ID O53043_KLEPN Unreviewed; 286 AA.
AC O53043;
DT 01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JUN-1998, sequence version 1.
DT 27-MAR-2024, entry version 92.
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=bla TEM-48 {ECO:0000313|EMBL:CAA71323.1};
OS Klebsiella pneumoniae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573 {ECO:0000313|EMBL:CAA71323.1};
RN [1] {ECO:0000313|EMBL:CAA71323.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CLSiS L-491 {ECO:0000313|EMBL:CAA71323.1};
RX PubMed=9517925;
RA Gniadkowski M., Schneider I., Jungwirth R., Hryniewicz W., Bauernfeind A.;
RT "Ceftazidime-resistant Enterobacteriaceae isolates from three Polish
RT hospitals: identification of three novel TEM- and SHV-5-type extended-
RT spectrum beta-lactamases.";
RL Antimicrob. Agents Chemother. 42:514-520(1998).
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; Y10280; CAA71323.1; -; Genomic_DNA.
DR RefSeq; WP_063864915.1; NG_050270.1.
DR AlphaFoldDB; O53043; -.
DR MEROPS; S11.A01; -.
DR KEGG; ag:CAA71323; -.
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..286
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004159669"
FT DOMAIN 48..260
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 286 AA; 31608 MW; 06BFA3BE6864534E CRC64;
MSIQHFRVAL IPFFAAFCFP VFAHPETLVK VKDAEDQLGA RVGYIELDLN SGKILESFRP
EERFPMMSTF KVLLCGAVLS RVDAGQEQLG RRIHYSQNDL VEYSPVTEKH LTDGMTVREL
CSAAITMSDN TAANLLLTTI GGPKELTAFL HNMGDHVTRL DRWEPELNEA IPNDERDTTM
PAAMATTLRK LLTGELLTLA SRQQLIDWME ADKVAGPLLR SALPAGWFIA DKSGASKRGS
RGIIAALGPD GKPSRIVVIY MTGSQATMDE RNRQIAEIGA SLIKHW
//