ID   BLA13_KLEPN             Reviewed;         286 AA.
AC   Q9S424;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Beta-lactamase SHV-13;
DE            EC=3.5.2.6;
DE   Flags: Precursor;
GN   Name=bla; Synonyms=shv13;
OS   Klebsiella pneumoniae.
OG   Plasmid.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=803;
RX   PubMed=10722518; DOI=10.1128/aac.44.4.1081-1084.2000;
RA   Yuan M., Hall L.M.C., Savelkoul P.H.M., Vandenbroucke-Grauls C.M.J.E.,
RA   Livermore D.M.;
RT   "SHV-13, a novel extended-spectrum beta-lactamase, in Klebsiella pneumoniae
RT   isolates from patients in an intensive care unit in Amsterdam.";
RL   Antimicrob. Agents Chemother. 44:1081-1084(2000).
CC   -!- FUNCTION: Broad spectrum beta-lactamase which hydrolyzes penicillins,
CC       as well as cephalosporins except cephamycins. Also hydrolyzes
CC       aztreonam, but not imipenem. Confers highly resistance to ceftazidime,
CC       cefotaxime, aztreonam and piperacillin.
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   -!- ACTIVITY REGULATION: Inhibited 16-fold better by the beta-lactamase
CC       inhibitor clavulanic acid than by tazobactam.
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; AF164577; AAD43815.1; -; Genomic_DNA.
DR   RefSeq; WP_063864619.1; NG_050008.1.
DR   AlphaFoldDB; Q9S424; -.
DR   SMR; Q9S424; -.
DR   KEGG; ag:AAD43815; -.
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-13"
FT                   /id="PRO_0000016987"
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;  CBBF426DA3FF5502 CRC64;
     MRYIRLCIIS LLATLPLAVH ASPQPLEQIK QSESQLSGRV GMIEMDLASG RTLTAWRADE
     RFPMMSTFKV VLCGAVLARV DAGDEQLERK IHYRQQDLVD YSPVSEKHLA DGMTVGELCA
     AAITMSDNSA ANLLLATVGG PAGLTAFLRQ IGDNVTRLDR WETELNEALP GDARDTTTPA
     SMAATLRKLL TSQRLSARSQ RQLLQWMVDD RVAGPLIRSV LPAGWFIADK TGAAERGARG
     IVALLGPNNK AERIVVIYLR DTPASMAERN QQIAGIGAAL IEHWQR