ID   BLO9_KLEAE              Reviewed;         274 AA.
AC   P0A3M4; P22070;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   03-AUG-2022, entry version 61.
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 aerogenes (Enterobacter aerogenes).
OG   Plasmid pIP833.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=548;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BM2688-1; TRANSPOSON=In40;
RX   PubMed=9756755; DOI=10.1128/aac.42.10.2557;
RA   Ploy M.-C., Courvalin P., Lambert T.;
RT   "Characterization of In40 of Enterobacter aerogenes BM2688, a class 1
RT   integron with two new gene cassettes, cmlA2 and qacF.";
RL   Antimicrob. Agents Chemother. 42:2557-2563(1998).
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.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD22145.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF034958; AAD22145.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000722315.1; NZ_WFLR01000100.1.
DR   AlphaFoldDB; P0A3M4; -.
DR   SMR; P0A3M4; -.
DR   ChEMBL; CHEMBL1744486; -.
DR   PATRIC; fig|548.60.peg.3688; -.
DR   SABIO-RK; P0A3M4; -.
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_0000017035"
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