ID   BLAC_MYCTO              Reviewed;         307 AA.
AC   P9WKD2; L0T8I9; P0A5I6; P0C5C1; Q10670;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
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=MT2128;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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 M.tuberculosis 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}.
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; AE000516; AAK46408.1; -; Genomic_DNA.
DR   PIR; G70764; G70764.
DR   RefSeq; WP_003410677.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WKD2; -.
DR   SMR; P9WKD2; -.
DR   BindingDB; P9WKD2; -.
DR   EnsemblBacteria; AAK46408; AAK46408; MT2128.
DR   GeneID; 45426045; -.
DR   KEGG; mtc:MT2128; -.
DR   PATRIC; fig|83331.31.peg.2296; -.
DR   HOGENOM; CLU_031960_6_0_11; -.
DR   Proteomes; UP000001020; 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_0000427674"
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