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CAT2_STAAU
ID   CAT2_STAAU              Reviewed;         215 AA.
AC   P00486;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Chloramphenicol acetyltransferase;
DE            Short=CAT;
DE            EC=2.3.1.28;
GN   Name=cat;
OS   Staphylococcus aureus.
OG   Plasmid pC221, and Plasmid pTZ12.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pC221;
RX   PubMed=3855295; DOI=10.1016/0014-5793(85)80200-3;
RA   Shaw W.V., Brenner D.G., Legrice S.F.J., Skinner S.E., Hawkins A.R.;
RT   "Chloramphenicol acetyltransferase gene of staphylococcal plasmid pC221.
RT   Nucleotide sequence analysis and expression studies.";
RL   FEBS Lett. 179:101-106(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pC221;
RX   PubMed=3860383; DOI=10.1002/j.1460-2075.1985.tb03665.x;
RA   Brenner D.G., Shaw W.V.;
RT   "The use of synthetic oligonucleotides with universal templates for rapid
RT   DNA sequencing: results with staphylococcal replicon pC221.";
RL   EMBO J. 4:561-568(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pC221;
RX   PubMed=2993795; DOI=10.1007/bf00330758;
RA   Projan S.J., Kornblum J., Moghazeh S.L., Edelman I., Gennaro M.L.,
RA   Novick R.P.;
RT   "Comparative sequence and functional analysis of pT181 and pC221, cognate
RT   plasmid replicons from Staphylococcus aureus.";
RL   Mol. Gen. Genet. 199:452-464(1985).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pTZ12;
RX   PubMed=3110008; DOI=10.1016/0378-1119(87)90481-1;
RA   Aoki T., Noguchi N., Sasatsu M., Kono M.;
RT   "Complete nucleotide sequence of pTZ12, a chloramphenicol-resistance
RT   plasmid of Bacillus subtilis.";
RL   Gene 51:107-111(1987).
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; M16192; AAA72572.1; -; Genomic_DNA.
DR   EMBL; X02166; CAA26105.1; -; Genomic_DNA.
DR   EMBL; X02529; CAA26367.1; -; Genomic_DNA.
DR   PIR; A00569; XXSAC2.
DR   RefSeq; NP_052694.1; NC_002129.1.
DR   RefSeq; WP_002489529.1; NZ_WKHL01000027.1.
DR   RefSeq; YP_001595586.1; NC_010111.1.
DR   RefSeq; YP_232727.1; NC_006977.1.
DR   AlphaFoldDB; P00486; -.
DR   SMR; P00486; -.
DR   PRIDE; P00486; -.
DR   KEGG; ag:CAA26367; -.
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..215
FT                   /note="Chloramphenicol acetyltransferase"
FT                   /id="PRO_0000165871"
FT   ACT_SITE        189
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10021"
SQ   SEQUENCE   215 AA;  25745 MW;  04268B1D0406E572 CRC64;
     MTFNIIKLEN WDRKEYFEHY FNQQTTYSIT KEIDITLFKD MIKKKGYEIY PSLIYAIMEV
     VNKNKVFRTG INSENKLGYW DKLNPLYTVF NKQTEKFTNI WTESDNNFTS FYNNYKNDLL
     EYKDKEEMFP KKPIPENTIP ISMIPWIDFS SFNLNIGNNS NFLLPIITIG KFYSENNKIY
     IPVALQLHHA VCDGYHASLF MNEFQDIIHK VDDWI
 
 
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