ID R4M7M0_MYCTX Unreviewed; 369 AA.
AC R4M7M0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=I917_25215 {ECO:0000313|EMBL:AGL25143.1};
OS Mycobacterium tuberculosis str. Haarlem/NITR202.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=1304279 {ECO:0000313|EMBL:AGL25143.1, ECO:0000313|Proteomes:UP000013563};
RN [1] {ECO:0000313|EMBL:AGL25143.1, ECO:0000313|Proteomes:UP000013563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Haarlem/NITR202 {ECO:0000313|EMBL:AGL25143.1,
RC ECO:0000313|Proteomes:UP000013563};
RX PubMed=23788533;
RA Narayanan S., Deshpande U.;
RT "Whole-Genome Sequences of Four Clinical Isolates of Mycobacterium
RT tuberculosis from Tamil Nadu, South India.";
RL Genome Announc. 1:e00186-13(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC ChEBI:CHEBI:140347; EC=3.5.2.6;
CC Evidence={ECO:0000256|ARBA:ARBA00001526};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP004886; AGL25143.1; -; Genomic_DNA.
DR KEGG; mtuh:I917_25215; -.
DR PATRIC; fig|1304279.3.peg.5127; -.
DR HOGENOM; CLU_042385_1_0_11; -.
DR BioCyc; MTUB1304279:G13AB-3412-MONOMER; -.
DR Proteomes; UP000013563; Chromosome.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 1.10.8.620; ORF12 helical bundle domain-like; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR045155; Beta-lactam_cat.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR InterPro; IPR040846; ORF_12_N.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR Pfam; PF18042; ORF_12_N; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Lipoprotein {ECO:0000313|EMBL:AGL25143.1}.
FT DOMAIN 2..55
FT /note="ORF 12 gene product N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18042"
FT DOMAIN 90..200
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 369 AA; 40139 MW; B30CA3F4EFE66B2C CRC64;
MQVDTVKTTM EALWWDRPFA LAGVDIGASV AXLHLISSYG AQQDIRIHTD DDGWVXRFDV
ETQAPSIASW RDVDAVLSKT GARYSFQVAK VDNGRCDPVA GTNTGESLPL ASIFKLYVLH
ALAGAVQHNT VSWDDLLTVT AKSKAVGSSG LELPVGARVS VRTAAEKMIA TSDNMATDLL
IERLGTRAIE EALASAGHHD PASMTPFPTM YELFSVGWGK PDLRDQWKHA TQQVRAQILR
QTNSTPYQPD PTRAHTPASN YGAEWYGSAE DICRVHAALR ADAVGPASPV RQIMSAVPGI
QLDRSVWPYI GAKAGGLPGD LTFSWYAVDK TGQPWVVSFQ LNWPRDHGPT VTGWMLQVAR
QVFALIAPQ
//
