ID   ATSE_STAAC              Reviewed;         144 AA.
AC   Q5HH30;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Acetyltransferase SACOL1063 {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=SACOL1063;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
RN   [2]
RP   FUNCTION, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=COL;
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 displays the highest activity for L-
CC       threonine. It can also use L-tryptophan, and to a much lesser extent L-
CC       tyrosine. {ECO:0000269|PubMed:23184347}.
CC   -!- SIMILARITY: Belongs to the UPF0039 (ElaA) family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000046; AAW36527.1; -; Genomic_DNA.
DR   RefSeq; WP_000491986.1; NC_002951.2.
DR   PDB; 5JPH; X-ray; 1.46 A; A/B/C=1-141.
DR   PDB; 5JQ4; X-ray; 1.80 A; A/B=1-143.
DR   PDBsum; 5JPH; -.
DR   PDBsum; 5JQ4; -.
DR   AlphaFoldDB; Q5HH30; -.
DR   SMR; Q5HH30; -.
DR   EnsemblBacteria; AAW36527; AAW36527; SACOL1063.
DR   KEGG; sac:SACOL1063; -.
DR   HOGENOM; CLU_056607_6_2_9; -.
DR   OMA; PHVEMRK; -.
DR   Proteomes; UP000000530; Chromosome.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA: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   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Transferase.
FT   CHAIN           1..144
FT                   /note="Acetyltransferase SACOL1063"
FT                   /id="PRO_0000201923"
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"
FT   STRAND          2..4
FT                   /evidence="ECO:0007829|PDB:5JPH"
FT   HELIX           8..22
FT                   /evidence="ECO:0007829|PDB:5JPH"
FT   TURN            23..26
FT                   /evidence="ECO:0007829|PDB:5JPH"
FT   HELIX           30..33
FT                   /evidence="ECO:0007829|PDB:5JPH"
FT   TURN            36..40
FT                   /evidence="ECO:0007829|PDB:5JPH"
FT   STRAND          41..48
FT                   /evidence="ECO:0007829|PDB:5JPH"
FT   STRAND          51..60
FT                   /evidence="ECO:0007829|PDB:5JPH"
FT   STRAND          62..73
FT                   /evidence="ECO:0007829|PDB:5JPH"
FT   HELIX           75..77
FT                   /evidence="ECO:0007829|PDB:5JPH"
FT   HELIX           82..96
FT                   /evidence="ECO:0007829|PDB:5JPH"
FT   STRAND          101..107
FT                   /evidence="ECO:0007829|PDB:5JPH"
FT   HELIX           108..110
FT                   /evidence="ECO:0007829|PDB:5JPH"
FT   HELIX           111..116
FT                   /evidence="ECO:0007829|PDB:5JPH"
FT   STRAND          120..128
FT                   /evidence="ECO:0007829|PDB:5JPH"
FT   STRAND          131..139
FT                   /evidence="ECO:0007829|PDB:5JPH"
SQ   SEQUENCE   144 AA;  16556 MW;  E1273A514803B71B CRC64;
     MFSKVNNQKM LEDCFYIRKK VFVEEQGVPE ESEIDEYESE SIHLIGYDNG QPVATARIRP
     INETTVKIER VAVMKSHRGQ GMGRMLMQAV ESLAKDEGFY VATMNAQCHA IPFYESLNFK
     MRGNIFLEEG IEHIEMTKKL TSLN