RSBRD_BACSU
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 03-AUG-2022, entry version 121.
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; Firmicutes; 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 / 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 [5]
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 [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; P54504; -.
DR PRIDE; P54504; -.
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 OMA; DTMVAYQ; -.
DR PhylomeDB; P54504; -.
DR BioCyc; BSUB:BSU24760-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR Gene3D; 3.30.750.24; -; 1.
DR InterPro; IPR025751; RsbRD_N_dom.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR Pfam; PF14361; RsbRD_N; 1.
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..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
