ID   BLAC_KLEPN              Reviewed;         279 AA.
AC   P05192;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, 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;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LEN-1;
RX   PubMed=3533626; DOI=10.1016/0014-5793(86)80014-x;
RA   Arakawa Y., Ohta M., Kido N., Fujii Y., Komatsu T., Kato N.;
RT   "Close evolutionary relationship between the chromosomally encoded beta-
RT   lactamase gene of Klebsiella pneumoniae and the TEM beta-lactamase gene
RT   mediated by R plasmids.";
RL   FEBS Lett. 207:69-74(1986).
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; X04515; CAA28198.1; -; Genomic_DNA.
DR   PIR; A24469; A24469.
DR   RefSeq; WP_063860799.1; NG_049268.1.
DR   AlphaFoldDB; P05192; -.
DR   SMR; P05192; -.
DR   KEGG; ag:CAA28198; -.
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; Disulfide bond; Hydrolase; Signal.
FT   SIGNAL          1..21
FT   CHAIN           22..279
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000016999"
FT   ACT_SITE        66
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   BINDING         230..232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..119
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   279 AA;  30269 MW;  C5C88E34E6BCDAEB CRC64;
     MRYVRLCVIS LLATLPLVVY AGPQPLEQIK QSESQLSGRV GMVEMDLANG RTLAAWRADE
     RFPMVSTFKV LLCGAVLARV DAGLEQLDRR IHYRQQDLVD YSPVSEKHLV DGMTIGELCA
     AAITLSDNSA GNLLLATVGG PAGLTAFLRQ IGDNVTRLDR WETALNEALP GDARDTTTPA
     SMAATLRKLL TAQHLSARSQ QQLLQWMVDD RVAGPLIRAV LPPGWFIADK TGAGERGARG
     IVALLGPDGK PERIVVIYLR DTPASMAERN QHIAGIGQR