CAT4_STAAU
ID CAT4_STAAU Reviewed; 215 AA.
AC P36882;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Chloramphenicol acetyltransferase;
DE Short=CAT;
DE EC=2.3.1.28;
GN Name=cat;
OS Staphylococcus aureus.
OG Plasmid pSCS6.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1517170; DOI=10.1111/j.1365-2672.1992.tb01837.x;
RA Cardoso M., Schwarz S.;
RT "Nucleotide sequence and structural relationships of a chloramphenicol
RT acetyltransferase encoded by the plasmid pSCS6 from Staphylococcus
RT aureus.";
RL J. Appl. Bacteriol. 72:289-293(1992).
RN [2]
RP CHARACTERIZATION.
RX PubMed=1564439; DOI=10.1099/00221287-138-2-275;
RA Cardoso M., Schwarz S.;
RT "Characterization of the chloramphenicol acetyltransferase variants encoded
RT by the plasmids pSCS6 and pSCS7 from Staphylococcus aureus.";
RL J. Gen. Microbiol. 138:275-281(1992).
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; X60827; CAA43218.1; -; Genomic_DNA.
DR RefSeq; WP_032488466.1; NG_047567.1.
DR AlphaFoldDB; P36882; -.
DR SMR; P36882; -.
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 1: Evidence at protein level;
KW Acyltransferase; Antibiotic resistance; Plasmid; Transferase.
FT CHAIN 1..215
FT /note="Chloramphenicol acetyltransferase"
FT /id="PRO_0000165873"
FT ACT_SITE 189
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10021"
SQ SEQUENCE 215 AA; 25692 MW; B481476CD68425E7 CRC64;
MTFNIIKLEN WDRKEYFEHY FNQQTTYSIT KEIDITLFKD MSKKKGYEIY PSLIYAIMEV
VNKNKVFRTG INSENKLGYW DKLNPLYTVF NKQTEKFTNI WTESDNNFTS FYNNYKNDLL
EYKDKEEMFP KKPIPENTLP ISMIPWIDFS SFNLNIGNNS NFLLPIITIG KFYSENNKIY
IPVALQLHHA VCDGYHASLF INEFQDIIKK VDDWI