ID Q6ZY54_KLEPN Unreviewed; 263 AA. AC Q6ZY54; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 13-SEP-2023, entry version 69. 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=blaLEN {ECO:0000313|EMBL:CAG25835.1}; OS Klebsiella pneumoniae. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella. OX NCBI_TaxID=573 {ECO:0000313|EMBL:CAG25835.1}; RN [1] {ECO:0000313|EMBL:CAG25835.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UD827:1 {ECO:0000313|EMBL:CAG25835.1}; RX PubMed=15215087; DOI=10.1128/AAC.48.7.2400-2408.2004; RA Haeggman S., Loefdahl S., Paauw A., Verhoef J., Brisse S.; RT "Diversity and evolution of the class A chromosomal beta-lactamase gene in RT Klebsiella pneumoniae."; RL Antimicrob. Agents Chemother. 48:2400-2408(2004). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ635424; CAG25835.1; -; Genomic_DNA. DR AlphaFoldDB; Q6ZY54; -. 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}; Hydrolase {ECO:0000256|RuleBase:RU361140}. FT DOMAIN 33..245 FT /note="Beta-lactamase class A catalytic" FT /evidence="ECO:0000259|Pfam:PF13354" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:CAG25835.1" FT NON_TER 263 FT /evidence="ECO:0000313|EMBL:CAG25835.1" SQ SEQUENCE 263 AA; 28331 MW; 7A71E3F2267930B8 CRC64; ATLPLVVYAG PQPLEQIKQS ESQLPGRVGM VEMDLASGRT LAAWRADERF PMVSTFKVLL CGAVLARVDA GLEQLDRRIH YRQQDLVDYS PVSEKHLVDG MTIGELCAAA ITLSDNSAGN LLLATVGGPA GLTAFLRQIG DNVTHLDRWE TALNEALPGD ARDTTTPASM AATLRKLLTA QHLSARSQQQ LLQWMVDDRV AGPLIRAVLP PGWFIADKTG AGERGARGIV ALLGPDGKPE RIVVIYLRDT PASMAERNQH IAG //