LOCUS SIU01017.1 565 aa PRT BCT 25-MAY-2020
DEFINITION Mycobacterium tuberculosis variant bovis AF2122/97 BIFUNCTIONAL
ENZYME MBTA: SALICYL-AMP LIGASE (SAL-AMP LIGASE) + SALICYL-
S-ArCP SYNTHETASE protein.
ACCESSION LT708304-2431
PROTEIN_ID SIU01017.1
SOURCE Mycobacterium tuberculosis variant bovis AF2122/97
ORGANISM Mycobacterium tuberculosis variant bovis AF2122/97
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
REFERENCE 1
AUTHORS Malone K.M.
JOURNAL Submitted (06-DEC-2016) to the INSDC. School of Veterinary
Medicine, Tuberculosis Molecular Microbiology Research Group,
University College Dublin, Tuberculosis Molecular Microbiology
Research Group, School of Veterinary Medicine, University College
Dublin, D4, Ireland
REFERENCE 2
AUTHORS Malone M K., Farrell D., Malone K.
JOURNAL Submitted (15-APR-2020) to the INSDC. School of Veterinary
Medicine, Tuberculosis Molecular Microbiology Research Group,
University College Dublin, Tuberculosis Molecular Microbiology
Research Group, School of Veterinary Medicine,, University College
Dublin, D4, Ireland
FEATURES Qualifiers
source /organism="Mycobacterium tuberculosis variant bovis
AF2122/97"
/chromosome="Mycobacterium_bovis_AF212297"
/isolate="AF2122/97"
/mol_type="genomic DNA"
/isolation_source="Mycobacterium bovis subsp. bovis strain
AF2122/97. This strain is a fully virulent strain that was
isolated in 1997 in the UK from a cow suffering necrotic
lesions in lung and bronchomediastinal lymph nodes. The
strain was also reported to infect and persist in badgers
that are considered to be a significant source of bovine
infection."
/db_xref="taxon:233413"
protein /transl_table=11
/gene="mbtA"
/locus_tag="BQ2027_MB2405"
/note="Mb2405, mbtA, len: 565 aa. Equivalent to Rv2384,
len: 565 aa, from Mycobacterium tuberculosis strain H37Rv,
(100.0% identity in 565 aa overlap). mbtA, bifunctional
enzyme, including salicyl-AMP ligase (Sal-AMP ligase) (EC
6.-.-.-) and salicyl-S-ArCP synthetase (see first and
second citations below), 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 third
citation below); P40871|DHBE_BACSU|ENTE
2,3-DIHYDROXYBENZOATE-AMP LIGASE (EC 6.3.2.-) 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="GOA:A0A1R3Y1F4"
/db_xref="InterPro:IPR000873"
/db_xref="InterPro:IPR025110"
/db_xref="InterPro:IPR042099"
/db_xref="UniProtKB/TrEMBL:A0A1R3Y1F4"
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
//