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Database: UniProt
Entry: C0KTA5_ECOLX
LinkDB: C0KTA5_ECOLX
Original site: C0KTA5_ECOLX 
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}.
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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
//
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