ID   BLO15_PSEAI             Reviewed;         275 AA.
AC   Q51574;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Beta-lactamase OXA-15;
DE            EC=3.5.2.6 {ECO:0000269|PubMed:9087490};
DE   Flags: Precursor;
GN   Name=bla; Synonyms=oxa15;
OS   Pseudomonas aeruginosa.
OG   Plasmid pMLH54.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=AH;
RX   PubMed=9087490; DOI=10.1128/aac.41.4.785;
RA   Danel F., Hall L.M.C., Gur D., Livermore D.M.;
RT   "OXA-15, an extended-spectrum variant of OXA-2 beta-lactamase, isolated
RT   from a Pseudomonas aeruginosa strain.";
RL   Antimicrob. Agents Chemother. 41:785-790(1997).
CC   -!- FUNCTION: Hydrolyzes oxacillin, first-generation cephalosporins and
CC       ceftazidime. Does not hydrolyze cefotaxime or carbapenems.
CC       {ECO:0000269|PubMed:9087490}.
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:0000269|PubMed:9087490};
CC   -!- SIMILARITY: Belongs to the class-D beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; U63835; AAB05874.1; -; Genomic_DNA.
DR   RefSeq; WP_063861048.1; NZ_SDAJ01000170.1.
DR   AlphaFoldDB; Q51574; -.
DR   SMR; Q51574; -.
DR   KEGG; ag:AAB05874; -.
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   1: Evidence at protein level;
KW   Antibiotic resistance; Hydrolase; Plasmid; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..275
FT                   /note="Beta-lactamase OXA-15"
FT                   /id="PRO_0000017032"
FT   ACT_SITE        72
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10103"
FT   BINDING         210..212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         75
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   275 AA;  31628 MW;  D3678DFE678C38B5 CRC64;
     MAIRIFAILF SIFSLATFAH AQEGTLERSD WRKFFSEFQA KGTIVVADER QADRAMLVFD
     PVRSKKRYSP ASTFKIPHTL FALDAGAVRD EFQIFRWDGV NRGFAGHNQD QDLRSAMRNS
     TVWVYELFAK EIGDDKARRY LKKIDYGNAG PSTSNGDYWI EGSLAISAQE QIAFLRKLYR
     NELPFRVEHQ RLVKDLMIVE AGRNWILRAK TGWEGRMGWW VGWVEWPTGS VFFALNIDTP
     NRMDDLFKRE AIVRAILRSI EALPPNPAVN SDAAR