ID   BLA8_ECOLX              Reviewed;         286 AA.
AC   O08337;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Beta-lactamase SHV-8;
DE            EC=3.5.2.6;
DE   Flags: Precursor;
GN   Name=bla; Synonyms=shv8;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9056008; DOI=10.1128/aac.41.3.647;
RA   Rasheed J.K., Jay C., Metchock B., Berkowitz F., Weigel L., Crellin J.,
RA   Steward C., Hill B., Medeiros A.A., Tenover F.C.;
RT   "Evolution of extended-spectrum beta-lactam resistance (SHV-8) in a strain
RT   of Escherichia coli during multiple episodes of bacteremia.";
RL   Antimicrob. Agents Chemother. 41:647-653(1997).
CC   -!- FUNCTION: SHV enzymes hydrolyze broad spectrum cephalosporins notably
CC       cefotaxime 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; U92041; AAB51384.1; -; Genomic_DNA.
DR   RefSeq; WP_063864710.1; NG_050115.1.
DR   AlphaFoldDB; O08337; -.
DR   SMR; O08337; -.
DR   KEGG; ag:AAB51384; -.
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                   /evidence="ECO:0000255"
FT   CHAIN           22..286
FT                   /note="Beta-lactamase SHV-8"
FT                   /id="PRO_0000016986"
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;  31223 MW;  F159990BC8BF5504 CRC64;
     MRYIRLCIIS LLATLPLAVH ASPQPLEQIK LSESQLSGRV GMIEMDLASG RTLTAWRADE
     RFPMMSTFKV VLCGAVLARV DAGDEQLERK IHYRQQDLVD YSPVSEKHLA DGMTVGELCA
     AAITMSDNSA ANLLLATVGG PAGLTAFLRQ IGDNVTRLDR WETELNEALP GDARNTTTPA
     SMAATLRKLL TSQRLSARSQ RQLLQWMVDD RVAGPLIRSV LPAGWFIADK TGAGERGARG
     IVALLGPNNK AERIVVIYLR DTPASMAERN QQIAGIGAAL IEHWQR