ID   BLA1_ECOLX              Reviewed;         286 AA.
AC   P0AD63; O07941; P14557; P23982;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Beta-lactamase SHV-1;
DE            EC=3.5.2.6;
DE   AltName: Full=PIT-2;
DE   Flags: Precursor;
GN   Name=bla; Synonyms=shv1;
OS   Escherichia coli.
OG   Plasmid p453.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33694 / HB101;
RX   PubMed=10582889; DOI=10.1128/aac.43.12.2960;
RA   Bradford P.A.;
RT   "Automated thermal cycling is superior to traditional methods for
RT   nucleotide sequencing of bla(SHV) genes.";
RL   Antimicrob. Agents Chemother. 43:2960-2963(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 22-286.
RC   PLASMID=p453;
RX   PubMed=3260490; DOI=10.1042/bj2510073;
RA   Barthelemy M., Peduzzi J., Labia R.;
RT   "Complete amino acid sequence of p453-plasmid-mediated PIT-2 beta-lactamase
RT   (SHV-1).";
RL   Biochem. J. 251:73-79(1988).
RN   [3]
RP   PROTEIN SEQUENCE OF 22-128.
RC   PLASMID=p453;
RX   PubMed=3497152; DOI=10.1093/jac/19.6.839;
RA   Barthelemy M., Peduzzi J., Labia R.;
RT   "N-terminal amino acid sequence of PIT-2 beta-lactamase (SHV-1).";
RL   J. Antimicrob. Chemother. 19:839-841(1987).
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; AF148850; AAD37412.1; -; Genomic_DNA.
DR   RefSeq; WP_001620095.1; NZ_VKYG01000130.1.
DR   AlphaFoldDB; P0AD63; -.
DR   SMR; P0AD63; -.
DR   BindingDB; P0AD63; -.
DR   ChEMBL; CHEMBL5956; -.
DR   DrugBank; DB03445; (3S)-3-(dioxidosulfanyl)-N-[(1E)-3-oxoprop-1-en-1-yl]-4-(1H-1,2,3-triazol-1-yl)-D-valine.
DR   DrugBank; DB03834; (3S)-3-(dioxidosulfanyl)-N-[(1Z)-3-oxoprop-1-en-1-yl]-4-(1H-1,2,3-triazol-1-yl)-D-valine.
DR   DrugBank; DB03970; (7R)-7-(6,7-Dihydro-5H-cyclopenta[d]imidazo[2,1-b][1,3]thiazol-2-yl)-2,7-dihydro-1,4-thiazepine-3,6-dicarboxylic acid.
DR   DrugBank; DB02579; Acrylic Acid.
DR   DrugBank; DB09060; Avibactam.
DR   DrugBank; DB03472; Cyclohexyl-Hexyl-Beta-D-Maltoside.
DR   DrugBank; DB01598; Imipenem.
DR   DrugBank; DB03057; Malonaldehyde.
DR   DrugBank; DB12377; Relebactam.
DR   DrugBank; DB01606; Tazobactam.
DR   DrugCentral; P0AD63; -.
DR   KEGG; ag:AAD37412; -.
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   1: Evidence at protein level;
KW   Antibiotic resistance; Direct protein sequencing; Disulfide bond;
KW   Hydrolase; Plasmid; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:3260490,
FT                   ECO:0000269|PubMed:3497152"
FT   CHAIN           22..286
FT                   /note="Beta-lactamase SHV-1"
FT                   /id="PRO_0000016980"
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        136..137
FT                   /note="AT -> TA (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   286 AA;  31224 MW;  C78F42667E698E6C CRC64;
     MRYIRLCIIS LLATLPLAVH ASPQPLEQIK LSESQLSGRV GMIEMDLASG RTLTAWRADE
     RFPMMSTFKV VLCGAVLARV DAGDEQLERK IHYRQQDLVD YSPVSEKHLA DGMTVGELCA
     AAITMSDNSA ANLLLATVGG PAGLTAFLRQ IGDNVTRLDR WETELNEALP GDARDTTTPA
     SMAATLRKLL TSQRLSARSQ RQLLQWMVDD RVAGPLIRSV LPAGWFIADK TGAGERGARG
     IVALLGPNNK AERIVVIYLR DTPASMAERN QQIAGIGAAL IEHWQR