ID   CAT5_STAAU              Reviewed;         209 AA.
AC   P36883;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Chloramphenicol acetyltransferase;
DE            Short=CAT;
DE            EC=2.3.1.28;
OS   Staphylococcus aureus.
OG   Plasmid pSCS7.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=436;
RX   PubMed=1929326; DOI=10.1128/aac.35.8.1551;
RA   Schwarz S., Cardoso M.;
RT   "Nucleotide sequence and phylogeny of a chloramphenicol acetyltransferase
RT   encoded by the plasmid pSCS7 from Staphylococcus aureus.";
RL   Antimicrob. Agents Chemother. 35:1551-1556(1991).
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   -!- SIMILARITY: Belongs to the chloramphenicol acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; M58516; AAA16529.1; -; Unassigned_DNA.
DR   PIR; A61152; A61152.
DR   RefSeq; WP_063843210.1; NG_047571.1.
DR   AlphaFoldDB; P36883; -.
DR   SMR; P36883; -.
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   3: Inferred from homology;
KW   Acyltransferase; Antibiotic resistance; Plasmid; Transferase.
FT   CHAIN           1..209
FT                   /note="Chloramphenicol acetyltransferase"
FT                   /id="PRO_0000165874"
FT   ACT_SITE        189
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10021"
SQ   SEQUENCE   209 AA;  24746 MW;  FA7AB26572AD7EC0 CRC64;
     MTFNIINLET WDRKEYFNHY FNQQTTYSVT KELDITLLKS MIKNKGYELY PALIHAIVSV
     INRNKVFRTG INSEGNLGYW DKLEPLYTVF NKETENFSNI WTESNASFTL FYNSYKNDLI
     KYKDKNEMFP KKPIPENTVP ISMIPWIDFS SFNLNIGNNS RFLLPIITIG KFYSKDDKIY
     LPFPLQVHHA VCDGYHVSLF MNEFQNIIR