ID   BLA2_ECOLX              Reviewed;         286 AA.
AC   P0A9Z7; P14558;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 63.
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   Escherichia coli.
OG   Plasmid pBWH77.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-204 / JC2926 pBP60-1;
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   STRAIN=A2302; PLASMID=pBWH77;
RX   PubMed=3129309; DOI=10.1016/0014-5793(88)80734-8;
RA   Barthelemy M., Peduzzi J., Yaghlane H.B., Labia R.;
RT   "Single amino acid substitution between SHV-1 beta-lactamase and
RT   cefotaxime-hydrolyzing SHV-2 enzyme.";
RL   FEBS Lett. 231:217-220(1988).
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}.
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DR   EMBL; AF148851; AAD37413.1; -; Genomic_DNA.
DR   PIR; S02434; S02434.
DR   RefSeq; WP_012477587.1; NZ_UDID01000061.1.
DR   AlphaFoldDB; P0A9Z7; -.
DR   SMR; P0A9Z7; -.
DR   DrugBank; DB09060; Avibactam.
DR   DrugBank; DB03472; Cyclohexyl-Hexyl-Beta-D-Maltoside.
DR   KEGG; ag:AAD37413; -.
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   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:3129309"
FT   CHAIN           22..286
FT                   /note="Beta-lactamase SHV-2"
FT                   /id="PRO_0000016981"
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
//