ID BLA29_KLEPN Reviewed; 286 AA.
AC Q9AHN9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Beta-lactamase SHV-29;
DE EC=3.5.2.6;
DE Flags: Precursor;
GN Name=bla; Synonyms=shv29;
OS Klebsiella pneumoniae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1534;
RX PubMed=11257029; DOI=10.1128/aac.45.4.1151-1161.2001;
RA Yigit H., Queenan A.M., Anderson G.J., Domenech-Sanchez A., Biddle J.W.,
RA Steward C.D., Alberti S., Bush K., Tenover F.C.;
RT "Novel carbapenem-hydrolyzing beta-lactamase, KPC-1, from a carbapenem-
RT resistant strain of Klebsiella pneumoniae.";
RL Antimicrob. Agents Chemother. 45:1151-1161(2001).
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10101};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000305}.
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DR EMBL; AF301532; AAG49894.1; -; Genomic_DNA.
DR RefSeq; WP_063864672.1; NG_050066.1.
DR AlphaFoldDB; Q9AHN9; -.
DR SMR; Q9AHN9; -.
DR KEGG; ag:AAG49894; -.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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; Disulfide bond; Hydrolase; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..286
FT /note="Beta-lactamase SHV-29"
FT /id="PRO_0000349141"
FT ACT_SITE 66
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 230..232
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 73..119
FT /evidence="ECO:0000250"
SQ SEQUENCE 286 AA; 31184 MW; 8EBF426D13FF5502 CRC64;
MRYIRLCIIS LLATLPLAVH ASPQPLEQIK QSESQLSGSV GMIEMDLASG RTLTAWRADE
RFPMMSTFKV VLCGAVLARV DAGDEQLERK IHYRQQDLVD YSPVSEKHLA DGMTVGELCA
AAITMSDNSA ANLLLATVGG PAGLTAFLRQ IGDNVTRLDR WETELNEALP GDARDTTTPA
SMAATLRKLL TSQRLSARSQ RQLLQWMVDD RVAGPLIRSV LPAGWFIADK TGAAERGARG
IVALLGPNNK AERIVVIYLR DTPASMAERN QQIAGIGAAL IEHWQR
//
