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
//