ID   CAT1_STAAU              Reviewed;         216 AA.
AC   P00485;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Chloramphenicol acetyltransferase;
DE            Short=CAT;
DE            EC=2.3.1.28;
GN   Name=cat;
OS   Staphylococcus aureus.
OG   Plasmid pC194, and Plasmid pCB64.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pC194;
RX   PubMed=6950931; DOI=10.1128/jb.150.2.815-825.1982;
RA   Horinouchi S., Weisblum B.;
RT   "Nucleotide sequence and functional map of pC194, a plasmid that specifies
RT   inducible chloramphenicol resistance.";
RL   J. Bacteriol. 150:815-825(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pC194;
RX   PubMed=6202672; DOI=10.1128/jb.158.2.543-550.1984;
RA   Byeon W.-H., Weisblum B.;
RT   "Post-transcriptional regulation of chloramphenicol acetyl transferase.";
RL   J. Bacteriol. 158:543-550(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pCB64;
RX   PubMed=2326208; DOI=10.1093/nar/18.6.1651;
RA   Minton N.P., Swinfield T.-J., Brehm J.K., Oultram J.D.;
RT   "The Gram-positive cloning vector pBD64 arose by a 1844 bp deletion of
RT   pC194 derived DNA.";
RL   Nucleic Acids Res. 18:1651-1651(1990).
CC   -!- FUNCTION: This enzyme is an effector of chloramphenicol resistance in
CC       bacteria.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + chloramphenicol = chloramphenicol 3-acetate +
CC         CoA; Xref=Rhea:RHEA:18421, ChEBI:CHEBI:16730, ChEBI:CHEBI:17698,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.28;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10021};
CC   -!- SUBUNIT: Homotrimer.
CC   -!- INDUCTION: By subinhibitory concentrations of chloramphenicol.
CC   -!- SIMILARITY: Belongs to the chloramphenicol acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; V01277; CAA24586.1; -; Genomic_DNA.
DR   EMBL; K01998; AAA92251.1; -; Genomic_DNA.
DR   EMBL; X51450; CAA35816.1; -; Other_DNA.
DR   PIR; A00568; XXSACC.
DR   RefSeq; NP_040437.1; NC_002013.1.
DR   RefSeq; WP_001010387.1; NG_047564.1.
DR   RefSeq; YP_001718362.1; NC_010426.1.
DR   RefSeq; YP_001718364.1; NC_010427.1.
DR   RefSeq; YP_006937524.1; NC_013314.1.
DR   RefSeq; YP_006958103.1; NC_019140.1.
DR   AlphaFoldDB; P00485; -.
DR   SMR; P00485; -.
DR   KEGG; ag:CAA24586; -.
DR   GO; GO:0008811; F:chloramphenicol O-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 1.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR018372; Chloramphenicol_AcTrfase_AS.
DR   InterPro; IPR001707; Cmp_AcTrfase.
DR   PANTHER; PTHR38474; PTHR38474; 1.
DR   Pfam; PF00302; CAT; 1.
DR   PIRSF; PIRSF000440; CAT; 1.
DR   SMART; SM01059; CAT; 1.
DR   PROSITE; PS00100; CAT; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Antibiotic resistance; Plasmid; Transferase.
FT   CHAIN           1..216
FT                   /note="Chloramphenicol acetyltransferase"
FT                   /id="PRO_0000165870"
FT   ACT_SITE        189
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10021"
SQ   SEQUENCE   216 AA;  25039 MW;  02FCC398ACBB7C9D CRC64;
     MNFNKIDLDN WKRKEIFNHY LNQQTTFSIT TEIDISVLYR NIKQEGYKFY PAFIFLVTRV
     INSNTAFRTG YNSDGELGYW DKLEPLYTIF DGVSKTFSGI WTPVKNDFKE FYDLYLSDVE
     KYNGSGKLFP KTPIPENAFS LSIIPWTSFT GFNLNINNNS NYLLPIITAG KFINKGNSIY
     LPLSLQVHHS VCDGYHAGLF MNSIQELSDR PNDWLL