MIDPOINT POTENTIAL OF THE 71.3 1e-13pdb|1FP6|1FP6-A THE NITROGENASE FE PROTEIN FROM AZOTOBACTER 71.3 1e-13pdb|1ION|1ION-A THE SEPTUM SITE-DETERMINING PROTEIN MIND 58.8 8e-10pdb|1G3Q|1G3Q-A CRYSTAL STRUCTURE ANALYSIS OF PYROCOCCUS 55.7 7e-09pdb|1HYQ|1HYQ-A MIND BACTERIAL CELL DIVISION REGULATOR FROM A. 55.3 9e-09pdb|1CP2|1CP2-A NITROGENASE IRON PROTEIN FROM CLOSTRIDIUM 53.4 4e-08pdb|1JPJ|1JPJ-A GMPPNP COMPLEX OF SRP GTPASE NG DOMAIN 46.0 6e-06pdb|1LS1|1LS1-A T. AQUATICUS FFH NG DOMAIN AT 1.1A RESOLUTION 46.0 6e-06pdb|1NG1|1NG1 N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE 46.0 6e-06pdb|2FFH|2FFH-A THE SIGNAL SEQUENCE BINDING PROTEIN FFH FROM 46.0 6e-06pdb|1FFH|1FFH N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE 46.0 6e-06pdb|2NG1|2NG1 N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE 46.0 6e-06pdb|1J8M|1J8M-F SIGNAL RECOGNITION PARTICLE CONSERVED GTPASE 44.4 2e-05pdb|1J8Y|1J8Y-F SIGNAL RECOGNITION PARTICLE CONSERVED GTPASE 42.8 5e-05pdb|1ION|1ION-A THE SEPTUM SITE-DETERMINING PROTEIN MIND 91.7 1e-19pdb|1G3Q|1G3Q-A CRYSTAL STRUCTURE ANALYSIS OF PYROCOCCUS 90.6 2e-19pdb|1FTS|1FTS SIGNAL RECOGNITION PARTICLE RECEPTOR FROM E. COLI 73.8 2e-14pdb|1NG1|1NG1 N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE 63.7 3e-11pdb|1JPJ|1JPJ-A GMPPNP COMPLEX OF SRP GTPASE NG DOMAIN 63.7 3e-11pdb|1LS1|1LS1-A T. AQUATICUS FFH NG DOMAIN AT 1.1A RESOLUTION 63.7 3e-11pdb|2FFH|2FFH-A THE SIGNAL SEQUENCE BINDING PROTEIN FFH FROM 63.7 3e-11pdb|1FFH|1FFH N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE 63.7 3e-11pdb|2NG1|2NG1 N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE 63.7 3e-11pdb|1HYQ|1HYQ-A MIND BACTERIAL CELL DIVISION REGULATOR FROM A. 61.8 1e-10pdb|1FP6|1FP6-A THE NITROGENASE FE PROTEIN FROM AZOTOBACTER 57.1 3e-09pdb|1G20|1G20-E MGATP-BOUND AND NUCLEOTIDE-FREE STRUCTURES OF 57.1 3e-09pdb|1DE0|1DE0-A MODULATING THE MIDPOINT POTENTIAL OF THE 57.1 3e-09pdb|1CP2|1CP2-A NITROGENASE IRON PROTEIN FROM CLOSTRIDIUM 54.3 2e-08pdb|1J8M|1J8M-F SIGNAL RECOGNITION PARTICLE CONSERVED GTPASE 53.2 4e-08pdb|1J8Y|1J8Y-F SIGNAL RECOGNITION PARTICLE CONSERVED GTPASE 51.2 2e-07pdb|1F48|1F48-A CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI 50.8 2e-07","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160089Chen J, Leblanc DJ, Galli DM.DNA inversion on conjugative plasmid pVT745.J Bacteriol. 2002 Nov;184(21):5926-34.PMID: 12374826Novak KF, Dougherty B, Peláez M.Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid andin the chromosome.Microbiology. 2001 Nov;147(Pt 11):3027-35.PMID: 11700353","Kwong SM, Yeo CC, Chuah D, Poh CL.Sequence analysis of plasmid pRA2 from Pseudomonas alcaligenes NCIB 9867 (P25X) reveals a novel replication region.FEMS Microbiol Lett. 1998 Jan;158(2):159-65.PMID: 9465390","Sat Aug 23 16:52:35 2003","Thu Jun 19 15:57:31 2003","4","","","" "pVT2","630","1208","579","ATGTTAGTTGGTTATGCCCGCGTATCGACAAAAGAACCAAACTATGAAATGCAGATCCAAGCACTGAGAAATGCCGGATGTGAAAAAATTTTTTCTGAAAAGGAAAGTGGAAATTCTGATGACCGTAGGGAATTCAAAAAGGCATTAACTTTTCTCAGAGAAGGAGATACGCTCATAGTATGGAAATTAGATAGGTTAGGACGTAGCGTTTCTCAATCAAGCCGGTTTCTTGAAATACTAAAGGAGAAAAAGGTGAGTGTTGTCAGCCTTATCGAAAACATAGACACAAGAACAATATTTGGAGAATGGTTATTTTATTTTGCGTCCATATTTGCAGAAATGGAACGTAACAGTATCATTGAACGCACAAAAGCAGGCATAAAATTTGCAAGGGAACAGGGTGTAAGAATAGGACGCCCCCCTAAAATGACAGAAGATAATATAGAGATAATAAGAGAACTGTTAAAGGCCGGTTGGACGGTAAAAAAAATAGCAGAGAAATTAGGCATATCACAGTCAAGTATATATGCCTATTTTCCTAGTGATATTCTCGAGGATTTACGCCCTAACGCATTATAA","","","22103","MLVGYARVSTKEPNYEMQIQALRNAGCEKIFSEKESGNSDDRREFKKALTFLREGDTLIVWKLDRLGRSVSQSSRFLEILKEKKVSVVSLIENIDTRTIFGEWLFYFASIFAEMERNSIIERTKAGIKFAREQGVRIGRPPKMTEDNIEIIRELLKAGWTVKKIAEKLGISQSSIYAYFPSDILEDLRPNAL$","","Galli and colleagues report that \"sequences homologous to pVT745 have previously been detected in the chromosomes of numerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183 (5), 1585-1594 (2001)).Plasmid pVT745 is said to be a conjugative plasmid.Chen et al. analyze a 9-kb inversion that is mediated by this recombinase (not a RecA protein but related to Din family proteins). A host factor appears to be also necessary for this event.","site-specific recombinase/invertase from pVT745 taken from A. actinomycetemcomitans","Cytoplasm","This sequence corresponds to 10954411, a predicted site-specific recombinase from pVT745 (labeled gene AA01 in GenBank) and taken from A.actinomycetemcomitans.Nearest neighbor is GI:24376250, a predicted DNA-invertase from ISSod9 taken from Shewanella oneidensis MR-1. See also GI:10956730 from the plant Xylella fastidiosa 9a5c.","
InterPro
IPR006118
Family
Site-specific recombinase
PS00398\"[55-67]TRECOMBINASES_2
InterPro
IPR006119
Domain
Resolvase, N-terminal
PF00239\"[2-136]TResolvase
InterPro
IPR006120
Domain
Resolvase, helix-turn-helix region
PF02796\"[138-182]THTH_7
InterPro
IPR009057
Domain
Homeodomain-like
SSF46689\"[138-189]THomeodomain_like
InterPro
IPR012287
Domain
Homeodomain-related
G3DSA:1.10.10.60\"[138-189]THomeodomain-rel
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1390\"[1-119]TG3DSA:3.40.50.1390
SSF53041\"[1-137]TSSF53041


","BeTs to 8 clades of COG1961COG name: Site-specific recombinases, DNA invertase Pin homologsFunctional Class: LThe phylogenetic pattern of COG1961 is ---pk----drlb-efg-s--j----Number of proteins in this genome belonging to this COG is","***** IPB001822 (Site-specific recombinase) with a combined E-value of 2.7e-56. IPB001822A 3-16 IPB001822B 30-80 IPB001822C 100-140 IPB001822D 158-177","Residues 70-112 are identical to a protein domain (PD236883) which is seen in Q9F277_ACTAC. Residues 113-178 are identical to a protein domain (PD477347) which is seen in Q9F277_ACTAC. Residues 29-69 are identical to a protein domain (PD000772) which is seen in Q9F277_ACTAC. Residues 4-134 are 28% similar to a protein domain (PD138410) which is seen in Q8YWY3_ANASP. Residues 70-124 are 43% similar to a protein domain (PD338134) which is seen in Q97HQ7_CLOAB. Residues 5-94 are 33% similar to a protein domain (PD542119) which is seen in Q8YF66_BRUME. Residues 112-178 are 35% similar to a protein domain (PD582019) which is seen in Q93MJ2_BBBBB. Residues 5-90 are 38% similar to a protein domain (PD387332) which is seen in Q48489_KLEPN. Residues 3-139 are 33% similar to a protein domain (PD463229) which is seen in Q98DH0_RHILO.","","","","Thu Jun 19 09:50:44 2003","Sun Aug 24 19:27:32 2003","","","Thu Jun 19 09:50:44 2003","Thu Jun 19 09:50:44 2003","","Sun Aug 24 19:27:32 2003","Sat Aug 23 17:44:15 2003","Wed Jun 18 15:21:03 2003","Sat Aug 23 16:45:28 2003","Sat Aug 23 16:45:28 2003","Sat Aug 23 17:41:53 2003","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found in A.actinomycetemcomitans.","Wed Jun 18 15:12:15 2003","Sat Aug 23 16:45:28 2003","pdb|1GDT|1GDT-A CRYSTAL STRUCTURE OF A SITE-SPECIFIC 98.3 1e-21pdb|2RSL|2RSL-A GAMMA 86.2 4e-18pdb|1GHT|1GHT-A SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF 68.3 1e-12pdb|1GDT|1GDT-A CRYSTAL STRUCTURE OF A SITE-SPECIFIC 267.0 1e-72pdb|2RSL|2RSL-A GAMMA 212.0 5e-56pdb|1GHT|1GHT-A SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF 160.0 1e-40pdb|1RES|1RES GAMMA DELTA RESOLVASE (DNA BINDING DOMAIN) (NMR, 59.5 5e-10pdb|1GDT|1GDT-A CRYSTAL STRUCTURE OF A SITE-SPECIFIC 268.0 6e-73pdb|2RSL|2RSL-A GAMMA 211.0 7e-56pdb|1GHT|1GHT-A SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF 160.0 1e-40pdb|1RES|1RES GAMMA DELTA RESOLVASE (DNA BINDING DOMAIN) (NMR, 61.0 2e-10","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160089Chen J, Leblanc DJ, Galli DM.DNA inversion on conjugative plasmid pVT745.J Bacteriol. 2002 Nov;184(21):5926-34.PMID: 12374826Novak KF, Dougherty B, Peláez M.Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid andin the chromosome.Microbiology. 2001 Nov;147(Pt 11):3027-35.PMID: 11700353","Mintz KP, Brissette C, Fives-Taylor PM.A recombinase A-deficient strain of Actinobacillus actinomycetemcomitans constructed by insertional mutagenesis using a mobilizable plasmid.FEMS Microbiol Lett. 2002 Jan;206(1):87-92.PMID: 11786262Iida S, Sandmeier H, Hübner P, Hiestand-Nauer R, Schneitz K, Arber W.The Min DNA inversion enzyme of plasmid p15B of Escherichia coli 15T-: a new member of the Din family of site-specific recombinases.Mol Microbiol. 1990 Jun;4(6):991-7.PMID: 2215218","Sat Aug 23 17:43:08 2003","Sun Aug 24 19:27:32 2003","4","","","" "pVT20","12435","12307","129","ATGAAACTTAATCATATCATTATCTCTCTTCTTATCGCAAGACAAACCGGCAGACCGGTACACATTCCGGCGATGAAAGGCAAGGAATTTGCCGAATTCATGTCATTGTTACGCGTTGCATTACAATCT","","","4842","MKLNHIIISLLIARQTGRPVHIPAMKGKEFAEFMSLLRVALQS","","Galli and colleagues report that \"sequences homologous to pVT745 have previously been detected in the chromosomes of numerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183 (5), 1585-1594 (2001)). Plasmid pVT745 is said to be a conjugative plasmid.","hypothetical protein from pVT745 taken from A.actinomycetemcomitans","Cytoplasm","This sequence corresponds to GI:10954429 (labeled AA16), an unknown from pVT745 taken from A.actinomycetemcomitans.There are no near neighbors in GenBank at this time.","
noIPR
unintegrated
unintegrated
signalp\"[1-19]?signal-peptide


","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-43 are identical to a protein domain (PD237874) which is seen in Q9F259_ACTAC. ","","Wed Jun 25 17:15:20 2003","Wed Jun 25 17:15:20 2003","Wed Jun 25 17:15:20 2003","Wed Jun 25 17:15:20 2003","","","Wed Jun 25 17:15:08 2003","","","Thu Mar 18 16:53:35 2004","Thu Jun 19 16:11:22 2003","Thu Jun 19 16:11:22 2003","Sat Aug 23 16:52:57 2003","","Sat Aug 23 16:52:57 2003","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found in A.actinomycetemcomitans.","Thu Jun 19 16:11:22 2003","Sat Aug 23 16:52:57 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160089Chen J, Leblanc DJ, Galli DM.DNA inversion on conjugative plasmid pVT745.J Bacteriol. 2002 Nov;184(21):5926-34.PMID: 12374826Novak KF, Dougherty B, Pelez M.Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid andin the chromosome.Microbiology. 2001 Nov;147(Pt 11):3027-35.PMID: 11700353","","Thu Mar 18 16:53:35 2004","","4","","","" "pVT21","12696","12860","165","ATGAGCTTAAATACACAGAATAACTATCGTAAAGATGACTACCTACCRCMAAAAGTGACGCTTTCCGAAGAAGCGTTATTTTTTGCACGGCTAGATAACGGAGAAATTAAAGTCAAATCCAATGAAGAAGTATTAGCTAACCTGGAAAAAGTATTGGGCTTAAAA","","","6182","MSLNTQNNYRKDDYLPXKVTLSEEALFFARLDNGEIKVKSNEEVLANLEKVLGLK","","","hypothetical protein taken from A.actinomycetemcomitans plasmid pVT745","Cytoplasm","This sequence corresponds to GI:10954430, a hypothetical from pVT745 in GenBank.No near neighbors using gapped BLAST at this time.","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-55 are identical to a protein domain (PD253686) which is seen in Q9F258_ACTAC. ","","","Wed Jun 25 17:15:42 2003","Wed Jun 25 17:15:42 2003","Wed Jun 25 17:15:42 2003","","","Wed Jun 25 17:15:31 2003","Wed Jun 25 17:15:42 2003","","","Sun Aug 24 13:56:01 2003","Sun Aug 24 13:57:50 2003","Sat Aug 23 16:54:27 2003","","Sat Aug 23 16:54:27 2003","yes","Fri Feb 20 15:41:32 MST 1998","There are no paralogous sequence in A.actinomycetemcomitans.","Sun Aug 24 13:59:25 2003","Sat Aug 23 16:54:27 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Chen J, Leblanc DJ, Galli DM.DNA inversion on conjugative plasmid pVT745.J Bacteriol. 2002 Nov;184(21):5926-34.PMID: 12374826Novak KF, Dougherty B, Peláez M.Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid andin the chromosome.Microbiology. 2001 Nov;147(Pt 11):3027-35.PMID: 11700353Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160089","","Sun Aug 24 13:56:01 2003","","4","","","" "pVT22","12860","13144","285","ATGAAATTGGATTACACCGTAGTTTGGATGGAAGAAGCGGAACAACAGCTTTTAGAAAAAGCTCGTTTTATTTTGTATGATAGTCAAAGCAGGGAAGTTTCTTTTCGCTTTCACCGGGAAATTAGAGAACTGACCCAAAAACTATCCTATGTAGCAACCGCTTATAATGATGGTCGATTTCATATCTATACGGTTAAGAACGGGCATAGCGTAAAATTTATTGTGCGGAATGGCAGGGTTTATATTTCCGCTTTCTTGGCAAAAGGGCGTGAATTTGTAATATAG","","","11223","MKLDYTVVWMEEAEQQLLEKARFILYDSQSREVSFRFHREIRELTQKLSYVATAYNDGRFHIYTVKNGHSVKFIVRNGRVYISAFLAKGREFVI$","","","conserved hypothetical protein taken from plsmid pVT745 in A.actinomycetemcomitans","Cytoplasm","This sequence corresponds to GI:10954431, classified unknown in GenBank.Nearest neighbor is GI:23467550, a hypothetical from H.somnus.","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-94 are identical to a protein domain (PD281588) which is seen in Q9F257_ACTAC. ","","","","Wed Jun 25 17:31:57 2003","Wed Jun 25 17:31:57 2003","","","Wed Jun 25 17:31:57 2003","Wed Jun 25 17:31:57 2003","","","Sun Aug 24 14:04:06 2003","Sun Aug 24 14:04:06 2003","Sat Aug 23 16:55:08 2003","","Sat Aug 23 16:55:08 2003","yes","Fri Feb 20 15:41:32 MST 1998","There are no paralogous sequences in A.actinomycetemcomitans.","Sun Aug 24 14:05:01 2003","Sat Aug 23 16:55:08 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Chen J, Leblanc DJ, Galli DM. DNA inversion on conjugative plasmid pVT745. J Bacteriol. 2002 Nov;184(21):5926-34. PMID: 12374826 Novak KF, Dougherty B, Peláez M. Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid and in the chromosome. Microbiology. 2001 Nov;147(Pt 11):3027-35. PMID: 11700353Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 1116","","Sun Aug 24 14:05:01 2003","","4","","","" "pVT23","13556","13227","330","ATGAAAAAGCCCTTTAAAATTGGTGTAATCTTTCTTGCTTTATGCAGTATGAGCCAAATAAGCCATGCGGTGGATGAATTAACCGGTGATACAAAAACCGCCTGTGAAGCTCTACTCTGCTTATCATCACCAAAAGACGCGGCGAAAACGCCGGAATGTCATCCGCCGTTAAATAAGTTCTATTCAATTCGGGCTAAAAAACCACACGAAACATTAAAGAAACGTCGTAATTTTTTAAAATTGTGTCCGGATTCTAACGAGGACTCTATTAATCAAGCGTTATCGAGCAAATGCGCCCGCAAGCCGTTCAGTCGAAAATGTATATTTAAA","","","12325","MKKPFKIGVIFLALCSMSQISHAVDELTGDTKTACEALLCLSSPKDAAKTPECHPPLNKFYSIRAKKPHETLKKRRNFLKLCPDSNEDSINQALSSKCARKPFSRKCIFK","","mating-associated","conserved hypothetical protein taken from plasmid pVT745 in A.actinomycetemcomitans","Periplasm","This sequence corresponds to GI:10954432, classified an unknown in GenBank. Galli et al. speculate that it may be an export signal protein related to TrbM from E.coli plasmid IncPa.Nearest neighbor is GI:21628946, a YggA-like protein from Haemophilus influenzae.","
InterPro
IPR009989
Family
TrbM
PF07424\"[1-102]TTrbM


","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-23 are identical to a protein domain (PD521886) which is seen in Q9F256_ACTAC. Residues 24-104 are identical to a protein domain (PD337976) which is seen in Q9F256_ACTAC. ","","Wed Jun 25 17:31:41 2003","Wed Jun 25 17:31:41 2003","Wed Jun 25 17:31:41 2003","Wed Jun 25 17:31:41 2003","","","Wed Jun 25 17:31:41 2003","","","","Sun Aug 24 14:09:36 2003","Sun Aug 24 14:09:36 2003","Sat Aug 23 16:56:07 2003","","Sat Aug 23 16:56:07 2003","yes","Fri Feb 20 15:41:32 MST 1998","There are no paralogus sequences in A.actinomycetemcomitans.","Sun Aug 24 14:10:52 2003","Sat Aug 23 16:56:07 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Chen J, Leblanc DJ, Galli DM. DNA inversion on conjugative plasmid pVT745. J Bacteriol. 2002 Nov;184(21):5926-34. PMID: 12374826 Novak KF, Dougherty B, Peláez M. Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid and in the chromosome. Microbiology. 2001 Nov;147(Pt 11):3027-35. PMID: 11700353Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160","","Sun Aug 24 14:10:52 2003","","4","","","" "pVT24","13977","13543","435","ATGAAAAAATTTTTAATTATGAATACGTTAATCCCTGTTTGCTTTTTAAGCGCATGCAGCTCATCACCGCCTTTACCGCCACAAATCGATGAAGACGCCCCGGCAATCCATTTAAATAATCAGGTGTACCGACAAACACCAACTGCAACAGTGCCAAAAAACGCCGGCGATCATAATGGGCAACCTTGGGTATATCAATATGTGAACCTAGATAGAAGCGATTATGTGAATGAAACAGAAAAAGTTCGTTTTTTCTACTTTGCGCATCATGCAGATAGTATTGAAATCTACGGTCAGCCGGCGCGTACCGAAGCCTATAAATACTGGTTACAGGCAAATGGGGTAAGTGCCAATATCAGTACATATCAGAAAGACCTATTAAAAAATAATGTCAATATAACTTTCAGGAAAGGAGTTAAAAATGAAAAAGCCCTT","","","16538","MKKFLIMNTLIPVCFLSACSSSPPLPPQIDEDAPAIHLNNQVYRQTPTATVPKNAGDHNGQPWVYQYVNLDRSDYVNETEKVRFFYFAHHADSIEIYGQPARTEAYKYWLQANGVSANISTYQKDLLKNNVNITFRKGVKNEKAL","","","hypothetical protein taken from pVT745 in A.actinomycetemcomitans; possible mating-associated lipoprotein","Periplasm, Outer membrane","This sequence coresponds to GI:10954433, a predicted lipoprotein in GenBank. Galli et al. suggest that it is mating-associated.There are no near neighbors in GenBank at this time. There are several very weak matches to cagT proteins from bacteria.","
noIPR
unintegrated
unintegrated
PS51257\"[1-19]TPROKAR_LIPOPROTEIN


","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-145 are 91% similar to a protein domain (PD300009) which is seen in Q9F255_ACTAC. ","","Wed Jun 25 17:18:37 2003","Wed Jun 25 17:18:37 2003","Wed Jun 25 17:18:37 2003","Wed Jun 25 17:18:37 2003","","","Wed Jun 25 17:18:24 2003","","","Sun Aug 24 14:17:50 2003","Sun Aug 24 14:16:33 2003","Sun Aug 24 14:16:33 2003","Sat Aug 23 16:56:27 2003","","Sat Aug 23 16:56:27 2003","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found in A.actinomycetemcomitans.","Sun Aug 24 14:17:50 2003","Sat Aug 23 16:56:27 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Chen J, Leblanc DJ, Galli DM. DNA inversion on conjugative plasmid pVT745. J Bacteriol. 2002 Nov;184(21):5926-34. PMID: 12374826 Novak KF, Dougherty B, Peláez M. Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid and in the chromosome. Microbiology. 2001 Nov;147(Pt 11):3027-35. PMID: 11700353Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 1116","","Sun Aug 24 14:17:50 2003","","4","","","" "pVT25","15750","14014","1737","ATGATGAAAAAAGCCAATATTGCATTATTTCTGTTTGTCACTTTGATTCCGACGTATTTTCTAAGTGGGCTTTTACTTCTACTGGCAAATAAAATTCGTTTAATCGAAGCATTTAAGCGCTACTACCCTACTCTAACGCTGGATGCCATTTGGGGTAATTATCCGAAAATATGGCAGTCTCTCCTTATTAGTTTTGTAGTGAGCTTATTAATCATGCTAAAACTATTCTATCAACCTAAAAAATCCCTTTATGGTAACGCTGAATTTGCCACAAAATCAGAAGTACAAAAAATGGGTTTATTGGAAGAAAAAAACGGGATTATTGTCGGCAAACTCGGTAATAAACTGCTCCGTTTTATCGGTGCGCAATTTGTTTCACTGGCAGCGCCGACACGGGGAGGTAAAAGCGTAGGGATTGTTATTCCAAATTTGCTGGCATGGGAACAATCTGTGGTTGTGAAGGACATTAAAAACGAATGCTATCGTATCACCAGTAAATATCGACAAAAAATATTAGGGCAAAAGGTATATCGCTTTGCCCCGTTTGACCGTAATACGCACCGGTTTAATCCGCTGGATTGTATTGATATGCGCGACCAGGCGCGCGCCGAACTCGATTTAAAAAATCAGGCTATGGGCTTATATCCGCTCACCGGCGACCCGGATAAAGACTTTTGCCAGCACCAGGCACAGAATCTTTTTGTAGCAACCACTTTTTTACTGTGGGATATGCGCCAAAAAAGCCTTACCGATATGATACTGACCTATGCCAATCTATTACGCTTACATGCCGGTTTTGATGAAACTCAAGAAGACGGTTCGATAGAACATATCGATTTTGCACAACATGCGCGCTTATGCGTTCAATCCGGCATTGCTCACCCAACAACTGCCGATAAACTTAACATTTATTTAATGGCGTGCGAATCCGGTAAAACAAAAAGTAGTATCGATTCAACCTTTATCAGTCCGTTAACCATTTTTCAAAATGAAATTGTTGAACACGCTACCTCTGCCAGTGATTTTGATTTACGCGCCTTGCGCCGGGAAAAAATCACGATTTATTTCCACATTTCAGCAAATGATTTAATCCTGGCTCCGCAAGTCGCTAATCTGTTTATGAGCATGGTTATTGCCAACAATATTGACGAACTACCGGAAACCAACCCGGCATTAAAATATCAGTTATTACTACTCATGGATGAATTTACTGCTGTCGGGATGTTGAGCATTATCAATAAATCGGTAGGTTTTATCGCCGGTTATGGTTTACGCTTATTAATCATTTATCAATCGCAAGGGCAACTTCGTGCTGATAAACCAAATGGTTATAGTAAAGATGGTGCTAAAGCTATCCTGGATAATATCGCCTGTAAAATTCTATATGCCCCCGACAATCAGGAGGACGCGGAAGAATATTCTAAGGTGCTAGGTAATCGCACTGTAAATAAATTAAGCCATAGTCGAGGTAAAACACCCAGTCACAGTATTACCGACCATGGGCGACCATTGCTTTTACCGCAGGAATTTAGATTAATCGGCGAATTTAAAGAAGTGGTAATGTTAAATAACAGCAAACCGATTATGTGTAATAAGGCAGTGTATTACAACGATCCTTATTTTATAGACAAACTCAAAGCGGTATCTCCGCAATTGCGGGCATTAGGTAAAAAATTACCGACTAAAGAGCAACTGGAAAAAGCCATGTTCAGTGGCGAGCTGTCAGTCCAATCAATT","","","65365","MMKKANIALFLFVTLIPTYFLSGLLLLLANKIRLIEAFKRYYPTLTLDAIWGNYPKIWQSLLISFVVSLLIMLKLFYQPKKSLYGNAEFATKSEVQKMGLLEEKNGIIVGKLGNKLLRFIGAQFVSLAAPTRGGKSVGIVIPNLLAWEQSVVVKDIKNECYRITSKYRQKILGQKVYRFAPFDRNTHRFNPLDCIDMRDQARAELDLKNQAMGLYPLTGDPDKDFCQHQAQNLFVATTFLLWDMRQKSLTDMILTYANLLRLHAGFDETQEDGSIEHIDFAQHARLCVQSGIAHPTTADKLNIYLMACESGKTKSSIDSTFISPLTIFQNEIVEHATSASDFDLRALRREKITIYFHISANDLILAPQVANLFMSMVIANNIDELPETNPALKYQLLLLMDEFTAVGMLSIINKSVGFIAGYGLRLLIIYQSQGQLRADKPNGYSKDGAKAILDNIACKILYAPDNQEDAEEYSKVLGNRTVNKLSHSRGKTPSHSITDHGRPLLLPQEFRLIGEFKEVVMLNNSKPIMCNKAVYYNDPYFIDKLKAVSPQLRALGKKLPTKEQLEKAMFSGELSVQSI","","Galli et al. propose that this ATPase is involved in \"coupling of DNA processing to DNA transport.\"","conserved hypothetical protein taken from plasmid pVT745 in A.actinomycetemcomitans.","Inner membrane, Cytoplasm","This sequence corresponds to GI:10954434, a predicted ATPase in GenBank.Nearest neighbor is GI:16751946, a predicted traN protein from Plasmid pIPO2T taken from wheat. See also GI:10956727, a predicted conjugal transfer protein from Xylella fastidiosa.","
InterPro
IPR003688
Family
TRAG protein
PF02534\"[88-562]TTraG
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.300\"[123-545]Tno description
signalp\"[1-37]?signal-peptide
tmhmm\"[9-29]?\"[57-77]?transmembrane_regions


","BeTs to 4 clades of COG3505COG name: Type IV secretory pathway, VirD4 componentsFunctional Class: NThe phylogenetic pattern of COG3505 is ------------------s-ujx---Number of proteins in this genome belonging to this COG is","***** IPB003688 (TRAG protein) with a combined E-value of 2.9e-28. IPB003688B 124-169 IPB003688C 327-342 IPB003688D 393-431 IPB003688E 465-490","Residues 389-550 are identical to a protein domain (PD003889) which is seen in Q9F254_ACTAC. Residues 125-378 are 38% similar to a protein domain (PD296999) which is seen in Q93TC4_XANCP. Residues 83-393 are 25% similar to a protein domain (PD042125) which is seen in O25260_HELPY. Residues 314-378 are identical to a protein domain (PD491279) which is seen in Q9F254_ACTAC. Residues 325-378 are 46% similar to a protein domain (PD519955) which is seen in Q91UW5_ECOLI. Residues 212-313 are identical to a protein domain (PD566638) which is seen in Q9F254_ACTAC. Residues 312-387 are 42% similar to a protein domain (PD491280) which is seen in Q9F531_ECOLI. Residues 84-211 are identical to a protein domain (PD007793) which is seen in Q9F254_ACTAC. Residues 1-83 are 77% similar to a protein domain (PD454634) which is seen in Q9F254_ACTAC.","","Wed Jun 25 17:16:55 2003","Wed Jun 25 17:16:55 2003","Wed Jun 25 17:16:55 2003","Sun Aug 24 14:28:27 2003","","","Wed Jun 25 17:16:41 2003","Sun Aug 24 14:28:27 2003","","Sun Aug 24 14:28:27 2003","Sun Aug 24 14:27:21 2003","Sun Aug 24 14:28:27 2003","Sat Aug 23 16:56:54 2003","Sat Aug 23 16:56:54 2003","Sun Aug 24 14:22:47 2003","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found in A.actinomycetemcomitans.","Sun Aug 24 14:28:27 2003","Sat Aug 23 16:56:54 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Chen J, Leblanc DJ, Galli DM. DNA inversion on conjugative plasmid pVT745. J Bacteriol. 2002 Nov;184(21):5926-34. PMID: 12374826 Novak KF, Dougherty B, Peláez M. Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid and in the chromosome. Microbiology. 2001 Nov;147(Pt 11):3027-35. PMID: 11700353Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 1116","","Sun Aug 24 14:28:27 2003","","4","","","" "pVT26","16781","15753","1029","ATGGTCATAAATTCTTCCGGTGATGTATCAATTTTACTTCATGCCAATAAATTATTCGGAGAATTGCTCGAAGACGAAGCCATTACAGAAATTGCGATTAATCGCCCCGGTGAAATTTTCTTTGAAAAAAAAGGCGTATGGCATTATCAAGACGCTCCGCATATTACTTATGATTTATGTGATTCTTTTGNTCGGGCGTTAGCCAAGTATCGCGGGGATTATATCAGTGATACCAAACCAATTTTATCTGCGGTATTACCGAACGGCGAGCGGACACAGATTATTCTTCCGCCCGCCAGTGAACGGGAAACCATCAGTATTACGGTGCGAAAACCGAATAAGTCTTTTTTTGACCTGGATTATTACATCAACAACGGCTTTTTTAGTCGTGTTATCAAGACGGAAAATCGTTTGTCAGATGATGACCGGACACTACTGGAAATTTATCATAAGGGTGATTATGCGGAATTCCTTAAACAAGCGGTCATTTGCGGGAAAAATATTGTGATTGCCGGGGAAACCGGTTCCGGGAAAACCACTTTAATGAAAGCCCTGGTCGATTATATTCCGTTGCATGAACGCCTAGGCACCATCGAAGATACTCCGGAATTATTCTTACGCCAACATAAGAATTATTTCCACTTATTCTATCCAAGTGAAGCAAAAAATGGTGATTTAATCACAGCAGCCTCTTTGCTGAAATCCTGCTTACGGATGAAGCCTGATCGTATTCTGCTTGCGGAATTACGCGGAGGGGAAACCTATGATTTTATCAATGTTGTTTCTTCCGGGCATAACGGCTCGATTACCTCTTGTCACGCCGGTTCGGTTGCTGAAACTTGGGAACGGCTTATCTTAATGACCTTGCAAAATGACCAGGGACGCACCCTCTCTTATGATGTGATCCGTCGTTTATTGCAACAAACCATAGATATTATCATGCATGTTACAAATAGCCACGAATACGGCAGACATATGACGGAAATCTATTTTGATCCGCAAGCTAAAATAAATTCGCTCAAGGTAGGT","","","38794","MVINSSGDVSILLHANKLFGELLEDEAITEIAINRPGEIFFEKKGVWHYQDAPHITYDLCDSFXRALAKYRGDYISDTKPILSAVLPNGERTQIILPPASERETISITVRKPNKSFFDLDYYINNGFFSRVIKTENRLSDDDRTLLEIYHKGDYAEFLKQAVICGKNIVIAGETGSGKTTLMKALVDYIPLHERLGTIEDTPELFLRQHKNYFHLFYPSEAKNGDLITAASLLKSCLRMKPDRILLAELRGGETYDFINVVSSGHNGSITSCHAGSVAETWERLILMTLQNDQGRTLSYDVIRRLLQQTIDIIMHVTNSHEYGRHMTEIYFDPQAKINSLKVG","","","ATPase (related to VirB11 proteins) taken from plasmid pVT745 in A.actinomycemtemcomitans","Cytoplasm","This sequence corrsponds to GI:10954435, a predicted mating-associated ATPase in GenBank (Galli et al.). It is also equal to GI:13345959, a predicted transport associated protein 11 (Novak et al.)Nearest neighbor is GI:15919979, a predicted TraM protein from plasmid pSB102 taken from alfalfa. See also GI:17988379, a predicted ATPase (virB11) from Brucella melitensis.","
InterPro
IPR001482
Domain
Bacterial type II secretion system protein E
PD000739\"[153-242]TGSPII_E
PF00437\"[6-320]TGSPII_E
InterPro
IPR002078
Domain
RNA polymerase sigma factor 54, interaction
PS00675\"[168-181]TSIGMA54_INTERACT_1
InterPro
IPR014155
Family
P-type DNA transfer ATPase VirB11
TIGR02788\"[22-331]TVirB11
noIPR
unintegrated
unintegrated
G3DSA:3.30.450.90\"[8-112]TG3DSA:3.30.450.90
G3DSA:3.40.50.300\"[130-330]TG3DSA:3.40.50.300
SSF52540\"[16-328]TSSF52540


","No hits to the COGs database.","***** IPB001482 (Bacterial type II secretion system protein E) with a combined E-value of 2.8e-30. IPB001482B 164-186 IPB001482C 194-204 IPB001482D 233-277 IPB001482E 291-300","Residues 22-159 are 28% similar to a protein domain (PD545194) which is seen in Q8VMF6_PSEPU. Residues 28-119 are 42% similar to a protein domain (PD003019) which is seen in Q9F530_ECOLI. Residues 271-336 are identical to a protein domain (PD249357) which is seen in Q9F253_ACTAC. Residues 22-166 are 38% similar to a protein domain (PD548463) which is seen in Q8VRC8_HAEAE. Residues 23-111 are 30% similar to a protein domain (PD035142) which is seen in O50338_ECOLI. Residues 248-331 are 32% similar to a protein domain (PD022237) which is seen in Q9ZDN5_RICPR. Residues 21-113 are identical to a protein domain (PD270007) which is seen in Q9F253_ACTAC. Residues 12-139 are 34% similar to a protein domain (PD486547) which is seen in P96528_HELPY. Residues 167-265 are identical to a protein domain (PD000739) which is seen in Q9F253_ACTAC. Residues 23-100 are 35% similar to a protein domain (PD274147) which is seen in Q981R8_RHILO. Residues 114-166 are identical to a protein domain (PD536814) which is seen in Q9F253_ACTAC.","","Wed Jun 25 17:18:11 2003","Wed Jun 25 17:18:11 2003","Wed Jun 25 17:18:11 2003","Sun Aug 24 14:39:55 2003","","","Wed Jun 25 17:17:58 2003","","","Sun Aug 24 14:39:55 2003","Sun Aug 24 14:37:02 2003","Sun Aug 24 14:37:02 2003","Sat Aug 23 16:57:13 2003","Sat Aug 23 16:57:13 2003","Sun Aug 24 14:37:02 2003","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to the chromosomal AA0572 tadA gene that is predicted to encode a tight adherence protein A in A.actinomycetemcomitans.","Sun Aug 24 14:39:55 2003","Sat Aug 23 16:57:13 2003","pdb|1G6O|1G6O-A CRYSTAL STRUCTURE OF THE HELICOBACTER PYLORI 200.0 4e-52","","","No significant hits to the Pfam 7.3 database.","","","","Chen J, Leblanc DJ, Galli DM. DNA inversion on conjugative plasmid pVT745. J Bacteriol. 2002 Nov;184(21):5926-34. PMID: 12374826 Novak KF, Dougherty B, Peláez M. Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid and in the chromosome. Microbiology. 2001 Nov;147(Pt 11):3027-35. PMID: 11700353Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160","","Sun Aug 24 14:39:55 2003","","4","","","" "pVT27","17903","16797","1107","ATGAACGATAACAAAACCATTCAGCCGACGGATGACAAAACGGAAACCGATTATCAACCGGAAGTCAGCAAAATTGCCAAACGCGGTAAAAACCAAAATTTATTTATTTTTCTGATTATTGCACTGCTTGCCGTGGCGTTTTTGGGTTATTCCTTTTTGAATAAAAAGGATACGCAACCGGCACAAGCTAAGGAAAAAGAAGAATTCGGTACGACGGTGCGTTCAAAAACATTTACGGCACCACCGGCAGAAATCCCGGCGATTTTAAATCCGGAGCCACAACCAATTTCTACCGCAACCGCTCCAGTAGAAAATCATAGTACGACAGAGGCGTTAGATATGCCATCCGCCCCACGTTTAATCAAAGGATTGTCTCCGGGTACTATCAATGGCGAAACGTTACAANCCGTTTCAGATGTTCAGAATACAGATACAACTGACACGGTAACTAACCAACCACCGGAACCGGCAAAAGGCGATATATTTGAAGATAACGTCAGTACGTTTAAAGCAGGTAAAGCCCATAAACTCCCGGTCAATGCCAATTTACTGTTGGCAAAAGGCACGTTTATACAATGTTCCTTACGCACAAAACTTGTTTCCACTGTGGCCGGCAATCTAGGCTGCGTTGTGGCAAACGATGTATATAGTGCAAACGGTACGGTATTACTGATTGAAAAAGGCTCTACCGTGTTTGGTGAATTCCGTAACGGTCAAATTCAGCAGGGCGAAGAACGTTTATTTGTTGTTTGGAGTGAAATACGTACACCCAAAAATATCATTATCAACGTTAATTCCGGCGCAACTGATGAATTAGGCGGAACCGGTATTCCGGGCTATGTAGATAATCATTTCTGGGAACGTTTCGGTAATGCCATCATGTTAAGCATGATCACCGATTCAACCAGTGCACTATCTACCCAATTAGCCAAACGGGGGACATTTAATCCGACTGATACGGTGCAAGCCGGCTCGGAAATTGCACAAAGTATCTTAGAGAAAACCATTAATATTCCCCCTACGCTTTATAAGAACCAAGGGGATTTAGTGGGGATTTTTGTTGCACGAGATATTGATTTTGGCGATGTGTACGAATTGAAACAGAAA","","","39893","MNDNKTIQPTDDKTETDYQPEVSKIAKRGKNQNLFIFLIIALLAVAFLGYSFLNKKDTQPAQAKEKEEFGTTVRSKTFTAPPAEIPAILNPEPQPISTATAPVENHSTTEALDMPSAPRLIKGLSPGTINGETLQXVSDVQNTDTTDTVTNQPPEPAKGDIFEDNVSTFKAGKAHKLPVNANLLLAKGTFIQCSLRTKLVSTVAGNLGCVVANDVYSANGTVLLIEKGSTVFGEFRNGQIQQGEERLFVVWSEIRTPKNIIINVNSGATDELGGTGIPGYVDNHFWERFGNAIMLSMITDSTSALSTQLAKRGTFNPTDTVQAGSEIAQSILEKTINIPPTLYKNQGDLVGIFVARDIDFGDVYELKQK","","mating-associated","virB10-related protein involved in channel formation taken from plasmid pVT745 in A.actinomycetemcomitans.","Periplasm, Inner membrane, Extracellular","This sequence coresponds to GI:13345958 in GenBank, a predicted transport associated protein 10 similar to virB10 according to Novak et al. See also GI:10954436.Nearest neighbor is GI:16751944, a TraL protein from plasmid pIPO2T from wheat. See also GI:17988378, a predicted channel protein (virB10 related) from Brucella melitensis.","
InterPro
IPR005498
Family
Bacterial conjugation TrbI-like protein
PF03743\"[185-365]TTrbI


","BeTs to 4 clades of COG2948COG name: Type IV secretory pathway, VirB10 componentsFunctional Class: 0, ,NThe phylogenetic pattern of COG2948 is ------------------s-ujx---Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 1-197 are 83% similar to a protein domain (PD305750) which is seen in Q9F252_ACTAC. Residues 198-358 are identical to a protein domain (PD005005) which is seen in Q9F252_ACTAC. ","","Wed Jun 25 17:31:25 2003","Wed Jun 25 17:31:25 2003","Wed Jun 25 17:31:25 2003","Sun Aug 24 14:48:22 2003","","","Wed Jun 25 17:31:25 2003","","","","Sun Aug 24 14:48:22 2003","Sun Aug 24 14:47:04 2003","Sat Aug 23 16:57:37 2003","","Sat Aug 23 16:57:37 2003","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found in A.actinomycetemcomitans.","Sun Aug 24 14:47:04 2003","Sat Aug 23 16:57:37 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Chen J, Leblanc DJ, Galli DM. DNA inversion on conjugative plasmid pVT745. J Bacteriol. 2002 Nov;184(21):5926-34. PMID: 12374826 Novak KF, Dougherty B, Peláez M. Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid and in the chromosome. Microbiology. 2001 Nov;147(Pt 11):3027-35. PMID: 11700353Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 111","","Sun Aug 24 14:48:22 2003","","4","","","" "pVT28","18782","17916","867","ATGAGGCTTAATATGCGAATTTTAATCTGTTTATTACTTATCGTGTTTGGTACAGAAACTTATGCAGCCAGCACACCGATAAAATCAAAATATGATAACCGTATTCAGTCACAAGTTTATAACGCTTTAGATGTCACAAAGGTTTATGCAAAAGATGGATTTTCTACCGTAATCATTTTTGCCGATGATGAACGTATTCTATACAAACACACCGGTTTTAAAGACGGTTGGGATATTACCGATAATGATAATTTTGTATTGATTAAACCAATGGCGGTAAAACAACAAAGCAGTGAGGGCGAAAACTATTTTGAACCGACCCCGGGGCAGTGGAATACGAACTTGTTTATTAATACTAATAAACGCACGTACTCCTTTGATTTAATACTCGTACCGGAAAACTCAACGTCATCATATCAGGTAAATTTTTCCTATCCGACGGAGAAACAAAAACAGTTAGCCGCACAACGTCAAAAGAATAAACGCGAACGTGAACAACAAGCGATTGAAAAATCTTTGCAAAGCACTAAAACACCGAAAAATTGGGATTACGTAATGAAAGTGAAAGCCGGTAGCGAAACCATTACACCGAACTATGCGTACGATGATGGCATATTTACTTATCTTGGCTTCGCCCCGAATAAAACCTTTCCTGCAGCCTTCTTGTTAGAAGGCTCCACGGAAAGTCTGTTAAATACCAATGTTAAACAAGATGGTAATTATCAGGTATTAGTCATCCAAAAAACAGCAGAAAAATTGGTGTTACGTAGCGGTGAAAAAGTGGTCGGCATTTACAATCAAAGTTACGGAAAAACACCGGTAACTTATAACACGACCATTTCACCAAATGTGGCAAGAGACGAACGA","","","32971","MRLNMRILICLLLIVFGTETYAASTPIKSKYDNRIQSQVYNALDVTKVYAKDGFSTVIIFADDERILYKHTGFKDGWDITDNDNFVLIKPMAVKQQSSEGENYFEPTPGQWNTNLFINTNKRTYSFDLILVPENSTSSYQVNFSYPTEKQKQLAAQRQKNKREREQQAIEKSLQSTKTPKNWDYVMKVKAGSETITPNYAYDDGIFTYLGFAPNKTFPAAFLLEGSTESLLNTNVKQDGNYQVLVIQKTAEKLVLRSGEKVVGIYNQSYGKTPVTYNTTISPNVARDER","","mating-associated","VirB9-like protein possibly involved in channel formation; taken from plasmid pVT745 in A.actinomycetemcomitans","Outer membrane, Extracellular","This sequence corresponds to GI:10954437, an unknown according to Galli et al. in GenBank. See also GI:13345957, a predicted transport associated protein 9 according to Novak et al.Nearest neighbor is GI:29164812, a VirB9-like protein from Campylobacter jejuni.","
InterPro
IPR010258
Family
Conjugal transfer protein TrbG/VirB9/CagX
PF03524\"[32-268]TCagX
InterPro
IPR014148
Family
P-type conjugative transfer protein VirB9
TIGR02781\"[6-269]TVirB9


","BeTs to 4 clades of COG3504COG name: Type IV secretory pathway, VirB9 componentsFunctional Class: NThe phylogenetic pattern of COG3504 is ------------------s-ujx---Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 181-258 are 45% similar to a protein domain (PD013911) which is seen in Q9RPX6_BRUSU. Residues 259-289 are identical to a protein domain (PD485399) which is seen in Q9F251_ACTAC. Residues 168-258 are identical to a protein domain (PD290473) which is seen in Q9F251_ACTAC. Residues 21-148 are identical to a protein domain (PD275166) which is seen in Q9F251_ACTAC. ","","Wed Jun 25 17:31:08 2003","Wed Jun 25 17:31:08 2003","Wed Jun 25 17:31:08 2003","Sun Aug 24 14:53:40 2003","","","Wed Jun 25 17:31:08 2003","","","","Sun Aug 24 14:52:52 2003","Sun Aug 24 14:52:52 2003","Sat Aug 23 16:57:55 2003","","Sat Aug 23 16:57:55 2003","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found in A.actinomycetemcomitans.","Sun Aug 24 14:53:40 2003","Sat Aug 23 16:57:55 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Chen J, Leblanc DJ, Galli DM. DNA inversion on conjugative plasmid pVT745. J Bacteriol. 2002 Nov;184(21):5926-34. PMID: 12374826 Novak KF, Dougherty B, Peláez M. Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid and in the chromosome. Microbiology. 2001 Nov;147(Pt 11):3027-35. PMID: 11700353Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160","","Sun Aug 24 14:53:40 2003","","4","","","" "pVT29","19458","18775","684","ATGACCAATATCGAACAAGAANTTCTTGACCAAAATCGGGATTTAGAAGCCAAAAACCAGGAGAACATCGAAAAATCGGAAGCCCGCGCCTGGAAAGTGGCCAGAGTATCCTGGCTGATTAGCCTTGTTCTCGGTGCGGTCACTGTCAGTATTTTACCGTTGCGCGAGGTTGTGCCATTTCTGATTCGTGATAACGGTACGGGTATTCCTGACGTCATTACTCGTTTGGATGTGGAAACGTTGACCACGGATGACGCCATGGATAAACATTTCATCAGTCAATATATCACAAACCGTGAAGGCTATTATTTCAACACCTTNCAACAAGAATATGAACTTACGCAAATGATGAGTAGTGATGAAGTTGCGAAGGATTATCGTAGCATTTATGAAGGTAAGAATGCACGTGACCAAAAATTAGGTAGTAGTAACACCGTTAAACCAGAAATCAATTCTATTGTGTTATCTAAAAAAGAAGTTGGTACGGATGGCCAAGCAAGCAATATTGCCACTGCCCGCGTTCGTTTAATTCAACGTAATTTGTCAACTGGAGAAGAAACGGCAAAAAATATCGTAGTTTCTTTAACATACGAATATTTACCGGTAAAAAATATGGTTGAAGGGTTCCGCATGGATAACCCGTTAGGATTTATTGTGACACATTACCGGGTAGATAATGAGGCT","","","25656","MTNIEQEXLDQNRDLEAKNQENIEKSEARAWKVARVSWLISLVLGAVTVSILPLREVVPFLIRDNGTGIPDVITRLDVETLTTDDAMDKHFISQYITNREGYYFNTXQQEYELTQMMSSDEVAKDYRSIYEGKNARDQKLGSSNTVKPEINSIVLSKKEVGTDGQASNIATARVRLIQRNLSTGEETAKNIVVSLTYEYLPVKNMVEGFRMDNPLGFIVTHYRVDNEA","","Galli et al. speculate that this protein is a LysR regulatory protein involved in channel formation.","VirB8 homolog taken from plasmid pVT745 in A.actinomycetemcomitans","Outer membrane, Cytoplasm","This sequence corresponds to GI:10954438, an unknown in GenBank (Galli et al.). See also GI:13345956, predicted transport associated protein 8 according to Novak et al.Nearest neighbor is GI:29164810, a VirB8-like protein from Campylobacter jejuni.","
InterPro
IPR007430
Family
VirB8
PF04335\"[48-225]TVirB8


","BeTs to 4 clades of COG3736COG name: Type IV secretion system, component VirB8Functional Class: NThe phylogenetic pattern of COG3736 is ------------------s-ujx---Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 1-38 are identical to a protein domain (PD231136) which is seen in Q9F250_ACTAC. Residues 39-227 are identical to a protein domain (PD009791) which is seen in Q9F250_ACTAC. ","","Wed Jun 25 17:30:54 2003","Wed Jun 25 17:30:54 2003","Wed Jun 25 17:30:54 2003","Sun Aug 24 15:00:52 2003","","","Wed Jun 25 17:30:54 2003","","","Sun Aug 24 15:00:52 2003","Sun Aug 24 14:58:51 2003","Sun Aug 24 14:58:51 2003","Sat Aug 23 16:58:15 2003","","Sat Aug 23 16:58:15 2003","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found in A.actinomycetemcomitans.","Sun Aug 24 14:59:59 2003","Sat Aug 23 16:58:15 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Chen J, Leblanc DJ, Galli DM. DNA inversion on conjugative plasmid pVT745. J Bacteriol. 2002 Nov;184(21):5926-34. PMID: 12374826 Novak KF, Dougherty B, Peláez M. Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid and in the chromosome. Microbiology. 2001 Nov;147(Pt 11):3027-35. PMID: 11700353Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 111","","Sun Aug 24 15:00:52 2003","","4","","","" "pVT3","2369","1215","1155","ATGGGCGTTCGTATCGAAAAAGAATGGTTAGTTAGAAGAGCTAAAAAGGATTCTTTAATTTCTTATTCTGGCAATAAGAAATTTAGAGAGTCTAGCTATTCTTATCATGCTTCANCAAAACCAAAAACATTGCGTAATTCTAATGAGGTTATGGTTAAAATTACAAGTAGCGGGAAGAATCTTAAAGCTATCAAGTCACATATGGATTATATTTCAAGAAATGGTGAGATTCAGTTAGAGGATGAACAAGGGTTAGTTTATAAAGGTCGTGAGGAAGTGCGCGAGCTTAGAGATTATTTGCGTGATAATGGTGTTAAAATCAAGAAGAAAAATGAACCTAAACGCGAGTATCGACAAACGATGAATATTGTTTTTTCTATGCGTGATAAAAACATTCCGGAGGAAAAAATTAAGAAGGCTGTTAAAGCCACTTTGAAAAAATTATATCCTGATAATATGTTCGTGTTGGCTTATCATGGTGATACGGATAATCCTCATTGTCATGTTATTTTAAAAATTGCCGATAACAATGGAAATCGAGTTAATATCAATCTTCAYGATTTACAAGAAATCAGAACGCATTTTGCAAGATACCTTAATTCATTAAGTGTTGAGGCTAAGGCAACGCCGTTTAAAAAATCCATTAATAAATTACCTAGCCGAGCTGTCGAAATTGTCGATTTTGGTAAAGATTTTTATCAGCATAAGCCTGAAAATAAAATGAGTTATTTTGTGACGTATAAGGCGCAAAATGGTAAAAATGTGACGATATGGAGTAAAACATTAGAGCAAAGTTTATTATCCTCAGATGTTAAACGCGGTGATGTTATATCGCTTAAAGTTAGCCACATTGAAAAAGTTTCCTTGCCTCGATTTATAAATGATAAATCGGGAAATATGAGTAATGAAATTATCTTGAATCGTAAGCATTGGAAAACTGATATTGTTGAACGGTATAAAGGATTATCGTACAAAGCTGATCCGTTAATTGAATATCAACGTGCGAGACGGTTATCAATGTTGAATGCTTTAAATCAACAAGAACGCATTGCTAAGAGTAATGAAAAAGCCCTTTCTCCGAAAGAGCGTTATGAGCAAAATAAACGTAAGCTATTAAGTGAACGTAAATTGCCGTCTGCACAAGAACGTTTTAGG","","","44955","MGVRIEKEWLVRRAKKDSLISYSGNKKFRESSYSYHASXKPKTLRNSNEVMVKITSSGKNLKAIKSHMDYISRNGEIQLEDEQGLVYKGREEVRELRDYLRDNGVKIKKKNEPKREYRQTMNIVFSMRDKNIPEEKIKKAVKATLKKLYPDNMFVLAYHGDTDNPHCHVILKIADNNGNRVNINLHDLQEIRTHFARYLNSLSVEAKATPFKKSINKLPSRAVEIVDFGKDFYQHKPENKMSYFVTYKAQNGKNVTIWSKTLEQSLLSSDVKRGDVISLKVSHIEKVSLPRFINDKSGNMSNEIILNRKHWKTDIVERYKGLSYKADPLIEYQRARRLSMLNALNQQERIAKSNEKALSPKERYEQNKRKLLSERKLPSAQERFR","","Galli and colleagues report that \"sequences homologous to pVT745 have previously been detected in the chromosomes of numerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183 (5), 1585-1594 (2001)).Plasmid pVT745 is said to be a conjugative plasmid.","nickase from pVT745 taken from A.actinomycetemcomitans","Periplasm, Cytoplasm","This sequence corresponds to GI:10954412, a predicted nickase (labeled gene MagA2 in GenBank) taken from A.actinomycetemcomitans.Nearest neighbor is GI:7466660, a predicted nickase from plasmid R6K taken from E.coli. See also GI:1588987, a predicted DNA distortion polypeptide also from plasmid R6K taken from E.coli.","
InterPro
IPR005094
Family
Relaxase/mobilization nuclease
PF03432\"[60-307]TRelaxase


","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 291-385 are identical to a protein domain (PD282196) which is seen in Q9F276_ACTAC. Residues 215-290 are identical to a protein domain (PD351308) which is seen in Q9F276_ACTAC. Residues 43-212 are 92% similar to a protein domain (PD017616) which is seen in Q9F276_ACTAC. Residues 1-42 are identical to a protein domain (PD556317) which is seen in Q9F276_ACTAC. ","","Thu Jun 19 10:03:53 2003","Thu Jun 19 10:03:53 2003","Thu Jun 19 10:03:53 2003","Sat Aug 23 16:46:02 2003","","","Thu Jun 19 10:03:33 2003","","","Sat Aug 23 16:46:02 2003","Wed Jun 18 14:52:33 2003","Wed Jun 18 14:52:33 2003","Sat Aug 23 16:46:02 2003","","Sat Aug 23 16:46:02 2003","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are apparent in A.actinomycetemcomitans (however see the subthreshold match to AA0288).","Wed Jun 18 15:05:41 2003","Sat Aug 23 16:46:02 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160089Chen J, Leblanc DJ, Galli DM.DNA inversion on conjugative plasmid pVT745.J Bacteriol. 2002 Nov;184(21):5926-34.PMID: 12374826Novak KF, Dougherty B, Peláez M.Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid andin the chromosome.Microbiology. 2001 Nov;147(Pt 11):3027-35.PMID: 11700353","Flashner Y, Schlomai J, Shafferman A.Three novel plasmid R6K proteins act in concert to distort DNA within the alpha and beta origins of DNA replication.Mol Microbiol. 1996 Mar;19(5):985-96.PMID: 8830279Avila P, Núñez B, de la Cruz F.Plasmid R6K contains two functional oriTs which can assemble simultaneously in relaxosomes in vivo.J Mol Biol. 1996 Aug;261(2):135-43.PMID: 8757282","Sat Aug 23 16:46:02 2003","Wed Jun 18 15:02:28 2003","4","","","" "pVT30","19598","19458","141","ATGCAAAAAATATACAAATTATGCTTATTTTTTGTGCTTTTTAATCTGGTCGGTTGTTCGTCAAGTTGGCCGGATGATTTAAAAGGTACATCCTTTGAACCCATTAATAAAACAATGCAACCGCAAGGAGAACATAAAAAA","","","5418","MQKIYKLCLFFVLFNLVGCSSSWPDDLKGTSFEPINKTMQPQGEHKK","","Galli et al. speculate that this protein is a lipoprotein involved in channel formation.","hypothetical protein taken from pVT745 in A.actinomycetemcomitans; possible lipoprotein","Cytoplasm, Outer membrane","This sequence corresponds to GI:10954439, a predicted lipoprotein in GenBank.There are no near neighbors at this time.","
noIPR
unintegrated
unintegrated
signalp\"[1-22]?signal-peptide
tmhmm\"[5-23]?transmembrane_regions


","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-47 are identical to a protein domain (PD242891) which is seen in Q9F249_ACTAC. ","","Wed Jun 25 17:19:47 2003","Wed Jun 25 17:19:47 2003","Wed Jun 25 17:19:47 2003","Wed Jun 25 17:19:47 2003","","","Wed Jun 25 17:19:37 2003","","","Sun Aug 24 15:04:10 2003","Sun Aug 24 15:04:10 2003","Sun Aug 24 15:05:04 2003","Sat Aug 23 16:58:50 2003","","Sat Aug 23 16:58:50 2003","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences are found in A.actinomycetemcomitans.","Sun Aug 24 15:05:04 2003","Sat Aug 23 16:58:50 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Chen J, Leblanc DJ, Galli DM. DNA inversion on conjugative plasmid pVT745. J Bacteriol. 2002 Nov;184(21):5926-34. PMID: 12374826 Novak KF, Dougherty B, Peláez M. Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid and in the chromosome. Microbiology. 2001 Nov;147(Pt 11):3027-35. PMID: 11700353Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160","","Sun Aug 24 15:05:04 2003","","4","","","" "pVT31","20668","19670","999","ATGAGATTCTTTGAGAGTATCGATTCTTTCGTTATTCAGTTATTGGATTCAGTTAGTCAATCTATGAGTAGCAATTTTGCTAACTCACTTTTTACAATTATTGGCGTAACACTGACAATTTACTTTTTAGGAAAAGGATTTGCCGTAATATCTGGCAAGATTGAAGCTCCAGCAACAGCATTAATTTATGATTTTGCCACAAAAATGATCATTGTAGCATTTATGATGAATTATGGAGGGTATCTGGATAACTCTTTAGCGATAATTGATGATCTCAAAACTAGCTTAACCGGCTTTACCGGAAACGGTATAGCCGGTTTAATGGATGACCAATTGGAATTAGGATCGGATATTGCTGGTCAACTCTTTGATCTAGATAAATCTAAATATGTCCCCTTAGAAGGTGGAATTGCTTCATTTCTTGCCTGGATTGGTGTAGCAGTATCTTTATTTGTGCCATTTATTATTTTTATTACTACAACTATCACATTAAAACTATTGACTGTAACTGCCCCTATTTTCATCTTTTGTCTATTATACAATTTCTTACGCAATACCTTTAATCAGTGGTTACAGCTTATTTTGGCAAATATACTTACTGTTGTATTTATTGGTATTTCACTTCGCATGGGGATGTCATTTTGTGCCAMAAATATAAGTGGACTTATAACTCAAGCTAAAGAATTTAATTTAATATTGATAGGTTTTTACGTCTTACTATTTGGTCTTTTCATGGGGTATCTAGCTTATCTTTCATTAAATTATGCGTCTCAATTAGCCTCTGTCTCGGTCGAGGGTGTCGCTTATTCCGCCGGATTACGCGGAATAGGCGGAATCTTTAGCGGGGCTAAAAATTCCGTACAAAATRCCGCCCGTTTTGGCATGGGCGCAAGCGGTGCCGGATACAGTCGCGCGCCGACTGCTTATAAAGTTGGTAGTGCAATACATCGAACGGCGCGGGCAGTTGCTAATTCAGTAAGGAATCGCGCCGGCAAGTCT","","","35610","MRFFESIDSFVIQLLDSVSQSMSSNFANSLFTIIGVTLTIYFLGKGFAVISGKIEAPATALIYDFATKMIIVAFMMNYGGYLDNSLAIIDDLKTSLTGFTGNGIAGLMDDQLELGSDIAGQLFDLDKSKYVPLEGGIASFLAWIGVAVSLFVPFIIFITTTITLKLLTVTAPIFIFCLLYNFLRNTFNQWLQLILANILTVVFIGISLRMGMSFCAXNISGLITQAKEFNLILIGFYVLLFGLFMGYLAYLSLNYASQLASVSVEGVAYSAGLRGIGGIFSGAKNSVQNXARFGMGASGAGYSRAPTAYKVGSAIHRTARAVANSVRNRAGKS","","The protein is thought to be type IV secretion-related and mating-associated (Novak et al.).Galli and colleagues report that \"sequences homologous to pVT745 have previously been detected in the chromosomes of numerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183 (5):1585-94)). Galli et al. speculate that this protein is involved in channel formation.Plasmid pVT745 is said to be a conjugative plasmid.","transport associated protein 6 from pVT745 taken from A.actinomycetemcomitans","Inner membrane, Cytoplasm","This sequence corresponds to gi|10954440, an unknown from pVT745 taken from A.actinomycetemcomitans(Galli et al.) See also GI:13345955, predicted transport associated protein 6 (Novak et al.).Nearest neighbor is gi|12053572, the Pilx6 protein from IncX plasmid R6K taken from E.coli.","
InterPro
IPR007688
Family
TrbL/VirB6 plasmid conjugal transfer protein
PF04610\"[32-268]TTrbL


","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 267-333 are 77% similar to a protein domain (PD264908) which is seen in Q9AGH0_ACTAC. Residues 71-283 are 22% similar to a protein domain (PD275748) which is seen in Q91UR2_RHIME. Residues 3-266 are 92% similar to a protein domain (PD404851) which is seen in Q9F248_ACTAC. ","","Wed Jun 25 17:20:11 2003","Wed Jun 25 17:20:11 2003","Wed Jun 25 17:20:11 2003","Sun Aug 24 15:10:16 2003","","","Wed Jun 25 17:19:59 2003","","","Sun Aug 24 15:10:16 2003","Tue Jun 24 16:28:23 2003","Sun Aug 24 15:07:54 2003","Sat Aug 23 16:59:49 2003","","Sat Aug 23 16:59:49 2003","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is virtually identical to gi|13345955, a predicted transport associated protein 6 from chromosomal A. actinomycetemcomitans.","Tue Jun 24 16:27:20 2003","Sat Aug 23 16:59:49 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ. Nucleotide sequence and analysis of conjugative plasmid pVT745. J Bacteriol. 2001 Mar;183(5):1585-94. PMID: 11160089Novak,K.F., Dougherty,B. and Pelaez,M.Actinobacillus actinomycetemcomitans harbours type IV secretionsystem genes on a plasmid and in the chromosomeMicrobiology 147 (Pt 11), 3027-3035 (2001)PubMed: 21557162 Chen J, Leblanc DJ, Galli DM. DNA inversion on conjugative plasmid pVT745. J Bacteriol. 2002 Nov;184(21):5926-34. PMID: 12374826","","Sun Aug 24 15:07:54 2003","","4","","","" "pVT32","20905","20681","225","ATGAAAAAACTTTTTATCGCATTATTTATATTAACTTTAAGTGCTTGTTCAGAAGAAGTTAAAAGTGTGGAGTATTACAAAGAACATACGACTGAACGTCAAAAAATGTTAGAAGAATGTGAGAAAAAGGCGGAGCCATTAATGGCAAACTCCAATTGTAGTAATGCAAATAAAGCACAAGCAAGTATTCGACGTATGAATACTCGAGGTGTTAATTTTTCTAAT","","","8589","MKKLFIALFILTLSACSEEVKSVEYYKEHTTERQKMLEECEKKAEPLMANSNCSNANKAQASIRRMNTRGVNFSN","","This possible lipoprotein is though to be mating-associated.Galli and colleagues report that \"sequences homologous to pVT745 have previously been detected in the chromosomes of numerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183 (5):1585-94)). Plasmid pVT745 is said to be a conjugative plasmid.","probable lipoprotein from pVT745 taken from A. actinomycetemcomitans","Outer membrane, Periplasm, Cytoplasm","This sequence corresponds to gi|10954441, a predicted lipoprotein from pVT745 taken from A.actinomycetemcomitans.Nearest neighbor is gi|10956749, an hypothetical from plasmid pXF51 taken from Xylella fastidiosa. See also gi|28867761, a predicted lipoprotein from P.syringae pv. tomato str. DC3000.","
noIPR
unintegrated
unintegrated
PS51257\"[1-16]TPROKAR_LIPOPROTEIN


","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-75 are identical to a protein domain (PD270900) which is seen in Q9F247_ACTAC. ","","Wed Jun 25 17:20:37 2003","Wed Jun 25 17:20:37 2003","Wed Jun 25 17:20:37 2003","Wed Jun 25 17:20:37 2003","","","Wed Jun 25 17:20:24 2003","","","Sat Aug 23 17:00:15 2003","Tue Jun 24 15:58:17 2003","Tue Jun 24 15:58:17 2003","Sat Aug 23 17:00:15 2003","","Sat Aug 23 17:00:15 2003","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found in A.actinomycetemcomitans.","Tue Jun 24 15:59:44 2003","Sat Aug 23 17:00:15 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ. Nucleotide sequence and analysis of conjugative plasmid pVT745. J Bacteriol. 2001 Mar;183(5):1585-94. PMID: 11160089Chen J, Leblanc DJ, Galli DM. DNA inversion on conjugative plasmid pVT745. J Bacteriol. 2002 Nov;184(21):5926-34. PMID: 12374826 Novak KF, Dougherty B, Peláez M. Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid and in the chromosome. Microbiology. 2001 Nov;147(Pt 11):3027-35. PMID: 11700353","","Sat Aug 23 17:00:15 2003","","4","","","" "pVT33","21695","20922","774","ATGACTGGATTCCGATTTATAAACAACGTTGTGTATAAGGAGAACGTGATGAAAATGTTTAAAAAACTCACTTTAGTTGCCGTTTTATCTATGCCGGCATTAGTGCAAGCCGGAATTCCGGTTGTTGATGCCGCAGCTGCCGGTCAACGTCAAATGAGCATGCTTCAAACGGTGCAACAATGGGCAAAAGAGGCTAAACAGTGGACGGATACAGTTTCGCATTATAAAAATGAGCTGAAAGCGTATGCCGACCAATTAGCCTCACAAACCGGTATTCGTGATGTACAAGCCTTTATTGGTGAAGCGCATAGTTTATATGGTGAAATAAATGGCTTAAAATCTGAGTTTACCCCGGTAATCGATTTAGTTTCCGGTGGGAAAAACGCATTAAGCGCGAATGCCAAAAGCCTGTTTGAAAAATACAACCTTTTTGACCGTTGTAAAAATTTGCGTCAAGGTGAAATCACTTCCTGCGAAGCAAATATTGTTTCCACCGTGGAAAGTATGAGCTTCTTAGATTCGTTTGAAAGTAACGTCAATAGTAAATTGAAAACTATTGATAAACTCGCTAAACGGATGACAAAATCTCAAGACGTCAAAGAAAGCCAGGACTTAAAAAATGCAATGGACGTGCAGTTGGCCGCATTGCAATCACAAAAAGTCCAGTTGGATTTATTCAACGCACGGCAAACGGAATACCGACGCTTAATGAATGAGCAACAAAAACAGTTAGCGTCTCAACGTCGCTCAAACGTTAAGGGCGTTATATTCAAT","","","28976","MTGFRFINNVVYKENVMKMFKKLTLVAVLSMPALVQAGIPVVDAAAAGQRQMSMLQTVQQWAKEAKQWTDTVSHYKNELKAYADQLASQTGIRDVQAFIGEAHSLYGEINGLKSEFTPVIDLVSGGKNALSANAKSLFEKYNLFDRCKNLRQGEITSCEANIVSTVESMSFLDSFESNVNSKLKTIDKLAKRMTKSQDVKESQDLKNAMDVQLAALQSQKVQLDLFNARQTEYRRLMNEQQKQLASQRRSNVKGVIFN","","Galli and colleagues report that \"sequences homologous to pVT745 have previously been detected in the chromosomes of numerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183 (5):1585-94)). Plasmid pVT745 is said to be a conjugative plasmid.","transport associated protein from pVT745 taken from A.actinomycetemcomitans","Periplasm","This sequence corresponds to gi|10954442, an unknown thought to be mating-associated from pVT745 taken from A.actinomycetemcomitans (Galli et al.). See also GI:13345954, a transport associated protein 6 (Novak et al.).Nearest neighbor is gi|10955840, an uncharacterized ORF from plasmid pYC taken from Y.pestis. Several similarities to other plasmid genes, e.g. Pilx5 from E.coli.","
InterPro
IPR012991
Family
Type IV secretion system
PF07996\"[17-258]TT4SS
noIPR
unintegrated
unintegrated
SSF101082\"[38-244]TSSF101082


","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 26-243 are 18% similar to a protein domain (PD312180) which is seen in Q9F514_ECOLI. Residues 53-243 are 23% similar to a protein domain (PD037985) which is seen in Q91UX3_ECOLI. Residues 17-258 are identical to a protein domain (PD359676) which is seen in Q9F246_ACTAC. ","","Wed Jun 25 17:21:04 2003","Wed Jun 25 17:21:04 2003","Wed Jun 25 17:21:04 2003","Sun Aug 24 15:12:38 2003","","","Wed Jun 25 17:20:47 2003","","","Sun Aug 24 15:12:38 2003","Tue Jun 24 15:26:43 2003","Sun Aug 24 15:12:05 2003","Sat Aug 23 17:00:48 2003","","Sat Aug 23 17:00:48 2003","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to GI:13345954,a predicted transport associated protein 4 (type IV secretion-related) from chromosomal A.actinomycetemcomitans.","Tue Jun 24 15:33:48 2003","Sat Aug 23 17:00:48 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ. Nucleotide sequence and analysis of conjugative plasmid pVT745. J Bacteriol. 2001 Mar;183(5):1585-94. PMID: 11160089Novak,K.F., Dougherty,B. and Pelaez,M.Actinobacillus actinomycetemcomitans harbours type IV secretionsystem genes on a plasmid and in the chromosomeMicrobiology 147 (Pt 11), 3027-3035 (2001)PubMed: 21557162Chen J, Leblanc DJ, Galli DM. DNA inversion on conjugative plasmid pVT745. J Bacteriol. 2002 Nov;184(21):5926-34. PMID: 12374826","","Sun Aug 24 15:12:05 2003","","4","","","" "pVT34","24429","21694","2736","ATGCAAGCCGATTCAGAAAATACAATCAGTGGTGAACCGCTTTTTAAAGGCATGATAACACAGGCCACAATCAGCGGTATTCCCATTCCAATAATATTTGTCATTGCTTTTCTTAGTGGTCTGGCATATTTCATCAGCGGGAAATTATATGCCGTATTACCGGCTATTCCGCTACTTATTGGCACAAGATTACTGTATGAAACAGATAGGGATTTTTTAACATTGAATATGCTAAATTTTAAGACAAATAGCGGGTTAGGTAAGATCGTGCGTTTTTTTGGCAGTAAAACATTTACGGCACAAAAATACAATCGAACCGCTTTTTCTGAAAATCGAATCGAAACATTAGGTATTAAACTGAGTGAACAAAAGGATTATTCCAAATTCATTCCTTATTCTTCTCATATTGCACCGAATGTCGTGATTACCCGTAACGGTGATTTAGTCGCCACCTGGTGTTGTAAAGGGGTGACGTTTGAAACCGCAGAAAATTATGAGCTCAATCTTAGTAAAGAAAAGTTGAATACCTTAATCCAATCTTTTTCTAAAAAAGGGGTTAGTTTTTATCAGCATAATATTCGCCATAAAGTTAATGAAACCTTGGATGGTCATTTTTCTTCCGAGTTTACGCAGGAAGTAAATGATAAATACTATGCCGGTTTTAATAATGGAACATTACAACGTAACATACTATACATTACGTTGGTTTATACCCCTTATTCAAAATTGGAAAAAATATCTCGTAAAACAACCAAGTTAAAGGATAAAAAACAGGAGCTTGCTTATCAATTAGAGACTATGCAAGAAATGTGTTCCCGCTTGGATAAAGCACTGGAAGATTTTCGCGGTGAAGCGTTAACTACCTTTAGTAAAGGAGGTGCGCTTTATTCTGAACAATTATCGTTTTACAACTATCTGATTACAAATCGTTGGCAACCGGTACGCGTTACTTCCACGTCGTTTTATCACTTACTGGGGAATACCGATTTACATTTTGGCAAAGAAACCGGGCAAATTACTTTTAATGGTGAAAGCCGTTTCTTCCGCTGTCTTGAAATTAAAGATTATACGGAAGAAACCTGTGAAGGTTTTTTTGACGCATTAATGTATATCAATGCCGATTATGTCATTACACAATCTTTTCAGGCTATGCCAAGCAATGTTGCAAAAGAGAAGTTAGACAGACAGCAAAAACGCTTAAATTCCTCAAATGAGGCTGCCATTTCGCAAGTTGATAATTTAACTGTTGCATTGGATGATTTAGCAAGTGGTCGTTTATCCTTTGGTTATTATCATTTTGGCATGATGGTGTACGGTGATTCTATAAAAGATGTTACTGATAAAACCAATGAAATTATTGCGGTATTAAGTAGTTTAGGTTTGATTATTACATTGGCAAATACGGCGTTAAGCGCGTCTTATTTCGGTCAATTCCCGGCAAATTTTGCCTACCGTCCACGCCTGGCAATGTTAAGTTCAAGAAATTATGCGTCGCTAACTTCTTTACATAATTTTGCCTCCGGTAAATGCAACGGGAACCCTTGGGGAGACGCGGTAACGTTGGTGAAAACGCCAAACGCTCAACCGTACTATTTTAACTTTCACCAAAGCGCACCCGGTGTTGATGACAGAGGCGAAAAACGGTTGGGGAATACCGCAGTATTCGGACAAGCGGGTTCCGGTAAAACTATGTTGATGACGTTTCTCATGACACAACTGGATAAATTCAGACATACCTCTACTTTTTTACCGACCTCGGTAAAACGTGAATTGACAATGGTATATCTGGATAAAGATTACGGTGCGGAAGCCTGTATTCGTGCCATGGGCGGAAAATACATGTTGATCCGTAAAGGGGTGCCGACCGGTTTTAATCCGTTTATGTGTGAAAACACGCCGGAAAATCTGTCTTTCCTTTCTACGTTGATGAAAATGTTAGTTACGCGTAACGGCAGAACGTTGTCATCGCTCGATGAAGAAGAATTATTCAAGGCGGTTAAATCGGTGATGGAATTTGATATGGAATACCGCAGTTATCCGATTTCACGCGTCGTTGAGCATTTGCCGGAAGGCTCAACTAAAGCCGAAAAAGAAAACTCCCTTGCCCGTCGTTTGAAAAACTGGGCGCAAGGTGGGGAATTCGGTTGGGTATTTGATAATCCTGCCGATACGTTAGATTTTACCGGGCATGCCGTATTTGGCATTGATGGTACGGAATTTTTAGATGACCAGGATACTTGTAGTCCGCTTTCTTTCTATTTATTACACCGTATCGGAAAATTATTAGATGGTCGTCGTTTGATCATTTTTATGGATGAATTCTGGAAATGGTTAAAAGATGAAGCGTTTTCCGACTTTGCCTATAACAAATTAAAAGTTATTCGGAAAGAAGATGGAATTGTCATACCGATGACCCAAAGTATGGATGAAGTGTTGAAAAGCCCAATTTCCCGCGCGGTAGTTGAGGAATGTGAAACAACCATTTGTTTACCTAACCCGATTGCCCGCAAAGTGGATTATGTGGATGGTTTCGGAATCAGCGAAAAACAATTTGAAATTATCCGTGAATTACAACCGGATTCCCGTACTTTCTTAGTCCGTAAAGGGCTCGAAACCGCCTTAGCTAAGTTAGATTTAAGCGGTTTAGGGCGTGAAAACTTAAAAATTCTGTCAACCAGTAAGGATAACGCAGAAATCCTACATCAAATTATCGAAGAAGTCGGCGAAGCCGCTAAT","","","103090","MQADSENTISGEPLFKGMITQATISGIPIPIIFVIAFLSGLAYFISGKLYAVLPAIPLLIGTRLLYETDRDFLTLNMLNFKTNSGLGKIVRFFGSKTFTAQKYNRTAFSENRIETLGIKLSEQKDYSKFIPYSSHIAPNVVITRNGDLVATWCCKGVTFETAENYELNLSKEKLNTLIQSFSKKGVSFYQHNIRHKVNETLDGHFSSEFTQEVNDKYYAGFNNGTLQRNILYITLVYTPYSKLEKISRKTTKLKDKKQELAYQLETMQEMCSRLDKALEDFRGEALTTFSKGGALYSEQLSFYNYLITNRWQPVRVTSTSFYHLLGNTDLHFGKETGQITFNGESRFFRCLEIKDYTEETCEGFFDALMYINADYVITQSFQAMPSNVAKEKLDRQQKRLNSSNEAAISQVDNLTVALDDLASGRLSFGYYHFGMMVYGDSIKDVTDKTNEIIAVLSSLGLIITLANTALSASYFGQFPANFAYRPRLAMLSSRNYASLTSLHNFASGKCNGNPWGDAVTLVKTPNAQPYYFNFHQSAPGVDDRGEKRLGNTAVFGQAGSGKTMLMTFLMTQLDKFRHTSTFLPTSVKRELTMVYLDKDYGAEACIRAMGGKYMLIRKGVPTGFNPFMCENTPENLSFLSTLMKMLVTRNGRTLSSLDEEELFKAVKSVMEFDMEYRSYPISRVVEHLPEGSTKAEKENSLARRLKNWAQGGEFGWVFDNPADTLDFTGHAVFGIDGTEFLDDQDTCSPLSFYLLHRIGKLLDGRRLIIFMDEFWKWLKDEAFSDFAYNKLKVIRKEDGIVIPMTQSMDEVLKSPISRAVVEECETTICLPNPIARKVDYVDGFGISEKQFEIIRELQPDSRTFLVRKGLETALAKLDLSGLGRENLKILSTSKDNAEILHQIIEEVGEAAN","","Transport- and mating-associated protein (possible type IV secretion system element).Galli and colleagues report that \"sequences homologous to pVT745 have previously been detected in the chromosomes of numerous A.actinomycetemcomitans strains\" ((J. Bacteriol. 183 (5):1585-94)). Plasmid pVT745 is said to be a conjugative plasmid.","CagE-related (transport associated, mating associated) protein from pVT745 taken from A.actinomycetemcomitans","Outer membrane, Cytoplasm","This sequence corresponds to gi|10954443, a predicted mating-associated ATPase from pVT745 taken from A.actinomycetemcomitans(Galli et al.). See also GI:13345953, transport associated protein 4 (Novak et al.).Nearest neighbor is gi|15919988, a predicted TraE protein (NTP binding) from plasmid pSB102 taken from Sinorhizobium meliloti strain FP2.","
InterPro
IPR004346
Family
CagE, TrbE, VirB component of type IV transporter system
PF03135\"[284-487]TCagE_TrbE_VirB
TIGR00929\"[119-909]TVirB4_CagE: type IV secretion/conjugal tran
InterPro
IPR007792
Family
Type IV secretory pathway, VirB3-like
PF05101\"[13-100]TVirB3
noIPR
unintegrated
unintegrated
signalp\"[1-42]?signal-peptide
tmhmm\"[24-44]?transmembrane_regions


","BeTs to 4 clades of COG3451COG name: Type IV secretory pathway, VirB4 componentsFunctional Class: NThe phylogenetic pattern of COG3451 is ------------------s-ujx---Number of proteins in this genome belonging to this COG is","No significant hits to the Blocks database.","Residues 717-880 are 27% similar to a protein domain (PD572923) which is seen in Q8VME8_PSEPU. Residues 451-781 are 25% similar to a protein domain (PD467722) which is seen in O25206_HELPY. Residues 636-752 are 31% similar to a protein domain (PD191774) which is seen in CAGE_HELPY. Residues 717-768 are identical to a protein domain (PD567048) which is seen in Q9F245_ACTAC. Residues 477-717 are 27% similar to a protein domain (PD572925) which is seen in Q93TD0_BBBBB. Residues 719-868 are 29% similar to a protein domain (PD393268) which is seen in Q9F525_ECOLI. Residues 306-716 are identical to a protein domain (PD005092) which is seen in Q9F245_ACTAC. Residues 1-115 are 94% similar to a protein domain (PD290858) which is seen in Q9F245_ACTAC. Residues 875-912 are identical to a protein domain (PD404094) which is seen in Q9F245_ACTAC. Residues 116-298 are identical to a protein domain (PD011220) which is seen in Q9F245_ACTAC. Residues 769-854 are identical to a protein domain (PD044096) which is seen in Q9F245_ACTAC. Residues 749-830 are 36% similar to a protein domain (PD572920) which is seen in Q52363_ECOLI.","","Wed Jun 25 17:27:44 2003","Wed Jun 25 17:27:44 2003","Wed Jun 25 17:27:44 2003","Sun Aug 24 15:16:22 2003","","","Wed Jun 25 17:21:18 2003","Sun Aug 24 15:16:22 2003","","Sun Aug 24 15:16:22 2003","Tue Jun 24 14:56:52 2003","Sun Aug 24 15:16:22 2003","Sat Aug 23 17:01:24 2003","","Sun Aug 24 15:16:22 2003","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is highly similar to AA1914, a predicted CagE transport associateed protein. It is also similar to pVT36 from A.actinomycetemcomitans.","Sun Aug 24 15:16:22 2003","Sat Aug 23 17:01:24 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ. Nucleotide sequence and analysis of conjugative plasmid pVT745. J Bacteriol. 2001 Mar;183(5):1585-94. PMID: 11160089Novak,K.F., Dougherty,B. and Pelaez,M.Actinobacillus actinomycetemcomitans harbours type IV secretionsystem genes on a plasmid and in the chromosomeMicrobiology 147 (Pt 11), 3027-3035 (2001)PubMed: 21557162Chen J, Leblanc DJ, Galli DM. DNA inversion on conjugative plasmid pVT745. J Bacteriol. 2002 Nov;184(21):5926-34. PMID: 12374826","Schneiker,S., Keller,M., Droge,M., Lanka,E., Puhler,A. andSelbitschka,W.The genetic organization and evolution of the broad host rangemercury resistance plasmid pSB102 isolated from a microbialpopulation residing in the rhizosphere of alfalfaNucleic Acids Res. 29 (24), 5169-5181 (2001)PubMed: 11812851","Sun Aug 24 15:16:22 2003","Tue Jun 24 14:46:04 2003","4","","","" "pVT35","24729","24445","285","ATGTTTAATAAACTTTCTCATAAACTACATTACACACTTATTCCAGCACTTTTCATGATGGCAACCAATCCCGCTTTTGCCGGTGGTTTACAAAAAACAAAACAGTATTTAAGTCAATTTTCGACTGAAATTCATAGTTTTGCGGGTATTGTCTTTGTATTAGCCGGTTTCTTTGCGGCTTATCAAATGATGTGGAGAGGGCAACCTTTCGAAAGTATAGCAAAAGTGATTTATGGTGCAATTACATTAATTGTTGTTCCCGAAATCGGACTATGGTTATTCCCT","","","10688","MFNKLSHKLHYTLIPALFMMATNPAFAGGLQKTKQYLSQFSTEIHSFAGIVFVLAGFFAAYQMMWRGQPFESIAKVIYGAITLIVVPEIGLWLFP","","This protein is thought to be mating-associated and is suggested to have an export signal (Galli et al.).Galli and colleagues report that \"sequences homologous topVT745 have previously been detected in the chromosomes of numerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183 (5):1585-94)). Plasmid pVT745 is said to be a conjugative plasmid.","possible mating-associated protein from pVT745 taken from A.actinomycetemcomitans","Inner membrane, Cytoplasm","This sequence corresponds to gi|10954444, an unknown from plasmid pVT745 taken from A.actinomycetemcomitans.There are no other matches to GenBank at this time.","
noIPR
unintegrated
unintegrated
signalp\"[1-27]?signal-peptide
tmhmm\"[9-27]?\"[41-61]?\"[76-94]?transmembrane_regions


","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-95 are identical to a protein domain (PD282289) which is seen in Q9F244_ACTAC. ","","Wed Jun 25 17:28:24 2003","Wed Jun 25 17:28:24 2003","Wed Jun 25 17:28:24 2003","Wed Jun 25 17:28:24 2003","","","Wed Jun 25 17:28:06 2003","","","Sun Aug 24 15:17:52 2003","Tue Jun 24 14:27:48 2003","Tue Jun 24 14:26:29 2003","Sat Aug 23 17:01:49 2003","","Sat Aug 23 17:01:49 2003","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found in A.actinomycetemcomitans.","Tue Jun 24 14:00:54 2003","Sat Aug 23 17:01:49 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ. Nucleotide sequence and analysis of conjugative plasmid pVT745. J Bacteriol. 2001 Mar;183(5):1585-94. PMID: 11160089 Chen J, Leblanc DJ, Galli DM. DNA inversion on conjugative plasmid pVT745. J Bacteriol. 2002 Nov;184(21):5926-34. PMID: 12374826 Novak KF, Dougherty B, Peláez M. Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid and in the chromosome. Microbiology. 2001 Nov;147(Pt 11):3027-35. PMID: 11700353","","Sun Aug 24 15:17:52 2003","","4","","","" "pVT36","25406","24759","648","ATGTCGATGACCGCCTTACAACTGATTGCGATGTGCGCCCCGCTTGTTCATCCCGATACTGCGTTATCCGTGATGAAAGAGGAAAGTAAATTAAATCAATTTGCGATAGGCGTAGTAGATGGCTGGGTAAAACAACCCACTGACTTTAATAGTGCGGTATTAACCGCACAACAACTTGAAAAGGAGGGAAAAAACTATTCTGTCGGACTTATGCAAATCAACAAACATAACTTTTCACGCTATGGGGTAACACTTGAGCAAATGTTTGACCCTTGCAATAACTTGCAGGTGGCGCAACAAATTTTGCAAGACTGTTATCAACGTAGCGGCAGTGTCAATGACGCGTTAAGTTGCTATTACTCCGGAAATTTCTTACGTGGATACAAAAGAGATTTTCGAGGATCCAGTTATGTCGAAAGAGTGCATGCACAACTCTTTGAACCGACCCCGGAAAAAAGTTTTGCGATTCCCTCTTTGAAAAATGAACCTTTACCTGTTGCTGCTGTTGCCGAAGTAGCAAAAGTAACCACAACTAAAAAGGAAAAAAAGCCACAACAAGCCAGAAAAAACCGTCATCAAGTCAGATTATATAAAAATCTTCCTCCGGTAACACCGCCGGCAGAATATAAGAAACTTGCTTCTATCAAC","","","24268","MSMTALQLIAMCAPLVHPDTALSVMKEESKLNQFAIGVVDGWVKQPTDFNSAVLTAQQLEKEGKNYSVGLMQINKHNFSRYGVTLEQMFDPCNNLQVAQQILQDCYQRSGSVNDALSCYYSGNFLRGYKRDFRGSSYVERVHAQLFEPTPEKSFAIPSLKNEPLPVAAVAEVAKVTTTKKEKKPQQARKNRHQVRLYKNLPPVTPPAEYKKLASIN","","Said in GI:10954445 to be mating-associated; clearly a type IV secretion protein.See AA02919. Galli and colleagues report that \"sequences homologous to pVT745 have previously been detected in the chromosomes of numerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183 (5):1585-94)).Plasmid pVT745 is said to be a conjugative plasmid.","type IV secretion-related CagE-related protein from pVT745 taken from A.actinomycetemcomitans","Periplasm","This sequence corresponds to GI:10954445, an unknown from pVT745 taken from A. actinomycetemcomitans (however see below and the Paralog field).Nearest neighbor is GI:8163884, a predicted virB sequence (attachment mediating protein) from Brucella abortus. See also GI:23499836 from Brucella suis.","
InterPro
IPR008258
Domain
Lytic transglycosylase, catalytic
PF01464\"[5-141]TSLT
noIPR
unintegrated
unintegrated
SSF53955\"[16-168]TSSF53955


","BeTs to 3 clades of COG0741COG name: Soluble lytic murein transglycosylase and related regulatory proteins (some contain LysM/invasin domains)Functional Class: MThe phylogenetic pattern of COG0741 is -------qv---bcefghsnujx-t-Number of proteins in this genome belonging to this COG is","***** IPB000189 (SLT domain) with a combined E-value of 9.2e-06. IPB000189A 54-78 IPB000189B 88-102","Residues 58-121 are 36% similar to a protein domain (PD481099) which is seen in Q92HT5_RICCN. Residues 3-128 are identical to a protein domain (PD017223) which is seen in Q9F243_ACTAC. Residues 129-216 are 79% similar to a protein domain (PD278810) which is seen in Q9F243_ACTAC. ","","Wed Jun 25 17:28:47 2003","Wed Jun 25 17:28:47 2003","Wed Jun 25 17:28:47 2003","Sun Aug 24 15:21:45 2003","","","Wed Jun 25 17:28:47 2003","","","Fri Jan 7 18:26:28 2005","Wed Jun 18 16:05:51 2003","Sun Aug 24 15:21:45 2003","Fri Jan 7 18:26:28 2005","Sat Aug 23 17:02:23 2003","Sat Aug 23 17:02:23 2003","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is paralogous to the chromosomal AA02919, a predicted CagE protein in the Aa chromosome. It also displays similarity to pVT34, a shorter segment.","Fri Jan 7 18:26:28 2005","Sat Aug 23 17:02:23 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160089Novak KF, Dougherty B, Pelez M.Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid and in the chromosome.Microbiology. 2001 Nov;147(Pt 11):3027-35.PMID: 11700353Chen J, Leblanc DJ, Galli DM. DNA inversion on conjugative plasmid pVT745. J Bacteriol. 2002 Nov;184(21):5926-34. PMID: 12374826","","Fri Jan 7 18:26:28 2005","","4","","","" "pVT4","2365","2339","294","ATGGATTTTCAATTAGTGAGGAAATTGTTTTTAGGGGTTTTATCTACACTTTCCAACGAACCTAAACTTTTGRATGATGAATTATCTGAAATCATAAAGTTAAGAACAGCATTAAATCAAGTTGGMCKRMASGTCAACCAGATTGCTAGGAAGTCATCTAAGGATATAAACAGTAAGGAACTTTCAATAGCATTAAAAAATACTCAATTTTGGATTAATAAACTAGATAAAAAACTTGATGATTTAATTTCAAAAACGGTGGATAGATGGGCGTTCGTATCGAAAAAGAATGGT","","","10957","MDFQLVRKLFLGVLSTLSNEPKLLXDELSEIIKLRTALNQVGXXVNQIARKSSKDINSKELSIALKNTQFWINKLDKKLDDLISKTVDRWAFVSKKNG","","Galli and colleagues report that \"sequences homologous to pVT745 have previously been detected in the chromosomes of numerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183 (5), 1585-1594 (2001)). They speculate that this protein may be an oriT-recognizing protein. Plasmid pVT745 is said to be a conjugative plasmid.","hypothetical protein from pVT745 taken from A. actinomycetemcomitans","Periplasm, Cytoplasm","This sequence corresponds to GI:10954413 (labeled gene magA1), an unknown in GenBank taken from A.actinomycetemcomitans.There are no near neighbors in GenBank at this time.","
noIPR
unintegrated
unintegrated
signalp\"[1-18]?signal-peptide


","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-98 are 90% similar to a protein domain (PD283375) which is seen in Q9F275_ACTAC. ","","","","Wed Jun 25 17:05:07 2003","Wed Jun 25 17:06:56 2003","","","Wed Jun 25 16:52:15 2003","","","Thu Oct 11 16:58:43 2007","Wed Jun 18 14:33:45 2003","Wed Jun 18 14:33:45 2003","Thu Oct 11 13:29:38 2007","","Sat Aug 23 16:46:32 2003","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found in A.actinomycetemcomitans.","Wed Jun 18 14:33:45 2003","Sat Aug 23 16:46:32 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160089Chen J, Leblanc DJ, Galli DM.DNA inversion on conjugative plasmid pVT745.J Bacteriol. 2002 Nov;184(21):5926-34.PMID: 12374826Novak KF, Dougherty B, Pelez M.Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid andin the chromosome.Microbiology. 2001 Nov;147(Pt 11):3027-35.PMID: 11700353","","Thu Mar 18 16:41:03 2004","","4","","","" "pVT5","3996","4382","387","ATGGAAATCGTAATAAAAGAAACAGGTGCAGTGGAAACATTATTACTTATTGATAGCTCAACAGGTTGTGATTGGTTTAATGACTTGGTCGGCAATCATGATGGGTTTGGAGATGATTCCGAGTGCCAGTTTGCAAAAGAAACCGACGAAGACGGCTTAGATACCGGAAGATATATCACAAGCAAGGCGAATKTTGAGTGGTGGGAGGATATTGTTTGCCAAATCGATAATGTAAATAATCGCATTGACAACTTAAAAGATGAGTTTGGGGTGGCTCGTGTTGATGAAGTGGTTTATCAATGTAATTATGGCAATACAGACCTAGAGTATTACGCGGCAGAACTTAATCGGTGGCTTGATGATGAGTTTGGCGAGGATGCCGGTAGA","","","14561","MEIVIKETGAVETLLLIDSSTGCDWFNDLVGNHDGFGDDSECQFAKETDEDGLDTGRYITSKANXEWWEDIVCQIDNVNNRIDNLKDEFGVARVDEVVYQCNYGNTDLEYYAAELNRWLDDEFGEDAGR","","Galli and colleagues report that \"sequences homologous to pVT745 have previously been detected in the chromosomes of numerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183(5):1585-94)).Plasmid pVT745 is said to be a conjugative plasmid.","hypothetical protein from pVT745 taken from A.actinomycetemcomitans","Cytoplasm","This sequence corresponds to GI:10954414, an unknown (labeled AA02) in GenBank.There are no near neighbors at this time.","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-129 are identical to a protein domain (PD295438) which is seen in Q9F274_ACTAC. ","","","Wed Jun 25 16:54:51 2003","Wed Jun 25 16:54:51 2003","Wed Jun 25 16:54:51 2003","","","Wed Jun 25 16:54:51 2003","","","Thu Mar 18 16:43:08 2004","Tue Jun 17 14:02:43 2003","Tue Jun 17 14:01:41 2003","Sat Aug 23 16:46:57 2003","","Sat Aug 23 16:46:57 2003","yes","Fri Feb 20 15:41:32 MST 1998","","","Sat Aug 23 16:46:57 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160089Chen J, Leblanc DJ, Galli DM.DNA inversion on conjugative plasmid pVT745.J Bacteriol. 2002 Nov;184(21):5926-34.PMID: 12374826Novak KF, Dougherty B, Pelez M.Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid andin the chromosome.Microbiology. 2001 Nov;147(Pt 11):3027-35.PMID: 11700353","","Thu Mar 18 16:43:08 2004","","4","","","" "pVT6","4426","4800","375","ATGGCAAAAACAGCAGTACATTTATCAGATAATACTTGGCAATACATCACAGACCGCACACCACAGGGCGAGCAAAAAGGACTGTCGGCACACATTAATAATGCGTTTGAGCAGTTGGCACATTTAGCCCGCGCGGAAAAGCCAGAATTATCAAAAACTGAGTGGGTTGAGTTATACAATGTCTATGCCGGCAGTGATTTAACTCGCCTTGTAATGCCGTTTGATTTAGCCGATGACTTTCGCACGCATTACGGCACTTTGCCGCAAGATTTGACCGCGCTTTATGATAAGTTAAATGGGATGACGCAAGCACAGCAATTTTCCGTGCTTGATGCCGTCCGCGTATATTGGGCGAGTGGCGAAGATGGGGATTAA","","","14007","MAKTAVHLSDNTWQYITDRTPQGEQKGLSAHINNAFEQLAHLARAEKPELSKTEWVELYNVYAGSDLTRLVMPFDLADDFRTHYGTLPQDLTALYDKLNGMTQAQQFSVLDAVRVYWASGEDGD$","","Galli and colleagues report that \"sequences homologous to pVT745 have previously been detected in the chromosomes of numerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183(5):1585-94)).Plasmid pVT745 is said to be a conjugative plasmid.","hypothetical protein from pVT745 taken from A. actinomycetemcomitans","Cytoplasm","This sequence corresponds to GI:10954415, an unknown (labeled gene AA03) in Genbank.There are no near neighbors in GenBank at this time.","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-124 are identical to a protein domain (PD293864) which is seen in Q9F273_ACTAC. ","","","","Wed Jun 25 17:07:34 2003","Wed Jun 25 17:07:34 2003","","","Wed Jun 25 17:07:34 2003","Wed Jun 25 17:07:34 2003","","Thu Mar 18 16:42:43 2004","Tue Jun 17 13:55:12 2003","Tue Jun 17 13:54:34 2003","Sat Aug 23 16:47:24 2003","","Sat Aug 23 16:47:24 2003","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found in A.a.","Tue Jun 17 13:58:02 2003","Sat Aug 23 16:47:24 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160089Chen J, Leblanc DJ, Galli DM.DNA inversion on conjugative plasmid pVT745.J Bacteriol. 2002 Nov;184(21):5926-34.PMID: 12374826Novak KF, Dougherty B, Pelez M.Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid andin the chromosome.Microbiology. 2001 Nov;147(Pt 11):3027-35.PMID: 11700353","","Thu Mar 18 16:42:43 2004","","4","","","" "pVT7","4790","5467","678","ATGGGGATTAAAAACAAACCGATAACAAGACCATGCCCACAGTGCGGTAGAAATTATCAATATAGACGGGCAAGTGGTCGTACTTTTGAGCTTTGCGAATATTGTCGCAATCTTGATTGTGTTGTTTGCGGGCAAAAGGTTCCGCCTGAACGCGGTCGGAAAAATACTTGCTGTGCGGAGTGCGAAAAATTGAAGATACACAATATCCAAAATGCGCACTACGCCAAGCGGATTGCGGAAGACCCGGAGTTAAATAAACGCAACCACGCCAAATCCCGCGAAAACCGAAAAGCAGACCCGGAGCGAATGCGCGAACATTTGGAAGCGCAAAGGGAAAGGAATTATAGACGTGCGCAAGATCCAAAATATCAAGCCACACGGAAAGTTTATCAGGCTCAACGATGGCAGGATAAAAAAGACGAGATACAGGCTCAACGTCGCGAATTTTGGGATAGCTTAAACGACGTTGAGAAAGCGGAACGACTTGAGCGCAATCAAGCAATACAACGTAAGCATAAAGCCAAAAAGCGTGAGCAGTTGAAATTAGATCCGCAAAAGTGGGCGGAGTATCAAGAGTATCAACGCACAAAACGGCGCGAACATAGACAGAGAAAGGCGCTAAATGAATTAATGACCGGCACAAAGGAGTTATTAAATGTTACCAACAAAGACAAATAG","","","27263","MGIKNKPITRPCPQCGRNYQYRRASGRTFELCEYCRNLDCVVCGQKVPPERGRKNTCCAECEKLKIHNIQNAHYAKRIAEDPELNKRNHAKSRENRKADPERMREHLEAQRERNYRRAQDPKYQATRKVYQAQRWQDKKDEIQAQRREFWDSLNDVEKAERLERNQAIQRKHKAKKREQLKLDPQKWAEYQEYQRTKRREHRQRKALNELMTGTKELLNVTNKDK$","","Galli and colleagues report that \"sequences homologous to pVT745 have previously been detected in the chromosomes of numerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183 (5), 1585-1594 (2001)).Plasmid pVT745 is said to be a conjugative plasmid.","hypothetical protein from pVT745 taken from A.actinomycetemcomitans","Cytoplasm, Extracellular","This sequence corresponds to GI:10954416, an unknown (labeled gene AA04) in GenBank.There are no near neighbors in GenBank at this time.","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 49-222 are 20% similar to a protein domain (PD137485) which is seen in Q21461_CAEEL. Residues 76-209 are 20% similar to a protein domain (PD465584) which is seen in Q9BHM3_PARTE. Residues 1-225 are identical to a protein domain (PD313094) which is seen in Q9F272_ACTAC. Residues 83-210 are 27% similar to a protein domain (PD315291) which is seen in Q9Y102_DROME. Residues 73-205 are 23% similar to a protein domain (PD064515) which is seen in Q17909_CAEEL. Residues 60-214 are 23% similar to a protein domain (PD256798) which is seen in Q9N4C7_CAEEL. Residues 70-201 are 23% similar to a protein domain (PD026728) which is seen in TRHY_RABIT. Residues 85-220 are 18% similar to a protein domain (PD182826) which is seen in Q19135_CAEEL.","","","","Wed Jun 25 17:07:55 2003","Sun Aug 24 13:36:10 2003","","","Wed Jun 25 17:07:55 2003","Wed Jun 25 17:07:55 2003","","Thu Mar 18 16:41:29 2004","Tue Jun 17 13:49:10 2003","Tue Jun 17 13:42:56 2003","Thu Mar 18 16:41:29 2004","","Thu Mar 18 16:41:29 2004","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is weakly similar to AA1525, a predicted chromosomal gene for immunoglobulin A1 protease precursor (iga gene).","Tue Jun 17 13:42:56 2003","Sat Aug 23 16:47:49 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli,D.M., Chen,J., Novak,K.F. and Leblanc,D.J.Nucleotide Sequence and Analysis of Conjugative Plasmid pVT745J. Bacteriol. 183 (5), 1585-1594 (2001)PUBMED 11160089Chen J, Leblanc DJ, Galli DM.DNA inversion on conjugative plasmid pVT745.J Bacteriol. 2002 Nov;184(21):5926-34.PMID: 12374826Novak KF, Dougherty B, Pelez M.Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid andin the chromosome.Microbiology. 2001 Nov;147(Pt 11):3027-35.PMID: 117003","","Thu Mar 18 16:41:29 2004","","4","","","" "pVT8","5445","6062","618","ATGTTACCAACAAAGACAAATAGTTTTGATATTGTCGCCGTTAAAAGCATGACAATCCAAGATTTAAAGGCCGAATTAGCCAAAACACAAACCGTTACGGCGGAATGCATTATGTATATTGCGGCAATATGGCGGGAGTTAGAGGAGCGTGGAGAGGATTTAAGCGAGTTACGCCATGGCATGATGACTTATATCCCGTTAATCGCAACAAATCAATTGGATGCGCGTCTTGTCGTTAATTATGCCGGTCAGAAAACACTCTTATCAAGTATGGCAAAATTACCGTTAAAAGAGCAACAAAAACTAGCCGAAAAAGGAACTTTGGATGTTGTTATTTTGGGTGATGATAATAAACAGGTGATCAAAGAGGTTAAAATATCCGATTTAACGGCAGCTCAAGTTTATCAAACCATGGGGGACGGCAAAATAAAGACGCCGGAACAGCAGTATCAAATCTTGCTAGTCCGTAATAAAGTGCGGTCAAAATCAAAGCCGAAAAAGACTTACCGACTAACGCAAAATTTAAAAATAGATGGTAAAAATTTAGTAATCGCCGGCAAACATGCGGTATCCATTGAGCTTCTAAAAAAGTACTTAGAGGATAACAATGAGCTATAG","","","23103","MLPTKTNSFDIVAVKSMTIQDLKAELAKTQTVTAECIMYIAAIWRELEERGEDLSELRHGMMTYIPLIATNQLDARLVVNYAGQKTLLSSMAKLPLKEQQKLAEKGTLDVVILGDDNKQVIKEVKISDLTAAQVYQTMGDGKIKTPEQQYQILLVRNKVRSKSKPKKTYRLTQNLKIDGKNLVIAGKHAVSIELLKKYLEDNNEL$","","Galli and colleagues report that \"sequences homologous topVT745 have previously been detected in the chromosomes ofnumerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183(5), 1585-1594 (2001)).Plasmid pVT745 is said to be a conjugative plasmid.","hypothetical protein from pVT745 taken from A.actinomycetemcomitans","Cytoplasm","This sequence corresponds to GI:10954417 (labeled AA05), an unknown in GenBank.There are no near neighbors in GenBank at this time.","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-204 are 99% similar to a protein domain (PD310795) which is seen in Q9F271_ACTAC. ","","","","Wed Jun 25 17:08:16 2003","Sun Aug 24 13:36:49 2003","","","Wed Jun 25 17:08:16 2003","Wed Jun 25 17:08:16 2003","","Thu Mar 18 16:42:20 2004","Wed Jun 18 14:21:04 2003","Tue Jun 17 13:46:00 2003","Sat Aug 23 16:48:19 2003","","Sat Aug 23 16:48:19 2003","yes","Fri Feb 20 15:41:32 MST 1998","No paralogous sequences were found in A.actinomycetemcomitans.","Tue Jun 17 13:48:12 2003","Sat Aug 23 16:48:19 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160089Chen J, Leblanc DJ, Galli DM.DNA inversion on conjugative plasmid pVT745.J Bacteriol. 2002 Nov;184(21):5926-34.PMID: 12374826Novak KF, Dougherty B, Pelez M.Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid andin the chromosome.Microbiology. 2001 Nov;147(Pt 11):3027-35.PMID: 11700353","","Thu Mar 18 16:42:20 2004","","4","","","" "pVT9","6052","6249","198","ATGAGCTATAGCAAGCTAAGCAGCACCCGAAAAAAGACTATCAGTGTTAATGCTAATAAATACACCAAGGATAACTATAGACAGATACTTTTACGCCTAAAGCCAGATGTTGCCGATATGTTTGATTCAGCCTGCAAGGCGGAAAAATTATCACGGGCGGAAATGCTAAAAAAACTCCTAGAAACTTATTCAATATAA","","","7519","MSYSKLSSTRKKTISVNANKYTKDNYRQILLRLKPDVADMFDSACKAEKLSRAEMLKKLLETYSI$","","Galli and colleagues report that \"sequences homologous topVT745 have previously been detected in the chromosomes ofnumerous A. actinomycetemcomitans strains\" ((J. Bacteriol. 183(5), 1585-1594 (2001)).Plasmid pVT745 is said to be a conjugative plasmid.","hypothetical protein from pVT745 taken from A.actinomycetemcomitans","Periplasm, Cytoplasm","This sequence corresponds to GI:10954418 (labeled gene AA06), an unknown in GenBank.Otherwise there are no near neighbors in GenBank at this time.","No hits reported.","No hits to the COGs database.","No significant hits to the Blocks database.","Residues 1-65 are identical to a protein domain (PD263486) which is seen in Q9F270_ACTAC. ","","","","Wed Jun 25 17:08:29 2003","Wed Jun 25 17:08:29 2003","","","Wed Jun 25 17:08:29 2003","Wed Jun 25 17:08:29 2003","","Thu Mar 18 16:41:56 2004","Tue Jun 17 13:49:51 2003","Tue Jun 17 13:41:50 2003","Sat Aug 23 16:48:44 2003","","Sat Aug 23 16:48:44 2003","yes","Fri Feb 20 15:41:32 MST 1998","This sequence is weakly similar to the AA chromosomal gene reported in GenBank as GI:19568173. ","Tue Jun 17 13:41:50 2003","Sat Aug 23 16:48:44 2003","No hits to the PDB database.","","","No significant hits to the Pfam 7.3 database.","","","","Galli DM, Chen J, Novak KF, Leblanc DJ.Nucleotide sequence and analysis of conjugative plasmid pVT745.J Bacteriol. 2001 Mar;183(5):1585-94.PMID: 11160089Chen J, Leblanc DJ, Galli DM.DNA inversion on conjugative plasmid pVT745.J Bacteriol. 2002 Nov;184(21):5926-34.PMID: 12374826Novak KF, Dougherty B, Pelez M.Actinobacillus actinomycetemcomitans harbours type IV secretion system genes on a plasmid andin the chromosome.Microbiology. 2001 Nov;147(Pt 11):3027-35.PMID: 11700353","","Thu Mar 18 16:41:56 2004","","4","","",""