ID A8I448_KLEPN Unreviewed; 286 AA.
AC A8I448;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=blaSHV-101 {ECO:0000313|EMBL:ABV72593.1};
OS Klebsiella pneumoniae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573 {ECO:0000313|EMBL:ABV72593.1};
RN [1] {ECO:0000313|EMBL:ABV72593.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RS4225 {ECO:0000313|EMBL:ABV72593.1};
RX PubMed=17804424; DOI=10.1093/jac/dkm319;
RA Brasme L., Nordmann P., Fidel F., Lartigue M.F., Bajolet O., Poirel L.,
RA Forte D., Vernet-Garnier V., Madoux J., Reveil J.C., Alba-Sauviat C.,
RA Baudinat I., Bineau P., Bouquigny-Saison C., Eloy C., Lafaurie C.,
RA Simeon D., Verquin J.P., Noel F., Strady C., De Champs C.;
RT "Incidence of class A extended-spectrum beta-lactamases in Champagne-
RT Ardenne (France): a 1 year prospective study.";
RL J. Antimicrob. Chemother. 60:956-964(2007).
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; EU155018; ABV72593.1; -; Genomic_DNA.
DR RefSeq; WP_063864605.1; NG_049991.1.
DR AlphaFoldDB; A8I448; -.
DR SMR; A8I448; -.
DR MEROPS; S11.A01; -.
DR KEGG; ag:ABV72593; -.
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_5002724122"
FT DOMAIN 45..258
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 286 AA; 31166 MW; 7872D2667DA5416F CRC64;
MRYIRLCIIS LLATLPLAVH ASPQPLEQIK LSESQLSGRV GMIEMDLASG RTLTAWRADE
RFPMMSTFKV VLCGAVLARV DAGDEQLERK IHYRQQDLVD YSPVSEKHLA DGMTVGELCA
AAITMSDNSA ANLLLATVGG PAGLTAFLRQ IGDNVTRLDR WETELNEALP GDARDTTTPA
SMAATLRKLL TSQRLSARSQ RQLLQWMVDG RVAGPLIRSV LPAGWFIADK TGAGERGARG
IVALLGPNNK AERIVVIYLR DTPASMAERN QQIAGIGAAL IEHWQR
//