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
//