YSNE_BACSU
ID YSNE_BACSU Reviewed; 151 AA.
AC P94562; Q795X9;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Uncharacterized N-acetyltransferase YsnE;
DE EC=2.3.1.-;
GN Name=ysnE; OrderedLocusNames=BSU28330;
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=8969504; DOI=10.1099/13500872-142-11-3067;
RA Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA Emmerson P.T., Harwood C.R.;
RT "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT chromosome containing genes responsible for stress responses, the
RT utilization of plant cell walls and primary metabolism.";
RL Microbiology 142:3067-3078(1996).
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).
RN [3]
RP STRUCTURE BY NMR.
RG Northeast structural genomics consortium (NESG);
RT "Solution structure of Bacillus subtilis protein ysnE.";
RL Submitted (MAR-2005) to the PDB data bank.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; Z75208; CAA99559.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14793.1; -; Genomic_DNA.
DR PIR; F69986; F69986.
DR RefSeq; NP_390711.1; NC_000964.3.
DR RefSeq; WP_004399128.1; NZ_JNCM01000036.1.
DR PDB; 1YX0; NMR; -; A=1-151.
DR PDBsum; 1YX0; -.
DR AlphaFoldDB; P94562; -.
DR BMRB; P94562; -.
DR SMR; P94562; -.
DR STRING; 224308.BSU28330; -.
DR PaxDb; P94562; -.
DR PRIDE; P94562; -.
DR EnsemblBacteria; CAB14793; CAB14793; BSU_28330.
DR GeneID; 937464; -.
DR KEGG; bsu:BSU28330; -.
DR PATRIC; fig|224308.179.peg.3077; -.
DR eggNOG; COG0454; Bacteria.
DR InParanoid; P94562; -.
DR OMA; ADMYATS; -.
DR PhylomeDB; P94562; -.
DR BioCyc; BSUB:BSU28330-MON; -.
DR EvolutionaryTrace; P94562; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..151
FT /note="Uncharacterized N-acetyltransferase YsnE"
FT /id="PRO_0000360166"
FT DOMAIN 3..151
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1YX0"
FT HELIX 11..19
FT /evidence="ECO:0007829|PDB:1YX0"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:1YX0"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:1YX0"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:1YX0"
FT STRAND 54..67
FT /evidence="ECO:0007829|PDB:1YX0"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1YX0"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:1YX0"
FT HELIX 87..102
FT /evidence="ECO:0007829|PDB:1YX0"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:1YX0"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:1YX0"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:1YX0"
SQ SEQUENCE 151 AA; 17052 MW; CB75E5CAD1D7D80C CRC64;
MHIKIDDLTG RQVVSLVNEH LHSMTLMSPP ESIHALGLEK LRGPEITFWS AWEGDELAGC
GALKELDTRH GEIKSMRTSA SHLRKGVAKQ VLQHIIEEAE KRGYERLSLE TGSMASFEPA
RKLYESFGFQ YCEPFADYGE DPNSVFMTKK L
