ID   BLO20_PSEAI             Reviewed;         266 AA.
AC   O84955;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-MAY-2023, entry version 84.
DE   RecName: Full=Beta-lactamase OXA-20;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
DE   Flags: Precursor;
GN   Name=bla; Synonyms=oxa20;
OS   Pseudomonas aeruginosa.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Mus;
RX   PubMed=9687410; DOI=10.1128/aac.42.8.2074;
RA   Naas T., Sougakoff W., Casetta A., Nordmann P.;
RT   "Molecular characterization of OXA-20, a novel class D beta-lactamase, and
RT   its integron from Pseudomonas aeruginosa.";
RL   Antimicrob. Agents Chemother. 42:2074-2083(1998).
CC   -!- FUNCTION: This is an oxacillin-hydrolyzing beta-lactamase.
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}.
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DR   EMBL; AF024602; AAC23554.1; -; Genomic_DNA.
DR   RefSeq; WP_000586782.1; NG_049497.1.
DR   AlphaFoldDB; O84955; -.
DR   SMR; O84955; -.
DR   KEGG; ag:AAC23554; -.
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; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR002137; Beta-lactam_class-D_AS.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   PANTHER; PTHR30627:SF6; BETA-LACTAMASE YBXI-RELATED; 1.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS00337; BETA_LACTAMASE_D; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Hydrolase; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..266
FT                   /note="Beta-lactamase OXA-20"
FT                   /id="PRO_0000017034"
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   266 AA;  30449 MW;  8E7270EA924F2FB9 CRC64;
     MIIRFLALLF SAVVLVSLGH AQEKTHESSN WGKYFSDFNA KGTIVVVDER TNGNSTSVYN
     ESRAQQRYSP ASTFKIPHTL FALDAGAVRD EFHVFRWDGA KRSFAGHNQD QNLRSAMRNS
     TVWVYQLFAK EIGENKARSY LEKLNYGNAD PSTKSGDYWI DGNLAISANE QISILKKLYR
     NELPFRVEHQ RLVKDLMIVE AKRDWILRAK TGWDGQMGWW VGWVEWPTGP VFFALNIDTP
     NRMEDLHKRE AIARAILQSV NALPPN
//