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Protein

RsbT co-antagonist protein RsbRD

Gene

rsbRD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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 Componenti: 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 – 1811Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylated by RsbT.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP54504.

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.
InParanoidiP54504.
KOiK17763.
OMAiHIMFEWI.
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

        10         20         30         40         50
MIALDQHLTE HKKDITQQWL EVCTSNGSWL YSAKDQQKLE QKLKDQHELL
60 70 80 90 100
VTIVAKSLRK EDVEDELNRW SLQCARDRAV HEVTVTQSVG QFNTFRHIMF
110 120 130 140 150
EWIHKFSEAS SQDISIQEFY EWSRILNQNI DEIIEVFTEE YHQVTMIQLN
160 170 180 190 200
AQKEMINELS APIMPITDGI GILPLVGEID THRARTILES VLEQCSALKL
210 220 230 240 250
SYLFLDISGV PIVDTMVAYQ IFKVIDSTKL LGIETIISGI RPEIAQTVVK
260 270
LGLDFSNVKT EQSLAKALAN KGFKIKEC
Length:278
Mass (Da):31,835
Last modified:July 6, 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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
D84432 Genomic DNA. Translation: BAA12530.1.
AL009126 Genomic DNA. Translation: CAB14407.2.
PIRiD69958.
RefSeqiNP_390356.2. NC_000964.3.

3D structure databases

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

Protein-protein interaction databases

STRINGi224308.BSU24760.

Proteomic databases

PaxDbiP54504.

Protocols and materials databases

DNASUi938513.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

GenoListiBSU24760. [Micado]

Phylogenomic databases

eggNOGiCOG1366.
HOGENOMiHOG000008785.
InParanoidiP54504.
KOiK17763.
OMAiHIMFEWI.
OrthoDBiEOG6G4VQG.
PhylomeDBiP54504.

Enzyme and pathway databases

BioCyciBSUB:BSU24760-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1995) [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(1996) [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(2008) [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(2000) [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(2003) [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(2006) [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: September 30, 1996
Last sequence update: July 6, 2009
Last modified: March 3, 2015
This is version 95 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.