ID   BLA2_KLEPO              Reviewed;         286 AA.
AC   P0A9Z9; P14558;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 53.
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 subsp. ozaenae.
OG   Plasmid pBP60-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=574;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=2180;
RX   PubMed=2395654; DOI=10.1093/nar/18.16.4916;
RA   Podbielski A., Melzer B.;
RT   "Nucleotide sequence of the gene encoding the SHV-2 beta-lactamase (blaSHV-
RT   2) of Klebsiella ozaenae.";
RL   Nucleic Acids Res. 18:4916-4916(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pBP60-1;
RX   PubMed=2285285; DOI=10.1128/aac.34.9.1725;
RA   Huletsky A., Couture F., Levesque R.C.;
RT   "Nucleotide sequence and phylogeny of SHV-2 beta-lactamase.";
RL   Antimicrob. Agents Chemother. 34:1725-1732(1990).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X53433; CAA37524.1; -; Genomic_DNA.
DR   EMBL; M95179; AAA25526.1; -; Genomic_DNA.
DR   PIR; A44998; A44998.
DR   AlphaFoldDB; P0A9Z9; -.
DR   SMR; P0A9Z9; -.
DR   SABIO-RK; P0A9Z9; -.
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; DD-peptidase/beta-lactamase superfamily; 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; BETA-LACTAMASE; 1.
DR   PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   PRINTS; PR00118; BLACTAMASEA.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 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_0000041958"
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;  31254 MW;  738F4266651F551A CRC64;
     MRYIRLCIIS LLATLPLAVH ASPQPLEQIK LSESQLSGRV 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
//