ID Q2XPY6_SALET Unreviewed; 291 AA.
AC Q2XPY6;
DT 20-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN Name=blaCTX-M-53 {ECO:0000313|EMBL:ABB72225.1};
OS Salmonella enterica subsp. enterica serovar Westhampton.
OG Plasmid pWES-1 {ECO:0000313|EMBL:ABB72225.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=356621 {ECO:0000313|EMBL:ABB72225.1};
RN [1] {ECO:0000313|EMBL:ABB72225.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=05-686 {ECO:0000313|EMBL:ABB72225.1};
RC PLASMID=pWES-1 {ECO:0000313|EMBL:ABB72225.1};
RA Weill F.-X., Fabre L., Brisabois A., Grimont P.A.D., Bonnet R.;
RT "Characterization of a novel CTX-M (CTX-M-53) extended-spectrum beta-
RT lactamase from Salmonella enterica serotype Westhampton in France.";
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABB72225.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=05-686 {ECO:0000313|EMBL:ABB72225.1};
RC PLASMID=pWES-1 {ECO:0000313|EMBL:ABB72225.1};
RX PubMed=19273683; DOI=10.1128/AAC.01581-08;
RA Doublet B., Granier S.A., Robin F., Bonnet R., Fabre L., Brisabois A.,
RA Cloeckaert A., Weill F.X.;
RT "Novel plasmid-encoded ceftazidime-hydrolyzing CTX-M-53 extended-spectrum
RT beta-lactamase from Salmonella enterica serotypes Westhampton and
RT Senftenberg.";
RL Antimicrob. Agents Chemother. 53:1944-1951(2009).
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;
CC Evidence={ECO:0000256|ARBA:ARBA00001526,
CC ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; DQ268764; ABB72225.1; -; Genomic_DNA.
DR RefSeq; WP_012579062.1; NG_049004.1.
DR RefSeq; YP_002332251.1; NC_011604.1.
DR AlphaFoldDB; Q2XPY6; -.
DR SMR; Q2XPY6; -.
DR BindingDB; Q2XPY6; -.
DR ChEMBL; CHEMBL1667678; -.
DR DrugCentral; Q2XPY6; -.
DR KEGG; ag:ABB72225; -.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251,
KW ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361140};
KW Plasmid {ECO:0000313|EMBL:ABB72225.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..291
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004218417"
FT DOMAIN 50..265
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 291 AA; 31184 MW; BA11CFC4BA857BEC CRC64;
MVKKSLRQFT LMATATVTLL LGSVPLYAQT VDVQQKLAEL EQQSGGRLGV ALINTADNSQ
ILYRADERFA MCSTSKVMAV AAVLKKSESE PNLLNQRVEI KKSDLVNYNP IAEKHVNGTM
SLAELSAAAL QYSDNVAMNK LIAHVGGPAS VTAFARQLGD ETFRLDRTEP TLNTAIPGDP
RDTTSPRAMA QTLRNLTLGK ALGDSQRAQL VTWMKGNTTG AASIQAGLPA SWVVGDKTGS
GGYGTTNDIA VIWPKDRAPL ILVIYFTQPQ PKAESRRDVL ASAAKIVTDG L
//
