ID Q9L8E2_KLEPN Unreviewed; 286 AA.
AC Q9L8E2;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 105.
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};
GN Name=shv-25 {ECO:0000313|EMBL:AAF37209.2};
GN Synonyms=blaSHV {ECO:0000313|EMBL:ACY68238.1};
OS Klebsiella pneumoniae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573 {ECO:0000313|EMBL:AAF37209.2};
RN [1] {ECO:0000313|EMBL:AAF37209.2}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11502506; DOI=10.1128/AAC.45.9.2407-2413.2001;
RA Chang F.Y., Siu L.K., Fung C.P., Huang M.H., Ho M.;
RT "Diversity of SHV and TEM beta-lactamases in Klebsiella pneumoniae: gene
RT evolution in Northern Taiwan and two novel beta-lactamases, SHV-25 and SHV-
RT 26.";
RL Antimicrob. Agents Chemother. 45:2407-2413(2001).
RN [2] {ECO:0000313|EMBL:ACY68238.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HB 31 {ECO:0000313|EMBL:ACY68238.1};
RA Tolentino F.M., Polotto M., Remeli G.A., Nogueira M.L., Nogueira M.C.L.;
RT "Diversity of TEM-, SHV-, and CTX-M- type beta-lactamases present in
RT clinical isolates of Klebsiella pneumoniae from a Brazilian hospital.";
RL Submitted (OCT-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; AF208796; AAF37209.2; -; Genomic_DNA.
DR EMBL; GU064391; ACY68238.1; -; Genomic_DNA.
DR RefSeq; WP_063864671.1; NZ_UJSK01000001.1.
DR AlphaFoldDB; Q9L8E2; -.
DR SMR; Q9L8E2; -.
DR MEROPS; S11.A01; -.
DR KEGG; ag:AAF37209; -.
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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..286
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014312979"
FT DOMAIN 45..258
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 286 AA; 31177 MW; E6B797EF2B682B7E CRC64;
MRYIRLCIIS LLAALPLAVH ASPQPLEQIK QSESQLSGRV GMIEMDLASG RTLTAWRADE
RFPMMSTFKV VLCGAVLARV DAGDEQLERK IHYRQQDLVD YSPVSEKHLA DGMTVGELCA
AAITVSDNSA ANLLLATVGG PAGLTAFLRQ IGDNVTRLDR WETELNEALP GDARDTTTPA
SMAATLRKLL TSQRLSARSQ RQLLQWMVDD RVAGPLIRSV LPAGWFIADK TGAGERGARG
IVALLGPNNK AERIVVIYLR DTPASMAERN QQIAGIGAAL IEHWQR
//
