ID   ATSE_CLOD6              Reviewed;         159 AA.
AC   Q18B70;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Acetyltransferase CD1211 {ECO:0000303|PubMed:23184347};
DE            EC=2.3.1.-;
DE   AltName: Full=GCN5-related N-acetyltransferase {ECO:0000303|PubMed:23184347};
DE            Short=GNAT {ECO:0000303|PubMed:23184347};
GN   OrderedLocusNames=CD630_12110;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
RN   [2]
RP   FUNCTION, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=630;
RX   PubMed=23184347; DOI=10.1002/pro.2199;
RA   Kuhn M.L., Majorek K.A., Minor W., Anderson W.F.;
RT   "Broad-substrate screen as a tool to identify substrates for bacterial
RT   Gcn5-related N-acetyltransferases with unknown substrate specificity.";
RL   Protein Sci. 22:222-230(2013).
CC   -!- FUNCTION: Catalyzes the transfer of an acetyl group from acetyl
CC       coenzyme A (AcCoA) to an acceptor substrate and releases both CoA and
CC       the acetylated product. It prefers L-threonine, L-serine and L-
CC       methionine. It can also use O-acetyl-L-serine, L-tryptophan, L-
CC       isoleucine, L-valine, L-homoserine, 7-aminocephalosporanic acid,
CC       thiamine pyrophosphate and thiamine. {ECO:0000269|PubMed:23184347}.
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DR   EMBL; AM180355; CAJ68065.1; -; Genomic_DNA.
DR   RefSeq; YP_001087704.1; NC_009089.1.
DR   AlphaFoldDB; Q18B70; -.
DR   SMR; Q18B70; -.
DR   STRING; 272563.CD630_12110; -.
DR   EnsemblBacteria; CAJ68065; CAJ68065; CD630_12110.
DR   KEGG; cdf:CD630_12110; -.
DR   PATRIC; fig|272563.8.peg.1270; -.
DR   eggNOG; COG0456; Bacteria.
DR   OMA; GCCALRP; -.
DR   PhylomeDB; Q18B70; -.
DR   BioCyc; PDIF272563:G12WB-1342-MON; -.
DR   Proteomes; UP000001978; Chromosome.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:UniProtKB.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   4: Predicted;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..159
FT                   /note="Acetyltransferase CD1211"
FT                   /id="PRO_0000433352"
FT   DOMAIN          5..159
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   BINDING         87..89
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I0Q8"
FT   BINDING         95
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I0Q8"
FT   BINDING         131..133
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I0Q8"
SQ   SEQUENCE   159 AA;  18435 MW;  A7C16B926A518792 CRC64;
     MAQNITLQFV EEKDLENLEN VKLLFTEYSN SLNIDLCFQD FNNELKTLPG KYKKPSGSLI
     LAFVDENLAG CVALKKLEGK ICELKRLYVR NQFRGLKIGK ILLEEIIEEA KKFGYTHMRL
     DTLPSMKSAQ GLYEKFGFYD IEPYTYNPIE GARYMELKL