ID   D3JYW2_KLEPN            Unreviewed;       258 AA.
AC   D3JYW2;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, 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;
OS   Klebsiella pneumoniae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573 {ECO:0000313|EMBL:ADB90405.1};
RN   [1] {ECO:0000313|EMBL:ADB90405.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Iranian 8896 {ECO:0000313|EMBL:ADB90405.1};
RA   Riyahi-Zaniani F., Meshkat Z., Naderi-Nasab M., Khaje-Karamadini M.,
RA   Ghazvini K., Rezaee A., Esmaily H., Nabavinia M.-S., Darban-Hoseini M.;
RT   "Klebsiella pneumoniae TEM-1b beta-lactamase gene, Iranian isolate from a
RT   wound specimen.";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
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; GU338984; ADB90405.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3JYW2; -.
DR   MEROPS; S11.A01; -.
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          34..247
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADB90405.1"
FT   NON_TER         258
FT                   /evidence="ECO:0000313|EMBL:ADB90405.1"
SQ   SEQUENCE   258 AA;  28223 MW;  DDA92E901AAE2669 CRC64;
     AAFCLPVFAH PETLVKVKDA EDQLGARVGY IELDLNSGKI LESFRPEERF PMMSTFKVLL
     CGAVLSRVDA GQEQLGRRIH YSQNDLVEYS PVTEKHLTDG MTVRELCSAA ITMSDNTAAN
     LLLTTIGGPK ELTAFLHNMG DHVTRLDRWE PELNEAIPND ERDTTMPAAM ATTLRKLLTG
     ELLTLASRQQ LIDWMEADKV AGPLLRSALP AGWFIADKSG AGERGSRGII AALGPDGKPS
     RIVVIYTTGS QATMDERN
//