LOCUS CCP45172.1 565 aa PRT BCT 27-FEB-2015 DEFINITION Mycobacterium tuberculosis H37Rv Bifunctional enzyme MbtA: salicyl-AMP ligase (SAL-AMP ligase) + salicyl-S-ArCP synthetase protein. ACCESSION AL123456-2450 PROTEIN_ID CCP45172.1 SOURCE Mycobacterium tuberculosis H37Rv ORGANISM Mycobacterium tuberculosis H37Rv Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex. REFERENCE 1 AUTHORS Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D., Gordon S.V., Eiglmeier K., Gas S., Barry C.E.III., Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R., Devlin K., Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L., Oliver K., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton J., Squares R., Squares S., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. TITLE Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence JOURNAL Nature 393(6685), 537-544(1998). PUBMED 9634230 REMARK Erratum:[Nature 1998 Nov 12;396(6707):190] REFERENCE 2 AUTHORS Camus J.C., Pryor M.J., Medigue C., Cole S.T. TITLE Re-annotation of the genome sequence of Mycobacterium tuberculosis H37Rv JOURNAL Microbiology (Reading, Engl.) 148(Pt 10), 2967-2973(2002). PUBMED 12368430 REFERENCE 3 AUTHORS Lew J.M., Kapopoulou A., Jones L.M., Cole S.T. TITLE TubercuList--10 years after JOURNAL Tuberculosis (Edinb) 91(1), 1-7(2011). PUBMED 20980199 REFERENCE 4 (bases 1 to 4411529) AUTHORS Parkhill J. JOURNAL Submitted (11-JUN-1998) to the INSDC. Submitted on behalf of the Mycobacterium tuberculosis sequencing and mapping teams, Sanger Centre, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SA Unite de Genetique Moleculaire Bacterienne, Institut Pasteur, 28 rue du Docteur Roux, 75724 Paris Cedex 15, France E-mail: parkhill@sanger.ac.uk REFERENCE 5 (bases 1 to 4411532) AUTHORS Lew J.M. JOURNAL Submitted (18-DEC-2012) to the INSDC. Lew J., Ecole Polytechnique Federale de Lausanne, CH-1015, Lausanne, Switzerland, and the Swiss Institute of Bioinformatics, CMU - Rue Michel-Servet 1, 1211 Geneva 4, SWITZERLAND COMMENT On or before Feb 1, 2013 this sequence version replaced gi:41352722, gi:38490165, gi:38490207, gi:41353619, gi:38490250, gi:38684030, gi:38490288, gi:41353667, gi:41353422, gi:41352756, gi:38490319, gi:41352785, gi:38490370, gi:41353971. Note: This annotation is from the TubercuList website, Release 26, Dec 2012 (URL: http://tuberculist.epfl.ch) (email: tuberculist@epfl.ch). FEATURES Qualifiers source /organism="Mycobacterium tuberculosis H37Rv" /strain="H37Rv" /mol_type="genomic DNA" /db_xref="taxon:83332" protein /transl_table=11 /gene="mbtA" /locus_tag="Rv2384" /note="Rv2384, (MTCY22H8.01, MTCY253.37c), len: 565 aa. mbtA, bifunctional enzyme, including salicyl-AMP ligase (Sal-AMP ligase) and salicyl-S-ArCP synthetase (see Quadri et al., 1998; De Voss et al., 1999), highly similar to other ligases e.g. Q9F638|MXCE from Stigmatella aurantiaca 2,3-DHBA-AMP ligase (protein involved in the biosynthesis of 2,3-dihydroxybenzoic acid, contains the AMP binding signature) (543 aa), FASTA scores: opt: 1683, E(): 2.8e-90,(48.25% identity in 545 aa overlap) (see Silakowski et al.,2000); P40871|DHBE_BACSU|ENTE 2,3-dihydroxybenzoate-AMP ligase from Bacillus subtilis (539 aa), FASTA scores: opt: 1569, E(): 1.2e-83, (44.9% identity in 532 aa overlap); O07899|VIBE_VIBCHVC0772 vibriobactin-specific 2,3-dihydroxybenzoate-AMP ligase from Vibrio cholerae (543 aa), FASTA scores: opt: 1457, E(): 3.7e-77, (44.6% identity in 545 aa overlap); etc. Also similar to P95819|SNBA pristinamycin I synthetase I from Streptomyces pristinaespiralis (582 aa), FASTA scores: opt: 1532, E(): 1.7e-81, (46.35% identity in 548 aa overlap); and Q9RFM9|PCHD salicyl-AMP ligase from Pseudomonas aeruginosa (547 aa), FASTA scores: opt: 1415, E(): 1e-74, (45.95% identity in 533 aa overlap). Contains PS00455 Putative AMP-binding domain signature. Belongs to the ATP-dependent AMP-binding enzyme family." /db_xref="EnsemblGenomes-Gn:Rv2384" /db_xref="EnsemblGenomes-Tr:CCP45172" /db_xref="GOA:P71716" /db_xref="InterPro:IPR000873" /db_xref="InterPro:IPR025110" /db_xref="InterPro:IPR042099" /db_xref="UniProtKB/Swiss-Prot:P71716" /inference="protein motif:PROSITE:PS00455" /experiment="EXISTENCE: identified in proteomics study" BEGIN 1 MPPKAADGRR PSPDGGLGGF VPFPADRAAS YRAAGYWSGR TLDTVLSDAA RRWPDRLAVA 61 DAGDRPGHGG LSYAELDQRA DRAAAALHGL GITPGDRVLL QLPNGCQFAV ALFALLRAGA 121 IPVMCLPGHR AAELGHFAAV SAATGLVVAD VASGFDYRPM ARELVADHPT LRHVIVDGDP 181 GPFVSWAQLC AQAGTGSPAP PADPGSPALL LVSGGTTGMP KLIPRTHDDY VFNATASAAL 241 CRLSADDVYL VVLAAGHNFP LACPGLLGAM TVGATAVFAP DPSPEAAFAA IERHGVTVTA 301 LVPALAKLWA QSCEWEPVTP KSLRLLQVGG SKLEPEDARR VRTALTPGLQ QVFGMAEGLL 361 NFTRIGDPPE VVEHTQGRPL CPADELRIVN ADGEPVGPGE EGELLVRGPY TLNGYFAAER 421 DNERCFDPDG FYRSGDLVRR RDDGNLVVTG RVKDVICRAG ETIAASDLEE QLLSHPAIFS 481 AAAVGLPDQY LGEKICAAVV FAGAPITLAE LNGYLDRRGV AAHTRPDQLV AMPALPTTPI 541 GKIDKRAIVR QLGIATGPVT TQRCH //