YTRH_BACSU
ID YTRH_BACSU Reviewed; 113 AA.
AC C0H3P8;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Sporulation membrane protein YtrH;
GN Name=ytrH; Synonyms=spoVIGA; OrderedLocusNames=BSU29239;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP SUBCELLULAR LOCATION, AND INDUCTION BY SIGMA-E.
RC STRAIN=168 / PY79;
RX PubMed=12662922; DOI=10.1016/s0022-2836(03)00205-5;
RA Eichenberger P., Jensen S.T., Conlon E.M., van Ooij C., Silvaggi J.,
RA Gonzalez-Pastor J.-E., Fujita M., Ben-Yehuda S., Stragier P., Liu J.S.,
RA Losick R.;
RT "The sigmaE regulon and the identification of additional sporulation genes
RT in Bacillus subtilis.";
RL J. Mol. Biol. 327:945-972(2003).
RN [3]
RP FUNCTION IN SPORULATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / PY79;
RX PubMed=15547282; DOI=10.1128/jb.186.23.8089-8095.2004;
RA Silvaggi J.M., Popham D.L., Driks A., Eichenberger P., Losick R.;
RT "Unmasking novel sporulation genes in Bacillus subtilis.";
RL J. Bacteriol. 186:8089-8095(2004).
CC -!- FUNCTION: Involved in sporulation. May contribute to cortex formation
CC or stability. {ECO:0000269|PubMed:15547282}.
CC -!- SUBCELLULAR LOCATION: Forespore outer membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000305}. Note=Shortly after the initiation
CC of the engulfment, is localized to the sporulation septum. During later
CC stages of sporulation, remains associated with the forespore outer
CC membrane. {ECO:0000269|PubMed:12662922}.
CC -!- INDUCTION: Transcriptionally regulated by sigma-E.
CC {ECO:0000269|PubMed:12662922}.
CC -!- DISRUPTION PHENOTYPE: Impaired ability to form spores when associated
CC with a ytrI deletion. In combination with a ybaN deletion, cells show a
CC severe sporulation defect. {ECO:0000269|PubMed:15547282}.
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DR EMBL; AL009126; CAX52677.1; -; Genomic_DNA.
DR RefSeq; WP_003229410.1; NZ_JNCM01000036.1.
DR RefSeq; YP_003097771.1; NC_000964.3.
DR AlphaFoldDB; C0H3P8; -.
DR STRING; 224308.BSU29239; -.
DR PaxDb; C0H3P8; -.
DR EnsemblBacteria; CAX52677; CAX52677; BSU_29239.
DR GeneID; 8303067; -.
DR KEGG; bsu:BSU29239; -.
DR PATRIC; fig|224308.179.peg.3175; -.
DR eggNOG; ENOG50330BE; Bacteria.
DR OMA; AGSLKIW; -.
DR BioCyc; BSUB:BSU29239-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR025689; Spore_YtrH.
DR Pfam; PF14034; Spore_YtrH; 1.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Sporulation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..113
FT /note="Sporulation membrane protein YtrH"
FT /id="PRO_0000387957"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 113 AA; 12060 MW; 61AD1F65A6E96453 CRC64;
MDQEAGFMVN FINSYFIALG VLIGGALIGG LGAYLAGEPP LTAITKLANR LKIWALVAAI
GGTFDAVYSF ERGILEGNTR DIFKQLLLII SAMGGAQSGW LIISWLTQEH LSS