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Database: UniProt
Entry: D0EK08_KLEPN
LinkDB: D0EK08_KLEPN
Original site: D0EK08_KLEPN 
ID   D0EK08_KLEPN            Unreviewed;       138 AA.
AC   D0EK08;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   08-NOV-2023, entry version 45.
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};
DE   Flags: Fragment;
GN   Name=blaCTX-M-15 {ECO:0000313|EMBL:ACW83067.1};
OS   Klebsiella pneumoniae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573 {ECO:0000313|EMBL:ACW83067.1};
RN   [1] {ECO:0000313|EMBL:ACW83067.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HVH-kp33 {ECO:0000313|EMBL:ACW83067.1};
RX   PubMed=20392607; DOI=10.1016/j.ijantimicag.2010.03.005;
RA   Coelho A., Gonzalez-Lopez J.J., Miro E., Alonso-Tarres C., Mirelis B.,
RA   Larrosa M.N., Bartolome R.M., Andreu A., Navarro F., Johnson J.R.,
RA   Prats G.;
RT   "Characterisation of the CTX-M-15-encoding gene in Klebsiella pneumoniae
RT   strains from the Barcelona metropolitan area: plasmid diversity and
RT   chromosomal integration.";
RL   Int. J. Antimicrob. Agents 36:73-78(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; GQ845086; ACW83067.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0EK08; -.
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; D-ALANYL-D-ALANINE ENDOPEPTIDASE; 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..138
FT                   /note="Beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003007677"
FT   DOMAIN          50..137
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
FT   NON_TER         138
FT                   /evidence="ECO:0000313|EMBL:ACW83067.1"
SQ   SEQUENCE   138 AA;  14990 MW;  E01FC418A0A43F2E CRC64;
     MVKKSLRQFT LMATATVTLL LGSVPLYAQT ADVQQKLAEL ERQSGGRLGV ALINTADNSQ
     ILYRADERFA MCSTSKVMAA AAVLKKSESE PNLLNQRVEI KKSDLVNYNP IAEKHVNGTM
     SLAELSAAAL QYSDNVAM
//
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