ID   BLO18_PSEAI             Reviewed;         275 AA.
AC   O07293;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-MAY-2023, entry version 84.
DE   RecName: Full=Beta-lactamase OXA-18 {ECO:0000303|PubMed:9333046};
DE            EC=3.5.2.6 {ECO:0000269|PubMed:9333046};
DE   AltName: Full=Penicillinase {ECO:0000305};
DE   Flags: Precursor;
GN   Name=bla {ECO:0000303|PubMed:9333046}; Synonyms=oxa18;
OS   Pseudomonas aeruginosa.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   ACTIVITY REGULATION.
RC   STRAIN=Mus;
RX   PubMed=9333046; DOI=10.1128/aac.41.10.2188;
RA   Philippon L.N., Naas T., Bouthors A.T., Barakett V., Nordmann P.;
RT   "OXA-18, a class D clavulanic acid-inhibited extended-spectrum beta-
RT   lactamase from Pseudomonas aeruginosa.";
RL   Antimicrob. Agents Chemother. 41:2188-2195(1997).
CC   -!- FUNCTION: Has a broad substrate profile, hydrolyzes amoxicillin,
CC       ticarcillin, cephalothin, ceftazidime, cefotaxime, and aztreonam, but
CC       not imipenem or cephamycins. {ECO:0000269|PubMed:9333046}.
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:9333046};
CC   -!- ACTIVITY REGULATION: Inhibited by clavulanic acid, sulbactam,
CC       tazobactam, and imipenem. {ECO:0000269|PubMed:9333046}.
CC   -!- SIMILARITY: Belongs to the class-D beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; U85514; AAB58555.1; -; Genomic_DNA.
DR   RefSeq; WP_063861237.1; NG_049480.1.
DR   AlphaFoldDB; O07293; -.
DR   SMR; O07293; -.
DR   KEGG; ag:AAB58555; -.
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   1: Evidence at protein level;
KW   Antibiotic resistance; Hydrolase; Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..275
FT                   /note="Beta-lactamase OXA-18"
FT                   /id="PRO_0000017033"
FT   ACT_SITE        65
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         68
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000250|UniProtKB:P13661"
SQ   SEQUENCE   275 AA;  30602 MW;  7D3B71C3ABCE411A CRC64;
     MQRSLSMSGK RHFIFAVSFV ISTVCLTFSP ANAAQKLSCT LVIDEASGDL LHREGSCDKA
     FAPMSTFKLP LAIMGYDADI LLDATTPRWD YKPEFNGYKS QQKPTDPTIW LKDSIVWYSQ
     ELTRRLGESR FSDYVQRFDY GNKDVSGDPG KHNGLTHAWL ASSLKISPEE QVRFLRRFLR
     GELPVSEDAL EMTKAVVPHF EAGDWDVQGK TGTGSLSDAK GGKAPIGWFI GWATRDDRRV
     VFARLTVGAR KGEQPAGPAA RDEFLNTLPA LSENF
//