BLAC_MYCBO
ID BLAC_MYCBO Reviewed; 307 AA.
AC P0A5I7; A0A1R3Y039; Q10670; X2BJD5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Beta-lactamase {ECO:0000250|UniProtKB:P9WKD3};
DE EC=3.5.2.6 {ECO:0000250|UniProtKB:P9WKD3};
DE AltName: Full=Ambler class A beta-lactamase {ECO:0000250|UniProtKB:P9WKD3};
DE Flags: Precursor;
GN Name=blaC; Synonyms=blaA; OrderedLocusNames=BQ2027_MB2094C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
CC -!- FUNCTION: Extended spectrum beta-lactamase (ESBL) that inactivates
CC beta-lactam antibiotics by hydrolyzing the amide group of the beta-
CC lactam ring. Displays high levels of penicillinase and cephalosporinase
CC activity as well as measurable activity with carbapenems, including
CC imipenem and meropenem. Plays a primary role in the intrinsic
CC resistance of mycobacteria to beta-lactam antibiotics.
CC {ECO:0000250|UniProtKB:P9WKD3}.
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:0000250|UniProtKB:P9WKD3};
CC -!- ACTIVITY REGULATION: Is inhibited by clavulanate.
CC {ECO:0000250|UniProtKB:P9WKD3}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P9WKD3}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P9WKD3}.
CC Secreted {ECO:0000250|UniProtKB:A5U493}.
CC -!- PTM: Exported by the Tat system. The position of the signal peptide
CC cleavage has not been experimentally proven.
CC {ECO:0000250|UniProtKB:P9WKD3}.
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000305}.
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DR EMBL; LT708304; SIU00701.1; -; Genomic_DNA.
DR RefSeq; NP_855744.1; NC_002945.3.
DR RefSeq; WP_003410677.1; NC_002945.4.
DR AlphaFoldDB; P0A5I7; -.
DR SMR; P0A5I7; -.
DR EnsemblBacteria; SIU00701; SIU00701; BQ2027_MB2094C.
DR GeneID; 45426045; -.
DR PATRIC; fig|233413.5.peg.2303; -.
DR OMA; EWMKGNA; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
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; -; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR045155; Beta-lactam_cat.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR InterPro; IPR023650; Beta-lactam_class-A_AS.
DR PANTHER; PTHR35333; PTHR35333; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR PRINTS; PR00118; BLACTAMASEA.
DR SUPFAM; SSF56601; SSF56601; 1.
DR PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Hydrolase; Periplasm; Secreted; Signal.
FT SIGNAL 1..34
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 35..307
FT /note="Beta-lactamase"
FT /id="PRO_0000017004"
FT ACT_SITE 84
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P9WKD3"
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WKD3"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKD3"
FT BINDING 251..253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKD3"
FT SITE 87
FT /note="Increases nucleophilicity of active site Ser"
FT /evidence="ECO:0000250|UniProtKB:P9WKD3"
FT SITE 117
FT /note="Functions as a gatekeeper residue that regulates
FT substrate accessibility to the enzyme active site"
FT /evidence="ECO:0000250|UniProtKB:P9WKD3"
SQ SEQUENCE 307 AA; 32568 MW; 448CB2A0E05F4315 CRC64;
MRNRGFGRRE LLVAMAMLVS VTGCARHASG ARPASTTLPA GADLADRFAE LERRYDARLG
VYVPATGTTA AIEYRADERF AFCSTFKAPL VAAVLHQNPL THLDKLITYT SDDIRSISPV
AQQHVQTGMT IGQLCDAAIR YSDGTAANLL LADLGGPGGG TAAFTGYLRS LGDTVSRLDA
EEPELNRDPP GDERDTTTPH AIALVLQQLV LGNALPPDKR ALLTDWMARN TTGAKRIRAG
FPADWKVIDK TGTGDYGRAN DIAVVWSPTG VPYVVAVMSD RAGGGYDAEP REALLAEAAT
CVAGVLA
