ID   YTMI_BACSU              Reviewed;         178 AA.
AC   O34350; Q795U5;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Uncharacterized N-acetyltransferase YtmI;
DE            EC=2.3.1.-;
GN   Name=ytmI; OrderedLocusNames=BSU29390;
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=9387221; DOI=10.1099/00221287-143-11-3431;
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT   200 kb rrnB-dnaB region.";
RL   Microbiology 143:3431-3441(1997).
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   INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11390694; DOI=10.1099/00221287-147-6-1631;
RA   Coppee J.Y., Auger S., Turlin E., Sekowska A., Le Caer J.-P., Labas V.,
RA   Vagner V., Danchin A., Martin-Verstraete I.;
RT   "Sulfur-limitation-regulated proteins in Bacillus subtilis: a two-
RT   dimensional gel electrophoresis study.";
RL   Microbiology 147:1631-1640(2001).
RN   [4]
RP   INDUCTION.
RX   PubMed=16109943; DOI=10.1128/jb.187.17.6019-6030.2005;
RA   Burguiere P., Fert J., Guillouard I., Auger S., Danchin A.,
RA   Martin-Verstraete I.;
RT   "Regulation of the Bacillus subtilis ytmI operon, involved in sulfur
RT   metabolism.";
RL   J. Bacteriol. 187:6019-6030(2005).
CC   -!- INDUCTION: Induced by glutathione but not sulfate (at protein level).
CC       Induced by methionine and taurine. Positively regulated by YtlI under
CC       supply of glutathione as sulfur source. {ECO:0000269|PubMed:11390694,
CC       ECO:0000269|PubMed:16109943}.
CC   -!- DISRUPTION PHENOTYPE: Growth rate decreased by 4-fold when grown in
CC       presence of taurine as sulfur source. {ECO:0000269|PubMed:11390694}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase 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; AF008220; AAC00324.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14899.1; -; Genomic_DNA.
DR   PIR; C69996; C69996.
DR   RefSeq; NP_390817.1; NC_000964.3.
DR   RefSeq; WP_003245971.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O34350; -.
DR   SMR; O34350; -.
DR   STRING; 224308.BSU29390; -.
DR   PaxDb; O34350; -.
DR   EnsemblBacteria; CAB14899; CAB14899; BSU_29390.
DR   GeneID; 937353; -.
DR   KEGG; bsu:BSU29390; -.
DR   PATRIC; fig|224308.179.peg.3193; -.
DR   eggNOG; COG0454; Bacteria.
DR   InParanoid; O34350; -.
DR   OMA; RYPWGPE; -.
DR   PhylomeDB; O34350; -.
DR   BioCyc; BSUB:BSU29390-MON; -.
DR   BioCyc; MetaCyc:BSU29390-MON; -.
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   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..178
FT                   /note="Uncharacterized N-acetyltransferase YtmI"
FT                   /id="PRO_0000360505"
FT   DOMAIN          4..163
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   178 AA;  20468 MW;  DBF21F14C393510C CRC64;
     MSDDIFRLAT VEDASELLKL VNSAFQPIRQ LDIDWPSTRA DIQMVSENIE HHSAIVLERD
     GKLISTITIR FPWESETPPS KYPFVWWFAT LPEYKGQGAG SKLLTYVEEK VLRDMLKAPA
     LTLGTSARKH PWLADMYRRR GYEVYFEQEK DGDIGVMMHK VLIPERFNPT LLGAPSWA