ID   RSBRD_BACSU             Reviewed;         278 AA.
AC   P54504;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=RsbT co-antagonist protein RsbRD;
DE   AltName: Full=Stressosome protein RsbRD;
GN   Name=rsbRD; Synonyms=yqhA; OrderedLocusNames=BSU24760;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(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   SEQUENCE REVISION TO 40 AND 89.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   FUNCTION, PHOSPHORYLATION BY RSBT, COMPLEX SUGGESTION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
RC   NCIMB 3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=11157946; DOI=10.1128/jb.183.4.1329-1338.2001;
RA   Akbar S., Gaidenko T.A., Kang C.M., O'Reilly M., Devine K.M., Price C.W.;
RT   "New family of regulators in the environmental signaling pathway which
RT   activates the general stress transcription factor sigma(B) of Bacillus
RT   subtilis.";
RL   J. Bacteriol. 183:1329-1338(2001).
RN   [5]
RP   FUNCTION, AND POSSIBLE SUBUNIT.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
RC   NCIMB 3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=15312768; DOI=10.1016/j.jmb.2004.05.043;
RA   Kim T.-J., Gaidenko T.A., Price C.W.;
RT   "A multicomponent protein complex mediates environmental stress signaling
RT   in Bacillus subtilis.";
RL   J. Mol. Biol. 341:135-150(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-181, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=168;
RX   PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA   Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA   Mann M.;
RT   "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT   Bacillus subtilis.";
RL   Mol. Cell. Proteomics 6:697-707(2007).
CC   -!- FUNCTION: One of 4 functionally non-identical RsbR paralogs, it
CC       functions in the environmental signaling branch of the general stress
CC       response.
CC   -!- FUNCTION: Negative regulator of sigma-B activity. Non-phosphorylated
CC       RsbS binds to RsbT, preventing its association with RsbU. Requires any
CC       one of RsbRA, RsbRB, RsbRC or RsbRD to sequester RsbT. When RsbS and
CC       the RsbR paralog(s) are phosphorylated, they release RsbT, which can
CC       then bind and activate RsbU.
CC   -!- SUBUNIT: Probably present in the stressosome with RsbRA, RsbRB, RsbRC
CC       and RsbS.
CC   -!- PTM: Phosphorylated by RsbT. {ECO:0000269|PubMed:11157946,
CC       ECO:0000269|PubMed:17218307}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene have no visible phenotype
CC       is response to salt, ethanol or energy stress. However cells with
CC       multiple disruption (RsbRA, RsbRB and RsbRD) have an increased basal
CC       level of sigma-B, indicating this protein is a negative regulator of
CC       sigma-B. {ECO:0000269|PubMed:11157946}.
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DR   EMBL; D84432; BAA12530.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14407.2; -; Genomic_DNA.
DR   PIR; D69958; D69958.
DR   RefSeq; NP_390356.2; NC_000964.3.
DR   RefSeq; WP_004398754.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P54504; -.
DR   SMR; P54504; -.
DR   STRING; 224308.BSU24760; -.
DR   iPTMnet; P54504; -.
DR   jPOST; P54504; -.
DR   PaxDb; 224308-BSU24760; -.
DR   DNASU; 938513; -.
DR   EnsemblBacteria; CAB14407; CAB14407; BSU_24760.
DR   GeneID; 938513; -.
DR   KEGG; bsu:BSU24760; -.
DR   PATRIC; fig|224308.179.peg.2695; -.
DR   eggNOG; COG1366; Bacteria.
DR   InParanoid; P54504; -.
DR   OrthoDB; 9800154at2; -.
DR   PhylomeDB; P54504; -.
DR   BioCyc; BSUB:BSU24760-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   CDD; cd07041; STAS_RsbR_RsbS_like; 1.
DR   Gene3D; 1.10.490.70; Histidine kinase N-terminal domain; 1.
DR   Gene3D; 3.30.750.24; STAS domain; 1.
DR   InterPro; IPR025751; RsbRD_N_dom.
DR   InterPro; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   PANTHER; PTHR33745; RSBT ANTAGONIST PROTEIN RSBS-RELATED; 1.
DR   PANTHER; PTHR33745:SF3; RSBT CO-ANTAGONIST PROTEIN RSBRC; 1.
DR   Pfam; PF14361; RsbRD_N; 1.
DR   Pfam; PF01740; STAS; 1.
DR   SUPFAM; SSF52091; SpoIIaa-like; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..278
FT                   /note="RsbT co-antagonist protein RsbRD"
FT                   /id="PRO_0000049817"
FT   DOMAIN          160..271
FT                   /note="STAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT   MOD_RES         181
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:17218307"
FT   CONFLICT        40
FT                   /note="E -> G (in Ref. 1; BAA12530)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        89
FT                   /note="V -> F (in Ref. 1; BAA12530)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   278 AA;  31835 MW;  B5057DE23E0914D7 CRC64;
     MIALDQHLTE HKKDITQQWL EVCTSNGSWL YSAKDQQKLE QKLKDQHELL VTIVAKSLRK
     EDVEDELNRW SLQCARDRAV HEVTVTQSVG QFNTFRHIMF EWIHKFSEAS SQDISIQEFY
     EWSRILNQNI DEIIEVFTEE YHQVTMIQLN AQKEMINELS APIMPITDGI GILPLVGEID
     THRARTILES VLEQCSALKL SYLFLDISGV PIVDTMVAYQ IFKVIDSTKL LGIETIISGI
     RPEIAQTVVK LGLDFSNVKT EQSLAKALAN KGFKIKEC
//