ID   BLAC_SERFO              Reviewed;         267 AA.
AC   P80545;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
DE   Contains:
DE     RecName: Full=Beta-lactamase form I;
DE   Contains:
DE     RecName: Full=Beta-lactamase form II;
OS   Serratia fonticola.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=47917;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=CUV;
RX   PubMed=9300809; DOI=10.1016/s0167-4838(97)00020-4;
RA   Peduzzi J., Farzaneh S., Reynaud A., Barthelemy M., Labia R.;
RT   "Characterization and amino acid sequence analysis of a new oxyimino
RT   cephalosporin-hydrolyzing class A beta-lactamase from Serratia fonticola
RT   CUV.";
RL   Biochim. Biophys. Acta 1341:58-70(1997).
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;
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   AlphaFoldDB; P80545; -.
DR   SMR; P80545; -.
DR   STRING; 47917.AV650_16940; -.
DR   PRIDE; P80545; -.
DR   SABIO-RK; P80545; -.
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   PANTHER; PTHR35333; PTHR35333; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   PRINTS; PR00118; BLACTAMASEA.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; Direct protein sequencing; Hydrolase.
FT   CHAIN           1..267
FT                   /note="Beta-lactamase form I"
FT                   /id="PRO_0000017010"
FT   CHAIN           6..267
FT                   /note="Beta-lactamase form II"
FT                   /id="PRO_0000017011"
FT   ACT_SITE        49
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         213..215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   267 AA;  28755 MW;  D70C1FDEE63F09C3 CRC64;
     QPANAKANIQ QQLSELEKNS GGRLGVALID TADNSQILYR GDERFPMCST SKVMAVSALL
     KQSETDKNLL AKRMEIKQSD LVNYNPIAEK HLDTGMTLAE FSAATIQYSD NTAMNKILEH
     LGGPAKVTEF ARTIGDKTFR LDRTEPTLNT AIPGDKRDTT SPQAMAISLQ NLTLGKALAE
     PQRAQLVEWM KGNTTGGASI RAGLPTTWVV GDKTGSGDYG TTNDIAVIWP ANHAPLVLVT
     YFTQPQQNAE ARKDVLAAAA KIVTAGL