ID   BLA2_KLEPN              Reviewed;         286 AA.
AC   P0A9Z8; P14558;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Beta-lactamase SHV-2;
DE            EC=3.5.2.6;
DE   AltName: Full=SHV-2A;
DE   Flags: Precursor;
GN   Name=bla; Synonyms=shv2;
OS   Klebsiella pneumoniae.
OG   Plasmid pZMP1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2160941; DOI=10.1128/jb.172.6.3229-3236.1990;
RA   Lee K.Y., Hopkins J.D., Syvanen M.;
RT   "Direct involvement of IS26 in an antibiotic resistance operon.";
RL   J. Bacteriol. 172:3229-3236(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KPR 14; PLASMID=pZMP1;
RX   PubMed=2033379; DOI=10.1099/00221287-137-3-569;
RA   Podbielski A., Schoenling J., Melzer B., Warnatz K., Leusch H.G.;
RT   "Molecular characterization of a new plasmid-encoded SHV-type beta-
RT   lactamase (SHV-2 variant) conferring high-level cefotaxime resistance upon
RT   Klebsiella pneumoniae.";
RL   J. Gen. Microbiol. 137:569-578(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KPZU-3;
RX   PubMed=7486909; DOI=10.1128/aac.39.8.1726;
RA   Nuesch-Inderbinen M., Hachler H., Kayser F.H.;
RT   "New system based on site-directed mutagenesis for highly accurate
RT   comparison of resistance levels conferred by SHV beta-lactamases.";
RL   Antimicrob. Agents Chemother. 39:1726-1730(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KPLA-10;
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: This enzyme hydrolyzes cefotaxime, ceftazidime and other
CC       broad spectrum 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   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; X62115; CAA44025.1; -; Genomic_DNA.
DR   EMBL; X53817; CAA37813.1; -; Genomic_DNA.
DR   EMBL; X84314; CAA59058.1; -; Genomic_DNA.
DR   EMBL; X98102; CAA66730.1; -; Genomic_DNA.
DR   RefSeq; WP_032488413.1; NZ_WRXI01000049.1.
DR   RefSeq; YP_001966240.1; NC_010886.1.
DR   AlphaFoldDB; P0A9Z8; -.
DR   SMR; P0A9Z8; -.
DR   KEGG; ag:CAA37813; -.
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:0000250"
FT   CHAIN           22..286
FT                   /note="Beta-lactamase SHV-2"
FT                   /id="PRO_0000041957"
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"
FT   CONFLICT        31
FT                   /note="Q -> L (in Ref. 1; CAA44025)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   286 AA;  31269 MW;  49BF426DBC1F551D CRC64;
     MRYIRLCIIS LLATLPLAVH ASPQPLEQIK QSESQLSGRV GMIEMDLASG RTLTAWRADE
     RFPMMSTFKV VLCGAVLARV DAGDEQLERK IHYRQQDLVD YSPVSEKHLA DGMTVGELCA
     AAITMSDNSA ANLLLATVGG PAGLTAFLRQ IGDNVTRLDR WETELNEALP GDARDTTTPA
     SMAATLRKLL TSQRLSARSQ RQLLQWMVDD RVAGPLIRSV LPAGWFIADK TGASERGARG
     IVALLGPNNK AERIVVIYLR DTPASMAERN QQIAGIGAAL IEHWQR