BLO9_KLEPN
ID BLO9_KLEPN Reviewed; 274 AA.
AC P0A3M3; P22070; Q7WWR7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Beta-lactamase OXA-9;
DE EC=3.5.2.6;
DE AltName: Full=Oxacillinase;
DE AltName: Full=Penicillinase;
DE Flags: Precursor;
GN Name=bla; Synonyms=oxa9;
OS Klebsiella pneumoniae.
OG Plasmid pJMCMW1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TRANSPOSON=Tn1331;
RX PubMed=1963948; DOI=10.1016/0147-619x(90)90005-w;
RA Tolmasky M.E.;
RT "Sequencing and expression of aadA, bla, and tnpR from the multiresistance
RT transposon Tn1331.";
RL Plasmid 24:218-226(1990).
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS.
RA Tolmasky M.E.;
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12384346; DOI=10.1128/aac.46.11.3422-3427.2002;
RA Sarno R., McGillivary G., Sherratt D.J., Actis L.A., Tolmasky M.E.;
RT "Complete nucleotide sequence of Klebsiella pneumoniae multiresistance
RT plasmid pJHCMW1.";
RL Antimicrob. Agents Chemother. 46:3422-3427(2002).
RN [4]
RP FUNCTION.
RX PubMed=8382826; DOI=10.1006/plas.1993.1004;
RA Tolmasky M.E., Crosa J.H.;
RT "Genetic organization of antibiotic resistance genes (aac(6')-Ib, aadA, and
RT oxa9) in the multiresistance transposon Tn1331.";
RL Plasmid 29:31-40(1993).
CC -!- FUNCTION: Oxacillin-hydrolyzing beta-lactamase. Confers resistance to
CC beta-lactam antibiotics but at a significantly lower level than the TEM
CC bla gene product. {ECO:0000269|PubMed:8382826}.
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:PRU10103};
CC -!- SIMILARITY: Belongs to the class-D beta-lactamase family.
CC {ECO:0000305}.
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DR EMBL; M55547; AAA98406.2; -; Genomic_DNA.
DR EMBL; AF479774; AAL93143.2; -; Genomic_DNA.
DR PIR; D37392; D37392.
DR RefSeq; NP_608309.2; NC_003486.1.
DR RefSeq; WP_000722315.1; NZ_WWEX01000056.1.
DR RefSeq; YP_007878590.1; NC_021079.1.
DR RefSeq; YP_008603397.1; NC_022520.1.
DR RefSeq; YP_009067787.1; NC_025131.1.
DR RefSeq; YP_009071734.1; NC_025185.1.
DR AlphaFoldDB; P0A3M3; -.
DR SMR; P0A3M3; -.
DR KEGG; ag:AAA98406; -.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR002137; Beta-lactam_class-D_AS.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR PROSITE; PS00337; BETA_LACTAMASE_D; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Hydrolase; Plasmid; Signal; Transposable element.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..274
FT /note="Beta-lactamase OXA-9"
FT /id="PRO_0000017036"
FT ACT_SITE 58
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10103"
FT BINDING 206..208
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 61
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 274 AA; 30568 MW; CA96C211CEFF5F2D CRC64;
MKKILLLHML VFVSATLPIS SVASDEVETL KCTIIADAIT GNTLYETGEC ARRVSPCSSF
KLPLAIMGFD SGILQSPKSP TWELKPEYNP SPRDRTYKQV YPALWQSDSV VWFSQQLTSR
LGVDRFTEYV KKFEYGNQDV SGDSGKHNGL TQSWLMSSLT ISPKEQIQFL LRFVAHKLPV
SEAAYDMAYA TIPQYQAAEG WAVHGKSGSG WLRDNNGKIN ESRPQGWFVG WAEKNGRQVV
FARLEIGKEK SDIPGGSKAR EDILVELPVL MGNK