BLA2_ECOLX
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 03-AUG-2022, entry version 59.
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; Proteobacteria; 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; -; 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: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
