ID   BLAC_PROVU              Reviewed;         271 AA.
AC   P80298;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
OS   Proteus vulgaris.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=585;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=RO104;
RX   PubMed=8043607; DOI=10.1016/0167-4838(94)90048-5;
RA   Peduzzi J., Reynaud A., Barthelemy M., Baron P., Labia R.;
RT   "Chromosomally encoded cephalosporin-hydrolyzing beta-lactamase of Proteus
RT   vulgaris RO104 belongs to Ambler's class A.";
RL   Biochim. Biophys. Acta 1207:31-39(1994).
CC   -!- FUNCTION: Hydrolyzes broad-spectrum beta-lactam antibiotics. Active
CC       against cephalosporins.
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   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   PIR; S47620; S47620.
DR   AlphaFoldDB; P80298; -.
DR   SMR; P80298; -.
DR   ChEMBL; CHEMBL4782; -.
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   1: Evidence at protein level;
KW   Antibiotic resistance; Direct protein sequencing; Hydrolase.
FT   CHAIN           1..271
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000195441"
FT   ACT_SITE        46
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   BINDING         210..212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   271 AA;  29803 MW;  C6148E4F2500DDFF CRC64;
     NTNNTIEEQL STLEKYSQGR LGVALINTED NSQITYRGEE RFAMASTSKV MAVAAILKES
     EKQAGLLDKN IIITKSDLVA YSPITEKHLA TGMSLAQLSA ATLQYSDNTA MNKILDYLGG
     PSKVTQFARS INDVTYRLDR KEPELNTAIH GDPRDTTSPI AMAKSLQALT LGDALGQSQR
     QQLVTWLKGN TTGDHSIKAG LPKHWIVGDK TGSGDYGTTN DIAVIWPKNH APLILVVYFT
     QQEQDAKYRK DIIVKATEIV TKEFSNTSQK K