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P54504

- RSBRD_BACSU

UniProt

P54504 - RSBRD_BACSU

Protein

RsbT co-antagonist protein RsbRD

Gene

rsbRD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 2 (07 Jul 2009)
      Previous versions | rss
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    Functioni

    One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response.
    Negative regulator of sigma-B activity. Non-phosphorylated RsbS binds to RsbT, preventing its association with RsbU. Requires any one of RsbRA, RsbRB, RsbRC or RsbRD to sequester RsbT. When RsbS and the RsbR paralog(s) are phosphorylated, they release RsbT, which can then bind and activate RsbU.

    Enzyme and pathway databases

    BioCyciBSUB:BSU24760-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RsbT co-antagonist protein RsbRD
    Alternative name(s):
    Stressosome protein RsbRD
    Gene namesi
    Name:rsbRD
    Synonyms:yqhA
    Ordered Locus Names:BSU24760
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU24760. [Micado]

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene have no visible phenotype is response to salt, ethanol or energy stress. However cells with multiple disruption (RsbRA, RsbRB and RsbRD) have an increased basal level of sigma-B, indicating this protein is a negative regulator of sigma-B.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 278278RsbT co-antagonist protein RsbRDPRO_0000049817Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei181 – 1811Phosphothreonine2 Publications

    Post-translational modificationi

    Phosphorylated by RsbT.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP54504.

    PTM databases

    PhosSiteiP0712194.

    Interactioni

    Subunit structurei

    Probably present in the stressosome with RsbRA, RsbRB, RsbRC and RsbS.

    Protein-protein interaction databases

    STRINGi224308.BSU24760.

    Structurei

    3D structure databases

    ProteinModelPortaliP54504.
    SMRiP54504. Positions 162-276.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini160 – 271112STASPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 STAS domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1366.
    HOGENOMiHOG000008785.
    KOiK17763.
    OrthoDBiEOG6G4VQG.
    PhylomeDBiP54504.

    Family and domain databases

    Gene3Di3.30.750.24. 1 hit.
    InterProiIPR025751. RsbRD_N_dom.
    IPR002645. STAS_dom.
    [Graphical view]
    PfamiPF14361. RsbRD_N. 1 hit.
    PF01740. STAS. 1 hit.
    [Graphical view]
    SUPFAMiSSF52091. SSF52091. 1 hit.
    PROSITEiPS50801. STAS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P54504-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIALDQHLTE HKKDITQQWL EVCTSNGSWL YSAKDQQKLE QKLKDQHELL    50
    VTIVAKSLRK EDVEDELNRW SLQCARDRAV HEVTVTQSVG QFNTFRHIMF 100
    EWIHKFSEAS SQDISIQEFY EWSRILNQNI DEIIEVFTEE YHQVTMIQLN 150
    AQKEMINELS APIMPITDGI GILPLVGEID THRARTILES VLEQCSALKL 200
    SYLFLDISGV PIVDTMVAYQ IFKVIDSTKL LGIETIISGI RPEIAQTVVK 250
    LGLDFSNVKT EQSLAKALAN KGFKIKEC 278
    Length:278
    Mass (Da):31,835
    Last modified:July 7, 2009 - v2
    Checksum:iB5057DE23E0914D7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti40 – 401E → G in BAA12530. (PubMed:8969508)Curated
    Sequence conflicti89 – 891V → F in BAA12530. (PubMed:8969508)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D84432 Genomic DNA. Translation: BAA12530.1.
    AL009126 Genomic DNA. Translation: CAB14407.2.
    PIRiD69958.
    RefSeqiNP_390356.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB14407; CAB14407; BSU24760.
    GeneIDi938513.
    KEGGibsu:BSU24760.
    PATRICi18976786. VBIBacSub10457_2583.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D84432 Genomic DNA. Translation: BAA12530.1 .
    AL009126 Genomic DNA. Translation: CAB14407.2 .
    PIRi D69958.
    RefSeqi NP_390356.2. NC_000964.3.

    3D structure databases

    ProteinModelPortali P54504.
    SMRi P54504. Positions 162-276.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU24760.

    PTM databases

    PhosSitei P0712194.

    Proteomic databases

    PaxDbi P54504.

    Protocols and materials databases

    DNASUi 938513.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB14407 ; CAB14407 ; BSU24760 .
    GeneIDi 938513.
    KEGGi bsu:BSU24760.
    PATRICi 18976786. VBIBacSub10457_2583.

    Organism-specific databases

    GenoListi BSU24760. [Micado ]

    Phylogenomic databases

    eggNOGi COG1366.
    HOGENOMi HOG000008785.
    KOi K17763.
    OrthoDBi EOG6G4VQG.
    PhylomeDBi P54504.

    Enzyme and pathway databases

    BioCyci BSUB:BSU24760-MONOMER.

    Family and domain databases

    Gene3Di 3.30.750.24. 1 hit.
    InterProi IPR025751. RsbRD_N_dom.
    IPR002645. STAS_dom.
    [Graphical view ]
    Pfami PF14361. RsbRD_N. 1 hit.
    PF01740. STAS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52091. SSF52091. 1 hit.
    PROSITEi PS50801. STAS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes."
      Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.
      Microbiology 142:3103-3111(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168 / JH642.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
      Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
      Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 40 AND 89.
    4. "New family of regulators in the environmental signaling pathway which activates the general stress transcription factor sigma(B) of Bacillus subtilis."
      Akbar S., Gaidenko T.A., Kang C.M., O'Reilly M., Devine K.M., Price C.W.
      J. Bacteriol. 183:1329-1338(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION BY RSBT, COMPLEX SUGGESTION, DISRUPTION PHENOTYPE.
      Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
    5. "A multicomponent protein complex mediates environmental stress signaling in Bacillus subtilis."
      Kim T.-J., Gaidenko T.A., Price C.W.
      J. Mol. Biol. 341:135-150(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, POSSIBLE SUBUNIT.
      Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
    6. "The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis."
      Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.
      Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-181, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: 168.

    Entry informationi

    Entry nameiRSBRD_BACSU
    AccessioniPrimary (citable) accession number: P54504
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 7, 2009
    Last modified: October 1, 2014
    This is version 92 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3