ID C0KTA5_ECOLX Unreviewed; 284 AA.
AC C0KTA5;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
DE Flags: Fragment;
GN Name=blaKPC {ECO:0000313|EMBL:ACM91559.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ACM91559.1};
RN [1] {ECO:0000313|EMBL:ACM91559.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P3000136 {ECO:0000313|EMBL:ACM91559.1};
RX PubMed=22964247; DOI=10.1128/AAC.01156-12;
RA Hidalgo-Grass C., Warburg G., Temper V., Benenson S., Moses A.E., Block C.,
RA Strahilevitz J.;
RT "KPC-9, a Novel Carbapenemase from Clinical Specimens in Israel.";
RL Antimicrob. Agents Chemother. 56:6057-6059(2012).
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 -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009}.
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; FJ624872; ACM91559.1; -; Genomic_DNA.
DR AlphaFoldDB; C0KTA5; -.
DR SMR; C0KTA5; -.
DR KEGG; ag:ACM91559; -.
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 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.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..284
FT /note="beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002899805"
FT DOMAIN 40..258
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACM91559.1"
FT NON_TER 284
FT /evidence="ECO:0000313|EMBL:ACM91559.1"
SQ SEQUENCE 284 AA; 30064 MW; 497B57A72C962B37 CRC64;
RLVLLSCLSW PLAGFSATAL TNLVAEPFAK LEQDFGGSIG VYAMDTGSGA TVSYRAEERF
PLCSSFKGFL AAAVLARSQQ QAGLLDTPIR YGKNALVPWS PISEKYLTTG MTVAELSAAA
VQYSDNAAAN LLLKELGGPA GLTAFMRSIG DTTFRLDRWE LELNSAIPGD ARDTSSPRAV
TESLQKLTLG SALAAPQRQQ FVDWLKGNTT GNHRIRAAVP ADWAVGDKTG TCGAYGTAND
YAVVWPTGRA PIVLAVYTRA PNKDDKYSEA VIAAAARLAL EGLG
//