ID   BLAC_YEREN              Reviewed;         294 AA.
AC   Q01166;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
DE   Flags: Precursor;
GN   Name=blaA;
OS   Yersinia enterocolitica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Y-56 / Serotype O:3;
RX   PubMed=1886608; DOI=10.1007/bf00282468;
RA   Seoane A., Garcia Lobo J.M.;
RT   "Nucleotide sequence of a new class A beta-lactamase gene from the
RT   chromosome of Yersinia enterocolitica: implications for the evolution of
RT   class A beta-lactamases.";
RL   Mol. Gen. Genet. 228:215-220(1991).
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; X57074; CAA40357.1; -; Genomic_DNA.
DR   PIR; S16553; S16553.
DR   RefSeq; WP_005165780.1; NZ_LR698980.1.
DR   AlphaFoldDB; Q01166; -.
DR   SMR; Q01166; -.
DR   BRENDA; 3.5.2.6; 6741.
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..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..294
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000017022"
FT   ACT_SITE        75
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   BINDING         239..241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   294 AA;  31931 MW;  45E5B721A98B98C5 CRC64;
     MKHSSLRRSL LLAGITLPLV SFALPAWANA LPASVDKQLA ELERNANGRL GVAMINTGNG
     TKILYRAAQR FPFCSTFKFM LAAAVLDQSQ SQPNLLNKHI NYHESDLLSY APITRKNLAH
     GMTVSELCAA TIQYSDNTAA NLLIKELGGL AAVNQFARSI GDQMFRLDRW EPDLNTARPN
     DPRDTTTPAA MAASMNKLVL GDALRPAQRS QLAVWLKGNT TGDATIRAGA PTDWIVGDKT
     GSGDYGTTND IAVLWPTKGA PIVLVVYFTQ REKDAKPRRD VLASVTKIIL SQIS