ID   BLC6_VIBCL              Reviewed;         288 AA.
AC   P81781;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Beta-lactamase CARB-6;
DE            EC=3.5.2.6;
DE   AltName: Full=Carbenicillinase 6;
DE   Flags: Precursor;
GN   Name=carB6;
OS   Vibrio cholerae.
OG   Plasmid.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=NON-O1, and NON-O139;
RX   PubMed=9925522; DOI=10.1128/aac.43.2.297;
RA   Choury D., Aubert G., Szajnert M.-F., Azibi K., Delpech M., Paul G.;
RT   "Characterization and nucleotide sequence of CARB-6, a new carbenicillin-
RT   hydrolyzing beta-lactamase from Vibrio cholerae.";
RL   Antimicrob. Agents Chemother. 43:297-301(1999).
CC   -!- FUNCTION: Hydrolyzes both ticarcillin and oxacillin.
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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10101};
CC   -!- ACTIVITY REGULATION: Inhibited by clavulanic acid, sulbactam and
CC       tazobactam.
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; AF030945; AAD19217.1; -; Genomic_DNA.
DR   RefSeq; WP_063859348.1; NG_048751.1.
DR   AlphaFoldDB; P81781; -.
DR   SMR; P81781; -.
DR   KEGG; ag:AAD19217; -.
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; DD-peptidase/beta-lactamase superfamily; 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; BETA-LACTAMASE; 1.
DR   PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   PRINTS; PR00118; BLACTAMASEA.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; Disulfide bond; Hydrolase; Plasmid; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..288
FT                   /note="Beta-lactamase CARB-6"
FT                   /id="PRO_0000017045"
FT   ACT_SITE        65
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   BINDING         229..231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        72..118
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   288 AA;  31430 MW;  FBBE71A6AB090928 CRC64;
     MKFLLAFSLL IPSVVFASSS KFQQVEQDVK AIEVSLSARI GVSVLDTQNG EYWDYNGNQR
     FPLTSTFKTI ACAKLLYDAE QGKVNPNSTV EIKKADLVTY SPVIEKQVGQ AITLDDACFA
     TMTTSDNTAA NIILSAVGGP KGVTDFLRQI GDKETRLDRI EPDLNEGKLG DLRDTTTPKA
     IASTLNQLLF GSTLSEASQK KLESWMVNNQ VTGNLLRSVL PVKWSIADRS GAGGFGARSI
     TAIVWSEEKK TIIVSIYLAQ TEASMAERND AIVKIGRSIF EVYTSQSR
//