RSBRA_BACSU
ID RSBRA_BACSU Reviewed; 274 AA.
AC P42409;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=RsbT co-antagonist protein RsbRA;
DE AltName: Full=Stressosome protein RsbRA;
GN Name=rsbRA; Synonyms=rsbR, ycxR; OrderedLocusNames=BSU04670;
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 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8002610; DOI=10.1128/jb.177.1.123-133.1995;
RA Wise A.A., Price C.W.;
RT "Four additional genes in the sigB operon of Bacillus subtilis that control
RT activity of the general stress factor sigma B in response to environmental
RT signals.";
RL J. Bacteriol. 177:123-133(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT subtilis genome.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP FUNCTION, COMPLEX SUGGESTION, AND DISRUPTION 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 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 AT THR-171 AND THR-205, AND MUTAGENESIS OF THR-171 AND
RP THR-205.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=10329124; DOI=10.1006/jmbi.1999.2665;
RA Gaidenko T.A., Yang X., Lee Y.M., Price C.W.;
RT "Threonine phosphorylation of modulator protein RsbR governs its ability to
RT regulate a serine kinase in the environmental stress signaling pathway of
RT Bacillus subtilis.";
RL J. Mol. Biol. 288:29-39(1999).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-171, 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: Acts as a positive regulator of sigma-B activity in response
CC to salt and heat stress by stimulating the activity of the RsbT kinase
CC toward RsbS in vitro.
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: Interacts with RsbRB and RsbS in the stressosome. The
CC stressosome probably also contains RsbRC and RsbRD.
CC {ECO:0000269|PubMed:15312768}.
CC -!- PTM: Phosphorylated by RsbT. This threonine phosphorylation abrogates
CC the ability of RsbRA to stimulate RsbT in vitro.
CC {ECO:0000269|PubMed:10329124, ECO:0000269|PubMed:17218307}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have a decreased response
CC to salt stress, indicating that RsbRA is a positive regulator of sigma-
CC B activity. Its activity is dependent on RsbRB.
CC {ECO:0000269|PubMed:11157946}.
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; L35574; AAA85080.1; -; Genomic_DNA.
DR EMBL; AB001488; BAA19304.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12274.1; -; Genomic_DNA.
DR PIR; E69701; E69701.
DR RefSeq; NP_388348.1; NC_000964.3.
DR RefSeq; WP_009966610.1; NZ_JNCM01000031.1.
DR PDB; 2BNL; X-ray; 2.00 A; A/B/C/D/E/F=1-136.
DR PDBsum; 2BNL; -.
DR AlphaFoldDB; P42409; -.
DR SMR; P42409; -.
DR DIP; DIP-375N; -.
DR IntAct; P42409; 2.
DR STRING; 224308.BSU04670; -.
DR iPTMnet; P42409; -.
DR jPOST; P42409; -.
DR PaxDb; P42409; -.
DR PRIDE; P42409; -.
DR EnsemblBacteria; CAB12274; CAB12274; BSU_04670.
DR GeneID; 938176; -.
DR KEGG; bsu:BSU04670; -.
DR PATRIC; fig|224308.43.peg.487; -.
DR eggNOG; COG1366; Bacteria.
DR InParanoid; P42409; -.
DR OMA; NQYSISW; -.
DR PhylomeDB; P42409; -.
DR BioCyc; BSUB:BSU04670-MON; -.
DR EvolutionaryTrace; P42409; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR Gene3D; 1.10.490.10; -; 1.
DR Gene3D; 3.30.750.24; -; 1.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR014792; RsbRA_N.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR Pfam; PF08678; Rsbr_N; 1.
DR Pfam; PF01740; STAS; 1.
DR SUPFAM; SSF52091; SSF52091; 1.
DR PROSITE; PS50801; STAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Phosphoprotein; Reference proteome.
FT CHAIN 1..274
FT /note="RsbT co-antagonist protein RsbRA"
FT /id="PRO_0000097470"
FT DOMAIN 150..265
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT MOD_RES 171
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:10329124,
FT ECO:0000269|PubMed:17218307"
FT MOD_RES 205
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:10329124"
FT MUTAGEN 171
FT /note="T->A: No phosphorylation; when associated with A-
FT 205. No stress response. In absence of the other RsbR
FT paralogs greatly reduced stress response."
FT /evidence="ECO:0000269|PubMed:10329124"
FT MUTAGEN 171
FT /note="T->D: Decrease in induction of sigma-B activity in
FT response to a salt stress. In absence of the other RsbR
FT paralogs no change in stress response."
FT /evidence="ECO:0000269|PubMed:10329124"
FT MUTAGEN 205
FT /note="T->A: No phosphorylation; when associated with A-
FT 171. In absence of the other RsbR paralogs unable to
FT function as a co-antagonist when RsbRB."
FT /evidence="ECO:0000269|PubMed:10329124"
FT MUTAGEN 205
FT /note="T->D: Decrease in induction of sigma-B activity in
FT response to a salt stress. In absence of the other RsbR
FT paralogs no change in stress response when RsbRB."
FT /evidence="ECO:0000269|PubMed:10329124"
FT HELIX 5..13
FT /evidence="ECO:0007829|PDB:2BNL"
FT HELIX 15..30
FT /evidence="ECO:0007829|PDB:2BNL"
FT HELIX 39..54
FT /evidence="ECO:0007829|PDB:2BNL"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:2BNL"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:2BNL"
FT HELIX 81..100
FT /evidence="ECO:0007829|PDB:2BNL"
FT HELIX 109..135
FT /evidence="ECO:0007829|PDB:2BNL"
SQ SEQUENCE 274 AA; 31050 MW; 4E14615EA6FC0493 CRC64;
MMSNQTVYQF IAENQNELLQ LWTDTLKELS EQESYQLTDQ VYENISKEYI DILLLSVKDE
NAAESQISEL ALRAVQIGLS MKFLATALAE FWKRLYTKMN DKRLPDQEST ELIWQIDRFF
SPINTEIFNQ YSISWEKTVS LQKIALQELS APLIPVFENI TVMPLVGTID TERAKRIMEN
LLNGVVKHRS QVVLIDITGV PVVDTMVAHH IIQASEAVRL VGAKCLLAGI RPEIAQTIVN
LGIDLSQVIT KNTLQKGIQT ALEMTDRKIV SLGE
