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   02-SEP-2026, entry version 72.
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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; 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).
RN   [4]
RP   AMINO ACID NUMBERING SCHEME.
RX   PubMed=2039479; DOI=10.1042/bj2760269;
RA   Ambler R.P., Coulson A.F., Frere J.M., Ghuysen J.M., Joris B., Forsman M.,
RA   Levesque R.C., Tiraby G., Waley S.G.;
RT   "A standard numbering scheme for the class A beta-lactamases.";
RL   Biochem. J. 276:269-270(1991).
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   -!- MISCELLANEOUS: The class A beta-lactamase family has a specific amino-
CC       acid numbering system, sometimes called Ambler or ABL numbering and
CC       often misspelt as Amber. A multiple sequence alignment was used to
CC       derive a consensus sequence and then the consensus was numbered taking
CC       into account insertions and deletions. This allows use of identical
CC       numbers, e.g. for active site residues, despite differences in protein
CC       length. UniProt always uses natural numbering of residues, hence there
CC       appear to be differences in numbering between this entry and some
CC       papers. {ECO:0000305|PubMed:2039479}.
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; AF148850; AAD37412.1; -; Genomic_DNA.
DR   RefSeq; WP_001620095.1; NZ_CP041539.1.
DR   AlphaFoldDB; P0AD63; -.
DR   SMR; P0AD63; -.
DR   BindingDB; P0AD63; -.
DR   ChEMBL; CHEMBL5956; -.
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   DrugBank; DB03445; Tazobactam trans-enamine intermediate.
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:InterPro.
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   NCBIfam; NF033103; bla_class_A; 1.
DR   NCBIfam; NF000285; SHV; 1.
DR   NCBIfam; NF012143; SHV_LEN_OKP; 1.
DR   PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR   PANTHER; PTHR35333:SF3; BETA-LACTAMASE-TYPE TRANSPEPTIDASE FOLD 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   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="Nucleophile; acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P62593"
FT   ACT_SITE        69
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P62593"
FT   ACT_SITE        126
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P62593"
FT   ACT_SITE        162
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P62593"
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
//