ID   BLO5_PSEAI              Reviewed;         267 AA.
AC   Q00982;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Beta-lactamase OXA-5;
DE            EC=3.5.2.6;
DE   Flags: Precursor;
GN   Name=bla; Synonyms=oxa5;
OS   Pseudomonas aeruginosa.
OG   Plasmid pMG54.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=76072601; TRANSPOSON=Tn1406;
RX   PubMed=1495394; DOI=10.1111/j.1365-2958.1992.tb00894.x;
RA   Couture F., Lachapelle J., Levesque R.C.;
RT   "Phylogeny of LCR-1 and OXA-5 with class A and class D beta-lactamases.";
RL   Mol. Microbiol. 6:1693-1705(1992).
CC   -!- FUNCTION: Hydrolyzes both oxacillin and methicillin.
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   -!- ACTIVITY REGULATION: Inhibited by clavulanic acid.
CC   -!- SIMILARITY: Belongs to the class-D beta-lactamase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X58272; CAA41211.1; -; Genomic_DNA.
DR   PIR; S22684; S22684.
DR   RefSeq; WP_032488483.1; NG_049776.1.
DR   AlphaFoldDB; Q00982; -.
DR   SMR; Q00982; -.
DR   KEGG; ag:CAA41211; -.
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.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..267
FT                   /note="Beta-lactamase OXA-5"
FT                   /id="PRO_0000017028"
FT   ACT_SITE        67
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10103"
FT   BINDING         205..207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         70
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   267 AA;  29432 MW;  BAFB61380DB7D536 CRC64;
     MKTIAAYLVL VFYASTALSE SISENLAWNK EFSSESVHGV FVLCKSSSNS CTTNNAARAS
     TAYIPASTFK IPNALIGLET GAIKDERQVF KWDGKPRAMK QWEKDLKLRG AIQVSAVPVF
     QQIAREVGEI RMQKYLNLFS YGNANIGGGI DKFWLEGQLR ISAFNQVKFL ESLYLNNLPA
     SKANQLIVKE AIVTEATPEY IVHSKTGYSG VGTESSPGVA WWVGWVEKGT EVYFFAFNMD
     IDNESKLPSR KSISTKIMAS EGIIIGG