ID   RSBRC_BACSU             Reviewed;         282 AA.
AC   O31856; Q7BV96;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=RsbT co-antagonist protein RsbRC;
DE   AltName: Full=Stressosome protein RsbRC;
GN   Name=rsbRC; Synonyms=yojH; OrderedLocusNames=BSU19450;
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=9734814; DOI=10.1093/dnares/5.3.195;
RA   Ghim S.-Y., Choi S.-K., Shin B.-S., Jeong Y.-M., Sorokin A., Ehrlich S.D.,
RA   Park S.-H.;
RT   "Sequence analysis of the Bacillus subtilis 168 chromosome region between
RT   the sspC and odhA loci (184 degrees-180 degrees).";
RL   DNA Res. 5:195-201(1998).
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   FUNCTION, PHOSPHORYLATION BY RSBT, COMPLEX SUGGESTION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   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   [4]
RP   FUNCTION, AND POSSIBLE SUBUNIT.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-174 AND THR-186, AND
RP   IDENTIFICATION BY 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, RsbRD
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       in response to salt, ethanol or energy stress. However cells with
CC       multiple disruptions (RsbRA, RsbRB, RsbRC and RsbRD) have an increased
CC       basal level of sigma-B, indicating this protein is a negative regulator
CC       of sigma-B. {ECO:0000269|PubMed:11157946}.
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DR   EMBL; AF026147; AAC17856.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13837.1; -; Genomic_DNA.
DR   PIR; E69906; E69906.
DR   RefSeq; NP_389827.1; NC_000964.3.
DR   RefSeq; WP_003231216.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O31856; -.
DR   SMR; O31856; -.
DR   STRING; 224308.BSU19450; -.
DR   iPTMnet; O31856; -.
DR   PaxDb; O31856; -.
DR   PRIDE; O31856; -.
DR   DNASU; 940093; -.
DR   EnsemblBacteria; CAB13837; CAB13837; BSU_19450.
DR   GeneID; 940093; -.
DR   KEGG; bsu:BSU19450; -.
DR   PATRIC; fig|224308.179.peg.2127; -.
DR   eggNOG; COG1366; Bacteria.
DR   InParanoid; O31856; -.
DR   OMA; IHIFIEE; -.
DR   PhylomeDB; O31856; -.
DR   BioCyc; BSUB:BSU19450-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   Gene3D; 3.30.750.24; -; 1.
DR   InterPro; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   Pfam; PF01740; STAS; 1.
DR   SUPFAM; SSF52091; SSF52091; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..282
FT                   /note="RsbT co-antagonist protein RsbRC"
FT                   /id="PRO_0000361686"
FT   DOMAIN          165..276
FT                   /note="STAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT   MOD_RES         165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17218307"
FT   MOD_RES         174
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17218307"
FT   MOD_RES         186
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:17218307"
SQ   SEQUENCE   282 AA;  32109 MW;  AA694786619394A0 CRC64;
     MAKNKKLFEY LSQHAETISS TWYETIEETD PNSIYASTDP VVIHNLKSQN LAFNYKINRI
     FIDDEDVYLP ILKEWAFEVT QDQEHLKTPI HYIIREFVRV RDLYVSYVKE FVHLNQNTVK
     SEEAEDLYHA LIKAFDLVIH IFIEEMYKNT SLQLQAQKDM ITELSAPVIV LFHSVGLLPL
     IGDIDTVRAK LIMENTLHQC AKKKVTQLYI DLSGVAVIDT MVAHQLFSLI EALRLIGVSS
     TLSGIRPEIA QTAVQLGLSF EGISLRSTLA SAIASDLKLK KV