ID   ATSE_STAAR              Reviewed;         144 AA.
AC   Q6GI30;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Putative acetyltransferase SAR1027 {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=SAR1027;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
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; BX571856; CAG40031.1; -; Genomic_DNA.
DR   RefSeq; WP_000491975.1; NC_002952.2.
DR   AlphaFoldDB; Q6GI30; -.
DR   SMR; Q6GI30; -.
DR   KEGG; sar:SAR1027; -.
DR   HOGENOM; CLU_056607_6_2_9; -.
DR   OMA; PHVEMRK; -.
DR   OrthoDB; 1777515at2; -.
DR   Proteomes; UP000000596; Chromosome.
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 SAR1027"
FT                   /id="PRO_0000201926"
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;  16480 MW;  6C4470B3A5CC068C CRC64;
     MFSKVIDPEM LEDCFYIRKK VFVEEQGVPE ESEIDEYESE SIHLIGYDNG QPVATARIRP
     INETTVKIER VAVIKSHRGQ GMGKMLMQAV ESLAKDEGFY VATMNAQCHA IPFYESLNFK
     MRGNIFLEEG IEHIEMTKKL TSLN