ID C5I573_KLEOX Unreviewed; 286 AA.
AC C5I573;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
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 {ECO:0000313|EMBL:ACR66326.1};
OS Klebsiella oxytoca.
OG Plasmid unnamed {ECO:0000313|EMBL:ACR66326.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=571 {ECO:0000313|EMBL:ACR66326.1};
RN [1] {ECO:0000313|EMBL:ACR66326.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=55 {ECO:0000313|EMBL:ACR66326.1};
RC PLASMID=unnamed {ECO:0000313|EMBL:ACR66326.1};
RX PubMed=20007393; DOI=10.1128/JCM.00765-09;
RA Leinberger D.M., Grimm V., Rubtsova M., Weile J., Schroppel K.,
RA Wichelhaus T.A., Knabbe C., Schmid R.D., Bachmann T.T.;
RT "Integrated detection of extended-spectrum-beta-lactam resistance by DNA
RT microarray-based genotyping of TEM, SHV, and CTX-M genes.";
RL J. Clin. Microbiol. 48:460-471(2010).
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; FJ668817; ACR66326.1; -; Genomic_DNA.
DR RefSeq; WP_002904004.1; NZ_NWES01000098.1.
DR AlphaFoldDB; C5I573; -.
DR SMR; C5I573; -.
DR GeneID; 84667473; -.
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:ACR66326.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..286
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030167435"
FT DOMAIN 45..258
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 286 AA; 31268 MW; 49BF42671C1F5FBD CRC64;
MRYIRLCIIS LLATLPLAVH ASPQPLEQIK QSESQLSGRV GMIEMDLASG RTLTAWRADE
RFPMMSTFKV VLCGAVLARV DAGDEQLERK IHYRQQDLVD YSPVSEKHLA DGMTVGELCA
AAITMSDNSA ANLLLATVGG PAGLTAFLRQ IGDNVTRLDR WETELNEALP GDARDTTTPA
SMAATLRKLL TSQRLSARSQ RQLLQWMVDD RVAGPLIRSV LPAGWFIADK TGASKRGARG
IVALLGPNNK AERIVVIYLR DTPASMAERN QQIAGIGAAL IEHWQR
//
