(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 130.
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 / 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 / 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 / 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 / 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}.
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   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; BSU04670.
DR   GeneID; 938176; -.
DR   KEGG; bsu:BSU04670; -.
DR   PATRIC; fig|224308.43.peg.487; -.
DR   eggNOG; ENOG4107MMM; Bacteria.
DR   eggNOG; COG1366; LUCA.
DR   HOGENOM; HOG000269596; -.
DR   InParanoid; P42409; -.
DR   KO; K17763; -.
DR   OMA; NQYSISW; -.
DR   PhylomeDB; P42409; -.
DR   BioCyc; BSUB:BSU04670-MONOMER; -.
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   CDD; cd01067; Globin_like; 1.
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;
DR   PRODOM; P42409.
DR   SWISS-2DPAGE; P42409.
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:0000244|PDB:2BNL"
FT   HELIX           15..30
FT                   /evidence="ECO:0000244|PDB:2BNL"
FT   HELIX           39..54
FT                   /evidence="ECO:0000244|PDB:2BNL"
FT   TURN            60..63
FT                   /evidence="ECO:0000244|PDB:2BNL"
FT   HELIX           64..76
FT                   /evidence="ECO:0000244|PDB:2BNL"
FT   HELIX           81..100
FT                   /evidence="ECO:0000244|PDB:2BNL"
FT   HELIX           109..135
FT                   /evidence="ECO:0000244|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
//

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