ID Q842A4_ECOLX Unreviewed; 291 AA.
AC Q842A4;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 103.
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=ctx-M-32 {ECO:0000313|EMBL:CAD89606.1};
OS Escherichia coli.
OG Plasmid pMC-2 {ECO:0000313|EMBL:CAD89606.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:CAD89606.1};
RN [1] {ECO:0000313|EMBL:CAD89606.1}
RP NUCLEOTIDE SEQUENCE.
RC PLASMID=pMC-2 {ECO:0000313|EMBL:CAD89606.1};
RX PubMed=15155242; DOI=10.1128/AAC.48.6.2308-2313.2004;
RA Cartelle M., del mar Tomas M., Molina F., Moure R., Villamueva R., Bou G.;
RT "High-level resistance to ceftazidime conferred by a novel enzyme, CTX-M-
RT 32, derived from CTX-M-1 through a single Asp240-Gly substitution.";
RL Antimicrob. Agents Chemother. 48:2308-2313(2004).
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}.
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; AJ557142; CAD89606.1; -; Genomic_DNA.
DR RefSeq; WP_000239591.1; NZ_WSVY01000072.1.
DR AlphaFoldDB; Q842A4; -.
DR SMR; Q842A4; -.
DR MEROPS; S11.A01; -.
DR KEGG; ag:CAD89606; -.
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:CAD89606.1}.
FT DOMAIN 50..264
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 291 AA; 31188 MW; D8274AA23E755FC5 CRC64;
MVKKSLRQFT LMATATVTLL LGSVPLYAQT ADVQQKLAEL ERQSGGRLGV ALINTADNSQ
ILYRADERFA MCSTSKVMAV AAVLKKSESE PNLLNQRVEI KKSDLVNYNP IAEKHVDGTM
SLAELSAAAL QYSDNVAMNK LISHVGGPAS VTAFARQLGD ETFRLDRTEP TLNTAIPGDP
RDTTSPRAMA QTLRNLTLGK ALGDSQRAQL VTWMKGNTTG AASIQAGLPA SWVVGDKTGS
GGYGTTNDIA VIWPKDRAPL ILVTYFTQPQ PKAESRRDVL ASAAKIVTNG L
//