ID   BLO2_ECOLX              Reviewed;         275 AA.
AC   P0A1V9; P05191; Q57015;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Beta-lactamase OXA-2;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
DE   Flags: Precursor;
GN   Name=bla; Synonyms=oxa2;
OS   Escherichia coli.
OG   Plasmid IncN R46.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2821509; DOI=10.1093/nar/15.18.7491;
RA   Hall R.M., Vockler C.;
RT   "The region of the IncN plasmid R46 coding for resistance to beta-lactam
RT   antibiotics, streptomycin/spectinomycin and sulphonamides is closely
RT   related to antibiotic resistance segments found in IncW plasmids and in
RT   Tn21-like transposons.";
RL   Nucleic Acids Res. 15:7491-7501(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1334268; DOI=10.1016/0147-619x(92)90054-e;
RA   Stokes H.W., Hall R.M.;
RT   "The integron In1 in plasmid R46 includes two copies of the oxa2 gene
RT   cassette.";
RL   Plasmid 28:225-234(1992).
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   -!- SIMILARITY: Belongs to the class-D beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; M95287; AAB59082.1; -; Genomic_DNA.
DR   EMBL; M95287; AAB59084.2; -; Genomic_DNA.
DR   RefSeq; WP_001007673.1; NZ_VTMO01000151.1.
DR   RefSeq; YP_006953608.1; NC_019081.1.
DR   AlphaFoldDB; P0A1V9; -.
DR   SMR; P0A1V9; -.
DR   BindingDB; P0A1V9; -.
DR   ChEMBL; CHEMBL1744485; -.
DR   GeneID; 67369352; -.
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..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..275
FT                   /note="Beta-lactamase OXA-2"
FT                   /id="PRO_0000017025"
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;  31686 MW;  D3678DFCB78DE8B6 CRC64;
     MAIRIFAILF SIFSLATFAH AQEGTLERSD WRKFFSEFQA KGTIVVADER QADRAMLVFD
     PVRSKKRYSP ASTFKIPHTL FALDAGAVRD EFQIFRWDGV NRGFAGHNQD QDLRSAMRNS
     TVWVYELFAK EIGDDKARRY LKKIDYGNAD PSTSNGDYWI EGSLAISAQE QIAFLRKLYR
     NELPFRVEHQ RLVKDLMIVE AGRNWILRAK TGWEGRMGWW VGWVEWPTGS VFFALNIDTP
     NRMDDLFKRE AIVRAILRSI EALPPNPAVN SDAAR