ID   BLO7_ECOLX              Reviewed;         266 AA.
AC   P35695;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-MAY-2023, entry version 85.
DE   RecName: Full=Beta-lactamase OXA-7;
DE            EC=3.5.2.6;
DE   Flags: Precursor;
GN   Name=bla; Synonyms=oxa7;
OS   Escherichia coli.
OG   Plasmid pMG202.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=7181;
RX   PubMed=7574536; DOI=10.1128/aac.39.6.1379;
RA   Scoulica E., Aransay A., Tselentis Y.;
RT   "Molecular characterization of the OXA-7 beta-lactamase gene.";
RL   Antimicrob. Agents Chemother. 39:1379-1382(1995).
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; X75562; CAA53242.1; -; Genomic_DNA.
DR   PIR; S38503; S38503.
DR   PIR; S38671; S38671.
DR   RefSeq; WP_063864530.1; NG_049810.1.
DR   AlphaFoldDB; P35695; -.
DR   SMR; P35695; -.
DR   ChEMBL; CHEMBL1255135; -.
DR   KEGG; ag:CAA53242; -.
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; Plasmid; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..266
FT                   /note="Beta-lactamase OXA-7"
FT                   /id="PRO_0000017029"
FT   ACT_SITE        68
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10103"
FT   BINDING         205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         71
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   266 AA;  29461 MW;  77531E35389DB866 CRC64;
     MKTFAAYVIT ACLSSTALAS SITENTFWNK EFSAEAVNGV FVLCKSSSKL ACATNNLARA
     SKEYLPASTF KIPNAIIGLE TGVIKNEHQI FKWDGKPRAM KQWERDLSLR GAIQVSAVPV
     FQQIAREVGE VRMQKYLKKF SYGNQNISGG IDKFWLEGQL RISAVNQVEF LESLFLNKLS
     ASKENQLIVK EALVTEAPEY LVHSKTGFSG VGTESNPGVA WWVGWVEKGA EVYFFAFNMD
     IDNENKLPLR KSIPTKIMAS EGIIGG
//