ATSE_STAAM
ID ATSE_STAAM Reviewed; 144 AA.
AC P0A0M6; P52080;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Putative acetyltransferase SAV1054 {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=SAV1054;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
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; BA000017; BAB57216.1; -; Genomic_DNA.
DR RefSeq; WP_000491986.1; NC_002758.2.
DR AlphaFoldDB; P0A0M6; -.
DR SMR; P0A0M6; -.
DR World-2DPAGE; 0002:P0A0M6; -.
DR PaxDb; P0A0M6; -.
DR EnsemblBacteria; BAB57216; BAB57216; SAV1054.
DR KEGG; sav:SAV1054; -.
DR HOGENOM; CLU_056607_6_2_9; -.
DR OMA; PHVEMRK; -.
DR PhylomeDB; P0A0M6; -.
DR Proteomes; UP000002481; 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 SAV1054"
FT /id="PRO_0000201924"
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