ATSE_STAA8
ID ATSE_STAA8 Reviewed; 144 AA.
AC P0A0M9; P52080; Q2FZK6;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Putative acetyltransferase SAOUHSC_00995 {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=SAOUHSC_00995;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7816834; DOI=10.1073/pnas.92.1.285;
RA Oshida T., Sugai M., Komatsuzawa H., Hong Y.-M., Suginaka H., Tomasz A.;
RT "A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine
RT amidase domain and an endo-beta-N-acetylglucosaminidase domain: cloning,
RT sequence analysis, and characterization.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:285-289(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Foster S.J.;
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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; D17366; BAA04184.1; -; Genomic_DNA.
DR EMBL; L41499; AAA99981.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD30119.1; -; Genomic_DNA.
DR RefSeq; WP_000491986.1; NZ_LS483365.1.
DR RefSeq; YP_499547.1; NC_007795.1.
DR AlphaFoldDB; P0A0M9; -.
DR SMR; P0A0M9; -.
DR STRING; 1280.SAXN108_1051; -.
DR EnsemblBacteria; ABD30119; ABD30119; SAOUHSC_00995.
DR GeneID; 3920395; -.
DR KEGG; sao:SAOUHSC_00995; -.
DR PATRIC; fig|93061.5.peg.913; -.
DR eggNOG; COG2153; Bacteria.
DR HOGENOM; CLU_056607_6_2_9; -.
DR OMA; PHVEMRK; -.
DR PRO; PR:P0A0M9; -.
DR Proteomes; UP000008816; 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:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
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; Reference proteome; Transferase.
FT CHAIN 1..144
FT /note="Putative acetyltransferase SAOUHSC_00995"
FT /id="PRO_0000201929"
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