ID   BLA5_KLEPN              Reviewed;         286 AA.
AC   P0A3M1; P37320;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Beta-lactamase SHV-5;
DE            EC=3.5.2.6;
DE   Flags: Precursor;
GN   Name=bla; Synonyms=shv5;
OS   Klebsiella pneumoniae.
OG   Plasmid pAFF1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pAFF1;
RX   PubMed=2088203; DOI=10.1128/aac.34.12.2439;
RA   Billot-Klein D., Gutmann L., Collatz E.;
RT   "Nucleotide sequence of the SHV-5 beta-lactamase gene of a Klebsiella
RT   pneumoniae plasmid.";
RL   Antimicrob. Agents Chemother. 34:2439-2441(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KPGE-2, and KPLA-4;
RX   PubMed=9145849; DOI=10.1128/aac.41.5.943;
RA   Nuesch-Inderbinen M., Kayser F.H., Hachler H.;
RT   "Survey and molecular genetics of SHV beta-lactamases in Enterobacteriaceae
RT   in Switzerland: two novel enzymes, SHV-11 and SHV-12.";
RL   Antimicrob. Agents Chemother. 41:943-949(1997).
CC   -!- FUNCTION: SHV enzymes hydrolyze broad spectrum cephalosporins notably
CC       cefotaxime and ceftazidime. SHV-5 causes particularly high levels of
CC       resistance to aztreonam and ceftazidime.
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; X55640; CAA39164.1; -; Genomic_DNA.
DR   EMBL; X98103; CAA66731.1; -; Genomic_DNA.
DR   EMBL; X98104; CAA66732.1; -; Genomic_DNA.
DR   PIR; A60632; A60632.
DR   RefSeq; WP_011117369.1; NZ_WULK01000045.1.
DR   AlphaFoldDB; P0A3M1; -.
DR   SMR; P0A3M1; -.
DR   BindingDB; P0A3M1; -.
DR   ChEMBL; CHEMBL1075174; -.
DR   DrugCentral; P0A3M1; -.
DR   KEGG; ag:CAA39164; -.
DR   BRENDA; 3.5.2.6; 2814.
DR   SABIO-RK; P0A3M1; -.
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; Plasmid; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..286
FT                   /note="Beta-lactamase SHV-5"
FT                   /id="PRO_0000016983"
FT   ACT_SITE        66
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   ACT_SITE        164
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         230..232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..119
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   286 AA;  31253 MW;  738F426CC51F5FBA CRC64;
     MRYIRLCIIS LLATLPLAVH ASPQPLEQIK LSESQLSGRV GMIEMDLASG RTLTAWRADE
     RFPMMSTFKV VLCGAVLARV DAGDEQLERK IHYRQQDLVD YSPVSEKHLA DGMTVGELCA
     AAITMSDNSA ANLLLATVGG PAGLTAFLRQ IGDNVTRLDR WETELNEALP GDARDTTTPA
     SMAATLRKLL TSQRLSARSQ RQLLQWMVDD RVAGPLIRSV LPAGWFIADK TGASKRGARG
     IVALLGPNNK AERIVVIYLR DTPASMAERN QQIAGIGAAL IEHWQR