ID   ATSE_STAAS              Reviewed;         144 AA.
AC   Q6GAF9;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Putative acetyltransferase SAS0989 {ECO:0000250|UniProtKB:Q5HH30};
DE            EC=2.3.1.-;
DE   AltName: Full=GCN5-related N-acetyltransferase {ECO:0000250|UniProtKB:Q5HH30};
DE            Short=GNAT {ECO:0000250|UniProtKB:Q5HH30};
GN   OrderedLocusNames=SAS0989;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Could catalyze the transfer of an acetyl group from acetyl
CC       coenzyme A (AcCoA) to an acceptor substrate and release both CoA and
CC       the acetylated product. {ECO:0000250|UniProtKB:Q5HH30}.
CC   -!- SIMILARITY: Belongs to the UPF0039 (ElaA) family. {ECO:0000305}.
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DR   EMBL; BX571857; CAG42764.1; -; Genomic_DNA.
DR   RefSeq; WP_000491986.1; NC_002953.3.
DR   AlphaFoldDB; Q6GAF9; -.
DR   SMR; Q6GAF9; -.
DR   KEGG; sas:SAS0989; -.
DR   HOGENOM; CLU_056607_6_2_9; -.
DR   OMA; PHVEMRK; -.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; ISS:UniProtKB.
DR   GO; GO:0004343; F:glucosamine 6-phosphate N-acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:InterPro.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR039143; GNPNAT1.
DR   PANTHER; PTHR13355; PTHR13355; 1.
DR   Pfam; PF13673; Acetyltransf_10; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Transferase.
FT   CHAIN           1..144
FT                   /note="Putative acetyltransferase SAS0989"
FT                   /id="PRO_0000201927"
FT   DOMAIN          1..141
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   BINDING         71..73
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I0Q8"
FT   BINDING         79
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I0Q8"
FT   BINDING         112..114
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I0Q8"
SQ   SEQUENCE   144 AA;  16556 MW;  E1273A514803B71B CRC64;
     MFSKVNNQKM LEDCFYIRKK VFVEEQGVPE ESEIDEYESE SIHLIGYDNG QPVATARIRP
     INETTVKIER VAVMKSHRGQ GMGRMLMQAV ESLAKDEGFY VATMNAQCHA IPFYESLNFK
     MRGNIFLEEG IEHIEMTKKL TSLN