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Database: UniProt
Entry: A8I448_KLEPN
LinkDB: A8I448_KLEPN
Original site: A8I448_KLEPN 
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
//
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