ID   CAT_BACPU               Reviewed;         220 AA.
AC   P00487;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Chloramphenicol acetyltransferase;
DE            Short=CAT;
DE            EC=2.3.1.28;
DE   AltName: Full=Cat-86;
GN   Name=cat86;
OS   Bacillus pumilus (Bacillus mesentericus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1408;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2414270; DOI=10.1128/jb.164.2.696-703.1985;
RA   Ambulos N.P. Jr., Mongkolsuk S., Kaufman J.D., Lovett P.S.;
RT   "Chloramphenicol-induced translation of cat-86 mRNA requires two cis-acting
RT   regulatory regions.";
RL   J. Bacteriol. 164:696-703(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NBRC 12089 / NCIMB 8600 / CDA 658;
RX   PubMed=6315534; DOI=10.1016/0378-1119(83)90076-8;
RA   Harwood C.R., Williams D.M., Lovett P.S.;
RT   "Nucleotide sequence of a Bacillus pumilus gene specifying chloramphenicol
RT   acetyltransferase.";
RL   Gene 24:163-169(1983).
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; K00544; AAA22289.1; -; Genomic_DNA.
DR   PIR; A00570; XXBSCP.
DR   RefSeq; WP_050945244.1; NZ_PTXV01000001.1.
DR   AlphaFoldDB; P00487; -.
DR   SMR; P00487; -.
DR   PRIDE; P00487; -.
DR   KEGG; ag:AAA22289; -.
DR   PATRIC; fig|1408.90.peg.3135; -.
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; Transferase.
FT   CHAIN           1..220
FT                   /note="Chloramphenicol acetyltransferase"
FT                   /id="PRO_0000165857"
FT   ACT_SITE        187
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10021"
SQ   SEQUENCE   220 AA;  26018 MW;  2F70FDA877C6E90B CRC64;
     MFKQIDENYL RKEHFHHYMT LTRCSYSLVI NLDITKLHAI LKEKKLKVYP VQIYLLARAV
     QKIPEFRMDQ VNDELGYWEI LHPSYTILNK ETKTFSSIWT PFDENFAQFY KSCVADIETF
     SKSSNLFPKP HMPENMFNIS SLPWIDFTSF NLNVSTDEAY LLPIFTIGKF KVEEGKIILP
     VAIQVHHAVC DGYHAGQYVE YLRWLIEHCD EWLNDSLHIT