ID   BLAC_BACUN              Reviewed;         296 AA.
AC   P30898;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
DE   Flags: Precursor;
GN   Name=cblA;
OS   Bacteroides uniformis.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WAL-7088;
RX   PubMed=7985999; DOI=10.1128/aac.38.8.1711;
RA   Smith C.J., Bennett T.K., Parker A.C.;
RT   "Molecular and genetic analysis of the Bacteroides uniformis
RT   cephalosporinase gene, cblA, encoding the species-specific beta-
RT   lactamase.";
RL   Antimicrob. Agents Chemother. 38:1711-1715(1994).
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   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; L08472; AAA66962.1; -; Genomic_DNA.
DR   PIR; I40231; I40231.
DR   RefSeq; WP_005827792.1; NZ_WCWS01000008.1.
DR   AlphaFoldDB; P30898; -.
DR   SMR; P30898; -.
DR   STRING; 820.ERS852554_00192; -.
DR   PRIDE; P30898; -.
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; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..296
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000017037"
FT   ACT_SITE        66
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   BINDING         235..237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   296 AA;  33450 MW;  87ACA38331207004 CRC64;
     MKAYFIAILT LFTCIATVVR AQQMSELENR IDSLLNGKKA TVGIAVWTDK GDMLRYNDHV
     HFPLLSVFKF HVALAVLDKM DKQSISLDSI VSIKASQMPP NTYSPLRKKF PDQDFTITLR
     ELMQYSISQS DNNACDILIE YAGGIKHIND YIHRLSIDSF NLSETEDGMH SSFEAVYRNW
     STPSAMVRLL RTADEKELFS NKELKDFLWQ TMIDTETGAN KLKGMLPAKT VVGHKTGSSD
     RNADGMKTAD NDAGLVILPD GRKYYIAAFV MDSYETDEDN ANIIARISRM VYDAMR