ID   ATSE_BACSU              Reviewed;         147 AA.
AC   P37500;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Putative acetyltransferase BSU40680 {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   Name=yybD; OrderedLocusNames=BSU40680;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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; D26185; BAA05199.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB16105.1; -; Genomic_DNA.
DR   PIR; S65993; S65993.
DR   RefSeq; NP_391948.1; NC_000964.3.
DR   RefSeq; WP_003226881.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P37500; -.
DR   SMR; P37500; -.
DR   STRING; 224308.BSU40680; -.
DR   PaxDb; P37500; -.
DR   PRIDE; P37500; -.
DR   EnsemblBacteria; CAB16105; CAB16105; BSU_40680.
DR   GeneID; 938072; -.
DR   KEGG; bsu:BSU40680; -.
DR   PATRIC; fig|224308.179.peg.4410; -.
DR   eggNOG; COG2153; Bacteria.
DR   InParanoid; P37500; -.
DR   OMA; CPISDEF; -.
DR   PhylomeDB; P37500; -.
DR   BioCyc; BSUB:BSU40680-MON; -.
DR   Proteomes; UP000001570; 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..147
FT                   /note="Putative acetyltransferase BSU40680"
FT                   /id="PRO_0000201919"
FT   DOMAIN          1..144
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   BINDING         74..76
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I0Q8"
FT   BINDING         115..117
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I0Q8"
SQ   SEQUENCE   147 AA;  16564 MW;  4D301B306A9E1D5B CRC64;
     MNVKKITSEQ DLHTAFEIRK AVFVEEQGCP ISDEFDEFDT LHGDCQHILA YHQNVPVGTA
     RVRIVGHTGK LERICILKSY RKFGLGKVIV DALERIVKEQ GISAFKLHGQ TQAAGFYEKL
     GYRTASEEFM LDGIPHVLMT KQDDSAL