ID D3YMB3_KLEPN Unreviewed; 102 AA.
AC D3YMB3;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
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;
OS Klebsiella pneumoniae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573 {ECO:0000313|EMBL:ADD37848.1};
RN [1] {ECO:0000313|EMBL:ADD37848.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SHNKP {ECO:0000313|EMBL:ADD37848.1};
RX PubMed=21860105; DOI=10.4103/0255-0857.83908;
RA Nematzadeh S., Shahcheraghi F., Feizabadi M.M., Nikbin V.S., Nasehi L.;
RT "Molecular characterization of CTX-M?-lactamases among Klebsiella
RT pneumoniae isolated from patients at Tehran hospitals.";
RL Indian J Med Microbiol 29:254-257(2011).
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; GU585367; ADD37848.1; -; Genomic_DNA.
DR AlphaFoldDB; D3YMB3; -.
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}.
FT DOMAIN 2..100
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADD37848.1"
FT NON_TER 102
FT /evidence="ECO:0000313|EMBL:ADD37848.1"
SQ SEQUENCE 102 AA; 11053 MW; D126B151DAFFBA46 CRC64;
RFAMCSTSKV MAAAAVLKKS ESEPNLLNQR VEIKKSDLVN YNPIAEKHVN GTMSLAELSA
AALQYSDNVA MNKLIAHVGG PASVTAFARQ LGDETFRLDR TE
//