ID   ATSE_STAAN              Reviewed;         144 AA.
AC   P0A0M7; P52080;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Putative acetyltransferase SA0906 {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=SA0906;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000018; BAB42151.1; -; Genomic_DNA.
DR   PIR; D89874; D89874.
DR   RefSeq; WP_000491986.1; NC_002745.2.
DR   AlphaFoldDB; P0A0M7; -.
DR   SMR; P0A0M7; -.
DR   EnsemblBacteria; BAB42151; BAB42151; BAB42151.
DR   KEGG; sau:SA0906; -.
DR   HOGENOM; CLU_056607_6_2_9; -.
DR   OMA; PHVEMRK; -.
DR   Proteomes; UP000000751; 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 SA0906"
FT                   /id="PRO_0000201925"
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