ID   BLAC_PHOVU              Reviewed;         321 AA.
AC   P30899;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
DE   Flags: Precursor;
GN   Name=cfxA;
OS   Phocaeicola vulgatus (Bacteroides vulgatus).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Phocaeicola.
OX   NCBI_TaxID=821;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CLA341;
RX   PubMed=8517690; DOI=10.1128/aac.37.5.1028;
RA   Parker A.C., Smith C.J.;
RT   "Genetic and biochemical analysis of a novel Ambler class A beta-lactamase
RT   responsible for cefoxitin resistance in Bacteroides species.";
RL   Antimicrob. Agents Chemother. 37:1028-1036(1993).
CC   -!- FUNCTION: Can hydrolyze cephalosporins, penicillins and also cefoxitin;
CC       but at a slow rate.
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.
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; U38243; AAB17891.1; -; Genomic_DNA.
DR   PIR; I40600; S27528.
DR   RefSeq; WP_063843237.1; NG_047633.1.
DR   AlphaFoldDB; P30899; -.
DR   SMR; P30899; -.
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   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Hydrolase; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..321
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000017038"
FT   ACT_SITE        83
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   BINDING         233..235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   321 AA;  35376 MW;  6ADD45ED16F0BDFA CRC64;
     MEKNRKKQIV VLSIALVCIF ILVFSLFHKS ATKDSANPPL TNVLTDSISQ IVSACPGEIG
     VAVIVNNRDT VKVNNKSVYP MMSVFKVHQA LALCNDFDNK GISLDTLVNI NRDKLDPKTW
     SPMLKDYSGP VISLTVRDLL RYTLTQSDNN ASNLMFKDMV NVAQTDSFIA TLIPRSSFQI
     AYTEEEMSAD HNKAYSNYTS PLGAAMLMNR LFTEGLIDDE KQSFIKNTLK ECKTGVDRIA
     APLLDKEGVV IAHKTGSGYV NENGVLAAHN DVAYICLPNN ISYTLAVFVK DFKGNKSQAS
     QYVAHISAVV YSLLMQTSVK S
//